data_9L30
# 
_entry.id   9L30 
# 
_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   9L30         pdb_00009l30 10.2210/pdb9l30/pdb 
WWPDB D_1300054856 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-30 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9L30 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'PDB entries for the same citation' 
_pdbx_database_related.db_id          7Y2A 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              cukim@unist.ac.kr 
_pdbx_contact_author.name_first         'Chae Un' 
_pdbx_contact_author.name_last          Kim 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9350-8441 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kim, C.U.' 1 0000-0001-9350-8441 
'Kim, J.K.' 2 0000-0003-2650-9879 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                4404 
_citation.page_last                 4404 
_citation.title                     'Fast product release requires active-site water dynamics in carbonic anhydrase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59645-x 
_citation.pdbx_database_id_PubMed   40355440 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kim, J.K.'     1  0000-0003-2650-9879 
primary 'Lim, S.W.'     2  ?                   
primary 'Jeong, H.'     3  ?                   
primary 'Lee, C.'       4  0000-0002-3939-2457 
primary 'Kim, S.'       5  ?                   
primary 'Son, D.W.'     6  ?                   
primary 'Kumar, R.'     7  ?                   
primary 'Andring, J.T.' 8  ?                   
primary 'Lomelino, C.'  9  ?                   
primary 'Wierman, J.L.' 10 ?                   
primary 'Cohen, A.E.'   11 0000-0003-2414-9427 
primary 'Shin, T.J.'    12 0000-0002-1438-3298 
primary 'Ghim, C.M.'    13 0000-0002-1460-9218 
primary 'McKenna, R.'   14 0000-0002-2792-935X 
primary 'Jo, B.H.'      15 0000-0002-6408-4317 
primary 'Min, D.'       16 0000-0002-2856-8082 
primary 'Choi, J.M.'    17 ?                   
primary 'Kim, C.U.'     18 0000-0001-9350-8441 
# 
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 '2-(3-NITROPHENYL)ACETIC ACID' 181.145   1   ?       ? ? ? 
4 water       nat water                          18.015    242 ?       ? ? ? 
# 
_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 '2-(3-NITROPHENYL)ACETIC ACID' MNP 
4 water                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                        ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                       ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                     ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                       ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                      ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                        ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                      ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                          ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                     ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                        ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                         ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                     ? 'C5 H11 N O2 S'  149.211 
MNP non-polymer         . '2-(3-NITROPHENYL)ACETIC ACID' ? 'C8 H7 N O4'     181.145 
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   ?   ?   ?   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 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 MNP ? ? MNP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ZN  ? ? ZN  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 301 ZN  ZN  A . 
C 3 MNP 1   302 302 MNP MNP A . 
D 4 HOH 1   401 401 HOH HOH A . 
D 4 HOH 2   402 404 HOH HOH A . 
D 4 HOH 3   403 434 HOH HOH A . 
D 4 HOH 4   404 576 HOH HOH A . 
D 4 HOH 5   405 410 HOH HOH A . 
D 4 HOH 6   406 432 HOH HOH A . 
D 4 HOH 7   407 408 HOH HOH A . 
D 4 HOH 8   408 559 HOH HOH A . 
D 4 HOH 9   409 406 HOH HOH A . 
D 4 HOH 10  410 570 HOH HOH A . 
D 4 HOH 11  411 503 HOH HOH A . 
D 4 HOH 12  412 403 HOH HOH A . 
D 4 HOH 13  413 563 HOH HOH A . 
D 4 HOH 14  414 412 HOH HOH A . 
D 4 HOH 15  415 415 HOH HOH A . 
D 4 HOH 16  416 455 HOH HOH A . 
D 4 HOH 17  417 452 HOH HOH A . 
D 4 HOH 18  418 417 HOH HOH A . 
D 4 HOH 19  419 413 HOH HOH A . 
D 4 HOH 20  420 411 HOH HOH A . 
D 4 HOH 21  421 414 HOH HOH A . 
D 4 HOH 22  422 419 HOH HOH A . 
D 4 HOH 23  423 424 HOH HOH A . 
D 4 HOH 24  424 430 HOH HOH A . 
D 4 HOH 25  425 481 HOH HOH A . 
D 4 HOH 26  426 493 HOH HOH A . 
D 4 HOH 27  427 442 HOH HOH A . 
D 4 HOH 28  428 428 HOH HOH A . 
D 4 HOH 29  429 407 HOH HOH A . 
D 4 HOH 30  430 421 HOH HOH A . 
D 4 HOH 31  431 555 HOH HOH A . 
D 4 HOH 32  432 496 HOH HOH A . 
D 4 HOH 33  433 459 HOH HOH A . 
D 4 HOH 34  434 439 HOH HOH A . 
D 4 HOH 35  435 444 HOH HOH A . 
D 4 HOH 36  436 402 HOH HOH A . 
D 4 HOH 37  437 431 HOH HOH A . 
D 4 HOH 38  438 416 HOH HOH A . 
D 4 HOH 39  439 448 HOH HOH A . 
D 4 HOH 40  440 425 HOH HOH A . 
D 4 HOH 41  441 423 HOH HOH A . 
D 4 HOH 42  442 484 HOH HOH A . 
D 4 HOH 43  443 518 HOH HOH A . 
D 4 HOH 44  444 451 HOH HOH A . 
D 4 HOH 45  445 456 HOH HOH A . 
D 4 HOH 46  446 472 HOH HOH A . 
D 4 HOH 47  447 473 HOH HOH A . 
D 4 HOH 48  448 420 HOH HOH A . 
D 4 HOH 49  449 458 HOH HOH A . 
D 4 HOH 50  450 435 HOH HOH A . 
D 4 HOH 51  451 447 HOH HOH A . 
D 4 HOH 52  452 460 HOH HOH A . 
D 4 HOH 53  453 443 HOH HOH A . 
D 4 HOH 54  454 409 HOH HOH A . 
D 4 HOH 55  455 453 HOH HOH A . 
D 4 HOH 56  456 454 HOH HOH A . 
D 4 HOH 57  457 464 HOH HOH A . 
D 4 HOH 58  458 463 HOH HOH A . 
D 4 HOH 59  459 445 HOH HOH A . 
D 4 HOH 60  460 427 HOH HOH A . 
D 4 HOH 61  461 436 HOH HOH A . 
D 4 HOH 62  462 467 HOH HOH A . 
D 4 HOH 63  463 468 HOH HOH A . 
D 4 HOH 64  464 482 HOH HOH A . 
D 4 HOH 65  465 446 HOH HOH A . 
D 4 HOH 66  466 462 HOH HOH A . 
D 4 HOH 67  467 437 HOH HOH A . 
D 4 HOH 68  468 429 HOH HOH A . 
D 4 HOH 69  469 422 HOH HOH A . 
D 4 HOH 70  470 479 HOH HOH A . 
D 4 HOH 71  471 502 HOH HOH A . 
D 4 HOH 72  472 471 HOH HOH A . 
D 4 HOH 73  473 450 HOH HOH A . 
D 4 HOH 74  474 515 HOH HOH A . 
D 4 HOH 75  475 507 HOH HOH A . 
D 4 HOH 76  476 470 HOH HOH A . 
D 4 HOH 77  477 489 HOH HOH A . 
D 4 HOH 78  478 461 HOH HOH A . 
D 4 HOH 79  479 553 HOH HOH A . 
D 4 HOH 80  480 438 HOH HOH A . 
D 4 HOH 81  481 474 HOH HOH A . 
D 4 HOH 82  482 494 HOH HOH A . 
D 4 HOH 83  483 476 HOH HOH A . 
D 4 HOH 84  484 497 HOH HOH A . 
D 4 HOH 85  485 491 HOH HOH A . 
D 4 HOH 86  486 488 HOH HOH A . 
D 4 HOH 87  487 449 HOH HOH A . 
D 4 HOH 88  488 511 HOH HOH A . 
D 4 HOH 89  489 405 HOH HOH A . 
D 4 HOH 90  490 517 HOH HOH A . 
D 4 HOH 91  491 549 HOH HOH A . 
D 4 HOH 92  492 486 HOH HOH A . 
D 4 HOH 93  493 426 HOH HOH A . 
D 4 HOH 94  494 504 HOH HOH A . 
D 4 HOH 95  495 469 HOH HOH A . 
D 4 HOH 96  496 478 HOH HOH A . 
D 4 HOH 97  497 498 HOH HOH A . 
D 4 HOH 98  498 495 HOH HOH A . 
D 4 HOH 99  499 542 HOH HOH A . 
D 4 HOH 100 500 508 HOH HOH A . 
D 4 HOH 101 501 509 HOH HOH A . 
D 4 HOH 102 502 475 HOH HOH A . 
D 4 HOH 103 503 501 HOH HOH A . 
D 4 HOH 104 504 418 HOH HOH A . 
D 4 HOH 105 505 520 HOH HOH A . 
D 4 HOH 106 506 516 HOH HOH A . 
D 4 HOH 107 507 521 HOH HOH A . 
D 4 HOH 108 508 457 HOH HOH A . 
D 4 HOH 109 509 505 HOH HOH A . 
D 4 HOH 110 510 492 HOH HOH A . 
D 4 HOH 111 511 547 HOH HOH A . 
D 4 HOH 112 512 465 HOH HOH A . 
D 4 HOH 113 513 528 HOH HOH A . 
D 4 HOH 114 514 499 HOH HOH A . 
D 4 HOH 115 515 527 HOH HOH A . 
D 4 HOH 116 516 510 HOH HOH A . 
D 4 HOH 117 517 514 HOH HOH A . 
D 4 HOH 118 518 506 HOH HOH A . 
D 4 HOH 119 519 546 HOH HOH A . 
D 4 HOH 120 520 433 HOH HOH A . 
D 4 HOH 121 521 597 HOH HOH A . 
D 4 HOH 122 522 490 HOH HOH A . 
D 4 HOH 123 523 558 HOH HOH A . 
D 4 HOH 124 524 573 HOH HOH A . 
D 4 HOH 125 525 526 HOH HOH A . 
D 4 HOH 126 526 512 HOH HOH A . 
D 4 HOH 127 527 543 HOH HOH A . 
D 4 HOH 128 528 513 HOH HOH A . 
D 4 HOH 129 529 524 HOH HOH A . 
D 4 HOH 130 530 586 HOH HOH A . 
D 4 HOH 131 531 536 HOH HOH A . 
D 4 HOH 132 532 551 HOH HOH A . 
D 4 HOH 133 533 533 HOH HOH A . 
D 4 HOH 134 534 557 HOH HOH A . 
D 4 HOH 135 535 522 HOH HOH A . 
D 4 HOH 136 536 538 HOH HOH A . 
D 4 HOH 137 537 539 HOH HOH A . 
D 4 HOH 138 538 531 HOH HOH A . 
D 4 HOH 139 539 535 HOH HOH A . 
D 4 HOH 140 540 480 HOH HOH A . 
D 4 HOH 141 541 574 HOH HOH A . 
D 4 HOH 142 542 529 HOH HOH A . 
D 4 HOH 143 543 554 HOH HOH A . 
D 4 HOH 144 544 550 HOH HOH A . 
D 4 HOH 145 545 537 HOH HOH A . 
D 4 HOH 146 546 571 HOH HOH A . 
D 4 HOH 147 547 500 HOH HOH A . 
D 4 HOH 148 548 525 HOH HOH A . 
D 4 HOH 149 549 548 HOH HOH A . 
D 4 HOH 150 550 540 HOH HOH A . 
D 4 HOH 151 551 534 HOH HOH A . 
D 4 HOH 152 552 441 HOH HOH A . 
D 4 HOH 153 553 545 HOH HOH A . 
D 4 HOH 154 554 565 HOH HOH A . 
D 4 HOH 155 555 519 HOH HOH A . 
D 4 HOH 156 556 541 HOH HOH A . 
D 4 HOH 157 557 556 HOH HOH A . 
D 4 HOH 158 558 564 HOH HOH A . 
D 4 HOH 159 559 566 HOH HOH A . 
D 4 HOH 160 560 583 HOH HOH A . 
D 4 HOH 161 561 477 HOH HOH A . 
D 4 HOH 162 562 544 HOH HOH A . 
D 4 HOH 163 563 562 HOH HOH A . 
D 4 HOH 164 564 561 HOH HOH A . 
D 4 HOH 165 565 580 HOH HOH A . 
D 4 HOH 166 566 578 HOH HOH A . 
D 4 HOH 167 567 560 HOH HOH A . 
D 4 HOH 168 568 575 HOH HOH A . 
D 4 HOH 169 569 485 HOH HOH A . 
D 4 HOH 170 570 466 HOH HOH A . 
D 4 HOH 171 571 594 HOH HOH A . 
D 4 HOH 172 572 530 HOH HOH A . 
D 4 HOH 173 573 483 HOH HOH A . 
D 4 HOH 174 574 581 HOH HOH A . 
D 4 HOH 175 575 596 HOH HOH A . 
D 4 HOH 176 576 568 HOH HOH A . 
D 4 HOH 177 577 599 HOH HOH A . 
D 4 HOH 178 578 577 HOH HOH A . 
D 4 HOH 179 579 569 HOH HOH A . 
D 4 HOH 180 580 532 HOH HOH A . 
D 4 HOH 181 581 579 HOH HOH A . 
D 4 HOH 182 582 584 HOH HOH A . 
D 4 HOH 183 583 567 HOH HOH A . 
D 4 HOH 184 584 590 HOH HOH A . 
D 4 HOH 185 585 572 HOH HOH A . 
D 4 HOH 186 586 593 HOH HOH A . 
D 4 HOH 187 587 582 HOH HOH A . 
D 4 HOH 188 588 595 HOH HOH A . 
D 4 HOH 189 589 600 HOH HOH A . 
D 4 HOH 190 590 487 HOH HOH A . 
D 4 HOH 191 591 440 HOH HOH A . 
D 4 HOH 192 592 603 HOH HOH A . 
D 4 HOH 193 593 588 HOH HOH A . 
D 4 HOH 194 594 552 HOH HOH A . 
D 4 HOH 195 595 587 HOH HOH A . 
D 4 HOH 196 596 585 HOH HOH A . 
D 4 HOH 197 597 592 HOH HOH A . 
D 4 HOH 198 598 591 HOH HOH A . 
D 4 HOH 199 599 589 HOH HOH A . 
D 4 HOH 200 600 523 HOH HOH A . 
D 4 HOH 201 601 604 HOH HOH A . 
D 4 HOH 202 602 598 HOH HOH A . 
D 4 HOH 203 603 612 HOH HOH A . 
D 4 HOH 204 604 602 HOH HOH A . 
D 4 HOH 205 605 601 HOH HOH A . 
D 4 HOH 206 606 609 HOH HOH A . 
D 4 HOH 207 607 605 HOH HOH A . 
D 4 HOH 208 608 627 HOH HOH A . 
D 4 HOH 209 609 608 HOH HOH A . 
D 4 HOH 210 610 606 HOH HOH A . 
D 4 HOH 211 611 607 HOH HOH A . 
D 4 HOH 212 612 614 HOH HOH A . 
D 4 HOH 213 613 610 HOH HOH A . 
D 4 HOH 214 614 615 HOH HOH A . 
D 4 HOH 215 615 611 HOH HOH A . 
D 4 HOH 216 616 625 HOH HOH A . 
D 4 HOH 217 617 618 HOH HOH A . 
D 4 HOH 218 618 617 HOH HOH A . 
D 4 HOH 219 619 623 HOH HOH A . 
D 4 HOH 220 620 619 HOH HOH A . 
D 4 HOH 221 621 621 HOH HOH A . 
D 4 HOH 222 622 622 HOH HOH A . 
D 4 HOH 223 623 620 HOH HOH A . 
D 4 HOH 224 624 613 HOH HOH A . 
D 4 HOH 225 625 616 HOH HOH A . 
D 4 HOH 226 626 624 HOH HOH A . 
D 4 HOH 227 627 628 HOH HOH A . 
D 4 HOH 228 628 631 HOH HOH A . 
D 4 HOH 229 629 629 HOH HOH A . 
D 4 HOH 230 630 630 HOH HOH A . 
D 4 HOH 231 631 626 HOH HOH A . 
D 4 HOH 232 632 633 HOH HOH A . 
D 4 HOH 233 633 632 HOH HOH A . 
D 4 HOH 234 634 634 HOH HOH A . 
D 4 HOH 235 635 635 HOH HOH A . 
D 4 HOH 236 636 636 HOH HOH A . 
D 4 HOH 237 637 637 HOH HOH A . 
D 4 HOH 238 638 638 HOH HOH A . 
D 4 HOH 239 639 639 HOH HOH A . 
D 4 HOH 240 640 640 HOH HOH A . 
D 4 HOH 241 641 642 HOH HOH A . 
D 4 HOH 242 642 641 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0135 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0135 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.27 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9L30 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.911 
_cell.length_a_esd                 ? 
_cell.length_b                     41.155 
_cell.length_b_esd                 ? 
_cell.length_c                     72.232 
_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                         9L30 
_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                   9L30 
_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          40.33 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.8 
_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    '1.3 M sodium citrate, 50 mM Tris-HCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     140 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX225-HS' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-07-19 
_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                    'Si(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97934 
_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                        'PAL/PLS BEAMLINE 6D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97934 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   6D 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9L30 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.20 
_reflns.d_resolution_low                               30 
_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                                     74230 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.088 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   0.998 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.075 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.20 
_reflns_shell.d_res_low                                     1.22 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3551 
_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                               2.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.378 
_reflns_shell.pdbx_Rpim_I_all                               0.212 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.860 
_reflns_shell.pdbx_CC_star                                  0.962 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.310 
_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]                            0.49 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.23 
_refine.aniso_B[2][2]                            -0.05 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.29 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               14.592 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9L30 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.20 
_refine.ls_d_res_low                             30.00 
_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                     70539 
_refine.ls_number_reflns_R_free                  3675 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.47 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14650 
_refine.ls_R_factor_R_free                       0.17935 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14486 
_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               'FREE R-VALUE' 
_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                       0.039 
_refine.pdbx_overall_ESU_R_Free                  0.040 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_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                             1.348 
_refine.overall_SU_ML                            0.028 
_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                       1.20 
_refine_hist.d_res_low                        30.00 
_refine_hist.number_atoms_solvent             242 
_refine_hist.number_atoms_total               2305 
_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         14 
_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' ? 0.029  0.019  2230 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  2065 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.560  1.952  3041 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.228  3.000  4797 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.024  5.000  281  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 35.229 24.952 105  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.304 15.000 371  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 25.888 15.000 7    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.177  0.200  315  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  2574 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  517  ? 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' ? 2.317  1.142  1079 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.299  1.138  1078 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.632  1.721  1363 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.658  1.724  1364 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.922  1.456  1151 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.921  1.455  1150 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.744  2.051  1671 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.682  10.687 2704 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.226  10.285 2612 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 5.163  3.000  4295 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 36.783 5.000  63   ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 15.551 5.000  4398 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.201 
_refine_ls_shell.d_res_low                        1.232 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             259 
_refine_ls_shell.number_reflns_R_work             4995 
_refine_ls_shell.percent_reflns_obs               95.77 
_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                  0.188 
_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                  0.255 
# 
_struct.entry_id                     9L30 
_struct.title                        'Zn-Carbonic Anhydrase II complexed with 3NPA at 140 K' 
_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        9L30 
_struct_keywords.text            'Carbonic Anhydrase, enzyme mechanism, metalloenzymes, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_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              9L30 
_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_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 90    ? 
1 MORE         -33   ? 
1 'SSA (A^2)'  11680 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_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 ? ? ? ? ? ? ? 2.046 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D HOH . O  ? ? A ZN  301 A HOH 421 1_555 ? ? ? ? ? ? ? 1.952 ? ? 
# 
_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_555 108.9 ? 
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_555 112.2 ? 
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_555 103.4 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? D HOH .   ? A HOH 421 ? 1_555 107.3 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? D HOH .   ? A HOH 421 ? 1_555 110.6 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? D HOH .   ? A HOH 421 ? 1_555 114.3 ? 
# 
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 -0.42 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 18.71 
# 
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 LEU A 211 ? O LEU A 212 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 VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
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 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
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                   9L30 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    76 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    402 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLN 
_pdbx_validate_symm_contact.auth_seq_id_1     103 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    B 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NZ 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    LYS 
_pdbx_validate_symm_contact.auth_seq_id_2     133 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_545 
_pdbx_validate_symm_contact.dist              2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 CD A GLU 14  ? A OE2 A GLU 14  ? A 1.381 1.252 0.129  0.011 N 
2  1 CD A GLU 14  ? B OE2 A GLU 14  ? B 1.320 1.252 0.068  0.011 N 
3  1 CD A ARG 27  ? ? NE  A ARG 27  ? ? 1.619 1.460 0.159  0.017 N 
4  1 NE A ARG 27  ? ? CZ  A ARG 27  ? ? 1.241 1.326 -0.085 0.013 N 
5  1 CA A GLY 63  ? ? C   A GLY 63  ? ? 1.617 1.514 0.103  0.016 N 
6  1 CG A GLU 69  ? ? CD  A GLU 69  ? ? 1.422 1.515 -0.093 0.015 N 
7  1 N  A GLY 86  ? ? CA  A GLY 86  ? ? 1.352 1.456 -0.104 0.015 N 
8  1 CB A ARG 89  ? ? CG  A ARG 89  ? ? 1.333 1.521 -0.188 0.027 N 
9  1 N  A GLY 235 ? ? CA  A GLY 235 ? ? 1.327 1.456 -0.129 0.015 N 
10 1 CD A GLU 239 ? A OE1 A GLU 239 ? A 1.330 1.252 0.078  0.011 N 
11 1 CD A GLU 239 ? A OE2 A GLU 239 ? A 1.329 1.252 0.077  0.011 N 
12 1 C  A ASN 253 ? ? O   A ASN 253 ? ? 1.369 1.229 0.140  0.019 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 OE1 A GLU 14  ? A CD A GLU 14  ? A OE2 A GLU 14  ? A 134.98 123.30 11.68  1.20 N 
2  1 CA  A ARG 27  ? ? CB A ARG 27  ? ? CG  A ARG 27  ? ? 127.28 113.40 13.88  2.20 N 
3  1 CB  A LEU 47  ? A CG A LEU 47  ? A CD1 A LEU 47  ? A 99.61  111.00 -11.39 1.70 N 
4  1 CB  A ASP 52  ? ? CG A ASP 52  ? ? OD2 A ASP 52  ? ? 112.09 118.30 -6.21  0.90 N 
5  1 CA  A THR 55  ? ? CB A THR 55  ? ? CG2 A THR 55  ? ? 103.08 112.40 -9.32  1.40 N 
6  1 CB  A LEU 57  ? ? CG A LEU 57  ? ? CD1 A LEU 57  ? ? 100.08 111.00 -10.92 1.70 N 
7  1 CB  A LEU 57  ? ? CG A LEU 57  ? ? CD2 A LEU 57  ? ? 122.55 111.00 11.55  1.70 N 
8  1 NE  A ARG 58  ? ? CZ A ARG 58  ? ? NH2 A ARG 58  ? ? 116.78 120.30 -3.52  0.50 N 
9  1 N   A ASP 75  ? ? CA A ASP 75  ? ? CB  A ASP 75  ? ? 122.68 110.60 12.08  1.80 N 
10 1 CG  A ARG 89  ? ? CD A ARG 89  ? ? NE  A ARG 89  ? ? 84.44  111.80 -27.36 2.10 N 
11 1 NE  A ARG 89  ? ? CZ A ARG 89  ? ? NH2 A ARG 89  ? ? 115.22 120.30 -5.08  0.50 N 
12 1 CB  A LEU 100 ? ? CG A LEU 100 ? ? CD2 A LEU 100 ? ? 99.27  111.00 -11.73 1.70 N 
13 1 OD1 A ASP 130 ? ? CG A ASP 130 ? ? OD2 A ASP 130 ? ? 109.81 123.30 -13.49 1.90 N 
14 1 CB  A ASP 130 ? ? CG A ASP 130 ? ? OD1 A ASP 130 ? ? 127.16 118.30 8.86   0.90 N 
15 1 CB  A LEU 141 ? ? CG A LEU 141 ? ? CD2 A LEU 141 ? ? 124.87 111.00 13.87  1.70 N 
16 1 NE  A ARG 182 ? ? CZ A ARG 182 ? ? NH1 A ARG 182 ? ? 123.75 120.30 3.45   0.50 N 
17 1 NE  A ARG 182 ? ? CZ A ARG 182 ? ? NH2 A ARG 182 ? ? 116.92 120.30 -3.38  0.50 N 
18 1 CD  A LYS 213 ? ? CE A LYS 213 ? ? NZ  A LYS 213 ? ? 128.84 111.70 17.14  2.30 N 
19 1 CB  A PHE 226 ? ? CG A PHE 226 ? ? CD1 A PHE 226 ? ? 126.56 120.80 5.76   0.70 N 
20 1 NE  A ARG 246 ? ? CZ A ARG 246 ? ? NH1 A ARG 246 ? ? 123.92 120.30 3.62   0.50 N 
21 1 NE  A ARG 246 ? ? CZ A ARG 246 ? ? NH2 A ARG 246 ? ? 116.43 120.30 -3.87  0.50 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 ARG A 27  ? ? -140.33 51.65   
2 1 ALA A 65  ? ? -169.97 -167.60 
3 1 GLU A 106 ? ? -91.45  -61.95  
4 1 LYS A 111 ? ? 73.66   -1.83   
5 1 PHE A 176 ? ? -155.25 73.04   
6 1 ASN A 244 ? ? -96.10  46.99   
7 1 LYS A 252 ? ? 54.10   -135.34 
8 1 ASN A 253 ? ? -94.04  58.38   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     58 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.077 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 640 ? 5.87 . 
2 1 O ? A HOH 641 ? 6.01 . 
3 1 O ? A HOH 642 ? 6.39 . 
# 
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 HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N     N  N N 1   
ALA CA    C  N S 2   
ALA C     C  N N 3   
ALA O     O  N N 4   
ALA CB    C  N N 5   
ALA OXT   O  N N 6   
ALA H     H  N N 7   
ALA H2    H  N N 8   
ALA HA    H  N N 9   
ALA HB1   H  N N 10  
ALA HB2   H  N N 11  
ALA HB3   H  N N 12  
ALA HXT   H  N N 13  
ARG N     N  N N 14  
ARG CA    C  N S 15  
ARG C     C  N N 16  
ARG O     O  N N 17  
ARG CB    C  N N 18  
ARG CG    C  N N 19  
ARG CD    C  N N 20  
ARG NE    N  N N 21  
ARG CZ    C  N N 22  
ARG NH1   N  N N 23  
ARG NH2   N  N N 24  
ARG OXT   O  N N 25  
ARG H     H  N N 26  
ARG H2    H  N N 27  
ARG HA    H  N N 28  
ARG HB2   H  N N 29  
ARG HB3   H  N N 30  
ARG HG2   H  N N 31  
ARG HG3   H  N N 32  
ARG HD2   H  N N 33  
ARG HD3   H  N N 34  
ARG HE    H  N N 35  
ARG HH11  H  N N 36  
ARG HH12  H  N N 37  
ARG HH21  H  N N 38  
ARG HH22  H  N N 39  
ARG HXT   H  N N 40  
ASN N     N  N N 41  
ASN CA    C  N S 42  
ASN C     C  N N 43  
ASN O     O  N N 44  
ASN CB    C  N N 45  
ASN CG    C  N N 46  
ASN OD1   O  N N 47  
ASN ND2   N  N N 48  
ASN OXT   O  N N 49  
ASN H     H  N N 50  
ASN H2    H  N N 51  
ASN HA    H  N N 52  
ASN HB2   H  N N 53  
ASN HB3   H  N N 54  
ASN HD21  H  N N 55  
ASN HD22  H  N N 56  
ASN HXT   H  N N 57  
ASP N     N  N N 58  
ASP CA    C  N S 59  
ASP C     C  N N 60  
ASP O     O  N N 61  
ASP CB    C  N N 62  
ASP CG    C  N N 63  
ASP OD1   O  N N 64  
ASP OD2   O  N N 65  
ASP OXT   O  N N 66  
ASP H     H  N N 67  
ASP H2    H  N N 68  
ASP HA    H  N N 69  
ASP HB2   H  N N 70  
ASP HB3   H  N N 71  
ASP HD2   H  N N 72  
ASP HXT   H  N N 73  
CYS N     N  N N 74  
CYS CA    C  N R 75  
CYS C     C  N N 76  
CYS O     O  N N 77  
CYS CB    C  N N 78  
CYS SG    S  N N 79  
CYS OXT   O  N N 80  
CYS H     H  N N 81  
CYS H2    H  N N 82  
CYS HA    H  N N 83  
CYS HB2   H  N N 84  
CYS HB3   H  N N 85  
CYS HG    H  N N 86  
CYS HXT   H  N N 87  
GLN N     N  N N 88  
GLN CA    C  N S 89  
GLN C     C  N N 90  
GLN O     O  N N 91  
GLN CB    C  N N 92  
GLN CG    C  N N 93  
GLN CD    C  N N 94  
GLN OE1   O  N N 95  
GLN NE2   N  N N 96  
GLN OXT   O  N N 97  
GLN H     H  N N 98  
GLN H2    H  N N 99  
GLN HA    H  N N 100 
GLN HB2   H  N N 101 
GLN HB3   H  N N 102 
GLN HG2   H  N N 103 
GLN HG3   H  N N 104 
GLN HE21  H  N N 105 
GLN HE22  H  N N 106 
GLN HXT   H  N N 107 
GLU N     N  N N 108 
GLU CA    C  N S 109 
GLU C     C  N N 110 
GLU O     O  N N 111 
GLU CB    C  N N 112 
GLU CG    C  N N 113 
GLU CD    C  N N 114 
GLU OE1   O  N N 115 
GLU OE2   O  N N 116 
GLU OXT   O  N N 117 
GLU H     H  N N 118 
GLU H2    H  N N 119 
GLU HA    H  N N 120 
GLU HB2   H  N N 121 
GLU HB3   H  N N 122 
GLU HG2   H  N N 123 
GLU HG3   H  N N 124 
GLU HE2   H  N N 125 
GLU HXT   H  N N 126 
GLY N     N  N N 127 
GLY CA    C  N N 128 
GLY C     C  N N 129 
GLY O     O  N N 130 
GLY OXT   O  N N 131 
GLY H     H  N N 132 
GLY H2    H  N N 133 
GLY HA2   H  N N 134 
GLY HA3   H  N N 135 
GLY HXT   H  N N 136 
HIS N     N  N N 137 
HIS CA    C  N S 138 
HIS C     C  N N 139 
HIS O     O  N N 140 
HIS CB    C  N N 141 
HIS CG    C  Y N 142 
HIS ND1   N  Y N 143 
HIS CD2   C  Y N 144 
HIS CE1   C  Y N 145 
HIS NE2   N  Y N 146 
HIS OXT   O  N N 147 
HIS H     H  N N 148 
HIS H2    H  N N 149 
HIS HA    H  N N 150 
HIS HB2   H  N N 151 
HIS HB3   H  N N 152 
HIS HD1   H  N N 153 
HIS HD2   H  N N 154 
HIS HE1   H  N N 155 
HIS HE2   H  N N 156 
HIS HXT   H  N N 157 
HOH O     O  N N 158 
HOH H1    H  N N 159 
HOH H2    H  N N 160 
ILE N     N  N N 161 
ILE CA    C  N S 162 
ILE C     C  N N 163 
ILE O     O  N N 164 
ILE CB    C  N S 165 
ILE CG1   C  N N 166 
ILE CG2   C  N N 167 
ILE CD1   C  N N 168 
ILE OXT   O  N N 169 
ILE H     H  N N 170 
ILE H2    H  N N 171 
ILE HA    H  N N 172 
ILE HB    H  N N 173 
ILE HG12  H  N N 174 
ILE HG13  H  N N 175 
ILE HG21  H  N N 176 
ILE HG22  H  N N 177 
ILE HG23  H  N N 178 
ILE HD11  H  N N 179 
ILE HD12  H  N N 180 
ILE HD13  H  N N 181 
ILE HXT   H  N N 182 
LEU N     N  N N 183 
LEU CA    C  N S 184 
LEU C     C  N N 185 
LEU O     O  N N 186 
LEU CB    C  N N 187 
LEU CG    C  N N 188 
LEU CD1   C  N N 189 
LEU CD2   C  N N 190 
LEU OXT   O  N N 191 
LEU H     H  N N 192 
LEU H2    H  N N 193 
LEU HA    H  N N 194 
LEU HB2   H  N N 195 
LEU HB3   H  N N 196 
LEU HG    H  N N 197 
LEU HD11  H  N N 198 
LEU HD12  H  N N 199 
LEU HD13  H  N N 200 
LEU HD21  H  N N 201 
LEU HD22  H  N N 202 
LEU HD23  H  N N 203 
LEU HXT   H  N N 204 
LYS N     N  N N 205 
LYS CA    C  N S 206 
LYS C     C  N N 207 
LYS O     O  N N 208 
LYS CB    C  N N 209 
LYS CG    C  N N 210 
LYS CD    C  N N 211 
LYS CE    C  N N 212 
LYS NZ    N  N N 213 
LYS OXT   O  N N 214 
LYS H     H  N N 215 
LYS H2    H  N N 216 
LYS HA    H  N N 217 
LYS HB2   H  N N 218 
LYS HB3   H  N N 219 
LYS HG2   H  N N 220 
LYS HG3   H  N N 221 
LYS HD2   H  N N 222 
LYS HD3   H  N N 223 
LYS HE2   H  N N 224 
LYS HE3   H  N N 225 
LYS HZ1   H  N N 226 
LYS HZ2   H  N N 227 
LYS HZ3   H  N N 228 
LYS HXT   H  N N 229 
MET N     N  N N 230 
MET CA    C  N S 231 
MET C     C  N N 232 
MET O     O  N N 233 
MET CB    C  N N 234 
MET CG    C  N N 235 
MET SD    S  N N 236 
MET CE    C  N N 237 
MET OXT   O  N N 238 
MET H     H  N N 239 
MET H2    H  N N 240 
MET HA    H  N N 241 
MET HB2   H  N N 242 
MET HB3   H  N N 243 
MET HG2   H  N N 244 
MET HG3   H  N N 245 
MET HE1   H  N N 246 
MET HE2   H  N N 247 
MET HE3   H  N N 248 
MET HXT   H  N N 249 
MNP C1    C  N N 250 
MNP C2    C  N N 251 
MNP "C1'" C  Y N 252 
MNP "C2'" C  Y N 253 
MNP "C3'" C  Y N 254 
MNP "N3'" N  N N 255 
MNP "O3'" O  N N 256 
MNP "O4'" O  N N 257 
MNP "C4'" C  Y N 258 
MNP "C5'" C  Y N 259 
MNP "C6'" C  Y N 260 
MNP O1    O  N N 261 
MNP O2    O  N N 262 
MNP H21   H  N N 263 
MNP H22   H  N N 264 
MNP "H2'" H  N N 265 
MNP "H4'" H  N N 266 
MNP "H5'" H  N N 267 
MNP "H6'" H  N N 268 
MNP HO2   H  N N 269 
PHE N     N  N N 270 
PHE CA    C  N S 271 
PHE C     C  N N 272 
PHE O     O  N N 273 
PHE CB    C  N N 274 
PHE CG    C  Y N 275 
PHE CD1   C  Y N 276 
PHE CD2   C  Y N 277 
PHE CE1   C  Y N 278 
PHE CE2   C  Y N 279 
PHE CZ    C  Y N 280 
PHE OXT   O  N N 281 
PHE H     H  N N 282 
PHE H2    H  N N 283 
PHE HA    H  N N 284 
PHE HB2   H  N N 285 
PHE HB3   H  N N 286 
PHE HD1   H  N N 287 
PHE HD2   H  N N 288 
PHE HE1   H  N N 289 
PHE HE2   H  N N 290 
PHE HZ    H  N N 291 
PHE HXT   H  N N 292 
PRO N     N  N N 293 
PRO CA    C  N S 294 
PRO C     C  N N 295 
PRO O     O  N N 296 
PRO CB    C  N N 297 
PRO CG    C  N N 298 
PRO CD    C  N N 299 
PRO OXT   O  N N 300 
PRO H     H  N N 301 
PRO HA    H  N N 302 
PRO HB2   H  N N 303 
PRO HB3   H  N N 304 
PRO HG2   H  N N 305 
PRO HG3   H  N N 306 
PRO HD2   H  N N 307 
PRO HD3   H  N N 308 
PRO HXT   H  N N 309 
SER N     N  N N 310 
SER CA    C  N S 311 
SER C     C  N N 312 
SER O     O  N N 313 
SER CB    C  N N 314 
SER OG    O  N N 315 
SER OXT   O  N N 316 
SER H     H  N N 317 
SER H2    H  N N 318 
SER HA    H  N N 319 
SER HB2   H  N N 320 
SER HB3   H  N N 321 
SER HG    H  N N 322 
SER HXT   H  N N 323 
THR N     N  N N 324 
THR CA    C  N S 325 
THR C     C  N N 326 
THR O     O  N N 327 
THR CB    C  N R 328 
THR OG1   O  N N 329 
THR CG2   C  N N 330 
THR OXT   O  N N 331 
THR H     H  N N 332 
THR H2    H  N N 333 
THR HA    H  N N 334 
THR HB    H  N N 335 
THR HG1   H  N N 336 
THR HG21  H  N N 337 
THR HG22  H  N N 338 
THR HG23  H  N N 339 
THR HXT   H  N N 340 
TRP N     N  N N 341 
TRP CA    C  N S 342 
TRP C     C  N N 343 
TRP O     O  N N 344 
TRP CB    C  N N 345 
TRP CG    C  Y N 346 
TRP CD1   C  Y N 347 
TRP CD2   C  Y N 348 
TRP NE1   N  Y N 349 
TRP CE2   C  Y N 350 
TRP CE3   C  Y N 351 
TRP CZ2   C  Y N 352 
TRP CZ3   C  Y N 353 
TRP CH2   C  Y N 354 
TRP OXT   O  N N 355 
TRP H     H  N N 356 
TRP H2    H  N N 357 
TRP HA    H  N N 358 
TRP HB2   H  N N 359 
TRP HB3   H  N N 360 
TRP HD1   H  N N 361 
TRP HE1   H  N N 362 
TRP HE3   H  N N 363 
TRP HZ2   H  N N 364 
TRP HZ3   H  N N 365 
TRP HH2   H  N N 366 
TRP HXT   H  N N 367 
TYR N     N  N N 368 
TYR CA    C  N S 369 
TYR C     C  N N 370 
TYR O     O  N N 371 
TYR CB    C  N N 372 
TYR CG    C  Y N 373 
TYR CD1   C  Y N 374 
TYR CD2   C  Y N 375 
TYR CE1   C  Y N 376 
TYR CE2   C  Y N 377 
TYR CZ    C  Y N 378 
TYR OH    O  N N 379 
TYR OXT   O  N N 380 
TYR H     H  N N 381 
TYR H2    H  N N 382 
TYR HA    H  N N 383 
TYR HB2   H  N N 384 
TYR HB3   H  N N 385 
TYR HD1   H  N N 386 
TYR HD2   H  N N 387 
TYR HE1   H  N N 388 
TYR HE2   H  N N 389 
TYR HH    H  N N 390 
TYR HXT   H  N N 391 
VAL N     N  N N 392 
VAL CA    C  N S 393 
VAL C     C  N N 394 
VAL O     O  N N 395 
VAL CB    C  N N 396 
VAL CG1   C  N N 397 
VAL CG2   C  N N 398 
VAL OXT   O  N N 399 
VAL H     H  N N 400 
VAL H2    H  N N 401 
VAL HA    H  N N 402 
VAL HB    H  N N 403 
VAL HG11  H  N N 404 
VAL HG12  H  N N 405 
VAL HG13  H  N N 406 
VAL HG21  H  N N 407 
VAL HG22  H  N N 408 
VAL HG23  H  N N 409 
VAL HXT   H  N N 410 
ZN  ZN    ZN N N 411 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA    sing N N 1   
ALA N     H     sing N N 2   
ALA N     H2    sing N N 3   
ALA CA    C     sing N N 4   
ALA CA    CB    sing N N 5   
ALA CA    HA    sing N N 6   
ALA C     O     doub N N 7   
ALA C     OXT   sing N N 8   
ALA CB    HB1   sing N N 9   
ALA CB    HB2   sing N N 10  
ALA CB    HB3   sing N N 11  
ALA OXT   HXT   sing N N 12  
ARG N     CA    sing N N 13  
ARG N     H     sing N N 14  
ARG N     H2    sing N N 15  
ARG CA    C     sing N N 16  
ARG CA    CB    sing N N 17  
ARG CA    HA    sing N N 18  
ARG C     O     doub N N 19  
ARG C     OXT   sing N N 20  
ARG CB    CG    sing N N 21  
ARG CB    HB2   sing N N 22  
ARG CB    HB3   sing N N 23  
ARG CG    CD    sing N N 24  
ARG CG    HG2   sing N N 25  
ARG CG    HG3   sing N N 26  
ARG CD    NE    sing N N 27  
ARG CD    HD2   sing N N 28  
ARG CD    HD3   sing N N 29  
ARG NE    CZ    sing N N 30  
ARG NE    HE    sing N N 31  
ARG CZ    NH1   sing N N 32  
ARG CZ    NH2   doub N N 33  
ARG NH1   HH11  sing N N 34  
ARG NH1   HH12  sing N N 35  
ARG NH2   HH21  sing N N 36  
ARG NH2   HH22  sing N N 37  
ARG OXT   HXT   sing N N 38  
ASN N     CA    sing N N 39  
ASN N     H     sing N N 40  
ASN N     H2    sing N N 41  
ASN CA    C     sing N N 42  
ASN CA    CB    sing N N 43  
ASN CA    HA    sing N N 44  
ASN C     O     doub N N 45  
ASN C     OXT   sing N N 46  
ASN CB    CG    sing N N 47  
ASN CB    HB2   sing N N 48  
ASN CB    HB3   sing N N 49  
ASN CG    OD1   doub N N 50  
ASN CG    ND2   sing N N 51  
ASN ND2   HD21  sing N N 52  
ASN ND2   HD22  sing N N 53  
ASN OXT   HXT   sing N N 54  
ASP N     CA    sing N N 55  
ASP N     H     sing N N 56  
ASP N     H2    sing N N 57  
ASP CA    C     sing N N 58  
ASP CA    CB    sing N N 59  
ASP CA    HA    sing N N 60  
ASP C     O     doub N N 61  
ASP C     OXT   sing N N 62  
ASP CB    CG    sing N N 63  
ASP CB    HB2   sing N N 64  
ASP CB    HB3   sing N N 65  
ASP CG    OD1   doub N N 66  
ASP CG    OD2   sing N N 67  
ASP OD2   HD2   sing N N 68  
ASP OXT   HXT   sing N N 69  
CYS N     CA    sing N N 70  
CYS N     H     sing N N 71  
CYS N     H2    sing N N 72  
CYS CA    C     sing N N 73  
CYS CA    CB    sing N N 74  
CYS CA    HA    sing N N 75  
CYS C     O     doub N N 76  
CYS C     OXT   sing N N 77  
CYS CB    SG    sing N N 78  
CYS CB    HB2   sing N N 79  
CYS CB    HB3   sing N N 80  
CYS SG    HG    sing N N 81  
CYS OXT   HXT   sing N N 82  
GLN N     CA    sing N N 83  
GLN N     H     sing N N 84  
GLN N     H2    sing N N 85  
GLN CA    C     sing N N 86  
GLN CA    CB    sing N N 87  
GLN CA    HA    sing N N 88  
GLN C     O     doub N N 89  
GLN C     OXT   sing N N 90  
GLN CB    CG    sing N N 91  
GLN CB    HB2   sing N N 92  
GLN CB    HB3   sing N N 93  
GLN CG    CD    sing N N 94  
GLN CG    HG2   sing N N 95  
GLN CG    HG3   sing N N 96  
GLN CD    OE1   doub N N 97  
GLN CD    NE2   sing N N 98  
GLN NE2   HE21  sing N N 99  
GLN NE2   HE22  sing N N 100 
GLN OXT   HXT   sing N N 101 
GLU N     CA    sing N N 102 
GLU N     H     sing N N 103 
GLU N     H2    sing N N 104 
GLU CA    C     sing N N 105 
GLU CA    CB    sing N N 106 
GLU CA    HA    sing N N 107 
GLU C     O     doub N N 108 
GLU C     OXT   sing N N 109 
GLU CB    CG    sing N N 110 
GLU CB    HB2   sing N N 111 
GLU CB    HB3   sing N N 112 
GLU CG    CD    sing N N 113 
GLU CG    HG2   sing N N 114 
GLU CG    HG3   sing N N 115 
GLU CD    OE1   doub N N 116 
GLU CD    OE2   sing N N 117 
GLU OE2   HE2   sing N N 118 
GLU OXT   HXT   sing N N 119 
GLY N     CA    sing N N 120 
GLY N     H     sing N N 121 
GLY N     H2    sing N N 122 
GLY CA    C     sing N N 123 
GLY CA    HA2   sing N N 124 
GLY CA    HA3   sing N N 125 
GLY C     O     doub N N 126 
GLY C     OXT   sing N N 127 
GLY OXT   HXT   sing N N 128 
HIS N     CA    sing N N 129 
HIS N     H     sing N N 130 
HIS N     H2    sing N N 131 
HIS CA    C     sing N N 132 
HIS CA    CB    sing N N 133 
HIS CA    HA    sing N N 134 
HIS C     O     doub N N 135 
HIS C     OXT   sing N N 136 
HIS CB    CG    sing N N 137 
HIS CB    HB2   sing N N 138 
HIS CB    HB3   sing N N 139 
HIS CG    ND1   sing Y N 140 
HIS CG    CD2   doub Y N 141 
HIS ND1   CE1   doub Y N 142 
HIS ND1   HD1   sing N N 143 
HIS CD2   NE2   sing Y N 144 
HIS CD2   HD2   sing N N 145 
HIS CE1   NE2   sing Y N 146 
HIS CE1   HE1   sing N N 147 
HIS NE2   HE2   sing N N 148 
HIS OXT   HXT   sing N N 149 
HOH O     H1    sing N N 150 
HOH O     H2    sing N N 151 
ILE N     CA    sing N N 152 
ILE N     H     sing N N 153 
ILE N     H2    sing N N 154 
ILE CA    C     sing N N 155 
ILE CA    CB    sing N N 156 
ILE CA    HA    sing N N 157 
ILE C     O     doub N N 158 
ILE C     OXT   sing N N 159 
ILE CB    CG1   sing N N 160 
ILE CB    CG2   sing N N 161 
ILE CB    HB    sing N N 162 
ILE CG1   CD1   sing N N 163 
ILE CG1   HG12  sing N N 164 
ILE CG1   HG13  sing N N 165 
ILE CG2   HG21  sing N N 166 
ILE CG2   HG22  sing N N 167 
ILE CG2   HG23  sing N N 168 
ILE CD1   HD11  sing N N 169 
ILE CD1   HD12  sing N N 170 
ILE CD1   HD13  sing N N 171 
ILE OXT   HXT   sing N N 172 
LEU N     CA    sing N N 173 
LEU N     H     sing N N 174 
LEU N     H2    sing N N 175 
LEU CA    C     sing N N 176 
LEU CA    CB    sing N N 177 
LEU CA    HA    sing N N 178 
LEU C     O     doub N N 179 
LEU C     OXT   sing N N 180 
LEU CB    CG    sing N N 181 
LEU CB    HB2   sing N N 182 
LEU CB    HB3   sing N N 183 
LEU CG    CD1   sing N N 184 
LEU CG    CD2   sing N N 185 
LEU CG    HG    sing N N 186 
LEU CD1   HD11  sing N N 187 
LEU CD1   HD12  sing N N 188 
LEU CD1   HD13  sing N N 189 
LEU CD2   HD21  sing N N 190 
LEU CD2   HD22  sing N N 191 
LEU CD2   HD23  sing N N 192 
LEU OXT   HXT   sing N N 193 
LYS N     CA    sing N N 194 
LYS N     H     sing N N 195 
LYS N     H2    sing N N 196 
LYS CA    C     sing N N 197 
LYS CA    CB    sing N N 198 
LYS CA    HA    sing N N 199 
LYS C     O     doub N N 200 
LYS C     OXT   sing N N 201 
LYS CB    CG    sing N N 202 
LYS CB    HB2   sing N N 203 
LYS CB    HB3   sing N N 204 
LYS CG    CD    sing N N 205 
LYS CG    HG2   sing N N 206 
LYS CG    HG3   sing N N 207 
LYS CD    CE    sing N N 208 
LYS CD    HD2   sing N N 209 
LYS CD    HD3   sing N N 210 
LYS CE    NZ    sing N N 211 
LYS CE    HE2   sing N N 212 
LYS CE    HE3   sing N N 213 
LYS NZ    HZ1   sing N N 214 
LYS NZ    HZ2   sing N N 215 
LYS NZ    HZ3   sing N N 216 
LYS OXT   HXT   sing N N 217 
MET N     CA    sing N N 218 
MET N     H     sing N N 219 
MET N     H2    sing N N 220 
MET CA    C     sing N N 221 
MET CA    CB    sing N N 222 
MET CA    HA    sing N N 223 
MET C     O     doub N N 224 
MET C     OXT   sing N N 225 
MET CB    CG    sing N N 226 
MET CB    HB2   sing N N 227 
MET CB    HB3   sing N N 228 
MET CG    SD    sing N N 229 
MET CG    HG2   sing N N 230 
MET CG    HG3   sing N N 231 
MET SD    CE    sing N N 232 
MET CE    HE1   sing N N 233 
MET CE    HE2   sing N N 234 
MET CE    HE3   sing N N 235 
MET OXT   HXT   sing N N 236 
MNP C1    C2    sing N N 237 
MNP C1    O1    doub N N 238 
MNP C1    O2    sing N N 239 
MNP C2    "C1'" sing N N 240 
MNP C2    H21   sing N N 241 
MNP C2    H22   sing N N 242 
MNP "C1'" "C2'" doub Y N 243 
MNP "C1'" "C6'" sing Y N 244 
MNP "C2'" "C3'" sing Y N 245 
MNP "C2'" "H2'" sing N N 246 
MNP "C3'" "N3'" sing N N 247 
MNP "C3'" "C4'" doub Y N 248 
MNP "N3'" "O3'" sing N N 249 
MNP "N3'" "O4'" doub N N 250 
MNP "C4'" "C5'" sing Y N 251 
MNP "C4'" "H4'" sing N N 252 
MNP "C5'" "C6'" doub Y N 253 
MNP "C5'" "H5'" sing N N 254 
MNP "C6'" "H6'" sing N N 255 
MNP O2    HO2   sing N N 256 
PHE N     CA    sing N N 257 
PHE N     H     sing N N 258 
PHE N     H2    sing N N 259 
PHE CA    C     sing N N 260 
PHE CA    CB    sing N N 261 
PHE CA    HA    sing N N 262 
PHE C     O     doub N N 263 
PHE C     OXT   sing N N 264 
PHE CB    CG    sing N N 265 
PHE CB    HB2   sing N N 266 
PHE CB    HB3   sing N N 267 
PHE CG    CD1   doub Y N 268 
PHE CG    CD2   sing Y N 269 
PHE CD1   CE1   sing Y N 270 
PHE CD1   HD1   sing N N 271 
PHE CD2   CE2   doub Y N 272 
PHE CD2   HD2   sing N N 273 
PHE CE1   CZ    doub Y N 274 
PHE CE1   HE1   sing N N 275 
PHE CE2   CZ    sing Y N 276 
PHE CE2   HE2   sing N N 277 
PHE CZ    HZ    sing N N 278 
PHE OXT   HXT   sing N N 279 
PRO N     CA    sing N N 280 
PRO N     CD    sing N N 281 
PRO N     H     sing N N 282 
PRO CA    C     sing N N 283 
PRO CA    CB    sing N N 284 
PRO CA    HA    sing N N 285 
PRO C     O     doub N N 286 
PRO C     OXT   sing N N 287 
PRO CB    CG    sing N N 288 
PRO CB    HB2   sing N N 289 
PRO CB    HB3   sing N N 290 
PRO CG    CD    sing N N 291 
PRO CG    HG2   sing N N 292 
PRO CG    HG3   sing N N 293 
PRO CD    HD2   sing N N 294 
PRO CD    HD3   sing N N 295 
PRO OXT   HXT   sing N N 296 
SER N     CA    sing N N 297 
SER N     H     sing N N 298 
SER N     H2    sing N N 299 
SER CA    C     sing N N 300 
SER CA    CB    sing N N 301 
SER CA    HA    sing N N 302 
SER C     O     doub N N 303 
SER C     OXT   sing N N 304 
SER CB    OG    sing N N 305 
SER CB    HB2   sing N N 306 
SER CB    HB3   sing N N 307 
SER OG    HG    sing N N 308 
SER OXT   HXT   sing N N 309 
THR N     CA    sing N N 310 
THR N     H     sing N N 311 
THR N     H2    sing N N 312 
THR CA    C     sing N N 313 
THR CA    CB    sing N N 314 
THR CA    HA    sing N N 315 
THR C     O     doub N N 316 
THR C     OXT   sing N N 317 
THR CB    OG1   sing N N 318 
THR CB    CG2   sing N N 319 
THR CB    HB    sing N N 320 
THR OG1   HG1   sing N N 321 
THR CG2   HG21  sing N N 322 
THR CG2   HG22  sing N N 323 
THR CG2   HG23  sing N N 324 
THR OXT   HXT   sing N N 325 
TRP N     CA    sing N N 326 
TRP N     H     sing N N 327 
TRP N     H2    sing N N 328 
TRP CA    C     sing N N 329 
TRP CA    CB    sing N N 330 
TRP CA    HA    sing N N 331 
TRP C     O     doub N N 332 
TRP C     OXT   sing N N 333 
TRP CB    CG    sing N N 334 
TRP CB    HB2   sing N N 335 
TRP CB    HB3   sing N N 336 
TRP CG    CD1   doub Y N 337 
TRP CG    CD2   sing Y N 338 
TRP CD1   NE1   sing Y N 339 
TRP CD1   HD1   sing N N 340 
TRP CD2   CE2   doub Y N 341 
TRP CD2   CE3   sing Y N 342 
TRP NE1   CE2   sing Y N 343 
TRP NE1   HE1   sing N N 344 
TRP CE2   CZ2   sing Y N 345 
TRP CE3   CZ3   doub Y N 346 
TRP CE3   HE3   sing N N 347 
TRP CZ2   CH2   doub Y N 348 
TRP CZ2   HZ2   sing N N 349 
TRP CZ3   CH2   sing Y N 350 
TRP CZ3   HZ3   sing N N 351 
TRP CH2   HH2   sing N N 352 
TRP OXT   HXT   sing N N 353 
TYR N     CA    sing N N 354 
TYR N     H     sing N N 355 
TYR N     H2    sing N N 356 
TYR CA    C     sing N N 357 
TYR CA    CB    sing N N 358 
TYR CA    HA    sing N N 359 
TYR C     O     doub N N 360 
TYR C     OXT   sing N N 361 
TYR CB    CG    sing N N 362 
TYR CB    HB2   sing N N 363 
TYR CB    HB3   sing N N 364 
TYR CG    CD1   doub Y N 365 
TYR CG    CD2   sing Y N 366 
TYR CD1   CE1   sing Y N 367 
TYR CD1   HD1   sing N N 368 
TYR CD2   CE2   doub Y N 369 
TYR CD2   HD2   sing N N 370 
TYR CE1   CZ    doub Y N 371 
TYR CE1   HE1   sing N N 372 
TYR CE2   CZ    sing Y N 373 
TYR CE2   HE2   sing N N 374 
TYR CZ    OH    sing N N 375 
TYR OH    HH    sing N N 376 
TYR OXT   HXT   sing N N 377 
VAL N     CA    sing N N 378 
VAL N     H     sing N N 379 
VAL N     H2    sing N N 380 
VAL CA    C     sing N N 381 
VAL CA    CB    sing N N 382 
VAL CA    HA    sing N N 383 
VAL C     O     doub N N 384 
VAL C     OXT   sing N N 385 
VAL CB    CG1   sing N N 386 
VAL CB    CG2   sing N N 387 
VAL CB    HB    sing N N 388 
VAL CG1   HG11  sing N N 389 
VAL CG1   HG12  sing N N 390 
VAL CG1   HG13  sing N N 391 
VAL CG2   HG21  sing N N 392 
VAL CG2   HG22  sing N N 393 
VAL CG2   HG23  sing N N 394 
VAL OXT   HXT   sing N N 395 
# 
_pdbx_audit_support.funding_organization   'Samsung Science and Technology Foundation' 
_pdbx_audit_support.country                'Korea, Republic Of' 
_pdbx_audit_support.grant_number           SSTF-BA1702-04 
_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   7Y2A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9L30 
_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]   0.023860 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006070 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024298 
_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]   0.014285 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
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 4   ? 32.004  1.455   8.139   1.00 36.16  ? 4   HIS A N     1 
ATOM   2    C  CA    . HIS A 1 4   ? 30.885  2.006   8.944   1.00 33.74  ? 4   HIS A CA    1 
ATOM   3    C  C     . HIS A 1 4   ? 30.129  0.874   9.564   1.00 18.96  ? 4   HIS A C     1 
ATOM   4    O  O     . HIS A 1 4   ? 30.303  -0.301  9.250   1.00 20.55  ? 4   HIS A O     1 
ATOM   5    C  CB    . HIS A 1 4   ? 30.018  3.027   8.145   1.00 50.22  ? 4   HIS A CB    1 
ATOM   6    C  CG    . HIS A 1 4   ? 30.527  4.449   8.231   1.00 66.97  ? 4   HIS A CG    1 
ATOM   7    N  ND1   . HIS A 1 4   ? 30.307  5.261   9.331   1.00 70.56  ? 4   HIS A ND1   1 
ATOM   8    C  CD2   . HIS A 1 4   ? 31.310  5.177   7.389   1.00 77.37  ? 4   HIS A CD2   1 
ATOM   9    C  CE1   . HIS A 1 4   ? 30.927  6.421   9.165   1.00 79.67  ? 4   HIS A CE1   1 
ATOM   10   N  NE2   . HIS A 1 4   ? 31.555  6.394   7.999   1.00 73.32  ? 4   HIS A NE2   1 
ATOM   11   N  N     . TRP A 1 5   ? 29.311  1.217   10.510  1.00 17.35  ? 5   TRP A N     1 
ATOM   12   C  CA    . TRP A 1 5   ? 28.607  0.205   11.328  1.00 13.72  ? 5   TRP A CA    1 
ATOM   13   C  C     . TRP A 1 5   ? 27.607  -0.611  10.538  1.00 14.29  ? 5   TRP A C     1 
ATOM   14   O  O     . TRP A 1 5   ? 27.095  -0.141  9.527   1.00 15.82  ? 5   TRP A O     1 
ATOM   15   C  CB    . TRP A 1 5   ? 27.949  0.867   12.493  1.00 13.39  ? 5   TRP A CB    1 
ATOM   16   C  CG    . TRP A 1 5   ? 26.785  1.708   12.146  1.00 13.93  ? 5   TRP A CG    1 
ATOM   17   C  CD1   . TRP A 1 5   ? 26.820  3.031   11.841  1.00 15.97  ? 5   TRP A CD1   1 
ATOM   18   C  CD2   . TRP A 1 5   ? 25.404  1.318   12.039  1.00 11.96  ? 5   TRP A CD2   1 
ATOM   19   N  NE1   . TRP A 1 5   ? 25.573  3.498   11.632  1.00 14.17  ? 5   TRP A NE1   1 
ATOM   20   C  CE2   . TRP A 1 5   ? 24.692  2.451   11.690  1.00 12.60  ? 5   TRP A CE2   1 
ATOM   21   C  CE3   . TRP A 1 5   ? 24.725  0.095   12.257  1.00 11.33  ? 5   TRP A CE3   1 
ATOM   22   C  CZ2   . TRP A 1 5   ? 23.292  2.439   11.550  1.00 14.84  ? 5   TRP A CZ2   1 
ATOM   23   C  CZ3   . TRP A 1 5   ? 23.335  0.086   12.052  1.00 12.75  ? 5   TRP A CZ3   1 
ATOM   24   C  CH2   . TRP A 1 5   ? 22.684  1.232   11.710  1.00 12.68  ? 5   TRP A CH2   1 
ATOM   25   N  N     . GLY A 1 6   ? 27.371  -1.815  11.019  1.00 12.34  ? 6   GLY A N     1 
ATOM   26   C  CA    . GLY A 1 6   ? 26.344  -2.676  10.383  1.00 13.15  ? 6   GLY A CA    1 
ATOM   27   C  C     . GLY A 1 6   ? 25.995  -3.811  11.338  1.00 11.64  ? 6   GLY A C     1 
ATOM   28   O  O     . GLY A 1 6   ? 25.975  -3.629  12.554  1.00 12.30  ? 6   GLY A O     1 
ATOM   29   N  N     . TYR A 1 7   ? 25.702  -4.948  10.741  1.00 12.58  ? 7   TYR A N     1 
ATOM   30   C  CA    . TYR A 1 7   ? 25.342  -6.117  11.537  1.00 14.40  ? 7   TYR A CA    1 
ATOM   31   C  C     . TYR A 1 7   ? 26.206  -7.383  11.384  1.00 21.10  ? 7   TYR A C     1 
ATOM   32   O  O     . TYR A 1 7   ? 25.883  -8.457  11.929  1.00 38.49  ? 7   TYR A O     1 
ATOM   33   C  CB    . TYR A 1 7   ? 23.817  -6.448  11.297  1.00 12.69  ? 7   TYR A CB    1 
ATOM   34   C  CG    . TYR A 1 7   ? 22.900  -5.363  11.800  1.00 9.51   ? 7   TYR A CG    1 
ATOM   35   C  CD1   . TYR A 1 7   ? 22.522  -5.375  13.117  1.00 9.04   ? 7   TYR A CD1   1 
ATOM   36   C  CD2   . TYR A 1 7   ? 22.484  -4.355  11.002  1.00 10.56  ? 7   TYR A CD2   1 
ATOM   37   C  CE1   . TYR A 1 7   ? 21.665  -4.399  13.589  1.00 7.45   ? 7   TYR A CE1   1 
ATOM   38   C  CE2   . TYR A 1 7   ? 21.619  -3.369  11.458  1.00 9.25   ? 7   TYR A CE2   1 
ATOM   39   C  CZ    . TYR A 1 7   ? 21.231  -3.369  12.789  1.00 7.42   ? 7   TYR A CZ    1 
ATOM   40   O  OH    . TYR A 1 7   ? 20.392  -2.393  13.210  1.00 8.12   ? 7   TYR A OH    1 
ATOM   41   N  N     . GLY A 1 8   ? 27.328  -7.212  10.709  1.00 22.27  ? 8   GLY A N     1 
ATOM   42   C  CA    . GLY A 1 8   ? 28.359  -8.311  10.563  1.00 23.30  ? 8   GLY A CA    1 
ATOM   43   C  C     . GLY A 1 8   ? 29.277  -8.620  11.703  1.00 26.59  ? 8   GLY A C     1 
ATOM   44   O  O     . GLY A 1 8   ? 29.446  -7.870  12.716  1.00 30.59  ? 8   GLY A O     1 
ATOM   45   N  N     . LYS A 1 9   ? 30.122  -9.580  11.382  1.00 30.89  ? 9   LYS A N     1 
ATOM   46   C  CA    . LYS A 1 9   ? 31.169  -9.994  12.327  1.00 37.14  ? 9   LYS A CA    1 
ATOM   47   C  C     . LYS A 1 9   ? 32.104  -8.867  12.636  1.00 33.15  ? 9   LYS A C     1 
ATOM   48   O  O     . LYS A 1 9   ? 32.584  -8.713  13.815  1.00 24.49  ? 9   LYS A O     1 
ATOM   49   C  CB    . LYS A 1 9   ? 31.960  -11.076 11.730  1.00 30.50  ? 9   LYS A CB    1 
ATOM   50   C  CG    . LYS A 1 9   ? 31.277  -12.423 11.870  1.00 60.05  ? 9   LYS A CG    1 
ATOM   51   C  CD    . LYS A 1 9   ? 31.647  -13.360 10.730  1.00 72.83  ? 9   LYS A CD    1 
ATOM   52   C  CE    . LYS A 1 9   ? 31.032  -14.733 10.943  1.00 68.57  ? 9   LYS A CE    1 
ATOM   53   N  NZ    . LYS A 1 9   ? 30.663  -15.339 9.641   1.00 69.65  ? 9   LYS A NZ    1 
ATOM   54   N  N     . HIS A 1 10  ? 32.354  -8.063  11.585  1.00 26.78  ? 10  HIS A N     1 
ATOM   55   C  CA    . HIS A 1 10  ? 33.361  -7.096  11.713  1.00 24.45  ? 10  HIS A CA    1 
ATOM   56   C  C     . HIS A 1 10  ? 32.855  -5.766  12.035  1.00 18.61  ? 10  HIS A C     1 
ATOM   57   O  O     . HIS A 1 10  ? 33.673  -4.989  12.473  1.00 19.68  ? 10  HIS A O     1 
ATOM   58   C  CB    . HIS A 1 10  ? 34.259  -7.047  10.492  1.00 22.55  ? 10  HIS A CB    1 
ATOM   59   C  CG    . HIS A 1 10  ? 34.926  -8.366  10.263  1.00 29.32  ? 10  HIS A CG    1 
ATOM   60   N  ND1   . HIS A 1 10  ? 35.972  -8.834  11.033  1.00 34.08  ? 10  HIS A ND1   1 
ATOM   61   C  CD2   . HIS A 1 10  ? 34.574  -9.382  9.461   1.00 30.92  ? 10  HIS A CD2   1 
ATOM   62   C  CE1   . HIS A 1 10  ? 36.323  -10.032 10.619  1.00 44.50  ? 10  HIS A CE1   1 
ATOM   63   N  NE2   . HIS A 1 10  ? 35.471  -10.378 9.664   1.00 29.99  ? 10  HIS A NE2   1 
ATOM   64   N  N     . ASN A 1 11  ? 31.525  -5.553  11.919  1.00 18.23  ? 11  ASN A N     1 
ATOM   65   C  CA    . ASN A 1 11  ? 31.027  -4.193  12.138  1.00 15.10  ? 11  ASN A CA    1 
ATOM   66   C  C     . ASN A 1 11  ? 29.701  -4.166  12.931  1.00 14.68  ? 11  ASN A C     1 
ATOM   67   O  O     . ASN A 1 11  ? 29.029  -3.149  12.980  1.00 15.46  ? 11  ASN A O     1 
ATOM   68   C  CB    . ASN A 1 11  ? 30.853  -3.462  10.811  1.00 13.96  ? 11  ASN A CB    1 
ATOM   69   C  CG    . ASN A 1 11  ? 29.762  -4.058  9.932   1.00 16.87  ? 11  ASN A CG    1 
ATOM   70   O  OD1   . ASN A 1 11  ? 29.114  -5.015  10.263  1.00 19.26  ? 11  ASN A OD1   1 
ATOM   71   N  ND2   . ASN A 1 11  ? 29.543  -3.452  8.803   1.00 19.63  ? 11  ASN A ND2   1 
ATOM   72   N  N     . GLY A 1 12  ? 29.378  -5.283  13.562  1.00 14.03  ? 12  GLY A N     1 
ATOM   73   C  CA    . GLY A 1 12  ? 28.072  -5.435  14.160  1.00 13.62  ? 12  GLY A CA    1 
ATOM   74   C  C     . GLY A 1 12  ? 28.017  -4.865  15.556  1.00 12.73  ? 12  GLY A C     1 
ATOM   75   O  O     . GLY A 1 12  ? 28.944  -4.186  16.040  1.00 12.35  ? 12  GLY A O     1 
ATOM   76   N  N     . PRO A 1 13  ? 26.919  -5.149  16.266  1.00 11.57  ? 13  PRO A N     1 
ATOM   77   C  CA    . PRO A 1 13  ? 26.668  -4.550  17.541  1.00 11.20  ? 13  PRO A CA    1 
ATOM   78   C  C     . PRO A 1 13  ? 27.791  -4.558  18.552  1.00 10.67  ? 13  PRO A C     1 
ATOM   79   O  O     . PRO A 1 13  ? 27.897  -3.613  19.332  1.00 11.59  ? 13  PRO A O     1 
ATOM   80   C  CB    . PRO A 1 13  ? 25.479  -5.320  18.071  1.00 12.11  ? 13  PRO A CB    1 
ATOM   81   C  CG    . PRO A 1 13  ? 24.715  -5.646  16.820  1.00 12.78  ? 13  PRO A CG    1 
ATOM   82   C  CD    . PRO A 1 13  ? 25.758  -5.915  15.799  1.00 12.66  ? 13  PRO A CD    1 
ATOM   83   N  N     A GLU A 1 14  ? 28.596  -5.610  18.492  0.50 13.49  ? 14  GLU A N     1 
ATOM   84   N  N     B GLU A 1 14  ? 28.625  -5.617  18.664  0.50 12.57  ? 14  GLU A N     1 
ATOM   85   C  CA    A GLU A 1 14  ? 29.619  -5.776  19.456  0.50 14.51  ? 14  GLU A CA    1 
ATOM   86   C  CA    B GLU A 1 14  ? 29.738  -5.603  19.685  0.50 12.79  ? 14  GLU A CA    1 
ATOM   87   C  C     A GLU A 1 14  ? 30.807  -4.818  19.214  0.50 12.60  ? 14  GLU A C     1 
ATOM   88   C  C     B GLU A 1 14  ? 30.832  -4.662  19.297  0.50 11.56  ? 14  GLU A C     1 
ATOM   89   O  O     A GLU A 1 14  ? 31.660  -4.633  20.096  0.50 15.08  ? 14  GLU A O     1 
ATOM   90   O  O     B GLU A 1 14  ? 31.738  -4.425  20.126  0.50 13.47  ? 14  GLU A O     1 
ATOM   91   C  CB    A GLU A 1 14  ? 29.868  -7.268  19.489  0.50 17.68  ? 14  GLU A CB    1 
ATOM   92   C  CB    B GLU A 1 14  ? 30.331  -6.963  19.902  0.50 14.71  ? 14  GLU A CB    1 
ATOM   93   C  CG    A GLU A 1 14  ? 30.670  -7.918  18.400  0.50 15.44  ? 14  GLU A CG    1 
ATOM   94   C  CG    B GLU A 1 14  ? 29.334  -8.140  20.221  0.50 16.73  ? 14  GLU A CG    1 
ATOM   95   C  CD    A GLU A 1 14  ? 30.021  -8.252  17.013  0.50 16.89  ? 14  GLU A CD    1 
ATOM   96   C  CD    B GLU A 1 14  ? 28.308  -7.770  21.323  0.50 17.43  ? 14  GLU A CD    1 
ATOM   97   O  OE1   A GLU A 1 14  ? 28.908  -7.684  16.769  0.50 12.30  ? 14  GLU A OE1   1 
ATOM   98   O  OE1   B GLU A 1 14  ? 28.812  -7.470  22.407  0.50 20.97  ? 14  GLU A OE1   1 
ATOM   99   O  OE2   A GLU A 1 14  ? 30.901  -9.028  16.285  0.50 16.35  ? 14  GLU A OE2   1 
ATOM   100  O  OE2   B GLU A 1 14  ? 27.000  -7.686  21.165  0.50 21.42  ? 14  GLU A OE2   1 
ATOM   101  N  N     . HIS A 1 15  ? 30.812  -4.140  18.070  1.00 11.57  ? 15  HIS A N     1 
ATOM   102  C  CA    . HIS A 1 15  ? 31.809  -3.128  17.675  1.00 12.18  ? 15  HIS A CA    1 
ATOM   103  C  C     . HIS A 1 15  ? 31.367  -1.668  17.813  1.00 10.99  ? 15  HIS A C     1 
ATOM   104  O  O     . HIS A 1 15  ? 32.175  -0.762  17.746  1.00 12.33  ? 15  HIS A O     1 
ATOM   105  C  CB    . HIS A 1 15  ? 32.195  -3.353  16.197  1.00 11.93  ? 15  HIS A CB    1 
ATOM   106  C  CG    . HIS A 1 15  ? 32.891  -4.632  15.960  1.00 13.88  ? 15  HIS A CG    1 
ATOM   107  N  ND1   . HIS A 1 15  ? 34.255  -4.748  16.028  1.00 16.36  ? 15  HIS A ND1   1 
ATOM   108  C  CD2   . HIS A 1 15  ? 32.409  -5.832  15.640  1.00 17.37  ? 15  HIS A CD2   1 
ATOM   109  C  CE1   . HIS A 1 15  ? 34.573  -5.980  15.765  1.00 22.24  ? 15  HIS A CE1   1 
ATOM   110  N  NE2   . HIS A 1 15  ? 33.482  -6.649  15.510  1.00 21.33  ? 15  HIS A NE2   1 
ATOM   111  N  N     . TRP A 1 16  ? 30.043  -1.470  17.946  1.00 9.81   ? 16  TRP A N     1 
ATOM   112  C  CA    . TRP A 1 16  ? 29.492  -0.132  17.859  1.00 8.70   ? 16  TRP A CA    1 
ATOM   113  C  C     . TRP A 1 16  ? 30.072  0.844   18.891  1.00 8.97   ? 16  TRP A C     1 
ATOM   114  O  O     . TRP A 1 16  ? 30.169  2.040   18.579  1.00 9.67   ? 16  TRP A O     1 
ATOM   115  C  CB    . TRP A 1 16  ? 27.996  -0.162  17.934  1.00 8.41   ? 16  TRP A CB    1 
ATOM   116  C  CG    . TRP A 1 16  ? 27.314  -0.853  16.812  1.00 8.61   ? 16  TRP A CG    1 
ATOM   117  C  CD1   . TRP A 1 16  ? 27.875  -1.330  15.691  1.00 10.09  ? 16  TRP A CD1   1 
ATOM   118  C  CD2   . TRP A 1 16  ? 25.890  -1.124  16.739  1.00 8.19   ? 16  TRP A CD2   1 
ATOM   119  N  NE1   . TRP A 1 16  ? 26.898  -1.858  14.885  1.00 10.06  ? 16  TRP A NE1   1 
ATOM   120  C  CE2   . TRP A 1 16  ? 25.678  -1.764  15.512  1.00 8.10   ? 16  TRP A CE2   1 
ATOM   121  C  CE3   . TRP A 1 16  ? 24.816  -0.906  17.595  1.00 7.58   ? 16  TRP A CE3   1 
ATOM   122  C  CZ2   . TRP A 1 16  ? 24.388  -2.192  15.091  1.00 8.98   ? 16  TRP A CZ2   1 
ATOM   123  C  CZ3   . TRP A 1 16  ? 23.556  -1.313  17.181  1.00 7.71   ? 16  TRP A CZ3   1 
ATOM   124  C  CH2   . TRP A 1 16  ? 23.361  -1.883  15.966  1.00 8.37   ? 16  TRP A CH2   1 
ATOM   125  N  N     . HIS A 1 17  ? 30.432  0.347   20.034  1.00 9.62   ? 17  HIS A N     1 
ATOM   126  C  CA    . HIS A 1 17  ? 30.946  1.218   21.095  1.00 10.59  ? 17  HIS A CA    1 
ATOM   127  C  C     . HIS A 1 17  ? 32.192  1.999   20.658  1.00 10.34  ? 17  HIS A C     1 
ATOM   128  O  O     . HIS A 1 17  ? 32.459  3.053   21.282  1.00 11.75  ? 17  HIS A O     1 
ATOM   129  C  CB    . HIS A 1 17  ? 31.199  0.437   22.343  1.00 11.23  ? 17  HIS A CB    1 
ATOM   130  C  CG    . HIS A 1 17  ? 32.430  -0.430  22.253  1.00 11.96  ? 17  HIS A CG    1 
ATOM   131  N  ND1   . HIS A 1 17  ? 33.641  -0.031  22.775  1.00 15.24  ? 17  HIS A ND1   1 
ATOM   132  C  CD2   . HIS A 1 17  ? 32.579  -1.653  21.721  1.00 13.64  ? 17  HIS A CD2   1 
ATOM   133  C  CE1   . HIS A 1 17  ? 34.484  -0.975  22.536  1.00 16.85  ? 17  HIS A CE1   1 
ATOM   134  N  NE2   . HIS A 1 17  ? 33.907  -1.953  21.883  1.00 15.62  ? 17  HIS A NE2   1 
ATOM   135  N  N     . LYS A 1 18  ? 32.943  1.480   19.716  1.00 11.54  ? 18  LYS A N     1 
ATOM   136  C  CA    . LYS A 1 18  ? 34.200  2.225   19.359  1.00 12.72  ? 18  LYS A CA    1 
ATOM   137  C  C     . LYS A 1 18  ? 33.873  3.538   18.675  1.00 13.09  ? 18  LYS A C     1 
ATOM   138  O  O     . LYS A 1 18  ? 34.488  4.517   19.025  1.00 19.07  ? 18  LYS A O     1 
ATOM   139  C  CB    . LYS A 1 18  ? 35.081  1.376   18.454  1.00 14.97  ? 18  LYS A CB    1 
ATOM   140  C  CG    . LYS A 1 18  ? 35.621  0.130   19.146  1.00 14.33  ? 18  LYS A CG    1 
ATOM   141  C  CD    . LYS A 1 18  ? 36.363  -0.818  18.253  1.00 15.46  ? 18  LYS A CD    1 
ATOM   142  C  CE    . LYS A 1 18  ? 35.413  -1.803  17.584  1.00 15.05  ? 18  LYS A CE    1 
ATOM   143  N  NZ    . LYS A 1 18  ? 36.053  -2.623  16.552  1.00 15.41  ? 18  LYS A NZ    1 
ATOM   144  N  N     . ASP A 1 19  ? 32.887  3.570   17.795  1.00 11.86  ? 19  ASP A N     1 
ATOM   145  C  CA    . ASP A 1 19  ? 32.488  4.860   17.236  1.00 12.37  ? 19  ASP A CA    1 
ATOM   146  C  C     . ASP A 1 19  ? 31.392  5.606   18.028  1.00 11.75  ? 19  ASP A C     1 
ATOM   147  O  O     . ASP A 1 19  ? 31.323  6.799   17.886  1.00 13.29  ? 19  ASP A O     1 
ATOM   148  C  CB    . ASP A 1 19  ? 31.990  4.711   15.845  1.00 13.80  ? 19  ASP A CB    1 
ATOM   149  C  CG    . ASP A 1 19  ? 32.995  4.421   14.829  1.00 21.56  ? 19  ASP A CG    1 
ATOM   150  O  OD1   . ASP A 1 19  ? 33.931  5.075   14.768  1.00 25.86  ? 19  ASP A OD1   1 
ATOM   151  O  OD2   . ASP A 1 19  ? 32.962  3.388   14.163  1.00 37.01  ? 19  ASP A OD2   1 
ATOM   152  N  N     . PHE A 1 20  ? 30.681  4.875   18.885  1.00 10.33  ? 20  PHE A N     1 
ATOM   153  C  CA    . PHE A 1 20  ? 29.560  5.390   19.642  1.00 10.11  ? 20  PHE A CA    1 
ATOM   154  C  C     . PHE A 1 20  ? 29.651  4.901   21.061  1.00 11.22  ? 20  PHE A C     1 
ATOM   155  O  O     . PHE A 1 20  ? 29.012  3.947   21.466  1.00 10.19  ? 20  PHE A O     1 
ATOM   156  C  CB    . PHE A 1 20  ? 28.225  4.967   19.020  1.00 9.87   ? 20  PHE A CB    1 
ATOM   157  C  CG    . PHE A 1 20  ? 28.156  5.325   17.538  1.00 10.75  ? 20  PHE A CG    1 
ATOM   158  C  CD1   . PHE A 1 20  ? 27.839  6.577   17.169  1.00 13.21  ? 20  PHE A CD1   1 
ATOM   159  C  CD2   . PHE A 1 20  ? 28.474  4.409   16.569  1.00 13.16  ? 20  PHE A CD2   1 
ATOM   160  C  CE1   . PHE A 1 20  ? 27.824  6.950   15.799  1.00 15.51  ? 20  PHE A CE1   1 
ATOM   161  C  CE2   . PHE A 1 20  ? 28.497  4.743   15.262  1.00 15.48  ? 20  PHE A CE2   1 
ATOM   162  C  CZ    . PHE A 1 20  ? 28.165  6.028   14.866  1.00 15.24  ? 20  PHE A CZ    1 
ATOM   163  N  N     . PRO A 1 21  ? 30.505  5.517   21.891  1.00 10.71  ? 21  PRO A N     1 
ATOM   164  C  CA    . PRO A 1 21  ? 30.793  5.000   23.226  1.00 11.17  ? 21  PRO A CA    1 
ATOM   165  C  C     . PRO A 1 21  ? 29.554  4.934   24.123  1.00 10.53  ? 21  PRO A C     1 
ATOM   166  O  O     . PRO A 1 21  ? 29.564  4.139   25.061  1.00 11.55  ? 21  PRO A O     1 
ATOM   167  C  CB    . PRO A 1 21  ? 31.827  5.957   23.810  1.00 14.62  ? 21  PRO A CB    1 
ATOM   168  C  CG    . PRO A 1 21  ? 32.029  6.979   22.820  1.00 19.94  ? 21  PRO A CG    1 
ATOM   169  C  CD    . PRO A 1 21  ? 31.444  6.580   21.522  1.00 13.32  ? 21  PRO A CD    1 
ATOM   170  N  N     A ILE A 1 22  ? 28.497  5.697   23.803  0.50 9.57   ? 22  ILE A N     1 
ATOM   171  N  N     B ILE A 1 22  ? 28.479  5.688   23.859  0.50 9.95   ? 22  ILE A N     1 
ATOM   172  C  CA    A ILE A 1 22  ? 27.233  5.616   24.520  0.50 9.07   ? 22  ILE A CA    1 
ATOM   173  C  CA    B ILE A 1 22  ? 27.243  5.571   24.648  0.50 9.69   ? 22  ILE A CA    1 
ATOM   174  C  C     A ILE A 1 22  ? 26.604  4.220   24.404  0.50 8.03   ? 22  ILE A C     1 
ATOM   175  C  C     B ILE A 1 22  ? 26.645  4.155   24.506  0.50 8.40   ? 22  ILE A C     1 
ATOM   176  O  O     A ILE A 1 22  ? 25.647  3.928   25.097  0.50 8.66   ? 22  ILE A O     1 
ATOM   177  O  O     B ILE A 1 22  ? 25.785  3.758   25.302  0.50 9.74   ? 22  ILE A O     1 
ATOM   178  C  CB    A ILE A 1 22  ? 26.240  6.717   24.043  0.50 8.44   ? 22  ILE A CB    1 
ATOM   179  C  CB    B ILE A 1 22  ? 26.204  6.641   24.210  0.50 9.57   ? 22  ILE A CB    1 
ATOM   180  C  CG1   A ILE A 1 22  ? 25.172  6.972   25.121  0.50 9.26   ? 22  ILE A CG1   1 
ATOM   181  C  CG1   B ILE A 1 22  ? 25.127  6.888   25.271  0.50 12.53  ? 22  ILE A CG1   1 
ATOM   182  C  CG2   A ILE A 1 22  ? 25.660  6.345   22.664  0.50 8.30   ? 22  ILE A CG2   1 
ATOM   183  C  CG2   B ILE A 1 22  ? 25.552  6.210   22.904  0.50 9.35   ? 22  ILE A CG2   1 
ATOM   184  C  CD1   A ILE A 1 22  ? 24.249  8.106   24.835  0.50 10.86  ? 22  ILE A CD1   1 
ATOM   185  C  CD1   B ILE A 1 22  ? 25.705  7.523   26.484  0.50 15.20  ? 22  ILE A CD1   1 
ATOM   186  N  N     . ALA A 1 23  ? 27.117  3.358   23.532  1.00 8.32   ? 23  ALA A N     1 
ATOM   187  C  CA    . ALA A 1 23  ? 26.705  1.957   23.452  1.00 8.24   ? 23  ALA A CA    1 
ATOM   188  C  C     . ALA A 1 23  ? 26.811  1.255   24.756  1.00 8.82   ? 23  ALA A C     1 
ATOM   189  O  O     . ALA A 1 23  ? 26.112  0.247   24.938  1.00 10.13  ? 23  ALA A O     1 
ATOM   190  C  CB    . ALA A 1 23  ? 27.500  1.211   22.421  1.00 8.77   ? 23  ALA A CB    1 
ATOM   191  N  N     . LYS A 1 24  ? 27.712  1.670   25.632  1.00 8.98   ? 24  LYS A N     1 
ATOM   192  C  CA    . LYS A 1 24  ? 27.918  1.064   26.939  1.00 9.99   ? 24  LYS A CA    1 
ATOM   193  C  C     . LYS A 1 24  ? 27.334  1.943   28.042  1.00 10.82  ? 24  LYS A C     1 
ATOM   194  O  O     . LYS A 1 24  ? 27.742  1.806   29.162  1.00 13.34  ? 24  LYS A O     1 
ATOM   195  C  CB    . LYS A 1 24  ? 29.400  0.821   27.262  1.00 12.17  ? 24  LYS A CB    1 
ATOM   196  C  CG    . LYS A 1 24  ? 30.001  -0.163  26.302  1.00 13.74  ? 24  LYS A CG    1 
ATOM   197  C  CD    . LYS A 1 24  ? 31.415  -0.498  26.677  1.00 18.39  ? 24  LYS A CD    1 
ATOM   198  C  CE    . LYS A 1 24  ? 31.976  -1.535  25.719  1.00 24.14  ? 24  LYS A CE    1 
ATOM   199  N  NZ    . LYS A 1 24  ? 31.878  -2.870  26.219  1.00 36.70  ? 24  LYS A NZ    1 
ATOM   200  N  N     . GLY A 1 25  ? 26.338  2.760   27.698  1.00 10.65  ? 25  GLY A N     1 
ATOM   201  C  CA    . GLY A 1 25  ? 25.736  3.715   28.626  1.00 11.49  ? 25  GLY A CA    1 
ATOM   202  C  C     . GLY A 1 25  ? 24.747  3.053   29.586  1.00 10.69  ? 25  GLY A C     1 
ATOM   203  O  O     . GLY A 1 25  ? 24.560  1.812   29.687  1.00 11.73  ? 25  GLY A O     1 
ATOM   204  N  N     . GLU A 1 26  ? 24.105  3.964   30.302  1.00 10.96  ? 26  GLU A N     1 
ATOM   205  C  CA    . GLU A 1 26  ? 23.240  3.554   31.419  1.00 11.61  ? 26  GLU A CA    1 
ATOM   206  C  C     . GLU A 1 26  ? 21.828  3.304   31.036  1.00 10.03  ? 26  GLU A C     1 
ATOM   207  O  O     . GLU A 1 26  ? 21.041  2.784   31.827  1.00 11.84  ? 26  GLU A O     1 
ATOM   208  C  CB    . GLU A 1 26  ? 23.301  4.584   32.521  1.00 14.77  ? 26  GLU A CB    1 
ATOM   209  C  CG    . GLU A 1 26  ? 24.714  4.822   33.104  1.00 15.81  ? 26  GLU A CG    1 
ATOM   210  C  CD    . GLU A 1 26  ? 25.294  3.593   33.733  1.00 20.11  ? 26  GLU A CD    1 
ATOM   211  O  OE1   . GLU A 1 26  ? 24.672  2.948   34.584  1.00 27.69  ? 26  GLU A OE1   1 
ATOM   212  O  OE2   . GLU A 1 26  ? 26.422  3.322   33.403  1.00 29.29  ? 26  GLU A OE2   1 
ATOM   213  N  N     . ARG A 1 27  ? 21.436  3.682   29.803  1.00 7.90   ? 27  ARG A N     1 
ATOM   214  C  CA    . ARG A 1 27  ? 20.036  3.540   29.404  1.00 7.56   ? 27  ARG A CA    1 
ATOM   215  C  C     . ARG A 1 27  ? 19.937  3.063   27.944  1.00 6.81   ? 27  ARG A C     1 
ATOM   216  O  O     . ARG A 1 27  ? 19.211  3.636   27.114  1.00 7.44   ? 27  ARG A O     1 
ATOM   217  C  CB    . ARG A 1 27  ? 19.228  4.772   29.636  1.00 10.94  ? 27  ARG A CB    1 
ATOM   218  C  CG    . ARG A 1 27  ? 19.505  6.126   29.135  1.00 16.97  ? 27  ARG A CG    1 
ATOM   219  C  CD    . ARG A 1 27  ? 18.390  7.221   29.368  1.00 21.15  ? 27  ARG A CD    1 
ATOM   220  N  NE    . ARG A 1 27  ? 17.123  7.165   28.362  1.00 13.83  ? 27  ARG A NE    1 
ATOM   221  C  CZ    . ARG A 1 27  ? 16.272  8.068   28.352  1.00 14.67  ? 27  ARG A CZ    1 
ATOM   222  N  NH1   . ARG A 1 27  ? 16.326  9.097   29.212  1.00 17.14  ? 27  ARG A NH1   1 
ATOM   223  N  NH2   . ARG A 1 27  ? 15.314  7.995   27.554  1.00 17.10  ? 27  ARG A NH2   1 
ATOM   224  N  N     . GLN A 1 28  ? 20.652  1.982   27.650  1.00 6.58   ? 28  GLN A N     1 
ATOM   225  C  CA    . GLN A 1 28  ? 20.677  1.415   26.295  1.00 6.12   ? 28  GLN A CA    1 
ATOM   226  C  C     . GLN A 1 28  ? 19.501  0.472   26.100  1.00 6.39   ? 28  GLN A C     1 
ATOM   227  O  O     . GLN A 1 28  ? 18.996  -0.228  26.957  1.00 6.77   ? 28  GLN A O     1 
ATOM   228  C  CB    . GLN A 1 28  ? 22.038  0.771   26.051  1.00 6.83   ? 28  GLN A CB    1 
ATOM   229  C  CG    . GLN A 1 28  ? 23.163  1.765   25.931  1.00 7.14   ? 28  GLN A CG    1 
ATOM   230  C  CD    . GLN A 1 28  ? 22.991  2.599   24.678  1.00 7.05   ? 28  GLN A CD    1 
ATOM   231  O  OE1   . GLN A 1 28  ? 23.171  2.042   23.577  1.00 7.37   ? 28  GLN A OE1   1 
ATOM   232  N  NE2   . GLN A 1 28  ? 22.679  3.857   24.789  1.00 6.98   ? 28  GLN A NE2   1 
ATOM   233  N  N     . SER A 1 29  ? 19.151  0.388   24.810  1.00 5.89   ? 29  SER A N     1 
ATOM   234  C  CA    . SER A 1 29  ? 18.074  -0.491  24.297  1.00 5.61   ? 29  SER A CA    1 
ATOM   235  C  C     . SER A 1 29  ? 18.564  -1.370  23.215  1.00 5.81   ? 29  SER A C     1 
ATOM   236  O  O     . SER A 1 29  ? 19.540  -1.001  22.513  1.00 6.77   ? 29  SER A O     1 
ATOM   237  C  CB    . SER A 1 29  ? 16.917  0.344   23.789  1.00 6.01   ? 29  SER A CB    1 
ATOM   238  O  OG    . SER A 1 29  ? 16.320  1.100   24.870  1.00 5.85   ? 29  SER A OG    1 
ATOM   239  N  N     . PRO A 1 30  ? 17.969  -2.511  22.941  1.00 5.47   ? 30  PRO A N     1 
ATOM   240  C  CA    . PRO A 1 30  ? 16.776  -3.047  23.665  1.00 5.37   ? 30  PRO A CA    1 
ATOM   241  C  C     . PRO A 1 30  ? 17.236  -3.708  24.987  1.00 5.22   ? 30  PRO A C     1 
ATOM   242  O  O     . PRO A 1 30  ? 18.408  -3.712  25.324  1.00 6.10   ? 30  PRO A O     1 
ATOM   243  C  CB    . PRO A 1 30  ? 16.279  -4.082  22.666  1.00 5.40   ? 30  PRO A CB    1 
ATOM   244  C  CG    . PRO A 1 30  ? 17.540  -4.633  22.087  1.00 5.96   ? 30  PRO A CG    1 
ATOM   245  C  CD    . PRO A 1 30  ? 18.439  -3.437  21.898  1.00 6.10   ? 30  PRO A CD    1 
ATOM   246  N  N     . VAL A 1 31  ? 16.257  -4.276  25.694  1.00 5.76   ? 31  VAL A N     1 
ATOM   247  C  CA    . VAL A 1 31  ? 16.403  -4.997  26.925  1.00 5.89   ? 31  VAL A CA    1 
ATOM   248  C  C     . VAL A 1 31  ? 15.553  -6.222  26.887  1.00 6.54   ? 31  VAL A C     1 
ATOM   249  O  O     . VAL A 1 31  ? 14.572  -6.279  26.110  1.00 6.88   ? 31  VAL A O     1 
ATOM   250  C  CB    . VAL A 1 31  ? 16.102  -4.134  28.145  1.00 6.51   ? 31  VAL A CB    1 
ATOM   251  C  CG1   . VAL A 1 31  ? 17.019  -2.971  28.245  1.00 7.40   ? 31  VAL A CG1   1 
ATOM   252  C  CG2   . VAL A 1 31  ? 14.612  -3.746  28.185  1.00 7.22   ? 31  VAL A CG2   1 
ATOM   253  N  N     . ASP A 1 32  ? 15.880  -7.198  27.741  1.00 6.06   ? 32  ASP A N     1 
ATOM   254  C  CA    . ASP A 1 32  ? 14.982  -8.284  28.045  1.00 6.46   ? 32  ASP A CA    1 
ATOM   255  C  C     . ASP A 1 32  ? 13.943  -7.759  29.037  1.00 7.15   ? 32  ASP A C     1 
ATOM   256  O  O     . ASP A 1 32  ? 14.245  -7.062  30.013  1.00 7.89   ? 32  ASP A O     1 
ATOM   257  C  CB    . ASP A 1 32  ? 15.736  -9.434  28.656  1.00 7.19   ? 32  ASP A CB    1 
ATOM   258  C  CG    . ASP A 1 32  ? 14.820  -10.643 28.927  1.00 8.49   ? 32  ASP A CG    1 
ATOM   259  O  OD1   . ASP A 1 32  ? 14.129  -11.073 27.979  1.00 8.57   ? 32  ASP A OD1   1 
ATOM   260  O  OD2   . ASP A 1 32  ? 14.766  -11.074 30.105  1.00 10.44  ? 32  ASP A OD2   1 
ATOM   261  N  N     . ILE A 1 33  ? 12.659  -8.072  28.760  1.00 6.12   ? 33  ILE A N     1 
ATOM   262  C  CA    . ILE A 1 33  ? 11.546  -7.739  29.627  1.00 6.67   ? 33  ILE A CA    1 
ATOM   263  C  C     . ILE A 1 33  ? 11.269  -8.969  30.464  1.00 7.20   ? 33  ILE A C     1 
ATOM   264  O  O     . ILE A 1 33  ? 10.755  -9.996  29.958  1.00 8.38   ? 33  ILE A O     1 
ATOM   265  C  CB    . ILE A 1 33  ? 10.346  -7.322  28.785  1.00 6.73   ? 33  ILE A CB    1 
ATOM   266  C  CG1   . ILE A 1 33  ? 10.723  -6.102  27.954  1.00 7.91   ? 33  ILE A CG1   1 
ATOM   267  C  CG2   . ILE A 1 33  ? 9.171   -7.089  29.715  1.00 9.96   ? 33  ILE A CG2   1 
ATOM   268  C  CD1   . ILE A 1 33  ? 9.686   -5.803  26.856  1.00 9.38   ? 33  ILE A CD1   1 
ATOM   269  N  N     A ASP A 1 34  ? 11.556  -8.893  31.766  0.50 8.12   ? 34  ASP A N     1 
ATOM   270  N  N     B ASP A 1 34  ? 11.665  -8.920  31.727  0.50 9.00   ? 34  ASP A N     1 
ATOM   271  C  CA    A ASP A 1 34  ? 11.316  -9.970  32.676  0.50 8.64   ? 34  ASP A CA    1 
ATOM   272  C  CA    B ASP A 1 34  ? 11.366  -9.957  32.649  0.50 9.46   ? 34  ASP A CA    1 
ATOM   273  C  C     A ASP A 1 34  ? 9.928   -9.760  33.220  0.50 9.54   ? 34  ASP A C     1 
ATOM   274  C  C     B ASP A 1 34  ? 9.940   -9.712  33.158  0.50 9.94   ? 34  ASP A C     1 
ATOM   275  O  O     A ASP A 1 34  ? 9.705   -8.824  34.049  0.50 12.14  ? 34  ASP A O     1 
ATOM   276  O  O     B ASP A 1 34  ? 9.702   -8.683  33.883  0.50 11.01  ? 34  ASP A O     1 
ATOM   277  C  CB    A ASP A 1 34  ? 12.356  -9.983  33.815  0.50 10.63  ? 34  ASP A CB    1 
ATOM   278  C  CB    B ASP A 1 34  ? 12.401  -9.945  33.783  0.50 11.68  ? 34  ASP A CB    1 
ATOM   279  C  CG    A ASP A 1 34  ? 12.067  -11.049 34.899  0.50 11.17  ? 34  ASP A CG    1 
ATOM   280  C  CG    B ASP A 1 34  ? 12.306  -11.174 34.659  0.50 12.55  ? 34  ASP A CG    1 
ATOM   281  O  OD1   A ASP A 1 34  ? 10.903  -11.499 35.018  0.50 13.67  ? 34  ASP A OD1   1 
ATOM   282  O  OD1   B ASP A 1 34  ? 12.693  -12.254 34.215  0.50 14.54  ? 34  ASP A OD1   1 
ATOM   283  O  OD2   A ASP A 1 34  ? 12.978  -11.393 35.623  0.50 13.03  ? 34  ASP A OD2   1 
ATOM   284  O  OD2   B ASP A 1 34  ? 11.716  -11.081 35.710  0.50 17.41  ? 34  ASP A OD2   1 
ATOM   285  N  N     . THR A 1 35  ? 8.991   -10.521 32.740  1.00 10.06  ? 35  THR A N     1 
ATOM   286  C  CA    . THR A 1 35  ? 7.611   -10.256 33.016  1.00 11.20  ? 35  THR A CA    1 
ATOM   287  C  C     . THR A 1 35  ? 7.248   -10.388 34.434  1.00 13.21  ? 35  THR A C     1 
ATOM   288  O  O     . THR A 1 35  ? 6.303   -9.735  34.891  1.00 18.40  ? 35  THR A O     1 
ATOM   289  C  CB    . THR A 1 35  ? 6.704   -11.166 32.170  1.00 12.64  ? 35  THR A CB    1 
ATOM   290  O  OG1   . THR A 1 35  ? 6.887   -12.490 32.622  1.00 12.23  ? 35  THR A OG1   1 
ATOM   291  C  CG2   . THR A 1 35  ? 6.910   -11.018 30.706  1.00 14.35  ? 35  THR A CG2   1 
ATOM   292  N  N     . HIS A 1 36  ? 7.982   -11.182 35.173  1.00 12.37  ? 36  HIS A N     1 
ATOM   293  C  CA    . HIS A 1 36  ? 7.730   -11.344 36.587  1.00 14.86  ? 36  HIS A CA    1 
ATOM   294  C  C     . HIS A 1 36  ? 8.216   -10.209 37.473  1.00 17.29  ? 36  HIS A C     1 
ATOM   295  O  O     . HIS A 1 36  ? 7.648   -10.004 38.541  1.00 29.57  ? 36  HIS A O     1 
ATOM   296  C  CB    . HIS A 1 36  ? 8.274   -12.642 37.077  1.00 16.01  ? 36  HIS A CB    1 
ATOM   297  C  CG    . HIS A 1 36  ? 7.442   -13.747 36.596  1.00 27.32  ? 36  HIS A CG    1 
ATOM   298  N  ND1   . HIS A 1 36  ? 7.859   -14.505 35.546  1.00 29.40  ? 36  HIS A ND1   1 
ATOM   299  C  CD2   . HIS A 1 36  ? 6.122   -14.054 36.793  1.00 31.16  ? 36  HIS A CD2   1 
ATOM   300  C  CE1   . HIS A 1 36  ? 6.896   -15.314 35.158  1.00 41.43  ? 36  HIS A CE1   1 
ATOM   301  N  NE2   . HIS A 1 36  ? 5.836   -15.080 35.917  1.00 41.24  ? 36  HIS A NE2   1 
ATOM   302  N  N     . THR A 1 37  ? 9.189   -9.436  36.983  1.00 13.90  ? 37  THR A N     1 
ATOM   303  C  CA    . THR A 1 37  ? 9.611   -8.317  37.722  1.00 13.93  ? 37  THR A CA    1 
ATOM   304  C  C     . THR A 1 37  ? 9.164   -6.981  37.254  1.00 14.06  ? 37  THR A C     1 
ATOM   305  O  O     . THR A 1 37  ? 9.265   -6.040  38.010  1.00 19.04  ? 37  THR A O     1 
ATOM   306  C  CB    . THR A 1 37  ? 11.039  -8.308  37.945  1.00 18.06  ? 37  THR A CB    1 
ATOM   307  O  OG1   . THR A 1 37  ? 11.779  -8.314  36.774  1.00 18.68  ? 37  THR A OG1   1 
ATOM   308  C  CG2   . THR A 1 37  ? 11.444  -9.595  38.537  1.00 22.97  ? 37  THR A CG2   1 
ATOM   309  N  N     . ALA A 1 38  ? 8.514   -6.909  36.099  1.00 12.91  ? 38  ALA A N     1 
ATOM   310  C  CA    . ALA A 1 38  ? 7.937   -5.680  35.635  1.00 12.56  ? 38  ALA A CA    1 
ATOM   311  C  C     . ALA A 1 38  ? 6.730   -5.426  36.527  1.00 16.29  ? 38  ALA A C     1 
ATOM   312  O  O     . ALA A 1 38  ? 5.901   -6.300  36.792  1.00 22.69  ? 38  ALA A O     1 
ATOM   313  C  CB    . ALA A 1 38  ? 7.476   -5.787  34.241  1.00 12.97  ? 38  ALA A CB    1 
ATOM   314  N  N     . LYS A 1 39  ? 6.701   -4.263  37.107  1.00 15.88  ? 39  LYS A N     1 
ATOM   315  C  CA    . LYS A 1 39  ? 5.560   -4.032  38.074  1.00 17.54  ? 39  LYS A CA    1 
ATOM   316  C  C     . LYS A 1 39  ? 4.425   -3.317  37.396  1.00 12.45  ? 39  LYS A C     1 
ATOM   317  O  O     . LYS A 1 39  ? 4.580   -2.322  36.646  1.00 12.99  ? 39  LYS A O     1 
ATOM   318  C  CB    . LYS A 1 39  ? 5.962   -3.346  39.328  1.00 19.24  ? 39  LYS A CB    1 
ATOM   319  C  CG    . LYS A 1 39  ? 4.914   -3.361  40.462  1.00 20.20  ? 39  LYS A CG    1 
ATOM   320  C  CD    . LYS A 1 39  ? 5.443   -2.523  41.618  1.00 20.78  ? 39  LYS A CD    1 
ATOM   321  C  CE    . LYS A 1 39  ? 4.416   -2.529  42.759  1.00 22.89  ? 39  LYS A CE    1 
ATOM   322  N  NZ    . LYS A 1 39  ? 4.671   -1.612  43.884  1.00 30.32  ? 39  LYS A NZ    1 
ATOM   323  N  N     . TYR A 1 40  ? 3.227   -3.776  37.624  1.00 14.27  ? 40  TYR A N     1 
ATOM   324  C  CA    . TYR A 1 40  ? 2.013   -3.077  37.256  1.00 13.28  ? 40  TYR A CA    1 
ATOM   325  C  C     . TYR A 1 40  ? 2.035   -1.691  37.905  1.00 11.93  ? 40  TYR A C     1 
ATOM   326  O  O     . TYR A 1 40  ? 2.205   -1.548  39.137  1.00 14.45  ? 40  TYR A O     1 
ATOM   327  C  CB    . TYR A 1 40  ? 0.779   -3.890  37.690  1.00 15.46  ? 40  TYR A CB    1 
ATOM   328  C  CG    . TYR A 1 40  ? -0.473  -3.091  37.498  1.00 17.35  ? 40  TYR A CG    1 
ATOM   329  C  CD1   . TYR A 1 40  ? -0.844  -2.566  36.266  1.00 16.99  ? 40  TYR A CD1   1 
ATOM   330  C  CD2   . TYR A 1 40  ? -1.308  -2.894  38.518  1.00 22.27  ? 40  TYR A CD2   1 
ATOM   331  C  CE1   . TYR A 1 40  ? -2.029  -1.864  36.139  1.00 22.71  ? 40  TYR A CE1   1 
ATOM   332  C  CE2   . TYR A 1 40  ? -2.449  -2.172  38.413  1.00 24.88  ? 40  TYR A CE2   1 
ATOM   333  C  CZ    . TYR A 1 40  ? -2.795  -1.691  37.230  1.00 22.84  ? 40  TYR A CZ    1 
ATOM   334  O  OH    . TYR A 1 40  ? -3.972  -1.057  37.164  1.00 30.61  ? 40  TYR A OH    1 
ATOM   335  N  N     . ASP A 1 41  ? 1.802   -0.679  37.090  1.00 10.84  ? 41  ASP A N     1 
ATOM   336  C  CA    . ASP A 1 41  ? 1.755   0.666   37.582  1.00 11.06  ? 41  ASP A CA    1 
ATOM   337  C  C     . ASP A 1 41  ? 0.388   1.238   37.314  1.00 15.03  ? 41  ASP A C     1 
ATOM   338  O  O     . ASP A 1 41  ? 0.074   1.579   36.189  1.00 13.28  ? 41  ASP A O     1 
ATOM   339  C  CB    . ASP A 1 41  ? 2.846   1.541   36.933  1.00 12.01  ? 41  ASP A CB    1 
ATOM   340  C  CG    . ASP A 1 41  ? 2.880   2.913   37.427  1.00 14.48  ? 41  ASP A CG    1 
ATOM   341  O  OD1   . ASP A 1 41  ? 1.956   3.352   38.178  1.00 16.48  ? 41  ASP A OD1   1 
ATOM   342  O  OD2   . ASP A 1 41  ? 3.841   3.659   37.104  1.00 17.37  ? 41  ASP A OD2   1 
ATOM   343  N  N     . PRO A 1 42  ? -0.470  1.330   38.327  1.00 16.18  ? 42  PRO A N     1 
ATOM   344  C  CA    . PRO A 1 42  ? -1.842  1.811   38.090  1.00 19.40  ? 42  PRO A CA    1 
ATOM   345  C  C     . PRO A 1 42  ? -1.906  3.264   37.648  1.00 19.71  ? 42  PRO A C     1 
ATOM   346  O  O     . PRO A 1 42  ? -2.963  3.794   37.205  1.00 27.32  ? 42  PRO A O     1 
ATOM   347  C  CB    . PRO A 1 42  ? -2.493  1.643   39.474  1.00 21.95  ? 42  PRO A CB    1 
ATOM   348  C  CG    . PRO A 1 42  ? -1.443  1.606   40.448  1.00 24.18  ? 42  PRO A CG    1 
ATOM   349  C  CD    . PRO A 1 42  ? -0.297  0.919   39.716  1.00 19.04  ? 42  PRO A CD    1 
ATOM   350  N  N     . SER A 1 43  ? -0.787  3.961   37.876  1.00 18.52  ? 43  SER A N     1 
ATOM   351  C  CA    . SER A 1 43  ? -0.740  5.370   37.446  1.00 20.66  ? 43  SER A CA    1 
ATOM   352  C  C     . SER A 1 43  ? -0.526  5.523   35.945  1.00 17.28  ? 43  SER A C     1 
ATOM   353  O  O     . SER A 1 43  ? -0.757  6.629   35.376  1.00 23.08  ? 43  SER A O     1 
ATOM   354  C  CB    . SER A 1 43  ? 0.329   6.176   38.169  1.00 21.70  ? 43  SER A CB    1 
ATOM   355  O  OG    . SER A 1 43  ? 1.580   5.871   37.684  1.00 21.14  ? 43  SER A OG    1 
ATOM   356  N  N     . LEU A 1 44  ? -0.173  4.459   35.229  1.00 16.66  ? 44  LEU A N     1 
ATOM   357  C  CA    . LEU A 1 44  ? 0.007   4.570   33.754  1.00 17.13  ? 44  LEU A CA    1 
ATOM   358  C  C     . LEU A 1 44  ? -1.326  4.676   33.128  1.00 22.07  ? 44  LEU A C     1 
ATOM   359  O  O     . LEU A 1 44  ? -2.270  4.061   33.523  1.00 25.33  ? 44  LEU A O     1 
ATOM   360  C  CB    . LEU A 1 44  ? 0.726   3.368   33.174  1.00 15.55  ? 44  LEU A CB    1 
ATOM   361  C  CG    . LEU A 1 44  ? 2.182   3.265   33.502  1.00 12.65  ? 44  LEU A CG    1 
ATOM   362  C  CD1   . LEU A 1 44  ? 2.621   1.893   33.108  1.00 15.79  ? 44  LEU A CD1   1 
ATOM   363  C  CD2   . LEU A 1 44  ? 2.963   4.340   32.823  1.00 15.29  ? 44  LEU A CD2   1 
ATOM   364  N  N     . LYS A 1 45  ? -1.379  5.456   32.056  1.00 21.22  ? 45  LYS A N     1 
ATOM   365  C  CA    . LYS A 1 45  ? -2.598  5.606   31.258  1.00 19.06  ? 45  LYS A CA    1 
ATOM   366  C  C     . LYS A 1 45  ? -2.635  4.686   30.100  1.00 21.22  ? 45  LYS A C     1 
ATOM   367  O  O     . LYS A 1 45  ? -1.640  4.022   29.727  1.00 30.61  ? 45  LYS A O     1 
ATOM   368  C  CB    . LYS A 1 45  ? -2.781  7.028   30.835  1.00 18.38  ? 45  LYS A CB    1 
ATOM   369  C  CG    . LYS A 1 45  ? -2.458  8.052   31.901  1.00 22.77  ? 45  LYS A CG    1 
ATOM   370  C  CD    . LYS A 1 45  ? -2.869  9.463   31.651  1.00 35.31  ? 45  LYS A CD    1 
ATOM   371  C  CE    . LYS A 1 45  ? -2.710  10.106  33.041  1.00 49.70  ? 45  LYS A CE    1 
ATOM   372  N  NZ    . LYS A 1 45  ? -2.716  11.590  33.078  1.00 60.12  ? 45  LYS A NZ    1 
ATOM   373  N  N     . PRO A 1 46  ? -3.928  4.589   29.583  1.00 17.05  ? 46  PRO A N     1 
ATOM   374  C  CA    . PRO A 1 46  ? -4.015  3.984   28.277  1.00 15.96  ? 46  PRO A CA    1 
ATOM   375  C  C     . PRO A 1 46  ? -3.279  4.799   27.289  1.00 17.04  ? 46  PRO A C     1 
ATOM   376  O  O     . PRO A 1 46  ? -3.218  6.004   27.318  1.00 18.14  ? 46  PRO A O     1 
ATOM   377  C  CB    . PRO A 1 46  ? -5.539  3.994   27.984  1.00 16.86  ? 46  PRO A CB    1 
ATOM   378  C  CG    . PRO A 1 46  ? -6.249  4.139   29.304  1.00 21.86  ? 46  PRO A CG    1 
ATOM   379  C  CD    . PRO A 1 46  ? -5.270  4.825   30.210  1.00 20.76  ? 46  PRO A CD    1 
ATOM   380  N  N     . LEU A 1 47  ? -2.699  4.032   26.389  1.00 16.35  ? 47  LEU A N     1 
ATOM   381  C  CA    A LEU A 1 47  ? -2.016  4.662   25.284  0.50 15.67  ? 47  LEU A CA    1 
ATOM   382  C  CA    B LEU A 1 47  ? -1.948  4.588   25.347  0.50 12.65  ? 47  LEU A CA    1 
ATOM   383  C  C     . LEU A 1 47  ? -3.023  5.250   24.349  1.00 14.94  ? 47  LEU A C     1 
ATOM   384  O  O     . LEU A 1 47  ? -4.053  4.650   24.089  1.00 20.97  ? 47  LEU A O     1 
ATOM   385  C  CB    A LEU A 1 47  ? -1.314  3.703   24.370  0.50 21.49  ? 47  LEU A CB    1 
ATOM   386  C  CB    B LEU A 1 47  ? -1.060  3.464   24.731  0.50 12.29  ? 47  LEU A CB    1 
ATOM   387  C  CG    A LEU A 1 47  ? 0.010   3.307   24.805  0.50 22.81  ? 47  LEU A CG    1 
ATOM   388  C  CG    B LEU A 1 47  ? -0.223  3.950   23.583  0.50 11.30  ? 47  LEU A CG    1 
ATOM   389  C  CD1   A LEU A 1 47  ? 0.299   2.273   23.801  0.50 18.55  ? 47  LEU A CD1   1 
ATOM   390  C  CD1   B LEU A 1 47  ? 0.760   4.943   24.164  0.50 12.64  ? 47  LEU A CD1   1 
ATOM   391  C  CD2   A LEU A 1 47  ? 1.083   4.446   24.912  0.50 17.99  ? 47  LEU A CD2   1 
ATOM   392  C  CD2   B LEU A 1 47  ? 0.473   2.818   22.775  0.50 11.54  ? 47  LEU A CD2   1 
ATOM   393  N  N     . SER A 1 48  ? -2.721  6.414   23.737  1.00 11.37  ? 48  SER A N     1 
ATOM   394  C  CA    . SER A 1 48  ? -3.556  6.991   22.721  1.00 12.24  ? 48  SER A CA    1 
ATOM   395  C  C     . SER A 1 48  ? -2.755  7.027   21.435  1.00 10.71  ? 48  SER A C     1 
ATOM   396  O  O     . SER A 1 48  ? -1.755  7.764   21.300  1.00 11.53  ? 48  SER A O     1 
ATOM   397  C  CB    . SER A 1 48  ? -3.865  8.483   23.117  1.00 13.37  ? 48  SER A CB    1 
ATOM   398  O  OG    . SER A 1 48  ? -4.540  9.133   22.101  1.00 16.27  ? 48  SER A OG    1 
ATOM   399  N  N     . VAL A 1 49  ? -3.193  6.237   20.501  1.00 11.56  ? 49  VAL A N     1 
ATOM   400  C  CA    . VAL A 1 49  ? -2.585  6.117   19.205  1.00 13.08  ? 49  VAL A CA    1 
ATOM   401  C  C     . VAL A 1 49  ? -3.572  6.703   18.220  1.00 12.84  ? 49  VAL A C     1 
ATOM   402  O  O     . VAL A 1 49  ? -4.558  6.112   17.938  1.00 18.16  ? 49  VAL A O     1 
ATOM   403  C  CB    . VAL A 1 49  ? -2.300  4.640   18.825  1.00 15.62  ? 49  VAL A CB    1 
ATOM   404  C  CG1   . VAL A 1 49  ? -1.513  4.553   17.527  1.00 21.64  ? 49  VAL A CG1   1 
ATOM   405  C  CG2   . VAL A 1 49  ? -1.494  3.980   19.971  1.00 17.27  ? 49  VAL A CG2   1 
ATOM   406  N  N     . SER A 1 50  ? -3.231  7.823   17.638  1.00 12.65  ? 50  SER A N     1 
ATOM   407  C  CA    . SER A 1 50  ? -4.161  8.508   16.739  1.00 16.18  ? 50  SER A CA    1 
ATOM   408  C  C     . SER A 1 50  ? -3.556  8.628   15.375  1.00 13.74  ? 50  SER A C     1 
ATOM   409  O  O     . SER A 1 50  ? -2.868  9.610   15.088  1.00 14.21  ? 50  SER A O     1 
ATOM   410  C  CB    . SER A 1 50  ? -4.552  9.905   17.300  1.00 20.60  ? 50  SER A CB    1 
ATOM   411  O  OG    . SER A 1 50  ? -5.172  9.697   18.570  1.00 27.38  ? 50  SER A OG    1 
ATOM   412  N  N     . TYR A 1 51  ? -3.826  7.624   14.524  1.00 13.90  ? 51  TYR A N     1 
ATOM   413  C  CA    . TYR A 1 51  ? -3.251  7.566   13.238  1.00 12.95  ? 51  TYR A CA    1 
ATOM   414  C  C     . TYR A 1 51  ? -4.251  7.720   12.108  1.00 13.32  ? 51  TYR A C     1 
ATOM   415  O  O     . TYR A 1 51  ? -3.867  7.571   10.989  1.00 16.90  ? 51  TYR A O     1 
ATOM   416  C  CB    . TYR A 1 51  ? -2.567  6.133   13.054  1.00 12.95  ? 51  TYR A CB    1 
ATOM   417  C  CG    . TYR A 1 51  ? -1.307  5.867   13.826  1.00 9.38   ? 51  TYR A CG    1 
ATOM   418  C  CD1   . TYR A 1 51  ? -0.566  6.878   14.433  1.00 11.03  ? 51  TYR A CD1   1 
ATOM   419  C  CD2   . TYR A 1 51  ? -0.839  4.607   13.914  1.00 9.71   ? 51  TYR A CD2   1 
ATOM   420  C  CE1   . TYR A 1 51  ? 0.610   6.582   15.129  1.00 9.92   ? 51  TYR A CE1   1 
ATOM   421  C  CE2   . TYR A 1 51  ? 0.313   4.310   14.573  1.00 9.90   ? 51  TYR A CE2   1 
ATOM   422  C  CZ    . TYR A 1 51  ? 1.049   5.274   15.187  1.00 8.97   ? 51  TYR A CZ    1 
ATOM   423  O  OH    . TYR A 1 51  ? 2.216   4.912   15.804  1.00 10.01  ? 51  TYR A OH    1 
ATOM   424  N  N     . ASP A 1 52  ? -5.432  8.198   12.387  1.00 16.70  ? 52  ASP A N     1 
ATOM   425  C  CA    . ASP A 1 52  ? -6.414  8.421   11.314  1.00 18.41  ? 52  ASP A CA    1 
ATOM   426  C  C     . ASP A 1 52  ? -6.002  9.349   10.215  1.00 20.18  ? 52  ASP A C     1 
ATOM   427  O  O     . ASP A 1 52  ? -6.430  9.155   9.103   1.00 23.81  ? 52  ASP A O     1 
ATOM   428  C  CB    . ASP A 1 52  ? -7.739  8.769   11.840  1.00 25.04  ? 52  ASP A CB    1 
ATOM   429  C  CG    . ASP A 1 52  ? -7.691  9.782   12.919  1.00 34.06  ? 52  ASP A CG    1 
ATOM   430  O  OD1   . ASP A 1 52  ? -7.145  9.546   14.059  1.00 50.94  ? 52  ASP A OD1   1 
ATOM   431  O  OD2   . ASP A 1 52  ? -8.261  10.810  12.607  1.00 47.55  ? 52  ASP A OD2   1 
ATOM   432  N  N     . GLN A 1 53  ? -5.191  10.356  10.511  1.00 17.69  ? 53  GLN A N     1 
ATOM   433  C  CA    . GLN A 1 53  ? -4.684  11.251  9.418   1.00 17.78  ? 53  GLN A CA    1 
ATOM   434  C  C     . GLN A 1 53  ? -3.250  11.030  9.019   1.00 14.03  ? 53  GLN A C     1 
ATOM   435  O  O     . GLN A 1 53  ? -2.677  11.886  8.406   1.00 16.43  ? 53  GLN A O     1 
ATOM   436  C  CB    . GLN A 1 53  ? -4.918  12.711  9.847   1.00 22.86  ? 53  GLN A CB    1 
ATOM   437  C  CG    . GLN A 1 53  ? -6.380  13.015  10.096  1.00 29.38  ? 53  GLN A CG    1 
ATOM   438  C  CD    . GLN A 1 53  ? -7.154  13.015  8.802   1.00 35.46  ? 53  GLN A CD    1 
ATOM   439  O  OE1   . GLN A 1 53  ? -6.881  13.769  7.885   1.00 59.78  ? 53  GLN A OE1   1 
ATOM   440  N  NE2   . GLN A 1 53  ? -8.099  12.104  8.718   1.00 45.47  ? 53  GLN A NE2   1 
ATOM   441  N  N     . ALA A 1 54  ? -2.669  9.904   9.329   1.00 14.60  ? 54  ALA A N     1 
ATOM   442  C  CA    . ALA A 1 54  ? -1.322  9.661   8.965   1.00 14.39  ? 54  ALA A CA    1 
ATOM   443  C  C     . ALA A 1 54  ? -1.155  9.694   7.492   1.00 15.99  ? 54  ALA A C     1 
ATOM   444  O  O     . ALA A 1 54  ? -1.997  9.145   6.768   1.00 19.48  ? 54  ALA A O     1 
ATOM   445  C  CB    . ALA A 1 54  ? -0.846  8.283   9.499   1.00 15.61  ? 54  ALA A CB    1 
ATOM   446  N  N     . THR A 1 55  ? -0.067  10.351  7.008   1.00 13.15  ? 55  THR A N     1 
ATOM   447  C  CA    . THR A 1 55  ? 0.212   10.527  5.612   1.00 14.10  ? 55  THR A CA    1 
ATOM   448  C  C     . THR A 1 55  ? 1.579   10.002  5.294   1.00 12.40  ? 55  THR A C     1 
ATOM   449  O  O     . THR A 1 55  ? 2.539   10.586  5.574   1.00 12.31  ? 55  THR A O     1 
ATOM   450  C  CB    . THR A 1 55  ? 0.120   12.056  5.150   1.00 19.79  ? 55  THR A CB    1 
ATOM   451  O  OG1   . THR A 1 55  ? -1.088  12.680  5.576   1.00 32.58  ? 55  THR A OG1   1 
ATOM   452  C  CG2   . THR A 1 55  ? 0.309   11.975  3.683   1.00 21.82  ? 55  THR A CG2   1 
ATOM   453  N  N     . SER A 1 56  ? 1.549   8.767   4.829   1.00 13.96  ? 56  SER A N     1 
ATOM   454  C  CA    . SER A 1 56  ? 2.770   8.152   4.453   1.00 15.32  ? 56  SER A CA    1 
ATOM   455  C  C     . SER A 1 56  ? 3.133   8.740   3.122   1.00 15.30  ? 56  SER A C     1 
ATOM   456  O  O     . SER A 1 56  ? 2.325   9.193   2.334   1.00 18.63  ? 56  SER A O     1 
ATOM   457  C  CB    . SER A 1 56  ? 2.743   6.637   4.268   1.00 17.26  ? 56  SER A CB    1 
ATOM   458  O  OG    . SER A 1 56  ? 2.010   6.265   3.145   1.00 16.23  ? 56  SER A OG    1 
ATOM   459  N  N     . LEU A 1 57  ? 4.428   8.868   2.978   1.00 12.95  ? 57  LEU A N     1 
ATOM   460  C  CA    . LEU A 1 57  ? 4.962   9.354   1.669   1.00 13.60  ? 57  LEU A CA    1 
ATOM   461  C  C     . LEU A 1 57  ? 5.815   8.453   0.905   1.00 13.80  ? 57  LEU A C     1 
ATOM   462  O  O     . LEU A 1 57  ? 5.837   8.554   -0.312  1.00 16.14  ? 57  LEU A O     1 
ATOM   463  C  CB    . LEU A 1 57  ? 5.870   10.476  1.983   1.00 15.53  ? 57  LEU A CB    1 
ATOM   464  C  CG    . LEU A 1 57  ? 4.925   11.682  2.561   1.00 18.98  ? 57  LEU A CG    1 
ATOM   465  C  CD1   . LEU A 1 57  ? 5.983   12.682  2.952   1.00 20.20  ? 57  LEU A CD1   1 
ATOM   466  C  CD2   . LEU A 1 57  ? 3.740   12.272  1.755   1.00 24.18  ? 57  LEU A CD2   1 
ATOM   467  N  N     . ARG A 1 58  ? 6.687   7.676   1.536   1.00 15.05  ? 58  ARG A N     1 
ATOM   468  C  CA    . ARG A 1 58  ? 7.755   7.044   0.785   1.00 14.20  ? 58  ARG A CA    1 
ATOM   469  C  C     . ARG A 1 58  ? 8.260   5.903   1.611   1.00 12.39  ? 58  ARG A C     1 
ATOM   470  O  O     . ARG A 1 58  ? 8.229   5.933   2.885   1.00 15.01  ? 58  ARG A O     1 
ATOM   471  C  CB    . ARG A 1 58  ? 9.005   7.940   0.742   1.00 14.10  ? 58  ARG A CB    1 
ATOM   472  C  CG    . ARG A 1 58  ? 9.951   7.740   -0.255  1.00 16.29  ? 58  ARG A CG    1 
ATOM   473  C  CD    . ARG A 1 58  ? 10.907  8.812   -0.486  1.00 19.70  ? 58  ARG A CD    1 
ATOM   474  N  NE    . ARG A 1 58  ? 11.887  8.839   0.614   1.00 15.18  ? 58  ARG A NE    1 
ATOM   475  C  CZ    . ARG A 1 58  ? 13.241  8.832   0.560   1.00 13.90  ? 58  ARG A CZ    1 
ATOM   476  N  NH1   . ARG A 1 58  ? 13.815  9.323   -0.490  1.00 18.06  ? 58  ARG A NH1   1 
ATOM   477  N  NH2   . ARG A 1 58  ? 13.896  8.882   1.737   1.00 15.79  ? 58  ARG A NH2   1 
ATOM   478  N  N     . ILE A 1 59  ? 8.951   4.927   0.933   1.00 13.09  ? 59  ILE A N     1 
ATOM   479  C  CA    . ILE A 1 59  ? 9.653   3.804   1.610   1.00 12.57  ? 59  ILE A CA    1 
ATOM   480  C  C     . ILE A 1 59  ? 11.046  3.876   1.143   1.00 11.36  ? 59  ILE A C     1 
ATOM   481  O  O     . ILE A 1 59  ? 11.375  4.056   -0.110  1.00 15.21  ? 59  ILE A O     1 
ATOM   482  C  CB    . ILE A 1 59  ? 8.913   2.541   1.372   1.00 11.85  ? 59  ILE A CB    1 
ATOM   483  C  CG1   . ILE A 1 59  ? 9.455   1.414   2.251   1.00 12.75  ? 59  ILE A CG1   1 
ATOM   484  C  CG2   . ILE A 1 59  ? 8.951   2.201   -0.137  1.00 14.32  ? 59  ILE A CG2   1 
ATOM   485  C  CD1   . ILE A 1 59  ? 8.702   0.168   2.161   1.00 14.03  ? 59  ILE A CD1   1 
ATOM   486  N  N     . LEU A 1 60  ? 11.996  3.663   1.994   1.00 13.46  ? 60  LEU A N     1 
ATOM   487  C  CA    . LEU A 1 60  ? 13.339  3.803   1.849   1.00 8.88   ? 60  LEU A CA    1 
ATOM   488  C  C     . LEU A 1 60  ? 14.218  2.578   2.307   1.00 11.32  ? 60  LEU A C     1 
ATOM   489  O  O     . LEU A 1 60  ? 14.086  2.228   3.460   1.00 11.92  ? 60  LEU A O     1 
ATOM   490  C  CB    . LEU A 1 60  ? 13.901  5.059   2.501   1.00 12.06  ? 60  LEU A CB    1 
ATOM   491  C  CG    . LEU A 1 60  ? 15.375  5.172   2.429   1.00 10.31  ? 60  LEU A CG    1 
ATOM   492  C  CD1   . LEU A 1 60  ? 15.828  5.489   0.949   1.00 15.55  ? 60  LEU A CD1   1 
ATOM   493  C  CD2   . LEU A 1 60  ? 15.919  6.317   3.338   1.00 14.21  ? 60  LEU A CD2   1 
ATOM   494  N  N     . ASN A 1 61  ? 15.126  1.986   1.480   1.00 12.09  ? 61  ASN A N     1 
ATOM   495  C  CA    . ASN A 1 61  ? 16.167  1.028   1.963   1.00 12.49  ? 61  ASN A CA    1 
ATOM   496  C  C     . ASN A 1 61  ? 17.359  1.774   2.361   1.00 13.25  ? 61  ASN A C     1 
ATOM   497  O  O     . ASN A 1 61  ? 17.989  2.326   1.456   1.00 14.46  ? 61  ASN A O     1 
ATOM   498  C  CB    . ASN A 1 61  ? 16.481  -0.060  0.915   1.00 12.20  ? 61  ASN A CB    1 
ATOM   499  C  CG    . ASN A 1 61  ? 17.529  -1.047  1.346   1.00 12.81  ? 61  ASN A CG    1 
ATOM   500  O  OD1   . ASN A 1 61  ? 18.398  -0.791  2.197   1.00 13.73  ? 61  ASN A OD1   1 
ATOM   501  N  ND2   . ASN A 1 61  ? 17.525  -2.265  0.745   1.00 12.35  ? 61  ASN A ND2   1 
ATOM   502  N  N     . ASN A 1 62  ? 17.617  1.938   3.633   1.00 12.10  ? 62  ASN A N     1 
ATOM   503  C  CA    . ASN A 1 62  ? 18.685  2.729   4.101   1.00 13.23  ? 62  ASN A CA    1 
ATOM   504  C  C     . ASN A 1 62  ? 19.959  1.980   4.284   1.00 13.06  ? 62  ASN A C     1 
ATOM   505  O  O     . ASN A 1 62  ? 20.970  2.404   4.915   1.00 18.22  ? 62  ASN A O     1 
ATOM   506  C  CB    . ASN A 1 62  ? 18.382  3.572   5.341   1.00 13.15  ? 62  ASN A CB    1 
ATOM   507  C  CG    . ASN A 1 62  ? 18.033  2.713   6.496   1.00 12.61  ? 62  ASN A CG    1 
ATOM   508  O  OD1   . ASN A 1 62  ? 18.432  1.489   6.570   1.00 14.25  ? 62  ASN A OD1   1 
ATOM   509  N  ND2   . ASN A 1 62  ? 17.347  3.357   7.438   1.00 18.56  ? 62  ASN A ND2   1 
ATOM   510  N  N     . GLY A 1 63  ? 19.984  0.688   3.908   1.00 13.79  ? 63  GLY A N     1 
ATOM   511  C  CA    . GLY A 1 63  ? 21.089  -0.112  4.057   1.00 11.34  ? 63  GLY A CA    1 
ATOM   512  C  C     . GLY A 1 63  ? 21.139  -0.939  5.446   1.00 13.31  ? 63  GLY A C     1 
ATOM   513  O  O     . GLY A 1 63  ? 22.014  -1.786  5.605   1.00 13.34  ? 63  GLY A O     1 
ATOM   514  N  N     A HIS A 1 64  ? 20.374  -0.540  6.409   0.35 13.50  ? 64  HIS A N     1 
ATOM   515  N  N     B HIS A 1 64  ? 20.207  -0.661  6.299   0.65 13.71  ? 64  HIS A N     1 
ATOM   516  C  CA    A HIS A 1 64  ? 20.221  -1.383  7.566   0.35 11.45  ? 64  HIS A CA    1 
ATOM   517  C  CA    B HIS A 1 64  ? 20.099  -1.266  7.662   0.65 13.58  ? 64  HIS A CA    1 
ATOM   518  C  C     A HIS A 1 64  ? 18.846  -2.037  7.617   0.35 10.18  ? 64  HIS A C     1 
ATOM   519  C  C     B HIS A 1 64  ? 18.723  -1.828  7.918   0.65 10.90  ? 64  HIS A C     1 
ATOM   520  O  O     A HIS A 1 64  ? 18.838  -3.263  7.990   0.35 10.59  ? 64  HIS A O     1 
ATOM   521  O  O     B HIS A 1 64  ? 18.536  -2.740  8.774   0.65 10.57  ? 64  HIS A O     1 
ATOM   522  C  CB    A HIS A 1 64  ? 20.617  -0.708  8.904   0.35 9.06   ? 64  HIS A CB    1 
ATOM   523  C  CB    B HIS A 1 64  ? 20.352  -0.179  8.670   0.65 12.21  ? 64  HIS A CB    1 
ATOM   524  C  CG    A HIS A 1 64  ? 20.224  0.760   9.138   0.35 12.25  ? 64  HIS A CG    1 
ATOM   525  C  CG    B HIS A 1 64  ? 21.651  0.483   8.516   0.65 15.06  ? 64  HIS A CG    1 
ATOM   526  N  ND1   A HIS A 1 64  ? 19.227  1.286   10.042  0.35 11.25  ? 64  HIS A ND1   1 
ATOM   527  N  ND1   B HIS A 1 64  ? 21.769  1.836   8.398   0.65 22.57  ? 64  HIS A ND1   1 
ATOM   528  C  CD2   A HIS A 1 64  ? 20.841  1.829   8.584   0.35 11.24  ? 64  HIS A CD2   1 
ATOM   529  C  CD2   B HIS A 1 64  ? 22.897  -0.022  8.527   0.65 16.42  ? 64  HIS A CD2   1 
ATOM   530  C  CE1   A HIS A 1 64  ? 19.341  2.599   9.992   0.35 12.24  ? 64  HIS A CE1   1 
ATOM   531  C  CE1   B HIS A 1 64  ? 23.056  2.148   8.250   0.65 26.10  ? 64  HIS A CE1   1 
ATOM   532  N  NE2   A HIS A 1 64  ? 20.299  2.940   9.139   0.35 14.46  ? 64  HIS A NE2   1 
ATOM   533  N  NE2   B HIS A 1 64  ? 23.767  1.053   8.431   0.65 17.71  ? 64  HIS A NE2   1 
ATOM   534  N  N     . ALA A 1 65  ? 17.757  -1.307  7.239   1.00 11.60  ? 65  ALA A N     1 
ATOM   535  C  CA    . ALA A 1 65  ? 16.380  -1.723  7.284   1.00 10.85  ? 65  ALA A CA    1 
ATOM   536  C  C     . ALA A 1 65  ? 15.620  -1.020  6.152   1.00 9.04   ? 65  ALA A C     1 
ATOM   537  O  O     . ALA A 1 65  ? 16.316  -0.339  5.323   1.00 12.06  ? 65  ALA A O     1 
ATOM   538  C  CB    . ALA A 1 65  ? 15.809  -1.431  8.649   1.00 12.54  ? 65  ALA A CB    1 
ATOM   539  N  N     . PHE A 1 66  ? 14.321  -1.041  6.127   1.00 9.86   ? 66  PHE A N     1 
ATOM   540  C  CA    . PHE A 1 66  ? 13.601  -0.123  5.318   1.00 9.97   ? 66  PHE A CA    1 
ATOM   541  C  C     . PHE A 1 66  ? 12.705  0.748   6.211   1.00 10.89  ? 66  PHE A C     1 
ATOM   542  O  O     . PHE A 1 66  ? 12.073  0.278   7.173   1.00 10.62  ? 66  PHE A O     1 
ATOM   543  C  CB    . PHE A 1 66  ? 12.788  -0.878  4.236   1.00 10.14  ? 66  PHE A CB    1 
ATOM   544  C  CG    . PHE A 1 66  ? 11.726  -1.774  4.775   1.00 9.86   ? 66  PHE A CG    1 
ATOM   545  C  CD1   . PHE A 1 66  ? 10.509  -1.300  5.089   1.00 11.63  ? 66  PHE A CD1   1 
ATOM   546  C  CD2   . PHE A 1 66  ? 11.960  -3.130  4.919   1.00 10.91  ? 66  PHE A CD2   1 
ATOM   547  C  CE1   . PHE A 1 66  ? 9.552   -2.136  5.604   1.00 11.38  ? 66  PHE A CE1   1 
ATOM   548  C  CE2   . PHE A 1 66  ? 11.061  -4.001  5.464   1.00 11.71  ? 66  PHE A CE2   1 
ATOM   549  C  CZ    . PHE A 1 66  ? 9.773   -3.528  5.754   1.00 11.67  ? 66  PHE A CZ    1 
ATOM   550  N  N     . ASN A 1 67  ? 12.643  1.998   5.848   1.00 11.26  ? 67  ASN A N     1 
ATOM   551  C  CA    . ASN A 1 67  ? 11.842  2.964   6.569   1.00 10.29  ? 67  ASN A CA    1 
ATOM   552  C  C     . ASN A 1 67  ? 10.496  3.378   5.880   1.00 10.37  ? 67  ASN A C     1 
ATOM   553  O  O     . ASN A 1 67  ? 10.612  3.805   4.657   1.00 12.44  ? 67  ASN A O     1 
ATOM   554  C  CB    . ASN A 1 67  ? 12.491  4.230   6.925   1.00 13.24  ? 67  ASN A CB    1 
ATOM   555  C  CG    . ASN A 1 67  ? 13.590  4.120   7.861   1.00 13.18  ? 67  ASN A CG    1 
ATOM   556  O  OD1   . ASN A 1 67  ? 14.351  5.118   8.107   1.00 18.84  ? 67  ASN A OD1   1 
ATOM   557  N  ND2   . ASN A 1 67  ? 13.652  3.009   8.528   1.00 11.93  ? 67  ASN A ND2   1 
ATOM   558  N  N     . VAL A 1 68  ? 9.284   3.228   6.373   1.00 11.30  ? 68  VAL A N     1 
ATOM   559  C  CA    . VAL A 1 68  ? 8.065   3.792   5.852   1.00 8.92   ? 68  VAL A CA    1 
ATOM   560  C  C     . VAL A 1 68  ? 7.912   5.216   6.455   1.00 10.12  ? 68  VAL A C     1 
ATOM   561  O  O     . VAL A 1 68  ? 7.813   5.322   7.713   1.00 11.33  ? 68  VAL A O     1 
ATOM   562  C  CB    . VAL A 1 68  ? 6.808   2.981   6.023   1.00 12.48  ? 68  VAL A CB    1 
ATOM   563  C  CG1   . VAL A 1 68  ? 5.577   3.760   5.508   1.00 12.50  ? 68  VAL A CG1   1 
ATOM   564  C  CG2   . VAL A 1 68  ? 7.037   1.731   5.270   1.00 12.94  ? 68  VAL A CG2   1 
ATOM   565  N  N     . GLU A 1 69  ? 8.013   6.240   5.607   1.00 11.07  ? 69  GLU A N     1 
ATOM   566  C  CA    . GLU A 1 69  ? 8.163   7.646   6.098   1.00 11.66  ? 69  GLU A CA    1 
ATOM   567  C  C     . GLU A 1 69  ? 6.883   8.395   6.023   1.00 12.52  ? 69  GLU A C     1 
ATOM   568  O  O     . GLU A 1 69  ? 6.040   8.128   5.037   1.00 13.24  ? 69  GLU A O     1 
ATOM   569  C  CB    . GLU A 1 69  ? 9.114   8.374   5.190   1.00 12.10  ? 69  GLU A CB    1 
ATOM   570  C  CG    . GLU A 1 69  ? 10.555  7.860   5.240   1.00 11.34  ? 69  GLU A CG    1 
ATOM   571  C  CD    . GLU A 1 69  ? 11.381  8.249   4.150   1.00 13.69  ? 69  GLU A CD    1 
ATOM   572  O  OE1   . GLU A 1 69  ? 10.886  8.987   3.207   1.00 15.14  ? 69  GLU A OE1   1 
ATOM   573  O  OE2   . GLU A 1 69  ? 12.588  8.006   4.090   1.00 15.85  ? 69  GLU A OE2   1 
ATOM   574  N  N     . PHE A 1 70  ? 6.701   9.287   6.970   1.00 12.12  ? 70  PHE A N     1 
ATOM   575  C  CA    . PHE A 1 70  ? 5.484   10.039  7.061   1.00 11.40  ? 70  PHE A CA    1 
ATOM   576  C  C     . PHE A 1 70  ? 5.716   11.548  6.925   1.00 12.23  ? 70  PHE A C     1 
ATOM   577  O  O     . PHE A 1 70  ? 6.806   12.010  7.277   1.00 12.32  ? 70  PHE A O     1 
ATOM   578  C  CB    . PHE A 1 70  ? 4.767   9.707   8.362   1.00 10.99  ? 70  PHE A CB    1 
ATOM   579  C  CG    . PHE A 1 70  ? 4.171   8.321   8.353   1.00 10.89  ? 70  PHE A CG    1 
ATOM   580  C  CD1   . PHE A 1 70  ? 4.989   7.187   8.595   1.00 12.04  ? 70  PHE A CD1   1 
ATOM   581  C  CD2   . PHE A 1 70  ? 2.858   8.091   8.024   1.00 11.43  ? 70  PHE A CD2   1 
ATOM   582  C  CE1   . PHE A 1 70  ? 4.499   5.917   8.461   1.00 12.06  ? 70  PHE A CE1   1 
ATOM   583  C  CE2   . PHE A 1 70  ? 2.366   6.802   7.986   1.00 12.11  ? 70  PHE A CE2   1 
ATOM   584  C  CZ    . PHE A 1 70  ? 3.188   5.721   8.197   1.00 13.43  ? 70  PHE A CZ    1 
ATOM   585  N  N     . ASP A 1 71  ? 4.720   12.270  6.495   1.00 14.30  ? 71  ASP A N     1 
ATOM   586  C  CA    . ASP A 1 71  ? 4.749   13.714  6.569   1.00 12.90  ? 71  ASP A CA    1 
ATOM   587  C  C     . ASP A 1 71  ? 4.486   14.057  8.026   1.00 12.11  ? 71  ASP A C     1 
ATOM   588  O  O     . ASP A 1 71  ? 3.344   14.003  8.465   1.00 17.84  ? 71  ASP A O     1 
ATOM   589  C  CB    . ASP A 1 71  ? 3.665   14.266  5.691   1.00 19.10  ? 71  ASP A CB    1 
ATOM   590  C  CG    . ASP A 1 71  ? 3.440   15.741  5.901   1.00 21.19  ? 71  ASP A CG    1 
ATOM   591  O  OD1   . ASP A 1 71  ? 4.318   16.399  6.394   1.00 18.01  ? 71  ASP A OD1   1 
ATOM   592  O  OD2   . ASP A 1 71  ? 2.312   16.263  5.637   1.00 27.17  ? 71  ASP A OD2   1 
ATOM   593  N  N     . ASP A 1 72  ? 5.517   14.550  8.664   1.00 12.24  ? 72  ASP A N     1 
ATOM   594  C  CA    . ASP A 1 72  ? 5.452   14.997  10.064  1.00 13.40  ? 72  ASP A CA    1 
ATOM   595  C  C     . ASP A 1 72  ? 5.497   16.519  10.169  1.00 16.89  ? 72  ASP A C     1 
ATOM   596  O  O     . ASP A 1 72  ? 5.938   17.047  11.182  1.00 19.92  ? 72  ASP A O     1 
ATOM   597  C  CB    . ASP A 1 72  ? 6.545   14.322  10.925  1.00 14.46  ? 72  ASP A CB    1 
ATOM   598  C  CG    . ASP A 1 72  ? 7.906   14.687  10.521  1.00 19.52  ? 72  ASP A CG    1 
ATOM   599  O  OD1   . ASP A 1 72  ? 8.141   15.278  9.403   1.00 25.76  ? 72  ASP A OD1   1 
ATOM   600  O  OD2   . ASP A 1 72  ? 8.820   14.430  11.343  1.00 21.19  ? 72  ASP A OD2   1 
ATOM   601  N  N     . SER A 1 73  ? 5.005   17.250  9.138   1.00 15.48  ? 73  SER A N     1 
ATOM   602  C  CA    . SER A 1 73  ? 5.007   18.706  9.132   1.00 16.67  ? 73  SER A CA    1 
ATOM   603  C  C     . SER A 1 73  ? 3.734   19.276  9.790   1.00 20.60  ? 73  SER A C     1 
ATOM   604  O  O     . SER A 1 73  ? 3.578   20.509  9.944   1.00 19.58  ? 73  SER A O     1 
ATOM   605  C  CB    . SER A 1 73  ? 5.195   19.265  7.722   1.00 19.49  ? 73  SER A CB    1 
ATOM   606  O  OG    . SER A 1 73  ? 4.033   19.041  6.971   1.00 18.59  ? 73  SER A OG    1 
ATOM   607  N  N     . GLN A 1 74  ? 2.828   18.395  10.176  1.00 22.73  ? 74  GLN A N     1 
ATOM   608  C  CA    . GLN A 1 74  ? 1.733   18.833  11.048  1.00 26.31  ? 74  GLN A CA    1 
ATOM   609  C  C     . GLN A 1 74  ? 1.361   17.762  12.011  1.00 25.67  ? 74  GLN A C     1 
ATOM   610  O  O     . GLN A 1 74  ? 1.841   16.754  11.758  1.00 17.61  ? 74  GLN A O     1 
ATOM   611  C  CB    . GLN A 1 74  ? 0.566   19.000  10.118  1.00 27.99  ? 74  GLN A CB    1 
ATOM   612  C  CG    . GLN A 1 74  ? 0.684   19.927  9.022   1.00 31.02  ? 74  GLN A CG    1 
ATOM   613  C  CD    . GLN A 1 74  ? -0.657  20.220  8.606   1.00 32.84  ? 74  GLN A CD    1 
ATOM   614  O  OE1   . GLN A 1 74  ? -1.353  20.999  9.297   1.00 53.03  ? 74  GLN A OE1   1 
ATOM   615  N  NE2   . GLN A 1 74  ? -1.106  19.636  7.421   1.00 28.90  ? 74  GLN A NE2   1 
ATOM   616  N  N     . ASP A 1 75  ? 0.380   18.000  12.966  1.00 31.85  ? 75  ASP A N     1 
ATOM   617  C  CA    . ASP A 1 75  ? -0.009  16.963  13.978  1.00 31.23  ? 75  ASP A CA    1 
ATOM   618  C  C     . ASP A 1 75  ? -1.100  16.238  13.273  1.00 27.42  ? 75  ASP A C     1 
ATOM   619  O  O     . ASP A 1 75  ? -2.340  16.602  13.212  1.00 34.70  ? 75  ASP A O     1 
ATOM   620  C  CB    . ASP A 1 75  ? -0.576  17.329  15.382  1.00 32.99  ? 75  ASP A CB    1 
ATOM   621  C  CG    . ASP A 1 75  ? 0.502   17.658  16.382  1.00 39.21  ? 75  ASP A CG    1 
ATOM   622  O  OD1   . ASP A 1 75  ? 1.556   17.006  16.324  1.00 54.76  ? 75  ASP A OD1   1 
ATOM   623  O  OD2   . ASP A 1 75  ? 0.273   18.533  17.247  1.00 48.37  ? 75  ASP A OD2   1 
ATOM   624  N  N     . LYS A 1 76  ? -0.598  15.238  12.671  1.00 18.71  ? 76  LYS A N     1 
ATOM   625  C  CA    . LYS A 1 76  ? -1.421  14.228  11.908  1.00 21.51  ? 76  LYS A CA    1 
ATOM   626  C  C     . LYS A 1 76  ? -1.542  12.793  12.316  1.00 25.60  ? 76  LYS A C     1 
ATOM   627  O  O     . LYS A 1 76  ? -2.503  12.120  12.006  1.00 36.71  ? 76  LYS A O     1 
ATOM   628  C  CB    . LYS A 1 76  ? -0.937  14.135  10.516  1.00 25.49  ? 76  LYS A CB    1 
ATOM   629  C  CG    . LYS A 1 76  ? -1.290  15.346  9.651   1.00 28.14  ? 76  LYS A CG    1 
ATOM   630  C  CD    . LYS A 1 76  ? -0.868  14.940  8.247   1.00 35.49  ? 76  LYS A CD    1 
ATOM   631  C  CE    . LYS A 1 76  ? -0.911  16.065  7.229   1.00 28.87  ? 76  LYS A CE    1 
ATOM   632  N  NZ    . LYS A 1 76  ? -0.495  15.656  5.854   1.00 29.71  ? 76  LYS A NZ    1 
ATOM   633  N  N     . ALA A 1 77  ? -0.558  12.301  12.878  1.00 21.20  ? 77  ALA A N     1 
ATOM   634  C  CA    . ALA A 1 77  ? -0.409  10.912  13.437  1.00 15.21  ? 77  ALA A CA    1 
ATOM   635  C  C     . ALA A 1 77  ? 0.356   11.001  14.755  1.00 13.62  ? 77  ALA A C     1 
ATOM   636  O  O     . ALA A 1 77  ? 1.597   11.173  14.758  1.00 19.32  ? 77  ALA A O     1 
ATOM   637  C  CB    . ALA A 1 77  ? 0.381   10.186  12.394  1.00 18.27  ? 77  ALA A CB    1 
ATOM   638  N  N     . VAL A 1 78  ? -0.288  10.996  15.853  1.00 12.80  ? 78  VAL A N     1 
ATOM   639  C  CA    . VAL A 1 78  ? 0.354   11.286  17.124  1.00 12.61  ? 78  VAL A CA    1 
ATOM   640  C  C     . VAL A 1 78  ? 0.110   10.189  18.145  1.00 10.79  ? 78  VAL A C     1 
ATOM   641  O  O     . VAL A 1 78  ? -0.928  9.487   18.183  1.00 13.50  ? 78  VAL A O     1 
ATOM   642  C  CB    . VAL A 1 78  ? -0.008  12.656  17.650  1.00 17.78  ? 78  VAL A CB    1 
ATOM   643  C  CG1   . VAL A 1 78  ? 0.305   13.818  16.737  1.00 21.54  ? 78  VAL A CG1   1 
ATOM   644  C  CG2   . VAL A 1 78  ? -1.372  12.670  18.042  1.00 19.09  ? 78  VAL A CG2   1 
ATOM   645  N  N     . LEU A 1 79  ? 1.114   10.047  18.987  1.00 9.86   ? 79  LEU A N     1 
ATOM   646  C  CA    . LEU A 1 79  ? 1.070   9.190   20.142  1.00 10.05  ? 79  LEU A CA    1 
ATOM   647  C  C     . LEU A 1 79  ? 1.081   10.029  21.388  1.00 10.31  ? 79  LEU A C     1 
ATOM   648  O  O     . LEU A 1 79  ? 1.891   11.004  21.457  1.00 12.43  ? 79  LEU A O     1 
ATOM   649  C  CB    . LEU A 1 79  ? 2.321   8.283   20.084  1.00 10.84  ? 79  LEU A CB    1 
ATOM   650  C  CG    . LEU A 1 79  ? 2.443   7.215   21.122  1.00 12.04  ? 79  LEU A CG    1 
ATOM   651  C  CD1   . LEU A 1 79  ? 1.417   6.181   20.902  1.00 15.68  ? 79  LEU A CD1   1 
ATOM   652  C  CD2   . LEU A 1 79  ? 3.817   6.541   20.994  1.00 11.66  ? 79  LEU A CD2   1 
ATOM   653  N  N     . LYS A 1 80  ? 0.219   9.738   22.314  1.00 10.78  ? 80  LYS A N     1 
ATOM   654  C  CA    . LYS A 1 80  ? 0.075   10.487  23.566  1.00 12.04  ? 80  LYS A CA    1 
ATOM   655  C  C     . LYS A 1 80  ? -0.357  9.524   24.604  1.00 10.43  ? 80  LYS A C     1 
ATOM   656  O  O     . LYS A 1 80  ? -0.646  8.328   24.358  1.00 10.98  ? 80  LYS A O     1 
ATOM   657  C  CB    . LYS A 1 80  ? -0.988  11.629  23.412  1.00 18.33  ? 80  LYS A CB    1 
ATOM   658  C  CG    . LYS A 1 80  ? -0.839  12.668  22.319  1.00 22.39  ? 80  LYS A CG    1 
ATOM   659  C  CD    . LYS A 1 80  ? -2.151  13.513  22.352  1.00 32.45  ? 80  LYS A CD    1 
ATOM   660  C  CE    . LYS A 1 80  ? -2.179  14.287  23.705  1.00 45.42  ? 80  LYS A CE    1 
ATOM   661  N  NZ    . LYS A 1 80  ? -2.954  15.585  23.788  1.00 52.67  ? 80  LYS A NZ    1 
ATOM   662  N  N     . GLY A 1 81  ? -0.459  10.022  25.834  1.00 11.95  ? 81  GLY A N     1 
ATOM   663  C  CA    . GLY A 1 81  ? -0.966  9.149   26.921  1.00 12.26  ? 81  GLY A CA    1 
ATOM   664  C  C     . GLY A 1 81  ? 0.022   8.113   27.252  1.00 11.49  ? 81  GLY A C     1 
ATOM   665  O  O     . GLY A 1 81  ? 1.230   8.279   27.094  1.00 11.19  ? 81  GLY A O     1 
ATOM   666  N  N     . GLY A 1 82  ? -0.448  7.029   27.796  1.00 14.80  ? 82  GLY A N     1 
ATOM   667  C  CA    . GLY A 1 82  ? 0.449   6.019   28.242  1.00 16.67  ? 82  GLY A CA    1 
ATOM   668  C  C     . GLY A 1 82  ? 1.335   6.566   29.332  1.00 14.88  ? 82  GLY A C     1 
ATOM   669  O  O     . GLY A 1 82  ? 0.845   7.201   30.238  1.00 18.92  ? 82  GLY A O     1 
ATOM   670  N  N     . PRO A 1 83  ? 2.687   6.388   29.238  1.00 11.70  ? 83  PRO A N     1 
ATOM   671  C  CA    . PRO A 1 83  ? 3.647   6.971   30.154  1.00 11.97  ? 83  PRO A CA    1 
ATOM   672  C  C     . PRO A 1 83  ? 4.019   8.414   29.775  1.00 11.89  ? 83  PRO A C     1 
ATOM   673  O  O     . PRO A 1 83  ? 4.890   9.021   30.454  1.00 14.96  ? 83  PRO A O     1 
ATOM   674  C  CB    . PRO A 1 83  ? 4.882   6.068   29.979  1.00 11.96  ? 83  PRO A CB    1 
ATOM   675  C  CG    . PRO A 1 83  ? 4.861   5.716   28.537  1.00 9.86   ? 83  PRO A CG    1 
ATOM   676  C  CD    . PRO A 1 83  ? 3.379   5.555   28.227  1.00 10.35  ? 83  PRO A CD    1 
ATOM   677  N  N     . LEU A 1 84  ? 3.524   8.933   28.676  1.00 9.73   ? 84  LEU A N     1 
ATOM   678  C  CA    . LEU A 1 84  ? 4.057   10.125  28.076  1.00 9.62   ? 84  LEU A CA    1 
ATOM   679  C  C     . LEU A 1 84  ? 3.423   11.387  28.678  1.00 12.65  ? 84  LEU A C     1 
ATOM   680  O  O     . LEU A 1 84  ? 2.246   11.383  28.942  1.00 16.09  ? 84  LEU A O     1 
ATOM   681  C  CB    . LEU A 1 84  ? 3.825   10.097  26.597  1.00 8.44   ? 84  LEU A CB    1 
ATOM   682  C  CG    . LEU A 1 84  ? 4.360   8.858   25.866  1.00 8.65   ? 84  LEU A CG    1 
ATOM   683  C  CD1   . LEU A 1 84  ? 3.902   8.840   24.441  1.00 9.75   ? 84  LEU A CD1   1 
ATOM   684  C  CD2   . LEU A 1 84  ? 5.911   8.853   25.929  1.00 8.62   ? 84  LEU A CD2   1 
ATOM   685  N  N     . ASP A 1 85  ? 4.118   12.482  28.635  1.00 12.84  ? 85  ASP A N     1 
ATOM   686  C  CA    . ASP A 1 85  ? 3.638   13.839  28.877  1.00 15.63  ? 85  ASP A CA    1 
ATOM   687  C  C     . ASP A 1 85  ? 3.694   14.456  27.416  1.00 16.59  ? 85  ASP A C     1 
ATOM   688  O  O     . ASP A 1 85  ? 4.774   14.421  26.756  1.00 24.56  ? 85  ASP A O     1 
ATOM   689  C  CB    . ASP A 1 85  ? 4.584   14.581  29.857  1.00 21.74  ? 85  ASP A CB    1 
ATOM   690  C  CG    . ASP A 1 85  ? 4.551   14.035  31.133  1.00 29.83  ? 85  ASP A CG    1 
ATOM   691  O  OD1   . ASP A 1 85  ? 3.401   13.766  31.579  1.00 53.43  ? 85  ASP A OD1   1 
ATOM   692  O  OD2   . ASP A 1 85  ? 5.684   13.920  31.696  1.00 54.13  ? 85  ASP A OD2   1 
ATOM   693  N  N     . GLY A 1 86  ? 2.677   15.118  26.986  1.00 22.00  ? 86  GLY A N     1 
ATOM   694  C  CA    . GLY A 1 86  ? 2.711   15.754  25.793  1.00 20.36  ? 86  GLY A CA    1 
ATOM   695  C  C     . GLY A 1 86  ? 2.521   14.814  24.579  1.00 19.98  ? 86  GLY A C     1 
ATOM   696  O  O     . GLY A 1 86  ? 2.041   13.603  24.702  1.00 23.46  ? 86  GLY A O     1 
ATOM   697  N  N     . THR A 1 87  ? 2.888   15.338  23.429  1.00 13.31  ? 87  THR A N     1 
ATOM   698  C  CA    . THR A 1 87  ? 2.422   14.855  22.140  1.00 13.55  ? 87  THR A CA    1 
ATOM   699  C  C     . THR A 1 87  ? 3.615   14.503  21.297  1.00 10.97  ? 87  THR A C     1 
ATOM   700  O  O     . THR A 1 87  ? 4.548   15.299  21.138  1.00 12.21  ? 87  THR A O     1 
ATOM   701  C  CB    . THR A 1 87  ? 1.639   16.074  21.437  1.00 20.93  ? 87  THR A CB    1 
ATOM   702  O  OG1   . THR A 1 87  ? 0.431   16.248  22.174  1.00 30.77  ? 87  THR A OG1   1 
ATOM   703  C  CG2   . THR A 1 87  ? 1.318   15.701  19.953  1.00 21.80  ? 87  THR A CG2   1 
ATOM   704  N  N     . TYR A 1 88  ? 3.578   13.319  20.697  1.00 9.02   ? 88  TYR A N     1 
ATOM   705  C  CA    . TYR A 1 88  ? 4.659   12.817  19.927  1.00 9.06   ? 88  TYR A CA    1 
ATOM   706  C  C     . TYR A 1 88  ? 4.195   12.443  18.498  1.00 9.62   ? 88  TYR A C     1 
ATOM   707  O  O     . TYR A 1 88  ? 3.251   11.763  18.284  1.00 12.66  ? 88  TYR A O     1 
ATOM   708  C  CB    . TYR A 1 88  ? 5.317   11.627  20.560  1.00 8.58   ? 88  TYR A CB    1 
ATOM   709  C  CG    . TYR A 1 88  ? 6.025   11.819  21.891  1.00 8.53   ? 88  TYR A CG    1 
ATOM   710  C  CD1   . TYR A 1 88  ? 5.374   12.114  23.060  1.00 9.05   ? 88  TYR A CD1   1 
ATOM   711  C  CD2   . TYR A 1 88  ? 7.413   11.709  21.945  1.00 7.89   ? 88  TYR A CD2   1 
ATOM   712  C  CE1   . TYR A 1 88  ? 6.030   12.308  24.208  1.00 8.89   ? 88  TYR A CE1   1 
ATOM   713  C  CE2   . TYR A 1 88  ? 8.086   11.834  23.120  1.00 7.89   ? 88  TYR A CE2   1 
ATOM   714  C  CZ    . TYR A 1 88  ? 7.408   12.127  24.269  1.00 7.77   ? 88  TYR A CZ    1 
ATOM   715  O  OH    . TYR A 1 88  ? 8.103   12.214  25.456  1.00 8.42   ? 88  TYR A OH    1 
ATOM   716  N  N     . ARG A 1 89  ? 4.892   13.017  17.522  1.00 9.56   ? 89  ARG A N     1 
ATOM   717  C  CA    . ARG A 1 89  ? 4.431   12.896  16.094  1.00 9.38   ? 89  ARG A CA    1 
ATOM   718  C  C     . ARG A 1 89  ? 5.152   11.776  15.428  1.00 7.48   ? 89  ARG A C     1 
ATOM   719  O  O     . ARG A 1 89  ? 6.393   11.675  15.489  1.00 7.63   ? 89  ARG A O     1 
ATOM   720  C  CB    . ARG A 1 89  ? 4.895   14.188  15.405  1.00 14.37  ? 89  ARG A CB    1 
ATOM   721  C  CG    . ARG A 1 89  ? 4.117   15.236  15.135  1.00 22.93  ? 89  ARG A CG    1 
ATOM   722  C  CD    . ARG A 1 89  ? 4.254   15.914  13.829  1.00 18.40  ? 89  ARG A CD    1 
ATOM   723  N  NE    . ARG A 1 89  ? 3.577   16.949  14.447  1.00 23.08  ? 89  ARG A NE    1 
ATOM   724  C  CZ    . ARG A 1 89  ? 3.695   18.209  14.219  1.00 25.66  ? 89  ARG A CZ    1 
ATOM   725  N  NH1   . ARG A 1 89  ? 4.572   18.619  13.382  1.00 29.56  ? 89  ARG A NH1   1 
ATOM   726  N  NH2   . ARG A 1 89  ? 2.997   18.989  15.012  1.00 29.23  ? 89  ARG A NH2   1 
ATOM   727  N  N     . LEU A 1 90  ? 4.424   10.959  14.679  1.00 7.93   ? 90  LEU A N     1 
ATOM   728  C  CA    . LEU A 1 90  ? 4.979   9.857   13.912  1.00 7.32   ? 90  LEU A CA    1 
ATOM   729  C  C     . LEU A 1 90  ? 5.856   10.394  12.799  1.00 7.62   ? 90  LEU A C     1 
ATOM   730  O  O     . LEU A 1 90  ? 5.385   11.179  11.966  1.00 10.33  ? 90  LEU A O     1 
ATOM   731  C  CB    . LEU A 1 90  ? 3.877   9.028   13.332  1.00 7.33   ? 90  LEU A CB    1 
ATOM   732  C  CG    . LEU A 1 90  ? 4.299   7.826   12.475  1.00 8.50   ? 90  LEU A CG    1 
ATOM   733  C  CD1   . LEU A 1 90  ? 5.084   6.758   13.252  1.00 9.53   ? 90  LEU A CD1   1 
ATOM   734  C  CD2   . LEU A 1 90  ? 3.098   7.134   11.841  1.00 10.36  ? 90  LEU A CD2   1 
ATOM   735  N  N     . ILE A 1 91  ? 7.105   9.918   12.704  1.00 7.50   ? 91  ILE A N     1 
ATOM   736  C  CA    . ILE A 1 91  ? 7.996   10.243  11.569  1.00 8.06   ? 91  ILE A CA    1 
ATOM   737  C  C     . ILE A 1 91  ? 8.287   9.049   10.686  1.00 7.68   ? 91  ILE A C     1 
ATOM   738  O  O     . ILE A 1 91  ? 8.382   9.245   9.482   1.00 8.03   ? 91  ILE A O     1 
ATOM   739  C  CB    . ILE A 1 91  ? 9.297   10.899  12.096  1.00 9.45   ? 91  ILE A CB    1 
ATOM   740  C  CG1   . ILE A 1 91  ? 10.289  11.195  10.963  1.00 12.19  ? 91  ILE A CG1   1 
ATOM   741  C  CG2   . ILE A 1 91  ? 10.011  10.096  13.187  1.00 9.84   ? 91  ILE A CG2   1 
ATOM   742  C  CD1   . ILE A 1 91  ? 11.400  12.111  11.334  1.00 16.24  ? 91  ILE A CD1   1 
ATOM   743  N  N     . GLN A 1 92  ? 8.422   7.836   11.239  1.00 7.34   ? 92  GLN A N     1 
ATOM   744  C  CA    . GLN A 1 92  ? 8.716   6.669   10.375  1.00 8.95   ? 92  GLN A CA    1 
ATOM   745  C  C     . GLN A 1 92  ? 8.459   5.445   11.146  1.00 7.93   ? 92  GLN A C     1 
ATOM   746  O  O     . GLN A 1 92  ? 8.423   5.465   12.398  1.00 7.47   ? 92  GLN A O     1 
ATOM   747  C  CB    . GLN A 1 92  ? 10.034  6.614   9.774   1.00 11.17  ? 92  GLN A CB    1 
ATOM   748  C  CG    . GLN A 1 92  ? 11.166  6.834   10.730  1.00 11.90  ? 92  GLN A CG    1 
ATOM   749  C  CD    . GLN A 1 92  ? 11.972  5.479   11.144  1.00 10.89  ? 92  GLN A CD    1 
ATOM   750  O  OE1   . GLN A 1 92  ? 11.433  4.416   11.257  1.00 10.35  ? 92  GLN A OE1   1 
ATOM   751  N  NE2   . GLN A 1 92  ? 13.071  5.672   11.616  1.00 14.85  ? 92  GLN A NE2   1 
ATOM   752  N  N     . PHE A 1 93  ? 8.313   4.349   10.423  1.00 7.89   ? 93  PHE A N     1 
ATOM   753  C  CA    . PHE A 1 93  ? 8.372   3.027   11.040  1.00 7.29   ? 93  PHE A CA    1 
ATOM   754  C  C     . PHE A 1 93  ? 9.374   2.183   10.256  1.00 8.00   ? 93  PHE A C     1 
ATOM   755  O  O     . PHE A 1 93  ? 9.609   2.375   9.057   1.00 10.34  ? 93  PHE A O     1 
ATOM   756  C  CB    . PHE A 1 93  ? 7.045   2.329   11.280  1.00 7.81   ? 93  PHE A CB    1 
ATOM   757  C  CG    . PHE A 1 93  ? 6.293   1.853   10.032  1.00 8.83   ? 93  PHE A CG    1 
ATOM   758  C  CD1   . PHE A 1 93  ? 6.640   0.686   9.372   1.00 9.83   ? 93  PHE A CD1   1 
ATOM   759  C  CD2   . PHE A 1 93  ? 5.175   2.523   9.601   1.00 10.74  ? 93  PHE A CD2   1 
ATOM   760  C  CE1   . PHE A 1 93  ? 5.953   0.269   8.266   1.00 11.13  ? 93  PHE A CE1   1 
ATOM   761  C  CE2   . PHE A 1 93  ? 4.419   2.044   8.516   1.00 10.25  ? 93  PHE A CE2   1 
ATOM   762  C  CZ    . PHE A 1 93  ? 4.831   0.979   7.842   1.00 11.49  ? 93  PHE A CZ    1 
ATOM   763  N  N     . HIS A 1 94  ? 9.891   1.178   10.946  1.00 7.08   ? 94  HIS A N     1 
ATOM   764  C  CA    . HIS A 1 94  ? 10.743  0.205   10.350  1.00 6.91   ? 94  HIS A CA    1 
ATOM   765  C  C     . HIS A 1 94  ? 10.694  -1.051  11.158  1.00 6.18   ? 94  HIS A C     1 
ATOM   766  O  O     . HIS A 1 94  ? 10.085  -1.078  12.222  1.00 7.21   ? 94  HIS A O     1 
ATOM   767  C  CB    . HIS A 1 94  ? 12.202  0.684   10.291  1.00 8.02   ? 94  HIS A CB    1 
ATOM   768  C  CG    . HIS A 1 94  ? 12.784  0.996   11.654  1.00 7.69   ? 94  HIS A CG    1 
ATOM   769  N  ND1   . HIS A 1 94  ? 12.631  2.201   12.307  1.00 7.22   ? 94  HIS A ND1   1 
ATOM   770  C  CD2   . HIS A 1 94  ? 13.346  0.160   12.559  1.00 6.85   ? 94  HIS A CD2   1 
ATOM   771  C  CE1   . HIS A 1 94  ? 13.104  2.103   13.529  1.00 7.13   ? 94  HIS A CE1   1 
ATOM   772  N  NE2   . HIS A 1 94  ? 13.520  0.860   13.701  1.00 6.49   ? 94  HIS A NE2   1 
ATOM   773  N  N     . PHE A 1 95  ? 11.366  -2.118  10.682  1.00 6.51   ? 95  PHE A N     1 
ATOM   774  C  CA    . PHE A 1 95  ? 11.376  -3.368  11.359  1.00 6.89   ? 95  PHE A CA    1 
ATOM   775  C  C     . PHE A 1 95  ? 12.853  -3.862  11.572  1.00 6.94   ? 95  PHE A C     1 
ATOM   776  O  O     . PHE A 1 95  ? 13.773  -3.381  10.917  1.00 7.89   ? 95  PHE A O     1 
ATOM   777  C  CB    . PHE A 1 95  ? 10.649  -4.465  10.534  1.00 7.78   ? 95  PHE A CB    1 
ATOM   778  C  CG    . PHE A 1 95  ? 9.230   -4.186  10.225  1.00 7.37   ? 95  PHE A CG    1 
ATOM   779  C  CD1   . PHE A 1 95  ? 8.868   -3.332  9.179   1.00 8.11   ? 95  PHE A CD1   1 
ATOM   780  C  CD2   . PHE A 1 95  ? 8.210   -4.842  10.878  1.00 8.17   ? 95  PHE A CD2   1 
ATOM   781  C  CE1   . PHE A 1 95  ? 7.579   -3.134  8.860   1.00 8.30   ? 95  PHE A CE1   1 
ATOM   782  C  CE2   . PHE A 1 95  ? 6.890   -4.640  10.548  1.00 8.76   ? 95  PHE A CE2   1 
ATOM   783  C  CZ    . PHE A 1 95  ? 6.591   -3.794  9.519   1.00 7.91   ? 95  PHE A CZ    1 
ATOM   784  N  N     . HIS A 1 96  ? 12.951  -4.834  12.479  1.00 6.16   ? 96  HIS A N     1 
ATOM   785  C  CA    . HIS A 1 96  ? 14.119  -5.630  12.633  1.00 6.39   ? 96  HIS A CA    1 
ATOM   786  C  C     . HIS A 1 96  ? 13.699  -7.094  12.511  1.00 6.49   ? 96  HIS A C     1 
ATOM   787  O  O     . HIS A 1 96  ? 12.603  -7.445  12.997  1.00 6.30   ? 96  HIS A O     1 
ATOM   788  C  CB    . HIS A 1 96  ? 14.820  -5.419  14.014  1.00 6.69   ? 96  HIS A CB    1 
ATOM   789  C  CG    . HIS A 1 96  ? 15.089  -4.007  14.295  1.00 6.10   ? 96  HIS A CG    1 
ATOM   790  N  ND1   . HIS A 1 96  ? 16.269  -3.413  14.023  1.00 6.85   ? 96  HIS A ND1   1 
ATOM   791  C  CD2   . HIS A 1 96  ? 14.302  -3.011  14.747  1.00 5.69   ? 96  HIS A CD2   1 
ATOM   792  C  CE1   . HIS A 1 96  ? 16.232  -2.134  14.370  1.00 6.95   ? 96  HIS A CE1   1 
ATOM   793  N  NE2   . HIS A 1 96  ? 15.038  -1.852  14.787  1.00 6.49   ? 96  HIS A NE2   1 
ATOM   794  N  N     . TRP A 1 97  ? 14.498  -7.941  11.850  1.00 6.04   ? 97  TRP A N     1 
ATOM   795  C  CA    . TRP A 1 97  ? 14.103  -9.325  11.657  1.00 6.33   ? 97  TRP A CA    1 
ATOM   796  C  C     . TRP A 1 97  ? 15.283  -10.204 11.518  1.00 6.33   ? 97  TRP A C     1 
ATOM   797  O  O     . TRP A 1 97  ? 16.444  -9.800  11.436  1.00 6.94   ? 97  TRP A O     1 
ATOM   798  C  CB    . TRP A 1 97  ? 13.185  -9.438  10.416  1.00 7.23   ? 97  TRP A CB    1 
ATOM   799  C  CG    . TRP A 1 97  ? 13.838  -9.021  9.131   1.00 6.98   ? 97  TRP A CG    1 
ATOM   800  C  CD1   . TRP A 1 97  ? 14.548  -9.822  8.273   1.00 7.87   ? 97  TRP A CD1   1 
ATOM   801  C  CD2   . TRP A 1 97  ? 13.891  -7.738  8.552   1.00 7.21   ? 97  TRP A CD2   1 
ATOM   802  N  NE1   . TRP A 1 97  ? 14.974  -9.139  7.181   1.00 8.32   ? 97  TRP A NE1   1 
ATOM   803  C  CE2   . TRP A 1 97  ? 14.611  -7.832  7.357   1.00 8.58   ? 97  TRP A CE2   1 
ATOM   804  C  CE3   . TRP A 1 97  ? 13.381  -6.486  8.923   1.00 6.73   ? 97  TRP A CE3   1 
ATOM   805  C  CZ2   . TRP A 1 97  ? 14.832  -6.732  6.487   1.00 8.91   ? 97  TRP A CZ2   1 
ATOM   806  C  CZ3   . TRP A 1 97  ? 13.651  -5.393  8.113   1.00 8.40   ? 97  TRP A CZ3   1 
ATOM   807  C  CH2   . TRP A 1 97  ? 14.347  -5.518  6.932   1.00 8.07   ? 97  TRP A CH2   1 
ATOM   808  N  N     . GLY A 1 98  ? 15.013  -11.517 11.539  1.00 6.85   ? 98  GLY A N     1 
ATOM   809  C  CA    . GLY A 1 98  ? 15.991  -12.537 11.584  1.00 7.04   ? 98  GLY A CA    1 
ATOM   810  C  C     . GLY A 1 98  ? 16.232  -13.199 10.280  1.00 7.87   ? 98  GLY A C     1 
ATOM   811  O  O     . GLY A 1 98  ? 15.475  -13.087 9.297   1.00 8.46   ? 98  GLY A O     1 
ATOM   812  N  N     . SER A 1 99  ? 17.248  -14.092 10.280  1.00 7.52   ? 99  SER A N     1 
ATOM   813  C  CA    . SER A 1 99  ? 17.461  -15.021 9.186   1.00 8.62   ? 99  SER A CA    1 
ATOM   814  C  C     . SER A 1 99  ? 16.492  -16.213 9.257   1.00 9.30   ? 99  SER A C     1 
ATOM   815  O  O     . SER A 1 99  ? 16.331  -16.886 8.248   1.00 11.82  ? 99  SER A O     1 
ATOM   816  C  CB    . SER A 1 99  ? 18.890  -15.462 9.196   1.00 9.71   ? 99  SER A CB    1 
ATOM   817  O  OG    . SER A 1 99  ? 19.356  -15.909 10.429  1.00 10.84  ? 99  SER A OG    1 
ATOM   818  N  N     . LEU A 1 100 ? 15.974  -16.514 10.443  1.00 8.24   ? 100 LEU A N     1 
ATOM   819  C  CA    . LEU A 1 100 ? 15.068  -17.608 10.722  1.00 10.11  ? 100 LEU A CA    1 
ATOM   820  C  C     . LEU A 1 100 ? 14.060  -17.097 11.680  1.00 8.75   ? 100 LEU A C     1 
ATOM   821  O  O     . LEU A 1 100 ? 14.264  -16.101 12.350  1.00 8.84   ? 100 LEU A O     1 
ATOM   822  C  CB    . LEU A 1 100 ? 15.787  -18.784 11.327  1.00 14.41  ? 100 LEU A CB    1 
ATOM   823  C  CG    . LEU A 1 100 ? 17.081  -19.269 10.739  1.00 21.68  ? 100 LEU A CG    1 
ATOM   824  C  CD1   . LEU A 1 100 ? 17.999  -20.073 11.692  1.00 30.46  ? 100 LEU A CD1   1 
ATOM   825  C  CD2   . LEU A 1 100 ? 16.554  -20.224 9.765   1.00 28.32  ? 100 LEU A CD2   1 
ATOM   826  N  N     . ASP A 1 101 ? 12.942  -17.816 11.862  1.00 9.31   ? 101 ASP A N     1 
ATOM   827  C  CA    . ASP A 1 101 ? 11.807  -17.293 12.619  1.00 9.98   ? 101 ASP A CA    1 
ATOM   828  C  C     . ASP A 1 101 ? 12.115  -17.216 14.116  1.00 9.46   ? 101 ASP A C     1 
ATOM   829  O  O     . ASP A 1 101 ? 11.481  -16.445 14.827  1.00 10.86  ? 101 ASP A O     1 
ATOM   830  C  CB    . ASP A 1 101 ? 10.534  -18.121 12.455  1.00 11.02  ? 101 ASP A CB    1 
ATOM   831  C  CG    . ASP A 1 101 ? 9.969   -18.108 11.072  1.00 13.72  ? 101 ASP A CG    1 
ATOM   832  O  OD1   . ASP A 1 101 ? 10.381  -17.355 10.206  1.00 12.36  ? 101 ASP A OD1   1 
ATOM   833  O  OD2   . ASP A 1 101 ? 9.049   -18.961 10.902  1.00 17.97  ? 101 ASP A OD2   1 
ATOM   834  N  N     . GLY A 1 102 ? 13.117  -17.980 14.573  1.00 10.41  ? 102 GLY A N     1 
ATOM   835  C  CA    . GLY A 1 102 ? 13.528  -18.030 15.973  1.00 10.70  ? 102 GLY A CA    1 
ATOM   836  C  C     . GLY A 1 102 ? 14.336  -16.850 16.503  1.00 9.57   ? 102 GLY A C     1 
ATOM   837  O  O     . GLY A 1 102 ? 14.720  -16.832 17.683  1.00 11.53  ? 102 GLY A O     1 
ATOM   838  N  N     A GLN A 1 103 ? 14.621  -15.878 15.679  0.50 8.36   ? 103 GLN A N     1 
ATOM   839  N  N     B GLN A 1 103 ? 14.546  -15.855 15.677  0.50 8.87   ? 103 GLN A N     1 
ATOM   840  C  CA    A GLN A 1 103 ? 15.271  -14.666 16.156  0.50 8.32   ? 103 GLN A CA    1 
ATOM   841  C  CA    B GLN A 1 103 ? 15.286  -14.675 16.077  0.50 8.71   ? 103 GLN A CA    1 
ATOM   842  C  C     A GLN A 1 103 ? 14.854  -13.526 15.235  0.50 6.54   ? 103 GLN A C     1 
ATOM   843  C  C     B GLN A 1 103 ? 14.869  -13.509 15.186  0.50 6.83   ? 103 GLN A C     1 
ATOM   844  O  O     A GLN A 1 103 ? 14.297  -13.761 14.184  0.50 8.80   ? 103 GLN A O     1 
ATOM   845  O  O     B GLN A 1 103 ? 14.351  -13.696 14.096  0.50 8.62   ? 103 GLN A O     1 
ATOM   846  C  CB    A GLN A 1 103 ? 16.799  -14.790 16.272  0.50 8.80   ? 103 GLN A CB    1 
ATOM   847  C  CB    B GLN A 1 103 ? 16.801  -14.886 16.028  0.50 9.78   ? 103 GLN A CB    1 
ATOM   848  C  CG    A GLN A 1 103 ? 17.479  -15.088 14.937  0.50 9.92   ? 103 GLN A CG    1 
ATOM   849  C  CG    B GLN A 1 103 ? 17.326  -15.186 14.637  0.50 10.81  ? 103 GLN A CG    1 
ATOM   850  C  CD    A GLN A 1 103 ? 18.975  -15.368 15.058  0.50 11.05  ? 103 GLN A CD    1 
ATOM   851  C  CD    B GLN A 1 103 ? 18.678  -15.898 14.655  0.50 12.62  ? 103 GLN A CD    1 
ATOM   852  O  OE1   A GLN A 1 103 ? 19.729  -15.048 14.137  0.50 13.32  ? 103 GLN A OE1   1 
ATOM   853  O  OE1   B GLN A 1 103 ? 18.847  -16.913 15.377  0.50 15.68  ? 103 GLN A OE1   1 
ATOM   854  N  NE2   A GLN A 1 103 ? 19.387  -15.971 16.172  0.50 11.02  ? 103 GLN A NE2   1 
ATOM   855  N  NE2   B GLN A 1 103 ? 19.637  -15.357 13.903  0.50 16.08  ? 103 GLN A NE2   1 
ATOM   856  N  N     . GLY A 1 104 ? 15.120  -12.296 15.659  1.00 7.18   ? 104 GLY A N     1 
ATOM   857  C  CA    . GLY A 1 104 ? 14.792  -11.122 14.903  1.00 7.02   ? 104 GLY A CA    1 
ATOM   858  C  C     . GLY A 1 104 ? 14.394  -9.953  15.724  1.00 6.49   ? 104 GLY A C     1 
ATOM   859  O  O     . GLY A 1 104 ? 14.632  -8.825  15.353  1.00 7.40   ? 104 GLY A O     1 
ATOM   860  N  N     . SER A 1 105 ? 13.689  -10.215 16.844  1.00 5.84   ? 105 SER A N     1 
ATOM   861  C  CA    . SER A 1 105 ? 13.296  -9.100  17.679  1.00 5.91   ? 105 SER A CA    1 
ATOM   862  C  C     . SER A 1 105 ? 14.501  -8.554  18.434  1.00 5.60   ? 105 SER A C     1 
ATOM   863  O  O     . SER A 1 105 ? 15.516  -9.231  18.637  1.00 6.77   ? 105 SER A O     1 
ATOM   864  C  CB    . SER A 1 105 ? 12.169  -9.467  18.620  1.00 6.03   ? 105 SER A CB    1 
ATOM   865  O  OG    . SER A 1 105 ? 12.523  -10.389 19.615  1.00 6.43   ? 105 SER A OG    1 
ATOM   866  N  N     . GLU A 1 106 ? 14.346  -7.304  18.839  1.00 5.59   ? 106 GLU A N     1 
ATOM   867  C  CA    . GLU A 1 106 ? 15.335  -6.600  19.664  1.00 5.44   ? 106 GLU A CA    1 
ATOM   868  C  C     . GLU A 1 106 ? 15.027  -6.773  21.139  1.00 5.39   ? 106 GLU A C     1 
ATOM   869  O  O     . GLU A 1 106 ? 15.819  -7.328  21.881  1.00 6.14   ? 106 GLU A O     1 
ATOM   870  C  CB    . GLU A 1 106 ? 15.406  -5.140  19.202  1.00 5.51   ? 106 GLU A CB    1 
ATOM   871  C  CG    . GLU A 1 106 ? 15.990  -4.998  17.798  1.00 7.49   ? 106 GLU A CG    1 
ATOM   872  C  CD    . GLU A 1 106 ? 16.568  -3.696  17.497  1.00 5.73   ? 106 GLU A CD    1 
ATOM   873  O  OE1   . GLU A 1 106 ? 15.953  -2.648  17.791  1.00 6.15   ? 106 GLU A OE1   1 
ATOM   874  O  OE2   . GLU A 1 106 ? 17.696  -3.727  16.922  1.00 7.61   ? 106 GLU A OE2   1 
ATOM   875  N  N     . HIS A 1 107 ? 13.848  -6.279  21.560  1.00 5.08   ? 107 HIS A N     1 
ATOM   876  C  CA    . HIS A 1 107 ? 13.364  -6.690  22.854  1.00 5.18   ? 107 HIS A CA    1 
ATOM   877  C  C     . HIS A 1 107 ? 13.082  -8.145  22.886  1.00 5.53   ? 107 HIS A C     1 
ATOM   878  O  O     . HIS A 1 107 ? 12.739  -8.780  21.860  1.00 6.13   ? 107 HIS A O     1 
ATOM   879  C  CB    . HIS A 1 107 ? 12.125  -5.879  23.225  1.00 5.37   ? 107 HIS A CB    1 
ATOM   880  C  CG    . HIS A 1 107 ? 12.459  -4.414  23.355  1.00 5.08   ? 107 HIS A CG    1 
ATOM   881  N  ND1   . HIS A 1 107 ? 12.410  -3.537  22.320  1.00 5.87   ? 107 HIS A ND1   1 
ATOM   882  C  CD2   . HIS A 1 107 ? 12.910  -3.694  24.430  1.00 5.17   ? 107 HIS A CD2   1 
ATOM   883  C  CE1   . HIS A 1 107 ? 12.825  -2.353  22.766  1.00 5.95   ? 107 HIS A CE1   1 
ATOM   884  N  NE2   . HIS A 1 107 ? 13.159  -2.420  24.031  1.00 5.31   ? 107 HIS A NE2   1 
ATOM   885  N  N     . THR A 1 108 ? 13.220  -8.731  24.053  1.00 6.37   ? 108 THR A N     1 
ATOM   886  C  CA    . THR A 1 108 ? 12.854  -10.099 24.325  1.00 6.47   ? 108 THR A CA    1 
ATOM   887  C  C     . THR A 1 108 ? 11.930  -10.113 25.532  1.00 5.45   ? 108 THR A C     1 
ATOM   888  O  O     . THR A 1 108 ? 11.926  -9.147  26.313  1.00 6.13   ? 108 THR A O     1 
ATOM   889  C  CB    . THR A 1 108 ? 14.132  -11.008 24.497  1.00 6.74   ? 108 THR A CB    1 
ATOM   890  O  OG1   . THR A 1 108 ? 14.957  -10.512 25.543  1.00 6.71   ? 108 THR A OG1   1 
ATOM   891  C  CG2   . THR A 1 108 ? 14.874  -11.064 23.245  1.00 7.63   ? 108 THR A CG2   1 
ATOM   892  N  N     . VAL A 1 109 ? 11.183  -11.198 25.672  1.00 6.29   ? 109 VAL A N     1 
ATOM   893  C  CA    . VAL A 1 109 ? 10.169  -11.291 26.748  1.00 7.45   ? 109 VAL A CA    1 
ATOM   894  C  C     . VAL A 1 109 ? 10.528  -12.577 27.512  1.00 7.19   ? 109 VAL A C     1 
ATOM   895  O  O     . VAL A 1 109 ? 10.380  -13.694 26.953  1.00 7.73   ? 109 VAL A O     1 
ATOM   896  C  CB    . VAL A 1 109 ? 8.747   -11.290 26.215  1.00 7.52   ? 109 VAL A CB    1 
ATOM   897  C  CG1   . VAL A 1 109 ? 7.754   -11.459 27.355  1.00 8.91   ? 109 VAL A CG1   1 
ATOM   898  C  CG2   . VAL A 1 109 ? 8.441   -9.999  25.448  1.00 9.26   ? 109 VAL A CG2   1 
ATOM   899  N  N     . ASP A 1 110 ? 11.056  -12.473 28.729  1.00 7.70   ? 110 ASP A N     1 
ATOM   900  C  CA    . ASP A 1 110 ? 11.514  -13.655 29.432  1.00 8.27   ? 110 ASP A CA    1 
ATOM   901  C  C     . ASP A 1 110 ? 12.491  -14.478 28.543  1.00 8.53   ? 110 ASP A C     1 
ATOM   902  O  O     . ASP A 1 110 ? 12.438  -15.695 28.501  1.00 9.09   ? 110 ASP A O     1 
ATOM   903  C  CB    . ASP A 1 110 ? 10.420  -14.532 29.958  1.00 9.46   ? 110 ASP A CB    1 
ATOM   904  C  CG    . ASP A 1 110 ? 9.528   -13.775 30.931  1.00 9.96   ? 110 ASP A CG    1 
ATOM   905  O  OD1   . ASP A 1 110 ? 10.023  -12.880 31.628  1.00 11.45  ? 110 ASP A OD1   1 
ATOM   906  O  OD2   . ASP A 1 110 ? 8.318   -14.066 31.071  1.00 12.96  ? 110 ASP A OD2   1 
ATOM   907  N  N     . LYS A 1 111 ? 13.364  -13.726 27.845  1.00 8.07   ? 111 LYS A N     1 
ATOM   908  C  CA    . LYS A 1 111 ? 14.406  -14.278 26.933  1.00 8.45   ? 111 LYS A CA    1 
ATOM   909  C  C     . LYS A 1 111 ? 13.835  -14.820 25.602  1.00 9.30   ? 111 LYS A C     1 
ATOM   910  O  O     . LYS A 1 111 ? 14.601  -15.171 24.719  1.00 10.12  ? 111 LYS A O     1 
ATOM   911  C  CB    . LYS A 1 111 ? 15.287  -15.270 27.580  1.00 10.86  ? 111 LYS A CB    1 
ATOM   912  C  CG    . LYS A 1 111 ? 16.037  -14.737 28.826  1.00 13.43  ? 111 LYS A CG    1 
ATOM   913  C  CD    . LYS A 1 111 ? 16.954  -13.549 28.437  1.00 17.31  ? 111 LYS A CD    1 
ATOM   914  C  CE    . LYS A 1 111 ? 17.762  -12.894 29.610  1.00 18.03  ? 111 LYS A CE    1 
ATOM   915  N  NZ    . LYS A 1 111 ? 18.786  -13.837 30.005  1.00 20.35  ? 111 LYS A NZ    1 
ATOM   916  N  N     . LYS A 1 112 ? 12.540  -14.786 25.410  1.00 8.35   ? 112 LYS A N     1 
ATOM   917  C  CA    . LYS A 1 112 ? 11.953  -15.206 24.127  1.00 9.08   ? 112 LYS A CA    1 
ATOM   918  C  C     . LYS A 1 112 ? 12.209  -14.129 23.066  1.00 7.32   ? 112 LYS A C     1 
ATOM   919  O  O     . LYS A 1 112 ? 11.950  -12.955 23.283  1.00 7.53   ? 112 LYS A O     1 
ATOM   920  C  CB    . LYS A 1 112 ? 10.378  -15.310 24.246  1.00 10.88  ? 112 LYS A CB    1 
ATOM   921  C  CG    . LYS A 1 112 ? 9.668   -15.657 22.891  1.00 12.79  ? 112 LYS A CG    1 
ATOM   922  C  CD    . LYS A 1 112 ? 8.161   -15.689 22.900  1.00 13.71  ? 112 LYS A CD    1 
ATOM   923  C  CE    . LYS A 1 112 ? 7.532   -15.826 21.572  1.00 15.34  ? 112 LYS A CE    1 
ATOM   924  N  NZ    . LYS A 1 112 ? 7.711   -17.113 21.148  1.00 14.20  ? 112 LYS A NZ    1 
ATOM   925  N  N     . LYS A 1 113 ? 12.717  -14.615 21.940  1.00 7.17   ? 113 LYS A N     1 
ATOM   926  C  CA    . LYS A 1 113 ? 12.908  -13.777 20.778  1.00 7.62   ? 113 LYS A CA    1 
ATOM   927  C  C     . LYS A 1 113 ? 11.758  -14.029 19.812  1.00 8.17   ? 113 LYS A C     1 
ATOM   928  O  O     . LYS A 1 113 ? 11.429  -15.156 19.518  1.00 10.02  ? 113 LYS A O     1 
ATOM   929  C  CB    . LYS A 1 113 ? 14.197  -14.140 20.060  1.00 8.49   ? 113 LYS A CB    1 
ATOM   930  C  CG    . LYS A 1 113 ? 15.493  -13.851 20.853  1.00 8.78   ? 113 LYS A CG    1 
ATOM   931  C  CD    . LYS A 1 113 ? 16.695  -14.443 20.166  1.00 10.02  ? 113 LYS A CD    1 
ATOM   932  C  CE    . LYS A 1 113 ? 17.972  -13.876 20.719  1.00 13.35  ? 113 LYS A CE    1 
ATOM   933  N  NZ    . LYS A 1 113 ? 18.532  -14.613 21.703  1.00 20.83  ? 113 LYS A NZ    1 
ATOM   934  N  N     . TYR A 1 114 ? 11.169  -12.948 19.300  1.00 7.11   ? 114 TYR A N     1 
ATOM   935  C  CA    . TYR A 1 114 ? 10.210  -13.022 18.243  1.00 7.42   ? 114 TYR A CA    1 
ATOM   936  C  C     . TYR A 1 114 ? 10.893  -12.970 16.891  1.00 6.62   ? 114 TYR A C     1 
ATOM   937  O  O     . TYR A 1 114 ? 12.062  -12.678 16.749  1.00 7.62   ? 114 TYR A O     1 
ATOM   938  C  CB    . TYR A 1 114 ? 9.132   -11.898 18.379  1.00 7.45   ? 114 TYR A CB    1 
ATOM   939  C  CG    . TYR A 1 114 ? 8.212   -12.139 19.553  1.00 7.51   ? 114 TYR A CG    1 
ATOM   940  C  CD1   . TYR A 1 114 ? 8.494   -11.706 20.864  1.00 8.83   ? 114 TYR A CD1   1 
ATOM   941  C  CD2   . TYR A 1 114 ? 7.031   -12.778 19.341  1.00 8.78   ? 114 TYR A CD2   1 
ATOM   942  C  CE1   . TYR A 1 114 ? 7.574   -11.880 21.890  1.00 10.03  ? 114 TYR A CE1   1 
ATOM   943  C  CE2   . TYR A 1 114 ? 6.115   -12.941 20.364  1.00 9.73   ? 114 TYR A CE2   1 
ATOM   944  C  CZ    . TYR A 1 114 ? 6.394   -12.503 21.606  1.00 12.00  ? 114 TYR A CZ    1 
ATOM   945  O  OH    . TYR A 1 114 ? 5.500   -12.658 22.649  1.00 15.86  ? 114 TYR A OH    1 
ATOM   946  N  N     . ALA A 1 115 ? 10.122  -13.297 15.849  1.00 6.69   ? 115 ALA A N     1 
ATOM   947  C  CA    . ALA A 1 115 ? 10.642  -13.312 14.486  1.00 6.83   ? 115 ALA A CA    1 
ATOM   948  C  C     . ALA A 1 115 ? 11.027  -11.947 13.986  1.00 6.94   ? 115 ALA A C     1 
ATOM   949  O  O     . ALA A 1 115 ? 11.861  -11.811 13.108  1.00 8.11   ? 115 ALA A O     1 
ATOM   950  C  CB    . ALA A 1 115 ? 9.604   -13.961 13.570  1.00 7.68   ? 115 ALA A CB    1 
ATOM   951  N  N     . ALA A 1 116 ? 10.405  -10.906 14.494  1.00 6.62   ? 116 ALA A N     1 
ATOM   952  C  CA    . ALA A 1 116 ? 10.640  -9.568  14.045  1.00 6.14   ? 116 ALA A CA    1 
ATOM   953  C  C     . ALA A 1 116 ? 10.070  -8.602  15.056  1.00 6.23   ? 116 ALA A C     1 
ATOM   954  O  O     . ALA A 1 116 ? 9.326   -8.992  15.967  1.00 6.97   ? 116 ALA A O     1 
ATOM   955  C  CB    . ALA A 1 116 ? 10.140  -9.320  12.646  1.00 7.09   ? 116 ALA A CB    1 
ATOM   956  N  N     . GLU A 1 117 ? 10.430  -7.346  14.884  1.00 5.64   ? 117 GLU A N     1 
ATOM   957  C  CA    . GLU A 1 117 ? 9.891   -6.258  15.756  1.00 5.10   ? 117 GLU A CA    1 
ATOM   958  C  C     . GLU A 1 117 ? 9.754   -5.007  14.890  1.00 5.51   ? 117 GLU A C     1 
ATOM   959  O  O     . GLU A 1 117 ? 10.663  -4.621  14.173  1.00 6.90   ? 117 GLU A O     1 
ATOM   960  C  CB    . GLU A 1 117 ? 10.894  -6.065  16.909  1.00 6.37   ? 117 GLU A CB    1 
ATOM   961  C  CG    . GLU A 1 117 ? 10.374  -5.070  17.964  1.00 5.53   ? 117 GLU A CG    1 
ATOM   962  C  CD    . GLU A 1 117 ? 11.281  -4.994  19.174  1.00 5.37   ? 117 GLU A CD    1 
ATOM   963  O  OE1   . GLU A 1 117 ? 11.902  -6.018  19.499  1.00 6.33   ? 117 GLU A OE1   1 
ATOM   964  O  OE2   . GLU A 1 117 ? 11.310  -3.914  19.821  1.00 6.20   ? 117 GLU A OE2   1 
ATOM   965  N  N     . LEU A 1 118 ? 8.561   -4.414  15.009  1.00 5.80   ? 118 LEU A N     1 
ATOM   966  C  CA    . LEU A 1 118 ? 8.213   -3.194  14.354  1.00 5.79   ? 118 LEU A CA    1 
ATOM   967  C  C     . LEU A 1 118 ? 8.390   -2.012  15.359  1.00 5.72   ? 118 LEU A C     1 
ATOM   968  O  O     . LEU A 1 118 ? 7.992   -2.100  16.514  1.00 6.00   ? 118 LEU A O     1 
ATOM   969  C  CB    . LEU A 1 118 ? 6.703   -3.270  14.012  1.00 6.56   ? 118 LEU A CB    1 
ATOM   970  C  CG    . LEU A 1 118 ? 5.974   -1.999  13.593  1.00 7.31   ? 118 LEU A CG    1 
ATOM   971  C  CD1   . LEU A 1 118 ? 6.583   -1.318  12.373  1.00 7.92   ? 118 LEU A CD1   1 
ATOM   972  C  CD2   . LEU A 1 118 ? 4.472   -2.307  13.370  1.00 8.71   ? 118 LEU A CD2   1 
ATOM   973  N  N     . HIS A 1 119 ? 9.039   -0.951  14.875  1.00 5.14   ? 119 HIS A N     1 
ATOM   974  C  CA    . HIS A 1 119 ? 9.249   0.244   15.613  1.00 4.97   ? 119 HIS A CA    1 
ATOM   975  C  C     . HIS A 1 119 ? 8.610   1.406   14.933  1.00 5.20   ? 119 HIS A C     1 
ATOM   976  O  O     . HIS A 1 119 ? 8.988   1.767   13.814  1.00 6.65   ? 119 HIS A O     1 
ATOM   977  C  CB    . HIS A 1 119 ? 10.779  0.515   15.745  1.00 5.45   ? 119 HIS A CB    1 
ATOM   978  C  CG    . HIS A 1 119 ? 11.446  -0.426  16.655  1.00 5.07   ? 119 HIS A CG    1 
ATOM   979  N  ND1   . HIS A 1 119 ? 12.811  -0.616  16.662  1.00 4.84   ? 119 HIS A ND1   1 
ATOM   980  C  CD2   . HIS A 1 119 ? 10.918  -1.254  17.590  1.00 5.67   ? 119 HIS A CD2   1 
ATOM   981  C  CE1   . HIS A 1 119 ? 13.089  -1.572  17.511  1.00 5.53   ? 119 HIS A CE1   1 
ATOM   982  N  NE2   . HIS A 1 119 ? 11.963  -1.953  18.119  1.00 5.96   ? 119 HIS A NE2   1 
ATOM   983  N  N     . LEU A 1 120 ? 7.593   2.006   15.572  1.00 5.29   ? 120 LEU A N     1 
ATOM   984  C  CA    . LEU A 1 120 ? 6.988   3.232   15.137  1.00 5.89   ? 120 LEU A CA    1 
ATOM   985  C  C     . LEU A 1 120 ? 7.577   4.353   15.928  1.00 5.26   ? 120 LEU A C     1 
ATOM   986  O  O     . LEU A 1 120 ? 7.456   4.412   17.165  1.00 5.64   ? 120 LEU A O     1 
ATOM   987  C  CB    . LEU A 1 120 ? 5.494   3.138   15.269  1.00 6.79   ? 120 LEU A CB    1 
ATOM   988  C  CG    . LEU A 1 120 ? 4.794   2.091   14.439  1.00 8.16   ? 120 LEU A CG    1 
ATOM   989  C  CD1   . LEU A 1 120 ? 3.994   1.145   15.268  1.00 11.29  ? 120 LEU A CD1   1 
ATOM   990  C  CD2   . LEU A 1 120 ? 3.976   2.722   13.338  1.00 10.55  ? 120 LEU A CD2   1 
ATOM   991  N  N     . VAL A 1 121 ? 8.287   5.246   15.241  1.00 6.05   ? 121 VAL A N     1 
ATOM   992  C  CA    . VAL A 1 121 ? 9.089   6.263   15.867  1.00 6.46   ? 121 VAL A CA    1 
ATOM   993  C  C     . VAL A 1 121 ? 8.403   7.622   15.858  1.00 5.88   ? 121 VAL A C     1 
ATOM   994  O  O     . VAL A 1 121 ? 7.978   8.068   14.793  1.00 6.64   ? 121 VAL A O     1 
ATOM   995  C  CB    . VAL A 1 121 ? 10.464  6.373   15.125  1.00 7.03   ? 121 VAL A CB    1 
ATOM   996  C  CG1   . VAL A 1 121 ? 11.324  7.438   15.755  1.00 8.32   ? 121 VAL A CG1   1 
ATOM   997  C  CG2   . VAL A 1 121 ? 11.152  5.021   15.036  1.00 8.12   ? 121 VAL A CG2   1 
ATOM   998  N  N     . HIS A 1 122 ? 8.310   8.239   17.012  1.00 5.98   ? 122 HIS A N     1 
ATOM   999  C  CA    . HIS A 1 122 ? 7.637   9.494   17.187  1.00 6.05   ? 122 HIS A CA    1 
ATOM   1000 C  C     . HIS A 1 122 ? 8.512   10.454  17.961  1.00 6.27   ? 122 HIS A C     1 
ATOM   1001 O  O     . HIS A 1 122 ? 9.236   10.060  18.870  1.00 7.07   ? 122 HIS A O     1 
ATOM   1002 C  CB    . HIS A 1 122 ? 6.351   9.306   17.996  1.00 6.95   ? 122 HIS A CB    1 
ATOM   1003 C  CG    . HIS A 1 122 ? 5.472   8.164   17.579  1.00 6.08   ? 122 HIS A CG    1 
ATOM   1004 N  ND1   . HIS A 1 122 ? 5.784   6.850   17.888  1.00 6.26   ? 122 HIS A ND1   1 
ATOM   1005 C  CD2   . HIS A 1 122 ? 4.277   8.101   16.959  1.00 6.92   ? 122 HIS A CD2   1 
ATOM   1006 C  CE1   . HIS A 1 122 ? 4.819   6.087   17.422  1.00 7.08   ? 122 HIS A CE1   1 
ATOM   1007 N  NE2   . HIS A 1 122 ? 3.890   6.807   16.845  1.00 7.37   ? 122 HIS A NE2   1 
ATOM   1008 N  N     . TRP A 1 123 ? 8.434   11.726  17.605  1.00 6.62   ? 123 TRP A N     1 
ATOM   1009 C  CA    . TRP A 1 123 ? 9.230   12.782  18.296  1.00 6.77   ? 123 TRP A CA    1 
ATOM   1010 C  C     . TRP A 1 123 ? 8.339   13.761  19.015  1.00 6.66   ? 123 TRP A C     1 
ATOM   1011 O  O     . TRP A 1 123 ? 7.244   14.098  18.579  1.00 8.54   ? 123 TRP A O     1 
ATOM   1012 C  CB    . TRP A 1 123 ? 10.198  13.477  17.367  1.00 9.34   ? 123 TRP A CB    1 
ATOM   1013 C  CG    . TRP A 1 123 ? 9.599   14.092  16.127  1.00 9.57   ? 123 TRP A CG    1 
ATOM   1014 C  CD1   . TRP A 1 123 ? 9.412   13.460  14.906  1.00 10.65  ? 123 TRP A CD1   1 
ATOM   1015 C  CD2   . TRP A 1 123 ? 9.146   15.438  15.974  1.00 12.26  ? 123 TRP A CD2   1 
ATOM   1016 N  NE1   . TRP A 1 123 ? 8.847   14.365  14.035  1.00 12.32  ? 123 TRP A NE1   1 
ATOM   1017 C  CE2   . TRP A 1 123 ? 8.711   15.562  14.647  1.00 13.09  ? 123 TRP A CE2   1 
ATOM   1018 C  CE3   . TRP A 1 123 ? 9.150   16.551  16.762  1.00 14.16  ? 123 TRP A CE3   1 
ATOM   1019 C  CZ2   . TRP A 1 123 ? 8.241   16.735  14.121  1.00 16.68  ? 123 TRP A CZ2   1 
ATOM   1020 C  CZ3   . TRP A 1 123 ? 8.634   17.701  16.269  1.00 17.88  ? 123 TRP A CZ3   1 
ATOM   1021 C  CH2   . TRP A 1 123 ? 8.197   17.794  14.937  1.00 19.61  ? 123 TRP A CH2   1 
ATOM   1022 N  N     . ASN A 1 124 ? 8.876   14.238  20.147  1.00 7.78   ? 124 ASN A N     1 
ATOM   1023 C  CA    . ASN A 1 124 ? 8.118   15.144  21.032  1.00 8.19   ? 124 ASN A CA    1 
ATOM   1024 C  C     . ASN A 1 124 ? 8.036   16.532  20.398  1.00 8.46   ? 124 ASN A C     1 
ATOM   1025 O  O     . ASN A 1 124 ? 9.020   17.166  20.168  1.00 9.37   ? 124 ASN A O     1 
ATOM   1026 C  CB    . ASN A 1 124 ? 8.890   15.201  22.369  1.00 8.20   ? 124 ASN A CB    1 
ATOM   1027 C  CG    . ASN A 1 124 ? 8.109   15.790  23.474  1.00 9.31   ? 124 ASN A CG    1 
ATOM   1028 O  OD1   . ASN A 1 124 ? 7.291   16.649  23.234  1.00 10.57  ? 124 ASN A OD1   1 
ATOM   1029 N  ND2   . ASN A 1 124 ? 8.342   15.343  24.694  1.00 10.06  ? 124 ASN A ND2   1 
ATOM   1030 N  N     . THR A 1 125 ? 6.795   16.954  20.182  1.00 10.18  ? 125 THR A N     1 
ATOM   1031 C  CA    . THR A 1 125 ? 6.568   18.173  19.491  1.00 11.52  ? 125 THR A CA    1 
ATOM   1032 C  C     . THR A 1 125 ? 7.128   19.395  20.246  1.00 11.38  ? 125 THR A C     1 
ATOM   1033 O  O     . THR A 1 125 ? 7.293   20.410  19.627  1.00 12.76  ? 125 THR A O     1 
ATOM   1034 C  CB    . THR A 1 125 ? 5.082   18.370  19.110  1.00 15.16  ? 125 THR A CB    1 
ATOM   1035 O  OG1   . THR A 1 125 ? 4.306   18.388  20.284  1.00 19.90  ? 125 THR A OG1   1 
ATOM   1036 C  CG2   . THR A 1 125 ? 4.611   17.275  18.149  1.00 18.08  ? 125 THR A CG2   1 
ATOM   1037 N  N     . LYS A 1 126 ? 7.376   19.225  21.594  1.00 11.03  ? 127 LYS A N     1 
ATOM   1038 C  CA    . LYS A 1 126 ? 7.879   20.386  22.283  1.00 12.18  ? 127 LYS A CA    1 
ATOM   1039 C  C     . LYS A 1 126 ? 9.285   20.757  21.843  1.00 9.96   ? 127 LYS A C     1 
ATOM   1040 O  O     . LYS A 1 126 ? 9.702   21.815  22.229  1.00 14.14  ? 127 LYS A O     1 
ATOM   1041 C  CB    . LYS A 1 126 ? 7.734   20.158  23.785  1.00 14.17  ? 127 LYS A CB    1 
ATOM   1042 C  CG    . LYS A 1 126 ? 8.755   19.274  24.412  1.00 13.90  ? 127 LYS A CG    1 
ATOM   1043 C  CD    . LYS A 1 126 ? 8.315   18.979  25.811  1.00 20.27  ? 127 LYS A CD    1 
ATOM   1044 C  CE    . LYS A 1 126 ? 9.370   18.321  26.552  1.00 23.17  ? 127 LYS A CE    1 
ATOM   1045 N  NZ    . LYS A 1 126 ? 8.908   17.930  27.897  1.00 35.92  ? 127 LYS A NZ    1 
ATOM   1046 N  N     . TYR A 1 127 ? 9.991   19.901  21.099  1.00 10.09  ? 128 TYR A N     1 
ATOM   1047 C  CA    . TYR A 1 127 ? 11.360  20.179  20.618  1.00 10.85  ? 128 TYR A CA    1 
ATOM   1048 C  C     . TYR A 1 127 ? 11.373  20.588  19.145  1.00 9.27   ? 128 TYR A C     1 
ATOM   1049 O  O     . TYR A 1 127 ? 12.477  20.829  18.609  1.00 11.45  ? 128 TYR A O     1 
ATOM   1050 C  CB    . TYR A 1 127 ? 12.243  18.990  20.925  1.00 9.55   ? 128 TYR A CB    1 
ATOM   1051 C  CG    . TYR A 1 127 ? 12.362  18.661  22.381  1.00 9.83   ? 128 TYR A CG    1 
ATOM   1052 C  CD1   . TYR A 1 127 ? 12.703  19.633  23.316  1.00 11.04  ? 128 TYR A CD1   1 
ATOM   1053 C  CD2   . TYR A 1 127 ? 11.998  17.437  22.889  1.00 8.86   ? 128 TYR A CD2   1 
ATOM   1054 C  CE1   . TYR A 1 127 ? 12.760  19.358  24.680  1.00 11.34  ? 128 TYR A CE1   1 
ATOM   1055 C  CE2   . TYR A 1 127 ? 12.056  17.138  24.262  1.00 10.33  ? 128 TYR A CE2   1 
ATOM   1056 C  CZ    . TYR A 1 127 ? 12.415  18.120  25.159  1.00 10.30  ? 128 TYR A CZ    1 
ATOM   1057 O  OH    . TYR A 1 127 ? 12.483  17.892  26.493  1.00 13.63  ? 128 TYR A OH    1 
ATOM   1058 N  N     . GLY A 1 128 ? 10.206  20.652  18.505  1.00 10.59  ? 129 GLY A N     1 
ATOM   1059 C  CA    . GLY A 1 128 ? 10.148  21.271  17.223  1.00 11.10  ? 129 GLY A CA    1 
ATOM   1060 C  C     . GLY A 1 128 ? 10.538  20.457  16.016  1.00 13.25  ? 129 GLY A C     1 
ATOM   1061 O  O     . GLY A 1 128 ? 9.889   20.572  14.959  1.00 14.78  ? 129 GLY A O     1 
ATOM   1062 N  N     . ASP A 1 129 ? 11.638  19.679  16.063  1.00 12.56  ? 130 ASP A N     1 
ATOM   1063 C  CA    . ASP A 1 129 ? 12.020  18.757  14.984  1.00 13.92  ? 130 ASP A CA    1 
ATOM   1064 C  C     . ASP A 1 129 ? 12.707  17.541  15.563  1.00 14.52  ? 130 ASP A C     1 
ATOM   1065 O  O     . ASP A 1 129 ? 13.099  17.501  16.732  1.00 14.18  ? 130 ASP A O     1 
ATOM   1066 C  CB    . ASP A 1 129 ? 12.927  19.511  13.957  1.00 13.28  ? 130 ASP A CB    1 
ATOM   1067 C  CG    . ASP A 1 129 ? 14.312  19.899  14.380  1.00 22.63  ? 130 ASP A CG    1 
ATOM   1068 O  OD1   . ASP A 1 129 ? 15.262  19.133  14.646  1.00 16.14  ? 130 ASP A OD1   1 
ATOM   1069 O  OD2   . ASP A 1 129 ? 14.768  21.161  14.239  1.00 16.51  ? 130 ASP A OD2   1 
ATOM   1070 N  N     . PHE A 1 130 ? 12.806  16.522  14.725  1.00 11.92  ? 131 PHE A N     1 
ATOM   1071 C  CA    . PHE A 1 130 ? 13.399  15.270  15.144  1.00 9.86   ? 131 PHE A CA    1 
ATOM   1072 C  C     . PHE A 1 130 ? 14.848  15.420  15.624  1.00 10.27  ? 131 PHE A C     1 
ATOM   1073 O  O     . PHE A 1 130 ? 15.261  14.858  16.604  1.00 10.45  ? 131 PHE A O     1 
ATOM   1074 C  CB    . PHE A 1 130 ? 13.276  14.290  14.006  1.00 10.27  ? 131 PHE A CB    1 
ATOM   1075 C  CG    . PHE A 1 130 ? 13.896  12.949  14.278  1.00 9.11   ? 131 PHE A CG    1 
ATOM   1076 C  CD1   . PHE A 1 130 ? 13.185  11.978  14.889  1.00 9.76   ? 131 PHE A CD1   1 
ATOM   1077 C  CD2   . PHE A 1 130 ? 15.195  12.677  13.935  1.00 11.35  ? 131 PHE A CD2   1 
ATOM   1078 C  CE1   . PHE A 1 130 ? 13.736  10.746  15.141  1.00 12.01  ? 131 PHE A CE1   1 
ATOM   1079 C  CE2   . PHE A 1 130 ? 15.755  11.496  14.249  1.00 13.18  ? 131 PHE A CE2   1 
ATOM   1080 C  CZ    . PHE A 1 130 ? 15.024  10.512  14.873  1.00 14.31  ? 131 PHE A CZ    1 
ATOM   1081 N  N     . GLY A 1 131 ? 15.649  16.217  14.862  1.00 11.62  ? 132 GLY A N     1 
ATOM   1082 C  CA    . GLY A 1 131 ? 17.034  16.315  15.197  1.00 12.58  ? 132 GLY A CA    1 
ATOM   1083 C  C     . GLY A 1 131 ? 17.263  16.983  16.557  1.00 11.62  ? 132 GLY A C     1 
ATOM   1084 O  O     . GLY A 1 131 ? 18.227  16.679  17.220  1.00 13.81  ? 132 GLY A O     1 
ATOM   1085 N  N     . LYS A 1 132 ? 16.427  17.906  16.941  1.00 11.72  ? 133 LYS A N     1 
ATOM   1086 C  CA    . LYS A 1 132 ? 16.476  18.514  18.281  1.00 10.60  ? 133 LYS A CA    1 
ATOM   1087 C  C     . LYS A 1 132 ? 15.942  17.543  19.306  1.00 9.29   ? 133 LYS A C     1 
ATOM   1088 O  O     . LYS A 1 132 ? 16.458  17.469  20.418  1.00 9.83   ? 133 LYS A O     1 
ATOM   1089 C  CB    . LYS A 1 132 ? 15.736  19.811  18.333  1.00 11.12  ? 133 LYS A CB    1 
ATOM   1090 C  CG    . LYS A 1 132 ? 16.494  20.926  17.631  1.00 13.17  ? 133 LYS A CG    1 
ATOM   1091 C  CD    . LYS A 1 132 ? 17.678  21.387  18.521  1.00 17.90  ? 133 LYS A CD    1 
ATOM   1092 C  CE    . LYS A 1 132 ? 18.159  22.697  18.015  1.00 23.93  ? 133 LYS A CE    1 
ATOM   1093 N  NZ    . LYS A 1 132 ? 18.821  22.510  16.721  1.00 34.09  ? 133 LYS A NZ    1 
ATOM   1094 N  N     . ALA A 1 133 ? 14.886  16.801  18.968  1.00 9.26   ? 134 ALA A N     1 
ATOM   1095 C  CA    . ALA A 1 133 ? 14.332  15.861  19.939  1.00 8.72   ? 134 ALA A CA    1 
ATOM   1096 C  C     . ALA A 1 133 ? 15.293  14.793  20.349  1.00 8.72   ? 134 ALA A C     1 
ATOM   1097 O  O     . ALA A 1 133 ? 15.281  14.406  21.517  1.00 8.56   ? 134 ALA A O     1 
ATOM   1098 C  CB    . ALA A 1 133 ? 13.014  15.261  19.342  1.00 8.85   ? 134 ALA A CB    1 
ATOM   1099 N  N     . VAL A 1 134 ? 16.105  14.264  19.433  1.00 8.90   ? 135 VAL A N     1 
ATOM   1100 C  CA    . VAL A 1 134 ? 16.996  13.199  19.815  1.00 9.04   ? 135 VAL A CA    1 
ATOM   1101 C  C     . VAL A 1 134 ? 18.096  13.622  20.792  1.00 9.22   ? 135 VAL A C     1 
ATOM   1102 O  O     . VAL A 1 134 ? 18.758  12.754  21.336  1.00 9.50   ? 135 VAL A O     1 
ATOM   1103 C  CB    . VAL A 1 134 ? 17.614  12.471  18.612  1.00 10.17  ? 135 VAL A CB    1 
ATOM   1104 C  CG1   . VAL A 1 134 ? 16.575  11.825  17.765  1.00 11.69  ? 135 VAL A CG1   1 
ATOM   1105 C  CG2   . VAL A 1 134 ? 18.520  13.348  17.818  1.00 10.95  ? 135 VAL A CG2   1 
ATOM   1106 N  N     . GLN A 1 135 ? 18.210  14.914  20.991  1.00 9.31   ? 136 GLN A N     1 
ATOM   1107 C  CA    . GLN A 1 135 ? 19.174  15.426  21.979  1.00 10.19  ? 136 GLN A CA    1 
ATOM   1108 C  C     . GLN A 1 135 ? 18.603  15.537  23.380  1.00 10.35  ? 136 GLN A C     1 
ATOM   1109 O  O     . GLN A 1 135 ? 19.268  16.090  24.264  1.00 12.39  ? 136 GLN A O     1 
ATOM   1110 C  CB    . GLN A 1 135 ? 19.724  16.787  21.496  1.00 11.73  ? 136 GLN A CB    1 
ATOM   1111 C  CG    . GLN A 1 135 ? 20.392  16.698  20.099  1.00 15.52  ? 136 GLN A CG    1 
ATOM   1112 C  CD    . GLN A 1 135 ? 20.864  18.028  19.660  1.00 19.62  ? 136 GLN A CD    1 
ATOM   1113 O  OE1   . GLN A 1 135 ? 21.679  18.618  20.330  1.00 25.20  ? 136 GLN A OE1   1 
ATOM   1114 N  NE2   . GLN A 1 135 ? 20.351  18.522  18.574  1.00 21.24  ? 136 GLN A NE2   1 
ATOM   1115 N  N     . GLN A 1 136 ? 17.384  15.067  23.567  1.00 8.56   ? 137 GLN A N     1 
ATOM   1116 C  CA    . GLN A 1 136 ? 16.681  15.240  24.870  1.00 7.90   ? 137 GLN A CA    1 
ATOM   1117 C  C     . GLN A 1 136 ? 16.304  13.907  25.423  1.00 7.41   ? 137 GLN A C     1 
ATOM   1118 O  O     . GLN A 1 136 ? 15.938  12.998  24.670  1.00 7.77   ? 137 GLN A O     1 
ATOM   1119 C  CB    . GLN A 1 136 ? 15.413  16.043  24.683  1.00 9.94   ? 137 GLN A CB    1 
ATOM   1120 C  CG    . GLN A 1 136 ? 15.552  17.356  23.967  1.00 13.80  ? 137 GLN A CG    1 
ATOM   1121 C  CD    . GLN A 1 136 ? 16.469  18.357  24.550  1.00 17.83  ? 137 GLN A CD    1 
ATOM   1122 O  OE1   . GLN A 1 136 ? 17.137  19.143  23.826  1.00 32.14  ? 137 GLN A OE1   1 
ATOM   1123 N  NE2   . GLN A 1 136 ? 16.610  18.325  25.723  1.00 17.25  ? 137 GLN A NE2   1 
ATOM   1124 N  N     . PRO A 1 137 ? 16.265  13.750  26.762  1.00 7.64   ? 138 PRO A N     1 
ATOM   1125 C  CA    . PRO A 1 137 ? 15.989  12.433  27.318  1.00 8.14   ? 138 PRO A CA    1 
ATOM   1126 C  C     . PRO A 1 137 ? 14.550  11.985  27.100  1.00 7.92   ? 138 PRO A C     1 
ATOM   1127 O  O     . PRO A 1 137 ? 14.279  10.790  27.155  1.00 11.38  ? 138 PRO A O     1 
ATOM   1128 C  CB    . PRO A 1 137 ? 16.244  12.582  28.814  1.00 10.48  ? 138 PRO A CB    1 
ATOM   1129 C  CG    . PRO A 1 137 ? 16.660  13.932  28.983  1.00 20.57  ? 138 PRO A CG    1 
ATOM   1130 C  CD    . PRO A 1 137 ? 16.855  14.673  27.743  1.00 11.09  ? 138 PRO A CD    1 
ATOM   1131 N  N     . ASP A 1 138 ? 13.648  12.957  26.888  1.00 8.02   ? 139 ASP A N     1 
ATOM   1132 C  CA    . ASP A 1 138 ? 12.266  12.664  26.574  1.00 7.40   ? 139 ASP A CA    1 
ATOM   1133 C  C     . ASP A 1 138 ? 11.924  13.084  25.174  1.00 7.09   ? 139 ASP A C     1 
ATOM   1134 O  O     . ASP A 1 138 ? 10.783  13.472  24.877  1.00 7.69   ? 139 ASP A O     1 
ATOM   1135 C  CB    . ASP A 1 138 ? 11.320  13.269  27.554  1.00 9.14   ? 139 ASP A CB    1 
ATOM   1136 C  CG    . ASP A 1 138 ? 11.393  14.736  27.675  1.00 9.65   ? 139 ASP A CG    1 
ATOM   1137 O  OD1   . ASP A 1 138 ? 12.320  15.354  27.047  1.00 10.20  ? 139 ASP A OD1   1 
ATOM   1138 O  OD2   . ASP A 1 138 ? 10.589  15.373  28.356  1.00 13.41  ? 139 ASP A OD2   1 
ATOM   1139 N  N     . GLY A 1 139 ? 12.876  12.940  24.258  1.00 6.63   ? 140 GLY A N     1 
ATOM   1140 C  CA    . GLY A 1 139 ? 12.667  13.418  22.924  1.00 6.73   ? 140 GLY A CA    1 
ATOM   1141 C  C     . GLY A 1 139 ? 11.841  12.524  22.003  1.00 6.67   ? 140 GLY A C     1 
ATOM   1142 O  O     . GLY A 1 139 ? 11.156  13.009  21.105  1.00 7.03   ? 140 GLY A O     1 
ATOM   1143 N  N     . LEU A 1 140 ? 11.946  11.210  22.192  1.00 6.02   ? 141 LEU A N     1 
ATOM   1144 C  CA    . LEU A 1 140 ? 11.274  10.251  21.310  1.00 5.73   ? 141 LEU A CA    1 
ATOM   1145 C  C     . LEU A 1 140 ? 10.454  9.313   22.111  1.00 5.80   ? 141 LEU A C     1 
ATOM   1146 O  O     . LEU A 1 140 ? 10.693  9.010   23.268  1.00 6.19   ? 141 LEU A O     1 
ATOM   1147 C  CB    . LEU A 1 140 ? 12.260  9.402   20.511  1.00 6.30   ? 141 LEU A CB    1 
ATOM   1148 C  CG    . LEU A 1 140 ? 13.072  10.057  19.461  1.00 9.84   ? 141 LEU A CG    1 
ATOM   1149 C  CD1   . LEU A 1 140 ? 13.891  8.996   18.708  1.00 8.82   ? 141 LEU A CD1   1 
ATOM   1150 C  CD2   . LEU A 1 140 ? 12.621  11.167  18.629  1.00 13.77  ? 141 LEU A CD2   1 
ATOM   1151 N  N     . ALA A 1 141 ? 9.369   8.819   21.446  1.00 5.36   ? 142 ALA A N     1 
ATOM   1152 C  CA    . ALA A 1 141 ? 8.598   7.681   21.948  1.00 6.18   ? 142 ALA A CA    1 
ATOM   1153 C  C     . ALA A 1 141 ? 8.585   6.694   20.824  1.00 5.89   ? 142 ALA A C     1 
ATOM   1154 O  O     . ALA A 1 141 ? 8.162   7.011   19.721  1.00 6.74   ? 142 ALA A O     1 
ATOM   1155 C  CB    . ALA A 1 141 ? 7.166   8.132   22.319  1.00 7.46   ? 142 ALA A CB    1 
ATOM   1156 N  N     . VAL A 1 142 ? 9.048   5.466   21.118  1.00 5.29   ? 143 VAL A N     1 
ATOM   1157 C  CA    . VAL A 1 142 ? 9.028   4.406   20.133  1.00 5.77   ? 143 VAL A CA    1 
ATOM   1158 C  C     . VAL A 1 142 ? 8.072   3.348   20.619  1.00 5.68   ? 143 VAL A C     1 
ATOM   1159 O  O     . VAL A 1 142 ? 8.183   2.830   21.714  1.00 5.87   ? 143 VAL A O     1 
ATOM   1160 C  CB    . VAL A 1 142 ? 10.444  3.842   19.790  1.00 5.92   ? 143 VAL A CB    1 
ATOM   1161 C  CG1   . VAL A 1 142 ? 10.269  2.814   18.663  1.00 7.20   ? 143 VAL A CG1   1 
ATOM   1162 C  CG2   . VAL A 1 142 ? 11.340  4.976   19.379  1.00 7.46   ? 143 VAL A CG2   1 
ATOM   1163 N  N     . LEU A 1 143 ? 7.104   3.046   19.726  1.00 5.58   ? 144 LEU A N     1 
ATOM   1164 C  CA    . LEU A 1 143 ? 6.165   1.972   19.962  1.00 5.67   ? 144 LEU A CA    1 
ATOM   1165 C  C     . LEU A 1 143 ? 6.687   0.738   19.290  1.00 5.87   ? 144 LEU A C     1 
ATOM   1166 O  O     . LEU A 1 143 ? 6.907   0.695   18.076  1.00 7.07   ? 144 LEU A O     1 
ATOM   1167 C  CB    . LEU A 1 143 ? 4.782   2.433   19.372  1.00 7.80   ? 144 LEU A CB    1 
ATOM   1168 C  CG    . LEU A 1 143 ? 3.658   1.449   19.537  1.00 8.50   ? 144 LEU A CG    1 
ATOM   1169 C  CD1   . LEU A 1 143 ? 3.385   1.099   20.981  1.00 10.46  ? 144 LEU A CD1   1 
ATOM   1170 C  CD2   . LEU A 1 143 ? 2.401   2.052   18.879  1.00 10.97  ? 144 LEU A CD2   1 
ATOM   1171 N  N     . GLY A 1 144 ? 6.958   -0.280  20.108  1.00 5.48   ? 145 GLY A N     1 
ATOM   1172 C  CA    . GLY A 1 144 ? 7.508   -1.539  19.605  1.00 5.82   ? 145 GLY A CA    1 
ATOM   1173 C  C     . GLY A 1 144 ? 6.439   -2.605  19.637  1.00 5.26   ? 145 GLY A C     1 
ATOM   1174 O  O     . GLY A 1 144 ? 5.703   -2.760  20.614  1.00 6.82   ? 145 GLY A O     1 
ATOM   1175 N  N     . ILE A 1 145 ? 6.408   -3.346  18.538  1.00 5.59   ? 146 ILE A N     1 
ATOM   1176 C  CA    . ILE A 1 145 ? 5.370   -4.366  18.342  1.00 5.86   ? 146 ILE A CA    1 
ATOM   1177 C  C     . ILE A 1 145 ? 6.063   -5.597  17.808  1.00 5.48   ? 146 ILE A C     1 
ATOM   1178 O  O     . ILE A 1 145 ? 6.779   -5.586  16.822  1.00 6.67   ? 146 ILE A O     1 
ATOM   1179 C  CB    . ILE A 1 145 ? 4.268   -3.902  17.359  1.00 6.85   ? 146 ILE A CB    1 
ATOM   1180 C  CG1   . ILE A 1 145 ? 3.637   -2.610  17.892  1.00 8.08   ? 146 ILE A CG1   1 
ATOM   1181 C  CG2   . ILE A 1 145 ? 3.269   -5.001  17.080  1.00 9.45   ? 146 ILE A CG2   1 
ATOM   1182 C  CD1   . ILE A 1 145 ? 2.577   -1.998  16.995  1.00 8.48   ? 146 ILE A CD1   1 
ATOM   1183 N  N     . PHE A 1 146 ? 5.890   -6.710  18.510  1.00 5.50   ? 147 PHE A N     1 
ATOM   1184 C  CA    . PHE A 1 146 ? 6.514   -7.990  18.098  1.00 6.16   ? 147 PHE A CA    1 
ATOM   1185 C  C     . PHE A 1 146 ? 5.731   -8.584  16.982  1.00 6.58   ? 147 PHE A C     1 
ATOM   1186 O  O     . PHE A 1 146 ? 4.483   -8.467  16.880  1.00 7.46   ? 147 PHE A O     1 
ATOM   1187 C  CB    . PHE A 1 146 ? 6.481   -8.942  19.287  1.00 6.15   ? 147 PHE A CB    1 
ATOM   1188 C  CG    . PHE A 1 146 ? 7.315   -8.499  20.444  1.00 5.60   ? 147 PHE A CG    1 
ATOM   1189 C  CD1   . PHE A 1 146 ? 8.673   -8.319  20.293  1.00 6.26   ? 147 PHE A CD1   1 
ATOM   1190 C  CD2   . PHE A 1 146 ? 6.783   -8.268  21.666  1.00 7.13   ? 147 PHE A CD2   1 
ATOM   1191 C  CE1   . PHE A 1 146 ? 9.483   -7.920  21.337  1.00 6.74   ? 147 PHE A CE1   1 
ATOM   1192 C  CE2   . PHE A 1 146 ? 7.595   -7.881  22.722  1.00 6.41   ? 147 PHE A CE2   1 
ATOM   1193 C  CZ    . PHE A 1 146 ? 8.940   -7.740  22.577  1.00 6.43   ? 147 PHE A CZ    1 
ATOM   1194 N  N     . LEU A 1 147 ? 6.426   -9.330  16.109  1.00 6.61   ? 148 LEU A N     1 
ATOM   1195 C  CA    . LEU A 1 147 ? 5.866   -10.131 15.049  1.00 7.49   ? 148 LEU A CA    1 
ATOM   1196 C  C     . LEU A 1 147 ? 6.172   -11.612 15.289  1.00 6.89   ? 148 LEU A C     1 
ATOM   1197 O  O     . LEU A 1 147 ? 7.343   -11.927 15.517  1.00 7.62   ? 148 LEU A O     1 
ATOM   1198 C  CB    . LEU A 1 147 ? 6.416   -9.760  13.703  1.00 7.83   ? 148 LEU A CB    1 
ATOM   1199 C  CG    . LEU A 1 147 ? 5.881   -8.512  13.005  1.00 8.46   ? 148 LEU A CG    1 
ATOM   1200 C  CD1   . LEU A 1 147 ? 6.099   -7.218  13.816  1.00 9.11   ? 148 LEU A CD1   1 
ATOM   1201 C  CD2   . LEU A 1 147 ? 6.497   -8.361  11.614  1.00 8.79   ? 148 LEU A CD2   1 
ATOM   1202 N  N     . LYS A 1 148 ? 5.168   -12.454 15.200  1.00 7.78   ? 149 LYS A N     1 
ATOM   1203 C  CA    . LYS A 1 148 ? 5.293   -13.855 15.144  1.00 8.00   ? 149 LYS A CA    1 
ATOM   1204 C  C     . LYS A 1 148 ? 4.808   -14.376 13.799  1.00 8.56   ? 149 LYS A C     1 
ATOM   1205 O  O     . LYS A 1 148 ? 4.034   -13.689 13.121  1.00 9.62   ? 149 LYS A O     1 
ATOM   1206 C  CB    . LYS A 1 148 ? 4.560   -14.578 16.255  1.00 9.65   ? 149 LYS A CB    1 
ATOM   1207 C  CG    . LYS A 1 148 ? 3.042   -14.440 16.207  1.00 11.67  ? 149 LYS A CG    1 
ATOM   1208 C  CD    . LYS A 1 148 ? 2.448   -15.106 17.447  1.00 16.82  ? 149 LYS A CD    1 
ATOM   1209 C  CE    . LYS A 1 148 ? 0.981   -15.101 17.368  1.00 23.20  ? 149 LYS A CE    1 
ATOM   1210 N  NZ    . LYS A 1 148 ? 0.484   -16.034 18.388  1.00 36.80  ? 149 LYS A NZ    1 
ATOM   1211 N  N     . VAL A 1 149 ? 5.261   -15.522 13.390  1.00 8.65   ? 150 VAL A N     1 
ATOM   1212 C  CA    . VAL A 1 149 ? 4.910   -16.108 12.099  1.00 10.07  ? 150 VAL A CA    1 
ATOM   1213 C  C     . VAL A 1 149 ? 3.718   -17.029 12.284  1.00 10.48  ? 150 VAL A C     1 
ATOM   1214 O  O     . VAL A 1 149 ? 3.762   -18.015 13.007  1.00 12.17  ? 150 VAL A O     1 
ATOM   1215 C  CB    . VAL A 1 149 ? 6.114   -16.835 11.530  1.00 10.72  ? 150 VAL A CB    1 
ATOM   1216 C  CG1   . VAL A 1 149 ? 5.694   -17.604 10.214  1.00 12.75  ? 150 VAL A CG1   1 
ATOM   1217 C  CG2   . VAL A 1 149 ? 7.176   -15.771 11.248  1.00 12.44  ? 150 VAL A CG2   1 
ATOM   1218 N  N     . GLY A 1 150 ? 2.690   -16.741 11.535  1.00 10.19  ? 151 GLY A N     1 
ATOM   1219 C  CA    . GLY A 1 150 ? 1.460   -17.605 11.525  1.00 12.28  ? 151 GLY A CA    1 
ATOM   1220 C  C     . GLY A 1 150 ? 0.592   -17.130 10.404  1.00 11.50  ? 151 GLY A C     1 
ATOM   1221 O  O     . GLY A 1 150 ? 0.976   -17.203 9.238   1.00 12.81  ? 151 GLY A O     1 
ATOM   1222 N  N     A SER A 1 151 ? -0.592  -16.615 10.721  0.50 11.83  ? 152 SER A N     1 
ATOM   1223 N  N     B SER A 1 151 ? -0.609  -16.647 10.709  0.50 11.88  ? 152 SER A N     1 
ATOM   1224 C  CA    A SER A 1 151 ? -1.474  -15.975 9.752   0.50 13.05  ? 152 SER A CA    1 
ATOM   1225 C  CA    B SER A 1 151 ? -1.507  -16.061 9.716   0.50 13.76  ? 152 SER A CA    1 
ATOM   1226 C  C     A SER A 1 151 ? -0.885  -14.727 9.164   0.50 12.46  ? 152 SER A C     1 
ATOM   1227 C  C     B SER A 1 151 ? -0.931  -14.770 9.170   0.50 12.26  ? 152 SER A C     1 
ATOM   1228 O  O     A SER A 1 151 ? -0.136  -14.014 9.819   0.50 12.10  ? 152 SER A O     1 
ATOM   1229 O  O     B SER A 1 151 ? -0.222  -14.066 9.871   0.50 11.82  ? 152 SER A O     1 
ATOM   1230 C  CB    A SER A 1 151 ? -2.825  -15.654 10.388  0.50 15.60  ? 152 SER A CB    1 
ATOM   1231 C  CB    B SER A 1 151 ? -2.894  -15.795 10.319  0.50 17.50  ? 152 SER A CB    1 
ATOM   1232 O  OG    A SER A 1 151 ? -3.417  -16.881 10.765  0.50 18.42  ? 152 SER A OG    1 
ATOM   1233 O  OG    B SER A 1 151 ? -2.866  -14.686 11.199  0.50 18.59  ? 152 SER A OG    1 
ATOM   1234 N  N     . ALA A 1 152 ? -1.217  -14.469 7.890   1.00 11.86  ? 153 ALA A N     1 
ATOM   1235 C  CA    . ALA A 1 152 ? -0.809  -13.265 7.302   1.00 10.99  ? 153 ALA A CA    1 
ATOM   1236 C  C     . ALA A 1 152 ? -1.471  -12.037 7.934   1.00 11.96  ? 153 ALA A C     1 
ATOM   1237 O  O     . ALA A 1 152 ? -2.606  -12.105 8.403   1.00 13.47  ? 153 ALA A O     1 
ATOM   1238 C  CB    . ALA A 1 152 ? -1.170  -13.261 5.792   1.00 13.99  ? 153 ALA A CB    1 
ATOM   1239 N  N     . LYS A 1 153 ? -0.757  -10.908 7.883   1.00 10.99  ? 154 LYS A N     1 
ATOM   1240 C  CA    . LYS A 1 153 ? -1.275  -9.627  8.301   1.00 13.41  ? 154 LYS A CA    1 
ATOM   1241 C  C     . LYS A 1 153 ? -1.692  -8.891  7.051   1.00 12.86  ? 154 LYS A C     1 
ATOM   1242 O  O     . LYS A 1 153 ? -0.825  -8.396  6.329   1.00 12.25  ? 154 LYS A O     1 
ATOM   1243 C  CB    . LYS A 1 153 ? -0.278  -8.836  9.141   1.00 12.01  ? 154 LYS A CB    1 
ATOM   1244 C  CG    . LYS A 1 153 ? -0.757  -7.651  9.920   1.00 15.72  ? 154 LYS A CG    1 
ATOM   1245 C  CD    . LYS A 1 153 ? -1.675  -8.051  11.057  1.00 16.90  ? 154 LYS A CD    1 
ATOM   1246 C  CE    . LYS A 1 153 ? -1.933  -6.828  11.913  1.00 21.98  ? 154 LYS A CE    1 
ATOM   1247 N  NZ    . LYS A 1 153 ? -2.894  -7.266  12.901  1.00 28.38  ? 154 LYS A NZ    1 
ATOM   1248 N  N     . PRO A 1 154 ? -3.024  -8.806  6.794   1.00 14.22  ? 155 PRO A N     1 
ATOM   1249 C  CA    . PRO A 1 154 ? -3.397  -8.197  5.549   1.00 15.87  ? 155 PRO A CA    1 
ATOM   1250 C  C     . PRO A 1 154 ? -2.857  -6.766  5.373   1.00 15.06  ? 155 PRO A C     1 
ATOM   1251 O  O     . PRO A 1 154 ? -2.382  -6.345  4.281   1.00 19.76  ? 155 PRO A O     1 
ATOM   1252 C  CB    . PRO A 1 154 ? -4.916  -8.308  5.636   1.00 19.02  ? 155 PRO A CB    1 
ATOM   1253 C  CG    . PRO A 1 154 ? -5.176  -9.511  6.494   1.00 22.31  ? 155 PRO A CG    1 
ATOM   1254 C  CD    . PRO A 1 154 ? -4.169  -9.330  7.554   1.00 16.90  ? 155 PRO A CD    1 
ATOM   1255 N  N     . GLY A 1 155 ? -2.817  -6.005  6.494   1.00 14.34  ? 156 GLY A N     1 
ATOM   1256 C  CA    . GLY A 1 155 ? -2.341  -4.683  6.478   1.00 15.35  ? 156 GLY A CA    1 
ATOM   1257 C  C     . GLY A 1 155 ? -0.869  -4.450  6.191   1.00 15.58  ? 156 GLY A C     1 
ATOM   1258 O  O     . GLY A 1 155 ? -0.423  -3.296  6.004   1.00 18.99  ? 156 GLY A O     1 
ATOM   1259 N  N     . LEU A 1 156 ? -0.083  -5.525  6.226   1.00 12.71  ? 157 LEU A N     1 
ATOM   1260 C  CA    . LEU A 1 156 ? 1.340   -5.441  5.928   1.00 11.76  ? 157 LEU A CA    1 
ATOM   1261 C  C     . LEU A 1 156 ? 1.627   -5.655  4.423   1.00 12.08  ? 157 LEU A C     1 
ATOM   1262 O  O     . LEU A 1 156 ? 2.690   -5.385  3.965   1.00 13.33  ? 157 LEU A O     1 
ATOM   1263 C  CB    . LEU A 1 156 ? 2.053   -6.525  6.763   1.00 12.16  ? 157 LEU A CB    1 
ATOM   1264 C  CG    . LEU A 1 156 ? 3.534   -6.628  6.611   1.00 12.01  ? 157 LEU A CG    1 
ATOM   1265 C  CD1   . LEU A 1 156 ? 4.244   -5.354  7.011   1.00 13.58  ? 157 LEU A CD1   1 
ATOM   1266 C  CD2   . LEU A 1 156 ? 4.082   -7.809  7.389   1.00 12.49  ? 157 LEU A CD2   1 
ATOM   1267 N  N     . GLN A 1 157 ? 0.645   -6.190  3.701   1.00 12.70  ? 158 GLN A N     1 
ATOM   1268 C  CA    . GLN A 1 157 ? 0.938   -6.768  2.385   1.00 13.82  ? 158 GLN A CA    1 
ATOM   1269 C  C     . GLN A 1 157 ? 1.384   -5.640  1.477   1.00 14.95  ? 158 GLN A C     1 
ATOM   1270 O  O     . GLN A 1 157 ? 2.229   -5.847  0.622   1.00 15.45  ? 158 GLN A O     1 
ATOM   1271 C  CB    . GLN A 1 157 ? -0.229  -7.629  1.816   1.00 15.98  ? 158 GLN A CB    1 
ATOM   1272 C  CG    . GLN A 1 157 ? 0.087   -8.432  0.555   1.00 17.24  ? 158 GLN A CG    1 
ATOM   1273 C  CD    . GLN A 1 157 ? 1.302   -9.328  0.771   1.00 15.05  ? 158 GLN A CD    1 
ATOM   1274 O  OE1   . GLN A 1 157 ? 1.482   -9.925  1.863   1.00 15.17  ? 158 GLN A OE1   1 
ATOM   1275 N  NE2   . GLN A 1 157 ? 2.045   -9.567  -0.235  1.00 18.92  ? 158 GLN A NE2   1 
ATOM   1276 N  N     . LYS A 1 158 ? 0.831   -4.455  1.563   1.00 15.50  ? 159 LYS A N     1 
ATOM   1277 C  CA    . LYS A 1 158 ? 1.232   -3.294  0.721   1.00 15.91  ? 159 LYS A CA    1 
ATOM   1278 C  C     . LYS A 1 158 ? 2.704   -2.974  0.881   1.00 15.02  ? 159 LYS A C     1 
ATOM   1279 O  O     . LYS A 1 158 ? 3.451   -2.619  -0.050  1.00 16.79  ? 159 LYS A O     1 
ATOM   1280 C  CB    . LYS A 1 158 ? 0.388   -2.075  0.854   1.00 18.64  ? 159 LYS A CB    1 
ATOM   1281 C  CG    . LYS A 1 158 ? -1.031  -2.100  0.188   1.00 24.93  ? 159 LYS A CG    1 
ATOM   1282 C  CD    . LYS A 1 158 ? -1.665  -0.664  -0.008  1.00 38.60  ? 159 LYS A CD    1 
ATOM   1283 C  CE    . LYS A 1 158 ? -2.451  -0.036  1.187   1.00 48.91  ? 159 LYS A CE    1 
ATOM   1284 N  NZ    . LYS A 1 158 ? -3.017  1.401   1.173   1.00 30.06  ? 159 LYS A NZ    1 
ATOM   1285 N  N     . VAL A 1 159 ? 3.196   -3.137  2.121   1.00 14.91  ? 160 VAL A N     1 
ATOM   1286 C  CA    . VAL A 1 159 ? 4.614   -2.944  2.369   1.00 12.53  ? 160 VAL A CA    1 
ATOM   1287 C  C     . VAL A 1 159 ? 5.450   -4.055  1.735   1.00 12.31  ? 160 VAL A C     1 
ATOM   1288 O  O     . VAL A 1 159 ? 6.403   -3.793  1.055   1.00 13.00  ? 160 VAL A O     1 
ATOM   1289 C  CB    . VAL A 1 159 ? 4.927   -2.913  3.901   1.00 13.71  ? 160 VAL A CB    1 
ATOM   1290 C  CG1   . VAL A 1 159 ? 6.404   -3.031  4.214   1.00 14.70  ? 160 VAL A CG1   1 
ATOM   1291 C  CG2   . VAL A 1 159 ? 4.273   -1.715  4.548   1.00 15.59  ? 160 VAL A CG2   1 
ATOM   1292 N  N     . VAL A 1 160 ? 5.068   -5.288  1.940   1.00 11.31  ? 161 VAL A N     1 
ATOM   1293 C  CA    . VAL A 1 160 ? 5.810   -6.407  1.346   1.00 12.36  ? 161 VAL A CA    1 
ATOM   1294 C  C     . VAL A 1 160 ? 5.880   -6.298  -0.150  1.00 13.41  ? 161 VAL A C     1 
ATOM   1295 O  O     . VAL A 1 160 ? 6.928   -6.559  -0.746  1.00 14.08  ? 161 VAL A O     1 
ATOM   1296 C  CB    . VAL A 1 160 ? 5.037   -7.782  1.752   1.00 16.84  ? 161 VAL A CB    1 
ATOM   1297 C  CG1   . VAL A 1 160 ? 5.438   -8.930  0.867   1.00 19.16  ? 161 VAL A CG1   1 
ATOM   1298 C  CG2   . VAL A 1 160 ? 5.242   -8.003  3.237   1.00 20.06  ? 161 VAL A CG2   1 
ATOM   1299 N  N     A ASP A 1 161 ? 4.788   -5.904  -0.769  0.50 14.09  ? 162 ASP A N     1 
ATOM   1300 N  N     B ASP A 1 161 ? 4.722   -5.894  -0.744  0.50 14.54  ? 162 ASP A N     1 
ATOM   1301 C  CA    A ASP A 1 161 ? 4.788   -5.944  -2.231  0.50 15.57  ? 162 ASP A CA    1 
ATOM   1302 C  CA    B ASP A 1 161 ? 4.569   -5.730  -2.244  0.50 18.17  ? 162 ASP A CA    1 
ATOM   1303 C  C     A ASP A 1 161 ? 5.662   -4.816  -2.859  0.50 16.57  ? 162 ASP A C     1 
ATOM   1304 C  C     B ASP A 1 161 ? 5.627   -4.806  -2.843  0.50 18.80  ? 162 ASP A C     1 
ATOM   1305 O  O     A ASP A 1 161 ? 6.006   -4.917  -4.035  0.50 21.04  ? 162 ASP A O     1 
ATOM   1306 O  O     B ASP A 1 161 ? 5.997   -4.994  -3.997  0.50 25.80  ? 162 ASP A O     1 
ATOM   1307 C  CB    A ASP A 1 161 ? 3.367   -5.886  -2.700  0.50 15.78  ? 162 ASP A CB    1 
ATOM   1308 C  CB    B ASP A 1 161 ? 3.276   -5.006  -2.648  0.50 22.33  ? 162 ASP A CB    1 
ATOM   1309 C  CG    A ASP A 1 161 ? 2.664   -7.261  -2.631  0.50 13.07  ? 162 ASP A CG    1 
ATOM   1310 C  CG    B ASP A 1 161 ? 2.020   -5.854  -2.523  0.50 25.82  ? 162 ASP A CG    1 
ATOM   1311 O  OD1   A ASP A 1 161 ? 3.339   -8.325  -2.678  0.50 15.25  ? 162 ASP A OD1   1 
ATOM   1312 O  OD1   B ASP A 1 161 ? 2.180   -7.094  -2.528  0.50 27.66  ? 162 ASP A OD1   1 
ATOM   1313 O  OD2   A ASP A 1 161 ? 1.414   -7.255  -2.515  0.50 17.20  ? 162 ASP A OD2   1 
ATOM   1314 O  OD2   B ASP A 1 161 ? 0.877   -5.269  -2.453  0.50 30.12  ? 162 ASP A OD2   1 
ATOM   1315 N  N     . VAL A 1 162 ? 6.021   -3.754  -2.119  1.00 17.33  ? 163 VAL A N     1 
ATOM   1316 C  CA    . VAL A 1 162 ? 6.866   -2.705  -2.642  1.00 17.24  ? 163 VAL A CA    1 
ATOM   1317 C  C     . VAL A 1 162 ? 8.377   -3.013  -2.477  1.00 14.84  ? 163 VAL A C     1 
ATOM   1318 O  O     . VAL A 1 162 ? 9.289   -2.371  -3.033  1.00 15.15  ? 163 VAL A O     1 
ATOM   1319 C  CB    . VAL A 1 162 ? 6.491   -1.336  -2.025  1.00 17.19  ? 163 VAL A CB    1 
ATOM   1320 C  CG1   . VAL A 1 162 ? 7.110   -1.106  -0.668  1.00 22.34  ? 163 VAL A CG1   1 
ATOM   1321 C  CG2   . VAL A 1 162 ? 6.825   -0.158  -2.926  1.00 20.68  ? 163 VAL A CG2   1 
ATOM   1322 N  N     . LEU A 1 163 ? 8.693   -4.034  -1.671  1.00 14.05  ? 164 LEU A N     1 
ATOM   1323 C  CA    . LEU A 1 163 ? 10.076  -4.279  -1.352  1.00 12.43  ? 164 LEU A CA    1 
ATOM   1324 C  C     . LEU A 1 163 ? 11.026  -4.656  -2.559  1.00 14.89  ? 164 LEU A C     1 
ATOM   1325 O  O     . LEU A 1 163 ? 12.212  -4.392  -2.549  1.00 14.33  ? 164 LEU A O     1 
ATOM   1326 C  CB    . LEU A 1 163 ? 10.248  -5.338  -0.263  1.00 12.55  ? 164 LEU A CB    1 
ATOM   1327 C  CG    . LEU A 1 163 ? 9.603   -5.006  1.090   1.00 12.38  ? 164 LEU A CG    1 
ATOM   1328 C  CD1   . LEU A 1 163 ? 9.771   -6.128  2.087   1.00 13.47  ? 164 LEU A CD1   1 
ATOM   1329 C  CD2   . LEU A 1 163 ? 10.097  -3.680  1.634   1.00 12.58  ? 164 LEU A CD2   1 
ATOM   1330 N  N     . ASP A 1 164 ? 10.427  -5.327  -3.540  1.00 17.31  ? 165 ASP A N     1 
ATOM   1331 C  CA    . ASP A 1 164 ? 11.144  -5.631  -4.764  1.00 20.71  ? 165 ASP A CA    1 
ATOM   1332 C  C     . ASP A 1 164 ? 11.710  -4.411  -5.455  1.00 18.95  ? 165 ASP A C     1 
ATOM   1333 O  O     . ASP A 1 164 ? 12.680  -4.552  -6.175  1.00 23.18  ? 165 ASP A O     1 
ATOM   1334 C  CB    . ASP A 1 164 ? 10.204  -6.305  -5.814  1.00 26.36  ? 165 ASP A CB    1 
ATOM   1335 C  CG    . ASP A 1 164 ? 9.927   -7.682  -5.509  1.00 41.40  ? 165 ASP A CG    1 
ATOM   1336 O  OD1   . ASP A 1 164 ? 10.846  -8.346  -4.919  1.00 46.44  ? 165 ASP A OD1   1 
ATOM   1337 O  OD2   . ASP A 1 164 ? 8.792   -8.084  -5.893  1.00 56.07  ? 165 ASP A OD2   1 
ATOM   1338 N  N     . SER A 1 165 ? 11.076  -3.270  -5.207  1.00 17.15  ? 166 SER A N     1 
ATOM   1339 C  CA    . SER A 1 165 ? 11.503  -2.019  -5.838  1.00 17.14  ? 166 SER A CA    1 
ATOM   1340 C  C     . SER A 1 165 ? 12.539  -1.244  -5.068  1.00 14.91  ? 166 SER A C     1 
ATOM   1341 O  O     . SER A 1 165 ? 13.096  -0.269  -5.555  1.00 17.59  ? 166 SER A O     1 
ATOM   1342 C  CB    . SER A 1 165 ? 10.355  -1.135  -6.103  1.00 19.02  ? 166 SER A CB    1 
ATOM   1343 O  OG    . SER A 1 165 ? 9.919   -0.506  -4.962  1.00 20.08  ? 166 SER A OG    1 
ATOM   1344 N  N     . ILE A 1 166 ? 12.875  -1.728  -3.845  1.00 13.02  ? 167 ILE A N     1 
ATOM   1345 C  CA    . ILE A 1 166 ? 13.917  -1.120  -2.998  1.00 12.15  ? 167 ILE A CA    1 
ATOM   1346 C  C     . ILE A 1 166 ? 14.867  -2.133  -2.474  1.00 12.00  ? 167 ILE A C     1 
ATOM   1347 O  O     . ILE A 1 166 ? 15.249  -2.151  -1.330  1.00 12.80  ? 167 ILE A O     1 
ATOM   1348 C  CB    . ILE A 1 166 ? 13.295  -0.223  -1.852  1.00 13.71  ? 167 ILE A CB    1 
ATOM   1349 C  CG1   . ILE A 1 166 ? 12.365  -1.037  -0.994  1.00 12.89  ? 167 ILE A CG1   1 
ATOM   1350 C  CG2   . ILE A 1 166 ? 12.627  0.987   -2.468  1.00 14.69  ? 167 ILE A CG2   1 
ATOM   1351 C  CD1   . ILE A 1 166 ? 12.340  -0.487  0.441   1.00 13.56  ? 167 ILE A CD1   1 
ATOM   1352 N  N     . LYS A 1 167 ? 15.317  -3.019  -3.394  1.00 12.55  ? 168 LYS A N     1 
ATOM   1353 C  CA    . LYS A 1 167 ? 16.067  -4.176  -2.963  1.00 11.61  ? 168 LYS A CA    1 
ATOM   1354 C  C     . LYS A 1 167 ? 17.376  -3.792  -2.231  1.00 11.52  ? 168 LYS A C     1 
ATOM   1355 O  O     . LYS A 1 167 ? 17.810  -4.456  -1.286  1.00 12.42  ? 168 LYS A O     1 
ATOM   1356 C  CB    . LYS A 1 167 ? 16.384  -5.103  -4.120  1.00 14.20  ? 168 LYS A CB    1 
ATOM   1357 C  CG    . LYS A 1 167 ? 17.048  -6.423  -3.695  1.00 15.22  ? 168 LYS A CG    1 
ATOM   1358 C  CD    . LYS A 1 167 ? 17.239  -7.255  -4.964  1.00 20.26  ? 168 LYS A CD    1 
ATOM   1359 C  CE    . LYS A 1 167 ? 17.969  -8.491  -4.591  1.00 21.52  ? 168 LYS A CE    1 
ATOM   1360 N  NZ    . LYS A 1 167 ? 18.206  -9.400  -5.717  1.00 35.30  ? 168 LYS A NZ    1 
ATOM   1361 N  N     . THR A 1 168 ? 18.001  -2.757  -2.785  1.00 12.64  ? 169 THR A N     1 
ATOM   1362 C  CA    . THR A 1 168 ? 19.307  -2.444  -2.353  1.00 12.95  ? 169 THR A CA    1 
ATOM   1363 C  C     . THR A 1 168 ? 19.369  -0.932  -1.762  1.00 11.27  ? 169 THR A C     1 
ATOM   1364 O  O     . THR A 1 168 ? 18.466  -0.153  -1.847  1.00 14.09  ? 169 THR A O     1 
ATOM   1365 C  CB    . THR A 1 168 ? 20.306  -2.511  -3.550  1.00 14.78  ? 169 THR A CB    1 
ATOM   1366 O  OG1   . THR A 1 168 ? 19.731  -1.767  -4.634  1.00 15.58  ? 169 THR A OG1   1 
ATOM   1367 C  CG2   . THR A 1 168 ? 20.563  -3.976  -3.971  1.00 15.36  ? 169 THR A CG2   1 
ATOM   1368 N  N     . LYS A 1 169 ? 20.420  -0.914  -0.974  1.00 14.36  ? 170 LYS A N     1 
ATOM   1369 C  CA    . LYS A 1 169 ? 20.716  0.331   -0.147  1.00 15.06  ? 170 LYS A CA    1 
ATOM   1370 C  C     . LYS A 1 169 ? 20.708  1.621   -0.958  1.00 13.22  ? 170 LYS A C     1 
ATOM   1371 O  O     . LYS A 1 169 ? 21.206  1.620   -2.116  1.00 17.08  ? 170 LYS A O     1 
ATOM   1372 C  CB    . LYS A 1 169 ? 22.104  0.166   0.384   1.00 14.31  ? 170 LYS A CB    1 
ATOM   1373 C  CG    . LYS A 1 169 ? 22.560  1.387   1.241   1.00 17.38  ? 170 LYS A CG    1 
ATOM   1374 C  CD    . LYS A 1 169 ? 23.892  1.151   1.809   1.00 19.27  ? 170 LYS A CD    1 
ATOM   1375 C  CE    . LYS A 1 169 ? 25.003  1.023   0.827   1.00 28.72  ? 170 LYS A CE    1 
ATOM   1376 N  NZ    . LYS A 1 169 ? 26.252  0.386   1.275   1.00 40.17  ? 170 LYS A NZ    1 
ATOM   1377 N  N     . GLY A 1 170 ? 19.883  2.553   -0.500  1.00 16.25  ? 171 GLY A N     1 
ATOM   1378 C  CA    . GLY A 1 170 ? 19.685  3.815   -1.222  1.00 15.09  ? 171 GLY A CA    1 
ATOM   1379 C  C     . GLY A 1 170 ? 18.566  3.904   -2.179  1.00 16.22  ? 171 GLY A C     1 
ATOM   1380 O  O     . GLY A 1 170 ? 18.444  4.954   -2.765  1.00 20.85  ? 171 GLY A O     1 
ATOM   1381 N  N     . LYS A 1 171 ? 17.959  2.792   -2.511  1.00 16.61  ? 172 LYS A N     1 
ATOM   1382 C  CA    . LYS A 1 171 ? 16.688  2.838   -3.196  1.00 14.23  ? 172 LYS A CA    1 
ATOM   1383 C  C     . LYS A 1 171 ? 15.491  3.325   -2.442  1.00 14.54  ? 172 LYS A C     1 
ATOM   1384 O  O     . LYS A 1 171 ? 15.307  2.875   -1.285  1.00 15.18  ? 172 LYS A O     1 
ATOM   1385 C  CB    . LYS A 1 171 ? 16.442  1.479   -3.894  1.00 15.07  ? 172 LYS A CB    1 
ATOM   1386 C  CG    . LYS A 1 171 ? 17.452  1.084   -4.935  1.00 17.55  ? 172 LYS A CG    1 
ATOM   1387 C  CD    . LYS A 1 171 ? 17.086  -0.006  -5.948  1.00 23.11  ? 172 LYS A CD    1 
ATOM   1388 C  CE    . LYS A 1 171 ? 17.815  -0.036  -7.270  1.00 33.35  ? 172 LYS A CE    1 
ATOM   1389 N  NZ    . LYS A 1 171 ? 17.588  0.998   -8.328  1.00 41.60  ? 172 LYS A NZ    1 
ATOM   1390 N  N     . SER A 1 172 ? 14.717  4.206   -2.926  1.00 16.63  ? 173 SER A N     1 
ATOM   1391 C  CA    . SER A 1 172 ? 13.388  4.585   -2.400  1.00 17.87  ? 173 SER A CA    1 
ATOM   1392 C  C     . SER A 1 172 ? 12.291  4.440   -3.318  1.00 15.38  ? 173 SER A C     1 
ATOM   1393 O  O     . SER A 1 172 ? 12.567  4.368   -4.624  1.00 19.05  ? 173 SER A O     1 
ATOM   1394 C  CB    . SER A 1 172 ? 13.264  6.013   -1.940  1.00 15.96  ? 173 SER A CB    1 
ATOM   1395 O  OG    . SER A 1 172 ? 13.530  6.899   -2.985  1.00 22.54  ? 173 SER A OG    1 
ATOM   1396 N  N     . ALA A 1 173 ? 11.056  4.506   -2.952  1.00 16.54  ? 174 ALA A N     1 
ATOM   1397 C  CA    . ALA A 1 173 ? 9.883   4.485   -3.803  1.00 18.91  ? 174 ALA A CA    1 
ATOM   1398 C  C     . ALA A 1 173 ? 8.706   5.241   -3.181  1.00 17.36  ? 174 ALA A C     1 
ATOM   1399 O  O     . ALA A 1 173 ? 8.499   5.263   -1.930  1.00 15.41  ? 174 ALA A O     1 
ATOM   1400 C  CB    . ALA A 1 173 ? 9.506   3.073   -4.011  1.00 21.24  ? 174 ALA A CB    1 
ATOM   1401 N  N     . ASP A 1 174 ? 7.966   5.944   -3.966  1.00 19.48  ? 175 ASP A N     1 
ATOM   1402 C  CA    . ASP A 1 174 ? 6.687   6.527   -3.501  1.00 19.70  ? 175 ASP A CA    1 
ATOM   1403 C  C     . ASP A 1 174 ? 5.889   5.489   -2.752  1.00 18.99  ? 175 ASP A C     1 
ATOM   1404 O  O     . ASP A 1 174 ? 5.876   4.377   -3.124  1.00 22.79  ? 175 ASP A O     1 
ATOM   1405 C  CB    . ASP A 1 174 ? 5.870   7.050   -4.738  1.00 22.26  ? 175 ASP A CB    1 
ATOM   1406 C  CG    . ASP A 1 174 ? 6.530   8.270   -5.329  1.00 31.33  ? 175 ASP A CG    1 
ATOM   1407 O  OD1   . ASP A 1 174 ? 6.980   9.187   -4.605  1.00 37.93  ? 175 ASP A OD1   1 
ATOM   1408 O  OD2   . ASP A 1 174 ? 6.636   8.319   -6.560  1.00 32.54  ? 175 ASP A OD2   1 
ATOM   1409 N  N     . PHE A 1 175 ? 5.303   5.929   -1.629  1.00 17.38  ? 176 PHE A N     1 
ATOM   1410 C  CA    . PHE A 1 175 ? 4.554   5.018   -0.770  1.00 16.59  ? 176 PHE A CA    1 
ATOM   1411 C  C     . PHE A 1 175 ? 3.567   5.836   -0.008  1.00 16.41  ? 176 PHE A C     1 
ATOM   1412 O  O     . PHE A 1 175 ? 3.745   6.131   1.191   1.00 19.72  ? 176 PHE A O     1 
ATOM   1413 C  CB    . PHE A 1 175 ? 5.469   4.208   0.145   1.00 16.30  ? 176 PHE A CB    1 
ATOM   1414 C  CG    . PHE A 1 175 ? 4.836   2.933   0.687   1.00 18.40  ? 176 PHE A CG    1 
ATOM   1415 C  CD1   . PHE A 1 175 ? 4.428   1.972   -0.124  1.00 20.18  ? 176 PHE A CD1   1 
ATOM   1416 C  CD2   . PHE A 1 175 ? 4.532   2.806   2.036   1.00 18.60  ? 176 PHE A CD2   1 
ATOM   1417 C  CE1   . PHE A 1 175 ? 3.826   0.798   0.301   1.00 22.48  ? 176 PHE A CE1   1 
ATOM   1418 C  CE2   . PHE A 1 175 ? 3.881   1.655   2.504   1.00 17.65  ? 176 PHE A CE2   1 
ATOM   1419 C  CZ    . PHE A 1 175 ? 3.540   0.653   1.638   1.00 19.46  ? 176 PHE A CZ    1 
ATOM   1420 N  N     . THR A 1 176 ? 2.574   6.255   -0.729  1.00 15.92  ? 177 THR A N     1 
ATOM   1421 C  CA    . THR A 1 176 ? 1.570   7.070   -0.203  1.00 13.47  ? 177 THR A CA    1 
ATOM   1422 C  C     . THR A 1 176 ? 0.412   6.290   0.245   1.00 14.87  ? 177 THR A C     1 
ATOM   1423 O  O     . THR A 1 176 ? 0.178   5.157   -0.215  1.00 15.74  ? 177 THR A O     1 
ATOM   1424 C  CB    . THR A 1 176 ? 1.179   8.150   -1.223  1.00 14.86  ? 177 THR A CB    1 
ATOM   1425 O  OG1   . THR A 1 176 ? 0.882   7.524   -2.460  1.00 22.82  ? 177 THR A OG1   1 
ATOM   1426 C  CG2   . THR A 1 176 ? 2.244   9.161   -1.504  1.00 20.92  ? 177 THR A CG2   1 
ATOM   1427 N  N     . ASN A 1 177 ? -0.388  6.873   1.132   1.00 14.84  ? 178 ASN A N     1 
ATOM   1428 C  CA    . ASN A 1 177 ? -1.685  6.351   1.566   1.00 16.84  ? 178 ASN A CA    1 
ATOM   1429 C  C     . ASN A 1 177 ? -1.628  5.019   2.304   1.00 16.09  ? 178 ASN A C     1 
ATOM   1430 O  O     . ASN A 1 177 ? -2.551  4.321   2.317   1.00 22.59  ? 178 ASN A O     1 
ATOM   1431 C  CB    . ASN A 1 177 ? -2.619  6.219   0.397   1.00 17.98  ? 178 ASN A CB    1 
ATOM   1432 C  CG    . ASN A 1 177 ? -2.761  7.576   -0.328  1.00 17.84  ? 178 ASN A CG    1 
ATOM   1433 O  OD1   . ASN A 1 177 ? -2.218  7.863   -1.394  1.00 20.81  ? 178 ASN A OD1   1 
ATOM   1434 N  ND2   . ASN A 1 177 ? -3.410  8.435   0.301   1.00 17.50  ? 178 ASN A ND2   1 
ATOM   1435 N  N     . PHE A 1 178 ? -0.491  4.764   2.921   1.00 13.51  ? 179 PHE A N     1 
ATOM   1436 C  CA    . PHE A 1 178 ? -0.473  3.530   3.693   1.00 14.40  ? 179 PHE A CA    1 
ATOM   1437 C  C     . PHE A 1 178 ? -0.906  3.796   5.136   1.00 12.42  ? 179 PHE A C     1 
ATOM   1438 O  O     . PHE A 1 178 ? -0.433  4.780   5.720   1.00 13.97  ? 179 PHE A O     1 
ATOM   1439 C  CB    . PHE A 1 178 ? 0.960   3.058   3.751   1.00 14.18  ? 179 PHE A CB    1 
ATOM   1440 C  CG    . PHE A 1 178 ? 1.094   1.832   4.593   1.00 14.97  ? 179 PHE A CG    1 
ATOM   1441 C  CD1   . PHE A 1 178 ? 0.685   0.567   4.093   1.00 16.55  ? 179 PHE A CD1   1 
ATOM   1442 C  CD2   . PHE A 1 178 ? 1.545   1.888   5.943   1.00 13.43  ? 179 PHE A CD2   1 
ATOM   1443 C  CE1   . PHE A 1 178 ? 0.688   -0.568  4.891   1.00 17.31  ? 179 PHE A CE1   1 
ATOM   1444 C  CE2   . PHE A 1 178 ? 1.539   0.709   6.716   1.00 12.28  ? 179 PHE A CE2   1 
ATOM   1445 C  CZ    . PHE A 1 178 ? 1.132   -0.500  6.197   1.00 15.60  ? 179 PHE A CZ    1 
ATOM   1446 N  N     . ASP A 1 179 ? -1.756  2.973   5.674   1.00 12.05  ? 180 ASP A N     1 
ATOM   1447 C  CA    . ASP A 1 179 ? -2.378  3.215   6.942   1.00 12.46  ? 180 ASP A CA    1 
ATOM   1448 C  C     . ASP A 1 179 ? -1.701  2.307   8.002   1.00 10.00  ? 180 ASP A C     1 
ATOM   1449 O  O     . ASP A 1 179 ? -1.927  1.097   8.028   1.00 11.94  ? 180 ASP A O     1 
ATOM   1450 C  CB    . ASP A 1 179 ? -3.862  2.864   6.811   1.00 14.14  ? 180 ASP A CB    1 
ATOM   1451 C  CG    . ASP A 1 179 ? -4.626  3.193   8.057   1.00 15.25  ? 180 ASP A CG    1 
ATOM   1452 O  OD1   . ASP A 1 179 ? -4.044  3.467   9.096   1.00 13.23  ? 180 ASP A OD1   1 
ATOM   1453 O  OD2   . ASP A 1 179 ? -5.827  3.230   7.944   1.00 25.84  ? 180 ASP A OD2   1 
ATOM   1454 N  N     . PRO A 1 180 ? -0.913  2.879   8.903   1.00 10.23  ? 181 PRO A N     1 
ATOM   1455 C  CA    . PRO A 1 180 ? -0.249  2.059   9.897   1.00 10.64  ? 181 PRO A CA    1 
ATOM   1456 C  C     . PRO A 1 180 ? -1.153  1.462   10.935  1.00 9.55   ? 181 PRO A C     1 
ATOM   1457 O  O     . PRO A 1 180 ? -0.702  0.584   11.686  1.00 10.34  ? 181 PRO A O     1 
ATOM   1458 C  CB    . PRO A 1 180 ? 0.746   3.058   10.501  1.00 11.89  ? 181 PRO A CB    1 
ATOM   1459 C  CG    . PRO A 1 180 ? 0.157   4.358   10.351  1.00 11.89  ? 181 PRO A CG    1 
ATOM   1460 C  CD    . PRO A 1 180 ? -0.563  4.282   8.997   1.00 11.73  ? 181 PRO A CD    1 
ATOM   1461 N  N     . ARG A 1 181 ? -2.415  1.850   10.964  1.00 9.54   ? 182 ARG A N     1 
ATOM   1462 C  CA    . ARG A 1 181 ? -3.349  1.171   11.896  1.00 10.31  ? 182 ARG A CA    1 
ATOM   1463 C  C     . ARG A 1 181 ? -3.447  -0.273  11.552  1.00 10.43  ? 182 ARG A C     1 
ATOM   1464 O  O     . ARG A 1 181 ? -3.806  -1.055  12.402  1.00 12.56  ? 182 ARG A O     1 
ATOM   1465 C  CB    . ARG A 1 181 ? -4.738  1.845   11.819  1.00 11.11  ? 182 ARG A CB    1 
ATOM   1466 C  CG    . ARG A 1 181 ? -4.645  3.255   12.379  1.00 10.88  ? 182 ARG A CG    1 
ATOM   1467 C  CD    . ARG A 1 181 ? -5.998  3.956   12.296  1.00 12.26  ? 182 ARG A CD    1 
ATOM   1468 N  NE    . ARG A 1 181 ? -6.367  4.186   10.910  1.00 14.42  ? 182 ARG A NE    1 
ATOM   1469 C  CZ    . ARG A 1 181 ? -7.382  4.893   10.588  1.00 15.49  ? 182 ARG A CZ    1 
ATOM   1470 N  NH1   . ARG A 1 181 ? -8.216  5.431   11.470  1.00 20.76  ? 182 ARG A NH1   1 
ATOM   1471 N  NH2   . ARG A 1 181 ? -7.640  5.027   9.270   1.00 20.91  ? 182 ARG A NH2   1 
ATOM   1472 N  N     . GLY A 1 182 ? -3.192  -0.662  10.291  1.00 10.83  ? 183 GLY A N     1 
ATOM   1473 C  CA    . GLY A 1 182 ? -3.197  -2.038  9.928   1.00 14.44  ? 183 GLY A CA    1 
ATOM   1474 C  C     . GLY A 1 182 ? -2.154  -2.907  10.480  1.00 11.56  ? 183 GLY A C     1 
ATOM   1475 O  O     . GLY A 1 182 ? -2.191  -4.116  10.215  1.00 14.49  ? 183 GLY A O     1 
ATOM   1476 N  N     . LEU A 1 183 ? -1.187  -2.327  11.203  1.00 12.08  ? 184 LEU A N     1 
ATOM   1477 C  CA    . LEU A 1 183 ? -0.121  -3.052  11.800  1.00 11.47  ? 184 LEU A CA    1 
ATOM   1478 C  C     . LEU A 1 183 ? -0.247  -3.245  13.292  1.00 11.51  ? 184 LEU A C     1 
ATOM   1479 O  O     . LEU A 1 183 ? 0.666   -3.750  13.942  1.00 12.36  ? 184 LEU A O     1 
ATOM   1480 C  CB    . LEU A 1 183 ? 1.192   -2.371  11.472  1.00 11.60  ? 184 LEU A CB    1 
ATOM   1481 C  CG    . LEU A 1 183 ? 1.477   -2.273  10.000  1.00 13.24  ? 184 LEU A CG    1 
ATOM   1482 C  CD1   . LEU A 1 183 ? 2.698   -1.512  9.808   1.00 14.58  ? 184 LEU A CD1   1 
ATOM   1483 C  CD2   . LEU A 1 183 ? 1.627   -3.581  9.295   1.00 18.66  ? 184 LEU A CD2   1 
ATOM   1484 N  N     . LEU A 1 184 ? -1.336  -2.763  13.871  1.00 10.87  ? 185 LEU A N     1 
ATOM   1485 C  CA    . LEU A 1 184 ? -1.468  -2.768  15.306  1.00 10.94  ? 185 LEU A CA    1 
ATOM   1486 C  C     . LEU A 1 184 ? -2.236  -4.042  15.814  1.00 13.07  ? 185 LEU A C     1 
ATOM   1487 O  O     . LEU A 1 184 ? -3.270  -4.414  15.224  1.00 21.81  ? 185 LEU A O     1 
ATOM   1488 C  CB    . LEU A 1 184 ? -2.261  -1.542  15.840  1.00 9.50   ? 185 LEU A CB    1 
ATOM   1489 C  CG    . LEU A 1 184 ? -1.683  -0.221  15.371  1.00 8.57   ? 185 LEU A CG    1 
ATOM   1490 C  CD1   . LEU A 1 184 ? -2.558  0.900   15.827  1.00 10.08  ? 185 LEU A CD1   1 
ATOM   1491 C  CD2   . LEU A 1 184 ? -0.296  -0.051  15.923  1.00 11.45  ? 185 LEU A CD2   1 
ATOM   1492 N  N     . PRO A 1 185 ? -1.890  -4.540  16.952  1.00 10.63  ? 186 PRO A N     1 
ATOM   1493 C  CA    . PRO A 1 185 ? -2.607  -5.664  17.546  1.00 11.22  ? 186 PRO A CA    1 
ATOM   1494 C  C     . PRO A 1 185 ? -3.909  -5.159  18.176  1.00 11.39  ? 186 PRO A C     1 
ATOM   1495 O  O     . PRO A 1 185 ? -4.125  -3.983  18.255  1.00 13.88  ? 186 PRO A O     1 
ATOM   1496 C  CB    . PRO A 1 185 ? -1.668  -6.255  18.529  1.00 10.17  ? 186 PRO A CB    1 
ATOM   1497 C  CG    . PRO A 1 185 ? -0.905  -5.023  18.984  1.00 8.82   ? 186 PRO A CG    1 
ATOM   1498 C  CD    . PRO A 1 185 ? -0.731  -4.150  17.757  1.00 8.45   ? 186 PRO A CD    1 
ATOM   1499 N  N     . GLU A 1 186 ? -4.735  -6.050  18.628  1.00 11.58  ? 187 GLU A N     1 
ATOM   1500 C  CA    . GLU A 1 186 ? -5.993  -5.695  19.260  1.00 12.45  ? 187 GLU A CA    1 
ATOM   1501 C  C     . GLU A 1 186 ? -5.770  -4.938  20.565  1.00 12.34  ? 187 GLU A C     1 
ATOM   1502 O  O     . GLU A 1 186 ? -6.365  -3.864  20.745  1.00 14.16  ? 187 GLU A O     1 
ATOM   1503 C  CB    . GLU A 1 186 ? -6.651  -6.998  19.515  1.00 17.14  ? 187 GLU A CB    1 
ATOM   1504 C  CG    . GLU A 1 186 ? -7.907  -6.879  20.145  1.00 23.02  ? 187 GLU A CG    1 
ATOM   1505 C  CD    . GLU A 1 186 ? -8.485  -8.214  20.576  1.00 22.22  ? 187 GLU A CD    1 
ATOM   1506 O  OE1   . GLU A 1 186 ? -8.314  -9.106  19.792  1.00 21.68  ? 187 GLU A OE1   1 
ATOM   1507 O  OE2   . GLU A 1 186 ? -9.116  -8.272  21.666  1.00 34.88  ? 187 GLU A OE2   1 
ATOM   1508 N  N     . SER A 1 187 ? -4.888  -5.433  21.444  1.00 10.45  ? 188 SER A N     1 
ATOM   1509 C  CA    . SER A 1 187 ? -4.664  -4.798  22.710  1.00 10.58  ? 188 SER A CA    1 
ATOM   1510 C  C     . SER A 1 187 ? -3.524  -3.783  22.631  1.00 10.68  ? 188 SER A C     1 
ATOM   1511 O  O     . SER A 1 187 ? -2.478  -4.080  22.014  1.00 10.94  ? 188 SER A O     1 
ATOM   1512 C  CB    . SER A 1 187 ? -4.235  -5.876  23.724  1.00 12.54  ? 188 SER A CB    1 
ATOM   1513 O  OG    . SER A 1 187 ? -4.008  -5.339  25.018  1.00 12.04  ? 188 SER A OG    1 
ATOM   1514 N  N     . LEU A 1 188 ? -3.706  -2.744  23.425  1.00 9.35   ? 189 LEU A N     1 
ATOM   1515 C  CA    . LEU A 1 188 ? -2.643  -1.756  23.641  1.00 10.18  ? 189 LEU A CA    1 
ATOM   1516 C  C     . LEU A 1 188 ? -1.983  -1.909  25.002  1.00 9.60   ? 189 LEU A C     1 
ATOM   1517 O  O     . LEU A 1 188 ? -1.321  -1.022  25.461  1.00 10.95  ? 189 LEU A O     1 
ATOM   1518 C  CB    . LEU A 1 188 ? -3.116  -0.306  23.346  1.00 11.94  ? 189 LEU A CB    1 
ATOM   1519 C  CG    . LEU A 1 188 ? -3.561  -0.014  21.963  1.00 12.54  ? 189 LEU A CG    1 
ATOM   1520 C  CD1   . LEU A 1 188 ? -4.123  1.455   21.906  1.00 15.97  ? 189 LEU A CD1   1 
ATOM   1521 C  CD2   . LEU A 1 188 ? -2.414  -0.242  20.957  1.00 14.62  ? 189 LEU A CD2   1 
ATOM   1522 N  N     . ASP A 1 189 ? -2.129  -3.063  25.650  1.00 8.91   ? 190 ASP A N     1 
ATOM   1523 C  CA    . ASP A 1 189 ? -1.349  -3.318  26.877  1.00 9.78   ? 190 ASP A CA    1 
ATOM   1524 C  C     . ASP A 1 189 ? 0.151   -3.207  26.571  1.00 7.95   ? 190 ASP A C     1 
ATOM   1525 O  O     . ASP A 1 189 ? 0.555   -3.741  25.529  1.00 7.95   ? 190 ASP A O     1 
ATOM   1526 C  CB    . ASP A 1 189 ? -1.702  -4.675  27.478  1.00 12.29  ? 190 ASP A CB    1 
ATOM   1527 C  CG    . ASP A 1 189 ? -3.147  -4.779  28.116  1.00 15.26  ? 190 ASP A CG    1 
ATOM   1528 O  OD1   . ASP A 1 189 ? -3.746  -3.781  28.283  1.00 21.28  ? 190 ASP A OD1   1 
ATOM   1529 O  OD2   . ASP A 1 189 ? -3.523  -5.913  28.369  1.00 25.21  ? 190 ASP A OD2   1 
ATOM   1530 N  N     . TYR A 1 190 ? 0.891   -2.641  27.479  1.00 8.06   ? 191 TYR A N     1 
ATOM   1531 C  CA    . TYR A 1 190 ? 2.297   -2.385  27.177  1.00 7.26   ? 191 TYR A CA    1 
ATOM   1532 C  C     . TYR A 1 190 ? 3.155   -2.475  28.404  1.00 7.47   ? 191 TYR A C     1 
ATOM   1533 O  O     . TYR A 1 190 ? 2.730   -2.337  29.554  1.00 7.98   ? 191 TYR A O     1 
ATOM   1534 C  CB    . TYR A 1 190 ? 2.453   -0.988  26.504  1.00 7.93   ? 191 TYR A CB    1 
ATOM   1535 C  CG    . TYR A 1 190 ? 2.044   0.167   27.363  1.00 8.12   ? 191 TYR A CG    1 
ATOM   1536 C  CD1   . TYR A 1 190 ? 2.940   0.767   28.245  1.00 8.19   ? 191 TYR A CD1   1 
ATOM   1537 C  CD2   . TYR A 1 190 ? 0.752   0.677   27.310  1.00 8.91   ? 191 TYR A CD2   1 
ATOM   1538 C  CE1   . TYR A 1 190 ? 2.589   1.813   29.045  1.00 8.86   ? 191 TYR A CE1   1 
ATOM   1539 C  CE2   . TYR A 1 190 ? 0.413   1.745   28.093  1.00 9.47   ? 191 TYR A CE2   1 
ATOM   1540 C  CZ    . TYR A 1 190 ? 1.278   2.288   28.990  1.00 8.31   ? 191 TYR A CZ    1 
ATOM   1541 O  OH    . TYR A 1 190 ? 0.938   3.327   29.810  1.00 9.92   ? 191 TYR A OH    1 
ATOM   1542 N  N     . TRP A 1 191 ? 4.448   -2.587  28.119  1.00 6.66   ? 192 TRP A N     1 
ATOM   1543 C  CA    . TRP A 1 191 ? 5.548   -2.332  29.062  1.00 6.73   ? 192 TRP A CA    1 
ATOM   1544 C  C     . TRP A 1 191 ? 6.235   -1.050  28.626  1.00 6.51   ? 192 TRP A C     1 
ATOM   1545 O  O     . TRP A 1 191 ? 6.299   -0.712  27.444  1.00 7.19   ? 192 TRP A O     1 
ATOM   1546 C  CB    . TRP A 1 191 ? 6.573   -3.461  29.011  1.00 7.13   ? 192 TRP A CB    1 
ATOM   1547 C  CG    . TRP A 1 191 ? 6.038   -4.779  29.450  1.00 7.33   ? 192 TRP A CG    1 
ATOM   1548 C  CD1   . TRP A 1 191 ? 5.809   -5.226  30.735  1.00 8.20   ? 192 TRP A CD1   1 
ATOM   1549 C  CD2   . TRP A 1 191 ? 5.758   -5.911  28.626  1.00 6.68   ? 192 TRP A CD2   1 
ATOM   1550 N  NE1   . TRP A 1 191 ? 5.409   -6.519  30.715  1.00 10.10  ? 192 TRP A NE1   1 
ATOM   1551 C  CE2   . TRP A 1 191 ? 5.339   -6.966  29.421  1.00 8.37   ? 192 TRP A CE2   1 
ATOM   1552 C  CE3   . TRP A 1 191 ? 5.850   -6.141  27.246  1.00 7.38   ? 192 TRP A CE3   1 
ATOM   1553 C  CZ2   . TRP A 1 191 ? 5.068   -8.226  28.915  1.00 10.17  ? 192 TRP A CZ2   1 
ATOM   1554 C  CZ3   . TRP A 1 191 ? 5.594   -7.370  26.753  1.00 9.27   ? 192 TRP A CZ3   1 
ATOM   1555 C  CH2   . TRP A 1 191 ? 5.222   -8.404  27.601  1.00 10.05  ? 192 TRP A CH2   1 
ATOM   1556 N  N     . THR A 1 192 ? 6.774   -0.329  29.611  1.00 5.90   ? 193 THR A N     1 
ATOM   1557 C  CA    . THR A 1 192 ? 7.495   0.892   29.291  1.00 5.75   ? 193 THR A CA    1 
ATOM   1558 C  C     . THR A 1 192 ? 8.741   1.038   30.138  1.00 6.02   ? 193 THR A C     1 
ATOM   1559 O  O     . THR A 1 192 ? 8.765   0.639   31.314  1.00 7.09   ? 193 THR A O     1 
ATOM   1560 C  CB    . THR A 1 192 ? 6.575   2.077   29.392  1.00 6.20   ? 193 THR A CB    1 
ATOM   1561 O  OG1   . THR A 1 192 ? 7.255   3.305   29.036  1.00 6.59   ? 193 THR A OG1   1 
ATOM   1562 C  CG2   . THR A 1 192 ? 6.024   2.320   30.808  1.00 7.32   ? 193 THR A CG2   1 
ATOM   1563 N  N     . TYR A 1 193 ? 9.777   1.645   29.569  1.00 5.51   ? 194 TYR A N     1 
ATOM   1564 C  CA    . TYR A 1 193 ? 10.985  1.904   30.263  1.00 5.83   ? 194 TYR A CA    1 
ATOM   1565 C  C     . TYR A 1 193 ? 11.759  2.973   29.480  1.00 5.80   ? 194 TYR A C     1 
ATOM   1566 O  O     . TYR A 1 193 ? 11.531  3.180   28.300  1.00 6.19   ? 194 TYR A O     1 
ATOM   1567 C  CB    . TYR A 1 193 ? 11.855  0.652   30.430  1.00 6.29   ? 194 TYR A CB    1 
ATOM   1568 C  CG    . TYR A 1 193 ? 12.519  0.167   29.209  1.00 6.20   ? 194 TYR A CG    1 
ATOM   1569 C  CD1   . TYR A 1 193 ? 11.853  -0.532  28.217  1.00 6.10   ? 194 TYR A CD1   1 
ATOM   1570 C  CD2   . TYR A 1 193 ? 13.844  0.493   28.958  1.00 6.04   ? 194 TYR A CD2   1 
ATOM   1571 C  CE1   . TYR A 1 193 ? 12.496  -0.863  26.990  1.00 6.06   ? 194 TYR A CE1   1 
ATOM   1572 C  CE2   . TYR A 1 193 ? 14.442  0.176   27.787  1.00 6.31   ? 194 TYR A CE2   1 
ATOM   1573 C  CZ    . TYR A 1 193 ? 13.817  -0.489  26.792  1.00 5.99   ? 194 TYR A CZ    1 
ATOM   1574 O  OH    . TYR A 1 193 ? 14.453  -0.782  25.624  1.00 6.14   ? 194 TYR A OH    1 
ATOM   1575 N  N     . PRO A 1 194 ? 12.745  3.642   30.144  1.00 5.80   ? 195 PRO A N     1 
ATOM   1576 C  CA    . PRO A 1 194 ? 13.552  4.649   29.451  1.00 5.49   ? 195 PRO A CA    1 
ATOM   1577 C  C     . PRO A 1 194 ? 14.733  4.040   28.769  1.00 5.76   ? 195 PRO A C     1 
ATOM   1578 O  O     . PRO A 1 194 ? 15.462  3.244   29.412  1.00 6.32   ? 195 PRO A O     1 
ATOM   1579 C  CB    . PRO A 1 194 ? 14.007  5.560   30.601  1.00 6.77   ? 195 PRO A CB    1 
ATOM   1580 C  CG    . PRO A 1 194 ? 14.051  4.652   31.815  1.00 8.50   ? 195 PRO A CG    1 
ATOM   1581 C  CD    . PRO A 1 194 ? 12.943  3.676   31.607  1.00 7.54   ? 195 PRO A CD    1 
ATOM   1582 N  N     . GLY A 1 195 ? 14.980  4.361   27.512  1.00 5.41   ? 196 GLY A N     1 
ATOM   1583 C  CA    . GLY A 1 195 ? 16.108  3.740   26.807  1.00 5.80   ? 196 GLY A CA    1 
ATOM   1584 C  C     . GLY A 1 195 ? 16.596  4.633   25.679  1.00 5.41   ? 196 GLY A C     1 
ATOM   1585 O  O     . GLY A 1 195 ? 16.665  5.842   25.786  1.00 5.76   ? 196 GLY A O     1 
ATOM   1586 N  N     . SER A 1 196 ? 17.025  3.913   24.623  1.00 5.55   ? 197 SER A N     1 
ATOM   1587 C  CA    . SER A 1 196 ? 17.807  4.535   23.588  1.00 5.91   ? 197 SER A CA    1 
ATOM   1588 C  C     . SER A 1 196 ? 17.332  4.156   22.202  1.00 5.74   ? 197 SER A C     1 
ATOM   1589 O  O     . SER A 1 196 ? 16.611  3.201   22.003  1.00 5.91   ? 197 SER A O     1 
ATOM   1590 C  CB    . SER A 1 196 ? 19.289  4.133   23.738  1.00 5.80   ? 197 SER A CB    1 
ATOM   1591 O  OG    . SER A 1 196 ? 19.509  2.828   23.296  1.00 5.98   ? 197 SER A OG    1 
ATOM   1592 N  N     . LEU A 1 197 ? 17.873  4.860   21.192  1.00 5.67   ? 198 LEU A N     1 
ATOM   1593 C  CA    . LEU A 1 197 ? 17.845  4.346   19.850  1.00 6.28   ? 198 LEU A CA    1 
ATOM   1594 C  C     . LEU A 1 197 ? 18.572  3.002   19.845  1.00 5.36   ? 198 LEU A C     1 
ATOM   1595 O  O     . LEU A 1 197 ? 19.590  2.853   20.551  1.00 6.20   ? 198 LEU A O     1 
ATOM   1596 C  CB    . LEU A 1 197 ? 18.595  5.294   18.904  1.00 7.66   ? 198 LEU A CB    1 
ATOM   1597 C  CG    . LEU A 1 197 ? 18.219  6.735   18.869  1.00 9.60   ? 198 LEU A CG    1 
ATOM   1598 C  CD1   . LEU A 1 197 ? 18.990  7.510   17.848  1.00 11.89  ? 198 LEU A CD1   1 
ATOM   1599 C  CD2   . LEU A 1 197 ? 16.731  6.888   18.619  1.00 13.02  ? 198 LEU A CD2   1 
ATOM   1600 N  N     . THR A 1 198 ? 18.175  2.088   18.981  1.00 5.43   ? 199 THR A N     1 
ATOM   1601 C  CA    . THR A 1 198 ? 18.849  0.788   18.892  1.00 6.23   ? 199 THR A CA    1 
ATOM   1602 C  C     . THR A 1 198 ? 19.813  0.681   17.764  1.00 6.56   ? 199 THR A C     1 
ATOM   1603 O  O     . THR A 1 198 ? 20.425  -0.376  17.613  1.00 6.95   ? 199 THR A O     1 
ATOM   1604 C  CB    . THR A 1 198 ? 17.861  -0.374  18.890  1.00 6.00   ? 199 THR A CB    1 
ATOM   1605 O  OG1   . THR A 1 198 ? 17.189  -0.396  17.635  1.00 6.66   ? 199 THR A OG1   1 
ATOM   1606 C  CG2   . THR A 1 198 ? 16.926  -0.380  20.051  1.00 6.37   ? 199 THR A CG2   1 
ATOM   1607 N  N     . THR A 1 199 ? 19.964  1.760   16.973  1.00 6.34   ? 200 THR A N     1 
ATOM   1608 C  CA    . THR A 1 199 ? 21.009  1.850   15.973  1.00 6.68   ? 200 THR A CA    1 
ATOM   1609 C  C     . THR A 1 199 ? 21.819  3.070   16.290  1.00 6.18   ? 200 THR A C     1 
ATOM   1610 O  O     . THR A 1 199 ? 21.341  4.037   16.914  1.00 7.02   ? 200 THR A O     1 
ATOM   1611 C  CB    . THR A 1 199 ? 20.427  1.979   14.565  1.00 7.62   ? 200 THR A CB    1 
ATOM   1612 O  OG1   . THR A 1 199 ? 19.440  3.055   14.586  1.00 9.72   ? 200 THR A OG1   1 
ATOM   1613 C  CG2   . THR A 1 199 ? 19.785  0.764   14.139  1.00 8.92   ? 200 THR A CG2   1 
ATOM   1614 N  N     . PRO A 1 200 ? 23.085  3.106   15.860  1.00 7.50   ? 201 PRO A N     1 
ATOM   1615 C  CA    . PRO A 1 200 ? 23.871  4.318   15.988  1.00 7.84   ? 201 PRO A CA    1 
ATOM   1616 C  C     . PRO A 1 200 ? 23.098  5.573   15.452  1.00 8.56   ? 201 PRO A C     1 
ATOM   1617 O  O     . PRO A 1 200 ? 22.448  5.443   14.416  1.00 9.74   ? 201 PRO A O     1 
ATOM   1618 C  CB    . PRO A 1 200 ? 25.108  4.011   15.128  1.00 9.85   ? 201 PRO A CB    1 
ATOM   1619 C  CG    . PRO A 1 200 ? 25.271  2.510   15.363  1.00 8.93   ? 201 PRO A CG    1 
ATOM   1620 C  CD    . PRO A 1 200 ? 23.877  1.993   15.272  1.00 7.95   ? 201 PRO A CD    1 
ATOM   1621 N  N     . PRO A 1 201 ? 23.123  6.663   16.198  1.00 8.32   ? 202 PRO A N     1 
ATOM   1622 C  CA    . PRO A 1 201 ? 24.053  6.993   17.256  1.00 8.26   ? 202 PRO A CA    1 
ATOM   1623 C  C     . PRO A 1 201 ? 23.672  6.542   18.666  1.00 7.46   ? 202 PRO A C     1 
ATOM   1624 O  O     . PRO A 1 201 ? 24.311  6.955   19.616  1.00 8.38   ? 202 PRO A O     1 
ATOM   1625 C  CB    . PRO A 1 201 ? 24.129  8.508   17.150  1.00 11.05  ? 202 PRO A CB    1 
ATOM   1626 C  CG    . PRO A 1 201 ? 22.739  8.947   16.628  1.00 12.38  ? 202 PRO A CG    1 
ATOM   1627 C  CD    . PRO A 1 201 ? 22.400  7.842   15.647  1.00 11.21  ? 202 PRO A CD    1 
ATOM   1628 N  N     . LEU A 1 202 ? 22.629  5.716   18.821  1.00 6.99   ? 203 LEU A N     1 
ATOM   1629 C  CA    . LEU A 1 202 ? 22.351  5.060   20.116  1.00 6.45   ? 203 LEU A CA    1 
ATOM   1630 C  C     . LEU A 1 202 ? 22.001  6.045   21.226  1.00 6.57   ? 203 LEU A C     1 
ATOM   1631 O  O     . LEU A 1 202 ? 22.185  5.790   22.395  1.00 6.92   ? 203 LEU A O     1 
ATOM   1632 C  CB    . LEU A 1 202 ? 23.512  4.151   20.573  1.00 7.04   ? 203 LEU A CB    1 
ATOM   1633 C  CG    . LEU A 1 202 ? 23.819  3.002   19.612  1.00 6.72   ? 203 LEU A CG    1 
ATOM   1634 C  CD1   . LEU A 1 202 ? 25.105  2.346   20.024  1.00 9.59   ? 203 LEU A CD1   1 
ATOM   1635 C  CD2   . LEU A 1 202 ? 22.750  2.005   19.435  1.00 7.74   ? 203 LEU A CD2   1 
ATOM   1636 N  N     . LEU A 1 203 ? 21.432  7.184   20.824  1.00 7.04   ? 204 LEU A N     1 
ATOM   1637 C  CA    . LEU A 1 203 ? 21.155  8.258   21.749  1.00 7.20   ? 204 LEU A CA    1 
ATOM   1638 C  C     . LEU A 1 203 ? 20.097  7.863   22.772  1.00 6.61   ? 204 LEU A C     1 
ATOM   1639 O  O     . LEU A 1 203 ? 19.126  7.180   22.452  1.00 7.22   ? 204 LEU A O     1 
ATOM   1640 C  CB    . LEU A 1 203 ? 20.716  9.517   20.997  1.00 9.05   ? 204 LEU A CB    1 
ATOM   1641 C  CG    . LEU A 1 203 ? 21.792  10.100  20.108  1.00 10.26  ? 204 LEU A CG    1 
ATOM   1642 C  CD1   . LEU A 1 203 ? 21.240  11.211  19.213  1.00 13.19  ? 204 LEU A CD1   1 
ATOM   1643 C  CD2   . LEU A 1 203 ? 22.958  10.658  20.912  1.00 14.72  ? 204 LEU A CD2   1 
ATOM   1644 N  N     . GLU A 1 204 ? 20.303  8.323   24.002  1.00 7.43   ? 205 GLU A N     1 
ATOM   1645 C  CA    . GLU A 1 204 ? 19.496  7.906   25.134  1.00 7.40   ? 205 GLU A CA    1 
ATOM   1646 C  C     . GLU A 1 204 ? 18.320  8.907   25.298  1.00 6.76   ? 205 GLU A C     1 
ATOM   1647 O  O     . GLU A 1 204 ? 18.249  9.706   26.211  1.00 8.50   ? 205 GLU A O     1 
ATOM   1648 C  CB    . GLU A 1 204 ? 20.352  7.765   26.376  1.00 8.35   ? 205 GLU A CB    1 
ATOM   1649 C  CG    . GLU A 1 204 ? 21.274  6.573   26.222  1.00 8.06   ? 205 GLU A CG    1 
ATOM   1650 C  CD    . GLU A 1 204 ? 22.157  6.282   27.379  1.00 8.82   ? 205 GLU A CD    1 
ATOM   1651 O  OE1   . GLU A 1 204 ? 22.462  7.213   28.181  1.00 11.20  ? 205 GLU A OE1   1 
ATOM   1652 O  OE2   . GLU A 1 204 ? 22.601  5.105   27.513  1.00 8.80   ? 205 GLU A OE2   1 
ATOM   1653 N  N     . CYS A 1 205 ? 17.421  8.836   24.320  1.00 6.43   ? 206 CYS A N     1 
ATOM   1654 C  CA    . CYS A 1 205 ? 16.355  9.826   24.110  1.00 6.50   ? 206 CYS A CA    1 
ATOM   1655 C  C     . CYS A 1 205 ? 14.982  9.240   23.989  1.00 5.82   ? 206 CYS A C     1 
ATOM   1656 O  O     . CYS A 1 205 ? 14.063  9.950   23.603  1.00 7.30   ? 206 CYS A O     1 
ATOM   1657 C  CB    . CYS A 1 205 ? 16.682  10.695  22.904  1.00 7.48   ? 206 CYS A CB    1 
ATOM   1658 S  SG    . CYS A 1 205 ? 16.683  9.717   21.347  1.00 7.88   ? 206 CYS A SG    1 
ATOM   1659 N  N     . VAL A 1 206 ? 14.830  7.947   24.322  1.00 6.07   ? 207 VAL A N     1 
ATOM   1660 C  CA    . VAL A 1 206 ? 13.588  7.237   23.984  1.00 5.67   ? 207 VAL A CA    1 
ATOM   1661 C  C     . VAL A 1 206 ? 12.829  6.812   25.241  1.00 5.78   ? 207 VAL A C     1 
ATOM   1662 O  O     . VAL A 1 206 ? 13.370  6.164   26.101  1.00 6.72   ? 207 VAL A O     1 
ATOM   1663 C  CB    . VAL A 1 206 ? 13.903  5.993   23.148  1.00 6.61   ? 207 VAL A CB    1 
ATOM   1664 C  CG1   . VAL A 1 206 ? 12.570  5.276   22.800  1.00 6.90   ? 207 VAL A CG1   1 
ATOM   1665 C  CG2   . VAL A 1 206 ? 14.657  6.361   21.876  1.00 7.01   ? 207 VAL A CG2   1 
ATOM   1666 N  N     . THR A 1 207 ? 11.514  7.132   25.258  1.00 5.43   ? 208 THR A N     1 
ATOM   1667 C  CA    . THR A 1 207 ? 10.593  6.377   26.134  1.00 5.63   ? 208 THR A CA    1 
ATOM   1668 C  C     . THR A 1 207 ? 10.098  5.214   25.262  1.00 5.49   ? 208 THR A C     1 
ATOM   1669 O  O     . THR A 1 207 ? 9.392   5.402   24.257  1.00 5.93   ? 208 THR A O     1 
ATOM   1670 C  CB    . THR A 1 207 ? 9.434   7.237   26.549  1.00 6.34   ? 208 THR A CB    1 
ATOM   1671 O  OG1   . THR A 1 207 ? 9.933   8.376   27.272  1.00 6.89   ? 208 THR A OG1   1 
ATOM   1672 C  CG2   . THR A 1 207 ? 8.511   6.451   27.451  1.00 7.68   ? 208 THR A CG2   1 
ATOM   1673 N  N     . TRP A 1 208 ? 10.445  3.998   25.667  1.00 5.06   ? 209 TRP A N     1 
ATOM   1674 C  CA    . TRP A 1 208 ? 9.994   2.809   24.975  1.00 4.86   ? 209 TRP A CA    1 
ATOM   1675 C  C     . TRP A 1 208 ? 8.636   2.396   25.475  1.00 5.14   ? 209 TRP A C     1 
ATOM   1676 O  O     . TRP A 1 208 ? 8.389   2.351   26.697  1.00 6.22   ? 209 TRP A O     1 
ATOM   1677 C  CB    . TRP A 1 208 ? 10.970  1.656   25.181  1.00 5.50   ? 209 TRP A CB    1 
ATOM   1678 C  CG    . TRP A 1 208 ? 12.127  1.756   24.197  1.00 4.99   ? 209 TRP A CG    1 
ATOM   1679 C  CD1   . TRP A 1 208 ? 13.352  2.336   24.418  1.00 6.48   ? 209 TRP A CD1   1 
ATOM   1680 C  CD2   . TRP A 1 208 ? 12.079  1.336   22.861  1.00 5.29   ? 209 TRP A CD2   1 
ATOM   1681 N  NE1   . TRP A 1 208 ? 14.071  2.309   23.256  1.00 6.79   ? 209 TRP A NE1   1 
ATOM   1682 C  CE2   . TRP A 1 208 ? 13.328  1.671   22.293  1.00 5.89   ? 209 TRP A CE2   1 
ATOM   1683 C  CE3   . TRP A 1 208 ? 11.128  0.685   22.076  1.00 5.48   ? 209 TRP A CE3   1 
ATOM   1684 C  CZ2   . TRP A 1 208 ? 13.613  1.431   20.969  1.00 7.12   ? 209 TRP A CZ2   1 
ATOM   1685 C  CZ3   . TRP A 1 208 ? 11.426  0.400   20.792  1.00 6.53   ? 209 TRP A CZ3   1 
ATOM   1686 C  CH2   . TRP A 1 208 ? 12.672  0.749   20.243  1.00 6.68   ? 209 TRP A CH2   1 
ATOM   1687 N  N     . ILE A 1 209 ? 7.793   2.000   24.535  1.00 4.77   ? 210 ILE A N     1 
ATOM   1688 C  CA    . ILE A 1 209 ? 6.454   1.472   24.828  1.00 5.27   ? 210 ILE A CA    1 
ATOM   1689 C  C     . ILE A 1 209 ? 6.361   0.197   23.977  1.00 5.47   ? 210 ILE A C     1 
ATOM   1690 O  O     . ILE A 1 209 ? 6.278   0.301   22.766  1.00 6.80   ? 210 ILE A O     1 
ATOM   1691 C  CB    . ILE A 1 209 ? 5.386   2.485   24.438  1.00 6.51   ? 210 ILE A CB    1 
ATOM   1692 C  CG1   . ILE A 1 209 ? 5.572   3.764   25.222  1.00 7.69   ? 210 ILE A CG1   1 
ATOM   1693 C  CG2   . ILE A 1 209 ? 4.002   1.915   24.656  1.00 6.94   ? 210 ILE A CG2   1 
ATOM   1694 C  CD1   . ILE A 1 209 ? 4.795   4.935   24.704  1.00 9.79   ? 210 ILE A CD1   1 
ATOM   1695 N  N     . VAL A 1 210 ? 6.437   -0.946  24.631  1.00 5.22   ? 211 VAL A N     1 
ATOM   1696 C  CA    . VAL A 1 210 ? 6.486   -2.239  23.949  1.00 5.13   ? 211 VAL A CA    1 
ATOM   1697 C  C     . VAL A 1 210 ? 5.161   -2.944  24.213  1.00 5.77   ? 211 VAL A C     1 
ATOM   1698 O  O     . VAL A 1 210 ? 4.837   -3.213  25.331  1.00 6.73   ? 211 VAL A O     1 
ATOM   1699 C  CB    . VAL A 1 210 ? 7.681   -3.058  24.381  1.00 5.77   ? 211 VAL A CB    1 
ATOM   1700 C  CG1   . VAL A 1 210 ? 7.665   -4.426  23.705  1.00 7.01   ? 211 VAL A CG1   1 
ATOM   1701 C  CG2   . VAL A 1 210 ? 8.947   -2.285  24.145  1.00 7.27   ? 211 VAL A CG2   1 
ATOM   1702 N  N     . LEU A 1 211 ? 4.428   -3.200  23.137  1.00 6.19   ? 212 LEU A N     1 
ATOM   1703 C  CA    . LEU A 1 211 ? 3.155   -3.848  23.285  1.00 6.57   ? 212 LEU A CA    1 
ATOM   1704 C  C     . LEU A 1 211 ? 3.305   -5.340  23.683  1.00 6.67   ? 212 LEU A C     1 
ATOM   1705 O  O     . LEU A 1 211 ? 4.167   -6.043  23.105  1.00 7.52   ? 212 LEU A O     1 
ATOM   1706 C  CB    . LEU A 1 211 ? 2.314   -3.738  22.028  1.00 6.86   ? 212 LEU A CB    1 
ATOM   1707 C  CG    . LEU A 1 211 ? 1.932   -2.335  21.622  1.00 7.84   ? 212 LEU A CG    1 
ATOM   1708 C  CD1   . LEU A 1 211 ? 0.918   -2.362  20.470  1.00 9.20   ? 212 LEU A CD1   1 
ATOM   1709 C  CD2   . LEU A 1 211 ? 1.399   -1.489  22.741  1.00 8.92   ? 212 LEU A CD2   1 
ATOM   1710 N  N     . LYS A 1 212 ? 2.459   -5.835  24.561  1.00 6.87   ? 213 LYS A N     1 
ATOM   1711 C  CA    . LYS A 1 212 ? 2.470   -7.209  24.924  1.00 8.65   ? 213 LYS A CA    1 
ATOM   1712 C  C     . LYS A 1 212 ? 2.018   -8.142  23.860  1.00 7.92   ? 213 LYS A C     1 
ATOM   1713 O  O     . LYS A 1 212 ? 2.509   -9.249  23.739  1.00 9.64   ? 213 LYS A O     1 
ATOM   1714 C  CB    . LYS A 1 212 ? 1.721   -7.436  26.201  1.00 10.82  ? 213 LYS A CB    1 
ATOM   1715 C  CG    . LYS A 1 212 ? 1.530   -8.851  26.625  1.00 13.79  ? 213 LYS A CG    1 
ATOM   1716 C  CD    . LYS A 1 212 ? 0.750   -8.980  27.879  1.00 19.63  ? 213 LYS A CD    1 
ATOM   1717 C  CE    . LYS A 1 212 ? -0.760  -8.412  27.625  1.00 32.16  ? 213 LYS A CE    1 
ATOM   1718 N  NZ    . LYS A 1 212 ? -1.577  -8.286  26.232  1.00 39.46  ? 213 LYS A NZ    1 
ATOM   1719 N  N     A GLU A 1 213 ? 0.999   -7.755  23.103  0.50 7.50   ? 214 GLU A N     1 
ATOM   1720 N  N     B GLU A 1 213 ? 1.028   -7.735  23.069  0.50 7.50   ? 214 GLU A N     1 
ATOM   1721 C  CA    A GLU A 1 213 ? 0.391   -8.647  22.138  0.50 7.80   ? 214 GLU A CA    1 
ATOM   1722 C  CA    B GLU A 1 213 ? 0.407   -8.611  22.083  0.50 7.71   ? 214 GLU A CA    1 
ATOM   1723 C  C     A GLU A 1 213 ? 1.120   -8.531  20.812  0.50 6.96   ? 214 GLU A C     1 
ATOM   1724 C  C     B GLU A 1 213 ? 1.147   -8.514  20.772  0.50 7.12   ? 214 GLU A C     1 
ATOM   1725 O  O     A GLU A 1 213 ? 1.183   -7.443  20.246  0.50 7.43   ? 214 GLU A O     1 
ATOM   1726 O  O     B GLU A 1 213 ? 1.251   -7.433  20.172  0.50 7.83   ? 214 GLU A O     1 
ATOM   1727 C  CB    A GLU A 1 213 ? -1.073  -8.344  21.984  0.50 9.62   ? 214 GLU A CB    1 
ATOM   1728 C  CB    B GLU A 1 213 ? -1.038  -8.251  21.902  0.50 9.30   ? 214 GLU A CB    1 
ATOM   1729 C  CG    A GLU A 1 213 ? -1.700  -9.311  21.000  0.50 10.72  ? 214 GLU A CG    1 
ATOM   1730 C  CG    B GLU A 1 213 ? -1.774  -9.114  20.869  0.50 10.02  ? 214 GLU A CG    1 
ATOM   1731 C  CD    A GLU A 1 213 ? -3.203  -9.199  20.783  0.50 13.57  ? 214 GLU A CD    1 
ATOM   1732 C  CD    B GLU A 1 213 ? -3.221  -8.656  20.606  0.50 11.05  ? 214 GLU A CD    1 
ATOM   1733 O  OE1   A GLU A 1 213 ? -3.841  -8.195  21.078  0.50 14.08  ? 214 GLU A OE1   1 
ATOM   1734 O  OE1   B GLU A 1 213 ? -3.847  -8.184  21.584  0.50 12.52  ? 214 GLU A OE1   1 
ATOM   1735 O  OE2   A GLU A 1 213 ? -3.708  -10.166 20.183  0.50 17.21  ? 214 GLU A OE2   1 
ATOM   1736 O  OE2   B GLU A 1 213 ? -3.716  -8.818  19.440  0.50 14.38  ? 214 GLU A OE2   1 
ATOM   1737 N  N     . PRO A 1 214 ? 1.718   -9.623  20.293  1.00 7.50   ? 215 PRO A N     1 
ATOM   1738 C  CA    . PRO A 1 214 ? 2.332   -9.612  18.982  1.00 8.02   ? 215 PRO A CA    1 
ATOM   1739 C  C     . PRO A 1 214 ? 1.291   -9.573  17.886  1.00 8.85   ? 215 PRO A C     1 
ATOM   1740 O  O     . PRO A 1 214 ? 0.140   -9.969  18.099  1.00 10.73  ? 215 PRO A O     1 
ATOM   1741 C  CB    . PRO A 1 214 ? 3.077   -10.913 18.902  1.00 8.86   ? 215 PRO A CB    1 
ATOM   1742 C  CG    . PRO A 1 214 ? 2.330   -11.842 19.752  1.00 14.74  ? 215 PRO A CG    1 
ATOM   1743 C  CD    . PRO A 1 214 ? 1.758   -10.973 20.888  1.00 9.93   ? 215 PRO A CD    1 
ATOM   1744 N  N     . ILE A 1 215 ? 1.707   -9.115  16.712  1.00 8.24   ? 216 ILE A N     1 
ATOM   1745 C  CA    . ILE A 1 215 ? 0.973   -9.360  15.518  1.00 8.96   ? 216 ILE A CA    1 
ATOM   1746 C  C     . ILE A 1 215 ? 1.448   -10.613 14.842  1.00 8.45   ? 216 ILE A C     1 
ATOM   1747 O  O     . ILE A 1 215 ? 2.655   -10.959 15.003  1.00 9.53   ? 216 ILE A O     1 
ATOM   1748 C  CB    . ILE A 1 215 ? 0.908   -8.156  14.551  1.00 9.86   ? 216 ILE A CB    1 
ATOM   1749 C  CG1   . ILE A 1 215 ? 2.303   -7.795  14.050  1.00 10.86  ? 216 ILE A CG1   1 
ATOM   1750 C  CG2   . ILE A 1 215 ? 0.197   -6.978  15.181  1.00 10.72  ? 216 ILE A CG2   1 
ATOM   1751 C  CD1   . ILE A 1 215 ? 2.316   -6.797  12.840  1.00 11.90  ? 216 ILE A CD1   1 
ATOM   1752 N  N     . SER A 1 216 ? 0.606   -11.243 14.056  1.00 8.95   ? 217 SER A N     1 
ATOM   1753 C  CA    A SER A 1 216 ? 0.971   -12.384 13.258  0.50 8.45   ? 217 SER A CA    1 
ATOM   1754 C  CA    C SER A 1 216 ? 1.066   -12.373 13.255  0.50 10.14  ? 217 SER A CA    1 
ATOM   1755 C  C     . SER A 1 216 ? 1.200   -11.979 11.835  1.00 9.37   ? 217 SER A C     1 
ATOM   1756 O  O     . SER A 1 216 ? 0.362   -11.240 11.291  1.00 10.66  ? 217 SER A O     1 
ATOM   1757 C  CB    A SER A 1 216 ? -0.176  -13.365 13.340  0.50 6.86   ? 217 SER A CB    1 
ATOM   1758 C  CB    C SER A 1 216 ? 0.222   -13.618 13.420  0.50 15.82  ? 217 SER A CB    1 
ATOM   1759 O  OG    A SER A 1 216 ? -0.138  -14.087 14.545  0.50 10.08  ? 217 SER A OG    1 
ATOM   1760 O  OG    C SER A 1 216 ? -1.108  -13.395 13.031  0.50 24.47  ? 217 SER A OG    1 
ATOM   1761 N  N     . VAL A 1 217 ? 2.274   -12.413 11.242  1.00 9.46   ? 218 VAL A N     1 
ATOM   1762 C  CA    . VAL A 1 217 ? 2.512   -12.252 9.804   1.00 9.80   ? 218 VAL A CA    1 
ATOM   1763 C  C     . VAL A 1 217 ? 2.781   -13.591 9.214   1.00 9.36   ? 218 VAL A C     1 
ATOM   1764 O  O     . VAL A 1 217 ? 3.124   -14.553 9.935   1.00 9.70   ? 218 VAL A O     1 
ATOM   1765 C  CB    . VAL A 1 217 ? 3.703   -11.303 9.594   1.00 10.14  ? 218 VAL A CB    1 
ATOM   1766 C  CG1   . VAL A 1 217 ? 3.429   -9.975  10.237  1.00 10.73  ? 218 VAL A CG1   1 
ATOM   1767 C  CG2   . VAL A 1 217 ? 5.031   -11.878 10.062  1.00 11.22  ? 218 VAL A CG2   1 
ATOM   1768 N  N     . SER A 1 218 ? 2.647   -13.770 7.896   1.00 9.74   ? 219 SER A N     1 
ATOM   1769 C  CA    . SER A 1 218 ? 2.874   -15.072 7.383   1.00 10.53  ? 219 SER A CA    1 
ATOM   1770 C  C     . SER A 1 218 ? 4.347   -15.310 7.060   1.00 10.60  ? 219 SER A C     1 
ATOM   1771 O  O     . SER A 1 218 ? 5.141   -14.383 6.900   1.00 10.35  ? 219 SER A O     1 
ATOM   1772 C  CB    . SER A 1 218 ? 2.074   -15.292 6.052   1.00 10.25  ? 219 SER A CB    1 
ATOM   1773 O  OG    . SER A 1 218 ? 2.491   -14.424 5.089   1.00 11.70  ? 219 SER A OG    1 
ATOM   1774 N  N     . SER A 1 219 ? 4.670   -16.578 6.915   1.00 9.60   ? 220 SER A N     1 
ATOM   1775 C  CA    A SER A 1 219 ? 6.058   -16.942 6.567   0.50 11.79  ? 220 SER A CA    1 
ATOM   1776 C  CA    B SER A 1 219 ? 6.043   -16.968 6.558   0.50 11.13  ? 220 SER A CA    1 
ATOM   1777 C  C     . SER A 1 219 ? 6.426   -16.269 5.254   1.00 12.16  ? 220 SER A C     1 
ATOM   1778 O  O     . SER A 1 219 ? 7.533   -15.826 5.110   1.00 13.27  ? 220 SER A O     1 
ATOM   1779 C  CB    A SER A 1 219 ? 6.193   -18.438 6.546   0.50 12.98  ? 220 SER A CB    1 
ATOM   1780 C  CB    B SER A 1 219 ? 6.089   -18.483 6.511   0.50 11.58  ? 220 SER A CB    1 
ATOM   1781 O  OG    A SER A 1 219 ? 7.532   -18.841 6.377   0.50 11.18  ? 220 SER A OG    1 
ATOM   1782 O  OG    B SER A 1 219 ? 5.281   -19.021 5.433   0.50 14.83  ? 220 SER A OG    1 
ATOM   1783 N  N     . GLU A 1 220 ? 5.466   -16.249 4.305   1.00 11.35  ? 221 GLU A N     1 
ATOM   1784 C  CA    . GLU A 1 220 ? 5.686   -15.605 3.026   1.00 13.07  ? 221 GLU A CA    1 
ATOM   1785 C  C     . GLU A 1 220 ? 6.040   -14.132 3.162   1.00 12.16  ? 221 GLU A C     1 
ATOM   1786 O  O     . GLU A 1 220 ? 6.875   -13.590 2.416   1.00 13.87  ? 221 GLU A O     1 
ATOM   1787 C  CB    . GLU A 1 220 ? 4.549   -15.811 2.080   1.00 14.64  ? 221 GLU A CB    1 
ATOM   1788 C  CG    . GLU A 1 220 ? 4.388   -17.309 1.680   1.00 19.43  ? 221 GLU A CG    1 
ATOM   1789 C  CD    . GLU A 1 220 ? 3.509   -18.116 2.628   1.00 23.90  ? 221 GLU A CD    1 
ATOM   1790 O  OE1   . GLU A 1 220 ? 3.074   -17.655 3.705   1.00 25.72  ? 221 GLU A OE1   1 
ATOM   1791 O  OE2   . GLU A 1 220 ? 3.226   -19.244 2.326   1.00 30.61  ? 221 GLU A OE2   1 
ATOM   1792 N  N     . GLN A 1 221 ? 5.325   -13.443 4.047   1.00 10.44  ? 222 GLN A N     1 
ATOM   1793 C  CA    . GLN A 1 221 ? 5.622   -12.035 4.281   1.00 10.43  ? 222 GLN A CA    1 
ATOM   1794 C  C     . GLN A 1 221 ? 7.044   -11.829 4.817   1.00 10.12  ? 222 GLN A C     1 
ATOM   1795 O  O     . GLN A 1 221 ? 7.756   -10.991 4.301   1.00 11.27  ? 222 GLN A O     1 
ATOM   1796 C  CB    . GLN A 1 221 ? 4.518   -11.462 5.177   1.00 10.01  ? 222 GLN A CB    1 
ATOM   1797 C  CG    . GLN A 1 221 ? 3.172   -11.331 4.485   1.00 9.97   ? 222 GLN A CG    1 
ATOM   1798 C  CD    . GLN A 1 221 ? 2.078   -10.801 5.370   1.00 11.29  ? 222 GLN A CD    1 
ATOM   1799 O  OE1   . GLN A 1 221 ? 1.932   -11.147 6.552   1.00 10.35  ? 222 GLN A OE1   1 
ATOM   1800 N  NE2   . GLN A 1 221 ? 1.286   -9.974  4.784   1.00 11.53  ? 222 GLN A NE2   1 
ATOM   1801 N  N     . VAL A 1 222 ? 7.398   -12.551 5.844   1.00 10.95  ? 223 VAL A N     1 
ATOM   1802 C  CA    A VAL A 1 222 ? 8.743   -12.385 6.390   0.50 10.96  ? 223 VAL A CA    1 
ATOM   1803 C  CA    B VAL A 1 222 ? 8.743   -12.334 6.402   0.50 10.04  ? 223 VAL A CA    1 
ATOM   1804 C  C     . VAL A 1 222 ? 9.833   -12.824 5.440   1.00 11.57  ? 223 VAL A C     1 
ATOM   1805 O  O     . VAL A 1 222 ? 10.909  -12.239 5.383   1.00 12.03  ? 223 VAL A O     1 
ATOM   1806 C  CB    A VAL A 1 222 ? 8.927   -13.161 7.686   0.50 15.80  ? 223 VAL A CB    1 
ATOM   1807 C  CB    B VAL A 1 222 ? 8.862   -12.883 7.862   0.50 9.52   ? 223 VAL A CB    1 
ATOM   1808 C  CG1   A VAL A 1 222 ? 10.387  -13.182 8.032   0.50 20.21  ? 223 VAL A CG1   1 
ATOM   1809 C  CG1   B VAL A 1 222 ? 8.803   -14.397 7.892   0.50 8.36   ? 223 VAL A CG1   1 
ATOM   1810 C  CG2   A VAL A 1 222 ? 8.184   -12.466 8.812   0.50 17.93  ? 223 VAL A CG2   1 
ATOM   1811 C  CG2   B VAL A 1 222 ? 10.073  -12.294 8.616   0.50 8.94   ? 223 VAL A CG2   1 
ATOM   1812 N  N     . LEU A 1 223 ? 9.560   -13.832 4.638   1.00 11.23  ? 224 LEU A N     1 
ATOM   1813 C  CA    . LEU A 1 223 ? 10.502  -14.265 3.635   1.00 13.79  ? 224 LEU A CA    1 
ATOM   1814 C  C     . LEU A 1 223 ? 10.820  -13.143 2.642   1.00 13.46  ? 224 LEU A C     1 
ATOM   1815 O  O     . LEU A 1 223 ? 11.982  -13.039 2.224   1.00 13.56  ? 224 LEU A O     1 
ATOM   1816 C  CB    . LEU A 1 223 ? 10.039  -15.539 2.955   1.00 15.66  ? 224 LEU A CB    1 
ATOM   1817 C  CG    . LEU A 1 223 ? 10.179  -16.776 3.776   1.00 19.42  ? 224 LEU A CG    1 
ATOM   1818 C  CD1   . LEU A 1 223 ? 9.289   -17.935 3.254   1.00 18.72  ? 224 LEU A CD1   1 
ATOM   1819 C  CD2   . LEU A 1 223 ? 11.695  -17.196 3.932   1.00 23.66  ? 224 LEU A CD2   1 
ATOM   1820 N  N     . LYS A 1 224 ? 9.869   -12.278 2.357   1.00 12.06  ? 225 LYS A N     1 
ATOM   1821 C  CA    . LYS A 1 224 ? 10.114  -11.148 1.466   1.00 12.05  ? 225 LYS A CA    1 
ATOM   1822 C  C     . LYS A 1 224 ? 10.983  -10.085 2.154   1.00 12.03  ? 225 LYS A C     1 
ATOM   1823 O  O     . LYS A 1 224 ? 11.822  -9.485  1.523   1.00 12.33  ? 225 LYS A O     1 
ATOM   1824 C  CB    . LYS A 1 224 ? 8.786   -10.629 0.903   1.00 15.66  ? 225 LYS A CB    1 
ATOM   1825 C  CG    . LYS A 1 224 ? 8.254   -11.680 -0.144  1.00 18.73  ? 225 LYS A CG    1 
ATOM   1826 C  CD    . LYS A 1 224 ? 6.986   -11.397 -0.899  1.00 24.70  ? 225 LYS A CD    1 
ATOM   1827 C  CE    . LYS A 1 224 ? 6.615   -12.476 -1.913  1.00 36.85  ? 225 LYS A CE    1 
ATOM   1828 N  NZ    . LYS A 1 224 ? 5.246   -12.250 -2.426  1.00 29.73  ? 225 LYS A NZ    1 
ATOM   1829 N  N     . PHE A 1 225 ? 10.866  -9.905  3.484   1.00 10.69  ? 226 PHE A N     1 
ATOM   1830 C  CA    . PHE A 1 225 ? 11.816  -9.035  4.155   1.00 9.67   ? 226 PHE A CA    1 
ATOM   1831 C  C     . PHE A 1 225 ? 13.236  -9.545  3.969   1.00 10.14  ? 226 PHE A C     1 
ATOM   1832 O  O     . PHE A 1 225 ? 14.193  -8.803  3.753   1.00 10.35  ? 226 PHE A O     1 
ATOM   1833 C  CB    . PHE A 1 225 ? 11.597  -9.044  5.669   1.00 9.94   ? 226 PHE A CB    1 
ATOM   1834 C  CG    . PHE A 1 225 ? 10.389  -8.274  6.182   1.00 10.46  ? 226 PHE A CG    1 
ATOM   1835 C  CD1   . PHE A 1 225 ? 9.340   -7.878  5.467   1.00 14.20  ? 226 PHE A CD1   1 
ATOM   1836 C  CD2   . PHE A 1 225 ? 10.293  -8.084  7.579   1.00 13.33  ? 226 PHE A CD2   1 
ATOM   1837 C  CE1   . PHE A 1 225 ? 8.326   -7.196  6.012   1.00 14.29  ? 226 PHE A CE1   1 
ATOM   1838 C  CE2   . PHE A 1 225 ? 9.264   -7.412  8.106   1.00 15.09  ? 226 PHE A CE2   1 
ATOM   1839 C  CZ    . PHE A 1 225 ? 8.287   -6.936  7.340   1.00 12.94  ? 226 PHE A CZ    1 
ATOM   1840 N  N     . ARG A 1 226 ? 13.381  -10.877 4.014   1.00 9.21   ? 227 ARG A N     1 
ATOM   1841 C  CA    . ARG A 1 226 ? 14.721  -11.477 3.973   1.00 9.49   ? 227 ARG A CA    1 
ATOM   1842 C  C     . ARG A 1 226 ? 15.360  -11.520 2.568   1.00 9.80   ? 227 ARG A C     1 
ATOM   1843 O  O     . ARG A 1 226 ? 16.466  -11.951 2.437   1.00 10.83  ? 227 ARG A O     1 
ATOM   1844 C  CB    . ARG A 1 226 ? 14.627  -12.905 4.534   1.00 10.28  ? 227 ARG A CB    1 
ATOM   1845 C  CG    . ARG A 1 226 ? 14.154  -12.990 5.990   1.00 10.00  ? 227 ARG A CG    1 
ATOM   1846 C  CD    . ARG A 1 226 ? 14.167  -14.453 6.437   1.00 11.73  ? 227 ARG A CD    1 
ATOM   1847 N  NE    . ARG A 1 226 ? 13.656  -14.587 7.780   1.00 10.97  ? 227 ARG A NE    1 
ATOM   1848 C  CZ    . ARG A 1 226 ? 12.784  -15.489 8.192   1.00 12.19  ? 227 ARG A CZ    1 
ATOM   1849 N  NH1   . ARG A 1 226 ? 12.336  -16.424 7.368   1.00 14.45  ? 227 ARG A NH1   1 
ATOM   1850 N  NH2   . ARG A 1 226 ? 12.303  -15.409 9.383   1.00 11.60  ? 227 ARG A NH2   1 
ATOM   1851 N  N     . LYS A 1 227 ? 14.599  -11.069 1.569   1.00 8.94   ? 228 LYS A N     1 
ATOM   1852 C  CA    . LYS A 1 227 ? 15.152  -10.956 0.211   1.00 11.33  ? 228 LYS A CA    1 
ATOM   1853 C  C     . LYS A 1 227 ? 15.760  -9.579  -0.036  1.00 11.37  ? 228 LYS A C     1 
ATOM   1854 O  O     . LYS A 1 227 ? 16.436  -9.374  -1.052  1.00 12.86  ? 228 LYS A O     1 
ATOM   1855 C  CB    . LYS A 1 227 ? 14.075  -11.170 -0.831  1.00 13.84  ? 228 LYS A CB    1 
ATOM   1856 C  CG    . LYS A 1 227 ? 13.457  -12.524 -0.853  1.00 17.89  ? 228 LYS A CG    1 
ATOM   1857 C  CD    . LYS A 1 227 ? 12.421  -12.714 -1.953  1.00 24.08  ? 228 LYS A CD    1 
ATOM   1858 C  CE    . LYS A 1 227 ? 13.000  -13.434 -3.162  1.00 35.96  ? 228 LYS A CE    1 
ATOM   1859 N  NZ    . LYS A 1 227 ? 11.913  -14.198 -3.866  1.00 55.77  ? 228 LYS A NZ    1 
ATOM   1860 N  N     . LEU A 1 228 ? 15.541  -8.619  0.887   1.00 10.19  ? 229 LEU A N     1 
ATOM   1861 C  CA    . LEU A 1 228 ? 16.215  -7.341  0.807   1.00 10.33  ? 229 LEU A CA    1 
ATOM   1862 C  C     . LEU A 1 228 ? 17.698  -7.520  0.925   1.00 9.89   ? 229 LEU A C     1 
ATOM   1863 O  O     . LEU A 1 228 ? 18.240  -8.578  1.358   1.00 10.76  ? 229 LEU A O     1 
ATOM   1864 C  CB    . LEU A 1 228 ? 15.733  -6.436  1.861   1.00 10.02  ? 229 LEU A CB    1 
ATOM   1865 C  CG    . LEU A 1 228 ? 14.283  -5.940  1.656   1.00 11.85  ? 229 LEU A CG    1 
ATOM   1866 C  CD1   . LEU A 1 228 ? 13.760  -5.296  2.925   1.00 11.59  ? 229 LEU A CD1   1 
ATOM   1867 C  CD2   . LEU A 1 228 ? 14.179  -4.880  0.503   1.00 13.05  ? 229 LEU A CD2   1 
ATOM   1868 N  N     . ASN A 1 229 ? 18.425  -6.493  0.544   1.00 11.79  ? 230 ASN A N     1 
ATOM   1869 C  CA    . ASN A 1 229 ? 19.889  -6.488  0.563   1.00 11.62  ? 230 ASN A CA    1 
ATOM   1870 C  C     . ASN A 1 229 ? 20.413  -5.309  1.440   1.00 12.29  ? 230 ASN A C     1 
ATOM   1871 O  O     . ASN A 1 229 ? 19.922  -4.198  1.371   1.00 13.65  ? 230 ASN A O     1 
ATOM   1872 C  CB    . ASN A 1 229 ? 20.463  -6.283  -0.832  1.00 12.60  ? 230 ASN A CB    1 
ATOM   1873 C  CG    . ASN A 1 229 ? 20.471  -7.474  -1.773  1.00 11.98  ? 230 ASN A CG    1 
ATOM   1874 O  OD1   . ASN A 1 229 ? 21.017  -7.319  -2.863  1.00 17.63  ? 230 ASN A OD1   1 
ATOM   1875 N  ND2   . ASN A 1 229 ? 19.882  -8.607  -1.447  1.00 12.51  ? 230 ASN A ND2   1 
ATOM   1876 N  N     . PHE A 1 230 ? 21.485  -5.654  2.191   1.00 12.18  ? 231 PHE A N     1 
ATOM   1877 C  CA    . PHE A 1 230 ? 22.238  -4.599  2.870   1.00 12.86  ? 231 PHE A CA    1 
ATOM   1878 C  C     . PHE A 1 230 ? 23.084  -3.789  1.908   1.00 14.86  ? 231 PHE A C     1 
ATOM   1879 O  O     . PHE A 1 230 ? 23.386  -2.635  2.136   1.00 15.70  ? 231 PHE A O     1 
ATOM   1880 C  CB    . PHE A 1 230 ? 23.197  -5.186  3.890   1.00 14.62  ? 231 PHE A CB    1 
ATOM   1881 C  CG    . PHE A 1 230 ? 22.582  -5.804  5.133   1.00 12.74  ? 231 PHE A CG    1 
ATOM   1882 C  CD1   . PHE A 1 230 ? 21.824  -5.042  6.005   1.00 11.33  ? 231 PHE A CD1   1 
ATOM   1883 C  CD2   . PHE A 1 230 ? 22.972  -7.022  5.548   1.00 14.01  ? 231 PHE A CD2   1 
ATOM   1884 C  CE1   . PHE A 1 230 ? 21.379  -5.593  7.208   1.00 12.88  ? 231 PHE A CE1   1 
ATOM   1885 C  CE2   . PHE A 1 230 ? 22.454  -7.599  6.781   1.00 13.00  ? 231 PHE A CE2   1 
ATOM   1886 C  CZ    . PHE A 1 230 ? 21.731  -6.800  7.609   1.00 12.73  ? 231 PHE A CZ    1 
ATOM   1887 N  N     . ASN A 1 231 ? 23.597  -4.477  0.893   1.00 14.35  ? 232 ASN A N     1 
ATOM   1888 C  CA    . ASN A 1 231 ? 24.460  -3.835  -0.100  1.00 15.30  ? 232 ASN A CA    1 
ATOM   1889 C  C     . ASN A 1 231 ? 23.649  -2.971  -1.068  1.00 12.73  ? 232 ASN A C     1 
ATOM   1890 O  O     . ASN A 1 231 ? 22.483  -3.005  -1.195  1.00 15.25  ? 232 ASN A O     1 
ATOM   1891 C  CB    . ASN A 1 231 ? 25.173  -4.912  -0.897  1.00 16.06  ? 232 ASN A CB    1 
ATOM   1892 C  CG    . ASN A 1 231 ? 24.120  -5.865  -1.454  1.00 13.29  ? 232 ASN A CG    1 
ATOM   1893 O  OD1   . ASN A 1 231 ? 23.704  -6.792  -0.764  1.00 15.94  ? 232 ASN A OD1   1 
ATOM   1894 N  ND2   . ASN A 1 231 ? 23.864  -5.770  -2.749  1.00 16.76  ? 232 ASN A ND2   1 
ATOM   1895 N  N     . GLY A 1 232 ? 24.460  -2.039  -1.718  1.00 16.14  ? 233 GLY A N     1 
ATOM   1896 C  CA    . GLY A 1 232 ? 23.987  -1.255  -2.837  1.00 16.41  ? 233 GLY A CA    1 
ATOM   1897 C  C     . GLY A 1 232 ? 23.868  -2.024  -4.182  1.00 15.30  ? 233 GLY A C     1 
ATOM   1898 O  O     . GLY A 1 232 ? 24.407  -3.112  -4.256  1.00 18.75  ? 233 GLY A O     1 
ATOM   1899 N  N     . GLU A 1 233 ? 23.102  -1.467  -5.139  1.00 15.27  ? 234 GLU A N     1 
ATOM   1900 C  CA    . GLU A 1 233 ? 23.009  -1.971  -6.486  1.00 16.69  ? 234 GLU A CA    1 
ATOM   1901 C  C     . GLU A 1 233 ? 24.353  -2.392  -6.962  1.00 19.70  ? 234 GLU A C     1 
ATOM   1902 O  O     . GLU A 1 233 ? 25.430  -1.742  -6.881  1.00 24.50  ? 234 GLU A O     1 
ATOM   1903 C  CB    . GLU A 1 233 ? 22.262  -1.052  -7.394  1.00 17.33  ? 234 GLU A CB    1 
ATOM   1904 C  CG    . GLU A 1 233 ? 21.862  -1.675  -8.720  1.00 16.10  ? 234 GLU A CG    1 
ATOM   1905 C  CD    . GLU A 1 233 ? 21.180  -0.687  -9.553  1.00 19.55  ? 234 GLU A CD    1 
ATOM   1906 O  OE1   . GLU A 1 233 ? 20.995  0.516   -9.177  1.00 21.11  ? 234 GLU A OE1   1 
ATOM   1907 O  OE2   . GLU A 1 233 ? 20.841  -1.085  -10.710 1.00 23.21  ? 234 GLU A OE2   1 
ATOM   1908 N  N     . GLY A 1 234 ? 24.281  -3.593  -7.565  1.00 22.78  ? 235 GLY A N     1 
ATOM   1909 C  CA    . GLY A 1 234 ? 25.333  -4.145  -8.156  1.00 28.97  ? 235 GLY A CA    1 
ATOM   1910 C  C     . GLY A 1 234 ? 26.522  -4.407  -7.334  1.00 41.83  ? 235 GLY A C     1 
ATOM   1911 O  O     . GLY A 1 234 ? 27.535  -4.597  -7.877  1.00 59.52  ? 235 GLY A O     1 
ATOM   1912 N  N     . GLU A 1 235 ? 26.442  -4.505  -6.030  1.00 23.26  ? 236 GLU A N     1 
ATOM   1913 C  CA    . GLU A 1 235 ? 27.608  -4.890  -5.236  1.00 20.35  ? 236 GLU A CA    1 
ATOM   1914 C  C     . GLU A 1 235 ? 27.424  -6.403  -4.777  1.00 24.96  ? 236 GLU A C     1 
ATOM   1915 O  O     . GLU A 1 235 ? 26.359  -6.910  -4.926  1.00 25.39  ? 236 GLU A O     1 
ATOM   1916 C  CB    . GLU A 1 235 ? 27.544  -4.030  -3.926  1.00 22.95  ? 236 GLU A CB    1 
ATOM   1917 C  CG    . GLU A 1 235 ? 27.862  -2.561  -4.191  1.00 23.53  ? 236 GLU A CG    1 
ATOM   1918 C  CD    . GLU A 1 235 ? 27.718  -1.694  -2.960  1.00 28.70  ? 236 GLU A CD    1 
ATOM   1919 O  OE1   . GLU A 1 235 ? 27.238  -2.115  -1.912  1.00 26.91  ? 236 GLU A OE1   1 
ATOM   1920 O  OE2   . GLU A 1 235 ? 27.991  -0.514  -3.115  1.00 35.43  ? 236 GLU A OE2   1 
ATOM   1921 N  N     . PRO A 1 236 ? 28.370  -7.033  -4.108  1.00 22.44  ? 237 PRO A N     1 
ATOM   1922 C  CA    . PRO A 1 236 ? 28.189  -8.479  -3.749  1.00 19.90  ? 237 PRO A CA    1 
ATOM   1923 C  C     . PRO A 1 236 ? 27.006  -8.618  -2.842  1.00 17.78  ? 237 PRO A C     1 
ATOM   1924 O  O     . PRO A 1 236 ? 26.917  -7.901  -1.855  1.00 17.90  ? 237 PRO A O     1 
ATOM   1925 C  CB    . PRO A 1 236 ? 29.451  -8.844  -3.012  1.00 22.31  ? 237 PRO A CB    1 
ATOM   1926 C  CG    . PRO A 1 236 ? 30.441  -7.880  -3.634  1.00 22.10  ? 237 PRO A CG    1 
ATOM   1927 C  CD    . PRO A 1 236 ? 29.745  -6.592  -3.919  1.00 25.38  ? 237 PRO A CD    1 
ATOM   1928 N  N     . GLU A 1 237 ? 26.128  -9.599  -3.102  1.00 17.71  ? 238 GLU A N     1 
ATOM   1929 C  CA    . GLU A 1 237 ? 24.868  -9.662  -2.407  1.00 18.42  ? 238 GLU A CA    1 
ATOM   1930 C  C     . GLU A 1 237 ? 25.005  -10.158 -1.017  1.00 15.81  ? 238 GLU A C     1 
ATOM   1931 O  O     . GLU A 1 237 ? 25.523  -11.210 -0.793  1.00 15.39  ? 238 GLU A O     1 
ATOM   1932 C  CB    . GLU A 1 237 ? 23.891  -10.586 -3.171  1.00 16.24  ? 238 GLU A CB    1 
ATOM   1933 C  CG    . GLU A 1 237 ? 22.508  -10.574 -2.526  1.00 20.32  ? 238 GLU A CG    1 
ATOM   1934 C  CD    . GLU A 1 237 ? 21.417  -11.249 -3.295  1.00 22.92  ? 238 GLU A CD    1 
ATOM   1935 O  OE1   . GLU A 1 237 ? 21.713  -12.150 -4.135  1.00 96.22  ? 238 GLU A OE1   1 
ATOM   1936 O  OE2   . GLU A 1 237 ? 20.245  -10.844 -3.196  1.00 17.38  ? 238 GLU A OE2   1 
ATOM   1937 N  N     A GLU A 1 238 ? 24.520  -9.399  -0.054  0.50 11.34  ? 239 GLU A N     1 
ATOM   1938 N  N     B GLU A 1 238 ? 24.508  -9.326  -0.105  0.50 14.50  ? 239 GLU A N     1 
ATOM   1939 C  CA    A GLU A 1 238 ? 24.509  -9.892  1.334   0.50 11.35  ? 239 GLU A CA    1 
ATOM   1940 C  CA    B GLU A 1 238 ? 24.410  -9.585  1.345   0.50 15.74  ? 239 GLU A CA    1 
ATOM   1941 C  C     A GLU A 1 238 ? 23.045  -9.594  1.791   0.50 12.19  ? 239 GLU A C     1 
ATOM   1942 C  C     B GLU A 1 238 ? 22.936  -9.516  1.723   0.50 12.50  ? 239 GLU A C     1 
ATOM   1943 O  O     A GLU A 1 238 ? 22.634  -8.469  1.914   0.50 12.48  ? 239 GLU A O     1 
ATOM   1944 O  O     B GLU A 1 238 ? 22.412  -8.403  1.759   0.50 15.26  ? 239 GLU A O     1 
ATOM   1945 C  CB    A GLU A 1 238 ? 25.579  -9.166  2.188   0.50 10.96  ? 239 GLU A CB    1 
ATOM   1946 C  CB    B GLU A 1 238 ? 25.059  -8.423  2.104   0.50 15.64  ? 239 GLU A CB    1 
ATOM   1947 C  CG    A GLU A 1 238 ? 25.393  -9.566  3.590   0.50 15.77  ? 239 GLU A CG    1 
ATOM   1948 C  CG    B GLU A 1 238 ? 26.559  -8.262  1.882   0.50 17.42  ? 239 GLU A CG    1 
ATOM   1949 C  CD    A GLU A 1 238 ? 25.996  -10.927 3.898   0.50 20.87  ? 239 GLU A CD    1 
ATOM   1950 C  CD    B GLU A 1 238 ? 27.107  -7.129  2.767   0.50 23.45  ? 239 GLU A CD    1 
ATOM   1951 O  OE1   A GLU A 1 238 ? 26.323  -11.758 2.912   0.50 24.46  ? 239 GLU A OE1   1 
ATOM   1952 O  OE1   B GLU A 1 238 ? 27.439  -7.340  3.984   0.50 28.70  ? 239 GLU A OE1   1 
ATOM   1953 O  OE2   A GLU A 1 238 ? 26.232  -11.172 5.183   0.50 23.88  ? 239 GLU A OE2   1 
ATOM   1954 O  OE2   B GLU A 1 238 ? 27.183  -6.014  2.259   0.50 25.47  ? 239 GLU A OE2   1 
ATOM   1955 N  N     . LEU A 1 239 ? 22.308  -10.653 2.063   1.00 12.10  ? 240 LEU A N     1 
ATOM   1956 C  CA    . LEU A 1 239 ? 20.920  -10.539 2.383   1.00 10.56  ? 240 LEU A CA    1 
ATOM   1957 C  C     . LEU A 1 239 ? 20.731  -9.680  3.660   1.00 10.01  ? 240 LEU A C     1 
ATOM   1958 O  O     . LEU A 1 239 ? 21.501  -9.912  4.649   1.00 11.41  ? 240 LEU A O     1 
ATOM   1959 C  CB    . LEU A 1 239 ? 20.303  -11.926 2.562   1.00 11.30  ? 240 LEU A CB    1 
ATOM   1960 C  CG    . LEU A 1 239 ? 20.230  -12.759 1.309   1.00 12.42  ? 240 LEU A CG    1 
ATOM   1961 C  CD1   . LEU A 1 239 ? 19.679  -14.123 1.782   1.00 17.18  ? 240 LEU A CD1   1 
ATOM   1962 C  CD2   . LEU A 1 239 ? 19.366  -12.125 0.248   1.00 13.43  ? 240 LEU A CD2   1 
ATOM   1963 N  N     . MET A 1 240 ? 19.698  -8.857  3.669   1.00 10.62  ? 241 MET A N     1 
ATOM   1964 C  CA    . MET A 1 240 ? 19.317  -8.061  4.828   1.00 9.87   ? 241 MET A CA    1 
ATOM   1965 C  C     . MET A 1 240 ? 18.528  -8.975  5.781   1.00 8.38   ? 241 MET A C     1 
ATOM   1966 O  O     . MET A 1 240 ? 17.328  -9.089  5.671   1.00 9.79   ? 241 MET A O     1 
ATOM   1967 C  CB    . MET A 1 240 ? 18.445  -6.870  4.417   1.00 11.82  ? 241 MET A CB    1 
ATOM   1968 C  CG    . MET A 1 240 ? 18.118  -5.894  5.552   1.00 11.96  ? 241 MET A CG    1 
ATOM   1969 S  SD    . MET A 1 240 ? 17.208  -4.502  5.061   1.00 12.43  ? 241 MET A SD    1 
ATOM   1970 C  CE    . MET A 1 240 ? 18.564  -3.474  4.384   1.00 13.39  ? 241 MET A CE    1 
ATOM   1971 N  N     . VAL A 1 241 ? 19.287  -9.566  6.709   1.00 8.69   ? 242 VAL A N     1 
ATOM   1972 C  CA    . VAL A 1 241 ? 18.760  -10.417 7.758   1.00 8.26   ? 242 VAL A CA    1 
ATOM   1973 C  C     . VAL A 1 241 ? 19.577  -10.191 9.037   1.00 8.41   ? 242 VAL A C     1 
ATOM   1974 O  O     . VAL A 1 241 ? 20.748  -9.807  8.967   1.00 8.98   ? 242 VAL A O     1 
ATOM   1975 C  CB    . VAL A 1 241 ? 18.826  -11.925 7.405   1.00 8.65   ? 242 VAL A CB    1 
ATOM   1976 C  CG1   . VAL A 1 241 ? 17.920  -12.246 6.183   1.00 9.78   ? 242 VAL A CG1   1 
ATOM   1977 C  CG2   . VAL A 1 241 ? 20.241  -12.399 7.150   1.00 10.31  ? 242 VAL A CG2   1 
ATOM   1978 N  N     . ASP A 1 242 ? 18.932  -10.477 10.166  1.00 7.17   ? 243 ASP A N     1 
ATOM   1979 C  CA    . ASP A 1 242 ? 19.578  -10.343 11.455  1.00 7.68   ? 243 ASP A CA    1 
ATOM   1980 C  C     . ASP A 1 242 ? 20.069  -8.901  11.701  1.00 6.95   ? 243 ASP A C     1 
ATOM   1981 O  O     . ASP A 1 242 ? 21.164  -8.666  12.202  1.00 9.09   ? 243 ASP A O     1 
ATOM   1982 C  CB    . ASP A 1 242 ? 20.683  -11.392 11.661  1.00 7.89   ? 243 ASP A CB    1 
ATOM   1983 C  CG    . ASP A 1 242 ? 20.128  -12.756 11.755  1.00 8.47   ? 243 ASP A CG    1 
ATOM   1984 O  OD1   . ASP A 1 242 ? 19.030  -12.936 12.377  1.00 8.44   ? 243 ASP A OD1   1 
ATOM   1985 O  OD2   . ASP A 1 242 ? 20.682  -13.680 11.118  1.00 11.43  ? 243 ASP A OD2   1 
ATOM   1986 N  N     . ASN A 1 243 ? 19.201  -7.976  11.385  1.00 6.61   ? 244 ASN A N     1 
ATOM   1987 C  CA    . ASN A 1 243 ? 19.480  -6.566  11.606  1.00 6.65   ? 244 ASN A CA    1 
ATOM   1988 C  C     . ASN A 1 243 ? 18.889  -6.048  12.935  1.00 6.58   ? 244 ASN A C     1 
ATOM   1989 O  O     . ASN A 1 243 ? 18.272  -5.035  13.023  1.00 7.80   ? 244 ASN A O     1 
ATOM   1990 C  CB    . ASN A 1 243 ? 18.941  -5.737  10.443  1.00 7.57   ? 244 ASN A CB    1 
ATOM   1991 C  CG    . ASN A 1 243 ? 17.460  -5.871  10.223  1.00 7.81   ? 244 ASN A CG    1 
ATOM   1992 O  OD1   . ASN A 1 243 ? 16.834  -6.722  10.823  1.00 8.51   ? 244 ASN A OD1   1 
ATOM   1993 N  ND2   . ASN A 1 243 ? 16.928  -5.032  9.379   1.00 12.01  ? 244 ASN A ND2   1 
ATOM   1994 N  N     . TRP A 1 244 ? 19.147  -6.856  13.964  1.00 7.00   ? 245 TRP A N     1 
ATOM   1995 C  CA    . TRP A 1 244 ? 18.730  -6.586  15.332  1.00 6.26   ? 245 TRP A CA    1 
ATOM   1996 C  C     . TRP A 1 244 ? 19.911  -6.459  16.284  1.00 6.29   ? 245 TRP A C     1 
ATOM   1997 O  O     . TRP A 1 244 ? 20.876  -7.217  16.169  1.00 7.77   ? 245 TRP A O     1 
ATOM   1998 C  CB    . TRP A 1 244 ? 17.784  -7.690  15.839  1.00 6.94   ? 245 TRP A CB    1 
ATOM   1999 C  CG    . TRP A 1 244 ? 18.251  -9.101  15.680  1.00 5.94   ? 245 TRP A CG    1 
ATOM   2000 C  CD1   . TRP A 1 244 ? 18.145  -9.868  14.575  1.00 6.66   ? 245 TRP A CD1   1 
ATOM   2001 C  CD2   . TRP A 1 244 ? 18.866  -9.928  16.662  1.00 6.13   ? 245 TRP A CD2   1 
ATOM   2002 N  NE1   . TRP A 1 244 ? 18.671  -11.102 14.781  1.00 7.31   ? 245 TRP A NE1   1 
ATOM   2003 C  CE2   . TRP A 1 244 ? 19.137  -11.149 16.060  1.00 6.33   ? 245 TRP A CE2   1 
ATOM   2004 C  CE3   . TRP A 1 244 ? 19.199  -9.739  18.009  1.00 8.08   ? 245 TRP A CE3   1 
ATOM   2005 C  CZ2   . TRP A 1 244 ? 19.709  -12.186 16.738  1.00 8.15   ? 245 TRP A CZ2   1 
ATOM   2006 C  CZ3   . TRP A 1 244 ? 19.776  -10.778 18.671  1.00 8.40   ? 245 TRP A CZ3   1 
ATOM   2007 C  CH2   . TRP A 1 244 ? 20.034  -12.004 18.068  1.00 8.50   ? 245 TRP A CH2   1 
ATOM   2008 N  N     . ARG A 1 245 ? 19.804  -5.548  17.203  1.00 6.15   ? 246 ARG A N     1 
ATOM   2009 C  CA    . ARG A 1 245 ? 20.762  -5.386  18.336  1.00 6.48   ? 246 ARG A CA    1 
ATOM   2010 C  C     . ARG A 1 245 ? 20.249  -6.318  19.430  1.00 6.28   ? 246 ARG A C     1 
ATOM   2011 O  O     . ARG A 1 245 ? 19.047  -6.308  19.769  1.00 7.98   ? 246 ARG A O     1 
ATOM   2012 C  CB    . ARG A 1 245 ? 20.793  -3.935  18.764  1.00 6.12   ? 246 ARG A CB    1 
ATOM   2013 C  CG    . ARG A 1 245 ? 21.884  -3.672  19.770  1.00 6.13   ? 246 ARG A CG    1 
ATOM   2014 C  CD    . ARG A 1 245 ? 21.825  -2.322  20.375  1.00 6.11   ? 246 ARG A CD    1 
ATOM   2015 N  NE    . ARG A 1 245 ? 23.035  -2.045  21.129  1.00 7.26   ? 246 ARG A NE    1 
ATOM   2016 C  CZ    . ARG A 1 245 ? 23.209  -1.027  21.967  1.00 6.70   ? 246 ARG A CZ    1 
ATOM   2017 N  NH1   . ARG A 1 245 ? 22.282  -0.234  22.321  1.00 7.54   ? 246 ARG A NH1   1 
ATOM   2018 N  NH2   . ARG A 1 245 ? 24.442  -0.830  22.407  1.00 8.98   ? 246 ARG A NH2   1 
ATOM   2019 N  N     . PRO A 1 246 ? 21.134  -7.056  20.082  1.00 7.05   ? 247 PRO A N     1 
ATOM   2020 C  CA    . PRO A 1 246 ? 20.708  -7.905  21.217  1.00 7.47   ? 247 PRO A CA    1 
ATOM   2021 C  C     . PRO A 1 246 ? 20.407  -7.056  22.454  1.00 7.39   ? 247 PRO A C     1 
ATOM   2022 O  O     . PRO A 1 246 ? 20.746  -5.880  22.573  1.00 7.91   ? 247 PRO A O     1 
ATOM   2023 C  CB    . PRO A 1 246 ? 21.898  -8.780  21.480  1.00 9.91   ? 247 PRO A CB    1 
ATOM   2024 C  CG    . PRO A 1 246 ? 22.934  -8.297  20.682  1.00 17.37  ? 247 PRO A CG    1 
ATOM   2025 C  CD    . PRO A 1 246 ? 22.566  -7.310  19.752  1.00 8.80   ? 247 PRO A CD    1 
ATOM   2026 N  N     . ALA A 1 247 ? 19.758  -7.728  23.427  1.00 7.61   ? 248 ALA A N     1 
ATOM   2027 C  CA    . ALA A 1 247 ? 19.425  -7.076  24.693  1.00 7.17   ? 248 ALA A CA    1 
ATOM   2028 C  C     . ALA A 1 247 ? 20.632  -6.580  25.422  1.00 6.91   ? 248 ALA A C     1 
ATOM   2029 O  O     . ALA A 1 247 ? 21.675  -7.265  25.438  1.00 8.50   ? 248 ALA A O     1 
ATOM   2030 C  CB    . ALA A 1 247 ? 18.665  -8.075  25.550  1.00 9.21   ? 248 ALA A CB    1 
ATOM   2031 N  N     . GLN A 1 248 ? 20.523  -5.375  26.003  1.00 7.16   ? 249 GLN A N     1 
ATOM   2032 C  CA    . GLN A 1 248 ? 21.555  -4.714  26.704  1.00 7.02   ? 249 GLN A CA    1 
ATOM   2033 C  C     . GLN A 1 248 ? 21.259  -4.721  28.188  1.00 8.08   ? 249 GLN A C     1 
ATOM   2034 O  O     . GLN A 1 248 ? 20.118  -4.933  28.623  1.00 8.65   ? 249 GLN A O     1 
ATOM   2035 C  CB    . GLN A 1 248 ? 21.622  -3.295  26.170  1.00 8.49   ? 249 GLN A CB    1 
ATOM   2036 C  CG    . GLN A 1 248 ? 21.934  -3.226  24.696  1.00 8.43   ? 249 GLN A CG    1 
ATOM   2037 C  CD    . GLN A 1 248 ? 23.230  -3.855  24.352  1.00 9.25   ? 249 GLN A CD    1 
ATOM   2038 O  OE1   . GLN A 1 248 ? 24.273  -3.505  24.945  1.00 11.85  ? 249 GLN A OE1   1 
ATOM   2039 N  NE2   . GLN A 1 248 ? 23.219  -4.781  23.433  1.00 9.69   ? 249 GLN A NE2   1 
ATOM   2040 N  N     . PRO A 1 249 ? 22.272  -4.423  29.018  1.00 9.34   ? 250 PRO A N     1 
ATOM   2041 C  CA    . PRO A 1 249 ? 22.044  -4.435  30.481  1.00 11.39  ? 250 PRO A CA    1 
ATOM   2042 C  C     . PRO A 1 249 ? 20.994  -3.456  30.939  1.00 8.75   ? 250 PRO A C     1 
ATOM   2043 O  O     . PRO A 1 249 ? 21.039  -2.301  30.563  1.00 9.38   ? 250 PRO A O     1 
ATOM   2044 C  CB    . PRO A 1 249 ? 23.430  -4.072  31.035  1.00 12.41  ? 250 PRO A CB    1 
ATOM   2045 C  CG    . PRO A 1 249 ? 24.335  -4.540  29.990  1.00 13.45  ? 250 PRO A CG    1 
ATOM   2046 C  CD    . PRO A 1 249 ? 23.696  -4.193  28.705  1.00 10.48  ? 250 PRO A CD    1 
ATOM   2047 N  N     . LEU A 1 250 ? 20.103  -3.900  31.792  1.00 9.97   ? 251 LEU A N     1 
ATOM   2048 C  CA    . LEU A 1 250 ? 19.041  -3.053  32.303  1.00 9.16   ? 251 LEU A CA    1 
ATOM   2049 C  C     . LEU A 1 250 ? 19.563  -1.960  33.219  1.00 9.24   ? 251 LEU A C     1 
ATOM   2050 O  O     . LEU A 1 250 ? 18.970  -0.878  33.294  1.00 9.68   ? 251 LEU A O     1 
ATOM   2051 C  CB    . LEU A 1 250 ? 17.995  -3.946  33.021  1.00 11.57  ? 251 LEU A CB    1 
ATOM   2052 C  CG    . LEU A 1 250 ? 16.727  -3.152  33.405  1.00 11.35  ? 251 LEU A CG    1 
ATOM   2053 C  CD1   . LEU A 1 250 ? 16.000  -2.620  32.172  1.00 11.70  ? 251 LEU A CD1   1 
ATOM   2054 C  CD2   . LEU A 1 250 ? 15.784  -4.195  34.114  1.00 14.26  ? 251 LEU A CD2   1 
ATOM   2055 N  N     . LYS A 1 251 ? 20.634  -2.237  33.969  1.00 10.69  ? 252 LYS A N     1 
ATOM   2056 C  CA    . LYS A 1 251 ? 21.234  -1.239  34.899  1.00 11.35  ? 252 LYS A CA    1 
ATOM   2057 C  C     . LYS A 1 251 ? 20.195  -0.689  35.858  1.00 11.98  ? 252 LYS A C     1 
ATOM   2058 O  O     . LYS A 1 251 ? 19.424  -1.490  36.371  1.00 15.80  ? 252 LYS A O     1 
ATOM   2059 C  CB    . LYS A 1 251 ? 21.975  -0.214  34.118  1.00 12.74  ? 252 LYS A CB    1 
ATOM   2060 C  CG    . LYS A 1 251 ? 23.080  -0.890  33.364  1.00 17.26  ? 252 LYS A CG    1 
ATOM   2061 C  CD    . LYS A 1 251 ? 24.105  0.029   32.831  1.00 20.32  ? 252 LYS A CD    1 
ATOM   2062 C  CE    . LYS A 1 251 ? 25.327  -0.773  32.399  1.00 24.37  ? 252 LYS A CE    1 
ATOM   2063 N  NZ    . LYS A 1 251 ? 26.051  0.071   31.387  1.00 29.78  ? 252 LYS A NZ    1 
ATOM   2064 N  N     . ASN A 1 252 ? 20.162  0.577   36.076  1.00 11.55  ? 253 ASN A N     1 
ATOM   2065 C  CA    . ASN A 1 252 ? 19.336  1.080   37.068  1.00 17.68  ? 253 ASN A CA    1 
ATOM   2066 C  C     . ASN A 1 252 ? 18.010  1.504   36.524  1.00 20.03  ? 253 ASN A C     1 
ATOM   2067 O  O     . ASN A 1 252 ? 17.862  2.864   36.562  1.00 22.73  ? 253 ASN A O     1 
ATOM   2068 C  CB    . ASN A 1 252 ? 20.098  2.265   37.780  1.00 23.00  ? 253 ASN A CB    1 
ATOM   2069 C  CG    . ASN A 1 252 ? 19.415  2.759   39.055  1.00 25.37  ? 253 ASN A CG    1 
ATOM   2070 O  OD1   . ASN A 1 252 ? 19.066  1.997   39.967  1.00 49.24  ? 253 ASN A OD1   1 
ATOM   2071 N  ND2   . ASN A 1 252 ? 19.248  4.072   39.130  1.00 31.87  ? 253 ASN A ND2   1 
ATOM   2072 N  N     . ARG A 1 253 ? 17.218  0.493   35.842  1.00 13.83  ? 254 ARG A N     1 
ATOM   2073 C  CA    . ARG A 1 253 ? 15.947  0.800   35.296  1.00 9.38   ? 254 ARG A CA    1 
ATOM   2074 C  C     . ARG A 1 253 ? 14.893  -0.077  35.771  1.00 11.02  ? 254 ARG A C     1 
ATOM   2075 O  O     . ARG A 1 253 ? 15.086  -1.237  35.937  1.00 17.41  ? 254 ARG A O     1 
ATOM   2076 C  CB    . ARG A 1 253 ? 16.023  0.911   33.806  1.00 8.60   ? 254 ARG A CB    1 
ATOM   2077 C  CG    . ARG A 1 253 ? 16.959  1.999   33.321  1.00 8.06   ? 254 ARG A CG    1 
ATOM   2078 C  CD    . ARG A 1 253 ? 17.151  2.014   31.837  1.00 7.99   ? 254 ARG A CD    1 
ATOM   2079 N  NE    . ARG A 1 253 ? 17.906  0.884   31.380  1.00 7.18   ? 254 ARG A NE    1 
ATOM   2080 C  CZ    . ARG A 1 253 ? 18.155  0.618   30.117  1.00 6.19   ? 254 ARG A CZ    1 
ATOM   2081 N  NH1   . ARG A 1 253 ? 17.562  1.270   29.136  1.00 6.73   ? 254 ARG A NH1   1 
ATOM   2082 N  NH2   . ARG A 1 253 ? 18.972  -0.353  29.767  1.00 6.80   ? 254 ARG A NH2   1 
ATOM   2083 N  N     . GLN A 1 254 ? 13.687  0.465   35.804  1.00 10.08  ? 255 GLN A N     1 
ATOM   2084 C  CA    . GLN A 1 254 ? 12.520  -0.283  36.075  1.00 12.10  ? 255 GLN A CA    1 
ATOM   2085 C  C     . GLN A 1 254 ? 11.670  -0.369  34.847  1.00 10.14  ? 255 GLN A C     1 
ATOM   2086 O  O     . GLN A 1 254 ? 11.440  0.660   34.166  1.00 13.07  ? 255 GLN A O     1 
ATOM   2087 C  CB    . GLN A 1 254 ? 11.737  0.363   37.207  1.00 16.44  ? 255 GLN A CB    1 
ATOM   2088 C  CG    . GLN A 1 254 ? 12.458  -0.034  38.535  1.00 22.11  ? 255 GLN A CG    1 
ATOM   2089 C  CD    . GLN A 1 254 ? 11.491  -0.148  39.631  1.00 28.39  ? 255 GLN A CD    1 
ATOM   2090 O  OE1   . GLN A 1 254 ? 10.464  0.564   39.581  1.00 36.58  ? 255 GLN A OE1   1 
ATOM   2091 N  NE2   . GLN A 1 254 ? 11.788  -0.965  40.720  1.00 30.13  ? 255 GLN A NE2   1 
ATOM   2092 N  N     . ILE A 1 255 ? 11.187  -1.536  34.491  1.00 8.26   ? 256 ILE A N     1 
ATOM   2093 C  CA    . ILE A 1 255 ? 10.202  -1.746  33.470  1.00 7.31   ? 256 ILE A CA    1 
ATOM   2094 C  C     . ILE A 1 255 ? 8.806   -1.775  34.127  1.00 8.27   ? 256 ILE A C     1 
ATOM   2095 O  O     . ILE A 1 255 ? 8.637   -2.529  35.100  1.00 9.91   ? 256 ILE A O     1 
ATOM   2096 C  CB    . ILE A 1 255 ? 10.453  -2.991  32.686  1.00 8.60   ? 256 ILE A CB    1 
ATOM   2097 C  CG1   . ILE A 1 255 ? 11.905  -2.992  32.108  1.00 8.98   ? 256 ILE A CG1   1 
ATOM   2098 C  CG2   . ILE A 1 255 ? 9.413   -3.219  31.593  1.00 9.57   ? 256 ILE A CG2   1 
ATOM   2099 C  CD1   . ILE A 1 255 ? 12.256  -4.153  31.291  1.00 10.49  ? 256 ILE A CD1   1 
ATOM   2100 N  N     . LYS A 1 256 ? 7.899   -0.986  33.647  1.00 7.86   ? 257 LYS A N     1 
ATOM   2101 C  CA    . LYS A 1 256 ? 6.559   -0.872  34.210  1.00 7.98   ? 257 LYS A CA    1 
ATOM   2102 C  C     . LYS A 1 256 ? 5.554   -1.451  33.237  1.00 7.52   ? 257 LYS A C     1 
ATOM   2103 O  O     . LYS A 1 256 ? 5.674   -1.270  32.040  1.00 9.47   ? 257 LYS A O     1 
ATOM   2104 C  CB    . LYS A 1 256 ? 6.256   0.597   34.540  1.00 10.10  ? 257 LYS A CB    1 
ATOM   2105 C  CG    . LYS A 1 256 ? 7.192   1.135   35.621  1.00 13.11  ? 257 LYS A CG    1 
ATOM   2106 C  CD    . LYS A 1 256 ? 7.140   2.581   35.981  1.00 17.20  ? 257 LYS A CD    1 
ATOM   2107 C  CE    . LYS A 1 256 ? 8.249   2.833   36.995  1.00 28.09  ? 257 LYS A CE    1 
ATOM   2108 N  NZ    . LYS A 1 256 ? 8.243   4.234   37.510  1.00 30.77  ? 257 LYS A NZ    1 
ATOM   2109 N  N     . ALA A 1 257 ? 4.556   -2.111  33.768  1.00 8.74   ? 258 ALA A N     1 
ATOM   2110 C  CA    . ALA A 1 257 ? 3.465   -2.693  33.009  1.00 8.58   ? 258 ALA A CA    1 
ATOM   2111 C  C     . ALA A 1 257 ? 2.224   -1.893  33.185  1.00 8.57   ? 258 ALA A C     1 
ATOM   2112 O  O     . ALA A 1 257 ? 1.869   -1.443  34.288  1.00 10.62  ? 258 ALA A O     1 
ATOM   2113 C  CB    . ALA A 1 257 ? 3.196   -4.118  33.435  1.00 10.39  ? 258 ALA A CB    1 
ATOM   2114 N  N     . SER A 1 258 ? 1.476   -1.739  32.068  1.00 8.78   ? 259 SER A N     1 
ATOM   2115 C  CA    . SER A 1 258 ? 0.241   -0.971  32.047  1.00 10.05  ? 259 SER A CA    1 
ATOM   2116 C  C     . SER A 1 258 ? -0.918  -1.822  32.510  1.00 10.60  ? 259 SER A C     1 
ATOM   2117 O  O     . SER A 1 258 ? -2.038  -1.381  32.610  1.00 14.03  ? 259 SER A O     1 
ATOM   2118 C  CB    . SER A 1 258 ? -0.052  -0.456  30.653  1.00 10.25  ? 259 SER A CB    1 
ATOM   2119 O  OG    . SER A 1 258 ? -0.459  -1.506  29.775  1.00 10.55  ? 259 SER A OG    1 
ATOM   2120 N  N     . PHE A 1 259 ? -0.707  -3.123  32.706  1.00 11.10  ? 260 PHE A N     1 
ATOM   2121 C  CA    . PHE A 1 259 ? -1.750  -4.145  32.858  1.00 12.98  ? 260 PHE A CA    1 
ATOM   2122 C  C     . PHE A 1 259 ? -1.404  -5.024  34.012  1.00 15.78  ? 260 PHE A C     1 
ATOM   2123 O  O     . PHE A 1 259 ? -0.220  -5.262  34.355  1.00 17.86  ? 260 PHE A O     1 
ATOM   2124 C  CB    . PHE A 1 259 ? -1.873  -4.948  31.563  1.00 13.83  ? 260 PHE A CB    1 
ATOM   2125 C  CG    . PHE A 1 259 ? -0.595  -5.692  31.209  1.00 12.48  ? 260 PHE A CG    1 
ATOM   2126 C  CD1   . PHE A 1 259 ? 0.395   -5.048  30.489  1.00 11.30  ? 260 PHE A CD1   1 
ATOM   2127 C  CD2   . PHE A 1 259 ? -0.337  -6.974  31.643  1.00 17.25  ? 260 PHE A CD2   1 
ATOM   2128 C  CE1   . PHE A 1 259 ? 1.604   -5.676  30.227  1.00 14.18  ? 260 PHE A CE1   1 
ATOM   2129 C  CE2   . PHE A 1 259 ? 0.849   -7.582  31.360  1.00 17.58  ? 260 PHE A CE2   1 
ATOM   2130 C  CZ    . PHE A 1 259 ? 1.824   -6.942  30.646  1.00 17.93  ? 260 PHE A CZ    1 
ATOM   2131 N  N     . LYS A 1 260 ? -2.461  -5.586  34.572  1.00 22.02  ? 261 LYS A N     1 
ATOM   2132 C  CA    . LYS A 1 260 ? -2.381  -6.537  35.705  1.00 29.36  ? 261 LYS A CA    1 
ATOM   2133 C  C     . LYS A 1 260 ? -2.084  -7.959  35.250  1.00 42.10  ? 261 LYS A C     1 
ATOM   2134 O  O     . LYS A 1 260 ? -1.389  -8.711  35.949  1.00 58.54  ? 261 LYS A O     1 
ATOM   2135 C  CB    . LYS A 1 260 ? -3.621  -6.471  36.596  1.00 36.09  ? 261 LYS A CB    1 
ATOM   2136 C  CG    . LYS A 1 260 ? -4.121  -5.058  36.894  1.00 42.23  ? 261 LYS A CG    1 
ATOM   2137 C  CD    . LYS A 1 260 ? -5.390  -5.026  37.713  1.00 55.75  ? 261 LYS A CD    1 
ATOM   2138 C  CE    . LYS A 1 260 ? -5.218  -5.778  39.012  1.00 66.76  ? 261 LYS A CE    1 
ATOM   2139 N  NZ    . LYS A 1 260 ? -6.047  -5.204  40.105  1.00 85.31  ? 261 LYS A NZ    1 
ATOM   2140 O  OXT   . LYS A 1 260 ? -2.499  -8.387  34.171  1.00 45.56  ? 261 LYS A OXT   1 
HETATM 2141 ZN ZN    . ZN  B 2 .   ? 14.268  -0.093  15.350  1.00 6.45   ? 301 ZN  A ZN    1 
HETATM 2142 C  C1    . MNP C 3 .   ? 19.257  5.737   12.410  1.00 28.13  ? 302 MNP A C1    1 
HETATM 2143 C  C2    . MNP C 3 .   ? 19.147  6.405   13.772  1.00 21.07  ? 302 MNP A C2    1 
HETATM 2144 C  "C1'" . MNP C 3 .   ? 17.699  6.315   14.157  1.00 14.91  ? 302 MNP A "C1'" 1 
HETATM 2145 C  "C2'" . MNP C 3 .   ? 17.264  5.331   15.029  1.00 16.35  ? 302 MNP A "C2'" 1 
HETATM 2146 C  "C3'" . MNP C 3 .   ? 15.919  5.147   15.408  1.00 19.10  ? 302 MNP A "C3'" 1 
HETATM 2147 N  "N3'" . MNP C 3 .   ? 15.592  4.187   16.390  1.00 17.80  ? 302 MNP A "N3'" 1 
HETATM 2148 O  "O3'" . MNP C 3 .   ? 14.338  3.867   16.541  1.00 21.30  ? 302 MNP A "O3'" 1 
HETATM 2149 O  "O4'" . MNP C 3 .   ? 16.411  3.516   17.026  1.00 21.56  ? 302 MNP A "O4'" 1 
HETATM 2150 C  "C4'" . MNP C 3 .   ? 15.001  6.011   14.859  1.00 16.78  ? 302 MNP A "C4'" 1 
HETATM 2151 C  "C5'" . MNP C 3 .   ? 15.400  7.035   14.009  1.00 14.82  ? 302 MNP A "C5'" 1 
HETATM 2152 C  "C6'" . MNP C 3 .   ? 16.672  7.140   13.645  1.00 17.75  ? 302 MNP A "C6'" 1 
HETATM 2153 O  O1    . MNP C 3 .   ? 19.005  6.339   11.296  1.00 32.61  ? 302 MNP A O1    1 
HETATM 2154 O  O2    . MNP C 3 .   ? 19.542  4.545   12.428  1.00 26.72  ? 302 MNP A O2    1 
HETATM 2155 O  O     . HOH D 4 .   ? 19.130  3.024   10.527  0.50 24.98  ? 401 HOH A O     1 
HETATM 2156 O  O     . HOH D 4 .   ? -4.223  11.369  13.126  1.00 25.24  ? 402 HOH A O     1 
HETATM 2157 O  O     . HOH D 4 .   ? 0.108   9.503   1.841   1.00 20.45  ? 403 HOH A O     1 
HETATM 2158 O  O     . HOH D 4 .   ? 11.480  7.733   -3.941  1.00 40.97  ? 404 HOH A O     1 
HETATM 2159 O  O     . HOH D 4 .   ? 2.114   19.369  18.630  1.00 27.42  ? 405 HOH A O     1 
HETATM 2160 O  O     . HOH D 4 .   ? 6.695   16.304  5.589   1.00 40.92  ? 406 HOH A O     1 
HETATM 2161 O  O     . HOH D 4 .   ? 25.351  -0.849  29.140  1.00 19.90  ? 407 HOH A O     1 
HETATM 2162 O  O     . HOH D 4 .   ? -3.395  13.638  6.047   1.00 35.01  ? 408 HOH A O     1 
HETATM 2163 O  O     . HOH D 4 .   ? 10.764  17.659  29.633  1.00 31.12  ? 409 HOH A O     1 
HETATM 2164 O  O     . HOH D 4 .   ? 1.675   13.568  13.043  1.00 39.17  ? 410 HOH A O     1 
HETATM 2165 O  O     . HOH D 4 .   ? 25.898  -5.659  22.312  1.00 21.12  ? 411 HOH A O     1 
HETATM 2166 O  O     . HOH D 4 .   ? 5.399   21.065  13.215  1.00 16.92  ? 412 HOH A O     1 
HETATM 2167 O  O     . HOH D 4 .   ? 5.313   -8.407  38.177  1.00 59.18  ? 413 HOH A O     1 
HETATM 2168 O  O     . HOH D 4 .   ? 19.559  11.025  28.018  1.00 29.38  ? 414 HOH A O     1 
HETATM 2169 O  O     . HOH D 4 .   ? 22.992  9.751   28.209  1.00 38.82  ? 415 HOH A O     1 
HETATM 2170 O  O     . HOH D 4 .   ? 4.894   7.234   -8.145  1.00 33.38  ? 416 HOH A O     1 
HETATM 2171 O  O     . HOH D 4 .   ? 1.548   18.742  5.598   1.00 34.23  ? 417 HOH A O     1 
HETATM 2172 O  O     . HOH D 4 .   ? 14.276  -18.461 19.659  1.00 12.10  ? 418 HOH A O     1 
HETATM 2173 O  O     . HOH D 4 .   ? 12.248  -2.186  7.984   1.00 9.25   ? 419 HOH A O     1 
HETATM 2174 O  O     . HOH D 4 .   ? 19.632  -2.330  15.696  1.00 7.81   ? 420 HOH A O     1 
HETATM 2175 O  O     . HOH D 4 .   ? 15.654  1.055   16.105  1.00 9.67   ? 421 HOH A O     1 
HETATM 2176 O  O     . HOH D 4 .   ? 24.389  6.765   29.906  1.00 14.26  ? 422 HOH A O     1 
HETATM 2177 O  O     . HOH D 4 .   ? -6.217  -5.830  26.351  1.00 30.66  ? 423 HOH A O     1 
HETATM 2178 O  O     . HOH D 4 .   ? 8.028   15.099  31.886  1.00 27.08  ? 424 HOH A O     1 
HETATM 2179 O  O     . HOH D 4 .   ? 0.620   12.557  26.654  1.00 16.63  ? 425 HOH A O     1 
HETATM 2180 O  O     . HOH D 4 .   ? 8.702   12.436  5.491   1.00 21.35  ? 426 HOH A O     1 
HETATM 2181 O  O     . HOH D 4 .   ? -4.969  7.965   27.072  1.00 24.86  ? 427 HOH A O     1 
HETATM 2182 O  O     . HOH D 4 .   ? 25.038  -1.594  26.600  1.00 18.72  ? 428 HOH A O     1 
HETATM 2183 O  O     . HOH D 4 .   ? 26.189  -9.461  19.385  1.00 29.15  ? 429 HOH A O     1 
HETATM 2184 O  O     . HOH D 4 .   ? -3.068  -1.310  29.375  1.00 44.83  ? 430 HOH A O     1 
HETATM 2185 O  O     . HOH D 4 .   ? 16.753  5.420   10.248  1.00 31.17  ? 431 HOH A O     1 
HETATM 2186 O  O     . HOH D 4 .   ? 21.838  16.732  24.426  1.00 30.40  ? 432 HOH A O     1 
HETATM 2187 O  O     . HOH D 4 .   ? 20.541  -18.218 10.990  1.00 36.65  ? 433 HOH A O     1 
HETATM 2188 O  O     . HOH D 4 .   ? 5.206   2.313   -4.655  1.00 48.78  ? 434 HOH A O     1 
HETATM 2189 O  O     . HOH D 4 .   ? 6.643   -14.878 29.175  1.00 17.46  ? 435 HOH A O     1 
HETATM 2190 O  O     . HOH D 4 .   ? -6.142  -11.191 20.494  1.00 46.62  ? 436 HOH A O     1 
HETATM 2191 O  O     . HOH D 4 .   ? -6.909  8.052   21.561  1.00 24.50  ? 437 HOH A O     1 
HETATM 2192 O  O     . HOH D 4 .   ? 16.067  -10.197 32.257  1.00 17.80  ? 438 HOH A O     1 
HETATM 2193 O  O     . HOH D 4 .   ? 14.821  -2.973  -6.325  1.00 20.08  ? 439 HOH A O     1 
HETATM 2194 O  O     . HOH D 4 .   ? 22.800  6.540   12.012  1.00 31.53  ? 440 HOH A O     1 
HETATM 2195 O  O     . HOH D 4 .   ? 0.938   -15.072 3.021   1.00 22.76  ? 441 HOH A O     1 
HETATM 2196 O  O     . HOH D 4 .   ? -1.943  -4.201  2.756   1.00 22.43  ? 442 HOH A O     1 
HETATM 2197 O  O     . HOH D 4 .   ? -6.167  -9.171  22.464  1.00 35.87  ? 443 HOH A O     1 
HETATM 2198 O  O     . HOH D 4 .   ? 32.318  -5.335  22.593  1.00 23.62  ? 444 HOH A O     1 
HETATM 2199 O  O     . HOH D 4 .   ? 14.304  -13.186 31.685  1.00 25.53  ? 445 HOH A O     1 
HETATM 2200 O  O     . HOH D 4 .   ? 23.434  -11.660 5.267   1.00 22.03  ? 446 HOH A O     1 
HETATM 2201 O  O     . HOH D 4 .   ? 19.159  -3.080  -6.898  1.00 26.02  ? 447 HOH A O     1 
HETATM 2202 O  O     . HOH D 4 .   ? 8.284   14.280  29.175  1.00 33.15  ? 448 HOH A O     1 
HETATM 2203 O  O     . HOH D 4 .   ? -3.106  10.315  20.169  1.00 17.43  ? 449 HOH A O     1 
HETATM 2204 O  O     . HOH D 4 .   ? 10.204  10.449  25.593  1.00 8.69   ? 450 HOH A O     1 
HETATM 2205 O  O     . HOH D 4 .   ? 10.464  -16.509 17.310  1.00 10.28  ? 451 HOH A O     1 
HETATM 2206 O  O     . HOH D 4 .   ? 0.318   9.934   30.120  1.00 22.91  ? 452 HOH A O     1 
HETATM 2207 O  O     . HOH D 4 .   ? 17.977  -17.827 6.348   1.00 25.54  ? 453 HOH A O     1 
HETATM 2208 O  O     . HOH D 4 .   ? -1.065  21.251  11.956  1.00 31.42  ? 454 HOH A O     1 
HETATM 2209 O  O     . HOH D 4 .   ? 4.578   -13.851 32.886  1.00 29.18  ? 455 HOH A O     1 
HETATM 2210 O  O     . HOH D 4 .   ? 18.368  -6.901  29.193  1.00 9.39   ? 456 HOH A O     1 
HETATM 2211 O  O     . HOH D 4 .   ? 6.953   12.059  27.888  1.00 13.85  ? 457 HOH A O     1 
HETATM 2212 O  O     . HOH D 4 .   ? 22.772  -14.024 9.451   1.00 26.30  ? 458 HOH A O     1 
HETATM 2213 O  O     . HOH D 4 .   ? 12.910  -13.737 11.541  1.00 9.06   ? 459 HOH A O     1 
HETATM 2214 O  O     . HOH D 4 .   ? 2.556   -10.763 -3.529  1.00 24.07  ? 460 HOH A O     1 
HETATM 2215 O  O     . HOH D 4 .   ? 21.109  0.553   -4.609  1.00 18.29  ? 461 HOH A O     1 
HETATM 2216 O  O     . HOH D 4 .   ? 12.182  -13.691 36.795  1.00 19.60  ? 462 HOH A O     1 
HETATM 2217 O  O     . HOH D 4 .   ? 20.670  2.960   34.496  1.00 26.06  ? 463 HOH A O     1 
HETATM 2218 O  O     . HOH D 4 .   ? 7.951   -7.223  -3.156  1.00 32.08  ? 464 HOH A O     1 
HETATM 2219 O  O     . HOH D 4 .   ? 6.855   16.092  27.181  1.00 23.21  ? 465 HOH A O     1 
HETATM 2220 O  O     . HOH D 4 .   ? 16.399  -11.742 18.144  1.00 7.79   ? 466 HOH A O     1 
HETATM 2221 O  O     . HOH D 4 .   ? 1.029   18.547  23.475  1.00 46.09  ? 467 HOH A O     1 
HETATM 2222 O  O     . HOH D 4 .   ? 20.479  15.580  16.181  1.00 23.52  ? 468 HOH A O     1 
HETATM 2223 O  O     . HOH D 4 .   ? 9.969   -17.935 7.588   1.00 22.73  ? 469 HOH A O     1 
HETATM 2224 O  O     . HOH D 4 .   ? 17.354  -9.380  20.990  1.00 8.47   ? 470 HOH A O     1 
HETATM 2225 O  O     . HOH D 4 .   ? 5.545   10.522  -2.163  1.00 19.05  ? 471 HOH A O     1 
HETATM 2226 O  O     . HOH D 4 .   ? 4.803   17.635  23.721  1.00 18.66  ? 472 HOH A O     1 
HETATM 2227 O  O     . HOH D 4 .   ? 11.756  7.742   29.191  1.00 12.67  ? 473 HOH A O     1 
HETATM 2228 O  O     . HOH D 4 .   ? 28.751  -6.625  -0.295  1.00 27.87  ? 474 HOH A O     1 
HETATM 2229 O  O     . HOH D 4 .   ? -5.325  4.581   20.898  1.00 21.98  ? 475 HOH A O     1 
HETATM 2230 O  O     . HOH D 4 .   ? 6.339   -16.757 18.816  1.00 12.40  ? 476 HOH A O     1 
HETATM 2231 O  O     . HOH D 4 .   ? 22.507  -9.404  16.079  1.00 23.73  ? 477 HOH A O     1 
HETATM 2232 O  O     . HOH D 4 .   ? 3.908   -6.624  20.450  1.00 7.85   ? 478 HOH A O     1 
HETATM 2233 O  O     . HOH D 4 .   ? 0.277   20.573  13.874  1.00 40.91  ? 479 HOH A O     1 
HETATM 2234 O  O     . HOH D 4 .   ? 13.864  7.499   6.452   1.00 17.22  ? 480 HOH A O     1 
HETATM 2235 O  O     . HOH D 4 .   ? 7.810   0.807   -6.109  1.00 34.09  ? 481 HOH A O     1 
HETATM 2236 O  O     . HOH D 4 .   ? 20.404  12.524  23.514  1.00 14.42  ? 482 HOH A O     1 
HETATM 2237 O  O     . HOH D 4 .   ? 12.512  2.270   -6.410  1.00 29.20  ? 483 HOH A O     1 
HETATM 2238 O  O     . HOH D 4 .   ? 0.993   -2.562  41.379  1.00 28.30  ? 484 HOH A O     1 
HETATM 2239 O  O     . HOH D 4 .   ? 3.490   -14.442 22.099  1.00 21.99  ? 485 HOH A O     1 
HETATM 2240 O  O     . HOH D 4 .   ? 17.416  -11.323 -2.721  1.00 21.28  ? 486 HOH A O     1 
HETATM 2241 O  O     . HOH D 4 .   ? 22.189  -9.940  25.081  1.00 26.14  ? 487 HOH A O     1 
HETATM 2242 O  O     . HOH D 4 .   ? 8.915   10.900  3.111   1.00 17.22  ? 488 HOH A O     1 
HETATM 2243 O  O     . HOH D 4 .   ? 32.512  1.378   16.054  1.00 22.47  ? 489 HOH A O     1 
HETATM 2244 O  O     . HOH D 4 .   ? 2.274   -19.324 14.913  1.00 24.02  ? 490 HOH A O     1 
HETATM 2245 O  O     . HOH D 4 .   ? 27.715  -3.961  6.811   1.00 28.50  ? 491 HOH A O     1 
HETATM 2246 O  O     . HOH D 4 .   ? 2.728   -2.059  -2.646  1.00 25.42  ? 492 HOH A O     1 
HETATM 2247 O  O     . HOH D 4 .   ? 28.813  -3.740  -0.345  1.00 42.89  ? 493 HOH A O     1 
HETATM 2248 O  O     . HOH D 4 .   ? 26.235  8.796   20.331  1.00 15.45  ? 494 HOH A O     1 
HETATM 2249 O  O     . HOH D 4 .   ? 3.005   -18.665 8.071   1.00 13.07  ? 495 HOH A O     1 
HETATM 2250 O  O     . HOH D 4 .   ? -2.337  1.502   34.558  1.00 26.41  ? 496 HOH A O     1 
HETATM 2251 O  O     . HOH D 4 .   ? 17.525  -11.481 25.227  1.00 9.96   ? 497 HOH A O     1 
HETATM 2252 O  O     . HOH D 4 .   ? -2.327  -1.330  6.768   1.00 22.02  ? 498 HOH A O     1 
HETATM 2253 O  O     . HOH D 4 .   ? -2.683  -16.109 6.216   1.00 40.43  ? 499 HOH A O     1 
HETATM 2254 O  O     . HOH D 4 .   ? -2.410  -9.363  17.064  1.00 24.56  ? 500 HOH A O     1 
HETATM 2255 O  O     . HOH D 4 .   ? 16.675  -6.687  31.283  1.00 16.27  ? 501 HOH A O     1 
HETATM 2256 O  O     . HOH D 4 .   ? 3.009   12.406  11.250  1.00 15.89  ? 502 HOH A O     1 
HETATM 2257 O  O     . HOH D 4 .   ? 18.415  -1.581  11.448  1.00 14.73  ? 503 HOH A O     1 
HETATM 2258 O  O     . HOH D 4 .   ? 19.663  19.875  16.256  1.00 38.86  ? 504 HOH A O     1 
HETATM 2259 O  O     . HOH D 4 .   ? 7.974   -15.059 26.760  1.00 12.09  ? 505 HOH A O     1 
HETATM 2260 O  O     . HOH D 4 .   ? 5.990   21.956  17.729  1.00 15.11  ? 506 HOH A O     1 
HETATM 2261 O  O     . HOH D 4 .   ? 23.478  -10.033 9.410   1.00 20.57  ? 507 HOH A O     1 
HETATM 2262 O  O     . HOH D 4 .   ? 15.778  2.155   10.098  1.00 17.95  ? 508 HOH A O     1 
HETATM 2263 O  O     . HOH D 4 .   ? 29.329  -2.069  21.144  1.00 13.04  ? 509 HOH A O     1 
HETATM 2264 O  O     . HOH D 4 .   ? -0.653  -5.393  23.647  1.00 11.42  ? 510 HOH A O     1 
HETATM 2265 O  O     . HOH D 4 .   ? 27.853  -1.631  30.130  1.00 38.96  ? 511 HOH A O     1 
HETATM 2266 O  O     . HOH D 4 .   ? 7.775   -20.280 8.812   1.00 23.97  ? 512 HOH A O     1 
HETATM 2267 O  O     . HOH D 4 .   ? 13.630  -15.178 1.559   1.00 20.19  ? 513 HOH A O     1 
HETATM 2268 O  O     . HOH D 4 .   ? 17.153  -14.094 24.445  1.00 11.79  ? 514 HOH A O     1 
HETATM 2269 O  O     . HOH D 4 .   ? 34.217  2.040   24.544  1.00 18.24  ? 515 HOH A O     1 
HETATM 2270 O  O     . HOH D 4 .   ? 18.667  9.091   11.041  1.00 44.92  ? 516 HOH A O     1 
HETATM 2271 O  O     . HOH D 4 .   ? 4.853   -10.530 24.530  1.00 12.64  ? 517 HOH A O     1 
HETATM 2272 O  O     . HOH D 4 .   ? 16.826  2.284   14.008  1.00 12.70  ? 518 HOH A O     1 
HETATM 2273 O  O     . HOH D 4 .   ? 10.364  10.147  7.743   1.00 17.39  ? 519 HOH A O     1 
HETATM 2274 O  O     . HOH D 4 .   ? -0.551  2.450   0.396   1.00 26.69  ? 520 HOH A O     1 
HETATM 2275 O  O     . HOH D 4 .   ? 34.746  7.296   19.097  1.00 31.24  ? 521 HOH A O     1 
HETATM 2276 O  O     . HOH D 4 .   ? 7.357   -16.810 14.718  1.00 14.12  ? 522 HOH A O     1 
HETATM 2277 O  O     . HOH D 4 .   ? -0.976  -12.428 18.826  1.00 32.69  ? 523 HOH A O     1 
HETATM 2278 O  O     . HOH D 4 .   ? -4.948  -4.672  33.673  1.00 59.55  ? 524 HOH A O     1 
HETATM 2279 O  O     . HOH D 4 .   ? -0.946  7.378   4.803   1.00 17.48  ? 525 HOH A O     1 
HETATM 2280 O  O     . HOH D 4 .   ? -3.962  -6.052  9.057   1.00 17.62  ? 526 HOH A O     1 
HETATM 2281 O  O     . HOH D 4 .   ? 14.957  19.221  27.816  1.00 27.53  ? 527 HOH A O     1 
HETATM 2282 O  O     . HOH D 4 .   ? 14.305  -3.401  37.558  1.00 19.49  ? 528 HOH A O     1 
HETATM 2283 O  O     . HOH D 4 .   ? -5.777  -0.872  14.404  1.00 16.70  ? 529 HOH A O     1 
HETATM 2284 O  O     . HOH D 4 .   ? 31.406  -7.084  9.118   1.00 31.78  ? 530 HOH A O     1 
HETATM 2285 O  O     . HOH D 4 .   ? 13.536  -6.894  32.739  1.00 14.65  ? 531 HOH A O     1 
HETATM 2286 O  O     . HOH D 4 .   ? 25.332  -4.990  7.943   1.00 22.98  ? 532 HOH A O     1 
HETATM 2287 O  O     . HOH D 4 .   ? 25.681  -3.154  21.020  1.00 12.02  ? 533 HOH A O     1 
HETATM 2288 O  O     . HOH D 4 .   ? -2.899  0.948   3.958   1.00 21.36  ? 534 HOH A O     1 
HETATM 2289 O  O     . HOH D 4 .   ? -5.367  -5.770  30.505  1.00 35.66  ? 535 HOH A O     1 
HETATM 2290 O  O     . HOH D 4 .   ? 19.929  5.652   -5.067  1.00 37.67  ? 536 HOH A O     1 
HETATM 2291 O  O     . HOH D 4 .   ? 1.703   11.732  8.865   1.00 13.30  ? 537 HOH A O     1 
HETATM 2292 O  O     . HOH D 4 .   ? 7.985   9.630   28.905  1.00 15.17  ? 538 HOH A O     1 
HETATM 2293 O  O     . HOH D 4 .   ? 24.658  -1.207  4.742   1.00 39.83  ? 539 HOH A O     1 
HETATM 2294 O  O     . HOH D 4 .   ? -4.825  -1.734  32.153  1.00 43.02  ? 540 HOH A O     1 
HETATM 2295 O  O     . HOH D 4 .   ? 2.922   5.811   -3.520  1.00 100.52 ? 541 HOH A O     1 
HETATM 2296 O  O     . HOH D 4 .   ? 32.007  2.922   25.874  1.00 22.04  ? 542 HOH A O     1 
HETATM 2297 O  O     . HOH D 4 .   ? 14.530  -17.590 5.969   1.00 28.50  ? 543 HOH A O     1 
HETATM 2298 O  O     . HOH D 4 .   ? -5.861  -2.195  25.211  1.00 19.45  ? 544 HOH A O     1 
HETATM 2299 O  O     . HOH D 4 .   ? -2.465  -11.626 11.249  1.00 17.87  ? 545 HOH A O     1 
HETATM 2300 O  O     . HOH D 4 .   ? 0.624   15.680  28.889  1.00 40.24  ? 546 HOH A O     1 
HETATM 2301 O  O     . HOH D 4 .   ? 16.248  -14.311 0.844   1.00 25.13  ? 547 HOH A O     1 
HETATM 2302 O  O     . HOH D 4 .   ? 12.396  -20.336 10.634  1.00 16.84  ? 548 HOH A O     1 
HETATM 2303 O  O     . HOH D 4 .   ? 8.819   4.409   31.159  1.00 12.88  ? 549 HOH A O     1 
HETATM 2304 O  O     . HOH D 4 .   ? 11.706  -8.384  -1.113  1.00 18.79  ? 550 HOH A O     1 
HETATM 2305 O  O     . HOH D 4 .   ? 22.127  10.490  24.428  1.00 14.90  ? 551 HOH A O     1 
HETATM 2306 O  O     . HOH D 4 .   ? 26.949  -9.463  15.667  1.00 33.41  ? 552 HOH A O     1 
HETATM 2307 O  O     . HOH D 4 .   ? 22.323  -4.494  34.491  1.00 22.38  ? 553 HOH A O     1 
HETATM 2308 O  O     . HOH D 4 .   ? 21.479  2.098   -6.831  1.00 24.37  ? 554 HOH A O     1 
HETATM 2309 O  O     . HOH D 4 .   ? 27.011  -11.394 -5.175  1.00 91.09  ? 555 HOH A O     1 
HETATM 2310 O  O     . HOH D 4 .   ? 3.164   -5.951  39.522  1.00 107.94 ? 556 HOH A O     1 
HETATM 2311 O  O     . HOH D 4 .   ? 9.764   2.944   33.605  1.00 16.22  ? 557 HOH A O     1 
HETATM 2312 O  O     . HOH D 4 .   ? 22.135  0.223   29.470  1.00 11.18  ? 558 HOH A O     1 
HETATM 2313 O  O     . HOH D 4 .   ? 7.215   21.691  15.208  1.00 20.83  ? 559 HOH A O     1 
HETATM 2314 O  O     . HOH D 4 .   ? 13.656  -6.902  -2.256  1.00 22.86  ? 560 HOH A O     1 
HETATM 2315 O  O     . HOH D 4 .   ? 33.818  -4.101  24.432  1.00 23.24  ? 561 HOH A O     1 
HETATM 2316 O  O     . HOH D 4 .   ? 13.857  3.331   35.279  1.00 21.19  ? 562 HOH A O     1 
HETATM 2317 O  O     . HOH D 4 .   ? -3.018  1.046   26.633  1.00 15.54  ? 563 HOH A O     1 
HETATM 2318 O  O     . HOH D 4 .   ? 20.175  -6.679  32.694  1.00 20.31  ? 564 HOH A O     1 
HETATM 2319 O  O     . HOH D 4 .   ? 18.109  7.574   -1.506  1.00 40.16  ? 565 HOH A O     1 
HETATM 2320 O  O     . HOH D 4 .   ? 12.799  -17.542 21.810  1.00 17.36  ? 566 HOH A O     1 
HETATM 2321 O  O     . HOH D 4 .   ? 36.755  4.897   15.537  1.00 25.36  ? 567 HOH A O     1 
HETATM 2322 O  O     . HOH D 4 .   ? 4.628   -8.223  33.012  1.00 16.30  ? 568 HOH A O     1 
HETATM 2323 O  O     . HOH D 4 .   ? -3.661  6.304   8.344   1.00 31.70  ? 569 HOH A O     1 
HETATM 2324 O  O     . HOH D 4 .   ? 18.159  19.569  14.363  1.00 25.39  ? 570 HOH A O     1 
HETATM 2325 O  O     . HOH D 4 .   ? 22.639  -2.616  -12.479 1.00 40.13  ? 571 HOH A O     1 
HETATM 2326 O  O     . HOH D 4 .   ? 23.648  -2.885  7.806   1.00 18.00  ? 572 HOH A O     1 
HETATM 2327 O  O     . HOH D 4 .   ? 13.779  -8.442  -4.575  1.00 26.86  ? 573 HOH A O     1 
HETATM 2328 O  O     . HOH D 4 .   ? 28.462  7.797   21.718  1.00 14.82  ? 574 HOH A O     1 
HETATM 2329 O  O     . HOH D 4 .   ? -0.279  -17.845 6.635   1.00 24.71  ? 575 HOH A O     1 
HETATM 2330 O  O     . HOH D 4 .   ? -1.392  -16.602 13.587  1.00 21.34  ? 576 HOH A O     1 
HETATM 2331 O  O     . HOH D 4 .   ? 20.602  -12.554 22.259  1.00 16.98  ? 577 HOH A O     1 
HETATM 2332 O  O     . HOH D 4 .   ? 14.348  8.159   10.593  1.00 24.73  ? 578 HOH A O     1 
HETATM 2333 O  O     . HOH D 4 .   ? 8.498   5.231   -6.812  1.00 28.98  ? 579 HOH A O     1 
HETATM 2334 O  O     . HOH D 4 .   ? 28.174  -5.946  -10.461 1.00 79.61  ? 580 HOH A O     1 
HETATM 2335 O  O     . HOH D 4 .   ? 18.833  -10.522 22.933  1.00 8.59   ? 581 HOH A O     1 
HETATM 2336 O  O     . HOH D 4 .   ? -2.123  -10.023 14.054  1.00 21.33  ? 582 HOH A O     1 
HETATM 2337 O  O     . HOH D 4 .   ? 11.267  16.759  12.173  1.00 28.16  ? 583 HOH A O     1 
HETATM 2338 O  O     . HOH D 4 .   ? 8.495   -1.447  38.558  1.00 70.56  ? 584 HOH A O     1 
HETATM 2339 O  O     . HOH D 4 .   ? 11.839  -4.022  36.061  1.00 16.18  ? 585 HOH A O     1 
HETATM 2340 O  O     . HOH D 4 .   ? 33.760  -2.157  13.496  1.00 25.08  ? 586 HOH A O     1 
HETATM 2341 O  O     . HOH D 4 .   ? 17.708  6.339   7.090   1.00 47.50  ? 587 HOH A O     1 
HETATM 2342 O  O     . HOH D 4 .   ? -2.846  1.446   31.864  1.00 28.21  ? 588 HOH A O     1 
HETATM 2343 O  O     . HOH D 4 .   ? 11.371  -6.183  34.326  1.00 18.20  ? 589 HOH A O     1 
HETATM 2344 O  O     . HOH D 4 .   ? 34.823  3.984   22.964  1.00 29.15  ? 590 HOH A O     1 
HETATM 2345 O  O     . HOH D 4 .   ? 35.386  1.729   14.983  1.00 26.90  ? 591 HOH A O     1 
HETATM 2346 O  O     . HOH D 4 .   ? 30.955  -0.961  13.890  1.00 22.06  ? 592 HOH A O     1 
HETATM 2347 O  O     . HOH D 4 .   ? 16.894  0.577   11.903  1.00 22.74  ? 593 HOH A O     1 
HETATM 2348 O  O     . HOH D 4 .   ? 4.483   16.199  33.383  1.00 29.67  ? 594 HOH A O     1 
HETATM 2349 O  O     . HOH D 4 .   ? -3.682  -7.893  1.957   1.00 26.94  ? 595 HOH A O     1 
HETATM 2350 O  O     . HOH D 4 .   ? 15.559  3.913   12.102  1.00 12.53  ? 596 HOH A O     1 
HETATM 2351 O  O     . HOH D 4 .   ? 10.093  19.309  12.151  1.00 19.59  ? 597 HOH A O     1 
HETATM 2352 O  O     . HOH D 4 .   ? 15.285  16.895  11.869  1.00 21.10  ? 598 HOH A O     1 
HETATM 2353 O  O     . HOH D 4 .   ? 15.777  5.079   -5.699  1.00 34.81  ? 599 HOH A O     1 
HETATM 2354 O  O     . HOH D 4 .   ? 2.230   -7.207  34.500  1.00 67.38  ? 600 HOH A O     1 
HETATM 2355 O  O     . HOH D 4 .   ? 30.329  3.661   12.229  1.00 23.92  ? 601 HOH A O     1 
HETATM 2356 O  O     . HOH D 4 .   ? 13.811  -18.212 24.333  1.00 115.64 ? 602 HOH A O     1 
HETATM 2357 O  O     . HOH D 4 .   ? -6.814  6.063   24.840  1.00 184.35 ? 603 HOH A O     1 
HETATM 2358 O  O     . HOH D 4 .   ? 8.040   -15.434 17.001  1.00 9.87   ? 604 HOH A O     1 
HETATM 2359 O  O     . HOH D 4 .   ? 19.299  13.126  25.964  1.00 23.48  ? 605 HOH A O     1 
HETATM 2360 O  O     . HOH D 4 .   ? -10.711 6.998   12.990  1.00 34.01  ? 606 HOH A O     1 
HETATM 2361 O  O     . HOH D 4 .   ? 22.495  -14.020 -1.505  1.00 48.42  ? 607 HOH A O     1 
HETATM 2362 O  O     . HOH D 4 .   ? 29.311  -2.896  23.758  1.00 26.47  ? 608 HOH A O     1 
HETATM 2363 O  O     . HOH D 4 .   ? -2.882  -1.733  3.714   1.00 41.65  ? 609 HOH A O     1 
HETATM 2364 O  O     . HOH D 4 .   ? 3.167   21.694  17.549  1.00 19.19  ? 610 HOH A O     1 
HETATM 2365 O  O     . HOH D 4 .   ? 20.393  15.044  27.650  1.00 43.24  ? 611 HOH A O     1 
HETATM 2366 O  O     . HOH D 4 .   ? 28.206  -2.054  -10.543 1.00 16.63  ? 612 HOH A O     1 
HETATM 2367 O  O     . HOH D 4 .   ? 16.075  22.205  21.615  1.00 17.27  ? 613 HOH A O     1 
HETATM 2368 O  O     . HOH D 4 .   ? 19.521  -11.226 27.133  1.00 20.06  ? 614 HOH A O     1 
HETATM 2369 O  O     . HOH D 4 .   ? 4.693   18.515  26.491  1.00 33.06  ? 615 HOH A O     1 
HETATM 2370 O  O     . HOH D 4 .   ? 27.379  -3.605  27.469  1.00 43.41  ? 616 HOH A O     1 
HETATM 2371 O  O     . HOH D 4 .   ? 22.542  14.228  22.855  1.00 23.40  ? 617 HOH A O     1 
HETATM 2372 O  O     . HOH D 4 .   ? 10.268  6.676   31.061  1.00 15.83  ? 618 HOH A O     1 
HETATM 2373 O  O     . HOH D 4 .   ? 19.624  4.387   -7.346  1.00 42.09  ? 619 HOH A O     1 
HETATM 2374 O  O     . HOH D 4 .   ? 4.057   -12.194 26.455  1.00 18.48  ? 620 HOH A O     1 
HETATM 2375 O  O     . HOH D 4 .   ? 36.032  0.545   26.067  1.00 21.09  ? 621 HOH A O     1 
HETATM 2376 O  O     . HOH D 4 .   ? 24.252  -12.174 12.878  1.00 34.05  ? 622 HOH A O     1 
HETATM 2377 O  O     . HOH D 4 .   ? 18.706  -10.017 31.747  1.00 29.29  ? 623 HOH A O     1 
HETATM 2378 O  O     . HOH D 4 .   ? 9.336   1.448   43.535  1.00 29.46  ? 624 HOH A O     1 
HETATM 2379 O  O     . HOH D 4 .   ? 11.705  2.534   43.140  1.00 20.17  ? 625 HOH A O     1 
HETATM 2380 O  O     . HOH D 4 .   ? 18.903  -15.770 25.791  1.00 27.81  ? 626 HOH A O     1 
HETATM 2381 O  O     . HOH D 4 .   ? 12.863  9.119   8.399   1.00 19.61  ? 627 HOH A O     1 
HETATM 2382 O  O     . HOH D 4 .   ? 30.985  -3.767  -5.395  1.00 49.48  ? 628 HOH A O     1 
HETATM 2383 O  O     . HOH D 4 .   ? 16.315  9.799   11.212  1.00 26.20  ? 629 HOH A O     1 
HETATM 2384 O  O     . HOH D 4 .   ? 19.614  -9.297  29.081  1.00 15.36  ? 630 HOH A O     1 
HETATM 2385 O  O     . HOH D 4 .   ? 15.678  -7.755  34.155  1.00 42.53  ? 631 HOH A O     1 
HETATM 2386 O  O     . HOH D 4 .   ? 17.150  -13.984 -2.158  1.00 29.40  ? 632 HOH A O     1 
HETATM 2387 O  O     . HOH D 4 .   ? 26.824  10.635  18.570  1.00 97.26  ? 633 HOH A O     1 
HETATM 2388 O  O     . HOH D 4 .   ? 22.743  4.856   -5.041  1.00 35.55  ? 634 HOH A O     1 
HETATM 2389 O  O     . HOH D 4 .   ? 8.123   -17.820 26.293  1.00 17.78  ? 635 HOH A O     1 
HETATM 2390 O  O     . HOH D 4 .   ? 26.150  10.796  21.980  1.00 36.16  ? 636 HOH A O     1 
HETATM 2391 O  O     . HOH D 4 .   ? 22.892  -12.246 20.660  1.00 21.41  ? 637 HOH A O     1 
HETATM 2392 O  O     . HOH D 4 .   ? 24.681  11.518  23.893  1.00 25.56  ? 638 HOH A O     1 
HETATM 2393 O  O     . HOH D 4 .   ? 32.633  -8.117  -0.661  1.00 24.10  ? 639 HOH A O     1 
HETATM 2394 O  O     . HOH D 4 .   ? -9.111  6.105   27.277  1.00 38.88  ? 640 HOH A O     1 
HETATM 2395 O  O     . HOH D 4 .   ? 2.669   14.797  -0.182  1.00 61.70  ? 641 HOH A O     1 
HETATM 2396 O  O     . HOH D 4 .   ? 26.094  13.064  20.217  1.00 41.62  ? 642 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . HIS A 4   ? 0.3730 0.4982 0.5025 -0.0513 0.2570  0.0678  4   HIS A N     
2    C  CA    . HIS A 4   ? 0.3543 0.4683 0.4592 -0.1645 0.2887  0.0554  4   HIS A CA    
3    C  C     . HIS A 4   ? 0.2285 0.2687 0.2230 -0.0673 0.1144  -0.0359 4   HIS A C     
4    O  O     . HIS A 4   ? 0.1891 0.2945 0.2968 0.0150  0.1345  -0.0400 4   HIS A O     
5    C  CB    . HIS A 4   ? 0.2859 0.8302 0.7917 -0.0900 0.2571  0.2213  4   HIS A CB    
6    C  CG    . HIS A 4   ? 0.6917 0.8200 1.0328 -0.0882 0.0211  0.1738  4   HIS A CG    
7    N  ND1   . HIS A 4   ? 0.8157 0.8303 1.0350 0.3927  0.0663  0.2727  4   HIS A ND1   
8    C  CD2   . HIS A 4   ? 0.8301 1.0759 1.0335 0.0093  -0.0107 0.4344  4   HIS A CD2   
9    C  CE1   . HIS A 4   ? 0.9902 0.9221 1.1146 0.1970  0.0194  0.2700  4   HIS A CE1   
10   N  NE2   . HIS A 4   ? 0.5228 0.9272 1.3356 -0.3282 0.0510  0.7087  4   HIS A NE2   
11   N  N     . TRP A 5   ? 0.1576 0.2050 0.2963 -0.0614 0.1208  -0.0190 5   TRP A N     
12   C  CA    . TRP A 5   ? 0.1503 0.1495 0.2215 -0.0051 0.0740  0.0006  5   TRP A CA    
13   C  C     . TRP A 5   ? 0.1674 0.1772 0.1981 -0.0200 0.0992  -0.0275 5   TRP A C     
14   O  O     . TRP A 5   ? 0.2016 0.2104 0.1891 -0.0445 0.0823  -0.0276 5   TRP A O     
15   C  CB    . TRP A 5   ? 0.1394 0.1338 0.2353 -0.0368 0.0969  -0.0089 5   TRP A CB    
16   C  CG    . TRP A 5   ? 0.1348 0.1787 0.2156 -0.0199 0.0965  -0.0175 5   TRP A CG    
17   C  CD1   . TRP A 5   ? 0.1580 0.2007 0.2479 -0.0496 0.0748  0.0219  5   TRP A CD1   
18   C  CD2   . TRP A 5   ? 0.1499 0.1458 0.1585 -0.0041 0.0415  -0.0114 5   TRP A CD2   
19   N  NE1   . TRP A 5   ? 0.2076 0.1332 0.1973 -0.0049 0.0706  0.0417  5   TRP A NE1   
20   C  CE2   . TRP A 5   ? 0.2029 0.1528 0.1228 -0.0136 0.0362  0.0302  5   TRP A CE2   
21   C  CE3   . TRP A 5   ? 0.1609 0.1543 0.1150 -0.0158 0.0453  -0.0347 5   TRP A CE3   
22   C  CZ2   . TRP A 5   ? 0.1921 0.2140 0.1575 0.0075  0.0304  0.0049  5   TRP A CZ2   
23   C  CZ3   . TRP A 5   ? 0.1501 0.1890 0.1453 -0.0205 0.0421  -0.0608 5   TRP A CZ3   
24   C  CH2   . TRP A 5   ? 0.1554 0.2130 0.1133 0.0101  0.0353  -0.0214 5   TRP A CH2   
25   N  N     . GLY A 6   ? 0.1449 0.1679 0.1560 -0.0073 0.0735  -0.0355 6   GLY A N     
26   C  CA    . GLY A 6   ? 0.1779 0.1585 0.1630 -0.0176 0.0624  -0.0355 6   GLY A CA    
27   C  C     . GLY A 6   ? 0.1138 0.1419 0.1866 -0.0042 0.0823  -0.0391 6   GLY A C     
28   O  O     . GLY A 6   ? 0.1247 0.1494 0.1932 0.0046  0.0745  -0.0205 6   GLY A O     
29   N  N     . TYR A 7   ? 0.1179 0.1420 0.2178 -0.0133 0.0920  -0.0452 7   TYR A N     
30   C  CA    . TYR A 7   ? 0.1337 0.1333 0.2798 0.0159  0.0948  -0.0161 7   TYR A CA    
31   C  C     . TYR A 7   ? 0.1612 0.1492 0.4911 0.0279  0.1194  -0.0574 7   TYR A C     
32   O  O     . TYR A 7   ? 0.2212 0.1235 1.1174 0.0227  0.2815  0.0202  7   TYR A O     
33   C  CB    . TYR A 7   ? 0.1359 0.1120 0.2341 -0.0066 0.0903  -0.0472 7   TYR A CB    
34   C  CG    . TYR A 7   ? 0.0744 0.1185 0.1681 -0.0208 0.0491  -0.0398 7   TYR A CG    
35   C  CD1   . TYR A 7   ? 0.0857 0.1026 0.1549 -0.0140 0.0430  -0.0344 7   TYR A CD1   
36   C  CD2   . TYR A 7   ? 0.1119 0.1416 0.1475 -0.0224 0.0532  -0.0104 7   TYR A CD2   
37   C  CE1   . TYR A 7   ? 0.0772 0.0904 0.1152 -0.0120 0.0305  -0.0050 7   TYR A CE1   
38   C  CE2   . TYR A 7   ? 0.1124 0.1421 0.0969 -0.0084 0.0377  0.0069  7   TYR A CE2   
39   C  CZ    . TYR A 7   ? 0.0907 0.0917 0.0992 -0.0238 0.0398  -0.0011 7   TYR A CZ    
40   O  OH    . TYR A 7   ? 0.1061 0.0928 0.1095 -0.0088 0.0238  -0.0062 7   TYR A OH    
41   N  N     . GLY A 8   ? 0.1314 0.1691 0.5457 0.0043  0.1168  -0.0904 8   GLY A N     
42   C  CA    . GLY A 8   ? 0.1231 0.1555 0.6065 -0.0018 0.1068  -0.1084 8   GLY A CA    
43   C  C     . GLY A 8   ? 0.2776 0.2248 0.5078 0.1005  0.2145  0.0165  8   GLY A C     
44   O  O     . GLY A 8   ? 0.2522 0.2689 0.6409 -0.0545 0.2723  -0.1070 8   GLY A O     
45   N  N     . LYS A 9   ? 0.2177 0.1554 0.8005 0.0244  0.1540  -0.0759 9   LYS A N     
46   C  CA    . LYS A 9   ? 0.3880 0.2918 0.7311 0.0757  0.0798  -0.0424 9   LYS A CA    
47   C  C     . LYS A 9   ? 0.1604 0.5750 0.5240 0.0407  -0.1074 0.1613  9   LYS A C     
48   O  O     . LYS A 9   ? 0.1255 0.2466 0.5582 -0.0279 0.1160  -0.0030 9   LYS A O     
49   C  CB    . LYS A 9   ? 0.1930 0.4502 0.5155 0.1865  0.0889  0.1657  9   LYS A CB    
50   C  CG    . LYS A 9   ? 0.7808 0.5552 0.9453 -0.0478 0.0182  -0.0816 9   LYS A CG    
51   C  CD    . LYS A 9   ? 0.9223 0.7602 1.0845 -0.0528 0.0802  -0.2331 9   LYS A CD    
52   C  CE    . LYS A 9   ? 0.9513 0.6665 0.9872 -0.1227 -0.0935 -0.5422 9   LYS A CE    
53   N  NZ    . LYS A 9   ? 0.8719 0.9720 0.8023 0.0087  -0.0997 -0.4073 9   LYS A NZ    
54   N  N     . HIS A 10  ? 0.2122 0.2714 0.5337 0.1008  0.2235  0.0196  10  HIS A N     
55   C  CA    . HIS A 10  ? 0.2147 0.2645 0.4498 0.0382  0.2335  0.0085  10  HIS A CA    
56   C  C     . HIS A 10  ? 0.1906 0.2152 0.3012 0.0139  0.1696  0.0117  10  HIS A C     
57   O  O     . HIS A 10  ? 0.1737 0.2978 0.2760 0.0947  0.0976  -0.0114 10  HIS A O     
58   C  CB    . HIS A 10  ? 0.2295 0.2374 0.3898 0.0234  0.2016  -0.0805 10  HIS A CB    
59   C  CG    . HIS A 10  ? 0.2506 0.2936 0.5698 0.0654  0.2142  0.0094  10  HIS A CG    
60   N  ND1   . HIS A 10  ? 0.3261 0.4418 0.5269 0.1150  0.2817  0.1315  10  HIS A ND1   
61   C  CD2   . HIS A 10  ? 0.1526 0.3410 0.6810 0.0423  0.1837  -0.0442 10  HIS A CD2   
62   C  CE1   . HIS A 10  ? 0.4240 0.4553 0.8112 0.2422  -0.0989 0.2196  10  HIS A CE1   
63   N  NE2   . HIS A 10  ? 0.2084 0.2124 0.7184 0.0573  0.2598  -0.0831 10  HIS A NE2   
64   N  N     . ASN A 11  ? 0.1911 0.1648 0.3368 -0.0010 0.1672  0.0038  11  ASN A N     
65   C  CA    . ASN A 11  ? 0.1394 0.1895 0.2446 0.0236  0.0823  -0.0098 11  ASN A CA    
66   C  C     . ASN A 11  ? 0.1382 0.1898 0.2295 0.0338  0.0788  0.0218  11  ASN A C     
67   O  O     . ASN A 11  ? 0.1652 0.1860 0.2362 0.0485  0.0938  0.0295  11  ASN A O     
68   C  CB    . ASN A 11  ? 0.1448 0.1924 0.1931 0.0025  0.1090  -0.0319 11  ASN A CB    
69   C  CG    . ASN A 11  ? 0.1696 0.2529 0.2183 0.0025  0.1195  -0.0442 11  ASN A CG    
70   O  OD1   . ASN A 11  ? 0.1371 0.2524 0.3423 -0.0006 0.0852  0.0027  11  ASN A OD1   
71   N  ND2   . ASN A 11  ? 0.2082 0.2888 0.2485 -0.0607 0.0795  -0.0421 11  ASN A ND2   
72   N  N     . GLY A 12  ? 0.1301 0.1844 0.2182 0.0359  0.1017  -0.0023 12  GLY A N     
73   C  CA    . GLY A 12  ? 0.1086 0.2136 0.1950 0.0386  0.0799  -0.0219 12  GLY A CA    
74   C  C     . GLY A 12  ? 0.1353 0.1758 0.1725 -0.0099 0.0489  0.0017  12  GLY A C     
75   O  O     . GLY A 12  ? 0.0989 0.1692 0.2009 0.0301  0.0526  0.0149  12  GLY A O     
76   N  N     . PRO A 13  ? 0.1303 0.1286 0.1807 0.0138  0.0615  -0.0155 13  PRO A N     
77   C  CA    . PRO A 13  ? 0.1379 0.1057 0.1817 0.0126  0.0757  0.0051  13  PRO A CA    
78   C  C     . PRO A 13  ? 0.1385 0.0914 0.1753 0.0018  0.0624  0.0058  13  PRO A C     
79   O  O     . PRO A 13  ? 0.1116 0.1445 0.1842 -0.0056 0.0496  -0.0158 13  PRO A O     
80   C  CB    . PRO A 13  ? 0.1431 0.1450 0.1717 -0.0057 0.0797  0.0068  13  PRO A CB    
81   C  CG    . PRO A 13  ? 0.1625 0.1558 0.1670 0.0093  0.0704  -0.0089 13  PRO A CG    
82   C  CD    . PRO A 13  ? 0.1374 0.1719 0.1714 0.0109  0.0550  -0.0214 13  PRO A CD    
83   N  N     A GLU A 14  ? 0.1477 0.1313 0.2336 0.0321  0.0547  0.0082  14  GLU A N     
84   N  N     B GLU A 14  ? 0.1305 0.1153 0.2317 0.0115  0.0568  0.0398  14  GLU A N     
85   C  CA    A GLU A 14  ? 0.1856 0.1658 0.1996 0.0526  0.0739  0.0129  14  GLU A CA    
86   C  CA    B GLU A 14  ? 0.1464 0.1257 0.2139 0.0260  0.0690  0.0112  14  GLU A CA    
87   C  C     A GLU A 14  ? 0.1401 0.1433 0.1951 0.0759  0.0388  0.0328  14  GLU A C     
88   C  C     B GLU A 14  ? 0.1147 0.1258 0.1986 0.0478  0.0457  0.0430  14  GLU A C     
89   O  O     A GLU A 14  ? 0.1675 0.1629 0.2426 0.0406  0.0316  0.0389  14  GLU A O     
90   O  O     B GLU A 14  ? 0.1525 0.1283 0.2308 0.0445  0.0333  0.0262  14  GLU A O     
91   C  CB    A GLU A 14  ? 0.2576 0.1794 0.2345 0.0722  -0.0175 0.0363  14  GLU A CB    
92   C  CB    B GLU A 14  ? 0.1851 0.1198 0.2538 -0.0017 -0.0297 0.0456  14  GLU A CB    
93   C  CG    A GLU A 14  ? 0.1404 0.1466 0.2994 0.0552  -0.0348 0.0179  14  GLU A CG    
94   C  CG    B GLU A 14  ? 0.2507 0.1489 0.2362 -0.0230 0.0404  0.0589  14  GLU A CG    
95   C  CD    A GLU A 14  ? 0.1773 0.1181 0.3464 0.0692  -0.0513 0.0081  14  GLU A CD    
96   C  CD    B GLU A 14  ? 0.2233 0.2003 0.2384 0.0832  -0.0154 0.0244  14  GLU A CD    
97   O  OE1   A GLU A 14  ? 0.1586 0.1310 0.1775 0.0841  -0.0434 -0.0937 14  GLU A OE1   
98   O  OE1   B GLU A 14  ? 0.1807 0.2928 0.3232 0.0269  -0.0632 -0.0560 14  GLU A OE1   
99   O  OE2   A GLU A 14  ? 0.3288 0.0656 0.2268 0.0134  0.0289  -0.0088 14  GLU A OE2   
100  O  OE2   B GLU A 14  ? 0.2222 0.2586 0.3329 0.1454  0.0349  -0.0454 14  GLU A OE2   
101  N  N     . HIS A 15  ? 0.0763 0.1827 0.1804 0.0483  0.0239  0.0289  15  HIS A N     
102  C  CA    . HIS A 15  ? 0.0863 0.1503 0.2259 0.0379  0.0443  0.0031  15  HIS A CA    
103  C  C     . HIS A 15  ? 0.0590 0.1536 0.2046 0.0207  0.0370  -0.0051 15  HIS A C     
104  O  O     . HIS A 15  ? 0.0468 0.1781 0.2434 0.0159  0.0356  0.0317  15  HIS A O     
105  C  CB    . HIS A 15  ? 0.0562 0.1595 0.2376 0.0332  0.0314  0.0046  15  HIS A CB    
106  C  CG    . HIS A 15  ? 0.1053 0.1893 0.2328 0.0642  0.0595  0.0233  15  HIS A CG    
107  N  ND1   . HIS A 15  ? 0.1216 0.2833 0.2167 0.1284  0.0154  0.0125  15  HIS A ND1   
108  C  CD2   . HIS A 15  ? 0.1813 0.1887 0.2897 0.0803  0.0950  -0.0146 15  HIS A CD2   
109  C  CE1   . HIS A 15  ? 0.2501 0.3404 0.2544 0.1921  0.0087  -0.0299 15  HIS A CE1   
110  N  NE2   . HIS A 15  ? 0.3039 0.2182 0.2882 0.1686  0.0553  -0.0333 15  HIS A NE2   
111  N  N     . TRP A 16  ? 0.0537 0.1326 0.1864 0.0119  0.0344  0.0038  16  TRP A N     
112  C  CA    . TRP A 16  ? 0.0352 0.1196 0.1758 0.0076  0.0223  -0.0074 16  TRP A CA    
113  C  C     . TRP A 16  ? 0.0510 0.1265 0.1630 0.0154  0.0101  0.0045  16  TRP A C     
114  O  O     . TRP A 16  ? 0.0453 0.1276 0.1943 0.0051  -0.0111 -0.0041 16  TRP A O     
115  C  CB    . TRP A 16  ? 0.0341 0.1199 0.1653 0.0054  0.0277  -0.0108 16  TRP A CB    
116  C  CG    . TRP A 16  ? 0.0550 0.1272 0.1449 0.0146  0.0227  -0.0059 16  TRP A CG    
117  C  CD1   . TRP A 16  ? 0.0973 0.1440 0.1419 -0.0076 0.0461  0.0019  16  TRP A CD1   
118  C  CD2   . TRP A 16  ? 0.0542 0.1040 0.1529 0.0205  0.0265  -0.0241 16  TRP A CD2   
119  N  NE1   . TRP A 16  ? 0.0890 0.1463 0.1470 0.0133  0.0522  -0.0350 16  TRP A NE1   
120  C  CE2   . TRP A 16  ? 0.0670 0.1010 0.1395 -0.0005 0.0352  0.0010  16  TRP A CE2   
121  C  CE3   . TRP A 16  ? 0.0446 0.0986 0.1448 0.0045  0.0188  -0.0181 16  TRP A CE3   
122  C  CZ2   . TRP A 16  ? 0.0842 0.1091 0.1478 -0.0078 0.0289  -0.0270 16  TRP A CZ2   
123  C  CZ3   . TRP A 16  ? 0.0375 0.1130 0.1423 -0.0020 0.0376  -0.0140 16  TRP A CZ3   
124  C  CH2   . TRP A 16  ? 0.0815 0.1016 0.1347 -0.0087 0.0332  -0.0030 16  TRP A CH2   
125  N  N     . HIS A 17  ? 0.0496 0.1536 0.1623 0.0306  -0.0032 0.0032  17  HIS A N     
126  C  CA    . HIS A 17  ? 0.0543 0.1739 0.1739 -0.0035 0.0116  0.0162  17  HIS A CA    
127  C  C     . HIS A 17  ? 0.0420 0.1856 0.1650 0.0080  0.0006  0.0273  17  HIS A C     
128  O  O     . HIS A 17  ? 0.0489 0.1973 0.2003 -0.0072 -0.0027 0.0090  17  HIS A O     
129  C  CB    . HIS A 17  ? 0.0609 0.1948 0.1709 0.0019  0.0105  0.0151  17  HIS A CB    
130  C  CG    . HIS A 17  ? 0.0662 0.1862 0.2019 0.0094  0.0000  0.0477  17  HIS A CG    
131  N  ND1   . HIS A 17  ? 0.0928 0.2383 0.2479 0.0195  -0.0184 0.0488  17  HIS A ND1   
132  C  CD2   . HIS A 17  ? 0.0899 0.2184 0.2096 0.0506  0.0504  0.0454  17  HIS A CD2   
133  C  CE1   . HIS A 17  ? 0.0666 0.3286 0.2449 0.0814  0.0190  0.0821  17  HIS A CE1   
134  N  NE2   . HIS A 17  ? 0.1108 0.2175 0.2650 0.0847  0.0345  0.0455  17  HIS A NE2   
135  N  N     . LYS A 18  ? 0.0462 0.1963 0.1959 0.0013  0.0020  0.0175  18  LYS A N     
136  C  CA    . LYS A 18  ? 0.0422 0.2252 0.2159 0.0011  -0.0030 0.0476  18  LYS A CA    
137  C  C     . LYS A 18  ? 0.0604 0.2236 0.2135 -0.0463 -0.0153 0.0390  18  LYS A C     
138  O  O     . LYS A 18  ? 0.0996 0.2441 0.3807 -0.0915 -0.0913 0.1001  18  LYS A O     
139  C  CB    . LYS A 18  ? 0.0790 0.2373 0.2525 0.0464  0.0012  0.0459  18  LYS A CB    
140  C  CG    . LYS A 18  ? 0.0822 0.2297 0.2325 0.0335  0.0225  0.0531  18  LYS A CG    
141  C  CD    . LYS A 18  ? 0.0870 0.3002 0.1999 0.0591  -0.0017 0.0715  18  LYS A CD    
142  C  CE    . LYS A 18  ? 0.0854 0.2504 0.2359 0.0571  0.0312  0.0830  18  LYS A CE    
143  N  NZ    . LYS A 18  ? 0.0701 0.2581 0.2574 0.0766  0.0350  0.0638  18  LYS A NZ    
144  N  N     . ASP A 19  ? 0.0513 0.2016 0.1975 -0.0120 0.0040  0.0337  19  ASP A N     
145  C  CA    . ASP A 19  ? 0.0676 0.1811 0.2210 -0.0030 0.0231  0.0213  19  ASP A CA    
146  C  C     . ASP A 19  ? 0.0680 0.1514 0.2271 -0.0117 0.0199  0.0199  19  ASP A C     
147  O  O     . ASP A 19  ? 0.0940 0.1620 0.2490 -0.0313 0.0322  0.0478  19  ASP A O     
148  C  CB    . ASP A 19  ? 0.1023 0.2105 0.2113 0.0139  0.0168  0.0216  19  ASP A CB    
149  C  CG    . ASP A 19  ? 0.1517 0.3655 0.3019 -0.0089 0.0677  -0.0736 19  ASP A CG    
150  O  OD1   . ASP A 19  ? 0.2421 0.3831 0.3570 -0.0823 0.1813  -0.0492 19  ASP A OD1   
151  O  OD2   . ASP A 19  ? 0.3060 0.5467 0.5533 -0.1108 0.1001  -0.2827 19  ASP A OD2   
152  N  N     . PHE A 20  ? 0.0721 0.1392 0.1811 0.0110  0.0138  0.0186  20  PHE A N     
153  C  CA    . PHE A 20  ? 0.0463 0.1479 0.1897 0.0015  0.0124  0.0023  20  PHE A CA    
154  C  C     . PHE A 20  ? 0.0719 0.1766 0.1777 -0.0225 0.0049  0.0121  20  PHE A C     
155  O  O     . PHE A 20  ? 0.0751 0.1357 0.1762 -0.0161 0.0106  0.0061  20  PHE A O     
156  C  CB    . PHE A 20  ? 0.0651 0.1297 0.1800 -0.0045 -0.0047 0.0092  20  PHE A CB    
157  C  CG    . PHE A 20  ? 0.0451 0.1749 0.1884 -0.0416 -0.0054 0.0049  20  PHE A CG    
158  C  CD1   . PHE A 20  ? 0.0948 0.1822 0.2250 -0.0392 0.0151  0.0458  20  PHE A CD1   
159  C  CD2   . PHE A 20  ? 0.0856 0.2215 0.1928 -0.0538 0.0051  0.0059  20  PHE A CD2   
160  C  CE1   . PHE A 20  ? 0.0983 0.2468 0.2439 -0.0374 0.0002  0.0425  20  PHE A CE1   
161  C  CE2   . PHE A 20  ? 0.0954 0.2924 0.2002 -0.0247 0.0183  0.0258  20  PHE A CE2   
162  C  CZ    . PHE A 20  ? 0.0739 0.2780 0.2270 -0.0739 0.0140  0.0734  20  PHE A CZ    
163  N  N     . PRO A 21  ? 0.0702 0.1469 0.1897 -0.0183 0.0089  0.0023  21  PRO A N     
164  C  CA    . PRO A 21  ? 0.0612 0.1758 0.1872 -0.0374 -0.0123 0.0168  21  PRO A CA    
165  C  C     . PRO A 21  ? 0.0606 0.1530 0.1863 -0.0284 -0.0204 -0.0135 21  PRO A C     
166  O  O     . PRO A 21  ? 0.0785 0.1786 0.1815 -0.0135 -0.0184 0.0049  21  PRO A O     
167  C  CB    . PRO A 21  ? 0.0665 0.2940 0.1948 -0.0988 -0.0242 0.0255  21  PRO A CB    
168  C  CG    . PRO A 21  ? 0.2537 0.2448 0.2589 -0.1395 -0.0703 0.0171  21  PRO A CG    
169  C  CD    . PRO A 21  ? 0.0941 0.1956 0.2161 -0.0345 -0.0131 0.0402  21  PRO A CD    
170  N  N     A ILE A 22  ? 0.0672 0.1347 0.1614 -0.0277 -0.0188 -0.0180 22  ILE A N     
171  N  N     B ILE A 22  ? 0.0695 0.1349 0.1736 -0.0247 -0.0165 -0.0207 22  ILE A N     
172  C  CA    A ILE A 22  ? 0.0811 0.1196 0.1438 -0.0112 -0.0080 0.0024  22  ILE A CA    
173  C  CA    B ILE A 22  ? 0.0803 0.1289 0.1590 -0.0153 -0.0103 -0.0016 22  ILE A CA    
174  C  C     A ILE A 22  ? 0.0565 0.1132 0.1353 0.0011  -0.0076 -0.0054 22  ILE A C     
175  C  C     B ILE A 22  ? 0.0586 0.1104 0.1498 0.0100  -0.0109 -0.0082 22  ILE A C     
176  O  O     A ILE A 22  ? 0.0752 0.1472 0.1064 0.0038  0.0066  -0.0075 22  ILE A O     
177  O  O     B ILE A 22  ? 0.0468 0.1510 0.1720 -0.0391 -0.0151 -0.0111 22  ILE A O     
178  C  CB    A ILE A 22  ? 0.0530 0.1152 0.1522 -0.0101 -0.0086 -0.0115 22  ILE A CB    
179  C  CB    B ILE A 22  ? 0.0790 0.1305 0.1539 -0.0050 -0.0080 -0.0081 22  ILE A CB    
180  C  CG1   A ILE A 22  ? 0.0868 0.1189 0.1459 -0.0077 -0.0047 -0.0261 22  ILE A CG1   
181  C  CG1   B ILE A 22  ? 0.1175 0.1624 0.1961 0.0159  0.0167  -0.0328 22  ILE A CG1   
182  C  CG2   A ILE A 22  ? 0.0511 0.1148 0.1492 -0.0139 -0.0167 -0.0065 22  ILE A CG2   
183  C  CG2   B ILE A 22  ? 0.0900 0.1109 0.1543 0.0059  -0.0226 -0.0089 22  ILE A CG2   
184  C  CD1   A ILE A 22  ? 0.1098 0.1292 0.1734 -0.0085 0.0000  0.0189  22  ILE A CD1   
185  C  CD1   B ILE A 22  ? 0.2122 0.1744 0.1909 0.0115  0.0094  -0.0407 22  ILE A CD1   
186  N  N     . ALA A 23  ? 0.0622 0.1224 0.1315 -0.0072 0.0045  -0.0002 23  ALA A N     
187  C  CA    . ALA A 23  ? 0.0521 0.1197 0.1410 -0.0122 0.0027  -0.0127 23  ALA A CA    
188  C  C     . ALA A 23  ? 0.0473 0.1340 0.1538 -0.0033 -0.0064 0.0004  23  ALA A C     
189  O  O     . ALA A 23  ? 0.0761 0.1406 0.1681 -0.0169 -0.0011 0.0131  23  ALA A O     
190  C  CB    . ALA A 23  ? 0.0632 0.1172 0.1528 -0.0010 -0.0263 -0.0128 23  ALA A CB    
191  N  N     . LYS A 24  ? 0.0665 0.1471 0.1273 -0.0008 -0.0119 0.0043  24  LYS A N     
192  C  CA    . LYS A 24  ? 0.0822 0.1571 0.1399 -0.0002 -0.0203 0.0110  24  LYS A CA    
193  C  C     . LYS A 24  ? 0.0717 0.1938 0.1454 -0.0057 -0.0198 -0.0017 24  LYS A C     
194  O  O     . LYS A 24  ? 0.0945 0.2496 0.1623 -0.0033 -0.0369 -0.0074 24  LYS A O     
195  C  CB    . LYS A 24  ? 0.1020 0.1898 0.1703 0.0281  -0.0224 0.0290  24  LYS A CB    
196  C  CG    . LYS A 24  ? 0.1178 0.2478 0.1565 0.0404  -0.0204 0.0271  24  LYS A CG    
197  C  CD    . LYS A 24  ? 0.1342 0.3127 0.2517 0.0838  -0.0079 0.0691  24  LYS A CD    
198  C  CE    . LYS A 24  ? 0.1651 0.4801 0.2721 0.1883  0.0301  0.0364  24  LYS A CE    
199  N  NZ    . LYS A 24  ? 0.4965 0.3608 0.5372 0.1013  0.0529  -0.0189 24  LYS A NZ    
200  N  N     . GLY A 25  ? 0.0675 0.1715 0.1656 -0.0083 -0.0278 -0.0208 25  GLY A N     
201  C  CA    . GLY A 25  ? 0.0717 0.2011 0.1636 -0.0209 -0.0095 -0.0284 25  GLY A CA    
202  C  C     . GLY A 25  ? 0.0704 0.2085 0.1271 0.0021  -0.0190 -0.0113 25  GLY A C     
203  O  O     . GLY A 25  ? 0.0925 0.2003 0.1529 -0.0013 -0.0217 0.0002  25  GLY A O     
204  N  N     . GLU A 26  ? 0.0789 0.1927 0.1446 -0.0209 -0.0229 -0.0152 26  GLU A N     
205  C  CA    . GLU A 26  ? 0.0882 0.2316 0.1210 -0.0064 -0.0172 -0.0244 26  GLU A CA    
206  C  C     . GLU A 26  ? 0.0809 0.1817 0.1184 0.0040  -0.0169 -0.0092 26  GLU A C     
207  O  O     . GLU A 26  ? 0.1062 0.2311 0.1126 -0.0235 -0.0171 0.0002  26  GLU A O     
208  C  CB    . GLU A 26  ? 0.1344 0.2772 0.1494 -0.0545 -0.0360 -0.0444 26  GLU A CB    
209  C  CG    . GLU A 26  ? 0.1427 0.2999 0.1581 -0.0214 -0.0558 -0.0255 26  GLU A CG    
210  C  CD    . GLU A 26  ? 0.1626 0.3655 0.2357 -0.0133 -0.1019 0.0028  26  GLU A CD    
211  O  OE1   . GLU A 26  ? 0.3526 0.3945 0.3047 -0.0622 -0.1143 0.0422  26  GLU A OE1   
212  O  OE2   . GLU A 26  ? 0.2313 0.5127 0.3689 0.1278  -0.0681 0.0460  26  GLU A OE2   
213  N  N     . ARG A 27  ? 0.0815 0.1021 0.1163 -0.0204 -0.0212 -0.0120 27  ARG A N     
214  C  CA    . ARG A 27  ? 0.0772 0.1052 0.1047 0.0041  -0.0142 -0.0194 27  ARG A CA    
215  C  C     . ARG A 27  ? 0.0614 0.1058 0.0915 0.0036  -0.0057 -0.0151 27  ARG A C     
216  O  O     . ARG A 27  ? 0.0694 0.1171 0.0963 0.0039  -0.0203 -0.0125 27  ARG A O     
217  C  CB    . ARG A 27  ? 0.1562 0.1515 0.1078 0.0267  -0.0483 -0.0571 27  ARG A CB    
218  C  CG    . ARG A 27  ? 0.2121 0.2329 0.1997 0.0256  -0.0390 -0.0237 27  ARG A CG    
219  C  CD    . ARG A 27  ? 0.2076 0.3293 0.2665 0.1081  -0.0268 0.0550  27  ARG A CD    
220  N  NE    . ARG A 27  ? 0.2011 0.1512 0.1729 -0.0243 0.0575  -0.0410 27  ARG A NE    
221  C  CZ    . ARG A 27  ? 0.1491 0.2454 0.1628 -0.0056 0.0031  -0.0167 27  ARG A CZ    
222  N  NH1   . ARG A 27  ? 0.1253 0.2722 0.2536 0.0192  0.0184  -0.1143 27  ARG A NH1   
223  N  NH2   . ARG A 27  ? 0.1665 0.2587 0.2245 -0.0283 -0.0196 -0.0429 27  ARG A NH2   
224  N  N     . GLN A 28  ? 0.0543 0.0996 0.0960 -0.0066 -0.0032 -0.0130 28  GLN A N     
225  C  CA    . GLN A 28  ? 0.0552 0.0839 0.0932 -0.0091 -0.0025 -0.0083 28  GLN A CA    
226  C  C     . GLN A 28  ? 0.0594 0.0953 0.0878 -0.0122 -0.0013 -0.0058 28  GLN A C     
227  O  O     . GLN A 28  ? 0.0571 0.1154 0.0846 -0.0167 0.0015  0.0021  28  GLN A O     
228  C  CB    . GLN A 28  ? 0.0527 0.1213 0.0855 -0.0017 -0.0052 0.0060  28  GLN A CB    
229  C  CG    . GLN A 28  ? 0.0578 0.1138 0.0994 -0.0101 0.0074  -0.0168 28  GLN A CG    
230  C  CD    . GLN A 28  ? 0.0511 0.1066 0.1098 -0.0217 0.0048  -0.0144 28  GLN A CD    
231  O  OE1   . GLN A 28  ? 0.0720 0.1044 0.1035 -0.0165 0.0014  -0.0008 28  GLN A OE1   
232  N  NE2   . GLN A 28  ? 0.0497 0.1141 0.1011 -0.0124 0.0000  -0.0129 28  GLN A NE2   
233  N  N     . SER A 29  ? 0.0562 0.0833 0.0840 -0.0033 0.0023  -0.0013 29  SER A N     
234  C  CA    . SER A 29  ? 0.0621 0.0725 0.0785 -0.0041 0.0032  -0.0025 29  SER A CA    
235  C  C     . SER A 29  ? 0.0550 0.0796 0.0862 0.0036  -0.0049 -0.0056 29  SER A C     
236  O  O     . SER A 29  ? 0.0705 0.0939 0.0927 0.0012  0.0079  -0.0155 29  SER A O     
237  C  CB    . SER A 29  ? 0.0764 0.0768 0.0750 -0.0022 -0.0079 -0.0013 29  SER A CB    
238  O  OG    . SER A 29  ? 0.0567 0.0784 0.0872 -0.0052 0.0037  -0.0130 29  SER A OG    
239  N  N     . PRO A 30  ? 0.0414 0.0931 0.0730 -0.0015 0.0015  -0.0086 30  PRO A N     
240  C  CA    . PRO A 30  ? 0.0492 0.0797 0.0748 0.0039  0.0027  0.0025  30  PRO A CA    
241  C  C     . PRO A 30  ? 0.0590 0.0740 0.0653 -0.0021 0.0001  0.0044  30  PRO A C     
242  O  O     . PRO A 30  ? 0.0613 0.0883 0.0820 0.0052  -0.0067 0.0082  30  PRO A O     
243  C  CB    . PRO A 30  ? 0.0445 0.0820 0.0785 -0.0014 0.0096  0.0021  30  PRO A CB    
244  C  CG    . PRO A 30  ? 0.0465 0.1030 0.0769 -0.0023 0.0091  0.0031  30  PRO A CG    
245  C  CD    . PRO A 30  ? 0.0696 0.0857 0.0763 -0.0012 0.0134  -0.0048 30  PRO A CD    
246  N  N     . VAL A 31  ? 0.0579 0.0849 0.0760 -0.0072 0.0027  0.0101  31  VAL A N     
247  C  CA    . VAL A 31  ? 0.0587 0.0877 0.0771 -0.0030 0.0082  0.0159  31  VAL A CA    
248  C  C     . VAL A 31  ? 0.0839 0.0928 0.0715 -0.0076 0.0008  0.0254  31  VAL A C     
249  O  O     . VAL A 31  ? 0.0799 0.0873 0.0940 0.0005  -0.0060 0.0272  31  VAL A O     
250  C  CB    . VAL A 31  ? 0.0734 0.0863 0.0877 0.0031  -0.0030 0.0071  31  VAL A CB    
251  C  CG1   . VAL A 31  ? 0.0975 0.0956 0.0879 -0.0003 0.0132  -0.0113 31  VAL A CG1   
252  C  CG2   . VAL A 31  ? 0.0784 0.0924 0.1033 0.0049  0.0105  -0.0050 31  VAL A CG2   
253  N  N     . ASP A 32  ? 0.0790 0.0812 0.0701 -0.0004 -0.0094 0.0138  32  ASP A N     
254  C  CA    . ASP A 32  ? 0.0851 0.0757 0.0846 0.0000  0.0077  0.0066  32  ASP A CA    
255  C  C     . ASP A 32  ? 0.0942 0.1079 0.0694 0.0217  -0.0068 0.0147  32  ASP A C     
256  O  O     . ASP A 32  ? 0.0841 0.1148 0.1007 0.0025  -0.0072 -0.0035 32  ASP A O     
257  C  CB    . ASP A 32  ? 0.0875 0.1061 0.0794 0.0128  0.0195  0.0180  32  ASP A CB    
258  C  CG    . ASP A 32  ? 0.1095 0.1076 0.1052 0.0101  0.0200  0.0272  32  ASP A CG    
259  O  OD1   . ASP A 32  ? 0.1201 0.1000 0.1053 -0.0081 -0.0006 0.0197  32  ASP A OD1   
260  O  OD2   . ASP A 32  ? 0.1624 0.1318 0.1023 -0.0074 0.0097  0.0388  32  ASP A OD2   
261  N  N     . ILE A 33  ? 0.0819 0.0762 0.0744 0.0119  0.0051  0.0068  33  ILE A N     
262  C  CA    . ILE A 33  ? 0.0812 0.0838 0.0885 0.0007  0.0149  0.0054  33  ILE A CA    
263  C  C     . ILE A 33  ? 0.0925 0.0965 0.0843 0.0199  0.0197  0.0220  33  ILE A C     
264  O  O     . ILE A 33  ? 0.1147 0.1064 0.0970 0.0032  0.0242  0.0251  33  ILE A O     
265  C  CB    . ILE A 33  ? 0.0797 0.0782 0.0975 0.0173  0.0118  0.0086  33  ILE A CB    
266  C  CG1   . ILE A 33  ? 0.0853 0.1085 0.1067 0.0132  0.0082  0.0330  33  ILE A CG1   
267  C  CG2   . ILE A 33  ? 0.1080 0.1518 0.1184 0.0342  0.0206  0.0109  33  ILE A CG2   
268  C  CD1   . ILE A 33  ? 0.0903 0.1250 0.1411 0.0036  -0.0155 0.0396  33  ILE A CD1   
269  N  N     A ASP A 34  ? 0.1497 0.0819 0.0768 0.0159  0.0276  0.0112  34  ASP A N     
270  N  N     B ASP A 34  ? 0.1421 0.1093 0.0903 0.0051  0.0024  0.0309  34  ASP A N     
271  C  CA    A ASP A 34  ? 0.1598 0.1121 0.0562 0.0182  0.0299  0.0244  34  ASP A CA    
272  C  CA    B ASP A 34  ? 0.1737 0.1178 0.0677 0.0197  0.0208  0.0303  34  ASP A CA    
273  C  C     A ASP A 34  ? 0.1737 0.1238 0.0649 0.0201  0.0482  0.0235  34  ASP A C     
274  C  C     B ASP A 34  ? 0.1783 0.1113 0.0880 0.0234  0.0290  0.0465  34  ASP A C     
275  O  O     A ASP A 34  ? 0.2154 0.1618 0.0838 0.0421  0.0325  -0.0100 34  ASP A O     
276  O  O     B ASP A 34  ? 0.1985 0.1366 0.0829 0.0586  0.0517  0.0428  34  ASP A O     
277  C  CB    A ASP A 34  ? 0.1824 0.1294 0.0919 0.0298  0.0100  0.0494  34  ASP A CB    
278  C  CB    B ASP A 34  ? 0.2049 0.1411 0.0977 0.0458  0.0028  0.0268  34  ASP A CB    
279  C  CG    A ASP A 34  ? 0.1463 0.1528 0.1251 0.0052  0.0083  0.0698  34  ASP A CG    
280  C  CG    B ASP A 34  ? 0.2164 0.1433 0.1171 0.0339  0.0166  0.0326  34  ASP A CG    
281  O  OD1   A ASP A 34  ? 0.1439 0.2342 0.1414 -0.0137 -0.0153 0.1064  34  ASP A OD1   
282  O  OD1   B ASP A 34  ? 0.2871 0.1182 0.1471 0.0622  -0.0030 0.0499  34  ASP A OD1   
283  O  OD2   A ASP A 34  ? 0.1698 0.1955 0.1294 -0.0027 -0.0011 0.1004  34  ASP A OD2   
284  O  OD2   B ASP A 34  ? 0.3681 0.1551 0.1382 0.0903  0.0757  0.0492  34  ASP A OD2   
285  N  N     . THR A 35  ? 0.1393 0.1322 0.1108 0.0314  0.0499  0.0343  35  THR A N     
286  C  CA    . THR A 35  ? 0.1456 0.1702 0.1096 0.0719  0.0371  0.0432  35  THR A CA    
287  C  C     . THR A 35  ? 0.1618 0.2089 0.1312 0.0640  0.0760  0.0627  35  THR A C     
288  O  O     . THR A 35  ? 0.2256 0.3174 0.1558 0.1406  0.0828  0.0513  35  THR A O     
289  C  CB    . THR A 35  ? 0.1325 0.1862 0.1615 0.0549  0.0356  0.0671  35  THR A CB    
290  O  OG1   . THR A 35  ? 0.1564 0.1657 0.1423 0.0143  0.0510  0.0440  35  THR A OG1   
291  C  CG2   . THR A 35  ? 0.2014 0.2036 0.1402 0.0736  0.0329  0.0269  35  THR A CG2   
292  N  N     . HIS A 36  ? 0.2172 0.1329 0.1195 0.0273  0.0593  0.0516  36  HIS A N     
293  C  CA    . HIS A 36  ? 0.2289 0.2009 0.1348 -0.0164 0.0516  0.0859  36  HIS A CA    
294  C  C     . HIS A 36  ? 0.3070 0.2576 0.0922 0.0302  0.0340  0.0584  36  HIS A C     
295  O  O     . HIS A 36  ? 0.5880 0.4036 0.1317 -0.1497 0.1502  -0.0546 36  HIS A O     
296  C  CB    . HIS A 36  ? 0.2921 0.2152 0.1008 -0.0044 0.0432  0.0708  36  HIS A CB    
297  C  CG    . HIS A 36  ? 0.6071 0.1795 0.2512 0.0224  -0.1474 0.0300  36  HIS A CG    
298  N  ND1   . HIS A 36  ? 0.6570 0.3037 0.1561 0.1451  -0.0295 0.1105  36  HIS A ND1   
299  C  CD2   . HIS A 36  ? 0.6635 0.2455 0.2749 -0.0753 -0.2203 0.1055  36  HIS A CD2   
300  C  CE1   . HIS A 36  ? 0.8983 0.2441 0.4317 0.0988  -0.2575 0.1482  36  HIS A CE1   
301  N  NE2   . HIS A 36  ? 0.8473 0.3657 0.3538 0.0069  -0.2973 -0.0134 36  HIS A NE2   
302  N  N     . THR A 37  ? 0.2563 0.1583 0.1135 0.0499  0.0425  0.0135  37  THR A N     
303  C  CA    . THR A 37  ? 0.2074 0.1775 0.1442 0.0419  0.0487  0.0201  37  THR A CA    
304  C  C     . THR A 37  ? 0.2323 0.2033 0.0985 0.0806  0.0214  0.0023  37  THR A C     
305  O  O     . THR A 37  ? 0.3663 0.2543 0.1025 0.0944  -0.0376 -0.0233 37  THR A O     
306  C  CB    . THR A 37  ? 0.1862 0.2358 0.2642 0.0605  0.0518  0.0106  37  THR A CB    
307  O  OG1   . THR A 37  ? 0.2476 0.2501 0.2120 0.0692  0.0304  0.0174  37  THR A OG1   
308  C  CG2   . THR A 37  ? 0.2775 0.1987 0.3965 0.0591  -0.0068 0.0017  37  THR A CG2   
309  N  N     . ALA A 38  ? 0.2569 0.1553 0.0781 0.0493  0.0184  0.0129  38  ALA A N     
310  C  CA    . ALA A 38  ? 0.1902 0.1775 0.1092 0.0531  0.0282  0.0237  38  ALA A CA    
311  C  C     . ALA A 38  ? 0.2279 0.1891 0.2017 0.0512  0.0793  -0.0059 38  ALA A C     
312  O  O     . ALA A 38  ? 0.3386 0.2217 0.3016 -0.0036 0.1624  -0.0282 38  ALA A O     
313  C  CB    . ALA A 38  ? 0.1578 0.1696 0.1652 0.0430  -0.0124 0.0169  38  ALA A CB    
314  N  N     . LYS A 39  ? 0.2097 0.2479 0.1455 0.1157  0.0103  -0.0361 39  LYS A N     
315  C  CA    . LYS A 39  ? 0.2121 0.2869 0.1674 0.1269  0.0204  -0.0439 39  LYS A CA    
316  C  C     . LYS A 39  ? 0.1670 0.2095 0.0962 0.0523  0.0148  -0.0326 39  LYS A C     
317  O  O     . LYS A 39  ? 0.1368 0.2344 0.1223 0.0279  0.0272  -0.0131 39  LYS A O     
318  C  CB    . LYS A 39  ? 0.1458 0.3817 0.2033 0.1455  -0.0257 -0.0570 39  LYS A CB    
319  C  CG    . LYS A 39  ? 0.2781 0.3141 0.1752 0.1282  0.0033  0.0178  39  LYS A CG    
320  C  CD    . LYS A 39  ? 0.2142 0.3383 0.2369 0.0631  -0.0617 0.0378  39  LYS A CD    
321  C  CE    . LYS A 39  ? 0.2339 0.4119 0.2238 0.1065  -0.0344 -0.0517 39  LYS A CE    
322  N  NZ    . LYS A 39  ? 0.4214 0.4521 0.2783 0.0710  -0.0862 -0.0376 39  LYS A NZ    
323  N  N     . TYR A 40  ? 0.1977 0.1955 0.1488 0.0309  0.0322  0.0168  40  TYR A N     
324  C  CA    . TYR A 40  ? 0.1614 0.2015 0.1416 0.0091  0.0490  0.0076  40  TYR A CA    
325  C  C     . TYR A 40  ? 0.1330 0.2105 0.1095 0.0112  0.0295  0.0040  40  TYR A C     
326  O  O     . TYR A 40  ? 0.1615 0.2816 0.1057 0.0615  0.0320  -0.0081 40  TYR A O     
327  C  CB    . TYR A 40  ? 0.2328 0.2285 0.1259 -0.0560 0.0825  0.0083  40  TYR A CB    
328  C  CG    . TYR A 40  ? 0.1816 0.2916 0.1857 -0.0506 0.0971  -0.0392 40  TYR A CG    
329  C  CD1   . TYR A 40  ? 0.1954 0.2984 0.1517 -0.0892 0.0891  -0.0679 40  TYR A CD1   
330  C  CD2   . TYR A 40  ? 0.2260 0.4561 0.1637 -0.0409 0.1081  -0.0065 40  TYR A CD2   
331  C  CE1   . TYR A 40  ? 0.1862 0.5052 0.1713 -0.0288 0.0486  -0.0384 40  TYR A CE1   
332  C  CE2   . TYR A 40  ? 0.1843 0.6022 0.1588 -0.0373 0.1038  -0.0255 40  TYR A CE2   
333  C  CZ    . TYR A 40  ? 0.1283 0.5713 0.1680 -0.0206 0.0258  -0.0392 40  TYR A CZ    
334  O  OH    . TYR A 40  ? 0.1445 0.7151 0.3035 0.0468  0.0476  -0.1057 40  TYR A OH    
335  N  N     . ASP A 41  ? 0.1304 0.1823 0.0990 0.0102  0.0379  -0.0194 41  ASP A N     
336  C  CA    . ASP A 41  ? 0.1300 0.1712 0.1191 -0.0078 -0.0062 -0.0231 41  ASP A CA    
337  C  C     . ASP A 41  ? 0.1571 0.2966 0.1173 0.0262  0.0064  -0.0104 41  ASP A C     
338  O  O     . ASP A 41  ? 0.1282 0.2495 0.1268 0.0089  0.0077  -0.0008 41  ASP A O     
339  C  CB    . ASP A 41  ? 0.1476 0.1751 0.1334 0.0037  -0.0075 -0.0103 41  ASP A CB    
340  C  CG    . ASP A 41  ? 0.2143 0.1590 0.1766 -0.0314 -0.0135 -0.0387 41  ASP A CG    
341  O  OD1   . ASP A 41  ? 0.2597 0.2037 0.1626 0.0369  -0.0161 -0.0501 41  ASP A OD1   
342  O  OD2   . ASP A 41  ? 0.2104 0.2164 0.2328 -0.0379 -0.0434 -0.0205 41  ASP A OD2   
343  N  N     . PRO A 42  ? 0.1472 0.3266 0.1409 0.0522  0.0306  0.0093  42  PRO A N     
344  C  CA    . PRO A 42  ? 0.1593 0.3827 0.1948 0.0553  0.0526  0.0358  42  PRO A CA    
345  C  C     . PRO A 42  ? 0.2307 0.3530 0.1650 0.1206  0.0359  0.0072  42  PRO A C     
346  O  O     . PRO A 42  ? 0.2558 0.5324 0.2497 0.2231  0.0713  0.0550  42  PRO A O     
347  C  CB    . PRO A 42  ? 0.1883 0.4256 0.2201 0.1258  0.0954  0.0657  42  PRO A CB    
348  C  CG    . PRO A 42  ? 0.2714 0.4883 0.1591 0.1366  0.0959  0.0517  42  PRO A CG    
349  C  CD    . PRO A 42  ? 0.2069 0.3553 0.1613 0.0861  0.0657  0.0492  42  PRO A CD    
350  N  N     . SER A 43  ? 0.2563 0.2920 0.1550 0.1307  0.0188  -0.0233 43  SER A N     
351  C  CA    . SER A 43  ? 0.3534 0.2540 0.1775 0.1648  -0.0358 -0.0759 43  SER A CA    
352  C  C     . SER A 43  ? 0.1637 0.3043 0.1884 0.0447  -0.0264 -0.0555 43  SER A C     
353  O  O     . SER A 43  ? 0.3113 0.2963 0.2690 0.0893  0.0137  -0.0044 43  SER A O     
354  C  CB    . SER A 43  ? 0.3680 0.2883 0.1682 0.1541  -0.0362 -0.0840 43  SER A CB    
355  O  OG    . SER A 43  ? 0.3816 0.2030 0.2183 0.0572  -0.0656 -0.0596 43  SER A OG    
356  N  N     . LEU A 44  ? 0.1815 0.2857 0.1656 0.0376  -0.0063 -0.0211 44  LEU A N     
357  C  CA    . LEU A 44  ? 0.1664 0.2912 0.1931 0.0340  -0.0245 0.0275  44  LEU A CA    
358  C  C     . LEU A 44  ? 0.1621 0.4094 0.2670 -0.0749 -0.0417 0.1333  44  LEU A C     
359  O  O     . LEU A 44  ? 0.1546 0.4869 0.3208 -0.0998 -0.0395 0.1494  44  LEU A O     
360  C  CB    . LEU A 44  ? 0.1656 0.2666 0.1584 -0.0446 0.0190  -0.0458 44  LEU A CB    
361  C  CG    . LEU A 44  ? 0.1423 0.2183 0.1198 -0.0025 0.0271  -0.0174 44  LEU A CG    
362  C  CD1   . LEU A 44  ? 0.2202 0.2482 0.1315 -0.0097 0.0283  -0.0618 44  LEU A CD1   
363  C  CD2   . LEU A 44  ? 0.2105 0.2026 0.1680 -0.0121 -0.0205 0.0226  44  LEU A CD2   
364  N  N     . LYS A 45  ? 0.1340 0.3620 0.3101 -0.0389 -0.0580 0.1435  45  LYS A N     
365  C  CA    . LYS A 45  ? 0.0979 0.2860 0.3401 -0.0110 -0.0567 0.0368  45  LYS A CA    
366  C  C     . LYS A 45  ? 0.2902 0.2796 0.2364 -0.0682 -0.1671 0.0967  45  LYS A C     
367  O  O     . LYS A 45  ? 0.1310 0.7758 0.2561 -0.0776 0.0247  -0.1596 45  LYS A O     
368  C  CB    . LYS A 45  ? 0.1836 0.3041 0.2104 0.0488  -0.0237 0.0333  45  LYS A CB    
369  C  CG    . LYS A 45  ? 0.1944 0.4577 0.2129 0.1018  -0.0548 -0.0378 45  LYS A CG    
370  C  CD    . LYS A 45  ? 0.4602 0.4696 0.4118 0.0990  -0.0906 -0.0712 45  LYS A CD    
371  C  CE    . LYS A 45  ? 0.7639 0.6476 0.4768 0.1514  -0.0817 -0.2107 45  LYS A CE    
372  N  NZ    . LYS A 45  ? 0.8951 0.7787 0.6103 0.3251  0.1052  -0.3258 45  LYS A NZ    
373  N  N     . PRO A 46  ? 0.1685 0.3072 0.1721 -0.0550 0.0192  -0.0092 46  PRO A N     
374  C  CA    . PRO A 46  ? 0.1199 0.3018 0.1845 0.0133  0.0009  0.0119  46  PRO A CA    
375  C  C     . PRO A 46  ? 0.0936 0.4058 0.1480 0.0030  0.0347  0.0010  46  PRO A C     
376  O  O     . PRO A 46  ? 0.0770 0.4044 0.2076 -0.0463 -0.0147 0.0767  46  PRO A O     
377  C  CB    . PRO A 46  ? 0.1163 0.3055 0.2186 -0.0085 0.0033  0.0155  46  PRO A CB    
378  C  CG    . PRO A 46  ? 0.1195 0.4533 0.2574 -0.0645 0.0214  -0.0300 46  PRO A CG    
379  C  CD    . PRO A 46  ? 0.1740 0.3603 0.2542 0.0187  0.0012  -0.0965 46  PRO A CD    
380  N  N     . LEU A 47  ? 0.1081 0.2848 0.2282 -0.0321 -0.0043 0.0320  47  LEU A N     
381  C  CA    A LEU A 47  ? 0.0899 0.2695 0.2359 -0.0141 -0.0144 0.0540  47  LEU A CA    
382  C  CA    B LEU A 47  ? 0.0789 0.2071 0.1944 -0.0386 -0.0276 0.0079  47  LEU A CA    
383  C  C     . LEU A 47  ? 0.0819 0.2451 0.2406 -0.0378 -0.0276 0.0581  47  LEU A C     
384  O  O     . LEU A 47  ? 0.1255 0.3329 0.3381 -0.1064 -0.0727 0.1515  47  LEU A O     
385  C  CB    A LEU A 47  ? 0.2185 0.3479 0.2501 0.0446  -0.0147 0.0265  47  LEU A CB    
386  C  CB    B LEU A 47  ? 0.1120 0.1407 0.2141 -0.0232 -0.1034 0.0307  47  LEU A CB    
387  C  CG    A LEU A 47  ? 0.1446 0.3691 0.3529 -0.0533 -0.0443 -0.0312 47  LEU A CG    
388  C  CG    B LEU A 47  ? 0.0947 0.1246 0.2099 -0.0103 -0.0791 0.0078  47  LEU A CG    
389  C  CD1   A LEU A 47  ? 0.1462 0.2412 0.3172 -0.0982 -0.1163 0.0272  47  LEU A CD1   
390  C  CD1   B LEU A 47  ? 0.1242 0.1618 0.1941 -0.0259 -0.0949 0.0103  47  LEU A CD1   
391  C  CD2   A LEU A 47  ? 0.0694 0.3793 0.2347 -0.0347 -0.0699 -0.0418 47  LEU A CD2   
392  C  CD2   B LEU A 47  ? 0.1031 0.1064 0.2287 -0.0061 -0.0609 0.0186  47  LEU A CD2   
393  N  N     . SER A 48  ? 0.0874 0.1926 0.1518 -0.0201 -0.0077 0.0162  48  SER A N     
394  C  CA    . SER A 48  ? 0.0991 0.2036 0.1624 -0.0049 -0.0009 0.0214  48  SER A CA    
395  C  C     . SER A 48  ? 0.0891 0.1602 0.1575 -0.0005 -0.0037 -0.0032 48  SER A C     
396  O  O     . SER A 48  ? 0.0916 0.1794 0.1670 -0.0276 0.0014  -0.0289 48  SER A O     
397  C  CB    . SER A 48  ? 0.0974 0.2214 0.1889 0.0007  -0.0092 0.0190  48  SER A CB    
398  O  OG    . SER A 48  ? 0.1404 0.2388 0.2390 0.0494  0.0221  0.0358  48  SER A OG    
399  N  N     . VAL A 49  ? 0.1236 0.1658 0.1495 -0.0543 0.0074  0.0061  49  VAL A N     
400  C  CA    . VAL A 49  ? 0.1183 0.2053 0.1733 -0.0700 0.0033  -0.0032 49  VAL A CA    
401  C  C     . VAL A 49  ? 0.1323 0.2138 0.1416 -0.0720 -0.0133 -0.0061 49  VAL A C     
402  O  O     . VAL A 49  ? 0.1483 0.3262 0.2155 -0.1282 -0.0524 0.0575  49  VAL A O     
403  C  CB    . VAL A 49  ? 0.2269 0.1966 0.1698 -0.0859 0.0389  -0.0163 49  VAL A CB    
404  C  CG1   . VAL A 49  ? 0.3725 0.2323 0.2173 -0.0913 0.0950  -0.0607 49  VAL A CG1   
405  C  CG2   . VAL A 49  ? 0.1781 0.1615 0.3164 -0.0474 0.0454  -0.0195 49  VAL A CG2   
406  N  N     . SER A 50  ? 0.1187 0.1925 0.1693 -0.0590 -0.0012 -0.0013 50  SER A N     
407  C  CA    . SER A 50  ? 0.0994 0.2660 0.2491 -0.0100 -0.0396 0.0046  50  SER A CA    
408  C  C     . SER A 50  ? 0.0937 0.2229 0.2053 -0.0107 -0.0669 0.0052  50  SER A C     
409  O  O     . SER A 50  ? 0.1438 0.1745 0.2216 -0.0071 -0.0498 0.0113  50  SER A O     
410  C  CB    . SER A 50  ? 0.2441 0.2809 0.2574 0.0406  -0.0255 0.0322  50  SER A CB    
411  O  OG    . SER A 50  ? 0.2108 0.4554 0.3738 0.0984  0.0110  -0.1124 50  SER A OG    
412  N  N     . TYR A 51  ? 0.1012 0.2081 0.2188 -0.0424 -0.0443 0.0206  51  TYR A N     
413  C  CA    . TYR A 51  ? 0.1153 0.1695 0.2071 -0.0103 -0.0487 0.0114  51  TYR A CA    
414  C  C     . TYR A 51  ? 0.1155 0.1745 0.2159 -0.0173 -0.0322 0.0706  51  TYR A C     
415  O  O     . TYR A 51  ? 0.1920 0.2369 0.2130 -0.0127 -0.0564 0.0235  51  TYR A O     
416  C  CB    . TYR A 51  ? 0.1153 0.1865 0.1902 -0.0318 -0.0689 -0.0009 51  TYR A CB    
417  C  CG    . TYR A 51  ? 0.0922 0.1409 0.1231 -0.0136 -0.0224 -0.0158 51  TYR A CG    
418  C  CD1   . TYR A 51  ? 0.1064 0.1355 0.1770 -0.0229 -0.0435 0.0016  51  TYR A CD1   
419  C  CD2   . TYR A 51  ? 0.0984 0.1414 0.1288 -0.0177 -0.0110 -0.0108 51  TYR A CD2   
420  C  CE1   . TYR A 51  ? 0.0895 0.1264 0.1608 -0.0316 -0.0301 0.0030  51  TYR A CE1   
421  C  CE2   . TYR A 51  ? 0.1162 0.1194 0.1407 -0.0419 -0.0183 -0.0103 51  TYR A CE2   
422  C  CZ    . TYR A 51  ? 0.0922 0.1340 0.1144 -0.0221 -0.0189 -0.0199 51  TYR A CZ    
423  O  OH    . TYR A 51  ? 0.0901 0.1330 0.1570 -0.0145 -0.0237 -0.0054 51  TYR A OH    
424  N  N     . ASP A 52  ? 0.1057 0.2747 0.2541 -0.0155 -0.0470 0.0691  52  ASP A N     
425  C  CA    . ASP A 52  ? 0.1451 0.2769 0.2775 -0.0193 -0.0696 0.1000  52  ASP A CA    
426  C  C     . ASP A 52  ? 0.1969 0.3002 0.2694 -0.0403 -0.0553 0.0826  52  ASP A C     
427  O  O     . ASP A 52  ? 0.3094 0.2621 0.3331 -0.0633 -0.1488 0.0877  52  ASP A O     
428  C  CB    . ASP A 52  ? 0.1733 0.4862 0.2918 0.0531  -0.0809 0.1556  52  ASP A CB    
429  C  CG    . ASP A 52  ? 0.3063 0.4514 0.5362 0.0419  0.0230  0.0526  52  ASP A CG    
430  O  OD1   . ASP A 52  ? 0.6413 0.7382 0.5560 -0.0054 0.0242  0.0500  52  ASP A OD1   
431  O  OD2   . ASP A 52  ? 0.5432 0.5875 0.6759 0.0990  0.1768  0.3504  52  ASP A OD2   
432  N  N     . GLN A 53  ? 0.1868 0.2030 0.2823 0.0000  -0.0591 0.0801  53  GLN A N     
433  C  CA    . GLN A 53  ? 0.1652 0.2155 0.2947 -0.0039 -0.0555 0.0860  53  GLN A CA    
434  C  C     . GLN A 53  ? 0.2029 0.1351 0.1950 -0.0028 -0.0272 0.0068  53  GLN A C     
435  O  O     . GLN A 53  ? 0.2293 0.1870 0.2078 -0.0178 -0.0239 0.0340  53  GLN A O     
436  C  CB    . GLN A 53  ? 0.3106 0.2525 0.3054 0.0073  -0.0334 0.0495  53  GLN A CB    
437  C  CG    . GLN A 53  ? 0.3634 0.3098 0.4431 -0.0030 0.0626  0.0774  53  GLN A CG    
438  C  CD    . GLN A 53  ? 0.4711 0.4828 0.3934 0.0783  0.0817  0.2445  53  GLN A CD    
439  O  OE1   . GLN A 53  ? 1.1042 0.6637 0.5035 -0.0998 0.2641  0.2995  53  GLN A OE1   
440  N  NE2   . GLN A 53  ? 0.6472 0.5396 0.5409 -0.0520 0.2195  0.2748  53  GLN A NE2   
441  N  N     . ALA A 54  ? 0.1964 0.1415 0.2165 -0.0152 -0.0329 0.0051  54  ALA A N     
442  C  CA    . ALA A 54  ? 0.2034 0.1515 0.1916 0.0025  -0.0425 -0.0364 54  ALA A CA    
443  C  C     . ALA A 54  ? 0.2200 0.2040 0.1835 -0.0071 -0.0659 -0.0240 54  ALA A C     
444  O  O     . ALA A 54  ? 0.2525 0.2848 0.2027 -0.0414 -0.0470 -0.1105 54  ALA A O     
445  C  CB    . ALA A 54  ? 0.2016 0.1849 0.2065 0.0119  -0.0641 -0.0332 54  ALA A CB    
446  N  N     . THR A 55  ? 0.1783 0.1633 0.1578 0.0403  -0.0441 -0.0148 55  THR A N     
447  C  CA    . THR A 55  ? 0.1936 0.1766 0.1654 0.0246  -0.0382 0.0144  55  THR A CA    
448  C  C     . THR A 55  ? 0.2207 0.1422 0.1079 -0.0004 -0.0471 0.0210  55  THR A C     
449  O  O     . THR A 55  ? 0.1886 0.1458 0.1334 0.0383  -0.0199 0.0310  55  THR A O     
450  C  CB    . THR A 55  ? 0.2720 0.2553 0.2246 0.0381  0.0201  0.0810  55  THR A CB    
451  O  OG1   . THR A 55  ? 0.4464 0.2469 0.5443 0.1441  -0.1253 0.0012  55  THR A OG1   
452  C  CG2   . THR A 55  ? 0.3589 0.2623 0.2075 0.1116  -0.0198 0.0655  55  THR A CG2   
453  N  N     . SER A 56  ? 0.2365 0.1437 0.1501 0.0226  -0.0741 0.0078  56  SER A N     
454  C  CA    . SER A 56  ? 0.2841 0.1869 0.1110 0.0300  -0.0407 0.0083  56  SER A CA    
455  C  C     . SER A 56  ? 0.2234 0.2079 0.1497 0.1007  -0.0134 -0.0141 56  SER A C     
456  O  O     . SER A 56  ? 0.3436 0.2264 0.1378 0.1021  -0.0546 0.0255  56  SER A O     
457  C  CB    . SER A 56  ? 0.3200 0.1727 0.1628 0.0450  -0.0463 -0.0099 56  SER A CB    
458  O  OG    . SER A 56  ? 0.2982 0.1863 0.1318 0.0636  -0.0330 -0.0114 56  SER A OG    
459  N  N     . LEU A 57  ? 0.1945 0.1920 0.1055 0.0607  -0.0226 0.0619  57  LEU A N     
460  C  CA    . LEU A 57  ? 0.1719 0.1927 0.1520 0.0365  -0.0006 0.0535  57  LEU A CA    
461  C  C     . LEU A 57  ? 0.2110 0.1861 0.1271 0.0244  0.0338  0.0481  57  LEU A C     
462  O  O     . LEU A 57  ? 0.3184 0.1698 0.1247 0.0717  0.0140  0.0430  57  LEU A O     
463  C  CB    . LEU A 57  ? 0.2925 0.1876 0.1097 -0.0356 0.0298  0.0594  57  LEU A CB    
464  C  CG    . LEU A 57  ? 0.2875 0.2092 0.2245 0.0056  0.0001  0.0293  57  LEU A CG    
465  C  CD1   . LEU A 57  ? 0.3280 0.2466 0.1927 -0.0717 0.0247  0.0697  57  LEU A CD1   
466  C  CD2   . LEU A 57  ? 0.4253 0.1711 0.3220 -0.0024 -0.0581 0.0455  57  LEU A CD2   
467  N  N     . ARG A 58  ? 0.2598 0.1601 0.1517 0.0643  -0.0035 0.0351  58  ARG A N     
468  C  CA    . ARG A 58  ? 0.2105 0.1703 0.1585 0.0279  -0.0027 0.0263  58  ARG A CA    
469  C  C     . ARG A 58  ? 0.1970 0.1486 0.1251 -0.0209 -0.0112 0.0285  58  ARG A C     
470  O  O     . ARG A 58  ? 0.2868 0.1661 0.1171 0.0522  0.0286  0.0165  58  ARG A O     
471  C  CB    . ARG A 58  ? 0.2185 0.1822 0.1349 0.0443  0.0187  -0.0235 58  ARG A CB    
472  C  CG    . ARG A 58  ? 0.1520 0.2128 0.2541 0.0084  0.0674  0.1066  58  ARG A CG    
473  C  CD    . ARG A 58  ? 0.2756 0.2578 0.2148 -0.0854 0.0032  0.0510  58  ARG A CD    
474  N  NE    . ARG A 58  ? 0.1293 0.2288 0.2188 -0.0156 0.0362  0.0078  58  ARG A NE    
475  C  CZ    . ARG A 58  ? 0.1197 0.2522 0.1560 -0.0613 0.0170  0.0445  58  ARG A CZ    
476  N  NH1   . ARG A 58  ? 0.2094 0.2598 0.2169 -0.0716 0.0702  0.0238  58  ARG A NH1   
477  N  NH2   . ARG A 58  ? 0.1849 0.2192 0.1957 -0.0331 0.0453  0.0544  58  ARG A NH2   
478  N  N     . ILE A 59  ? 0.2425 0.1764 0.0784 0.0081  0.0200  0.0102  59  ILE A N     
479  C  CA    . ILE A 59  ? 0.2052 0.1933 0.0790 -0.0327 0.0003  0.0489  59  ILE A CA    
480  C  C     . ILE A 59  ? 0.1756 0.1221 0.1337 -0.0108 0.0003  0.0508  59  ILE A C     
481  O  O     . ILE A 59  ? 0.2882 0.1992 0.0904 0.0070  0.0189  0.0232  59  ILE A O     
482  C  CB    . ILE A 59  ? 0.1822 0.1631 0.1049 0.0052  0.0065  0.0329  59  ILE A CB    
483  C  CG1   . ILE A 59  ? 0.2201 0.1744 0.0899 0.0228  0.0150  0.0257  59  ILE A CG1   
484  C  CG2   . ILE A 59  ? 0.2779 0.1666 0.0996 0.0385  -0.0012 0.0239  59  ILE A CG2   
485  C  CD1   . ILE A 59  ? 0.2401 0.1659 0.1270 0.0142  0.0141  0.0163  59  ILE A CD1   
486  N  N     . LEU A 60  ? 0.1855 0.1791 0.1466 0.0240  -0.0160 -0.0070 60  LEU A N     
487  C  CA    . LEU A 60  ? 0.1562 0.1220 0.0590 -0.0126 -0.0267 0.0325  60  LEU A CA    
488  C  C     . LEU A 60  ? 0.2307 0.1026 0.0966 -0.0142 -0.0240 0.0320  60  LEU A C     
489  O  O     . LEU A 60  ? 0.2268 0.1383 0.0876 -0.0167 0.0120  0.0308  60  LEU A O     
490  C  CB    . LEU A 60  ? 0.1785 0.0993 0.1803 -0.0097 0.0419  -0.0092 60  LEU A CB    
491  C  CG    . LEU A 60  ? 0.1386 0.1000 0.1530 -0.0033 -0.0149 0.0257  60  LEU A CG    
492  C  CD1   . LEU A 60  ? 0.1980 0.2009 0.1920 -0.0160 0.0065  0.0337  60  LEU A CD1   
493  C  CD2   . LEU A 60  ? 0.2558 0.1279 0.1559 -0.0094 -0.0022 0.0135  60  LEU A CD2   
494  N  N     . ASN A 61  ? 0.2598 0.1154 0.0839 -0.0331 0.0181  0.0200  61  ASN A N     
495  C  CA    . ASN A 61  ? 0.2279 0.1533 0.0934 -0.0383 0.0203  -0.0390 61  ASN A CA    
496  C  C     . ASN A 61  ? 0.2234 0.1872 0.0926 -0.0344 -0.0106 0.0255  61  ASN A C     
497  O  O     . ASN A 61  ? 0.2892 0.1532 0.1070 -0.0651 0.0199  0.0187  61  ASN A O     
498  C  CB    . ASN A 61  ? 0.2315 0.1212 0.1107 -0.0474 0.0161  -0.0208 61  ASN A CB    
499  C  CG    . ASN A 61  ? 0.2133 0.1385 0.1350 -0.0469 0.0144  -0.0306 61  ASN A CG    
500  O  OD1   . ASN A 61  ? 0.2477 0.1402 0.1337 -0.0589 0.0029  0.0273  61  ASN A OD1   
501  N  ND2   . ASN A 61  ? 0.2347 0.1259 0.1084 -0.0448 0.0438  -0.0122 61  ASN A ND2   
502  N  N     . ASN A 62  ? 0.2518 0.1185 0.0892 -0.0550 0.0194  0.0188  62  ASN A N     
503  C  CA    . ASN A 62  ? 0.2343 0.1276 0.1406 -0.0683 0.0259  0.0202  62  ASN A CA    
504  C  C     . ASN A 62  ? 0.2097 0.1627 0.1237 -0.0657 0.0318  -0.0238 62  ASN A C     
505  O  O     . ASN A 62  ? 0.3188 0.2243 0.1488 -0.1171 -0.0187 0.0369  62  ASN A O     
506  C  CB    . ASN A 62  ? 0.2504 0.1103 0.1390 -0.0460 -0.0199 0.0125  62  ASN A CB    
507  C  CG    . ASN A 62  ? 0.2031 0.1495 0.1265 -0.0500 0.0268  -0.0054 62  ASN A CG    
508  O  OD1   . ASN A 62  ? 0.2637 0.1365 0.1411 -0.0834 -0.0206 0.0133  62  ASN A OD1   
509  N  ND2   . ASN A 62  ? 0.3601 0.2023 0.1425 0.0113  0.0655  0.0070  62  ASN A ND2   
510  N  N     . GLY A 63  ? 0.2215 0.1561 0.1462 -0.0317 0.0211  0.0013  63  GLY A N     
511  C  CA    . GLY A 63  ? 0.1580 0.1533 0.1195 -0.0683 0.0378  -0.0074 63  GLY A CA    
512  C  C     . GLY A 63  ? 0.1912 0.1363 0.1782 -0.0424 -0.0113 0.0005  63  GLY A C     
513  O  O     . GLY A 63  ? 0.1884 0.1595 0.1588 -0.0545 -0.0023 0.0111  63  GLY A O     
514  N  N     A HIS A 64  ? 0.2168 0.1617 0.1342 -0.0524 -0.0087 0.0631  64  HIS A N     
515  N  N     B HIS A 64  ? 0.2105 0.1678 0.1424 -0.0527 -0.0186 0.0468  64  HIS A N     
516  C  CA    A HIS A 64  ? 0.1645 0.1398 0.1308 -0.0740 -0.0179 0.0500  64  HIS A CA    
517  C  CA    B HIS A 64  ? 0.2038 0.1685 0.1433 -0.0824 -0.0164 0.0421  64  HIS A CA    
518  C  C     A HIS A 64  ? 0.1587 0.1015 0.1263 -0.0695 -0.0002 0.0230  64  HIS A C     
519  C  C     B HIS A 64  ? 0.1558 0.1137 0.1445 -0.0424 -0.0124 0.0212  64  HIS A C     
520  O  O     A HIS A 64  ? 0.1557 0.1186 0.1278 -0.0613 0.0016  0.0500  64  HIS A O     
521  O  O     B HIS A 64  ? 0.1595 0.1232 0.1188 -0.0282 0.0354  0.0075  64  HIS A O     
522  C  CB    A HIS A 64  ? 0.1106 0.1259 0.1075 -0.0372 -0.0256 0.0696  64  HIS A CB    
523  C  CB    B HIS A 64  ? 0.1727 0.1861 0.1048 -0.0725 -0.0425 0.0441  64  HIS A CB    
524  C  CG    A HIS A 64  ? 0.1889 0.1506 0.1259 -0.0261 -0.0049 -0.0001 64  HIS A CG    
525  C  CG    B HIS A 64  ? 0.2051 0.2487 0.1183 -0.1078 -0.0278 0.0287  64  HIS A CG    
526  N  ND1   A HIS A 64  ? 0.2012 0.1464 0.0794 0.0221  -0.0683 0.0101  64  HIS A ND1   
527  N  ND1   B HIS A 64  ? 0.3134 0.2755 0.2686 -0.2126 -0.0258 0.0422  64  HIS A ND1   
528  C  CD2   A HIS A 64  ? 0.1195 0.1417 0.1656 -0.0033 -0.0224 0.0133  64  HIS A CD2   
529  C  CD2   B HIS A 64  ? 0.1948 0.3445 0.0845 -0.1456 0.0266  -0.0942 64  HIS A CD2   
530  C  CE1   A HIS A 64  ? 0.1535 0.1723 0.1393 0.0715  -0.0033 -0.0735 64  HIS A CE1   
531  C  CE1   B HIS A 64  ? 0.2882 0.3378 0.3655 -0.1493 0.0223  0.0004  64  HIS A CE1   
532  N  NE2   A HIS A 64  ? 0.2054 0.2005 0.1434 0.0149  -0.0242 -0.0409 64  HIS A NE2   
533  N  NE2   B HIS A 64  ? 0.1475 0.4031 0.1222 -0.1649 0.0807  -0.0955 64  HIS A NE2   
534  N  N     . ALA A 65  ? 0.1795 0.1175 0.1436 -0.0537 -0.0276 0.0286  65  ALA A N     
535  C  CA    . ALA A 65  ? 0.1713 0.1167 0.1240 -0.0337 -0.0161 0.0099  65  ALA A CA    
536  C  C     . ALA A 65  ? 0.1726 0.0925 0.0781 0.0007  0.0116  0.0052  65  ALA A C     
537  O  O     . ALA A 65  ? 0.1765 0.1581 0.1236 -0.0472 0.0045  0.0146  65  ALA A O     
538  C  CB    . ALA A 65  ? 0.1773 0.1758 0.1232 -0.0507 -0.0294 0.0062  65  ALA A CB    
539  N  N     . PHE A 66  ? 0.1692 0.1102 0.0950 -0.0062 -0.0044 0.0129  66  PHE A N     
540  C  CA    . PHE A 66  ? 0.1797 0.1196 0.0795 -0.0075 0.0111  0.0302  66  PHE A CA    
541  C  C     . PHE A 66  ? 0.2087 0.0960 0.1089 -0.0038 0.0139  0.0048  66  PHE A C     
542  O  O     . PHE A 66  ? 0.2228 0.0958 0.0848 -0.0025 0.0212  0.0097  66  PHE A O     
543  C  CB    . PHE A 66  ? 0.1594 0.1498 0.0759 0.0036  -0.0038 0.0045  66  PHE A CB    
544  C  CG    . PHE A 66  ? 0.1805 0.1287 0.0652 -0.0186 -0.0051 -0.0130 66  PHE A CG    
545  C  CD1   . PHE A 66  ? 0.2085 0.1469 0.0864 0.0039  0.0133  -0.0329 66  PHE A CD1   
546  C  CD2   . PHE A 66  ? 0.1852 0.1360 0.0931 0.0035  0.0201  -0.0388 66  PHE A CD2   
547  C  CE1   . PHE A 66  ? 0.1894 0.1400 0.1029 0.0042  -0.0190 -0.0125 66  PHE A CE1   
548  C  CE2   . PHE A 66  ? 0.2136 0.1235 0.1077 -0.0192 -0.0109 -0.0100 66  PHE A CE2   
549  C  CZ    . PHE A 66  ? 0.1935 0.1247 0.1251 -0.0334 -0.0134 -0.0104 66  PHE A CZ    
550  N  N     . ASN A 67  ? 0.2283 0.1025 0.0967 0.0112  0.0101  0.0119  67  ASN A N     
551  C  CA    . ASN A 67  ? 0.2006 0.1195 0.0708 0.0094  0.0043  -0.0094 67  ASN A CA    
552  C  C     . ASN A 67  ? 0.1598 0.1050 0.1290 0.0088  0.0001  0.0671  67  ASN A C     
553  O  O     . ASN A 67  ? 0.1909 0.1786 0.1030 -0.0032 0.0113  0.0410  67  ASN A O     
554  C  CB    . ASN A 67  ? 0.2183 0.1695 0.1152 -0.0485 0.0044  0.0131  67  ASN A CB    
555  C  CG    . ASN A 67  ? 0.1817 0.1171 0.2019 -0.0399 -0.0113 0.0039  67  ASN A CG    
556  O  OD1   . ASN A 67  ? 0.1987 0.2239 0.2929 -0.0764 -0.0466 -0.0361 67  ASN A OD1   
557  N  ND2   . ASN A 67  ? 0.2231 0.1434 0.0865 -0.0527 0.0030  0.0103  67  ASN A ND2   
558  N  N     . VAL A 68  ? 0.1765 0.1312 0.1216 0.0078  0.0020  0.0119  68  VAL A N     
559  C  CA    . VAL A 68  ? 0.1562 0.1197 0.0629 0.0204  0.0016  0.0038  68  VAL A CA    
560  C  C     . VAL A 68  ? 0.1582 0.1273 0.0988 0.0215  -0.0100 -0.0062 68  VAL A C     
561  O  O     . VAL A 68  ? 0.2035 0.1285 0.0985 0.0273  0.0145  0.0059  68  VAL A O     
562  C  CB    . VAL A 68  ? 0.1858 0.1340 0.1541 0.0198  0.0148  -0.0034 68  VAL A CB    
563  C  CG1   . VAL A 68  ? 0.1665 0.1450 0.1634 -0.0180 -0.0042 0.0057  68  VAL A CG1   
564  C  CG2   . VAL A 68  ? 0.1761 0.1734 0.1420 0.0415  0.0004  -0.0223 68  VAL A CG2   
565  N  N     . GLU A 69  ? 0.1846 0.1268 0.1090 0.0241  0.0198  0.0110  69  GLU A N     
566  C  CA    . GLU A 69  ? 0.2083 0.1422 0.0923 0.0136  -0.0010 0.0432  69  GLU A CA    
567  C  C     . GLU A 69  ? 0.2227 0.1038 0.1491 0.0324  -0.0198 0.0148  69  GLU A C     
568  O  O     . GLU A 69  ? 0.2215 0.1377 0.1437 0.0051  -0.0036 0.0014  69  GLU A O     
569  C  CB    . GLU A 69  ? 0.1478 0.1430 0.1689 0.0042  0.0082  0.0326  69  GLU A CB    
570  C  CG    . GLU A 69  ? 0.1224 0.1520 0.1562 -0.0353 0.0294  0.0386  69  GLU A CG    
571  C  CD    . GLU A 69  ? 0.1714 0.1480 0.2005 -0.0005 0.0693  0.0637  69  GLU A CD    
572  O  OE1   . GLU A 69  ? 0.2021 0.1897 0.1833 -0.0217 0.0148  0.0699  69  GLU A OE1   
573  O  OE2   . GLU A 69  ? 0.1485 0.1726 0.2809 -0.0098 0.0594  0.0651  69  GLU A OE2   
574  N  N     . PHE A 70  ? 0.2312 0.1390 0.0901 0.0513  0.0096  0.0183  70  PHE A N     
575  C  CA    . PHE A 70  ? 0.2043 0.1171 0.1117 0.0447  -0.0206 0.0261  70  PHE A CA    
576  C  C     . PHE A 70  ? 0.2099 0.1325 0.1221 0.0475  -0.0213 -0.0048 70  PHE A C     
577  O  O     . PHE A 70  ? 0.1960 0.1253 0.1466 0.0405  0.0057  0.0397  70  PHE A O     
578  C  CB    . PHE A 70  ? 0.1826 0.1358 0.0992 0.0331  -0.0215 0.0223  70  PHE A CB    
579  C  CG    . PHE A 70  ? 0.1777 0.1148 0.1213 0.0370  -0.0047 0.0123  70  PHE A CG    
580  C  CD1   . PHE A 70  ? 0.1741 0.1426 0.1405 0.0383  -0.0115 0.0235  70  PHE A CD1   
581  C  CD2   . PHE A 70  ? 0.1859 0.1342 0.1141 0.0403  -0.0168 0.0246  70  PHE A CD2   
582  C  CE1   . PHE A 70  ? 0.1790 0.1250 0.1541 0.0386  0.0203  0.0298  70  PHE A CE1   
583  C  CE2   . PHE A 70  ? 0.1837 0.1454 0.1310 0.0359  -0.0235 0.0345  70  PHE A CE2   
584  C  CZ    . PHE A 70  ? 0.2045 0.1443 0.1614 0.0363  0.0021  -0.0033 70  PHE A CZ    
585  N  N     . ASP A 71  ? 0.2642 0.1162 0.1628 0.0482  -0.0765 0.0044  71  ASP A N     
586  C  CA    . ASP A 71  ? 0.1922 0.1017 0.1963 0.0598  -0.0124 0.0190  71  ASP A CA    
587  C  C     . ASP A 71  ? 0.1963 0.0793 0.1843 0.0103  -0.0036 -0.0063 71  ASP A C     
588  O  O     . ASP A 71  ? 0.1787 0.1610 0.3379 -0.0287 0.0214  -0.0301 71  ASP A O     
589  C  CB    . ASP A 71  ? 0.3087 0.1629 0.2539 0.0362  -0.1393 0.0153  71  ASP A CB    
590  C  CG    . ASP A 71  ? 0.2833 0.1763 0.3454 0.0577  -0.1196 0.0045  71  ASP A CG    
591  O  OD1   . ASP A 71  ? 0.2481 0.1172 0.3188 0.0237  -0.0624 0.0540  71  ASP A OD1   
592  O  OD2   . ASP A 71  ? 0.2679 0.2088 0.5555 0.0001  -0.1410 0.0987  71  ASP A OD2   
593  N  N     . ASP A 72  ? 0.1471 0.1279 0.1900 -0.0102 0.0073  0.0212  72  ASP A N     
594  C  CA    . ASP A 72  ? 0.1823 0.1282 0.1985 -0.0528 0.0157  -0.0276 72  ASP A CA    
595  C  C     . ASP A 72  ? 0.2794 0.1190 0.2430 -0.0383 -0.0074 -0.0041 72  ASP A C     
596  O  O     . ASP A 72  ? 0.4364 0.1329 0.1873 -0.1149 0.0057  0.0013  72  ASP A O     
597  C  CB    . ASP A 72  ? 0.2275 0.1503 0.1716 -0.0289 0.0025  0.0030  72  ASP A CB    
598  C  CG    . ASP A 72  ? 0.2267 0.3097 0.2050 -0.0554 -0.0621 0.1403  72  ASP A CG    
599  O  OD1   . ASP A 72  ? 0.2211 0.5199 0.2376 -0.0938 -0.0742 0.2219  72  ASP A OD1   
600  O  OD2   . ASP A 72  ? 0.2324 0.3773 0.1954 -0.1184 -0.0910 0.1369  72  ASP A OD2   
601  N  N     . SER A 73  ? 0.2443 0.1133 0.2303 -0.0353 0.0098  -0.0337 73  SER A N     
602  C  CA    . SER A 73  ? 0.2784 0.1124 0.2425 -0.0640 -0.0229 0.0192  73  SER A CA    
603  C  C     . SER A 73  ? 0.3552 0.1080 0.3193 -0.0707 0.0514  -0.0693 73  SER A C     
604  O  O     . SER A 73  ? 0.3695 0.1125 0.2620 -0.0505 0.0516  -0.0009 73  SER A O     
605  C  CB    . SER A 73  ? 0.3151 0.1403 0.2851 -0.0151 0.0217  0.0556  73  SER A CB    
606  O  OG    . SER A 73  ? 0.2968 0.1346 0.2748 0.0502  0.0746  0.0450  73  SER A OG    
607  N  N     . GLN A 74  ? 0.3837 0.1338 0.3459 -0.0448 0.1139  -0.0813 74  GLN A N     
608  C  CA    . GLN A 74  ? 0.4532 0.2046 0.3418 0.0481  0.0962  -0.0755 74  GLN A CA    
609  C  C     . GLN A 74  ? 0.3272 0.2612 0.3867 -0.0091 -0.0477 -0.0161 74  GLN A C     
610  O  O     . GLN A 74  ? 0.2697 0.1709 0.2283 -0.0730 -0.0476 0.0034  74  GLN A O     
611  C  CB    . GLN A 74  ? 0.4330 0.2023 0.4280 0.0649  0.0881  0.0930  74  GLN A CB    
612  C  CG    . GLN A 74  ? 0.4181 0.3868 0.3736 0.0115  -0.0363 0.0793  74  GLN A CG    
613  C  CD    . GLN A 74  ? 0.5062 0.3810 0.3604 -0.0164 -0.1944 0.1654  74  GLN A CD    
614  O  OE1   . GLN A 74  ? 0.7995 0.6883 0.5269 0.0455  -0.0478 -0.0549 74  GLN A OE1   
615  N  NE2   . GLN A 74  ? 0.4498 0.4034 0.2446 0.0599  -0.0645 0.0913  74  GLN A NE2   
616  N  N     . ASP A 75  ? 0.3796 0.3640 0.4665 -0.1004 -0.0371 -0.1556 75  ASP A N     
617  C  CA    . ASP A 75  ? 0.3088 0.3734 0.5043 -0.0808 -0.1012 -0.0567 75  ASP A CA    
618  C  C     . ASP A 75  ? 0.3153 0.3733 0.3533 -0.0141 -0.1308 -0.0925 75  ASP A C     
619  O  O     . ASP A 75  ? 0.2734 0.7106 0.3342 -0.0872 -0.0234 -0.1646 75  ASP A O     
620  C  CB    . ASP A 75  ? 0.4587 0.2848 0.5098 0.1730  -0.1959 -0.0978 75  ASP A CB    
621  C  CG    . ASP A 75  ? 0.4110 0.6270 0.4517 -0.0360 -0.0529 -0.0553 75  ASP A CG    
622  O  OD1   . ASP A 75  ? 0.6724 1.0994 0.3086 0.4626  -0.2948 -0.2580 75  ASP A OD1   
623  O  OD2   . ASP A 75  ? 0.6410 0.7478 0.4488 0.4516  0.0621  0.1472  75  ASP A OD2   
624  N  N     . LYS A 76  ? 0.2305 0.2093 0.2710 -0.0245 -0.0946 0.0776  76  LYS A N     
625  C  CA    . LYS A 76  ? 0.2028 0.1930 0.4213 0.0054  -0.0784 -0.0066 76  LYS A CA    
626  C  C     . LYS A 76  ? 0.2361 0.2848 0.4516 0.0136  -0.0930 0.0768  76  LYS A C     
627  O  O     . LYS A 76  ? 0.3881 0.5338 0.4727 -0.1320 -0.1026 -0.0698 76  LYS A O     
628  C  CB    . LYS A 76  ? 0.4573 0.1844 0.3267 -0.0987 -0.1011 0.0078  76  LYS A CB    
629  C  CG    . LYS A 76  ? 0.4910 0.1182 0.4599 0.0214  -0.0320 0.0017  76  LYS A CG    
630  C  CD    . LYS A 76  ? 0.6153 0.3774 0.3557 -0.0954 -0.0512 0.0745  76  LYS A CD    
631  C  CE    . LYS A 76  ? 0.3829 0.4045 0.3095 0.0005  -0.0141 0.0550  76  LYS A CE    
632  N  NZ    . LYS A 76  ? 0.3080 0.4585 0.3621 -0.0487 -0.0679 -0.0429 76  LYS A NZ    
633  N  N     . ALA A 77  ? 0.2239 0.2898 0.2917 0.0268  -0.1156 0.0402  77  ALA A N     
634  C  CA    . ALA A 77  ? 0.1563 0.2240 0.1973 -0.0326 -0.0850 0.0106  77  ALA A CA    
635  C  C     . ALA A 77  ? 0.1176 0.2020 0.1979 -0.0203 -0.0502 -0.0201 77  ALA A C     
636  O  O     . ALA A 77  ? 0.1275 0.2934 0.3132 -0.0430 -0.0452 -0.0885 77  ALA A O     
637  C  CB    . ALA A 77  ? 0.2589 0.2764 0.1586 0.0441  -0.0983 0.0048  77  ALA A CB    
638  N  N     . VAL A 78  ? 0.1148 0.1733 0.1983 0.0009  -0.0667 -0.0117 78  VAL A N     
639  C  CA    . VAL A 78  ? 0.1645 0.1287 0.1858 -0.0083 -0.0628 0.0074  78  VAL A CA    
640  C  C     . VAL A 78  ? 0.1289 0.1185 0.1625 -0.0002 -0.0520 -0.0226 78  VAL A C     
641  O  O     . VAL A 78  ? 0.1460 0.1422 0.2244 -0.0299 -0.0681 0.0099  78  VAL A O     
642  C  CB    . VAL A 78  ? 0.2780 0.2070 0.1903 0.0392  -0.0601 -0.0093 78  VAL A CB    
643  C  CG1   . VAL A 78  ? 0.3906 0.1549 0.2730 0.0515  -0.1104 0.0200  78  VAL A CG1   
644  C  CG2   . VAL A 78  ? 0.2708 0.1908 0.2636 -0.0027 0.0020  -0.0374 78  VAL A CG2   
645  N  N     . LEU A 79  ? 0.1085 0.1122 0.1537 0.0009  -0.0354 0.0045  79  LEU A N     
646  C  CA    . LEU A 79  ? 0.1079 0.1152 0.1586 -0.0083 -0.0325 0.0026  79  LEU A CA    
647  C  C     . LEU A 79  ? 0.1215 0.1315 0.1385 -0.0222 -0.0058 0.0004  79  LEU A C     
648  O  O     . LEU A 79  ? 0.1437 0.1700 0.1584 -0.0389 -0.0016 -0.0203 79  LEU A O     
649  C  CB    . LEU A 79  ? 0.0944 0.1544 0.1629 -0.0129 -0.0178 0.0127  79  LEU A CB    
650  C  CG    . LEU A 79  ? 0.1218 0.1644 0.1711 0.0057  -0.0064 0.0063  79  LEU A CG    
651  C  CD1   . LEU A 79  ? 0.1368 0.1694 0.2896 -0.0072 0.0075  0.0545  79  LEU A CD1   
652  C  CD2   . LEU A 79  ? 0.1241 0.1595 0.1591 0.0080  0.0111  0.0073  79  LEU A CD2   
653  N  N     . LYS A 80  ? 0.1339 0.1436 0.1318 -0.0246 -0.0208 -0.0131 80  LYS A N     
654  C  CA    . LYS A 80  ? 0.1389 0.1541 0.1643 -0.0364 -0.0017 -0.0363 80  LYS A CA    
655  C  C     . LYS A 80  ? 0.0871 0.1358 0.1733 0.0369  -0.0078 -0.0115 80  LYS A C     
656  O  O     . LYS A 80  ? 0.0994 0.1406 0.1772 0.0027  -0.0109 -0.0017 80  LYS A O     
657  C  CB    . LYS A 80  ? 0.4291 0.0808 0.1865 0.0611  0.0405  -0.0050 80  LYS A CB    
658  C  CG    . LYS A 80  ? 0.3020 0.2526 0.2961 0.0100  0.0478  0.0658  80  LYS A CG    
659  C  CD    . LYS A 80  ? 0.2540 0.4841 0.4946 0.0991  -0.1033 0.0065  80  LYS A CD    
660  C  CE    . LYS A 80  ? 0.5380 0.6375 0.5502 0.0814  -0.0004 -0.0190 80  LYS A CE    
661  N  NZ    . LYS A 80  ? 0.5352 0.7429 0.7231 0.0991  0.1850  -0.0486 80  LYS A NZ    
662  N  N     . GLY A 81  ? 0.1271 0.1545 0.1723 0.0019  0.0157  -0.0114 81  GLY A N     
663  C  CA    . GLY A 81  ? 0.1294 0.1697 0.1667 0.0274  0.0359  -0.0034 81  GLY A CA    
664  C  C     . GLY A 81  ? 0.1108 0.1630 0.1624 0.0209  0.0353  0.0053  81  GLY A C     
665  O  O     . GLY A 81  ? 0.1133 0.1579 0.1540 -0.0185 0.0288  -0.0299 81  GLY A O     
666  N  N     . GLY A 82  ? 0.0953 0.1800 0.2868 0.0019  0.0333  0.0395  82  GLY A N     
667  C  CA    . GLY A 82  ? 0.1519 0.1328 0.3486 -0.0042 0.0349  0.0551  82  GLY A CA    
668  C  C     . GLY A 82  ? 0.1214 0.1692 0.2746 0.0287  0.0535  0.0318  82  GLY A C     
669  O  O     . GLY A 82  ? 0.1468 0.3557 0.2162 0.1067  0.0661  0.0507  82  GLY A O     
670  N  N     . PRO A 83  ? 0.1203 0.1217 0.2025 0.0284  0.0469  0.0351  83  PRO A N     
671  C  CA    . PRO A 83  ? 0.1293 0.1776 0.1479 0.0574  0.0042  0.0261  83  PRO A CA    
672  C  C     . PRO A 83  ? 0.1259 0.1831 0.1427 0.0640  0.0165  -0.0071 83  PRO A C     
673  O  O     . PRO A 83  ? 0.1574 0.2453 0.1655 0.0312  -0.0338 -0.0018 83  PRO A O     
674  C  CB    . PRO A 83  ? 0.1224 0.1763 0.1555 0.0407  -0.0173 0.0140  83  PRO A CB    
675  C  CG    . PRO A 83  ? 0.0811 0.1460 0.1474 0.0241  0.0025  0.0180  83  PRO A CG    
676  C  CD    . PRO A 83  ? 0.0804 0.1404 0.1724 0.0221  0.0319  0.0414  83  PRO A CD    
677  N  N     . LEU A 84  ? 0.1223 0.1333 0.1140 0.0286  0.0135  -0.0240 84  LEU A N     
678  C  CA    . LEU A 84  ? 0.1006 0.1230 0.1416 0.0179  -0.0196 -0.0132 84  LEU A CA    
679  C  C     . LEU A 84  ? 0.1504 0.1719 0.1582 0.0221  0.0116  -0.0604 84  LEU A C     
680  O  O     . LEU A 84  ? 0.1641 0.1802 0.2669 0.0260  0.0512  -0.0860 84  LEU A O     
681  C  CB    . LEU A 84  ? 0.0819 0.0963 0.1422 0.0080  0.0150  -0.0102 84  LEU A CB    
682  C  CG    . LEU A 84  ? 0.0938 0.1080 0.1266 0.0143  0.0039  -0.0207 84  LEU A CG    
683  C  CD1   . LEU A 84  ? 0.0946 0.1195 0.1561 0.0226  0.0050  -0.0191 84  LEU A CD1   
684  C  CD2   . LEU A 84  ? 0.0897 0.0986 0.1392 0.0216  0.0183  -0.0208 84  LEU A CD2   
685  N  N     . ASP A 85  ? 0.1527 0.1656 0.1695 0.0339  -0.0096 -0.0838 85  ASP A N     
686  C  CA    . ASP A 85  ? 0.2265 0.1240 0.2433 -0.0042 0.0502  -0.0783 85  ASP A CA    
687  C  C     . ASP A 85  ? 0.2062 0.0849 0.3390 0.0237  0.0738  -0.0211 85  ASP A C     
688  O  O     . ASP A 85  ? 0.2679 0.3090 0.3561 0.0168  0.1144  -0.0743 85  ASP A O     
689  C  CB    . ASP A 85  ? 0.3717 0.1837 0.2704 0.0357  -0.0025 -0.1202 85  ASP A CB    
690  C  CG    . ASP A 85  ? 0.4336 0.2610 0.4385 0.1864  -0.0043 -0.0492 85  ASP A CG    
691  O  OD1   . ASP A 85  ? 0.4397 0.9430 0.6471 -0.1737 -0.1051 -0.2801 85  ASP A OD1   
692  O  OD2   . ASP A 85  ? 0.4160 0.7387 0.9019 0.1944  -0.0871 -0.0803 85  ASP A OD2   
693  N  N     . GLY A 86  ? 0.2625 0.2605 0.3126 -0.0321 -0.0218 -0.0765 86  GLY A N     
694  C  CA    . GLY A 86  ? 0.2822 0.2288 0.2624 -0.0634 0.0303  -0.0512 86  GLY A CA    
695  C  C     . GLY A 86  ? 0.3066 0.2083 0.2443 -0.0358 -0.0366 -0.0376 86  GLY A C     
696  O  O     . GLY A 86  ? 0.3607 0.2834 0.2473 -0.1039 -0.0402 -0.0324 86  GLY A O     
697  N  N     . THR A 87  ? 0.1288 0.1513 0.2254 0.0230  -0.0410 -0.0732 87  THR A N     
698  C  CA    . THR A 87  ? 0.1302 0.1764 0.2081 0.0141  -0.0088 -0.0734 87  THR A CA    
699  C  C     . THR A 87  ? 0.1081 0.1262 0.1823 0.0227  -0.0389 -0.0485 87  THR A C     
700  O  O     . THR A 87  ? 0.1320 0.0960 0.2356 0.0086  -0.0281 -0.0468 87  THR A O     
701  C  CB    . THR A 87  ? 0.1517 0.4260 0.2172 0.1613  -0.0947 -0.0743 87  THR A CB    
702  O  OG1   . THR A 87  ? 0.2849 0.4815 0.4026 0.2662  -0.0413 -0.1711 87  THR A OG1   
703  C  CG2   . THR A 87  ? 0.2730 0.2809 0.2744 0.1759  -0.0656 -0.0917 87  THR A CG2   
704  N  N     . TYR A 88  ? 0.0852 0.0957 0.1616 0.0187  -0.0286 -0.0180 88  TYR A N     
705  C  CA    . TYR A 88  ? 0.0735 0.0943 0.1764 0.0148  -0.0323 -0.0145 88  TYR A CA    
706  C  C     . TYR A 88  ? 0.0762 0.0966 0.1926 0.0062  -0.0394 -0.0215 88  TYR A C     
707  O  O     . TYR A 88  ? 0.1236 0.1612 0.1961 -0.0480 -0.0614 0.0194  88  TYR A O     
708  C  CB    . TYR A 88  ? 0.0901 0.0846 0.1511 0.0099  -0.0075 -0.0182 88  TYR A CB    
709  C  CG    . TYR A 88  ? 0.0937 0.0930 0.1373 0.0112  -0.0120 -0.0310 88  TYR A CG    
710  C  CD1   . TYR A 88  ? 0.0938 0.1025 0.1476 0.0021  -0.0080 -0.0052 88  TYR A CD1   
711  C  CD2   . TYR A 88  ? 0.1031 0.0834 0.1131 0.0160  -0.0039 -0.0114 88  TYR A CD2   
712  C  CE1   . TYR A 88  ? 0.0819 0.1251 0.1305 0.0025  0.0066  -0.0163 88  TYR A CE1   
713  C  CE2   . TYR A 88  ? 0.0809 0.0894 0.1293 0.0038  -0.0060 -0.0132 88  TYR A CE2   
714  C  CZ    . TYR A 88  ? 0.0860 0.0909 0.1183 -0.0128 -0.0051 -0.0282 88  TYR A CZ    
715  O  OH    . TYR A 88  ? 0.0924 0.0966 0.1305 0.0056  -0.0092 -0.0145 88  TYR A OH    
716  N  N     . ARG A 89  ? 0.0832 0.1054 0.1746 0.0200  -0.0408 -0.0309 89  ARG A N     
717  C  CA    . ARG A 89  ? 0.1079 0.0722 0.1762 0.0198  -0.0615 0.0080  89  ARG A CA    
718  C  C     . ARG A 89  ? 0.1194 0.0590 0.1055 -0.0058 -0.0262 0.0266  89  ARG A C     
719  O  O     . ARG A 89  ? 0.0984 0.0789 0.1127 -0.0057 -0.0237 0.0063  89  ARG A O     
720  C  CB    . ARG A 89  ? 0.2481 0.1088 0.1889 0.0049  -0.1421 0.0384  89  ARG A CB    
721  C  CG    . ARG A 89  ? 0.2855 0.2491 0.3366 0.1102  0.0093  0.1063  89  ARG A CG    
722  C  CD    . ARG A 89  ? 0.2896 0.1522 0.2574 0.0948  0.0042  0.0847  89  ARG A CD    
723  N  NE    . ARG A 89  ? 0.3819 0.3468 0.1482 0.1990  -0.1228 -0.0540 89  ARG A NE    
724  C  CZ    . ARG A 89  ? 0.5133 0.2698 0.1918 0.2184  -0.0512 -0.0286 89  ARG A CZ    
725  N  NH1   . ARG A 89  ? 0.6758 0.2433 0.2039 0.2795  0.0125  -0.0223 89  ARG A NH1   
726  N  NH2   . ARG A 89  ? 0.5035 0.3952 0.2116 0.2973  -0.0840 -0.0427 89  ARG A NH2   
727  N  N     . LEU A 90  ? 0.0923 0.0902 0.1187 -0.0106 -0.0266 0.0097  90  LEU A N     
728  C  CA    . LEU A 90  ? 0.0954 0.0767 0.1057 -0.0131 -0.0246 0.0176  90  LEU A CA    
729  C  C     . LEU A 90  ? 0.1088 0.0826 0.0980 -0.0243 -0.0332 0.0313  90  LEU A C     
730  O  O     . LEU A 90  ? 0.1144 0.1403 0.1375 0.0009  -0.0325 0.0630  90  LEU A O     
731  C  CB    . LEU A 90  ? 0.1042 0.0791 0.0950 -0.0283 -0.0154 0.0252  90  LEU A CB    
732  C  CG    . LEU A 90  ? 0.1282 0.1032 0.0915 -0.0192 -0.0059 0.0093  90  LEU A CG    
733  C  CD1   . LEU A 90  ? 0.1478 0.1057 0.1083 -0.0042 -0.0212 -0.0038 90  LEU A CD1   
734  C  CD2   . LEU A 90  ? 0.1300 0.1535 0.1101 -0.0086 -0.0212 -0.0076 90  LEU A CD2   
735  N  N     . ILE A 91  ? 0.1161 0.0825 0.0862 0.0071  -0.0020 0.0120  91  ILE A N     
736  C  CA    . ILE A 91  ? 0.1291 0.0981 0.0788 0.0052  -0.0014 0.0172  91  ILE A CA    
737  C  C     . ILE A 91  ? 0.1257 0.0779 0.0880 -0.0007 -0.0027 0.0224  91  ILE A C     
738  O  O     . ILE A 91  ? 0.1423 0.0771 0.0856 0.0008  0.0022  0.0186  91  ILE A O     
739  C  CB    . ILE A 91  ? 0.1608 0.1041 0.0940 -0.0229 -0.0091 0.0122  91  ILE A CB    
740  C  CG1   . ILE A 91  ? 0.1869 0.1675 0.1088 -0.0740 0.0026  0.0071  91  ILE A CG1   
741  C  CG2   . ILE A 91  ? 0.1323 0.1367 0.1048 -0.0152 -0.0198 -0.0111 91  ILE A CG2   
742  C  CD1   . ILE A 91  ? 0.2394 0.2694 0.1079 -0.1467 0.0027  0.0318  91  ILE A CD1   
743  N  N     . GLN A 92  ? 0.1178 0.0730 0.0879 -0.0069 -0.0005 0.0195  92  GLN A N     
744  C  CA    . GLN A 92  ? 0.1574 0.0746 0.1079 0.0099  0.0150  0.0190  92  GLN A CA    
745  C  C     . GLN A 92  ? 0.1451 0.0742 0.0820 0.0156  0.0061  0.0183  92  GLN A C     
746  O  O     . GLN A 92  ? 0.1333 0.0685 0.0820 -0.0114 -0.0003 0.0046  92  GLN A O     
747  C  CB    . GLN A 92  ? 0.1409 0.1207 0.1628 -0.0107 -0.0077 0.0417  92  GLN A CB    
748  C  CG    . GLN A 92  ? 0.1578 0.0947 0.1994 -0.0593 -0.0258 0.0493  92  GLN A CG    
749  C  CD    . GLN A 92  ? 0.1454 0.1217 0.1467 -0.0267 -0.0347 0.0249  92  GLN A CD    
750  O  OE1   . GLN A 92  ? 0.1732 0.0844 0.1356 0.0025  0.0219  0.0118  92  GLN A OE1   
751  N  NE2   . GLN A 92  ? 0.1607 0.1235 0.2798 -0.0245 -0.0495 0.0462  92  GLN A NE2   
752  N  N     . PHE A 93  ? 0.1649 0.0821 0.0525 0.0228  0.0079  0.0190  93  PHE A N     
753  C  CA    . PHE A 93  ? 0.1535 0.0762 0.0471 0.0192  -0.0023 0.0148  93  PHE A CA    
754  C  C     . PHE A 93  ? 0.1409 0.0854 0.0777 0.0161  0.0164  0.0297  93  PHE A C     
755  O  O     . PHE A 93  ? 0.2029 0.1148 0.0751 0.0303  0.0042  0.0249  93  PHE A O     
756  C  CB    . PHE A 93  ? 0.1451 0.0804 0.0711 0.0039  -0.0149 0.0139  93  PHE A CB    
757  C  CG    . PHE A 93  ? 0.1338 0.1130 0.0886 0.0184  -0.0189 -0.0059 93  PHE A CG    
758  C  CD1   . PHE A 93  ? 0.1742 0.0913 0.1077 0.0216  -0.0418 -0.0120 93  PHE A CD1   
759  C  CD2   . PHE A 93  ? 0.1728 0.1298 0.1055 0.0358  -0.0589 0.0075  93  PHE A CD2   
760  C  CE1   . PHE A 93  ? 0.1714 0.1292 0.1222 0.0351  -0.0499 -0.0298 93  PHE A CE1   
761  C  CE2   . PHE A 93  ? 0.1783 0.1044 0.1067 0.0533  -0.0488 0.0008  93  PHE A CE2   
762  C  CZ    . PHE A 93  ? 0.2156 0.1148 0.1059 0.0470  -0.0653 -0.0310 93  PHE A CZ    
763  N  N     . HIS A 94  ? 0.1421 0.0735 0.0532 0.0226  0.0009  0.0099  94  HIS A N     
764  C  CA    . HIS A 94  ? 0.1294 0.0682 0.0646 0.0127  0.0040  0.0041  94  HIS A CA    
765  C  C     . HIS A 94  ? 0.0883 0.0732 0.0731 0.0102  -0.0078 0.0048  94  HIS A C     
766  O  O     . HIS A 94  ? 0.1341 0.0653 0.0743 0.0176  0.0122  0.0050  94  HIS A O     
767  C  CB    . HIS A 94  ? 0.1452 0.0864 0.0728 0.0257  0.0167  0.0084  94  HIS A CB    
768  C  CG    . HIS A 94  ? 0.1212 0.0842 0.0867 0.0000  0.0221  0.0116  94  HIS A CG    
769  N  ND1   . HIS A 94  ? 0.0998 0.0813 0.0930 0.0036  0.0194  0.0182  94  HIS A ND1   
770  C  CD2   . HIS A 94  ? 0.0859 0.0770 0.0974 0.0107  0.0126  -0.0080 94  HIS A CD2   
771  C  CE1   . HIS A 94  ? 0.1167 0.0539 0.1002 -0.0158 -0.0040 0.0000  94  HIS A CE1   
772  N  NE2   . HIS A 94  ? 0.0762 0.0714 0.0988 -0.0044 0.0282  0.0108  94  HIS A NE2   
773  N  N     . PHE A 95  ? 0.1118 0.0683 0.0669 0.0043  0.0243  0.0127  95  PHE A N     
774  C  CA    . PHE A 95  ? 0.1268 0.0758 0.0590 -0.0118 0.0109  0.0167  95  PHE A CA    
775  C  C     . PHE A 95  ? 0.1300 0.0597 0.0738 -0.0117 0.0183  -0.0057 95  PHE A C     
776  O  O     . PHE A 95  ? 0.1166 0.0819 0.1012 0.0063  0.0240  0.0100  95  PHE A O     
777  C  CB    . PHE A 95  ? 0.1387 0.0811 0.0757 0.0084  -0.0036 -0.0084 95  PHE A CB    
778  C  CG    . PHE A 95  ? 0.1273 0.0839 0.0687 0.0019  -0.0092 -0.0078 95  PHE A CG    
779  C  CD1   . PHE A 95  ? 0.1173 0.0990 0.0918 0.0019  -0.0125 0.0022  95  PHE A CD1   
780  C  CD2   . PHE A 95  ? 0.1283 0.0843 0.0978 -0.0117 -0.0089 -0.0299 95  PHE A CD2   
781  C  CE1   . PHE A 95  ? 0.1153 0.1119 0.0880 0.0090  -0.0219 0.0000  95  PHE A CE1   
782  C  CE2   . PHE A 95  ? 0.1332 0.0987 0.1007 0.0109  -0.0105 -0.0189 95  PHE A CE2   
783  C  CZ    . PHE A 95  ? 0.1078 0.0905 0.1020 0.0080  -0.0132 -0.0203 95  PHE A CZ    
784  N  N     . HIS A 96  ? 0.0950 0.0760 0.0629 0.0019  0.0016  -0.0031 96  HIS A N     
785  C  CA    . HIS A 96  ? 0.0927 0.0769 0.0728 -0.0061 0.0101  0.0100  96  HIS A CA    
786  C  C     . HIS A 96  ? 0.1006 0.0779 0.0678 -0.0146 0.0199  -0.0028 96  HIS A C     
787  O  O     . HIS A 96  ? 0.0952 0.0611 0.0830 -0.0069 0.0166  -0.0010 96  HIS A O     
788  C  CB    . HIS A 96  ? 0.0895 0.0750 0.0896 -0.0006 0.0051  -0.0137 96  HIS A CB    
789  C  CG    . HIS A 96  ? 0.0924 0.0651 0.0741 -0.0077 0.0148  0.0007  96  HIS A CG    
790  N  ND1   . HIS A 96  ? 0.0839 0.0624 0.1138 -0.0064 0.0211  -0.0012 96  HIS A ND1   
791  C  CD2   . HIS A 96  ? 0.0714 0.0743 0.0703 -0.0102 0.0086  -0.0051 96  HIS A CD2   
792  C  CE1   . HIS A 96  ? 0.0806 0.0614 0.1221 -0.0191 0.0295  -0.0027 96  HIS A CE1   
793  N  NE2   . HIS A 96  ? 0.0926 0.0675 0.0862 -0.0125 0.0221  -0.0054 96  HIS A NE2   
794  N  N     . TRP A 97  ? 0.0895 0.0681 0.0717 -0.0190 0.0155  0.0017  97  TRP A N     
795  C  CA    . TRP A 97  ? 0.0977 0.0587 0.0841 0.0071  0.0112  -0.0051 97  TRP A CA    
796  C  C     . TRP A 97  ? 0.0839 0.0729 0.0835 0.0001  0.0116  -0.0029 97  TRP A C     
797  O  O     . TRP A 97  ? 0.0927 0.0692 0.1016 -0.0090 0.0224  -0.0041 97  TRP A O     
798  C  CB    . TRP A 97  ? 0.1131 0.0734 0.0881 -0.0012 0.0132  -0.0086 97  TRP A CB    
799  C  CG    . TRP A 97  ? 0.1083 0.0674 0.0893 0.0026  0.0137  -0.0146 97  TRP A CG    
800  C  CD1   . TRP A 97  ? 0.1339 0.0627 0.1022 0.0070  0.0263  -0.0140 97  TRP A CD1   
801  C  CD2   . TRP A 97  ? 0.1230 0.0717 0.0789 -0.0114 0.0092  -0.0112 97  TRP A CD2   
802  N  NE1   . TRP A 97  ? 0.1509 0.0821 0.0828 -0.0093 0.0310  -0.0210 97  TRP A NE1   
803  C  CE2   . TRP A 97  ? 0.1492 0.0931 0.0837 -0.0039 0.0224  -0.0250 97  TRP A CE2   
804  C  CE3   . TRP A 97  ? 0.1158 0.0743 0.0653 0.0074  0.0142  0.0012  97  TRP A CE3   
805  C  CZ2   . TRP A 97  ? 0.1402 0.1029 0.0954 -0.0090 0.0211  -0.0059 97  TRP A CZ2   
806  C  CZ3   . TRP A 97  ? 0.1528 0.0841 0.0823 -0.0044 0.0068  0.0016  97  TRP A CZ3   
807  C  CH2   . TRP A 97  ? 0.1518 0.0736 0.0810 -0.0219 0.0176  0.0121  97  TRP A CH2   
808  N  N     . GLY A 98  ? 0.1032 0.0621 0.0948 0.0011  0.0261  0.0015  98  GLY A N     
809  C  CA    . GLY A 98  ? 0.1021 0.0670 0.0983 0.0045  0.0283  0.0006  98  GLY A CA    
810  C  C     . GLY A 98  ? 0.1186 0.0723 0.1079 -0.0066 0.0153  -0.0093 98  GLY A C     
811  O  O     . GLY A 98  ? 0.1375 0.0756 0.1084 -0.0118 0.0136  -0.0112 98  GLY A O     
812  N  N     . SER A 99  ? 0.1216 0.0595 0.1044 -0.0040 0.0089  -0.0116 99  SER A N     
813  C  CA    . SER A 99  ? 0.1365 0.0694 0.1213 -0.0065 0.0334  -0.0270 99  SER A CA    
814  C  C     . SER A 99  ? 0.1548 0.0732 0.1253 -0.0163 0.0274  -0.0265 99  SER A C     
815  O  O     . SER A 99  ? 0.2147 0.1085 0.1258 -0.0286 0.0209  -0.0233 99  SER A O     
816  C  CB    . SER A 99  ? 0.1501 0.0791 0.1397 -0.0066 0.0332  -0.0526 99  SER A CB    
817  O  OG    . SER A 99  ? 0.1246 0.1093 0.1780 0.0021  0.0386  -0.0287 99  SER A OG    
818  N  N     . LEU A 100 ? 0.1085 0.0790 0.1254 -0.0102 0.0269  -0.0148 100 LEU A N     
819  C  CA    . LEU A 100 ? 0.1554 0.0648 0.1639 -0.0169 0.0471  -0.0268 100 LEU A CA    
820  C  C     . LEU A 100 ? 0.1376 0.0535 0.1413 0.0082  0.0206  -0.0116 100 LEU A C     
821  O  O     . LEU A 100 ? 0.1338 0.0635 0.1384 -0.0117 0.0302  -0.0189 100 LEU A O     
822  C  CB    . LEU A 100 ? 0.2261 0.0929 0.2284 0.0146  0.1093  0.0085  100 LEU A CB    
823  C  CG    . LEU A 100 ? 0.3067 0.1660 0.3507 0.0886  0.1627  0.0897  100 LEU A CG    
824  C  CD1   . LEU A 100 ? 0.3537 0.3599 0.4436 0.1308  0.1421  0.1117  100 LEU A CD1   
825  C  CD2   . LEU A 100 ? 0.3311 0.3336 0.4110 -0.0048 0.2017  -0.1269 100 LEU A CD2   
826  N  N     . ASP A 101 ? 0.1306 0.0681 0.1549 -0.0092 -0.0041 0.0062  101 ASP A N     
827  C  CA    . ASP A 101 ? 0.1233 0.0844 0.1715 0.0046  -0.0076 0.0387  101 ASP A CA    
828  C  C     . ASP A 101 ? 0.1225 0.0691 0.1678 -0.0044 0.0097  0.0298  101 ASP A C     
829  O  O     . ASP A 101 ? 0.1324 0.1130 0.1670 0.0194  0.0313  0.0372  101 ASP A O     
830  C  CB    . ASP A 101 ? 0.1135 0.1032 0.2019 -0.0010 0.0161  0.0497  101 ASP A CB    
831  C  CG    . ASP A 101 ? 0.1369 0.1263 0.2580 -0.0278 -0.0280 0.0798  101 ASP A CG    
832  O  OD1   . ASP A 101 ? 0.1500 0.1311 0.1883 -0.0403 -0.0232 0.0513  101 ASP A OD1   
833  O  OD2   . ASP A 101 ? 0.1704 0.1943 0.3178 -0.0662 -0.0707 0.1007  101 ASP A OD2   
834  N  N     . GLY A 102 ? 0.1490 0.0769 0.1696 0.0103  0.0000  0.0303  102 GLY A N     
835  C  CA    . GLY A 102 ? 0.1681 0.0871 0.1513 0.0261  0.0332  0.0175  102 GLY A CA    
836  C  C     . GLY A 102 ? 0.1336 0.0871 0.1429 0.0378  0.0208  0.0376  102 GLY A C     
837  O  O     . GLY A 102 ? 0.1821 0.1131 0.1429 0.0197  0.0357  0.0277  102 GLY A O     
838  N  N     A GLN A 103 ? 0.0911 0.0985 0.1278 0.0193  0.0139  0.0268  103 GLN A N     
839  N  N     B GLN A 103 ? 0.1104 0.0986 0.1280 0.0125  0.0112  0.0275  103 GLN A N     
840  C  CA    A GLN A 103 ? 0.1021 0.1043 0.1095 0.0109  0.0298  0.0165  103 GLN A CA    
841  C  CA    B GLN A 103 ? 0.1112 0.1035 0.1159 0.0149  0.0159  0.0107  103 GLN A CA    
842  C  C     A GLN A 103 ? 0.0685 0.0815 0.0984 0.0022  0.0228  -0.0005 103 GLN A C     
843  C  C     B GLN A 103 ? 0.0686 0.0802 0.1104 0.0015  0.0154  -0.0014 103 GLN A C     
844  O  O     A GLN A 103 ? 0.1402 0.0857 0.1084 0.0000  0.0012  0.0065  103 GLN A O     
845  O  O     B GLN A 103 ? 0.1265 0.0761 0.1249 0.0019  0.0027  -0.0115 103 GLN A O     
846  C  CB    A GLN A 103 ? 0.1054 0.1053 0.1235 0.0105  0.0268  0.0153  103 GLN A CB    
847  C  CB    B GLN A 103 ? 0.1141 0.1125 0.1447 0.0216  0.0042  0.0225  103 GLN A CB    
848  C  CG    A GLN A 103 ? 0.1600 0.0845 0.1322 0.0015  0.0536  0.0144  103 GLN A CG    
849  C  CG    B GLN A 103 ? 0.1420 0.1195 0.1491 0.0310  0.0245  0.0257  103 GLN A CG    
850  C  CD    A GLN A 103 ? 0.1855 0.0562 0.1779 0.0020  0.0603  0.0259  103 GLN A CD    
851  C  CD    B GLN A 103 ? 0.1750 0.1173 0.1871 0.0473  0.0768  0.0409  103 GLN A CD    
852  O  OE1   A GLN A 103 ? 0.1709 0.1418 0.1932 0.0031  0.0518  0.0375  103 GLN A OE1   
853  O  OE1   B GLN A 103 ? 0.1701 0.1544 0.2713 0.0600  0.1111  0.0885  103 GLN A OE1   
854  N  NE2   A GLN A 103 ? 0.1398 0.0663 0.2125 0.0287  0.1017  0.0549  103 GLN A NE2   
855  N  NE2   B GLN A 103 ? 0.1806 0.1627 0.2675 0.0213  0.0706  0.0818  103 GLN A NE2   
856  N  N     . GLY A 104 ? 0.0968 0.0826 0.0934 0.0097  0.0170  -0.0080 104 GLY A N     
857  C  CA    . GLY A 104 ? 0.0990 0.0903 0.0773 -0.0139 0.0157  -0.0091 104 GLY A CA    
858  C  C     . GLY A 104 ? 0.0849 0.0805 0.0812 -0.0062 0.0020  0.0017  104 GLY A C     
859  O  O     . GLY A 104 ? 0.1010 0.0854 0.0946 -0.0157 0.0106  0.0052  104 GLY A O     
860  N  N     . SER A 105 ? 0.0827 0.0621 0.0768 -0.0144 0.0055  0.0020  105 SER A N     
861  C  CA    . SER A 105 ? 0.0895 0.0735 0.0616 -0.0047 0.0028  -0.0023 105 SER A CA    
862  C  C     . SER A 105 ? 0.0850 0.0548 0.0730 -0.0190 0.0124  0.0026  105 SER A C     
863  O  O     . SER A 105 ? 0.0941 0.0702 0.0926 0.0037  -0.0017 -0.0072 105 SER A O     
864  C  CB    . SER A 105 ? 0.0898 0.0629 0.0762 -0.0128 0.0069  -0.0013 105 SER A CB    
865  O  OG    . SER A 105 ? 0.0852 0.0730 0.0858 0.0014  0.0179  0.0113  105 SER A OG    
866  N  N     . GLU A 106 ? 0.0715 0.0592 0.0814 0.0034  0.0006  -0.0070 106 GLU A N     
867  C  CA    . GLU A 106 ? 0.0603 0.0703 0.0759 -0.0101 0.0010  0.0054  106 GLU A CA    
868  C  C     . GLU A 106 ? 0.0635 0.0606 0.0804 -0.0012 0.0056  0.0060  106 GLU A C     
869  O  O     . GLU A 106 ? 0.0748 0.0783 0.0800 0.0011  -0.0004 -0.0012 106 GLU A O     
870  C  CB    . GLU A 106 ? 0.0686 0.0658 0.0746 -0.0179 0.0118  -0.0025 106 GLU A CB    
871  C  CG    . GLU A 106 ? 0.1099 0.0886 0.0859 -0.0080 0.0259  0.0145  106 GLU A CG    
872  C  CD    . GLU A 106 ? 0.0688 0.0750 0.0738 -0.0069 0.0038  0.0001  106 GLU A CD    
873  O  OE1   . GLU A 106 ? 0.0738 0.0689 0.0908 -0.0132 0.0107  -0.0040 106 GLU A OE1   
874  O  OE2   . GLU A 106 ? 0.0750 0.0977 0.1165 -0.0011 0.0254  -0.0019 106 GLU A OE2   
875  N  N     . HIS A 107 ? 0.0678 0.0606 0.0645 -0.0007 0.0098  0.0089  107 HIS A N     
876  C  CA    . HIS A 107 ? 0.0732 0.0599 0.0635 0.0070  0.0143  0.0019  107 HIS A CA    
877  C  C     . HIS A 107 ? 0.0612 0.0711 0.0774 -0.0043 0.0133  0.0117  107 HIS A C     
878  O  O     . HIS A 107 ? 0.0861 0.0680 0.0787 0.0028  0.0144  0.0097  107 HIS A O     
879  C  CB    . HIS A 107 ? 0.0695 0.0663 0.0680 0.0118  0.0045  0.0034  107 HIS A CB    
880  C  CG    . HIS A 107 ? 0.0526 0.0701 0.0701 0.0043  0.0093  -0.0015 107 HIS A CG    
881  N  ND1   . HIS A 107 ? 0.0834 0.0674 0.0723 -0.0050 -0.0026 0.0050  107 HIS A ND1   
882  C  CD2   . HIS A 107 ? 0.0509 0.0800 0.0655 0.0097  -0.0117 0.0074  107 HIS A CD2   
883  C  CE1   . HIS A 107 ? 0.0759 0.0659 0.0841 0.0026  -0.0072 -0.0031 107 HIS A CE1   
884  N  NE2   . HIS A 107 ? 0.0555 0.0678 0.0784 -0.0020 -0.0112 -0.0154 107 HIS A NE2   
885  N  N     . THR A 108 ? 0.0990 0.0655 0.0774 -0.0019 0.0119  0.0003  108 THR A N     
886  C  CA    . THR A 108 ? 0.0968 0.0676 0.0811 -0.0022 -0.0021 0.0111  108 THR A CA    
887  C  C     . THR A 108 ? 0.0706 0.0575 0.0790 0.0029  -0.0061 0.0045  108 THR A C     
888  O  O     . THR A 108 ? 0.0763 0.0716 0.0849 -0.0009 0.0063  0.0100  108 THR A O     
889  C  CB    . THR A 108 ? 0.0856 0.0841 0.0862 0.0007  -0.0001 0.0198  108 THR A CB    
890  O  OG1   . THR A 108 ? 0.0952 0.0743 0.0855 0.0048  -0.0031 0.0122  108 THR A OG1   
891  C  CG2   . THR A 108 ? 0.1183 0.0767 0.0947 0.0028  0.0036  0.0132  108 THR A CG2   
892  N  N     . VAL A 109 ? 0.0970 0.0589 0.0830 -0.0031 0.0155  0.0061  109 VAL A N     
893  C  CA    . VAL A 109 ? 0.0892 0.1039 0.0898 -0.0090 0.0085  0.0124  109 VAL A CA    
894  C  C     . VAL A 109 ? 0.1128 0.0783 0.0819 -0.0043 0.0278  0.0092  109 VAL A C     
895  O  O     . VAL A 109 ? 0.1100 0.0822 0.1013 -0.0025 0.0128  0.0038  109 VAL A O     
896  C  CB    . VAL A 109 ? 0.0867 0.1006 0.0983 -0.0079 0.0009  0.0165  109 VAL A CB    
897  C  CG1   . VAL A 109 ? 0.1044 0.1026 0.1315 -0.0084 0.0131  0.0308  109 VAL A CG1   
898  C  CG2   . VAL A 109 ? 0.1151 0.1095 0.1270 -0.0032 -0.0043 0.0287  109 VAL A CG2   
899  N  N     . ASP A 110 ? 0.1330 0.0793 0.0802 0.0140  0.0199  0.0219  110 ASP A N     
900  C  CA    . ASP A 110 ? 0.1539 0.0928 0.0672 0.0032  0.0310  0.0375  110 ASP A CA    
901  C  C     . ASP A 110 ? 0.1476 0.0839 0.0926 0.0155  0.0252  0.0285  110 ASP A C     
902  O  O     . ASP A 110 ? 0.1426 0.0831 0.1196 0.0185  0.0200  0.0315  110 ASP A O     
903  C  CB    . ASP A 110 ? 0.1567 0.0880 0.1146 0.0153  0.0493  0.0407  110 ASP A CB    
904  C  CG    . ASP A 110 ? 0.1886 0.1004 0.0894 0.0239  0.0482  0.0388  110 ASP A CG    
905  O  OD1   . ASP A 110 ? 0.1905 0.1232 0.1210 0.0211  0.0566  0.0308  110 ASP A OD1   
906  O  OD2   . ASP A 110 ? 0.1634 0.1799 0.1491 0.0372  0.0627  0.0184  110 ASP A OD2   
907  N  N     . LYS A 111 ? 0.1191 0.0902 0.0973 0.0196  0.0143  0.0357  111 LYS A N     
908  C  CA    . LYS A 111 ? 0.1204 0.0955 0.1050 0.0109  0.0233  0.0461  111 LYS A CA    
909  C  C     . LYS A 111 ? 0.1480 0.0957 0.1097 0.0385  0.0260  0.0363  111 LYS A C     
910  O  O     . LYS A 111 ? 0.1343 0.1190 0.1309 0.0294  0.0401  0.0298  111 LYS A O     
911  C  CB    . LYS A 111 ? 0.1613 0.1396 0.1115 0.0353  0.0142  0.0523  111 LYS A CB    
912  C  CG    . LYS A 111 ? 0.2030 0.1655 0.1418 0.0887  -0.0215 0.0312  111 LYS A CG    
913  C  CD    . LYS A 111 ? 0.1759 0.2204 0.2613 0.0101  -0.0293 -0.0056 111 LYS A CD    
914  C  CE    . LYS A 111 ? 0.1903 0.2601 0.2345 0.0195  -0.0575 0.0212  111 LYS A CE    
915  N  NZ    . LYS A 111 ? 0.2169 0.2694 0.2867 0.0168  -0.0656 0.0617  111 LYS A NZ    
916  N  N     . LYS A 112 ? 0.1553 0.0740 0.0877 0.0120  0.0411  0.0139  112 LYS A N     
917  C  CA    . LYS A 112 ? 0.1642 0.0902 0.0904 0.0063  0.0326  0.0038  112 LYS A CA    
918  C  C     . LYS A 112 ? 0.0854 0.0794 0.1131 0.0069  0.0121  0.0099  112 LYS A C     
919  O  O     . LYS A 112 ? 0.0998 0.0731 0.1131 0.0048  0.0116  0.0033  112 LYS A O     
920  C  CB    . LYS A 112 ? 0.1593 0.1095 0.1444 -0.0581 0.0497  -0.0305 112 LYS A CB    
921  C  CG    . LYS A 112 ? 0.1647 0.1788 0.1424 -0.0804 0.0718  -0.0685 112 LYS A CG    
922  C  CD    . LYS A 112 ? 0.1887 0.1759 0.1562 -0.0178 0.0191  0.0139  112 LYS A CD    
923  C  CE    . LYS A 112 ? 0.2328 0.1538 0.1962 -0.0301 -0.0096 -0.0297 112 LYS A CE    
924  N  NZ    . LYS A 112 ? 0.2031 0.1347 0.2016 -0.0183 -0.0111 0.0399  112 LYS A NZ    
925  N  N     . LYS A 113 ? 0.1058 0.0780 0.0887 0.0235  0.0034  0.0081  113 LYS A N     
926  C  CA    . LYS A 113 ? 0.1010 0.0946 0.0940 0.0095  0.0126  0.0200  113 LYS A CA    
927  C  C     . LYS A 113 ? 0.1258 0.0651 0.1195 -0.0014 0.0090  0.0168  113 LYS A C     
928  O  O     . LYS A 113 ? 0.1702 0.0693 0.1411 -0.0048 -0.0214 0.0148  113 LYS A O     
929  C  CB    . LYS A 113 ? 0.1104 0.1101 0.1019 0.0161  0.0118  0.0105  113 LYS A CB    
930  C  CG    . LYS A 113 ? 0.1039 0.1268 0.1027 0.0169  0.0213  0.0208  113 LYS A CG    
931  C  CD    . LYS A 113 ? 0.1013 0.1326 0.1466 0.0268  0.0336  0.0250  113 LYS A CD    
932  C  CE    . LYS A 113 ? 0.0971 0.1407 0.2692 0.0323  0.0030  0.0013  113 LYS A CE    
933  N  NZ    . LYS A 113 ? 0.1927 0.2321 0.3664 0.0101  -0.1400 0.0072  113 LYS A NZ    
934  N  N     . TYR A 114 ? 0.0916 0.0785 0.0999 0.0077  0.0064  0.0079  114 TYR A N     
935  C  CA    . TYR A 114 ? 0.0998 0.0776 0.1045 -0.0049 0.0022  0.0074  114 TYR A CA    
936  C  C     . TYR A 114 ? 0.0925 0.0602 0.0985 -0.0082 0.0073  -0.0194 114 TYR A C     
937  O  O     . TYR A 114 ? 0.0826 0.0931 0.1136 -0.0033 0.0235  -0.0059 114 TYR A O     
938  C  CB    . TYR A 114 ? 0.0973 0.0680 0.1176 -0.0060 0.0068  -0.0056 114 TYR A CB    
939  C  CG    . TYR A 114 ? 0.0950 0.0698 0.1204 0.0020  -0.0002 0.0051  114 TYR A CG    
940  C  CD1   . TYR A 114 ? 0.1361 0.0693 0.1299 -0.0102 0.0193  -0.0081 114 TYR A CD1   
941  C  CD2   . TYR A 114 ? 0.1231 0.0833 0.1269 -0.0238 0.0155  0.0049  114 TYR A CD2   
942  C  CE1   . TYR A 114 ? 0.1984 0.0743 0.1083 0.0259  0.0311  -0.0008 114 TYR A CE1   
943  C  CE2   . TYR A 114 ? 0.1164 0.0922 0.1609 -0.0002 0.0351  0.0077  114 TYR A CE2   
944  C  CZ    . TYR A 114 ? 0.2033 0.1187 0.1338 -0.0070 0.0596  -0.0004 114 TYR A CZ    
945  O  OH    . TYR A 114 ? 0.2350 0.1751 0.1924 0.0290  0.1175  0.0164  114 TYR A OH    
946  N  N     . ALA A 115 ? 0.0943 0.0599 0.0996 -0.0290 0.0108  -0.0057 115 ALA A N     
947  C  CA    . ALA A 115 ? 0.0982 0.0648 0.0963 -0.0013 0.0132  -0.0082 115 ALA A CA    
948  C  C     . ALA A 115 ? 0.1086 0.0635 0.0914 -0.0072 -0.0021 -0.0012 115 ALA A C     
949  O  O     . ALA A 115 ? 0.1242 0.0721 0.1118 -0.0033 0.0253  0.0013  115 ALA A O     
950  C  CB    . ALA A 115 ? 0.1067 0.0729 0.1120 -0.0017 0.0082  0.0021  115 ALA A CB    
951  N  N     . ALA A 116 ? 0.0971 0.0658 0.0883 -0.0101 0.0184  0.0064  116 ALA A N     
952  C  CA    . ALA A 116 ? 0.0836 0.0597 0.0898 -0.0093 0.0058  0.0052  116 ALA A CA    
953  C  C     . ALA A 116 ? 0.0743 0.0685 0.0938 -0.0164 -0.0022 -0.0035 116 ALA A C     
954  O  O     . ALA A 116 ? 0.0893 0.0784 0.0971 -0.0139 0.0026  0.0026  116 ALA A O     
955  C  CB    . ALA A 116 ? 0.0920 0.0747 0.1024 -0.0116 -0.0040 0.0032  116 ALA A CB    
956  N  N     . GLU A 117 ? 0.0911 0.0568 0.0663 -0.0101 0.0070  -0.0080 117 GLU A N     
957  C  CA    . GLU A 117 ? 0.0671 0.0543 0.0722 -0.0068 0.0059  -0.0023 117 GLU A CA    
958  C  C     . GLU A 117 ? 0.0827 0.0601 0.0662 -0.0120 0.0021  0.0019  117 GLU A C     
959  O  O     . GLU A 117 ? 0.0798 0.0870 0.0951 -0.0076 0.0133  0.0133  117 GLU A O     
960  C  CB    . GLU A 117 ? 0.0914 0.0695 0.0810 -0.0114 -0.0078 -0.0044 117 GLU A CB    
961  C  CG    . GLU A 117 ? 0.0706 0.0619 0.0776 -0.0053 -0.0038 0.0093  117 GLU A CG    
962  C  CD    . GLU A 117 ? 0.0684 0.0683 0.0670 0.0022  0.0090  0.0054  117 GLU A CD    
963  O  OE1   . GLU A 117 ? 0.0656 0.0920 0.0829 0.0019  -0.0123 0.0088  117 GLU A OE1   
964  O  OE2   . GLU A 117 ? 0.0889 0.0721 0.0745 -0.0097 -0.0049 0.0019  117 GLU A OE2   
965  N  N     . LEU A 118 ? 0.0854 0.0630 0.0717 -0.0097 -0.0016 0.0028  118 LEU A N     
966  C  CA    . LEU A 118 ? 0.0953 0.0605 0.0641 -0.0098 -0.0091 0.0044  118 LEU A CA    
967  C  C     . LEU A 118 ? 0.0844 0.0647 0.0681 -0.0049 0.0026  -0.0032 118 LEU A C     
968  O  O     . LEU A 118 ? 0.0850 0.0779 0.0650 0.0001  -0.0009 0.0067  118 LEU A O     
969  C  CB    . LEU A 118 ? 0.0955 0.0650 0.0885 -0.0056 -0.0167 0.0017  118 LEU A CB    
970  C  CG    . LEU A 118 ? 0.1013 0.0811 0.0952 0.0039  -0.0189 -0.0012 118 LEU A CG    
971  C  CD1   . LEU A 118 ? 0.1333 0.0777 0.0898 0.0190  -0.0253 0.0157  118 LEU A CD1   
972  C  CD2   . LEU A 118 ? 0.0981 0.1348 0.0978 0.0251  -0.0281 -0.0039 118 LEU A CD2   
973  N  N     . HIS A 119 ? 0.0828 0.0577 0.0547 0.0088  0.0063  0.0015  119 HIS A N     
974  C  CA    . HIS A 119 ? 0.0818 0.0586 0.0484 0.0000  0.0015  0.0043  119 HIS A CA    
975  C  C     . HIS A 119 ? 0.0646 0.0642 0.0687 -0.0067 -0.0033 0.0148  119 HIS A C     
976  O  O     . HIS A 119 ? 0.1011 0.0801 0.0715 0.0055  0.0093  0.0102  119 HIS A O     
977  C  CB    . HIS A 119 ? 0.0873 0.0617 0.0578 0.0053  0.0011  -0.0012 119 HIS A CB    
978  C  CG    . HIS A 119 ? 0.0552 0.0686 0.0687 -0.0041 0.0002  0.0022  119 HIS A CG    
979  N  ND1   . HIS A 119 ? 0.0538 0.0585 0.0715 -0.0176 0.0070  0.0064  119 HIS A ND1   
980  C  CD2   . HIS A 119 ? 0.0589 0.0879 0.0687 0.0015  0.0103  0.0083  119 HIS A CD2   
981  C  CE1   . HIS A 119 ? 0.0804 0.0515 0.0781 0.0022  0.0009  0.0009  119 HIS A CE1   
982  N  NE2   . HIS A 119 ? 0.0747 0.0755 0.0760 0.0058  -0.0002 0.0101  119 HIS A NE2   
983  N  N     . LEU A 120 ? 0.0778 0.0516 0.0712 -0.0001 -0.0042 0.0055  120 LEU A N     
984  C  CA    . LEU A 120 ? 0.0924 0.0662 0.0651 0.0019  -0.0121 0.0068  120 LEU A CA    
985  C  C     . LEU A 120 ? 0.0686 0.0543 0.0769 -0.0006 -0.0194 0.0130  120 LEU A C     
986  O  O     . LEU A 120 ? 0.0863 0.0567 0.0712 -0.0061 -0.0093 0.0015  120 LEU A O     
987  C  CB    . LEU A 120 ? 0.0885 0.0715 0.0978 0.0058  -0.0289 0.0052  120 LEU A CB    
988  C  CG    . LEU A 120 ? 0.1204 0.0862 0.1033 -0.0023 -0.0299 -0.0118 120 LEU A CG    
989  C  CD1   . LEU A 120 ? 0.1728 0.1278 0.1284 -0.0592 -0.0258 -0.0071 120 LEU A CD1   
990  C  CD2   . LEU A 120 ? 0.1372 0.1439 0.1195 0.0165  -0.0635 -0.0376 120 LEU A CD2   
991  N  N     . VAL A 121 ? 0.0927 0.0700 0.0669 -0.0080 -0.0089 0.0169  121 VAL A N     
992  C  CA    . VAL A 121 ? 0.1078 0.0587 0.0788 -0.0042 0.0012  0.0184  121 VAL A CA    
993  C  C     . VAL A 121 ? 0.0799 0.0613 0.0821 -0.0031 0.0028  0.0071  121 VAL A C     
994  O  O     . VAL A 121 ? 0.0988 0.0712 0.0821 0.0045  0.0035  0.0116  121 VAL A O     
995  C  CB    . VAL A 121 ? 0.0908 0.0778 0.0985 0.0034  0.0032  0.0115  121 VAL A CB    
996  C  CG1   . VAL A 121 ? 0.0945 0.0961 0.1256 -0.0137 0.0094  0.0181  121 VAL A CG1   
997  C  CG2   . VAL A 121 ? 0.1052 0.0761 0.1272 0.0062  0.0111  0.0237  121 VAL A CG2   
998  N  N     . HIS A 122 ? 0.0769 0.0628 0.0873 -0.0051 -0.0099 -0.0002 122 HIS A N     
999  C  CA    . HIS A 122 ? 0.0896 0.0567 0.0834 -0.0062 -0.0079 0.0020  122 HIS A CA    
1000 C  C     . HIS A 122 ? 0.0806 0.0609 0.0965 -0.0083 -0.0097 0.0046  122 HIS A C     
1001 O  O     . HIS A 122 ? 0.0871 0.0792 0.1020 -0.0117 -0.0291 0.0094  122 HIS A O     
1002 C  CB    . HIS A 122 ? 0.0831 0.0627 0.1179 0.0042  -0.0237 0.0165  122 HIS A CB    
1003 C  CG    . HIS A 122 ? 0.0715 0.0631 0.0964 -0.0096 -0.0049 0.0085  122 HIS A CG    
1004 N  ND1   . HIS A 122 ? 0.0635 0.0617 0.1124 0.0004  -0.0010 0.0062  122 HIS A ND1   
1005 C  CD2   . HIS A 122 ? 0.0721 0.0690 0.1215 0.0064  -0.0152 0.0051  122 HIS A CD2   
1006 C  CE1   . HIS A 122 ? 0.0632 0.0850 0.1207 -0.0068 0.0064  -0.0063 122 HIS A CE1   
1007 N  NE2   . HIS A 122 ? 0.0722 0.0878 0.1198 -0.0158 -0.0127 -0.0183 122 HIS A NE2   
1008 N  N     . TRP A 123 ? 0.0883 0.0666 0.0965 -0.0107 -0.0241 0.0043  123 TRP A N     
1009 C  CA    . TRP A 123 ? 0.0935 0.0668 0.0966 -0.0085 -0.0191 0.0019  123 TRP A CA    
1010 C  C     . TRP A 123 ? 0.0760 0.0823 0.0945 -0.0137 -0.0108 0.0043  123 TRP A C     
1011 O  O     . TRP A 123 ? 0.1036 0.0801 0.1407 -0.0064 -0.0452 -0.0065 123 TRP A O     
1012 C  CB    . TRP A 123 ? 0.1273 0.1105 0.1169 -0.0406 -0.0122 0.0198  123 TRP A CB    
1013 C  CG    . TRP A 123 ? 0.1519 0.0901 0.1215 -0.0487 -0.0246 0.0148  123 TRP A CG    
1014 C  CD1   . TRP A 123 ? 0.1935 0.0902 0.1208 -0.0649 -0.0332 0.0341  123 TRP A CD1   
1015 C  CD2   . TRP A 123 ? 0.2715 0.0706 0.1236 -0.0583 -0.0412 0.0081  123 TRP A CD2   
1016 N  NE1   . TRP A 123 ? 0.2837 0.0817 0.1027 -0.0384 -0.0483 0.0163  123 TRP A NE1   
1017 C  CE2   . TRP A 123 ? 0.2883 0.0831 0.1260 -0.0345 -0.0637 0.0123  123 TRP A CE2   
1018 C  CE3   . TRP A 123 ? 0.3291 0.0671 0.1419 -0.0680 -0.0584 0.0060  123 TRP A CE3   
1019 C  CZ2   . TRP A 123 ? 0.3838 0.0853 0.1645 -0.0348 -0.0728 0.0337  123 TRP A CZ2   
1020 C  CZ3   . TRP A 123 ? 0.4257 0.0773 0.1764 -0.0483 -0.0876 0.0061  123 TRP A CZ3   
1021 C  CH2   . TRP A 123 ? 0.5007 0.0585 0.1858 -0.0598 -0.0886 0.0414  123 TRP A CH2   
1022 N  N     . ASN A 124 ? 0.0846 0.0871 0.1237 0.0031  -0.0287 -0.0206 124 ASN A N     
1023 C  CA    . ASN A 124 ? 0.1089 0.0692 0.1328 0.0074  -0.0247 -0.0224 124 ASN A CA    
1024 C  C     . ASN A 124 ? 0.1006 0.0899 0.1306 0.0078  -0.0252 -0.0190 124 ASN A C     
1025 O  O     . ASN A 124 ? 0.1279 0.0792 0.1486 -0.0025 -0.0150 -0.0105 124 ASN A O     
1026 C  CB    . ASN A 124 ? 0.1071 0.0681 0.1361 0.0025  -0.0150 -0.0177 124 ASN A CB    
1027 C  CG    . ASN A 124 ? 0.1230 0.0830 0.1475 0.0135  -0.0010 -0.0067 124 ASN A CG    
1028 O  OD1   . ASN A 124 ? 0.1181 0.1068 0.1766 0.0291  -0.0238 -0.0348 124 ASN A OD1   
1029 N  ND2   . ASN A 124 ? 0.1433 0.1086 0.1303 0.0074  -0.0077 -0.0273 124 ASN A ND2   
1030 N  N     . THR A 125 ? 0.1271 0.0802 0.1792 0.0310  -0.0574 -0.0364 125 THR A N     
1031 C  CA    . THR A 125 ? 0.1683 0.0853 0.1838 0.0310  -0.0554 -0.0220 125 THR A CA    
1032 C  C     . THR A 125 ? 0.1669 0.0669 0.1986 0.0348  -0.0318 -0.0149 125 THR A C     
1033 O  O     . THR A 125 ? 0.1972 0.0746 0.2129 0.0283  -0.0673 -0.0053 125 THR A O     
1034 C  CB    . THR A 125 ? 0.1948 0.1425 0.2385 0.0208  -0.1277 -0.0025 125 THR A CB    
1035 O  OG1   . THR A 125 ? 0.2070 0.1739 0.3751 0.0805  -0.0762 -0.0695 125 THR A OG1   
1036 C  CG2   . THR A 125 ? 0.2501 0.1772 0.2593 0.0185  -0.1660 -0.0188 125 THR A CG2   
1037 N  N     . LYS A 126 ? 0.1842 0.0640 0.1707 0.0155  -0.0286 -0.0293 127 LYS A N     
1038 C  CA    . LYS A 126 ? 0.1789 0.0799 0.2038 0.0212  0.0099  -0.0677 127 LYS A CA    
1039 C  C     . LYS A 126 ? 0.1663 0.0503 0.1616 0.0087  -0.0005 -0.0051 127 LYS A C     
1040 O  O     . LYS A 126 ? 0.2199 0.0763 0.2410 -0.0084 0.0220  -0.0666 127 LYS A O     
1041 C  CB    . LYS A 126 ? 0.2284 0.1103 0.1994 -0.0061 -0.0050 -0.0403 127 LYS A CB    
1042 C  CG    . LYS A 126 ? 0.2077 0.1285 0.1916 -0.0201 -0.0248 -0.0319 127 LYS A CG    
1043 C  CD    . LYS A 126 ? 0.3734 0.2293 0.1672 -0.1000 -0.0454 -0.0302 127 LYS A CD    
1044 C  CE    . LYS A 126 ? 0.2711 0.3419 0.2672 -0.1053 -0.0143 -0.0350 127 LYS A CE    
1045 N  NZ    . LYS A 126 ? 0.4627 0.6869 0.2151 0.0258  -0.0497 0.0483  127 LYS A NZ    
1046 N  N     . TYR A 127 ? 0.1811 0.0706 0.1316 0.0176  -0.0368 -0.0341 128 TYR A N     
1047 C  CA    . TYR A 127 ? 0.1977 0.0720 0.1423 0.0114  -0.0309 -0.0001 128 TYR A CA    
1048 C  C     . TYR A 127 ? 0.1613 0.0602 0.1304 0.0124  -0.0371 -0.0332 128 TYR A C     
1049 O  O     . TYR A 127 ? 0.1708 0.1065 0.1575 0.0259  -0.0128 -0.0077 128 TYR A O     
1050 C  CB    . TYR A 127 ? 0.1481 0.0694 0.1453 -0.0031 -0.0062 -0.0127 128 TYR A CB    
1051 C  CG    . TYR A 127 ? 0.1610 0.0729 0.1394 0.0122  -0.0452 -0.0073 128 TYR A CG    
1052 C  CD1   . TYR A 127 ? 0.1707 0.1054 0.1432 -0.0156 -0.0337 -0.0172 128 TYR A CD1   
1053 C  CD2   . TYR A 127 ? 0.1220 0.0734 0.1409 0.0054  -0.0286 -0.0227 128 TYR A CD2   
1054 C  CE1   . TYR A 127 ? 0.1980 0.0942 0.1387 0.0196  -0.0559 -0.0319 128 TYR A CE1   
1055 C  CE2   . TYR A 127 ? 0.1479 0.1097 0.1346 0.0197  -0.0113 -0.0227 128 TYR A CE2   
1056 C  CZ    . TYR A 127 ? 0.1535 0.0928 0.1451 0.0400  -0.0157 -0.0275 128 TYR A CZ    
1057 O  OH    . TYR A 127 ? 0.2717 0.1142 0.1317 0.0405  -0.0466 -0.0342 128 TYR A OH    
1058 N  N     . GLY A 128 ? 0.1770 0.0794 0.1458 -0.0250 -0.0520 -0.0053 129 GLY A N     
1059 C  CA    . GLY A 128 ? 0.1779 0.0702 0.1735 -0.0069 0.0016  0.0219  129 GLY A CA    
1060 C  C     . GLY A 128 ? 0.2565 0.1075 0.1392 0.0201  -0.0364 0.0008  129 GLY A C     
1061 O  O     . GLY A 128 ? 0.3276 0.0847 0.1492 0.0137  -0.0632 0.0249  129 GLY A O     
1062 N  N     . ASP A 129 ? 0.2615 0.0878 0.1277 0.0114  -0.0422 -0.0132 130 ASP A N     
1063 C  CA    . ASP A 129 ? 0.2994 0.0858 0.1435 0.0263  -0.0392 -0.0081 130 ASP A CA    
1064 C  C     . ASP A 129 ? 0.3278 0.0871 0.1367 0.0192  -0.0772 -0.0171 130 ASP A C     
1065 O  O     . ASP A 129 ? 0.3239 0.1010 0.1136 0.0616  -0.0601 -0.0151 130 ASP A O     
1066 C  CB    . ASP A 129 ? 0.3288 0.0792 0.0964 0.0686  0.0083  -0.0081 130 ASP A CB    
1067 C  CG    . ASP A 129 ? 0.2700 0.1317 0.4580 0.0726  -0.0307 -0.1998 130 ASP A CG    
1068 O  OD1   . ASP A 129 ? 0.2441 0.1764 0.1924 0.0100  0.0124  -0.0027 130 ASP A OD1   
1069 O  OD2   . ASP A 129 ? 0.1770 0.1927 0.2573 0.0155  -0.0088 -0.0336 130 ASP A OD2   
1070 N  N     . PHE A 130 ? 0.2773 0.0656 0.1100 0.0073  -0.0306 0.0082  131 PHE A N     
1071 C  CA    . PHE A 130 ? 0.2098 0.0737 0.0909 0.0046  -0.0095 0.0008  131 PHE A CA    
1072 C  C     . PHE A 130 ? 0.2150 0.0726 0.1023 0.0037  0.0151  -0.0062 131 PHE A C     
1073 O  O     . PHE A 130 ? 0.2016 0.0943 0.1012 -0.0293 -0.0040 -0.0035 131 PHE A O     
1074 C  CB    . PHE A 130 ? 0.1790 0.0777 0.1335 -0.0031 -0.0181 -0.0222 131 PHE A CB    
1075 C  CG    . PHE A 130 ? 0.1625 0.0708 0.1128 -0.0033 0.0145  -0.0204 131 PHE A CG    
1076 C  CD1   . PHE A 130 ? 0.1352 0.1029 0.1326 -0.0236 0.0020  -0.0071 131 PHE A CD1   
1077 C  CD2   . PHE A 130 ? 0.1622 0.1038 0.1651 -0.0145 0.0381  -0.0063 131 PHE A CD2   
1078 C  CE1   . PHE A 130 ? 0.2015 0.1078 0.1471 -0.0318 -0.0107 0.0000  131 PHE A CE1   
1079 C  CE2   . PHE A 130 ? 0.2029 0.1357 0.1620 0.0433  0.0111  -0.0321 131 PHE A CE2   
1080 C  CZ    . PHE A 130 ? 0.2253 0.1164 0.2020 0.0110  -0.0286 -0.0463 131 PHE A CZ    
1081 N  N     . GLY A 131 ? 0.2301 0.0947 0.1164 -0.0171 0.0247  0.0100  132 GLY A N     
1082 C  CA    . GLY A 131 ? 0.2281 0.1068 0.1430 -0.0534 0.0513  0.0105  132 GLY A CA    
1083 C  C     . GLY A 131 ? 0.2023 0.1046 0.1345 -0.0484 0.0304  0.0109  132 GLY A C     
1084 O  O     . GLY A 131 ? 0.2031 0.1266 0.1948 -0.0533 0.0431  -0.0263 132 GLY A O     
1085 N  N     . LYS A 132 ? 0.2066 0.1034 0.1350 -0.0492 0.0050  0.0128  133 LYS A N     
1086 C  CA    . LYS A 132 ? 0.2129 0.0599 0.1296 -0.0527 -0.0059 -0.0026 133 LYS A CA    
1087 C  C     . LYS A 132 ? 0.1494 0.0884 0.1149 -0.0500 -0.0012 -0.0090 133 LYS A C     
1088 O  O     . LYS A 132 ? 0.1423 0.1094 0.1216 -0.0564 -0.0082 -0.0108 133 LYS A O     
1089 C  CB    . LYS A 132 ? 0.1907 0.0862 0.1455 -0.0442 0.0133  -0.0129 133 LYS A CB    
1090 C  CG    . LYS A 132 ? 0.1998 0.0946 0.2060 -0.0334 0.0120  0.0348  133 LYS A CG    
1091 C  CD    . LYS A 132 ? 0.1730 0.1557 0.3513 -0.0170 -0.0289 0.0545  133 LYS A CD    
1092 C  CE    . LYS A 132 ? 0.2688 0.2489 0.3914 -0.1262 -0.1562 0.1151  133 LYS A CE    
1093 N  NZ    . LYS A 132 ? 0.3632 0.3604 0.5714 -0.1234 0.0430  0.1715  133 LYS A NZ    
1094 N  N     . ALA A 133 ? 0.1467 0.0891 0.1157 -0.0470 -0.0117 0.0050  134 ALA A N     
1095 C  CA    . ALA A 133 ? 0.1291 0.1007 0.1013 -0.0308 0.0073  -0.0019 134 ALA A CA    
1096 C  C     . ALA A 133 ? 0.1304 0.0933 0.1073 -0.0326 -0.0026 0.0070  134 ALA A C     
1097 O  O     . ALA A 133 ? 0.0954 0.1276 0.1021 -0.0264 0.0052  0.0087  134 ALA A O     
1098 C  CB    . ALA A 133 ? 0.1408 0.0985 0.0970 -0.0177 -0.0164 0.0210  134 ALA A CB    
1099 N  N     . VAL A 134 ? 0.1305 0.1131 0.0946 -0.0235 -0.0013 0.0174  135 VAL A N     
1100 C  CA    . VAL A 134 ? 0.1380 0.0991 0.1061 -0.0313 0.0000  0.0160  135 VAL A CA    
1101 C  C     . VAL A 134 ? 0.1365 0.1059 0.1077 -0.0263 0.0149  -0.0029 135 VAL A C     
1102 O  O     . VAL A 134 ? 0.1054 0.1204 0.1350 -0.0215 0.0091  0.0148  135 VAL A O     
1103 C  CB    . VAL A 134 ? 0.1494 0.1054 0.1313 -0.0490 0.0055  0.0031  135 VAL A CB    
1104 C  CG1   . VAL A 134 ? 0.1981 0.1166 0.1295 -0.0608 -0.0150 0.0051  135 VAL A CG1   
1105 C  CG2   . VAL A 134 ? 0.1504 0.1337 0.1317 -0.0587 0.0326  -0.0135 135 VAL A CG2   
1106 N  N     . GLN A 135 ? 0.1048 0.1058 0.1431 -0.0383 0.0057  0.0122  136 GLN A N     
1107 C  CA    . GLN A 135 ? 0.1084 0.1292 0.1494 -0.0280 0.0064  -0.0249 136 GLN A CA    
1108 C  C     . GLN A 135 ? 0.1013 0.1521 0.1398 -0.0423 -0.0100 -0.0101 136 GLN A C     
1109 O  O     . GLN A 135 ? 0.1307 0.1813 0.1587 -0.0577 -0.0169 -0.0196 136 GLN A O     
1110 C  CB    . GLN A 135 ? 0.1109 0.1684 0.1664 -0.0669 0.0177  -0.0146 136 GLN A CB    
1111 C  CG    . GLN A 135 ? 0.2137 0.1978 0.1779 -0.0700 0.0531  0.0590  136 GLN A CG    
1112 C  CD    . GLN A 135 ? 0.2902 0.2026 0.2525 -0.0936 0.0389  0.0300  136 GLN A CD    
1113 O  OE1   . GLN A 135 ? 0.3031 0.3296 0.3245 -0.1603 -0.0217 0.0627  136 GLN A OE1   
1114 N  NE2   . GLN A 135 ? 0.2935 0.2236 0.2897 -0.0893 0.0478  0.0792  136 GLN A NE2   
1115 N  N     . GLN A 136 ? 0.0876 0.1080 0.1297 -0.0197 0.0057  -0.0075 137 GLN A N     
1116 C  CA    . GLN A 136 ? 0.0957 0.1000 0.1043 -0.0269 -0.0197 -0.0130 137 GLN A CA    
1117 C  C     . GLN A 136 ? 0.0853 0.0962 0.0999 -0.0018 0.0050  -0.0054 137 GLN A C     
1118 O  O     . GLN A 136 ? 0.1019 0.0971 0.0962 -0.0019 -0.0014 -0.0125 137 GLN A O     
1119 C  CB    . GLN A 136 ? 0.1441 0.1237 0.1096 -0.0035 -0.0193 -0.0169 137 GLN A CB    
1120 C  CG    . GLN A 136 ? 0.2333 0.1483 0.1427 0.0314  0.0445  -0.0103 137 GLN A CG    
1121 C  CD    . GLN A 136 ? 0.1482 0.2498 0.2795 0.0291  0.0474  0.0768  137 GLN A CD    
1122 O  OE1   . GLN A 136 ? 0.3545 0.2851 0.5815 -0.0465 0.1290  0.1597  137 GLN A OE1   
1123 N  NE2   . GLN A 136 ? 0.2366 0.1187 0.3000 -0.0038 0.0096  -0.1074 137 GLN A NE2   
1124 N  N     . PRO A 137 ? 0.0844 0.1225 0.0833 -0.0021 -0.0064 -0.0144 138 PRO A N     
1125 C  CA    . PRO A 137 ? 0.0880 0.1301 0.0911 -0.0020 -0.0025 0.0117  138 PRO A CA    
1126 C  C     . PRO A 137 ? 0.0976 0.1096 0.0937 0.0037  0.0033  0.0007  138 PRO A C     
1127 O  O     . PRO A 137 ? 0.1228 0.1223 0.1871 -0.0113 -0.0197 0.0287  138 PRO A O     
1128 C  CB    . PRO A 137 ? 0.1143 0.1790 0.1046 0.0119  -0.0097 -0.0098 138 PRO A CB    
1129 C  CG    . PRO A 137 ? 0.4171 0.2546 0.1097 -0.0878 -0.0338 -0.0107 138 PRO A CG    
1130 C  CD    . PRO A 137 ? 0.1307 0.1828 0.1077 -0.0410 -0.0007 -0.0327 138 PRO A CD    
1131 N  N     . ASP A 138 ? 0.0781 0.1201 0.1064 0.0021  -0.0122 -0.0217 139 ASP A N     
1132 C  CA    . ASP A 138 ? 0.0733 0.1066 0.1011 -0.0048 -0.0016 -0.0131 139 ASP A CA    
1133 C  C     . ASP A 138 ? 0.0643 0.0949 0.1099 -0.0238 0.0011  0.0004  139 ASP A C     
1134 O  O     . ASP A 138 ? 0.0753 0.1066 0.1104 -0.0080 -0.0093 -0.0149 139 ASP A O     
1135 C  CB    . ASP A 138 ? 0.1139 0.1208 0.1126 0.0088  0.0054  0.0050  139 ASP A CB    
1136 C  CG    . ASP A 138 ? 0.1346 0.1365 0.0956 0.0198  0.0054  -0.0277 139 ASP A CG    
1137 O  OD1   . ASP A 138 ? 0.1517 0.0987 0.1368 0.0107  -0.0199 -0.0248 139 ASP A OD1   
1138 O  OD2   . ASP A 138 ? 0.1935 0.1616 0.1542 0.0539  0.0133  -0.0501 139 ASP A OD2   
1139 N  N     . GLY A 139 ? 0.0814 0.0779 0.0925 0.0100  -0.0091 -0.0046 140 GLY A N     
1140 C  CA    . GLY A 139 ? 0.0763 0.0875 0.0918 -0.0121 -0.0085 -0.0050 140 GLY A CA    
1141 C  C     . GLY A 139 ? 0.0791 0.0753 0.0988 -0.0087 -0.0158 -0.0024 140 GLY A C     
1142 O  O     . GLY A 139 ? 0.0950 0.0744 0.0976 0.0045  -0.0089 -0.0045 140 GLY A O     
1143 N  N     . LEU A 140 ? 0.0552 0.0687 0.1048 -0.0010 -0.0160 -0.0067 141 LEU A N     
1144 C  CA    . LEU A 140 ? 0.0644 0.0647 0.0886 -0.0085 -0.0045 -0.0066 141 LEU A CA    
1145 C  C     . LEU A 140 ? 0.0732 0.0646 0.0825 0.0027  -0.0066 0.0029  141 LEU A C     
1146 O  O     . LEU A 140 ? 0.0867 0.0673 0.0811 -0.0024 -0.0016 0.0039  141 LEU A O     
1147 C  CB    . LEU A 140 ? 0.0805 0.0821 0.0766 -0.0036 -0.0067 -0.0063 141 LEU A CB    
1148 C  CG    . LEU A 140 ? 0.1195 0.1055 0.1486 0.0158  0.0340  0.0211  141 LEU A CG    
1149 C  CD1   . LEU A 140 ? 0.0985 0.1165 0.1200 0.0198  0.0204  0.0184  141 LEU A CD1   
1150 C  CD2   . LEU A 140 ? 0.2445 0.1044 0.1741 0.0399  0.0676  0.0342  141 LEU A CD2   
1151 N  N     . ALA A 141 ? 0.0655 0.0629 0.0751 0.0063  -0.0122 0.0114  142 ALA A N     
1152 C  CA    . ALA A 141 ? 0.0763 0.0749 0.0836 -0.0097 -0.0066 0.0038  142 ALA A CA    
1153 C  C     . ALA A 141 ? 0.0608 0.0760 0.0869 -0.0116 -0.0117 0.0125  142 ALA A C     
1154 O  O     . ALA A 141 ? 0.0959 0.0727 0.0871 -0.0098 -0.0191 0.0006  142 ALA A O     
1155 C  CB    . ALA A 141 ? 0.0770 0.0945 0.1119 -0.0106 0.0117  -0.0099 142 ALA A CB    
1156 N  N     . VAL A 142 ? 0.0680 0.0613 0.0715 -0.0046 -0.0051 -0.0023 143 VAL A N     
1157 C  CA    . VAL A 142 ? 0.0872 0.0744 0.0576 0.0031  0.0086  0.0021  143 VAL A CA    
1158 C  C     . VAL A 142 ? 0.0775 0.0614 0.0767 0.0125  0.0036  0.0115  143 VAL A C     
1159 O  O     . VAL A 142 ? 0.0760 0.0730 0.0738 -0.0022 -0.0047 0.0075  143 VAL A O     
1160 C  CB    . VAL A 142 ? 0.0754 0.0827 0.0665 0.0103  0.0001  0.0135  143 VAL A CB    
1161 C  CG1   . VAL A 142 ? 0.0985 0.0921 0.0828 0.0284  0.0066  0.0059  143 VAL A CG1   
1162 C  CG2   . VAL A 142 ? 0.0973 0.1123 0.0735 -0.0040 0.0085  0.0165  143 VAL A CG2   
1163 N  N     . LEU A 143 ? 0.0842 0.0552 0.0724 -0.0057 0.0007  0.0182  144 LEU A N     
1164 C  CA    . LEU A 143 ? 0.0734 0.0759 0.0661 -0.0128 0.0068  0.0115  144 LEU A CA    
1165 C  C     . LEU A 143 ? 0.0712 0.0899 0.0617 -0.0152 -0.0093 0.0040  144 LEU A C     
1166 O  O     . LEU A 143 ? 0.1202 0.0788 0.0693 -0.0087 0.0017  -0.0030 144 LEU A O     
1167 C  CB    . LEU A 143 ? 0.0850 0.1069 0.1042 -0.0214 -0.0158 0.0098  144 LEU A CB    
1168 C  CG    . LEU A 143 ? 0.0837 0.0952 0.1438 -0.0151 -0.0085 -0.0172 144 LEU A CG    
1169 C  CD1   . LEU A 143 ? 0.0837 0.1592 0.1546 0.0003  -0.0049 0.0272  144 LEU A CD1   
1170 C  CD2   . LEU A 143 ? 0.0858 0.1693 0.1617 0.0022  -0.0151 -0.0060 144 LEU A CD2   
1171 N  N     . GLY A 144 ? 0.0681 0.0734 0.0666 -0.0108 -0.0079 0.0017  145 GLY A N     
1172 C  CA    . GLY A 144 ? 0.0831 0.0638 0.0742 -0.0117 0.0085  0.0110  145 GLY A CA    
1173 C  C     . GLY A 144 ? 0.0650 0.0614 0.0733 -0.0087 -0.0058 0.0015  145 GLY A C     
1174 O  O     . GLY A 144 ? 0.0871 0.0962 0.0757 -0.0165 0.0127  -0.0055 145 GLY A O     
1175 N  N     . ILE A 145 ? 0.0787 0.0620 0.0715 -0.0049 0.0047  -0.0016 146 ILE A N     
1176 C  CA    . ILE A 145 ? 0.0698 0.0802 0.0726 -0.0004 -0.0029 -0.0096 146 ILE A CA    
1177 C  C     . ILE A 145 ? 0.0626 0.0754 0.0702 -0.0069 -0.0088 0.0013  146 ILE A C     
1178 O  O     . ILE A 145 ? 0.0880 0.0723 0.0930 -0.0126 0.0120  -0.0042 146 ILE A O     
1179 C  CB    . ILE A 145 ? 0.0800 0.0934 0.0869 -0.0070 -0.0179 -0.0177 146 ILE A CB    
1180 C  CG1   . ILE A 145 ? 0.0909 0.1101 0.1060 0.0125  -0.0233 -0.0117 146 ILE A CG1   
1181 C  CG2   . ILE A 145 ? 0.1009 0.1060 0.1521 -0.0147 -0.0533 -0.0059 146 ILE A CG2   
1182 C  CD1   . ILE A 145 ? 0.1094 0.0907 0.1221 -0.0104 -0.0313 0.0215  146 ILE A CD1   
1183 N  N     . PHE A 146 ? 0.0617 0.0749 0.0721 -0.0015 -0.0039 0.0034  147 PHE A N     
1184 C  CA    . PHE A 146 ? 0.0784 0.0634 0.0923 -0.0047 -0.0129 -0.0064 147 PHE A CA    
1185 C  C     . PHE A 146 ? 0.0695 0.0834 0.0970 -0.0186 -0.0128 -0.0078 147 PHE A C     
1186 O  O     . PHE A 146 ? 0.0833 0.0925 0.1074 -0.0078 -0.0095 -0.0279 147 PHE A O     
1187 C  CB    . PHE A 146 ? 0.0778 0.0635 0.0924 -0.0166 0.0003  -0.0023 147 PHE A CB    
1188 C  CG    . PHE A 146 ? 0.0728 0.0559 0.0841 -0.0105 -0.0066 0.0175  147 PHE A CG    
1189 C  CD1   . PHE A 146 ? 0.0694 0.0743 0.0938 0.0070  0.0049  -0.0135 147 PHE A CD1   
1190 C  CD2   . PHE A 146 ? 0.1011 0.0736 0.0963 -0.0133 -0.0052 0.0215  147 PHE A CD2   
1191 C  CE1   . PHE A 146 ? 0.0772 0.0889 0.0898 -0.0045 -0.0023 0.0016  147 PHE A CE1   
1192 C  CE2   . PHE A 146 ? 0.0823 0.0777 0.0831 -0.0077 0.0074  0.0075  147 PHE A CE2   
1193 C  CZ    . PHE A 146 ? 0.0848 0.0687 0.0906 -0.0037 -0.0144 0.0105  147 PHE A CZ    
1194 N  N     . LEU A 147 ? 0.0812 0.0711 0.0988 -0.0214 -0.0111 -0.0061 148 LEU A N     
1195 C  CA    . LEU A 147 ? 0.1273 0.0656 0.0916 -0.0270 -0.0224 0.0058  148 LEU A CA    
1196 C  C     . LEU A 147 ? 0.0993 0.0638 0.0986 -0.0230 0.0050  -0.0004 148 LEU A C     
1197 O  O     . LEU A 147 ? 0.0934 0.0759 0.1200 -0.0071 -0.0012 -0.0006 148 LEU A O     
1198 C  CB    . LEU A 147 ? 0.1135 0.0850 0.0988 -0.0187 -0.0120 -0.0021 148 LEU A CB    
1199 C  CG    . LEU A 147 ? 0.1199 0.0924 0.1091 -0.0004 -0.0168 -0.0185 148 LEU A CG    
1200 C  CD1   . LEU A 147 ? 0.1543 0.0910 0.1007 -0.0046 -0.0286 -0.0055 148 LEU A CD1   
1201 C  CD2   . LEU A 147 ? 0.1296 0.0898 0.1145 -0.0070 -0.0201 -0.0054 148 LEU A CD2   
1202 N  N     . LYS A 148 ? 0.0851 0.0591 0.1513 -0.0102 -0.0028 -0.0208 149 LYS A N     
1203 C  CA    . LYS A 148 ? 0.1132 0.0573 0.1332 -0.0044 -0.0201 -0.0141 149 LYS A CA    
1204 C  C     . LYS A 148 ? 0.1259 0.0606 0.1385 -0.0036 -0.0194 0.0038  149 LYS A C     
1205 O  O     . LYS A 148 ? 0.1290 0.0950 0.1412 0.0116  -0.0147 -0.0075 149 LYS A O     
1206 C  CB    . LYS A 148 ? 0.1189 0.0854 0.1620 -0.0434 -0.0420 0.0094  149 LYS A CB    
1207 C  CG    . LYS A 148 ? 0.1170 0.1256 0.2007 -0.0171 0.0091  0.0169  149 LYS A CG    
1208 C  CD    . LYS A 148 ? 0.2363 0.1977 0.2050 -0.0154 -0.0252 0.0581  149 LYS A CD    
1209 C  CE    . LYS A 148 ? 0.2724 0.2881 0.3210 0.0770  0.0805  0.0436  149 LYS A CE    
1210 N  NZ    . LYS A 148 ? 0.4110 0.4284 0.5585 -0.2036 0.0463  0.1389  149 LYS A NZ    
1211 N  N     . VAL A 149 ? 0.1200 0.0766 0.1320 0.0100  -0.0210 -0.0151 150 VAL A N     
1212 C  CA    . VAL A 149 ? 0.1444 0.0810 0.1570 -0.0028 -0.0286 -0.0340 150 VAL A CA    
1213 C  C     . VAL A 149 ? 0.1286 0.1174 0.1521 -0.0031 0.0017  -0.0279 150 VAL A C     
1214 O  O     . VAL A 149 ? 0.1723 0.1028 0.1873 -0.0202 -0.0152 0.0050  150 VAL A O     
1215 C  CB    . VAL A 149 ? 0.1386 0.1126 0.1559 -0.0096 0.0020  -0.0293 150 VAL A CB    
1216 C  CG1   . VAL A 149 ? 0.1762 0.1523 0.1559 0.0144  -0.0006 -0.0266 150 VAL A CG1   
1217 C  CG2   . VAL A 149 ? 0.1403 0.1583 0.1740 -0.0176 -0.0037 -0.0199 150 VAL A CG2   
1218 N  N     . GLY A 150 ? 0.1513 0.0908 0.1448 -0.0306 -0.0048 -0.0060 151 GLY A N     
1219 C  CA    . GLY A 150 ? 0.1602 0.1520 0.1541 -0.0546 -0.0096 -0.0139 151 GLY A CA    
1220 C  C     . GLY A 150 ? 0.1404 0.1380 0.1586 -0.0465 0.0000  -0.0309 151 GLY A C     
1221 O  O     . GLY A 150 ? 0.1420 0.1727 0.1719 -0.0481 0.0019  -0.0527 151 GLY A O     
1222 N  N     A SER A 151 ? 0.1589 0.1385 0.1519 -0.0090 -0.0092 -0.0472 152 SER A N     
1223 N  N     B SER A 151 ? 0.1563 0.1445 0.1505 -0.0068 -0.0089 -0.0418 152 SER A N     
1224 C  CA    A SER A 151 ? 0.1599 0.1786 0.1572 -0.0157 -0.0252 -0.0505 152 SER A CA    
1225 C  CA    B SER A 151 ? 0.1546 0.2011 0.1668 -0.0133 -0.0292 -0.0424 152 SER A CA    
1226 C  C     A SER A 151 ? 0.1555 0.1548 0.1628 -0.0070 -0.0402 -0.0652 152 SER A C     
1227 C  C     B SER A 151 ? 0.1571 0.1526 0.1561 0.0161  -0.0264 -0.0680 152 SER A C     
1228 O  O     A SER A 151 ? 0.1580 0.1646 0.1368 -0.0148 -0.0354 -0.0611 152 SER A O     
1229 O  O     B SER A 151 ? 0.1273 0.1657 0.1561 -0.0120 -0.0253 -0.0397 152 SER A O     
1230 C  CB    A SER A 151 ? 0.1159 0.2122 0.2644 -0.0530 -0.0495 -0.0783 152 SER A CB    
1231 C  CB    B SER A 151 ? 0.1291 0.2758 0.2598 -0.0378 -0.0401 -0.0490 152 SER A CB    
1232 O  OG    A SER A 151 ? 0.1630 0.2603 0.2764 -0.0226 -0.0382 0.0388  152 SER A OG    
1233 O  OG    B SER A 151 ? 0.1417 0.3276 0.2369 -0.0379 -0.0184 -0.0778 152 SER A OG    
1234 N  N     . ALA A 152 ? 0.1652 0.1234 0.1620 -0.0181 -0.0451 -0.0531 153 ALA A N     
1235 C  CA    . ALA A 152 ? 0.1323 0.1270 0.1581 0.0137  -0.0376 -0.0330 153 ALA A CA    
1236 C  C     . ALA A 152 ? 0.1357 0.1521 0.1664 -0.0142 -0.0134 -0.0546 153 ALA A C     
1237 O  O     . ALA A 152 ? 0.1452 0.1521 0.2145 -0.0029 0.0028  -0.0533 153 ALA A O     
1238 C  CB    . ALA A 152 ? 0.2149 0.1545 0.1621 0.0375  -0.0387 -0.0595 153 ALA A CB    
1239 N  N     . LYS A 153 ? 0.1229 0.1476 0.1468 -0.0128 -0.0055 -0.0586 154 LYS A N     
1240 C  CA    . LYS A 153 ? 0.1926 0.1518 0.1649 0.0194  -0.0151 -0.0332 154 LYS A CA    
1241 C  C     . LYS A 153 ? 0.1688 0.1497 0.1700 0.0071  -0.0315 -0.0880 154 LYS A C     
1242 O  O     . LYS A 153 ? 0.1450 0.1915 0.1288 0.0401  -0.0440 -0.0533 154 LYS A O     
1243 C  CB    . LYS A 153 ? 0.1869 0.1224 0.1469 0.0204  -0.0400 -0.0149 154 LYS A CB    
1244 C  CG    . LYS A 153 ? 0.2438 0.1297 0.2234 0.0050  -0.0628 -0.0582 154 LYS A CG    
1245 C  CD    . LYS A 153 ? 0.2744 0.1683 0.1993 0.0490  -0.0178 -0.0608 154 LYS A CD    
1246 C  CE    . LYS A 153 ? 0.4471 0.1896 0.1981 0.0646  -0.0218 -0.0579 154 LYS A CE    
1247 N  NZ    . LYS A 153 ? 0.5310 0.2932 0.2539 0.0706  0.0339  -0.0466 154 LYS A NZ    
1248 N  N     . PRO A 154 ? 0.1872 0.1700 0.1828 -0.0041 -0.0597 -0.0416 155 PRO A N     
1249 C  CA    . PRO A 154 ? 0.1889 0.2046 0.2094 0.0664  -0.0292 -0.0472 155 PRO A CA    
1250 C  C     . PRO A 154 ? 0.1828 0.2366 0.1526 0.0601  -0.0520 -0.0126 155 PRO A C     
1251 O  O     . PRO A 154 ? 0.2806 0.3117 0.1583 0.0658  -0.0532 -0.0062 155 PRO A O     
1252 C  CB    . PRO A 154 ? 0.1620 0.2692 0.2913 0.0573  -0.0659 -0.0194 155 PRO A CB    
1253 C  CG    . PRO A 154 ? 0.1944 0.3091 0.3440 -0.0058 -0.0425 -0.0317 155 PRO A CG    
1254 C  CD    . PRO A 154 ? 0.2107 0.1860 0.2453 0.0178  -0.0129 -0.0586 155 PRO A CD    
1255 N  N     . GLY A 155 ? 0.1833 0.1936 0.1678 0.0696  -0.0353 -0.0214 156 GLY A N     
1256 C  CA    . GLY A 155 ? 0.1987 0.2102 0.1740 0.0467  -0.0205 -0.0003 156 GLY A CA    
1257 C  C     . GLY A 155 ? 0.2311 0.1773 0.1836 0.0164  -0.0124 -0.0045 156 GLY A C     
1258 O  O     . GLY A 155 ? 0.2843 0.1554 0.2816 0.0431  -0.0032 0.0206  156 GLY A O     
1259 N  N     . LEU A 156 ? 0.2070 0.1437 0.1320 0.0141  -0.0279 -0.0006 157 LEU A N     
1260 C  CA    . LEU A 156 ? 0.1867 0.1404 0.1197 -0.0031 -0.0428 -0.0314 157 LEU A CA    
1261 C  C     . LEU A 156 ? 0.1805 0.1284 0.1500 -0.0007 -0.0321 -0.0382 157 LEU A C     
1262 O  O     . LEU A 156 ? 0.2129 0.1615 0.1320 0.0010  -0.0403 -0.0252 157 LEU A O     
1263 C  CB    . LEU A 156 ? 0.1686 0.1581 0.1351 0.0026  -0.0508 -0.0421 157 LEU A CB    
1264 C  CG    . LEU A 156 ? 0.1751 0.1516 0.1296 0.0117  -0.0104 -0.0336 157 LEU A CG    
1265 C  CD1   . LEU A 156 ? 0.2013 0.1574 0.1572 -0.0172 -0.0124 -0.0146 157 LEU A CD1   
1266 C  CD2   . LEU A 156 ? 0.1548 0.1632 0.1564 -0.0014 -0.0342 -0.0071 157 LEU A CD2   
1267 N  N     . GLN A 157 ? 0.1798 0.1878 0.1148 -0.0059 -0.0342 -0.0214 158 GLN A N     
1268 C  CA    . GLN A 157 ? 0.1866 0.2047 0.1337 0.0087  -0.0292 -0.0407 158 GLN A CA    
1269 C  C     . GLN A 157 ? 0.2164 0.2011 0.1504 0.0047  -0.0722 -0.0363 158 GLN A C     
1270 O  O     . GLN A 157 ? 0.2154 0.2426 0.1291 0.0151  -0.0515 -0.0251 158 GLN A O     
1271 C  CB    . GLN A 157 ? 0.2561 0.1844 0.1665 -0.0132 -0.0259 -0.0280 158 GLN A CB    
1272 C  CG    . GLN A 157 ? 0.2866 0.1816 0.1867 -0.0168 -0.0494 -0.0814 158 GLN A CG    
1273 C  CD    . GLN A 157 ? 0.2343 0.1407 0.1968 -0.0104 -0.0082 -0.0554 158 GLN A CD    
1274 O  OE1   . GLN A 157 ? 0.2657 0.1630 0.1477 0.0012  -0.0153 -0.0317 158 GLN A OE1   
1275 N  NE2   . GLN A 157 ? 0.3203 0.2334 0.1653 -0.0637 -0.0133 -0.0905 158 GLN A NE2   
1276 N  N     . LYS A 158 ? 0.2766 0.2229 0.0893 0.0095  -0.0392 -0.0210 159 LYS A N     
1277 C  CA    . LYS A 158 ? 0.2275 0.2002 0.1768 0.0223  -0.0274 -0.0194 159 LYS A CA    
1278 C  C     . LYS A 158 ? 0.2389 0.2023 0.1293 -0.0081 -0.0368 -0.0246 159 LYS A C     
1279 O  O     . LYS A 158 ? 0.2786 0.2297 0.1297 0.0329  -0.0097 -0.0135 159 LYS A O     
1280 C  CB    . LYS A 158 ? 0.2941 0.1958 0.2183 0.0202  -0.0192 -0.0326 159 LYS A CB    
1281 C  CG    . LYS A 158 ? 0.3025 0.3315 0.3131 -0.0074 -0.0399 -0.0029 159 LYS A CG    
1282 C  CD    . LYS A 158 ? 0.4131 0.4175 0.6359 0.1004  0.1008  -0.0384 159 LYS A CD    
1283 C  CE    . LYS A 158 ? 0.7349 0.5599 0.5632 0.1208  0.1348  0.0243  159 LYS A CE    
1284 N  NZ    . LYS A 158 ? 0.4793 0.4566 0.2060 0.0047  0.0000  0.1367  159 LYS A NZ    
1285 N  N     . VAL A 159 ? 0.2528 0.1966 0.1171 0.0413  -0.0309 -0.0257 160 VAL A N     
1286 C  CA    . VAL A 159 ? 0.2503 0.1303 0.0953 -0.0198 -0.0026 0.0053  160 VAL A CA    
1287 C  C     . VAL A 159 ? 0.2248 0.1493 0.0937 -0.0153 -0.0045 -0.0088 160 VAL A C     
1288 O  O     . VAL A 159 ? 0.2308 0.1157 0.1471 -0.0043 -0.0255 -0.0203 160 VAL A O     
1289 C  CB    . VAL A 159 ? 0.2717 0.1444 0.1047 -0.0086 -0.0185 -0.0066 160 VAL A CB    
1290 C  CG1   . VAL A 159 ? 0.2856 0.1449 0.1277 -0.0356 -0.0196 -0.0008 160 VAL A CG1   
1291 C  CG2   . VAL A 159 ? 0.2907 0.1722 0.1294 0.0234  -0.0042 -0.0323 160 VAL A CG2   
1292 N  N     . VAL A 160 ? 0.2056 0.1226 0.1015 0.0021  -0.0088 -0.0268 161 VAL A N     
1293 C  CA    . VAL A 160 ? 0.1824 0.1485 0.1386 0.0081  -0.0019 -0.0265 161 VAL A CA    
1294 C  C     . VAL A 160 ? 0.2049 0.1521 0.1524 -0.0278 -0.0004 -0.0602 161 VAL A C     
1295 O  O     . VAL A 160 ? 0.2125 0.1581 0.1641 0.0023  0.0127  -0.0351 161 VAL A O     
1296 C  CB    . VAL A 160 ? 0.3266 0.1093 0.2039 0.0156  0.0171  -0.0297 161 VAL A CB    
1297 C  CG1   . VAL A 160 ? 0.3111 0.1630 0.2537 -0.0231 0.0203  -0.0853 161 VAL A CG1   
1298 C  CG2   . VAL A 160 ? 0.3915 0.1416 0.2290 0.0532  0.0393  -0.0149 161 VAL A CG2   
1299 N  N     A ASP A 161 ? 0.2341 0.1890 0.1122 -0.0386 -0.0248 -0.0516 162 ASP A N     
1300 N  N     B ASP A 161 ? 0.2248 0.2027 0.1247 -0.0277 -0.0020 -0.0496 162 ASP A N     
1301 C  CA    A ASP A 161 ? 0.2564 0.2224 0.1128 -0.0207 -0.0098 -0.0383 162 ASP A CA    
1302 C  CA    B ASP A 161 ? 0.2864 0.2795 0.1244 -0.0228 0.0109  -0.0563 162 ASP A CA    
1303 C  C     A ASP A 161 ? 0.2549 0.2599 0.1147 -0.0429 -0.0293 -0.0335 162 ASP A C     
1304 C  C     B ASP A 161 ? 0.2977 0.2948 0.1216 -0.0448 -0.0126 -0.0626 162 ASP A C     
1305 O  O     A ASP A 161 ? 0.3654 0.2908 0.1430 -0.0596 0.0423  -0.0393 162 ASP A O     
1306 O  O     B ASP A 161 ? 0.4396 0.3893 0.1512 -0.0366 0.0619  -0.0736 162 ASP A O     
1307 C  CB    A ASP A 161 ? 0.2791 0.1910 0.1294 -0.0348 -0.0365 -0.0789 162 ASP A CB    
1308 C  CB    B ASP A 161 ? 0.3512 0.3230 0.1741 0.0165  -0.0329 -0.0442 162 ASP A CB    
1309 C  CG    A ASP A 161 ? 0.2214 0.2016 0.0734 -0.0324 -0.0193 -0.0541 162 ASP A CG    
1310 C  CG    B ASP A 161 ? 0.4685 0.2883 0.2241 -0.0745 -0.0220 -0.0398 162 ASP A CG    
1311 O  OD1   A ASP A 161 ? 0.2350 0.1517 0.1925 -0.0437 -0.0105 -0.0409 162 ASP A OD1   
1312 O  OD1   B ASP A 161 ? 0.5100 0.3121 0.2286 -0.0134 0.1007  -0.0403 162 ASP A OD1   
1313 O  OD2   A ASP A 161 ? 0.2431 0.2433 0.1670 -0.0833 0.0126  -0.0614 162 ASP A OD2   
1314 O  OD2   B ASP A 161 ? 0.5167 0.3414 0.2861 0.0015  -0.1967 -0.0444 162 ASP A OD2   
1315 N  N     . VAL A 162 ? 0.2980 0.2406 0.1197 -0.0101 -0.0527 -0.0288 163 VAL A N     
1316 C  CA    . VAL A 162 ? 0.2746 0.2606 0.1195 0.0027  -0.0455 -0.0251 163 VAL A CA    
1317 C  C     . VAL A 162 ? 0.2486 0.2019 0.1133 -0.0251 -0.0168 0.0131  163 VAL A C     
1318 O  O     . VAL A 162 ? 0.2891 0.1803 0.1060 -0.0161 0.0104  -0.0097 163 VAL A O     
1319 C  CB    . VAL A 162 ? 0.2719 0.2158 0.1655 0.0136  0.0016  0.0221  163 VAL A CB    
1320 C  CG1   . VAL A 162 ? 0.3888 0.2671 0.1929 0.0093  -0.0085 -0.0340 163 VAL A CG1   
1321 C  CG2   . VAL A 162 ? 0.4022 0.2273 0.1563 0.0547  0.0010  0.0343  163 VAL A CG2   
1322 N  N     . LEU A 163 ? 0.2614 0.1556 0.1167 -0.0348 -0.0245 0.0006  164 LEU A N     
1323 C  CA    . LEU A 163 ? 0.2323 0.1136 0.1261 -0.0400 0.0212  -0.0006 164 LEU A CA    
1324 C  C     . LEU A 163 ? 0.2825 0.1806 0.1025 -0.0238 0.0274  -0.0194 164 LEU A C     
1325 O  O     . LEU A 163 ? 0.2654 0.1469 0.1322 -0.0032 0.0209  -0.0102 164 LEU A O     
1326 C  CB    . LEU A 163 ? 0.2076 0.1416 0.1276 -0.0155 -0.0042 -0.0005 164 LEU A CB    
1327 C  CG    . LEU A 163 ? 0.1997 0.1521 0.1184 -0.0238 0.0004  0.0065  164 LEU A CG    
1328 C  CD1   . LEU A 163 ? 0.2219 0.1421 0.1478 -0.0128 0.0104  0.0178  164 LEU A CD1   
1329 C  CD2   . LEU A 163 ? 0.2053 0.1664 0.1061 -0.0178 -0.0150 0.0060  164 LEU A CD2   
1330 N  N     . ASP A 164 ? 0.3343 0.1918 0.1315 -0.0373 0.0306  -0.0658 165 ASP A N     
1331 C  CA    . ASP A 164 ? 0.3906 0.2520 0.1440 -0.0429 0.0582  -0.0687 165 ASP A CA    
1332 C  C     . ASP A 164 ? 0.3109 0.2633 0.1458 -0.0134 0.0186  -0.0184 165 ASP A C     
1333 O  O     . ASP A 164 ? 0.4113 0.2867 0.1827 -0.0009 0.0818  -0.0415 165 ASP A O     
1334 C  CB    . ASP A 164 ? 0.5020 0.3217 0.1779 -0.1497 0.0676  -0.1790 165 ASP A CB    
1335 C  CG    . ASP A 164 ? 0.5719 0.4684 0.5325 -0.2051 0.0405  -0.0448 165 ASP A CG    
1336 O  OD1   . ASP A 164 ? 0.4845 0.7159 0.5639 -0.0466 0.0853  -0.1869 165 ASP A OD1   
1337 O  OD2   . ASP A 164 ? 0.6715 0.7534 0.7052 -0.3168 -0.0923 -0.0813 165 ASP A OD2   
1338 N  N     . SER A 165 ? 0.3015 0.2398 0.1102 -0.0150 0.0118  -0.0049 166 SER A N     
1339 C  CA    . SER A 165 ? 0.3039 0.2397 0.1074 -0.0372 -0.0085 0.0104  166 SER A CA    
1340 C  C     . SER A 165 ? 0.2412 0.2317 0.0934 -0.0290 0.0000  0.0303  166 SER A C     
1341 O  O     . SER A 165 ? 0.3933 0.1777 0.0970 -0.0277 0.0175  0.0286  166 SER A O     
1342 C  CB    . SER A 165 ? 0.3223 0.2394 0.1606 0.0088  0.0216  0.0236  166 SER A CB    
1343 O  OG    . SER A 165 ? 0.3912 0.2156 0.1561 0.0042  0.0051  0.0276  166 SER A OG    
1344 N  N     . ILE A 166 ? 0.2890 0.1202 0.0853 -0.0323 0.0060  0.0220  167 ILE A N     
1345 C  CA    . ILE A 166 ? 0.2183 0.1391 0.1042 -0.0112 0.0107  0.0127  167 ILE A CA    
1346 C  C     . ILE A 166 ? 0.2220 0.1382 0.0956 -0.0132 -0.0110 -0.0227 167 ILE A C     
1347 O  O     . ILE A 166 ? 0.2776 0.1221 0.0863 -0.0448 -0.0017 -0.0006 167 ILE A O     
1348 C  CB    . ILE A 166 ? 0.2718 0.1562 0.0927 -0.0125 0.0043  -0.0138 167 ILE A CB    
1349 C  CG1   . ILE A 166 ? 0.2490 0.1304 0.1104 -0.0125 0.0076  -0.0078 167 ILE A CG1   
1350 C  CG2   . ILE A 166 ? 0.2710 0.1769 0.1099 -0.0105 -0.0155 -0.0042 167 ILE A CG2   
1351 C  CD1   . ILE A 166 ? 0.2655 0.1332 0.1165 -0.0444 0.0127  -0.0215 167 ILE A CD1   
1352 N  N     . LYS A 167 ? 0.2326 0.1302 0.1139 -0.0224 0.0298  -0.0030 168 LYS A N     
1353 C  CA    . LYS A 167 ? 0.1627 0.1681 0.1102 -0.0305 0.0435  -0.0345 168 LYS A CA    
1354 C  C     . LYS A 167 ? 0.1874 0.1707 0.0795 -0.0344 0.0308  0.0023  168 LYS A C     
1355 O  O     . LYS A 167 ? 0.2309 0.1250 0.1161 -0.0589 0.0199  -0.0139 168 LYS A O     
1356 C  CB    . LYS A 167 ? 0.2652 0.1599 0.1140 -0.0139 -0.0014 -0.0515 168 LYS A CB    
1357 C  CG    . LYS A 167 ? 0.2360 0.1796 0.1625 -0.0107 0.0073  -0.0626 168 LYS A CG    
1358 C  CD    . LYS A 167 ? 0.3743 0.2071 0.1883 0.0010  -0.0354 -0.0833 168 LYS A CD    
1359 C  CE    . LYS A 167 ? 0.2890 0.2907 0.2378 0.0311  -0.0061 -0.0818 168 LYS A CE    
1360 N  NZ    . LYS A 167 ? 0.5609 0.4387 0.3415 0.0090  0.0374  -0.2011 168 LYS A NZ    
1361 N  N     . THR A 168 ? 0.2585 0.1336 0.0881 -0.0439 0.0294  0.0047  169 THR A N     
1362 C  CA    . THR A 168 ? 0.2493 0.1639 0.0786 -0.0072 0.0360  0.0296  169 THR A CA    
1363 C  C     . THR A 168 ? 0.1523 0.1853 0.0904 -0.0338 0.0420  -0.0180 169 THR A C     
1364 O  O     . THR A 168 ? 0.2303 0.1503 0.1546 -0.0533 0.0390  -0.0035 169 THR A O     
1365 C  CB    . THR A 168 ? 0.2561 0.1939 0.1114 -0.0340 0.0427  -0.0091 169 THR A CB    
1366 O  OG1   . THR A 168 ? 0.2939 0.1974 0.1007 -0.0515 0.0412  0.0000  169 THR A OG1   
1367 C  CG2   . THR A 168 ? 0.2402 0.1889 0.1544 -0.0333 0.0679  0.0108  169 THR A CG2   
1368 N  N     . LYS A 169 ? 0.2250 0.1649 0.1554 -0.0944 0.0303  0.0495  170 LYS A N     
1369 C  CA    . LYS A 169 ? 0.2685 0.1582 0.1455 -0.0850 0.0382  0.0186  170 LYS A CA    
1370 C  C     . LYS A 169 ? 0.2249 0.1852 0.0919 -0.0687 0.0213  0.0448  170 LYS A C     
1371 O  O     . LYS A 169 ? 0.3307 0.1944 0.1239 -0.1111 0.0655  -0.0130 170 LYS A O     
1372 C  CB    . LYS A 169 ? 0.2659 0.1446 0.1332 -0.0439 0.0508  0.0189  170 LYS A CB    
1373 C  CG    . LYS A 169 ? 0.3179 0.1900 0.1524 -0.0735 0.0110  0.0293  170 LYS A CG    
1374 C  CD    . LYS A 169 ? 0.3312 0.1978 0.2029 -0.1035 0.0217  0.0432  170 LYS A CD    
1375 C  CE    . LYS A 169 ? 0.1564 0.4642 0.4706 -0.0234 -0.0060 -0.0295 170 LYS A CE    
1376 N  NZ    . LYS A 169 ? 0.4276 0.5821 0.5166 0.0604  -0.1037 0.1155  170 LYS A NZ    
1377 N  N     . GLY A 170 ? 0.2965 0.1428 0.1779 -0.0703 0.0544  0.0409  171 GLY A N     
1378 C  CA    . GLY A 170 ? 0.2760 0.1207 0.1767 -0.0578 0.0130  0.0331  171 GLY A CA    
1379 C  C     . GLY A 170 ? 0.3325 0.1128 0.1707 -0.0502 -0.0063 0.0396  171 GLY A C     
1380 O  O     . GLY A 170 ? 0.4297 0.1390 0.2235 -0.0803 0.0133  0.0776  171 GLY A O     
1381 N  N     . LYS A 171 ? 0.3049 0.1323 0.1939 -0.0946 0.0247  0.0518  172 LYS A N     
1382 C  CA    . LYS A 171 ? 0.2585 0.1188 0.1632 -0.0578 0.0323  0.0451  172 LYS A CA    
1383 C  C     . LYS A 171 ? 0.2777 0.1759 0.0986 -0.0078 0.0180  0.0153  172 LYS A C     
1384 O  O     . LYS A 171 ? 0.3187 0.1621 0.0958 -0.0551 0.0275  0.0140  172 LYS A O     
1385 C  CB    . LYS A 171 ? 0.2542 0.1694 0.1488 -0.0540 0.0124  0.0139  172 LYS A CB    
1386 C  CG    . LYS A 171 ? 0.2456 0.2241 0.1969 -0.0649 0.0096  -0.0270 172 LYS A CG    
1387 C  CD    . LYS A 171 ? 0.3856 0.2065 0.2860 -0.0722 -0.0005 -0.0714 172 LYS A CD    
1388 C  CE    . LYS A 171 ? 0.4357 0.4903 0.3412 -0.0444 0.0245  -0.0089 172 LYS A CE    
1389 N  NZ    . LYS A 171 ? 0.4731 0.6917 0.4155 0.0392  -0.1423 0.0575  172 LYS A NZ    
1390 N  N     . SER A 172 ? 0.2986 0.1831 0.1499 -0.0388 -0.0165 0.0876  173 SER A N     
1391 C  CA    . SER A 172 ? 0.3109 0.2041 0.1636 0.0268  0.0060  0.0335  173 SER A CA    
1392 C  C     . SER A 172 ? 0.2519 0.2270 0.1052 0.0089  0.0198  0.0690  173 SER A C     
1393 O  O     . SER A 172 ? 0.3938 0.2271 0.1027 0.0787  0.0434  0.0107  173 SER A O     
1394 C  CB    . SER A 172 ? 0.2059 0.2257 0.1747 0.0191  0.0518  0.0210  173 SER A CB    
1395 O  OG    . SER A 172 ? 0.4178 0.2644 0.1741 0.0386  0.0691  0.0507  173 SER A OG    
1396 N  N     . ALA A 173 ? 0.2790 0.2289 0.1202 0.0734  0.0413  0.0050  174 ALA A N     
1397 C  CA    . ALA A 173 ? 0.3404 0.2712 0.1070 0.1051  0.0114  0.0732  174 ALA A CA    
1398 C  C     . ALA A 173 ? 0.2586 0.2750 0.1259 0.0540  -0.0153 0.0168  174 ALA A C     
1399 O  O     . ALA A 173 ? 0.2357 0.2392 0.1104 0.0328  -0.0037 0.0265  174 ALA A O     
1400 C  CB    . ALA A 173 ? 0.4254 0.2645 0.1170 0.1123  0.0237  -0.0036 174 ALA A CB    
1401 N  N     . ASP A 174 ? 0.3223 0.2955 0.1224 0.0972  0.0344  0.0930  175 ASP A N     
1402 C  CA    . ASP A 174 ? 0.3453 0.2288 0.1743 0.0825  0.0365  0.0690  175 ASP A CA    
1403 C  C     . ASP A 174 ? 0.4081 0.1907 0.1225 0.0240  -0.0050 0.0341  175 ASP A C     
1404 O  O     . ASP A 174 ? 0.4657 0.2515 0.1486 0.0831  0.0106  -0.0496 175 ASP A O     
1405 C  CB    . ASP A 174 ? 0.3234 0.2795 0.2427 0.1188  0.0313  0.1182  175 ASP A CB    
1406 C  CG    . ASP A 174 ? 0.3759 0.4352 0.3793 -0.1508 -0.0187 0.0226  175 ASP A CG    
1407 O  OD1   . ASP A 174 ? 0.7299 0.4296 0.2813 -0.0860 -0.1925 0.0510  175 ASP A OD1   
1408 O  OD2   . ASP A 174 ? 0.3561 0.5566 0.3238 -0.0723 -0.0814 -0.0970 175 ASP A OD2   
1409 N  N     . PHE A 175 ? 0.2787 0.2256 0.1559 0.0393  0.0324  0.0081  176 PHE A N     
1410 C  CA    . PHE A 175 ? 0.3298 0.1621 0.1382 0.0574  0.0011  0.0421  176 PHE A CA    
1411 C  C     . PHE A 175 ? 0.2531 0.2065 0.1637 0.0430  -0.0264 -0.0091 176 PHE A C     
1412 O  O     . PHE A 175 ? 0.3344 0.3021 0.1127 0.1279  -0.0410 0.0204  176 PHE A O     
1413 C  CB    . PHE A 175 ? 0.2763 0.1829 0.1602 0.0616  0.0021  -0.0219 176 PHE A CB    
1414 C  CG    . PHE A 175 ? 0.3809 0.1559 0.1621 0.0782  0.0213  0.0093  176 PHE A CG    
1415 C  CD1   . PHE A 175 ? 0.3665 0.2240 0.1763 0.0215  0.0645  -0.0210 176 PHE A CD1   
1416 C  CD2   . PHE A 175 ? 0.3337 0.2077 0.1650 0.0172  0.0346  -0.0036 176 PHE A CD2   
1417 C  CE1   . PHE A 175 ? 0.4735 0.1817 0.1989 0.0340  0.0331  0.0091  176 PHE A CE1   
1418 C  CE2   . PHE A 175 ? 0.2572 0.2076 0.2056 0.0358  -0.0283 0.0443  176 PHE A CE2   
1419 C  CZ    . PHE A 175 ? 0.3338 0.2022 0.2031 0.0192  0.0128  0.0262  176 PHE A CZ    
1420 N  N     . THR A 176 ? 0.3124 0.1868 0.1056 0.0616  -0.0336 0.0178  177 THR A N     
1421 C  CA    . THR A 176 ? 0.2607 0.1532 0.0980 0.0296  -0.0109 0.0323  177 THR A CA    
1422 C  C     . THR A 176 ? 0.3045 0.1525 0.1078 -0.0133 -0.0523 0.0683  177 THR A C     
1423 O  O     . THR A 176 ? 0.3318 0.1308 0.1355 -0.0143 -0.0291 0.0393  177 THR A O     
1424 C  CB    . THR A 176 ? 0.2610 0.1798 0.1236 0.0032  -0.0425 0.0534  177 THR A CB    
1425 O  OG1   . THR A 176 ? 0.4924 0.2495 0.1248 0.0674  -0.0924 0.0505  177 THR A OG1   
1426 C  CG2   . THR A 176 ? 0.2786 0.2469 0.2693 0.0356  -0.0073 0.1342  177 THR A CG2   
1427 N  N     . ASN A 177 ? 0.2816 0.1549 0.1272 0.0287  -0.0560 0.0398  178 ASN A N     
1428 C  CA    . ASN A 177 ? 0.2848 0.2089 0.1459 0.0215  -0.0239 0.0689  178 ASN A CA    
1429 C  C     . ASN A 177 ? 0.2436 0.2166 0.1511 -0.0082 -0.0280 0.0819  178 ASN A C     
1430 O  O     . ASN A 177 ? 0.3494 0.2432 0.2655 -0.0627 -0.0815 0.1674  178 ASN A O     
1431 C  CB    . ASN A 177 ? 0.2842 0.2226 0.1764 -0.0345 -0.0495 0.1034  178 ASN A CB    
1432 C  CG    . ASN A 177 ? 0.2476 0.2236 0.2066 0.0241  -0.0288 0.0834  178 ASN A CG    
1433 O  OD1   . ASN A 177 ? 0.3323 0.2469 0.2111 -0.0292 -0.0492 0.1097  178 ASN A OD1   
1434 N  ND2   . ASN A 177 ? 0.2579 0.2177 0.1889 0.0360  -0.0164 0.0839  178 ASN A ND2   
1435 N  N     . PHE A 178 ? 0.2592 0.1321 0.1217 0.0121  -0.0342 0.0182  179 PHE A N     
1436 C  CA    . PHE A 178 ? 0.2887 0.1449 0.1134 -0.0047 -0.0040 0.0183  179 PHE A CA    
1437 C  C     . PHE A 178 ? 0.2017 0.1669 0.1030 0.0187  -0.0418 -0.0125 179 PHE A C     
1438 O  O     . PHE A 178 ? 0.2776 0.1569 0.0963 0.0085  -0.0400 0.0165  179 PHE A O     
1439 C  CB    . PHE A 178 ? 0.2744 0.1858 0.0784 0.0177  0.0075  0.0340  179 PHE A CB    
1440 C  CG    . PHE A 178 ? 0.2919 0.1743 0.1023 -0.0159 -0.0011 0.0321  179 PHE A CG    
1441 C  CD1   . PHE A 178 ? 0.3603 0.1594 0.1089 0.0475  -0.0292 0.0147  179 PHE A CD1   
1442 C  CD2   . PHE A 178 ? 0.2480 0.1584 0.1038 0.0377  0.0046  0.0160  179 PHE A CD2   
1443 C  CE1   . PHE A 178 ? 0.3788 0.1485 0.1303 0.0222  -0.0268 0.0109  179 PHE A CE1   
1444 C  CE2   . PHE A 178 ? 0.2026 0.1650 0.0988 0.0167  0.0032  0.0313  179 PHE A CE2   
1445 C  CZ    . PHE A 178 ? 0.2854 0.1790 0.1282 0.0439  -0.0148 0.0384  179 PHE A CZ    
1446 N  N     . ASP A 179 ? 0.1920 0.1501 0.1156 0.0419  -0.0246 -0.0057 180 ASP A N     
1447 C  CA    . ASP A 179 ? 0.2106 0.1658 0.0968 0.0568  -0.0252 -0.0008 180 ASP A CA    
1448 C  C     . ASP A 179 ? 0.1548 0.1423 0.0829 0.0164  -0.0124 0.0056  180 ASP A C     
1449 O  O     . ASP A 179 ? 0.2032 0.1340 0.1163 0.0173  -0.0300 0.0002  180 ASP A O     
1450 C  CB    . ASP A 179 ? 0.2029 0.2065 0.1276 0.0595  -0.0592 0.0321  180 ASP A CB    
1451 C  CG    . ASP A 179 ? 0.1632 0.2731 0.1430 -0.0097 -0.0397 -0.0016 180 ASP A CG    
1452 O  OD1   . ASP A 179 ? 0.1874 0.1865 0.1284 0.0350  -0.0426 0.0067  180 ASP A OD1   
1453 O  OD2   . ASP A 179 ? 0.1873 0.5537 0.2407 0.0249  -0.0650 -0.1196 180 ASP A OD2   
1454 N  N     . PRO A 180 ? 0.1521 0.1371 0.0991 0.0277  -0.0124 0.0069  181 PRO A N     
1455 C  CA    . PRO A 180 ? 0.1347 0.1482 0.1212 0.0473  -0.0142 0.0085  181 PRO A CA    
1456 C  C     . PRO A 180 ? 0.1256 0.1384 0.0988 0.0309  -0.0119 -0.0119 181 PRO A C     
1457 O  O     . PRO A 180 ? 0.1398 0.1531 0.0999 0.0236  -0.0167 0.0098  181 PRO A O     
1458 C  CB    . PRO A 180 ? 0.1449 0.1730 0.1335 0.0259  -0.0119 0.0124  181 PRO A CB    
1459 C  CG    . PRO A 180 ? 0.1721 0.1494 0.1301 -0.0137 -0.0390 0.0202  181 PRO A CG    
1460 C  CD    . PRO A 180 ? 0.1851 0.1501 0.1104 0.0314  -0.0363 0.0103  181 PRO A CD    
1461 N  N     . ARG A 181 ? 0.1283 0.1352 0.0988 0.0217  -0.0296 0.0216  182 ARG A N     
1462 C  CA    . ARG A 181 ? 0.1104 0.1543 0.1268 -0.0021 -0.0365 -0.0100 182 ARG A CA    
1463 C  C     . ARG A 181 ? 0.1205 0.1474 0.1283 0.0124  -0.0373 0.0094  182 ARG A C     
1464 O  O     . ARG A 181 ? 0.1837 0.1543 0.1390 0.0176  -0.0365 0.0297  182 ARG A O     
1465 C  CB    . ARG A 181 ? 0.1306 0.1375 0.1537 -0.0053 -0.0183 -0.0011 182 ARG A CB    
1466 C  CG    . ARG A 181 ? 0.1307 0.1214 0.1610 0.0018  0.0023  0.0071  182 ARG A CG    
1467 C  CD    . ARG A 181 ? 0.1305 0.1343 0.2008 -0.0091 0.0326  0.0268  182 ARG A CD    
1468 N  NE    . ARG A 181 ? 0.1535 0.1564 0.2380 0.0293  0.0190  0.0529  182 ARG A NE    
1469 C  CZ    . ARG A 181 ? 0.1242 0.2092 0.2551 0.0044  -0.0047 0.0562  182 ARG A CZ    
1470 N  NH1   . ARG A 181 ? 0.1573 0.2686 0.3628 0.0668  0.0576  0.0913  182 ARG A NH1   
1471 N  NH2   . ARG A 181 ? 0.1966 0.3216 0.2761 0.0855  0.0178  0.0851  182 ARG A NH2   
1472 N  N     . GLY A 182 ? 0.1473 0.1518 0.1121 0.0390  -0.0382 -0.0020 183 GLY A N     
1473 C  CA    . GLY A 182 ? 0.2400 0.1458 0.1629 0.0252  -0.0757 0.0050  183 GLY A CA    
1474 C  C     . GLY A 182 ? 0.1982 0.1128 0.1281 0.0288  -0.0352 -0.0016 183 GLY A C     
1475 O  O     . GLY A 182 ? 0.2445 0.1149 0.1909 0.0394  -0.0720 -0.0216 183 GLY A O     
1476 N  N     . LEU A 183 ? 0.1949 0.1389 0.1249 0.0294  -0.0513 -0.0171 184 LEU A N     
1477 C  CA    . LEU A 183 ? 0.2047 0.1029 0.1280 0.0486  -0.0262 -0.0174 184 LEU A CA    
1478 C  C     . LEU A 183 ? 0.1599 0.1502 0.1269 0.0333  -0.0465 -0.0154 184 LEU A C     
1479 O  O     . LEU A 183 ? 0.1471 0.1657 0.1567 0.0389  -0.0311 0.0256  184 LEU A O     
1480 C  CB    . LEU A 183 ? 0.1922 0.1342 0.1141 0.0520  -0.0240 0.0108  184 LEU A CB    
1481 C  CG    . LEU A 183 ? 0.2133 0.1824 0.1072 0.0502  -0.0239 0.0013  184 LEU A CG    
1482 C  CD1   . LEU A 183 ? 0.2192 0.2153 0.1194 0.0560  -0.0115 0.0653  184 LEU A CD1   
1483 C  CD2   . LEU A 183 ? 0.3338 0.2235 0.1518 0.0690  -0.0087 -0.0341 184 LEU A CD2   
1484 N  N     . LEU A 184 ? 0.1578 0.1194 0.1356 0.0348  -0.0275 -0.0031 185 LEU A N     
1485 C  CA    . LEU A 184 ? 0.1514 0.1353 0.1287 -0.0074 -0.0415 0.0133  185 LEU A CA    
1486 C  C     . LEU A 184 ? 0.1934 0.1427 0.1602 -0.0341 -0.0759 0.0251  185 LEU A C     
1487 O  O     . LEU A 184 ? 0.3416 0.1963 0.2905 -0.1180 -0.2204 0.0916  185 LEU A O     
1488 C  CB    . LEU A 184 ? 0.0881 0.1491 0.1236 -0.0095 -0.0338 0.0168  185 LEU A CB    
1489 C  CG    . LEU A 184 ? 0.0758 0.1331 0.1164 0.0101  -0.0245 0.0281  185 LEU A CG    
1490 C  CD1   . LEU A 184 ? 0.0978 0.1346 0.1505 -0.0024 -0.0297 0.0076  185 LEU A CD1   
1491 C  CD2   . LEU A 184 ? 0.0892 0.1469 0.1987 0.0027  -0.0422 0.0595  185 LEU A CD2   
1492 N  N     . PRO A 185 ? 0.1223 0.1300 0.1513 -0.0122 -0.0391 0.0216  186 PRO A N     
1493 C  CA    . PRO A 185 ? 0.1508 0.1152 0.1600 -0.0075 -0.0474 0.0160  186 PRO A CA    
1494 C  C     . PRO A 185 ? 0.1144 0.1184 0.1998 -0.0323 -0.0618 0.0376  186 PRO A C     
1495 O  O     . PRO A 185 ? 0.0834 0.1218 0.3220 -0.0118 -0.0751 0.0499  186 PRO A O     
1496 C  CB    . PRO A 185 ? 0.1059 0.1450 0.1353 0.0094  -0.0069 0.0220  186 PRO A CB    
1497 C  CG    . PRO A 185 ? 0.0752 0.1408 0.1188 0.0266  -0.0160 -0.0035 186 PRO A CG    
1498 C  CD    . PRO A 185 ? 0.1009 0.1168 0.1032 0.0173  -0.0228 -0.0012 186 PRO A CD    
1499 N  N     . GLU A 186 ? 0.1219 0.1184 0.1995 -0.0340 -0.0406 0.0210  187 GLU A N     
1500 C  CA    . GLU A 186 ? 0.0859 0.1832 0.2040 -0.0370 -0.0641 0.0538  187 GLU A CA    
1501 C  C     . GLU A 186 ? 0.0795 0.1642 0.2248 -0.0274 -0.0384 0.0397  187 GLU A C     
1502 O  O     . GLU A 186 ? 0.1042 0.1654 0.2682 0.0131  -0.0322 0.0355  187 GLU A O     
1503 C  CB    . GLU A 186 ? 0.1304 0.1998 0.3209 -0.0740 -0.1257 0.0429  187 GLU A CB    
1504 C  CG    . GLU A 186 ? 0.2662 0.2590 0.3494 -0.0029 -0.0446 0.0440  187 GLU A CG    
1505 C  CD    . GLU A 186 ? 0.2181 0.2930 0.3330 0.0028  -0.0645 0.0668  187 GLU A CD    
1506 O  OE1   . GLU A 186 ? 0.1117 0.1972 0.5147 -0.0393 0.0186  -0.0114 187 GLU A OE1   
1507 O  OE2   . GLU A 186 ? 0.3952 0.3728 0.5572 0.0006  0.0957  0.2186  187 GLU A OE2   
1508 N  N     . SER A 187 ? 0.0580 0.1511 0.1878 -0.0109 -0.0285 0.0253  188 SER A N     
1509 C  CA    . SER A 187 ? 0.0594 0.1554 0.1872 -0.0148 -0.0078 0.0235  188 SER A CA    
1510 C  C     . SER A 187 ? 0.0619 0.1491 0.1944 -0.0176 -0.0073 0.0196  188 SER A C     
1511 O  O     . SER A 187 ? 0.0715 0.1734 0.1705 -0.0248 -0.0074 -0.0125 188 SER A O     
1512 C  CB    . SER A 187 ? 0.0673 0.1917 0.2172 -0.0081 -0.0028 0.0491  188 SER A CB    
1513 O  OG    . SER A 187 ? 0.1168 0.1686 0.1719 -0.0027 -0.0021 0.0367  188 SER A OG    
1514 N  N     . LEU A 188 ? 0.0477 0.1441 0.1633 -0.0150 0.0015  0.0152  189 LEU A N     
1515 C  CA    . LEU A 188 ? 0.0592 0.1506 0.1767 -0.0120 -0.0069 0.0025  189 LEU A CA    
1516 C  C     . LEU A 188 ? 0.0617 0.1352 0.1676 0.0029  -0.0055 0.0005  189 LEU A C     
1517 O  O     . LEU A 188 ? 0.0883 0.1615 0.1660 -0.0235 -0.0020 -0.0231 189 LEU A O     
1518 C  CB    . LEU A 188 ? 0.0983 0.1521 0.2033 -0.0125 0.0033  0.0164  189 LEU A CB    
1519 C  CG    . LEU A 188 ? 0.0739 0.1736 0.2287 0.0099  -0.0134 0.0438  189 LEU A CG    
1520 C  CD1   . LEU A 188 ? 0.1163 0.1805 0.3100 -0.0010 -0.0240 0.0437  189 LEU A CD1   
1521 C  CD2   . LEU A 188 ? 0.0845 0.2415 0.2295 0.0196  -0.0253 0.0561  189 LEU A CD2   
1522 N  N     . ASP A 189 ? 0.0491 0.1444 0.1450 0.0061  -0.0002 -0.0121 190 ASP A N     
1523 C  CA    . ASP A 189 ? 0.0753 0.1705 0.1256 -0.0180 0.0140  -0.0004 190 ASP A CA    
1524 C  C     . ASP A 189 ? 0.0675 0.1166 0.1178 -0.0147 0.0087  0.0114  190 ASP A C     
1525 O  O     . ASP A 189 ? 0.0546 0.1286 0.1188 -0.0192 0.0020  0.0006  190 ASP A O     
1526 C  CB    . ASP A 189 ? 0.1022 0.2181 0.1463 -0.0608 -0.0157 0.0305  190 ASP A CB    
1527 C  CG    . ASP A 189 ? 0.1387 0.2995 0.1413 -0.0853 0.0186  0.0035  190 ASP A CG    
1528 O  OD1   . ASP A 189 ? 0.1270 0.4375 0.2441 -0.0681 0.0811  -0.0695 190 ASP A OD1   
1529 O  OD2   . ASP A 189 ? 0.1892 0.4760 0.2923 -0.2049 -0.0196 0.1112  190 ASP A OD2   
1530 N  N     . TYR A 190 ? 0.0862 0.1355 0.0844 -0.0215 0.0155  0.0081  191 TYR A N     
1531 C  CA    . TYR A 190 ? 0.0773 0.1162 0.0824 -0.0095 0.0170  0.0012  191 TYR A CA    
1532 C  C     . TYR A 190 ? 0.0872 0.1046 0.0921 -0.0154 0.0036  0.0036  191 TYR A C     
1533 O  O     . TYR A 190 ? 0.0775 0.1281 0.0975 -0.0101 0.0253  0.0079  191 TYR A O     
1534 C  CB    . TYR A 190 ? 0.0875 0.1278 0.0856 -0.0172 -0.0050 0.0041  191 TYR A CB    
1535 C  CG    . TYR A 190 ? 0.0893 0.1233 0.0958 -0.0016 -0.0008 0.0072  191 TYR A CG    
1536 C  CD1   . TYR A 190 ? 0.0734 0.1320 0.1058 -0.0097 0.0065  -0.0010 191 TYR A CD1   
1537 C  CD2   . TYR A 190 ? 0.0928 0.1241 0.1216 0.0041  -0.0007 0.0252  191 TYR A CD2   
1538 C  CE1   . TYR A 190 ? 0.1018 0.1338 0.1007 0.0059  -0.0146 -0.0036 191 TYR A CE1   
1539 C  CE2   . TYR A 190 ? 0.0973 0.1179 0.1443 0.0055  -0.0071 0.0181  191 TYR A CE2   
1540 C  CZ    . TYR A 190 ? 0.0921 0.1122 0.1112 -0.0222 0.0046  0.0201  191 TYR A CZ    
1541 O  OH    . TYR A 190 ? 0.1076 0.1413 0.1278 -0.0032 0.0079  -0.0029 191 TYR A OH    
1542 N  N     . TRP A 191 ? 0.0872 0.0902 0.0754 -0.0028 0.0093  -0.0027 192 TRP A N     
1543 C  CA    . TRP A 191 ? 0.0764 0.1059 0.0733 -0.0070 0.0143  0.0098  192 TRP A CA    
1544 C  C     . TRP A 191 ? 0.0529 0.1168 0.0775 0.0048  0.0115  0.0034  192 TRP A C     
1545 O  O     . TRP A 191 ? 0.0868 0.1081 0.0781 -0.0173 0.0098  -0.0015 192 TRP A O     
1546 C  CB    . TRP A 191 ? 0.0797 0.1071 0.0838 -0.0093 0.0159  -0.0053 192 TRP A CB    
1547 C  CG    . TRP A 191 ? 0.0899 0.0998 0.0887 0.0063  0.0142  0.0108  192 TRP A CG    
1548 C  CD1   . TRP A 191 ? 0.1106 0.1046 0.0961 0.0142  0.0293  0.0055  192 TRP A CD1   
1549 C  CD2   . TRP A 191 ? 0.0641 0.0900 0.0995 0.0135  0.0023  0.0031  192 TRP A CD2   
1550 N  NE1   . TRP A 191 ? 0.1444 0.1165 0.1228 -0.0047 0.0103  0.0322  192 TRP A NE1   
1551 C  CE2   . TRP A 191 ? 0.0831 0.1038 0.1311 -0.0074 -0.0034 0.0092  192 TRP A CE2   
1552 C  CE3   . TRP A 191 ? 0.0501 0.1185 0.1118 -0.0005 0.0014  0.0083  192 TRP A CE3   
1553 C  CZ2   . TRP A 191 ? 0.0821 0.1144 0.1899 -0.0028 -0.0028 0.0139  192 TRP A CZ2   
1554 C  CZ3   . TRP A 191 ? 0.0647 0.1381 0.1492 0.0029  -0.0102 -0.0456 192 TRP A CZ3   
1555 C  CH2   . TRP A 191 ? 0.0755 0.1294 0.1769 -0.0058 -0.0296 -0.0355 192 TRP A CH2   
1556 N  N     . THR A 192 ? 0.0617 0.0982 0.0640 -0.0051 0.0025  0.0086  193 THR A N     
1557 C  CA    . THR A 192 ? 0.0596 0.0850 0.0736 -0.0014 0.0013  0.0036  193 THR A CA    
1558 C  C     . THR A 192 ? 0.0628 0.0894 0.0765 -0.0051 0.0107  0.0039  193 THR A C     
1559 O  O     . THR A 192 ? 0.0689 0.1267 0.0735 -0.0017 0.0116  0.0184  193 THR A O     
1560 C  CB    . THR A 192 ? 0.0670 0.0915 0.0769 0.0074  0.0054  0.0029  193 THR A CB    
1561 O  OG1   . THR A 192 ? 0.0684 0.0953 0.0866 0.0040  0.0110  -0.0029 193 THR A OG1   
1562 C  CG2   . THR A 192 ? 0.0865 0.1050 0.0867 -0.0072 0.0146  -0.0119 193 THR A CG2   
1563 N  N     . TYR A 193 ? 0.0631 0.0857 0.0605 -0.0119 -0.0075 0.0120  194 TYR A N     
1564 C  CA    . TYR A 193 ? 0.0642 0.0978 0.0595 -0.0032 -0.0139 0.0080  194 TYR A CA    
1565 C  C     . TYR A 193 ? 0.0472 0.0979 0.0751 0.0022  -0.0127 0.0068  194 TYR A C     
1566 O  O     . TYR A 193 ? 0.0561 0.1062 0.0728 -0.0073 -0.0102 0.0019  194 TYR A O     
1567 C  CB    . TYR A 193 ? 0.0643 0.1025 0.0721 -0.0106 -0.0017 0.0015  194 TYR A CB    
1568 C  CG    . TYR A 193 ? 0.0702 0.0850 0.0800 -0.0049 0.0045  0.0043  194 TYR A CG    
1569 C  CD1   . TYR A 193 ? 0.0726 0.0846 0.0746 0.0063  -0.0027 0.0092  194 TYR A CD1   
1570 C  CD2   . TYR A 193 ? 0.0610 0.0918 0.0766 0.0141  -0.0030 -0.0157 194 TYR A CD2   
1571 C  CE1   . TYR A 193 ? 0.0671 0.0858 0.0771 0.0060  -0.0140 0.0006  194 TYR A CE1   
1572 C  CE2   . TYR A 193 ? 0.0564 0.0962 0.0869 -0.0115 0.0028  -0.0173 194 TYR A CE2   
1573 C  CZ    . TYR A 193 ? 0.0812 0.0739 0.0726 0.0115  -0.0050 -0.0048 194 TYR A CZ    
1574 O  OH    . TYR A 193 ? 0.0680 0.0819 0.0835 -0.0026 0.0048  -0.0098 194 TYR A OH    
1575 N  N     . PRO A 194 ? 0.0437 0.1082 0.0682 -0.0012 -0.0068 -0.0005 195 PRO A N     
1576 C  CA    . PRO A 194 ? 0.0499 0.0737 0.0849 0.0145  0.0066  0.0008  195 PRO A CA    
1577 C  C     . PRO A 194 ? 0.0503 0.0899 0.0785 0.0153  0.0041  -0.0015 195 PRO A C     
1578 O  O     . PRO A 194 ? 0.0689 0.0957 0.0752 0.0152  -0.0035 0.0009  195 PRO A O     
1579 C  CB    . PRO A 194 ? 0.0648 0.1001 0.0923 0.0045  0.0107  -0.0119 195 PRO A CB    
1580 C  CG    . PRO A 194 ? 0.1009 0.1132 0.1088 -0.0067 -0.0171 -0.0092 195 PRO A CG    
1581 C  CD    . PRO A 194 ? 0.0917 0.1212 0.0736 -0.0034 -0.0019 -0.0045 195 PRO A CD    
1582 N  N     . GLY A 195 ? 0.0412 0.0892 0.0751 0.0063  -0.0047 -0.0065 196 GLY A N     
1583 C  CA    . GLY A 195 ? 0.0537 0.0855 0.0809 0.0176  -0.0006 0.0030  196 GLY A CA    
1584 C  C     . GLY A 195 ? 0.0396 0.0747 0.0909 -0.0006 -0.0034 -0.0031 196 GLY A C     
1585 O  O     . GLY A 195 ? 0.0602 0.0703 0.0881 0.0081  0.0060  -0.0040 196 GLY A O     
1586 N  N     . SER A 196 ? 0.0502 0.0722 0.0883 -0.0092 0.0025  -0.0042 197 SER A N     
1587 C  CA    . SER A 196 ? 0.0540 0.0795 0.0909 -0.0136 0.0087  -0.0060 197 SER A CA    
1588 C  C     . SER A 196 ? 0.0526 0.0668 0.0985 -0.0040 -0.0065 0.0034  197 SER A C     
1589 O  O     . SER A 196 ? 0.0565 0.0781 0.0897 -0.0003 -0.0006 -0.0074 197 SER A O     
1590 C  CB    . SER A 196 ? 0.0538 0.0847 0.0819 -0.0109 -0.0021 -0.0125 197 SER A CB    
1591 O  OG    . SER A 196 ? 0.0439 0.0821 0.1010 -0.0040 0.0025  -0.0112 197 SER A OG    
1592 N  N     . LEU A 197 ? 0.0578 0.0749 0.0827 0.0065  0.0066  -0.0077 198 LEU A N     
1593 C  CA    . LEU A 197 ? 0.0743 0.0817 0.0826 -0.0069 0.0072  -0.0148 198 LEU A CA    
1594 C  C     . LEU A 197 ? 0.0401 0.0825 0.0807 -0.0122 0.0126  -0.0107 198 LEU A C     
1595 O  O     . LEU A 197 ? 0.0494 0.0930 0.0930 -0.0059 0.0028  -0.0132 198 LEU A O     
1596 C  CB    . LEU A 197 ? 0.1017 0.1112 0.0782 0.0028  0.0107  0.0015  198 LEU A CB    
1597 C  CG    . LEU A 197 ? 0.1461 0.1116 0.1069 -0.0042 0.0081  -0.0055 198 LEU A CG    
1598 C  CD1   . LEU A 197 ? 0.1800 0.1209 0.1508 -0.0281 -0.0029 0.0194  198 LEU A CD1   
1599 C  CD2   . LEU A 197 ? 0.1298 0.1905 0.1743 0.0079  0.0372  0.0231  198 LEU A CD2   
1600 N  N     . THR A 198 ? 0.0496 0.0734 0.0833 -0.0017 -0.0004 -0.0055 199 THR A N     
1601 C  CA    . THR A 198 ? 0.0622 0.0825 0.0918 -0.0023 -0.0010 -0.0175 199 THR A CA    
1602 C  C     . THR A 198 ? 0.0526 0.0867 0.1098 -0.0036 0.0071  0.0006  199 THR A C     
1603 O  O     . THR A 198 ? 0.0679 0.0948 0.1013 -0.0061 0.0203  -0.0044 199 THR A O     
1604 C  CB    . THR A 198 ? 0.0544 0.0842 0.0893 -0.0053 -0.0002 -0.0175 199 THR A CB    
1605 O  OG1   . THR A 198 ? 0.0656 0.1002 0.0870 -0.0210 0.0005  0.0049  199 THR A OG1   
1606 C  CG2   . THR A 198 ? 0.0599 0.0889 0.0929 -0.0047 0.0041  -0.0104 199 THR A CG2   
1607 N  N     . THR A 199 ? 0.0636 0.0877 0.0895 -0.0043 0.0153  -0.0160 200 THR A N     
1608 C  CA    . THR A 199 ? 0.0696 0.0857 0.0985 -0.0135 0.0174  -0.0140 200 THR A CA    
1609 C  C     . THR A 199 ? 0.0488 0.0984 0.0875 -0.0167 0.0135  -0.0029 200 THR A C     
1610 O  O     . THR A 199 ? 0.0731 0.0902 0.1034 -0.0288 0.0135  -0.0172 200 THR A O     
1611 C  CB    . THR A 199 ? 0.0898 0.1052 0.0942 -0.0206 0.0139  0.0033  200 THR A CB    
1612 O  OG1   . THR A 199 ? 0.1187 0.1178 0.1328 -0.0064 -0.0098 0.0040  200 THR A OG1   
1613 C  CG2   . THR A 199 ? 0.1209 0.1036 0.1142 -0.0209 0.0008  -0.0057 200 THR A CG2   
1614 N  N     . PRO A 200 ? 0.0642 0.1114 0.1094 -0.0202 0.0320  -0.0095 201 PRO A N     
1615 C  CA    . PRO A 200 ? 0.0645 0.1263 0.1069 -0.0343 0.0197  -0.0074 201 PRO A CA    
1616 C  C     . PRO A 200 ? 0.0980 0.1148 0.1125 -0.0436 0.0185  0.0059  201 PRO A C     
1617 O  O     . PRO A 200 ? 0.1330 0.1233 0.1136 -0.0360 0.0047  0.0014  201 PRO A O     
1618 C  CB    . PRO A 200 ? 0.0655 0.1514 0.1572 -0.0303 0.0257  -0.0068 201 PRO A CB    
1619 C  CG    . PRO A 200 ? 0.0742 0.1474 0.1174 -0.0030 0.0198  -0.0321 201 PRO A CG    
1620 C  CD    . PRO A 200 ? 0.0720 0.1321 0.0979 -0.0105 0.0200  -0.0200 201 PRO A CD    
1621 N  N     . PRO A 201 ? 0.0806 0.1197 0.1159 -0.0183 0.0150  -0.0049 202 PRO A N     
1622 C  CA    . PRO A 201 ? 0.0951 0.1121 0.1063 -0.0224 0.0110  0.0048  202 PRO A CA    
1623 C  C     . PRO A 201 ? 0.0717 0.0990 0.1127 -0.0220 0.0139  0.0056  202 PRO A C     
1624 O  O     . PRO A 201 ? 0.0743 0.1159 0.1280 -0.0201 0.0038  -0.0113 202 PRO A O     
1625 C  CB    . PRO A 201 ? 0.1480 0.1238 0.1478 -0.0702 0.0175  0.0020  202 PRO A CB    
1626 C  CG    . PRO A 201 ? 0.1730 0.1427 0.1543 -0.0344 0.0044  -0.0063 202 PRO A CG    
1627 C  CD    . PRO A 201 ? 0.1566 0.1137 0.1554 -0.0096 0.0182  0.0038  202 PRO A CD    
1628 N  N     . LEU A 202 ? 0.0571 0.0911 0.1173 -0.0147 0.0032  0.0085  203 LEU A N     
1629 C  CA    . LEU A 202 ? 0.0610 0.0811 0.1028 -0.0129 0.0030  0.0004  203 LEU A CA    
1630 C  C     . LEU A 202 ? 0.0443 0.0856 0.1196 0.0039  0.0059  -0.0081 203 LEU A C     
1631 O  O     . LEU A 202 ? 0.0717 0.0878 0.1032 0.0017  -0.0006 -0.0027 203 LEU A O     
1632 C  CB    . LEU A 202 ? 0.0614 0.1055 0.1006 -0.0050 -0.0039 -0.0112 203 LEU A CB    
1633 C  CG    . LEU A 202 ? 0.0521 0.1039 0.0994 -0.0105 0.0035  0.0001  203 LEU A CG    
1634 C  CD1   . LEU A 202 ? 0.0794 0.1280 0.1568 0.0103  -0.0087 -0.0167 203 LEU A CD1   
1635 C  CD2   . LEU A 202 ? 0.0713 0.0962 0.1264 -0.0019 0.0167  -0.0191 203 LEU A CD2   
1636 N  N     . LEU A 203 ? 0.0662 0.0905 0.1106 -0.0039 0.0035  0.0015  204 LEU A N     
1637 C  CA    . LEU A 203 ? 0.0598 0.0780 0.1355 -0.0168 0.0113  -0.0162 204 LEU A CA    
1638 C  C     . LEU A 203 ? 0.0664 0.0671 0.1175 -0.0097 0.0069  -0.0071 204 LEU A C     
1639 O  O     . LEU A 203 ? 0.0693 0.0932 0.1115 -0.0127 0.0020  -0.0154 204 LEU A O     
1640 C  CB    . LEU A 203 ? 0.0928 0.0982 0.1528 -0.0021 0.0270  -0.0004 204 LEU A CB    
1641 C  CG    . LEU A 203 ? 0.1190 0.1046 0.1661 -0.0015 0.0364  0.0061  204 LEU A CG    
1642 C  CD1   . LEU A 203 ? 0.1642 0.1302 0.2066 -0.0080 0.0414  0.0350  204 LEU A CD1   
1643 C  CD2   . LEU A 203 ? 0.1247 0.1484 0.2861 -0.0588 0.0355  0.0164  204 LEU A CD2   
1644 N  N     . GLU A 204 ? 0.0673 0.0949 0.1201 -0.0210 -0.0003 -0.0199 205 GLU A N     
1645 C  CA    . GLU A 204 ? 0.0721 0.0959 0.1130 -0.0127 -0.0031 -0.0121 205 GLU A CA    
1646 C  C     . GLU A 204 ? 0.0603 0.0892 0.1073 -0.0165 -0.0091 -0.0172 205 GLU A C     
1647 O  O     . GLU A 204 ? 0.0952 0.1152 0.1124 -0.0013 -0.0145 -0.0306 205 GLU A O     
1648 C  CB    . GLU A 204 ? 0.0639 0.1304 0.1229 0.0125  -0.0130 -0.0198 205 GLU A CB    
1649 C  CG    . GLU A 204 ? 0.0728 0.1137 0.1196 0.0082  -0.0177 -0.0330 205 GLU A CG    
1650 C  CD    . GLU A 204 ? 0.0745 0.1404 0.1200 -0.0120 -0.0255 -0.0279 205 GLU A CD    
1651 O  OE1   . GLU A 204 ? 0.1032 0.1473 0.1752 0.0276  -0.0751 -0.0477 205 GLU A OE1   
1652 O  OE2   . GLU A 204 ? 0.0874 0.1372 0.1096 -0.0113 -0.0273 -0.0031 205 GLU A OE2   
1653 N  N     . CYS A 205 ? 0.0710 0.0710 0.1023 -0.0107 -0.0127 -0.0157 206 CYS A N     
1654 C  CA    . CYS A 205 ? 0.0803 0.0685 0.0981 -0.0134 -0.0130 -0.0076 206 CYS A CA    
1655 C  C     . CYS A 205 ? 0.0681 0.0595 0.0933 0.0033  0.0011  -0.0201 206 CYS A C     
1656 O  O     . CYS A 205 ? 0.0763 0.0732 0.1277 -0.0004 -0.0177 -0.0047 206 CYS A O     
1657 C  CB    . CYS A 205 ? 0.0788 0.0878 0.1176 -0.0147 -0.0076 0.0025  206 CYS A CB    
1658 S  SG    . CYS A 205 ? 0.1108 0.0893 0.0991 -0.0054 0.0101  0.0035  206 CYS A SG    
1659 N  N     . VAL A 206 ? 0.0547 0.0768 0.0990 -0.0040 -0.0169 0.0090  207 VAL A N     
1660 C  CA    . VAL A 206 ? 0.0616 0.0664 0.0872 -0.0046 -0.0079 0.0002  207 VAL A CA    
1661 C  C     . VAL A 206 ? 0.0574 0.0734 0.0888 0.0041  -0.0138 0.0097  207 VAL A C     
1662 O  O     . VAL A 206 ? 0.0571 0.0983 0.0999 0.0047  -0.0170 0.0140  207 VAL A O     
1663 C  CB    . VAL A 206 ? 0.0683 0.0844 0.0982 -0.0102 0.0051  -0.0005 207 VAL A CB    
1664 C  CG1   . VAL A 206 ? 0.0541 0.0929 0.1149 0.0136  -0.0182 -0.0121 207 VAL A CG1   
1665 C  CG2   . VAL A 206 ? 0.0709 0.0976 0.0975 0.0042  0.0054  -0.0141 207 VAL A CG2   
1666 N  N     . THR A 207 ? 0.0613 0.0618 0.0831 0.0050  -0.0024 0.0017  208 THR A N     
1667 C  CA    . THR A 207 ? 0.0643 0.0694 0.0801 -0.0038 -0.0025 -0.0066 208 THR A CA    
1668 C  C     . THR A 207 ? 0.0577 0.0689 0.0818 -0.0056 -0.0034 0.0056  208 THR A C     
1669 O  O     . THR A 207 ? 0.0639 0.0698 0.0916 -0.0014 -0.0146 -0.0089 208 THR A O     
1670 C  CB    . THR A 207 ? 0.0721 0.0772 0.0916 0.0099  -0.0002 -0.0029 208 THR A CB    
1671 O  OG1   . THR A 207 ? 0.0864 0.0803 0.0949 0.0036  0.0050  -0.0155 208 THR A OG1   
1672 C  CG2   . THR A 207 ? 0.0961 0.0900 0.1054 -0.0069 0.0105  0.0088  208 THR A CG2   
1673 N  N     . TRP A 208 ? 0.0549 0.0657 0.0714 0.0003  -0.0015 -0.0027 209 TRP A N     
1674 C  CA    . TRP A 208 ? 0.0424 0.0703 0.0719 0.0020  -0.0019 -0.0041 209 TRP A CA    
1675 C  C     . TRP A 208 ? 0.0465 0.0816 0.0669 0.0053  0.0000  -0.0035 209 TRP A C     
1676 O  O     . TRP A 208 ? 0.0699 0.0969 0.0695 -0.0109 0.0066  -0.0053 209 TRP A O     
1677 C  CB    . TRP A 208 ? 0.0599 0.0746 0.0742 0.0064  -0.0016 -0.0005 209 TRP A CB    
1678 C  CG    . TRP A 208 ? 0.0456 0.0692 0.0745 0.0073  0.0011  -0.0055 209 TRP A CG    
1679 C  CD1   . TRP A 208 ? 0.0661 0.0931 0.0869 -0.0094 -0.0146 -0.0011 209 TRP A CD1   
1680 C  CD2   . TRP A 208 ? 0.0466 0.0683 0.0857 0.0057  0.0074  -0.0112 209 TRP A CD2   
1681 N  NE1   . TRP A 208 ? 0.0425 0.1092 0.1060 0.0018  0.0021  -0.0022 209 TRP A NE1   
1682 C  CE2   . TRP A 208 ? 0.0535 0.0755 0.0948 0.0016  0.0069  0.0034  209 TRP A CE2   
1683 C  CE3   . TRP A 208 ? 0.0637 0.0679 0.0764 0.0097  -0.0066 -0.0044 209 TRP A CE3   
1684 C  CZ2   . TRP A 208 ? 0.0708 0.0943 0.1052 0.0275  0.0258  -0.0083 209 TRP A CZ2   
1685 C  CZ3   . TRP A 208 ? 0.0824 0.0804 0.0851 0.0078  -0.0021 -0.0190 209 TRP A CZ3   
1686 C  CH2   . TRP A 208 ? 0.0859 0.0737 0.0940 0.0198  0.0188  -0.0015 209 TRP A CH2   
1687 N  N     . ILE A 209 ? 0.0530 0.0685 0.0594 -0.0016 0.0010  -0.0021 210 ILE A N     
1688 C  CA    . ILE A 209 ? 0.0565 0.0764 0.0672 -0.0007 0.0121  0.0011  210 ILE A CA    
1689 C  C     . ILE A 209 ? 0.0630 0.0747 0.0699 0.0019  0.0120  0.0066  210 ILE A C     
1690 O  O     . ILE A 209 ? 0.1019 0.0835 0.0726 0.0007  0.0061  -0.0005 210 ILE A O     
1691 C  CB    . ILE A 209 ? 0.0629 0.0826 0.1019 0.0034  0.0155  -0.0032 210 ILE A CB    
1692 C  CG1   . ILE A 209 ? 0.0771 0.0932 0.1217 0.0125  0.0048  -0.0127 210 ILE A CG1   
1693 C  CG2   . ILE A 209 ? 0.0619 0.0852 0.1164 0.0092  0.0132  0.0060  210 ILE A CG2   
1694 C  CD1   . ILE A 209 ? 0.0912 0.0996 0.1812 0.0191  0.0030  -0.0173 210 ILE A CD1   
1695 N  N     . VAL A 210 ? 0.0615 0.0660 0.0708 -0.0004 0.0131  0.0018  211 VAL A N     
1696 C  CA    . VAL A 210 ? 0.0580 0.0678 0.0690 0.0023  0.0201  0.0049  211 VAL A CA    
1697 C  C     . VAL A 210 ? 0.0677 0.0767 0.0748 -0.0129 0.0082  0.0089  211 VAL A C     
1698 O  O     . VAL A 210 ? 0.0777 0.0972 0.0805 -0.0165 0.0190  0.0108  211 VAL A O     
1699 C  CB    . VAL A 210 ? 0.0612 0.0753 0.0826 0.0074  0.0137  0.0044  211 VAL A CB    
1700 C  CG1   . VAL A 210 ? 0.0927 0.0797 0.0938 0.0015  -0.0074 0.0002  211 VAL A CG1   
1701 C  CG2   . VAL A 210 ? 0.0799 0.0840 0.1123 -0.0096 0.0035  0.0126  211 VAL A CG2   
1702 N  N     . LEU A 211 ? 0.0472 0.0926 0.0952 -0.0114 0.0014  0.0033  212 LEU A N     
1703 C  CA    . LEU A 211 ? 0.0543 0.1046 0.0904 -0.0167 0.0107  -0.0078 212 LEU A CA    
1704 C  C     . LEU A 211 ? 0.0563 0.1009 0.0963 -0.0208 -0.0089 0.0251  212 LEU A C     
1705 O  O     . LEU A 211 ? 0.0732 0.1098 0.1026 -0.0147 0.0067  0.0133  212 LEU A O     
1706 C  CB    . LEU A 211 ? 0.0655 0.0958 0.0992 -0.0154 -0.0056 -0.0007 212 LEU A CB    
1707 C  CG    . LEU A 211 ? 0.0910 0.0995 0.1074 -0.0267 -0.0136 -0.0025 212 LEU A CG    
1708 C  CD1   . LEU A 211 ? 0.0752 0.1272 0.1471 -0.0046 -0.0281 -0.0010 212 LEU A CD1   
1709 C  CD2   . LEU A 211 ? 0.1046 0.1138 0.1204 -0.0272 -0.0017 -0.0006 212 LEU A CD2   
1710 N  N     . LYS A 212 ? 0.0550 0.1089 0.0968 -0.0212 0.0034  0.0129  213 LYS A N     
1711 C  CA    . LYS A 212 ? 0.1096 0.1149 0.1042 -0.0272 -0.0020 0.0362  213 LYS A CA    
1712 C  C     . LYS A 212 ? 0.0852 0.0933 0.1223 -0.0185 -0.0025 0.0296  213 LYS A C     
1713 O  O     . LYS A 212 ? 0.0860 0.1058 0.1743 -0.0068 -0.0284 0.0367  213 LYS A O     
1714 C  CB    . LYS A 212 ? 0.1109 0.1697 0.1302 -0.0673 0.0120  0.0275  213 LYS A CB    
1715 C  CG    . LYS A 212 ? 0.1833 0.1772 0.1634 -0.0406 0.0000  0.0286  213 LYS A CG    
1716 C  CD    . LYS A 212 ? 0.3447 0.2256 0.1753 -0.0962 0.0441  0.0202  213 LYS A CD    
1717 C  CE    . LYS A 212 ? 0.3686 0.4727 0.3804 -0.0711 0.1354  -0.0270 213 LYS A CE    
1718 N  NZ    . LYS A 212 ? 0.1880 0.5280 0.7834 -0.1997 0.0183  -0.2348 213 LYS A NZ    
1719 N  N     A GLU A 213 ? 0.0821 0.0865 0.1163 -0.0167 -0.0051 0.0152  214 GLU A N     
1720 N  N     B GLU A 213 ? 0.0850 0.0860 0.1139 -0.0143 -0.0055 0.0157  214 GLU A N     
1721 C  CA    A GLU A 213 ? 0.0775 0.0902 0.1287 -0.0091 -0.0075 0.0103  214 GLU A CA    
1722 C  CA    B GLU A 213 ? 0.0806 0.0874 0.1248 -0.0095 -0.0118 0.0169  214 GLU A CA    
1723 C  C     A GLU A 213 ? 0.0593 0.0905 0.1144 -0.0199 -0.0134 0.0049  214 GLU A C     
1724 C  C     B GLU A 213 ? 0.0675 0.0878 0.1149 -0.0218 -0.0128 0.0067  214 GLU A C     
1725 O  O     A GLU A 213 ? 0.0593 0.0977 0.1252 -0.0085 0.0059  0.0183  214 GLU A O     
1726 O  O     B GLU A 213 ? 0.0821 0.0902 0.1252 -0.0162 -0.0120 0.0160  214 GLU A O     
1727 C  CB    A GLU A 213 ? 0.0821 0.1190 0.1641 0.0055  -0.0087 -0.0006 214 GLU A CB    
1728 C  CB    B GLU A 213 ? 0.0765 0.1246 0.1519 -0.0125 -0.0092 0.0058  214 GLU A CB    
1729 C  CG    A GLU A 213 ? 0.0982 0.1226 0.1865 -0.0133 -0.0035 -0.0097 214 GLU A CG    
1730 C  CG    B GLU A 213 ? 0.0791 0.1274 0.1741 -0.0499 -0.0088 0.0140  214 GLU A CG    
1731 C  CD    A GLU A 213 ? 0.1068 0.1611 0.2475 -0.0122 -0.0182 -0.0298 214 GLU A CD    
1732 C  CD    B GLU A 213 ? 0.0933 0.1424 0.1840 -0.0449 -0.0314 0.0078  214 GLU A CD    
1733 O  OE1   A GLU A 213 ? 0.1134 0.1367 0.2846 0.0000  -0.0572 0.0102  214 GLU A OE1   
1734 O  OE1   B GLU A 213 ? 0.0960 0.1352 0.2442 -0.0355 -0.0409 -0.0100 214 GLU A OE1   
1735 O  OE2   A GLU A 213 ? 0.1742 0.1560 0.3236 -0.0092 -0.0248 -0.0749 214 GLU A OE2   
1736 O  OE2   B GLU A 213 ? 0.1405 0.1861 0.2197 -0.0702 -0.1015 0.0235  214 GLU A OE2   
1737 N  N     . PRO A 214 ? 0.0824 0.0928 0.1095 -0.0161 -0.0046 0.0128  215 PRO A N     
1738 C  CA    . PRO A 214 ? 0.1006 0.0864 0.1177 -0.0264 -0.0011 -0.0136 215 PRO A CA    
1739 C  C     . PRO A 214 ? 0.1101 0.0985 0.1273 -0.0254 -0.0053 -0.0119 215 PRO A C     
1740 O  O     . PRO A 214 ? 0.1120 0.1578 0.1378 -0.0401 -0.0201 -0.0136 215 PRO A O     
1741 C  CB    . PRO A 214 ? 0.1204 0.0921 0.1239 -0.0114 -0.0142 -0.0042 215 PRO A CB    
1742 C  CG    . PRO A 214 ? 0.2084 0.1449 0.2068 0.0183  0.0440  0.0334  215 PRO A CG    
1743 C  CD    . PRO A 214 ? 0.1158 0.1026 0.1586 -0.0064 0.0169  0.0299  215 PRO A CD    
1744 N  N     . ILE A 215 ? 0.1068 0.0927 0.1136 -0.0263 -0.0227 -0.0188 216 ILE A N     
1745 C  CA    . ILE A 215 ? 0.0954 0.1032 0.1416 0.0024  -0.0336 -0.0317 216 ILE A CA    
1746 C  C     . ILE A 215 ? 0.1139 0.0806 0.1265 -0.0081 -0.0413 -0.0120 216 ILE A C     
1747 O  O     . ILE A 215 ? 0.0989 0.1018 0.1611 0.0104  -0.0293 -0.0319 216 ILE A O     
1748 C  CB    . ILE A 215 ? 0.1484 0.1094 0.1168 0.0030  -0.0190 -0.0379 216 ILE A CB    
1749 C  CG1   . ILE A 215 ? 0.1628 0.1263 0.1233 0.0041  -0.0076 -0.0196 216 ILE A CG1   
1750 C  CG2   . ILE A 215 ? 0.1521 0.1352 0.1200 0.0172  -0.0074 -0.0333 216 ILE A CG2   
1751 C  CD1   . ILE A 215 ? 0.1633 0.1472 0.1414 0.0039  -0.0152 -0.0049 216 ILE A CD1   
1752 N  N     . SER A 216 ? 0.0836 0.1105 0.1459 0.0026  -0.0257 -0.0409 217 SER A N     
1753 C  CA    A SER A 216 ? 0.0882 0.0972 0.1357 -0.0052 -0.0379 -0.0320 217 SER A CA    
1754 C  CA    C SER A 216 ? 0.1050 0.1388 0.1413 0.0209  -0.0216 -0.0399 217 SER A CA    
1755 C  C     . SER A 216 ? 0.1042 0.1176 0.1340 0.0106  -0.0418 -0.0243 217 SER A C     
1756 O  O     . SER A 216 ? 0.1424 0.1237 0.1386 0.0177  -0.0269 -0.0354 217 SER A O     
1757 C  CB    A SER A 216 ? 0.0942 0.0519 0.1145 0.0102  -0.0305 -0.0480 217 SER A CB    
1758 C  CB    C SER A 216 ? 0.1991 0.1464 0.2554 0.0092  -0.0233 0.0304  217 SER A CB    
1759 O  OG    A SER A 216 ? 0.1290 0.1173 0.1365 -0.0216 -0.0172 0.0048  217 SER A OG    
1760 O  OG    C SER A 216 ? 0.2306 0.3962 0.3029 0.0131  -0.0870 -0.0202 217 SER A OG    
1761 N  N     . VAL A 217 ? 0.1156 0.1230 0.1208 -0.0204 -0.0286 -0.0363 218 VAL A N     
1762 C  CA    . VAL A 217 ? 0.1400 0.0978 0.1342 -0.0108 -0.0237 -0.0346 218 VAL A CA    
1763 C  C     . VAL A 217 ? 0.1322 0.1098 0.1133 -0.0112 -0.0101 -0.0447 218 VAL A C     
1764 O  O     . VAL A 217 ? 0.1316 0.1008 0.1359 -0.0142 -0.0110 -0.0221 218 VAL A O     
1765 C  CB    . VAL A 217 ? 0.1414 0.0917 0.1521 -0.0072 -0.0286 -0.0293 218 VAL A CB    
1766 C  CG1   . VAL A 217 ? 0.1662 0.0953 0.1459 0.0000  -0.0355 -0.0242 218 VAL A CG1   
1767 C  CG2   . VAL A 217 ? 0.1311 0.0976 0.1973 -0.0068 -0.0235 -0.0269 218 VAL A CG2   
1768 N  N     . SER A 218 ? 0.1514 0.1006 0.1178 -0.0260 -0.0171 -0.0342 219 SER A N     
1769 C  CA    . SER A 218 ? 0.1483 0.1067 0.1450 -0.0345 0.0051  -0.0552 219 SER A CA    
1770 C  C     . SER A 218 ? 0.1675 0.0791 0.1560 -0.0198 0.0072  -0.0466 219 SER A C     
1771 O  O     . SER A 218 ? 0.1465 0.0864 0.1601 -0.0130 0.0035  -0.0376 219 SER A O     
1772 C  CB    . SER A 218 ? 0.1526 0.1135 0.1231 -0.0183 -0.0036 -0.0262 219 SER A CB    
1773 O  OG    . SER A 218 ? 0.1835 0.1224 0.1384 -0.0297 -0.0154 -0.0336 219 SER A OG    
1774 N  N     . SER A 219 ? 0.1347 0.0711 0.1588 -0.0376 0.0137  -0.0409 220 SER A N     
1775 C  CA    A SER A 219 ? 0.1556 0.1025 0.1897 -0.0168 0.0247  -0.0362 220 SER A CA    
1776 C  CA    B SER A 219 ? 0.1579 0.0783 0.1864 -0.0089 0.0168  -0.0280 220 SER A CA    
1777 C  C     . SER A 219 ? 0.1863 0.0873 0.1885 -0.0162 0.0016  -0.0381 220 SER A C     
1778 O  O     . SER A 219 ? 0.1610 0.1211 0.2221 -0.0116 0.0412  -0.0195 220 SER A O     
1779 C  CB    A SER A 219 ? 0.1878 0.1097 0.1957 -0.0127 0.0045  -0.0744 220 SER A CB    
1780 C  CB    B SER A 219 ? 0.2039 0.0807 0.1553 0.0149  0.0347  0.0017  220 SER A CB    
1781 O  OG    A SER A 219 ? 0.1795 0.1173 0.1278 -0.0057 0.0325  -0.0240 220 SER A OG    
1782 O  OG    B SER A 219 ? 0.1942 0.1201 0.2491 -0.0072 0.0188  -0.0409 220 SER A OG    
1783 N  N     . GLU A 220 ? 0.1630 0.0918 0.1762 -0.0138 0.0276  -0.0293 221 GLU A N     
1784 C  CA    . GLU A 220 ? 0.2085 0.1121 0.1758 -0.0081 0.0072  -0.0371 221 GLU A CA    
1785 C  C     . GLU A 220 ? 0.1853 0.1105 0.1660 -0.0046 0.0368  -0.0286 221 GLU A C     
1786 O  O     . GLU A 220 ? 0.2204 0.1382 0.1683 -0.0101 0.0518  -0.0419 221 GLU A O     
1787 C  CB    . GLU A 220 ? 0.2358 0.1559 0.1645 -0.0559 0.0086  -0.0316 221 GLU A CB    
1788 C  CG    . GLU A 220 ? 0.3118 0.1930 0.2334 -0.0115 -0.0300 -0.1031 221 GLU A CG    
1789 C  CD    . GLU A 220 ? 0.4115 0.1645 0.3319 -0.0851 0.0316  -0.0956 221 GLU A CD    
1790 O  OE1   . GLU A 220 ? 0.3307 0.2368 0.4096 -0.1135 0.1187  -0.1696 221 GLU A OE1   
1791 O  OE2   . GLU A 220 ? 0.4960 0.2304 0.4365 -0.1362 0.0164  -0.1679 221 GLU A OE2   
1792 N  N     . GLN A 221 ? 0.1295 0.1182 0.1489 -0.0091 0.0005  -0.0332 222 GLN A N     
1793 C  CA    . GLN A 221 ? 0.1537 0.0984 0.1441 -0.0116 0.0022  -0.0059 222 GLN A CA    
1794 C  C     . GLN A 221 ? 0.1441 0.0995 0.1408 -0.0039 -0.0060 -0.0194 222 GLN A C     
1795 O  O     . GLN A 221 ? 0.1670 0.1158 0.1454 -0.0215 0.0096  -0.0077 222 GLN A O     
1796 C  CB    . GLN A 221 ? 0.1588 0.0886 0.1328 -0.0186 -0.0129 -0.0220 222 GLN A CB    
1797 C  CG    . GLN A 221 ? 0.1775 0.0888 0.1124 -0.0084 -0.0070 -0.0045 222 GLN A CG    
1798 C  CD    . GLN A 221 ? 0.1701 0.1014 0.1572 0.0124  -0.0189 -0.0308 222 GLN A CD    
1799 O  OE1   . GLN A 221 ? 0.1542 0.1243 0.1148 0.0015  -0.0108 -0.0277 222 GLN A OE1   
1800 N  NE2   . GLN A 221 ? 0.1852 0.1440 0.1089 0.0181  -0.0118 -0.0289 222 GLN A NE2   
1801 N  N     . VAL A 222 ? 0.1725 0.1008 0.1424 0.0000  -0.0212 0.0102  223 VAL A N     
1802 C  CA    A VAL A 222 ? 0.1588 0.1160 0.1414 0.0111  0.0045  0.0053  223 VAL A CA    
1803 C  CA    B VAL A 222 ? 0.1565 0.0948 0.1299 -0.0007 0.0043  0.0068  223 VAL A CA    
1804 C  C     . VAL A 222 ? 0.1883 0.0924 0.1586 -0.0141 0.0404  -0.0114 223 VAL A C     
1805 O  O     . VAL A 222 ? 0.1792 0.1141 0.1638 -0.0205 0.0086  0.0119  223 VAL A O     
1806 C  CB    A VAL A 222 ? 0.2447 0.1983 0.1571 0.0148  -0.0025 0.0371  223 VAL A CB    
1807 C  CB    B VAL A 222 ? 0.1443 0.0948 0.1224 -0.0095 -0.0074 -0.0120 223 VAL A CB    
1808 C  CG1   A VAL A 222 ? 0.2051 0.2598 0.3030 -0.1120 0.0741  0.0623  223 VAL A CG1   
1809 C  CG1   B VAL A 222 ? 0.0944 0.0961 0.1271 -0.0233 -0.0241 0.0272  223 VAL A CG1   
1810 C  CG2   A VAL A 222 ? 0.2334 0.2656 0.1822 0.0245  0.0056  0.0163  223 VAL A CG2   
1811 C  CG2   B VAL A 222 ? 0.1408 0.0974 0.1015 -0.0013 -0.0099 -0.0254 223 VAL A CG2   
1812 N  N     . LEU A 223 ? 0.1362 0.1073 0.1829 -0.0170 0.0189  -0.0243 224 LEU A N     
1813 C  CA    . LEU A 223 ? 0.2054 0.1202 0.1982 0.0060  0.0514  -0.0356 224 LEU A CA    
1814 C  C     . LEU A 223 ? 0.1754 0.1798 0.1560 0.0086  0.0258  -0.0294 224 LEU A C     
1815 O  O     . LEU A 223 ? 0.1573 0.1574 0.2005 -0.0076 0.0504  -0.0570 224 LEU A O     
1816 C  CB    . LEU A 223 ? 0.2108 0.1731 0.2111 -0.0047 0.0387  -0.0493 224 LEU A CB    
1817 C  CG    . LEU A 223 ? 0.3186 0.1511 0.2681 -0.0070 0.0392  -0.0709 224 LEU A CG    
1818 C  CD1   . LEU A 223 ? 0.2358 0.2235 0.2518 -0.0192 -0.0019 -0.0191 224 LEU A CD1   
1819 C  CD2   . LEU A 223 ? 0.3386 0.2504 0.3097 -0.0139 0.0355  -0.1300 224 LEU A CD2   
1820 N  N     . LYS A 224 ? 0.1593 0.1517 0.1469 -0.0159 0.0244  -0.0214 225 LYS A N     
1821 C  CA    . LYS A 224 ? 0.1420 0.1869 0.1287 -0.0090 0.0303  -0.0331 225 LYS A CA    
1822 C  C     . LYS A 224 ? 0.1444 0.2005 0.1119 -0.0231 0.0054  -0.0124 225 LYS A C     
1823 O  O     . LYS A 224 ? 0.2005 0.1541 0.1136 -0.0171 0.0349  -0.0152 225 LYS A O     
1824 C  CB    . LYS A 224 ? 0.1616 0.2673 0.1660 -0.0061 0.0197  0.0236  225 LYS A CB    
1825 C  CG    . LYS A 224 ? 0.1977 0.3153 0.1984 -0.0290 -0.0042 0.0013  225 LYS A CG    
1826 C  CD    . LYS A 224 ? 0.3649 0.3482 0.2254 -0.0080 -0.0804 0.0200  225 LYS A CD    
1827 C  CE    . LYS A 224 ? 0.4821 0.5396 0.3784 -0.0850 -0.1909 -0.0759 225 LYS A CE    
1828 N  NZ    . LYS A 224 ? 0.4395 0.3803 0.3097 0.0459  -0.0067 -0.1615 225 LYS A NZ    
1829 N  N     . PHE A 225 ? 0.1806 0.1237 0.1018 -0.0162 0.0240  -0.0032 226 PHE A N     
1830 C  CA    . PHE A 225 ? 0.1659 0.0903 0.1112 -0.0239 0.0371  0.0013  226 PHE A CA    
1831 C  C     . PHE A 225 ? 0.1633 0.1147 0.1073 -0.0117 0.0179  -0.0089 226 PHE A C     
1832 O  O     . PHE A 225 ? 0.1848 0.1000 0.1082 -0.0223 0.0291  -0.0153 226 PHE A O     
1833 C  CB    . PHE A 225 ? 0.1812 0.0935 0.1027 -0.0109 0.0361  0.0026  226 PHE A CB    
1834 C  CG    . PHE A 225 ? 0.1556 0.1071 0.1347 -0.0208 0.0344  -0.0024 226 PHE A CG    
1835 C  CD1   . PHE A 225 ? 0.2311 0.1869 0.1212 0.0425  0.0595  -0.0093 226 PHE A CD1   
1836 C  CD2   . PHE A 225 ? 0.1565 0.1920 0.1577 -0.0195 0.0173  -0.0692 226 PHE A CD2   
1837 C  CE1   . PHE A 225 ? 0.2168 0.1635 0.1623 0.0436  0.0298  0.0049  226 PHE A CE1   
1838 C  CE2   . PHE A 225 ? 0.1591 0.2152 0.1988 0.0104  -0.0014 -0.1012 226 PHE A CE2   
1839 C  CZ    . PHE A 225 ? 0.1558 0.1412 0.1946 -0.0087 0.0341  -0.0889 226 PHE A CZ    
1840 N  N     . ARG A 226 ? 0.1489 0.1033 0.0977 -0.0235 0.0320  0.0035  227 ARG A N     
1841 C  CA    . ARG A 226 ? 0.1545 0.0987 0.1072 -0.0182 0.0252  -0.0195 227 ARG A CA    
1842 C  C     . ARG A 226 ? 0.1425 0.1056 0.1240 -0.0177 0.0203  -0.0215 227 ARG A C     
1843 O  O     . ARG A 226 ? 0.1678 0.1133 0.1305 -0.0017 0.0466  -0.0022 227 ARG A O     
1844 C  CB    . ARG A 226 ? 0.1557 0.1050 0.1296 -0.0263 0.0367  -0.0071 227 ARG A CB    
1845 C  CG    . ARG A 226 ? 0.1593 0.1058 0.1147 -0.0058 0.0141  0.0118  227 ARG A CG    
1846 C  CD    . ARG A 226 ? 0.2122 0.1058 0.1274 -0.0213 0.0144  0.0201  227 ARG A CD    
1847 N  NE    . ARG A 226 ? 0.1902 0.1155 0.1109 -0.0497 -0.0061 0.0010  227 ARG A NE    
1848 C  CZ    . ARG A 226 ? 0.2160 0.1362 0.1107 -0.0673 0.0148  -0.0340 227 ARG A CZ    
1849 N  NH1   . ARG A 226 ? 0.2623 0.1246 0.1618 -0.0567 -0.0126 -0.0448 227 ARG A NH1   
1850 N  NH2   . ARG A 226 ? 0.2161 0.1103 0.1144 -0.0642 0.0166  -0.0079 227 ARG A NH2   
1851 N  N     . LYS A 227 ? 0.1345 0.1034 0.1017 -0.0157 0.0232  -0.0154 228 LYS A N     
1852 C  CA    . LYS A 227 ? 0.1806 0.1317 0.1182 -0.0381 0.0555  -0.0390 228 LYS A CA    
1853 C  C     . LYS A 227 ? 0.2088 0.1258 0.0972 -0.0109 0.0416  -0.0100 228 LYS A C     
1854 O  O     . LYS A 227 ? 0.2438 0.1401 0.1046 -0.0288 0.0526  -0.0059 228 LYS A O     
1855 C  CB    . LYS A 227 ? 0.2571 0.1684 0.1001 -0.0297 0.0271  -0.0445 228 LYS A CB    
1856 C  CG    . LYS A 227 ? 0.2907 0.1815 0.2075 -0.0523 0.0156  -0.0649 228 LYS A CG    
1857 C  CD    . LYS A 227 ? 0.3991 0.2922 0.2235 -0.1881 -0.0299 -0.0062 228 LYS A CD    
1858 C  CE    . LYS A 227 ? 0.5046 0.5328 0.3289 -0.0949 -0.0839 -0.1593 228 LYS A CE    
1859 N  NZ    . LYS A 227 ? 0.7396 0.8976 0.4816 -0.2327 -0.2359 -0.1948 228 LYS A NZ    
1860 N  N     . LEU A 228 ? 0.1856 0.1103 0.0911 -0.0347 0.0400  -0.0099 229 LEU A N     
1861 C  CA    . LEU A 228 ? 0.1871 0.1131 0.0920 -0.0338 0.0294  -0.0097 229 LEU A CA    
1862 C  C     . LEU A 228 ? 0.1901 0.1037 0.0819 -0.0259 0.0294  -0.0167 229 LEU A C     
1863 O  O     . LEU A 228 ? 0.1707 0.1380 0.1001 -0.0244 0.0318  -0.0195 229 LEU A O     
1864 C  CB    . LEU A 228 ? 0.1937 0.1066 0.0805 -0.0531 0.0233  -0.0203 229 LEU A CB    
1865 C  CG    . LEU A 228 ? 0.1904 0.1373 0.1226 -0.0281 0.0245  -0.0120 229 LEU A CG    
1866 C  CD1   . LEU A 228 ? 0.1810 0.1451 0.1140 -0.0276 0.0066  -0.0207 229 LEU A CD1   
1867 C  CD2   . LEU A 228 ? 0.1801 0.1773 0.1385 0.0194  0.0229  0.0155  229 LEU A CD2   
1868 N  N     . ASN A 229 ? 0.1994 0.1323 0.1161 -0.0488 0.0465  -0.0034 230 ASN A N     
1869 C  CA    . ASN A 229 ? 0.1918 0.1580 0.0915 -0.0471 0.0453  -0.0081 230 ASN A CA    
1870 C  C     . ASN A 229 ? 0.1833 0.1797 0.1037 0.0012  0.0465  -0.0313 230 ASN A C     
1871 O  O     . ASN A 229 ? 0.2394 0.1482 0.1309 -0.0307 0.0210  -0.0051 230 ASN A O     
1872 C  CB    . ASN A 229 ? 0.2160 0.1720 0.0905 -0.0536 0.0446  -0.0061 230 ASN A CB    
1873 C  CG    . ASN A 229 ? 0.1830 0.1552 0.1167 -0.0224 0.0415  -0.0159 230 ASN A CG    
1874 O  OD1   . ASN A 229 ? 0.3300 0.2235 0.1162 -0.0594 0.0679  -0.0150 230 ASN A OD1   
1875 N  ND2   . ASN A 229 ? 0.2116 0.1569 0.1066 -0.0527 0.0329  -0.0315 230 ASN A ND2   
1876 N  N     . PHE A 230 ? 0.1984 0.1450 0.1192 -0.0703 0.0540  -0.0081 231 PHE A N     
1877 C  CA    . PHE A 230 ? 0.1883 0.1551 0.1453 -0.0663 0.0388  -0.0015 231 PHE A CA    
1878 C  C     . PHE A 230 ? 0.2540 0.1767 0.1337 -0.0553 0.0624  0.0158  231 PHE A C     
1879 O  O     . PHE A 230 ? 0.2790 0.1662 0.1511 -0.1094 0.0349  0.0106  231 PHE A O     
1880 C  CB    . PHE A 230 ? 0.2367 0.1865 0.1323 -0.0674 0.0284  -0.0003 231 PHE A CB    
1881 C  CG    . PHE A 230 ? 0.2061 0.1330 0.1449 -0.0689 0.0296  -0.0097 231 PHE A CG    
1882 C  CD1   . PHE A 230 ? 0.1915 0.1341 0.1046 -0.0446 0.0074  -0.0072 231 PHE A CD1   
1883 C  CD2   . PHE A 230 ? 0.2230 0.1751 0.1341 -0.0392 0.0375  -0.0312 231 PHE A CD2   
1884 C  CE1   . PHE A 230 ? 0.2035 0.1541 0.1314 -0.0455 0.0388  -0.0040 231 PHE A CE1   
1885 C  CE2   . PHE A 230 ? 0.1922 0.1397 0.1619 -0.0529 0.0259  0.0117  231 PHE A CE2   
1886 C  CZ    . PHE A 230 ? 0.2160 0.1593 0.1085 -0.0564 0.0178  -0.0127 231 PHE A CZ    
1887 N  N     . ASN A 231 ? 0.2259 0.1889 0.1304 -0.0887 0.0542  -0.0304 232 ASN A N     
1888 C  CA    . ASN A 231 ? 0.1955 0.2228 0.1630 -0.0980 0.0345  -0.0196 232 ASN A CA    
1889 C  C     . ASN A 231 ? 0.1757 0.2107 0.0973 -0.0130 0.0686  -0.0070 232 ASN A C     
1890 O  O     . ASN A 231 ? 0.2448 0.1752 0.1591 -0.0531 0.0938  -0.0112 232 ASN A O     
1891 C  CB    . ASN A 231 ? 0.1735 0.2338 0.2030 -0.0879 0.0808  0.0344  232 ASN A CB    
1892 C  CG    . ASN A 231 ? 0.1884 0.1771 0.1392 -0.0580 0.0581  0.0242  232 ASN A CG    
1893 O  OD1   . ASN A 231 ? 0.2834 0.1776 0.1445 -0.0992 0.0776  -0.0094 232 ASN A OD1   
1894 N  ND2   . ASN A 231 ? 0.2773 0.2168 0.1427 -0.0624 0.0615  0.0166  232 ASN A ND2   
1895 N  N     . GLY A 232 ? 0.2582 0.1973 0.1575 -0.0577 0.0593  -0.0012 233 GLY A N     
1896 C  CA    . GLY A 232 ? 0.2496 0.1884 0.1855 -0.0559 0.0796  0.0298  233 GLY A CA    
1897 C  C     . GLY A 232 ? 0.1765 0.1591 0.2454 -0.0381 -0.0370 -0.0061 233 GLY A C     
1898 O  O     . GLY A 232 ? 0.3051 0.2490 0.1580 0.0259  0.1016  0.0491  233 GLY A O     
1899 N  N     . GLU A 233 ? 0.2546 0.1621 0.1635 -0.0123 0.0462  -0.0092 234 GLU A N     
1900 C  CA    . GLU A 233 ? 0.2468 0.1950 0.1924 -0.0036 -0.0055 -0.0149 234 GLU A CA    
1901 C  C     . GLU A 233 ? 0.2862 0.2091 0.2531 0.1157  -0.0353 -0.0644 234 GLU A C     
1902 O  O     . GLU A 233 ? 0.3593 0.3928 0.1786 -0.0554 0.1380  -0.0226 234 GLU A O     
1903 C  CB    . GLU A 233 ? 0.2857 0.2273 0.1453 0.0277  0.0613  0.0246  234 GLU A CB    
1904 C  CG    . GLU A 233 ? 0.2202 0.2306 0.1609 -0.0548 0.0815  0.0146  234 GLU A CG    
1905 C  CD    . GLU A 233 ? 0.2441 0.3078 0.1907 0.0427  0.0598  -0.0111 234 GLU A CD    
1906 O  OE1   . GLU A 233 ? 0.3337 0.2530 0.2154 -0.0374 0.0760  0.0186  234 GLU A OE1   
1907 O  OE2   . GLU A 233 ? 0.2869 0.3937 0.2010 -0.0555 0.0207  0.0163  234 GLU A OE2   
1908 N  N     . GLY A 234 ? 0.3615 0.2679 0.2359 0.0985  -0.0188 -0.1173 235 GLY A N     
1909 C  CA    . GLY A 234 ? 0.4173 0.3576 0.3258 0.2265  0.0750  0.0408  235 GLY A CA    
1910 C  C     . GLY A 234 ? 0.4623 0.9062 0.2209 0.3408  0.1016  -0.0040 235 GLY A C     
1911 O  O     . GLY A 234 ? 0.4429 1.5738 0.2445 0.3961  0.1713  0.0756  235 GLY A O     
1912 N  N     . GLU A 235 ? 0.2348 0.4061 0.2426 0.0615  0.0725  -0.0053 236 GLU A N     
1913 C  CA    . GLU A 235 ? 0.2373 0.2732 0.2626 0.0688  0.0218  -0.0291 236 GLU A CA    
1914 C  C     . GLU A 235 ? 0.4086 0.3975 0.1422 0.0474  0.1096  0.0233  236 GLU A C     
1915 O  O     . GLU A 235 ? 0.5006 0.1928 0.2711 0.0087  0.1434  0.0010  236 GLU A O     
1916 C  CB    . GLU A 235 ? 0.3176 0.3752 0.1791 0.1110  0.0643  0.0510  236 GLU A CB    
1917 C  CG    . GLU A 235 ? 0.2678 0.3577 0.2685 0.0858  0.0180  0.0644  236 GLU A CG    
1918 C  CD    . GLU A 235 ? 0.4755 0.3216 0.2934 -0.1734 0.1189  0.0570  236 GLU A CD    
1919 O  OE1   . GLU A 235 ? 0.2988 0.3871 0.3367 -0.1452 0.1337  0.0341  236 GLU A OE1   
1920 O  OE2   . GLU A 235 ? 0.6938 0.2914 0.3608 -0.1744 0.1386  0.0016  236 GLU A OE2   
1921 N  N     . PRO A 236 ? 0.2875 0.3461 0.2188 -0.0591 0.1376  0.0733  237 PRO A N     
1922 C  CA    . PRO A 236 ? 0.2272 0.3600 0.1686 0.0243  0.0798  0.0494  237 PRO A CA    
1923 C  C     . PRO A 236 ? 0.2088 0.3549 0.1118 -0.0897 0.0304  0.0207  237 PRO A C     
1924 O  O     . PRO A 236 ? 0.2331 0.3042 0.1428 -0.0806 0.0648  -0.0004 237 PRO A O     
1925 C  CB    . PRO A 236 ? 0.1845 0.4273 0.2356 -0.0787 0.0974  0.0322  237 PRO A CB    
1926 C  CG    . PRO A 236 ? 0.1689 0.4394 0.2312 -0.0430 0.0606  0.1371  237 PRO A CG    
1927 C  CD    . PRO A 236 ? 0.2915 0.4350 0.2378 -0.0076 0.1021  0.1091  237 PRO A CD    
1928 N  N     . GLU A 237 ? 0.2449 0.2935 0.1345 -0.0744 0.0618  -0.0383 238 GLU A N     
1929 C  CA    . GLU A 237 ? 0.2306 0.3379 0.1313 -0.0398 0.0541  -0.0219 238 GLU A CA    
1930 C  C     . GLU A 237 ? 0.2145 0.1980 0.1880 -0.0274 0.0593  -0.0150 238 GLU A C     
1931 O  O     . GLU A 237 ? 0.1162 0.2908 0.1775 -0.0501 0.0276  -0.0354 238 GLU A O     
1932 C  CB    . GLU A 237 ? 0.2647 0.2118 0.1402 0.0156  0.0177  -0.0362 238 GLU A CB    
1933 C  CG    . GLU A 237 ? 0.2622 0.3207 0.1890 -0.0224 0.0062  -0.0675 238 GLU A CG    
1934 C  CD    . GLU A 237 ? 0.2307 0.4564 0.1836 -0.0215 -0.0052 -0.1036 238 GLU A CD    
1935 O  OE1   . GLU A 237 ? 0.5353 1.8428 1.2778 0.6250  -0.5470 -1.3801 238 GLU A OE1   
1936 O  OE2   . GLU A 237 ? 0.2817 0.2081 0.1703 -0.0718 0.0297  -0.0808 238 GLU A OE2   
1937 N  N     A GLU A 238 ? 0.1645 0.1353 0.1310 -0.0858 0.0459  0.0013  239 GLU A N     
1938 N  N     B GLU A 238 ? 0.2245 0.1702 0.1559 -0.0591 0.0535  -0.0208 239 GLU A N     
1939 C  CA    A GLU A 238 ? 0.1549 0.1571 0.1190 -0.0556 0.0494  -0.0094 239 GLU A CA    
1940 C  CA    B GLU A 238 ? 0.1677 0.2604 0.1697 -0.0047 0.0423  0.0017  239 GLU A CA    
1941 C  C     A GLU A 238 ? 0.1728 0.1749 0.1152 -0.0397 0.0510  -0.0281 239 GLU A C     
1942 C  C     B GLU A 238 ? 0.1755 0.1938 0.1056 -0.0432 0.0538  -0.0201 239 GLU A C     
1943 O  O     A GLU A 238 ? 0.1747 0.1455 0.1538 -0.0537 0.0238  0.0168  239 GLU A O     
1944 O  O     B GLU A 238 ? 0.1885 0.2034 0.1878 -0.0528 0.0286  -0.0481 239 GLU A O     
1945 C  CB    A GLU A 238 ? 0.1260 0.1309 0.1594 -0.0378 0.0443  -0.0130 239 GLU A CB    
1946 C  CB    B GLU A 238 ? 0.2130 0.1318 0.2492 0.0680  -0.0028 0.0271  239 GLU A CB    
1947 C  CG    A GLU A 238 ? 0.2144 0.2016 0.1829 0.0169  0.0157  0.0292  239 GLU A CG    
1948 C  CG    B GLU A 238 ? 0.2025 0.2191 0.2401 0.1227  -0.0217 0.0211  239 GLU A CG    
1949 C  CD    A GLU A 238 ? 0.1870 0.3220 0.2837 0.2027  0.0365  -0.0057 239 GLU A CD    
1950 C  CD    B GLU A 238 ? 0.3090 0.2893 0.2925 0.0225  -0.0796 0.0214  239 GLU A CD    
1951 O  OE1   A GLU A 238 ? 0.2646 0.3779 0.2869 0.2218  0.0746  -0.0066 239 GLU A OE1   
1952 O  OE1   B GLU A 238 ? 0.3658 0.4149 0.3096 0.1021  -0.1203 -0.0260 239 GLU A OE1   
1953 O  OE2   A GLU A 238 ? 0.2815 0.3132 0.3123 0.1283  0.1425  0.1412  239 GLU A OE2   
1954 O  OE2   B GLU A 238 ? 0.3608 0.3440 0.2627 -0.1284 -0.0473 0.0104  239 GLU A OE2   
1955 N  N     . LEU A 239 ? 0.1630 0.1909 0.1057 -0.0321 0.0415  -0.0149 240 LEU A N     
1956 C  CA    . LEU A 239 ? 0.1412 0.1389 0.1212 -0.0159 0.0341  0.0042  240 LEU A CA    
1957 C  C     . LEU A 239 ? 0.1446 0.1402 0.0955 -0.0245 0.0326  0.0177  240 LEU A C     
1958 O  O     . LEU A 239 ? 0.1495 0.1718 0.1119 -0.0292 0.0280  -0.0087 240 LEU A O     
1959 C  CB    . LEU A 239 ? 0.1462 0.1336 0.1492 -0.0153 0.0210  -0.0005 240 LEU A CB    
1960 C  CG    . LEU A 239 ? 0.1243 0.1474 0.1999 -0.0036 0.0155  -0.0424 240 LEU A CG    
1961 C  CD1   . LEU A 239 ? 0.2247 0.1345 0.2934 -0.0048 -0.0633 -0.0241 240 LEU A CD1   
1962 C  CD2   . LEU A 239 ? 0.2099 0.1542 0.1459 0.0228  0.0242  -0.0512 240 LEU A CD2   
1963 N  N     . MET A 240 ? 0.1767 0.1256 0.1009 -0.0106 0.0362  -0.0091 241 MET A N     
1964 C  CA    . MET A 240 ? 0.1608 0.1195 0.0948 -0.0158 0.0406  -0.0094 241 MET A CA    
1965 C  C     . MET A 240 ? 0.1283 0.1146 0.0756 -0.0109 0.0295  -0.0265 241 MET A C     
1966 O  O     . MET A 240 ? 0.1422 0.1300 0.0998 -0.0222 0.0177  -0.0025 241 MET A O     
1967 C  CB    . MET A 240 ? 0.2028 0.1342 0.1119 -0.0124 0.0173  0.0090  241 MET A CB    
1968 C  CG    . MET A 240 ? 0.1952 0.1348 0.1242 -0.0481 0.0429  -0.0117 241 MET A CG    
1969 S  SD    . MET A 240 ? 0.2237 0.1122 0.1361 -0.0395 0.0295  0.0071  241 MET A SD    
1970 C  CE    . MET A 240 ? 0.2603 0.1151 0.1332 -0.0639 0.0583  0.0257  241 MET A CE    
1971 N  N     . VAL A 241 ? 0.1362 0.0963 0.0976 -0.0317 0.0310  -0.0255 242 VAL A N     
1972 C  CA    . VAL A 241 ? 0.1135 0.1019 0.0984 -0.0228 0.0400  -0.0164 242 VAL A CA    
1973 C  C     . VAL A 241 ? 0.1266 0.0906 0.1023 -0.0159 0.0339  -0.0146 242 VAL A C     
1974 O  O     . VAL A 241 ? 0.1107 0.1277 0.1025 -0.0266 0.0444  -0.0335 242 VAL A O     
1975 C  CB    . VAL A 241 ? 0.1302 0.1003 0.0980 -0.0262 0.0393  -0.0132 242 VAL A CB    
1976 C  CG1   . VAL A 241 ? 0.1413 0.1180 0.1121 -0.0278 0.0463  -0.0333 242 VAL A CG1   
1977 C  CG2   . VAL A 241 ? 0.1575 0.1060 0.1282 -0.0098 0.0374  -0.0179 242 VAL A CG2   
1978 N  N     . ASP A 242 ? 0.0966 0.0784 0.0972 -0.0230 0.0302  -0.0133 243 ASP A N     
1979 C  CA    . ASP A 242 ? 0.1071 0.0730 0.1116 -0.0041 0.0243  -0.0061 243 ASP A CA    
1980 C  C     . ASP A 242 ? 0.0992 0.0756 0.0892 -0.0060 0.0301  -0.0136 243 ASP A C     
1981 O  O     . ASP A 242 ? 0.1170 0.0923 0.1359 -0.0042 0.0133  -0.0259 243 ASP A O     
1982 C  CB    . ASP A 242 ? 0.1060 0.0966 0.0970 -0.0031 0.0109  -0.0179 243 ASP A CB    
1983 C  CG    . ASP A 242 ? 0.0908 0.0994 0.1315 0.0060  0.0199  -0.0280 243 ASP A CG    
1984 O  OD1   . ASP A 242 ? 0.1013 0.0793 0.1399 0.0041  0.0317  -0.0165 243 ASP A OD1   
1985 O  OD2   . ASP A 242 ? 0.1532 0.1148 0.1660 0.0204  0.0479  -0.0384 243 ASP A OD2   
1986 N  N     . ASN A 243 ? 0.0920 0.0681 0.0908 -0.0100 0.0265  -0.0173 244 ASN A N     
1987 C  CA    . ASN A 243 ? 0.0924 0.0607 0.0993 -0.0119 0.0340  -0.0043 244 ASN A CA    
1988 C  C     . ASN A 243 ? 0.0736 0.0906 0.0858 0.0005  0.0185  -0.0018 244 ASN A C     
1989 O  O     . ASN A 243 ? 0.1160 0.0846 0.0957 0.0085  0.0245  -0.0019 244 ASN A O     
1990 C  CB    . ASN A 243 ? 0.1158 0.0874 0.0842 0.0017  0.0501  -0.0034 244 ASN A CB    
1991 C  CG    . ASN A 243 ? 0.1305 0.0815 0.0846 -0.0270 0.0093  0.0082  244 ASN A CG    
1992 O  OD1   . ASN A 243 ? 0.1264 0.0791 0.1178 -0.0168 0.0197  0.0206  244 ASN A OD1   
1993 N  ND2   . ASN A 243 ? 0.1403 0.1693 0.1467 -0.0340 -0.0237 0.0620  244 ASN A ND2   
1994 N  N     . TRP A 244 ? 0.1078 0.0755 0.0825 0.0068  0.0227  -0.0130 245 TRP A N     
1995 C  CA    . TRP A 244 ? 0.0747 0.0767 0.0862 -0.0119 0.0215  -0.0174 245 TRP A CA    
1996 C  C     . TRP A 244 ? 0.0743 0.0729 0.0916 -0.0090 0.0314  -0.0057 245 TRP A C     
1997 O  O     . TRP A 244 ? 0.0812 0.1076 0.1062 0.0098  0.0127  -0.0272 245 TRP A O     
1998 C  CB    . TRP A 244 ? 0.1067 0.0752 0.0819 -0.0100 0.0175  -0.0038 245 TRP A CB    
1999 C  CG    . TRP A 244 ? 0.0593 0.0799 0.0863 -0.0056 0.0128  -0.0022 245 TRP A CG    
2000 C  CD1   . TRP A 244 ? 0.0950 0.0768 0.0810 -0.0025 0.0173  0.0049  245 TRP A CD1   
2001 C  CD2   . TRP A 244 ? 0.0651 0.0772 0.0904 0.0025  0.0108  -0.0019 245 TRP A CD2   
2002 N  NE1   . TRP A 244 ? 0.1199 0.0643 0.0934 -0.0042 0.0273  0.0009  245 TRP A NE1   
2003 C  CE2   . TRP A 244 ? 0.0704 0.0652 0.1046 -0.0054 0.0237  0.0098  245 TRP A CE2   
2004 C  CE3   . TRP A 244 ? 0.1078 0.0957 0.1035 -0.0026 0.0065  0.0027  245 TRP A CE3   
2005 C  CZ2   . TRP A 244 ? 0.1224 0.0687 0.1184 0.0118  0.0133  0.0028  245 TRP A CZ2   
2006 C  CZ3   . TRP A 244 ? 0.1069 0.0992 0.1127 -0.0043 0.0140  0.0134  245 TRP A CZ3   
2007 C  CH2   . TRP A 244 ? 0.1073 0.0869 0.1284 0.0028  0.0174  0.0289  245 TRP A CH2   
2008 N  N     . ARG A 245 ? 0.0823 0.0654 0.0859 0.0024  0.0170  -0.0107 246 ARG A N     
2009 C  CA    . ARG A 245 ? 0.0752 0.0837 0.0869 0.0063  0.0137  -0.0168 246 ARG A CA    
2010 C  C     . ARG A 245 ? 0.0746 0.0909 0.0730 0.0062  0.0010  -0.0180 246 ARG A C     
2011 O  O     . ARG A 245 ? 0.0845 0.1132 0.1056 -0.0004 0.0117  -0.0153 246 ARG A O     
2012 C  CB    . ARG A 245 ? 0.0652 0.0760 0.0913 -0.0036 0.0191  -0.0135 246 ARG A CB    
2013 C  CG    . ARG A 245 ? 0.0487 0.0938 0.0902 0.0090  0.0129  -0.0109 246 ARG A CG    
2014 C  CD    . ARG A 245 ? 0.0522 0.1015 0.0784 0.0067  0.0052  -0.0166 246 ARG A CD    
2015 N  NE    . ARG A 245 ? 0.0430 0.1092 0.1236 0.0005  0.0018  -0.0264 246 ARG A NE    
2016 C  CZ    . ARG A 245 ? 0.0604 0.1089 0.0852 -0.0087 0.0212  -0.0151 246 ARG A CZ    
2017 N  NH1   . ARG A 245 ? 0.0799 0.1022 0.1042 0.0034  0.0173  -0.0234 246 ARG A NH1   
2018 N  NH2   . ARG A 245 ? 0.0868 0.1292 0.1252 -0.0043 0.0000  -0.0290 246 ARG A NH2   
2019 N  N     . PRO A 246 ? 0.0673 0.0954 0.1052 -0.0059 0.0067  0.0054  247 PRO A N     
2020 C  CA    . PRO A 246 ? 0.0831 0.1005 0.0999 -0.0008 -0.0031 0.0107  247 PRO A CA    
2021 C  C     . PRO A 246 ? 0.0791 0.0958 0.1056 0.0183  -0.0207 0.0062  247 PRO A C     
2022 O  O     . PRO A 246 ? 0.0938 0.1026 0.1039 -0.0060 0.0045  0.0028  247 PRO A O     
2023 C  CB    . PRO A 246 ? 0.1329 0.1206 0.1227 0.0475  0.0115  0.0042  247 PRO A CB    
2024 C  CG    . PRO A 246 ? 0.1418 0.2477 0.2705 0.0665  0.0361  0.1100  247 PRO A CG    
2025 C  CD    . PRO A 246 ? 0.0704 0.1114 0.1523 0.0047  0.0203  0.0150  247 PRO A CD    
2026 N  N     . ALA A 247 ? 0.1052 0.0836 0.1004 0.0060  -0.0004 0.0058  248 ALA A N     
2027 C  CA    . ALA A 247 ? 0.0986 0.0781 0.0955 0.0235  -0.0032 0.0104  248 ALA A CA    
2028 C  C     . ALA A 247 ? 0.0633 0.1030 0.0961 0.0207  0.0094  0.0128  248 ALA A C     
2029 O  O     . ALA A 247 ? 0.0791 0.1204 0.1232 0.0283  -0.0025 0.0145  248 ALA A O     
2030 C  CB    . ALA A 247 ? 0.1170 0.1239 0.1089 0.0045  0.0170  0.0042  248 ALA A CB    
2031 N  N     . GLN A 248 ? 0.0762 0.1003 0.0953 0.0158  -0.0038 0.0094  249 GLN A N     
2032 C  CA    . GLN A 248 ? 0.0545 0.1113 0.1010 0.0111  -0.0022 0.0180  249 GLN A CA    
2033 C  C     . GLN A 248 ? 0.1002 0.1081 0.0984 0.0081  -0.0083 0.0290  249 GLN A C     
2034 O  O     . GLN A 248 ? 0.0890 0.1175 0.1222 0.0091  0.0081  0.0129  249 GLN A O     
2035 C  CB    . GLN A 248 ? 0.0892 0.1151 0.1179 -0.0063 0.0028  0.0076  249 GLN A CB    
2036 C  CG    . GLN A 248 ? 0.0938 0.1039 0.1225 -0.0125 0.0070  0.0231  249 GLN A CG    
2037 C  CD    . GLN A 248 ? 0.1027 0.1399 0.1086 -0.0138 0.0076  0.0013  249 GLN A CD    
2038 O  OE1   . GLN A 248 ? 0.1010 0.1928 0.1563 -0.0344 -0.0006 -0.0271 249 GLN A OE1   
2039 N  NE2   . GLN A 248 ? 0.0950 0.1537 0.1192 -0.0052 -0.0063 -0.0016 249 GLN A NE2   
2040 N  N     . PRO A 249 ? 0.1000 0.1544 0.1003 0.0315  -0.0059 0.0004  250 PRO A N     
2041 C  CA    . PRO A 249 ? 0.1287 0.1992 0.1048 0.0539  -0.0096 0.0028  250 PRO A CA    
2042 C  C     . PRO A 249 ? 0.1131 0.1221 0.0970 0.0255  -0.0212 -0.0006 250 PRO A C     
2043 O  O     . PRO A 249 ? 0.0905 0.1493 0.1166 0.0315  0.0016  0.0254  250 PRO A O     
2044 C  CB    . PRO A 249 ? 0.1270 0.2062 0.1381 0.0937  -0.0536 -0.0232 250 PRO A CB    
2045 C  CG    . PRO A 249 ? 0.1202 0.2439 0.1466 0.0415  -0.0544 -0.0454 250 PRO A CG    
2046 C  CD    . PRO A 249 ? 0.0800 0.1811 0.1370 0.0410  -0.0211 -0.0066 250 PRO A CD    
2047 N  N     . LEU A 250 ? 0.1447 0.1380 0.0960 0.0419  0.0040  0.0175  251 LEU A N     
2048 C  CA    . LEU A 250 ? 0.1118 0.1244 0.1117 0.0109  0.0028  -0.0104 251 LEU A CA    
2049 C  C     . LEU A 250 ? 0.0886 0.1591 0.1033 0.0260  -0.0165 -0.0018 251 LEU A C     
2050 O  O     . LEU A 250 ? 0.1251 0.1296 0.1129 0.0221  -0.0358 -0.0106 251 LEU A O     
2051 C  CB    . LEU A 250 ? 0.1607 0.1389 0.1401 0.0052  0.0293  0.0091  251 LEU A CB    
2052 C  CG    . LEU A 250 ? 0.1556 0.1546 0.1209 -0.0072 0.0348  -0.0138 251 LEU A CG    
2053 C  CD1   . LEU A 250 ? 0.1277 0.1837 0.1329 -0.0037 -0.0124 -0.0604 251 LEU A CD1   
2054 C  CD2   . LEU A 250 ? 0.1696 0.1841 0.1880 -0.0111 0.0390  -0.0093 251 LEU A CD2   
2055 N  N     . LYS A 251 ? 0.1287 0.1662 0.1111 0.0606  -0.0358 -0.0074 252 LYS A N     
2056 C  CA    . LYS A 251 ? 0.1343 0.1948 0.1019 0.0321  -0.0468 0.0059  252 LYS A CA    
2057 C  C     . LYS A 251 ? 0.1359 0.1778 0.1412 0.0517  -0.0391 0.0062  252 LYS A C     
2058 O  O     . LYS A 251 ? 0.2032 0.2507 0.1463 0.0168  0.0282  0.0208  252 LYS A O     
2059 C  CB    . LYS A 251 ? 0.1476 0.2136 0.1227 0.0011  -0.0446 -0.0275 252 LYS A CB    
2060 C  CG    . LYS A 251 ? 0.2011 0.2676 0.1871 -0.0120 -0.0039 -0.0698 252 LYS A CG    
2061 C  CD    . LYS A 251 ? 0.2568 0.2831 0.2320 0.0075  0.0401  -0.0110 252 LYS A CD    
2062 C  CE    . LYS A 251 ? 0.2106 0.3214 0.3938 -0.0031 0.0652  -0.0644 252 LYS A CE    
2063 N  NZ    . LYS A 251 ? 0.2998 0.3129 0.5187 0.0438  0.0056  0.0445  252 LYS A NZ    
2064 N  N     . ASN A 252 ? 0.1378 0.1876 0.1134 0.0195  -0.0238 -0.0301 253 ASN A N     
2065 C  CA    . ASN A 252 ? 0.1671 0.3455 0.1590 0.0452  -0.0365 -0.0866 253 ASN A CA    
2066 C  C     . ASN A 252 ? 0.2021 0.3062 0.2525 0.0875  -0.0696 -0.0571 253 ASN A C     
2067 O  O     . ASN A 252 ? 0.2745 0.2724 0.3165 0.0662  0.0341  0.0054  253 ASN A O     
2068 C  CB    . ASN A 252 ? 0.2495 0.3948 0.2293 0.0159  -0.0733 -0.1175 253 ASN A CB    
2069 C  CG    . ASN A 252 ? 0.3434 0.3436 0.2769 0.0458  0.0414  -0.0567 253 ASN A CG    
2070 O  OD1   . ASN A 252 ? 0.7012 0.6946 0.4750 -0.1897 0.0472  0.1613  253 ASN A OD1   
2071 N  ND2   . ASN A 252 ? 0.4115 0.3536 0.4456 0.0472  0.0377  -0.1104 253 ASN A ND2   
2072 N  N     . ARG A 253 ? 0.1562 0.2684 0.1008 0.0434  -0.0289 0.0295  254 ARG A N     
2073 C  CA    . ARG A 253 ? 0.1250 0.1442 0.0871 0.0429  -0.0021 0.0005  254 ARG A CA    
2074 C  C     . ARG A 253 ? 0.1580 0.1221 0.1384 0.0297  0.0309  -0.0262 254 ARG A C     
2075 O  O     . ARG A 253 ? 0.2211 0.1357 0.3047 0.0519  0.1221  0.0346  254 ARG A O     
2076 C  CB    . ARG A 253 ? 0.1343 0.1060 0.0865 0.0394  -0.0118 0.0024  254 ARG A CB    
2077 C  CG    . ARG A 253 ? 0.1151 0.1020 0.0891 0.0323  -0.0087 -0.0131 254 ARG A CG    
2078 C  CD    . ARG A 253 ? 0.1104 0.0979 0.0952 0.0102  0.0057  -0.0095 254 ARG A CD    
2079 N  NE    . ARG A 253 ? 0.1031 0.1006 0.0691 0.0193  -0.0113 0.0036  254 ARG A NE    
2080 C  CZ    . ARG A 253 ? 0.0612 0.0948 0.0792 -0.0001 0.0076  0.0105  254 ARG A CZ    
2081 N  NH1   . ARG A 253 ? 0.0740 0.1032 0.0784 0.0015  -0.0006 0.0086  254 ARG A NH1   
2082 N  NH2   . ARG A 253 ? 0.0784 0.1095 0.0702 0.0058  -0.0118 0.0089  254 ARG A NH2   
2083 N  N     . GLN A 254 ? 0.1288 0.1388 0.1154 0.0091  0.0055  -0.0154 255 GLN A N     
2084 C  CA    . GLN A 254 ? 0.1429 0.2137 0.1030 -0.0184 0.0015  -0.0351 255 GLN A CA    
2085 C  C     . GLN A 254 ? 0.1216 0.1487 0.1146 0.0035  -0.0074 -0.0022 255 GLN A C     
2086 O  O     . GLN A 254 ? 0.1749 0.1484 0.1731 -0.0173 -0.0380 0.0058  255 GLN A O     
2087 C  CB    . GLN A 254 ? 0.1684 0.3039 0.1523 -0.0215 0.0245  -0.0771 255 GLN A CB    
2088 C  CG    . GLN A 254 ? 0.2853 0.3451 0.2094 -0.0562 0.0077  0.0000  255 GLN A CG    
2089 C  CD    . GLN A 254 ? 0.2726 0.5407 0.2654 0.0605  0.0505  0.1099  255 GLN A CD    
2090 O  OE1   . GLN A 254 ? 0.3934 0.5161 0.4804 0.1366  0.1282  -0.0621 255 GLN A OE1   
2091 N  NE2   . GLN A 254 ? 0.4813 0.3904 0.2728 0.0500  0.0950  0.0198  255 GLN A NE2   
2092 N  N     . ILE A 255 ? 0.1073 0.1232 0.0833 0.0034  0.0011  0.0049  256 ILE A N     
2093 C  CA    . ILE A 255 ? 0.0922 0.1184 0.0669 0.0136  0.0060  0.0126  256 ILE A CA    
2094 C  C     . ILE A 255 ? 0.0996 0.1329 0.0817 0.0172  0.0167  0.0177  256 ILE A C     
2095 O  O     . ILE A 255 ? 0.1256 0.1420 0.1090 0.0125  0.0219  0.0369  256 ILE A O     
2096 C  CB    . ILE A 255 ? 0.1137 0.1299 0.0831 0.0139  0.0057  -0.0102 256 ILE A CB    
2097 C  CG1   . ILE A 255 ? 0.1133 0.1136 0.1144 0.0306  0.0115  -0.0117 256 ILE A CG1   
2098 C  CG2   . ILE A 255 ? 0.1016 0.1447 0.1173 0.0109  0.0117  0.0004  256 ILE A CG2   
2099 C  CD1   . ILE A 255 ? 0.1257 0.1346 0.1380 -0.0152 0.0243  -0.0381 256 ILE A CD1   
2100 N  N     . LYS A 256 ? 0.0929 0.1314 0.0741 0.0002  0.0099  0.0104  257 LYS A N     
2101 C  CA    . LYS A 256 ? 0.0957 0.1299 0.0776 -0.0034 0.0152  0.0100  257 LYS A CA    
2102 C  C     . LYS A 256 ? 0.0778 0.1231 0.0848 -0.0012 0.0124  0.0197  257 LYS A C     
2103 O  O     . LYS A 256 ? 0.1070 0.1759 0.0768 -0.0473 0.0107  -0.0002 257 LYS A O     
2104 C  CB    . LYS A 256 ? 0.1131 0.1495 0.1211 -0.0062 0.0388  -0.0098 257 LYS A CB    
2105 C  CG    . LYS A 256 ? 0.1487 0.1922 0.1572 -0.0582 0.0433  -0.0459 257 LYS A CG    
2106 C  CD    . LYS A 256 ? 0.1966 0.2099 0.2468 -0.0087 0.0594  -0.0521 257 LYS A CD    
2107 C  CE    . LYS A 256 ? 0.4173 0.3734 0.2764 -0.1860 -0.0172 -0.1919 257 LYS A CE    
2108 N  NZ    . LYS A 256 ? 0.4523 0.4077 0.3089 -0.0637 -0.1800 -0.0937 257 LYS A NZ    
2109 N  N     . ALA A 257 ? 0.0945 0.1531 0.0843 -0.0134 0.0378  0.0067  258 ALA A N     
2110 C  CA    . ALA A 257 ? 0.0786 0.1471 0.1003 -0.0035 0.0284  0.0021  258 ALA A CA    
2111 C  C     . ALA A 257 ? 0.0830 0.1348 0.1078 -0.0090 0.0145  0.0049  258 ALA A C     
2112 O  O     . ALA A 257 ? 0.0967 0.2041 0.1027 0.0048  0.0328  -0.0203 258 ALA A O     
2113 C  CB    . ALA A 257 ? 0.1129 0.1612 0.1206 0.0016  0.0164  0.0082  258 ALA A CB    
2114 N  N     . SER A 258 ? 0.0770 0.1608 0.0956 -0.0163 0.0171  0.0006  259 SER A N     
2115 C  CA    . SER A 258 ? 0.1027 0.1529 0.1261 -0.0022 0.0324  -0.0066 259 SER A CA    
2116 C  C     . SER A 258 ? 0.0984 0.1707 0.1334 -0.0086 0.0428  -0.0074 259 SER A C     
2117 O  O     . SER A 258 ? 0.1203 0.2350 0.1778 0.0379  0.0506  -0.0155 259 SER A O     
2118 C  CB    . SER A 258 ? 0.0969 0.1358 0.1567 0.0117  0.0124  0.0120  259 SER A CB    
2119 O  OG    . SER A 258 ? 0.1019 0.1887 0.1102 -0.0253 0.0215  0.0046  259 SER A OG    
2120 N  N     . PHE A 259 ? 0.1093 0.1769 0.1356 -0.0101 0.0475  0.0130  260 PHE A N     
2121 C  CA    . PHE A 259 ? 0.1373 0.1918 0.1638 -0.0321 0.0588  0.0248  260 PHE A CA    
2122 C  C     . PHE A 259 ? 0.2147 0.2426 0.1420 -0.0826 0.0466  0.0416  260 PHE A C     
2123 O  O     . PHE A 259 ? 0.2521 0.2330 0.1935 -0.0832 -0.0160 0.0798  260 PHE A O     
2124 C  CB    . PHE A 259 ? 0.1264 0.2108 0.1881 -0.0336 0.0328  0.0308  260 PHE A CB    
2125 C  CG    . PHE A 259 ? 0.1483 0.1668 0.1591 -0.0316 0.0374  0.0190  260 PHE A CG    
2126 C  CD1   . PHE A 259 ? 0.1360 0.1699 0.1232 -0.0431 0.0122  0.0202  260 PHE A CD1   
2127 C  CD2   . PHE A 259 ? 0.1947 0.1990 0.2617 -0.0429 0.0710  0.0951  260 PHE A CD2   
2128 C  CE1   . PHE A 259 ? 0.1583 0.1827 0.1976 -0.0476 0.0610  -0.0031 260 PHE A CE1   
2129 C  CE2   . PHE A 259 ? 0.1937 0.1543 0.3196 -0.0311 0.0195  0.0406  260 PHE A CE2   
2130 C  CZ    . PHE A 259 ? 0.2041 0.2015 0.2755 -0.0424 0.0065  0.0210  260 PHE A CZ    
2131 N  N     . LYS A 260 ? 0.2743 0.3399 0.2222 -0.1361 0.0517  0.1013  261 LYS A N     
2132 C  CA    . LYS A 260 ? 0.3313 0.5169 0.2673 -0.1419 -0.0579 0.2072  261 LYS A CA    
2133 C  C     . LYS A 260 ? 0.6613 0.5017 0.4364 0.0087  0.0323  0.3118  261 LYS A C     
2134 O  O     . LYS A 260 ? 0.8380 0.6578 0.7283 -0.1418 -0.2883 0.4100  261 LYS A O     
2135 C  CB    . LYS A 260 ? 0.6504 0.4176 0.3032 -0.1989 0.1738  0.1101  261 LYS A CB    
2136 C  CG    . LYS A 260 ? 0.6427 0.5902 0.3714 -0.1471 0.2743  0.0115  261 LYS A CG    
2137 C  CD    . LYS A 260 ? 0.7127 0.8503 0.5550 -0.2191 0.3748  0.1237  261 LYS A CD    
2138 C  CE    . LYS A 260 ? 1.0855 0.8791 0.5719 -0.1009 0.1912  0.0992  261 LYS A CE    
2139 N  NZ    . LYS A 260 ? 1.1962 1.1956 0.8496 0.0013  0.4511  0.0797  261 LYS A NZ    
2140 O  OXT   . LYS A 260 ? 0.5407 0.6077 0.5827 -0.1482 0.0462  0.3871  261 LYS A OXT   
2141 ZN ZN    . ZN  B .   ? 0.0848 0.0724 0.0878 -0.0046 0.0164  0.0041  301 ZN  A ZN    
2142 C  C1    . MNP C .   ? 0.4528 0.3143 0.3017 0.0588  0.0706  0.0681  302 MNP A C1    
2143 C  C2    . MNP C .   ? 0.2042 0.2715 0.3248 -0.1300 0.0300  0.0079  302 MNP A C2    
2144 C  "C1'" . MNP C .   ? 0.1709 0.1905 0.2048 0.0027  0.0101  -0.0294 302 MNP A "C1'" 
2145 C  "C2'" . MNP C .   ? 0.1919 0.2047 0.2244 0.0074  -0.0263 0.0040  302 MNP A "C2'" 
2146 C  "C3'" . MNP C .   ? 0.2493 0.2146 0.2619 0.0354  0.0420  0.0336  302 MNP A "C3'" 
2147 N  "N3'" . MNP C .   ? 0.2041 0.2375 0.2345 0.0007  -0.0118 0.0328  302 MNP A "N3'" 
2148 O  "O3'" . MNP C .   ? 0.1865 0.3065 0.3161 0.0024  0.0087  -0.0352 302 MNP A "O3'" 
2149 O  "O4'" . MNP C .   ? 0.3178 0.1778 0.3232 0.0318  -0.1424 -0.0145 302 MNP A "O4'" 
2150 C  "C4'" . MNP C .   ? 0.2011 0.2151 0.2213 0.0031  -0.0103 -0.0104 302 MNP A "C4'" 
2151 C  "C5'" . MNP C .   ? 0.1917 0.1520 0.2192 -0.0158 -0.0203 -0.0246 302 MNP A "C5'" 
2152 C  "C6'" . MNP C .   ? 0.2218 0.1837 0.2687 -0.0062 0.0068  -0.0151 302 MNP A "C6'" 
2153 O  O1    . MNP C .   ? 0.4826 0.4385 0.3178 0.0111  0.0619  0.1660  302 MNP A O1    
2154 O  O2    . MNP C .   ? 0.2905 0.3203 0.4044 0.0252  0.0835  0.1217  302 MNP A O2    
2155 O  O     . HOH D .   ? 0.2643 0.4499 0.2348 0.1513  0.1254  -0.0158 401 HOH A O     
2156 O  O     . HOH D .   ? 0.2842 0.2500 0.4246 0.0236  -0.1375 0.0114  402 HOH A O     
2157 O  O     . HOH D .   ? 0.4472 0.1676 0.1619 0.0590  -0.0836 0.0216  403 HOH A O     
2158 O  O     . HOH D .   ? 0.8354 0.3614 0.3599 0.2893  0.1589  0.1635  404 HOH A O     
2159 O  O     . HOH D .   ? 0.2295 0.3266 0.4858 0.0735  0.0259  0.0557  405 HOH A O     
2160 O  O     . HOH D .   ? 0.5704 0.4137 0.5706 0.0203  0.2107  0.1441  406 HOH A O     
2161 O  O     . HOH D .   ? 0.2973 0.2017 0.2570 -0.0264 0.0800  -0.0341 407 HOH A O     
2162 O  O     . HOH D .   ? 0.4469 0.5466 0.3364 -0.1703 -0.0883 0.1595  408 HOH A O     
2163 O  O     . HOH D .   ? 0.5656 0.2497 0.3671 -0.0910 0.1590  -0.1914 409 HOH A O     
2164 O  O     . HOH D .   ? 0.8610 0.2699 0.3571 0.2441  -0.1309 -0.0631 410 HOH A O     
2165 O  O     . HOH D .   ? 0.1704 0.2574 0.3743 0.0407  0.0804  0.0471  411 HOH A O     
2166 O  O     . HOH D .   ? 0.2125 0.1830 0.2472 0.0225  -0.0247 0.0059  412 HOH A O     
2167 O  O     . HOH D .   ? 0.8527 0.4187 0.9769 -0.1246 -0.3863 0.4101  413 HOH A O     
2168 O  O     . HOH D .   ? 0.2783 0.3884 0.4494 0.1279  -0.1649 -0.2730 414 HOH A O     
2169 O  O     . HOH D .   ? 0.7530 0.1913 0.5305 -0.1581 -0.1205 -0.0533 415 HOH A O     
2170 O  O     . HOH D .   ? 0.3855 0.3381 0.5446 0.1222  -0.2634 -0.1421 416 HOH A O     
2171 O  O     . HOH D .   ? 0.3822 0.3720 0.5461 0.0708  -0.0689 0.0910  417 HOH A O     
2172 O  O     . HOH D .   ? 0.2014 0.1266 0.1315 0.0133  0.0385  0.0083  418 HOH A O     
2173 O  O     . HOH D .   ? 0.1951 0.0874 0.0688 -0.0005 0.0017  -0.0001 419 HOH A O     
2174 O  O     . HOH D .   ? 0.0997 0.0954 0.1013 -0.0105 0.0242  -0.0054 420 HOH A O     
2175 O  O     . HOH D .   ? 0.1097 0.0848 0.1730 -0.0330 -0.0398 -0.0021 421 HOH A O     
2176 O  O     . HOH D .   ? 0.1530 0.1875 0.2013 0.0078  -0.0926 -0.0405 422 HOH A O     
2177 O  O     . HOH D .   ? 0.2086 0.5028 0.4534 -0.0844 0.1122  -0.0321 423 HOH A O     
2178 O  O     . HOH D .   ? 0.2976 0.3524 0.3787 -0.0624 0.1339  -0.0393 424 HOH A O     
2179 O  O     . HOH D .   ? 0.1664 0.1882 0.2770 0.0074  -0.0082 -0.0542 425 HOH A O     
2180 O  O     . HOH D .   ? 0.2320 0.3074 0.2716 -0.0111 0.1201  0.0061  426 HOH A O     
2181 O  O     . HOH D .   ? 0.1323 0.3224 0.4895 0.0000  -0.0004 0.0075  427 HOH A O     
2182 O  O     . HOH D .   ? 0.3407 0.2008 0.1695 -0.1243 -0.0417 0.0182  428 HOH A O     
2183 O  O     . HOH D .   ? 0.1680 0.5042 0.4352 0.0431  0.0201  -0.0828 429 HOH A O     
2184 O  O     . HOH D .   ? 0.1363 0.9919 0.5748 0.1865  -0.1096 -0.4670 430 HOH A O     
2185 O  O     . HOH D .   ? 0.4618 0.4632 0.2591 -0.2447 0.0020  -0.1002 431 HOH A O     
2186 O  O     . HOH D .   ? 0.2773 0.6181 0.2597 -0.1503 -0.0321 -0.0034 432 HOH A O     
2187 O  O     . HOH D .   ? 0.6918 0.1847 0.5160 0.1335  -0.2577 -0.0295 433 HOH A O     
2188 O  O     . HOH D .   ? 0.9079 0.4960 0.4492 0.2349  -0.4037 -0.1548 434 HOH A O     
2189 O  O     . HOH D .   ? 0.2191 0.2422 0.2019 -0.0801 0.0896  -0.0400 435 HOH A O     
2190 O  O     . HOH D .   ? 0.5545 0.4873 0.7294 0.1119  -0.2947 0.0446  436 HOH A O     
2191 O  O     . HOH D .   ? 0.1398 0.2988 0.4920 0.0084  -0.0069 -0.0253 437 HOH A O     
2192 O  O     . HOH D .   ? 0.2770 0.2277 0.1714 0.0269  -0.0683 -0.0060 438 HOH A O     
2193 O  O     . HOH D .   ? 0.4149 0.2209 0.1268 0.0324  0.0312  0.0179  439 HOH A O     
2194 O  O     . HOH D .   ? 0.4585 0.4355 0.3039 -0.0893 0.0383  0.1111  440 HOH A O     
2195 O  O     . HOH D .   ? 0.2734 0.4546 0.1366 -0.1232 -0.0634 0.0195  441 HOH A O     
2196 O  O     . HOH D .   ? 0.3007 0.2925 0.2590 0.0292  -0.0174 0.0661  442 HOH A O     
2197 O  O     . HOH D .   ? 0.4884 0.3832 0.4911 -0.1359 0.0867  0.1575  443 HOH A O     
2198 O  O     . HOH D .   ? 0.3399 0.2969 0.2606 0.0660  0.0068  0.0586  444 HOH A O     
2199 O  O     . HOH D .   ? 0.5977 0.2138 0.1584 -0.2034 -0.0364 0.0883  445 HOH A O     
2200 O  O     . HOH D .   ? 0.3744 0.2376 0.2249 0.0388  -0.0197 0.0376  446 HOH A O     
2201 O  O     . HOH D .   ? 0.5213 0.2966 0.1706 -0.1280 -0.0294 0.0067  447 HOH A O     
2202 O  O     . HOH D .   ? 0.3852 0.4624 0.4118 -0.1582 0.1984  -0.2577 448 HOH A O     
2203 O  O     . HOH D .   ? 0.1917 0.2553 0.2150 0.0335  -0.0083 0.0139  449 HOH A O     
2204 O  O     . HOH D .   ? 0.1311 0.0966 0.1025 -0.0067 -0.0055 -0.0126 450 HOH A O     
2205 O  O     . HOH D .   ? 0.1269 0.0820 0.1816 -0.0226 0.0206  0.0237  451 HOH A O     
2206 O  O     . HOH D .   ? 0.2015 0.3366 0.3320 0.0695  0.0951  -0.0090 452 HOH A O     
2207 O  O     . HOH D .   ? 0.3293 0.4460 0.1950 0.1191  -0.0048 -0.0865 453 HOH A O     
2208 O  O     . HOH D .   ? 0.6621 0.1933 0.3385 -0.1323 -0.0371 0.0957  454 HOH A O     
2209 O  O     . HOH D .   ? 0.3015 0.5044 0.3025 -0.0919 -0.0212 0.2301  455 HOH A O     
2210 O  O     . HOH D .   ? 0.1079 0.1268 0.1220 -0.0006 -0.0184 0.0281  456 HOH A O     
2211 O  O     . HOH D .   ? 0.1687 0.1950 0.1623 0.0222  0.0633  -0.0250 457 HOH A O     
2212 O  O     . HOH D .   ? 0.2421 0.4780 0.2792 0.1396  0.0470  -0.0306 458 HOH A O     
2213 O  O     . HOH D .   ? 0.1262 0.0943 0.1238 -0.0078 0.0286  -0.0111 459 HOH A O     
2214 O  O     . HOH D .   ? 0.3302 0.3182 0.2662 -0.0913 -0.1159 -0.0244 460 HOH A O     
2215 O  O     . HOH D .   ? 0.3366 0.2235 0.1348 -0.0955 0.0580  0.0396  461 HOH A O     
2216 O  O     . HOH D .   ? 0.2242 0.2483 0.2719 -0.0332 -0.0589 0.1321  462 HOH A O     
2217 O  O     . HOH D .   ? 0.5897 0.2873 0.1131 -0.0683 0.0325  -0.0529 463 HOH A O     
2218 O  O     . HOH D .   ? 0.4121 0.5612 0.2454 0.0254  0.0048  -0.2315 464 HOH A O     
2219 O  O     . HOH D .   ? 0.4196 0.2666 0.1954 -0.1319 0.1066  -0.0907 465 HOH A O     
2220 O  O     . HOH D .   ? 0.1071 0.0885 0.1003 -0.0076 0.0023  0.0000  466 HOH A O     
2221 O  O     . HOH D .   ? 0.4339 0.4875 0.8297 0.1367  -0.0726 -0.3686 467 HOH A O     
2222 O  O     . HOH D .   ? 0.2459 0.3503 0.2974 0.0030  0.1160  0.0955  468 HOH A O     
2223 O  O     . HOH D .   ? 0.3712 0.2381 0.2540 -0.0569 -0.1169 -0.0062 469 HOH A O     
2224 O  O     . HOH D .   ? 0.0994 0.1105 0.1118 0.0178  0.0023  0.0122  470 HOH A O     
2225 O  O     . HOH D .   ? 0.2980 0.2044 0.2212 0.0100  -0.0090 0.1214  471 HOH A O     
2226 O  O     . HOH D .   ? 0.1804 0.1698 0.3586 0.0300  -0.0212 -0.0795 472 HOH A O     
2227 O  O     . HOH D .   ? 0.1098 0.1892 0.1821 0.0218  -0.0234 0.0139  473 HOH A O     
2228 O  O     . HOH D .   ? 0.3429 0.5182 0.1975 -0.2198 0.0315  -0.0393 474 HOH A O     
2229 O  O     . HOH D .   ? 0.2270 0.3379 0.2700 -0.1677 -0.0209 0.0250  475 HOH A O     
2230 O  O     . HOH D .   ? 0.1831 0.1168 0.1711 -0.0035 0.0125  -0.0024 476 HOH A O     
2231 O  O     . HOH D .   ? 0.1951 0.1739 0.5327 0.0383  0.1338  -0.0224 477 HOH A O     
2232 O  O     . HOH D .   ? 0.0780 0.0982 0.1219 -0.0069 0.0200  0.0007  478 HOH A O     
2233 O  O     . HOH D .   ? 0.6619 0.3263 0.5662 0.2480  -0.0917 -0.0147 479 HOH A O     
2234 O  O     . HOH D .   ? 0.1947 0.1998 0.2595 0.0156  -0.0022 -0.0102 480 HOH A O     
2235 O  O     . HOH D .   ? 0.5568 0.3631 0.3752 0.1000  0.0549  -0.0996 481 HOH A O     
2236 O  O     . HOH D .   ? 0.1874 0.1890 0.1711 -0.0207 -0.0055 0.0050  482 HOH A O     
2237 O  O     . HOH D .   ? 0.7044 0.2476 0.1573 0.1016  0.0688  0.0301  483 HOH A O     
2238 O  O     . HOH D .   ? 0.3398 0.5516 0.1837 -0.0802 -0.0468 0.1248  484 HOH A O     
2239 O  O     . HOH D .   ? 0.2887 0.2376 0.3091 0.0036  0.1207  0.0796  485 HOH A O     
2240 O  O     . HOH D .   ? 0.3412 0.2735 0.1938 -0.0089 0.0114  -0.0956 486 HOH A O     
2241 O  O     . HOH D .   ? 0.4300 0.2224 0.3405 0.1823  -0.1319 -0.0137 487 HOH A O     
2242 O  O     . HOH D .   ? 0.2079 0.1993 0.2468 -0.0147 -0.0009 0.0598  488 HOH A O     
2243 O  O     . HOH D .   ? 0.2056 0.3048 0.3433 0.0648  0.0250  0.0505  489 HOH A O     
2244 O  O     . HOH D .   ? 0.2211 0.3586 0.3326 -0.0106 -0.0323 0.1907  490 HOH A O     
2245 O  O     . HOH D .   ? 0.2404 0.5466 0.2959 0.0047  0.0615  0.0143  491 HOH A O     
2246 O  O     . HOH D .   ? 0.3453 0.4329 0.1876 0.0586  -0.0748 0.0786  492 HOH A O     
2247 O  O     . HOH D .   ? 0.5074 0.6180 0.5041 -0.0930 0.0576  -0.3327 493 HOH A O     
2248 O  O     . HOH D .   ? 0.1307 0.1709 0.2854 -0.0207 -0.0569 0.0200  494 HOH A O     
2249 O  O     . HOH D .   ? 0.1772 0.1399 0.1793 -0.0329 0.0189  -0.0412 495 HOH A O     
2250 O  O     . HOH D .   ? 0.2093 0.5436 0.2504 -0.0525 -0.0620 0.1364  496 HOH A O     
2251 O  O     . HOH D .   ? 0.0924 0.1495 0.1363 0.0095  -0.0031 0.0341  497 HOH A O     
2252 O  O     . HOH D .   ? 0.3130 0.2379 0.2856 0.0524  -0.0769 -0.0980 498 HOH A O     
2253 O  O     . HOH D .   ? 0.6197 0.6682 0.2481 -0.3981 -0.1222 -0.0438 499 HOH A O     
2254 O  O     . HOH D .   ? 0.2044 0.4276 0.3009 -0.0333 -0.1171 0.0561  500 HOH A O     
2255 O  O     . HOH D .   ? 0.1667 0.2666 0.1849 -0.0160 -0.0085 -0.0510 501 HOH A O     
2256 O  O     . HOH D .   ? 0.1637 0.2537 0.1861 -0.0148 -0.0591 0.0301  502 HOH A O     
2257 O  O     . HOH D .   ? 0.1858 0.2374 0.1362 0.0731  -0.0254 -0.0373 503 HOH A O     
2258 O  O     . HOH D .   ? 0.5531 0.3600 0.5634 0.2053  0.2334  0.2050  504 HOH A O     
2259 O  O     . HOH D .   ? 0.1438 0.1344 0.1811 -0.0135 0.0397  -0.0078 505 HOH A O     
2260 O  O     . HOH D .   ? 0.2571 0.1596 0.1573 -0.0131 -0.0516 0.0194  506 HOH A O     
2261 O  O     . HOH D .   ? 0.1829 0.2723 0.3262 -0.0328 0.0454  0.0016  507 HOH A O     
2262 O  O     . HOH D .   ? 0.2074 0.2768 0.1978 -0.0323 -0.0052 -0.0634 508 HOH A O     
2263 O  O     . HOH D .   ? 0.1297 0.1568 0.2088 -0.0056 0.0213  0.0086  509 HOH A O     
2264 O  O     . HOH D .   ? 0.0567 0.1723 0.2048 0.0053  -0.0211 -0.0448 510 HOH A O     
2265 O  O     . HOH D .   ? 0.4960 0.5828 0.4013 0.3355  0.1118  0.1549  511 HOH A O     
2266 O  O     . HOH D .   ? 0.3051 0.2415 0.3640 -0.0329 -0.0990 0.0729  512 HOH A O     
2267 O  O     . HOH D .   ? 0.2667 0.2255 0.2746 0.0092  0.0276  -0.0339 513 HOH A O     
2268 O  O     . HOH D .   ? 0.1520 0.1334 0.1625 0.0401  0.0370  0.0115  514 HOH A O     
2269 O  O     . HOH D .   ? 0.1024 0.2711 0.3192 -0.0303 -0.0040 0.0230  515 HOH A O     
2270 O  O     . HOH D .   ? 0.4758 0.3482 0.8826 -0.1381 -0.1513 0.1260  516 HOH A O     
2271 O  O     . HOH D .   ? 0.1436 0.1732 0.1632 0.0009  -0.0309 0.0167  517 HOH A O     
2272 O  O     . HOH D .   ? 0.1295 0.1861 0.1668 -0.0393 -0.0179 0.0563  518 HOH A O     
2273 O  O     . HOH D .   ? 0.2490 0.2466 0.1649 -0.0355 0.0028  -0.0310 519 HOH A O     
2274 O  O     . HOH D .   ? 0.5028 0.2157 0.2954 -0.0441 0.0437  -0.0152 520 HOH A O     
2275 O  O     . HOH D .   ? 0.1088 0.2396 0.8384 -0.0570 0.0653  0.0067  521 HOH A O     
2276 O  O     . HOH D .   ? 0.2365 0.1405 0.1591 0.0403  -0.0195 -0.0169 522 HOH A O     
2277 O  O     . HOH D .   ? 0.4164 0.2097 0.6157 -0.1405 -0.0008 -0.0006 523 HOH A O     
2278 O  O     . HOH D .   ? 0.1769 1.1811 0.9046 -0.2387 0.1360  -0.0173 524 HOH A O     
2279 O  O     . HOH D .   ? 0.3172 0.1828 0.1640 0.0317  -0.0852 -0.0082 525 HOH A O     
2280 O  O     . HOH D .   ? 0.3236 0.1941 0.1517 0.0412  -0.0307 -0.0424 526 HOH A O     
2281 O  O     . HOH D .   ? 0.2781 0.5626 0.2053 0.0734  -0.0294 -0.0380 527 HOH A O     
2282 O  O     . HOH D .   ? 0.1919 0.2744 0.2741 0.0476  0.0208  0.0380  528 HOH A O     
2283 O  O     . HOH D .   ? 0.1104 0.3373 0.1865 -0.0037 -0.0063 0.1048  529 HOH A O     
2284 O  O     . HOH D .   ? 0.2099 0.5151 0.4823 -0.0273 0.1330  -0.1447 530 HOH A O     
2285 O  O     . HOH D .   ? 0.2189 0.1868 0.1507 -0.0089 -0.0182 -0.0181 531 HOH A O     
2286 O  O     . HOH D .   ? 0.3445 0.2831 0.2455 0.0797  0.1030  -0.0776 532 HOH A O     
2287 O  O     . HOH D .   ? 0.0770 0.2029 0.1767 0.0223  0.0265  -0.0219 533 HOH A O     
2288 O  O     . HOH D .   ? 0.4472 0.2116 0.1526 -0.0651 -0.0371 -0.0253 534 HOH A O     
2289 O  O     . HOH D .   ? 0.2194 0.6981 0.4370 0.0020  0.1446  0.1795  535 HOH A O     
2290 O  O     . HOH D .   ? 0.4687 0.6006 0.3617 -0.2523 -0.0327 0.3030  536 HOH A O     
2291 O  O     . HOH D .   ? 0.1858 0.1521 0.1674 0.0260  -0.0357 -0.0076 537 HOH A O     
2292 O  O     . HOH D .   ? 0.1733 0.2060 0.1970 0.0557  0.0153  -0.0255 538 HOH A O     
2293 O  O     . HOH D .   ? 0.4576 0.6100 0.4455 -0.0927 0.1926  0.1645  539 HOH A O     
2294 O  O     . HOH D .   ? 0.2151 0.5913 0.8282 -0.0664 0.1167  0.1029  540 HOH A O     
2295 O  O     . HOH D .   ? 1.4608 1.9425 0.4159 1.2699  -0.1348 -0.3908 541 HOH A O     
2296 O  O     . HOH D .   ? 0.1026 0.4002 0.3344 0.0158  0.0187  0.1731  542 HOH A O     
2297 O  O     . HOH D .   ? 0.4160 0.2647 0.4021 0.0868  0.0569  0.0650  543 HOH A O     
2298 O  O     . HOH D .   ? 0.1588 0.2735 0.3065 0.0814  0.0589  0.0544  544 HOH A O     
2299 O  O     . HOH D .   ? 0.1598 0.3274 0.1916 0.0354  -0.0408 -0.0325 545 HOH A O     
2300 O  O     . HOH D .   ? 0.4460 0.5845 0.4981 0.2434  0.2193  0.0204  546 HOH A O     
2301 O  O     . HOH D .   ? 0.3474 0.2259 0.3813 0.0083  -0.0264 -0.0348 547 HOH A O     
2302 O  O     . HOH D .   ? 0.3780 0.1262 0.1355 -0.0720 -0.0109 -0.0030 548 HOH A O     
2303 O  O     . HOH D .   ? 0.1521 0.1734 0.1639 -0.0248 -0.0120 -0.0195 549 HOH A O     
2304 O  O     . HOH D .   ? 0.3902 0.1812 0.1423 0.0132  0.0163  0.0021  550 HOH A O     
2305 O  O     . HOH D .   ? 0.1835 0.1452 0.2374 -0.0670 -0.0616 -0.0044 551 HOH A O     
2306 O  O     . HOH D .   ? 0.2328 0.4123 0.6241 -0.0390 0.0275  -0.1069 552 HOH A O     
2307 O  O     . HOH D .   ? 0.3856 0.2730 0.1917 0.1698  -0.0447 0.0331  553 HOH A O     
2308 O  O     . HOH D .   ? 0.4158 0.2822 0.2278 -0.0824 0.0636  0.0677  554 HOH A O     
2309 O  O     . HOH D .   ? 1.8252 1.3189 0.3166 -0.7299 0.4369  -0.3505 555 HOH A O     
2310 O  O     . HOH D .   ? 2.5350 1.1347 0.4314 0.9400  0.7324  0.4145  556 HOH A O     
2311 O  O     . HOH D .   ? 0.1844 0.2172 0.2144 -0.0102 0.0468  -0.0339 557 HOH A O     
2312 O  O     . HOH D .   ? 0.0944 0.1987 0.1315 -0.0195 -0.0401 0.0426  558 HOH A O     
2313 O  O     . HOH D .   ? 0.4277 0.0950 0.2687 0.0260  -0.1556 -0.0108 559 HOH A O     
2314 O  O     . HOH D .   ? 0.3761 0.2747 0.2176 -0.0132 0.0204  -0.0122 560 HOH A O     
2315 O  O     . HOH D .   ? 0.1375 0.3249 0.4206 0.0437  0.0498  0.1581  561 HOH A O     
2316 O  O     . HOH D .   ? 0.2188 0.2419 0.3441 0.0797  0.0523  0.0659  562 HOH A O     
2317 O  O     . HOH D .   ? 0.1344 0.2148 0.2412 0.0208  0.0038  -0.0247 563 HOH A O     
2318 O  O     . HOH D .   ? 0.3088 0.1888 0.2741 0.0768  0.0909  0.0985  564 HOH A O     
2319 O  O     . HOH D .   ? 0.2055 0.1647 1.1556 0.0456  0.2751  0.1373  565 HOH A O     
2320 O  O     . HOH D .   ? 0.3466 0.1010 0.2120 0.0279  0.0991  -0.0301 566 HOH A O     
2321 O  O     . HOH D .   ? 0.1469 0.5534 0.2630 0.0294  -0.0426 -0.1155 567 HOH A O     
2322 O  O     . HOH D .   ? 0.2229 0.1809 0.2153 0.0236  0.0550  0.0878  568 HOH A O     
2323 O  O     . HOH D .   ? 0.3342 0.3368 0.5335 0.1208  -0.1468 -0.1930 569 HOH A O     
2324 O  O     . HOH D .   ? 0.4348 0.2375 0.2922 -0.0293 0.1778  0.0227  570 HOH A O     
2325 O  O     . HOH D .   ? 1.0118 0.3123 0.2004 -0.2505 0.1600  -0.0478 571 HOH A O     
2326 O  O     . HOH D .   ? 0.2422 0.2126 0.2291 -0.0540 -0.0155 -0.0292 572 HOH A O     
2327 O  O     . HOH D .   ? 0.3638 0.4019 0.2546 0.0098  0.0570  -0.0559 573 HOH A O     
2328 O  O     . HOH D .   ? 0.0908 0.1944 0.2776 -0.0148 0.0023  0.0228  574 HOH A O     
2329 O  O     . HOH D .   ? 0.3284 0.2854 0.3249 0.0427  -0.0928 -0.0829 575 HOH A O     
2330 O  O     . HOH D .   ? 0.3041 0.2297 0.2770 -0.0195 0.0414  -0.0373 576 HOH A O     
2331 O  O     . HOH D .   ? 0.1475 0.1861 0.3113 0.0638  0.0174  0.0367  577 HOH A O     
2332 O  O     . HOH D .   ? 0.3580 0.3448 0.2367 -0.0330 0.0097  0.0924  578 HOH A O     
2333 O  O     . HOH D .   ? 0.5363 0.4294 0.1354 0.1724  0.0243  0.0374  579 HOH A O     
2334 O  O     . HOH D .   ? 2.4179 0.4634 0.1435 0.4236  0.1279  0.0263  580 HOH A O     
2335 O  O     . HOH D .   ? 0.0884 0.1094 0.1286 0.0101  0.0036  0.0082  581 HOH A O     
2336 O  O     . HOH D .   ? 0.1623 0.3242 0.3237 0.1319  -0.0685 -0.0275 582 HOH A O     
2337 O  O     . HOH D .   ? 0.6972 0.2414 0.1313 0.2174  -0.1107 -0.0346 583 HOH A O     
2338 O  O     . HOH D .   ? 0.3204 1.3434 1.0171 -0.3679 -0.3209 0.9719  584 HOH A O     
2339 O  O     . HOH D .   ? 0.1946 0.2143 0.2058 0.0408  -0.0164 0.0295  585 HOH A O     
2340 O  O     . HOH D .   ? 0.1072 0.5028 0.3429 -0.0676 0.0554  -0.0944 586 HOH A O     
2341 O  O     . HOH D .   ? 1.1921 0.1878 0.4249 -0.2681 0.3105  -0.1061 587 HOH A O     
2342 O  O     . HOH D .   ? 0.3490 0.3383 0.3843 -0.0522 0.2181  -0.0799 588 HOH A O     
2343 O  O     . HOH D .   ? 0.2159 0.1834 0.2919 0.0430  0.0546  0.0441  589 HOH A O     
2344 O  O     . HOH D .   ? 0.2116 0.4382 0.4576 0.1064  0.1342  0.1306  590 HOH A O     
2345 O  O     . HOH D .   ? 0.4386 0.3470 0.2364 0.1328  0.1113  0.0909  591 HOH A O     
2346 O  O     . HOH D .   ? 0.2423 0.2693 0.3263 -0.0513 0.0789  -0.0640 592 HOH A O     
2347 O  O     . HOH D .   ? 0.3627 0.2022 0.2989 0.0667  -0.1706 -0.0850 593 HOH A O     
2348 O  O     . HOH D .   ? 0.6100 0.2569 0.2604 -0.0926 0.0249  -0.1020 594 HOH A O     
2349 O  O     . HOH D .   ? 0.5316 0.3292 0.1627 -0.1648 0.0211  -0.0072 595 HOH A O     
2350 O  O     . HOH D .   ? 0.1553 0.1563 0.1642 -0.0241 -0.0036 0.0072  596 HOH A O     
2351 O  O     . HOH D .   ? 0.3813 0.1164 0.2465 -0.0053 -0.0674 0.0077  597 HOH A O     
2352 O  O     . HOH D .   ? 0.3228 0.3094 0.1694 -0.0571 0.0066  0.0808  598 HOH A O     
2353 O  O     . HOH D .   ? 0.5667 0.5166 0.2390 -0.0501 0.0837  0.2468  599 HOH A O     
2354 O  O     . HOH D .   ? 1.1856 0.1978 1.1766 -0.0380 -0.4241 0.2795  600 HOH A O     
2355 O  O     . HOH D .   ? 0.2520 0.2280 0.4287 -0.0283 0.0558  0.0341  601 HOH A O     
2356 O  O     . HOH D .   ? 2.7321 0.4373 1.2244 0.8584  -1.2160 -0.4019 602 HOH A O     
2357 O  O     . HOH D .   ? 1.4934 2.8741 2.6369 -1.6306 -1.9560 2.2478  603 HOH A O     
2358 O  O     . HOH D .   ? 0.1423 0.0911 0.1416 -0.0188 -0.0026 -0.0117 604 HOH A O     
2359 O  O     . HOH D .   ? 0.1767 0.5028 0.2123 0.0820  0.0405  0.0762  605 HOH A O     
2360 O  O     . HOH D .   ? 0.1903 0.7584 0.3435 -0.0617 -0.0145 0.1942  606 HOH A O     
2361 O  O     . HOH D .   ? 0.2731 0.8643 0.7022 0.3564  0.1943  0.4202  607 HOH A O     
2362 O  O     . HOH D .   ? 0.1782 0.5847 0.2427 0.0375  0.0015  -0.0214 608 HOH A O     
2363 O  O     . HOH D .   ? 0.4119 0.2684 0.9018 0.0425  -0.0726 0.1555  609 HOH A O     
2364 O  O     . HOH D .   ? 0.2083 0.2537 0.2671 -0.0680 -0.0244 0.0459  610 HOH A O     
2365 O  O     . HOH D .   ? 0.2866 0.9215 0.4347 -0.1813 0.0262  -0.1607 611 HOH A O     
2366 O  O     . HOH D .   ? 0.2190 0.2161 0.1965 0.0043  0.0226  0.0050  612 HOH A O     
2367 O  O     . HOH D .   ? 0.1898 0.1832 0.2829 0.0412  -0.0331 -0.0507 613 HOH A O     
2368 O  O     . HOH D .   ? 0.2602 0.1934 0.3085 0.0667  -0.1576 -0.0363 614 HOH A O     
2369 O  O     . HOH D .   ? 0.3576 0.5491 0.3492 0.1533  -0.1214 -0.2876 615 HOH A O     
2370 O  O     . HOH D .   ? 0.3203 0.7300 0.5988 0.1578  -0.0165 0.2196  616 HOH A O     
2371 O  O     . HOH D .   ? 0.1865 0.3343 0.3683 -0.0314 0.0455  -0.0388 617 HOH A O     
2372 O  O     . HOH D .   ? 0.2170 0.2047 0.1798 -0.0648 -0.0118 0.0021  618 HOH A O     
2373 O  O     . HOH D .   ? 0.6261 0.7121 0.2608 0.0469  0.1136  0.1698  619 HOH A O     
2374 O  O     . HOH D .   ? 0.2434 0.2108 0.2478 -0.0202 0.0106  0.0672  620 HOH A O     
2375 O  O     . HOH D .   ? 0.2612 0.2711 0.2686 0.0421  0.0135  -0.0201 621 HOH A O     
2376 O  O     . HOH D .   ? 0.3554 0.4017 0.5364 0.0906  0.0036  -0.0109 622 HOH A O     
2377 O  O     . HOH D .   ? 0.2624 0.6227 0.2278 0.0545  -0.0453 0.0395  623 HOH A O     
2378 O  O     . HOH D .   ? 0.5568 0.2164 0.3459 -0.0535 -0.1669 0.0234  624 HOH A O     
2379 O  O     . HOH D .   ? 0.3254 0.1714 0.2696 -0.0361 -0.0424 -0.0074 625 HOH A O     
2380 O  O     . HOH D .   ? 0.3745 0.4069 0.2750 0.2223  -0.0524 -0.0105 626 HOH A O     
2381 O  O     . HOH D .   ? 0.2247 0.2774 0.2427 -0.0076 0.0432  0.0417  627 HOH A O     
2382 O  O     . HOH D .   ? 0.5456 0.3099 1.0244 -0.1354 -0.0190 -0.0446 628 HOH A O     
2383 O  O     . HOH D .   ? 0.2900 0.3400 0.3653 0.0053  -0.0040 -0.0271 629 HOH A O     
2384 O  O     . HOH D .   ? 0.1822 0.2201 0.1813 0.0238  -0.0495 0.0196  630 HOH A O     
2385 O  O     . HOH D .   ? 0.3946 0.2507 0.9703 -0.0869 -0.4040 0.1789  631 HOH A O     
2386 O  O     . HOH D .   ? 0.3245 0.3020 0.4902 -0.0541 0.0519  -0.1174 632 HOH A O     
2387 O  O     . HOH D .   ? 1.6078 0.5454 1.5423 -0.5973 -1.0117 0.7018  633 HOH A O     
2388 O  O     . HOH D .   ? 0.7701 0.1937 0.3866 0.0399  0.0698  0.0464  634 HOH A O     
2389 O  O     . HOH D .   ? 0.2229 0.1361 0.3163 -0.0073 0.0873  -0.0113 635 HOH A O     
2390 O  O     . HOH D .   ? 0.3102 0.4009 0.6627 0.0563  -0.1869 -0.2854 636 HOH A O     
2391 O  O     . HOH D .   ? 0.1623 0.2387 0.4125 0.0528  0.0818  0.0847  637 HOH A O     
2392 O  O     . HOH D .   ? 0.2091 0.3751 0.3868 -0.1032 -0.0054 -0.1293 638 HOH A O     
2393 O  O     . HOH D .   ? 0.3558 0.3080 0.2518 -0.0825 -0.0269 -0.0795 639 HOH A O     
2394 O  O     . HOH D .   ? 0.3401 0.7596 0.3772 -0.2971 0.0319  -0.0194 640 HOH A O     
2395 O  O     . HOH D .   ? 1.2033 0.8546 0.2864 0.7102  -0.3054 -0.1583 641 HOH A O     
2396 O  O     . HOH D .   ? 0.3188 0.3728 0.8895 0.0532  -0.0215 -0.2104 642 HOH A O     
# 
