data_7Q0E
# 
_entry.id   7Q0E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.384 
_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   7Q0E         pdb_00007q0e 10.2210/pdb7q0e/pdb 
WWPDB D_1292118305 ?            ?                   
# 
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 
1 'Structure model' 1 0 2022-01-12 
2 'Structure model' 1 1 2022-01-26 
3 'Structure model' 1 2 2024-01-31 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Refinement description' 
# 
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 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' pdbx_initial_refinement_model 
# 
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.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
3 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                        7Q0E 
_pdbx_database_status.recvd_initial_deposition_date   2021-10-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              grazulis@ibt.lt 
_pdbx_contact_author.name_first         Saulius 
_pdbx_contact_author.name_last          Grazulis 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7928-5218 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Paketuryte-Latve, V.' 1 0000-0003-0919-7826 
'Smirnov, A.'          2 0000-0001-5080-9367 
'Manakova, E.'         3 0000-0002-6027-2265 
'Grazulis, S.'         4 0000-0002-7928-5218 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Int J Mol Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1422-0067 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            23 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates as High Affinity and Selective Inhibitors of Carbonic Anhydrase IX.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/ijms23010130 
_citation.pdbx_database_id_PubMed   35008553 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'       1  ? 
primary 'Capkauskaite, E.'     2  ? 
primary 'Paketuryte-Latve, V.' 3  ? 
primary 'Smirnov, A.'          4  ? 
primary 'Leitans, J.'          5  ? 
primary 'Kazaks, A.'           6  ? 
primary 'Dvinskis, E.'         7  ? 
primary 'Stancaitis, L.'       8  ? 
primary 'Mickeviciute, A.'     9  ? 
primary 'Jachno, J.'           10 ? 
primary 'Jezepcikas, L.'       11 ? 
primary 'Linkuviene, V.'       12 ? 
primary 'Sakalauskas, A.'      13 ? 
primary 'Manakova, E.'         14 ? 
primary 'Grazulis, S.'         15 ? 
primary 'Matuliene, J.'        16 ? 
primary 'Tars, K.'             17 ? 
primary 'Matulis, D.'          18 ? 
# 
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'                                       29070.785 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                   65.409    1   ?       ? ? ? 
3 non-polymer syn 'SODIUM ION'                                                 22.990    4   ?       ? ? ? 
4 non-polymer syn BICINE                                                       163.172   1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                         78.133    1   ?       ? ? ? 
6 non-polymer syn 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' 389.831   1   ?       ? ? ? 
7 water       nat water                                                        18.015    349 ?       ? ? ? 
# 
_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       
;HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG
PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG
PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
;
_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 'SODIUM ION'                                                 NA  
4 BICINE                                                       BCN 
5 'DIMETHYL SULFOXIDE'                                         DMS 
6 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' 84Z 
7 water                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   TRP n 
1 4   GLY n 
1 5   TYR n 
1 6   GLY n 
1 7   LYS n 
1 8   HIS n 
1 9   ASN n 
1 10  GLY n 
1 11  PRO n 
1 12  GLU n 
1 13  HIS n 
1 14  TRP n 
1 15  HIS n 
1 16  LYS n 
1 17  ASP n 
1 18  PHE n 
1 19  PRO n 
1 20  ILE n 
1 21  ALA n 
1 22  LYS n 
1 23  GLY n 
1 24  GLU n 
1 25  ARG n 
1 26  GLN n 
1 27  SER n 
1 28  PRO n 
1 29  VAL n 
1 30  ASP n 
1 31  ILE n 
1 32  ASP n 
1 33  THR n 
1 34  HIS n 
1 35  THR n 
1 36  ALA n 
1 37  LYS n 
1 38  TYR n 
1 39  ASP n 
1 40  PRO n 
1 41  SER n 
1 42  LEU n 
1 43  LYS n 
1 44  PRO n 
1 45  LEU n 
1 46  SER n 
1 47  VAL n 
1 48  SER n 
1 49  TYR n 
1 50  ASP n 
1 51  GLN n 
1 52  ALA n 
1 53  THR n 
1 54  SER n 
1 55  LEU n 
1 56  ARG n 
1 57  ILE n 
1 58  LEU n 
1 59  ASN n 
1 60  ASN n 
1 61  GLY n 
1 62  HIS n 
1 63  ALA n 
1 64  PHE n 
1 65  ASN n 
1 66  VAL n 
1 67  GLU n 
1 68  PHE n 
1 69  ASP n 
1 70  ASP n 
1 71  SER n 
1 72  GLN n 
1 73  ASP n 
1 74  LYS n 
1 75  ALA n 
1 76  VAL n 
1 77  LEU n 
1 78  LYS n 
1 79  GLY n 
1 80  GLY n 
1 81  PRO n 
1 82  LEU n 
1 83  ASP n 
1 84  GLY n 
1 85  THR n 
1 86  TYR n 
1 87  ARG n 
1 88  LEU n 
1 89  ILE n 
1 90  GLN n 
1 91  PHE n 
1 92  HIS n 
1 93  PHE n 
1 94  HIS n 
1 95  TRP n 
1 96  GLY n 
1 97  SER n 
1 98  LEU n 
1 99  ASP n 
1 100 GLY n 
1 101 GLN n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 ASP n 
1 109 LYS n 
1 110 LYS n 
1 111 LYS n 
1 112 TYR n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 LEU n 
1 119 VAL n 
1 120 HIS n 
1 121 TRP n 
1 122 ASN n 
1 123 THR n 
1 124 LYS n 
1 125 TYR n 
1 126 GLY n 
1 127 ASP n 
1 128 PHE n 
1 129 GLY n 
1 130 LYS n 
1 131 ALA n 
1 132 VAL n 
1 133 GLN n 
1 134 GLN n 
1 135 PRO n 
1 136 ASP n 
1 137 GLY n 
1 138 LEU n 
1 139 ALA n 
1 140 VAL n 
1 141 LEU n 
1 142 GLY n 
1 143 ILE n 
1 144 PHE n 
1 145 LEU n 
1 146 LYS n 
1 147 VAL n 
1 148 GLY n 
1 149 SER n 
1 150 ALA n 
1 151 LYS n 
1 152 PRO n 
1 153 GLY n 
1 154 LEU n 
1 155 GLN n 
1 156 LYS n 
1 157 VAL n 
1 158 VAL n 
1 159 ASP n 
1 160 VAL n 
1 161 LEU n 
1 162 ASP n 
1 163 SER n 
1 164 ILE n 
1 165 LYS n 
1 166 THR n 
1 167 LYS n 
1 168 GLY n 
1 169 LYS n 
1 170 SER n 
1 171 ALA n 
1 172 ASP n 
1 173 PHE n 
1 174 THR n 
1 175 ASN n 
1 176 PHE n 
1 177 ASP n 
1 178 PRO n 
1 179 ARG n 
1 180 GLY n 
1 181 LEU n 
1 182 LEU n 
1 183 PRO n 
1 184 GLU n 
1 185 SER n 
1 186 LEU n 
1 187 ASP n 
1 188 TYR n 
1 189 TRP n 
1 190 THR n 
1 191 TYR n 
1 192 PRO n 
1 193 GLY n 
1 194 SER n 
1 195 LEU n 
1 196 THR n 
1 197 THR n 
1 198 PRO n 
1 199 PRO n 
1 200 LEU n 
1 201 LEU n 
1 202 GLU n 
1 203 CYS n 
1 204 VAL n 
1 205 THR n 
1 206 TRP n 
1 207 ILE n 
1 208 VAL n 
1 209 LEU n 
1 210 LYS n 
1 211 GLU n 
1 212 PRO n 
1 213 ILE n 
1 214 SER n 
1 215 VAL n 
1 216 SER n 
1 217 SER n 
1 218 GLU n 
1 219 GLN n 
1 220 VAL n 
1 221 LEU n 
1 222 LYS n 
1 223 PHE n 
1 224 ARG n 
1 225 LYS n 
1 226 LEU n 
1 227 ASN n 
1 228 PHE n 
1 229 ASN n 
1 230 GLY n 
1 231 GLU n 
1 232 GLY n 
1 233 GLU n 
1 234 PRO n 
1 235 GLU n 
1 236 GLU n 
1 237 LEU n 
1 238 MET n 
1 239 VAL n 
1 240 ASP n 
1 241 ASN n 
1 242 TRP n 
1 243 ARG n 
1 244 PRO n 
1 245 ALA n 
1 246 GLN n 
1 247 PRO n 
1 248 LEU n 
1 249 LYS n 
1 250 ASN n 
1 251 ARG n 
1 252 GLN n 
1 253 ILE n 
1 254 LYS n 
1 255 ALA n 
1 256 SER n 
1 257 PHE n 
1 258 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                   258 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_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 
84Z non-polymer         . 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' ? 'C14 H12 Cl N O6 S2' 389.831 
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 
BCN non-polymer         . BICINE                                                       ? 'C6 H13 N O4'        163.172 
CYS 'L-peptide linking' y CYSTEINE                                                     ? 'C3 H7 N O2 S'       121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                         ? 'C2 H6 O S'          78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                    ? 'C5 H10 N2 O3'       146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                              ? 'C5 H9 N O4'         147.129 
GLY 'peptide linking'   y GLYCINE                                                      ? 'C2 H5 N O2'         75.067  
HIS 'L-peptide linking' y HISTIDINE                                                    ? 'C6 H10 N3 O2 1'     156.162 
HOH non-polymer         . WATER                                                        ? 'H2 O'               18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                   ? 'C6 H13 N O2'        131.173 
LEU 'L-peptide linking' y LEUCINE                                                      ? 'C6 H13 N O2'        131.173 
LYS 'L-peptide linking' y LYSINE                                                       ? 'C6 H15 N2 O2 1'     147.195 
MET 'L-peptide linking' y METHIONINE                                                   ? 'C5 H11 N O2 S'      149.211 
NA  non-polymer         . 'SODIUM ION'                                                 ? 'Na 1'               22.990  
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   HIS 1   3   3   HIS HIS A . n 
A 1 2   HIS 2   4   4   HIS HIS A . n 
A 1 3   TRP 3   5   5   TRP TRP A . n 
A 1 4   GLY 4   6   6   GLY GLY A . n 
A 1 5   TYR 5   7   7   TYR TYR A . n 
A 1 6   GLY 6   8   8   GLY GLY A . n 
A 1 7   LYS 7   9   9   LYS LYS A . n 
A 1 8   HIS 8   10  10  HIS HIS A . n 
A 1 9   ASN 9   11  11  ASN ASN A . n 
A 1 10  GLY 10  12  12  GLY GLY A . n 
A 1 11  PRO 11  13  13  PRO PRO A . n 
A 1 12  GLU 12  14  14  GLU GLU A . n 
A 1 13  HIS 13  15  15  HIS HIS A . n 
A 1 14  TRP 14  16  16  TRP TRP A . n 
A 1 15  HIS 15  17  17  HIS HIS A . n 
A 1 16  LYS 16  18  18  LYS LYS A . n 
A 1 17  ASP 17  19  19  ASP ASP A . n 
A 1 18  PHE 18  20  20  PHE PHE A . n 
A 1 19  PRO 19  21  21  PRO PRO A . n 
A 1 20  ILE 20  22  22  ILE ILE A . n 
A 1 21  ALA 21  23  23  ALA ALA A . n 
A 1 22  LYS 22  24  24  LYS LYS A . n 
A 1 23  GLY 23  25  25  GLY GLY A . n 
A 1 24  GLU 24  26  26  GLU GLU A . n 
A 1 25  ARG 25  27  27  ARG ARG A . n 
A 1 26  GLN 26  28  28  GLN GLN A . n 
A 1 27  SER 27  29  29  SER SER A . n 
A 1 28  PRO 28  30  30  PRO PRO A . n 
A 1 29  VAL 29  31  31  VAL VAL A . n 
A 1 30  ASP 30  32  32  ASP ASP A . n 
A 1 31  ILE 31  33  33  ILE ILE A . n 
A 1 32  ASP 32  34  34  ASP ASP A . n 
A 1 33  THR 33  35  35  THR THR A . n 
A 1 34  HIS 34  36  36  HIS HIS A . n 
A 1 35  THR 35  37  37  THR THR A . n 
A 1 36  ALA 36  38  38  ALA ALA A . n 
A 1 37  LYS 37  39  39  LYS LYS A . n 
A 1 38  TYR 38  40  40  TYR TYR A . n 
A 1 39  ASP 39  41  41  ASP ASP A . n 
A 1 40  PRO 40  42  42  PRO PRO A . n 
A 1 41  SER 41  43  43  SER SER A . n 
A 1 42  LEU 42  44  44  LEU LEU A . n 
A 1 43  LYS 43  45  45  LYS LYS A . n 
A 1 44  PRO 44  46  46  PRO PRO A . n 
A 1 45  LEU 45  47  47  LEU LEU A . n 
A 1 46  SER 46  48  48  SER SER A . n 
A 1 47  VAL 47  49  49  VAL VAL A . n 
A 1 48  SER 48  50  50  SER SER A . n 
A 1 49  TYR 49  51  51  TYR TYR A . n 
A 1 50  ASP 50  52  52  ASP ASP A . n 
A 1 51  GLN 51  53  53  GLN GLN A . n 
A 1 52  ALA 52  54  54  ALA ALA A . n 
A 1 53  THR 53  55  55  THR THR A . n 
A 1 54  SER 54  56  56  SER SER A . n 
A 1 55  LEU 55  57  57  LEU LEU A . n 
A 1 56  ARG 56  58  58  ARG ARG A . n 
A 1 57  ILE 57  59  59  ILE ILE A . n 
A 1 58  LEU 58  60  60  LEU LEU A . n 
A 1 59  ASN 59  61  61  ASN ASN A . n 
A 1 60  ASN 60  62  62  ASN ASN A . n 
A 1 61  GLY 61  63  63  GLY GLY A . n 
A 1 62  HIS 62  64  64  HIS HIS A . n 
A 1 63  ALA 63  65  65  ALA ALA A . n 
A 1 64  PHE 64  66  66  PHE PHE A . n 
A 1 65  ASN 65  67  67  ASN ASN A . n 
A 1 66  VAL 66  68  68  VAL VAL A . n 
A 1 67  GLU 67  69  69  GLU GLU A . n 
A 1 68  PHE 68  70  70  PHE PHE A . n 
A 1 69  ASP 69  71  71  ASP ASP A . n 
A 1 70  ASP 70  72  72  ASP ASP A . n 
A 1 71  SER 71  73  73  SER SER A . n 
A 1 72  GLN 72  74  74  GLN GLN A . n 
A 1 73  ASP 73  75  75  ASP ASP A . n 
A 1 74  LYS 74  76  76  LYS LYS A . n 
A 1 75  ALA 75  77  77  ALA ALA A . n 
A 1 76  VAL 76  78  78  VAL VAL A . n 
A 1 77  LEU 77  79  79  LEU LEU A . n 
A 1 78  LYS 78  80  80  LYS LYS A . n 
A 1 79  GLY 79  81  81  GLY GLY A . n 
A 1 80  GLY 80  82  82  GLY GLY A . n 
A 1 81  PRO 81  83  83  PRO PRO A . n 
A 1 82  LEU 82  84  84  LEU LEU A . n 
A 1 83  ASP 83  85  85  ASP ASP A . n 
A 1 84  GLY 84  86  86  GLY GLY A . n 
A 1 85  THR 85  87  87  THR THR A . n 
A 1 86  TYR 86  88  88  TYR TYR A . n 
A 1 87  ARG 87  89  89  ARG ARG A . n 
A 1 88  LEU 88  90  90  LEU LEU A . n 
A 1 89  ILE 89  91  91  ILE ILE A . n 
A 1 90  GLN 90  92  92  GLN GLN A . n 
A 1 91  PHE 91  93  93  PHE PHE A . n 
A 1 92  HIS 92  94  94  HIS HIS A . n 
A 1 93  PHE 93  95  95  PHE PHE A . n 
A 1 94  HIS 94  96  96  HIS HIS A . n 
A 1 95  TRP 95  97  97  TRP TRP A . n 
A 1 96  GLY 96  98  98  GLY GLY A . n 
A 1 97  SER 97  99  99  SER SER A . n 
A 1 98  LEU 98  100 100 LEU LEU A . n 
A 1 99  ASP 99  101 101 ASP ASP A . n 
A 1 100 GLY 100 102 102 GLY GLY A . n 
A 1 101 GLN 101 103 103 GLN GLN A . n 
A 1 102 GLY 102 104 104 GLY GLY A . n 
A 1 103 SER 103 105 105 SER SER A . n 
A 1 104 GLU 104 106 106 GLU GLU A . n 
A 1 105 HIS 105 107 107 HIS HIS A . n 
A 1 106 THR 106 108 108 THR THR A . n 
A 1 107 VAL 107 109 109 VAL VAL A . n 
A 1 108 ASP 108 110 110 ASP ASP A . n 
A 1 109 LYS 109 111 111 LYS LYS A . n 
A 1 110 LYS 110 112 112 LYS LYS A . n 
A 1 111 LYS 111 113 113 LYS LYS A . n 
A 1 112 TYR 112 114 114 TYR TYR A . n 
A 1 113 ALA 113 115 115 ALA ALA A . n 
A 1 114 ALA 114 116 116 ALA ALA A . n 
A 1 115 GLU 115 117 117 GLU GLU A . n 
A 1 116 LEU 116 118 118 LEU LEU A . n 
A 1 117 HIS 117 119 119 HIS HIS A . n 
A 1 118 LEU 118 120 120 LEU LEU A . n 
A 1 119 VAL 119 121 121 VAL VAL A . n 
A 1 120 HIS 120 122 122 HIS HIS A . n 
A 1 121 TRP 121 123 123 TRP TRP A . n 
A 1 122 ASN 122 124 124 ASN ASN A . n 
A 1 123 THR 123 125 125 THR THR A . n 
A 1 124 LYS 124 126 126 LYS LYS A . n 
A 1 125 TYR 125 127 127 TYR TYR A . n 
A 1 126 GLY 126 128 128 GLY GLY A . n 
A 1 127 ASP 127 129 129 ASP ASP A . n 
A 1 128 PHE 128 130 130 PHE PHE A . n 
A 1 129 GLY 129 131 131 GLY GLY A . n 
A 1 130 LYS 130 132 132 LYS LYS A . n 
A 1 131 ALA 131 133 133 ALA ALA A . n 
A 1 132 VAL 132 134 134 VAL VAL A . n 
A 1 133 GLN 133 135 135 GLN GLN A . n 
A 1 134 GLN 134 136 136 GLN GLN A . n 
A 1 135 PRO 135 137 137 PRO PRO A . n 
A 1 136 ASP 136 138 138 ASP ASP A . n 
A 1 137 GLY 137 139 139 GLY GLY A . n 
A 1 138 LEU 138 140 140 LEU LEU A . n 
A 1 139 ALA 139 141 141 ALA ALA A . n 
A 1 140 VAL 140 142 142 VAL VAL A . n 
A 1 141 LEU 141 143 143 LEU LEU A . n 
A 1 142 GLY 142 144 144 GLY GLY A . n 
A 1 143 ILE 143 145 145 ILE ILE A . n 
A 1 144 PHE 144 146 146 PHE PHE A . n 
A 1 145 LEU 145 147 147 LEU LEU A . n 
A 1 146 LYS 146 148 148 LYS LYS A . n 
A 1 147 VAL 147 149 149 VAL VAL A . n 
A 1 148 GLY 148 150 150 GLY GLY A . n 
A 1 149 SER 149 151 151 SER SER A . n 
A 1 150 ALA 150 152 152 ALA ALA A . n 
A 1 151 LYS 151 153 153 LYS LYS A . n 
A 1 152 PRO 152 154 154 PRO PRO A . n 
A 1 153 GLY 153 155 155 GLY GLY A . n 
A 1 154 LEU 154 156 156 LEU LEU A . n 
A 1 155 GLN 155 157 157 GLN GLN A . n 
A 1 156 LYS 156 158 158 LYS LYS A . n 
A 1 157 VAL 157 159 159 VAL VAL A . n 
A 1 158 VAL 158 160 160 VAL VAL A . n 
A 1 159 ASP 159 161 161 ASP ASP A . n 
A 1 160 VAL 160 162 162 VAL VAL A . n 
A 1 161 LEU 161 163 163 LEU LEU A . n 
A 1 162 ASP 162 164 164 ASP ASP A . n 
A 1 163 SER 163 165 165 SER SER A . n 
A 1 164 ILE 164 166 166 ILE ILE A . n 
A 1 165 LYS 165 167 167 LYS LYS A . n 
A 1 166 THR 166 168 168 THR THR A . n 
A 1 167 LYS 167 169 169 LYS LYS A . n 
A 1 168 GLY 168 170 170 GLY GLY A . n 
A 1 169 LYS 169 171 171 LYS LYS A . n 
A 1 170 SER 170 172 172 SER SER A . n 
A 1 171 ALA 171 173 173 ALA ALA A . n 
A 1 172 ASP 172 174 174 ASP ASP A . n 
A 1 173 PHE 173 175 175 PHE PHE A . n 
A 1 174 THR 174 176 176 THR THR A . n 
A 1 175 ASN 175 177 177 ASN ASN A . n 
A 1 176 PHE 176 178 178 PHE PHE A . n 
A 1 177 ASP 177 179 179 ASP ASP A . n 
A 1 178 PRO 178 180 180 PRO PRO A . n 
A 1 179 ARG 179 181 181 ARG ARG A . n 
A 1 180 GLY 180 182 182 GLY GLY A . n 
A 1 181 LEU 181 183 183 LEU LEU A . n 
A 1 182 LEU 182 184 184 LEU LEU A . n 
A 1 183 PRO 183 185 185 PRO PRO A . n 
A 1 184 GLU 184 186 186 GLU GLU A . n 
A 1 185 SER 185 187 187 SER SER A . n 
A 1 186 LEU 186 188 188 LEU LEU A . n 
A 1 187 ASP 187 189 189 ASP ASP A . n 
A 1 188 TYR 188 190 190 TYR TYR A . n 
A 1 189 TRP 189 191 191 TRP TRP A . n 
A 1 190 THR 190 192 192 THR THR A . n 
A 1 191 TYR 191 193 193 TYR TYR A . n 
A 1 192 PRO 192 194 194 PRO PRO A . n 
A 1 193 GLY 193 195 195 GLY GLY A . n 
A 1 194 SER 194 196 196 SER SER A . n 
A 1 195 LEU 195 197 197 LEU LEU A . n 
A 1 196 THR 196 198 198 THR THR A . n 
A 1 197 THR 197 199 199 THR THR A . n 
A 1 198 PRO 198 200 200 PRO PRO A . n 
A 1 199 PRO 199 201 201 PRO PRO A . n 
A 1 200 LEU 200 202 202 LEU LEU A . n 
A 1 201 LEU 201 203 203 LEU LEU A . n 
A 1 202 GLU 202 204 204 GLU GLU A . n 
A 1 203 CYS 203 205 205 CYS CYS A . n 
A 1 204 VAL 204 206 206 VAL VAL A . n 
A 1 205 THR 205 207 207 THR THR A . n 
A 1 206 TRP 206 208 208 TRP TRP A . n 
A 1 207 ILE 207 209 209 ILE ILE A . n 
A 1 208 VAL 208 210 210 VAL VAL A . n 
A 1 209 LEU 209 211 211 LEU LEU A . n 
A 1 210 LYS 210 212 212 LYS LYS A . n 
A 1 211 GLU 211 213 213 GLU GLU A . n 
A 1 212 PRO 212 214 214 PRO PRO A . n 
A 1 213 ILE 213 215 215 ILE ILE A . n 
A 1 214 SER 214 216 216 SER SER A . n 
A 1 215 VAL 215 217 217 VAL VAL A . n 
A 1 216 SER 216 218 218 SER SER A . n 
A 1 217 SER 217 219 219 SER SER A . n 
A 1 218 GLU 218 220 220 GLU GLU A . n 
A 1 219 GLN 219 221 221 GLN GLN A . n 
A 1 220 VAL 220 222 222 VAL VAL A . n 
A 1 221 LEU 221 223 223 LEU LEU A . n 
A 1 222 LYS 222 224 224 LYS LYS A . n 
A 1 223 PHE 223 225 225 PHE PHE A . n 
A 1 224 ARG 224 226 226 ARG ARG A . n 
A 1 225 LYS 225 227 227 LYS LYS A . n 
A 1 226 LEU 226 228 228 LEU LEU A . n 
A 1 227 ASN 227 229 229 ASN ASN A . n 
A 1 228 PHE 228 230 230 PHE PHE A . n 
A 1 229 ASN 229 231 231 ASN ASN A . n 
A 1 230 GLY 230 232 232 GLY GLY A . n 
A 1 231 GLU 231 233 233 GLU GLU A . n 
A 1 232 GLY 232 234 234 GLY GLY A . n 
A 1 233 GLU 233 235 235 GLU GLU A . n 
A 1 234 PRO 234 236 236 PRO PRO A . n 
A 1 235 GLU 235 237 237 GLU GLU A . n 
A 1 236 GLU 236 238 238 GLU GLU A . n 
A 1 237 LEU 237 239 239 LEU LEU A . n 
A 1 238 MET 238 240 240 MET MET A . n 
A 1 239 VAL 239 241 241 VAL VAL A . n 
A 1 240 ASP 240 242 242 ASP ASP A . n 
A 1 241 ASN 241 243 243 ASN ASN A . n 
A 1 242 TRP 242 244 244 TRP TRP A . n 
A 1 243 ARG 243 245 245 ARG ARG A . n 
A 1 244 PRO 244 246 246 PRO PRO A . n 
A 1 245 ALA 245 247 247 ALA ALA A . n 
A 1 246 GLN 246 248 248 GLN GLN A . n 
A 1 247 PRO 247 249 249 PRO PRO A . n 
A 1 248 LEU 248 250 250 LEU LEU A . n 
A 1 249 LYS 249 251 251 LYS LYS A . n 
A 1 250 ASN 250 252 252 ASN ASN A . n 
A 1 251 ARG 251 253 253 ARG ARG A . n 
A 1 252 GLN 252 254 254 GLN GLN A . n 
A 1 253 ILE 253 255 255 ILE ILE A . n 
A 1 254 LYS 254 256 256 LYS LYS A . n 
A 1 255 ALA 255 257 257 ALA ALA A . n 
A 1 256 SER 256 258 258 SER SER A . n 
A 1 257 PHE 257 259 259 PHE PHE A . n 
A 1 258 LYS 258 260 260 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 NA  1   302 1   NA  NA  A . 
D 3 NA  1   303 2   NA  NA  A . 
E 3 NA  1   304 3   NA  NA  A . 
F 3 NA  1   305 4   NA  NA  A . 
G 4 BCN 1   306 1   BCN BCN A . 
H 5 DMS 1   307 2   DMS DMS A . 
I 6 84Z 1   308 1   84Z E2A A . 
J 7 HOH 1   401 103 HOH HOH A . 
J 7 HOH 2   402 246 HOH HOH A . 
J 7 HOH 3   403 211 HOH HOH A . 
J 7 HOH 4   404 193 HOH HOH A . 
J 7 HOH 5   405 131 HOH HOH A . 
J 7 HOH 6   406 320 HOH HOH A . 
J 7 HOH 7   407 189 HOH HOH A . 
J 7 HOH 8   408 288 HOH HOH A . 
J 7 HOH 9   409 308 HOH HOH A . 
J 7 HOH 10  410 323 HOH HOH A . 
J 7 HOH 11  411 2   HOH HOH A . 
J 7 HOH 12  412 183 HOH HOH A . 
J 7 HOH 13  413 25  HOH HOH A . 
J 7 HOH 14  414 124 HOH HOH A . 
J 7 HOH 15  415 334 HOH HOH A . 
J 7 HOH 16  416 316 HOH HOH A . 
J 7 HOH 17  417 138 HOH HOH A . 
J 7 HOH 18  418 297 HOH HOH A . 
J 7 HOH 19  419 157 HOH HOH A . 
J 7 HOH 20  420 82  HOH HOH A . 
J 7 HOH 21  421 298 HOH HOH A . 
J 7 HOH 22  422 287 HOH HOH A . 
J 7 HOH 23  423 95  HOH HOH A . 
J 7 HOH 24  424 337 HOH HOH A . 
J 7 HOH 25  425 213 HOH HOH A . 
J 7 HOH 26  426 132 HOH HOH A . 
J 7 HOH 27  427 272 HOH HOH A . 
J 7 HOH 28  428 122 HOH HOH A . 
J 7 HOH 29  429 240 HOH HOH A . 
J 7 HOH 30  430 307 HOH HOH A . 
J 7 HOH 31  431 158 HOH HOH A . 
J 7 HOH 32  432 8   HOH HOH A . 
J 7 HOH 33  433 121 HOH HOH A . 
J 7 HOH 34  434 144 HOH HOH A . 
J 7 HOH 35  435 321 HOH HOH A . 
J 7 HOH 36  436 346 HOH HOH A . 
J 7 HOH 37  437 191 HOH HOH A . 
J 7 HOH 38  438 88  HOH HOH A . 
J 7 HOH 39  439 96  HOH HOH A . 
J 7 HOH 40  440 258 HOH HOH A . 
J 7 HOH 41  441 221 HOH HOH A . 
J 7 HOH 42  442 254 HOH HOH A . 
J 7 HOH 43  443 322 HOH HOH A . 
J 7 HOH 44  444 214 HOH HOH A . 
J 7 HOH 45  445 78  HOH HOH A . 
J 7 HOH 46  446 156 HOH HOH A . 
J 7 HOH 47  447 303 HOH HOH A . 
J 7 HOH 48  448 115 HOH HOH A . 
J 7 HOH 49  449 187 HOH HOH A . 
J 7 HOH 50  450 329 HOH HOH A . 
J 7 HOH 51  451 197 HOH HOH A . 
J 7 HOH 52  452 219 HOH HOH A . 
J 7 HOH 53  453 6   HOH HOH A . 
J 7 HOH 54  454 21  HOH HOH A . 
J 7 HOH 55  455 7   HOH HOH A . 
J 7 HOH 56  456 61  HOH HOH A . 
J 7 HOH 57  457 65  HOH HOH A . 
J 7 HOH 58  458 351 HOH HOH A . 
J 7 HOH 59  459 184 HOH HOH A . 
J 7 HOH 60  460 98  HOH HOH A . 
J 7 HOH 61  461 110 HOH HOH A . 
J 7 HOH 62  462 99  HOH HOH A . 
J 7 HOH 63  463 51  HOH HOH A . 
J 7 HOH 64  464 68  HOH HOH A . 
J 7 HOH 65  465 181 HOH HOH A . 
J 7 HOH 66  466 112 HOH HOH A . 
J 7 HOH 67  467 20  HOH HOH A . 
J 7 HOH 68  468 338 HOH HOH A . 
J 7 HOH 69  469 18  HOH HOH A . 
J 7 HOH 70  470 149 HOH HOH A . 
J 7 HOH 71  471 173 HOH HOH A . 
J 7 HOH 72  472 74  HOH HOH A . 
J 7 HOH 73  473 63  HOH HOH A . 
J 7 HOH 74  474 176 HOH HOH A . 
J 7 HOH 75  475 90  HOH HOH A . 
J 7 HOH 76  476 315 HOH HOH A . 
J 7 HOH 77  477 19  HOH HOH A . 
J 7 HOH 78  478 1   HOH HOH A . 
J 7 HOH 79  479 71  HOH HOH A . 
J 7 HOH 80  480 263 HOH HOH A . 
J 7 HOH 81  481 345 HOH HOH A . 
J 7 HOH 82  482 208 HOH HOH A . 
J 7 HOH 83  483 126 HOH HOH A . 
J 7 HOH 84  484 58  HOH HOH A . 
J 7 HOH 85  485 97  HOH HOH A . 
J 7 HOH 86  486 142 HOH HOH A . 
J 7 HOH 87  487 22  HOH HOH A . 
J 7 HOH 88  488 29  HOH HOH A . 
J 7 HOH 89  489 130 HOH HOH A . 
J 7 HOH 90  490 313 HOH HOH A . 
J 7 HOH 91  491 26  HOH HOH A . 
J 7 HOH 92  492 328 HOH HOH A . 
J 7 HOH 93  493 4   HOH HOH A . 
J 7 HOH 94  494 137 HOH HOH A . 
J 7 HOH 95  495 42  HOH HOH A . 
J 7 HOH 96  496 87  HOH HOH A . 
J 7 HOH 97  497 13  HOH HOH A . 
J 7 HOH 98  498 109 HOH HOH A . 
J 7 HOH 99  499 15  HOH HOH A . 
J 7 HOH 100 500 101 HOH HOH A . 
J 7 HOH 101 501 252 HOH HOH A . 
J 7 HOH 102 502 5   HOH HOH A . 
J 7 HOH 103 503 55  HOH HOH A . 
J 7 HOH 104 504 35  HOH HOH A . 
J 7 HOH 105 505 36  HOH HOH A . 
J 7 HOH 106 506 114 HOH HOH A . 
J 7 HOH 107 507 77  HOH HOH A . 
J 7 HOH 108 508 160 HOH HOH A . 
J 7 HOH 109 509 127 HOH HOH A . 
J 7 HOH 110 510 34  HOH HOH A . 
J 7 HOH 111 511 141 HOH HOH A . 
J 7 HOH 112 512 190 HOH HOH A . 
J 7 HOH 113 513 59  HOH HOH A . 
J 7 HOH 114 514 266 HOH HOH A . 
J 7 HOH 115 515 153 HOH HOH A . 
J 7 HOH 116 516 326 HOH HOH A . 
J 7 HOH 117 517 310 HOH HOH A . 
J 7 HOH 118 518 113 HOH HOH A . 
J 7 HOH 119 519 152 HOH HOH A . 
J 7 HOH 120 520 31  HOH HOH A . 
J 7 HOH 121 521 37  HOH HOH A . 
J 7 HOH 122 522 54  HOH HOH A . 
J 7 HOH 123 523 75  HOH HOH A . 
J 7 HOH 124 524 11  HOH HOH A . 
J 7 HOH 125 525 81  HOH HOH A . 
J 7 HOH 126 526 40  HOH HOH A . 
J 7 HOH 127 527 118 HOH HOH A . 
J 7 HOH 128 528 47  HOH HOH A . 
J 7 HOH 129 529 41  HOH HOH A . 
J 7 HOH 130 530 192 HOH HOH A . 
J 7 HOH 131 531 12  HOH HOH A . 
J 7 HOH 132 532 27  HOH HOH A . 
J 7 HOH 133 533 38  HOH HOH A . 
J 7 HOH 134 534 3   HOH HOH A . 
J 7 HOH 135 535 44  HOH HOH A . 
J 7 HOH 136 536 16  HOH HOH A . 
J 7 HOH 137 537 102 HOH HOH A . 
J 7 HOH 138 538 268 HOH HOH A . 
J 7 HOH 139 539 100 HOH HOH A . 
J 7 HOH 140 540 363 HOH HOH A . 
J 7 HOH 141 541 66  HOH HOH A . 
J 7 HOH 142 542 104 HOH HOH A . 
J 7 HOH 143 543 270 HOH HOH A . 
J 7 HOH 144 544 30  HOH HOH A . 
J 7 HOH 145 545 92  HOH HOH A . 
J 7 HOH 146 546 80  HOH HOH A . 
J 7 HOH 147 547 146 HOH HOH A . 
J 7 HOH 148 548 274 HOH HOH A . 
J 7 HOH 149 549 117 HOH HOH A . 
J 7 HOH 150 550 276 HOH HOH A . 
J 7 HOH 151 551 150 HOH HOH A . 
J 7 HOH 152 552 143 HOH HOH A . 
J 7 HOH 153 553 91  HOH HOH A . 
J 7 HOH 154 554 253 HOH HOH A . 
J 7 HOH 155 555 200 HOH HOH A . 
J 7 HOH 156 556 304 HOH HOH A . 
J 7 HOH 157 557 163 HOH HOH A . 
J 7 HOH 158 558 67  HOH HOH A . 
J 7 HOH 159 559 14  HOH HOH A . 
J 7 HOH 160 560 317 HOH HOH A . 
J 7 HOH 161 561 282 HOH HOH A . 
J 7 HOH 162 562 161 HOH HOH A . 
J 7 HOH 163 563 353 HOH HOH A . 
J 7 HOH 164 564 23  HOH HOH A . 
J 7 HOH 165 565 168 HOH HOH A . 
J 7 HOH 166 566 69  HOH HOH A . 
J 7 HOH 167 567 239 HOH HOH A . 
J 7 HOH 168 568 116 HOH HOH A . 
J 7 HOH 169 569 89  HOH HOH A . 
J 7 HOH 170 570 119 HOH HOH A . 
J 7 HOH 171 571 284 HOH HOH A . 
J 7 HOH 172 572 259 HOH HOH A . 
J 7 HOH 173 573 72  HOH HOH A . 
J 7 HOH 174 574 237 HOH HOH A . 
J 7 HOH 175 575 85  HOH HOH A . 
J 7 HOH 176 576 62  HOH HOH A . 
J 7 HOH 177 577 33  HOH HOH A . 
J 7 HOH 178 578 366 HOH HOH A . 
J 7 HOH 179 579 83  HOH HOH A . 
J 7 HOH 180 580 314 HOH HOH A . 
J 7 HOH 181 581 285 HOH HOH A . 
J 7 HOH 182 582 204 HOH HOH A . 
J 7 HOH 183 583 120 HOH HOH A . 
J 7 HOH 184 584 177 HOH HOH A . 
J 7 HOH 185 585 125 HOH HOH A . 
J 7 HOH 186 586 169 HOH HOH A . 
J 7 HOH 187 587 359 HOH HOH A . 
J 7 HOH 188 588 48  HOH HOH A . 
J 7 HOH 189 589 265 HOH HOH A . 
J 7 HOH 190 590 203 HOH HOH A . 
J 7 HOH 191 591 167 HOH HOH A . 
J 7 HOH 192 592 205 HOH HOH A . 
J 7 HOH 193 593 64  HOH HOH A . 
J 7 HOH 194 594 123 HOH HOH A . 
J 7 HOH 195 595 73  HOH HOH A . 
J 7 HOH 196 596 294 HOH HOH A . 
J 7 HOH 197 597 271 HOH HOH A . 
J 7 HOH 198 598 154 HOH HOH A . 
J 7 HOH 199 599 9   HOH HOH A . 
J 7 HOH 200 600 93  HOH HOH A . 
J 7 HOH 201 601 105 HOH HOH A . 
J 7 HOH 202 602 299 HOH HOH A . 
J 7 HOH 203 603 324 HOH HOH A . 
J 7 HOH 204 604 60  HOH HOH A . 
J 7 HOH 205 605 291 HOH HOH A . 
J 7 HOH 206 606 233 HOH HOH A . 
J 7 HOH 207 607 79  HOH HOH A . 
J 7 HOH 208 608 295 HOH HOH A . 
J 7 HOH 209 609 243 HOH HOH A . 
J 7 HOH 210 610 43  HOH HOH A . 
J 7 HOH 211 611 17  HOH HOH A . 
J 7 HOH 212 612 245 HOH HOH A . 
J 7 HOH 213 613 357 HOH HOH A . 
J 7 HOH 214 614 46  HOH HOH A . 
J 7 HOH 215 615 128 HOH HOH A . 
J 7 HOH 216 616 344 HOH HOH A . 
J 7 HOH 217 617 94  HOH HOH A . 
J 7 HOH 218 618 28  HOH HOH A . 
J 7 HOH 219 619 262 HOH HOH A . 
J 7 HOH 220 620 53  HOH HOH A . 
J 7 HOH 221 621 10  HOH HOH A . 
J 7 HOH 222 622 216 HOH HOH A . 
J 7 HOH 223 623 32  HOH HOH A . 
J 7 HOH 224 624 49  HOH HOH A . 
J 7 HOH 225 625 174 HOH HOH A . 
J 7 HOH 226 626 56  HOH HOH A . 
J 7 HOH 227 627 261 HOH HOH A . 
J 7 HOH 228 628 151 HOH HOH A . 
J 7 HOH 229 629 296 HOH HOH A . 
J 7 HOH 230 630 52  HOH HOH A . 
J 7 HOH 231 631 280 HOH HOH A . 
J 7 HOH 232 632 108 HOH HOH A . 
J 7 HOH 233 633 293 HOH HOH A . 
J 7 HOH 234 634 273 HOH HOH A . 
J 7 HOH 235 635 76  HOH HOH A . 
J 7 HOH 236 636 355 HOH HOH A . 
J 7 HOH 237 637 165 HOH HOH A . 
J 7 HOH 238 638 290 HOH HOH A . 
J 7 HOH 239 639 300 HOH HOH A . 
J 7 HOH 240 640 133 HOH HOH A . 
J 7 HOH 241 641 305 HOH HOH A . 
J 7 HOH 242 642 289 HOH HOH A . 
J 7 HOH 243 643 215 HOH HOH A . 
J 7 HOH 244 644 279 HOH HOH A . 
J 7 HOH 245 645 242 HOH HOH A . 
J 7 HOH 246 646 195 HOH HOH A . 
J 7 HOH 247 647 147 HOH HOH A . 
J 7 HOH 248 648 327 HOH HOH A . 
J 7 HOH 249 649 361 HOH HOH A . 
J 7 HOH 250 650 212 HOH HOH A . 
J 7 HOH 251 651 336 HOH HOH A . 
J 7 HOH 252 652 330 HOH HOH A . 
J 7 HOH 253 653 107 HOH HOH A . 
J 7 HOH 254 654 218 HOH HOH A . 
J 7 HOH 255 655 267 HOH HOH A . 
J 7 HOH 256 656 24  HOH HOH A . 
J 7 HOH 257 657 309 HOH HOH A . 
J 7 HOH 258 658 234 HOH HOH A . 
J 7 HOH 259 659 365 HOH HOH A . 
J 7 HOH 260 660 251 HOH HOH A . 
J 7 HOH 261 661 206 HOH HOH A . 
J 7 HOH 262 662 238 HOH HOH A . 
J 7 HOH 263 663 318 HOH HOH A . 
J 7 HOH 264 664 166 HOH HOH A . 
J 7 HOH 265 665 364 HOH HOH A . 
J 7 HOH 266 666 301 HOH HOH A . 
J 7 HOH 267 667 210 HOH HOH A . 
J 7 HOH 268 668 182 HOH HOH A . 
J 7 HOH 269 669 136 HOH HOH A . 
J 7 HOH 270 670 159 HOH HOH A . 
J 7 HOH 271 671 70  HOH HOH A . 
J 7 HOH 272 672 312 HOH HOH A . 
J 7 HOH 273 673 226 HOH HOH A . 
J 7 HOH 274 674 217 HOH HOH A . 
J 7 HOH 275 675 339 HOH HOH A . 
J 7 HOH 276 676 179 HOH HOH A . 
J 7 HOH 277 677 319 HOH HOH A . 
J 7 HOH 278 678 311 HOH HOH A . 
J 7 HOH 279 679 277 HOH HOH A . 
J 7 HOH 280 680 106 HOH HOH A . 
J 7 HOH 281 681 278 HOH HOH A . 
J 7 HOH 282 682 247 HOH HOH A . 
J 7 HOH 283 683 269 HOH HOH A . 
J 7 HOH 284 684 256 HOH HOH A . 
J 7 HOH 285 685 228 HOH HOH A . 
J 7 HOH 286 686 264 HOH HOH A . 
J 7 HOH 287 687 209 HOH HOH A . 
J 7 HOH 288 688 57  HOH HOH A . 
J 7 HOH 289 689 135 HOH HOH A . 
J 7 HOH 290 690 281 HOH HOH A . 
J 7 HOH 291 691 222 HOH HOH A . 
J 7 HOH 292 692 231 HOH HOH A . 
J 7 HOH 293 693 341 HOH HOH A . 
J 7 HOH 294 694 196 HOH HOH A . 
J 7 HOH 295 695 129 HOH HOH A . 
J 7 HOH 296 696 352 HOH HOH A . 
J 7 HOH 297 697 286 HOH HOH A . 
J 7 HOH 298 698 241 HOH HOH A . 
J 7 HOH 299 699 139 HOH HOH A . 
J 7 HOH 300 700 235 HOH HOH A . 
J 7 HOH 301 701 335 HOH HOH A . 
J 7 HOH 302 702 340 HOH HOH A . 
J 7 HOH 303 703 249 HOH HOH A . 
J 7 HOH 304 704 227 HOH HOH A . 
J 7 HOH 305 705 140 HOH HOH A . 
J 7 HOH 306 706 171 HOH HOH A . 
J 7 HOH 307 707 260 HOH HOH A . 
J 7 HOH 308 708 84  HOH HOH A . 
J 7 HOH 309 709 224 HOH HOH A . 
J 7 HOH 310 710 175 HOH HOH A . 
J 7 HOH 311 711 257 HOH HOH A . 
J 7 HOH 312 712 283 HOH HOH A . 
J 7 HOH 313 713 194 HOH HOH A . 
J 7 HOH 314 714 250 HOH HOH A . 
J 7 HOH 315 715 223 HOH HOH A . 
J 7 HOH 316 716 333 HOH HOH A . 
J 7 HOH 317 717 155 HOH HOH A . 
J 7 HOH 318 718 162 HOH HOH A . 
J 7 HOH 319 719 86  HOH HOH A . 
J 7 HOH 320 720 172 HOH HOH A . 
J 7 HOH 321 721 164 HOH HOH A . 
J 7 HOH 322 722 362 HOH HOH A . 
J 7 HOH 323 723 188 HOH HOH A . 
J 7 HOH 324 724 148 HOH HOH A . 
J 7 HOH 325 725 39  HOH HOH A . 
J 7 HOH 326 726 306 HOH HOH A . 
J 7 HOH 327 727 220 HOH HOH A . 
J 7 HOH 328 728 111 HOH HOH A . 
J 7 HOH 329 729 230 HOH HOH A . 
J 7 HOH 330 730 199 HOH HOH A . 
J 7 HOH 331 731 332 HOH HOH A . 
J 7 HOH 332 732 331 HOH HOH A . 
J 7 HOH 333 733 178 HOH HOH A . 
J 7 HOH 334 734 325 HOH HOH A . 
J 7 HOH 335 735 275 HOH HOH A . 
J 7 HOH 336 736 180 HOH HOH A . 
J 7 HOH 337 737 232 HOH HOH A . 
J 7 HOH 338 738 186 HOH HOH A . 
J 7 HOH 339 739 225 HOH HOH A . 
J 7 HOH 340 740 185 HOH HOH A . 
J 7 HOH 341 741 50  HOH HOH A . 
J 7 HOH 342 742 354 HOH HOH A . 
J 7 HOH 343 743 170 HOH HOH A . 
J 7 HOH 344 744 347 HOH HOH A . 
J 7 HOH 345 745 343 HOH HOH A . 
J 7 HOH 346 746 134 HOH HOH A . 
J 7 HOH 347 747 358 HOH HOH A . 
J 7 HOH 348 748 360 HOH HOH A . 
J 7 HOH 349 749 202 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CG ? A LYS 7   CG 
2  1 Y 1 A LYS 9   ? CD ? A LYS 7   CD 
3  1 Y 1 A LYS 9   ? CE ? A LYS 7   CE 
4  1 Y 1 A LYS 9   ? NZ ? A LYS 7   NZ 
5  1 Y 1 A LYS 45  ? CE ? A LYS 43  CE 
6  1 Y 1 A LYS 45  ? NZ ? A LYS 43  NZ 
7  1 Y 1 A LYS 80  ? NZ ? A LYS 78  NZ 
8  1 Y 1 A LYS 158 ? CD ? A LYS 156 CD 
9  1 Y 1 A LYS 158 ? CE ? A LYS 156 CE 
10 1 Y 1 A LYS 158 ? NZ ? A LYS 156 NZ 
11 1 Y 1 A LYS 212 ? NZ ? A LYS 210 NZ 
12 1 Y 1 A LYS 256 ? CE ? A LYS 254 CE 
13 1 Y 1 A LYS 256 ? NZ ? A LYS 254 NZ 
14 1 Y 1 A LYS 260 ? CD ? A LYS 258 CD 
15 1 Y 1 A LYS 260 ? CE ? A LYS 258 CE 
16 1 Y 1 A LYS 260 ? NZ ? A LYS 258 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0189 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.260 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7Q0E 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.161 
_cell.length_a_esd                 ? 
_cell.length_b                     41.347 
_cell.length_b_esd                 ? 
_cell.length_c                     71.990 
_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             ? 
# 
_symmetry.entry_id                         7Q0E 
_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                   7Q0E 
_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            2.09 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         41.20 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M sodium bicine (pH 9.0), 0.2 M ammonium sulfate and 2M sodium malonate (pH 7.0)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-07-19 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9797 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9797 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7Q0E 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.300 
_reflns.d_resolution_low                               69.770 
_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                                     57251 
_reflns.number_obs                                     57251 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.800 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.900 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.086 
_reflns.pdbx_netI_over_av_sigmaI                       5.700 
_reflns.pdbx_netI_over_sigmaI                          13.300 
_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                                0.100 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       394810 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_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 
1.300 1.370  ? 1.700  56892 ? ? ? 8135 94.600 ? ? ? ? 0.354 ? ? ? ? ? ? ? ? 7.000 0.354 ? ? 5.500  0.409 0.153 ? 1  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.370 1.450  ? 2.000  51623 ? ? ? 7726 95.100 ? ? ? ? 0.282 ? ? ? ? ? ? ? ? 6.700 0.282 ? ? 6.600  0.328 0.125 ? 2  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.450 1.550  ? 2.500  52172 ? ? ? 7358 96.200 ? ? ? ? 0.212 ? ? ? ? ? ? ? ? 7.100 0.212 ? ? 8.600  0.244 0.091 ? 3  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.550 1.680  ? 3.300  45894 ? ? ? 6860 96.400 ? ? ? ? 0.160 ? ? ? ? ? ? ? ? 6.700 0.160 ? ? 10.200 0.188 0.072 ? 4  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.680 1.840  ? 4.500  45111 ? ? ? 6404 97.300 ? ? ? ? 0.121 ? ? ? ? ? ? ? ? 7.000 0.121 ? ? 13.100 0.142 0.053 ? 5  1 ? ? ? ? ? ? 
? ? ? ? ? 
1.840 2.060  ? 6.400  40277 ? ? ? 5823 98.000 ? ? ? ? 0.092 ? ? ? ? ? ? ? ? 6.900 0.092 ? ? 16.600 0.108 0.041 ? 6  1 ? ? ? ? ? ? 
? ? ? ? ? 
2.060 2.370  ? 8.500  35628 ? ? ? 5138 98.000 ? ? ? ? 0.073 ? ? ? ? ? ? ? ? 6.900 0.073 ? ? 20.200 0.086 0.033 ? 7  1 ? ? ? ? ? ? 
? ? ? ? ? 
2.370 2.910  ? 9.500  30540 ? ? ? 4402 98.800 ? ? ? ? 0.064 ? ? ? ? ? ? ? ? 6.900 0.064 ? ? 22.700 0.075 0.028 ? 8  1 ? ? ? ? ? ? 
? ? ? ? ? 
2.910 4.110  ? 11.600 23757 ? ? ? 3456 99.200 ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 6.900 0.050 ? ? 27.600 0.058 0.022 ? 9  1 ? ? ? ? ? ? 
? ? ? ? ? 
4.110 69.770 ? 11.300 12916 ? ? ? 1949 99.000 ? ? ? ? 0.047 ? ? ? ? ? ? ? ? 6.600 0.047 ? ? 27.700 0.054 0.021 ? 10 1 ? ? ? ? ? ? 
? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.0800 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.1000 
_refine.aniso_B[2][2]                            0.0700 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            0.0500 
_refine.B_iso_max                                81.110 
_refine.B_iso_mean                               12.8550 
_refine.B_iso_min                                2.330 
_refine.correlation_coeff_Fo_to_Fc               0.9740 
_refine.correlation_coeff_Fo_to_Fc_free          0.9610 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_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                                 7Q0E 
_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                            1.3000 
_refine.ls_d_res_low                             40.8600 
_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                     51596 
_refine.ls_number_reflns_R_free                  5612 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.3800 
_refine.ls_percent_reflns_R_free                 9.8000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1303 
_refine.ls_R_factor_R_free                       0.1691 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1261 
_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                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4HT0 
_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                       0.0520 
_refine.pdbx_overall_ESU_R_Free                  0.0520 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.3000 
_refine_hist.d_res_low                        40.8600 
_refine_hist.number_atoms_solvent             351 
_refine_hist.number_atoms_total               2449 
_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       258 
_refine_hist.pdbx_B_iso_mean_ligand           16.74 
_refine_hist.pdbx_B_iso_mean_solvent          25.07 
_refine_hist.pdbx_number_atoms_protein        2043 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         55 
_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' ? 0.025  0.019  2328 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.304  1.965  3192 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.748  5.000  293  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 32.468 24.811 106  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.185 15.000 362  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.630 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.167  0.200  327  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.018  0.021  1858 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 6.980  3.000  2328 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 24.771 5.000  190  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 13.775 5.000  2412 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3000 
_refine_ls_shell.d_res_low                        1.3340 
_refine_ls_shell.number_reflns_all                4115 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             382 
_refine_ls_shell.number_reflns_R_work             3733 
_refine_ls_shell.percent_reflns_obs               93.9500 
_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                  0.2040 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1450 
_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                    ? 
# 
_struct.entry_id                     7Q0E 
_struct.title                        
'Human Carbonic Anhydrase II in complex with Methyl 2-(benzenesulfonyl)-4-chloro-5-sulfamoylbenzoate' 
_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        7Q0E 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 7 ? 
# 
_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   
;HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG
PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           3 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7Q0E 
_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                 258 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  3 
_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       3 
_struct_ref_seq.pdbx_auth_seq_align_end       260 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 10  ? ASP A 17  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 18  ? GLY A 23  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 124 ? GLY A 126 ? LYS A 126 GLY A 128 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 127 ? VAL A 132 ? ASP A 129 VAL A 134 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 151 ? GLY A 153 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 154 ? LEU A 161 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 162 ? LYS A 165 ? ASP A 164 LYS A 167 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 177 ? LEU A 182 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P9 AA9 SER A 216 ? ARG A 224 ? SER A 218 ARG A 226 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 34  O   A ? ? 1_555 E NA  . NA  ? ? A HIS 36  A NA  304 1_555 ? ? ? ? ? ? ? 2.478 ? ? 
metalc2  metalc ? ? A HIS 34  O   B ? ? 1_555 E NA  . NA  ? ? A HIS 36  A NA  304 1_555 ? ? ? ? ? ? ? 2.510 ? ? 
metalc3  metalc ? ? A ALA 36  O   ? ? ? 1_555 E NA  . NA  ? ? A ALA 38  A NA  304 1_555 ? ? ? ? ? ? ? 2.502 ? ? 
metalc4  metalc ? ? A SER 71  OG  ? ? ? 1_555 C NA  . NA  ? ? A SER 73  A NA  302 1_555 ? ? ? ? ? ? ? 2.218 ? ? 
metalc5  metalc ? ? A HIS 92  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.964 ? ? 
metalc6  metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.982 ? ? 
metalc7  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc8  metalc ? ? A SER 217 OG  A ? ? 1_555 C NA  . NA  ? ? A SER 219 A NA  302 1_545 ? ? ? ? ? ? ? 2.511 ? ? 
metalc9  metalc ? ? A GLY 232 O   ? ? ? 1_555 D NA  . NA  ? ? A GLY 234 A NA  303 2_645 ? ? ? ? ? ? ? 2.956 ? ? 
metalc10 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 I 84Z . S7  ? ? A ZN  301 A 84Z 308 1_555 ? ? ? ? ? ? ? 2.998 ? ? 
metalc11 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 I 84Z . N10 ? ? A ZN  301 A 84Z 308 1_555 ? ? ? ? ? ? ? 1.962 ? ? 
metalc12 metalc ? ? C NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  302 A HOH 491 1_565 ? ? ? ? ? ? ? 2.623 ? ? 
metalc13 metalc ? ? C NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  302 A HOH 562 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc14 metalc ? ? C NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  302 A HOH 606 1_555 ? ? ? ? ? ? ? 1.976 ? ? 
metalc15 metalc ? ? D NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  303 A HOH 447 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc16 metalc ? ? D NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  303 A HOH 622 1_555 ? ? ? ? ? ? ? 2.606 ? ? 
metalc17 metalc ? ? D NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  303 A HOH 624 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc18 metalc ? ? D NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  303 A HOH 670 2_655 ? ? ? ? ? ? ? 2.243 ? ? 
metalc19 metalc ? ? D NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  303 A HOH 737 1_555 ? ? ? ? ? ? ? 2.235 ? ? 
metalc20 metalc ? ? E NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  304 A HOH 449 1_555 ? ? ? ? ? ? ? 2.500 ? ? 
metalc21 metalc ? ? E NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  304 A HOH 458 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
metalc22 metalc ? ? F NA  .   NA  ? ? ? 1_555 J HOH . O   ? ? A NA  305 A HOH 696 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
# 
_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  O   A A HIS 34  ? A HIS 36  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   B A HIS 34  ? A HIS 36  ? 1_555 0.6   ? 
2  O   A A HIS 34  ? A HIS 36  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? A ALA 36  ? A ALA 38  ? 1_555 112.5 ? 
3  O   B A HIS 34  ? A HIS 36  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? A ALA 36  ? A ALA 38  ? 1_555 112.0 ? 
4  O   A A HIS 34  ? A HIS 36  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? J HOH .   ? A HOH 449 ? 1_555 64.7  ? 
5  O   B A HIS 34  ? A HIS 36  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? J HOH .   ? A HOH 449 ? 1_555 65.0  ? 
6  O   ? A ALA 36  ? A ALA 38  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? J HOH .   ? A HOH 449 ? 1_555 161.0 ? 
7  O   A A HIS 34  ? A HIS 36  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? J HOH .   ? A HOH 458 ? 1_555 107.8 ? 
8  O   B A HIS 34  ? A HIS 36  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? J HOH .   ? A HOH 458 ? 1_555 108.4 ? 
9  O   ? A ALA 36  ? A ALA 38  ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? J HOH .   ? A HOH 458 ? 1_555 115.7 ? 
10 O   ? J HOH .   ? A HOH 449 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? J HOH .   ? A HOH 458 ? 1_555 82.2  ? 
11 OG  ? A SER 71  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_555 OG  A A SER 217 ? A SER 219 ? 1_555 36.2  ? 
12 OG  ? A SER 71  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 491 ? 1_565 103.2 ? 
13 OG  A A SER 217 ? A SER 219 ? 1_555 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 491 ? 1_565 130.9 ? 
14 OG  ? A SER 71  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 562 ? 1_555 164.6 ? 
15 OG  A A SER 217 ? A SER 219 ? 1_555 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 562 ? 1_555 130.6 ? 
16 O   ? J HOH .   ? A HOH 491 ? 1_565 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 562 ? 1_555 82.2  ? 
17 OG  ? A SER 71  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 606 ? 1_555 88.6  ? 
18 OG  A A SER 217 ? A SER 219 ? 1_555 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 606 ? 1_555 68.8  ? 
19 O   ? J HOH .   ? A HOH 491 ? 1_565 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 606 ? 1_555 157.4 ? 
20 O   ? J HOH .   ? A HOH 562 ? 1_555 NA ? C NA . ? A NA 302 ? 1_555 O   ? J HOH .   ? A HOH 606 ? 1_555 91.4  ? 
21 NE2 ? A HIS 92  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 94  ? A HIS 96  ? 1_555 105.3 ? 
22 NE2 ? A HIS 92  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 119 ? 1_555 112.8 ? 
23 NE2 ? A HIS 94  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 119 ? 1_555 98.1  ? 
24 NE2 ? A HIS 92  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  ? I 84Z .   ? A 84Z 308 ? 1_555 98.8  ? 
25 NE2 ? A HIS 94  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  ? I 84Z .   ? A 84Z 308 ? 1_555 142.1 ? 
26 ND1 ? A HIS 117 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  ? I 84Z .   ? A 84Z 308 ? 1_555 99.0  ? 
27 NE2 ? A HIS 92  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? I 84Z .   ? A 84Z 308 ? 1_555 111.0 ? 
28 NE2 ? A HIS 94  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? I 84Z .   ? A 84Z 308 ? 1_555 113.3 ? 
29 ND1 ? A HIS 117 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? I 84Z .   ? A 84Z 308 ? 1_555 115.4 ? 
30 S7  ? I 84Z .   ? A 84Z 308 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? I 84Z .   ? A 84Z 308 ? 1_555 29.2  ? 
31 O   ? A GLY 232 ? A GLY 234 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 447 ? 1_555 45.7  ? 
32 O   ? A GLY 232 ? A GLY 234 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 622 ? 1_555 46.5  ? 
33 O   ? J HOH .   ? A HOH 447 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 622 ? 1_555 7.8   ? 
34 O   ? A GLY 232 ? A GLY 234 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 624 ? 1_555 45.2  ? 
35 O   ? J HOH .   ? A HOH 447 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 624 ? 1_555 2.1   ? 
36 O   ? J HOH .   ? A HOH 622 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 624 ? 1_555 5.8   ? 
37 O   ? A GLY 232 ? A GLY 234 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 670 ? 2_655 49.4  ? 
38 O   ? J HOH .   ? A HOH 447 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 670 ? 2_655 6.8   ? 
39 O   ? J HOH .   ? A HOH 622 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 670 ? 2_655 3.8   ? 
40 O   ? J HOH .   ? A HOH 624 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 670 ? 2_655 5.5   ? 
41 O   ? A GLY 232 ? A GLY 234 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 737 ? 1_555 44.5  ? 
42 O   ? J HOH .   ? A HOH 447 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 737 ? 1_555 4.4   ? 
43 O   ? J HOH .   ? A HOH 622 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 737 ? 1_555 3.9   ? 
44 O   ? J HOH .   ? A HOH 624 ? 1_555 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 737 ? 1_555 2.3   ? 
45 O   ? J HOH .   ? A HOH 670 ? 2_655 NA ? D NA . ? A NA 303 ? 2_645 O   ? J HOH .   ? A HOH 737 ? 1_555 5.1   ? 
# 
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 27  A . ? SER 29  A PRO 28  A ? PRO 30  A 1 -0.53 
2 PRO 198 A . ? PRO 200 A PRO 199 A ? PRO 201 A 1 10.83 
# 
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 30  ? ILE A 31  ? ASP A 32  ILE A 33  
AA1 2  THR A 106 ? VAL A 107 ? THR A 108 VAL A 109 
AA2 1  LYS A 37  ? TYR A 38  ? LYS A 39  TYR A 40  
AA2 2  LYS A 254 ? ALA A 255 ? LYS A 256 ALA A 257 
AA2 3  TYR A 188 ? GLY A 193 ? TYR A 190 GLY A 195 
AA2 4  VAL A 204 ? LEU A 209 ? VAL A 206 LEU A 211 
AA2 5  LEU A 138 ? VAL A 147 ? LEU A 140 VAL A 149 
AA2 6  ALA A 114 ? ASN A 122 ? ALA A 116 ASN A 124 
AA2 7  TYR A 86  ? TRP A 95  ? TYR A 88  TRP A 97  
AA2 8  PHE A 64  ? PHE A 68  ? PHE A 66  PHE A 70  
AA2 9  SER A 54  ? ASN A 59  ? SER A 56  ASN A 61  
AA2 10 SER A 170 ? ASP A 172 ? SER A 172 ASP A 174 
AA3 1  LEU A 45  ? SER A 48  ? LEU A 47  SER A 50  
AA3 2  VAL A 76  ? GLY A 79  ? VAL A 78  GLY A 81  
AA3 3  TYR A 86  ? TRP A 95  ? TYR A 88  TRP A 97  
AA3 4  ALA A 114 ? ASN A 122 ? ALA A 116 ASN A 124 
AA3 5  LEU A 138 ? VAL A 147 ? LEU A 140 VAL A 149 
AA3 6  ILE A 213 ? VAL A 215 ? ILE A 215 VAL A 217 
# 
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 31  ? N ILE A 33  O THR A 106 ? O THR A 108 
AA2 1 2  N LYS A 37  ? N LYS A 39  O ALA A 255 ? O ALA A 257 
AA2 2 3  O LYS A 254 ? O LYS A 256 N THR A 190 ? N THR A 192 
AA2 3 4  N GLY A 193 ? N GLY A 195 O VAL A 204 ? O VAL A 206 
AA2 4 5  O ILE A 207 ? O ILE A 209 N GLY A 142 ? N GLY A 144 
AA2 5 6  O ILE A 143 ? O ILE A 145 N LEU A 116 ? N LEU A 118 
AA2 6 7  O HIS A 117 ? O HIS A 119 N HIS A 92  ? N HIS A 94  
AA2 7 8  O PHE A 91  ? O PHE A 93  N VAL A 66  ? N VAL A 68  
AA2 8 9  O GLU A 67  ? O GLU A 69  N LEU A 55  ? N LEU A 57  
AA2 9 10 N ILE A 57  ? N ILE A 59  O ALA A 171 ? O ALA A 173 
AA3 1 2  N SER A 46  ? N SER A 48  O LYS A 78  ? O LYS A 80  
AA3 2 3  N LEU A 77  ? N LEU A 79  O TYR A 86  ? O TYR A 88  
AA3 3 4  N HIS A 92  ? N HIS A 94  O HIS A 117 ? O HIS A 119 
AA3 4 5  N LEU A 116 ? N LEU A 118 O ILE A 143 ? O ILE A 145 
AA3 5 6  N PHE A 144 ? N PHE A 146 O ILE A 213 ? O ILE A 215 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 450 ? ? O A HOH 578 ? ? 1.67 
2 1 NE2 A GLN 136 ? B O A HOH 401 ? ? 1.67 
3 1 OE2 A GLU 213 ? A O A HOH 402 ? ? 1.95 
4 1 CD2 A HIS 36  ? B O A HOH 419 ? ? 2.10 
5 1 O   A HOH 402 ? ? O A HOH 429 ? ? 2.16 
6 1 O   A HOH 429 ? ? O A HOH 560 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              129 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              129 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              129 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                125.91 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            7.61 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -150.49 21.77   
2 1 ARG A 27  ? ? -142.76 57.50   
3 1 ALA A 77  ? ? 47.02   76.62   
4 1 GLU A 106 ? ? -93.79  -60.47  
5 1 LYS A 111 ? ? 74.18   -3.18   
6 1 PHE A 175 ? ? -152.06 77.27   
7 1 ASN A 243 ? ? -94.05  48.05   
8 1 LYS A 251 ? ? 54.03   -139.37 
# 
_pdbx_entry_details.entry_id                 7Q0E 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
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 
84Z O18  O  N N 1   
84Z S16  S  N N 2   
84Z O17  O  N N 3   
84Z C19  C  Y N 4   
84Z C24  C  Y N 5   
84Z C23  C  Y N 6   
84Z C22  C  Y N 7   
84Z C21  C  Y N 8   
84Z C20  C  Y N 9   
84Z C3   C  Y N 10  
84Z C2   C  Y N 11  
84Z C4   C  Y N 12  
84Z C12  C  N N 13  
84Z O14  O  N N 14  
84Z C15  C  N N 15  
84Z O13  O  N N 16  
84Z C5   C  Y N 17  
84Z C6   C  Y N 18  
84Z C1   C  Y N 19  
84Z CL1  CL N N 20  
84Z S7   S  N N 21  
84Z O8   O  N N 22  
84Z O9   O  N N 23  
84Z N10  N  N N 24  
84Z H1   H  N N 25  
84Z H2   H  N N 26  
84Z H3   H  N N 27  
84Z H4   H  N N 28  
84Z H5   H  N N 29  
84Z H6   H  N N 30  
84Z H7   H  N N 31  
84Z H8   H  N N 32  
84Z H9   H  N N 33  
84Z H10  H  N N 34  
84Z H11  H  N N 35  
84Z H12  H  N N 36  
ALA N    N  N N 37  
ALA CA   C  N S 38  
ALA C    C  N N 39  
ALA O    O  N N 40  
ALA CB   C  N N 41  
ALA OXT  O  N N 42  
ALA H    H  N N 43  
ALA H2   H  N N 44  
ALA HA   H  N N 45  
ALA HB1  H  N N 46  
ALA HB2  H  N N 47  
ALA HB3  H  N N 48  
ALA HXT  H  N N 49  
ARG N    N  N N 50  
ARG CA   C  N S 51  
ARG C    C  N N 52  
ARG O    O  N N 53  
ARG CB   C  N N 54  
ARG CG   C  N N 55  
ARG CD   C  N N 56  
ARG NE   N  N N 57  
ARG CZ   C  N N 58  
ARG NH1  N  N N 59  
ARG NH2  N  N N 60  
ARG OXT  O  N N 61  
ARG H    H  N N 62  
ARG H2   H  N N 63  
ARG HA   H  N N 64  
ARG HB2  H  N N 65  
ARG HB3  H  N N 66  
ARG HG2  H  N N 67  
ARG HG3  H  N N 68  
ARG HD2  H  N N 69  
ARG HD3  H  N N 70  
ARG HE   H  N N 71  
ARG HH11 H  N N 72  
ARG HH12 H  N N 73  
ARG HH21 H  N N 74  
ARG HH22 H  N N 75  
ARG HXT  H  N N 76  
ASN N    N  N N 77  
ASN CA   C  N S 78  
ASN C    C  N N 79  
ASN O    O  N N 80  
ASN CB   C  N N 81  
ASN CG   C  N N 82  
ASN OD1  O  N N 83  
ASN ND2  N  N N 84  
ASN OXT  O  N N 85  
ASN H    H  N N 86  
ASN H2   H  N N 87  
ASN HA   H  N N 88  
ASN HB2  H  N N 89  
ASN HB3  H  N N 90  
ASN HD21 H  N N 91  
ASN HD22 H  N N 92  
ASN HXT  H  N N 93  
ASP N    N  N N 94  
ASP CA   C  N S 95  
ASP C    C  N N 96  
ASP O    O  N N 97  
ASP CB   C  N N 98  
ASP CG   C  N N 99  
ASP OD1  O  N N 100 
ASP OD2  O  N N 101 
ASP OXT  O  N N 102 
ASP H    H  N N 103 
ASP H2   H  N N 104 
ASP HA   H  N N 105 
ASP HB2  H  N N 106 
ASP HB3  H  N N 107 
ASP HD2  H  N N 108 
ASP HXT  H  N N 109 
BCN N1   N  N N 110 
BCN C1   C  N N 111 
BCN C2   C  N N 112 
BCN O21  O  N N 113 
BCN O22  O  N N 114 
BCN C3   C  N N 115 
BCN C4   C  N N 116 
BCN O4   O  N N 117 
BCN C5   C  N N 118 
BCN C6   C  N N 119 
BCN O6   O  N N 120 
BCN H11  H  N N 121 
BCN H12  H  N N 122 
BCN HO2  H  N N 123 
BCN H31  H  N N 124 
BCN H32  H  N N 125 
BCN H41  H  N N 126 
BCN H42  H  N N 127 
BCN HO4  H  N N 128 
BCN H51  H  N N 129 
BCN H52  H  N N 130 
BCN H61  H  N N 131 
BCN H62  H  N N 132 
BCN HO6  H  N N 133 
CYS N    N  N N 134 
CYS CA   C  N R 135 
CYS C    C  N N 136 
CYS O    O  N N 137 
CYS CB   C  N N 138 
CYS SG   S  N N 139 
CYS OXT  O  N N 140 
CYS H    H  N N 141 
CYS H2   H  N N 142 
CYS HA   H  N N 143 
CYS HB2  H  N N 144 
CYS HB3  H  N N 145 
CYS HG   H  N N 146 
CYS HXT  H  N N 147 
DMS S    S  N N 148 
DMS O    O  N N 149 
DMS C1   C  N N 150 
DMS C2   C  N N 151 
DMS H11  H  N N 152 
DMS H12  H  N N 153 
DMS H13  H  N N 154 
DMS H21  H  N N 155 
DMS H22  H  N N 156 
DMS H23  H  N N 157 
GLN N    N  N N 158 
GLN CA   C  N S 159 
GLN C    C  N N 160 
GLN O    O  N N 161 
GLN CB   C  N N 162 
GLN CG   C  N N 163 
GLN CD   C  N N 164 
GLN OE1  O  N N 165 
GLN NE2  N  N N 166 
GLN OXT  O  N N 167 
GLN H    H  N N 168 
GLN H2   H  N N 169 
GLN HA   H  N N 170 
GLN HB2  H  N N 171 
GLN HB3  H  N N 172 
GLN HG2  H  N N 173 
GLN HG3  H  N N 174 
GLN HE21 H  N N 175 
GLN HE22 H  N N 176 
GLN HXT  H  N N 177 
GLU N    N  N N 178 
GLU CA   C  N S 179 
GLU C    C  N N 180 
GLU O    O  N N 181 
GLU CB   C  N N 182 
GLU CG   C  N N 183 
GLU CD   C  N N 184 
GLU OE1  O  N N 185 
GLU OE2  O  N N 186 
GLU OXT  O  N N 187 
GLU H    H  N N 188 
GLU H2   H  N N 189 
GLU HA   H  N N 190 
GLU HB2  H  N N 191 
GLU HB3  H  N N 192 
GLU HG2  H  N N 193 
GLU HG3  H  N N 194 
GLU HE2  H  N N 195 
GLU HXT  H  N N 196 
GLY N    N  N N 197 
GLY CA   C  N N 198 
GLY C    C  N N 199 
GLY O    O  N N 200 
GLY OXT  O  N N 201 
GLY H    H  N N 202 
GLY H2   H  N N 203 
GLY HA2  H  N N 204 
GLY HA3  H  N N 205 
GLY HXT  H  N N 206 
HIS N    N  N N 207 
HIS CA   C  N S 208 
HIS C    C  N N 209 
HIS O    O  N N 210 
HIS CB   C  N N 211 
HIS CG   C  Y N 212 
HIS ND1  N  Y N 213 
HIS CD2  C  Y N 214 
HIS CE1  C  Y N 215 
HIS NE2  N  Y N 216 
HIS OXT  O  N N 217 
HIS H    H  N N 218 
HIS H2   H  N N 219 
HIS HA   H  N N 220 
HIS HB2  H  N N 221 
HIS HB3  H  N N 222 
HIS HD1  H  N N 223 
HIS HD2  H  N N 224 
HIS HE1  H  N N 225 
HIS HE2  H  N N 226 
HIS HXT  H  N N 227 
HOH O    O  N N 228 
HOH H1   H  N N 229 
HOH H2   H  N N 230 
ILE N    N  N N 231 
ILE CA   C  N S 232 
ILE C    C  N N 233 
ILE O    O  N N 234 
ILE CB   C  N S 235 
ILE CG1  C  N N 236 
ILE CG2  C  N N 237 
ILE CD1  C  N N 238 
ILE OXT  O  N N 239 
ILE H    H  N N 240 
ILE H2   H  N N 241 
ILE HA   H  N N 242 
ILE HB   H  N N 243 
ILE HG12 H  N N 244 
ILE HG13 H  N N 245 
ILE HG21 H  N N 246 
ILE HG22 H  N N 247 
ILE HG23 H  N N 248 
ILE HD11 H  N N 249 
ILE HD12 H  N N 250 
ILE HD13 H  N N 251 
ILE HXT  H  N N 252 
LEU N    N  N N 253 
LEU CA   C  N S 254 
LEU C    C  N N 255 
LEU O    O  N N 256 
LEU CB   C  N N 257 
LEU CG   C  N N 258 
LEU CD1  C  N N 259 
LEU CD2  C  N N 260 
LEU OXT  O  N N 261 
LEU H    H  N N 262 
LEU H2   H  N N 263 
LEU HA   H  N N 264 
LEU HB2  H  N N 265 
LEU HB3  H  N N 266 
LEU HG   H  N N 267 
LEU HD11 H  N N 268 
LEU HD12 H  N N 269 
LEU HD13 H  N N 270 
LEU HD21 H  N N 271 
LEU HD22 H  N N 272 
LEU HD23 H  N N 273 
LEU HXT  H  N N 274 
LYS N    N  N N 275 
LYS CA   C  N S 276 
LYS C    C  N N 277 
LYS O    O  N N 278 
LYS CB   C  N N 279 
LYS CG   C  N N 280 
LYS CD   C  N N 281 
LYS CE   C  N N 282 
LYS NZ   N  N N 283 
LYS OXT  O  N N 284 
LYS H    H  N N 285 
LYS H2   H  N N 286 
LYS HA   H  N N 287 
LYS HB2  H  N N 288 
LYS HB3  H  N N 289 
LYS HG2  H  N N 290 
LYS HG3  H  N N 291 
LYS HD2  H  N N 292 
LYS HD3  H  N N 293 
LYS HE2  H  N N 294 
LYS HE3  H  N N 295 
LYS HZ1  H  N N 296 
LYS HZ2  H  N N 297 
LYS HZ3  H  N N 298 
LYS HXT  H  N N 299 
MET N    N  N N 300 
MET CA   C  N S 301 
MET C    C  N N 302 
MET O    O  N N 303 
MET CB   C  N N 304 
MET CG   C  N N 305 
MET SD   S  N N 306 
MET CE   C  N N 307 
MET OXT  O  N N 308 
MET H    H  N N 309 
MET H2   H  N N 310 
MET HA   H  N N 311 
MET HB2  H  N N 312 
MET HB3  H  N N 313 
MET HG2  H  N N 314 
MET HG3  H  N N 315 
MET HE1  H  N N 316 
MET HE2  H  N N 317 
MET HE3  H  N N 318 
MET HXT  H  N N 319 
NA  NA   NA N N 320 
PHE N    N  N N 321 
PHE CA   C  N S 322 
PHE C    C  N N 323 
PHE O    O  N N 324 
PHE CB   C  N N 325 
PHE CG   C  Y N 326 
PHE CD1  C  Y N 327 
PHE CD2  C  Y N 328 
PHE CE1  C  Y N 329 
PHE CE2  C  Y N 330 
PHE CZ   C  Y N 331 
PHE OXT  O  N N 332 
PHE H    H  N N 333 
PHE H2   H  N N 334 
PHE HA   H  N N 335 
PHE HB2  H  N N 336 
PHE HB3  H  N N 337 
PHE HD1  H  N N 338 
PHE HD2  H  N N 339 
PHE HE1  H  N N 340 
PHE HE2  H  N N 341 
PHE HZ   H  N N 342 
PHE HXT  H  N N 343 
PRO N    N  N N 344 
PRO CA   C  N S 345 
PRO C    C  N N 346 
PRO O    O  N N 347 
PRO CB   C  N N 348 
PRO CG   C  N N 349 
PRO CD   C  N N 350 
PRO OXT  O  N N 351 
PRO H    H  N N 352 
PRO HA   H  N N 353 
PRO HB2  H  N N 354 
PRO HB3  H  N N 355 
PRO HG2  H  N N 356 
PRO HG3  H  N N 357 
PRO HD2  H  N N 358 
PRO HD3  H  N N 359 
PRO HXT  H  N N 360 
SER N    N  N N 361 
SER CA   C  N S 362 
SER C    C  N N 363 
SER O    O  N N 364 
SER CB   C  N N 365 
SER OG   O  N N 366 
SER OXT  O  N N 367 
SER H    H  N N 368 
SER H2   H  N N 369 
SER HA   H  N N 370 
SER HB2  H  N N 371 
SER HB3  H  N N 372 
SER HG   H  N N 373 
SER HXT  H  N N 374 
THR N    N  N N 375 
THR CA   C  N S 376 
THR C    C  N N 377 
THR O    O  N N 378 
THR CB   C  N R 379 
THR OG1  O  N N 380 
THR CG2  C  N N 381 
THR OXT  O  N N 382 
THR H    H  N N 383 
THR H2   H  N N 384 
THR HA   H  N N 385 
THR HB   H  N N 386 
THR HG1  H  N N 387 
THR HG21 H  N N 388 
THR HG22 H  N N 389 
THR HG23 H  N N 390 
THR HXT  H  N N 391 
TRP N    N  N N 392 
TRP CA   C  N S 393 
TRP C    C  N N 394 
TRP O    O  N N 395 
TRP CB   C  N N 396 
TRP CG   C  Y N 397 
TRP CD1  C  Y N 398 
TRP CD2  C  Y N 399 
TRP NE1  N  Y N 400 
TRP CE2  C  Y N 401 
TRP CE3  C  Y N 402 
TRP CZ2  C  Y N 403 
TRP CZ3  C  Y N 404 
TRP CH2  C  Y N 405 
TRP OXT  O  N N 406 
TRP H    H  N N 407 
TRP H2   H  N N 408 
TRP HA   H  N N 409 
TRP HB2  H  N N 410 
TRP HB3  H  N N 411 
TRP HD1  H  N N 412 
TRP HE1  H  N N 413 
TRP HE3  H  N N 414 
TRP HZ2  H  N N 415 
TRP HZ3  H  N N 416 
TRP HH2  H  N N 417 
TRP HXT  H  N N 418 
TYR N    N  N N 419 
TYR CA   C  N S 420 
TYR C    C  N N 421 
TYR O    O  N N 422 
TYR CB   C  N N 423 
TYR CG   C  Y N 424 
TYR CD1  C  Y N 425 
TYR CD2  C  Y N 426 
TYR CE1  C  Y N 427 
TYR CE2  C  Y N 428 
TYR CZ   C  Y N 429 
TYR OH   O  N N 430 
TYR OXT  O  N N 431 
TYR H    H  N N 432 
TYR H2   H  N N 433 
TYR HA   H  N N 434 
TYR HB2  H  N N 435 
TYR HB3  H  N N 436 
TYR HD1  H  N N 437 
TYR HD2  H  N N 438 
TYR HE1  H  N N 439 
TYR HE2  H  N N 440 
TYR HH   H  N N 441 
TYR HXT  H  N N 442 
VAL N    N  N N 443 
VAL CA   C  N S 444 
VAL C    C  N N 445 
VAL O    O  N N 446 
VAL CB   C  N N 447 
VAL CG1  C  N N 448 
VAL CG2  C  N N 449 
VAL OXT  O  N N 450 
VAL H    H  N N 451 
VAL H2   H  N N 452 
VAL HA   H  N N 453 
VAL HB   H  N N 454 
VAL HG11 H  N N 455 
VAL HG12 H  N N 456 
VAL HG13 H  N N 457 
VAL HG21 H  N N 458 
VAL HG22 H  N N 459 
VAL HG23 H  N N 460 
VAL HXT  H  N N 461 
ZN  ZN   ZN N N 462 
# 
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 
84Z CL1 C1   sing N N 1   
84Z O9  S7   doub N N 2   
84Z C21 C20  doub Y N 3   
84Z C21 C22  sing Y N 4   
84Z C1  C2   doub Y N 5   
84Z C1  C6   sing Y N 6   
84Z C20 C19  sing Y N 7   
84Z C2  C3   sing Y N 8   
84Z O8  S7   doub N N 9   
84Z C22 C23  doub Y N 10  
84Z S7  C6   sing N N 11  
84Z S7  N10  sing N N 12  
84Z C6  C5   doub Y N 13  
84Z O17 S16  doub N N 14  
84Z C19 S16  sing N N 15  
84Z C19 C24  doub Y N 16  
84Z C3  S16  sing N N 17  
84Z C3  C4   doub Y N 18  
84Z C23 C24  sing Y N 19  
84Z C5  C4   sing Y N 20  
84Z S16 O18  doub N N 21  
84Z C4  C12  sing N N 22  
84Z O14 C12  sing N N 23  
84Z O14 C15  sing N N 24  
84Z C12 O13  doub N N 25  
84Z C24 H1   sing N N 26  
84Z C23 H2   sing N N 27  
84Z C22 H3   sing N N 28  
84Z C21 H4   sing N N 29  
84Z C20 H5   sing N N 30  
84Z C2  H6   sing N N 31  
84Z C15 H7   sing N N 32  
84Z C15 H8   sing N N 33  
84Z C15 H9   sing N N 34  
84Z C5  H10  sing N N 35  
84Z N10 H11  sing N N 36  
84Z N10 H12  sing N N 37  
ALA N   CA   sing N N 38  
ALA N   H    sing N N 39  
ALA N   H2   sing N N 40  
ALA CA  C    sing N N 41  
ALA CA  CB   sing N N 42  
ALA CA  HA   sing N N 43  
ALA C   O    doub N N 44  
ALA C   OXT  sing N N 45  
ALA CB  HB1  sing N N 46  
ALA CB  HB2  sing N N 47  
ALA CB  HB3  sing N N 48  
ALA OXT HXT  sing N N 49  
ARG N   CA   sing N N 50  
ARG N   H    sing N N 51  
ARG N   H2   sing N N 52  
ARG CA  C    sing N N 53  
ARG CA  CB   sing N N 54  
ARG CA  HA   sing N N 55  
ARG C   O    doub N N 56  
ARG C   OXT  sing N N 57  
ARG CB  CG   sing N N 58  
ARG CB  HB2  sing N N 59  
ARG CB  HB3  sing N N 60  
ARG CG  CD   sing N N 61  
ARG CG  HG2  sing N N 62  
ARG CG  HG3  sing N N 63  
ARG CD  NE   sing N N 64  
ARG CD  HD2  sing N N 65  
ARG CD  HD3  sing N N 66  
ARG NE  CZ   sing N N 67  
ARG NE  HE   sing N N 68  
ARG CZ  NH1  sing N N 69  
ARG CZ  NH2  doub N N 70  
ARG NH1 HH11 sing N N 71  
ARG NH1 HH12 sing N N 72  
ARG NH2 HH21 sing N N 73  
ARG NH2 HH22 sing N N 74  
ARG OXT HXT  sing N N 75  
ASN N   CA   sing N N 76  
ASN N   H    sing N N 77  
ASN N   H2   sing N N 78  
ASN CA  C    sing N N 79  
ASN CA  CB   sing N N 80  
ASN CA  HA   sing N N 81  
ASN C   O    doub N N 82  
ASN C   OXT  sing N N 83  
ASN CB  CG   sing N N 84  
ASN CB  HB2  sing N N 85  
ASN CB  HB3  sing N N 86  
ASN CG  OD1  doub N N 87  
ASN CG  ND2  sing N N 88  
ASN ND2 HD21 sing N N 89  
ASN ND2 HD22 sing N N 90  
ASN OXT HXT  sing N N 91  
ASP N   CA   sing N N 92  
ASP N   H    sing N N 93  
ASP N   H2   sing N N 94  
ASP CA  C    sing N N 95  
ASP CA  CB   sing N N 96  
ASP CA  HA   sing N N 97  
ASP C   O    doub N N 98  
ASP C   OXT  sing N N 99  
ASP CB  CG   sing N N 100 
ASP CB  HB2  sing N N 101 
ASP CB  HB3  sing N N 102 
ASP CG  OD1  doub N N 103 
ASP CG  OD2  sing N N 104 
ASP OD2 HD2  sing N N 105 
ASP OXT HXT  sing N N 106 
BCN N1  C1   sing N N 107 
BCN N1  C3   sing N N 108 
BCN N1  C5   sing N N 109 
BCN C1  C2   sing N N 110 
BCN C1  H11  sing N N 111 
BCN C1  H12  sing N N 112 
BCN C2  O21  doub N N 113 
BCN C2  O22  sing N N 114 
BCN O22 HO2  sing N N 115 
BCN C3  C4   sing N N 116 
BCN C3  H31  sing N N 117 
BCN C3  H32  sing N N 118 
BCN C4  O4   sing N N 119 
BCN C4  H41  sing N N 120 
BCN C4  H42  sing N N 121 
BCN O4  HO4  sing N N 122 
BCN C5  C6   sing N N 123 
BCN C5  H51  sing N N 124 
BCN C5  H52  sing N N 125 
BCN C6  O6   sing N N 126 
BCN C6  H61  sing N N 127 
BCN C6  H62  sing N N 128 
BCN O6  HO6  sing N N 129 
CYS N   CA   sing N N 130 
CYS N   H    sing N N 131 
CYS N   H2   sing N N 132 
CYS CA  C    sing N N 133 
CYS CA  CB   sing N N 134 
CYS CA  HA   sing N N 135 
CYS C   O    doub N N 136 
CYS C   OXT  sing N N 137 
CYS CB  SG   sing N N 138 
CYS CB  HB2  sing N N 139 
CYS CB  HB3  sing N N 140 
CYS SG  HG   sing N N 141 
CYS OXT HXT  sing N N 142 
DMS S   O    doub N N 143 
DMS S   C1   sing N N 144 
DMS S   C2   sing N N 145 
DMS C1  H11  sing N N 146 
DMS C1  H12  sing N N 147 
DMS C1  H13  sing N N 148 
DMS C2  H21  sing N N 149 
DMS C2  H22  sing N N 150 
DMS C2  H23  sing N N 151 
GLN N   CA   sing N N 152 
GLN N   H    sing N N 153 
GLN N   H2   sing N N 154 
GLN CA  C    sing N N 155 
GLN CA  CB   sing N N 156 
GLN CA  HA   sing N N 157 
GLN C   O    doub N N 158 
GLN C   OXT  sing N N 159 
GLN CB  CG   sing N N 160 
GLN CB  HB2  sing N N 161 
GLN CB  HB3  sing N N 162 
GLN CG  CD   sing N N 163 
GLN CG  HG2  sing N N 164 
GLN CG  HG3  sing N N 165 
GLN CD  OE1  doub N N 166 
GLN CD  NE2  sing N N 167 
GLN NE2 HE21 sing N N 168 
GLN NE2 HE22 sing N N 169 
GLN OXT HXT  sing N N 170 
GLU N   CA   sing N N 171 
GLU N   H    sing N N 172 
GLU N   H2   sing N N 173 
GLU CA  C    sing N N 174 
GLU CA  CB   sing N N 175 
GLU CA  HA   sing N N 176 
GLU C   O    doub N N 177 
GLU C   OXT  sing N N 178 
GLU CB  CG   sing N N 179 
GLU CB  HB2  sing N N 180 
GLU CB  HB3  sing N N 181 
GLU CG  CD   sing N N 182 
GLU CG  HG2  sing N N 183 
GLU CG  HG3  sing N N 184 
GLU CD  OE1  doub N N 185 
GLU CD  OE2  sing N N 186 
GLU OE2 HE2  sing N N 187 
GLU OXT HXT  sing N N 188 
GLY N   CA   sing N N 189 
GLY N   H    sing N N 190 
GLY N   H2   sing N N 191 
GLY CA  C    sing N N 192 
GLY CA  HA2  sing N N 193 
GLY CA  HA3  sing N N 194 
GLY C   O    doub N N 195 
GLY C   OXT  sing N N 196 
GLY OXT HXT  sing N N 197 
HIS N   CA   sing N N 198 
HIS N   H    sing N N 199 
HIS N   H2   sing N N 200 
HIS CA  C    sing N N 201 
HIS CA  CB   sing N N 202 
HIS CA  HA   sing N N 203 
HIS C   O    doub N N 204 
HIS C   OXT  sing N N 205 
HIS CB  CG   sing N N 206 
HIS CB  HB2  sing N N 207 
HIS CB  HB3  sing N N 208 
HIS CG  ND1  sing Y N 209 
HIS CG  CD2  doub Y N 210 
HIS ND1 CE1  doub Y N 211 
HIS ND1 HD1  sing N N 212 
HIS CD2 NE2  sing Y N 213 
HIS CD2 HD2  sing N N 214 
HIS CE1 NE2  sing Y N 215 
HIS CE1 HE1  sing N N 216 
HIS NE2 HE2  sing N N 217 
HIS OXT HXT  sing N N 218 
HOH O   H1   sing N N 219 
HOH O   H2   sing N N 220 
ILE N   CA   sing N N 221 
ILE N   H    sing N N 222 
ILE N   H2   sing N N 223 
ILE CA  C    sing N N 224 
ILE CA  CB   sing N N 225 
ILE CA  HA   sing N N 226 
ILE C   O    doub N N 227 
ILE C   OXT  sing N N 228 
ILE CB  CG1  sing N N 229 
ILE CB  CG2  sing N N 230 
ILE CB  HB   sing N N 231 
ILE CG1 CD1  sing N N 232 
ILE CG1 HG12 sing N N 233 
ILE CG1 HG13 sing N N 234 
ILE CG2 HG21 sing N N 235 
ILE CG2 HG22 sing N N 236 
ILE CG2 HG23 sing N N 237 
ILE CD1 HD11 sing N N 238 
ILE CD1 HD12 sing N N 239 
ILE CD1 HD13 sing N N 240 
ILE OXT HXT  sing N N 241 
LEU N   CA   sing N N 242 
LEU N   H    sing N N 243 
LEU N   H2   sing N N 244 
LEU CA  C    sing N N 245 
LEU CA  CB   sing N N 246 
LEU CA  HA   sing N N 247 
LEU C   O    doub N N 248 
LEU C   OXT  sing N N 249 
LEU CB  CG   sing N N 250 
LEU CB  HB2  sing N N 251 
LEU CB  HB3  sing N N 252 
LEU CG  CD1  sing N N 253 
LEU CG  CD2  sing N N 254 
LEU CG  HG   sing N N 255 
LEU CD1 HD11 sing N N 256 
LEU CD1 HD12 sing N N 257 
LEU CD1 HD13 sing N N 258 
LEU CD2 HD21 sing N N 259 
LEU CD2 HD22 sing N N 260 
LEU CD2 HD23 sing N N 261 
LEU OXT HXT  sing N N 262 
LYS N   CA   sing N N 263 
LYS N   H    sing N N 264 
LYS N   H2   sing N N 265 
LYS CA  C    sing N N 266 
LYS CA  CB   sing N N 267 
LYS CA  HA   sing N N 268 
LYS C   O    doub N N 269 
LYS C   OXT  sing N N 270 
LYS CB  CG   sing N N 271 
LYS CB  HB2  sing N N 272 
LYS CB  HB3  sing N N 273 
LYS CG  CD   sing N N 274 
LYS CG  HG2  sing N N 275 
LYS CG  HG3  sing N N 276 
LYS CD  CE   sing N N 277 
LYS CD  HD2  sing N N 278 
LYS CD  HD3  sing N N 279 
LYS CE  NZ   sing N N 280 
LYS CE  HE2  sing N N 281 
LYS CE  HE3  sing N N 282 
LYS NZ  HZ1  sing N N 283 
LYS NZ  HZ2  sing N N 284 
LYS NZ  HZ3  sing N N 285 
LYS OXT HXT  sing N N 286 
MET N   CA   sing N N 287 
MET N   H    sing N N 288 
MET N   H2   sing N N 289 
MET CA  C    sing N N 290 
MET CA  CB   sing N N 291 
MET CA  HA   sing N N 292 
MET C   O    doub N N 293 
MET C   OXT  sing N N 294 
MET CB  CG   sing N N 295 
MET CB  HB2  sing N N 296 
MET CB  HB3  sing N N 297 
MET CG  SD   sing N N 298 
MET CG  HG2  sing N N 299 
MET CG  HG3  sing N N 300 
MET SD  CE   sing N N 301 
MET CE  HE1  sing N N 302 
MET CE  HE2  sing N N 303 
MET CE  HE3  sing N N 304 
MET OXT HXT  sing N N 305 
PHE N   CA   sing N N 306 
PHE N   H    sing N N 307 
PHE N   H2   sing N N 308 
PHE CA  C    sing N N 309 
PHE CA  CB   sing N N 310 
PHE CA  HA   sing N N 311 
PHE C   O    doub N N 312 
PHE C   OXT  sing N N 313 
PHE CB  CG   sing N N 314 
PHE CB  HB2  sing N N 315 
PHE CB  HB3  sing N N 316 
PHE CG  CD1  doub Y N 317 
PHE CG  CD2  sing Y N 318 
PHE CD1 CE1  sing Y N 319 
PHE CD1 HD1  sing N N 320 
PHE CD2 CE2  doub Y N 321 
PHE CD2 HD2  sing N N 322 
PHE CE1 CZ   doub Y N 323 
PHE CE1 HE1  sing N N 324 
PHE CE2 CZ   sing Y N 325 
PHE CE2 HE2  sing N N 326 
PHE CZ  HZ   sing N N 327 
PHE OXT HXT  sing N N 328 
PRO N   CA   sing N N 329 
PRO N   CD   sing N N 330 
PRO N   H    sing N N 331 
PRO CA  C    sing N N 332 
PRO CA  CB   sing N N 333 
PRO CA  HA   sing N N 334 
PRO C   O    doub N N 335 
PRO C   OXT  sing N N 336 
PRO CB  CG   sing N N 337 
PRO CB  HB2  sing N N 338 
PRO CB  HB3  sing N N 339 
PRO CG  CD   sing N N 340 
PRO CG  HG2  sing N N 341 
PRO CG  HG3  sing N N 342 
PRO CD  HD2  sing N N 343 
PRO CD  HD3  sing N N 344 
PRO OXT HXT  sing N N 345 
SER N   CA   sing N N 346 
SER N   H    sing N N 347 
SER N   H2   sing N N 348 
SER CA  C    sing N N 349 
SER CA  CB   sing N N 350 
SER CA  HA   sing N N 351 
SER C   O    doub N N 352 
SER C   OXT  sing N N 353 
SER CB  OG   sing N N 354 
SER CB  HB2  sing N N 355 
SER CB  HB3  sing N N 356 
SER OG  HG   sing N N 357 
SER OXT HXT  sing N N 358 
THR N   CA   sing N N 359 
THR N   H    sing N N 360 
THR N   H2   sing N N 361 
THR CA  C    sing N N 362 
THR CA  CB   sing N N 363 
THR CA  HA   sing N N 364 
THR C   O    doub N N 365 
THR C   OXT  sing N N 366 
THR CB  OG1  sing N N 367 
THR CB  CG2  sing N N 368 
THR CB  HB   sing N N 369 
THR OG1 HG1  sing N N 370 
THR CG2 HG21 sing N N 371 
THR CG2 HG22 sing N N 372 
THR CG2 HG23 sing N N 373 
THR OXT HXT  sing N N 374 
TRP N   CA   sing N N 375 
TRP N   H    sing N N 376 
TRP N   H2   sing N N 377 
TRP CA  C    sing N N 378 
TRP CA  CB   sing N N 379 
TRP CA  HA   sing N N 380 
TRP C   O    doub N N 381 
TRP C   OXT  sing N N 382 
TRP CB  CG   sing N N 383 
TRP CB  HB2  sing N N 384 
TRP CB  HB3  sing N N 385 
TRP CG  CD1  doub Y N 386 
TRP CG  CD2  sing Y N 387 
TRP CD1 NE1  sing Y N 388 
TRP CD1 HD1  sing N N 389 
TRP CD2 CE2  doub Y N 390 
TRP CD2 CE3  sing Y N 391 
TRP NE1 CE2  sing Y N 392 
TRP NE1 HE1  sing N N 393 
TRP CE2 CZ2  sing Y N 394 
TRP CE3 CZ3  doub Y N 395 
TRP CE3 HE3  sing N N 396 
TRP CZ2 CH2  doub Y N 397 
TRP CZ2 HZ2  sing N N 398 
TRP CZ3 CH2  sing Y N 399 
TRP CZ3 HZ3  sing N N 400 
TRP CH2 HH2  sing N N 401 
TRP OXT HXT  sing N N 402 
TYR N   CA   sing N N 403 
TYR N   H    sing N N 404 
TYR N   H2   sing N N 405 
TYR CA  C    sing N N 406 
TYR CA  CB   sing N N 407 
TYR CA  HA   sing N N 408 
TYR C   O    doub N N 409 
TYR C   OXT  sing N N 410 
TYR CB  CG   sing N N 411 
TYR CB  HB2  sing N N 412 
TYR CB  HB3  sing N N 413 
TYR CG  CD1  doub Y N 414 
TYR CG  CD2  sing Y N 415 
TYR CD1 CE1  sing Y N 416 
TYR CD1 HD1  sing N N 417 
TYR CD2 CE2  doub Y N 418 
TYR CD2 HD2  sing N N 419 
TYR CE1 CZ   doub Y N 420 
TYR CE1 HE1  sing N N 421 
TYR CE2 CZ   sing Y N 422 
TYR CE2 HE2  sing N N 423 
TYR CZ  OH   sing N N 424 
TYR OH  HH   sing N N 425 
TYR OXT HXT  sing N N 426 
VAL N   CA   sing N N 427 
VAL N   H    sing N N 428 
VAL N   H2   sing N N 429 
VAL CA  C    sing N N 430 
VAL CA  CB   sing N N 431 
VAL CA  HA   sing N N 432 
VAL C   O    doub N N 433 
VAL C   OXT  sing N N 434 
VAL CB  CG1  sing N N 435 
VAL CB  CG2  sing N N 436 
VAL CB  HB   sing N N 437 
VAL CG1 HG11 sing N N 438 
VAL CG1 HG12 sing N N 439 
VAL CG1 HG13 sing N N 440 
VAL CG2 HG21 sing N N 441 
VAL CG2 HG22 sing N N 442 
VAL CG2 HG23 sing N N 443 
VAL OXT HXT  sing N N 444 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        84Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   84Z 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_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   4HT0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7Q0E 
_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.fract_transf_matrix[1][1]   0.023719 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006030 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024186 
_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]   0.014333 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
NA 
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 1   ? 34.801 1.841   6.451   1.00 22.92 ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 1   ? 34.459 0.726   7.458   1.00 27.31 ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 1   ? 33.365 1.173   8.443   1.00 22.30 ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 1   ? 33.742 1.434   9.638   1.00 34.50 ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 1   ? 35.723 0.284   8.315   1.00 26.03 ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 1   ? 35.518 -1.011  9.020   1.00 26.70 ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 1   ? 35.224 -1.080  10.381  1.00 27.91 ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 1   ? 35.574 -2.300  8.561   1.00 29.48 ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 1   ? 35.182 -2.362  10.739  1.00 31.79 ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 1   ? 35.371 -3.123  9.660   1.00 33.77 ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 2   ? 32.081 1.252   7.962   1.00 20.17 ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 2   ? 30.951 1.906   8.685   1.00 20.24 ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 2   ? 30.306 0.798   9.523   1.00 14.91 ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 2   ? 30.473 -0.403  9.221   1.00 17.30 ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 2   ? 29.950 2.446   7.580   1.00 28.82 ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 2   ? 29.169 3.671   8.001   1.00 41.69 ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 2   ? 28.046 4.139   7.324   1.00 55.35 ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 2   ? 29.339 4.517   9.058   1.00 57.16 ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 2   ? 27.567 5.206   7.943   1.00 76.84 ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 2   ? 28.336 5.462   8.992   1.00 81.11 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 3   ? 29.449 1.172   10.418  1.00 12.68 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 3   ? 28.755 0.251   11.257  1.00 9.70  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 3   ? 27.761 -0.536  10.473  1.00 9.70  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 3   ? 27.228 -0.089  9.446   1.00 11.68 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 3   ? 28.070 0.967   12.420  1.00 10.76 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 3   ? 26.852 1.804   12.041  1.00 9.46  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 3   ? 26.814 3.114   11.688  1.00 10.79 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 3   ? 25.483 1.339   12.003  1.00 7.32  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 3   ? 25.525 3.502   11.472  1.00 10.33 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 3   ? 24.684 2.432   11.637  1.00 9.34  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 3   ? 24.870 0.069   12.281  1.00 8.26  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 3   ? 23.289 2.371   11.488  1.00 9.29  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 3   ? 23.495 -0.008  12.126  1.00 9.16  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 3   ? 22.727 1.130   11.728  1.00 8.87  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 4   ? 27.465 -1.739  10.954  1.00 9.31  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 4   ? 26.422 -2.549  10.316  1.00 9.30  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 4   ? 26.075 -3.707  11.254  1.00 9.67  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 4   ? 26.091 -3.553  12.503  1.00 10.39 ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 5   ? 25.769 -4.829  10.621  1.00 12.52 ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 5   ? 25.377 -6.025  11.311  1.00 13.31 ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 5   ? 26.189 -7.236  10.875  1.00 24.23 ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 5   ? 25.589 -8.164  10.332  1.00 19.78 ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 5   ? 23.859 -6.276  11.069  1.00 13.04 ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 5   ? 22.991 -5.164  11.717  1.00 7.47  ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 5   ? 22.664 -5.210  13.066  1.00 7.53  ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 5   ? 22.519 -4.097  10.965  1.00 9.49  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 5   ? 21.891 -4.223  13.648  1.00 6.22  ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 5   ? 21.745 -3.105  11.538  1.00 6.90  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 5   ? 21.435 -3.174  12.879  1.00 5.87  ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 5   ? 20.665 -2.189  13.455  1.00 5.88  ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 6   ? 27.511 -7.266  11.111  1.00 31.51 ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 6   ? 28.377 -8.394  10.724  1.00 22.78 ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 6   ? 29.484 -8.728  11.734  1.00 22.81 ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 6   ? 29.451 -8.175  12.833  1.00 31.57 ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 7   ? 30.353 -9.660  11.510  1.00 28.45 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 7   ? 31.208 -9.788  12.635  1.00 35.83 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 7   ? 32.206 -8.661  12.614  1.00 29.84 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 7   ? 32.905 -8.532  13.632  1.00 42.48 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 7   ? 31.935 -11.134 12.605  1.00 36.08 ? 9   LYS A CB  1 
ATOM   60   N  N   . HIS A 1 8   ? 32.437 -8.041  11.467  1.00 43.45 ? 10  HIS A N   1 
ATOM   61   C  CA  . HIS A 1 8   ? 33.462 -7.018  11.390  1.00 28.37 ? 10  HIS A CA  1 
ATOM   62   C  C   . HIS A 1 8   ? 32.933 -5.646  11.693  1.00 21.26 ? 10  HIS A C   1 
ATOM   63   O  O   . HIS A 1 8   ? 33.711 -4.711  11.888  1.00 19.97 ? 10  HIS A O   1 
ATOM   64   C  CB  . HIS A 1 8   ? 34.153 -7.037  10.027  1.00 16.80 ? 10  HIS A CB  1 
ATOM   65   C  CG  . HIS A 1 8   ? 34.678 -8.382  9.637   1.00 14.50 ? 10  HIS A CG  1 
ATOM   66   N  ND1 . HIS A 1 8   ? 35.589 -9.083  10.405  1.00 19.11 ? 10  HIS A ND1 1 
ATOM   67   C  CD2 . HIS A 1 8   ? 34.413 -9.157  8.557   1.00 14.58 ? 10  HIS A CD2 1 
ATOM   68   C  CE1 . HIS A 1 8   ? 35.862 -10.231 9.810   1.00 12.83 ? 10  HIS A CE1 1 
ATOM   69   N  NE2 . HIS A 1 8   ? 35.164 -10.300 8.690   1.00 17.09 ? 10  HIS A NE2 1 
ATOM   70   N  N   . ASN A 1 9   ? 31.617 -5.498  11.740  1.00 13.97 ? 11  ASN A N   1 
ATOM   71   C  CA  . ASN A 1 9   ? 31.144 -4.179  12.044  1.00 12.16 ? 11  ASN A CA  1 
ATOM   72   C  C   . ASN A 1 9   ? 29.780 -4.155  12.779  1.00 11.37 ? 11  ASN A C   1 
ATOM   73   O  O   . ASN A 1 9   ? 29.120 -3.113  12.897  1.00 11.34 ? 11  ASN A O   1 
ATOM   74   C  CB  . ASN A 1 9   ? 30.950 -3.363  10.759  1.00 11.00 ? 11  ASN A CB  1 
ATOM   75   C  CG  . ASN A 1 9   ? 29.818 -3.948  9.818   1.00 12.99 ? 11  ASN A CG  1 
ATOM   76   O  OD1 . ASN A 1 9   ? 29.256 -4.985  10.145  1.00 16.06 ? 11  ASN A OD1 1 
ATOM   77   N  ND2 . ASN A 1 9   ? 29.594 -3.310  8.642   1.00 16.87 ? 11  ASN A ND2 1 
ATOM   78   N  N   . GLY A 1 10  ? 29.432 -5.245  13.418  1.00 10.71 ? 12  GLY A N   1 
ATOM   79   C  CA  . GLY A 1 10  ? 28.188 -5.380  14.121  1.00 10.76 ? 12  GLY A CA  1 
ATOM   80   C  C   . GLY A 1 10  ? 28.161 -4.781  15.520  1.00 10.64 ? 12  GLY A C   1 
ATOM   81   O  O   . GLY A 1 10  ? 29.089 -4.140  15.960  1.00 9.87  ? 12  GLY A O   1 
ATOM   82   N  N   . PRO A 1 11  ? 27.094 -5.101  16.279  1.00 8.06  ? 13  PRO A N   1 
ATOM   83   C  CA  . PRO A 1 11  ? 26.840 -4.451  17.580  1.00 9.25  ? 13  PRO A CA  1 
ATOM   84   C  C   . PRO A 1 11  ? 28.005 -4.481  18.526  1.00 8.98  ? 13  PRO A C   1 
ATOM   85   O  O   . PRO A 1 11  ? 28.177 -3.495  19.295  1.00 9.15  ? 13  PRO A O   1 
ATOM   86   C  CB  . PRO A 1 11  ? 25.688 -5.304  18.128  1.00 10.89 ? 13  PRO A CB  1 
ATOM   87   C  CG  . PRO A 1 11  ? 24.891 -5.578  16.855  1.00 10.33 ? 13  PRO A CG  1 
ATOM   88   C  CD  . PRO A 1 11  ? 25.945 -5.900  15.801  1.00 9.33  ? 13  PRO A CD  1 
ATOM   89   N  N   . GLU A 1 12  ? 28.787 -5.534  18.538  1.00 9.81  ? 14  GLU A N   1 
ATOM   90   C  CA  . GLU A 1 12  ? 29.864 -5.614  19.491  1.00 11.03 ? 14  GLU A CA  1 
ATOM   91   C  C   . GLU A 1 12  ? 31.066 -4.639  19.186  1.00 11.05 ? 14  GLU A C   1 
ATOM   92   O  O   . GLU A 1 12  ? 31.967 -4.470  20.008  1.00 12.36 ? 14  GLU A O   1 
ATOM   93   C  CB  . GLU A 1 12  ? 30.348 -7.052  19.606  1.00 17.19 ? 14  GLU A CB  1 
ATOM   94   C  CG  . GLU A 1 12  ? 31.146 -7.536  18.406  1.00 17.29 ? 14  GLU A CG  1 
ATOM   95   C  CD  . GLU A 1 12  ? 30.265 -8.115  17.317  1.00 16.83 ? 14  GLU A CD  1 
ATOM   96   O  OE1 . GLU A 1 12  ? 29.071 -7.753  17.261  1.00 15.70 ? 14  GLU A OE1 1 
ATOM   97   O  OE2 . GLU A 1 12  ? 30.769 -8.932  16.516  1.00 22.86 ? 14  GLU A OE2 1 
ATOM   98   N  N   . HIS A 1 13  ? 31.037 -4.033  18.017  1.00 9.85  ? 15  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 32.002 -3.065  17.574  1.00 9.05  ? 15  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 31.575 -1.615  17.721  1.00 8.92  ? 15  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 32.398 -0.706  17.601  1.00 11.82 ? 15  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 32.363 -3.295  16.097  1.00 8.89  ? 15  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 33.063 -4.588  15.875  1.00 9.81  ? 15  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 34.452 -4.706  16.080  1.00 15.34 ? 15  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 32.587 -5.814  15.487  1.00 13.04 ? 15  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 34.792 -5.980  15.845  1.00 15.43 ? 15  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 33.713 -6.651  15.462  1.00 17.89 ? 15  HIS A NE2 1 
ATOM   108  N  N   . TRP A 1 14  ? 30.268 -1.357  17.885  1.00 7.55  ? 16  TRP A N   1 
ATOM   109  C  CA  . TRP A 1 14  ? 29.769 -0.028  17.774  1.00 7.59  ? 16  TRP A CA  1 
ATOM   110  C  C   . TRP A 1 14  ? 30.325 0.963   18.808  1.00 8.43  ? 16  TRP A C   1 
ATOM   111  O  O   . TRP A 1 14  ? 30.425 2.145   18.525  1.00 8.71  ? 16  TRP A O   1 
ATOM   112  C  CB  . TRP A 1 14  ? 28.206 -0.060  17.943  1.00 7.23  ? 16  TRP A CB  1 
ATOM   113  C  CG  . TRP A 1 14  ? 27.506 -0.786  16.813  1.00 6.53  ? 16  TRP A CG  1 
ATOM   114  C  CD1 . TRP A 1 14  ? 28.065 -1.212  15.598  1.00 6.70  ? 16  TRP A CD1 1 
ATOM   115  C  CD2 . TRP A 1 14  ? 26.127 -1.108  16.769  1.00 6.62  ? 16  TRP A CD2 1 
ATOM   116  N  NE1 . TRP A 1 14  ? 27.073 -1.854  14.814  1.00 7.03  ? 16  TRP A NE1 1 
ATOM   117  C  CE2 . TRP A 1 14  ? 25.877 -1.729  15.480  1.00 6.87  ? 16  TRP A CE2 1 
ATOM   118  C  CE3 . TRP A 1 14  ? 25.073 -0.885  17.670  1.00 5.89  ? 16  TRP A CE3 1 
ATOM   119  C  CZ2 . TRP A 1 14  ? 24.604 -2.188  15.113  1.00 6.00  ? 16  TRP A CZ2 1 
ATOM   120  C  CZ3 . TRP A 1 14  ? 23.828 -1.364  17.297  1.00 6.58  ? 16  TRP A CZ3 1 
ATOM   121  C  CH2 . TRP A 1 14  ? 23.590 -1.977  16.048  1.00 6.84  ? 16  TRP A CH2 1 
ATOM   122  N  N   . HIS A 1 15  ? 30.735 0.461   19.974  1.00 7.51  ? 17  HIS A N   1 
ATOM   123  C  CA  . HIS A 1 15  ? 31.201 1.300   21.027  1.00 8.14  ? 17  HIS A CA  1 
ATOM   124  C  C   . HIS A 1 15  ? 32.471 2.074   20.627  1.00 10.47 ? 17  HIS A C   1 
ATOM   125  O  O   . HIS A 1 15  ? 32.744 3.144   21.187  1.00 11.98 ? 17  HIS A O   1 
ATOM   126  C  CB  . HIS A 1 15  ? 31.519 0.514   22.297  1.00 9.44  ? 17  HIS A CB  1 
ATOM   127  C  CG  . HIS A 1 15  ? 32.714 -0.351  22.184  1.00 9.12  ? 17  HIS A CG  1 
ATOM   128  N  ND1 . HIS A 1 15  ? 33.947 0.059   22.683  1.00 14.08 ? 17  HIS A ND1 1 
ATOM   129  C  CD2 . HIS A 1 15  ? 32.903 -1.542  21.580  1.00 11.29 ? 17  HIS A CD2 1 
ATOM   130  C  CE1 . HIS A 1 15  ? 34.832 -0.842  22.416  1.00 13.72 ? 17  HIS A CE1 1 
ATOM   131  N  NE2 . HIS A 1 15  ? 34.245 -1.834  21.793  1.00 13.28 ? 17  HIS A NE2 1 
ATOM   132  N  N   . LYS A 1 16  ? 33.234 1.590   19.624  1.00 10.55 ? 18  LYS A N   1 
ATOM   133  C  CA  . LYS A 1 16  ? 34.425 2.317   19.311  1.00 11.71 ? 18  LYS A CA  1 
ATOM   134  C  C   . LYS A 1 16  ? 34.119 3.621   18.588  1.00 13.08 ? 18  LYS A C   1 
ATOM   135  O  O   . LYS A 1 16  ? 34.777 4.616   18.831  1.00 19.03 ? 18  LYS A O   1 
ATOM   136  C  CB  . LYS A 1 16  ? 35.317 1.434   18.416  1.00 12.10 ? 18  LYS A CB  1 
ATOM   137  C  CG  . LYS A 1 16  ? 35.929 0.223   19.119  1.00 12.19 ? 18  LYS A CG  1 
ATOM   138  C  CD  . LYS A 1 16  ? 36.634 -0.773  18.186  1.00 13.92 ? 18  LYS A CD  1 
ATOM   139  C  CE  . LYS A 1 16  ? 35.616 -1.747  17.567  1.00 13.08 ? 18  LYS A CE  1 
ATOM   140  N  NZ  . LYS A 1 16  ? 36.279 -2.576  16.497  1.00 13.38 ? 18  LYS A NZ  1 
ATOM   141  N  N   . ASP A 1 17  ? 33.118 3.637   17.710  1.00 11.70 ? 19  ASP A N   1 
ATOM   142  C  CA  . ASP A 1 17  ? 32.663 4.946   17.169  1.00 11.78 ? 19  ASP A CA  1 
ATOM   143  C  C   . ASP A 1 17  ? 31.641 5.675   17.971  1.00 11.41 ? 19  ASP A C   1 
ATOM   144  O  O   . ASP A 1 17  ? 31.572 6.878   17.899  1.00 12.24 ? 19  ASP A O   1 
ATOM   145  C  CB  . ASP A 1 17  ? 32.157 4.831   15.771  1.00 17.20 ? 19  ASP A CB  1 
ATOM   146  C  CG  . ASP A 1 17  ? 33.301 4.902   14.713  1.00 22.33 ? 19  ASP A CG  1 
ATOM   147  O  OD1 . ASP A 1 17  ? 34.390 5.423   14.944  1.00 28.24 ? 19  ASP A OD1 1 
ATOM   148  O  OD2 . ASP A 1 17  ? 33.141 4.362   13.703  1.00 26.27 ? 19  ASP A OD2 1 
ATOM   149  N  N   . PHE A 1 18  ? 30.918 4.924   18.807  1.00 10.44 ? 20  PHE A N   1 
ATOM   150  C  CA  . PHE A 1 18  ? 29.805 5.510   19.570  1.00 9.13  ? 20  PHE A CA  1 
ATOM   151  C  C   . PHE A 1 18  ? 29.931 5.026   21.016  1.00 8.92  ? 20  PHE A C   1 
ATOM   152  O  O   . PHE A 1 18  ? 29.273 4.055   21.404  1.00 8.17  ? 20  PHE A O   1 
ATOM   153  C  CB  . PHE A 1 18  ? 28.456 5.051   18.985  1.00 9.82  ? 20  PHE A CB  1 
ATOM   154  C  CG  . PHE A 1 18  ? 28.318 5.447   17.503  1.00 10.59 ? 20  PHE A CG  1 
ATOM   155  C  CD1 . PHE A 1 18  ? 27.957 6.717   17.136  1.00 13.57 ? 20  PHE A CD1 1 
ATOM   156  C  CD2 . PHE A 1 18  ? 28.683 4.496   16.499  1.00 12.32 ? 20  PHE A CD2 1 
ATOM   157  C  CE1 . PHE A 1 18  ? 27.948 7.053   15.737  1.00 13.90 ? 20  PHE A CE1 1 
ATOM   158  C  CE2 . PHE A 1 18  ? 28.676 4.818   15.159  1.00 12.96 ? 20  PHE A CE2 1 
ATOM   159  C  CZ  . PHE A 1 18  ? 28.337 6.091   14.803  1.00 13.31 ? 20  PHE A CZ  1 
ATOM   160  N  N   A PRO A 1 19  ? 30.755 5.671   21.865  0.50 8.90  ? 21  PRO A N   1 
ATOM   161  N  N   B PRO A 1 19  ? 30.790 5.659   21.843  0.50 8.76  ? 21  PRO A N   1 
ATOM   162  C  CA  A PRO A 1 19  ? 31.042 5.138   23.196  0.50 9.71  ? 21  PRO A CA  1 
ATOM   163  C  CA  B PRO A 1 19  ? 31.055 5.090   23.155  0.50 9.69  ? 21  PRO A CA  1 
ATOM   164  C  C   A PRO A 1 19  ? 29.795 5.077   24.108  0.50 9.01  ? 21  PRO A C   1 
ATOM   165  C  C   B PRO A 1 19  ? 29.816 5.087   24.103  0.50 8.90  ? 21  PRO A C   1 
ATOM   166  O  O   A PRO A 1 19  ? 29.805 4.294   25.061  0.50 9.10  ? 21  PRO A O   1 
ATOM   167  O  O   B PRO A 1 19  ? 29.850 4.323   25.066  0.50 9.38  ? 21  PRO A O   1 
ATOM   168  C  CB  A PRO A 1 19  ? 32.087 6.124   23.765  0.50 13.60 ? 21  PRO A CB  1 
ATOM   169  C  CB  B PRO A 1 19  ? 32.243 5.906   23.703  0.50 13.05 ? 21  PRO A CB  1 
ATOM   170  C  CG  A PRO A 1 19  ? 31.994 7.352   22.917  0.50 14.15 ? 21  PRO A CG  1 
ATOM   171  C  CG  B PRO A 1 19  ? 32.778 6.752   22.583  0.50 13.33 ? 21  PRO A CG  1 
ATOM   172  C  CD  A PRO A 1 19  ? 31.636 6.804   21.552  0.50 11.31 ? 21  PRO A CD  1 
ATOM   173  C  CD  B PRO A 1 19  ? 31.809 6.642   21.424  0.50 11.25 ? 21  PRO A CD  1 
ATOM   174  N  N   . ILE A 1 20  ? 28.728 5.822   23.777  1.00 7.46  ? 22  ILE A N   1 
ATOM   175  C  CA  . ILE A 1 20  ? 27.487 5.721   24.487  1.00 7.88  ? 22  ILE A CA  1 
ATOM   176  C  C   . ILE A 1 20  ? 26.911 4.306   24.411  1.00 6.32  ? 22  ILE A C   1 
ATOM   177  O  O   . ILE A 1 20  ? 25.987 3.974   25.150  1.00 7.06  ? 22  ILE A O   1 
ATOM   178  C  CB  . ILE A 1 20  ? 26.491 6.812   24.020  1.00 8.58  ? 22  ILE A CB  1 
ATOM   179  C  CG1 . ILE A 1 20  ? 25.446 7.130   25.055  1.00 8.97  ? 22  ILE A CG1 1 
ATOM   180  C  CG2 . ILE A 1 20  ? 25.893 6.457   22.687  1.00 8.34  ? 22  ILE A CG2 1 
ATOM   181  C  CD1 . ILE A 1 20  ? 24.488 8.250   24.616  1.00 12.29 ? 22  ILE A CD1 1 
ATOM   182  N  N   . ALA A 1 21  ? 27.437 3.471   23.492  1.00 6.67  ? 23  ALA A N   1 
ATOM   183  C  CA  . ALA A 1 21  ? 26.958 2.070   23.377  1.00 6.36  ? 23  ALA A CA  1 
ATOM   184  C  C   . ALA A 1 21  ? 27.054 1.378   24.738  1.00 6.45  ? 23  ALA A C   1 
ATOM   185  O  O   . ALA A 1 21  ? 26.325 0.386   24.947  1.00 6.97  ? 23  ALA A O   1 
ATOM   186  C  CB  . ALA A 1 21  ? 27.802 1.292   22.401  1.00 7.43  ? 23  ALA A CB  1 
ATOM   187  N  N   . LYS A 1 22  ? 28.004 1.787   25.635  1.00 7.20  ? 24  LYS A N   1 
ATOM   188  C  CA  . LYS A 1 22  ? 28.148 1.186   26.963  1.00 7.75  ? 24  LYS A CA  1 
ATOM   189  C  C   . LYS A 1 22  ? 27.552 2.095   28.029  1.00 8.94  ? 24  LYS A C   1 
ATOM   190  O  O   . LYS A 1 22  ? 27.883 1.942   29.218  1.00 12.01 ? 24  LYS A O   1 
ATOM   191  C  CB  . LYS A 1 22  ? 29.655 0.923   27.267  1.00 9.54  ? 24  LYS A CB  1 
ATOM   192  C  CG  . LYS A 1 22  ? 30.254 -0.039  26.270  1.00 11.60 ? 24  LYS A CG  1 
ATOM   193  C  CD  . LYS A 1 22  ? 31.730 -0.261  26.607  1.00 16.33 ? 24  LYS A CD  1 
ATOM   194  C  CE  . LYS A 1 22  ? 32.479 -1.138  25.635  1.00 18.68 ? 24  LYS A CE  1 
ATOM   195  N  NZ  . LYS A 1 22  ? 32.110 -2.532  25.969  1.00 21.10 ? 24  LYS A NZ  1 
ATOM   196  N  N   . GLY A 1 23  ? 26.537 2.873   27.664  1.00 8.17  ? 25  GLY A N   1 
ATOM   197  C  CA  . GLY A 1 23  ? 25.929 3.889   28.556  1.00 8.71  ? 25  GLY A CA  1 
ATOM   198  C  C   . GLY A 1 23  ? 24.946 3.305   29.551  1.00 7.52  ? 25  GLY A C   1 
ATOM   199  O  O   . GLY A 1 23  ? 24.750 2.071   29.668  1.00 8.91  ? 25  GLY A O   1 
ATOM   200  N  N   . GLU A 1 24  ? 24.287 4.228   30.283  1.00 8.82  ? 26  GLU A N   1 
ATOM   201  C  CA  . GLU A 1 24  ? 23.435 3.819   31.378  1.00 8.83  ? 26  GLU A CA  1 
ATOM   202  C  C   . GLU A 1 24  ? 21.995 3.614   31.028  1.00 7.17  ? 26  GLU A C   1 
ATOM   203  O  O   . GLU A 1 24  ? 21.236 3.077   31.858  1.00 8.91  ? 26  GLU A O   1 
ATOM   204  C  CB  . GLU A 1 24  ? 23.450 4.954   32.475  1.00 11.92 ? 26  GLU A CB  1 
ATOM   205  C  CG  . GLU A 1 24  ? 24.830 5.224   32.998  1.00 14.87 ? 26  GLU A CG  1 
ATOM   206  C  CD  . GLU A 1 24  ? 25.396 3.963   33.695  1.00 22.11 ? 26  GLU A CD  1 
ATOM   207  O  OE1 . GLU A 1 24  ? 24.627 3.388   34.516  1.00 24.34 ? 26  GLU A OE1 1 
ATOM   208  O  OE2 . GLU A 1 24  ? 26.476 3.476   33.308  1.00 29.30 ? 26  GLU A OE2 1 
ATOM   209  N  N   . ARG A 1 25  ? 21.586 3.921   29.784  1.00 6.22  ? 27  ARG A N   1 
ATOM   210  C  CA  . ARG A 1 25  ? 20.187 3.679   29.388  1.00 5.93  ? 27  ARG A CA  1 
ATOM   211  C  C   . ARG A 1 25  ? 20.136 3.202   27.929  1.00 4.96  ? 27  ARG A C   1 
ATOM   212  O  O   . ARG A 1 25  ? 19.435 3.790   27.096  1.00 4.65  ? 27  ARG A O   1 
ATOM   213  C  CB  . ARG A 1 25  ? 19.243 4.867   29.686  1.00 7.37  ? 27  ARG A CB  1 
ATOM   214  C  CG  . ARG A 1 25  ? 19.669 6.189   29.121  1.00 9.04  ? 27  ARG A CG  1 
ATOM   215  C  CD  . ARG A 1 25  ? 18.678 7.353   29.363  1.00 11.07 ? 27  ARG A CD  1 
ATOM   216  N  NE  . ARG A 1 25  ? 17.524 7.275   28.401  1.00 9.68  ? 27  ARG A NE  1 
ATOM   217  C  CZ  . ARG A 1 25  ? 16.579 8.189   28.369  1.00 7.89  ? 27  ARG A CZ  1 
ATOM   218  N  NH1 . ARG A 1 25  ? 16.591 9.252   29.178  1.00 11.40 ? 27  ARG A NH1 1 
ATOM   219  N  NH2 . ARG A 1 25  ? 15.605 8.050   27.530  1.00 8.53  ? 27  ARG A NH2 1 
ATOM   220  N  N   . GLN A 1 26  ? 20.833 2.103   27.639  1.00 4.43  ? 28  GLN A N   1 
ATOM   221  C  CA  . GLN A 1 26  ? 20.846 1.544   26.285  1.00 3.57  ? 28  GLN A CA  1 
ATOM   222  C  C   . GLN A 1 26  ? 19.689 0.593   26.056  1.00 3.42  ? 28  GLN A C   1 
ATOM   223  O  O   . GLN A 1 26  ? 19.187 -0.103  26.930  1.00 4.44  ? 28  GLN A O   1 
ATOM   224  C  CB  . GLN A 1 26  ? 22.181 0.862   26.055  1.00 4.86  ? 28  GLN A CB  1 
ATOM   225  C  CG  . GLN A 1 26  ? 23.330 1.913   25.965  1.00 4.80  ? 28  GLN A CG  1 
ATOM   226  C  CD  . GLN A 1 26  ? 23.194 2.699   24.674  1.00 4.62  ? 28  GLN A CD  1 
ATOM   227  O  OE1 . GLN A 1 26  ? 23.398 2.120   23.566  1.00 5.43  ? 28  GLN A OE1 1 
ATOM   228  N  NE2 . GLN A 1 26  ? 22.884 3.994   24.749  1.00 4.53  ? 28  GLN A NE2 1 
ATOM   229  N  N   . SER A 1 27  ? 19.322 0.483   24.744  1.00 3.62  ? 29  SER A N   1 
ATOM   230  C  CA  . SER A 1 27  ? 18.280 -0.386  24.285  1.00 3.41  ? 29  SER A CA  1 
ATOM   231  C  C   . SER A 1 27  ? 18.790 -1.263  23.171  1.00 3.53  ? 29  SER A C   1 
ATOM   232  O  O   . SER A 1 27  ? 19.745 -0.907  22.495  1.00 4.05  ? 29  SER A O   1 
ATOM   233  C  CB  . SER A 1 27  ? 17.109 0.467   23.714  1.00 3.54  ? 29  SER A CB  1 
ATOM   234  O  OG  . SER A 1 27  ? 16.498 1.200   24.805  1.00 3.38  ? 29  SER A OG  1 
ATOM   235  N  N   . PRO A 1 28  ? 18.143 -2.408  22.942  1.00 3.36  ? 30  PRO A N   1 
ATOM   236  C  CA  . PRO A 1 28  ? 16.988 -2.949  23.643  1.00 3.38  ? 30  PRO A CA  1 
ATOM   237  C  C   . PRO A 1 28  ? 17.381 -3.586  24.963  1.00 3.10  ? 30  PRO A C   1 
ATOM   238  O  O   . PRO A 1 28  ? 18.604 -3.623  25.308  1.00 4.03  ? 30  PRO A O   1 
ATOM   239  C  CB  . PRO A 1 28  ? 16.443 -3.981  22.644  1.00 3.57  ? 30  PRO A CB  1 
ATOM   240  C  CG  . PRO A 1 28  ? 17.763 -4.592  22.074  1.00 3.83  ? 30  PRO A CG  1 
ATOM   241  C  CD  . PRO A 1 28  ? 18.651 -3.350  21.882  1.00 3.73  ? 30  PRO A CD  1 
ATOM   242  N  N   . VAL A 1 29  ? 16.411 -4.175  25.644  1.00 3.68  ? 31  VAL A N   1 
ATOM   243  C  CA  . VAL A 1 29  ? 16.595 -4.911  26.892  1.00 4.34  ? 31  VAL A CA  1 
ATOM   244  C  C   . VAL A 1 29  ? 15.710 -6.112  26.853  1.00 4.01  ? 31  VAL A C   1 
ATOM   245  O  O   . VAL A 1 29  ? 14.727 -6.183  26.108  1.00 4.50  ? 31  VAL A O   1 
ATOM   246  C  CB  . VAL A 1 29  ? 16.283 -4.061  28.179  1.00 4.70  ? 31  VAL A CB  1 
ATOM   247  C  CG1 . VAL A 1 29  ? 17.215 -2.869  28.278  1.00 5.91  ? 31  VAL A CG1 1 
ATOM   248  C  CG2 . VAL A 1 29  ? 14.794 -3.628  28.189  1.00 6.02  ? 31  VAL A CG2 1 
ATOM   249  N  N   . ASP A 1 30  ? 16.054 -7.084  27.713  1.00 4.07  ? 32  ASP A N   1 
ATOM   250  C  CA  . ASP A 1 30  ? 15.119 -8.186  28.011  1.00 3.96  ? 32  ASP A CA  1 
ATOM   251  C  C   . ASP A 1 30  ? 14.075 -7.674  28.977  1.00 4.11  ? 32  ASP A C   1 
ATOM   252  O  O   . ASP A 1 30  ? 14.397 -7.013  30.003  1.00 6.80  ? 32  ASP A O   1 
ATOM   253  C  CB  . ASP A 1 30  ? 15.884 -9.360  28.608  1.00 6.13  ? 32  ASP A CB  1 
ATOM   254  C  CG  . ASP A 1 30  ? 14.935 -10.521 28.901  1.00 7.05  ? 32  ASP A CG  1 
ATOM   255  O  OD1 . ASP A 1 30  ? 14.224 -10.975 27.989  1.00 5.63  ? 32  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A 1 30  ? 14.890 -10.969 30.070  1.00 8.84  ? 32  ASP A OD2 1 
ATOM   257  N  N   . ILE A 1 31  ? 12.797 -7.979  28.707  1.00 4.43  ? 33  ILE A N   1 
ATOM   258  C  CA  . ILE A 1 31  ? 11.688 -7.599  29.573  1.00 4.87  ? 33  ILE A CA  1 
ATOM   259  C  C   . ILE A 1 31  ? 11.400 -8.856  30.379  1.00 5.14  ? 33  ILE A C   1 
ATOM   260  O  O   . ILE A 1 31  ? 10.875 -9.865  29.938  1.00 5.99  ? 33  ILE A O   1 
ATOM   261  C  CB  . ILE A 1 31  ? 10.484 -7.194  28.761  1.00 4.92  ? 33  ILE A CB  1 
ATOM   262  C  CG1 . ILE A 1 31  ? 10.850 -5.961  27.937  1.00 5.45  ? 33  ILE A CG1 1 
ATOM   263  C  CG2 . ILE A 1 31  ? 9.264  -6.941  29.709  1.00 7.03  ? 33  ILE A CG2 1 
ATOM   264  C  CD1 . ILE A 1 31  ? 9.779  -5.656  26.785  1.00 7.05  ? 33  ILE A CD1 1 
ATOM   265  N  N   . ASP A 1 32  ? 11.756 -8.769  31.664  1.00 6.89  ? 34  ASP A N   1 
ATOM   266  C  CA  . ASP A 1 32  ? 11.496 -9.863  32.646  1.00 7.99  ? 34  ASP A CA  1 
ATOM   267  C  C   . ASP A 1 32  ? 10.077 -9.614  33.133  1.00 7.29  ? 34  ASP A C   1 
ATOM   268  O  O   . ASP A 1 32  ? 9.819  -8.616  33.880  1.00 10.19 ? 34  ASP A O   1 
ATOM   269  C  CB  . ASP A 1 32  ? 12.571 -9.855  33.772  1.00 10.05 ? 34  ASP A CB  1 
ATOM   270  C  CG  . ASP A 1 32  ? 12.304 -10.875 34.901  1.00 13.58 ? 34  ASP A CG  1 
ATOM   271  O  OD1 . ASP A 1 32  ? 11.230 -11.194 35.202  1.00 17.20 ? 34  ASP A OD1 1 
ATOM   272  O  OD2 . ASP A 1 32  ? 13.235 -11.160 35.665  1.00 22.74 ? 34  ASP A OD2 1 
ATOM   273  N  N   . THR A 1 33  ? 9.116  -10.374 32.693  1.00 9.36  ? 35  THR A N   1 
ATOM   274  C  CA  . THR A 1 33  ? 7.713  -10.042 32.928  1.00 11.04 ? 35  THR A CA  1 
ATOM   275  C  C   . THR A 1 33  ? 7.352  -10.185 34.341  1.00 12.98 ? 35  THR A C   1 
ATOM   276  O  O   . THR A 1 33  ? 6.417  -9.529  34.801  1.00 13.52 ? 35  THR A O   1 
ATOM   277  C  CB  . THR A 1 33  ? 6.818  -10.977 32.120  1.00 12.02 ? 35  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 33  ? 6.981  -12.341 32.547  1.00 12.06 ? 35  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 33  ? 7.073  -10.901 30.614  1.00 13.15 ? 35  THR A CG2 1 
ATOM   280  N  N   A HIS A 1 34  ? 8.048  -11.013 35.063  0.50 12.63 ? 36  HIS A N   1 
ATOM   281  N  N   B HIS A 1 34  ? 8.087  -10.988 35.076  0.50 12.94 ? 36  HIS A N   1 
ATOM   282  C  CA  A HIS A 1 34  ? 7.737  -11.209 36.471  0.50 12.88 ? 36  HIS A CA  1 
ATOM   283  C  CA  B HIS A 1 34  ? 7.808  -11.191 36.513  0.50 13.16 ? 36  HIS A CA  1 
ATOM   284  C  C   A HIS A 1 34  ? 8.228  -10.072 37.332  0.50 13.31 ? 36  HIS A C   1 
ATOM   285  C  C   B HIS A 1 34  ? 8.246  -10.056 37.342  0.50 13.51 ? 36  HIS A C   1 
ATOM   286  O  O   A HIS A 1 34  ? 7.554  -9.787  38.304  0.50 16.34 ? 36  HIS A O   1 
ATOM   287  O  O   B HIS A 1 34  ? 7.593  -9.783  38.321  0.50 16.33 ? 36  HIS A O   1 
ATOM   288  C  CB  A HIS A 1 34  ? 8.189  -12.619 36.906  0.50 13.43 ? 36  HIS A CB  1 
ATOM   289  C  CB  B HIS A 1 34  ? 8.459  -12.474 37.004  0.50 14.75 ? 36  HIS A CB  1 
ATOM   290  C  CG  A HIS A 1 34  ? 7.199  -13.671 36.475  0.50 14.62 ? 36  HIS A CG  1 
ATOM   291  C  CG  B HIS A 1 34  ? 7.960  -13.652 36.249  0.50 17.78 ? 36  HIS A CG  1 
ATOM   292  N  ND1 A HIS A 1 34  ? 7.444  -14.615 35.486  0.50 17.60 ? 36  HIS A ND1 1 
ATOM   293  N  ND1 B HIS A 1 34  ? 6.664  -14.110 36.362  0.50 25.03 ? 36  HIS A ND1 1 
ATOM   294  C  CD2 A HIS A 1 34  ? 5.893  -13.808 36.819  0.50 12.75 ? 36  HIS A CD2 1 
ATOM   295  C  CD2 B HIS A 1 34  ? 8.527  -14.350 35.240  0.50 19.08 ? 36  HIS A CD2 1 
ATOM   296  C  CE1 A HIS A 1 34  ? 6.346  -15.323 35.295  0.50 21.17 ? 36  HIS A CE1 1 
ATOM   297  C  CE1 B HIS A 1 34  ? 6.497  -15.109 35.514  0.50 26.11 ? 36  HIS A CE1 1 
ATOM   298  N  NE2 A HIS A 1 34  ? 5.400  -14.871 36.113  0.50 20.27 ? 36  HIS A NE2 1 
ATOM   299  N  NE2 B HIS A 1 34  ? 7.605  -15.253 34.814  0.50 25.97 ? 36  HIS A NE2 1 
ATOM   300  N  N   . THR A 1 35  ? 9.288  -9.339  36.912  1.00 13.13 ? 37  THR A N   1 
ATOM   301  C  CA  . THR A 1 35  ? 9.856  -8.185  37.630  1.00 15.63 ? 37  THR A CA  1 
ATOM   302  C  C   . THR A 1 35  ? 9.321  -6.823  37.211  1.00 11.42 ? 37  THR A C   1 
ATOM   303  O  O   . THR A 1 35  ? 9.456  -5.831  37.943  1.00 15.14 ? 37  THR A O   1 
ATOM   304  C  CB  . THR A 1 35  ? 11.379 -8.106  37.625  1.00 23.71 ? 37  THR A CB  1 
ATOM   305  O  OG1 . THR A 1 35  ? 11.851 -8.121  36.327  1.00 34.27 ? 37  THR A OG1 1 
ATOM   306  C  CG2 . THR A 1 35  ? 11.868 -9.338  38.183  1.00 21.33 ? 37  THR A CG2 1 
ATOM   307  N  N   . ALA A 1 36  ? 8.731  -6.763  36.029  1.00 10.89 ? 38  ALA A N   1 
ATOM   308  C  CA  . ALA A 1 36  ? 8.101  -5.505  35.573  1.00 10.61 ? 38  ALA A CA  1 
ATOM   309  C  C   . ALA A 1 36  ? 7.005  -5.185  36.519  1.00 14.90 ? 38  ALA A C   1 
ATOM   310  O  O   . ALA A 1 36  ? 6.278  -6.100  36.920  1.00 21.37 ? 38  ALA A O   1 
ATOM   311  C  CB  . ALA A 1 36  ? 7.572  -5.684  34.162  1.00 10.81 ? 38  ALA A CB  1 
ATOM   312  N  N   . LYS A 1 37  ? 6.913  -3.988  37.001  1.00 13.31 ? 39  LYS A N   1 
ATOM   313  C  CA  . LYS A 1 37  ? 5.798  -3.728  37.997  1.00 18.33 ? 39  LYS A CA  1 
ATOM   314  C  C   . LYS A 1 37  ? 4.641  -3.047  37.347  1.00 12.15 ? 39  LYS A C   1 
ATOM   315  O  O   . LYS A 1 37  ? 4.800  -2.065  36.582  1.00 10.51 ? 39  LYS A O   1 
ATOM   316  C  CB  . LYS A 1 37  ? 6.217  -2.884  39.105  1.00 25.49 ? 39  LYS A CB  1 
ATOM   317  C  CG  . LYS A 1 37  ? 5.312  -2.966  40.329  1.00 25.93 ? 39  LYS A CG  1 
ATOM   318  C  CD  . LYS A 1 37  ? 5.941  -2.115  41.419  1.00 23.61 ? 39  LYS A CD  1 
ATOM   319  C  CE  . LYS A 1 37  ? 4.877  -1.406  42.216  1.00 28.27 ? 39  LYS A CE  1 
ATOM   320  N  NZ  . LYS A 1 37  ? 4.822  -2.246  43.421  1.00 31.86 ? 39  LYS A NZ  1 
ATOM   321  N  N   . TYR A 1 38  ? 3.445  -3.508  37.628  1.00 14.44 ? 40  TYR A N   1 
ATOM   322  C  CA  . TYR A 1 38  ? 2.298  -2.865  37.218  1.00 12.85 ? 40  TYR A CA  1 
ATOM   323  C  C   . TYR A 1 38  ? 2.240  -1.507  37.832  1.00 12.58 ? 40  TYR A C   1 
ATOM   324  O  O   . TYR A 1 38  ? 2.409  -1.304  39.077  1.00 13.81 ? 40  TYR A O   1 
ATOM   325  C  CB  . TYR A 1 38  ? 1.068  -3.694  37.657  1.00 16.90 ? 40  TYR A CB  1 
ATOM   326  C  CG  . TYR A 1 38  ? -0.190 -2.955  37.515  1.00 19.07 ? 40  TYR A CG  1 
ATOM   327  C  CD1 . TYR A 1 38  ? -0.626 -2.524  36.254  1.00 18.94 ? 40  TYR A CD1 1 
ATOM   328  C  CD2 . TYR A 1 38  ? -1.040 -2.709  38.613  1.00 22.50 ? 40  TYR A CD2 1 
ATOM   329  C  CE1 . TYR A 1 38  ? -1.869 -1.892  36.059  1.00 24.00 ? 40  TYR A CE1 1 
ATOM   330  C  CE2 . TYR A 1 38  ? -2.254 -2.051  38.393  1.00 25.01 ? 40  TYR A CE2 1 
ATOM   331  C  CZ  . TYR A 1 38  ? -2.650 -1.589  37.154  1.00 25.47 ? 40  TYR A CZ  1 
ATOM   332  O  OH  . TYR A 1 38  ? -3.890 -0.967  37.004  1.00 32.21 ? 40  TYR A OH  1 
ATOM   333  N  N   . ASP A 1 39  ? 1.989  -0.513  37.027  1.00 10.98 ? 41  ASP A N   1 
ATOM   334  C  CA  . ASP A 1 39  ? 1.941  0.907   37.500  1.00 11.44 ? 41  ASP A CA  1 
ATOM   335  C  C   . ASP A 1 39  ? 0.548  1.407   37.243  1.00 14.78 ? 41  ASP A C   1 
ATOM   336  O  O   . ASP A 1 39  ? 0.223  1.744   36.065  1.00 14.95 ? 41  ASP A O   1 
ATOM   337  C  CB  . ASP A 1 39  ? 2.983  1.780   36.840  1.00 12.68 ? 41  ASP A CB  1 
ATOM   338  C  CG  . ASP A 1 39  ? 3.008  3.145   37.322  1.00 17.27 ? 41  ASP A CG  1 
ATOM   339  O  OD1 . ASP A 1 39  ? 2.070  3.563   38.084  1.00 17.64 ? 41  ASP A OD1 1 
ATOM   340  O  OD2 . ASP A 1 39  ? 4.003  3.853   36.970  1.00 20.58 ? 41  ASP A OD2 1 
ATOM   341  N  N   . PRO A 1 40  ? -0.298 1.448   38.273  1.00 18.05 ? 42  PRO A N   1 
ATOM   342  C  CA  . PRO A 1 40  ? -1.697 1.839   38.014  1.00 21.25 ? 42  PRO A CA  1 
ATOM   343  C  C   . PRO A 1 40  ? -1.792 3.337   37.625  1.00 24.04 ? 42  PRO A C   1 
ATOM   344  O  O   . PRO A 1 40  ? -2.860 3.788   37.225  1.00 33.17 ? 42  PRO A O   1 
ATOM   345  C  CB  . PRO A 1 40  ? -2.385 1.583   39.384  1.00 24.24 ? 42  PRO A CB  1 
ATOM   346  C  CG  . PRO A 1 40  ? -1.314 1.873   40.290  1.00 23.76 ? 42  PRO A CG  1 
ATOM   347  C  CD  . PRO A 1 40  ? -0.096 1.101   39.700  1.00 20.19 ? 42  PRO A CD  1 
ATOM   348  N  N   . SER A 1 41  ? -0.716 4.123   37.787  1.00 18.54 ? 43  SER A N   1 
ATOM   349  C  CA  . SER A 1 41  ? -0.694 5.574   37.400  1.00 22.84 ? 43  SER A CA  1 
ATOM   350  C  C   . SER A 1 41  ? -0.485 5.718   35.874  1.00 21.01 ? 43  SER A C   1 
ATOM   351  O  O   . SER A 1 41  ? -0.742 6.797   35.285  1.00 27.46 ? 43  SER A O   1 
ATOM   352  C  CB  . SER A 1 41  ? 0.410  6.347   38.125  1.00 23.42 ? 43  SER A CB  1 
ATOM   353  O  OG  . SER A 1 41  ? 1.733  6.194   37.606  1.00 26.11 ? 43  SER A OG  1 
ATOM   354  N  N   . LEU A 1 42  ? -0.084 4.646   35.153  1.00 20.40 ? 44  LEU A N   1 
ATOM   355  C  CA  . LEU A 1 42  ? 0.148  4.664   33.688  1.00 16.35 ? 44  LEU A CA  1 
ATOM   356  C  C   . LEU A 1 42  ? -1.228 4.802   32.998  1.00 16.71 ? 44  LEU A C   1 
ATOM   357  O  O   . LEU A 1 42  ? -2.185 4.268   33.399  1.00 22.87 ? 44  LEU A O   1 
ATOM   358  C  CB  . LEU A 1 42  ? 0.828  3.425   33.163  1.00 14.47 ? 44  LEU A CB  1 
ATOM   359  C  CG  . LEU A 1 42  ? 2.290  3.426   33.408  1.00 11.25 ? 44  LEU A CG  1 
ATOM   360  C  CD1 . LEU A 1 42  ? 2.747  2.025   33.075  1.00 12.24 ? 44  LEU A CD1 1 
ATOM   361  C  CD2 . LEU A 1 42  ? 3.091  4.502   32.671  1.00 12.55 ? 44  LEU A CD2 1 
ATOM   362  N  N   . LYS A 1 43  ? -1.313 5.572   31.953  1.00 15.69 ? 45  LYS A N   1 
ATOM   363  C  CA  . LYS A 1 43  ? -2.597 5.812   31.200  1.00 16.62 ? 45  LYS A CA  1 
ATOM   364  C  C   . LYS A 1 43  ? -2.669 4.946   30.017  1.00 13.15 ? 45  LYS A C   1 
ATOM   365  O  O   . LYS A 1 43  ? -1.630 4.426   29.567  1.00 15.72 ? 45  LYS A O   1 
ATOM   366  C  CB  . LYS A 1 43  ? -2.657 7.184   30.767  1.00 16.58 ? 45  LYS A CB  1 
ATOM   367  C  CG  . LYS A 1 43  ? -2.516 8.239   31.838  1.00 21.45 ? 45  LYS A CG  1 
ATOM   368  C  CD  . LYS A 1 43  ? -2.411 9.615   31.199  1.00 26.22 ? 45  LYS A CD  1 
ATOM   369  N  N   . PRO A 1 44  ? -3.897 4.699   29.494  1.00 12.89 ? 46  PRO A N   1 
ATOM   370  C  CA  . PRO A 1 44  ? -3.986 3.996   28.214  1.00 13.58 ? 46  PRO A CA  1 
ATOM   371  C  C   . PRO A 1 44  ? -3.154 4.767   27.174  1.00 11.15 ? 46  PRO A C   1 
ATOM   372  O  O   . PRO A 1 44  ? -3.072 5.973   27.251  1.00 11.65 ? 46  PRO A O   1 
ATOM   373  C  CB  . PRO A 1 44  ? -5.479 4.148   27.870  1.00 14.58 ? 46  PRO A CB  1 
ATOM   374  C  CG  . PRO A 1 44  ? -6.191 4.293   29.177  1.00 18.94 ? 46  PRO A CG  1 
ATOM   375  C  CD  . PRO A 1 44  ? -5.196 5.003   30.111  1.00 17.35 ? 46  PRO A CD  1 
ATOM   376  N  N   . LEU A 1 45  ? -2.529 4.076   26.258  1.00 13.18 ? 47  LEU A N   1 
ATOM   377  C  CA  . LEU A 1 45  ? -1.849 4.768   25.250  1.00 11.40 ? 47  LEU A CA  1 
ATOM   378  C  C   . LEU A 1 45  ? -2.928 5.328   24.220  1.00 14.25 ? 47  LEU A C   1 
ATOM   379  O  O   . LEU A 1 45  ? -3.911 4.628   23.905  1.00 16.29 ? 47  LEU A O   1 
ATOM   380  C  CB  . LEU A 1 45  ? -1.033 3.709   24.502  1.00 16.85 ? 47  LEU A CB  1 
ATOM   381  C  CG  . LEU A 1 45  ? -0.041 4.053   23.582  1.00 17.99 ? 47  LEU A CG  1 
ATOM   382  C  CD1 . LEU A 1 45  ? 1.022  4.925   24.329  1.00 18.46 ? 47  LEU A CD1 1 
ATOM   383  C  CD2 . LEU A 1 45  ? 0.545  2.772   22.945  1.00 18.44 ? 47  LEU A CD2 1 
ATOM   384  N  N   . SER A 1 46  ? -2.642 6.525   23.715  1.00 9.78  ? 48  SER A N   1 
ATOM   385  C  CA  . SER A 1 46  ? -3.478 7.112   22.699  1.00 9.27  ? 48  SER A CA  1 
ATOM   386  C  C   . SER A 1 46  ? -2.715 7.140   21.393  1.00 9.48  ? 48  SER A C   1 
ATOM   387  O  O   . SER A 1 46  ? -1.700 7.861   21.245  1.00 9.67  ? 48  SER A O   1 
ATOM   388  C  CB  . SER A 1 46  ? -3.792 8.567   23.144  1.00 13.10 ? 48  SER A CB  1 
ATOM   389  O  OG  . SER A 1 46  ? -4.451 9.253   22.113  1.00 15.41 ? 48  SER A OG  1 
ATOM   390  N  N   . VAL A 1 47  ? -3.118 6.321   20.438  1.00 10.35 ? 49  VAL A N   1 
ATOM   391  C  CA  . VAL A 1 47  ? -2.506 6.262   19.135  1.00 11.25 ? 49  VAL A CA  1 
ATOM   392  C  C   . VAL A 1 47  ? -3.551 6.872   18.160  1.00 12.56 ? 49  VAL A C   1 
ATOM   393  O  O   . VAL A 1 47  ? -4.616 6.325   18.006  1.00 15.78 ? 49  VAL A O   1 
ATOM   394  C  CB  . VAL A 1 47  ? -2.265 4.753   18.790  1.00 13.62 ? 49  VAL A CB  1 
ATOM   395  C  CG1 . VAL A 1 47  ? -1.553 4.675   17.418  1.00 20.45 ? 49  VAL A CG1 1 
ATOM   396  C  CG2 . VAL A 1 47  ? -1.450 4.108   19.914  1.00 15.78 ? 49  VAL A CG2 1 
ATOM   397  N  N   . SER A 1 48  ? -3.212 8.001   17.548  1.00 12.83 ? 50  SER A N   1 
ATOM   398  C  CA  . SER A 1 48  ? -4.099 8.678   16.652  1.00 14.26 ? 50  SER A CA  1 
ATOM   399  C  C   . SER A 1 48  ? -3.475 8.764   15.286  1.00 13.41 ? 50  SER A C   1 
ATOM   400  O  O   . SER A 1 48  ? -2.774 9.725   15.002  1.00 14.07 ? 50  SER A O   1 
ATOM   401  C  CB  . SER A 1 48  ? -4.524 10.089  17.164  1.00 17.73 ? 50  SER A CB  1 
ATOM   402  O  OG  . SER A 1 48  ? -5.163 9.950   18.444  1.00 23.90 ? 50  SER A OG  1 
ATOM   403  N  N   . TYR A 1 49  ? -3.743 7.753   14.447  1.00 12.91 ? 51  TYR A N   1 
ATOM   404  C  CA  . TYR A 1 49  ? -3.137 7.628   13.146  1.00 13.19 ? 51  TYR A CA  1 
ATOM   405  C  C   . TYR A 1 49  ? -4.089 7.837   11.973  1.00 14.71 ? 51  TYR A C   1 
ATOM   406  O  O   . TYR A 1 49  ? -3.637 7.656   10.853  1.00 17.00 ? 51  TYR A O   1 
ATOM   407  C  CB  . TYR A 1 49  ? -2.450 6.256   12.964  1.00 11.08 ? 51  TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 49  ? -1.193 5.992   13.803  1.00 9.08  ? 51  TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 49  ? -0.514 7.002   14.464  1.00 11.15 ? 51  TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 49  ? -0.694 4.681   13.886  1.00 8.81  ? 51  TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 49  ? 0.702  6.710   15.157  1.00 8.48  ? 51  TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 49  ? 0.456  4.357   14.560  1.00 7.72  ? 51  TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 49  ? 1.170  5.398   15.170  1.00 7.53  ? 51  TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 49  ? 2.303  5.038   15.842  1.00 7.68  ? 51  TYR A OH  1 
ATOM   415  N  N   . ASP A 1 50  ? -5.307 8.293   12.262  1.00 15.31 ? 52  ASP A N   1 
ATOM   416  C  CA  . ASP A 1 50  ? -6.316 8.540   11.236  1.00 17.63 ? 52  ASP A CA  1 
ATOM   417  C  C   . ASP A 1 50  ? -5.848 9.482   10.106  1.00 19.87 ? 52  ASP A C   1 
ATOM   418  O  O   . ASP A 1 50  ? -6.166 9.274   8.903   1.00 22.58 ? 52  ASP A O   1 
ATOM   419  C  CB  . ASP A 1 50  ? -7.610 8.986   11.902  1.00 23.06 ? 52  ASP A CB  1 
ATOM   420  C  CG  . ASP A 1 50  ? -7.379 9.956   13.040  1.00 34.16 ? 52  ASP A CG  1 
ATOM   421  O  OD1 . ASP A 1 50  ? -6.755 9.590   14.096  1.00 44.92 ? 52  ASP A OD1 1 
ATOM   422  O  OD2 . ASP A 1 50  ? -7.836 11.107  12.866  1.00 49.79 ? 52  ASP A OD2 1 
ATOM   423  N  N   . GLN A 1 51  ? -5.120 10.518  10.473  1.00 20.14 ? 53  GLN A N   1 
ATOM   424  C  CA  . GLN A 1 51  ? -4.691 11.413  9.355   1.00 19.01 ? 53  GLN A CA  1 
ATOM   425  C  C   . GLN A 1 51  ? -3.201 11.248  8.920   1.00 14.16 ? 53  GLN A C   1 
ATOM   426  O  O   . GLN A 1 51  ? -2.641 12.160  8.361   1.00 16.98 ? 53  GLN A O   1 
ATOM   427  C  CB  . GLN A 1 51  ? -4.933 12.886  9.770   1.00 26.86 ? 53  GLN A CB  1 
ATOM   428  C  CG  . GLN A 1 51  ? -6.427 13.286  10.022  1.00 38.97 ? 53  GLN A CG  1 
ATOM   429  C  CD  . GLN A 1 51  ? -7.228 13.245  8.753   1.00 54.49 ? 53  GLN A CD  1 
ATOM   430  O  OE1 . GLN A 1 51  ? -6.678 13.355  7.604   1.00 65.49 ? 53  GLN A OE1 1 
ATOM   431  N  NE2 . GLN A 1 51  ? -8.533 13.042  8.930   1.00 60.23 ? 53  GLN A NE2 1 
ATOM   432  N  N   . ALA A 1 52  ? -2.598 10.104  9.196   1.00 13.29 ? 54  ALA A N   1 
ATOM   433  C  CA  . ALA A 1 52  ? -1.236 9.865   8.840   1.00 10.19 ? 54  ALA A CA  1 
ATOM   434  C  C   . ALA A 1 52  ? -1.068 9.911   7.352   1.00 13.24 ? 54  ALA A C   1 
ATOM   435  O  O   . ALA A 1 52  ? -1.958 9.440   6.593   1.00 20.61 ? 54  ALA A O   1 
ATOM   436  C  CB  . ALA A 1 52  ? -0.833 8.442   9.306   1.00 13.90 ? 54  ALA A CB  1 
ATOM   437  N  N   A THR A 1 53  ? 0.011  10.625  6.923   0.50 11.94 ? 55  THR A N   1 
ATOM   438  N  N   B THR A 1 53  ? 0.032  10.524  6.890   0.50 12.32 ? 55  THR A N   1 
ATOM   439  C  CA  A THR A 1 53  ? 0.369  10.832  5.486   0.50 12.92 ? 55  THR A CA  1 
ATOM   440  C  CA  B THR A 1 53  ? 0.225  10.623  5.441   0.50 13.69 ? 55  THR A CA  1 
ATOM   441  C  C   A THR A 1 53  ? 1.713  10.137  5.227   0.50 9.90  ? 55  THR A C   1 
ATOM   442  C  C   B THR A 1 53  ? 1.626  10.145  5.167   0.50 10.31 ? 55  THR A C   1 
ATOM   443  O  O   A THR A 1 53  ? 2.778  10.749  5.464   0.50 9.41  ? 55  THR A O   1 
ATOM   444  O  O   B THR A 1 53  ? 2.610  10.798  5.538   0.50 10.33 ? 55  THR A O   1 
ATOM   445  C  CB  A THR A 1 53  ? 0.538  12.356  5.074   0.50 13.41 ? 55  THR A CB  1 
ATOM   446  C  CB  B THR A 1 53  ? -0.048 12.040  4.932   0.50 19.66 ? 55  THR A CB  1 
ATOM   447  O  OG1 A THR A 1 53  ? -0.676 13.087  5.286   0.50 17.19 ? 55  THR A OG1 1 
ATOM   448  O  OG1 B THR A 1 53  ? 0.856  12.943  5.567   0.50 27.37 ? 55  THR A OG1 1 
ATOM   449  C  CG2 A THR A 1 53  ? 0.962  12.585  3.526   0.50 18.06 ? 55  THR A CG2 1 
ATOM   450  C  CG2 B THR A 1 53  ? -1.390 12.374  5.325   0.50 25.23 ? 55  THR A CG2 1 
ATOM   451  N  N   . SER A 1 54  ? 1.691  8.934   4.673   1.00 10.47 ? 56  SER A N   1 
ATOM   452  C  CA  . SER A 1 54  ? 3.010  8.324   4.341   1.00 11.19 ? 56  SER A CA  1 
ATOM   453  C  C   . SER A 1 54  ? 3.480  8.997   3.053   1.00 13.24 ? 56  SER A C   1 
ATOM   454  O  O   . SER A 1 54  ? 2.635  9.448   2.242   1.00 14.99 ? 56  SER A O   1 
ATOM   455  C  CB  . SER A 1 54  ? 2.990  6.815   4.142   1.00 11.55 ? 56  SER A CB  1 
ATOM   456  O  OG  . SER A 1 54  ? 2.132  6.452   3.048   1.00 12.63 ? 56  SER A OG  1 
ATOM   457  N  N   . LEU A 1 55  ? 4.784  9.054   2.798   1.00 12.68 ? 57  LEU A N   1 
ATOM   458  C  CA  . LEU A 1 55  ? 5.313  9.669   1.556   1.00 16.66 ? 57  LEU A CA  1 
ATOM   459  C  C   . LEU A 1 55  ? 6.114  8.729   0.784   1.00 12.51 ? 57  LEU A C   1 
ATOM   460  O  O   . LEU A 1 55  ? 6.061  8.729   -0.472  1.00 15.74 ? 57  LEU A O   1 
ATOM   461  C  CB  . LEU A 1 55  ? 6.222  10.804  2.009   1.00 19.72 ? 57  LEU A CB  1 
ATOM   462  C  CG  . LEU A 1 55  ? 5.513  12.081  2.628   1.00 26.15 ? 57  LEU A CG  1 
ATOM   463  C  CD1 . LEU A 1 55  ? 6.502  13.102  3.271   1.00 29.90 ? 57  LEU A CD1 1 
ATOM   464  C  CD2 . LEU A 1 55  ? 4.690  12.785  1.506   1.00 35.42 ? 57  LEU A CD2 1 
ATOM   465  N  N   . ARG A 1 56  ? 7.014  7.948   1.437   1.00 13.10 ? 58  ARG A N   1 
ATOM   466  C  CA  . ARG A 1 56  ? 8.011  7.234   0.679   1.00 10.58 ? 58  ARG A CA  1 
ATOM   467  C  C   . ARG A 1 56  ? 8.554  6.069   1.479   1.00 9.64  ? 58  ARG A C   1 
ATOM   468  O  O   . ARG A 1 56  ? 8.441  6.076   2.700   1.00 10.65 ? 58  ARG A O   1 
ATOM   469  C  CB  . ARG A 1 56  ? 9.165  8.220   0.475   1.00 11.73 ? 58  ARG A CB  1 
ATOM   470  C  CG  . ARG A 1 56  ? 10.187 7.739   -0.538  1.00 13.91 ? 58  ARG A CG  1 
ATOM   471  C  CD  . ARG A 1 56  ? 11.274 8.790   -0.752  1.00 13.63 ? 58  ARG A CD  1 
ATOM   472  N  NE  . ARG A 1 56  ? 12.105 8.924   0.466   1.00 11.79 ? 58  ARG A NE  1 
ATOM   473  C  CZ  . ARG A 1 56  ? 13.414 9.100   0.464   1.00 10.56 ? 58  ARG A CZ  1 
ATOM   474  N  NH1 . ARG A 1 56  ? 14.083 9.338   -0.694  1.00 12.74 ? 58  ARG A NH1 1 
ATOM   475  N  NH2 . ARG A 1 56  ? 14.061 9.175   1.610   1.00 11.96 ? 58  ARG A NH2 1 
ATOM   476  N  N   . ILE A 1 57  ? 9.180  5.116   0.786   1.00 10.20 ? 59  ILE A N   1 
ATOM   477  C  CA  . ILE A 1 57  ? 9.813  4.011   1.442   1.00 8.12  ? 59  ILE A CA  1 
ATOM   478  C  C   . ILE A 1 57  ? 11.229 3.983   0.991   1.00 7.87  ? 59  ILE A C   1 
ATOM   479  O  O   . ILE A 1 57  ? 11.527 4.174   -0.201  1.00 11.03 ? 59  ILE A O   1 
ATOM   480  C  CB  . ILE A 1 57  ? 9.049  2.660   1.255   1.00 8.06  ? 59  ILE A CB  1 
ATOM   481  C  CG1 . ILE A 1 57  ? 9.608  1.554   2.154   1.00 9.10  ? 59  ILE A CG1 1 
ATOM   482  C  CG2 . ILE A 1 57  ? 9.058  2.230   -0.262  1.00 10.27 ? 59  ILE A CG2 1 
ATOM   483  C  CD1 . ILE A 1 57  ? 8.834  0.281   2.010   1.00 10.45 ? 59  ILE A CD1 1 
ATOM   484  N  N   . LEU A 1 58  ? 12.190 3.763   1.886   1.00 8.65  ? 60  LEU A N   1 
ATOM   485  C  CA  . LEU A 1 58  ? 13.569 3.911   1.586   1.00 8.24  ? 60  LEU A CA  1 
ATOM   486  C  C   . LEU A 1 58  ? 14.374 2.724   2.122   1.00 8.45  ? 60  LEU A C   1 
ATOM   487  O  O   . LEU A 1 58  ? 14.210 2.356   3.327   1.00 7.84  ? 60  LEU A O   1 
ATOM   488  C  CB  . LEU A 1 58  ? 14.096 5.211   2.315   1.00 10.38 ? 60  LEU A CB  1 
ATOM   489  C  CG  . LEU A 1 58  ? 15.624 5.341   2.254   1.00 9.51  ? 60  LEU A CG  1 
ATOM   490  C  CD1 . LEU A 1 58  ? 16.151 5.639   0.790   1.00 11.50 ? 60  LEU A CD1 1 
ATOM   491  C  CD2 . LEU A 1 58  ? 16.175 6.454   3.212   1.00 11.69 ? 60  LEU A CD2 1 
ATOM   492  N  N   . ASN A 1 59  ? 15.270 2.113   1.366   1.00 8.54  ? 61  ASN A N   1 
ATOM   493  C  CA  . ASN A 1 59  ? 16.230 1.121   1.864   1.00 8.23  ? 61  ASN A CA  1 
ATOM   494  C  C   . ASN A 1 59  ? 17.427 1.976   2.241   1.00 9.42  ? 61  ASN A C   1 
ATOM   495  O  O   . ASN A 1 59  ? 18.065 2.532   1.348   1.00 10.67 ? 61  ASN A O   1 
ATOM   496  C  CB  . ASN A 1 59  ? 16.554 0.130   0.790   1.00 10.06 ? 61  ASN A CB  1 
ATOM   497  C  CG  . ASN A 1 59  ? 17.624 -0.879  1.194   1.00 8.52  ? 61  ASN A CG  1 
ATOM   498  O  OD1 . ASN A 1 59  ? 18.491 -0.594  2.066   1.00 10.14 ? 61  ASN A OD1 1 
ATOM   499  N  ND2 . ASN A 1 59  ? 17.570 -2.090  0.623   1.00 10.07 ? 61  ASN A ND2 1 
ATOM   500  N  N   . ASN A 1 60  ? 17.733 2.041   3.538   1.00 9.38  ? 62  ASN A N   1 
ATOM   501  C  CA  . ASN A 1 60  ? 18.829 2.876   4.033   1.00 11.33 ? 62  ASN A CA  1 
ATOM   502  C  C   . ASN A 1 60  ? 20.123 2.090   4.272   1.00 11.72 ? 62  ASN A C   1 
ATOM   503  O  O   . ASN A 1 60  ? 21.144 2.620   4.854   1.00 17.04 ? 62  ASN A O   1 
ATOM   504  C  CB  . ASN A 1 60  ? 18.395 3.712   5.234   1.00 13.07 ? 62  ASN A CB  1 
ATOM   505  C  CG  . ASN A 1 60  ? 18.170 2.791   6.401   1.00 11.60 ? 62  ASN A CG  1 
ATOM   506  O  OD1 . ASN A 1 60  ? 18.593 1.613   6.470   1.00 10.32 ? 62  ASN A OD1 1 
ATOM   507  N  ND2 . ASN A 1 60  ? 17.531 3.343   7.350   1.00 20.66 ? 62  ASN A ND2 1 
ATOM   508  N  N   . GLY A 1 61  ? 20.154 0.813   3.826   1.00 12.13 ? 63  GLY A N   1 
ATOM   509  C  CA  . GLY A 1 61  ? 21.298 0.051   3.970   1.00 10.58 ? 63  GLY A CA  1 
ATOM   510  C  C   . GLY A 1 61  ? 21.345 -0.779  5.254   1.00 9.22  ? 63  GLY A C   1 
ATOM   511  O  O   . GLY A 1 61  ? 22.221 -1.641  5.439   1.00 11.53 ? 63  GLY A O   1 
ATOM   512  N  N   A HIS A 1 62  ? 20.462 -0.458  6.196   0.50 8.76  ? 64  HIS A N   1 
ATOM   513  N  N   B HIS A 1 62  ? 20.405 -0.565  6.147   0.50 9.09  ? 64  HIS A N   1 
ATOM   514  C  CA  A HIS A 1 62  ? 20.350 -1.150  7.528   0.50 8.21  ? 64  HIS A CA  1 
ATOM   515  C  CA  B HIS A 1 62  ? 20.383 -1.433  7.333   0.50 11.60 ? 64  HIS A CA  1 
ATOM   516  C  C   A HIS A 1 62  ? 18.986 -1.843  7.609   0.50 7.39  ? 64  HIS A C   1 
ATOM   517  C  C   B HIS A 1 62  ? 18.957 -1.839  7.696   0.50 9.24  ? 64  HIS A C   1 
ATOM   518  O  O   A HIS A 1 62  ? 18.886 -3.007  8.052   0.50 11.94 ? 64  HIS A O   1 
ATOM   519  O  O   B HIS A 1 62  ? 18.784 -2.759  8.507   0.50 16.71 ? 64  HIS A O   1 
ATOM   520  C  CB  A HIS A 1 62  ? 20.556 -0.168  8.658   0.50 7.87  ? 64  HIS A CB  1 
ATOM   521  C  CB  B HIS A 1 62  ? 21.150 -0.792  8.463   0.50 13.04 ? 64  HIS A CB  1 
ATOM   522  C  CG  A HIS A 1 62  ? 21.808 0.614   8.495   0.50 10.11 ? 64  HIS A CG  1 
ATOM   523  C  CG  B HIS A 1 62  ? 20.535 0.461   8.966   0.50 13.81 ? 64  HIS A CG  1 
ATOM   524  N  ND1 A HIS A 1 62  ? 23.053 -0.001  8.554   0.50 13.04 ? 64  HIS A ND1 1 
ATOM   525  N  ND1 B HIS A 1 62  ? 20.881 1.753   8.573   0.50 13.39 ? 64  HIS A ND1 1 
ATOM   526  C  CD2 A HIS A 1 62  ? 22.056 1.937   8.312   0.50 11.35 ? 64  HIS A CD2 1 
ATOM   527  C  CD2 B HIS A 1 62  ? 19.587 0.580   9.911   0.50 13.74 ? 64  HIS A CD2 1 
ATOM   528  C  CE1 A HIS A 1 62  ? 24.006 0.881   8.371   0.50 12.65 ? 64  HIS A CE1 1 
ATOM   529  C  CE1 B HIS A 1 62  ? 20.098 2.604   9.247   0.50 12.80 ? 64  HIS A CE1 1 
ATOM   530  N  NE2 A HIS A 1 62  ? 23.436 2.062   8.134   0.50 14.36 ? 64  HIS A NE2 1 
ATOM   531  N  NE2 B HIS A 1 62  ? 19.287 1.891   10.056  0.50 14.20 ? 64  HIS A NE2 1 
ATOM   532  N  N   . ALA A 1 63  ? 17.960 -1.155  7.156   1.00 7.41  ? 65  ALA A N   1 
ATOM   533  C  CA  . ALA A 1 63  ? 16.563 -1.556  7.188   1.00 7.85  ? 65  ALA A CA  1 
ATOM   534  C  C   . ALA A 1 63  ? 15.831 -0.863  6.055   1.00 6.52  ? 65  ALA A C   1 
ATOM   535  O  O   . ALA A 1 63  ? 16.511 -0.219  5.205   1.00 8.90  ? 65  ALA A O   1 
ATOM   536  C  CB  . ALA A 1 63  ? 15.942 -1.241  8.588   1.00 9.20  ? 65  ALA A CB  1 
ATOM   537  N  N   . PHE A 1 64  ? 14.516 -0.845  6.112   1.00 6.74  ? 66  PHE A N   1 
ATOM   538  C  CA  . PHE A 1 64  ? 13.758 0.105   5.268   1.00 7.60  ? 66  PHE A CA  1 
ATOM   539  C  C   . PHE A 1 64  ? 12.874 0.956   6.113   1.00 7.23  ? 66  PHE A C   1 
ATOM   540  O  O   . PHE A 1 64  ? 12.281 0.493   7.110   1.00 7.46  ? 66  PHE A O   1 
ATOM   541  C  CB  . PHE A 1 64  ? 12.965 -0.631  4.135   1.00 9.15  ? 66  PHE A CB  1 
ATOM   542  C  CG  . PHE A 1 64  ? 11.875 -1.546  4.671   1.00 7.23  ? 66  PHE A CG  1 
ATOM   543  C  CD1 . PHE A 1 64  ? 10.620 -1.075  4.978   1.00 7.74  ? 66  PHE A CD1 1 
ATOM   544  C  CD2 . PHE A 1 64  ? 12.162 -2.914  4.852   1.00 7.82  ? 66  PHE A CD2 1 
ATOM   545  C  CE1 . PHE A 1 64  ? 9.664  -1.915  5.516   1.00 7.57  ? 66  PHE A CE1 1 
ATOM   546  C  CE2 . PHE A 1 64  ? 11.166 -3.798  5.369   1.00 8.02  ? 66  PHE A CE2 1 
ATOM   547  C  CZ  . PHE A 1 64  ? 9.906  -3.284  5.624   1.00 7.81  ? 66  PHE A CZ  1 
ATOM   548  N  N   . ASN A 1 65  ? 12.758 2.235   5.750   1.00 6.24  ? 67  ASN A N   1 
ATOM   549  C  CA  . ASN A 1 65  ? 11.942 3.200   6.512   1.00 6.85  ? 67  ASN A CA  1 
ATOM   550  C  C   . ASN A 1 65  ? 10.754 3.503   5.682   1.00 5.93  ? 67  ASN A C   1 
ATOM   551  O  O   . ASN A 1 65  ? 10.885 3.886   4.474   1.00 8.80  ? 67  ASN A O   1 
ATOM   552  C  CB  . ASN A 1 65  ? 12.642 4.512   6.815   1.00 7.94  ? 67  ASN A CB  1 
ATOM   553  C  CG  . ASN A 1 65  ? 13.806 4.321   7.721   1.00 7.60  ? 67  ASN A CG  1 
ATOM   554  O  OD1 . ASN A 1 65  ? 13.927 3.307   8.438   1.00 9.63  ? 67  ASN A OD1 1 
ATOM   555  N  ND2 . ASN A 1 65  ? 14.681 5.303   7.718   1.00 10.66 ? 67  ASN A ND2 1 
ATOM   556  N  N   . VAL A 1 66  ? 9.588  3.456   6.257   1.00 5.70  ? 68  VAL A N   1 
ATOM   557  C  CA  . VAL A 1 66  ? 8.384  4.091   5.717   1.00 7.29  ? 68  VAL A CA  1 
ATOM   558  C  C   . VAL A 1 66  ? 8.239  5.454   6.346   1.00 8.24  ? 68  VAL A C   1 
ATOM   559  O  O   . VAL A 1 66  ? 8.137  5.546   7.577   1.00 7.03  ? 68  VAL A O   1 
ATOM   560  C  CB  . VAL A 1 66  ? 7.088  3.271   5.896   1.00 8.73  ? 68  VAL A CB  1 
ATOM   561  C  CG1 . VAL A 1 66  ? 5.847  4.019   5.472   1.00 9.56  ? 68  VAL A CG1 1 
ATOM   562  C  CG2 . VAL A 1 66  ? 7.234  1.901   5.149   1.00 8.31  ? 68  VAL A CG2 1 
ATOM   563  N  N   . GLU A 1 67  ? 8.295  6.509   5.547   1.00 9.68  ? 69  GLU A N   1 
ATOM   564  C  CA  . GLU A 1 67  ? 8.392  7.894   6.028   1.00 10.12 ? 69  GLU A CA  1 
ATOM   565  C  C   . GLU A 1 67  ? 7.057  8.555   5.954   1.00 12.11 ? 69  GLU A C   1 
ATOM   566  O  O   . GLU A 1 67  ? 6.250  8.337   4.997   1.00 11.98 ? 69  GLU A O   1 
ATOM   567  C  CB  . GLU A 1 67  ? 9.277  8.638   5.032   1.00 11.92 ? 69  GLU A CB  1 
ATOM   568  C  CG  . GLU A 1 67  ? 10.673 8.089   5.113   1.00 9.84  ? 69  GLU A CG  1 
ATOM   569  C  CD  . GLU A 1 67  ? 11.475 8.481   3.924   1.00 10.60 ? 69  GLU A CD  1 
ATOM   570  O  OE1 . GLU A 1 67  ? 10.958 9.199   2.993   1.00 11.89 ? 69  GLU A OE1 1 
ATOM   571  O  OE2 . GLU A 1 67  ? 12.686 8.156   3.835   1.00 12.73 ? 69  GLU A OE2 1 
ATOM   572  N  N   . PHE A 1 68  ? 6.824  9.435   6.914   1.00 8.74  ? 70  PHE A N   1 
ATOM   573  C  CA  . PHE A 1 68  ? 5.555  10.194  7.002   1.00 8.07  ? 70  PHE A CA  1 
ATOM   574  C  C   . PHE A 1 68  ? 5.829  11.683  6.903   1.00 10.10 ? 70  PHE A C   1 
ATOM   575  O  O   . PHE A 1 68  ? 6.857  12.192  7.341   1.00 9.62  ? 70  PHE A O   1 
ATOM   576  C  CB  . PHE A 1 68  ? 4.852  9.875   8.301   1.00 8.13  ? 70  PHE A CB  1 
ATOM   577  C  CG  . PHE A 1 68  ? 4.285  8.462   8.288   1.00 7.85  ? 70  PHE A CG  1 
ATOM   578  C  CD1 . PHE A 1 68  ? 5.134  7.340   8.531   1.00 9.01  ? 70  PHE A CD1 1 
ATOM   579  C  CD2 . PHE A 1 68  ? 2.914  8.277   7.976   1.00 8.35  ? 70  PHE A CD2 1 
ATOM   580  C  CE1 . PHE A 1 68  ? 4.666  6.047   8.422   1.00 10.13 ? 70  PHE A CE1 1 
ATOM   581  C  CE2 . PHE A 1 68  ? 2.471  6.975   7.837   1.00 8.53  ? 70  PHE A CE2 1 
ATOM   582  C  CZ  . PHE A 1 68  ? 3.339  5.884   8.097   1.00 9.09  ? 70  PHE A CZ  1 
ATOM   583  N  N   . ASP A 1 69  ? 4.815  12.414  6.384   1.00 11.20 ? 71  ASP A N   1 
ATOM   584  C  CA  . ASP A 1 69  ? 4.872  13.836  6.472   1.00 10.41 ? 71  ASP A CA  1 
ATOM   585  C  C   . ASP A 1 69  ? 4.560  14.247  7.940   1.00 10.79 ? 71  ASP A C   1 
ATOM   586  O  O   . ASP A 1 69  ? 3.406  14.157  8.356   1.00 16.63 ? 71  ASP A O   1 
ATOM   587  C  CB  . ASP A 1 69  ? 3.923  14.416  5.479   1.00 18.10 ? 71  ASP A CB  1 
ATOM   588  C  CG  . ASP A 1 69  ? 3.713  15.927  5.582   1.00 23.21 ? 71  ASP A CG  1 
ATOM   589  O  OD1 . ASP A 1 69  ? 4.390  16.588  6.299   1.00 19.41 ? 71  ASP A OD1 1 
ATOM   590  O  OD2 . ASP A 1 69  ? 2.819  16.441  4.837   1.00 37.65 ? 71  ASP A OD2 1 
ATOM   591  N  N   . ASP A 1 70  ? 5.573  14.781  8.598   1.00 11.15 ? 72  ASP A N   1 
ATOM   592  C  CA  . ASP A 1 70  ? 5.447  15.232  9.993   1.00 11.40 ? 72  ASP A CA  1 
ATOM   593  C  C   . ASP A 1 70  ? 5.449  16.735  10.106  1.00 14.96 ? 72  ASP A C   1 
ATOM   594  O  O   . ASP A 1 70  ? 5.914  17.254  11.159  1.00 17.80 ? 72  ASP A O   1 
ATOM   595  C  CB  . ASP A 1 70  ? 6.518  14.580  10.873  1.00 11.71 ? 72  ASP A CB  1 
ATOM   596  C  CG  . ASP A 1 70  ? 7.946  15.032  10.548  1.00 13.33 ? 72  ASP A CG  1 
ATOM   597  O  OD1 . ASP A 1 70  ? 8.186  15.596  9.380   1.00 16.98 ? 72  ASP A OD1 1 
ATOM   598  O  OD2 . ASP A 1 70  ? 8.883  14.766  11.317  1.00 15.01 ? 72  ASP A OD2 1 
ATOM   599  N  N   . SER A 1 71  ? 5.103  17.462  9.025   1.00 14.64 ? 73  SER A N   1 
ATOM   600  C  CA  . SER A 1 71  ? 5.157  18.952  9.033   1.00 16.35 ? 73  SER A CA  1 
ATOM   601  C  C   . SER A 1 71  ? 3.828  19.549  9.659   1.00 22.09 ? 73  SER A C   1 
ATOM   602  O  O   . SER A 1 71  ? 3.751  20.777  9.874   1.00 19.93 ? 73  SER A O   1 
ATOM   603  C  CB  . SER A 1 71  ? 5.427  19.458  7.634   1.00 23.29 ? 73  SER A CB  1 
ATOM   604  O  OG  . SER A 1 71  ? 4.249  19.270  6.879   1.00 19.77 ? 73  SER A OG  1 
ATOM   605  N  N   . GLN A 1 72  ? 2.771  18.724  9.863   1.00 23.84 ? 74  GLN A N   1 
ATOM   606  C  CA  . GLN A 1 72  ? 1.609  19.244  10.560  1.00 25.49 ? 74  GLN A CA  1 
ATOM   607  C  C   . GLN A 1 72  ? 1.365  18.249  11.690  1.00 19.70 ? 74  GLN A C   1 
ATOM   608  O  O   . GLN A 1 72  ? 1.938  17.108  11.667  1.00 14.54 ? 74  GLN A O   1 
ATOM   609  C  CB  . GLN A 1 72  ? 0.358  19.293  9.641   1.00 26.53 ? 74  GLN A CB  1 
ATOM   610  C  CG  . GLN A 1 72  ? 0.293  20.453  8.639   1.00 32.74 ? 74  GLN A CG  1 
ATOM   611  C  CD  . GLN A 1 72  ? -0.265 19.974  7.315   1.00 29.72 ? 74  GLN A CD  1 
ATOM   612  O  OE1 . GLN A 1 72  ? -1.439 19.658  7.263   1.00 43.06 ? 74  GLN A OE1 1 
ATOM   613  N  NE2 . GLN A 1 72  ? 0.568  19.978  6.195   1.00 56.42 ? 74  GLN A NE2 1 
ATOM   614  N  N   . ASP A 1 73  ? 0.400  18.649  12.561  1.00 23.43 ? 75  ASP A N   1 
ATOM   615  C  CA  . ASP A 1 73  ? -0.089 17.881  13.687  1.00 20.53 ? 75  ASP A CA  1 
ATOM   616  C  C   . ASP A 1 73  ? -1.053 16.799  13.093  1.00 25.71 ? 75  ASP A C   1 
ATOM   617  O  O   . ASP A 1 73  ? -2.262 17.063  12.944  1.00 29.00 ? 75  ASP A O   1 
ATOM   618  C  CB  . ASP A 1 73  ? -0.905 18.945  14.555  1.00 22.08 ? 75  ASP A CB  1 
ATOM   619  C  CG  . ASP A 1 73  ? -1.499 18.343  15.843  1.00 28.59 ? 75  ASP A CG  1 
ATOM   620  O  OD1 . ASP A 1 73  ? -1.127 17.186  16.167  1.00 32.08 ? 75  ASP A OD1 1 
ATOM   621  O  OD2 . ASP A 1 73  ? -2.376 19.016  16.517  1.00 35.84 ? 75  ASP A OD2 1 
ATOM   622  N  N   . LYS A 1 74  ? -0.526 15.624  12.780  1.00 16.77 ? 76  LYS A N   1 
ATOM   623  C  CA  . LYS A 1 74  ? -1.178 14.474  12.240  1.00 21.20 ? 76  LYS A CA  1 
ATOM   624  C  C   . LYS A 1 74  ? -0.303 13.332  12.892  1.00 26.59 ? 76  LYS A C   1 
ATOM   625  O  O   . LYS A 1 74  ? 0.899  13.444  13.230  1.00 33.59 ? 76  LYS A O   1 
ATOM   626  C  CB  . LYS A 1 74  ? -0.945 14.307  10.751  1.00 21.71 ? 76  LYS A CB  1 
ATOM   627  C  CG  . LYS A 1 74  ? -1.341 15.425  9.758   1.00 35.99 ? 76  LYS A CG  1 
ATOM   628  C  CD  . LYS A 1 74  ? -0.863 14.988  8.333   1.00 38.74 ? 76  LYS A CD  1 
ATOM   629  C  CE  . LYS A 1 74  ? -1.212 16.147  7.356   1.00 38.02 ? 76  LYS A CE  1 
ATOM   630  N  NZ  . LYS A 1 74  ? -0.356 16.240  6.155   1.00 43.71 ? 76  LYS A NZ  1 
ATOM   631  N  N   . ALA A 1 75  ? -0.877 12.232  12.996  1.00 25.71 ? 77  ALA A N   1 
ATOM   632  C  CA  . ALA A 1 75  ? -0.343 10.963  13.457  1.00 16.18 ? 77  ALA A CA  1 
ATOM   633  C  C   . ALA A 1 75  ? 0.419  11.096  14.698  1.00 11.14 ? 77  ALA A C   1 
ATOM   634  O  O   . ALA A 1 75  ? 1.655  11.128  14.666  1.00 17.49 ? 77  ALA A O   1 
ATOM   635  C  CB  . ALA A 1 75  ? 0.501  10.316  12.350  1.00 15.37 ? 77  ALA A CB  1 
ATOM   636  N  N   . VAL A 1 76  ? -0.261 11.233  15.785  1.00 10.38 ? 78  VAL A N   1 
ATOM   637  C  CA  . VAL A 1 76  ? 0.430  11.405  17.089  1.00 10.91 ? 78  VAL A CA  1 
ATOM   638  C  C   . VAL A 1 76  ? 0.189  10.304  18.084  1.00 9.45  ? 78  VAL A C   1 
ATOM   639  O  O   . VAL A 1 76  ? -0.859 9.632   18.107  1.00 11.41 ? 78  VAL A O   1 
ATOM   640  C  CB  . VAL A 1 76  ? -0.097 12.690  17.606  1.00 16.41 ? 78  VAL A CB  1 
ATOM   641  C  CG1 . VAL A 1 76  ? 0.194  13.857  16.728  1.00 19.47 ? 78  VAL A CG1 1 
ATOM   642  C  CG2 . VAL A 1 76  ? -1.522 12.628  17.810  1.00 20.72 ? 78  VAL A CG2 1 
ATOM   643  N  N   . LEU A 1 77  ? 1.181  10.178  18.935  1.00 8.03  ? 79  LEU A N   1 
ATOM   644  C  CA  . LEU A 1 77  ? 1.145  9.269   20.074  1.00 8.02  ? 79  LEU A CA  1 
ATOM   645  C  C   . LEU A 1 77  ? 1.141  10.149  21.277  1.00 7.64  ? 79  LEU A C   1 
ATOM   646  O  O   . LEU A 1 77  ? 1.983  11.090  21.402  1.00 9.31  ? 79  LEU A O   1 
ATOM   647  C  CB  . LEU A 1 77  ? 2.431  8.381   19.955  1.00 8.80  ? 79  LEU A CB  1 
ATOM   648  C  CG  . LEU A 1 77  ? 2.551  7.309   21.011  1.00 9.26  ? 79  LEU A CG  1 
ATOM   649  C  CD1 . LEU A 1 77  ? 1.479  6.232   20.790  1.00 13.63 ? 79  LEU A CD1 1 
ATOM   650  C  CD2 . LEU A 1 77  ? 3.936  6.621   20.934  1.00 9.16  ? 79  LEU A CD2 1 
ATOM   651  N  N   . LYS A 1 78  ? 0.313  9.795   22.236  1.00 8.97  ? 80  LYS A N   1 
ATOM   652  C  CA  . LYS A 1 78  ? 0.251  10.543  23.521  1.00 10.10 ? 80  LYS A CA  1 
ATOM   653  C  C   . LYS A 1 78  ? -0.289 9.615   24.553  1.00 8.29  ? 80  LYS A C   1 
ATOM   654  O  O   . LYS A 1 78  ? -0.571 8.449   24.274  1.00 9.00  ? 80  LYS A O   1 
ATOM   655  C  CB  . LYS A 1 78  ? -0.522 11.848  23.450  1.00 12.77 ? 80  LYS A CB  1 
ATOM   656  C  CG  . LYS A 1 78  ? -1.922 11.602  23.185  1.00 15.66 ? 80  LYS A CG  1 
ATOM   657  C  CD  . LYS A 1 78  ? -2.700 12.963  23.104  1.00 23.42 ? 80  LYS A CD  1 
ATOM   658  C  CE  . LYS A 1 78  ? -2.322 13.660  21.832  1.00 32.65 ? 80  LYS A CE  1 
ATOM   659  N  N   . GLY A 1 79  ? -0.380 10.119  25.793  1.00 10.24 ? 81  GLY A N   1 
ATOM   660  C  CA  . GLY A 1 79  ? -0.931 9.246   26.847  1.00 11.30 ? 81  GLY A CA  1 
ATOM   661  C  C   . GLY A 1 79  ? 0.115  8.203   27.195  1.00 9.65  ? 81  GLY A C   1 
ATOM   662  O  O   . GLY A 1 79  ? 1.337  8.414   27.020  1.00 9.63  ? 81  GLY A O   1 
ATOM   663  N  N   . GLY A 1 80  ? -0.333 7.092   27.710  1.00 12.34 ? 82  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 80  ? 0.627  6.062   28.136  1.00 14.14 ? 82  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 80  ? 1.454  6.679   29.228  1.00 11.69 ? 82  GLY A C   1 
ATOM   666  O  O   . GLY A 1 80  ? 0.911  7.318   30.165  1.00 17.79 ? 82  GLY A O   1 
ATOM   667  N  N   . PRO A 1 81  ? 2.841  6.512   29.160  1.00 11.21 ? 83  PRO A N   1 
ATOM   668  C  CA  . PRO A 1 81  ? 3.741  7.115   30.121  1.00 11.09 ? 83  PRO A CA  1 
ATOM   669  C  C   . PRO A 1 81  ? 4.178  8.524   29.712  1.00 12.36 ? 83  PRO A C   1 
ATOM   670  O  O   . PRO A 1 81  ? 4.961  9.127   30.371  1.00 15.53 ? 83  PRO A O   1 
ATOM   671  C  CB  . PRO A 1 81  ? 4.999  6.245   29.956  1.00 13.08 ? 83  PRO A CB  1 
ATOM   672  C  CG  . PRO A 1 81  ? 4.996  5.880   28.484  1.00 9.45  ? 83  PRO A CG  1 
ATOM   673  C  CD  . PRO A 1 81  ? 3.526  5.681   28.161  1.00 9.21  ? 83  PRO A CD  1 
ATOM   674  N  N   . LEU A 1 82  ? 3.683  9.018   28.576  1.00 10.53 ? 84  LEU A N   1 
ATOM   675  C  CA  . LEU A 1 82  ? 4.211  10.251  27.980  1.00 9.61  ? 84  LEU A CA  1 
ATOM   676  C  C   . LEU A 1 82  ? 3.569  11.506  28.534  1.00 12.01 ? 84  LEU A C   1 
ATOM   677  O  O   . LEU A 1 82  ? 2.327  11.512  28.812  1.00 13.88 ? 84  LEU A O   1 
ATOM   678  C  CB  . LEU A 1 82  ? 3.957  10.226  26.492  1.00 8.90  ? 84  LEU A CB  1 
ATOM   679  C  CG  . LEU A 1 82  ? 4.545  8.976   25.765  1.00 7.30  ? 84  LEU A CG  1 
ATOM   680  C  CD1 . LEU A 1 82  ? 4.078  8.952   24.307  1.00 9.90  ? 84  LEU A CD1 1 
ATOM   681  C  CD2 . LEU A 1 82  ? 6.093  8.999   25.854  1.00 8.54  ? 84  LEU A CD2 1 
ATOM   682  N  N   A ASP A 1 83  ? 4.303  12.592  28.709  0.50 13.02 ? 85  ASP A N   1 
ATOM   683  N  N   B ASP A 1 83  ? 4.379  12.577  28.497  0.50 12.80 ? 85  ASP A N   1 
ATOM   684  C  CA  A ASP A 1 83  ? 3.540  13.766  29.221  0.50 12.87 ? 85  ASP A CA  1 
ATOM   685  C  CA  B ASP A 1 83  ? 3.884  13.930  28.683  0.50 13.45 ? 85  ASP A CA  1 
ATOM   686  C  C   A ASP A 1 83  ? 3.419  14.808  28.175  0.50 14.61 ? 85  ASP A C   1 
ATOM   687  C  C   B ASP A 1 83  ? 3.888  14.650  27.347  0.50 8.34  ? 85  ASP A C   1 
ATOM   688  O  O   A ASP A 1 83  ? 3.199  15.961  28.468  0.50 18.53 ? 85  ASP A O   1 
ATOM   689  O  O   B ASP A 1 83  ? 4.857  14.615  26.601  0.50 13.77 ? 85  ASP A O   1 
ATOM   690  C  CB  A ASP A 1 83  ? 4.118  14.307  30.475  0.50 13.22 ? 85  ASP A CB  1 
ATOM   691  C  CB  B ASP A 1 83  ? 4.662  14.646  29.743  0.50 13.39 ? 85  ASP A CB  1 
ATOM   692  C  CG  A ASP A 1 83  ? 5.601  14.700  30.312  0.50 14.30 ? 85  ASP A CG  1 
ATOM   693  C  CG  B ASP A 1 83  ? 4.451  14.047  31.181  0.50 21.62 ? 85  ASP A CG  1 
ATOM   694  O  OD1 A ASP A 1 83  ? 6.110  14.527  29.149  0.50 14.99 ? 85  ASP A OD1 1 
ATOM   695  O  OD1 B ASP A 1 83  ? 3.275  13.664  31.570  0.50 22.61 ? 85  ASP A OD1 1 
ATOM   696  O  OD2 A ASP A 1 83  ? 6.234  15.067  31.347  0.50 22.48 ? 85  ASP A OD2 1 
ATOM   697  O  OD2 B ASP A 1 83  ? 5.529  14.011  31.884  0.50 23.02 ? 85  ASP A OD2 1 
ATOM   698  N  N   A GLY A 1 84  ? 3.544  14.388  26.922  0.50 14.73 ? 86  GLY A N   1 
ATOM   699  N  N   B GLY A 1 84  ? 2.784  15.297  27.023  0.50 9.33  ? 86  GLY A N   1 
ATOM   700  C  CA  A GLY A 1 84  ? 3.512  15.297  25.820  0.50 16.67 ? 86  GLY A CA  1 
ATOM   701  C  CA  B GLY A 1 84  ? 2.670  16.051  25.809  0.50 11.25 ? 86  GLY A CA  1 
ATOM   702  C  C   A GLY A 1 84  ? 2.964  14.628  24.534  0.50 14.58 ? 86  GLY A C   1 
ATOM   703  C  C   B GLY A 1 84  ? 2.429  15.089  24.619  0.50 12.38 ? 86  GLY A C   1 
ATOM   704  O  O   A GLY A 1 84  ? 2.492  13.474  24.589  0.50 16.28 ? 86  GLY A O   1 
ATOM   705  O  O   B GLY A 1 84  ? 1.737  14.059  24.748  0.50 16.75 ? 86  GLY A O   1 
ATOM   706  N  N   A THR A 1 85  ? 2.965  15.388  23.414  0.50 12.47 ? 87  THR A N   1 
ATOM   707  N  N   B THR A 1 85  ? 2.928  15.459  23.438  0.50 10.20 ? 87  THR A N   1 
ATOM   708  C  CA  A THR A 1 85  ? 2.481  14.915  22.110  0.50 14.00 ? 87  THR A CA  1 
ATOM   709  C  CA  B THR A 1 85  ? 2.497  14.763  22.252  0.50 10.29 ? 87  THR A CA  1 
ATOM   710  C  C   A THR A 1 85  ? 3.701  14.609  21.265  0.50 8.85  ? 87  THR A C   1 
ATOM   711  C  C   B THR A 1 85  ? 3.698  14.580  21.323  0.50 8.13  ? 87  THR A C   1 
ATOM   712  O  O   A THR A 1 85  ? 4.643  15.407  21.130  0.50 9.40  ? 87  THR A O   1 
ATOM   713  O  O   B THR A 1 85  ? 4.622  15.409  21.202  0.50 8.67  ? 87  THR A O   1 
ATOM   714  C  CB  A THR A 1 85  ? 1.753  16.016  21.292  0.50 18.40 ? 87  THR A CB  1 
ATOM   715  C  CB  B THR A 1 85  ? 1.439  15.631  21.568  0.50 9.41  ? 87  THR A CB  1 
ATOM   716  O  OG1 A THR A 1 85  ? 0.513  16.437  21.895  0.50 19.48 ? 87  THR A OG1 1 
ATOM   717  O  OG1 B THR A 1 85  ? 2.027  16.968  21.452  0.50 11.71 ? 87  THR A OG1 1 
ATOM   718  C  CG2 A THR A 1 85  ? 1.544  15.599  19.789  0.50 17.24 ? 87  THR A CG2 1 
ATOM   719  C  CG2 B THR A 1 85  ? 0.176  15.792  22.444  0.50 13.39 ? 87  THR A CG2 1 
ATOM   720  N  N   . TYR A 1 86  ? 3.672  13.407  20.698  1.00 7.19  ? 88  TYR A N   1 
ATOM   721  C  CA  . TYR A 1 86  ? 4.772  12.935  19.856  1.00 6.57  ? 88  TYR A CA  1 
ATOM   722  C  C   . TYR A 1 86  ? 4.281  12.619  18.478  1.00 6.54  ? 88  TYR A C   1 
ATOM   723  O  O   . TYR A 1 86  ? 3.308  11.911  18.305  1.00 10.50 ? 88  TYR A O   1 
ATOM   724  C  CB  . TYR A 1 86  ? 5.446  11.704  20.471  1.00 5.88  ? 88  TYR A CB  1 
ATOM   725  C  CG  . TYR A 1 86  ? 6.184  11.910  21.793  1.00 5.50  ? 88  TYR A CG  1 
ATOM   726  C  CD1 . TYR A 1 86  ? 5.513  12.239  22.959  1.00 7.16  ? 88  TYR A CD1 1 
ATOM   727  C  CD2 . TYR A 1 86  ? 7.568  11.732  21.834  1.00 4.99  ? 88  TYR A CD2 1 
ATOM   728  C  CE1 . TYR A 1 86  ? 6.216  12.432  24.158  1.00 7.44  ? 88  TYR A CE1 1 
ATOM   729  C  CE2 . TYR A 1 86  ? 8.264  11.871  23.032  1.00 5.49  ? 88  TYR A CE2 1 
ATOM   730  C  CZ  . TYR A 1 86  ? 7.580  12.207  24.197  1.00 5.34  ? 88  TYR A CZ  1 
ATOM   731  O  OH  . TYR A 1 86  ? 8.273  12.342  25.380  1.00 6.79  ? 88  TYR A OH  1 
ATOM   732  N  N   . ARG A 1 87  ? 4.961  13.143  17.496  1.00 6.61  ? 89  ARG A N   1 
ATOM   733  C  CA  . ARG A 1 87  ? 4.524  13.021  16.121  1.00 6.69  ? 89  ARG A CA  1 
ATOM   734  C  C   . ARG A 1 87  ? 5.245  11.898  15.397  1.00 4.70  ? 89  ARG A C   1 
ATOM   735  O  O   . ARG A 1 87  ? 6.501  11.803  15.447  1.00 5.20  ? 89  ARG A O   1 
ATOM   736  C  CB  . ARG A 1 87  ? 4.862  14.342  15.402  1.00 9.95  ? 89  ARG A CB  1 
ATOM   737  C  CG  . ARG A 1 87  ? 4.048  14.503  14.141  1.00 13.17 ? 89  ARG A CG  1 
ATOM   738  C  CD  . ARG A 1 87  ? 4.319  15.939  13.663  1.00 14.74 ? 89  ARG A CD  1 
ATOM   739  N  NE  . ARG A 1 87  ? 3.557  16.964  14.496  1.00 13.71 ? 89  ARG A NE  1 
ATOM   740  C  CZ  . ARG A 1 87  ? 3.750  18.263  14.304  1.00 13.66 ? 89  ARG A CZ  1 
ATOM   741  N  NH1 . ARG A 1 87  ? 4.519  18.721  13.313  1.00 16.47 ? 89  ARG A NH1 1 
ATOM   742  N  NH2 . ARG A 1 87  ? 3.079  19.151  15.035  1.00 16.63 ? 89  ARG A NH2 1 
ATOM   743  N  N   . LEU A 1 88  ? 4.488  11.089  14.656  1.00 5.50  ? 90  LEU A N   1 
ATOM   744  C  CA  . LEU A 1 88  ? 5.077  9.987   13.900  1.00 5.57  ? 90  LEU A CA  1 
ATOM   745  C  C   . LEU A 1 88  ? 5.935  10.541  12.744  1.00 6.03  ? 90  LEU A C   1 
ATOM   746  O  O   . LEU A 1 88  ? 5.430  11.336  11.902  1.00 8.22  ? 90  LEU A O   1 
ATOM   747  C  CB  . LEU A 1 88  ? 3.957  9.124   13.323  1.00 6.15  ? 90  LEU A CB  1 
ATOM   748  C  CG  . LEU A 1 88  ? 4.405  7.967   12.425  1.00 6.72  ? 90  LEU A CG  1 
ATOM   749  C  CD1 . LEU A 1 88  ? 5.190  6.872   13.253  1.00 8.58  ? 90  LEU A CD1 1 
ATOM   750  C  CD2 . LEU A 1 88  ? 3.171  7.313   11.800  1.00 8.74  ? 90  LEU A CD2 1 
ATOM   751  N  N   . ILE A 1 89  ? 7.178  10.071  12.632  1.00 5.35  ? 91  ILE A N   1 
ATOM   752  C  CA  . ILE A 1 89  ? 8.049  10.432  11.514  1.00 5.70  ? 91  ILE A CA  1 
ATOM   753  C  C   . ILE A 1 89  ? 8.361  9.289   10.586  1.00 4.73  ? 91  ILE A C   1 
ATOM   754  O  O   . ILE A 1 89  ? 8.440  9.443   9.374   1.00 5.87  ? 91  ILE A O   1 
ATOM   755  C  CB  . ILE A 1 89  ? 9.364  11.141  12.015  1.00 6.35  ? 91  ILE A CB  1 
ATOM   756  C  CG1 . ILE A 1 89  ? 10.246 11.524  10.814  1.00 7.88  ? 91  ILE A CG1 1 
ATOM   757  C  CG2 . ILE A 1 89  ? 10.092 10.301  13.061  1.00 6.94  ? 91  ILE A CG2 1 
ATOM   758  C  CD1 . ILE A 1 89  ? 11.422 12.441  11.284  1.00 10.76 ? 91  ILE A CD1 1 
ATOM   759  N  N   . GLN A 1 90  ? 8.497  8.042   11.152  1.00 5.24  ? 92  GLN A N   1 
ATOM   760  C  CA  . GLN A 1 90  ? 8.824  6.903   10.275  1.00 5.27  ? 92  GLN A CA  1 
ATOM   761  C  C   . GLN A 1 90  ? 8.554  5.639   11.035  1.00 4.44  ? 92  GLN A C   1 
ATOM   762  O  O   . GLN A 1 90  ? 8.500  5.657   12.290  1.00 4.46  ? 92  GLN A O   1 
ATOM   763  C  CB  . GLN A 1 90  ? 10.274 6.929   9.797   1.00 6.12  ? 92  GLN A CB  1 
ATOM   764  C  CG  . GLN A 1 90  ? 11.364 7.009   10.952  1.00 6.72  ? 92  GLN A CG  1 
ATOM   765  C  CD  . GLN A 1 90  ? 12.104 5.724   11.042  1.00 6.05  ? 92  GLN A CD  1 
ATOM   766  O  OE1 . GLN A 1 90  ? 11.544 4.619   11.168  1.00 6.37  ? 92  GLN A OE1 1 
ATOM   767  N  NE2 . GLN A 1 90  ? 13.393 5.826   11.087  1.00 10.01 ? 92  GLN A NE2 1 
ATOM   768  N  N   . PHE A 1 91  ? 8.392  4.535   10.339  1.00 5.06  ? 93  PHE A N   1 
ATOM   769  C  CA  . PHE A 1 91  ? 8.550  3.219   10.956  1.00 4.88  ? 93  PHE A CA  1 
ATOM   770  C  C   . PHE A 1 91  ? 9.499  2.387   10.186  1.00 4.00  ? 93  PHE A C   1 
ATOM   771  O  O   . PHE A 1 91  ? 9.746  2.591   8.968   1.00 5.62  ? 93  PHE A O   1 
ATOM   772  C  CB  . PHE A 1 91  ? 7.195  2.528   11.189  1.00 5.37  ? 93  PHE A CB  1 
ATOM   773  C  CG  . PHE A 1 91  ? 6.465  2.051   9.994   1.00 5.78  ? 93  PHE A CG  1 
ATOM   774  C  CD1 . PHE A 1 91  ? 6.859  0.876   9.338   1.00 6.22  ? 93  PHE A CD1 1 
ATOM   775  C  CD2 . PHE A 1 91  ? 5.294  2.723   9.572   1.00 6.40  ? 93  PHE A CD2 1 
ATOM   776  C  CE1 . PHE A 1 91  ? 6.122  0.425   8.203   1.00 6.55  ? 93  PHE A CE1 1 
ATOM   777  C  CE2 . PHE A 1 91  ? 4.582  2.267   8.434   1.00 7.17  ? 93  PHE A CE2 1 
ATOM   778  C  CZ  . PHE A 1 91  ? 4.961  1.119   7.806   1.00 7.29  ? 93  PHE A CZ  1 
ATOM   779  N  N   . HIS A 1 92  ? 10.026 1.338   10.850  1.00 4.29  ? 94  HIS A N   1 
ATOM   780  C  CA  . HIS A 1 92  ? 10.940 0.364   10.244  1.00 4.00  ? 94  HIS A CA  1 
ATOM   781  C  C   . HIS A 1 92  ? 10.831 -0.900  11.053  1.00 4.13  ? 94  HIS A C   1 
ATOM   782  O  O   . HIS A 1 92  ? 10.213 -0.910  12.145  1.00 4.32  ? 94  HIS A O   1 
ATOM   783  C  CB  . HIS A 1 92  ? 12.382 0.882   10.166  1.00 4.80  ? 94  HIS A CB  1 
ATOM   784  C  CG  . HIS A 1 92  ? 12.886 1.181   11.536  1.00 3.66  ? 94  HIS A CG  1 
ATOM   785  N  ND1 . HIS A 1 92  ? 12.749 2.358   12.217  1.00 3.14  ? 94  HIS A ND1 1 
ATOM   786  C  CD2 . HIS A 1 92  ? 13.522 0.351   12.454  1.00 4.64  ? 94  HIS A CD2 1 
ATOM   787  C  CE1 . HIS A 1 92  ? 13.211 2.264   13.464  1.00 4.20  ? 94  HIS A CE1 1 
ATOM   788  N  NE2 . HIS A 1 92  ? 13.721 1.016   13.661  1.00 3.70  ? 94  HIS A NE2 1 
ATOM   789  N  N   . PHE A 1 93  ? 11.526 -1.950  10.606  1.00 4.30  ? 95  PHE A N   1 
ATOM   790  C  CA  . PHE A 1 93  ? 11.571 -3.219  11.307  1.00 3.80  ? 95  PHE A CA  1 
ATOM   791  C  C   . PHE A 1 93  ? 12.992 -3.686  11.511  1.00 3.59  ? 95  PHE A C   1 
ATOM   792  O  O   . PHE A 1 93  ? 13.902 -3.212  10.833  1.00 4.42  ? 95  PHE A O   1 
ATOM   793  C  CB  . PHE A 1 93  ? 10.844 -4.307  10.470  1.00 4.04  ? 95  PHE A CB  1 
ATOM   794  C  CG  . PHE A 1 93  ? 9.384  -3.983  10.148  1.00 4.12  ? 95  PHE A CG  1 
ATOM   795  C  CD1 . PHE A 1 93  ? 9.051  -3.166  9.060   1.00 5.81  ? 95  PHE A CD1 1 
ATOM   796  C  CD2 . PHE A 1 93  ? 8.360  -4.690  10.810  1.00 5.31  ? 95  PHE A CD2 1 
ATOM   797  C  CE1 . PHE A 1 93  ? 7.729  -2.978  8.731   1.00 5.48  ? 95  PHE A CE1 1 
ATOM   798  C  CE2 . PHE A 1 93  ? 7.026  -4.498  10.494  1.00 6.37  ? 95  PHE A CE2 1 
ATOM   799  C  CZ  . PHE A 1 93  ? 6.713  -3.630  9.407   1.00 5.59  ? 95  PHE A CZ  1 
ATOM   800  N  N   . HIS A 1 94  ? 13.082 -4.656  12.424  1.00 4.00  ? 96  HIS A N   1 
ATOM   801  C  CA  . HIS A 1 94  ? 14.291 -5.455  12.592  1.00 3.48  ? 96  HIS A CA  1 
ATOM   802  C  C   . HIS A 1 94  ? 13.851 -6.911  12.497  1.00 4.19  ? 96  HIS A C   1 
ATOM   803  O  O   . HIS A 1 94  ? 12.761 -7.264  12.960  1.00 4.51  ? 96  HIS A O   1 
ATOM   804  C  CB  . HIS A 1 94  ? 14.981 -5.234  13.956  1.00 3.60  ? 96  HIS A CB  1 
ATOM   805  C  CG  . HIS A 1 94  ? 15.270 -3.799  14.247  1.00 2.88  ? 96  HIS A CG  1 
ATOM   806  N  ND1 . HIS A 1 94  ? 16.516 -3.247  14.104  1.00 4.42  ? 96  HIS A ND1 1 
ATOM   807  C  CD2 . HIS A 1 94  ? 14.429 -2.771  14.618  1.00 3.39  ? 96  HIS A CD2 1 
ATOM   808  C  CE1 . HIS A 1 94  ? 16.446 -1.931  14.417  1.00 4.48  ? 96  HIS A CE1 1 
ATOM   809  N  NE2 . HIS A 1 94  ? 15.164 -1.580  14.673  1.00 3.93  ? 96  HIS A NE2 1 
ATOM   810  N  N   . TRP A 1 95  ? 14.617 -7.767  11.810  1.00 3.53  ? 97  TRP A N   1 
ATOM   811  C  CA  . TRP A 1 95  ? 14.203 -9.138  11.642  1.00 4.44  ? 97  TRP A CA  1 
ATOM   812  C  C   . TRP A 1 95  ? 15.405 -10.041 11.495  1.00 4.12  ? 97  TRP A C   1 
ATOM   813  O  O   . TRP A 1 95  ? 16.584 -9.634  11.397  1.00 5.16  ? 97  TRP A O   1 
ATOM   814  C  CB  . TRP A 1 95  ? 13.288 -9.267  10.372  1.00 4.97  ? 97  TRP A CB  1 
ATOM   815  C  CG  . TRP A 1 95  ? 13.952 -8.877  9.095   1.00 5.12  ? 97  TRP A CG  1 
ATOM   816  C  CD1 . TRP A 1 95  ? 14.625 -9.673  8.244   1.00 5.85  ? 97  TRP A CD1 1 
ATOM   817  C  CD2 . TRP A 1 95  ? 14.021 -7.575  8.509   1.00 5.04  ? 97  TRP A CD2 1 
ATOM   818  N  NE1 . TRP A 1 95  ? 15.070 -8.986  7.126   1.00 5.78  ? 97  TRP A NE1 1 
ATOM   819  C  CE2 . TRP A 1 95  ? 14.722 -7.658  7.284   1.00 5.47  ? 97  TRP A CE2 1 
ATOM   820  C  CE3 . TRP A 1 95  ? 13.520 -6.286  8.893   1.00 5.05  ? 97  TRP A CE3 1 
ATOM   821  C  CZ2 . TRP A 1 95  ? 14.889 -6.575  6.427   1.00 6.64  ? 97  TRP A CZ2 1 
ATOM   822  C  CZ3 . TRP A 1 95  ? 13.786 -5.187  8.079   1.00 6.85  ? 97  TRP A CZ3 1 
ATOM   823  C  CH2 . TRP A 1 95  ? 14.425 -5.359  6.846   1.00 6.79  ? 97  TRP A CH2 1 
ATOM   824  N  N   . GLY A 1 96  ? 15.094 -11.364 11.486  1.00 4.74  ? 98  GLY A N   1 
ATOM   825  C  CA  . GLY A 1 96  ? 16.152 -12.372 11.535  1.00 4.58  ? 98  GLY A CA  1 
ATOM   826  C  C   . GLY A 1 96  ? 16.347 -13.069 10.197  1.00 5.39  ? 98  GLY A C   1 
ATOM   827  O  O   . GLY A 1 96  ? 15.619 -12.902 9.225   1.00 5.98  ? 98  GLY A O   1 
ATOM   828  N  N   . SER A 1 97  ? 17.364 -13.951 10.215  1.00 5.40  ? 99  SER A N   1 
ATOM   829  C  CA  . SER A 1 97  ? 17.596 -14.869 9.086   1.00 6.71  ? 99  SER A CA  1 
ATOM   830  C  C   . SER A 1 97  ? 16.695 -16.108 9.196   1.00 6.75  ? 99  SER A C   1 
ATOM   831  O  O   . SER A 1 97  ? 16.541 -16.814 8.194   1.00 10.19 ? 99  SER A O   1 
ATOM   832  C  CB  . SER A 1 97  ? 19.057 -15.250 9.082   1.00 8.56  ? 99  SER A CB  1 
ATOM   833  O  OG  . SER A 1 97  ? 19.507 -15.746 10.341  1.00 9.54  ? 99  SER A OG  1 
ATOM   834  N  N   A LEU A 1 98  ? 16.154 -16.412 10.384  0.50 6.80  ? 100 LEU A N   1 
ATOM   835  N  N   B LEU A 1 98  ? 16.072 -16.283 10.372  0.50 7.62  ? 100 LEU A N   1 
ATOM   836  C  CA  A LEU A 1 98  ? 15.167 -17.476 10.592  0.50 7.77  ? 100 LEU A CA  1 
ATOM   837  C  CA  B LEU A 1 98  ? 15.324 -17.462 10.779  0.50 7.43  ? 100 LEU A CA  1 
ATOM   838  C  C   A LEU A 1 98  ? 14.136 -16.978 11.554  0.50 7.23  ? 100 LEU A C   1 
ATOM   839  C  C   B LEU A 1 98  ? 14.169 -16.985 11.634  0.50 7.29  ? 100 LEU A C   1 
ATOM   840  O  O   A LEU A 1 98  ? 14.376 -15.971 12.224  0.50 7.21  ? 100 LEU A O   1 
ATOM   841  O  O   B LEU A 1 98  ? 14.327 -15.937 12.266  0.50 7.57  ? 100 LEU A O   1 
ATOM   842  C  CB  A LEU A 1 98  ? 15.779 -18.781 11.208  0.50 9.69  ? 100 LEU A CB  1 
ATOM   843  C  CB  B LEU A 1 98  ? 16.269 -18.373 11.645  0.50 11.04 ? 100 LEU A CB  1 
ATOM   844  C  CG  A LEU A 1 98  ? 16.769 -19.568 10.379  0.50 15.09 ? 100 LEU A CG  1 
ATOM   845  C  CG  B LEU A 1 98  ? 17.541 -18.946 11.016  0.50 11.59 ? 100 LEU A CG  1 
ATOM   846  C  CD1 A LEU A 1 98  ? 16.144 -19.803 9.081   0.50 14.52 ? 100 LEU A CD1 1 
ATOM   847  C  CD1 B LEU A 1 98  ? 18.465 -19.523 12.088  0.50 16.84 ? 100 LEU A CD1 1 
ATOM   848  C  CD2 A LEU A 1 98  ? 17.975 -18.695 10.372  0.50 19.24 ? 100 LEU A CD2 1 
ATOM   849  C  CD2 B LEU A 1 98  ? 17.236 -20.121 10.106  0.50 15.91 ? 100 LEU A CD2 1 
ATOM   850  N  N   . ASP A 1 99  ? 13.062 -17.696 11.709  1.00 7.25  ? 101 ASP A N   1 
ATOM   851  C  CA  . ASP A 1 99  ? 11.904 -17.196 12.483  1.00 7.66  ? 101 ASP A CA  1 
ATOM   852  C  C   . ASP A 1 99  ? 12.216 -17.105 13.945  1.00 7.30  ? 101 ASP A C   1 
ATOM   853  O  O   . ASP A 1 99  ? 11.555 -16.376 14.643  1.00 9.34  ? 101 ASP A O   1 
ATOM   854  C  CB  . ASP A 1 99  ? 10.617 -18.038 12.256  1.00 8.60  ? 101 ASP A CB  1 
ATOM   855  C  CG  . ASP A 1 99  ? 10.187 -18.162 10.821  1.00 11.33 ? 101 ASP A CG  1 
ATOM   856  O  OD1 . ASP A 1 99  ? 10.513 -17.320 9.993   1.00 10.68 ? 101 ASP A OD1 1 
ATOM   857  O  OD2 . ASP A 1 99  ? 9.341  -19.049 10.605  1.00 15.01 ? 101 ASP A OD2 1 
ATOM   858  N  N   . GLY A 1 100 ? 13.182 -17.897 14.403  1.00 8.27  ? 102 GLY A N   1 
ATOM   859  C  CA  . GLY A 1 100 ? 13.495 -17.905 15.849  1.00 7.72  ? 102 GLY A CA  1 
ATOM   860  C  C   . GLY A 1 100 ? 14.331 -16.747 16.344  1.00 6.72  ? 102 GLY A C   1 
ATOM   861  O  O   . GLY A 1 100 ? 14.659 -16.692 17.539  1.00 7.85  ? 102 GLY A O   1 
ATOM   862  N  N   . GLN A 1 101 ? 14.641 -15.748 15.522  1.00 6.61  ? 103 GLN A N   1 
ATOM   863  C  CA  . GLN A 1 101 ? 15.363 -14.577 15.995  1.00 5.66  ? 103 GLN A CA  1 
ATOM   864  C  C   . GLN A 1 101 ? 14.914 -13.404 15.141  1.00 4.35  ? 103 GLN A C   1 
ATOM   865  O  O   . GLN A 1 101 ? 14.417 -13.583 14.030  1.00 5.96  ? 103 GLN A O   1 
ATOM   866  C  CB  . GLN A 1 101 ? 16.864 -14.796 16.066  1.00 7.39  ? 103 GLN A CB  1 
ATOM   867  C  CG  . GLN A 1 101 ? 17.453 -15.030 14.681  1.00 8.19  ? 103 GLN A CG  1 
ATOM   868  C  CD  . GLN A 1 101 ? 18.897 -15.512 14.793  1.00 11.71 ? 103 GLN A CD  1 
ATOM   869  O  OE1 . GLN A 1 101 ? 19.224 -16.250 15.722  1.00 20.70 ? 103 GLN A OE1 1 
ATOM   870  N  NE2 . GLN A 1 101 ? 19.761 -15.109 13.930  1.00 10.54 ? 103 GLN A NE2 1 
ATOM   871  N  N   . GLY A 1 102 ? 15.256 -12.178 15.622  1.00 4.64  ? 104 GLY A N   1 
ATOM   872  C  CA  . GLY A 1 102 ? 14.999 -10.950 14.804  1.00 4.63  ? 104 GLY A CA  1 
ATOM   873  C  C   . GLY A 1 102 ? 14.533 -9.807  15.642  1.00 4.10  ? 104 GLY A C   1 
ATOM   874  O  O   . GLY A 1 102 ? 14.815 -8.676  15.313  1.00 4.96  ? 104 GLY A O   1 
ATOM   875  N  N   . SER A 1 103 ? 13.821 -10.091 16.764  1.00 4.00  ? 105 SER A N   1 
ATOM   876  C  CA  . SER A 1 103 ? 13.425 -8.945  17.609  1.00 3.75  ? 105 SER A CA  1 
ATOM   877  C  C   . SER A 1 103 ? 14.671 -8.434  18.380  1.00 3.36  ? 105 SER A C   1 
ATOM   878  O  O   . SER A 1 103 ? 15.653 -9.118  18.575  1.00 4.74  ? 105 SER A O   1 
ATOM   879  C  CB  . SER A 1 103 ? 12.309 -9.288  18.568  1.00 3.99  ? 105 SER A CB  1 
ATOM   880  O  OG  . SER A 1 103 ? 12.667 -10.243 19.543  1.00 4.44  ? 105 SER A OG  1 
ATOM   881  N  N   . GLU A 1 104 ? 14.503 -7.172  18.789  1.00 3.20  ? 106 GLU A N   1 
ATOM   882  C  CA  . GLU A 1 104 ? 15.537 -6.485  19.611  1.00 3.22  ? 106 GLU A CA  1 
ATOM   883  C  C   . GLU A 1 104 ? 15.182 -6.656  21.080  1.00 2.92  ? 106 GLU A C   1 
ATOM   884  O  O   . GLU A 1 104 ? 15.976 -7.213  21.862  1.00 3.86  ? 106 GLU A O   1 
ATOM   885  C  CB  . GLU A 1 104 ? 15.611 -5.031  19.171  1.00 2.98  ? 106 GLU A CB  1 
ATOM   886  C  CG  . GLU A 1 104 ? 16.090 -4.943  17.717  1.00 4.98  ? 106 GLU A CG  1 
ATOM   887  C  CD  . GLU A 1 104 ? 16.768 -3.659  17.405  1.00 3.94  ? 106 GLU A CD  1 
ATOM   888  O  OE1 . GLU A 1 104 ? 16.117 -2.601  17.616  1.00 4.07  ? 106 GLU A OE1 1 
ATOM   889  O  OE2 . GLU A 1 104 ? 17.916 -3.685  16.968  1.00 5.41  ? 106 GLU A OE2 1 
ATOM   890  N  N   . HIS A 1 105 ? 14.003 -6.160  21.504  1.00 2.87  ? 107 HIS A N   1 
ATOM   891  C  CA  . HIS A 1 105 ? 13.539 -6.566  22.813  1.00 2.85  ? 107 HIS A CA  1 
ATOM   892  C  C   . HIS A 1 105 ? 13.271 -8.047  22.815  1.00 2.90  ? 107 HIS A C   1 
ATOM   893  O  O   . HIS A 1 105 ? 12.880 -8.631  21.797  1.00 3.60  ? 107 HIS A O   1 
ATOM   894  C  CB  . HIS A 1 105 ? 12.288 -5.721  23.171  1.00 3.20  ? 107 HIS A CB  1 
ATOM   895  C  CG  . HIS A 1 105 ? 12.620 -4.290  23.318  1.00 2.49  ? 107 HIS A CG  1 
ATOM   896  N  ND1 . HIS A 1 105 ? 12.584 -3.389  22.262  1.00 3.65  ? 107 HIS A ND1 1 
ATOM   897  C  CD2 . HIS A 1 105 ? 13.096 -3.562  24.379  1.00 3.01  ? 107 HIS A CD2 1 
ATOM   898  C  CE1 . HIS A 1 105 ? 13.011 -2.191  22.695  1.00 3.88  ? 107 HIS A CE1 1 
ATOM   899  N  NE2 . HIS A 1 105 ? 13.342 -2.276  23.979  1.00 3.17  ? 107 HIS A NE2 1 
ATOM   900  N  N   . THR A 1 106 ? 13.352 -8.623  24.027  1.00 3.82  ? 108 THR A N   1 
ATOM   901  C  CA  . THR A 1 106 ? 12.996 -9.996  24.288  1.00 3.57  ? 108 THR A CA  1 
ATOM   902  C  C   . THR A 1 106 ? 12.046 -10.022 25.475  1.00 3.05  ? 108 THR A C   1 
ATOM   903  O  O   . THR A 1 106 ? 12.013 -9.046  26.250  1.00 4.03  ? 108 THR A O   1 
ATOM   904  C  CB  . THR A 1 106 ? 14.209 -10.891 24.448  1.00 3.91  ? 108 THR A CB  1 
ATOM   905  O  OG1 . THR A 1 106 ? 15.058 -10.405 25.507  1.00 4.37  ? 108 THR A OG1 1 
ATOM   906  C  CG2 . THR A 1 106 ? 14.995 -10.955 23.159  1.00 5.35  ? 108 THR A CG2 1 
ATOM   907  N  N   . VAL A 1 107 ? 11.302 -11.089 25.608  1.00 3.72  ? 109 VAL A N   1 
ATOM   908  C  CA  . VAL A 1 107 ? 10.310 -11.208 26.698  1.00 4.97  ? 109 VAL A CA  1 
ATOM   909  C  C   . VAL A 1 107 ? 10.637 -12.479 27.445  1.00 4.53  ? 109 VAL A C   1 
ATOM   910  O  O   . VAL A 1 107 ? 10.466 -13.574 26.902  1.00 5.41  ? 109 VAL A O   1 
ATOM   911  C  CB  . VAL A 1 107 ? 8.847  -11.198 26.125  1.00 5.44  ? 109 VAL A CB  1 
ATOM   912  C  CG1 . VAL A 1 107 ? 7.827  -11.303 27.253  1.00 6.57  ? 109 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A 1 107 ? 8.550  -9.903  25.331  1.00 6.44  ? 109 VAL A CG2 1 
ATOM   914  N  N   . ASP A 1 108 ? 11.137 -12.360 28.666  1.00 5.40  ? 110 ASP A N   1 
ATOM   915  C  CA  . ASP A 1 108 ? 11.618 -13.566 29.421  1.00 7.26  ? 110 ASP A CA  1 
ATOM   916  C  C   . ASP A 1 108 ? 12.557 -14.364 28.474  1.00 6.71  ? 110 ASP A C   1 
ATOM   917  O  O   . ASP A 1 108 ? 12.483 -15.613 28.432  1.00 6.89  ? 110 ASP A O   1 
ATOM   918  C  CB  . ASP A 1 108 ? 10.457 -14.403 29.909  1.00 7.49  ? 110 ASP A CB  1 
ATOM   919  C  CG  . ASP A 1 108 ? 9.618  -13.645 30.916  1.00 8.24  ? 110 ASP A CG  1 
ATOM   920  O  OD1 . ASP A 1 108 ? 10.135 -12.744 31.580  1.00 9.27  ? 110 ASP A OD1 1 
ATOM   921  O  OD2 . ASP A 1 108 ? 8.406  -13.987 31.050  1.00 11.54 ? 110 ASP A OD2 1 
ATOM   922  N  N   . LYS A 1 109 ? 13.439 -13.630 27.771  1.00 5.61  ? 111 LYS A N   1 
ATOM   923  C  CA  . LYS A 1 109 ? 14.471 -14.188 26.871  1.00 6.01  ? 111 LYS A CA  1 
ATOM   924  C  C   . LYS A 1 109 ? 13.880 -14.699 25.578  1.00 5.74  ? 111 LYS A C   1 
ATOM   925  O  O   . LYS A 1 109 ? 14.649 -15.086 24.664  1.00 7.14  ? 111 LYS A O   1 
ATOM   926  C  CB  . LYS A 1 109 ? 15.392 -15.231 27.551  1.00 9.00  ? 111 LYS A CB  1 
ATOM   927  C  CG  . LYS A 1 109 ? 16.090 -14.704 28.818  1.00 11.64 ? 111 LYS A CG  1 
ATOM   928  C  CD  . LYS A 1 109 ? 16.995 -13.447 28.454  1.00 15.63 ? 111 LYS A CD  1 
ATOM   929  C  CE  . LYS A 1 109 ? 17.844 -12.830 29.592  1.00 16.98 ? 111 LYS A CE  1 
ATOM   930  N  NZ  . LYS A 1 109 ? 18.940 -13.684 29.913  1.00 19.13 ? 111 LYS A NZ  1 
ATOM   931  N  N   . LYS A 1 110 ? 12.566 -14.680 25.371  1.00 4.76  ? 112 LYS A N   1 
ATOM   932  C  CA  . LYS A 1 110 ? 12.011 -15.109 24.086  1.00 5.22  ? 112 LYS A CA  1 
ATOM   933  C  C   . LYS A 1 110 ? 12.310 -14.050 23.013  1.00 5.07  ? 112 LYS A C   1 
ATOM   934  O  O   . LYS A 1 110 ? 12.079 -12.824 23.220  1.00 4.81  ? 112 LYS A O   1 
ATOM   935  C  CB  . LYS A 1 110 ? 10.478 -15.139 24.202  1.00 6.03  ? 112 LYS A CB  1 
ATOM   936  C  CG  . LYS A 1 110 ? 9.778  -15.549 22.858  1.00 8.01  ? 112 LYS A CG  1 
ATOM   937  C  CD  . LYS A 1 110 ? 8.229  -15.461 22.962  1.00 8.84  ? 112 LYS A CD  1 
ATOM   938  C  CE  . LYS A 1 110 ? 7.641  -15.683 21.610  1.00 10.09 ? 112 LYS A CE  1 
ATOM   939  N  NZ  . LYS A 1 110 ? 7.830  -17.050 21.151  1.00 10.77 ? 112 LYS A NZ  1 
ATOM   940  N  N   A LYS A 1 111 ? 12.858 -14.505 21.905  0.50 5.18  ? 113 LYS A N   1 
ATOM   941  N  N   B LYS A 1 111 ? 12.853 -14.508 21.904  0.50 5.19  ? 113 LYS A N   1 
ATOM   942  C  CA  A LYS A 1 111 ? 13.045 -13.711 20.674  0.50 5.00  ? 113 LYS A CA  1 
ATOM   943  C  CA  B LYS A 1 111 ? 13.047 -13.708 20.680  0.50 4.90  ? 113 LYS A CA  1 
ATOM   944  C  C   A LYS A 1 111 ? 11.904 -13.906 19.729  0.50 5.22  ? 113 LYS A C   1 
ATOM   945  C  C   B LYS A 1 111 ? 11.908 -13.904 19.727  0.50 5.25  ? 113 LYS A C   1 
ATOM   946  O  O   A LYS A 1 111 ? 11.548 -15.049 19.436  0.50 6.30  ? 113 LYS A O   1 
ATOM   947  O  O   B LYS A 1 111 ? 11.565 -15.044 19.420  0.50 6.18  ? 113 LYS A O   1 
ATOM   948  C  CB  A LYS A 1 111 ? 14.352 -14.095 20.001  0.50 6.33  ? 113 LYS A CB  1 
ATOM   949  C  CB  B LYS A 1 111 ? 14.349 -14.091 20.004  0.50 6.02  ? 113 LYS A CB  1 
ATOM   950  C  CG  A LYS A 1 111 ? 15.589 -13.784 20.805  0.50 6.53  ? 113 LYS A CG  1 
ATOM   951  C  CG  B LYS A 1 111 ? 15.621 -13.855 20.787  0.50 5.99  ? 113 LYS A CG  1 
ATOM   952  C  CD  A LYS A 1 111 ? 16.837 -14.376 20.225  0.50 8.09  ? 113 LYS A CD  1 
ATOM   953  C  CD  B LYS A 1 111 ? 16.786 -14.428 20.031  0.50 7.13  ? 113 LYS A CD  1 
ATOM   954  C  CE  A LYS A 1 111 ? 18.036 -13.815 21.022  0.50 9.89  ? 113 LYS A CE  1 
ATOM   955  C  CE  B LYS A 1 111 ? 18.126 -13.895 20.591  0.50 8.08  ? 113 LYS A CE  1 
ATOM   956  N  NZ  A LYS A 1 111 ? 19.252 -14.529 20.605  0.50 12.57 ? 113 LYS A NZ  1 
ATOM   957  N  NZ  B LYS A 1 111 ? 18.515 -14.599 21.835  0.50 8.72  ? 113 LYS A NZ  1 
ATOM   958  N  N   . TYR A 1 112 ? 11.331 -12.813 19.226  1.00 4.79  ? 114 TYR A N   1 
ATOM   959  C  CA  . TYR A 1 112 ? 10.286 -12.890 18.212  1.00 4.67  ? 114 TYR A CA  1 
ATOM   960  C  C   . TYR A 1 112 ? 10.999 -12.853 16.807  1.00 4.18  ? 114 TYR A C   1 
ATOM   961  O  O   . TYR A 1 112 ? 12.200 -12.577 16.684  1.00 4.90  ? 114 TYR A O   1 
ATOM   962  C  CB  . TYR A 1 112 ? 9.294  -11.753 18.352  1.00 4.85  ? 114 TYR A CB  1 
ATOM   963  C  CG  . TYR A 1 112 ? 8.347  -11.952 19.508  1.00 4.25  ? 114 TYR A CG  1 
ATOM   964  C  CD1 . TYR A 1 112 ? 8.643  -11.530 20.792  1.00 6.38  ? 114 TYR A CD1 1 
ATOM   965  C  CD2 . TYR A 1 112 ? 7.128  -12.594 19.281  1.00 5.31  ? 114 TYR A CD2 1 
ATOM   966  C  CE1 . TYR A 1 112 ? 7.736  -11.713 21.824  1.00 7.40  ? 114 TYR A CE1 1 
ATOM   967  C  CE2 . TYR A 1 112 ? 6.212  -12.797 20.317  1.00 8.01  ? 114 TYR A CE2 1 
ATOM   968  C  CZ  . TYR A 1 112 ? 6.540  -12.355 21.568  1.00 8.43  ? 114 TYR A CZ  1 
ATOM   969  O  OH  . TYR A 1 112 ? 5.658  -12.513 22.622  1.00 11.37 ? 114 TYR A OH  1 
ATOM   970  N  N   . ALA A 1 113 ? 10.211 -13.150 15.767  1.00 4.88  ? 115 ALA A N   1 
ATOM   971  C  CA  . ALA A 1 113 ? 10.764 -13.185 14.380  1.00 4.46  ? 115 ALA A CA  1 
ATOM   972  C  C   . ALA A 1 113 ? 11.162 -11.801 13.940  1.00 4.26  ? 115 ALA A C   1 
ATOM   973  O  O   . ALA A 1 113 ? 12.001 -11.646 13.032  1.00 5.34  ? 115 ALA A O   1 
ATOM   974  C  CB  . ALA A 1 113 ? 9.712  -13.779 13.474  1.00 6.24  ? 115 ALA A CB  1 
ATOM   975  N  N   . ALA A 1 114 ? 10.501 -10.723 14.425  1.00 3.93  ? 116 ALA A N   1 
ATOM   976  C  CA  . ALA A 1 114 ? 10.826 -9.375  13.973  1.00 4.13  ? 116 ALA A CA  1 
ATOM   977  C  C   . ALA A 1 114 ? 10.221 -8.444  14.998  1.00 3.81  ? 116 ALA A C   1 
ATOM   978  O  O   . ALA A 1 114 ? 9.478  -8.815  15.893  1.00 4.25  ? 116 ALA A O   1 
ATOM   979  C  CB  . ALA A 1 114 ? 10.261 -9.145  12.518  1.00 4.48  ? 116 ALA A CB  1 
ATOM   980  N  N   . GLU A 1 115 ? 10.562 -7.170  14.804  1.00 3.95  ? 117 GLU A N   1 
ATOM   981  C  CA  . GLU A 1 115 ? 10.035 -6.085  15.698  1.00 3.58  ? 117 GLU A CA  1 
ATOM   982  C  C   . GLU A 1 115 ? 9.849  -4.860  14.869  1.00 3.38  ? 117 GLU A C   1 
ATOM   983  O  O   . GLU A 1 115 ? 10.788 -4.448  14.135  1.00 4.46  ? 117 GLU A O   1 
ATOM   984  C  CB  . GLU A 1 115 ? 11.031 -5.875  16.879  1.00 3.08  ? 117 GLU A CB  1 
ATOM   985  C  CG  . GLU A 1 115 ? 10.520 -4.918  17.945  1.00 4.28  ? 117 GLU A CG  1 
ATOM   986  C  CD  . GLU A 1 115 ? 11.432 -4.869  19.155  1.00 3.45  ? 117 GLU A CD  1 
ATOM   987  O  OE1 . GLU A 1 115 ? 12.090 -5.880  19.443  1.00 4.55  ? 117 GLU A OE1 1 
ATOM   988  O  OE2 . GLU A 1 115 ? 11.461 -3.781  19.776  1.00 4.46  ? 117 GLU A OE2 1 
ATOM   989  N  N   . LEU A 1 116 ? 8.669  -4.263  14.963  1.00 3.40  ? 118 LEU A N   1 
ATOM   990  C  CA  . LEU A 1 116 ? 8.320  -3.011  14.278  1.00 3.04  ? 118 LEU A CA  1 
ATOM   991  C  C   . LEU A 1 116 ? 8.554  -1.853  15.264  1.00 2.91  ? 118 LEU A C   1 
ATOM   992  O  O   . LEU A 1 116 ? 8.111  -1.937  16.434  1.00 3.53  ? 118 LEU A O   1 
ATOM   993  C  CB  . LEU A 1 116 ? 6.811  -3.127  13.941  1.00 3.80  ? 118 LEU A CB  1 
ATOM   994  C  CG  . LEU A 1 116 ? 6.113  -1.820  13.579  1.00 4.30  ? 118 LEU A CG  1 
ATOM   995  C  CD1 . LEU A 1 116 ? 6.678  -1.197  12.306  1.00 5.33  ? 118 LEU A CD1 1 
ATOM   996  C  CD2 . LEU A 1 116 ? 4.618  -2.159  13.269  1.00 5.96  ? 118 LEU A CD2 1 
ATOM   997  N  N   . HIS A 1 117 ? 9.192  -0.810  14.769  1.00 3.25  ? 119 HIS A N   1 
ATOM   998  C  CA  . HIS A 1 117 ? 9.426  0.406   15.552  1.00 3.09  ? 119 HIS A CA  1 
ATOM   999  C  C   . HIS A 1 117 ? 8.745  1.564   14.853  1.00 3.35  ? 119 HIS A C   1 
ATOM   1000 O  O   . HIS A 1 117 ? 9.137  1.956   13.712  1.00 4.01  ? 119 HIS A O   1 
ATOM   1001 C  CB  . HIS A 1 117 ? 10.916 0.699   15.649  1.00 3.38  ? 119 HIS A CB  1 
ATOM   1002 C  CG  . HIS A 1 117 ? 11.591 -0.299  16.504  1.00 3.27  ? 119 HIS A CG  1 
ATOM   1003 N  ND1 . HIS A 1 117 ? 12.949 -0.565  16.519  1.00 3.06  ? 119 HIS A ND1 1 
ATOM   1004 C  CD2 . HIS A 1 117 ? 11.023 -1.072  17.509  1.00 3.26  ? 119 HIS A CD2 1 
ATOM   1005 C  CE1 . HIS A 1 117 ? 13.230 -1.458  17.427  1.00 3.23  ? 119 HIS A CE1 1 
ATOM   1006 N  NE2 . HIS A 1 117 ? 12.093 -1.827  18.038  1.00 3.48  ? 119 HIS A NE2 1 
ATOM   1007 N  N   . LEU A 1 118 ? 7.744  2.157   15.492  1.00 3.12  ? 120 LEU A N   1 
ATOM   1008 C  CA  . LEU A 1 118 ? 7.071  3.384   15.043  1.00 3.78  ? 120 LEU A CA  1 
ATOM   1009 C  C   . LEU A 1 118 ? 7.706  4.543   15.827  1.00 2.88  ? 120 LEU A C   1 
ATOM   1010 O  O   . LEU A 1 118 ? 7.563  4.591   17.061  1.00 3.53  ? 120 LEU A O   1 
ATOM   1011 C  CB  . LEU A 1 118 ? 5.593  3.281   15.272  1.00 4.21  ? 120 LEU A CB  1 
ATOM   1012 C  CG  . LEU A 1 118 ? 4.894  2.213   14.364  1.00 4.70  ? 120 LEU A CG  1 
ATOM   1013 C  CD1 . LEU A 1 118 ? 4.048  1.337   15.223  1.00 7.40  ? 120 LEU A CD1 1 
ATOM   1014 C  CD2 . LEU A 1 118 ? 4.050  2.866   13.324  1.00 6.56  ? 120 LEU A CD2 1 
ATOM   1015 N  N   . VAL A 1 119 ? 8.453  5.388   15.119  1.00 3.63  ? 121 VAL A N   1 
ATOM   1016 C  CA  . VAL A 1 119 ? 9.286  6.427   15.748  1.00 3.94  ? 121 VAL A CA  1 
ATOM   1017 C  C   . VAL A 1 119 ? 8.549  7.751   15.750  1.00 3.81  ? 121 VAL A C   1 
ATOM   1018 O  O   . VAL A 1 119 ? 8.086  8.215   14.731  1.00 4.88  ? 121 VAL A O   1 
ATOM   1019 C  CB  . VAL A 1 119 ? 10.610 6.551   14.941  1.00 4.61  ? 121 VAL A CB  1 
ATOM   1020 C  CG1 . VAL A 1 119 ? 11.494 7.640   15.561  1.00 5.39  ? 121 VAL A CG1 1 
ATOM   1021 C  CG2 . VAL A 1 119 ? 11.308 5.193   14.818  1.00 4.91  ? 121 VAL A CG2 1 
ATOM   1022 N  N   . HIS A 1 120 ? 8.475  8.379   16.924  1.00 4.12  ? 122 HIS A N   1 
ATOM   1023 C  CA  . HIS A 1 120 ? 7.777  9.628   17.130  1.00 4.06  ? 122 HIS A CA  1 
ATOM   1024 C  C   . HIS A 1 120 ? 8.657  10.612  17.903  1.00 4.31  ? 122 HIS A C   1 
ATOM   1025 O  O   . HIS A 1 120 ? 9.390  10.227  18.780  1.00 4.83  ? 122 HIS A O   1 
ATOM   1026 C  CB  . HIS A 1 120 ? 6.483  9.444   17.981  1.00 4.41  ? 122 HIS A CB  1 
ATOM   1027 C  CG  . HIS A 1 120 ? 5.629  8.314   17.550  1.00 4.31  ? 122 HIS A CG  1 
ATOM   1028 N  ND1 . HIS A 1 120 ? 5.963  6.991   17.820  1.00 4.23  ? 122 HIS A ND1 1 
ATOM   1029 C  CD2 . HIS A 1 120 ? 4.383  8.269   16.950  1.00 4.80  ? 122 HIS A CD2 1 
ATOM   1030 C  CE1 . HIS A 1 120 ? 4.962  6.197   17.397  1.00 5.27  ? 122 HIS A CE1 1 
ATOM   1031 N  NE2 . HIS A 1 120 ? 3.992  6.949   16.847  1.00 5.16  ? 122 HIS A NE2 1 
ATOM   1032 N  N   . TRP A 1 121 ? 8.549  11.905  17.573  1.00 4.30  ? 123 TRP A N   1 
ATOM   1033 C  CA  . TRP A 1 121 ? 9.320  12.932  18.263  1.00 4.05  ? 123 TRP A CA  1 
ATOM   1034 C  C   . TRP A 1 121 ? 8.416  13.897  18.979  1.00 3.74  ? 123 TRP A C   1 
ATOM   1035 O  O   . TRP A 1 121 ? 7.306  14.239  18.594  1.00 5.68  ? 123 TRP A O   1 
ATOM   1036 C  CB  . TRP A 1 121 ? 10.244 13.690  17.299  1.00 6.61  ? 123 TRP A CB  1 
ATOM   1037 C  CG  . TRP A 1 121 ? 9.589  14.302  16.092  1.00 5.81  ? 123 TRP A CG  1 
ATOM   1038 C  CD1 . TRP A 1 121 ? 9.374  13.729  14.878  1.00 7.69  ? 123 TRP A CD1 1 
ATOM   1039 C  CD2 . TRP A 1 121 ? 9.182  15.650  15.997  1.00 6.69  ? 123 TRP A CD2 1 
ATOM   1040 N  NE1 . TRP A 1 121 ? 8.776  14.598  14.022  1.00 7.70  ? 123 TRP A NE1 1 
ATOM   1041 C  CE2 . TRP A 1 121 ? 8.679  15.816  14.658  1.00 7.61  ? 123 TRP A CE2 1 
ATOM   1042 C  CE3 . TRP A 1 121 ? 9.160  16.785  16.877  1.00 9.33  ? 123 TRP A CE3 1 
ATOM   1043 C  CZ2 . TRP A 1 121 ? 8.129  17.027  14.218  1.00 10.55 ? 123 TRP A CZ2 1 
ATOM   1044 C  CZ3 . TRP A 1 121 ? 8.631  17.987  16.398  1.00 12.42 ? 123 TRP A CZ3 1 
ATOM   1045 C  CH2 . TRP A 1 121 ? 8.154  18.085  15.053  1.00 12.02 ? 123 TRP A CH2 1 
ATOM   1046 N  N   . ASN A 1 122 ? 8.973  14.371  20.126  1.00 4.95  ? 124 ASN A N   1 
ATOM   1047 C  CA  . ASN A 1 122 ? 8.236  15.251  21.072  1.00 4.74  ? 124 ASN A CA  1 
ATOM   1048 C  C   . ASN A 1 122 ? 8.132  16.656  20.440  1.00 5.26  ? 124 ASN A C   1 
ATOM   1049 O  O   . ASN A 1 122 ? 9.136  17.342  20.218  1.00 5.70  ? 124 ASN A O   1 
ATOM   1050 C  CB  . ASN A 1 122 ? 9.050  15.305  22.380  1.00 5.66  ? 124 ASN A CB  1 
ATOM   1051 C  CG  . ASN A 1 122 ? 8.242  15.905  23.478  1.00 6.34  ? 124 ASN A CG  1 
ATOM   1052 O  OD1 . ASN A 1 122 ? 7.417  16.784  23.227  1.00 6.82  ? 124 ASN A OD1 1 
ATOM   1053 N  ND2 . ASN A 1 122 ? 8.508  15.451  24.710  1.00 7.39  ? 124 ASN A ND2 1 
ATOM   1054 N  N   . THR A 1 123 ? 6.871  17.076  20.219  1.00 6.15  ? 125 THR A N   1 
ATOM   1055 C  CA  . THR A 1 123 ? 6.677  18.334  19.509  1.00 7.67  ? 125 THR A CA  1 
ATOM   1056 C  C   . THR A 1 123 ? 7.180  19.537  20.271  1.00 7.66  ? 125 THR A C   1 
ATOM   1057 O  O   . THR A 1 123 ? 7.305  20.606  19.712  1.00 8.36  ? 125 THR A O   1 
ATOM   1058 C  CB  . THR A 1 123 ? 5.197  18.474  19.067  1.00 10.05 ? 125 THR A CB  1 
ATOM   1059 O  OG1 . THR A 1 123 ? 4.350  18.452  20.227  1.00 14.64 ? 125 THR A OG1 1 
ATOM   1060 C  CG2 . THR A 1 123 ? 4.788  17.385  18.057  1.00 11.84 ? 125 THR A CG2 1 
ATOM   1061 N  N   A LYS A 1 124 ? 7.414  19.382  21.672  0.50 7.24  ? 126 LYS A N   1 
ATOM   1062 N  N   B LYS A 1 124 ? 7.410  19.379  21.630  0.50 7.09  ? 126 LYS A N   1 
ATOM   1063 C  CA  A LYS A 1 124 ? 7.928  20.482  22.434  0.50 7.19  ? 126 LYS A CA  1 
ATOM   1064 C  CA  B LYS A 1 124 ? 7.875  20.527  22.344  0.50 7.21  ? 126 LYS A CA  1 
ATOM   1065 C  C   A LYS A 1 124 ? 9.328  20.939  21.948  0.50 6.87  ? 126 LYS A C   1 
ATOM   1066 C  C   B LYS A 1 124 ? 9.321  20.939  21.940  0.50 6.78  ? 126 LYS A C   1 
ATOM   1067 O  O   A LYS A 1 124 ? 9.764  22.042  22.273  0.50 9.16  ? 126 LYS A O   1 
ATOM   1068 O  O   B LYS A 1 124 ? 9.780  22.013  22.316  0.50 8.74  ? 126 LYS A O   1 
ATOM   1069 C  CB  A LYS A 1 124 ? 7.950  20.162  23.939  0.50 9.39  ? 126 LYS A CB  1 
ATOM   1070 C  CB  B LYS A 1 124 ? 7.755  20.315  23.846  0.50 9.85  ? 126 LYS A CB  1 
ATOM   1071 C  CG  A LYS A 1 124 ? 9.162  19.420  24.453  0.50 9.47  ? 126 LYS A CG  1 
ATOM   1072 C  CG  B LYS A 1 124 ? 8.792  19.411  24.455  0.50 8.93  ? 126 LYS A CG  1 
ATOM   1073 C  CD  A LYS A 1 124 ? 8.961  18.983  25.916  0.50 10.64 ? 126 LYS A CD  1 
ATOM   1074 C  CD  B LYS A 1 124 ? 8.460  19.281  25.947  0.50 10.82 ? 126 LYS A CD  1 
ATOM   1075 C  CE  A LYS A 1 124 ? 9.240  20.145  26.850  0.50 12.99 ? 126 LYS A CE  1 
ATOM   1076 C  CE  B LYS A 1 124 ? 9.482  18.427  26.617  0.50 11.49 ? 126 LYS A CE  1 
ATOM   1077 N  NZ  A LYS A 1 124 ? 9.007  19.640  28.283  0.50 16.07 ? 126 LYS A NZ  1 
ATOM   1078 N  NZ  B LYS A 1 124 ? 9.092  17.914  27.965  0.50 12.95 ? 126 LYS A NZ  1 
ATOM   1079 N  N   . TYR A 1 125 ? 10.018 20.094  21.139  1.00 6.74  ? 127 TYR A N   1 
ATOM   1080 C  CA  . TYR A 1 125 ? 11.349 20.409  20.678  1.00 7.32  ? 127 TYR A CA  1 
ATOM   1081 C  C   . TYR A 1 125 ? 11.372 20.842  19.232  1.00 6.82  ? 127 TYR A C   1 
ATOM   1082 O  O   . TYR A 1 125 ? 12.483 21.102  18.679  1.00 8.26  ? 127 TYR A O   1 
ATOM   1083 C  CB  . TYR A 1 125 ? 12.355 19.232  20.929  1.00 7.43  ? 127 TYR A CB  1 
ATOM   1084 C  CG  . TYR A 1 125 ? 12.421 18.912  22.380  1.00 5.99  ? 127 TYR A CG  1 
ATOM   1085 C  CD1 . TYR A 1 125 ? 12.776 19.904  23.349  1.00 7.34  ? 127 TYR A CD1 1 
ATOM   1086 C  CD2 . TYR A 1 125 ? 12.090 17.617  22.836  1.00 6.37  ? 127 TYR A CD2 1 
ATOM   1087 C  CE1 . TYR A 1 125 ? 12.819 19.539  24.711  1.00 7.80  ? 127 TYR A CE1 1 
ATOM   1088 C  CE2 . TYR A 1 125 ? 12.184 17.292  24.203  1.00 6.46  ? 127 TYR A CE2 1 
ATOM   1089 C  CZ  . TYR A 1 125 ? 12.541 18.292  25.141  1.00 6.69  ? 127 TYR A CZ  1 
ATOM   1090 O  OH  . TYR A 1 125 ? 12.546 18.030  26.475  1.00 9.57  ? 127 TYR A OH  1 
ATOM   1091 N  N   . GLY A 1 126 ? 10.195 20.963  18.604  1.00 6.98  ? 128 GLY A N   1 
ATOM   1092 C  CA  . GLY A 1 126 ? 10.103 21.673  17.314  1.00 8.70  ? 128 GLY A CA  1 
ATOM   1093 C  C   . GLY A 1 126 ? 10.490 20.820  16.091  1.00 8.29  ? 128 GLY A C   1 
ATOM   1094 O  O   . GLY A 1 126 ? 9.851  20.978  15.058  1.00 10.36 ? 128 GLY A O   1 
ATOM   1095 N  N   A ASP A 1 127 ? 11.486 19.953  16.143  0.50 8.85  ? 129 ASP A N   1 
ATOM   1096 N  N   B ASP A 1 127 ? 11.672 20.138  16.132  0.50 10.44 ? 129 ASP A N   1 
ATOM   1097 C  CA  A ASP A 1 127 ? 11.566 19.022  15.036  0.50 8.02  ? 129 ASP A CA  1 
ATOM   1098 C  CA  B ASP A 1 127 ? 12.177 19.285  15.008  0.50 8.24  ? 129 ASP A CA  1 
ATOM   1099 C  C   A ASP A 1 127 ? 12.331 17.842  15.589  0.50 8.35  ? 129 ASP A C   1 
ATOM   1100 C  C   B ASP A 1 127 ? 12.827 17.998  15.501  0.50 8.58  ? 129 ASP A C   1 
ATOM   1101 O  O   A ASP A 1 127 ? 12.695 17.781  16.813  0.50 8.06  ? 129 ASP A O   1 
ATOM   1102 O  O   B ASP A 1 127 ? 13.406 17.953  16.666  0.50 6.18  ? 129 ASP A O   1 
ATOM   1103 C  CB  A ASP A 1 127 ? 12.228 19.548  13.749  0.50 8.88  ? 129 ASP A CB  1 
ATOM   1104 C  CB  B ASP A 1 127 ? 13.024 20.045  13.933  0.50 6.79  ? 129 ASP A CB  1 
ATOM   1105 C  CG  A ASP A 1 127 ? 13.607 20.066  13.985  0.50 8.50  ? 129 ASP A CG  1 
ATOM   1106 C  CG  B ASP A 1 127 ? 14.499 20.351  14.341  0.50 7.88  ? 129 ASP A CG  1 
ATOM   1107 O  OD1 A ASP A 1 127 ? 14.146 19.858  15.093  0.50 10.53 ? 129 ASP A OD1 1 
ATOM   1108 O  OD1 B ASP A 1 127 ? 15.327 19.526  14.731  0.50 8.73  ? 129 ASP A OD1 1 
ATOM   1109 O  OD2 A ASP A 1 127 ? 14.162 20.724  13.087  0.50 11.35 ? 129 ASP A OD2 1 
ATOM   1110 O  OD2 B ASP A 1 127 ? 14.879 21.480  14.178  0.50 11.26 ? 129 ASP A OD2 1 
ATOM   1111 N  N   . PHE A 1 128 ? 12.684 16.914  14.691  1.00 9.30  ? 130 PHE A N   1 
ATOM   1112 C  CA  . PHE A 1 128 ? 13.265 15.623  15.103  1.00 8.20  ? 130 PHE A CA  1 
ATOM   1113 C  C   . PHE A 1 128 ? 14.733 15.818  15.519  1.00 6.90  ? 130 PHE A C   1 
ATOM   1114 O  O   . PHE A 1 128 ? 15.200 15.197  16.488  1.00 6.65  ? 130 PHE A O   1 
ATOM   1115 C  CB  . PHE A 1 128 ? 13.216 14.684  13.859  1.00 8.60  ? 130 PHE A CB  1 
ATOM   1116 C  CG  . PHE A 1 128 ? 13.806 13.315  14.149  1.00 7.36  ? 130 PHE A CG  1 
ATOM   1117 C  CD1 . PHE A 1 128 ? 13.030 12.345  14.790  1.00 7.85  ? 130 PHE A CD1 1 
ATOM   1118 C  CD2 . PHE A 1 128 ? 15.144 12.991  13.878  1.00 9.00  ? 130 PHE A CD2 1 
ATOM   1119 C  CE1 . PHE A 1 128 ? 13.495 11.117  15.051  1.00 8.97  ? 130 PHE A CE1 1 
ATOM   1120 C  CE2 . PHE A 1 128 ? 15.604 11.714  14.159  1.00 10.40 ? 130 PHE A CE2 1 
ATOM   1121 C  CZ  . PHE A 1 128 ? 14.787 10.802  14.788  1.00 10.30 ? 130 PHE A CZ  1 
ATOM   1122 N  N   . GLY A 1 129 ? 15.521 16.585  14.736  1.00 9.76  ? 131 GLY A N   1 
ATOM   1123 C  CA  . GLY A 1 129 ? 16.927 16.683  15.051  1.00 10.09 ? 131 GLY A CA  1 
ATOM   1124 C  C   . GLY A 1 129 ? 17.199 17.322  16.418  1.00 9.85  ? 131 GLY A C   1 
ATOM   1125 O  O   . GLY A 1 129 ? 18.216 17.000  17.077  1.00 10.88 ? 131 GLY A O   1 
ATOM   1126 N  N   . LYS A 1 130 ? 16.348 18.265  16.854  1.00 9.15  ? 132 LYS A N   1 
ATOM   1127 C  CA  . LYS A 1 130 ? 16.497 18.825  18.190  1.00 7.66  ? 132 LYS A CA  1 
ATOM   1128 C  C   . LYS A 1 130 ? 15.979 17.814  19.167  1.00 6.72  ? 132 LYS A C   1 
ATOM   1129 O  O   . LYS A 1 130 ? 16.552 17.667  20.246  1.00 7.45  ? 132 LYS A O   1 
ATOM   1130 C  CB  . LYS A 1 130 ? 15.717 20.133  18.318  1.00 8.77  ? 132 LYS A CB  1 
ATOM   1131 C  CG  . LYS A 1 130 ? 16.220 21.247  17.414  1.00 14.32 ? 132 LYS A CG  1 
ATOM   1132 C  CD  . LYS A 1 130 ? 17.738 21.316  17.415  1.00 20.49 ? 132 LYS A CD  1 
ATOM   1133 C  CE  . LYS A 1 130 ? 18.271 21.729  18.778  1.00 25.81 ? 132 LYS A CE  1 
ATOM   1134 N  NZ  . LYS A 1 130 ? 18.865 23.094  18.751  1.00 40.32 ? 132 LYS A NZ  1 
ATOM   1135 N  N   . ALA A 1 131 ? 14.908 17.100  18.842  1.00 6.90  ? 133 ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 131 ? 14.351 16.132  19.847  1.00 6.51  ? 133 ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 131 ? 15.345 15.077  20.234  1.00 6.06  ? 133 ALA A C   1 
ATOM   1138 O  O   . ALA A 1 131 ? 15.370 14.644  21.388  1.00 6.40  ? 133 ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 131 ? 13.076 15.501  19.273  1.00 5.65  ? 133 ALA A CB  1 
ATOM   1140 N  N   . VAL A 1 132 ? 16.127 14.565  19.288  1.00 6.44  ? 134 VAL A N   1 
ATOM   1141 C  CA  . VAL A 1 132 ? 17.045 13.454  19.625  1.00 7.27  ? 134 VAL A CA  1 
ATOM   1142 C  C   . VAL A 1 132 ? 18.169 13.864  20.571  1.00 6.83  ? 134 VAL A C   1 
ATOM   1143 O  O   . VAL A 1 132 ? 18.878 12.985  21.059  1.00 8.12  ? 134 VAL A O   1 
ATOM   1144 C  CB  . VAL A 1 132 ? 17.654 12.765  18.396  1.00 9.04  ? 134 VAL A CB  1 
ATOM   1145 C  CG1 . VAL A 1 132 ? 16.560 12.146  17.555  1.00 10.31 ? 134 VAL A CG1 1 
ATOM   1146 C  CG2 . VAL A 1 132 ? 18.583 13.643  17.574  1.00 8.88  ? 134 VAL A CG2 1 
ATOM   1147 N  N   . GLN A 1 133 ? 18.275 15.206  20.814  1.00 6.63  ? 135 GLN A N   1 
ATOM   1148 C  CA  . GLN A 1 133 ? 19.268 15.656  21.756  1.00 8.25  ? 135 GLN A CA  1 
ATOM   1149 C  C   . GLN A 1 133 ? 18.718 15.777  23.181  1.00 6.75  ? 135 GLN A C   1 
ATOM   1150 O  O   . GLN A 1 133 ? 19.411 16.283  24.076  1.00 9.62  ? 135 GLN A O   1 
ATOM   1151 C  CB  . GLN A 1 133 ? 19.785 17.044  21.276  1.00 9.54  ? 135 GLN A CB  1 
ATOM   1152 C  CG  . GLN A 1 133 ? 20.507 16.921  19.935  1.00 12.60 ? 135 GLN A CG  1 
ATOM   1153 C  CD  . GLN A 1 133 ? 21.002 18.233  19.407  1.00 18.55 ? 135 GLN A CD  1 
ATOM   1154 O  OE1 . GLN A 1 133 ? 21.866 18.869  20.101  1.00 26.18 ? 135 GLN A OE1 1 
ATOM   1155 N  NE2 . GLN A 1 133 ? 20.389 18.728  18.308  1.00 20.75 ? 135 GLN A NE2 1 
ATOM   1156 N  N   A GLN A 1 134 ? 17.465 15.332  23.411  0.50 5.96  ? 136 GLN A N   1 
ATOM   1157 N  N   B GLN A 1 134 ? 17.535 15.235  23.428  0.50 6.50  ? 136 GLN A N   1 
ATOM   1158 C  CA  A GLN A 1 134 ? 16.770 15.496  24.684  0.50 5.36  ? 136 GLN A CA  1 
ATOM   1159 C  CA  B GLN A 1 134 ? 16.961 15.410  24.723  0.50 6.70  ? 136 GLN A CA  1 
ATOM   1160 C  C   A GLN A 1 134 ? 16.391 14.123  25.273  0.50 5.69  ? 136 GLN A C   1 
ATOM   1161 C  C   B GLN A 1 134 ? 16.629 14.061  25.308  0.50 7.64  ? 136 GLN A C   1 
ATOM   1162 O  O   A GLN A 1 134 ? 16.002 13.196  24.539  0.50 2.94  ? 136 GLN A O   1 
ATOM   1163 O  O   B GLN A 1 134 ? 16.370 13.110  24.551  0.50 7.77  ? 136 GLN A O   1 
ATOM   1164 C  CB  A GLN A 1 134 ? 15.501 16.285  24.477  0.50 5.77  ? 136 GLN A CB  1 
ATOM   1165 C  CB  B GLN A 1 134 ? 15.701 16.205  24.590  0.50 6.85  ? 136 GLN A CB  1 
ATOM   1166 C  CG  A GLN A 1 134 ? 15.724 17.688  23.919  0.50 7.60  ? 136 GLN A CG  1 
ATOM   1167 C  CG  B GLN A 1 134 ? 15.808 17.354  23.641  0.50 10.14 ? 136 GLN A CG  1 
ATOM   1168 C  CD  A GLN A 1 134 ? 16.609 18.538  24.845  0.50 8.58  ? 136 GLN A CD  1 
ATOM   1169 C  CD  B GLN A 1 134 ? 16.691 18.452  24.015  0.50 12.12 ? 136 GLN A CD  1 
ATOM   1170 O  OE1 A GLN A 1 134 ? 16.678 18.266  25.987  0.50 13.76 ? 136 GLN A OE1 1 
ATOM   1171 O  OE1 B GLN A 1 134 ? 16.945 18.755  25.188  0.50 17.60 ? 136 GLN A OE1 1 
ATOM   1172 N  NE2 A GLN A 1 134 ? 17.275 19.615  24.323  0.50 17.95 ? 136 GLN A NE2 1 
ATOM   1173 N  NE2 B GLN A 1 134 ? 17.132 19.162  22.978  0.50 17.97 ? 136 GLN A NE2 1 
ATOM   1174 N  N   A PRO A 1 135 ? 16.460 13.959  26.592  0.50 5.54  ? 137 PRO A N   1 
ATOM   1175 N  N   B PRO A 1 135 ? 16.561 13.951  26.637  0.50 7.01  ? 137 PRO A N   1 
ATOM   1176 C  CA  A PRO A 1 135 ? 16.258 12.612  27.155  0.50 5.33  ? 137 PRO A CA  1 
ATOM   1177 C  CA  B PRO A 1 135 ? 16.242 12.655  27.278  0.50 6.22  ? 137 PRO A CA  1 
ATOM   1178 C  C   A PRO A 1 135 ? 14.831 12.116  26.932  0.50 6.23  ? 137 PRO A C   1 
ATOM   1179 C  C   B PRO A 1 135 ? 14.808 12.149  27.113  0.50 7.14  ? 137 PRO A C   1 
ATOM   1180 O  O   A PRO A 1 135 ? 14.603 10.896  26.880  0.50 6.82  ? 137 PRO A O   1 
ATOM   1181 O  O   B PRO A 1 135 ? 14.557 10.951  27.314  0.50 7.86  ? 137 PRO A O   1 
ATOM   1182 C  CB  A PRO A 1 135 ? 16.566 12.759  28.634  0.50 6.67  ? 137 PRO A CB  1 
ATOM   1183 C  CB  B PRO A 1 135 ? 16.477 12.869  28.778  0.50 9.44  ? 137 PRO A CB  1 
ATOM   1184 C  CG  A PRO A 1 135 ? 16.360 14.239  28.872  0.50 6.07  ? 137 PRO A CG  1 
ATOM   1185 C  CG  B PRO A 1 135 ? 17.302 14.116  28.872  0.50 12.86 ? 137 PRO A CG  1 
ATOM   1186 C  CD  A PRO A 1 135 ? 16.874 14.929  27.617  0.50 7.30  ? 137 PRO A CD  1 
ATOM   1187 C  CD  B PRO A 1 135 ? 17.247 14.885  27.557  0.50 8.69  ? 137 PRO A CD  1 
ATOM   1188 N  N   . ASP A 1 136 ? 13.883 13.061  26.764  1.00 5.63  ? 138 ASP A N   1 
ATOM   1189 C  CA  . ASP A 1 136 ? 12.480 12.747  26.508  1.00 6.46  ? 138 ASP A CA  1 
ATOM   1190 C  C   . ASP A 1 136 ? 12.155 13.196  25.069  1.00 4.61  ? 138 ASP A C   1 
ATOM   1191 O  O   . ASP A 1 136 ? 11.022 13.616  24.817  1.00 5.80  ? 138 ASP A O   1 
ATOM   1192 C  CB  . ASP A 1 136 ? 11.552 13.376  27.547  1.00 7.30  ? 138 ASP A CB  1 
ATOM   1193 C  CG  . ASP A 1 136 ? 11.620 14.885  27.597  1.00 8.06  ? 138 ASP A CG  1 
ATOM   1194 O  OD1 . ASP A 1 136 ? 12.552 15.448  26.979  1.00 8.07  ? 138 ASP A OD1 1 
ATOM   1195 O  OD2 . ASP A 1 136 ? 10.794 15.492  28.266  1.00 10.96 ? 138 ASP A OD2 1 
ATOM   1196 N  N   . GLY A 1 137 ? 13.096 13.054  24.141  1.00 4.63  ? 139 GLY A N   1 
ATOM   1197 C  CA  . GLY A 1 137 ? 12.822 13.574  22.776  1.00 5.33  ? 139 GLY A CA  1 
ATOM   1198 C  C   . GLY A 1 137 ? 11.997 12.684  21.898  1.00 3.79  ? 139 GLY A C   1 
ATOM   1199 O  O   . GLY A 1 137 ? 11.289 13.159  21.025  1.00 5.07  ? 139 GLY A O   1 
ATOM   1200 N  N   . LEU A 1 138 ? 12.164 11.343  22.092  1.00 3.57  ? 140 LEU A N   1 
ATOM   1201 C  CA  . LEU A 1 138 ? 11.481 10.387  21.199  1.00 3.92  ? 140 LEU A CA  1 
ATOM   1202 C  C   . LEU A 1 138 ? 10.645 9.454   22.004  1.00 3.71  ? 140 LEU A C   1 
ATOM   1203 O  O   . LEU A 1 138 ? 10.923 9.149   23.162  1.00 4.26  ? 140 LEU A O   1 
ATOM   1204 C  CB  . LEU A 1 138 ? 12.489 9.517   20.403  1.00 4.37  ? 140 LEU A CB  1 
ATOM   1205 C  CG  . LEU A 1 138 ? 13.363 10.249  19.359  1.00 5.03  ? 140 LEU A CG  1 
ATOM   1206 C  CD1 . LEU A 1 138 ? 14.128 9.250   18.533  1.00 5.71  ? 140 LEU A CD1 1 
ATOM   1207 C  CD2 . LEU A 1 138 ? 12.731 11.283  18.463  1.00 7.10  ? 140 LEU A CD2 1 
ATOM   1208 N  N   . ALA A 1 139 ? 9.586  8.931   21.349  1.00 4.08  ? 141 ALA A N   1 
ATOM   1209 C  CA  . ALA A 1 139 ? 8.802  7.816   21.897  1.00 3.75  ? 141 ALA A CA  1 
ATOM   1210 C  C   . ALA A 1 139 ? 8.732  6.821   20.764  1.00 3.90  ? 141 ALA A C   1 
ATOM   1211 O  O   . ALA A 1 139 ? 8.367  7.142   19.632  1.00 4.26  ? 141 ALA A O   1 
ATOM   1212 C  CB  . ALA A 1 139 ? 7.413  8.264   22.287  1.00 4.75  ? 141 ALA A CB  1 
ATOM   1213 N  N   . VAL A 1 140 ? 9.182  5.566   21.029  1.00 3.47  ? 142 VAL A N   1 
ATOM   1214 C  CA  . VAL A 1 140 ? 9.115  4.495   20.016  1.00 3.24  ? 142 VAL A CA  1 
ATOM   1215 C  C   . VAL A 1 140 ? 8.118  3.490   20.478  1.00 3.17  ? 142 VAL A C   1 
ATOM   1216 O  O   . VAL A 1 140 ? 8.196  2.982   21.627  1.00 3.53  ? 142 VAL A O   1 
ATOM   1217 C  CB  . VAL A 1 140 ? 10.485 3.872   19.715  1.00 3.94  ? 142 VAL A CB  1 
ATOM   1218 C  CG1 . VAL A 1 140 ? 10.296 2.862   18.615  1.00 5.93  ? 142 VAL A CG1 1 
ATOM   1219 C  CG2 . VAL A 1 140 ? 11.450 4.958   19.252  1.00 5.83  ? 142 VAL A CG2 1 
ATOM   1220 N  N   . LEU A 1 141 ? 7.123  3.209   19.611  1.00 3.50  ? 143 LEU A N   1 
ATOM   1221 C  CA  . LEU A 1 141 ? 6.154  2.154   19.893  1.00 3.83  ? 143 LEU A CA  1 
ATOM   1222 C  C   . LEU A 1 141 ? 6.730  0.935   19.215  1.00 3.22  ? 143 LEU A C   1 
ATOM   1223 O  O   . LEU A 1 141 ? 6.915  0.880   17.991  1.00 4.45  ? 143 LEU A O   1 
ATOM   1224 C  CB  . LEU A 1 141 ? 4.804  2.592   19.295  1.00 5.20  ? 143 LEU A CB  1 
ATOM   1225 C  CG  . LEU A 1 141 ? 3.664  1.577   19.453  1.00 6.01  ? 143 LEU A CG  1 
ATOM   1226 C  CD1 . LEU A 1 141 ? 3.405  1.281   20.919  1.00 8.16  ? 143 LEU A CD1 1 
ATOM   1227 C  CD2 . LEU A 1 141 ? 2.360  2.152   18.832  1.00 7.63  ? 143 LEU A CD2 1 
ATOM   1228 N  N   . GLY A 1 142 ? 7.027  -0.079  20.018  1.00 3.30  ? 144 GLY A N   1 
ATOM   1229 C  CA  . GLY A 1 142 ? 7.600  -1.335  19.530  1.00 3.06  ? 144 GLY A CA  1 
ATOM   1230 C  C   . GLY A 1 142 ? 6.572  -2.453  19.570  1.00 2.71  ? 144 GLY A C   1 
ATOM   1231 O  O   . GLY A 1 142 ? 5.829  -2.590  20.523  1.00 4.26  ? 144 GLY A O   1 
ATOM   1232 N  N   . ILE A 1 143 ? 6.493  -3.181  18.426  1.00 3.06  ? 145 ILE A N   1 
ATOM   1233 C  CA  . ILE A 1 143 ? 5.430  -4.236  18.292  1.00 3.06  ? 145 ILE A CA  1 
ATOM   1234 C  C   . ILE A 1 143 ? 6.176  -5.456  17.787  1.00 3.08  ? 145 ILE A C   1 
ATOM   1235 O  O   . ILE A 1 143 ? 6.878  -5.431  16.745  1.00 4.39  ? 145 ILE A O   1 
ATOM   1236 C  CB  . ILE A 1 143 ? 4.358  -3.745  17.296  1.00 4.01  ? 145 ILE A CB  1 
ATOM   1237 C  CG1 . ILE A 1 143 ? 3.728  -2.469  17.827  1.00 5.55  ? 145 ILE A CG1 1 
ATOM   1238 C  CG2 . ILE A 1 143 ? 3.353  -4.873  17.086  1.00 6.02  ? 145 ILE A CG2 1 
ATOM   1239 C  CD1 . ILE A 1 143 ? 2.686  -1.856  16.886  1.00 4.97  ? 145 ILE A CD1 1 
ATOM   1240 N  N   . PHE A 1 144 ? 6.003  -6.573  18.452  1.00 3.07  ? 146 PHE A N   1 
ATOM   1241 C  CA  . PHE A 1 144 ? 6.638  -7.848  18.046  1.00 3.75  ? 146 PHE A CA  1 
ATOM   1242 C  C   . PHE A 1 144 ? 5.840  -8.476  16.894  1.00 3.64  ? 146 PHE A C   1 
ATOM   1243 O  O   . PHE A 1 144 ? 4.621  -8.329  16.813  1.00 4.67  ? 146 PHE A O   1 
ATOM   1244 C  CB  . PHE A 1 144 ? 6.610  -8.791  19.211  1.00 3.69  ? 146 PHE A CB  1 
ATOM   1245 C  CG  . PHE A 1 144 ? 7.438  -8.364  20.372  1.00 3.19  ? 146 PHE A CG  1 
ATOM   1246 C  CD1 . PHE A 1 144 ? 8.825  -8.151  20.223  1.00 3.79  ? 146 PHE A CD1 1 
ATOM   1247 C  CD2 . PHE A 1 144 ? 6.935  -8.120  21.637  1.00 4.12  ? 146 PHE A CD2 1 
ATOM   1248 C  CE1 . PHE A 1 144 ? 9.655  -7.822  21.268  1.00 3.60  ? 146 PHE A CE1 1 
ATOM   1249 C  CE2 . PHE A 1 144 ? 7.751  -7.756  22.685  1.00 3.83  ? 146 PHE A CE2 1 
ATOM   1250 C  CZ  . PHE A 1 144 ? 9.099  -7.612  22.527  1.00 4.01  ? 146 PHE A CZ  1 
ATOM   1251 N  N   . LEU A 1 145 ? 6.580  -9.179  16.055  1.00 4.28  ? 147 LEU A N   1 
ATOM   1252 C  CA  . LEU A 1 145 ? 6.006  -9.968  14.977  1.00 4.66  ? 147 LEU A CA  1 
ATOM   1253 C  C   . LEU A 1 145 ? 6.339  -11.441 15.202  1.00 4.59  ? 147 LEU A C   1 
ATOM   1254 O  O   . LEU A 1 145 ? 7.507  -11.796 15.454  1.00 5.21  ? 147 LEU A O   1 
ATOM   1255 C  CB  . LEU A 1 145 ? 6.607  -9.591  13.589  1.00 5.30  ? 147 LEU A CB  1 
ATOM   1256 C  CG  . LEU A 1 145 ? 6.017  -8.343  12.940  1.00 5.50  ? 147 LEU A CG  1 
ATOM   1257 C  CD1 . LEU A 1 145 ? 6.258  -7.072  13.764  1.00 6.26  ? 147 LEU A CD1 1 
ATOM   1258 C  CD2 . LEU A 1 145 ? 6.677  -8.125  11.528  1.00 7.02  ? 147 LEU A CD2 1 
ATOM   1259 N  N   . LYS A 1 146 ? 5.297  -12.290 15.114  1.00 4.92  ? 148 LYS A N   1 
ATOM   1260 C  CA  . LYS A 1 146 ? 5.484  -13.724 15.059  1.00 5.16  ? 148 LYS A CA  1 
ATOM   1261 C  C   . LYS A 1 146 ? 4.971  -14.236 13.712  1.00 6.21  ? 148 LYS A C   1 
ATOM   1262 O  O   . LYS A 1 146 ? 4.148  -13.599 13.054  1.00 7.43  ? 148 LYS A O   1 
ATOM   1263 C  CB  . LYS A 1 146 ? 4.740  -14.410 16.205  1.00 7.22  ? 148 LYS A CB  1 
ATOM   1264 C  CG  . LYS A 1 146 ? 3.226  -14.332 16.098  1.00 9.19  ? 148 LYS A CG  1 
ATOM   1265 C  CD  . LYS A 1 146 ? 2.553  -14.824 17.371  1.00 16.45 ? 148 LYS A CD  1 
ATOM   1266 C  CE  . LYS A 1 146 ? 1.116  -15.236 17.113  1.00 21.85 ? 148 LYS A CE  1 
ATOM   1267 N  NZ  . LYS A 1 146 ? 0.581  -16.103 18.201  1.00 35.59 ? 148 LYS A NZ  1 
ATOM   1268 N  N   . VAL A 1 147 ? 5.475  -15.390 13.328  1.00 6.42  ? 149 VAL A N   1 
ATOM   1269 C  CA  . VAL A 1 147 ? 5.086  -15.983 12.028  1.00 7.52  ? 149 VAL A CA  1 
ATOM   1270 C  C   . VAL A 1 147 ? 3.890  -16.879 12.232  1.00 7.66  ? 149 VAL A C   1 
ATOM   1271 O  O   . VAL A 1 147 ? 3.959  -17.906 12.993  1.00 10.28 ? 149 VAL A O   1 
ATOM   1272 C  CB  . VAL A 1 147 ? 6.292  -16.720 11.441  1.00 8.20  ? 149 VAL A CB  1 
ATOM   1273 C  CG1 . VAL A 1 147 ? 5.915  -17.478 10.129  1.00 10.84 ? 149 VAL A CG1 1 
ATOM   1274 C  CG2 . VAL A 1 147 ? 7.348  -15.678 11.120  1.00 10.29 ? 149 VAL A CG2 1 
ATOM   1275 N  N   . GLY A 1 148 ? 2.845  -16.649 11.469  1.00 8.21  ? 150 GLY A N   1 
ATOM   1276 C  CA  . GLY A 1 148 ? 1.611  -17.521 11.535  1.00 10.84 ? 150 GLY A CA  1 
ATOM   1277 C  C   . GLY A 1 148 ? 0.733  -17.051 10.402  1.00 8.97  ? 150 GLY A C   1 
ATOM   1278 O  O   . GLY A 1 148 ? 1.130  -17.130 9.197   1.00 10.57 ? 150 GLY A O   1 
ATOM   1279 N  N   A SER A 1 149 ? -0.450 -16.553 10.737  0.50 10.00 ? 151 SER A N   1 
ATOM   1280 N  N   B SER A 1 149 ? -0.437 -16.549 10.771  0.50 9.85  ? 151 SER A N   1 
ATOM   1281 C  CA  A SER A 1 149 ? -1.352 -15.982 9.707   0.50 11.13 ? 151 SER A CA  1 
ATOM   1282 C  CA  B SER A 1 149 ? -1.344 -15.892 9.801   0.50 10.44 ? 151 SER A CA  1 
ATOM   1283 C  C   A SER A 1 149 ? -0.842 -14.655 9.193   0.50 9.04  ? 151 SER A C   1 
ATOM   1284 C  C   B SER A 1 149 ? -0.689 -14.683 9.151   0.50 8.92  ? 151 SER A C   1 
ATOM   1285 O  O   A SER A 1 149 ? -0.236 -13.861 9.941   0.50 8.84  ? 151 SER A O   1 
ATOM   1286 O  O   B SER A 1 149 ? 0.196  -14.022 9.759   0.50 8.62  ? 151 SER A O   1 
ATOM   1287 C  CB  A SER A 1 149 ? -2.743 -15.778 10.281  0.50 17.12 ? 151 SER A CB  1 
ATOM   1288 C  CB  B SER A 1 149 ? -2.654 -15.501 10.494  0.50 13.69 ? 151 SER A CB  1 
ATOM   1289 O  OG  A SER A 1 149 ? -2.714 -14.735 11.220  0.50 19.18 ? 151 SER A OG  1 
ATOM   1290 O  OG  B SER A 1 149 ? -3.323 -16.667 10.940  0.50 15.40 ? 151 SER A OG  1 
ATOM   1291 N  N   . ALA A 1 150 ? -1.064 -14.393 7.885   1.00 10.05 ? 152 ALA A N   1 
ATOM   1292 C  CA  . ALA A 1 150 ? -0.659 -13.128 7.291   1.00 8.48  ? 152 ALA A CA  1 
ATOM   1293 C  C   . ALA A 1 150 ? -1.327 -11.932 7.976   1.00 8.67  ? 152 ALA A C   1 
ATOM   1294 O  O   . ALA A 1 150 ? -2.451 -11.997 8.477   1.00 11.19 ? 152 ALA A O   1 
ATOM   1295 C  CB  . ALA A 1 150 ? -1.023 -13.131 5.794   1.00 11.04 ? 152 ALA A CB  1 
ATOM   1296 N  N   . LYS A 1 151 ? -0.589 -10.792 7.891   1.00 10.16 ? 153 LYS A N   1 
ATOM   1297 C  CA  . LYS A 1 151 ? -1.164 -9.492  8.298   1.00 9.73  ? 153 LYS A CA  1 
ATOM   1298 C  C   . LYS A 1 151 ? -1.569 -8.723  7.059   1.00 9.14  ? 153 LYS A C   1 
ATOM   1299 O  O   . LYS A 1 151 ? -0.718 -8.299  6.293   1.00 8.72  ? 153 LYS A O   1 
ATOM   1300 C  CB  . LYS A 1 151 ? -0.116 -8.725  9.128   1.00 9.75  ? 153 LYS A CB  1 
ATOM   1301 C  CG  . LYS A 1 151 ? -0.628 -7.485  9.831   1.00 13.50 ? 153 LYS A CG  1 
ATOM   1302 C  CD  . LYS A 1 151 ? -1.613 -7.847  11.017  1.00 15.91 ? 153 LYS A CD  1 
ATOM   1303 C  CE  . LYS A 1 151 ? -1.763 -6.765  12.067  1.00 21.03 ? 153 LYS A CE  1 
ATOM   1304 N  NZ  . LYS A 1 151 ? -2.750 -7.168  13.044  1.00 26.26 ? 153 LYS A NZ  1 
ATOM   1305 N  N   . PRO A 1 152 ? -2.861 -8.670  6.747   1.00 10.57 ? 154 PRO A N   1 
ATOM   1306 C  CA  . PRO A 1 152 ? -3.253 -8.082  5.432   1.00 12.56 ? 154 PRO A CA  1 
ATOM   1307 C  C   . PRO A 1 152 ? -2.722 -6.656  5.324   1.00 10.82 ? 154 PRO A C   1 
ATOM   1308 O  O   . PRO A 1 152 ? -2.297 -6.234  4.238   1.00 12.93 ? 154 PRO A O   1 
ATOM   1309 C  CB  . PRO A 1 152 ? -4.779 -8.158  5.456   1.00 13.76 ? 154 PRO A CB  1 
ATOM   1310 C  CG  . PRO A 1 152 ? -5.043 -9.322  6.407   1.00 18.40 ? 154 PRO A CG  1 
ATOM   1311 C  CD  . PRO A 1 152 ? -4.037 -9.168  7.524   1.00 14.20 ? 154 PRO A CD  1 
ATOM   1312 N  N   . GLY A 1 153 ? -2.684 -5.887  6.438   1.00 11.27 ? 155 GLY A N   1 
ATOM   1313 C  CA  . GLY A 1 153 ? -2.318 -4.484  6.397   1.00 12.35 ? 155 GLY A CA  1 
ATOM   1314 C  C   . GLY A 1 153 ? -0.841 -4.330  6.183   1.00 9.02  ? 155 GLY A C   1 
ATOM   1315 O  O   . GLY A 1 153 ? -0.412 -3.250  5.958   1.00 14.23 ? 155 GLY A O   1 
ATOM   1316 N  N   . LEU A 1 154 ? -0.063 -5.441  6.242   1.00 10.13 ? 156 LEU A N   1 
ATOM   1317 C  CA  . LEU A 1 154 ? 1.376  -5.359  5.905   1.00 7.75  ? 156 LEU A CA  1 
ATOM   1318 C  C   . LEU A 1 154 ? 1.676  -5.593  4.418   1.00 8.97  ? 156 LEU A C   1 
ATOM   1319 O  O   . LEU A 1 154 ? 2.778  -5.265  3.929   1.00 8.69  ? 156 LEU A O   1 
ATOM   1320 C  CB  . LEU A 1 154 ? 2.136  -6.378  6.749   1.00 9.04  ? 156 LEU A CB  1 
ATOM   1321 C  CG  . LEU A 1 154 ? 3.642  -6.492  6.575   1.00 8.76  ? 156 LEU A CG  1 
ATOM   1322 C  CD1 . LEU A 1 154 ? 4.413  -5.157  6.938   1.00 10.82 ? 156 LEU A CD1 1 
ATOM   1323 C  CD2 . LEU A 1 154 ? 4.188  -7.616  7.459   1.00 10.05 ? 156 LEU A CD2 1 
ATOM   1324 N  N   . GLN A 1 155 ? 0.706  -6.122  3.678   1.00 9.29  ? 157 GLN A N   1 
ATOM   1325 C  CA  . GLN A 1 155 ? 1.079  -6.643  2.296   1.00 9.35  ? 157 GLN A CA  1 
ATOM   1326 C  C   . GLN A 1 155 ? 1.506  -5.528  1.384   1.00 9.37  ? 157 GLN A C   1 
ATOM   1327 O  O   . GLN A 1 155 ? 2.350  -5.725  0.579   1.00 9.68  ? 157 GLN A O   1 
ATOM   1328 C  CB  . GLN A 1 155 ? -0.110 -7.440  1.747   1.00 10.82 ? 157 GLN A CB  1 
ATOM   1329 C  CG  . GLN A 1 155 ? 0.283  -8.214  0.472   1.00 13.14 ? 157 GLN A CG  1 
ATOM   1330 C  CD  . GLN A 1 155 ? 1.403  -9.195  0.694   1.00 11.33 ? 157 GLN A CD  1 
ATOM   1331 O  OE1 . GLN A 1 155 ? 1.495  -9.790  1.820   1.00 11.60 ? 157 GLN A OE1 1 
ATOM   1332 N  NE2 . GLN A 1 155 ? 2.248  -9.471  -0.326  1.00 12.73 ? 157 GLN A NE2 1 
ATOM   1333 N  N   . LYS A 1 156 ? 0.971  -4.294  1.510   1.00 10.70 ? 158 LYS A N   1 
ATOM   1334 C  CA  . LYS A 1 156 ? 1.382  -3.199  0.606   1.00 10.70 ? 158 LYS A CA  1 
ATOM   1335 C  C   . LYS A 1 156 ? 2.872  -2.887  0.806   1.00 10.09 ? 158 LYS A C   1 
ATOM   1336 O  O   . LYS A 1 156 ? 3.548  -2.506  -0.110  1.00 11.60 ? 158 LYS A O   1 
ATOM   1337 C  CB  . LYS A 1 156 ? 0.550  -1.972  0.862   1.00 12.27 ? 158 LYS A CB  1 
ATOM   1338 C  CG  . LYS A 1 156 ? -0.715 -2.112  0.092   1.00 20.23 ? 158 LYS A CG  1 
ATOM   1339 N  N   . VAL A 1 157 ? 3.325  -3.009  2.070   1.00 9.57  ? 159 VAL A N   1 
ATOM   1340 C  CA  . VAL A 1 157 ? 4.730  -2.817  2.361   1.00 8.20  ? 159 VAL A CA  1 
ATOM   1341 C  C   . VAL A 1 157 ? 5.538  -3.942  1.683   1.00 9.74  ? 159 VAL A C   1 
ATOM   1342 O  O   . VAL A 1 157 ? 6.487  -3.702  0.933   1.00 9.36  ? 159 VAL A O   1 
ATOM   1343 C  CB  . VAL A 1 157 ? 4.979  -2.844  3.853   1.00 9.38  ? 159 VAL A CB  1 
ATOM   1344 C  CG1 . VAL A 1 157 ? 6.507  -2.832  4.198   1.00 10.14 ? 159 VAL A CG1 1 
ATOM   1345 C  CG2 . VAL A 1 157 ? 4.329  -1.570  4.488   1.00 12.02 ? 159 VAL A CG2 1 
ATOM   1346 N  N   . VAL A 1 158 ? 5.135  -5.183  1.927   1.00 8.67  ? 160 VAL A N   1 
ATOM   1347 C  CA  . VAL A 1 158 ? 5.814  -6.353  1.385   1.00 11.01 ? 160 VAL A CA  1 
ATOM   1348 C  C   . VAL A 1 158 ? 5.842  -6.433  -0.139  1.00 11.25 ? 160 VAL A C   1 
ATOM   1349 O  O   . VAL A 1 158 ? 6.728  -7.075  -0.703  1.00 10.99 ? 160 VAL A O   1 
ATOM   1350 C  CB  . VAL A 1 158 ? 5.202  -7.657  1.935   1.00 13.80 ? 160 VAL A CB  1 
ATOM   1351 C  CG1 . VAL A 1 158 ? 5.685  -8.851  1.127   1.00 16.03 ? 160 VAL A CG1 1 
ATOM   1352 C  CG2 . VAL A 1 158 ? 5.546  -7.825  3.407   1.00 15.88 ? 160 VAL A CG2 1 
ATOM   1353 N  N   . ASP A 1 159 ? 4.889  -5.795  -0.813  1.00 11.40 ? 161 ASP A N   1 
ATOM   1354 C  CA  . ASP A 1 159 ? 4.882  -5.875  -2.292  1.00 13.00 ? 161 ASP A CA  1 
ATOM   1355 C  C   . ASP A 1 159 ? 5.691  -4.761  -2.893  1.00 13.95 ? 161 ASP A C   1 
ATOM   1356 O  O   . ASP A 1 159 ? 6.131  -4.911  -4.071  1.00 19.93 ? 161 ASP A O   1 
ATOM   1357 C  CB  . ASP A 1 159 ? 3.440  -5.781  -2.693  1.00 15.05 ? 161 ASP A CB  1 
ATOM   1358 C  CG  . ASP A 1 159 ? 2.746  -7.159  -2.652  1.00 12.89 ? 161 ASP A CG  1 
ATOM   1359 O  OD1 . ASP A 1 159 ? 3.472  -8.186  -2.773  1.00 17.80 ? 161 ASP A OD1 1 
ATOM   1360 O  OD2 . ASP A 1 159 ? 1.589  -7.151  -2.561  1.00 20.11 ? 161 ASP A OD2 1 
ATOM   1361 N  N   . VAL A 1 160 ? 6.081  -3.691  -2.165  1.00 12.59 ? 162 VAL A N   1 
ATOM   1362 C  CA  . VAL A 1 160 ? 6.936  -2.649  -2.746  1.00 13.14 ? 162 VAL A CA  1 
ATOM   1363 C  C   . VAL A 1 160 ? 8.414  -2.946  -2.565  1.00 10.04 ? 162 VAL A C   1 
ATOM   1364 O  O   . VAL A 1 160 ? 9.273  -2.327  -3.146  1.00 12.48 ? 162 VAL A O   1 
ATOM   1365 C  CB  . VAL A 1 160 ? 6.557  -1.269  -2.201  1.00 14.99 ? 162 VAL A CB  1 
ATOM   1366 C  CG1 . VAL A 1 160 ? 7.069  -0.995  -0.826  1.00 16.00 ? 162 VAL A CG1 1 
ATOM   1367 C  CG2 . VAL A 1 160 ? 6.812  -0.148  -3.177  1.00 19.03 ? 162 VAL A CG2 1 
ATOM   1368 N  N   . LEU A 1 161 ? 8.775  -3.962  -1.713  1.00 11.56 ? 163 LEU A N   1 
ATOM   1369 C  CA  . LEU A 1 161 ? 10.148 -4.188  -1.428  1.00 10.10 ? 163 LEU A CA  1 
ATOM   1370 C  C   . LEU A 1 161 ? 11.027 -4.566  -2.582  1.00 12.55 ? 163 LEU A C   1 
ATOM   1371 O  O   . LEU A 1 161 ? 12.224 -4.222  -2.610  1.00 12.08 ? 163 LEU A O   1 
ATOM   1372 C  CB  . LEU A 1 161 ? 10.286 -5.235  -0.316  1.00 10.13 ? 163 LEU A CB  1 
ATOM   1373 C  CG  . LEU A 1 161 ? 9.700  -4.851  1.057   1.00 8.60  ? 163 LEU A CG  1 
ATOM   1374 C  CD1 . LEU A 1 161 ? 9.891  -6.035  1.972   1.00 11.24 ? 163 LEU A CD1 1 
ATOM   1375 C  CD2 . LEU A 1 161 ? 10.235 -3.578  1.592   1.00 10.55 ? 163 LEU A CD2 1 
ATOM   1376 N  N   . ASP A 1 162 ? 10.444 -5.245  -3.600  1.00 15.09 ? 164 ASP A N   1 
ATOM   1377 C  CA  . ASP A 1 162 ? 11.265 -5.565  -4.780  1.00 17.61 ? 164 ASP A CA  1 
ATOM   1378 C  C   . ASP A 1 162 ? 11.769 -4.302  -5.541  1.00 18.03 ? 164 ASP A C   1 
ATOM   1379 O  O   . ASP A 1 162 ? 12.725 -4.349  -6.326  1.00 24.17 ? 164 ASP A O   1 
ATOM   1380 C  CB  . ASP A 1 162 ? 10.498 -6.482  -5.734  1.00 24.87 ? 164 ASP A CB  1 
ATOM   1381 C  CG  . ASP A 1 162 ? 9.478  -5.734  -6.565  1.00 33.45 ? 164 ASP A CG  1 
ATOM   1382 O  OD1 . ASP A 1 162 ? 8.571  -5.110  -5.974  1.00 34.90 ? 164 ASP A OD1 1 
ATOM   1383 O  OD2 . ASP A 1 162 ? 9.580  -5.768  -7.810  1.00 41.73 ? 164 ASP A OD2 1 
ATOM   1384 N  N   . SER A 1 163 ? 11.143 -3.162  -5.288  1.00 16.11 ? 165 SER A N   1 
ATOM   1385 C  CA  . SER A 1 163 ? 11.492 -1.931  -5.971  1.00 15.90 ? 165 SER A CA  1 
ATOM   1386 C  C   . SER A 1 163 ? 12.577 -1.184  -5.147  1.00 12.53 ? 165 SER A C   1 
ATOM   1387 O  O   . SER A 1 163 ? 13.125 -0.207  -5.636  1.00 15.45 ? 165 SER A O   1 
ATOM   1388 C  CB  . SER A 1 163 ? 10.267 -1.091  -6.282  1.00 21.57 ? 165 SER A CB  1 
ATOM   1389 O  OG  . SER A 1 163 ? 9.860  -0.473  -5.063  1.00 19.02 ? 165 SER A OG  1 
ATOM   1390 N  N   . ILE A 1 164 ? 12.837 -1.633  -3.910  1.00 11.01 ? 166 ILE A N   1 
ATOM   1391 C  CA  . ILE A 1 164 ? 13.889 -0.980  -3.111  1.00 11.53 ? 166 ILE A CA  1 
ATOM   1392 C  C   . ILE A 1 164 ? 14.859 -2.006  -2.618  1.00 10.40 ? 166 ILE A C   1 
ATOM   1393 O  O   . ILE A 1 164 ? 15.250 -1.998  -1.454  1.00 9.92  ? 166 ILE A O   1 
ATOM   1394 C  CB  . ILE A 1 164 ? 13.294 -0.098  -1.975  1.00 9.50  ? 166 ILE A CB  1 
ATOM   1395 C  CG1 . ILE A 1 164 ? 12.394 -0.961  -1.063  1.00 10.19 ? 166 ILE A CG1 1 
ATOM   1396 C  CG2 . ILE A 1 164 ? 12.550 1.083   -2.538  1.00 10.72 ? 166 ILE A CG2 1 
ATOM   1397 C  CD1 . ILE A 1 164 ? 12.405 -0.343  0.351   1.00 10.07 ? 166 ILE A CD1 1 
ATOM   1398 N  N   . LYS A 1 165 ? 15.293 -2.928  -3.480  1.00 10.36 ? 167 LYS A N   1 
ATOM   1399 C  CA  . LYS A 1 165 ? 16.078 -4.071  -3.039  1.00 9.52  ? 167 LYS A CA  1 
ATOM   1400 C  C   . LYS A 1 165 ? 17.379 -3.670  -2.364  1.00 9.27  ? 167 LYS A C   1 
ATOM   1401 O  O   . LYS A 1 165 ? 17.811 -4.315  -1.388  1.00 10.08 ? 167 LYS A O   1 
ATOM   1402 C  CB  . LYS A 1 165 ? 16.271 -5.026  -4.228  1.00 10.71 ? 167 LYS A CB  1 
ATOM   1403 C  CG  . LYS A 1 165 ? 17.113 -6.257  -3.816  1.00 12.59 ? 167 LYS A CG  1 
ATOM   1404 C  CD  . LYS A 1 165 ? 17.407 -7.192  -5.082  1.00 20.58 ? 167 LYS A CD  1 
ATOM   1405 C  CE  . LYS A 1 165 ? 17.937 -8.550  -4.661  1.00 26.21 ? 167 LYS A CE  1 
ATOM   1406 N  NZ  . LYS A 1 165 ? 18.174 -9.348  -5.941  1.00 29.41 ? 167 LYS A NZ  1 
ATOM   1407 N  N   . THR A 1 166 ? 17.986 -2.602  -2.909  1.00 10.74 ? 168 THR A N   1 
ATOM   1408 C  CA  . THR A 1 166 ? 19.367 -2.385  -2.571  1.00 10.01 ? 168 THR A CA  1 
ATOM   1409 C  C   . THR A 1 166 ? 19.466 -0.953  -1.898  1.00 9.62  ? 168 THR A C   1 
ATOM   1410 O  O   . THR A 1 166 ? 18.602 -0.111  -2.007  1.00 9.90  ? 168 THR A O   1 
ATOM   1411 C  CB  . THR A 1 166 ? 20.321 -2.438  -3.785  1.00 11.76 ? 168 THR A CB  1 
ATOM   1412 O  OG1 . THR A 1 166 ? 19.761 -1.630  -4.836  1.00 13.42 ? 168 THR A OG1 1 
ATOM   1413 C  CG2 . THR A 1 166 ? 20.524 -3.867  -4.189  1.00 12.38 ? 168 THR A CG2 1 
ATOM   1414 N  N   . LYS A 1 167 ? 20.530 -0.839  -1.106  1.00 12.04 ? 169 LYS A N   1 
ATOM   1415 C  CA  . LYS A 1 167 ? 20.786 0.382   -0.350  1.00 11.20 ? 169 LYS A CA  1 
ATOM   1416 C  C   . LYS A 1 167 ? 20.735 1.614   -1.154  1.00 11.05 ? 169 LYS A C   1 
ATOM   1417 O  O   . LYS A 1 167 ? 21.303 1.695   -2.244  1.00 13.58 ? 169 LYS A O   1 
ATOM   1418 C  CB  . LYS A 1 167 ? 22.143 0.244   0.293   1.00 12.73 ? 169 LYS A CB  1 
ATOM   1419 C  CG  . LYS A 1 167 ? 22.678 1.448   1.022   1.00 11.96 ? 169 LYS A CG  1 
ATOM   1420 C  CD  . LYS A 1 167 ? 23.990 1.263   1.691   1.00 13.82 ? 169 LYS A CD  1 
ATOM   1421 C  CE  . LYS A 1 167 ? 25.076 0.833   0.653   1.00 21.68 ? 169 LYS A CE  1 
ATOM   1422 N  NZ  . LYS A 1 167 ? 26.382 0.579   1.416   1.00 24.92 ? 169 LYS A NZ  1 
ATOM   1423 N  N   . GLY A 1 168 ? 19.964 2.588   -0.663  1.00 11.85 ? 170 GLY A N   1 
ATOM   1424 C  CA  . GLY A 1 168 ? 19.802 3.894   -1.357  1.00 14.12 ? 170 GLY A CA  1 
ATOM   1425 C  C   . GLY A 1 168 ? 18.635 3.958   -2.337  1.00 13.97 ? 170 GLY A C   1 
ATOM   1426 O  O   . GLY A 1 168 ? 18.368 5.105   -2.865  1.00 17.89 ? 170 GLY A O   1 
ATOM   1427 N  N   . LYS A 1 169 ? 17.974 2.857   -2.626  1.00 11.90 ? 171 LYS A N   1 
ATOM   1428 C  CA  . LYS A 1 169 ? 16.754 2.923   -3.433  1.00 12.35 ? 171 LYS A CA  1 
ATOM   1429 C  C   . LYS A 1 169 ? 15.593 3.447   -2.578  1.00 11.74 ? 171 LYS A C   1 
ATOM   1430 O  O   . LYS A 1 169 ? 15.454 3.029   -1.401  1.00 12.55 ? 171 LYS A O   1 
ATOM   1431 C  CB  . LYS A 1 169 ? 16.456 1.607   -4.040  1.00 13.55 ? 171 LYS A CB  1 
ATOM   1432 C  CG  . LYS A 1 169 ? 17.479 1.210   -5.078  1.00 15.13 ? 171 LYS A CG  1 
ATOM   1433 C  CD  . LYS A 1 169 ? 16.961 0.087   -6.085  1.00 20.04 ? 171 LYS A CD  1 
ATOM   1434 C  CE  . LYS A 1 169 ? 15.804 0.497   -7.045  1.00 18.93 ? 171 LYS A CE  1 
ATOM   1435 N  NZ  . LYS A 1 169 ? 15.338 -0.590  -8.014  1.00 23.12 ? 171 LYS A NZ  1 
ATOM   1436 N  N   . SER A 1 170 ? 14.708 4.232   -3.160  1.00 13.29 ? 172 SER A N   1 
ATOM   1437 C  CA  . SER A 1 170 ? 13.481 4.683   -2.535  1.00 14.50 ? 172 SER A CA  1 
ATOM   1438 C  C   . SER A 1 170 ? 12.353 4.534   -3.545  1.00 13.64 ? 172 SER A C   1 
ATOM   1439 O  O   . SER A 1 170 ? 12.546 4.406   -4.811  1.00 16.80 ? 172 SER A O   1 
ATOM   1440 C  CB  . SER A 1 170 ? 13.601 6.149   -2.092  1.00 13.46 ? 172 SER A CB  1 
ATOM   1441 O  OG  . SER A 1 170 ? 13.891 7.025   -3.162  1.00 22.95 ? 172 SER A OG  1 
ATOM   1442 N  N   . ALA A 1 171 ? 11.091 4.526   -3.059  1.00 14.11 ? 173 ALA A N   1 
ATOM   1443 C  CA  . ALA A 1 171 ? 9.924  4.440   -3.949  1.00 14.62 ? 173 ALA A CA  1 
ATOM   1444 C  C   . ALA A 1 171 ? 8.792  5.269   -3.347  1.00 15.17 ? 173 ALA A C   1 
ATOM   1445 O  O   . ALA A 1 171 ? 8.706  5.357   -2.078  1.00 13.95 ? 173 ALA A O   1 
ATOM   1446 C  CB  . ALA A 1 171 ? 9.466  3.021   -4.096  1.00 16.39 ? 173 ALA A CB  1 
ATOM   1447 N  N   . ASP A 1 172 ? 7.954  5.863   -4.177  1.00 16.00 ? 174 ASP A N   1 
ATOM   1448 C  CA  . ASP A 1 172 ? 6.751  6.532   -3.583  1.00 15.97 ? 174 ASP A CA  1 
ATOM   1449 C  C   . ASP A 1 172 ? 5.897  5.572   -2.850  1.00 16.35 ? 174 ASP A C   1 
ATOM   1450 O  O   . ASP A 1 172 ? 5.745  4.451   -3.254  1.00 18.06 ? 174 ASP A O   1 
ATOM   1451 C  CB  . ASP A 1 172 ? 5.921  7.110   -4.823  1.00 15.19 ? 174 ASP A CB  1 
ATOM   1452 C  CG  . ASP A 1 172 ? 6.703  8.138   -5.497  1.00 24.20 ? 174 ASP A CG  1 
ATOM   1453 O  OD1 . ASP A 1 172 ? 7.506  8.821   -4.869  1.00 27.19 ? 174 ASP A OD1 1 
ATOM   1454 O  OD2 . ASP A 1 172 ? 6.564  8.262   -6.752  1.00 19.27 ? 174 ASP A OD2 1 
ATOM   1455 N  N   . PHE A 1 173 ? 5.369  6.035   -1.690  1.00 13.29 ? 175 PHE A N   1 
ATOM   1456 C  CA  . PHE A 1 173 ? 4.599  5.106   -0.849  1.00 14.87 ? 175 PHE A CA  1 
ATOM   1457 C  C   . PHE A 1 173 ? 3.635  5.969   -0.116  1.00 13.03 ? 175 PHE A C   1 
ATOM   1458 O  O   . PHE A 1 173 ? 3.806  6.255   1.062   1.00 15.41 ? 175 PHE A O   1 
ATOM   1459 C  CB  . PHE A 1 173 ? 5.574  4.317   0.055   1.00 12.55 ? 175 PHE A CB  1 
ATOM   1460 C  CG  . PHE A 1 173 ? 4.928  3.082   0.559   1.00 12.88 ? 175 PHE A CG  1 
ATOM   1461 C  CD1 . PHE A 1 173 ? 4.582  2.036   -0.282  1.00 15.31 ? 175 PHE A CD1 1 
ATOM   1462 C  CD2 . PHE A 1 173 ? 4.703  2.963   1.911   1.00 12.79 ? 175 PHE A CD2 1 
ATOM   1463 C  CE1 . PHE A 1 173 ? 3.989  0.907   0.275   1.00 17.34 ? 175 PHE A CE1 1 
ATOM   1464 C  CE2 . PHE A 1 173 ? 4.086  1.811   2.481   1.00 12.92 ? 175 PHE A CE2 1 
ATOM   1465 C  CZ  . PHE A 1 173 ? 3.743  0.773   1.655   1.00 16.05 ? 175 PHE A CZ  1 
ATOM   1466 N  N   . THR A 1 174 ? 2.591  6.383   -0.792  1.00 13.36 ? 176 THR A N   1 
ATOM   1467 C  CA  . THR A 1 174 ? 1.550  7.216   -0.219  1.00 12.19 ? 176 THR A CA  1 
ATOM   1468 C  C   . THR A 1 174 ? 0.367  6.448   0.236   1.00 9.36  ? 176 THR A C   1 
ATOM   1469 O  O   . THR A 1 174 ? 0.160  5.299   -0.233  1.00 12.25 ? 176 THR A O   1 
ATOM   1470 C  CB  . THR A 1 174 ? 1.077  8.265   -1.259  1.00 15.54 ? 176 THR A CB  1 
ATOM   1471 O  OG1 . THR A 1 174 ? 0.622  7.668   -2.459  1.00 19.84 ? 176 THR A OG1 1 
ATOM   1472 C  CG2 . THR A 1 174 ? 2.228  9.202   -1.605  1.00 24.54 ? 176 THR A CG2 1 
ATOM   1473 N  N   . ASN A 1 175 ? -0.419 7.005   1.124   1.00 10.25 ? 177 ASN A N   1 
ATOM   1474 C  CA  . ASN A 1 175 ? -1.669 6.459   1.572   1.00 12.62 ? 177 ASN A CA  1 
ATOM   1475 C  C   . ASN A 1 175 ? -1.538 5.188   2.369   1.00 10.93 ? 177 ASN A C   1 
ATOM   1476 O  O   . ASN A 1 175 ? -2.454 4.419   2.339   1.00 16.68 ? 177 ASN A O   1 
ATOM   1477 C  CB  . ASN A 1 175 ? -2.645 6.359   0.377   1.00 12.62 ? 177 ASN A CB  1 
ATOM   1478 C  CG  . ASN A 1 175 ? -2.873 7.762   -0.215  1.00 14.05 ? 177 ASN A CG  1 
ATOM   1479 O  OD1 . ASN A 1 175 ? -3.588 8.565   0.380   1.00 15.40 ? 177 ASN A OD1 1 
ATOM   1480 N  ND2 . ASN A 1 175 ? -2.284 8.054   -1.369  1.00 12.81 ? 177 ASN A ND2 1 
ATOM   1481 N  N   . PHE A 1 176 ? -0.341 4.901   2.920   1.00 10.36 ? 178 PHE A N   1 
ATOM   1482 C  CA  . PHE A 1 176 ? -0.226 3.687   3.700   1.00 10.47 ? 178 PHE A CA  1 
ATOM   1483 C  C   . PHE A 1 176 ? -0.762 3.950   5.077   1.00 9.18  ? 178 PHE A C   1 
ATOM   1484 O  O   . PHE A 1 176 ? -0.311 4.916   5.695   1.00 10.00 ? 178 PHE A O   1 
ATOM   1485 C  CB  . PHE A 1 176 ? 1.198  3.197   3.755   1.00 11.36 ? 178 PHE A CB  1 
ATOM   1486 C  CG  . PHE A 1 176 ? 1.313  1.997   4.619   1.00 10.12 ? 178 PHE A CG  1 
ATOM   1487 C  CD1 . PHE A 1 176 ? 0.941  0.740   4.078   1.00 11.09 ? 178 PHE A CD1 1 
ATOM   1488 C  CD2 . PHE A 1 176 ? 1.672  2.070   6.014   1.00 10.01 ? 178 PHE A CD2 1 
ATOM   1489 C  CE1 . PHE A 1 176 ? 0.899  -0.402  4.855   1.00 11.11 ? 178 PHE A CE1 1 
ATOM   1490 C  CE2 . PHE A 1 176 ? 1.640  0.859   6.754   1.00 9.70  ? 178 PHE A CE2 1 
ATOM   1491 C  CZ  . PHE A 1 176 ? 1.281  -0.345  6.210   1.00 10.39 ? 178 PHE A CZ  1 
ATOM   1492 N  N   . ASP A 1 177 ? -1.667 3.145   5.604   1.00 10.10 ? 179 ASP A N   1 
ATOM   1493 C  CA  . ASP A 1 177 ? -2.269 3.399   6.922   1.00 9.39  ? 179 ASP A CA  1 
ATOM   1494 C  C   . ASP A 1 177 ? -1.677 2.507   7.965   1.00 6.71  ? 179 ASP A C   1 
ATOM   1495 O  O   . ASP A 1 177 ? -1.856 1.278   7.992   1.00 8.75  ? 179 ASP A O   1 
ATOM   1496 C  CB  . ASP A 1 177 ? -3.765 3.100   6.788   1.00 10.99 ? 179 ASP A CB  1 
ATOM   1497 C  CG  . ASP A 1 177 ? -4.562 3.451   8.004   1.00 12.28 ? 179 ASP A CG  1 
ATOM   1498 O  OD1 . ASP A 1 177 ? -3.979 3.654   9.091   1.00 11.08 ? 179 ASP A OD1 1 
ATOM   1499 O  OD2 . ASP A 1 177 ? -5.758 3.588   7.852   1.00 20.16 ? 179 ASP A OD2 1 
ATOM   1500 N  N   . PRO A 1 178 ? -0.836 3.062   8.895   1.00 7.48  ? 180 PRO A N   1 
ATOM   1501 C  CA  . PRO A 1 178 ? -0.120 2.231   9.869   1.00 7.46  ? 180 PRO A CA  1 
ATOM   1502 C  C   . PRO A 1 178 ? -1.093 1.635   10.883  1.00 7.40  ? 180 PRO A C   1 
ATOM   1503 O  O   . PRO A 1 178 ? -0.633 0.763   11.670  1.00 8.01  ? 180 PRO A O   1 
ATOM   1504 C  CB  . PRO A 1 178 ? 0.895  3.225   10.451  1.00 8.86  ? 180 PRO A CB  1 
ATOM   1505 C  CG  . PRO A 1 178 ? 0.226  4.592   10.317  1.00 9.10  ? 180 PRO A CG  1 
ATOM   1506 C  CD  . PRO A 1 178 ? -0.466 4.495   8.974   1.00 8.16  ? 180 PRO A CD  1 
ATOM   1507 N  N   . ARG A 1 179 ? -2.366 2.060   10.955  1.00 7.35  ? 181 ARG A N   1 
ATOM   1508 C  CA  . ARG A 1 179 ? -3.282 1.404   11.870  1.00 7.71  ? 181 ARG A CA  1 
ATOM   1509 C  C   . ARG A 1 179 ? -3.383 -0.104  11.551  1.00 9.92  ? 181 ARG A C   1 
ATOM   1510 O  O   . ARG A 1 179 ? -3.732 -0.923  12.431  1.00 10.67 ? 181 ARG A O   1 
ATOM   1511 C  CB  . ARG A 1 179 ? -4.666 2.052   11.801  1.00 9.73  ? 181 ARG A CB  1 
ATOM   1512 C  CG  . ARG A 1 179 ? -4.739 3.426   12.447  1.00 10.91 ? 181 ARG A CG  1 
ATOM   1513 C  CD  . ARG A 1 179 ? -6.123 4.036   12.291  1.00 12.99 ? 181 ARG A CD  1 
ATOM   1514 N  NE  . ARG A 1 179 ? -6.430 4.347   10.898  1.00 12.50 ? 181 ARG A NE  1 
ATOM   1515 C  CZ  . ARG A 1 179 ? -7.496 5.037   10.505  1.00 17.07 ? 181 ARG A CZ  1 
ATOM   1516 N  NH1 . ARG A 1 179 ? -8.361 5.492   11.400  1.00 24.86 ? 181 ARG A NH1 1 
ATOM   1517 N  NH2 . ARG A 1 179 ? -7.697 5.272   9.215   1.00 19.90 ? 181 ARG A NH2 1 
ATOM   1518 N  N   . GLY A 1 180 ? -3.159 -0.523  10.301  1.00 8.60  ? 182 GLY A N   1 
ATOM   1519 C  CA  . GLY A 1 180 ? -3.241 -1.933  9.944   1.00 9.98  ? 182 GLY A CA  1 
ATOM   1520 C  C   . GLY A 1 180 ? -2.136 -2.796  10.503  1.00 9.04  ? 182 GLY A C   1 
ATOM   1521 O  O   . GLY A 1 180 ? -2.109 -3.943  10.240  1.00 13.46 ? 182 GLY A O   1 
ATOM   1522 N  N   . LEU A 1 181 ? -1.152 -2.152  11.205  1.00 8.64  ? 183 LEU A N   1 
ATOM   1523 C  CA  . LEU A 1 181 ? -0.046 -2.876  11.765  1.00 8.75  ? 183 LEU A CA  1 
ATOM   1524 C  C   . LEU A 1 181 ? -0.207 -3.056  13.270  1.00 7.06  ? 183 LEU A C   1 
ATOM   1525 O  O   . LEU A 1 181 ? 0.693  -3.643  13.899  1.00 9.02  ? 183 LEU A O   1 
ATOM   1526 C  CB  . LEU A 1 181 ? 1.301  -2.177  11.472  1.00 8.27  ? 183 LEU A CB  1 
ATOM   1527 C  CG  . LEU A 1 181 ? 1.551  -2.120  9.973   1.00 8.60  ? 183 LEU A CG  1 
ATOM   1528 C  CD1 . LEU A 1 181 ? 2.860  -1.331  9.747   1.00 10.81 ? 183 LEU A CD1 1 
ATOM   1529 C  CD2 . LEU A 1 181 ? 1.557  -3.436  9.280   1.00 14.29 ? 183 LEU A CD2 1 
ATOM   1530 N  N   . LEU A 1 182 ? -1.302 -2.565  13.843  1.00 8.40  ? 184 LEU A N   1 
ATOM   1531 C  CA  . LEU A 1 182 ? -1.393 -2.627  15.304  1.00 8.54  ? 184 LEU A CA  1 
ATOM   1532 C  C   . LEU A 1 182 ? -2.159 -3.872  15.799  1.00 10.09 ? 184 LEU A C   1 
ATOM   1533 O  O   . LEU A 1 182 ? -3.156 -4.295  15.228  1.00 17.29 ? 184 LEU A O   1 
ATOM   1534 C  CB  . LEU A 1 182 ? -2.295 -1.401  15.795  1.00 8.06  ? 184 LEU A CB  1 
ATOM   1535 C  CG  . LEU A 1 182 ? -1.676 -0.040  15.431  1.00 7.05  ? 184 LEU A CG  1 
ATOM   1536 C  CD1 . LEU A 1 182 ? -2.597 1.072   15.864  1.00 9.78  ? 184 LEU A CD1 1 
ATOM   1537 C  CD2 . LEU A 1 182 ? -0.246 0.127   15.960  1.00 9.97  ? 184 LEU A CD2 1 
ATOM   1538 N  N   . PRO A 1 183 ? -1.769 -4.446  16.913  1.00 8.21  ? 185 PRO A N   1 
ATOM   1539 C  CA  . PRO A 1 183 ? -2.524 -5.614  17.473  1.00 9.40  ? 185 PRO A CA  1 
ATOM   1540 C  C   . PRO A 1 183 ? -3.810 -5.072  18.102  1.00 9.29  ? 185 PRO A C   1 
ATOM   1541 O  O   . PRO A 1 183 ? -4.018 -3.858  18.199  1.00 11.79 ? 185 PRO A O   1 
ATOM   1542 C  CB  . PRO A 1 183 ? -1.569 -6.196  18.516  1.00 8.14  ? 185 PRO A CB  1 
ATOM   1543 C  CG  . PRO A 1 183 ? -0.859 -4.921  19.014  1.00 7.94  ? 185 PRO A CG  1 
ATOM   1544 C  CD  . PRO A 1 183 ? -0.636 -4.052  17.733  1.00 7.25  ? 185 PRO A CD  1 
ATOM   1545 N  N   A GLU A 1 184 ? -4.694 -5.972  18.579  0.50 9.26  ? 186 GLU A N   1 
ATOM   1546 N  N   B GLU A 1 184 ? -4.574 -6.001  18.657  0.50 9.12  ? 186 GLU A N   1 
ATOM   1547 C  CA  A GLU A 1 184 ? -5.936 -5.519  19.264  0.50 10.09 ? 186 GLU A CA  1 
ATOM   1548 C  CA  B GLU A 1 184 ? -5.875 -5.662  19.157  0.50 9.31  ? 186 GLU A CA  1 
ATOM   1549 C  C   A GLU A 1 184 ? -5.540 -4.705  20.473  0.50 9.19  ? 186 GLU A C   1 
ATOM   1550 C  C   B GLU A 1 184 ? -5.708 -4.902  20.513  0.50 8.08  ? 186 GLU A C   1 
ATOM   1551 O  O   A GLU A 1 184 ? -6.042 -3.582  20.644  0.50 11.76 ? 186 GLU A O   1 
ATOM   1552 O  O   B GLU A 1 184 ? -6.446 -3.942  20.784  0.50 8.75  ? 186 GLU A O   1 
ATOM   1553 C  CB  A GLU A 1 184 ? -6.739 -6.706  19.824  0.50 14.01 ? 186 GLU A CB  1 
ATOM   1554 C  CB  B GLU A 1 184 ? -6.687 -6.970  19.249  0.50 10.63 ? 186 GLU A CB  1 
ATOM   1555 C  CG  A GLU A 1 184 ? -7.701 -7.297  18.840  0.50 14.71 ? 186 GLU A CG  1 
ATOM   1556 C  CG  B GLU A 1 184 ? -7.789 -6.849  20.284  0.50 10.75 ? 186 GLU A CG  1 
ATOM   1557 C  CD  A GLU A 1 184 ? -8.228 -8.638  19.291  0.50 14.46 ? 186 GLU A CD  1 
ATOM   1558 C  CD  B GLU A 1 184 ? -8.453 -8.179  20.612  0.50 9.35  ? 186 GLU A CD  1 
ATOM   1559 O  OE1 A GLU A 1 184 ? -8.706 -9.340  18.441  0.50 18.84 ? 186 GLU A OE1 1 
ATOM   1560 O  OE1 B GLU A 1 184 ? -8.316 -9.142  19.759  0.50 13.26 ? 186 GLU A OE1 1 
ATOM   1561 O  OE2 A GLU A 1 184 ? -8.247 -8.942  20.523  0.50 16.73 ? 186 GLU A OE2 1 
ATOM   1562 O  OE2 B GLU A 1 184 ? -9.187 -8.191  21.619  0.50 14.20 ? 186 GLU A OE2 1 
ATOM   1563 N  N   . SER A 1 185 ? -4.791 -5.343  21.367  1.00 8.38  ? 187 SER A N   1 
ATOM   1564 C  CA  . SER A 1 185 ? -4.584 -4.727  22.707  1.00 9.11  ? 187 SER A CA  1 
ATOM   1565 C  C   . SER A 1 185 ? -3.444 -3.723  22.673  1.00 7.82  ? 187 SER A C   1 
ATOM   1566 O  O   . SER A 1 185 ? -2.405 -3.976  22.017  1.00 9.03  ? 187 SER A O   1 
ATOM   1567 C  CB  . SER A 1 185 ? -4.171 -5.797  23.679  1.00 10.38 ? 187 SER A CB  1 
ATOM   1568 O  OG  . SER A 1 185 ? -3.947 -5.244  24.963  1.00 10.52 ? 187 SER A OG  1 
ATOM   1569 N  N   . LEU A 1 186 ? -3.611 -2.622  23.357  1.00 7.82  ? 188 LEU A N   1 
ATOM   1570 C  CA  . LEU A 1 186 ? -2.529 -1.632  23.608  1.00 7.91  ? 188 LEU A CA  1 
ATOM   1571 C  C   . LEU A 1 186 ? -1.906 -1.789  24.958  1.00 7.98  ? 188 LEU A C   1 
ATOM   1572 O  O   . LEU A 1 186 ? -1.193 -0.876  25.445  1.00 9.20  ? 188 LEU A O   1 
ATOM   1573 C  CB  . LEU A 1 186 ? -3.048 -0.211  23.294  1.00 10.69 ? 188 LEU A CB  1 
ATOM   1574 C  CG  . LEU A 1 186 ? -3.490 0.122   21.902  1.00 12.21 ? 188 LEU A CG  1 
ATOM   1575 C  CD1 . LEU A 1 186 ? -3.981 1.560   21.805  1.00 15.81 ? 188 LEU A CD1 1 
ATOM   1576 C  CD2 . LEU A 1 186 ? -2.356 -0.205  20.880  1.00 14.51 ? 188 LEU A CD2 1 
ATOM   1577 N  N   . ASP A 1 187 ? -2.044 -2.970  25.631  1.00 8.34  ? 189 ASP A N   1 
ATOM   1578 C  CA  . ASP A 1 187 ? -1.271 -3.166  26.840  1.00 7.90  ? 189 ASP A CA  1 
ATOM   1579 C  C   . ASP A 1 187 ? 0.251  -3.111  26.528  1.00 6.22  ? 189 ASP A C   1 
ATOM   1580 O  O   . ASP A 1 187 ? 0.679  -3.626  25.470  1.00 6.00  ? 189 ASP A O   1 
ATOM   1581 C  CB  . ASP A 1 187 ? -1.584 -4.510  27.432  1.00 10.12 ? 189 ASP A CB  1 
ATOM   1582 C  CG  . ASP A 1 187 ? -2.971 -4.601  28.087  1.00 15.48 ? 189 ASP A CG  1 
ATOM   1583 O  OD1 . ASP A 1 187 ? -3.631 -3.581  28.300  1.00 19.19 ? 189 ASP A OD1 1 
ATOM   1584 O  OD2 . ASP A 1 187 ? -3.465 -5.713  28.397  1.00 21.06 ? 189 ASP A OD2 1 
ATOM   1585 N  N   . TYR A 1 188 ? 1.038  -2.497  27.415  1.00 5.47  ? 190 TYR A N   1 
ATOM   1586 C  CA  . TYR A 1 188 ? 2.427  -2.233  27.112  1.00 5.44  ? 190 TYR A CA  1 
ATOM   1587 C  C   . TYR A 1 188 ? 3.348  -2.324  28.316  1.00 4.99  ? 190 TYR A C   1 
ATOM   1588 O  O   . TYR A 1 188 ? 2.897  -2.175  29.479  1.00 5.90  ? 190 TYR A O   1 
ATOM   1589 C  CB  . TYR A 1 188 ? 2.557  -0.878  26.429  1.00 6.18  ? 190 TYR A CB  1 
ATOM   1590 C  CG  . TYR A 1 188 ? 2.167  0.298   27.294  1.00 6.04  ? 190 TYR A CG  1 
ATOM   1591 C  CD1 . TYR A 1 188 ? 3.107  0.887   28.170  1.00 6.56  ? 190 TYR A CD1 1 
ATOM   1592 C  CD2 . TYR A 1 188 ? 0.865  0.799   27.253  1.00 7.23  ? 190 TYR A CD2 1 
ATOM   1593 C  CE1 . TYR A 1 188 ? 2.682  1.936   28.994  1.00 6.85  ? 190 TYR A CE1 1 
ATOM   1594 C  CE2 . TYR A 1 188 ? 0.471  1.884   28.036  1.00 7.29  ? 190 TYR A CE2 1 
ATOM   1595 C  CZ  . TYR A 1 188 ? 1.381  2.415   28.911  1.00 6.52  ? 190 TYR A CZ  1 
ATOM   1596 O  OH  . TYR A 1 188 ? 1.041  3.472   29.796  1.00 8.76  ? 190 TYR A OH  1 
ATOM   1597 N  N   . TRP A 1 189 ? 4.629  -2.450  28.045  1.00 4.83  ? 191 TRP A N   1 
ATOM   1598 C  CA  . TRP A 1 189 ? 5.712  -2.193  29.001  1.00 4.34  ? 191 TRP A CA  1 
ATOM   1599 C  C   . TRP A 1 189 ? 6.357  -0.890  28.570  1.00 3.58  ? 191 TRP A C   1 
ATOM   1600 O  O   . TRP A 1 189 ? 6.412  -0.572  27.379  1.00 5.57  ? 191 TRP A O   1 
ATOM   1601 C  CB  . TRP A 1 189 ? 6.722  -3.337  28.984  1.00 5.09  ? 191 TRP A CB  1 
ATOM   1602 C  CG  . TRP A 1 189 ? 6.157  -4.652  29.388  1.00 5.17  ? 191 TRP A CG  1 
ATOM   1603 C  CD1 . TRP A 1 189 ? 5.906  -5.055  30.664  1.00 5.94  ? 191 TRP A CD1 1 
ATOM   1604 C  CD2 . TRP A 1 189 ? 5.925  -5.783  28.542  1.00 5.07  ? 191 TRP A CD2 1 
ATOM   1605 N  NE1 . TRP A 1 189 ? 5.515  -6.400  30.657  1.00 7.03  ? 191 TRP A NE1 1 
ATOM   1606 C  CE2 . TRP A 1 189 ? 5.501  -6.839  29.371  1.00 7.06  ? 191 TRP A CE2 1 
ATOM   1607 C  CE3 . TRP A 1 189 ? 5.998  -5.999  27.149  1.00 6.36  ? 191 TRP A CE3 1 
ATOM   1608 C  CZ2 . TRP A 1 189 ? 5.220  -8.146  28.854  1.00 7.84  ? 191 TRP A CZ2 1 
ATOM   1609 C  CZ3 . TRP A 1 189 ? 5.757  -7.269  26.649  1.00 6.42  ? 191 TRP A CZ3 1 
ATOM   1610 C  CH2 . TRP A 1 189 ? 5.345  -8.301  27.491  1.00 7.45  ? 191 TRP A CH2 1 
ATOM   1611 N  N   . THR A 1 190 ? 6.945  -0.205  29.542  1.00 3.94  ? 192 THR A N   1 
ATOM   1612 C  CA  . THR A 1 190 ? 7.677  1.032   29.180  1.00 3.57  ? 192 THR A CA  1 
ATOM   1613 C  C   . THR A 1 190 ? 8.919  1.200   30.017  1.00 3.47  ? 192 THR A C   1 
ATOM   1614 O  O   . THR A 1 190 ? 8.937  0.818   31.207  1.00 4.69  ? 192 THR A O   1 
ATOM   1615 C  CB  . THR A 1 190 ? 6.737  2.250   29.281  1.00 3.81  ? 192 THR A CB  1 
ATOM   1616 O  OG1 . THR A 1 190 ? 7.419  3.430   28.871  1.00 4.54  ? 192 THR A OG1 1 
ATOM   1617 C  CG2 . THR A 1 190 ? 6.218  2.512   30.708  1.00 4.73  ? 192 THR A CG2 1 
ATOM   1618 N  N   . TYR A 1 191 ? 9.941  1.812   29.453  1.00 3.82  ? 193 TYR A N   1 
ATOM   1619 C  CA  . TYR A 1 191 ? 11.166 2.090   30.194  1.00 3.42  ? 193 TYR A CA  1 
ATOM   1620 C  C   . TYR A 1 191 ? 11.940 3.131   29.420  1.00 3.35  ? 193 TYR A C   1 
ATOM   1621 O  O   . TYR A 1 191 ? 11.727 3.318   28.221  1.00 3.92  ? 193 TYR A O   1 
ATOM   1622 C  CB  . TYR A 1 191 ? 12.012 0.805   30.370  1.00 4.74  ? 193 TYR A CB  1 
ATOM   1623 C  CG  . TYR A 1 191 ? 12.705 0.365   29.101  1.00 3.47  ? 193 TYR A CG  1 
ATOM   1624 C  CD1 . TYR A 1 191 ? 12.043 -0.367  28.122  1.00 3.70  ? 193 TYR A CD1 1 
ATOM   1625 C  CD2 . TYR A 1 191 ? 14.023 0.721   28.909  1.00 4.14  ? 193 TYR A CD2 1 
ATOM   1626 C  CE1 . TYR A 1 191 ? 12.675 -0.711  26.940  1.00 3.76  ? 193 TYR A CE1 1 
ATOM   1627 C  CE2 . TYR A 1 191 ? 14.701 0.347   27.723  1.00 3.91  ? 193 TYR A CE2 1 
ATOM   1628 C  CZ  . TYR A 1 191 ? 13.999 -0.340  26.758  1.00 3.35  ? 193 TYR A CZ  1 
ATOM   1629 O  OH  . TYR A 1 191 ? 14.650 -0.677  25.583  1.00 3.68  ? 193 TYR A OH  1 
ATOM   1630 N  N   . PRO A 1 192 ? 12.887 3.816   30.079  1.00 3.51  ? 194 PRO A N   1 
ATOM   1631 C  CA  . PRO A 1 192 ? 13.705 4.810   29.373  1.00 3.75  ? 194 PRO A CA  1 
ATOM   1632 C  C   . PRO A 1 192 ? 14.873 4.167   28.722  1.00 3.49  ? 194 PRO A C   1 
ATOM   1633 O  O   . PRO A 1 192 ? 15.641 3.413   29.388  1.00 4.53  ? 194 PRO A O   1 
ATOM   1634 C  CB  . PRO A 1 192 ? 14.165 5.725   30.530  1.00 5.54  ? 194 PRO A CB  1 
ATOM   1635 C  CG  . PRO A 1 192 ? 14.211 4.833   31.782  1.00 6.12  ? 194 PRO A CG  1 
ATOM   1636 C  CD  . PRO A 1 192 ? 13.067 3.833   31.571  1.00 5.37  ? 194 PRO A CD  1 
ATOM   1637 N  N   . GLY A 1 193 ? 15.156 4.503   27.449  1.00 3.21  ? 195 GLY A N   1 
ATOM   1638 C  CA  . GLY A 1 193 ? 16.267 3.852   26.756  1.00 3.32  ? 195 GLY A CA  1 
ATOM   1639 C  C   . GLY A 1 193 ? 16.781 4.745   25.669  1.00 2.97  ? 195 GLY A C   1 
ATOM   1640 O  O   . GLY A 1 193 ? 16.931 5.981   25.785  1.00 3.62  ? 195 GLY A O   1 
ATOM   1641 N  N   . SER A 1 194 ? 17.209 4.061   24.582  1.00 3.15  ? 196 SER A N   1 
ATOM   1642 C  CA  . SER A 1 194 ? 18.044 4.692   23.550  1.00 3.45  ? 196 SER A CA  1 
ATOM   1643 C  C   . SER A 1 194 ? 17.591 4.266   22.166  1.00 2.81  ? 196 SER A C   1 
ATOM   1644 O  O   . SER A 1 194 ? 16.821 3.303   22.025  1.00 3.65  ? 196 SER A O   1 
ATOM   1645 C  CB  . SER A 1 194 ? 19.505 4.302   23.718  1.00 3.62  ? 196 SER A CB  1 
ATOM   1646 O  OG  . SER A 1 194 ? 19.758 2.938   23.339  1.00 3.71  ? 196 SER A OG  1 
ATOM   1647 N  N   . LEU A 1 195 ? 18.166 4.926   21.141  1.00 3.05  ? 197 LEU A N   1 
ATOM   1648 C  CA  . LEU A 1 195 ? 18.147 4.326   19.813  1.00 3.57  ? 197 LEU A CA  1 
ATOM   1649 C  C   . LEU A 1 195 ? 18.805 2.966   19.937  1.00 3.50  ? 197 LEU A C   1 
ATOM   1650 O  O   . LEU A 1 195 ? 19.858 2.816   20.600  1.00 4.24  ? 197 LEU A O   1 
ATOM   1651 C  CB  . LEU A 1 195 ? 18.902 5.186   18.807  1.00 5.53  ? 197 LEU A CB  1 
ATOM   1652 C  CG  . LEU A 1 195 ? 18.621 6.715   18.741  1.00 7.40  ? 197 LEU A CG  1 
ATOM   1653 C  CD1 . LEU A 1 195 ? 19.457 7.303   17.623  1.00 11.50 ? 197 LEU A CD1 1 
ATOM   1654 C  CD2 . LEU A 1 195 ? 17.237 7.094   18.602  1.00 7.78  ? 197 LEU A CD2 1 
ATOM   1655 N  N   . THR A 1 196 ? 18.359 1.984   19.099  1.00 3.25  ? 198 THR A N   1 
ATOM   1656 C  CA  . THR A 1 196 ? 19.037 0.690   19.081  1.00 3.87  ? 198 THR A CA  1 
ATOM   1657 C  C   . THR A 1 196 ? 20.039 0.609   17.957  1.00 3.85  ? 198 THR A C   1 
ATOM   1658 O  O   . THR A 1 196 ? 20.684 -0.424  17.830  1.00 4.36  ? 198 THR A O   1 
ATOM   1659 C  CB  . THR A 1 196 ? 18.024 -0.439  18.939  1.00 3.31  ? 198 THR A CB  1 
ATOM   1660 O  OG1 . THR A 1 196 ? 17.499 -0.361  17.614  1.00 3.57  ? 198 THR A OG1 1 
ATOM   1661 C  CG2 . THR A 1 196 ? 16.953 -0.440  19.988  1.00 3.96  ? 198 THR A CG2 1 
ATOM   1662 N  N   . THR A 1 197 ? 20.216 1.643   17.192  1.00 4.42  ? 199 THR A N   1 
ATOM   1663 C  CA  . THR A 1 197 ? 21.242 1.743   16.163  1.00 4.53  ? 199 THR A CA  1 
ATOM   1664 C  C   . THR A 1 197 ? 22.128 2.917   16.460  1.00 5.32  ? 199 THR A C   1 
ATOM   1665 O  O   . THR A 1 197 ? 21.668 3.891   17.101  1.00 5.08  ? 199 THR A O   1 
ATOM   1666 C  CB  . THR A 1 197 ? 20.634 2.032   14.777  1.00 4.71  ? 199 THR A CB  1 
ATOM   1667 O  OG1 . THR A 1 197 ? 19.897 3.252   14.837  1.00 6.03  ? 199 THR A OG1 1 
ATOM   1668 C  CG2 . THR A 1 197 ? 19.674 0.954   14.339  1.00 5.28  ? 199 THR A CG2 1 
ATOM   1669 N  N   . PRO A 1 198 ? 23.406 2.952   16.009  1.00 5.65  ? 200 PRO A N   1 
ATOM   1670 C  CA  . PRO A 1 198 ? 24.164 4.203   15.982  1.00 5.76  ? 200 PRO A CA  1 
ATOM   1671 C  C   . PRO A 1 198 ? 23.254 5.317   15.470  1.00 6.48  ? 200 PRO A C   1 
ATOM   1672 O  O   . PRO A 1 198 ? 22.553 5.139   14.451  1.00 7.10  ? 200 PRO A O   1 
ATOM   1673 C  CB  . PRO A 1 198 ? 25.323 3.840   15.051  1.00 6.07  ? 200 PRO A CB  1 
ATOM   1674 C  CG  . PRO A 1 198 ? 25.529 2.393   15.387  1.00 6.48  ? 200 PRO A CG  1 
ATOM   1675 C  CD  . PRO A 1 198 ? 24.120 1.825   15.361  1.00 6.18  ? 200 PRO A CD  1 
ATOM   1676 N  N   . PRO A 1 199 ? 23.277 6.515   16.071  1.00 6.54  ? 201 PRO A N   1 
ATOM   1677 C  CA  . PRO A 1 199 ? 24.279 6.946   17.067  1.00 6.79  ? 201 PRO A CA  1 
ATOM   1678 C  C   . PRO A 1 199 ? 23.887 6.590   18.533  1.00 6.02  ? 201 PRO A C   1 
ATOM   1679 O  O   . PRO A 1 199 ? 24.574 7.048   19.455  1.00 7.19  ? 201 PRO A O   1 
ATOM   1680 C  CB  . PRO A 1 199 ? 24.252 8.478   16.853  1.00 8.09  ? 201 PRO A CB  1 
ATOM   1681 C  CG  . PRO A 1 199 ? 22.860 8.808   16.380  1.00 8.61  ? 201 PRO A CG  1 
ATOM   1682 C  CD  . PRO A 1 199 ? 22.529 7.649   15.453  1.00 7.27  ? 201 PRO A CD  1 
ATOM   1683 N  N   . LEU A 1 200 ? 22.892 5.723   18.753  1.00 4.72  ? 202 LEU A N   1 
ATOM   1684 C  CA  . LEU A 1 200 ? 22.677 5.139   20.096  1.00 4.67  ? 202 LEU A CA  1 
ATOM   1685 C  C   . LEU A 1 200 ? 22.281 6.178   21.134  1.00 4.37  ? 202 LEU A C   1 
ATOM   1686 O  O   . LEU A 1 200 ? 22.445 5.947   22.337  1.00 4.67  ? 202 LEU A O   1 
ATOM   1687 C  CB  . LEU A 1 200 ? 23.866 4.256   20.550  1.00 5.10  ? 202 LEU A CB  1 
ATOM   1688 C  CG  . LEU A 1 200 ? 24.118 3.063   19.602  1.00 4.82  ? 202 LEU A CG  1 
ATOM   1689 C  CD1 . LEU A 1 200 ? 25.455 2.404   20.001  1.00 7.04  ? 202 LEU A CD1 1 
ATOM   1690 C  CD2 . LEU A 1 200 ? 23.010 2.006   19.610  1.00 5.82  ? 202 LEU A CD2 1 
ATOM   1691 N  N   . LEU A 1 201 ? 21.703 7.298   20.713  1.00 4.97  ? 203 LEU A N   1 
ATOM   1692 C  CA  . LEU A 1 201 ? 21.390 8.411   21.601  1.00 4.62  ? 203 LEU A CA  1 
ATOM   1693 C  C   . LEU A 1 201 ? 20.362 7.988   22.633  1.00 4.16  ? 203 LEU A C   1 
ATOM   1694 O  O   . LEU A 1 201 ? 19.406 7.258   22.342  1.00 4.72  ? 203 LEU A O   1 
ATOM   1695 C  CB  . LEU A 1 201 ? 20.871 9.582   20.800  1.00 6.80  ? 203 LEU A CB  1 
ATOM   1696 C  CG  . LEU A 1 201 ? 21.917 10.190  19.828  1.00 7.59  ? 203 LEU A CG  1 
ATOM   1697 C  CD1 . LEU A 1 201 ? 21.203 11.231  18.917  1.00 10.13 ? 203 LEU A CD1 1 
ATOM   1698 C  CD2 . LEU A 1 201 ? 23.112 10.855  20.551  1.00 12.27 ? 203 LEU A CD2 1 
ATOM   1699 N  N   . GLU A 1 202 ? 20.554 8.488   23.841  1.00 5.28  ? 204 GLU A N   1 
ATOM   1700 C  CA  . GLU A 1 202 ? 19.763 8.110   24.985  1.00 4.84  ? 204 GLU A CA  1 
ATOM   1701 C  C   . GLU A 1 202 ? 18.583 9.072   25.111  1.00 4.77  ? 204 GLU A C   1 
ATOM   1702 O  O   . GLU A 1 202 ? 18.460 9.862   26.086  1.00 6.73  ? 204 GLU A O   1 
ATOM   1703 C  CB  . GLU A 1 202 ? 20.602 7.975   26.241  1.00 5.02  ? 204 GLU A CB  1 
ATOM   1704 C  CG  . GLU A 1 202 ? 21.499 6.737   26.123  1.00 5.83  ? 204 GLU A CG  1 
ATOM   1705 C  CD  . GLU A 1 202 ? 22.406 6.485   27.293  1.00 6.70  ? 204 GLU A CD  1 
ATOM   1706 O  OE1 . GLU A 1 202 ? 22.787 7.439   28.008  1.00 9.26  ? 204 GLU A OE1 1 
ATOM   1707 O  OE2 . GLU A 1 202 ? 22.798 5.307   27.479  1.00 6.51  ? 204 GLU A OE2 1 
ATOM   1708 N  N   . CYS A 1 203 ? 17.681 9.002   24.171  1.00 4.47  ? 205 CYS A N   1 
ATOM   1709 C  CA  . CYS A 1 203 ? 16.600 9.974   23.984  1.00 4.14  ? 205 CYS A CA  1 
ATOM   1710 C  C   . CYS A 1 203 ? 15.253 9.345   23.852  1.00 3.55  ? 205 CYS A C   1 
ATOM   1711 O  O   . CYS A 1 203 ? 14.307 10.083  23.458  1.00 5.21  ? 205 CYS A O   1 
ATOM   1712 C  CB  . CYS A 1 203 ? 16.877 10.857  22.725  1.00 5.13  ? 205 CYS A CB  1 
ATOM   1713 S  SG  . CYS A 1 203 ? 16.976 9.892   21.207  1.00 5.73  ? 205 CYS A SG  1 
ATOM   1714 N  N   . VAL A 1 204 ? 15.110 8.062   24.154  1.00 3.92  ? 206 VAL A N   1 
ATOM   1715 C  CA  . VAL A 1 204 ? 13.859 7.354   23.795  1.00 3.37  ? 206 VAL A CA  1 
ATOM   1716 C  C   . VAL A 1 204 ? 13.087 6.921   25.047  1.00 3.47  ? 206 VAL A C   1 
ATOM   1717 O  O   . VAL A 1 204 ? 13.628 6.260   25.934  1.00 5.16  ? 206 VAL A O   1 
ATOM   1718 C  CB  . VAL A 1 204 ? 14.137 6.087   22.979  1.00 3.37  ? 206 VAL A CB  1 
ATOM   1719 C  CG1 . VAL A 1 204 ? 12.826 5.410   22.622  1.00 4.08  ? 206 VAL A CG1 1 
ATOM   1720 C  CG2 . VAL A 1 204 ? 14.894 6.431   21.672  1.00 4.69  ? 206 VAL A CG2 1 
ATOM   1721 N  N   . THR A 1 205 ? 11.757 7.228   25.106  1.00 3.51  ? 207 THR A N   1 
ATOM   1722 C  CA  . THR A 1 205 ? 10.841 6.488   25.999  1.00 3.46  ? 207 THR A CA  1 
ATOM   1723 C  C   . THR A 1 205 ? 10.322 5.328   25.138  1.00 2.98  ? 207 THR A C   1 
ATOM   1724 O  O   . THR A 1 205 ? 9.643  5.507   24.110  1.00 3.69  ? 207 THR A O   1 
ATOM   1725 C  CB  . THR A 1 205 ? 9.666  7.360   26.416  1.00 4.04  ? 207 THR A CB  1 
ATOM   1726 O  OG1 . THR A 1 205 ? 10.183 8.493   27.136  1.00 5.48  ? 207 THR A OG1 1 
ATOM   1727 C  CG2 . THR A 1 205 ? 8.735  6.546   27.320  1.00 6.02  ? 207 THR A CG2 1 
ATOM   1728 N  N   . TRP A 1 206 ? 10.657 4.119   25.545  1.00 2.90  ? 208 TRP A N   1 
ATOM   1729 C  CA  . TRP A 1 206 ? 10.207 2.898   24.879  1.00 3.07  ? 208 TRP A CA  1 
ATOM   1730 C  C   . TRP A 1 206 ? 8.833  2.508   25.366  1.00 2.89  ? 208 TRP A C   1 
ATOM   1731 O  O   . TRP A 1 206 ? 8.618  2.438   26.585  1.00 3.52  ? 208 TRP A O   1 
ATOM   1732 C  CB  . TRP A 1 206 ? 11.187 1.743   25.098  1.00 3.62  ? 208 TRP A CB  1 
ATOM   1733 C  CG  . TRP A 1 206 ? 12.323 1.848   24.121  1.00 2.33  ? 208 TRP A CG  1 
ATOM   1734 C  CD1 . TRP A 1 206 ? 13.564 2.445   24.309  1.00 3.28  ? 208 TRP A CD1 1 
ATOM   1735 C  CD2 . TRP A 1 206 ? 12.297 1.432   22.753  1.00 2.72  ? 208 TRP A CD2 1 
ATOM   1736 N  NE1 . TRP A 1 206 ? 14.302 2.437   23.128  1.00 3.47  ? 208 TRP A NE1 1 
ATOM   1737 C  CE2 . TRP A 1 206 ? 13.540 1.829   22.166  1.00 3.00  ? 208 TRP A CE2 1 
ATOM   1738 C  CE3 . TRP A 1 206 ? 11.299 0.778   21.978  1.00 2.78  ? 208 TRP A CE3 1 
ATOM   1739 C  CZ2 . TRP A 1 206 ? 13.765 1.586   20.827  1.00 3.46  ? 208 TRP A CZ2 1 
ATOM   1740 C  CZ3 . TRP A 1 206 ? 11.584 0.514   20.664  1.00 3.46  ? 208 TRP A CZ3 1 
ATOM   1741 C  CH2 . TRP A 1 206 ? 12.823 0.915   20.080  1.00 3.72  ? 208 TRP A CH2 1 
ATOM   1742 N  N   . ILE A 1 207 ? 7.955  2.132   24.435  1.00 2.81  ? 209 ILE A N   1 
ATOM   1743 C  CA  . ILE A 1 207 ? 6.641  1.616   24.767  1.00 3.28  ? 209 ILE A CA  1 
ATOM   1744 C  C   . ILE A 1 207 ? 6.497  0.371   23.911  1.00 3.21  ? 209 ILE A C   1 
ATOM   1745 O  O   . ILE A 1 207 ? 6.417  0.440   22.667  1.00 4.27  ? 209 ILE A O   1 
ATOM   1746 C  CB  . ILE A 1 207 ? 5.555  2.656   24.414  1.00 4.84  ? 209 ILE A CB  1 
ATOM   1747 C  CG1 . ILE A 1 207 ? 5.779  3.942   25.221  1.00 5.92  ? 209 ILE A CG1 1 
ATOM   1748 C  CG2 . ILE A 1 207 ? 4.155  2.052   24.686  1.00 5.10  ? 209 ILE A CG2 1 
ATOM   1749 C  CD1 . ILE A 1 207 ? 4.942  5.092   24.666  1.00 6.23  ? 209 ILE A CD1 1 
ATOM   1750 N  N   . VAL A 1 208 ? 6.585  -0.815  24.553  1.00 3.38  ? 210 VAL A N   1 
ATOM   1751 C  CA  . VAL A 1 208 ? 6.612  -2.112  23.897  1.00 2.84  ? 210 VAL A CA  1 
ATOM   1752 C  C   . VAL A 1 208 ? 5.317  -2.818  24.117  1.00 3.14  ? 210 VAL A C   1 
ATOM   1753 O  O   . VAL A 1 208 ? 4.988  -3.088  25.258  1.00 4.22  ? 210 VAL A O   1 
ATOM   1754 C  CB  . VAL A 1 208 ? 7.829  -2.944  24.293  1.00 3.34  ? 210 VAL A CB  1 
ATOM   1755 C  CG1 . VAL A 1 208 ? 7.811  -4.294  23.644  1.00 4.56  ? 210 VAL A CG1 1 
ATOM   1756 C  CG2 . VAL A 1 208 ? 9.144  -2.184  24.048  1.00 5.06  ? 210 VAL A CG2 1 
ATOM   1757 N  N   . LEU A 1 209 ? 4.555  -3.062  23.046  1.00 4.33  ? 211 LEU A N   1 
ATOM   1758 C  CA  . LEU A 1 209 ? 3.251  -3.711  23.229  1.00 4.42  ? 211 LEU A CA  1 
ATOM   1759 C  C   . LEU A 1 209 ? 3.432  -5.188  23.588  1.00 3.99  ? 211 LEU A C   1 
ATOM   1760 O  O   . LEU A 1 209 ? 4.299  -5.913  23.084  1.00 5.00  ? 211 LEU A O   1 
ATOM   1761 C  CB  . LEU A 1 209 ? 2.439  -3.613  21.936  1.00 4.91  ? 211 LEU A CB  1 
ATOM   1762 C  CG  . LEU A 1 209 ? 2.043  -2.198  21.512  1.00 5.52  ? 211 LEU A CG  1 
ATOM   1763 C  CD1 . LEU A 1 209 ? 1.024  -2.266  20.381  1.00 7.48  ? 211 LEU A CD1 1 
ATOM   1764 C  CD2 . LEU A 1 209 ? 1.490  -1.350  22.680  1.00 6.84  ? 211 LEU A CD2 1 
ATOM   1765 N  N   . LYS A 1 210 ? 2.591  -5.661  24.522  1.00 5.20  ? 212 LYS A N   1 
ATOM   1766 C  CA  . LYS A 1 210 ? 2.626  -7.076  24.897  1.00 5.66  ? 212 LYS A CA  1 
ATOM   1767 C  C   . LYS A 1 210 ? 2.144  -8.000  23.796  1.00 4.82  ? 212 LYS A C   1 
ATOM   1768 O  O   . LYS A 1 210 ? 2.687  -9.099  23.655  1.00 6.61  ? 212 LYS A O   1 
ATOM   1769 C  CB  . LYS A 1 210 ? 1.826  -7.302  26.158  1.00 8.22  ? 212 LYS A CB  1 
ATOM   1770 C  CG  . LYS A 1 210 ? 1.728  -8.779  26.575  1.00 11.03 ? 212 LYS A CG  1 
ATOM   1771 C  CD  . LYS A 1 210 ? 0.958  -8.985  27.906  1.00 17.34 ? 212 LYS A CD  1 
ATOM   1772 C  CE  . LYS A 1 210 ? 0.796  -10.405 28.248  1.00 21.92 ? 212 LYS A CE  1 
ATOM   1773 N  N   A GLU A 1 211 ? 1.121  -7.611  23.046  0.50 4.55  ? 213 GLU A N   1 
ATOM   1774 N  N   B GLU A 1 211 ? 1.112  -7.618  23.053  0.50 4.75  ? 213 GLU A N   1 
ATOM   1775 C  CA  A GLU A 1 211 ? 0.493  -8.491  22.047  0.50 5.33  ? 213 GLU A CA  1 
ATOM   1776 C  CA  B GLU A 1 211 ? 0.557  -8.535  22.052  0.50 5.24  ? 213 GLU A CA  1 
ATOM   1777 C  C   A GLU A 1 211 ? 1.261  -8.427  20.745  0.50 4.43  ? 213 GLU A C   1 
ATOM   1778 C  C   B GLU A 1 211 ? 1.282  -8.417  20.734  0.50 4.86  ? 213 GLU A C   1 
ATOM   1779 O  O   A GLU A 1 211 ? 1.359  -7.321  20.184  0.50 4.85  ? 213 GLU A O   1 
ATOM   1780 O  O   B GLU A 1 211 ? 1.330  -7.303  20.156  0.50 5.06  ? 213 GLU A O   1 
ATOM   1781 C  CB  A GLU A 1 211 ? -0.928 -7.972  21.769  0.50 6.24  ? 213 GLU A CB  1 
ATOM   1782 C  CB  B GLU A 1 211 ? -0.945 -8.317  21.851  0.50 5.75  ? 213 GLU A CB  1 
ATOM   1783 C  CG  A GLU A 1 211 ? -1.720 -8.952  20.925  0.50 7.57  ? 213 GLU A CG  1 
ATOM   1784 C  CG  B GLU A 1 211 ? -1.536 -9.307  20.870  0.50 7.01  ? 213 GLU A CG  1 
ATOM   1785 C  CD  A GLU A 1 211 ? -3.169 -8.535  20.689  0.50 9.15  ? 213 GLU A CD  1 
ATOM   1786 C  CD  B GLU A 1 211 ? -3.035 -9.126  20.680  0.50 6.61  ? 213 GLU A CD  1 
ATOM   1787 O  OE1 A GLU A 1 211 ? -3.838 -8.066  21.659  0.50 9.59  ? 213 GLU A OE1 1 
ATOM   1788 O  OE1 B GLU A 1 211 ? -3.599 -8.096  21.072  0.50 6.53  ? 213 GLU A OE1 1 
ATOM   1789 O  OE2 A GLU A 1 211 ? -3.612 -8.733  19.481  0.50 12.74 ? 213 GLU A OE2 1 
ATOM   1790 O  OE2 B GLU A 1 211 ? -3.636 -10.000 20.056  0.50 9.60  ? 213 GLU A OE2 1 
ATOM   1791 N  N   A PRO A 1 212 ? 1.828  -9.527  20.272  0.50 4.14  ? 214 PRO A N   1 
ATOM   1792 N  N   B PRO A 1 212 ? 1.919  -9.484  20.304  0.50 4.66  ? 214 PRO A N   1 
ATOM   1793 C  CA  A PRO A 1 212 ? 2.443  -9.435  18.953  0.50 4.40  ? 214 PRO A CA  1 
ATOM   1794 C  CA  B PRO A 1 212 ? 2.493  -9.458  18.947  0.50 5.31  ? 214 PRO A CA  1 
ATOM   1795 C  C   A PRO A 1 212 ? 1.409  -9.384  17.863  0.50 5.01  ? 214 PRO A C   1 
ATOM   1796 C  C   B PRO A 1 212 ? 1.491  -9.525  17.830  0.50 5.73  ? 214 PRO A C   1 
ATOM   1797 O  O   A PRO A 1 212 ? 0.210  -9.657  18.110  0.50 5.33  ? 214 PRO A O   1 
ATOM   1798 O  O   B PRO A 1 212 ? 0.402  -10.071 17.987  0.50 6.59  ? 214 PRO A O   1 
ATOM   1799 C  CB  A PRO A 1 212 ? 3.223  -10.809 18.861  0.50 4.40  ? 214 PRO A CB  1 
ATOM   1800 C  CB  B PRO A 1 212 ? 3.289  -10.809 18.910  0.50 6.41  ? 214 PRO A CB  1 
ATOM   1801 C  CG  A PRO A 1 212 ? 2.404  -11.777 19.676  0.50 4.31  ? 214 PRO A CG  1 
ATOM   1802 C  CG  B PRO A 1 212 ? 3.271  -11.293 20.322  0.50 8.74  ? 214 PRO A CG  1 
ATOM   1803 C  CD  A PRO A 1 212 ? 1.702  -10.934 20.758  0.50 4.69  ? 214 PRO A CD  1 
ATOM   1804 C  CD  B PRO A 1 212 ? 2.120  -10.789 21.023  0.50 5.79  ? 214 PRO A CD  1 
ATOM   1805 N  N   . ILE A 1 213 ? 1.880  -8.990  16.662  1.00 5.72  ? 215 ILE A N   1 
ATOM   1806 C  CA  . ILE A 1 213 ? 1.050  -9.241  15.464  1.00 6.03  ? 215 ILE A CA  1 
ATOM   1807 C  C   . ILE A 1 213 ? 1.611  -10.455 14.785  1.00 5.93  ? 215 ILE A C   1 
ATOM   1808 O  O   . ILE A 1 213 ? 2.750  -10.836 14.913  1.00 6.73  ? 215 ILE A O   1 
ATOM   1809 C  CB  . ILE A 1 213 ? 0.997  -8.022  14.511  1.00 7.38  ? 215 ILE A CB  1 
ATOM   1810 C  CG1 . ILE A 1 213 ? 2.423  -7.664  14.005  1.00 7.69  ? 215 ILE A CG1 1 
ATOM   1811 C  CG2 . ILE A 1 213 ? 0.350  -6.819  15.198  1.00 8.35  ? 215 ILE A CG2 1 
ATOM   1812 C  CD1 . ILE A 1 213 ? 2.390  -6.642  12.831  1.00 9.06  ? 215 ILE A CD1 1 
ATOM   1813 N  N   A SER A 1 214 ? 0.684  -11.119 14.052  0.50 6.54  ? 216 SER A N   1 
ATOM   1814 N  N   B SER A 1 214 ? 0.726  -11.147 14.060  0.50 7.06  ? 216 SER A N   1 
ATOM   1815 C  CA  A SER A 1 214 ? 1.019  -12.269 13.180  0.50 7.03  ? 216 SER A CA  1 
ATOM   1816 C  CA  B SER A 1 214 ? 1.186  -12.289 13.279  0.50 7.34  ? 216 SER A CA  1 
ATOM   1817 C  C   A SER A 1 214 ? 1.303  -11.773 11.761  0.50 5.62  ? 216 SER A C   1 
ATOM   1818 C  C   B SER A 1 214 ? 1.291  -11.867 11.827  0.50 6.22  ? 216 SER A C   1 
ATOM   1819 O  O   A SER A 1 214 ? 0.549  -10.964 11.208  0.50 7.62  ? 216 SER A O   1 
ATOM   1820 O  O   B SER A 1 214 ? 0.372  -11.232 11.317  0.50 7.39  ? 216 SER A O   1 
ATOM   1821 C  CB  A SER A 1 214 ? -0.114 -13.350 13.242  0.50 7.81  ? 216 SER A CB  1 
ATOM   1822 C  CB  B SER A 1 214 ? 0.168  -13.407 13.475  0.50 9.83  ? 216 SER A CB  1 
ATOM   1823 O  OG  A SER A 1 214 ? -0.033 -14.081 14.496  0.50 7.70  ? 216 SER A OG  1 
ATOM   1824 O  OG  B SER A 1 214 ? 0.368  -14.454 12.572  0.50 13.24 ? 216 SER A OG  1 
ATOM   1825 N  N   . VAL A 1 215 ? 2.400  -12.301 11.196  1.00 7.02  ? 217 VAL A N   1 
ATOM   1826 C  CA  . VAL A 1 215 ? 2.647  -12.139 9.741   1.00 6.71  ? 217 VAL A CA  1 
ATOM   1827 C  C   . VAL A 1 215 ? 2.869  -13.472 9.203   1.00 6.40  ? 217 VAL A C   1 
ATOM   1828 O  O   . VAL A 1 215 ? 3.270  -14.411 9.899   1.00 6.84  ? 217 VAL A O   1 
ATOM   1829 C  CB  . VAL A 1 215 ? 3.853  -11.168 9.516   1.00 7.75  ? 217 VAL A CB  1 
ATOM   1830 C  CG1 . VAL A 1 215 ? 3.602  -9.805  10.229  1.00 7.97  ? 217 VAL A CG1 1 
ATOM   1831 C  CG2 . VAL A 1 215 ? 5.126  -11.824 10.042  1.00 8.91  ? 217 VAL A CG2 1 
ATOM   1832 N  N   . SER A 1 216 ? 2.753  -13.636 7.865   1.00 6.92  ? 218 SER A N   1 
ATOM   1833 C  CA  . SER A 1 216 ? 2.959  -14.974 7.302   1.00 7.45  ? 218 SER A CA  1 
ATOM   1834 C  C   . SER A 1 216 ? 4.458  -15.246 7.061   1.00 7.67  ? 218 SER A C   1 
ATOM   1835 O  O   . SER A 1 216 ? 5.266  -14.332 6.903   1.00 7.59  ? 218 SER A O   1 
ATOM   1836 C  CB  . SER A 1 216 ? 2.148  -15.198 6.033   1.00 9.70  ? 218 SER A CB  1 
ATOM   1837 O  OG  . SER A 1 216 ? 2.655  -14.306 5.049   1.00 9.79  ? 218 SER A OG  1 
ATOM   1838 N  N   A SER A 1 217 ? 4.759  -16.519 6.862   0.50 8.05  ? 219 SER A N   1 
ATOM   1839 N  N   B SER A 1 217 ? 4.756  -16.513 6.899   0.50 7.95  ? 219 SER A N   1 
ATOM   1840 C  CA  A SER A 1 217 ? 6.086  -16.943 6.472   0.50 8.81  ? 219 SER A CA  1 
ATOM   1841 C  CA  B SER A 1 217 ? 6.075  -16.881 6.533   0.50 8.49  ? 219 SER A CA  1 
ATOM   1842 C  C   A SER A 1 217 ? 6.499  -16.286 5.150   0.50 9.89  ? 219 SER A C   1 
ATOM   1843 C  C   B SER A 1 217 ? 6.464  -16.190 5.208   0.50 9.22  ? 219 SER A C   1 
ATOM   1844 O  O   A SER A 1 217 ? 7.615  -15.859 4.979   0.50 10.05 ? 219 SER A O   1 
ATOM   1845 O  O   B SER A 1 217 ? 7.527  -15.613 5.116   0.50 10.88 ? 219 SER A O   1 
ATOM   1846 C  CB  A SER A 1 217 ? 6.144  -18.480 6.437   0.50 10.88 ? 219 SER A CB  1 
ATOM   1847 C  CB  B SER A 1 217 ? 6.172  -18.396 6.539   0.50 8.90  ? 219 SER A CB  1 
ATOM   1848 O  OG  A SER A 1 217 ? 5.266  -19.026 5.446   0.50 11.07 ? 219 SER A OG  1 
ATOM   1849 O  OG  B SER A 1 217 ? 7.511  -18.802 6.300   0.50 9.73  ? 219 SER A OG  1 
ATOM   1850 N  N   . GLU A 1 218 ? 5.544  -16.161 4.216   1.00 9.63  ? 220 GLU A N   1 
ATOM   1851 C  CA  . GLU A 1 218 ? 5.833  -15.544 2.946   1.00 11.39 ? 220 GLU A CA  1 
ATOM   1852 C  C   . GLU A 1 218 ? 6.139  -14.040 3.095   1.00 9.14  ? 220 GLU A C   1 
ATOM   1853 O  O   . GLU A 1 218 ? 7.013  -13.498 2.396   1.00 11.63 ? 220 GLU A O   1 
ATOM   1854 C  CB  . GLU A 1 218 ? 4.703  -15.706 1.944   1.00 13.35 ? 220 GLU A CB  1 
ATOM   1855 C  CG  . GLU A 1 218 ? 4.443  -17.251 1.587   1.00 17.02 ? 220 GLU A CG  1 
ATOM   1856 C  CD  . GLU A 1 218 ? 3.490  -17.968 2.532   1.00 21.02 ? 220 GLU A CD  1 
ATOM   1857 O  OE1 . GLU A 1 218 ? 3.123  -17.483 3.586   1.00 16.42 ? 220 GLU A OE1 1 
ATOM   1858 O  OE2 . GLU A 1 218 ? 3.059  -19.056 2.186   1.00 30.32 ? 220 GLU A OE2 1 
ATOM   1859 N  N   . GLN A 1 219 ? 5.437  -13.350 4.021   1.00 7.41  ? 221 GLN A N   1 
ATOM   1860 C  CA  . GLN A 1 219 ? 5.713  -11.952 4.216   1.00 8.80  ? 221 GLN A CA  1 
ATOM   1861 C  C   . GLN A 1 219 ? 7.120  -11.684 4.767   1.00 7.78  ? 221 GLN A C   1 
ATOM   1862 O  O   . GLN A 1 219 ? 7.833  -10.851 4.246   1.00 8.07  ? 221 GLN A O   1 
ATOM   1863 C  CB  . GLN A 1 219 ? 4.620  -11.374 5.175   1.00 8.30  ? 221 GLN A CB  1 
ATOM   1864 C  CG  . GLN A 1 219 ? 3.280  -11.227 4.448   1.00 8.02  ? 221 GLN A CG  1 
ATOM   1865 C  CD  . GLN A 1 219 ? 2.163  -10.724 5.334   1.00 7.93  ? 221 GLN A CD  1 
ATOM   1866 O  OE1 . GLN A 1 219 ? 2.070  -11.039 6.526   1.00 7.78  ? 221 GLN A OE1 1 
ATOM   1867 N  NE2 . GLN A 1 219 ? 1.344  -9.793  4.755   1.00 7.96  ? 221 GLN A NE2 1 
ATOM   1868 N  N   . VAL A 1 220 ? 7.483  -12.471 5.771   1.00 8.08  ? 222 VAL A N   1 
ATOM   1869 C  CA  . VAL A 1 220 ? 8.816  -12.255 6.355   1.00 8.13  ? 222 VAL A CA  1 
ATOM   1870 C  C   . VAL A 1 220 ? 9.918  -12.735 5.401   1.00 9.27  ? 222 VAL A C   1 
ATOM   1871 O  O   . VAL A 1 220 ? 10.993 -12.120 5.336   1.00 8.58  ? 222 VAL A O   1 
ATOM   1872 C  CB  . VAL A 1 220 ? 8.945  -12.800 7.793   1.00 10.19 ? 222 VAL A CB  1 
ATOM   1873 C  CG1 . VAL A 1 220 ? 9.016  -14.286 7.820   1.00 13.36 ? 222 VAL A CG1 1 
ATOM   1874 C  CG2 . VAL A 1 220 ? 10.238 -12.240 8.520   1.00 12.03 ? 222 VAL A CG2 1 
ATOM   1875 N  N   . LEU A 1 221 ? 9.660  -13.713 4.559   1.00 9.50  ? 223 LEU A N   1 
ATOM   1876 C  CA  . LEU A 1 221 ? 10.648 -14.144 3.556   1.00 11.56 ? 223 LEU A CA  1 
ATOM   1877 C  C   . LEU A 1 221 ? 10.940 -13.032 2.593   1.00 10.60 ? 223 LEU A C   1 
ATOM   1878 O  O   . LEU A 1 221 ? 12.101 -12.898 2.199   1.00 11.94 ? 223 LEU A O   1 
ATOM   1879 C  CB  . LEU A 1 221 ? 10.191 -15.433 2.864   1.00 13.12 ? 223 LEU A CB  1 
ATOM   1880 C  CG  . LEU A 1 221 ? 10.374 -16.698 3.760   1.00 17.11 ? 223 LEU A CG  1 
ATOM   1881 C  CD1 . LEU A 1 221 ? 9.414  -17.881 3.326   1.00 20.30 ? 223 LEU A CD1 1 
ATOM   1882 C  CD2 . LEU A 1 221 ? 11.883 -17.082 3.884   1.00 21.78 ? 223 LEU A CD2 1 
ATOM   1883 N  N   . LYS A 1 222 ? 9.967  -12.143 2.278   1.00 9.90  ? 224 LYS A N   1 
ATOM   1884 C  CA  . LYS A 1 222 ? 10.227 -11.055 1.393   1.00 11.12 ? 224 LYS A CA  1 
ATOM   1885 C  C   . LYS A 1 222 ? 11.082 -9.986  2.077   1.00 8.73  ? 224 LYS A C   1 
ATOM   1886 O  O   . LYS A 1 222 ? 11.884 -9.395  1.425   1.00 10.59 ? 224 LYS A O   1 
ATOM   1887 C  CB  . LYS A 1 222 ? 8.892  -10.552 0.866   1.00 12.54 ? 224 LYS A CB  1 
ATOM   1888 C  CG  . LYS A 1 222 ? 8.317  -11.581 -0.246  1.00 18.35 ? 224 LYS A CG  1 
ATOM   1889 C  CD  . LYS A 1 222 ? 7.058  -11.284 -0.967  1.00 24.48 ? 224 LYS A CD  1 
ATOM   1890 C  CE  . LYS A 1 222 ? 6.549  -12.481 -1.880  1.00 24.17 ? 224 LYS A CE  1 
ATOM   1891 N  NZ  . LYS A 1 222 ? 5.200  -12.225 -2.552  1.00 24.36 ? 224 LYS A NZ  1 
ATOM   1892 N  N   . PHE A 1 223 ? 10.972 -9.770  3.405   1.00 7.24  ? 225 PHE A N   1 
ATOM   1893 C  CA  . PHE A 1 223 ? 11.895 -8.881  4.087   1.00 7.08  ? 225 PHE A CA  1 
ATOM   1894 C  C   . PHE A 1 223 ? 13.338 -9.404  3.887   1.00 7.87  ? 225 PHE A C   1 
ATOM   1895 O  O   . PHE A 1 223 ? 14.267 -8.640  3.681   1.00 7.61  ? 225 PHE A O   1 
ATOM   1896 C  CB  . PHE A 1 223 ? 11.657 -8.942  5.612   1.00 8.79  ? 225 PHE A CB  1 
ATOM   1897 C  CG  . PHE A 1 223 ? 10.489 -8.126  6.145   1.00 7.69  ? 225 PHE A CG  1 
ATOM   1898 C  CD1 . PHE A 1 223 ? 9.441  -7.708  5.367   1.00 11.64 ? 225 PHE A CD1 1 
ATOM   1899 C  CD2 . PHE A 1 223 ? 10.421 -7.905  7.524   1.00 11.40 ? 225 PHE A CD2 1 
ATOM   1900 C  CE1 . PHE A 1 223 ? 8.373  -6.975  5.921   1.00 12.93 ? 225 PHE A CE1 1 
ATOM   1901 C  CE2 . PHE A 1 223 ? 9.378  -7.142  8.084   1.00 13.01 ? 225 PHE A CE2 1 
ATOM   1902 C  CZ  . PHE A 1 223 ? 8.358  -6.690  7.255   1.00 11.54 ? 225 PHE A CZ  1 
ATOM   1903 N  N   . ARG A 1 224 ? 13.508 -10.762 3.955   1.00 7.43  ? 226 ARG A N   1 
ATOM   1904 C  CA  . ARG A 1 224 ? 14.853 -11.345 3.923   1.00 7.82  ? 226 ARG A CA  1 
ATOM   1905 C  C   . ARG A 1 224 ? 15.430 -11.398 2.479   1.00 7.95  ? 226 ARG A C   1 
ATOM   1906 O  O   . ARG A 1 224 ? 16.581 -11.802 2.359   1.00 9.43  ? 226 ARG A O   1 
ATOM   1907 C  CB  . ARG A 1 224 ? 14.763 -12.779 4.458   1.00 8.50  ? 226 ARG A CB  1 
ATOM   1908 C  CG  . ARG A 1 224 ? 14.264 -12.885 5.895   1.00 8.05  ? 226 ARG A CG  1 
ATOM   1909 C  CD  . ARG A 1 224 ? 14.320 -14.323 6.347   1.00 8.72  ? 226 ARG A CD  1 
ATOM   1910 N  NE  . ARG A 1 224 ? 13.761 -14.460 7.687   1.00 8.46  ? 226 ARG A NE  1 
ATOM   1911 C  CZ  . ARG A 1 224 ? 12.832 -15.314 8.062   1.00 8.92  ? 226 ARG A CZ  1 
ATOM   1912 N  NH1 . ARG A 1 224 ? 12.399 -16.245 7.244   1.00 11.90 ? 226 ARG A NH1 1 
ATOM   1913 N  NH2 . ARG A 1 224 ? 12.355 -15.237 9.309   1.00 9.94  ? 226 ARG A NH2 1 
ATOM   1914 N  N   . LYS A 1 225 ? 14.677 -10.915 1.472   1.00 7.55  ? 227 LYS A N   1 
ATOM   1915 C  CA  . LYS A 1 225 ? 15.205 -10.767 0.115   1.00 9.03  ? 227 LYS A CA  1 
ATOM   1916 C  C   . LYS A 1 225 ? 15.817 -9.433  -0.107  1.00 8.19  ? 227 LYS A C   1 
ATOM   1917 O  O   . LYS A 1 225 ? 16.517 -9.193  -1.152  1.00 10.75 ? 227 LYS A O   1 
ATOM   1918 C  CB  . LYS A 1 225 ? 14.054 -10.996 -0.916  1.00 11.11 ? 227 LYS A CB  1 
ATOM   1919 C  CG  . LYS A 1 225 ? 13.563 -12.431 -0.933  1.00 14.63 ? 227 LYS A CG  1 
ATOM   1920 C  CD  . LYS A 1 225 ? 12.527 -12.660 -2.038  1.00 20.94 ? 227 LYS A CD  1 
ATOM   1921 C  CE  . LYS A 1 225 ? 13.172 -12.771 -3.412  1.00 27.67 ? 227 LYS A CE  1 
ATOM   1922 N  NZ  . LYS A 1 225 ? 12.228 -13.094 -4.534  1.00 43.33 ? 227 LYS A NZ  1 
ATOM   1923 N  N   . LEU A 1 226 ? 15.582 -8.449  0.804   1.00 8.76  ? 228 LEU A N   1 
ATOM   1924 C  CA  . LEU A 1 226 ? 16.270 -7.186  0.710   1.00 8.21  ? 228 LEU A CA  1 
ATOM   1925 C  C   . LEU A 1 226 ? 17.778 -7.364  0.832   1.00 8.27  ? 228 LEU A C   1 
ATOM   1926 O  O   . LEU A 1 226 ? 18.333 -8.407  1.241   1.00 8.31  ? 228 LEU A O   1 
ATOM   1927 C  CB  . LEU A 1 226 ? 15.775 -6.233  1.771   1.00 8.80  ? 228 LEU A CB  1 
ATOM   1928 C  CG  . LEU A 1 226 ? 14.341 -5.735  1.583   1.00 9.48  ? 228 LEU A CG  1 
ATOM   1929 C  CD1 . LEU A 1 226 ? 13.921 -5.120  2.868   1.00 10.04 ? 228 LEU A CD1 1 
ATOM   1930 C  CD2 . LEU A 1 226 ? 14.292 -4.708  0.444   1.00 12.69 ? 228 LEU A CD2 1 
ATOM   1931 N  N   . ASN A 1 227 ? 18.476 -6.311  0.463   1.00 9.22  ? 229 ASN A N   1 
ATOM   1932 C  CA  . ASN A 1 227 ? 19.918 -6.361  0.497   1.00 8.66  ? 229 ASN A CA  1 
ATOM   1933 C  C   . ASN A 1 227 ? 20.520 -5.163  1.286   1.00 9.50  ? 229 ASN A C   1 
ATOM   1934 O  O   . ASN A 1 227 ? 20.038 -4.031  1.223   1.00 10.34 ? 229 ASN A O   1 
ATOM   1935 C  CB  . ASN A 1 227 ? 20.527 -6.160  -0.959  1.00 9.75  ? 229 ASN A CB  1 
ATOM   1936 C  CG  . ASN A 1 227 ? 20.479 -7.345  -1.865  1.00 10.15 ? 229 ASN A CG  1 
ATOM   1937 O  OD1 . ASN A 1 227 ? 21.044 -7.224  -2.977  1.00 13.88 ? 229 ASN A OD1 1 
ATOM   1938 N  ND2 . ASN A 1 227 ? 19.790 -8.418  -1.523  1.00 9.96  ? 229 ASN A ND2 1 
ATOM   1939 N  N   . PHE A 1 228 ? 21.581 -5.505  2.071   1.00 9.09  ? 230 PHE A N   1 
ATOM   1940 C  CA  . PHE A 1 228 ? 22.293 -4.401  2.719   1.00 8.99  ? 230 PHE A CA  1 
ATOM   1941 C  C   . PHE A 1 228 ? 23.221 -3.648  1.759   1.00 11.16 ? 230 PHE A C   1 
ATOM   1942 O  O   . PHE A 1 228 ? 23.521 -2.489  1.971   1.00 10.68 ? 230 PHE A O   1 
ATOM   1943 C  CB  . PHE A 1 228 ? 23.285 -4.953  3.737   1.00 10.40 ? 230 PHE A CB  1 
ATOM   1944 C  CG  . PHE A 1 228 ? 22.680 -5.569  5.026   1.00 9.28  ? 230 PHE A CG  1 
ATOM   1945 C  CD1 . PHE A 1 228 ? 21.918 -4.787  5.907   1.00 8.69  ? 230 PHE A CD1 1 
ATOM   1946 C  CD2 . PHE A 1 228 ? 23.009 -6.870  5.388   1.00 9.65  ? 230 PHE A CD2 1 
ATOM   1947 C  CE1 . PHE A 1 228 ? 21.459 -5.267  7.154   1.00 9.82  ? 230 PHE A CE1 1 
ATOM   1948 C  CE2 . PHE A 1 228 ? 22.549 -7.406  6.640   1.00 10.02 ? 230 PHE A CE2 1 
ATOM   1949 C  CZ  . PHE A 1 228 ? 21.836 -6.591  7.530   1.00 9.93  ? 230 PHE A CZ  1 
ATOM   1950 N  N   . ASN A 1 229 ? 23.690 -4.332  0.763   1.00 11.36 ? 231 ASN A N   1 
ATOM   1951 C  CA  . ASN A 1 229 ? 24.592 -3.739  -0.293  1.00 11.28 ? 231 ASN A CA  1 
ATOM   1952 C  C   . ASN A 1 229 ? 23.817 -2.851  -1.222  1.00 10.55 ? 231 ASN A C   1 
ATOM   1953 O  O   . ASN A 1 229 ? 22.568 -2.940  -1.368  1.00 12.03 ? 231 ASN A O   1 
ATOM   1954 C  CB  . ASN A 1 229 ? 25.199 -4.866  -1.105  1.00 13.19 ? 231 ASN A CB  1 
ATOM   1955 C  CG  . ASN A 1 229 ? 24.128 -5.755  -1.668  1.00 11.56 ? 231 ASN A CG  1 
ATOM   1956 O  OD1 . ASN A 1 229 ? 23.619 -6.615  -0.913  1.00 13.65 ? 231 ASN A OD1 1 
ATOM   1957 N  ND2 . ASN A 1 229 ? 23.819 -5.664  -2.979  1.00 13.03 ? 231 ASN A ND2 1 
ATOM   1958 N  N   . GLY A 1 230 ? 24.616 -1.984  -1.908  1.00 13.13 ? 232 GLY A N   1 
ATOM   1959 C  CA  . GLY A 1 230 ? 24.012 -1.180  -3.022  1.00 14.28 ? 232 GLY A CA  1 
ATOM   1960 C  C   . GLY A 1 230 ? 24.004 -1.922  -4.328  1.00 14.22 ? 232 GLY A C   1 
ATOM   1961 O  O   . GLY A 1 230 ? 24.567 -3.037  -4.387  1.00 14.01 ? 232 GLY A O   1 
ATOM   1962 N  N   . GLU A 1 231 ? 23.265 -1.392  -5.311  1.00 12.83 ? 233 GLU A N   1 
ATOM   1963 C  CA  . GLU A 1 231 ? 23.143 -1.936  -6.620  1.00 12.13 ? 233 GLU A CA  1 
ATOM   1964 C  C   . GLU A 1 231 ? 24.514 -2.136  -7.190  1.00 14.69 ? 233 GLU A C   1 
ATOM   1965 O  O   . GLU A 1 231 ? 25.400 -1.317  -7.039  1.00 16.31 ? 233 GLU A O   1 
ATOM   1966 C  CB  . GLU A 1 231 ? 22.295 -0.962  -7.532  1.00 12.50 ? 233 GLU A CB  1 
ATOM   1967 C  CG  . GLU A 1 231 ? 21.982 -1.516  -8.936  1.00 13.58 ? 233 GLU A CG  1 
ATOM   1968 C  CD  . GLU A 1 231 ? 21.263 -0.540  -9.767  1.00 22.57 ? 233 GLU A CD  1 
ATOM   1969 O  OE1 . GLU A 1 231 ? 21.023 0.638   -9.284  1.00 20.32 ? 233 GLU A OE1 1 
ATOM   1970 O  OE2 . GLU A 1 231 ? 20.904 -0.930  -10.925 1.00 19.40 ? 233 GLU A OE2 1 
ATOM   1971 N  N   . GLY A 1 232 ? 24.676 -3.260  -7.855  1.00 16.74 ? 234 GLY A N   1 
ATOM   1972 C  CA  . GLY A 1 232 ? 25.971 -3.559  -8.465  1.00 21.99 ? 234 GLY A CA  1 
ATOM   1973 C  C   . GLY A 1 232 ? 27.043 -4.047  -7.562  1.00 23.32 ? 234 GLY A C   1 
ATOM   1974 O  O   . GLY A 1 232 ? 28.195 -4.222  -7.930  1.00 35.60 ? 234 GLY A O   1 
ATOM   1975 N  N   . GLU A 1 233 ? 26.712 -4.259  -6.289  1.00 16.80 ? 235 GLU A N   1 
ATOM   1976 C  CA  . GLU A 1 233 ? 27.699 -4.864  -5.350  1.00 14.74 ? 235 GLU A CA  1 
ATOM   1977 C  C   . GLU A 1 233 ? 27.256 -6.308  -4.999  1.00 17.64 ? 235 GLU A C   1 
ATOM   1978 O  O   . GLU A 1 233 ? 26.098 -6.666  -5.216  1.00 19.52 ? 235 GLU A O   1 
ATOM   1979 C  CB  . GLU A 1 233 ? 27.686 -4.080  -4.010  1.00 15.06 ? 235 GLU A CB  1 
ATOM   1980 C  CG  . GLU A 1 233 ? 28.124 -2.625  -4.282  1.00 18.35 ? 235 GLU A CG  1 
ATOM   1981 C  CD  . GLU A 1 233 ? 28.038 -1.730  -3.050  1.00 23.27 ? 235 GLU A CD  1 
ATOM   1982 O  OE1 . GLU A 1 233 ? 27.481 -2.096  -1.986  1.00 21.13 ? 235 GLU A OE1 1 
ATOM   1983 O  OE2 . GLU A 1 233 ? 28.554 -0.571  -3.185  1.00 35.78 ? 235 GLU A OE2 1 
ATOM   1984 N  N   . PRO A 1 234 ? 28.183 -7.106  -4.511  1.00 16.48 ? 236 PRO A N   1 
ATOM   1985 C  CA  . PRO A 1 234 ? 27.838 -8.519  -4.254  1.00 17.23 ? 236 PRO A CA  1 
ATOM   1986 C  C   . PRO A 1 234 ? 26.733 -8.526  -3.190  1.00 14.03 ? 236 PRO A C   1 
ATOM   1987 O  O   . PRO A 1 234 ? 26.692 -7.758  -2.190  1.00 15.97 ? 236 PRO A O   1 
ATOM   1988 C  CB  . PRO A 1 234 ? 29.121 -9.048  -3.646  1.00 19.95 ? 236 PRO A CB  1 
ATOM   1989 C  CG  . PRO A 1 234 ? 30.235 -8.164  -4.233  1.00 23.56 ? 236 PRO A CG  1 
ATOM   1990 C  CD  . PRO A 1 234 ? 29.641 -6.780  -4.289  1.00 20.50 ? 236 PRO A CD  1 
ATOM   1991 N  N   . GLU A 1 235 ? 25.812 -9.431  -3.420  1.00 14.34 ? 237 GLU A N   1 
ATOM   1992 C  CA  . GLU A 1 235 ? 24.695 -9.521  -2.539  1.00 14.66 ? 237 GLU A CA  1 
ATOM   1993 C  C   . GLU A 1 235 ? 25.005 -9.935  -1.111  1.00 13.50 ? 237 GLU A C   1 
ATOM   1994 O  O   . GLU A 1 235 ? 25.574 -10.943 -0.825  1.00 12.63 ? 237 GLU A O   1 
ATOM   1995 C  CB  . GLU A 1 235 ? 23.641 -10.467 -3.126  1.00 13.19 ? 237 GLU A CB  1 
ATOM   1996 C  CG  . GLU A 1 235 ? 22.323 -10.475 -2.368  1.00 18.04 ? 237 GLU A CG  1 
ATOM   1997 C  CD  . GLU A 1 235 ? 21.253 -11.290 -3.069  1.00 14.63 ? 237 GLU A CD  1 
ATOM   1998 O  OE1 . GLU A 1 235 ? 21.552 -12.426 -3.492  1.00 25.21 ? 237 GLU A OE1 1 
ATOM   1999 O  OE2 . GLU A 1 235 ? 20.114 -10.794 -3.196  1.00 13.67 ? 237 GLU A OE2 1 
ATOM   2000 N  N   . GLU A 1 236 ? 24.525 -9.138  -0.180  1.00 11.08 ? 238 GLU A N   1 
ATOM   2001 C  CA  . GLU A 1 236 ? 24.490 -9.418  1.268   1.00 13.47 ? 238 GLU A CA  1 
ATOM   2002 C  C   . GLU A 1 236 ? 23.086 -9.316  1.712   1.00 9.96  ? 238 GLU A C   1 
ATOM   2003 O  O   . GLU A 1 236 ? 22.497 -8.188  1.803   1.00 13.30 ? 238 GLU A O   1 
ATOM   2004 C  CB  . GLU A 1 236 ? 25.210 -8.217  1.954   1.00 14.62 ? 238 GLU A CB  1 
ATOM   2005 C  CG  . GLU A 1 236 ? 26.581 -7.914  1.480   1.00 16.09 ? 238 GLU A CG  1 
ATOM   2006 C  CD  . GLU A 1 236 ? 27.322 -6.807  2.207   1.00 25.79 ? 238 GLU A CD  1 
ATOM   2007 O  OE1 . GLU A 1 236 ? 28.520 -6.903  2.028   1.00 38.57 ? 238 GLU A OE1 1 
ATOM   2008 O  OE2 . GLU A 1 236 ? 26.821 -6.108  3.154   1.00 23.64 ? 238 GLU A OE2 1 
ATOM   2009 N  N   . LEU A 1 237 ? 22.397 -10.463 2.012   1.00 8.95  ? 239 LEU A N   1 
ATOM   2010 C  CA  . LEU A 1 237 ? 20.978 -10.366 2.317   1.00 9.03  ? 239 LEU A CA  1 
ATOM   2011 C  C   . LEU A 1 237 ? 20.794 -9.552  3.599   1.00 7.74  ? 239 LEU A C   1 
ATOM   2012 O  O   . LEU A 1 237 ? 21.559 -9.687  4.571   1.00 9.05  ? 239 LEU A O   1 
ATOM   2013 C  CB  . LEU A 1 237 ? 20.392 -11.773 2.516   1.00 8.68  ? 239 LEU A CB  1 
ATOM   2014 C  CG  . LEU A 1 237 ? 20.367 -12.624 1.243   1.00 9.51  ? 239 LEU A CG  1 
ATOM   2015 C  CD1 . LEU A 1 237 ? 19.897 -14.021 1.700   1.00 14.85 ? 239 LEU A CD1 1 
ATOM   2016 C  CD2 . LEU A 1 237 ? 19.541 -11.999 0.139   1.00 12.10 ? 239 LEU A CD2 1 
ATOM   2017 N  N   . MET A 1 238 ? 19.764 -8.751  3.605   1.00 7.90  ? 240 MET A N   1 
ATOM   2018 C  CA  . MET A 1 238 ? 19.441 -7.892  4.744   1.00 8.12  ? 240 MET A CA  1 
ATOM   2019 C  C   . MET A 1 238 ? 18.652 -8.801  5.726   1.00 6.45  ? 240 MET A C   1 
ATOM   2020 O  O   . MET A 1 238 ? 17.445 -8.955  5.627   1.00 7.26  ? 240 MET A O   1 
ATOM   2021 C  CB  . MET A 1 238 ? 18.574 -6.734  4.266   1.00 8.77  ? 240 MET A CB  1 
ATOM   2022 C  CG  . MET A 1 238 ? 18.216 -5.721  5.499   1.00 9.00  ? 240 MET A CG  1 
ATOM   2023 S  SD  . MET A 1 238 ? 17.283 -4.321  4.955   1.00 9.39  ? 240 MET A SD  1 
ATOM   2024 C  CE  . MET A 1 238 ? 18.585 -3.245  4.230   1.00 11.44 ? 240 MET A CE  1 
ATOM   2025 N  N   . VAL A 1 239 ? 19.432 -9.370  6.665   1.00 6.74  ? 241 VAL A N   1 
ATOM   2026 C  CA  . VAL A 1 239 ? 18.857 -10.251 7.706   1.00 5.77  ? 241 VAL A CA  1 
ATOM   2027 C  C   . VAL A 1 239 ? 19.669 -10.016 8.962   1.00 5.17  ? 241 VAL A C   1 
ATOM   2028 O  O   . VAL A 1 239 ? 20.838 -9.607  8.922   1.00 7.10  ? 241 VAL A O   1 
ATOM   2029 C  CB  . VAL A 1 239 ? 18.971 -11.776 7.326   1.00 6.23  ? 241 VAL A CB  1 
ATOM   2030 C  CG1 . VAL A 1 239 ? 18.017 -12.072 6.118   1.00 7.31  ? 241 VAL A CG1 1 
ATOM   2031 C  CG2 . VAL A 1 239 ? 20.407 -12.256 7.138   1.00 8.00  ? 241 VAL A CG2 1 
ATOM   2032 N  N   . ASP A 1 240 ? 19.030 -10.326 10.133  1.00 5.06  ? 242 ASP A N   1 
ATOM   2033 C  CA  . ASP A 1 240 ? 19.742 -10.195 11.398  1.00 5.23  ? 242 ASP A CA  1 
ATOM   2034 C  C   . ASP A 1 240 ? 20.224 -8.760  11.665  1.00 4.47  ? 242 ASP A C   1 
ATOM   2035 O  O   . ASP A 1 240 ? 21.337 -8.533  12.142  1.00 6.09  ? 242 ASP A O   1 
ATOM   2036 C  CB  . ASP A 1 240 ? 20.820 -11.253 11.610  1.00 6.37  ? 242 ASP A CB  1 
ATOM   2037 C  CG  . ASP A 1 240 ? 20.232 -12.666 11.677  1.00 5.70  ? 242 ASP A CG  1 
ATOM   2038 O  OD1 . ASP A 1 240 ? 19.163 -12.813 12.331  1.00 6.50  ? 242 ASP A OD1 1 
ATOM   2039 O  OD2 . ASP A 1 240 ? 20.828 -13.568 11.086  1.00 7.66  ? 242 ASP A OD2 1 
ATOM   2040 N  N   . ASN A 1 241 ? 19.318 -7.858  11.352  1.00 4.51  ? 243 ASN A N   1 
ATOM   2041 C  CA  . ASN A 1 241 ? 19.615 -6.404  11.579  1.00 5.13  ? 243 ASN A CA  1 
ATOM   2042 C  C   . ASN A 1 241 ? 19.086 -5.955  12.931  1.00 4.48  ? 243 ASN A C   1 
ATOM   2043 O  O   . ASN A 1 241 ? 18.415 -4.929  13.047  1.00 5.62  ? 243 ASN A O   1 
ATOM   2044 C  CB  . ASN A 1 241 ? 19.072 -5.571  10.409  1.00 4.89  ? 243 ASN A CB  1 
ATOM   2045 C  CG  . ASN A 1 241 ? 17.622 -5.781  10.185  1.00 5.71  ? 243 ASN A CG  1 
ATOM   2046 O  OD1 . ASN A 1 241 ? 16.952 -6.559  10.788  1.00 6.48  ? 243 ASN A OD1 1 
ATOM   2047 N  ND2 . ASN A 1 241 ? 17.121 -5.039  9.191   1.00 12.56 ? 243 ASN A ND2 1 
ATOM   2048 N  N   . TRP A 1 242 ? 19.377 -6.727  13.973  1.00 4.13  ? 244 TRP A N   1 
ATOM   2049 C  CA  . TRP A 1 242 ? 18.908 -6.453  15.338  1.00 3.98  ? 244 TRP A CA  1 
ATOM   2050 C  C   . TRP A 1 242 ? 20.118 -6.370  16.268  1.00 4.23  ? 244 TRP A C   1 
ATOM   2051 O  O   . TRP A 1 242 ? 21.103 -7.096  16.124  1.00 4.84  ? 244 TRP A O   1 
ATOM   2052 C  CB  . TRP A 1 242 ? 17.954 -7.607  15.830  1.00 4.17  ? 244 TRP A CB  1 
ATOM   2053 C  CG  . TRP A 1 242 ? 18.427 -8.974  15.656  1.00 4.41  ? 244 TRP A CG  1 
ATOM   2054 C  CD1 . TRP A 1 242 ? 18.323 -9.730  14.480  1.00 5.45  ? 244 TRP A CD1 1 
ATOM   2055 C  CD2 . TRP A 1 242 ? 19.023 -9.841  16.599  1.00 4.33  ? 244 TRP A CD2 1 
ATOM   2056 N  NE1 . TRP A 1 242 ? 18.805 -11.000 14.698  1.00 5.15  ? 244 TRP A NE1 1 
ATOM   2057 C  CE2 . TRP A 1 242 ? 19.287 -11.085 15.993  1.00 4.77  ? 244 TRP A CE2 1 
ATOM   2058 C  CE3 . TRP A 1 242 ? 19.302 -9.677  17.967  1.00 5.67  ? 244 TRP A CE3 1 
ATOM   2059 C  CZ2 . TRP A 1 242 ? 19.843 -12.167 16.681  1.00 5.70  ? 244 TRP A CZ2 1 
ATOM   2060 C  CZ3 . TRP A 1 242 ? 19.886 -10.716 18.656  1.00 7.10  ? 244 TRP A CZ3 1 
ATOM   2061 C  CH2 . TRP A 1 242 ? 20.132 -11.994 18.008  1.00 7.67  ? 244 TRP A CH2 1 
ATOM   2062 N  N   . ARG A 1 243 ? 20.007 -5.479  17.250  1.00 4.08  ? 245 ARG A N   1 
ATOM   2063 C  CA  . ARG A 1 243 ? 20.978 -5.438  18.313  1.00 4.01  ? 245 ARG A CA  1 
ATOM   2064 C  C   . ARG A 1 243 ? 20.459 -6.307  19.498  1.00 4.28  ? 245 ARG A C   1 
ATOM   2065 O  O   . ARG A 1 243 ? 19.291 -6.278  19.809  1.00 4.94  ? 245 ARG A O   1 
ATOM   2066 C  CB  . ARG A 1 243 ? 21.217 -4.000  18.773  1.00 3.67  ? 245 ARG A CB  1 
ATOM   2067 C  CG  . ARG A 1 243 ? 22.182 -3.874  19.940  1.00 4.08  ? 245 ARG A CG  1 
ATOM   2068 C  CD  . ARG A 1 243 ? 22.092 -2.500  20.585  1.00 4.85  ? 245 ARG A CD  1 
ATOM   2069 N  NE  . ARG A 1 243 ? 23.366 -2.082  21.163  1.00 4.86  ? 245 ARG A NE  1 
ATOM   2070 C  CZ  . ARG A 1 243 ? 23.511 -1.046  21.982  1.00 3.84  ? 245 ARG A CZ  1 
ATOM   2071 N  NH1 . ARG A 1 243 ? 22.458 -0.316  22.324  1.00 5.52  ? 245 ARG A NH1 1 
ATOM   2072 N  NH2 . ARG A 1 243 ? 24.709 -0.739  22.460  1.00 6.18  ? 245 ARG A NH2 1 
ATOM   2073 N  N   A PRO A 1 244 ? 21.377 -7.082  20.074  0.50 4.02  ? 246 PRO A N   1 
ATOM   2074 N  N   B PRO A 1 244 ? 21.357 -7.066  20.111  0.50 4.84  ? 246 PRO A N   1 
ATOM   2075 C  CA  A PRO A 1 244 ? 21.026 -7.884  21.277  0.50 4.28  ? 246 PRO A CA  1 
ATOM   2076 C  CA  B PRO A 1 244 ? 20.855 -7.926  21.220  0.50 4.83  ? 246 PRO A CA  1 
ATOM   2077 C  C   A PRO A 1 244 ? 20.614 -7.042  22.482  0.50 4.07  ? 246 PRO A C   1 
ATOM   2078 C  C   B PRO A 1 244 ? 20.607 -7.079  22.454  0.50 4.30  ? 246 PRO A C   1 
ATOM   2079 O  O   A PRO A 1 244 ? 20.888 -5.850  22.611  0.50 4.96  ? 246 PRO A O   1 
ATOM   2080 O  O   B PRO A 1 244 ? 20.994 -5.930  22.567  0.50 5.46  ? 246 PRO A O   1 
ATOM   2081 C  CB  A PRO A 1 244 ? 22.326 -8.639  21.600  0.50 5.31  ? 246 PRO A CB  1 
ATOM   2082 C  CB  B PRO A 1 244 ? 21.989 -8.908  21.478  0.50 7.22  ? 246 PRO A CB  1 
ATOM   2083 C  CG  A PRO A 1 244 ? 22.945 -8.785  20.203  0.50 5.16  ? 246 PRO A CG  1 
ATOM   2084 C  CG  B PRO A 1 244 ? 23.213 -8.108  21.045  0.50 7.57  ? 246 PRO A CG  1 
ATOM   2085 C  CD  A PRO A 1 244 ? 22.711 -7.439  19.562  0.50 4.70  ? 246 PRO A CD  1 
ATOM   2086 C  CD  B PRO A 1 244 ? 22.812 -7.194  19.899  0.50 6.16  ? 246 PRO A CD  1 
ATOM   2087 N  N   . ALA A 1 245 ? 19.956 -7.715  23.412  1.00 5.22  ? 247 ALA A N   1 
ATOM   2088 C  CA  . ALA A 1 245 ? 19.582 -7.082  24.669  1.00 5.16  ? 247 ALA A CA  1 
ATOM   2089 C  C   . ALA A 1 245 ? 20.812 -6.547  25.402  1.00 5.61  ? 247 ALA A C   1 
ATOM   2090 O  O   . ALA A 1 245 ? 21.869 -7.223  25.431  1.00 5.91  ? 247 ALA A O   1 
ATOM   2091 C  CB  . ALA A 1 245 ? 18.817 -8.059  25.577  1.00 7.50  ? 247 ALA A CB  1 
ATOM   2092 N  N   . GLN A 1 246 ? 20.660 -5.354  25.986  1.00 5.07  ? 248 GLN A N   1 
ATOM   2093 C  CA  . GLN A 1 246 ? 21.730 -4.623  26.697  1.00 5.72  ? 248 GLN A CA  1 
ATOM   2094 C  C   . GLN A 1 246 ? 21.459 -4.647  28.227  1.00 5.81  ? 248 GLN A C   1 
ATOM   2095 O  O   . GLN A 1 246 ? 20.310 -4.836  28.649  1.00 6.23  ? 248 GLN A O   1 
ATOM   2096 C  CB  . GLN A 1 246 ? 21.780 -3.205  26.182  1.00 6.42  ? 248 GLN A CB  1 
ATOM   2097 C  CG  . GLN A 1 246 ? 22.079 -3.168  24.665  1.00 6.29  ? 248 GLN A CG  1 
ATOM   2098 C  CD  . GLN A 1 246 ? 23.416 -3.815  24.332  1.00 7.30  ? 248 GLN A CD  1 
ATOM   2099 O  OE1 . GLN A 1 246 ? 24.479 -3.481  24.947  1.00 9.91  ? 248 GLN A OE1 1 
ATOM   2100 N  NE2 . GLN A 1 246 ? 23.422 -4.759  23.426  1.00 7.82  ? 248 GLN A NE2 1 
ATOM   2101 N  N   . PRO A 1 247 ? 22.468 -4.325  29.023  1.00 7.14  ? 249 PRO A N   1 
ATOM   2102 C  CA  . PRO A 1 247 ? 22.235 -4.333  30.482  1.00 8.39  ? 249 PRO A CA  1 
ATOM   2103 C  C   . PRO A 1 247 ? 21.140 -3.379  30.895  1.00 5.81  ? 249 PRO A C   1 
ATOM   2104 O  O   . PRO A 1 247 ? 21.152 -2.166  30.561  1.00 7.35  ? 249 PRO A O   1 
ATOM   2105 C  CB  . PRO A 1 247 ? 23.669 -3.907  31.021  1.00 11.23 ? 249 PRO A CB  1 
ATOM   2106 C  CG  . PRO A 1 247 ? 24.635 -4.456  30.012  1.00 13.90 ? 249 PRO A CG  1 
ATOM   2107 C  CD  . PRO A 1 247 ? 23.902 -4.085  28.669  1.00 10.59 ? 249 PRO A CD  1 
ATOM   2108 N  N   . LEU A 1 248 ? 20.281 -3.820  31.820  1.00 7.03  ? 250 LEU A N   1 
ATOM   2109 C  CA  . LEU A 1 248 ? 19.201 -2.941  32.284  1.00 6.98  ? 250 LEU A CA  1 
ATOM   2110 C  C   . LEU A 1 248 ? 19.735 -1.875  33.217  1.00 5.88  ? 250 LEU A C   1 
ATOM   2111 O  O   . LEU A 1 248 ? 19.175 -0.775  33.270  1.00 6.65  ? 250 LEU A O   1 
ATOM   2112 C  CB  . LEU A 1 248 ? 18.166 -3.797  33.065  1.00 8.70  ? 250 LEU A CB  1 
ATOM   2113 C  CG  . LEU A 1 248 ? 16.883 -3.095  33.447  1.00 9.02  ? 250 LEU A CG  1 
ATOM   2114 C  CD1 . LEU A 1 248 ? 16.132 -2.533  32.203  1.00 10.26 ? 250 LEU A CD1 1 
ATOM   2115 C  CD2 . LEU A 1 248 ? 15.966 -4.025  34.288  1.00 13.97 ? 250 LEU A CD2 1 
ATOM   2116 N  N   . LYS A 1 249 ? 20.809 -2.144  33.946  1.00 7.88  ? 251 LYS A N   1 
ATOM   2117 C  CA  . LYS A 1 249 ? 21.431 -1.125  34.832  1.00 8.69  ? 251 LYS A CA  1 
ATOM   2118 C  C   . LYS A 1 249 ? 20.377 -0.545  35.795  1.00 9.93  ? 251 LYS A C   1 
ATOM   2119 O  O   . LYS A 1 249 ? 19.547 -1.352  36.307  1.00 13.08 ? 251 LYS A O   1 
ATOM   2120 C  CB  . LYS A 1 249 ? 22.187 -0.064  34.038  1.00 10.76 ? 251 LYS A CB  1 
ATOM   2121 C  CG  . LYS A 1 249 ? 23.379 -0.775  33.300  1.00 13.65 ? 251 LYS A CG  1 
ATOM   2122 C  CD  . LYS A 1 249 ? 24.295 0.223   32.588  1.00 14.19 ? 251 LYS A CD  1 
ATOM   2123 C  CE  . LYS A 1 249 ? 25.472 -0.491  32.052  1.00 21.58 ? 251 LYS A CE  1 
ATOM   2124 N  NZ  . LYS A 1 249 ? 26.389 0.365   31.249  1.00 23.58 ? 251 LYS A NZ  1 
ATOM   2125 N  N   . ASN A 1 250 ? 20.433 0.740   36.009  1.00 10.07 ? 252 ASN A N   1 
ATOM   2126 C  CA  . ASN A 1 250 ? 19.566 1.249   37.021  1.00 15.78 ? 252 ASN A CA  1 
ATOM   2127 C  C   . ASN A 1 250 ? 18.215 1.626   36.426  1.00 15.16 ? 252 ASN A C   1 
ATOM   2128 O  O   . ASN A 1 250 ? 17.929 2.882   36.480  1.00 18.71 ? 252 ASN A O   1 
ATOM   2129 C  CB  . ASN A 1 250 ? 20.194 2.496   37.708  1.00 23.08 ? 252 ASN A CB  1 
ATOM   2130 C  CG  . ASN A 1 250 ? 19.410 2.964   38.940  1.00 25.02 ? 252 ASN A CG  1 
ATOM   2131 O  OD1 . ASN A 1 250 ? 18.804 2.192   39.769  1.00 33.89 ? 252 ASN A OD1 1 
ATOM   2132 N  ND2 . ASN A 1 250 ? 19.461 4.289   39.121  1.00 27.71 ? 252 ASN A ND2 1 
ATOM   2133 N  N   . ARG A 1 251 ? 17.435 0.637   35.859  1.00 12.88 ? 253 ARG A N   1 
ATOM   2134 C  CA  . ARG A 1 251 ? 16.140 0.973   35.335  1.00 7.82  ? 253 ARG A CA  1 
ATOM   2135 C  C   . ARG A 1 251 ? 15.051 0.016   35.754  1.00 8.05  ? 253 ARG A C   1 
ATOM   2136 O  O   . ARG A 1 251 ? 15.264 -1.194  35.915  1.00 16.69 ? 253 ARG A O   1 
ATOM   2137 C  CB  . ARG A 1 251 ? 16.190 1.004   33.792  1.00 6.31  ? 253 ARG A CB  1 
ATOM   2138 C  CG  . ARG A 1 251 ? 17.112 2.137   33.334  1.00 6.58  ? 253 ARG A CG  1 
ATOM   2139 C  CD  . ARG A 1 251 ? 17.263 2.141   31.805  1.00 4.99  ? 253 ARG A CD  1 
ATOM   2140 N  NE  . ARG A 1 251 ? 18.063 0.975   31.357  1.00 4.82  ? 253 ARG A NE  1 
ATOM   2141 C  CZ  . ARG A 1 251 ? 18.324 0.709   30.084  1.00 3.88  ? 253 ARG A CZ  1 
ATOM   2142 N  NH1 . ARG A 1 251 ? 17.711 1.409   29.077  1.00 4.33  ? 253 ARG A NH1 1 
ATOM   2143 N  NH2 . ARG A 1 251 ? 19.136 -0.299  29.769  1.00 4.28  ? 253 ARG A NH2 1 
ATOM   2144 N  N   . GLN A 1 252 ? 13.842 0.552   35.823  1.00 8.42  ? 254 GLN A N   1 
ATOM   2145 C  CA  . GLN A 1 252 ? 12.659 -0.202  36.070  1.00 9.26  ? 254 GLN A CA  1 
ATOM   2146 C  C   . GLN A 1 252 ? 11.788 -0.248  34.863  1.00 8.62  ? 254 GLN A C   1 
ATOM   2147 O  O   . GLN A 1 252 ? 11.516 0.818   34.201  1.00 12.42 ? 254 GLN A O   1 
ATOM   2148 C  CB  . GLN A 1 252 ? 11.911 0.471   37.195  1.00 15.20 ? 254 GLN A CB  1 
ATOM   2149 C  CG  . GLN A 1 252 ? 12.645 0.183   38.516  1.00 23.05 ? 254 GLN A CG  1 
ATOM   2150 C  CD  . GLN A 1 252 ? 11.736 -0.764  39.235  1.00 38.54 ? 254 GLN A CD  1 
ATOM   2151 O  OE1 . GLN A 1 252 ? 11.589 -0.803  40.507  1.00 44.73 ? 254 GLN A OE1 1 
ATOM   2152 N  NE2 . GLN A 1 252 ? 11.006 -1.552  38.359  1.00 35.59 ? 254 GLN A NE2 1 
ATOM   2153 N  N   . ILE A 1 253 ? 11.353 -1.435  34.474  1.00 6.92  ? 255 ILE A N   1 
ATOM   2154 C  CA  . ILE A 1 253 ? 10.360 -1.609  33.425  1.00 5.85  ? 255 ILE A CA  1 
ATOM   2155 C  C   . ILE A 1 253 ? 8.963  -1.641  34.041  1.00 5.85  ? 255 ILE A C   1 
ATOM   2156 O  O   . ILE A 1 253 ? 8.755  -2.357  35.026  1.00 8.10  ? 255 ILE A O   1 
ATOM   2157 C  CB  . ILE A 1 253 ? 10.623 -2.847  32.587  1.00 6.57  ? 255 ILE A CB  1 
ATOM   2158 C  CG1 . ILE A 1 253 ? 12.122 -2.851  32.038  1.00 7.46  ? 255 ILE A CG1 1 
ATOM   2159 C  CG2 . ILE A 1 253 ? 9.553  -3.012  31.521  1.00 8.20  ? 255 ILE A CG2 1 
ATOM   2160 C  CD1 . ILE A 1 253 ? 12.409 -4.040  31.251  1.00 8.14  ? 255 ILE A CD1 1 
ATOM   2161 N  N   . LYS A 1 254 ? 8.079  -0.772  33.577  1.00 6.28  ? 256 LYS A N   1 
ATOM   2162 C  CA  . LYS A 1 254 ? 6.753  -0.653  34.153  1.00 6.04  ? 256 LYS A CA  1 
ATOM   2163 C  C   . LYS A 1 254 ? 5.729  -1.266  33.215  1.00 5.36  ? 256 LYS A C   1 
ATOM   2164 O  O   . LYS A 1 254 ? 5.903  -1.146  31.970  1.00 8.02  ? 256 LYS A O   1 
ATOM   2165 C  CB  . LYS A 1 254 ? 6.435  0.818   34.407  1.00 8.09  ? 256 LYS A CB  1 
ATOM   2166 C  CG  . LYS A 1 254 ? 7.388  1.396   35.523  1.00 12.56 ? 256 LYS A CG  1 
ATOM   2167 C  CD  . LYS A 1 254 ? 7.232  0.602   36.739  1.00 23.64 ? 256 LYS A CD  1 
ATOM   2168 N  N   . ALA A 1 255 ? 4.703  -1.914  33.703  1.00 6.27  ? 257 ALA A N   1 
ATOM   2169 C  CA  . ALA A 1 255 ? 3.644  -2.556  32.935  1.00 7.40  ? 257 ALA A CA  1 
ATOM   2170 C  C   . ALA A 1 255 ? 2.398  -1.718  33.082  1.00 6.44  ? 257 ALA A C   1 
ATOM   2171 O  O   . ALA A 1 255 ? 2.025  -1.300  34.201  1.00 7.99  ? 257 ALA A O   1 
ATOM   2172 C  CB  . ALA A 1 255 ? 3.375  -3.991  33.339  1.00 9.25  ? 257 ALA A CB  1 
ATOM   2173 N  N   . SER A 1 256 ? 1.643  -1.585  32.009  1.00 7.74  ? 258 SER A N   1 
ATOM   2174 C  CA  . SER A 1 256 ? 0.364  -0.881  32.042  1.00 9.03  ? 258 SER A CA  1 
ATOM   2175 C  C   . SER A 1 256 ? -0.813 -1.743  32.493  1.00 9.93  ? 258 SER A C   1 
ATOM   2176 O  O   . SER A 1 256 ? -1.953 -1.209  32.597  1.00 16.47 ? 258 SER A O   1 
ATOM   2177 C  CB  . SER A 1 256 ? 0.072  -0.360  30.648  1.00 8.76  ? 258 SER A CB  1 
ATOM   2178 O  OG  . SER A 1 256 ? -0.345 -1.344  29.726  1.00 8.57  ? 258 SER A OG  1 
ATOM   2179 N  N   . PHE A 1 257 ? -0.533 -3.025  32.694  1.00 11.10 ? 259 PHE A N   1 
ATOM   2180 C  CA  . PHE A 1 257 ? -1.518 -4.040  32.880  1.00 12.10 ? 259 PHE A CA  1 
ATOM   2181 C  C   . PHE A 1 257 ? -1.072 -4.992  34.016  1.00 18.59 ? 259 PHE A C   1 
ATOM   2182 O  O   . PHE A 1 257 ? 0.174  -5.155  34.301  1.00 18.53 ? 259 PHE A O   1 
ATOM   2183 C  CB  . PHE A 1 257 ? -1.699 -4.838  31.588  1.00 12.80 ? 259 PHE A CB  1 
ATOM   2184 C  CG  . PHE A 1 257 ? -0.448 -5.528  31.159  1.00 11.99 ? 259 PHE A CG  1 
ATOM   2185 C  CD1 . PHE A 1 257 ? 0.497  -4.858  30.416  1.00 9.14  ? 259 PHE A CD1 1 
ATOM   2186 C  CD2 . PHE A 1 257 ? -0.239 -6.866  31.563  1.00 16.67 ? 259 PHE A CD2 1 
ATOM   2187 C  CE1 . PHE A 1 257 ? 1.717  -5.513  30.104  1.00 12.02 ? 259 PHE A CE1 1 
ATOM   2188 C  CE2 . PHE A 1 257 ? 0.952  -7.519  31.259  1.00 17.36 ? 259 PHE A CE2 1 
ATOM   2189 C  CZ  . PHE A 1 257 ? 1.929  -6.878  30.514  1.00 15.89 ? 259 PHE A CZ  1 
ATOM   2190 N  N   . LYS A 1 258 ? -2.094 -5.615  34.602  1.00 25.06 ? 260 LYS A N   1 
ATOM   2191 C  CA  . LYS A 1 258 ? -2.183 -6.835  35.445  1.00 35.44 ? 260 LYS A CA  1 
ATOM   2192 C  C   . LYS A 1 258 ? -2.482 -6.407  36.826  1.00 42.34 ? 260 LYS A C   1 
ATOM   2193 O  O   . LYS A 1 258 ? -1.754 -6.790  37.739  1.00 51.79 ? 260 LYS A O   1 
ATOM   2194 C  CB  . LYS A 1 258 ? -0.957 -7.795  35.398  1.00 41.28 ? 260 LYS A CB  1 
ATOM   2195 C  CG  . LYS A 1 258 ? -1.187 -8.993  34.466  1.00 56.98 ? 260 LYS A CG  1 
ATOM   2196 O  OXT . LYS A 1 258 ? -3.462 -5.651  37.053  1.00 58.67 ? 260 LYS A OXT 1 
HETATM 2197 ZN ZN  . ZN  B 2 .   ? 14.433 0.160   15.279  1.00 3.62  ? 301 ZN  A ZN  1 
HETATM 2198 NA NA  . NA  C 3 .   ? 3.195  21.020  6.014   1.00 26.26 ? 302 NA  A NA  1 
HETATM 2199 NA NA  . NA  D 3 .   ? 12.837 16.812  10.638  1.00 34.57 ? 303 NA  A NA  1 
HETATM 2200 NA NA  . NA  E 3 .   ? 5.604  -8.360  37.755  1.00 43.57 ? 304 NA  A NA  1 
HETATM 2201 NA NA  . NA  F 3 .   ? 24.124 -8.040  29.465  1.00 40.60 ? 305 NA  A NA  1 
HETATM 2202 N  N1  A BCN G 4 .   ? 0.588  -12.477 23.286  0.50 20.72 ? 306 BCN A N1  1 
HETATM 2203 N  N1  B BCN G 4 .   ? 1.163  -12.304 23.706  0.50 22.49 ? 306 BCN A N1  1 
HETATM 2204 C  C1  A BCN G 4 .   ? 1.476  -12.359 24.473  0.50 19.98 ? 306 BCN A C1  1 
HETATM 2205 C  C1  B BCN G 4 .   ? 1.576  -12.193 25.111  0.50 19.96 ? 306 BCN A C1  1 
HETATM 2206 C  C2  A BCN G 4 .   ? 1.183  -13.365 25.570  0.50 19.62 ? 306 BCN A C2  1 
HETATM 2207 C  C2  B BCN G 4 .   ? 1.237  -13.471 25.840  0.50 20.31 ? 306 BCN A C2  1 
HETATM 2208 O  O21 A BCN G 4 .   ? 0.152  -14.077 25.621  0.50 29.05 ? 306 BCN A O21 1 
HETATM 2209 O  O21 B BCN G 4 .   ? 0.167  -14.052 25.556  0.50 29.54 ? 306 BCN A O21 1 
HETATM 2210 O  O22 A BCN G 4 .   ? 1.844  -13.193 26.593  0.50 26.08 ? 306 BCN A O22 1 
HETATM 2211 O  O22 B BCN G 4 .   ? 1.985  -13.842 26.770  0.50 26.10 ? 306 BCN A O22 1 
HETATM 2212 C  C3  A BCN G 4 .   ? 0.860  -13.669 22.455  0.50 12.88 ? 306 BCN A C3  1 
HETATM 2213 C  C3  B BCN G 4 .   ? 1.618  -13.591 23.162  0.50 14.86 ? 306 BCN A C3  1 
HETATM 2214 C  C4  A BCN G 4 .   ? -0.315 -13.902 21.496  0.50 32.65 ? 306 BCN A C4  1 
HETATM 2215 C  C4  B BCN G 4 .   ? 2.543  -13.343 21.978  0.50 40.24 ? 306 BCN A C4  1 
HETATM 2216 O  O4  A BCN G 4 .   ? 0.077  -14.482 20.235  0.50 22.52 ? 306 BCN A O4  1 
HETATM 2217 O  O4  B BCN G 4 .   ? 3.731  -14.127 22.129  0.50 20.44 ? 306 BCN A O4  1 
HETATM 2218 C  C5  A BCN G 4 .   ? -0.829 -12.475 23.681  0.50 17.09 ? 306 BCN A C5  1 
HETATM 2219 C  C5  B BCN G 4 .   ? -0.301 -12.225 23.618  0.50 16.81 ? 306 BCN A C5  1 
HETATM 2220 C  C6  A BCN G 4 .   ? -1.364 -11.050 23.644  0.50 37.93 ? 306 BCN A C6  1 
HETATM 2221 C  C6  B BCN G 4 .   ? -0.730 -10.763 23.590  0.50 39.54 ? 306 BCN A C6  1 
HETATM 2222 O  O6  A BCN G 4 .   ? -1.413 -10.541 24.980  0.50 21.83 ? 306 BCN A O6  1 
HETATM 2223 O  O6  B BCN G 4 .   ? -1.394 -10.437 24.816  0.50 22.69 ? 306 BCN A O6  1 
HETATM 2224 S  S   . DMS H 5 .   ? 22.656 -10.004 14.997  1.00 31.07 ? 307 DMS A S   1 
HETATM 2225 O  O   . DMS H 5 .   ? 21.354 -9.446  14.570  1.00 58.08 ? 307 DMS A O   1 
HETATM 2226 C  C1  . DMS H 5 .   ? 23.885 -9.446  13.952  1.00 29.37 ? 307 DMS A C1  1 
HETATM 2227 C  C2  . DMS H 5 .   ? 23.143 -9.261  16.455  1.00 20.45 ? 307 DMS A C2  1 
HETATM 2228 O  O18 . 84Z I 6 .   ? 16.838 6.840   11.652  1.00 8.86  ? 308 84Z A O18 1 
HETATM 2229 S  S16 . 84Z I 6 .   ? 16.661 7.402   12.974  1.00 7.29  ? 308 84Z A S16 1 
HETATM 2230 O  O17 . 84Z I 6 .   ? 15.521 8.241   13.160  1.00 8.23  ? 308 84Z A O17 1 
HETATM 2231 C  C19 . 84Z I 6 .   ? 18.102 8.326   13.415  1.00 8.07  ? 308 84Z A C19 1 
HETATM 2232 C  C24 . 84Z I 6 .   ? 19.183 8.407   12.487  1.00 11.61 ? 308 84Z A C24 1 
HETATM 2233 C  C23 . 84Z I 6 .   ? 20.248 9.232   12.739  1.00 14.10 ? 308 84Z A C23 1 
HETATM 2234 C  C22 . 84Z I 6 .   ? 20.302 9.902   13.956  1.00 13.89 ? 308 84Z A C22 1 
HETATM 2235 C  C21 . 84Z I 6 .   ? 19.295 9.798   14.903  1.00 12.61 ? 308 84Z A C21 1 
HETATM 2236 C  C20 . 84Z I 6 .   ? 18.131 8.986   14.618  1.00 10.09 ? 308 84Z A C20 1 
HETATM 2237 C  C3  . 84Z I 6 .   ? 16.424 6.128   14.151  1.00 5.73  ? 308 84Z A C3  1 
HETATM 2238 C  C2  . 84Z I 6 .   ? 15.547 6.322   15.181  1.00 6.03  ? 308 84Z A C2  1 
HETATM 2239 C  C4  . 84Z I 6 .   ? 17.017 4.821   13.951  1.00 5.47  ? 308 84Z A C4  1 
HETATM 2240 C  C12 . 84Z I 6 .   ? 18.021 4.489   12.949  1.00 6.70  ? 308 84Z A C12 1 
HETATM 2241 O  O14 . 84Z I 6 .   ? 19.057 5.365   12.889  1.00 7.88  ? 308 84Z A O14 1 
HETATM 2242 C  C15 . 84Z I 6 .   ? 20.031 5.170   11.935  1.00 11.29 ? 308 84Z A C15 1 
HETATM 2243 O  O13 . 84Z I 6 .   ? 18.066 3.472   12.318  1.00 7.77  ? 308 84Z A O13 1 
HETATM 2244 C  C5  . 84Z I 6 .   ? 16.592 3.780   14.759  1.00 5.48  ? 308 84Z A C5  1 
HETATM 2245 C  C6  . 84Z I 6 .   ? 15.726 3.982   15.826  1.00 4.54  ? 308 84Z A C6  1 
HETATM 2246 C  C1  . 84Z I 6 .   ? 15.206 5.288   16.003  1.00 5.24  ? 308 84Z A C1  1 
HETATM 2247 CL CL1 . 84Z I 6 .   ? 14.197 5.671   17.346  1.00 5.90  ? 308 84Z A CL1 1 
HETATM 2248 S  S7  . 84Z I 6 .   ? 15.168 2.627   16.816  1.00 3.99  ? 308 84Z A S7  1 
HETATM 2249 O  O8  . 84Z I 6 .   ? 13.723 2.663   16.690  1.00 4.05  ? 308 84Z A O8  1 
HETATM 2250 O  O9  . 84Z I 6 .   ? 15.714 2.858   18.125  1.00 4.12  ? 308 84Z A O9  1 
HETATM 2251 N  N10 . 84Z I 6 .   ? 15.771 1.302   16.147  1.00 3.37  ? 308 84Z A N10 1 
HETATM 2252 O  O   . HOH J 7 .   ? 17.530 19.960  21.566  1.00 18.80 ? 401 HOH A O   1 
HETATM 2253 O  O   . HOH J 7 .   ? -4.453 -8.766  17.718  1.00 19.83 ? 402 HOH A O   1 
HETATM 2254 O  O   . HOH J 7 .   ? 14.740 -9.755  36.532  1.00 27.86 ? 403 HOH A O   1 
HETATM 2255 O  O   . HOH J 7 .   ? 4.100  19.582  22.275  1.00 28.52 ? 404 HOH A O   1 
HETATM 2256 O  O   . HOH J 7 .   ? 24.123 -7.207  -6.423  1.00 27.03 ? 405 HOH A O   1 
HETATM 2257 O  O   . HOH J 7 .   ? -2.933 -12.356 19.769  1.00 29.61 ? 406 HOH A O   1 
HETATM 2258 O  O   . HOH J 7 .   ? 0.205  -5.172  -2.015  1.00 31.24 ? 407 HOH A O   1 
HETATM 2259 O  O   . HOH J 7 .   ? 24.433 4.345   8.092   1.00 36.56 ? 408 HOH A O   1 
HETATM 2260 O  O   . HOH J 7 .   ? 6.853  -6.887  -5.420  1.00 30.23 ? 409 HOH A O   1 
HETATM 2261 O  O   . HOH J 7 .   ? 13.571 -13.409 -6.626  1.00 44.60 ? 410 HOH A O   1 
HETATM 2262 O  O   . HOH J 7 .   ? 19.869 -2.264  15.831  1.00 4.58  ? 411 HOH A O   1 
HETATM 2263 O  O   . HOH J 7 .   ? 10.970 17.789  29.628  1.00 26.85 ? 412 HOH A O   1 
HETATM 2264 O  O   . HOH J 7 .   ? 14.788 -2.917  -6.438  1.00 18.86 ? 413 HOH A O   1 
HETATM 2265 O  O   . HOH J 7 .   ? 15.905 4.141   37.329  1.00 29.61 ? 414 HOH A O   1 
HETATM 2266 O  O   . HOH J 7 .   ? 0.686  15.758  28.748  1.00 33.66 ? 415 HOH A O   1 
HETATM 2267 O  O   . HOH J 7 .   ? 27.671 -3.743  3.533   1.00 41.46 ? 416 HOH A O   1 
HETATM 2268 O  O   . HOH J 7 .   ? 1.389  16.941  16.432  1.00 25.03 ? 417 HOH A O   1 
HETATM 2269 O  O   . HOH J 7 .   ? 5.074  5.530   35.363  1.00 25.75 ? 418 HOH A O   1 
HETATM 2270 O  O   . HOH J 7 .   ? 9.976  -13.208 34.243  1.00 21.52 ? 419 HOH A O   1 
HETATM 2271 O  O   . HOH J 7 .   ? 0.699  12.667  26.628  1.00 15.54 ? 420 HOH A O   1 
HETATM 2272 O  O   . HOH J 7 .   ? 8.982  12.532  5.922   1.00 33.61 ? 421 HOH A O   1 
HETATM 2273 O  O   . HOH J 7 .   ? 26.550 2.412   8.524   1.00 33.55 ? 422 HOH A O   1 
HETATM 2274 O  O   . HOH J 7 .   ? 4.643  -13.288 33.098  1.00 34.67 ? 423 HOH A O   1 
HETATM 2275 O  O   . HOH J 7 .   ? 13.490 10.050  29.488  1.00 26.63 ? 424 HOH A O   1 
HETATM 2276 O  O   . HOH J 7 .   ? -6.755 8.170   21.555  1.00 24.33 ? 425 HOH A O   1 
HETATM 2277 O  O   . HOH J 7 .   ? 8.721  14.246  29.258  1.00 20.66 ? 426 HOH A O   1 
HETATM 2278 O  O   . HOH J 7 .   ? -4.490 9.842   6.081   1.00 31.73 ? 427 HOH A O   1 
HETATM 2279 O  O   . HOH J 7 .   ? 23.640 -11.171 5.134   1.00 22.98 ? 428 HOH A O   1 
HETATM 2280 O  O   . HOH J 7 .   ? -2.398 -9.209  17.208  1.00 26.64 ? 429 HOH A O   1 
HETATM 2281 O  O   . HOH J 7 .   ? -4.516 -7.079  11.108  1.00 22.93 ? 430 HOH A O   1 
HETATM 2282 O  O   . HOH J 7 .   ? -0.903 -12.251 18.638  1.00 29.22 ? 431 HOH A O   1 
HETATM 2283 O  O   . HOH J 7 .   ? 12.398 -2.001  7.918   1.00 6.87  ? 432 HOH A O   1 
HETATM 2284 O  O   . HOH J 7 .   ? 11.890 7.829   29.020  1.00 14.51 ? 433 HOH A O   1 
HETATM 2285 O  O   . HOH J 7 .   ? 8.007  -20.285 8.708   1.00 18.00 ? 434 HOH A O   1 
HETATM 2286 O  O   . HOH J 7 .   ? -6.034 -11.052 20.277  1.00 38.53 ? 435 HOH A O   1 
HETATM 2287 O  O   . HOH J 7 .   ? -6.140 -3.452  27.520  1.00 30.27 ? 436 HOH A O   1 
HETATM 2288 O  O   . HOH J 7 .   ? 10.383 14.991  8.063   1.00 46.69 ? 437 HOH A O   1 
HETATM 2289 O  O   . HOH J 7 .   ? 32.185 -5.013  22.579  1.00 27.02 ? 438 HOH A O   1 
HETATM 2290 O  O   . HOH J 7 .   ? 12.543 -13.454 36.773  1.00 22.93 ? 439 HOH A O   1 
HETATM 2291 O  O   . HOH J 7 .   ? 9.190  10.675  -5.704  1.00 29.17 ? 440 HOH A O   1 
HETATM 2292 O  O   . HOH J 7 .   ? 4.228  -12.062 26.468  1.00 12.84 ? 441 HOH A O   1 
HETATM 2293 O  O   . HOH J 7 .   ? 21.574 -8.074  -5.428  1.00 29.09 ? 442 HOH A O   1 
HETATM 2294 O  O   . HOH J 7 .   ? -2.410 -11.333 27.304  1.00 35.10 ? 443 HOH A O   1 
HETATM 2295 O  O   . HOH J 7 .   ? -3.041 -1.236  29.387  1.00 31.16 ? 444 HOH A O   1 
HETATM 2296 O  O   . HOH J 7 .   ? 25.314 -0.543  28.999  1.00 20.49 ? 445 HOH A O   1 
HETATM 2297 O  O   . HOH J 7 .   ? -5.209 -5.631  30.401  1.00 35.56 ? 446 HOH A O   1 
HETATM 2298 O  O   . HOH J 7 .   ? 11.128 15.652  10.196  1.00 34.92 ? 447 HOH A O   1 
HETATM 2299 O  O   . HOH J 7 .   ? 20.114 -15.561 18.134  1.00 24.83 ? 448 HOH A O   1 
HETATM 2300 O  O   . HOH J 7 .   ? 5.133  -10.262 39.307  1.00 33.26 ? 449 HOH A O   1 
HETATM 2301 O  O   . HOH J 7 .   ? 15.392 3.579   10.649  1.00 18.11 ? 450 HOH A O   1 
HETATM 2302 O  O   . HOH J 7 .   ? 9.191  11.182  2.754   1.00 36.69 ? 451 HOH A O   1 
HETATM 2303 O  O   . HOH J 7 .   ? 0.384  10.131  30.012  1.00 29.27 ? 452 HOH A O   1 
HETATM 2304 O  O   . HOH J 7 .   ? 24.791 6.963   29.708  1.00 13.37 ? 453 HOH A O   1 
HETATM 2305 O  O   . HOH J 7 .   ? 6.749  -14.766 29.104  1.00 16.40 ? 454 HOH A O   1 
HETATM 2306 O  O   . HOH J 7 .   ? 10.431 10.579  25.483  1.00 5.99  ? 455 HOH A O   1 
HETATM 2307 O  O   . HOH J 7 .   ? 19.906 11.171  27.915  1.00 21.56 ? 456 HOH A O   1 
HETATM 2308 O  O   . HOH J 7 .   ? 25.309 -1.501  26.546  1.00 13.95 ? 457 HOH A O   1 
HETATM 2309 O  O   . HOH J 7 .   ? 4.327  -9.473  36.470  1.00 27.61 ? 458 HOH A O   1 
HETATM 2310 O  O   . HOH J 7 .   ? 14.954 19.499  27.620  1.00 30.21 ? 459 HOH A O   1 
HETATM 2311 O  O   . HOH J 7 .   ? 7.108  16.120  27.244  1.00 19.45 ? 460 HOH A O   1 
HETATM 2312 O  O   . HOH J 7 .   ? 21.224 3.039   34.537  1.00 23.88 ? 461 HOH A O   1 
HETATM 2313 O  O   . HOH J 7 .   ? -0.009 9.669   1.868   1.00 16.21 ? 462 HOH A O   1 
HETATM 2314 O  O   . HOH J 7 .   ? 16.265 -10.076 32.190  1.00 15.49 ? 463 HOH A O   1 
HETATM 2315 O  O   . HOH J 7 .   ? 9.895  -17.692 7.409   1.00 20.32 ? 464 HOH A O   1 
HETATM 2316 O  O   . HOH J 7 .   ? 2.444  -10.548 -3.528  1.00 19.43 ? 465 HOH A O   1 
HETATM 2317 O  O   . HOH J 7 .   ? 18.287 -17.634 6.324   1.00 20.42 ? 466 HOH A O   1 
HETATM 2318 O  O   . HOH J 7 .   ? 21.200 0.670   -4.729  1.00 12.91 ? 467 HOH A O   1 
HETATM 2319 O  O   . HOH J 7 .   ? -4.733 -13.400 8.187   1.00 29.43 ? 468 HOH A O   1 
HETATM 2320 O  O   . HOH J 7 .   ? 13.030 -13.564 11.441  1.00 6.21  ? 469 HOH A O   1 
HETATM 2321 O  O   . HOH J 7 .   ? 32.655 1.515   16.091  1.00 17.92 ? 470 HOH A O   1 
HETATM 2322 O  O   . HOH J 7 .   ? 20.562 16.020  16.163  1.00 19.87 ? 471 HOH A O   1 
HETATM 2323 O  O   . HOH J 7 .   ? 14.230 -13.054 31.657  1.00 22.35 ? 472 HOH A O   1 
HETATM 2324 O  O   . HOH J 7 .   ? -3.083 10.453  20.107  1.00 16.43 ? 473 HOH A O   1 
HETATM 2325 O  O   . HOH J 7 .   ? 22.085 16.601  24.403  1.00 30.45 ? 474 HOH A O   1 
HETATM 2326 O  O   . HOH J 7 .   ? 29.384 4.909   27.676  1.00 22.86 ? 475 HOH A O   1 
HETATM 2327 O  O   . HOH J 7 .   ? 26.003 -1.669  2.895   1.00 28.77 ? 476 HOH A O   1 
HETATM 2328 O  O   . HOH J 7 .   ? 7.149  12.184  27.850  1.00 12.25 ? 477 HOH A O   1 
HETATM 2329 O  O   . HOH J 7 .   ? 4.023  -6.478  20.438  1.00 5.15  ? 478 HOH A O   1 
HETATM 2330 O  O   . HOH J 7 .   ? -1.774 -4.048  2.703   1.00 17.55 ? 479 HOH A O   1 
HETATM 2331 O  O   . HOH J 7 .   ? 5.746  10.708  -2.321  1.00 41.75 ? 480 HOH A O   1 
HETATM 2332 O  O   . HOH J 7 .   ? 21.588 9.172   29.739  1.00 28.91 ? 481 HOH A O   1 
HETATM 2333 O  O   . HOH J 7 .   ? 30.659 -3.059  -7.800  1.00 32.16 ? 482 HOH A O   1 
HETATM 2334 O  O   . HOH J 7 .   ? -4.858 8.026   27.055  1.00 20.83 ? 483 HOH A O   1 
HETATM 2335 O  O   . HOH J 7 .   ? 5.627  -20.063 13.117  1.00 13.63 ? 484 HOH A O   1 
HETATM 2336 O  O   . HOH J 7 .   ? 2.437  -19.380 14.715  1.00 17.48 ? 485 HOH A O   1 
HETATM 2337 O  O   . HOH J 7 .   ? -4.101 11.396  12.850  1.00 35.89 ? 486 HOH A O   1 
HETATM 2338 O  O   . HOH J 7 .   ? 18.541 -6.847  29.184  1.00 6.80  ? 487 HOH A O   1 
HETATM 2339 O  O   . HOH J 7 .   ? 10.588 -16.373 17.199  1.00 7.70  ? 488 HOH A O   1 
HETATM 2340 O  O   . HOH J 7 .   ? -4.925 -4.276  13.145  1.00 34.39 ? 489 HOH A O   1 
HETATM 2341 O  O   . HOH J 7 .   ? 23.300 -12.930 -5.534  1.00 36.95 ? 490 HOH A O   1 
HETATM 2342 O  O   . HOH J 7 .   ? 3.083  -18.643 8.022   1.00 11.11 ? 491 HOH A O   1 
HETATM 2343 O  O   . HOH J 7 .   ? 17.092 5.276   9.421   1.00 22.97 ? 492 HOH A O   1 
HETATM 2344 O  O   . HOH J 7 .   ? 16.526 -11.673 18.128  1.00 5.52  ? 493 HOH A O   1 
HETATM 2345 O  O   . HOH J 7 .   ? 22.933 -14.035 9.398   1.00 20.27 ? 494 HOH A O   1 
HETATM 2346 O  O   . HOH J 7 .   ? 17.429 -11.202 -2.776  1.00 18.70 ? 495 HOH A O   1 
HETATM 2347 O  O   . HOH J 7 .   ? 19.147 -2.961  -7.151  1.00 24.06 ? 496 HOH A O   1 
HETATM 2348 O  O   . HOH J 7 .   ? 17.522 -9.295  20.977  1.00 6.13  ? 497 HOH A O   1 
HETATM 2349 O  O   . HOH J 7 .   ? -1.163 -16.481 13.603  1.00 17.75 ? 498 HOH A O   1 
HETATM 2350 O  O   . HOH J 7 .   ? 14.241 22.999  19.593  1.00 9.36  ? 499 HOH A O   1 
HETATM 2351 O  O   . HOH J 7 .   ? 16.810 -6.667  31.263  1.00 16.20 ? 500 HOH A O   1 
HETATM 2352 O  O   . HOH J 7 .   ? 17.786 -1.382  -8.975  1.00 31.54 ? 501 HOH A O   1 
HETATM 2353 O  O   . HOH J 7 .   ? 17.611 -11.384 25.244  1.00 7.23  ? 502 HOH A O   1 
HETATM 2354 O  O   . HOH J 7 .   ? -3.703 -5.865  8.989   1.00 17.64 ? 503 HOH A O   1 
HETATM 2355 O  O   . HOH J 7 .   ? 14.021 7.781   6.207   1.00 13.51 ? 504 HOH A O   1 
HETATM 2356 O  O   . HOH J 7 .   ? 29.638 -1.996  21.075  1.00 10.36 ? 505 HOH A O   1 
HETATM 2357 O  O   . HOH J 7 .   ? 1.413  -2.288  41.442  1.00 31.39 ? 506 HOH A O   1 
HETATM 2358 O  O   . HOH J 7 .   ? 23.557 -9.731  9.326   1.00 15.62 ? 507 HOH A O   1 
HETATM 2359 O  O   . HOH J 7 .   ? 12.462 2.329   -6.615  1.00 25.45 ? 508 HOH A O   1 
HETATM 2360 O  O   . HOH J 7 .   ? 23.724 -2.537  7.717   1.00 18.74 ? 509 HOH A O   1 
HETATM 2361 O  O   . HOH J 7 .   ? 3.037  12.546  11.272  1.00 14.99 ? 510 HOH A O   1 
HETATM 2362 O  O   . HOH J 7 .   ? 19.587 0.529   -12.855 1.00 39.73 ? 511 HOH A O   1 
HETATM 2363 O  O   . HOH J 7 .   ? 28.606 -6.273  -0.877  1.00 23.74 ? 512 HOH A O   1 
HETATM 2364 O  O   . HOH J 7 .   ? -2.382 -11.387 11.291  1.00 15.58 ? 513 HOH A O   1 
HETATM 2365 O  O   . HOH J 7 .   ? 27.592 1.268   -1.366  1.00 40.89 ? 514 HOH A O   1 
HETATM 2366 O  O   . HOH J 7 .   ? 6.083  8.061   32.656  1.00 26.36 ? 515 HOH A O   1 
HETATM 2367 O  O   . HOH J 7 .   ? 22.986 -5.428  -8.112  1.00 36.66 ? 516 HOH A O   1 
HETATM 2368 O  O   . HOH J 7 .   ? 13.987 -6.655  -7.177  1.00 31.30 ? 517 HOH A O   1 
HETATM 2369 O  O   . HOH J 7 .   ? 2.580  -2.010  -2.651  1.00 19.67 ? 518 HOH A O   1 
HETATM 2370 O  O   . HOH J 7 .   ? 19.924 5.904   -5.019  1.00 29.69 ? 519 HOH A O   1 
HETATM 2371 O  O   . HOH J 7 .   ? 20.558 12.719  23.252  1.00 12.36 ? 520 HOH A O   1 
HETATM 2372 O  O   . HOH J 7 .   ? 4.965  -10.451 24.485  1.00 8.68  ? 521 HOH A O   1 
HETATM 2373 O  O   . HOH J 7 .   ? 4.401  -14.420 -4.052  1.00 32.64 ? 522 HOH A O   1 
HETATM 2374 O  O   . HOH J 7 .   ? 13.676 -6.731  32.669  1.00 14.22 ? 523 HOH A O   1 
HETATM 2375 O  O   . HOH J 7 .   ? -0.553 -5.316  23.644  1.00 9.00  ? 524 HOH A O   1 
HETATM 2376 O  O   . HOH J 7 .   ? 14.398 -3.336  37.457  1.00 12.52 ? 525 HOH A O   1 
HETATM 2377 O  O   . HOH J 7 .   ? 26.449 8.978   20.149  1.00 12.78 ? 526 HOH A O   1 
HETATM 2378 O  O   . HOH J 7 .   ? 13.144 -17.202 30.618  1.00 23.92 ? 527 HOH A O   1 
HETATM 2379 O  O   . HOH J 7 .   ? 10.290 10.465  7.564   1.00 16.10 ? 528 HOH A O   1 
HETATM 2380 O  O   . HOH J 7 .   ? 22.336 -9.952  25.147  1.00 19.02 ? 529 HOH A O   1 
HETATM 2381 O  O   . HOH J 7 .   ? 18.524 -17.369 21.555  1.00 22.37 ? 530 HOH A O   1 
HETATM 2382 O  O   . HOH J 7 .   ? -0.753 7.497   4.746   1.00 14.89 ? 531 HOH A O   1 
HETATM 2383 O  O   . HOH J 7 .   ? 1.820  11.913  8.812   1.00 11.04 ? 532 HOH A O   1 
HETATM 2384 O  O   . HOH J 7 .   ? 10.383 -17.573 20.163  1.00 11.34 ? 533 HOH A O   1 
HETATM 2385 O  O   . HOH J 7 .   ? 17.216 -14.028 24.414  1.00 8.76  ? 534 HOH A O   1 
HETATM 2386 O  O   . HOH J 7 .   ? -1.178 5.600   -2.977  1.00 21.85 ? 535 HOH A O   1 
HETATM 2387 O  O   . HOH J 7 .   ? 25.976 -3.069  21.023  1.00 9.12  ? 536 HOH A O   1 
HETATM 2388 O  O   . HOH J 7 .   ? 3.443  8.189   38.558  1.00 29.11 ? 537 HOH A O   1 
HETATM 2389 O  O   . HOH J 7 .   ? 25.522 0.904   -5.347  1.00 27.51 ? 538 HOH A O   1 
HETATM 2390 O  O   . HOH J 7 .   ? -5.169 5.367   15.437  1.00 23.15 ? 539 HOH A O   1 
HETATM 2391 O  O   . HOH J 7 .   ? 27.104 -1.185  6.873   1.00 34.85 ? 540 HOH A O   1 
HETATM 2392 O  O   . HOH J 7 .   ? 36.810 4.717   20.753  1.00 24.17 ? 541 HOH A O   1 
HETATM 2393 O  O   . HOH J 7 .   ? 8.211  9.688   28.724  1.00 18.70 ? 542 HOH A O   1 
HETATM 2394 O  O   . HOH J 7 .   ? 4.407  -15.834 24.243  1.00 21.51 ? 543 HOH A O   1 
HETATM 2395 O  O   . HOH J 7 .   ? 7.557  -16.666 14.702  1.00 10.51 ? 544 HOH A O   1 
HETATM 2396 O  O   . HOH J 7 .   ? -2.210 -1.205  6.740   1.00 16.99 ? 545 HOH A O   1 
HETATM 2397 O  O   . HOH J 7 .   ? 7.239  21.976  15.258  1.00 14.08 ? 546 HOH A O   1 
HETATM 2398 O  O   . HOH J 7 .   ? 23.441 6.215   12.019  1.00 25.01 ? 547 HOH A O   1 
HETATM 2399 O  O   . HOH J 7 .   ? 6.306  11.330  31.580  1.00 36.66 ? 548 HOH A O   1 
HETATM 2400 O  O   . HOH J 7 .   ? 4.047  -16.144 20.199  1.00 16.73 ? 549 HOH A O   1 
HETATM 2401 O  O   . HOH J 7 .   ? 27.591 -3.882  6.752   1.00 25.48 ? 550 HOH A O   1 
HETATM 2402 O  O   . HOH J 7 .   ? 16.749 1.010   11.975  1.00 14.92 ? 551 HOH A O   1 
HETATM 2403 O  O   . HOH J 7 .   ? 21.226 -17.891 10.943  1.00 35.72 ? 552 HOH A O   1 
HETATM 2404 O  O   . HOH J 7 .   ? 36.428 -0.756  14.356  1.00 18.17 ? 553 HOH A O   1 
HETATM 2405 O  O   . HOH J 7 .   ? 1.099  17.776  18.920  1.00 28.61 ? 554 HOH A O   1 
HETATM 2406 O  O   . HOH J 7 .   ? 2.260  4.005   40.858  1.00 36.00 ? 555 HOH A O   1 
HETATM 2407 O  O   . HOH J 7 .   ? 18.087 19.896  14.316  1.00 34.98 ? 556 HOH A O   1 
HETATM 2408 O  O   . HOH J 7 .   ? -1.601 -7.683  25.370  1.00 16.05 ? 557 HOH A O   1 
HETATM 2409 O  O   . HOH J 7 .   ? 34.521 2.135   24.503  1.00 15.92 ? 558 HOH A O   1 
HETATM 2410 O  O   . HOH J 7 .   ? 8.045  -15.019 26.768  1.00 9.78  ? 559 HOH A O   1 
HETATM 2411 O  O   . HOH J 7 .   ? -3.421 -8.626  15.366  1.00 36.07 ? 560 HOH A O   1 
HETATM 2412 O  O   . HOH J 7 .   ? -1.881 -12.874 16.257  1.00 33.61 ? 561 HOH A O   1 
HETATM 2413 O  O   . HOH J 7 .   ? 1.723  22.357  5.190   1.00 23.98 ? 562 HOH A O   1 
HETATM 2414 O  O   . HOH J 7 .   ? 35.828 -5.169  7.760   1.00 34.67 ? 563 HOH A O   1 
HETATM 2415 O  O   . HOH J 7 .   ? 6.334  -16.758 18.767  1.00 9.54  ? 564 HOH A O   1 
HETATM 2416 O  O   . HOH J 7 .   ? 16.752 -3.084  11.205  1.00 18.40 ? 565 HOH A O   1 
HETATM 2417 O  O   . HOH J 7 .   ? 10.383 22.797  24.974  1.00 13.07 ? 566 HOH A O   1 
HETATM 2418 O  O   . HOH J 7 .   ? 16.321 -14.158 0.800   1.00 22.19 ? 567 HOH A O   1 
HETATM 2419 O  O   . HOH J 7 .   ? 18.415 -16.220 31.074  1.00 20.78 ? 568 HOH A O   1 
HETATM 2420 O  O   . HOH J 7 .   ? 12.720 -20.230 10.477  1.00 18.51 ? 569 HOH A O   1 
HETATM 2421 O  O   . HOH J 7 .   ? 4.778  17.757  23.636  1.00 15.68 ? 570 HOH A O   1 
HETATM 2422 O  O   . HOH J 7 .   ? 28.824 0.758   -5.684  1.00 26.94 ? 571 HOH A O   1 
HETATM 2423 O  O   . HOH J 7 .   ? -2.892 -16.037 6.450   1.00 29.79 ? 572 HOH A O   1 
HETATM 2424 O  O   . HOH J 7 .   ? 22.629 -4.273  34.476  1.00 18.98 ? 573 HOH A O   1 
HETATM 2425 O  O   . HOH J 7 .   ? -2.156 1.544   34.504  1.00 25.13 ? 574 HOH A O   1 
HETATM 2426 O  O   . HOH J 7 .   ? 32.341 3.199   25.887  1.00 21.37 ? 575 HOH A O   1 
HETATM 2427 O  O   . HOH J 7 .   ? 25.322 -4.808  7.801   1.00 19.21 ? 576 HOH A O   1 
HETATM 2428 O  O   . HOH J 7 .   ? 22.321 10.708  24.166  1.00 13.59 ? 577 HOH A O   1 
HETATM 2429 O  O   . HOH J 7 .   ? 16.248 2.402   9.835   1.00 30.00 ? 578 HOH A O   1 
HETATM 2430 O  O   . HOH J 7 .   ? 34.113 -3.923  24.480  1.00 19.26 ? 579 HOH A O   1 
HETATM 2431 O  O   . HOH J 7 .   ? 23.787 3.111   -2.305  1.00 32.58 ? 580 HOH A O   1 
HETATM 2432 O  O   . HOH J 7 .   ? 32.272 -1.976  7.648   1.00 29.65 ? 581 HOH A O   1 
HETATM 2433 O  O   . HOH J 7 .   ? -3.478 13.820  6.184   1.00 24.73 ? 582 HOH A O   1 
HETATM 2434 O  O   . HOH J 7 .   ? 13.835 -15.099 1.605   1.00 16.97 ? 583 HOH A O   1 
HETATM 2435 O  O   . HOH J 7 .   ? 9.981  3.139   33.514  1.00 20.72 ? 584 HOH A O   1 
HETATM 2436 O  O   . HOH J 7 .   ? 12.422 -17.969 26.797  1.00 18.17 ? 585 HOH A O   1 
HETATM 2437 O  O   . HOH J 7 .   ? 8.239  5.307   -6.980  1.00 23.81 ? 586 HOH A O   1 
HETATM 2438 O  O   . HOH J 7 .   ? -2.780 1.076   3.942   1.00 19.22 ? 587 HOH A O   1 
HETATM 2439 O  O   . HOH J 7 .   ? -1.923 -9.890  14.089  1.00 17.90 ? 588 HOH A O   1 
HETATM 2440 O  O   . HOH J 7 .   ? 19.788 -4.214  36.554  1.00 22.66 ? 589 HOH A O   1 
HETATM 2441 O  O   . HOH J 7 .   ? 8.141  -7.222  -3.222  1.00 24.50 ? 590 HOH A O   1 
HETATM 2442 O  O   . HOH J 7 .   ? 22.519 -14.293 -1.505  1.00 36.80 ? 591 HOH A O   1 
HETATM 2443 O  O   . HOH J 7 .   ? 7.660  -14.901 -0.051  1.00 35.84 ? 592 HOH A O   1 
HETATM 2444 O  O   . HOH J 7 .   ? 4.727  -8.038  32.985  1.00 13.63 ? 593 HOH A O   1 
HETATM 2445 O  O   . HOH J 7 .   ? 2.169  5.330   -3.457  1.00 31.38 ? 594 HOH A O   1 
HETATM 2446 O  O   . HOH J 7 .   ? -2.961 1.146   26.537  1.00 14.23 ? 595 HOH A O   1 
HETATM 2447 O  O   . HOH J 7 .   ? 27.848 -1.772  29.935  1.00 38.41 ? 596 HOH A O   1 
HETATM 2448 O  O   . HOH J 7 .   ? 7.661  1.017   -6.252  1.00 34.03 ? 597 HOH A O   1 
HETATM 2449 O  O   . HOH J 7 .   ? -3.598 6.578   8.150   1.00 28.77 ? 598 HOH A O   1 
HETATM 2450 O  O   . HOH J 7 .   ? 22.259 0.376   29.500  1.00 9.83  ? 599 HOH A O   1 
HETATM 2451 O  O   . HOH J 7 .   ? 14.656 -17.890 23.875  1.00 18.46 ? 600 HOH A O   1 
HETATM 2452 O  O   . HOH J 7 .   ? 20.421 -6.628  32.591  1.00 19.05 ? 601 HOH A O   1 
HETATM 2453 O  O   . HOH J 7 .   ? 12.637 -13.039 33.434  1.00 47.39 ? 602 HOH A O   1 
HETATM 2454 O  O   . HOH J 7 .   ? 22.916 -2.425  -12.424 1.00 28.74 ? 603 HOH A O   1 
HETATM 2455 O  O   . HOH J 7 .   ? 9.074  4.648   30.951  1.00 14.51 ? 604 HOH A O   1 
HETATM 2456 O  O   . HOH J 7 .   ? 34.972 7.532   18.932  1.00 28.30 ? 605 HOH A O   1 
HETATM 2457 O  O   . HOH J 7 .   ? 3.668  20.355  4.214   1.00 34.37 ? 606 HOH A O   1 
HETATM 2458 O  O   . HOH J 7 .   ? 11.741 -8.247  -1.284  1.00 22.09 ? 607 HOH A O   1 
HETATM 2459 O  O   . HOH J 7 .   ? -4.444 1.141   35.019  1.00 31.29 ? 608 HOH A O   1 
HETATM 2460 O  O   . HOH J 7 .   ? 14.633 -17.498 5.783   1.00 22.60 ? 609 HOH A O   1 
HETATM 2461 O  O   . HOH J 7 .   ? 11.989 -3.868  36.014  1.00 13.00 ? 610 HOH A O   1 
HETATM 2462 O  O   . HOH J 7 .   ? 18.951 -10.451 22.950  1.00 6.23  ? 611 HOH A O   1 
HETATM 2463 O  O   . HOH J 7 .   ? 31.213 -11.538 9.389   1.00 35.06 ? 612 HOH A O   1 
HETATM 2464 O  O   . HOH J 7 .   ? 0.118  -19.046 1.827   1.00 30.00 ? 613 HOH A O   1 
HETATM 2465 O  O   . HOH J 7 .   ? 25.949 -11.429 -5.609  1.00 14.30 ? 614 HOH A O   1 
HETATM 2466 O  O   . HOH J 7 .   ? -3.256 1.756   1.305   1.00 25.01 ? 615 HOH A O   1 
HETATM 2467 O  O   . HOH J 7 .   ? -0.505 2.443   0.221   1.00 37.26 ? 616 HOH A O   1 
HETATM 2468 O  O   . HOH J 7 .   ? 21.529 2.285   -6.867  1.00 23.87 ? 617 HOH A O   1 
HETATM 2469 O  O   . HOH J 7 .   ? 11.551 -6.073  34.198  1.00 16.75 ? 618 HOH A O   1 
HETATM 2470 O  O   . HOH J 7 .   ? 15.651 4.974   -5.883  1.00 37.44 ? 619 HOH A O   1 
HETATM 2471 O  O   . HOH J 7 .   ? 6.078  -18.126 23.314  1.00 20.24 ? 620 HOH A O   1 
HETATM 2472 O  O   . HOH J 7 .   ? 12.834 -17.491 21.772  1.00 10.67 ? 621 HOH A O   1 
HETATM 2473 O  O   . HOH J 7 .   ? 15.034 17.417  11.902  1.00 25.23 ? 622 HOH A O   1 
HETATM 2474 O  O   . HOH J 7 .   ? 18.600 -1.178  11.536  1.00 11.18 ? 623 HOH A O   1 
HETATM 2475 O  O   . HOH J 7 .   ? 11.121 17.012  12.137  1.00 22.74 ? 624 HOH A O   1 
HETATM 2476 O  O   . HOH J 7 .   ? 14.024 3.481   35.211  1.00 21.68 ? 625 HOH A O   1 
HETATM 2477 O  O   . HOH J 7 .   ? 28.668 7.955   21.664  1.00 12.17 ? 626 HOH A O   1 
HETATM 2478 O  O   . HOH J 7 .   ? 15.916 -11.689 34.415  1.00 33.78 ? 627 HOH A O   1 
HETATM 2479 O  O   . HOH J 7 .   ? 27.235 -9.425  15.532  1.00 25.12 ? 628 HOH A O   1 
HETATM 2480 O  O   . HOH J 7 .   ? 4.097  0.980   40.133  1.00 28.89 ? 629 HOH A O   1 
HETATM 2481 O  O   . HOH J 7 .   ? 14.428 8.400   9.853   1.00 16.66 ? 630 HOH A O   1 
HETATM 2482 O  O   . HOH J 7 .   ? -0.688 21.446  12.099  1.00 26.68 ? 631 HOH A O   1 
HETATM 2483 O  O   . HOH J 7 .   ? 26.255 -5.449  22.511  1.00 26.83 ? 632 HOH A O   1 
HETATM 2484 O  O   . HOH J 7 .   ? 34.155 -2.118  13.467  1.00 32.43 ? 633 HOH A O   1 
HETATM 2485 O  O   . HOH J 7 .   ? 23.824 -13.013 1.023   1.00 48.11 ? 634 HOH A O   1 
HETATM 2486 O  O   . HOH J 7 .   ? 20.781 -12.472 22.325  1.00 17.59 ? 635 HOH A O   1 
HETATM 2487 O  O   . HOH J 7 .   ? 20.860 -18.736 14.839  1.00 34.28 ? 636 HOH A O   1 
HETATM 2488 O  O   . HOH J 7 .   ? 20.649 -14.319 27.394  1.00 41.92 ? 637 HOH A O   1 
HETATM 2489 O  O   . HOH J 7 .   ? 30.963 2.207   14.237  1.00 38.23 ? 638 HOH A O   1 
HETATM 2490 O  O   . HOH J 7 .   ? 1.952  19.741  17.893  1.00 42.24 ? 639 HOH A O   1 
HETATM 2491 O  O   . HOH J 7 .   ? 13.719 -6.965  -2.391  1.00 26.12 ? 640 HOH A O   1 
HETATM 2492 O  O   . HOH J 7 .   ? 14.362 16.782  29.166  1.00 31.32 ? 641 HOH A O   1 
HETATM 2493 O  O   . HOH J 7 .   ? 31.084 -0.825  13.770  1.00 26.34 ? 642 HOH A O   1 
HETATM 2494 O  O   . HOH J 7 .   ? -2.900 1.674   31.765  1.00 32.57 ? 643 HOH A O   1 
HETATM 2495 O  O   . HOH J 7 .   ? 30.366 3.651   12.132  1.00 30.82 ? 644 HOH A O   1 
HETATM 2496 O  O   . HOH J 7 .   ? -3.759 -7.872  1.977   1.00 26.44 ? 645 HOH A O   1 
HETATM 2497 O  O   . HOH J 7 .   ? 8.219  20.781  12.353  1.00 27.03 ? 646 HOH A O   1 
HETATM 2498 O  O   . HOH J 7 .   ? 19.555 13.295  25.739  1.00 20.60 ? 647 HOH A O   1 
HETATM 2499 O  O   . HOH J 7 .   ? 29.656 -7.058  -7.669  1.00 37.24 ? 648 HOH A O   1 
HETATM 2500 O  O   . HOH J 7 .   ? 28.523 -9.087  4.374   1.00 28.92 ? 649 HOH A O   1 
HETATM 2501 O  O   . HOH J 7 .   ? 2.742  -7.055  34.710  1.00 34.89 ? 650 HOH A O   1 
HETATM 2502 O  O   . HOH J 7 .   ? 20.091 20.697  22.114  1.00 35.90 ? 651 HOH A O   1 
HETATM 2503 O  O   . HOH J 7 .   ? -4.403 12.942  19.459  1.00 27.24 ? 652 HOH A O   1 
HETATM 2504 O  O   . HOH J 7 .   ? 29.739 -2.795  23.760  1.00 19.50 ? 653 HOH A O   1 
HETATM 2505 O  O   . HOH J 7 .   ? 20.070 -1.801  39.510  1.00 36.81 ? 654 HOH A O   1 
HETATM 2506 O  O   . HOH J 7 .   ? 10.678 7.676   -4.385  1.00 27.16 ? 655 HOH A O   1 
HETATM 2507 O  O   . HOH J 7 .   ? 8.112  -15.343 17.029  1.00 8.08  ? 656 HOH A O   1 
HETATM 2508 O  O   . HOH J 7 .   ? 15.342 -10.782 -5.084  1.00 30.06 ? 657 HOH A O   1 
HETATM 2509 O  O   . HOH J 7 .   ? 31.210 -6.893  8.292   1.00 18.85 ? 658 HOH A O   1 
HETATM 2510 O  O   . HOH J 7 .   ? 20.240 5.140   8.234   1.00 30.00 ? 659 HOH A O   1 
HETATM 2511 O  O   . HOH J 7 .   ? 3.888  -12.249 37.620  1.00 27.88 ? 660 HOH A O   1 
HETATM 2512 O  O   . HOH J 7 .   ? -3.579 17.986  5.172   1.00 32.63 ? 661 HOH A O   1 
HETATM 2513 O  O   . HOH J 7 .   ? 32.948 -4.723  7.799   1.00 21.89 ? 662 HOH A O   1 
HETATM 2514 O  O   . HOH J 7 .   ? -5.628 -8.231  14.685  1.00 30.21 ? 663 HOH A O   1 
HETATM 2515 O  O   . HOH J 7 .   ? 25.304 -9.288  7.047   1.00 32.61 ? 664 HOH A O   1 
HETATM 2516 O  O   . HOH J 7 .   ? 12.559 -2.279  -9.396  1.00 37.01 ? 665 HOH A O   1 
HETATM 2517 O  O   . HOH J 7 .   ? 4.772  18.531  26.591  1.00 26.63 ? 666 HOH A O   1 
HETATM 2518 O  O   . HOH J 7 .   ? 26.550 -9.249  19.264  1.00 37.23 ? 667 HOH A O   1 
HETATM 2519 O  O   . HOH J 7 .   ? 35.594 2.082   15.017  1.00 34.88 ? 668 HOH A O   1 
HETATM 2520 O  O   . HOH J 7 .   ? 35.343 4.321   23.306  1.00 31.42 ? 669 HOH A O   1 
HETATM 2521 O  O   . HOH J 7 .   ? 28.422 -1.809  -10.578 1.00 24.13 ? 670 HOH A O   1 
HETATM 2522 O  O   . HOH J 7 .   ? 19.530 -11.294 27.211  1.00 22.53 ? 671 HOH A O   1 
HETATM 2523 O  O   . HOH J 7 .   ? 21.744 -10.899 -6.819  1.00 30.16 ? 672 HOH A O   1 
HETATM 2524 O  O   . HOH J 7 .   ? -0.191 23.543  6.692   1.00 19.97 ? 673 HOH A O   1 
HETATM 2525 O  O   . HOH J 7 .   ? 25.369 -9.547  -7.397  1.00 25.25 ? 674 HOH A O   1 
HETATM 2526 O  O   . HOH J 7 .   ? -5.372 -5.773  2.219   1.00 31.31 ? 675 HOH A O   1 
HETATM 2527 O  O   . HOH J 7 .   ? 3.341  1.671   -3.741  1.00 39.56 ? 676 HOH A O   1 
HETATM 2528 O  O   . HOH J 7 .   ? 4.399  -12.339 29.155  1.00 38.84 ? 677 HOH A O   1 
HETATM 2529 O  O   . HOH J 7 .   ? 16.565 -4.113  -8.098  1.00 33.45 ? 678 HOH A O   1 
HETATM 2530 O  O   . HOH J 7 .   ? 23.566 -0.756  37.384  1.00 40.05 ? 679 HOH A O   1 
HETATM 2531 O  O   . HOH J 7 .   ? 16.096 22.469  21.579  1.00 17.05 ? 680 HOH A O   1 
HETATM 2532 O  O   . HOH J 7 .   ? 8.553  8.499   31.267  1.00 26.61 ? 681 HOH A O   1 
HETATM 2533 O  O   . HOH J 7 .   ? 5.591  -14.431 25.884  1.00 28.28 ? 682 HOH A O   1 
HETATM 2534 O  O   . HOH J 7 .   ? -5.762 -4.422  4.781   1.00 32.02 ? 683 HOH A O   1 
HETATM 2535 O  O   . HOH J 7 .   ? -4.138 10.572  26.037  1.00 30.20 ? 684 HOH A O   1 
HETATM 2536 O  O   . HOH J 7 .   ? 27.923 -8.727  -7.931  1.00 25.40 ? 685 HOH A O   1 
HETATM 2537 O  O   . HOH J 7 .   ? 25.896 -11.370 3.184   1.00 27.06 ? 686 HOH A O   1 
HETATM 2538 O  O   . HOH J 7 .   ? 27.452 -3.278  27.336  1.00 32.55 ? 687 HOH A O   1 
HETATM 2539 O  O   . HOH J 7 .   ? 19.095 -15.553 25.527  1.00 23.44 ? 688 HOH A O   1 
HETATM 2540 O  O   . HOH J 7 .   ? 10.538 6.766   30.903  1.00 17.82 ? 689 HOH A O   1 
HETATM 2541 O  O   . HOH J 7 .   ? -8.664 1.354   11.902  1.00 32.73 ? 690 HOH A O   1 
HETATM 2542 O  O   . HOH J 7 .   ? 36.290 -2.125  25.077  1.00 17.04 ? 691 HOH A O   1 
HETATM 2543 O  O   . HOH J 7 .   ? 17.672 16.951  11.443  1.00 31.06 ? 692 HOH A O   1 
HETATM 2544 O  O   . HOH J 7 .   ? -0.860 -19.782 17.286  1.00 34.27 ? 693 HOH A O   1 
HETATM 2545 O  O   . HOH J 7 .   ? 16.151 -7.738  33.615  1.00 26.33 ? 694 HOH A O   1 
HETATM 2546 O  O   . HOH J 7 .   ? 24.070 -12.040 8.238   1.00 22.84 ? 695 HOH A O   1 
HETATM 2547 O  O   . HOH J 7 .   ? 22.739 -7.898  31.022  1.00 33.99 ? 696 HOH A O   1 
HETATM 2548 O  O   . HOH J 7 .   ? 25.198 -9.144  17.519  1.00 32.67 ? 697 HOH A O   1 
HETATM 2549 O  O   . HOH J 7 .   ? 19.853 -15.794 -1.816  1.00 26.65 ? 698 HOH A O   1 
HETATM 2550 O  O   . HOH J 7 .   ? 22.780 14.380  22.617  1.00 22.16 ? 699 HOH A O   1 
HETATM 2551 O  O   . HOH J 7 .   ? 18.915 -9.922  31.659  1.00 24.86 ? 700 HOH A O   1 
HETATM 2552 O  O   . HOH J 7 .   ? 4.321  21.559  23.394  1.00 32.47 ? 701 HOH A O   1 
HETATM 2553 O  O   . HOH J 7 .   ? 10.135 -9.330  -2.889  1.00 36.01 ? 702 HOH A O   1 
HETATM 2554 O  O   . HOH J 7 .   ? 9.596  2.771   -7.672  1.00 30.03 ? 703 HOH A O   1 
HETATM 2555 O  O   . HOH J 7 .   ? 24.474 -11.864 12.310  1.00 31.49 ? 704 HOH A O   1 
HETATM 2556 O  O   . HOH J 7 .   ? 36.455 0.645   26.043  1.00 19.82 ? 705 HOH A O   1 
HETATM 2557 O  O   . HOH J 7 .   ? 19.056 -15.594 4.996   1.00 35.88 ? 706 HOH A O   1 
HETATM 2558 O  O   . HOH J 7 .   ? 22.315 -15.855 7.152   1.00 27.40 ? 707 HOH A O   1 
HETATM 2559 O  O   . HOH J 7 .   ? 12.763 9.523   7.866   1.00 19.72 ? 708 HOH A O   1 
HETATM 2560 O  O   . HOH J 7 .   ? 11.749 5.030   34.802  1.00 17.55 ? 709 HOH A O   1 
HETATM 2561 O  O   . HOH J 7 .   ? -3.096 -5.403  0.125   1.00 35.73 ? 710 HOH A O   1 
HETATM 2562 O  O   . HOH J 7 .   ? 0.611  -3.115  -3.570  1.00 28.98 ? 711 HOH A O   1 
HETATM 2563 O  O   . HOH J 7 .   ? 13.810 -8.455  -4.388  1.00 29.38 ? 712 HOH A O   1 
HETATM 2564 O  O   . HOH J 7 .   ? 8.417  13.024  -5.083  1.00 25.31 ? 713 HOH A O   1 
HETATM 2565 O  O   . HOH J 7 .   ? 14.986 -19.036 26.377  1.00 26.08 ? 714 HOH A O   1 
HETATM 2566 O  O   . HOH J 7 .   ? 3.248  -19.439 17.509  1.00 18.80 ? 715 HOH A O   1 
HETATM 2567 O  O   . HOH J 7 .   ? 8.248  4.828   37.096  1.00 41.98 ? 716 HOH A O   1 
HETATM 2568 O  O   . HOH J 7 .   ? 17.518 1.655   -11.907 1.00 27.77 ? 717 HOH A O   1 
HETATM 2569 O  O   . HOH J 7 .   ? 6.292  7.579   36.920  1.00 26.25 ? 718 HOH A O   1 
HETATM 2570 O  O   . HOH J 7 .   ? 23.059 -12.357 20.518  1.00 27.95 ? 719 HOH A O   1 
HETATM 2571 O  O   . HOH J 7 .   ? 17.158 -13.911 -2.162  1.00 35.32 ? 720 HOH A O   1 
HETATM 2572 O  O   . HOH J 7 .   ? 22.662 11.645  26.657  1.00 27.00 ? 721 HOH A O   1 
HETATM 2573 O  O   . HOH J 7 .   ? 8.942  15.206  4.866   1.00 32.84 ? 722 HOH A O   1 
HETATM 2574 O  O   . HOH J 7 .   ? -4.733 -1.603  6.227   1.00 34.60 ? 723 HOH A O   1 
HETATM 2575 O  O   . HOH J 7 .   ? 4.741  9.319   36.570  1.00 19.64 ? 724 HOH A O   1 
HETATM 2576 O  O   . HOH J 7 .   ? 19.821 -9.266  29.081  1.00 12.60 ? 725 HOH A O   1 
HETATM 2577 O  O   . HOH J 7 .   ? -0.310 -18.901 14.584  1.00 28.87 ? 726 HOH A O   1 
HETATM 2578 O  O   . HOH J 7 .   ? 6.076  -19.288 17.683  1.00 12.77 ? 727 HOH A O   1 
HETATM 2579 O  O   . HOH J 7 .   ? 3.162  -10.150 31.525  1.00 23.01 ? 728 HOH A O   1 
HETATM 2580 O  O   . HOH J 7 .   ? 33.408 5.924   27.362  1.00 29.77 ? 729 HOH A O   1 
HETATM 2581 O  O   . HOH J 7 .   ? 9.384  12.771  0.669   1.00 31.74 ? 730 HOH A O   1 
HETATM 2582 O  O   . HOH J 7 .   ? 6.203  10.234  34.628  1.00 38.41 ? 731 HOH A O   1 
HETATM 2583 O  O   . HOH J 7 .   ? 24.478 4.438   -0.134  1.00 27.61 ? 732 HOH A O   1 
HETATM 2584 O  O   . HOH J 7 .   ? 27.561 7.208   28.801  1.00 31.85 ? 733 HOH A O   1 
HETATM 2585 O  O   . HOH J 7 .   ? 20.359 -5.227  -7.702  1.00 39.42 ? 734 HOH A O   1 
HETATM 2586 O  O   . HOH J 7 .   ? 27.494 10.406  18.126  1.00 32.49 ? 735 HOH A O   1 
HETATM 2587 O  O   . HOH J 7 .   ? 26.732 -12.501 8.951   1.00 29.12 ? 736 HOH A O   1 
HETATM 2588 O  O   . HOH J 7 .   ? 14.058 14.942  10.557  1.00 26.52 ? 737 HOH A O   1 
HETATM 2589 O  O   . HOH J 7 .   ? 15.338 -16.409 3.495   1.00 25.65 ? 738 HOH A O   1 
HETATM 2590 O  O   . HOH J 7 .   ? 20.599 13.909  14.312  1.00 27.45 ? 739 HOH A O   1 
HETATM 2591 O  O   . HOH J 7 .   ? 6.969  5.556   33.141  1.00 22.08 ? 740 HOH A O   1 
HETATM 2592 O  O   . HOH J 7 .   ? 8.133  -17.722 26.220  1.00 19.65 ? 741 HOH A O   1 
HETATM 2593 O  O   . HOH J 7 .   ? 35.884 -5.601  26.099  1.00 35.01 ? 742 HOH A O   1 
HETATM 2594 O  O   . HOH J 7 .   ? 26.468 10.993  21.705  1.00 26.51 ? 743 HOH A O   1 
HETATM 2595 O  O   . HOH J 7 .   ? 24.038 10.441  13.174  1.00 43.69 ? 744 HOH A O   1 
HETATM 2596 O  O   . HOH J 7 .   ? 35.205 0.439   28.423  1.00 27.32 ? 745 HOH A O   1 
HETATM 2597 O  O   . HOH J 7 .   ? 24.730 11.788  23.703  1.00 23.51 ? 746 HOH A O   1 
HETATM 2598 O  O   . HOH J 7 .   ? 12.264 11.025  -6.557  1.00 31.75 ? 747 HOH A O   1 
HETATM 2599 O  O   . HOH J 7 .   ? 10.640 5.168   37.471  1.00 30.52 ? 748 HOH A O   1 
HETATM 2600 O  O   . HOH J 7 .   ? 35.271 6.787   25.004  1.00 36.34 ? 749 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 1   ? 0.2289 0.3612 0.2809 0.0080  0.0187  0.0512  3   HIS A N   
2    C  CA  . HIS A 1   ? 0.1884 0.4389 0.4105 0.0929  0.0545  0.1787  3   HIS A CA  
3    C  C   . HIS A 1   ? 0.1891 0.4776 0.1805 -0.0283 -0.0229 0.0922  3   HIS A C   
4    O  O   . HIS A 1   ? 0.5410 0.5191 0.2506 -0.0816 -0.0652 -0.0964 3   HIS A O   
5    C  CB  . HIS A 1   ? 0.3840 0.3271 0.2781 -0.0168 -0.1302 0.1026  3   HIS A CB  
6    C  CG  . HIS A 1   ? 0.3158 0.4109 0.2879 -0.1685 -0.0613 0.1226  3   HIS A CG  
7    N  ND1 . HIS A 1   ? 0.3252 0.4461 0.2891 -0.1348 -0.0075 0.1042  3   HIS A ND1 
8    C  CD2 . HIS A 1   ? 0.4008 0.4466 0.2726 -0.0475 -0.1106 -0.0247 3   HIS A CD2 
9    C  CE1 . HIS A 1   ? 0.3353 0.4762 0.3962 -0.2134 -0.0331 0.1040  3   HIS A CE1 
10   N  NE2 . HIS A 1   ? 0.3459 0.4805 0.4567 -0.0766 -0.1163 0.0750  3   HIS A NE2 
11   N  N   . HIS A 2   ? 0.1421 0.3855 0.2387 -0.0029 0.0217  0.1135  4   HIS A N   
12   C  CA  . HIS A 2   ? 0.1460 0.3574 0.2657 -0.0380 0.0886  0.1488  4   HIS A CA  
13   C  C   . HIS A 2   ? 0.1564 0.2056 0.2045 -0.0299 0.0930  0.0245  4   HIS A C   
14   O  O   . HIS A 2   ? 0.2005 0.2060 0.2509 -0.0160 0.0679  -0.0077 4   HIS A O   
15   C  CB  . HIS A 2   ? 0.1823 0.5204 0.3924 -0.0483 0.0108  0.3221  4   HIS A CB  
16   C  CG  . HIS A 2   ? 0.6010 0.5694 0.4138 -0.1243 -0.0085 0.2992  4   HIS A CG  
17   N  ND1 . HIS A 2   ? 0.7016 0.4215 0.9798 0.1350  0.0546  0.3693  4   HIS A ND1 
18   C  CD2 . HIS A 2   ? 1.0383 0.4187 0.7148 -0.3282 0.2474  0.2967  4   HIS A CD2 
19   C  CE1 . HIS A 2   ? 0.9643 0.7411 1.2142 0.2909  -0.0840 0.1459  4   HIS A CE1 
20   N  NE2 . HIS A 2   ? 1.4991 0.5994 0.9835 -0.1051 0.0221  0.2894  4   HIS A NE2 
21   N  N   . TRP A 3   ? 0.0994 0.1931 0.1891 -0.0264 0.0537  0.0176  5   TRP A N   
22   C  CA  . TRP A 3   ? 0.0661 0.1446 0.1579 -0.0344 0.0374  -0.0175 5   TRP A CA  
23   C  C   . TRP A 3   ? 0.0854 0.1205 0.1625 -0.0268 0.0240  -0.0048 5   TRP A C   
24   O  O   . TRP A 3   ? 0.1568 0.1428 0.1442 -0.0170 0.0441  -0.0015 5   TRP A O   
25   C  CB  . TRP A 3   ? 0.0926 0.1460 0.1702 -0.0285 0.0378  -0.0436 5   TRP A CB  
26   C  CG  . TRP A 3   ? 0.1280 0.1155 0.1161 -0.0566 0.0256  -0.0079 5   TRP A CG  
27   C  CD1 . TRP A 3   ? 0.1381 0.1360 0.1360 -0.0375 0.0249  0.0346  5   TRP A CD1 
28   C  CD2 . TRP A 3   ? 0.0855 0.1084 0.0844 -0.0009 0.0204  -0.0215 5   TRP A CD2 
29   N  NE1 . TRP A 3   ? 0.1514 0.1338 0.1073 -0.0245 0.0184  0.0134  5   TRP A NE1 
30   C  CE2 . TRP A 3   ? 0.1409 0.1084 0.1056 0.0017  -0.0004 -0.0089 5   TRP A CE2 
31   C  CE3 . TRP A 3   ? 0.1023 0.1424 0.0689 -0.0361 0.0209  -0.0171 5   TRP A CE3 
32   C  CZ2 . TRP A 3   ? 0.1380 0.1380 0.0770 -0.0156 0.0187  -0.0115 5   TRP A CZ2 
33   C  CZ3 . TRP A 3   ? 0.1022 0.1496 0.0962 -0.0092 0.0337  -0.0574 5   TRP A CZ3 
34   C  CH2 . TRP A 3   ? 0.1241 0.1478 0.0650 -0.0212 0.0074  -0.0366 5   TRP A CH2 
35   N  N   . GLY A 4   ? 0.1064 0.1044 0.1429 -0.0320 0.0618  -0.0354 6   GLY A N   
36   C  CA  . GLY A 4   ? 0.1119 0.0829 0.1585 -0.0067 0.0135  -0.0118 6   GLY A CA  
37   C  C   . GLY A 4   ? 0.0925 0.0928 0.1819 0.0206  0.0728  -0.0185 6   GLY A C   
38   O  O   . GLY A 4   ? 0.1146 0.1220 0.1581 0.0138  0.0684  -0.0029 6   GLY A O   
39   N  N   . TYR A 5   ? 0.1581 0.0865 0.2311 -0.0075 0.1077  -0.0330 7   TYR A N   
40   C  CA  . TYR A 5   ? 0.1066 0.0750 0.3240 0.0155  0.1331  -0.0111 7   TYR A CA  
41   C  C   . TYR A 5   ? 0.1611 0.1542 0.6052 0.0714  0.1033  -0.1371 7   TYR A C   
42   O  O   . TYR A 5   ? 0.2036 0.1916 0.3564 0.0274  0.0286  -0.0363 7   TYR A O   
43   C  CB  . TYR A 5   ? 0.1298 0.0926 0.2730 0.0097  0.1049  -0.0451 7   TYR A CB  
44   C  CG  . TYR A 5   ? 0.0933 0.0506 0.1398 -0.0170 0.0544  -0.0278 7   TYR A CG  
45   C  CD1 . TYR A 5   ? 0.0592 0.0856 0.1413 -0.0141 0.0359  -0.0358 7   TYR A CD1 
46   C  CD2 . TYR A 5   ? 0.1543 0.0580 0.1482 -0.0219 0.0440  -0.0196 7   TYR A CD2 
47   C  CE1 . TYR A 5   ? 0.0732 0.0635 0.0996 -0.0046 0.0212  -0.0091 7   TYR A CE1 
48   C  CE2 . TYR A 5   ? 0.0971 0.0906 0.0741 -0.0289 0.0185  -0.0215 7   TYR A CE2 
49   C  CZ  . TYR A 5   ? 0.0652 0.0748 0.0829 -0.0018 0.0317  0.0000  7   TYR A CZ  
50   O  OH  . TYR A 5   ? 0.0732 0.0759 0.0741 0.0100  0.0052  -0.0020 7   TYR A OH  
51   N  N   . GLY A 6   ? 0.2283 0.2261 0.7429 0.0543  0.1869  -0.0856 8   GLY A N   
52   C  CA  . GLY A 6   ? 0.0847 0.1005 0.6804 -0.0450 0.0920  -0.1585 8   GLY A CA  
53   C  C   . GLY A 6   ? 0.3698 0.1959 0.3008 -0.0208 0.1703  -0.1377 8   GLY A C   
54   O  O   . GLY A 6   ? 0.3770 0.3177 0.5048 0.0192  0.1793  -0.1117 8   GLY A O   
55   N  N   . LYS A 7   ? 0.2527 0.2848 0.5435 0.0036  0.0752  0.0709  9   LYS A N   
56   C  CA  . LYS A 7   ? 0.4965 0.3569 0.5080 -0.0785 -0.2834 -0.2861 9   LYS A CA  
57   C  C   . LYS A 7   ? 0.2141 0.4102 0.5093 -0.0463 0.0961  0.1179  9   LYS A C   
58   O  O   . LYS A 7   ? 0.4773 0.4606 0.6761 -0.1804 -0.0179 -0.1066 9   LYS A O   
59   C  CB  . LYS A 7   ? 0.3641 0.6341 0.3728 0.0944  0.0955  -0.0247 9   LYS A CB  
60   N  N   . HIS A 8   ? 0.6184 0.3551 0.6774 0.0008  0.3105  0.1538  10  HIS A N   
61   C  CA  . HIS A 8   ? 0.4386 0.2462 0.3931 0.1435  0.2307  0.1439  10  HIS A CA  
62   C  C   . HIS A 8   ? 0.2098 0.2416 0.3562 0.0916  0.1303  0.0996  10  HIS A C   
63   O  O   . HIS A 8   ? 0.2185 0.2942 0.2462 0.1353  0.1071  0.0520  10  HIS A O   
64   C  CB  . HIS A 8   ? 0.1605 0.2153 0.2626 0.0482  0.1473  0.0163  10  HIS A CB  
65   C  CG  . HIS A 8   ? 0.1356 0.2683 0.1470 -0.0366 0.0269  -0.0750 10  HIS A CG  
66   N  ND1 . HIS A 8   ? 0.2071 0.2552 0.2638 0.0596  0.1053  0.0558  10  HIS A ND1 
67   C  CD2 . HIS A 8   ? 0.0917 0.2866 0.1757 0.0136  0.0259  -0.0912 10  HIS A CD2 
68   C  CE1 . HIS A 8   ? 0.1007 0.1995 0.1873 -0.0175 0.0249  0.0026  10  HIS A CE1 
69   N  NE2 . HIS A 8   ? 0.1898 0.2472 0.2124 0.0252  0.0100  -0.0879 10  HIS A NE2 
70   N  N   . ASN A 9   ? 0.1428 0.1413 0.2468 0.0344  0.1244  -0.0058 11  ASN A N   
71   C  CA  . ASN A 9   ? 0.1434 0.1470 0.1715 0.0605  0.1159  0.0134  11  ASN A CA  
72   C  C   . ASN A 9   ? 0.0924 0.1410 0.1985 0.0293  0.0819  0.0055  11  ASN A C   
73   O  O   . ASN A 9   ? 0.1156 0.1568 0.1585 0.0582  0.0863  0.0254  11  ASN A O   
74   C  CB  . ASN A 9   ? 0.1076 0.1222 0.1880 -0.0201 0.0709  0.0249  11  ASN A CB  
75   C  CG  . ASN A 9   ? 0.1284 0.1683 0.1970 0.0042  0.0977  -0.0580 11  ASN A CG  
76   O  OD1 . ASN A 9   ? 0.1679 0.1791 0.2633 -0.0265 0.0683  -0.0203 11  ASN A OD1 
77   N  ND2 . ASN A 9   ? 0.2220 0.1988 0.2200 -0.0089 0.1108  -0.0099 11  ASN A ND2 
78   N  N   . GLY A 10  ? 0.1144 0.1266 0.1661 0.0021  0.1000  -0.0204 12  GLY A N   
79   C  CA  . GLY A 10  ? 0.0785 0.1858 0.1445 0.0239  0.0644  0.0052  12  GLY A CA  
80   C  C   . GLY A 10  ? 0.1007 0.1427 0.1607 -0.0013 0.0669  0.0163  12  GLY A C   
81   O  O   . GLY A 10  ? 0.0855 0.1126 0.1769 0.0346  0.0541  0.0136  12  GLY A O   
82   N  N   . PRO A 11  ? 0.0864 0.0820 0.1377 0.0099  0.0607  -0.0012 13  PRO A N   
83   C  CA  . PRO A 11  ? 0.0812 0.1110 0.1592 0.0078  0.0626  -0.0240 13  PRO A CA  
84   C  C   . PRO A 11  ? 0.1242 0.0864 0.1306 0.0177  0.0418  0.0292  13  PRO A C   
85   O  O   . PRO A 11  ? 0.0724 0.1155 0.1596 0.0017  0.0232  -0.0003 13  PRO A O   
86   C  CB  . PRO A 11  ? 0.1309 0.1405 0.1424 -0.0361 0.0697  -0.0151 13  PRO A CB  
87   C  CG  . PRO A 11  ? 0.1187 0.1392 0.1345 -0.0017 0.0723  -0.0199 13  PRO A CG  
88   C  CD  . PRO A 11  ? 0.1020 0.1150 0.1374 -0.0098 0.0683  -0.0054 13  PRO A CD  
89   N  N   . GLU A 12  ? 0.1014 0.1048 0.1665 0.0149  0.0391  0.0364  14  GLU A N   
90   C  CA  . GLU A 12  ? 0.1205 0.1345 0.1640 0.0335  0.0227  0.0462  14  GLU A CA  
91   C  C   . GLU A 12  ? 0.0934 0.1532 0.1732 0.0681  0.0436  0.0265  14  GLU A C   
92   O  O   . GLU A 12  ? 0.1242 0.1288 0.2164 0.0542  0.0315  0.0589  14  GLU A O   
93   C  CB  . GLU A 12  ? 0.2520 0.1658 0.2352 0.1101  0.0229  0.0031  14  GLU A CB  
94   C  CG  . GLU A 12  ? 0.2149 0.2398 0.2024 0.0726  -0.0425 -0.0078 14  GLU A CG  
95   C  CD  . GLU A 12  ? 0.1725 0.1643 0.3025 0.0924  -0.0479 -0.0436 14  GLU A CD  
96   O  OE1 . GLU A 12  ? 0.1888 0.1859 0.2218 0.0738  -0.0543 -0.0486 14  GLU A OE1 
97   O  OE2 . GLU A 12  ? 0.4260 0.1737 0.2689 0.0335  0.0192  -0.0157 14  GLU A OE2 
98   N  N   . HIS A 13  ? 0.0926 0.1180 0.1636 0.0384  0.0359  0.0336  15  HIS A N   
99   C  CA  . HIS A 13  ? 0.0752 0.1234 0.1453 0.0489  0.0383  0.0278  15  HIS A CA  
100  C  C   . HIS A 13  ? 0.0434 0.1306 0.1650 0.0392  0.0189  0.0140  15  HIS A C   
101  O  O   . HIS A 13  ? 0.0520 0.1442 0.2529 0.0241  0.0216  0.0303  15  HIS A O   
102  C  CB  . HIS A 13  ? 0.0522 0.1470 0.1384 0.0444  0.0409  0.0162  15  HIS A CB  
103  C  CG  . HIS A 13  ? 0.1028 0.1526 0.1172 0.0556  0.0313  0.0168  15  HIS A CG  
104  N  ND1 . HIS A 13  ? 0.1169 0.2437 0.2222 0.1217  0.0225  0.0140  15  HIS A ND1 
105  C  CD2 . HIS A 13  ? 0.1611 0.1395 0.1949 0.0883  0.0545  0.0061  15  HIS A CD2 
106  C  CE1 . HIS A 13  ? 0.2128 0.2778 0.0955 0.1477  0.0245  -0.0052 15  HIS A CE1 
107  N  NE2 . HIS A 13  ? 0.2098 0.2035 0.2665 0.1373  0.0307  -0.0080 15  HIS A NE2 
108  N  N   . TRP A 14  ? 0.0387 0.0952 0.1531 0.0309  0.0252  0.0343  16  TRP A N   
109  C  CA  . TRP A 14  ? 0.0417 0.0838 0.1628 0.0223  0.0187  0.0105  16  TRP A CA  
110  C  C   . TRP A 14  ? 0.0584 0.1151 0.1467 0.0003  -0.0013 0.0320  16  TRP A C   
111  O  O   . TRP A 14  ? 0.0634 0.1023 0.1650 -0.0001 0.0044  -0.0047 16  TRP A O   
112  C  CB  . TRP A 14  ? 0.0379 0.1172 0.1194 0.0134  0.0071  -0.0212 16  TRP A CB  
113  C  CG  . TRP A 14  ? 0.0524 0.0856 0.1102 -0.0068 0.0089  0.0025  16  TRP A CG  
114  C  CD1 . TRP A 14  ? 0.0452 0.1012 0.1082 0.0157  0.0211  0.0231  16  TRP A CD1 
115  C  CD2 . TRP A 14  ? 0.0470 0.0777 0.1266 -0.0037 0.0244  0.0033  16  TRP A CD2 
116  N  NE1 . TRP A 14  ? 0.0339 0.0847 0.1485 0.0134  0.0148  0.0133  16  TRP A NE1 
117  C  CE2 . TRP A 14  ? 0.0399 0.0926 0.1287 0.0067  0.0170  0.0140  16  TRP A CE2 
118  C  CE3 . TRP A 14  ? 0.0417 0.0547 0.1273 0.0041  0.0226  0.0062  16  TRP A CE3 
119  C  CZ2 . TRP A 14  ? 0.0440 0.0624 0.1216 -0.0065 0.0344  0.0060  16  TRP A CZ2 
120  C  CZ3 . TRP A 14  ? 0.0477 0.0783 0.1241 -0.0087 0.0160  -0.0082 16  TRP A CZ3 
121  C  CH2 . TRP A 14  ? 0.0607 0.0761 0.1229 0.0066  0.0375  -0.0133 16  TRP A CH2 
122  N  N   . HIS A 15  ? 0.0398 0.1170 0.1287 0.0174  -0.0012 0.0019  17  HIS A N   
123  C  CA  . HIS A 15  ? 0.0408 0.1392 0.1291 -0.0084 -0.0084 0.0159  17  HIS A CA  
124  C  C   . HIS A 15  ? 0.0775 0.1320 0.1884 -0.0117 0.0178  0.0611  17  HIS A C   
125  O  O   . HIS A 15  ? 0.0544 0.1474 0.2534 -0.0038 -0.0047 0.0299  17  HIS A O   
126  C  CB  . HIS A 15  ? 0.0594 0.1194 0.1798 0.0231  -0.0074 0.0364  17  HIS A CB  
127  C  CG  . HIS A 15  ? 0.0575 0.1205 0.1686 0.0181  -0.0040 0.0541  17  HIS A CG  
128  N  ND1 . HIS A 15  ? 0.0530 0.2466 0.2352 0.0193  -0.0179 0.0948  17  HIS A ND1 
129  C  CD2 . HIS A 15  ? 0.0653 0.1524 0.2113 0.0490  0.0155  0.0468  17  HIS A CD2 
130  C  CE1 . HIS A 15  ? 0.1155 0.2292 0.1765 0.0462  -0.0140 0.0735  17  HIS A CE1 
131  N  NE2 . HIS A 15  ? 0.0732 0.2146 0.2169 0.0519  -0.0019 0.0785  17  HIS A NE2 
132  N  N   . LYS A 16  ? 0.0348 0.1733 0.1927 -0.0122 0.0018  0.0602  18  LYS A N   
133  C  CA  . LYS A 16  ? 0.0355 0.1880 0.2214 0.0008  0.0345  0.0653  18  LYS A CA  
134  C  C   . LYS A 16  ? 0.0768 0.1615 0.2584 0.0039  0.0139  0.0413  18  LYS A C   
135  O  O   . LYS A 16  ? 0.0962 0.2149 0.4117 -0.0491 -0.1102 0.1383  18  LYS A O   
136  C  CB  . LYS A 16  ? 0.0546 0.1927 0.2125 0.0243  0.0173  0.0822  18  LYS A CB  
137  C  CG  . LYS A 16  ? 0.0304 0.1837 0.2491 0.0509  -0.0093 0.0468  18  LYS A CG  
138  C  CD  . LYS A 16  ? 0.0427 0.2304 0.2556 0.0737  0.0130  0.0629  18  LYS A CD  
139  C  CE  . LYS A 16  ? 0.0531 0.2221 0.2217 0.0496  0.0154  0.0585  18  LYS A CE  
140  N  NZ  . LYS A 16  ? 0.0531 0.2469 0.2081 0.0542  0.0269  0.0632  18  LYS A NZ  
141  N  N   . ASP A 17  ? 0.0837 0.1557 0.2053 0.0085  0.0181  0.0476  19  ASP A N   
142  C  CA  . ASP A 17  ? 0.0813 0.1689 0.1974 0.0111  0.0137  0.0626  19  ASP A CA  
143  C  C   . ASP A 17  ? 0.0493 0.1223 0.2620 -0.0099 0.0043  0.0234  19  ASP A C   
144  O  O   . ASP A 17  ? 0.0916 0.1205 0.2529 -0.0138 0.0143  0.0457  19  ASP A O   
145  C  CB  . ASP A 17  ? 0.1775 0.3114 0.1646 0.1073  0.0166  0.0558  19  ASP A CB  
146  C  CG  . ASP A 17  ? 0.1036 0.4791 0.2657 -0.0156 0.0099  0.0187  19  ASP A CG  
147  O  OD1 . ASP A 17  ? 0.1446 0.5829 0.3456 -0.1036 0.0477  -0.0270 19  ASP A OD1 
148  O  OD2 . ASP A 17  ? 0.2520 0.3567 0.3895 0.0217  -0.0430 -0.0813 19  ASP A OD2 
149  N  N   . PHE A 18  ? 0.0575 0.1248 0.2142 -0.0147 0.0005  0.0158  20  PHE A N   
150  C  CA  . PHE A 18  ? 0.0375 0.1312 0.1783 -0.0020 -0.0171 -0.0002 20  PHE A CA  
151  C  C   . PHE A 18  ? 0.0557 0.1021 0.1812 -0.0230 -0.0114 0.0194  20  PHE A C   
152  O  O   . PHE A 18  ? 0.0564 0.0949 0.1593 -0.0144 0.0027  0.0072  20  PHE A O   
153  C  CB  . PHE A 18  ? 0.0548 0.1453 0.1729 -0.0278 -0.0200 0.0141  20  PHE A CB  
154  C  CG  . PHE A 18  ? 0.0477 0.1647 0.1898 -0.0473 -0.0128 0.0458  20  PHE A CG  
155  C  CD1 . PHE A 18  ? 0.0916 0.1895 0.2346 -0.0473 -0.0025 0.0794  20  PHE A CD1 
156  C  CD2 . PHE A 18  ? 0.1029 0.1880 0.1772 -0.0329 0.0049  0.0409  20  PHE A CD2 
157  C  CE1 . PHE A 18  ? 0.1133 0.1763 0.2383 -0.0115 -0.0314 0.0824  20  PHE A CE1 
158  C  CE2 . PHE A 18  ? 0.0864 0.2031 0.2030 -0.0315 -0.0146 0.0832  20  PHE A CE2 
159  C  CZ  . PHE A 18  ? 0.0371 0.2081 0.2606 -0.0295 -0.0068 0.0752  20  PHE A CZ  
160  N  N   A PRO A 19  ? 0.0472 0.1097 0.1812 -0.0154 -0.0086 0.0156  21  PRO A N   
161  N  N   B PRO A 19  ? 0.0549 0.0973 0.1805 -0.0223 -0.0040 0.0176  21  PRO A N   
162  C  CA  A PRO A 19  ? 0.0375 0.1521 0.1793 -0.0205 -0.0343 0.0167  21  PRO A CA  
163  C  CA  B PRO A 19  ? 0.0524 0.1348 0.1808 -0.0190 -0.0256 0.0240  21  PRO A CA  
164  C  C   A PRO A 19  ? 0.0506 0.1205 0.1712 -0.0156 -0.0278 0.0009  21  PRO A C   
165  C  C   B PRO A 19  ? 0.0565 0.1097 0.1719 -0.0163 -0.0275 0.0055  21  PRO A C   
166  O  O   A PRO A 19  ? 0.0408 0.1395 0.1654 -0.0040 -0.0420 0.0054  21  PRO A O   
167  O  O   B PRO A 19  ? 0.0591 0.1270 0.1702 -0.0083 -0.0473 0.0111  21  PRO A O   
168  C  CB  A PRO A 19  ? 0.0544 0.2401 0.2222 -0.0539 -0.0635 0.0143  21  PRO A CB  
169  C  CB  B PRO A 19  ? 0.0806 0.1931 0.2221 -0.0488 -0.0544 0.0392  21  PRO A CB  
170  C  CG  A PRO A 19  ? 0.0750 0.2109 0.2518 -0.0269 -0.0763 -0.0022 21  PRO A CG  
171  C  CG  B PRO A 19  ? 0.0840 0.1815 0.2408 -0.0823 -0.0248 0.0117  21  PRO A CG  
172  C  CD  A PRO A 19  ? 0.0260 0.1864 0.2171 -0.0571 -0.0275 0.0301  21  PRO A CD  
173  C  CD  B PRO A 19  ? 0.0546 0.1579 0.2149 -0.0425 0.0005  0.0398  21  PRO A CD  
174  N  N   . ILE A 20  ? 0.0301 0.1062 0.1471 -0.0294 -0.0345 -0.0263 22  ILE A N   
175  C  CA  . ILE A 20  ? 0.0497 0.0849 0.1646 -0.0119 -0.0135 -0.0121 22  ILE A CA  
176  C  C   . ILE A 20  ? 0.0373 0.0797 0.1229 0.0025  -0.0240 -0.0137 22  ILE A C   
177  O  O   . ILE A 20  ? 0.0484 0.0987 0.1212 0.0012  -0.0087 -0.0146 22  ILE A O   
178  C  CB  . ILE A 20  ? 0.0803 0.1102 0.1355 0.0102  -0.0406 -0.0346 22  ILE A CB  
179  C  CG1 . ILE A 20  ? 0.0730 0.1050 0.1629 -0.0009 -0.0165 -0.0353 22  ILE A CG1 
180  C  CG2 . ILE A 20  ? 0.0732 0.1050 0.1385 -0.0251 -0.0447 -0.0337 22  ILE A CG2 
181  C  CD1 . ILE A 20  ? 0.0856 0.1226 0.2587 0.0027  -0.0316 0.0030  22  ILE A CD1 
182  N  N   . ALA A 21  ? 0.0725 0.0818 0.0989 -0.0114 -0.0284 -0.0122 23  ALA A N   
183  C  CA  . ALA A 21  ? 0.0803 0.0756 0.0858 -0.0199 0.0266  0.0033  23  ALA A CA  
184  C  C   . ALA A 21  ? 0.0705 0.0835 0.0910 0.0039  -0.0137 -0.0041 23  ALA A C   
185  O  O   . ALA A 21  ? 0.0673 0.0977 0.0996 -0.0122 -0.0205 0.0006  23  ALA A O   
186  C  CB  . ALA A 21  ? 0.0679 0.1093 0.1049 0.0178  -0.0044 -0.0115 23  ALA A CB  
187  N  N   . LYS A 22  ? 0.0668 0.1014 0.1050 0.0072  -0.0227 0.0091  24  LYS A N   
188  C  CA  . LYS A 22  ? 0.0610 0.1331 0.1005 0.0107  -0.0281 0.0073  24  LYS A CA  
189  C  C   . LYS A 22  ? 0.0917 0.1252 0.1229 0.0116  -0.0194 0.0034  24  LYS A C   
190  O  O   . LYS A 22  ? 0.0891 0.2317 0.1356 -0.0001 -0.0406 0.0086  24  LYS A O   
191  C  CB  . LYS A 22  ? 0.0563 0.1391 0.1672 0.0255  -0.0025 0.0266  24  LYS A CB  
192  C  CG  . LYS A 22  ? 0.1032 0.1823 0.1550 0.0413  -0.0198 0.0049  24  LYS A CG  
193  C  CD  . LYS A 22  ? 0.1063 0.2570 0.2570 0.0559  -0.0091 0.0242  24  LYS A CD  
194  C  CE  . LYS A 22  ? 0.0943 0.2854 0.3301 0.0215  0.0538  -0.0021 24  LYS A CE  
195  N  NZ  . LYS A 22  ? 0.1941 0.2627 0.3449 0.0060  0.0622  -0.0510 24  LYS A NZ  
196  N  N   . GLY A 23  ? 0.0713 0.1084 0.1309 -0.0070 -0.0142 0.0000  25  GLY A N   
197  C  CA  . GLY A 23  ? 0.0967 0.1102 0.1240 -0.0228 -0.0140 -0.0250 25  GLY A CA  
198  C  C   . GLY A 23  ? 0.0707 0.1392 0.0758 -0.0148 -0.0494 -0.0119 25  GLY A C   
199  O  O   . GLY A 23  ? 0.0933 0.1526 0.0926 -0.0034 -0.0285 -0.0157 25  GLY A O   
200  N  N   . GLU A 24  ? 0.0680 0.1765 0.0905 -0.0214 -0.0232 -0.0183 26  GLU A N   
201  C  CA  . GLU A 24  ? 0.0759 0.1801 0.0794 -0.0121 -0.0104 -0.0362 26  GLU A CA  
202  C  C   . GLU A 24  ? 0.0739 0.1392 0.0593 0.0044  -0.0241 -0.0236 26  GLU A C   
203  O  O   . GLU A 24  ? 0.1056 0.1597 0.0732 -0.0220 -0.0319 -0.0109 26  GLU A O   
204  C  CB  . GLU A 24  ? 0.1238 0.1988 0.1302 -0.0290 -0.0648 -0.0779 26  GLU A CB  
205  C  CG  . GLU A 24  ? 0.1101 0.3563 0.0986 -0.0124 -0.0473 -0.0617 26  GLU A CG  
206  C  CD  . GLU A 24  ? 0.2063 0.4073 0.2264 -0.0135 -0.0911 -0.0089 26  GLU A CD  
207  O  OE1 . GLU A 24  ? 0.2573 0.3948 0.2726 -0.0335 -0.0583 -0.0129 26  GLU A OE1 
208  O  OE2 . GLU A 24  ? 0.2654 0.4291 0.4189 0.0761  -0.1208 -0.0348 26  GLU A OE2 
209  N  N   . ARG A 25  ? 0.0873 0.0802 0.0689 -0.0036 -0.0309 -0.0115 27  ARG A N   
210  C  CA  . ARG A 25  ? 0.0837 0.0890 0.0527 0.0136  -0.0186 -0.0139 27  ARG A CA  
211  C  C   . ARG A 25  ? 0.0495 0.0863 0.0527 0.0120  -0.0251 -0.0100 27  ARG A C   
212  O  O   . ARG A 25  ? 0.0409 0.0706 0.0651 0.0079  -0.0314 -0.0183 27  ARG A O   
213  C  CB  . ARG A 25  ? 0.1234 0.0994 0.0571 0.0355  -0.0272 -0.0141 27  ARG A CB  
214  C  CG  . ARG A 25  ? 0.1118 0.1395 0.0919 0.0142  -0.0332 -0.0057 27  ARG A CG  
215  C  CD  . ARG A 25  ? 0.1926 0.1345 0.0935 0.0541  -0.0673 0.0190  27  ARG A CD  
216  N  NE  . ARG A 25  ? 0.1503 0.1137 0.1037 0.0063  -0.0156 0.0086  27  ARG A NE  
217  C  CZ  . ARG A 25  ? 0.1111 0.1038 0.0849 0.0027  -0.0212 0.0209  27  ARG A CZ  
218  N  NH1 . ARG A 25  ? 0.1446 0.1725 0.1159 -0.0238 0.0234  -0.0656 27  ARG A NH1 
219  N  NH2 . ARG A 25  ? 0.0916 0.1313 0.1012 -0.0072 -0.0110 -0.0340 27  ARG A NH2 
220  N  N   . GLN A 26  ? 0.0518 0.0689 0.0476 -0.0025 -0.0214 -0.0069 28  GLN A N   
221  C  CA  . GLN A 26  ? 0.0329 0.0539 0.0487 0.0013  -0.0177 -0.0102 28  GLN A CA  
222  C  C   . GLN A 26  ? 0.0328 0.0461 0.0510 0.0029  -0.0212 -0.0058 28  GLN A C   
223  O  O   . GLN A 26  ? 0.0533 0.0747 0.0408 -0.0135 -0.0168 -0.0063 28  GLN A O   
224  C  CB  . GLN A 26  ? 0.0319 0.0625 0.0901 0.0025  -0.0085 -0.0121 28  GLN A CB  
225  C  CG  . GLN A 26  ? 0.0398 0.0606 0.0820 -0.0017 -0.0201 0.0043  28  GLN A CG  
226  C  CD  . GLN A 26  ? 0.0470 0.0637 0.0646 -0.0102 -0.0218 -0.0084 28  GLN A CD  
227  O  OE1 . GLN A 26  ? 0.0470 0.0794 0.0800 -0.0159 -0.0084 -0.0173 28  GLN A OE1 
228  N  NE2 . GLN A 26  ? 0.0361 0.0636 0.0724 -0.0185 -0.0133 -0.0081 28  GLN A NE2 
229  N  N   . SER A 27  ? 0.0391 0.0515 0.0469 0.0058  -0.0198 -0.0070 29  SER A N   
230  C  CA  . SER A 27  ? 0.0343 0.0443 0.0511 0.0067  -0.0146 -0.0093 29  SER A CA  
231  C  C   . SER A 27  ? 0.0337 0.0485 0.0520 0.0050  -0.0068 -0.0063 29  SER A C   
232  O  O   . SER A 27  ? 0.0443 0.0619 0.0477 0.0027  -0.0002 -0.0100 29  SER A O   
233  C  CB  . SER A 27  ? 0.0600 0.0416 0.0328 0.0183  -0.0155 -0.0098 29  SER A CB  
234  O  OG  . SER A 27  ? 0.0610 0.0357 0.0316 -0.0096 -0.0055 -0.0126 29  SER A OG  
235  N  N   . PRO A 28  ? 0.0408 0.0434 0.0436 0.0058  -0.0058 0.0013  30  PRO A N   
236  C  CA  . PRO A 28  ? 0.0540 0.0511 0.0232 -0.0108 -0.0104 0.0020  30  PRO A CA  
237  C  C   . PRO A 28  ? 0.0520 0.0396 0.0260 0.0024  -0.0102 -0.0027 30  PRO A C   
238  O  O   . PRO A 28  ? 0.0606 0.0538 0.0387 0.0078  -0.0162 0.0004  30  PRO A O   
239  C  CB  . PRO A 28  ? 0.0454 0.0558 0.0343 -0.0003 -0.0005 -0.0156 30  PRO A CB  
240  C  CG  . PRO A 28  ? 0.0267 0.0671 0.0518 -0.0059 -0.0006 0.0069  30  PRO A CG  
241  C  CD  . PRO A 28  ? 0.0469 0.0592 0.0355 -0.0076 0.0000  -0.0082 30  PRO A CD  
242  N  N   . VAL A 29  ? 0.0662 0.0449 0.0285 0.0073  -0.0041 0.0089  31  VAL A N   
243  C  CA  . VAL A 29  ? 0.0908 0.0506 0.0233 -0.0010 -0.0067 0.0092  31  VAL A CA  
244  C  C   . VAL A 29  ? 0.0669 0.0518 0.0335 0.0148  -0.0099 0.0055  31  VAL A C   
245  O  O   . VAL A 29  ? 0.0644 0.0496 0.0567 0.0055  -0.0215 0.0115  31  VAL A O   
246  C  CB  . VAL A 29  ? 0.0741 0.0505 0.0540 -0.0016 -0.0071 -0.0107 31  VAL A CB  
247  C  CG1 . VAL A 29  ? 0.1039 0.0603 0.0601 -0.0183 -0.0065 -0.0098 31  VAL A CG1 
248  C  CG2 . VAL A 29  ? 0.0788 0.0915 0.0583 0.0197  0.0076  -0.0006 31  VAL A CG2 
249  N  N   . ASP A 30  ? 0.0709 0.0503 0.0334 0.0086  0.0001  0.0114  32  ASP A N   
250  C  CA  . ASP A 30  ? 0.0522 0.0522 0.0460 0.0081  0.0066  -0.0002 32  ASP A CA  
251  C  C   . ASP A 30  ? 0.0759 0.0610 0.0190 0.0119  0.0091  0.0063  32  ASP A C   
252  O  O   . ASP A 30  ? 0.1023 0.0950 0.0610 0.0035  -0.0069 -0.0217 32  ASP A O   
253  C  CB  . ASP A 30  ? 0.1273 0.0459 0.0599 0.0122  -0.0153 0.0115  32  ASP A CB  
254  C  CG  . ASP A 30  ? 0.1212 0.0820 0.0644 -0.0063 -0.0245 0.0091  32  ASP A CG  
255  O  OD1 . ASP A 30  ? 0.1049 0.0572 0.0520 0.0134  -0.0174 0.0047  32  ASP A OD1 
256  O  OD2 . ASP A 30  ? 0.1725 0.0926 0.0706 -0.0292 -0.0160 0.0190  32  ASP A OD2 
257  N  N   . ILE A 31  ? 0.0610 0.0562 0.0511 0.0216  0.0074  0.0098  33  ILE A N   
258  C  CA  . ILE A 31  ? 0.0664 0.0566 0.0619 0.0253  0.0115  0.0168  33  ILE A CA  
259  C  C   . ILE A 31  ? 0.0989 0.0467 0.0496 0.0134  0.0039  0.0054  33  ILE A C   
260  O  O   . ILE A 31  ? 0.1143 0.0522 0.0610 0.0091  0.0111  0.0106  33  ILE A O   
261  C  CB  . ILE A 31  ? 0.0636 0.0549 0.0682 0.0197  0.0131  0.0161  33  ILE A CB  
262  C  CG1 . ILE A 31  ? 0.0774 0.0531 0.0767 0.0156  -0.0017 0.0242  33  ILE A CG1 
263  C  CG2 . ILE A 31  ? 0.0660 0.1047 0.0962 0.0268  0.0237  -0.0008 33  ILE A CG2 
264  C  CD1 . ILE A 31  ? 0.0646 0.0831 0.1199 0.0355  -0.0201 0.0128  33  ILE A CD1 
265  N  N   . ASP A 32  ? 0.1402 0.0765 0.0451 0.0269  0.0136  0.0142  34  ASP A N   
266  C  CA  . ASP A 32  ? 0.1373 0.0899 0.0761 0.0305  0.0061  0.0348  34  ASP A CA  
267  C  C   . ASP A 32  ? 0.1449 0.0882 0.0440 0.0486  0.0134  0.0253  34  ASP A C   
268  O  O   . ASP A 32  ? 0.2132 0.1147 0.0591 0.0672  0.0171  0.0117  34  ASP A O   
269  C  CB  . ASP A 32  ? 0.1895 0.0856 0.1067 0.0451  -0.0330 0.0263  34  ASP A CB  
270  C  CG  . ASP A 32  ? 0.2556 0.1040 0.1564 -0.0352 -0.0307 0.0312  34  ASP A CG  
271  O  OD1 . ASP A 32  ? 0.3059 0.1794 0.1683 0.0336  0.0685  0.0632  34  ASP A OD1 
272  O  OD2 . ASP A 32  ? 0.4079 0.2934 0.1629 0.0139  -0.0695 0.1036  34  ASP A OD2 
273  N  N   . THR A 33  ? 0.1747 0.1180 0.0628 0.0376  0.0278  0.0534  35  THR A N   
274  C  CA  . THR A 33  ? 0.1837 0.1334 0.1022 0.0606  0.0366  0.0697  35  THR A CA  
275  C  C   . THR A 33  ? 0.2469 0.1306 0.1155 0.0802  0.0797  0.0624  35  THR A C   
276  O  O   . THR A 33  ? 0.2401 0.1453 0.1283 0.0824  0.0691  0.0463  35  THR A O   
277  C  CB  . THR A 33  ? 0.1679 0.1701 0.1187 0.0582  0.0189  0.0772  35  THR A CB  
278  O  OG1 . THR A 33  ? 0.1862 0.1474 0.1248 0.0221  0.0548  0.0617  35  THR A OG1 
279  C  CG2 . THR A 33  ? 0.1758 0.2214 0.1023 0.0533  0.0316  0.0560  35  THR A CG2 
280  N  N   A HIS A 34  ? 0.2682 0.1355 0.0761 0.0605  0.0578  0.0469  36  HIS A N   
281  N  N   B HIS A 34  ? 0.2746 0.1403 0.0768 0.0614  0.0570  0.0489  36  HIS A N   
282  C  CA  A HIS A 34  ? 0.2982 0.1110 0.0803 0.0414  0.0674  0.0518  36  HIS A CA  
283  C  CA  B HIS A 34  ? 0.3140 0.1040 0.0820 0.0385  0.0672  0.0569  36  HIS A CA  
284  C  C   A HIS A 34  ? 0.2926 0.1934 0.0196 0.0535  0.0221  0.0159  36  HIS A C   
285  C  C   B HIS A 34  ? 0.3012 0.1944 0.0178 0.0476  0.0227  0.0172  36  HIS A C   
286  O  O   A HIS A 34  ? 0.2516 0.2922 0.0770 0.0760  0.0416  -0.0075 36  HIS A O   
287  O  O   B HIS A 34  ? 0.2433 0.2979 0.0793 0.0795  0.0375  -0.0107 36  HIS A O   
288  C  CB  A HIS A 34  ? 0.3146 0.1496 0.0461 0.0811  0.0127  0.0582  36  HIS A CB  
289  C  CB  B HIS A 34  ? 0.3431 0.1521 0.0653 0.0948  0.0395  0.0458  36  HIS A CB  
290  C  CG  A HIS A 34  ? 0.3699 0.1388 0.0469 0.0507  -0.0025 0.0411  36  HIS A CG  
291  C  CG  B HIS A 34  ? 0.4349 0.0891 0.1514 0.0801  -0.0386 0.0895  36  HIS A CG  
292  N  ND1 A HIS A 34  ? 0.4227 0.1625 0.0837 0.0752  -0.0272 0.0069  36  HIS A ND1 
293  N  ND1 B HIS A 34  ? 0.5029 0.1168 0.3312 -0.0990 -0.1091 0.0266  36  HIS A ND1 
294  C  CD2 A HIS A 34  ? 0.3439 0.1192 0.0211 0.0294  -0.0505 0.0237  36  HIS A CD2 
295  C  CD2 B HIS A 34  ? 0.4508 0.1686 0.1057 0.1157  -0.0636 0.0876  36  HIS A CD2 
296  C  CE1 A HIS A 34  ? 0.5776 0.0978 0.1291 0.0668  -0.0748 0.0199  36  HIS A CE1 
297  C  CE1 B HIS A 34  ? 0.6117 0.1080 0.2722 0.1407  -0.0390 -0.0081 36  HIS A CE1 
298  N  NE2 A HIS A 34  ? 0.4412 0.1316 0.1973 -0.0504 -0.1530 0.0319  36  HIS A NE2 
299  N  NE2 B HIS A 34  ? 0.5590 0.0691 0.3587 0.0762  -0.0780 0.0471  36  HIS A NE2 
300  N  N   . THR A 35  ? 0.3097 0.1012 0.0881 0.0707  0.0776  0.0291  37  THR A N   
301  C  CA  . THR A 35  ? 0.3906 0.1176 0.0856 0.0818  0.0136  0.0529  37  THR A CA  
302  C  C   . THR A 35  ? 0.2587 0.1255 0.0496 0.0902  0.0234  0.0129  37  THR A C   
303  O  O   . THR A 35  ? 0.3001 0.1805 0.0944 0.0758  -0.0295 -0.0192 37  THR A O   
304  C  CB  . THR A 35  ? 0.4087 0.2706 0.2214 0.1524  -0.0633 0.0789  37  THR A CB  
305  O  OG1 . THR A 35  ? 0.5540 0.3950 0.3532 0.1145  0.0015  -0.0208 37  THR A OG1 
306  C  CG2 . THR A 35  ? 0.3533 0.1399 0.3172 0.1318  -0.0972 0.0195  37  THR A CG2 
307  N  N   . ALA A 36  ? 0.2433 0.1280 0.0424 0.0702  0.0232  0.0354  38  ALA A N   
308  C  CA  . ALA A 36  ? 0.2404 0.1093 0.0533 0.0705  0.0507  0.0350  38  ALA A CA  
309  C  C   . ALA A 36  ? 0.2558 0.1485 0.1617 0.0565  0.1097  0.0467  38  ALA A C   
310  O  O   . ALA A 36  ? 0.3116 0.1855 0.3148 0.0322  0.1843  0.0274  38  ALA A O   
311  C  CB  . ALA A 36  ? 0.2071 0.1146 0.0891 0.0348  0.0097  0.0052  38  ALA A CB  
312  N  N   . LYS A 37  ? 0.2124 0.1808 0.1126 0.1231  0.0280  0.0092  39  LYS A N   
313  C  CA  . LYS A 37  ? 0.2493 0.3116 0.1355 0.1807  0.0188  -0.0226 39  LYS A CA  
314  C  C   . LYS A 37  ? 0.1564 0.2092 0.0959 0.0925  0.0401  0.0018  39  LYS A C   
315  O  O   . LYS A 37  ? 0.1438 0.1973 0.0584 0.0292  0.0093  -0.0073 39  LYS A O   
316  C  CB  . LYS A 37  ? 0.2584 0.4521 0.2579 0.2204  -0.0130 -0.1683 39  LYS A CB  
317  C  CG  . LYS A 37  ? 0.2454 0.4386 0.3014 0.2424  -0.0597 -0.0226 39  LYS A CG  
318  C  CD  . LYS A 37  ? 0.2786 0.3807 0.2376 0.0596  -0.0504 0.0592  39  LYS A CD  
319  C  CE  . LYS A 37  ? 0.2325 0.4993 0.3423 0.0444  -0.0146 0.0352  39  LYS A CE  
320  N  NZ  . LYS A 37  ? 0.2630 0.5288 0.4187 0.0955  -0.0814 0.2407  39  LYS A NZ  
321  N  N   . TYR A 38  ? 0.2174 0.2225 0.1089 0.0490  0.0603  0.0000  40  TYR A N   
322  C  CA  . TYR A 38  ? 0.1467 0.1948 0.1467 -0.0022 0.0844  -0.0091 40  TYR A CA  
323  C  C   . TYR A 38  ? 0.2046 0.2143 0.0590 -0.0070 0.0432  -0.0194 40  TYR A C   
324  O  O   . TYR A 38  ? 0.1999 0.2691 0.0557 0.0528  0.0350  -0.0274 40  TYR A O   
325  C  CB  . TYR A 38  ? 0.2441 0.2678 0.1301 -0.1152 0.0527  0.0312  40  TYR A CB  
326  C  CG  . TYR A 38  ? 0.2222 0.4016 0.1007 -0.0926 0.0505  -0.0133 40  TYR A CG  
327  C  CD1 . TYR A 38  ? 0.2296 0.3721 0.1180 -0.1703 -0.0331 -0.0253 40  TYR A CD1 
328  C  CD2 . TYR A 38  ? 0.2304 0.4229 0.2016 -0.0614 0.1090  0.0025  40  TYR A CD2 
329  C  CE1 . TYR A 38  ? 0.2408 0.5651 0.1059 -0.0551 0.0286  -0.0149 40  TYR A CE1 
330  C  CE2 . TYR A 38  ? 0.2059 0.5861 0.1582 -0.0394 0.0232  -0.0062 40  TYR A CE2 
331  C  CZ  . TYR A 38  ? 0.1743 0.6753 0.1180 -0.0794 0.0017  -0.0251 40  TYR A CZ  
332  O  OH  . TYR A 38  ? 0.1873 0.7698 0.2666 -0.0066 0.0793  -0.1384 40  TYR A OH  
333  N  N   . ASP A 39  ? 0.0998 0.2159 0.1014 0.0310  0.0323  -0.0174 41  ASP A N   
334  C  CA  . ASP A 39  ? 0.1471 0.1920 0.0953 0.0095  0.0057  -0.0054 41  ASP A CA  
335  C  C   . ASP A 39  ? 0.1586 0.2812 0.1216 0.0304  -0.0036 -0.0489 41  ASP A C   
336  O  O   . ASP A 39  ? 0.1546 0.2865 0.1269 0.0502  0.0157  -0.0034 41  ASP A O   
337  C  CB  . ASP A 39  ? 0.1582 0.1959 0.1277 -0.0243 -0.0161 0.0019  41  ASP A CB  
338  C  CG  . ASP A 39  ? 0.1834 0.2524 0.2205 -0.0267 -0.0454 -0.0484 41  ASP A CG  
339  O  OD1 . ASP A 39  ? 0.2805 0.2284 0.1614 0.0192  -0.0205 -0.0690 41  ASP A OD1 
340  O  OD2 . ASP A 39  ? 0.2638 0.2035 0.3148 -0.0499 -0.0251 -0.0275 41  ASP A OD2 
341  N  N   . PRO A 40  ? 0.1834 0.3512 0.1514 0.0959  0.0339  -0.0207 42  PRO A N   
342  C  CA  . PRO A 40  ? 0.1676 0.4364 0.2034 0.1172  0.0782  0.0257  42  PRO A CA  
343  C  C   . PRO A 40  ? 0.2408 0.4374 0.2354 0.1324  0.0904  0.0298  42  PRO A C   
344  O  O   . PRO A 40  ? 0.2656 0.7368 0.2579 0.2736  0.0955  0.0377  42  PRO A O   
345  C  CB  . PRO A 40  ? 0.2020 0.5278 0.1912 0.1762  0.0675  0.0785  42  PRO A CB  
346  C  CG  . PRO A 40  ? 0.2375 0.5256 0.1395 0.1858  0.0494  0.0474  42  PRO A CG  
347  C  CD  . PRO A 40  ? 0.2919 0.3692 0.1062 0.1089  0.0501  -0.0732 42  PRO A CD  
348  N  N   . SER A 41  ? 0.2365 0.3491 0.1190 0.1684  0.0173  -0.0261 43  SER A N   
349  C  CA  . SER A 41  ? 0.4163 0.2940 0.1575 0.1226  -0.0519 -0.0379 43  SER A CA  
350  C  C   . SER A 41  ? 0.3780 0.2712 0.1489 0.1685  -0.0005 -0.0648 43  SER A C   
351  O  O   . SER A 41  ? 0.4785 0.3067 0.2582 0.1879  -0.0709 -0.0336 43  SER A O   
352  C  CB  . SER A 41  ? 0.2981 0.3500 0.2419 0.1752  -0.0523 -0.0771 43  SER A CB  
353  O  OG  . SER A 41  ? 0.3647 0.3433 0.2841 0.0811  -0.1268 -0.1110 43  SER A OG  
354  N  N   . LEU A 42  ? 0.3783 0.2561 0.1406 0.1584  -0.0741 -0.0505 44  LEU A N   
355  C  CA  . LEU A 42  ? 0.2396 0.2426 0.1392 0.0845  -0.0861 -0.0350 44  LEU A CA  
356  C  C   . LEU A 42  ? 0.1635 0.3147 0.1567 -0.0066 -0.0074 0.0096  44  LEU A C   
357  O  O   . LEU A 42  ? 0.1611 0.4046 0.3034 -0.0133 0.0260  0.1534  44  LEU A O   
358  C  CB  . LEU A 42  ? 0.1439 0.2767 0.1291 0.0323  0.0027  -0.0385 44  LEU A CB  
359  C  CG  . LEU A 42  ? 0.1578 0.1780 0.0917 0.0116  -0.0420 0.0151  44  LEU A CG  
360  C  CD1 . LEU A 42  ? 0.1449 0.2170 0.1032 0.0148  0.0006  -0.0523 44  LEU A CD1 
361  C  CD2 . LEU A 42  ? 0.2063 0.1410 0.1294 0.0048  -0.0048 -0.0266 44  LEU A CD2 
362  N  N   . LYS A 43  ? 0.1823 0.2408 0.1729 0.0835  -0.0313 0.0019  45  LYS A N   
363  C  CA  . LYS A 43  ? 0.1776 0.2028 0.2511 0.0785  -0.0668 -0.0549 45  LYS A CA  
364  C  C   . LYS A 43  ? 0.1223 0.1823 0.1949 0.0375  -0.0032 -0.0104 45  LYS A C   
365  O  O   . LYS A 43  ? 0.1248 0.2171 0.2552 0.0211  0.0103  0.0215  45  LYS A O   
366  C  CB  . LYS A 43  ? 0.2229 0.1956 0.2115 0.1324  -0.0341 -0.0288 45  LYS A CB  
367  C  CG  . LYS A 43  ? 0.2412 0.2579 0.3159 0.1015  -0.0457 -0.0660 45  LYS A CG  
368  C  CD  . LYS A 43  ? 0.3197 0.2951 0.3815 0.0257  -0.0315 0.0081  45  LYS A CD  
369  N  N   . PRO A 44  ? 0.1398 0.1913 0.1587 -0.0182 -0.0002 -0.0015 46  PRO A N   
370  C  CA  . PRO A 44  ? 0.1363 0.2217 0.1578 -0.0463 -0.0067 0.0006  46  PRO A CA  
371  C  C   . PRO A 44  ? 0.0897 0.1385 0.1956 -0.0115 0.0086  0.0001  46  PRO A C   
372  O  O   . PRO A 44  ? 0.0704 0.1719 0.2005 -0.0287 -0.0036 0.0313  46  PRO A O   
373  C  CB  . PRO A 44  ? 0.1305 0.2419 0.1816 -0.0264 -0.0087 0.0192  46  PRO A CB  
374  C  CG  . PRO A 44  ? 0.1654 0.3419 0.2124 -0.0388 0.0212  -0.0703 46  PRO A CG  
375  C  CD  . PRO A 44  ? 0.1431 0.2566 0.2596 0.0515  -0.0133 -0.0902 46  PRO A CD  
376  N  N   . LEU A 45  ? 0.1198 0.1895 0.1916 0.0069  -0.0051 0.0205  47  LEU A N   
377  C  CA  . LEU A 45  ? 0.0695 0.1880 0.1757 -0.0030 -0.0029 0.0193  47  LEU A CA  
378  C  C   . LEU A 45  ? 0.0880 0.1661 0.2873 -0.0292 -0.0668 0.0432  47  LEU A C   
379  O  O   . LEU A 45  ? 0.1014 0.2207 0.2969 -0.0675 -0.0759 0.0745  47  LEU A O   
380  C  CB  . LEU A 45  ? 0.1830 0.1898 0.2674 0.0144  -0.0006 0.0158  47  LEU A CB  
381  C  CG  . LEU A 45  ? 0.1208 0.2460 0.3165 -0.0329 -0.0153 -0.0754 47  LEU A CG  
382  C  CD1 . LEU A 45  ? 0.0950 0.1959 0.4105 -0.0372 -0.0232 -0.0629 47  LEU A CD1 
383  C  CD2 . LEU A 45  ? 0.1164 0.2042 0.3799 0.0176  -0.0438 -0.0389 47  LEU A CD2 
384  N  N   . SER A 46  ? 0.0545 0.1453 0.1718 -0.0111 -0.0236 0.0228  48  SER A N   
385  C  CA  . SER A 46  ? 0.0418 0.1690 0.1413 -0.0097 -0.0113 0.0120  48  SER A CA  
386  C  C   . SER A 46  ? 0.0566 0.1431 0.1604 -0.0217 0.0024  0.0208  48  SER A C   
387  O  O   . SER A 46  ? 0.0944 0.1507 0.1224 -0.0471 0.0131  -0.0122 48  SER A O   
388  C  CB  . SER A 46  ? 0.1316 0.1654 0.2006 -0.0062 -0.0268 0.0272  48  SER A CB  
389  O  OG  . SER A 46  ? 0.1837 0.1808 0.2210 0.0295  0.0030  0.0649  48  SER A OG  
390  N  N   . VAL A 47  ? 0.1199 0.1424 0.1309 -0.0387 0.0137  0.0200  49  VAL A N   
391  C  CA  . VAL A 47  ? 0.1446 0.1392 0.1438 -0.0518 0.0142  0.0104  49  VAL A CA  
392  C  C   . VAL A 47  ? 0.1242 0.1780 0.1750 -0.0889 -0.0323 -0.0140 49  VAL A C   
393  O  O   . VAL A 47  ? 0.1327 0.2498 0.2171 -0.1193 -0.0462 0.0024  49  VAL A O   
394  C  CB  . VAL A 47  ? 0.1801 0.1499 0.1876 -0.0406 0.0380  -0.0146 49  VAL A CB  
395  C  CG1 . VAL A 47  ? 0.3441 0.2383 0.1945 -0.1092 0.0629  -0.0368 49  VAL A CG1 
396  C  CG2 . VAL A 47  ? 0.1367 0.2053 0.2577 -0.0705 -0.0179 -0.0026 49  VAL A CG2 
397  N  N   . SER A 48  ? 0.1226 0.1872 0.1775 -0.0726 -0.0580 0.0078  50  SER A N   
398  C  CA  . SER A 48  ? 0.0770 0.2455 0.2194 -0.0215 -0.0516 0.0044  50  SER A CA  
399  C  C   . SER A 48  ? 0.0696 0.1977 0.2424 -0.0211 -0.0391 0.0421  50  SER A C   
400  O  O   . SER A 48  ? 0.1395 0.1957 0.1992 -0.0634 -0.0649 0.0326  50  SER A O   
401  C  CB  . SER A 48  ? 0.1675 0.2416 0.2645 -0.0124 -0.0096 0.0471  50  SER A CB  
402  O  OG  . SER A 48  ? 0.1963 0.3646 0.3473 -0.0044 0.0128  0.0129  50  SER A OG  
403  N  N   . TYR A 49  ? 0.1089 0.1826 0.1992 -0.0465 -0.0628 0.0496  51  TYR A N   
404  C  CA  . TYR A 49  ? 0.1199 0.1931 0.1878 -0.0226 -0.0674 0.0552  51  TYR A CA  
405  C  C   . TYR A 49  ? 0.1221 0.2081 0.2286 -0.0012 -0.0853 0.0532  51  TYR A C   
406  O  O   . TYR A 49  ? 0.1536 0.2916 0.2006 -0.0100 -0.0792 0.0523  51  TYR A O   
407  C  CB  . TYR A 49  ? 0.0782 0.1758 0.1668 -0.0370 -0.0735 0.0209  51  TYR A CB  
408  C  CG  . TYR A 49  ? 0.0901 0.1416 0.1132 -0.0366 -0.0571 0.0268  51  TYR A CG  
409  C  CD1 . TYR A 49  ? 0.0967 0.1571 0.1697 -0.0642 -0.0411 0.0322  51  TYR A CD1 
410  C  CD2 . TYR A 49  ? 0.0901 0.1474 0.0971 -0.0060 -0.0203 0.0325  51  TYR A CD2 
411  C  CE1 . TYR A 49  ? 0.0791 0.1032 0.1398 -0.0359 -0.0200 0.0170  51  TYR A CE1 
412  C  CE2 . TYR A 49  ? 0.0811 0.1126 0.0996 -0.0476 -0.0359 0.0105  51  TYR A CE2 
413  C  CZ  . TYR A 49  ? 0.0766 0.0985 0.1111 -0.0402 -0.0341 0.0134  51  TYR A CZ  
414  O  OH  . TYR A 49  ? 0.0829 0.0964 0.1125 -0.0346 -0.0336 0.0058  51  TYR A OH  
415  N  N   . ASP A 50  ? 0.0914 0.2895 0.2010 -0.0350 -0.0395 0.1069  52  ASP A N   
416  C  CA  . ASP A 50  ? 0.1172 0.3204 0.2322 0.0064  -0.0414 0.1383  52  ASP A CA  
417  C  C   . ASP A 50  ? 0.2273 0.3125 0.2152 -0.0367 -0.0776 0.1267  52  ASP A C   
418  O  O   . ASP A 50  ? 0.2564 0.3308 0.2706 -0.0644 -0.1335 0.1082  52  ASP A O   
419  C  CB  . ASP A 50  ? 0.1145 0.4767 0.2850 0.0134  -0.0580 0.1445  52  ASP A CB  
420  C  CG  . ASP A 50  ? 0.3705 0.4889 0.4387 0.1207  0.0899  0.1074  52  ASP A CG  
421  O  OD1 . ASP A 50  ? 0.5088 0.6597 0.5382 -0.0855 0.0747  0.3391  52  ASP A OD1 
422  O  OD2 . ASP A 50  ? 0.4683 0.6422 0.7812 0.3522  0.0718  0.3714  52  ASP A OD2 
423  N  N   . GLN A 51  ? 0.1341 0.3343 0.2967 -0.0314 -0.0502 0.1201  53  GLN A N   
424  C  CA  . GLN A 51  ? 0.1500 0.2524 0.3199 -0.0281 -0.0144 0.0957  53  GLN A CA  
425  C  C   . GLN A 51  ? 0.1640 0.1737 0.2002 0.0114  -0.0285 0.0332  53  GLN A C   
426  O  O   . GLN A 51  ? 0.1754 0.2423 0.2273 -0.0135 -0.0355 0.0692  53  GLN A O   
427  C  CB  . GLN A 51  ? 0.2606 0.2939 0.4662 0.0847  0.0023  0.0788  53  GLN A CB  
428  C  CG  . GLN A 51  ? 0.3007 0.7015 0.4783 0.1581  0.1284  0.1805  53  GLN A CG  
429  C  CD  . GLN A 51  ? 0.5094 0.8193 0.7417 0.3635  -0.0085 0.2022  53  GLN A CD  
430  O  OE1 . GLN A 51  ? 0.6127 1.0546 0.8209 0.5130  0.0816  0.4731  53  GLN A OE1 
431  N  NE2 . GLN A 51  ? 0.6250 1.3011 0.3622 0.2023  0.1873  0.3362  53  GLN A NE2 
432  N  N   . ALA A 52  ? 0.1507 0.1621 0.1920 -0.0229 -0.0453 0.0447  54  ALA A N   
433  C  CA  . ALA A 52  ? 0.1471 0.1298 0.1102 -0.0239 -0.0453 0.0133  54  ALA A CA  
434  C  C   . ALA A 52  ? 0.2049 0.1860 0.1120 -0.0054 -0.0552 -0.0206 54  ALA A C   
435  O  O   . ALA A 52  ? 0.2425 0.3959 0.1446 -0.0693 -0.0685 -0.0724 54  ALA A O   
436  C  CB  . ALA A 52  ? 0.1977 0.1356 0.1949 0.0469  -0.0320 0.0093  54  ALA A CB  
437  N  N   A THR A 53  ? 0.1927 0.1345 0.1265 0.0061  -0.0463 0.0456  55  THR A N   
438  N  N   B THR A 53  ? 0.1995 0.1370 0.1316 0.0113  -0.0458 0.0541  55  THR A N   
439  C  CA  A THR A 53  ? 0.2103 0.1599 0.1208 0.0752  -0.0615 0.0351  55  THR A CA  
440  C  CA  B THR A 53  ? 0.2164 0.1719 0.1319 0.0886  -0.0629 0.0296  55  THR A CA  
441  C  C   A THR A 53  ? 0.1841 0.1277 0.0643 0.0297  -0.0890 0.0245  55  THR A C   
442  C  C   B THR A 53  ? 0.1913 0.1326 0.0677 0.0234  -0.0754 0.0190  55  THR A C   
443  O  O   A THR A 53  ? 0.1678 0.1155 0.0743 0.0392  -0.0560 0.0487  55  THR A O   
444  O  O   B THR A 53  ? 0.1801 0.1284 0.0840 0.0216  -0.0560 0.0388  55  THR A O   
445  C  CB  A THR A 53  ? 0.2986 0.1675 0.0434 0.0741  -0.0343 0.0436  55  THR A CB  
446  C  CB  B THR A 53  ? 0.3538 0.1944 0.1987 0.1238  -0.0631 0.0668  55  THR A CB  
447  O  OG1 A THR A 53  ? 0.2849 0.1093 0.2588 0.0462  -0.0671 0.0273  55  THR A OG1 
448  O  OG1 B THR A 53  ? 0.4577 0.2203 0.3621 0.0939  0.0083  -0.0508 55  THR A OG1 
449  C  CG2 A THR A 53  ? 0.3805 0.1956 0.1101 0.1751  0.0347  0.0694  55  THR A CG2 
450  C  CG2 B THR A 53  ? 0.3966 0.3321 0.2301 0.1288  -0.0583 -0.0197 55  THR A CG2 
451  N  N   . SER A 54  ? 0.2009 0.1127 0.0844 0.0187  -0.0582 0.0289  56  SER A N   
452  C  CA  . SER A 54  ? 0.2196 0.1067 0.0988 0.0346  -0.0280 0.0200  56  SER A CA  
453  C  C   . SER A 54  ? 0.2865 0.1467 0.0697 0.0688  -0.0507 0.0462  56  SER A C   
454  O  O   . SER A 54  ? 0.2985 0.1406 0.1306 0.0559  -0.0998 0.0252  56  SER A O   
455  C  CB  . SER A 54  ? 0.2812 0.1212 0.0364 0.0271  -0.0817 0.0061  56  SER A CB  
456  O  OG  . SER A 54  ? 0.2527 0.1435 0.0837 0.0252  -0.1000 -0.0030 56  SER A OG  
457  N  N   . LEU A 55  ? 0.2879 0.1205 0.0734 0.0829  0.0206  0.0465  57  LEU A N   
458  C  CA  . LEU A 55  ? 0.3388 0.1568 0.1374 0.0952  0.0539  0.0968  57  LEU A CA  
459  C  C   . LEU A 55  ? 0.2723 0.1238 0.0794 0.0522  0.0201  0.0771  57  LEU A C   
460  O  O   . LEU A 55  ? 0.3225 0.2005 0.0750 0.0702  0.0077  0.0877  57  LEU A O   
461  C  CB  . LEU A 55  ? 0.4338 0.1650 0.1506 0.0502  0.0989  0.0891  57  LEU A CB  
462  C  CG  . LEU A 55  ? 0.6039 0.1855 0.2041 0.0999  -0.0161 -0.0155 57  LEU A CG  
463  C  CD1 . LEU A 55  ? 0.7769 0.1065 0.2528 -0.1293 0.1892  0.0175  57  LEU A CD1 
464  C  CD2 . LEU A 55  ? 0.8887 0.2515 0.2056 0.1814  -0.0610 0.0402  57  LEU A CD2 
465  N  N   . ARG A 56  ? 0.2582 0.1330 0.1067 0.0716  0.0207  0.0454  58  ARG A N   
466  C  CA  . ARG A 56  ? 0.1955 0.1007 0.1058 0.0284  0.0150  0.0539  58  ARG A CA  
467  C  C   . ARG A 56  ? 0.2328 0.0795 0.0537 -0.0156 0.0055  0.0411  58  ARG A C   
468  O  O   . ARG A 56  ? 0.2240 0.1313 0.0495 0.0185  0.0211  0.0298  58  ARG A O   
469  C  CB  . ARG A 56  ? 0.1854 0.1467 0.1137 0.0200  -0.0087 0.0653  58  ARG A CB  
470  C  CG  . ARG A 56  ? 0.1453 0.1654 0.2178 -0.0265 0.0400  0.0661  58  ARG A CG  
471  C  CD  . ARG A 56  ? 0.1399 0.2146 0.1632 -0.0617 -0.0344 0.0408  58  ARG A CD  
472  N  NE  . ARG A 56  ? 0.1251 0.1747 0.1482 -0.0156 -0.0345 0.0575  58  ARG A NE  
473  C  CZ  . ARG A 56  ? 0.1076 0.1471 0.1464 -0.0484 -0.0088 0.0601  58  ARG A CZ  
474  N  NH1 . ARG A 56  ? 0.1561 0.1434 0.1844 -0.0460 0.0160  0.0513  58  ARG A NH1 
475  N  NH2 . ARG A 56  ? 0.1126 0.1905 0.1514 -0.0163 -0.0058 0.0361  58  ARG A NH2 
476  N  N   . ILE A 57  ? 0.2577 0.0803 0.0496 0.0031  -0.0062 0.0303  59  ILE A N   
477  C  CA  . ILE A 57  ? 0.2028 0.0633 0.0425 -0.0132 -0.0126 0.0167  59  ILE A CA  
478  C  C   . ILE A 57  ? 0.1740 0.1138 0.0109 -0.0334 -0.0227 0.0013  59  ILE A C   
479  O  O   . ILE A 57  ? 0.2429 0.1646 0.0117 -0.0059 -0.0196 0.0247  59  ILE A O   
480  C  CB  . ILE A 57  ? 0.1890 0.0777 0.0392 -0.0248 -0.0458 0.0316  59  ILE A CB  
481  C  CG1 . ILE A 57  ? 0.1985 0.0917 0.0557 -0.0179 -0.0387 0.0461  59  ILE A CG1 
482  C  CG2 . ILE A 57  ? 0.2291 0.1170 0.0443 -0.0121 -0.0779 0.0177  59  ILE A CG2 
483  C  CD1 . ILE A 57  ? 0.2354 0.0898 0.0718 -0.0160 -0.0344 -0.0033 59  ILE A CD1 
484  N  N   . LEU A 58  ? 0.1543 0.1111 0.0632 -0.0276 -0.0383 0.0148  60  LEU A N   
485  C  CA  . LEU A 58  ? 0.1640 0.0847 0.0644 -0.0264 -0.0272 0.0319  60  LEU A CA  
486  C  C   . LEU A 58  ? 0.1945 0.0646 0.0618 -0.0274 -0.0159 0.0187  60  LEU A C   
487  O  O   . LEU A 58  ? 0.1485 0.0863 0.0628 -0.0398 -0.0062 0.0296  60  LEU A O   
488  C  CB  . LEU A 58  ? 0.1701 0.0628 0.1615 -0.0232 -0.0299 0.0181  60  LEU A CB  
489  C  CG  . LEU A 58  ? 0.1654 0.0688 0.1273 -0.0114 -0.0229 0.0071  60  LEU A CG  
490  C  CD1 . LEU A 58  ? 0.1725 0.1224 0.1420 -0.0475 -0.0025 0.0391  60  LEU A CD1 
491  C  CD2 . LEU A 58  ? 0.2031 0.0944 0.1467 -0.0502 -0.0115 -0.0078 60  LEU A CD2 
492  N  N   . ASN A 59  ? 0.2098 0.0782 0.0364 -0.0408 -0.0022 0.0111  61  ASN A N   
493  C  CA  . ASN A 59  ? 0.2031 0.0688 0.0408 -0.0321 -0.0006 -0.0089 61  ASN A CA  
494  C  C   . ASN A 59  ? 0.2045 0.1110 0.0425 -0.0418 0.0032  0.0011  61  ASN A C   
495  O  O   . ASN A 59  ? 0.1974 0.1007 0.1074 -0.0601 0.0160  0.0242  61  ASN A O   
496  C  CB  . ASN A 59  ? 0.2171 0.0775 0.0874 -0.0344 0.0396  -0.0227 61  ASN A CB  
497  C  CG  . ASN A 59  ? 0.2010 0.0864 0.0364 -0.0260 0.0275  -0.0103 61  ASN A CG  
498  O  OD1 . ASN A 59  ? 0.2145 0.1101 0.0606 -0.0304 0.0245  -0.0006 61  ASN A OD1 
499  N  ND2 . ASN A 59  ? 0.2351 0.0891 0.0584 -0.0417 0.0653  -0.0166 61  ASN A ND2 
500  N  N   . ASN A 60  ? 0.2121 0.0971 0.0472 -0.0606 -0.0113 -0.0026 62  ASN A N   
501  C  CA  . ASN A 60  ? 0.2257 0.0803 0.1242 -0.0682 -0.0273 0.0172  62  ASN A CA  
502  C  C   . ASN A 60  ? 0.2159 0.1385 0.0908 -0.0640 0.0279  -0.0044 62  ASN A C   
503  O  O   . ASN A 60  ? 0.3083 0.1801 0.1589 -0.1338 0.0059  0.0117  62  ASN A O   
504  C  CB  . ASN A 60  ? 0.2649 0.0813 0.1503 -0.0292 -0.0521 0.0057  62  ASN A CB  
505  C  CG  . ASN A 60  ? 0.2436 0.0994 0.0976 -0.0162 -0.0161 -0.0402 62  ASN A CG  
506  O  OD1 . ASN A 60  ? 0.1970 0.0937 0.1014 -0.0216 0.0138  -0.0179 62  ASN A OD1 
507  N  ND2 . ASN A 60  ? 0.4162 0.1938 0.1751 0.0266  0.0937  -0.0524 62  ASN A ND2 
508  N  N   . GLY A 61  ? 0.2339 0.1367 0.0901 -0.0325 0.0461  0.0049  63  GLY A N   
509  C  CA  . GLY A 61  ? 0.1550 0.1403 0.1066 -0.0748 0.0658  0.0001  63  GLY A CA  
510  C  C   . GLY A 61  ? 0.1160 0.1164 0.1180 -0.0514 0.0457  -0.0085 63  GLY A C   
511  O  O   . GLY A 61  ? 0.1399 0.1575 0.1406 -0.0092 0.0392  -0.0179 63  GLY A O   
512  N  N   A HIS A 62  ? 0.1356 0.1068 0.0901 -0.0253 0.0549  0.0287  64  HIS A N   
513  N  N   B HIS A 62  ? 0.1532 0.1187 0.0734 -0.0044 0.0500  0.0234  64  HIS A N   
514  C  CA  A HIS A 62  ? 0.1238 0.0982 0.0899 -0.0421 0.0253  0.0294  64  HIS A CA  
515  C  CA  B HIS A 62  ? 0.1599 0.1672 0.1136 -0.0374 0.0416  0.0688  64  HIS A CA  
516  C  C   A HIS A 62  ? 0.1014 0.0923 0.0867 -0.0256 0.0094  0.0306  64  HIS A C   
517  C  C   B HIS A 62  ? 0.1161 0.1058 0.1291 -0.0208 -0.0080 0.0418  64  HIS A C   
518  O  O   A HIS A 62  ? 0.1037 0.1464 0.2035 -0.0289 -0.0025 0.1202  64  HIS A O   
519  O  O   B HIS A 62  ? 0.1478 0.2056 0.2814 0.0309  0.0234  0.1681  64  HIS A O   
520  C  CB  A HIS A 62  ? 0.0888 0.1331 0.0770 -0.0157 0.0399  0.0096  64  HIS A CB  
521  C  CB  B HIS A 62  ? 0.1349 0.1955 0.1650 -0.0179 -0.0296 0.0858  64  HIS A CB  
522  C  CG  A HIS A 62  ? 0.1332 0.1313 0.1194 -0.0567 -0.0033 -0.0026 64  HIS A CG  
523  C  CG  B HIS A 62  ? 0.1747 0.2603 0.0898 0.0140  -0.0595 0.0147  64  HIS A CG  
524  N  ND1 A HIS A 62  ? 0.1187 0.2404 0.1363 -0.0507 0.0308  -0.0616 64  HIS A ND1 
525  N  ND1 B HIS A 62  ? 0.1428 0.2761 0.0899 0.0176  -0.0274 -0.0392 64  HIS A ND1 
526  C  CD2 A HIS A 62  ? 0.1801 0.1294 0.1216 -0.0800 0.0357  -0.0177 64  HIS A CD2 
527  C  CD2 B HIS A 62  ? 0.1837 0.1877 0.1506 0.0695  -0.0457 0.0005  64  HIS A CD2 
528  C  CE1 A HIS A 62  ? 0.1253 0.2742 0.0810 -0.0802 0.0271  -0.0508 64  HIS A CE1 
529  C  CE1 B HIS A 62  ? 0.2406 0.2121 0.0337 0.0352  -0.0512 -0.0251 64  HIS A CE1 
530  N  NE2 A HIS A 62  ? 0.1755 0.2056 0.1647 -0.0774 0.0366  -0.0430 64  HIS A NE2 
531  N  NE2 B HIS A 62  ? 0.3127 0.1482 0.0785 0.0498  -0.0779 0.0504  64  HIS A NE2 
532  N  N   . ALA A 63  ? 0.1384 0.0979 0.0452 0.0039  0.0170  0.0091  65  ALA A N   
533  C  CA  . ALA A 63  ? 0.1435 0.0935 0.0610 -0.0073 0.0026  0.0035  65  ALA A CA  
534  C  C   . ALA A 63  ? 0.1521 0.0714 0.0241 0.0012  0.0177  -0.0068 65  ALA A C   
535  O  O   . ALA A 63  ? 0.1503 0.1014 0.0864 -0.0359 0.0379  -0.0035 65  ALA A O   
536  C  CB  . ALA A 63  ? 0.1284 0.1794 0.0417 0.0104  -0.0047 0.0168  65  ALA A CB  
537  N  N   . PHE A 64  ? 0.1406 0.0529 0.0627 0.0054  0.0138  0.0020  66  PHE A N   
538  C  CA  . PHE A 64  ? 0.1668 0.0697 0.0524 -0.0159 -0.0164 0.0111  66  PHE A CA  
539  C  C   . PHE A 64  ? 0.1812 0.0794 0.0142 -0.0043 -0.0219 0.0190  66  PHE A C   
540  O  O   . PHE A 64  ? 0.1884 0.0794 0.0158 -0.0194 -0.0179 0.0147  66  PHE A O   
541  C  CB  . PHE A 64  ? 0.1758 0.1171 0.0547 -0.0456 -0.0078 -0.0027 66  PHE A CB  
542  C  CG  . PHE A 64  ? 0.1356 0.0993 0.0399 -0.0189 -0.0318 -0.0186 66  PHE A CG  
543  C  CD1 . PHE A 64  ? 0.1398 0.1446 0.0098 -0.0190 -0.0212 0.0062  66  PHE A CD1 
544  C  CD2 . PHE A 64  ? 0.1661 0.0937 0.0373 -0.0162 0.0037  -0.0204 66  PHE A CD2 
545  C  CE1 . PHE A 64  ? 0.1066 0.1194 0.0615 -0.0086 -0.0431 0.0121  66  PHE A CE1 
546  C  CE2 . PHE A 64  ? 0.1474 0.1190 0.0384 -0.0256 -0.0242 -0.0111 66  PHE A CE2 
547  C  CZ  . PHE A 64  ? 0.1492 0.1118 0.0355 -0.0175 -0.0439 -0.0093 66  PHE A CZ  
548  N  N   . ASN A 65  ? 0.1253 0.0694 0.0423 -0.0002 -0.0160 0.0154  67  ASN A N   
549  C  CA  . ASN A 65  ? 0.1459 0.0714 0.0427 -0.0163 -0.0193 -0.0084 67  ASN A CA  
550  C  C   . ASN A 65  ? 0.1474 0.0625 0.0154 -0.0201 -0.0106 0.0111  67  ASN A C   
551  O  O   . ASN A 65  ? 0.1860 0.1241 0.0241 -0.0487 -0.0134 0.0340  67  ASN A O   
552  C  CB  . ASN A 65  ? 0.1471 0.0758 0.0786 -0.0314 -0.0329 0.0195  67  ASN A CB  
553  C  CG  . ASN A 65  ? 0.1471 0.0590 0.0827 -0.0287 -0.0295 0.0024  67  ASN A CG  
554  O  OD1 . ASN A 65  ? 0.1729 0.0961 0.0968 -0.0425 -0.0501 0.0403  67  ASN A OD1 
555  N  ND2 . ASN A 65  ? 0.2038 0.0820 0.1194 -0.0635 -0.0326 -0.0041 67  ASN A ND2 
556  N  N   . VAL A 66  ? 0.1298 0.0487 0.0380 -0.0018 -0.0047 0.0185  68  VAL A N   
557  C  CA  . VAL A 66  ? 0.1514 0.0926 0.0329 0.0291  -0.0177 0.0282  68  VAL A CA  
558  C  C   . VAL A 66  ? 0.1805 0.0971 0.0355 0.0039  -0.0260 0.0292  68  VAL A C   
559  O  O   . VAL A 66  ? 0.1636 0.0664 0.0369 0.0085  -0.0255 0.0163  68  VAL A O   
560  C  CB  . VAL A 66  ? 0.1332 0.0864 0.1120 0.0424  -0.0370 -0.0113 68  VAL A CB  
561  C  CG1 . VAL A 66  ? 0.1146 0.1535 0.0951 0.0253  -0.0668 0.0238  68  VAL A CG1 
562  C  CG2 . VAL A 66  ? 0.1313 0.0998 0.0844 0.0095  -0.0367 -0.0339 68  VAL A CG2 
563  N  N   . GLU A 67  ? 0.2495 0.0794 0.0390 0.0296  0.0148  0.0236  69  GLU A N   
564  C  CA  . GLU A 67  ? 0.2230 0.0894 0.0718 0.0155  0.0223  0.0176  69  GLU A CA  
565  C  C   . GLU A 67  ? 0.2748 0.0943 0.0908 0.0678  -0.0228 0.0226  69  GLU A C   
566  O  O   . GLU A 67  ? 0.2631 0.0838 0.1084 0.0424  -0.0414 0.0223  69  GLU A O   
567  C  CB  . GLU A 67  ? 0.1535 0.1553 0.1442 0.0163  0.0155  0.0447  69  GLU A CB  
568  C  CG  . GLU A 67  ? 0.1128 0.1273 0.1337 -0.0369 0.0285  0.0271  69  GLU A CG  
569  C  CD  . GLU A 67  ? 0.1647 0.0970 0.1410 -0.0460 0.0238  0.0490  69  GLU A CD  
570  O  OE1 . GLU A 67  ? 0.1702 0.1205 0.1610 -0.0186 -0.0025 0.0525  69  GLU A OE1 
571  O  OE2 . GLU A 67  ? 0.1535 0.1441 0.1859 -0.0358 0.0197  0.0365  69  GLU A OE2 
572  N  N   . PHE A 68  ? 0.1564 0.1117 0.0637 0.0187  0.0118  0.0172  70  PHE A N   
573  C  CA  . PHE A 68  ? 0.1377 0.0865 0.0822 0.0146  -0.0252 0.0302  70  PHE A CA  
574  C  C   . PHE A 68  ? 0.1970 0.0978 0.0891 0.0006  -0.0465 0.0229  70  PHE A C   
575  O  O   . PHE A 68  ? 0.1733 0.0883 0.1038 0.0152  -0.0190 0.0425  70  PHE A O   
576  C  CB  . PHE A 68  ? 0.1597 0.0900 0.0593 0.0097  -0.0262 0.0193  70  PHE A CB  
577  C  CG  . PHE A 68  ? 0.1411 0.0935 0.0635 0.0072  -0.0285 0.0357  70  PHE A CG  
578  C  CD1 . PHE A 68  ? 0.1852 0.1101 0.0469 0.0242  -0.0170 0.0430  70  PHE A CD1 
579  C  CD2 . PHE A 68  ? 0.1485 0.1093 0.0593 0.0004  -0.0384 0.0296  70  PHE A CD2 
580  C  CE1 . PHE A 68  ? 0.1704 0.1305 0.0838 0.0065  -0.0021 0.0212  70  PHE A CE1 
581  C  CE2 . PHE A 68  ? 0.1744 0.0993 0.0505 0.0085  -0.0231 0.0433  70  PHE A CE2 
582  C  CZ  . PHE A 68  ? 0.1793 0.1101 0.0558 0.0165  -0.0095 0.0204  70  PHE A CZ  
583  N  N   . ASP A 69  ? 0.2347 0.0793 0.1115 0.0119  -0.0632 0.0442  71  ASP A N   
584  C  CA  . ASP A 69  ? 0.1834 0.0730 0.1392 0.0377  -0.0283 0.0358  71  ASP A CA  
585  C  C   . ASP A 69  ? 0.1909 0.0496 0.1696 0.0092  -0.0006 0.0183  71  ASP A C   
586  O  O   . ASP A 69  ? 0.2153 0.1342 0.2822 -0.0253 0.0157  0.0269  71  ASP A O   
587  C  CB  . ASP A 69  ? 0.2799 0.1223 0.2854 0.0398  -0.1534 0.0298  71  ASP A CB  
588  C  CG  . ASP A 69  ? 0.4625 0.0942 0.3251 -0.0324 -0.1741 0.0709  71  ASP A CG  
589  O  OD1 . ASP A 69  ? 0.3125 0.0688 0.3563 0.0165  -0.0883 0.0609  71  ASP A OD1 
590  O  OD2 . ASP A 69  ? 0.5086 0.2092 0.7127 0.0555  -0.2535 0.1424  71  ASP A OD2 
591  N  N   . ASP A 70  ? 0.1794 0.0680 0.1761 0.0089  -0.0289 0.0403  72  ASP A N   
592  C  CA  . ASP A 70  ? 0.1773 0.0628 0.1930 -0.0086 0.0115  0.0372  72  ASP A CA  
593  C  C   . ASP A 70  ? 0.2282 0.0671 0.2730 0.0275  0.0321  0.0421  72  ASP A C   
594  O  O   . ASP A 70  ? 0.3129 0.1115 0.2520 -0.0287 0.0201  0.0179  72  ASP A O   
595  C  CB  . ASP A 70  ? 0.1621 0.0914 0.1916 -0.0220 0.0174  0.0579  72  ASP A CB  
596  C  CG  . ASP A 70  ? 0.1733 0.1306 0.2024 -0.0179 0.0164  0.0556  72  ASP A CG  
597  O  OD1 . ASP A 70  ? 0.1945 0.2566 0.1941 -0.0293 -0.0423 0.1168  72  ASP A OD1 
598  O  OD2 . ASP A 70  ? 0.1998 0.2170 0.1535 -0.0306 -0.0044 0.0279  72  ASP A OD2 
599  N  N   . SER A 71  ? 0.2301 0.0779 0.2483 0.0125  0.0188  0.0403  73  SER A N   
600  C  CA  . SER A 71  ? 0.2567 0.0766 0.2879 0.0062  0.0712  0.0511  73  SER A CA  
601  C  C   . SER A 71  ? 0.3114 0.1128 0.4153 -0.0293 0.1358  -0.0606 73  SER A C   
602  O  O   . SER A 71  ? 0.3734 0.0854 0.2983 0.0172  -0.0196 0.0359  73  SER A O   
603  C  CB  . SER A 71  ? 0.4152 0.1722 0.2976 -0.0093 0.0463  0.0834  73  SER A CB  
604  O  OG  . SER A 71  ? 0.3477 0.0989 0.3044 0.0200  0.0622  0.0807  73  SER A OG  
605  N  N   . GLN A 72  ? 0.1658 0.1575 0.5827 0.0307  0.0444  0.0209  74  GLN A N   
606  C  CA  . GLN A 72  ? 0.2887 0.2393 0.4404 0.0197  0.1258  0.0665  74  GLN A CA  
607  C  C   . GLN A 72  ? 0.2912 0.2466 0.2106 0.0819  0.0374  -0.0055 74  GLN A C   
608  O  O   . GLN A 72  ? 0.1963 0.1575 0.1987 0.0037  -0.0846 0.0257  74  GLN A O   
609  C  CB  . GLN A 72  ? 0.2843 0.3481 0.3758 0.1561  0.1175  0.1270  74  GLN A CB  
610  C  CG  . GLN A 72  ? 0.3679 0.3483 0.5279 0.0941  0.0367  0.1873  74  GLN A CG  
611  C  CD  . GLN A 72  ? 0.4203 0.1686 0.5405 -0.0521 0.1524  0.0794  74  GLN A CD  
612  O  OE1 . GLN A 72  ? 0.3779 0.5383 0.7198 0.1150  -0.0307 0.3190  74  GLN A OE1 
613  N  NE2 . GLN A 72  ? 0.9832 0.6948 0.4656 -0.1711 0.2357  -0.0184 74  GLN A NE2 
614  N  N   . ASP A 73  ? 0.3446 0.2329 0.3129 -0.0434 0.1112  -0.0753 75  ASP A N   
615  C  CA  . ASP A 73  ? 0.2745 0.2099 0.2955 -0.0570 0.0012  -0.0835 75  ASP A CA  
616  C  C   . ASP A 73  ? 0.2881 0.2387 0.4501 -0.0425 -0.0894 -0.0819 75  ASP A C   
617  O  O   . ASP A 73  ? 0.3132 0.4162 0.3725 -0.0053 -0.1068 0.0237  75  ASP A O   
618  C  CB  . ASP A 73  ? 0.2577 0.3114 0.2697 0.0122  0.0269  -0.0295 75  ASP A CB  
619  C  CG  . ASP A 73  ? 0.3592 0.2879 0.4390 0.1217  0.1532  0.1614  75  ASP A CG  
620  O  OD1 . ASP A 73  ? 0.3298 0.2734 0.6158 0.1243  -0.1286 0.1578  75  ASP A OD1 
621  O  OD2 . ASP A 73  ? 0.4652 0.4295 0.4670 0.0208  0.2457  -0.0501 75  ASP A OD2 
622  N  N   . LYS A 74  ? 0.2477 0.1768 0.2127 -0.0582 -0.0960 0.0829  76  LYS A N   
623  C  CA  . LYS A 74  ? 0.2769 0.1834 0.3452 -0.0502 -0.0675 0.0748  76  LYS A CA  
624  C  C   . LYS A 74  ? 0.5363 0.1223 0.3518 0.0179  -0.1088 0.0282  76  LYS A C   
625  O  O   . LYS A 74  ? 0.5853 0.3919 0.2992 0.1544  -0.0225 0.0731  76  LYS A O   
626  C  CB  . LYS A 74  ? 0.4006 0.1263 0.2981 -0.1133 -0.1659 0.0655  76  LYS A CB  
627  C  CG  . LYS A 74  ? 0.8449 0.1923 0.3301 0.0189  -0.1967 0.0467  76  LYS A CG  
628  C  CD  . LYS A 74  ? 1.0088 0.1607 0.3025 -0.1983 -0.1313 0.0334  76  LYS A CD  
629  C  CE  . LYS A 74  ? 0.6725 0.2284 0.5437 -0.0372 0.0542  0.1139  76  LYS A CE  
630  N  NZ  . LYS A 74  ? 0.7542 0.4588 0.4478 0.2978  0.1285  0.2216  76  LYS A NZ  
631  N  N   . ALA A 75  ? 0.3558 0.2304 0.3908 -0.0495 -0.2681 0.0131  77  ALA A N   
632  C  CA  . ALA A 75  ? 0.2847 0.2185 0.1115 -0.0421 -0.0620 0.0432  77  ALA A CA  
633  C  C   . ALA A 75  ? 0.0891 0.1593 0.1747 -0.0188 -0.0544 -0.0013 77  ALA A C   
634  O  O   . ALA A 75  ? 0.0767 0.2816 0.3061 -0.0196 -0.0617 -0.0712 77  ALA A O   
635  C  CB  . ALA A 75  ? 0.2335 0.2344 0.1162 -0.0423 -0.0670 0.0113  77  ALA A CB  
636  N  N   . VAL A 76  ? 0.1521 0.0998 0.1424 -0.0134 -0.0699 0.0478  78  VAL A N   
637  C  CA  . VAL A 76  ? 0.1880 0.0888 0.1377 0.0011  -0.0835 0.0443  78  VAL A CA  
638  C  C   . VAL A 76  ? 0.1013 0.0716 0.1859 -0.0065 -0.0797 0.0518  78  VAL A C   
639  O  O   . VAL A 76  ? 0.1238 0.0995 0.2103 -0.0341 -0.0930 0.0233  78  VAL A O   
640  C  CB  . VAL A 76  ? 0.3259 0.0855 0.2121 0.0020  -0.1130 0.0293  78  VAL A CB  
641  C  CG1 . VAL A 76  ? 0.3722 0.0694 0.2983 -0.0280 -0.1465 0.0604  78  VAL A CG1 
642  C  CG2 . VAL A 76  ? 0.3055 0.2444 0.2372 0.0304  0.0460  0.0458  78  VAL A CG2 
643  N  N   . LEU A 77  ? 0.0933 0.0803 0.1316 0.0279  -0.0507 0.0206  79  LEU A N   
644  C  CA  . LEU A 77  ? 0.1084 0.0660 0.1305 -0.0250 -0.0402 0.0110  79  LEU A CA  
645  C  C   . LEU A 77  ? 0.0932 0.0863 0.1108 -0.0396 -0.0154 0.0125  79  LEU A C   
646  O  O   . LEU A 77  ? 0.1005 0.1248 0.1284 -0.0567 -0.0074 -0.0106 79  LEU A O   
647  C  CB  . LEU A 77  ? 0.0849 0.1097 0.1395 -0.0155 -0.0267 0.0410  79  LEU A CB  
648  C  CG  . LEU A 77  ? 0.1027 0.1067 0.1424 -0.0011 -0.0173 0.0337  79  LEU A CG  
649  C  CD1 . LEU A 77  ? 0.1216 0.0905 0.3058 -0.0038 0.0071  0.0538  79  LEU A CD1 
650  C  CD2 . LEU A 77  ? 0.1145 0.1137 0.1198 0.0223  0.0053  0.0145  79  LEU A CD2 
651  N  N   . LYS A 78  ? 0.0944 0.1233 0.1233 -0.0365 -0.0015 0.0044  80  LYS A N   
652  C  CA  . LYS A 78  ? 0.1309 0.0998 0.1528 0.0019  0.0201  -0.0006 80  LYS A CA  
653  C  C   . LYS A 78  ? 0.0743 0.1144 0.1263 -0.0075 -0.0047 -0.0027 80  LYS A C   
654  O  O   . LYS A 78  ? 0.0928 0.1076 0.1413 -0.0144 -0.0080 0.0041  80  LYS A O   
655  C  CB  . LYS A 78  ? 0.1690 0.1224 0.1938 0.0175  0.0292  0.0267  80  LYS A CB  
656  C  CG  . LYS A 78  ? 0.1575 0.1331 0.3044 0.0113  0.0280  0.0442  80  LYS A CG  
657  C  CD  . LYS A 78  ? 0.2864 0.1492 0.4543 0.0502  -0.0527 0.0694  80  LYS A CD  
658  C  CE  . LYS A 78  ? 0.3708 0.3010 0.5687 0.0759  0.0804  0.0883  80  LYS A CE  
659  N  N   . GLY A 79  ? 0.1262 0.1344 0.1284 0.0064  0.0148  -0.0034 81  GLY A N   
660  C  CA  . GLY A 79  ? 0.1155 0.1464 0.1676 0.0294  0.0218  0.0342  81  GLY A CA  
661  C  C   . GLY A 79  ? 0.1111 0.1126 0.1431 0.0119  0.0326  0.0046  81  GLY A C   
662  O  O   . GLY A 79  ? 0.1040 0.1203 0.1417 -0.0104 0.0059  -0.0102 81  GLY A O   
663  N  N   . GLY A 80  ? 0.1163 0.1150 0.2376 -0.0078 -0.0016 0.0432  82  GLY A N   
664  C  CA  . GLY A 80  ? 0.1690 0.1171 0.2513 0.0305  -0.0189 0.0197  82  GLY A CA  
665  C  C   . GLY A 80  ? 0.1435 0.1352 0.1654 0.0540  0.0322  0.0102  82  GLY A C   
666  O  O   . GLY A 80  ? 0.2272 0.2569 0.1919 0.1082  0.0550  -0.0179 82  GLY A O   
667  N  N   . PRO A 81  ? 0.1521 0.1244 0.1492 0.0536  0.0254  -0.0012 83  PRO A N   
668  C  CA  . PRO A 81  ? 0.1999 0.1273 0.0942 0.0812  0.0065  -0.0055 83  PRO A CA  
669  C  C   . PRO A 81  ? 0.1786 0.1514 0.1395 0.0637  0.0160  -0.0278 83  PRO A C   
670  O  O   . PRO A 81  ? 0.1840 0.2213 0.1848 0.0539  -0.0133 -0.0480 83  PRO A O   
671  C  CB  . PRO A 81  ? 0.1901 0.1926 0.1143 0.0855  -0.0138 -0.0283 83  PRO A CB  
672  C  CG  . PRO A 81  ? 0.1270 0.1223 0.1097 0.0369  -0.0034 -0.0193 83  PRO A CG  
673  C  CD  . PRO A 81  ? 0.1040 0.0829 0.1629 0.0129  0.0435  -0.0072 83  PRO A CD  
674  N  N   . LEU A 82  ? 0.1653 0.0986 0.1363 0.0500  0.0328  -0.0054 84  LEU A N   
675  C  CA  . LEU A 82  ? 0.1581 0.0584 0.1485 0.0143  -0.0087 -0.0383 84  LEU A CA  
676  C  C   . LEU A 82  ? 0.1567 0.0876 0.2121 0.0456  -0.0168 -0.0490 84  LEU A C   
677  O  O   . LEU A 82  ? 0.1629 0.1388 0.2256 0.0504  -0.0134 -0.0943 84  LEU A O   
678  C  CB  . LEU A 82  ? 0.1145 0.0759 0.1478 0.0314  0.0114  -0.0298 84  LEU A CB  
679  C  CG  . LEU A 82  ? 0.0786 0.0650 0.1338 0.0218  0.0073  -0.0209 84  LEU A CG  
680  C  CD1 . LEU A 82  ? 0.1460 0.1073 0.1230 0.0150  0.0051  0.0173  84  LEU A CD1 
681  C  CD2 . LEU A 82  ? 0.0804 0.0897 0.1543 0.0138  0.0279  -0.0340 84  LEU A CD2 
682  N  N   A ASP A 83  ? 0.2239 0.0949 0.1758 0.0368  -0.0685 -0.1084 85  ASP A N   
683  N  N   B ASP A 83  ? 0.1854 0.0831 0.2178 0.0389  0.0043  -0.1112 85  ASP A N   
684  C  CA  A ASP A 83  ? 0.2512 0.0665 0.1713 0.0127  -0.0453 -0.0988 85  ASP A CA  
685  C  CA  B ASP A 83  ? 0.2188 0.0593 0.2329 0.0223  0.0218  -0.0636 85  ASP A CA  
686  C  C   A ASP A 83  ? 0.2619 0.1453 0.1478 0.0044  -0.0024 -0.0506 85  ASP A C   
687  C  C   B ASP A 83  ? 0.0501 0.0632 0.2036 0.0068  0.0100  -0.0802 85  ASP A C   
688  O  O   A ASP A 83  ? 0.3317 0.1793 0.1930 0.0097  -0.0043 -0.0785 85  ASP A O   
689  O  O   B ASP A 83  ? 0.0625 0.1787 0.2820 0.0556  0.0511  -0.0633 85  ASP A O   
690  C  CB  A ASP A 83  ? 0.2013 0.1320 0.1690 -0.0166 -0.0394 -0.0937 85  ASP A CB  
691  C  CB  B ASP A 83  ? 0.1873 0.0786 0.2426 0.0296  0.0104  -0.0471 85  ASP A CB  
692  C  CG  A ASP A 83  ? 0.1852 0.1332 0.2247 -0.0005 -0.0259 -0.1538 85  ASP A CG  
693  C  CG  B ASP A 83  ? 0.2797 0.2640 0.2778 -0.0032 0.0074  0.0267  85  ASP A CG  
694  O  OD1 A ASP A 83  ? 0.1967 0.1733 0.1995 -0.0718 -0.0660 -0.0850 85  ASP A OD1 
695  O  OD1 B ASP A 83  ? 0.3383 0.3855 0.1352 -0.0465 0.0612  -0.0223 85  ASP A OD1 
696  O  OD2 A ASP A 83  ? 0.3459 0.2107 0.2977 -0.0429 -0.1326 -0.1020 85  ASP A OD2 
697  O  OD2 B ASP A 83  ? 0.1962 0.3927 0.2858 -0.0862 0.0534  0.0989  85  ASP A OD2 
698  N  N   A GLY A 84  ? 0.2624 0.1251 0.1722 -0.0111 0.0500  -0.0767 86  GLY A N   
699  N  N   B GLY A 84  ? 0.0950 0.0650 0.1944 0.0155  -0.0431 -0.0567 86  GLY A N   
700  C  CA  A GLY A 84  ? 0.2741 0.2401 0.1190 -0.0414 -0.0005 -0.0414 86  GLY A CA  
701  C  CA  B GLY A 84  ? 0.1502 0.0671 0.2103 0.0190  0.0359  -0.0240 86  GLY A CA  
702  C  C   A GLY A 84  ? 0.2221 0.1805 0.1514 -0.0583 0.0010  -0.0430 86  GLY A C   
703  C  C   B GLY A 84  ? 0.1252 0.1288 0.2164 -0.0066 0.0253  -0.0361 86  GLY A C   
704  O  O   A GLY A 84  ? 0.2967 0.1708 0.1510 -0.0522 -0.0149 -0.0524 86  GLY A O   
705  O  O   B GLY A 84  ? 0.1902 0.1826 0.2638 -0.0611 0.0344  -0.0323 86  GLY A O   
706  N  N   A THR A 85  ? 0.1678 0.1607 0.1453 0.0110  0.0238  -0.0476 87  THR A N   
707  N  N   B THR A 85  ? 0.1230 0.1067 0.1579 0.0328  -0.0057 -0.0294 87  THR A N   
708  C  CA  A THR A 85  ? 0.1331 0.2196 0.1791 0.0298  0.0055  -0.0617 87  THR A CA  
709  C  CA  B THR A 85  ? 0.1127 0.1190 0.1593 0.0271  0.0000  -0.0251 87  THR A CA  
710  C  C   A THR A 85  ? 0.0689 0.0883 0.1790 0.0049  -0.0298 -0.0531 87  THR A C   
711  C  C   B THR A 85  ? 0.0530 0.0752 0.1805 -0.0009 -0.0248 -0.0405 87  THR A C   
712  O  O   A THR A 85  ? 0.1055 0.0864 0.1654 -0.0081 -0.0166 -0.0403 87  THR A O   
713  O  O   B THR A 85  ? 0.0845 0.0571 0.1878 -0.0049 -0.0003 -0.0392 87  THR A O   
714  C  CB  A THR A 85  ? 0.1794 0.2633 0.2563 0.0870  0.0264  -0.0461 87  THR A CB  
715  C  CB  B THR A 85  ? 0.1242 0.0995 0.1338 0.0042  -0.0081 -0.0091 87  THR A CB  
716  O  OG1 A THR A 85  ? 0.1129 0.2694 0.3579 0.0769  -0.0034 -0.0763 87  THR A OG1 
717  O  OG1 B THR A 85  ? 0.2013 0.0761 0.1676 0.0208  -0.0042 0.0369  87  THR A OG1 
718  C  CG2 A THR A 85  ? 0.2370 0.1507 0.2674 0.1300  0.0536  -0.0610 87  THR A CG2 
719  C  CG2 B THR A 85  ? 0.2098 0.1702 0.1288 0.0323  0.0428  -0.0637 87  THR A CG2 
720  N  N   . TYR A 86  ? 0.0608 0.0713 0.1410 0.0018  -0.0230 -0.0265 88  TYR A N   
721  C  CA  . TYR A 86  ? 0.0934 0.0628 0.0934 0.0133  -0.0081 -0.0121 88  TYR A CA  
722  C  C   . TYR A 86  ? 0.0810 0.0540 0.1136 0.0046  -0.0332 -0.0044 88  TYR A C   
723  O  O   . TYR A 86  ? 0.0959 0.1403 0.1628 -0.0409 -0.0479 0.0377  88  TYR A O   
724  C  CB  . TYR A 86  ? 0.0682 0.0461 0.1090 -0.0120 -0.0206 -0.0079 88  TYR A CB  
725  C  CG  . TYR A 86  ? 0.0713 0.0409 0.0964 0.0092  -0.0150 -0.0097 88  TYR A CG  
726  C  CD1 . TYR A 86  ? 0.0883 0.0876 0.0961 0.0278  -0.0166 0.0009  88  TYR A CD1 
727  C  CD2 . TYR A 86  ? 0.0761 0.0251 0.0881 0.0174  -0.0287 0.0135  88  TYR A CD2 
728  C  CE1 . TYR A 86  ? 0.0750 0.0926 0.1151 0.0108  -0.0057 -0.0095 88  TYR A CE1 
729  C  CE2 . TYR A 86  ? 0.0829 0.0452 0.0804 -0.0061 -0.0166 -0.0104 88  TYR A CE2 
730  C  CZ  . TYR A 86  ? 0.0721 0.0396 0.0910 -0.0025 -0.0209 -0.0201 88  TYR A CZ  
731  O  OH  . TYR A 86  ? 0.0973 0.0653 0.0952 0.0025  -0.0226 -0.0197 88  TYR A OH  
732  N  N   . ARG A 87  ? 0.0817 0.0582 0.1111 0.0160  -0.0273 -0.0080 89  ARG A N   
733  C  CA  . ARG A 87  ? 0.1161 0.0373 0.1007 0.0044  -0.0423 0.0125  89  ARG A CA  
734  C  C   . ARG A 87  ? 0.0662 0.0619 0.0502 -0.0039 -0.0302 0.0274  89  ARG A C   
735  O  O   . ARG A 87  ? 0.0687 0.0553 0.0734 -0.0061 -0.0223 0.0161  89  ARG A O   
736  C  CB  . ARG A 87  ? 0.1841 0.0686 0.1255 -0.0239 -0.0571 0.0425  89  ARG A CB  
737  C  CG  . ARG A 87  ? 0.2737 0.1109 0.1159 -0.0128 -0.0734 0.0267  89  ARG A CG  
738  C  CD  . ARG A 87  ? 0.2508 0.1029 0.2063 0.0505  0.0122  0.0610  89  ARG A CD  
739  N  NE  . ARG A 87  ? 0.2727 0.1076 0.1406 0.0569  -0.0597 0.0389  89  ARG A NE  
740  C  CZ  . ARG A 87  ? 0.2466 0.1076 0.1650 0.0106  -0.0198 0.0160  89  ARG A CZ  
741  N  NH1 . ARG A 87  ? 0.2458 0.1276 0.2522 0.0238  0.0340  0.0756  89  ARG A NH1 
742  N  NH2 . ARG A 87  ? 0.2689 0.1833 0.1798 0.0532  0.0208  0.0130  89  ARG A NH2 
743  N  N   . LEU A 88  ? 0.0813 0.0557 0.0716 -0.0067 -0.0364 0.0140  90  LEU A N   
744  C  CA  . LEU A 88  ? 0.0797 0.0632 0.0688 -0.0165 -0.0239 0.0096  90  LEU A CA  
745  C  C   . LEU A 88  ? 0.0980 0.0554 0.0756 -0.0176 -0.0221 0.0245  90  LEU A C   
746  O  O   . LEU A 88  ? 0.1247 0.0978 0.0898 0.0119  -0.0085 0.0440  90  LEU A O   
747  C  CB  . LEU A 88  ? 0.0977 0.0521 0.0838 -0.0255 -0.0221 0.0042  90  LEU A CB  
748  C  CG  . LEU A 88  ? 0.1155 0.0734 0.0662 -0.0152 -0.0390 -0.0074 90  LEU A CG  
749  C  CD1 . LEU A 88  ? 0.1783 0.0488 0.0988 0.0080  -0.0311 -0.0055 90  LEU A CD1 
750  C  CD2 . LEU A 88  ? 0.1341 0.1118 0.0862 -0.0276 -0.0591 -0.0032 90  LEU A CD2 
751  N  N   . ILE A 89  ? 0.1020 0.0452 0.0558 -0.0047 -0.0009 0.0100  91  ILE A N   
752  C  CA  . ILE A 89  ? 0.1076 0.0469 0.0619 -0.0051 -0.0017 0.0138  91  ILE A CA  
753  C  C   . ILE A 89  ? 0.0928 0.0477 0.0390 0.0010  -0.0204 0.0216  91  ILE A C   
754  O  O   . ILE A 89  ? 0.1241 0.0651 0.0339 -0.0099 -0.0310 0.0194  91  ILE A O   
755  C  CB  . ILE A 89  ? 0.1124 0.0643 0.0644 -0.0209 0.0006  0.0283  91  ILE A CB  
756  C  CG1 . ILE A 89  ? 0.1355 0.0964 0.0673 -0.0749 0.0073  0.0111  91  ILE A CG1 
757  C  CG2 . ILE A 89  ? 0.1352 0.0548 0.0734 -0.0121 -0.0020 0.0276  91  ILE A CG2 
758  C  CD1 . ILE A 89  ? 0.1428 0.1851 0.0811 -0.0983 0.0006  -0.0185 91  ILE A CD1 
759  N  N   . GLN A 90  ? 0.1101 0.0366 0.0522 -0.0083 -0.0204 0.0144  92  GLN A N   
760  C  CA  . GLN A 90  ? 0.1054 0.0320 0.0627 0.0036  0.0029  0.0231  92  GLN A CA  
761  C  C   . GLN A 90  ? 0.0996 0.0418 0.0272 -0.0027 -0.0097 0.0200  92  GLN A C   
762  O  O   . GLN A 90  ? 0.1053 0.0392 0.0250 -0.0044 -0.0135 0.0208  92  GLN A O   
763  C  CB  . GLN A 90  ? 0.1151 0.0662 0.0513 -0.0022 0.0024  0.0189  92  GLN A CB  
764  C  CG  . GLN A 90  ? 0.1446 0.0445 0.0660 -0.0058 -0.0201 0.0321  92  GLN A CG  
765  C  CD  . GLN A 90  ? 0.1285 0.0630 0.0384 -0.0025 -0.0247 0.0397  92  GLN A CD  
766  O  OE1 . GLN A 90  ? 0.1330 0.0496 0.0593 0.0053  -0.0187 0.0247  92  GLN A OE1 
767  N  NE2 . GLN A 90  ? 0.1326 0.0926 0.1550 -0.0037 -0.0196 0.0231  92  GLN A NE2 
768  N  N   . PHE A 91  ? 0.1177 0.0427 0.0319 0.0049  -0.0174 0.0111  93  PHE A N   
769  C  CA  . PHE A 91  ? 0.1124 0.0372 0.0357 -0.0089 -0.0087 0.0142  93  PHE A CA  
770  C  C   . PHE A 91  ? 0.0915 0.0424 0.0181 -0.0117 -0.0135 0.0200  93  PHE A C   
771  O  O   . PHE A 91  ? 0.1492 0.0541 0.0103 -0.0005 -0.0140 0.0112  93  PHE A O   
772  C  CB  . PHE A 91  ? 0.1068 0.0540 0.0433 -0.0276 -0.0390 0.0129  93  PHE A CB  
773  C  CG  . PHE A 91  ? 0.1142 0.0571 0.0484 -0.0107 -0.0469 0.0110  93  PHE A CG  
774  C  CD1 . PHE A 91  ? 0.1320 0.0686 0.0355 -0.0086 -0.0355 0.0019  93  PHE A CD1 
775  C  CD2 . PHE A 91  ? 0.1049 0.0885 0.0496 -0.0130 -0.0535 0.0309  93  PHE A CD2 
776  C  CE1 . PHE A 91  ? 0.1241 0.0734 0.0513 -0.0111 -0.0561 0.0192  93  PHE A CE1 
777  C  CE2 . PHE A 91  ? 0.1435 0.0732 0.0556 0.0124  -0.0580 0.0012  93  PHE A CE2 
778  C  CZ  . PHE A 91  ? 0.1442 0.0628 0.0697 0.0008  -0.0519 0.0064  93  PHE A CZ  
779  N  N   . HIS A 92  ? 0.1023 0.0250 0.0355 -0.0044 -0.0265 0.0009  94  HIS A N   
780  C  CA  . HIS A 92  ? 0.0908 0.0363 0.0250 -0.0020 -0.0135 0.0119  94  HIS A CA  
781  C  C   . HIS A 92  ? 0.0925 0.0478 0.0168 -0.0057 -0.0204 0.0165  94  HIS A C   
782  O  O   . HIS A 92  ? 0.1050 0.0380 0.0212 -0.0005 -0.0089 0.0155  94  HIS A O   
783  C  CB  . HIS A 92  ? 0.0971 0.0636 0.0215 -0.0120 -0.0284 0.0111  94  HIS A CB  
784  C  CG  . HIS A 92  ? 0.0777 0.0450 0.0163 -0.0151 -0.0092 -0.0011 94  HIS A CG  
785  N  ND1 . HIS A 92  ? 0.0677 0.0345 0.0171 -0.0155 -0.0106 0.0067  94  HIS A ND1 
786  C  CD2 . HIS A 92  ? 0.0916 0.0694 0.0153 -0.0199 -0.0272 0.0025  94  HIS A CD2 
787  C  CE1 . HIS A 92  ? 0.0971 0.0409 0.0212 -0.0126 -0.0184 0.0152  94  HIS A CE1 
788  N  NE2 . HIS A 92  ? 0.0882 0.0414 0.0109 -0.0186 -0.0044 0.0048  94  HIS A NE2 
789  N  N   . PHE A 93  ? 0.1023 0.0267 0.0339 -0.0208 -0.0156 0.0081  95  PHE A N   
790  C  CA  . PHE A 93  ? 0.0840 0.0266 0.0337 -0.0078 -0.0173 0.0075  95  PHE A CA  
791  C  C   . PHE A 93  ? 0.0822 0.0434 0.0107 -0.0102 -0.0073 0.0023  95  PHE A C   
792  O  O   . PHE A 93  ? 0.0970 0.0469 0.0241 -0.0150 -0.0058 0.0149  95  PHE A O   
793  C  CB  . PHE A 93  ? 0.0838 0.0312 0.0384 -0.0039 -0.0095 -0.0058 95  PHE A CB  
794  C  CG  . PHE A 93  ? 0.0861 0.0496 0.0206 -0.0095 -0.0198 -0.0104 95  PHE A CG  
795  C  CD1 . PHE A 93  ? 0.1093 0.0758 0.0354 -0.0041 -0.0342 0.0001  95  PHE A CD1 
796  C  CD2 . PHE A 93  ? 0.0899 0.0590 0.0530 -0.0274 -0.0197 -0.0282 95  PHE A CD2 
797  C  CE1 . PHE A 93  ? 0.1076 0.0562 0.0445 -0.0036 -0.0369 -0.0097 95  PHE A CE1 
798  C  CE2 . PHE A 93  ? 0.1080 0.0759 0.0580 0.0060  -0.0270 -0.0113 95  PHE A CE2 
799  C  CZ  . PHE A 93  ? 0.0946 0.0601 0.0575 -0.0081 -0.0330 -0.0179 95  PHE A CZ  
800  N  N   . HIS A 94  ? 0.0856 0.0384 0.0276 -0.0083 -0.0154 0.0058  96  HIS A N   
801  C  CA  . HIS A 94  ? 0.0743 0.0417 0.0162 -0.0116 -0.0116 -0.0010 96  HIS A CA  
802  C  C   . HIS A 94  ? 0.0741 0.0513 0.0337 -0.0201 -0.0194 -0.0088 96  HIS A C   
803  O  O   . HIS A 94  ? 0.0777 0.0520 0.0417 -0.0100 -0.0038 -0.0006 96  HIS A O   
804  C  CB  . HIS A 94  ? 0.0828 0.0303 0.0234 -0.0074 -0.0152 -0.0166 96  HIS A CB  
805  C  CG  . HIS A 94  ? 0.0729 0.0269 0.0097 -0.0113 -0.0072 -0.0055 96  HIS A CG  
806  N  ND1 . HIS A 94  ? 0.0743 0.0364 0.0572 -0.0208 -0.0124 -0.0034 96  HIS A ND1 
807  C  CD2 . HIS A 94  ? 0.0840 0.0231 0.0216 -0.0025 -0.0059 -0.0071 96  HIS A CD2 
808  C  CE1 . HIS A 94  ? 0.0944 0.0392 0.0364 0.0041  -0.0074 -0.0046 96  HIS A CE1 
809  N  NE2 . HIS A 94  ? 0.0829 0.0329 0.0334 -0.0106 -0.0154 0.0040  96  HIS A NE2 
810  N  N   . TRP A 95  ? 0.0696 0.0413 0.0232 -0.0222 -0.0110 -0.0006 97  TRP A N   
811  C  CA  . TRP A 95  ? 0.0925 0.0281 0.0480 -0.0039 -0.0151 -0.0082 97  TRP A CA  
812  C  C   . TRP A 95  ? 0.0873 0.0452 0.0241 -0.0127 -0.0088 -0.0022 97  TRP A C   
813  O  O   . TRP A 95  ? 0.1044 0.0443 0.0470 -0.0160 0.0084  -0.0129 97  TRP A O   
814  C  CB  . TRP A 95  ? 0.1058 0.0505 0.0326 -0.0354 -0.0050 -0.0226 97  TRP A CB  
815  C  CG  . TRP A 95  ? 0.1143 0.0470 0.0330 -0.0199 -0.0071 -0.0100 97  TRP A CG  
816  C  CD1 . TRP A 95  ? 0.1309 0.0454 0.0461 -0.0207 0.0025  -0.0131 97  TRP A CD1 
817  C  CD2 . TRP A 95  ? 0.1168 0.0558 0.0187 -0.0144 -0.0146 -0.0038 97  TRP A CD2 
818  N  NE1 . TRP A 95  ? 0.1332 0.0497 0.0366 -0.0233 0.0064  -0.0187 97  TRP A NE1 
819  C  CE2 . TRP A 95  ? 0.1269 0.0452 0.0355 -0.0293 0.0052  -0.0079 97  TRP A CE2 
820  C  CE3 . TRP A 95  ? 0.1137 0.0470 0.0309 -0.0093 -0.0353 0.0108  97  TRP A CE3 
821  C  CZ2 . TRP A 95  ? 0.1470 0.0503 0.0549 -0.0171 -0.0083 0.0088  97  TRP A CZ2 
822  C  CZ3 . TRP A 95  ? 0.1625 0.0593 0.0382 -0.0078 -0.0071 0.0155  97  TRP A CZ3 
823  C  CH2 . TRP A 95  ? 0.1636 0.0548 0.0396 -0.0161 -0.0008 -0.0001 97  TRP A CH2 
824  N  N   . GLY A 96  ? 0.1230 0.0346 0.0224 0.0021  0.0016  -0.0082 98  GLY A N   
825  C  CA  . GLY A 96  ? 0.0978 0.0470 0.0292 -0.0023 0.0124  0.0024  98  GLY A CA  
826  C  C   . GLY A 96  ? 0.1021 0.0513 0.0513 -0.0084 0.0039  -0.0201 98  GLY A C   
827  O  O   . GLY A 96  ? 0.1280 0.0390 0.0601 -0.0155 -0.0063 -0.0117 98  GLY A O   
828  N  N   . SER A 97  ? 0.1102 0.0399 0.0549 0.0012  0.0144  -0.0245 99  SER A N   
829  C  CA  . SER A 97  ? 0.1313 0.0348 0.0888 0.0010  0.0269  -0.0411 99  SER A CA  
830  C  C   . SER A 97  ? 0.1252 0.0466 0.0845 0.0022  -0.0037 -0.0272 99  SER A C   
831  O  O   . SER A 97  ? 0.2071 0.0979 0.0820 -0.0186 0.0119  -0.0438 99  SER A O   
832  C  CB  . SER A 97  ? 0.1384 0.0891 0.0976 0.0299  0.0094  -0.0417 99  SER A CB  
833  O  OG  . SER A 97  ? 0.1536 0.0673 0.1413 0.0164  0.0019  -0.0122 99  SER A OG  
834  N  N   A LEU A 98  ? 0.0987 0.0458 0.1137 -0.0175 0.0329  -0.0325 100 LEU A N   
835  N  N   B LEU A 98  ? 0.1230 0.0540 0.1124 0.0015  0.0251  -0.0089 100 LEU A N   
836  C  CA  A LEU A 98  ? 0.0986 0.0567 0.1398 -0.0245 0.0256  -0.0130 100 LEU A CA  
837  C  CA  B LEU A 98  ? 0.1187 0.0632 0.1005 -0.0166 0.0121  -0.0243 100 LEU A CA  
838  C  C   A LEU A 98  ? 0.1434 0.0445 0.0865 -0.0319 0.0176  -0.0250 100 LEU A C   
839  C  C   B LEU A 98  ? 0.1384 0.0567 0.0819 -0.0301 0.0269  -0.0127 100 LEU A C   
840  O  O   A LEU A 98  ? 0.1363 0.0309 0.1067 -0.0299 0.0053  -0.0189 100 LEU A O   
841  O  O   B LEU A 98  ? 0.1334 0.0562 0.0979 -0.0216 0.0151  -0.0171 100 LEU A O   
842  C  CB  A LEU A 98  ? 0.1557 0.0572 0.1553 -0.0196 0.0214  -0.0165 100 LEU A CB  
843  C  CB  B LEU A 98  ? 0.1546 0.1445 0.1205 0.0489  0.0526  0.0079  100 LEU A CB  
844  C  CG  A LEU A 98  ? 0.2545 0.1646 0.1543 -0.0152 0.1303  0.0029  100 LEU A CG  
845  C  CG  B LEU A 98  ? 0.1076 0.1647 0.1682 0.0183  0.0303  -0.0245 100 LEU A CG  
846  C  CD1 A LEU A 98  ? 0.2685 0.0747 0.2085 0.0768  0.0738  0.0221  100 LEU A CD1 
847  C  CD1 B LEU A 98  ? 0.1690 0.2110 0.2599 0.1733  0.0539  0.0197  100 LEU A CD1 
848  C  CD2 A LEU A 98  ? 0.2311 0.1690 0.3310 0.0109  0.1028  0.0161  100 LEU A CD2 
849  C  CD2 B LEU A 98  ? 0.1891 0.1714 0.2441 0.0734  0.1051  -0.1126 100 LEU A CD2 
850  N  N   . ASP A 99  ? 0.1031 0.0583 0.1138 -0.0107 -0.0094 0.0042  101 ASP A N   
851  C  CA  . ASP A 99  ? 0.1099 0.0721 0.1092 -0.0200 -0.0075 0.0348  101 ASP A CA  
852  C  C   . ASP A 99  ? 0.1062 0.0646 0.1063 -0.0032 -0.0034 0.0257  101 ASP A C   
853  O  O   . ASP A 99  ? 0.1474 0.0865 0.1208 0.0031  -0.0010 0.0280  101 ASP A O   
854  C  CB  . ASP A 99  ? 0.1067 0.0856 0.1345 -0.0372 -0.0111 0.0379  101 ASP A CB  
855  C  CG  . ASP A 99  ? 0.1812 0.0914 0.1579 -0.0365 -0.0440 0.0423  101 ASP A CG  
856  O  OD1 . ASP A 99  ? 0.1776 0.0820 0.1463 -0.0243 -0.0188 0.0279  101 ASP A OD1 
857  O  OD2 . ASP A 99  ? 0.2387 0.1647 0.1671 -0.0974 -0.0354 0.0209  101 ASP A OD2 
858  N  N   . GLY A 100 ? 0.1187 0.0792 0.1164 -0.0172 -0.0291 0.0363  102 GLY A N   
859  C  CA  . GLY A 100 ? 0.1532 0.0484 0.0917 -0.0186 0.0029  0.0093  102 GLY A CA  
860  C  C   . GLY A 100 ? 0.1242 0.0477 0.0831 -0.0003 0.0037  -0.0026 102 GLY A C   
861  O  O   . GLY A 100 ? 0.1395 0.0820 0.0768 -0.0148 0.0142  0.0183  102 GLY A O   
862  N  N   . GLN A 101 ? 0.0924 0.0643 0.0943 -0.0155 0.0038  0.0058  103 GLN A N   
863  C  CA  . GLN A 101 ? 0.0967 0.0427 0.0757 -0.0005 0.0039  0.0131  103 GLN A CA  
864  C  C   . GLN A 101 ? 0.0794 0.0463 0.0396 -0.0013 0.0130  0.0079  103 GLN A C   
865  O  O   . GLN A 101 ? 0.1111 0.0618 0.0536 -0.0003 0.0031  -0.0110 103 GLN A O   
866  C  CB  . GLN A 101 ? 0.1128 0.0801 0.0879 0.0245  0.0223  0.0353  103 GLN A CB  
867  C  CG  . GLN A 101 ? 0.1223 0.0891 0.0996 0.0229  0.0346  0.0100  103 GLN A CG  
868  C  CD  . GLN A 101 ? 0.1517 0.1049 0.1884 0.0560  0.0510  0.0703  103 GLN A CD  
869  O  OE1 . GLN A 101 ? 0.2290 0.2628 0.2946 0.1596  0.1292  0.1942  103 GLN A OE1 
870  N  NE2 . GLN A 101 ? 0.1059 0.1097 0.1848 0.0266  0.0296  0.0436  103 GLN A NE2 
871  N  N   . GLY A 102 ? 0.0882 0.0449 0.0431 0.0136  0.0053  0.0041  104 GLY A N   
872  C  CA  . GLY A 102 ? 0.0881 0.0330 0.0546 0.0100  0.0010  -0.0023 104 GLY A CA  
873  C  C   . GLY A 102 ? 0.0793 0.0399 0.0364 -0.0044 0.0006  -0.0044 104 GLY A C   
874  O  O   . GLY A 102 ? 0.0840 0.0511 0.0533 -0.0137 0.0102  0.0073  104 GLY A O   
875  N  N   . SER A 103 ? 0.0619 0.0522 0.0379 -0.0030 0.0043  -0.0086 105 SER A N   
876  C  CA  . SER A 103 ? 0.0590 0.0515 0.0320 -0.0074 -0.0058 -0.0149 105 SER A CA  
877  C  C   . SER A 103 ? 0.0549 0.0380 0.0346 -0.0093 -0.0033 -0.0025 105 SER A C   
878  O  O   . SER A 103 ? 0.0863 0.0364 0.0575 0.0013  -0.0166 -0.0136 105 SER A O   
879  C  CB  . SER A 103 ? 0.0725 0.0373 0.0417 -0.0053 -0.0018 0.0149  105 SER A CB  
880  O  OG  . SER A 103 ? 0.0897 0.0223 0.0566 0.0005  -0.0144 0.0066  105 SER A OG  
881  N  N   . GLU A 104 ? 0.0582 0.0381 0.0251 -0.0128 -0.0072 -0.0091 106 GLU A N   
882  C  CA  . GLU A 104 ? 0.0580 0.0334 0.0311 -0.0168 -0.0081 0.0003  106 GLU A CA  
883  C  C   . GLU A 104 ? 0.0503 0.0303 0.0303 -0.0003 -0.0075 -0.0025 106 GLU A C   
884  O  O   . GLU A 104 ? 0.0495 0.0519 0.0451 -0.0004 -0.0182 -0.0038 106 GLU A O   
885  C  CB  . GLU A 104 ? 0.0662 0.0326 0.0143 -0.0126 -0.0043 -0.0013 106 GLU A CB  
886  C  CG  . GLU A 104 ? 0.1020 0.0584 0.0290 -0.0154 0.0241  -0.0006 106 GLU A CG  
887  C  CD  . GLU A 104 ? 0.0655 0.0529 0.0312 -0.0104 0.0151  -0.0160 106 GLU A CD  
888  O  OE1 . GLU A 104 ? 0.0488 0.0505 0.0553 -0.0092 -0.0002 -0.0038 106 GLU A OE1 
889  O  OE2 . GLU A 104 ? 0.0589 0.0685 0.0782 -0.0023 0.0099  -0.0019 106 GLU A OE2 
890  N  N   . HIS A 105 ? 0.0549 0.0255 0.0285 -0.0036 0.0027  0.0044  107 HIS A N   
891  C  CA  . HIS A 105 ? 0.0574 0.0266 0.0241 -0.0005 0.0043  -0.0009 107 HIS A CA  
892  C  C   . HIS A 105 ? 0.0522 0.0276 0.0303 -0.0005 -0.0006 0.0040  107 HIS A C   
893  O  O   . HIS A 105 ? 0.0612 0.0406 0.0348 -0.0019 -0.0006 -0.0036 107 HIS A O   
894  C  CB  . HIS A 105 ? 0.0558 0.0187 0.0469 0.0006  -0.0001 0.0027  107 HIS A CB  
895  C  CG  . HIS A 105 ? 0.0414 0.0256 0.0276 -0.0122 0.0068  0.0010  107 HIS A CG  
896  N  ND1 . HIS A 105 ? 0.0715 0.0272 0.0399 -0.0044 -0.0006 0.0098  107 HIS A ND1 
897  C  CD2 . HIS A 105 ? 0.0452 0.0311 0.0381 0.0023  0.0044  -0.0158 107 HIS A CD2 
898  C  CE1 . HIS A 105 ? 0.0750 0.0409 0.0312 -0.0024 -0.0044 -0.0110 107 HIS A CE1 
899  N  NE2 . HIS A 105 ? 0.0443 0.0382 0.0380 -0.0049 -0.0087 -0.0078 107 HIS A NE2 
900  N  N   . THR A 106 ? 0.0696 0.0337 0.0417 -0.0076 0.0055  0.0198  108 THR A N   
901  C  CA  . THR A 106 ? 0.0653 0.0316 0.0387 -0.0027 0.0139  0.0210  108 THR A CA  
902  C  C   . THR A 106 ? 0.0637 0.0267 0.0255 -0.0068 0.0036  0.0131  108 THR A C   
903  O  O   . THR A 106 ? 0.0811 0.0339 0.0380 0.0086  -0.0033 0.0044  108 THR A O   
904  C  CB  . THR A 106 ? 0.0882 0.0398 0.0206 0.0104  -0.0129 0.0009  108 THR A CB  
905  O  OG1 . THR A 106 ? 0.0820 0.0434 0.0405 0.0050  -0.0160 -0.0048 108 THR A OG1 
906  C  CG2 . THR A 106 ? 0.1120 0.0584 0.0329 0.0102  0.0062  0.0003  108 THR A CG2 
907  N  N   . VAL A 107 ? 0.0697 0.0304 0.0409 -0.0104 0.0069  0.0223  109 VAL A N   
908  C  CA  . VAL A 107 ? 0.0774 0.0616 0.0497 -0.0055 0.0142  0.0372  109 VAL A CA  
909  C  C   . VAL A 107 ? 0.0910 0.0398 0.0414 -0.0006 0.0061  0.0119  109 VAL A C   
910  O  O   . VAL A 107 ? 0.1049 0.0335 0.0671 0.0111  0.0181  0.0059  109 VAL A O   
911  C  CB  . VAL A 107 ? 0.0741 0.0469 0.0856 -0.0050 0.0150  0.0216  109 VAL A CB  
912  C  CG1 . VAL A 107 ? 0.0826 0.0732 0.0937 0.0057  0.0240  0.0199  109 VAL A CG1 
913  C  CG2 . VAL A 107 ? 0.0819 0.0635 0.0993 0.0192  -0.0183 0.0239  109 VAL A CG2 
914  N  N   . ASP A 108 ? 0.1263 0.0592 0.0197 0.0200  0.0162  0.0219  110 ASP A N   
915  C  CA  . ASP A 108 ? 0.1456 0.0653 0.0646 0.0153  0.0240  0.0465  110 ASP A CA  
916  C  C   . ASP A 108 ? 0.1489 0.0609 0.0452 0.0078  0.0109  0.0299  110 ASP A C   
917  O  O   . ASP A 108 ? 0.1467 0.0566 0.0584 0.0183  -0.0015 0.0268  110 ASP A O   
918  C  CB  . ASP A 108 ? 0.1816 0.0575 0.0452 0.0021  0.0483  0.0359  110 ASP A CB  
919  C  CG  . ASP A 108 ? 0.1877 0.0556 0.0698 0.0152  0.0472  0.0303  110 ASP A CG  
920  O  OD1 . ASP A 108 ? 0.1715 0.0671 0.1137 0.0270  0.0475  0.0220  110 ASP A OD1 
921  O  OD2 . ASP A 108 ? 0.1668 0.1367 0.1348 0.0226  0.0358  0.0333  110 ASP A OD2 
922  N  N   . LYS A 109 ? 0.0944 0.0698 0.0487 0.0248  -0.0012 0.0348  111 LYS A N   
923  C  CA  . LYS A 109 ? 0.0942 0.0788 0.0553 0.0190  -0.0057 0.0334  111 LYS A CA  
924  C  C   . LYS A 109 ? 0.1032 0.0680 0.0469 0.0198  -0.0080 0.0337  111 LYS A C   
925  O  O   . LYS A 109 ? 0.0871 0.0872 0.0970 0.0209  0.0039  0.0174  111 LYS A O   
926  C  CB  . LYS A 109 ? 0.1320 0.1259 0.0840 0.0614  -0.0301 0.0245  111 LYS A CB  
927  C  CG  . LYS A 109 ? 0.2066 0.1510 0.0847 0.0694  -0.0578 0.0188  111 LYS A CG  
928  C  CD  . LYS A 109 ? 0.2289 0.2187 0.1464 0.0249  -0.0613 -0.0266 111 LYS A CD  
929  C  CE  . LYS A 109 ? 0.1967 0.3017 0.1467 0.0631  -0.0721 -0.0675 111 LYS A CE  
930  N  NZ  . LYS A 109 ? 0.1398 0.3398 0.2473 0.0040  -0.0524 0.0898  111 LYS A NZ  
931  N  N   . LYS A 110 ? 0.1038 0.0294 0.0477 -0.0052 -0.0165 0.0172  112 LYS A N   
932  C  CA  . LYS A 110 ? 0.0917 0.0513 0.0554 0.0118  -0.0179 -0.0046 112 LYS A CA  
933  C  C   . LYS A 110 ? 0.0831 0.0524 0.0571 0.0073  -0.0069 -0.0055 112 LYS A C   
934  O  O   . LYS A 110 ? 0.0898 0.0469 0.0459 -0.0005 0.0030  0.0013  112 LYS A O   
935  C  CB  . LYS A 110 ? 0.0892 0.0686 0.0714 -0.0253 -0.0229 0.0084  112 LYS A CB  
936  C  CG  . LYS A 110 ? 0.1048 0.1102 0.0892 -0.0005 -0.0289 -0.0440 112 LYS A CG  
937  C  CD  . LYS A 110 ? 0.1084 0.1036 0.1238 -0.0172 -0.0212 -0.0089 112 LYS A CD  
938  C  CE  . LYS A 110 ? 0.1726 0.0946 0.1161 -0.0445 -0.0245 -0.0154 112 LYS A CE  
939  N  NZ  . LYS A 110 ? 0.2156 0.0750 0.1185 -0.0412 -0.0190 0.0209  112 LYS A NZ  
940  N  N   A LYS A 111 ? 0.1030 0.0601 0.0337 0.0168  -0.0077 0.0154  113 LYS A N   
941  N  N   B LYS A 111 ? 0.0996 0.0610 0.0363 0.0149  -0.0064 0.0136  113 LYS A N   
942  C  CA  A LYS A 111 ? 0.0908 0.0583 0.0407 0.0089  0.0006  0.0147  113 LYS A CA  
943  C  CA  B LYS A 111 ? 0.0844 0.0574 0.0443 0.0084  0.0023  0.0130  113 LYS A CA  
944  C  C   A LYS A 111 ? 0.1014 0.0399 0.0571 -0.0053 -0.0079 0.0146  113 LYS A C   
945  C  C   B LYS A 111 ? 0.0977 0.0425 0.0591 -0.0026 -0.0079 0.0132  113 LYS A C   
946  O  O   A LYS A 111 ? 0.1153 0.0373 0.0865 0.0013  -0.0249 0.0070  113 LYS A O   
947  O  O   B LYS A 111 ? 0.1076 0.0388 0.0883 0.0121  -0.0248 -0.0004 113 LYS A O   
948  C  CB  A LYS A 111 ? 0.0773 0.0853 0.0779 0.0145  -0.0068 0.0042  113 LYS A CB  
949  C  CB  B LYS A 111 ? 0.0662 0.0812 0.0812 0.0094  -0.0065 0.0030  113 LYS A CB  
950  C  CG  A LYS A 111 ? 0.0840 0.1100 0.0540 0.0268  -0.0077 0.0040  113 LYS A CG  
951  C  CG  B LYS A 111 ? 0.0680 0.0961 0.0633 0.0151  -0.0025 0.0021  113 LYS A CG  
952  C  CD  A LYS A 111 ? 0.0809 0.1062 0.1204 0.0256  0.0160  0.0124  113 LYS A CD  
953  C  CD  B LYS A 111 ? 0.0518 0.1011 0.1179 0.0088  0.0127  -0.0006 113 LYS A CD  
954  C  CE  A LYS A 111 ? 0.0961 0.1514 0.1284 0.0356  -0.0068 0.0150  113 LYS A CE  
955  C  CE  B LYS A 111 ? 0.0644 0.1049 0.1377 0.0078  -0.0059 0.0069  113 LYS A CE  
956  N  NZ  A LYS A 111 ? 0.1084 0.1521 0.2171 0.0397  0.0157  0.0413  113 LYS A NZ  
957  N  NZ  B LYS A 111 ? 0.0829 0.1068 0.1417 0.0260  -0.0299 -0.0003 113 LYS A NZ  
958  N  N   . TYR A 112 ? 0.0862 0.0531 0.0425 0.0063  -0.0038 0.0115  114 TYR A N   
959  C  CA  . TYR A 112 ? 0.0906 0.0461 0.0408 0.0064  -0.0092 0.0064  114 TYR A CA  
960  C  C   . TYR A 112 ? 0.0838 0.0283 0.0466 0.0086  -0.0116 0.0067  114 TYR A C   
961  O  O   . TYR A 112 ? 0.0865 0.0493 0.0501 -0.0052 0.0062  -0.0126 114 TYR A O   
962  C  CB  . TYR A 112 ? 0.0575 0.0452 0.0813 0.0004  0.0062  0.0193  114 TYR A CB  
963  C  CG  . TYR A 112 ? 0.0729 0.0329 0.0556 -0.0113 -0.0066 0.0105  114 TYR A CG  
964  C  CD1 . TYR A 112 ? 0.1477 0.0384 0.0564 0.0013  0.0030  0.0063  114 TYR A CD1 
965  C  CD2 . TYR A 112 ? 0.0670 0.0337 0.1011 -0.0091 -0.0092 0.0264  114 TYR A CD2 
966  C  CE1 . TYR A 112 ? 0.1618 0.0401 0.0792 -0.0009 0.0211  0.0110  114 TYR A CE1 
967  C  CE2 . TYR A 112 ? 0.1262 0.0741 0.1039 -0.0265 0.0281  0.0027  114 TYR A CE2 
968  C  CZ  . TYR A 112 ? 0.1812 0.0572 0.0818 -0.0262 0.0452  0.0104  114 TYR A CZ  
969  O  OH  . TYR A 112 ? 0.1747 0.1258 0.1316 0.0076  0.0834  -0.0072 114 TYR A OH  
970  N  N   . ALA A 113 ? 0.0933 0.0390 0.0531 -0.0055 -0.0147 -0.0052 115 ALA A N   
971  C  CA  . ALA A 113 ? 0.0917 0.0259 0.0519 -0.0131 -0.0044 -0.0038 115 ALA A CA  
972  C  C   . ALA A 113 ? 0.0919 0.0276 0.0422 -0.0027 -0.0069 0.0050  115 ALA A C   
973  O  O   . ALA A 113 ? 0.1153 0.0346 0.0529 -0.0031 0.0078  0.0000  115 ALA A O   
974  C  CB  . ALA A 113 ? 0.1067 0.0389 0.0915 -0.0160 -0.0271 -0.0052 115 ALA A CB  
975  N  N   . ALA A 114 ? 0.1022 0.0187 0.0285 -0.0104 -0.0114 0.0008  116 ALA A N   
976  C  CA  . ALA A 114 ? 0.1029 0.0248 0.0293 -0.0099 -0.0070 0.0097  116 ALA A CA  
977  C  C   . ALA A 114 ? 0.0655 0.0294 0.0496 -0.0040 -0.0116 0.0072  116 ALA A C   
978  O  O   . ALA A 114 ? 0.0729 0.0417 0.0469 -0.0081 -0.0115 0.0124  116 ALA A O   
979  C  CB  . ALA A 114 ? 0.0970 0.0424 0.0310 -0.0185 -0.0128 0.0130  116 ALA A CB  
980  N  N   . GLU A 115 ? 0.0774 0.0250 0.0477 -0.0011 -0.0122 0.0051  117 GLU A N   
981  C  CA  . GLU A 115 ? 0.0721 0.0310 0.0328 0.0026  -0.0179 0.0013  117 GLU A CA  
982  C  C   . GLU A 115 ? 0.0627 0.0309 0.0348 -0.0063 -0.0122 0.0035  117 GLU A C   
983  O  O   . GLU A 115 ? 0.0651 0.0567 0.0476 -0.0092 -0.0022 0.0046  117 GLU A O   
984  C  CB  . GLU A 115 ? 0.0594 0.0346 0.0231 -0.0057 -0.0076 0.0115  117 GLU A CB  
985  C  CG  . GLU A 115 ? 0.0827 0.0505 0.0294 -0.0087 -0.0223 -0.0124 117 GLU A CG  
986  C  CD  . GLU A 115 ? 0.0582 0.0506 0.0223 -0.0074 -0.0066 0.0059  117 GLU A CD  
987  O  OE1 . GLU A 115 ? 0.0637 0.0680 0.0408 0.0039  -0.0175 0.0050  117 GLU A OE1 
988  O  OE2 . GLU A 115 ? 0.0803 0.0584 0.0308 -0.0085 -0.0333 -0.0022 117 GLU A OE2 
989  N  N   . LEU A 116 ? 0.0688 0.0362 0.0241 0.0050  -0.0237 -0.0033 118 LEU A N   
990  C  CA  . LEU A 116 ? 0.0593 0.0320 0.0241 -0.0086 -0.0223 -0.0006 118 LEU A CA  
991  C  C   . LEU A 116 ? 0.0685 0.0293 0.0127 -0.0086 -0.0164 0.0058  118 LEU A C   
992  O  O   . LEU A 116 ? 0.0854 0.0329 0.0158 -0.0055 -0.0117 0.0124  118 LEU A O   
993  C  CB  . LEU A 116 ? 0.0528 0.0443 0.0470 0.0037  -0.0217 0.0144  118 LEU A CB  
994  C  CG  . LEU A 116 ? 0.0628 0.0373 0.0628 0.0010  -0.0218 0.0190  118 LEU A CG  
995  C  CD1 . LEU A 116 ? 0.0865 0.0571 0.0590 -0.0148 -0.0344 0.0295  118 LEU A CD1 
996  C  CD2 . LEU A 116 ? 0.0712 0.0865 0.0687 -0.0150 -0.0307 0.0150  118 LEU A CD2 
997  N  N   . HIS A 117 ? 0.0691 0.0250 0.0292 -0.0126 -0.0261 0.0087  119 HIS A N   
998  C  CA  . HIS A 117 ? 0.0621 0.0267 0.0285 -0.0139 -0.0162 0.0074  119 HIS A CA  
999  C  C   . HIS A 117 ? 0.0567 0.0375 0.0329 -0.0087 -0.0153 0.0145  119 HIS A C   
1000 O  O   . HIS A 117 ? 0.0811 0.0425 0.0285 -0.0051 -0.0093 0.0039  119 HIS A O   
1001 C  CB  . HIS A 117 ? 0.0584 0.0388 0.0312 -0.0004 -0.0105 0.0073  119 HIS A CB  
1002 C  CG  . HIS A 117 ? 0.0655 0.0506 0.0081 0.0067  -0.0100 -0.0002 119 HIS A CG  
1003 N  ND1 . HIS A 117 ? 0.0615 0.0449 0.0098 -0.0170 -0.0034 0.0110  119 HIS A ND1 
1004 C  CD2 . HIS A 117 ? 0.0533 0.0562 0.0143 -0.0013 -0.0188 0.0047  119 HIS A CD2 
1005 C  CE1 . HIS A 117 ? 0.0730 0.0355 0.0143 -0.0154 -0.0141 0.0049  119 HIS A CE1 
1006 N  NE2 . HIS A 117 ? 0.0512 0.0469 0.0343 -0.0027 -0.0214 0.0018  119 HIS A NE2 
1007 N  N   . LEU A 118 ? 0.0723 0.0127 0.0336 -0.0081 -0.0157 -0.0012 120 LEU A N   
1008 C  CA  . LEU A 118 ? 0.0653 0.0312 0.0469 0.0015  -0.0314 0.0008  120 LEU A CA  
1009 C  C   . LEU A 118 ? 0.0549 0.0229 0.0317 -0.0008 -0.0234 0.0134  120 LEU A C   
1010 O  O   . LEU A 118 ? 0.0673 0.0364 0.0303 -0.0095 -0.0201 0.0168  120 LEU A O   
1011 C  CB  . LEU A 118 ? 0.0661 0.0408 0.0530 -0.0106 -0.0231 -0.0074 120 LEU A CB  
1012 C  CG  . LEU A 118 ? 0.0610 0.0449 0.0724 -0.0233 -0.0490 0.0107  120 LEU A CG  
1013 C  CD1 . LEU A 118 ? 0.1283 0.0785 0.0743 -0.0745 -0.0457 0.0164  120 LEU A CD1 
1014 C  CD2 . LEU A 118 ? 0.0849 0.1032 0.0612 0.0067  -0.0607 -0.0066 120 LEU A CD2 
1015 N  N   . VAL A 119 ? 0.0655 0.0300 0.0425 -0.0116 -0.0144 0.0121  121 VAL A N   
1016 C  CA  . VAL A 119 ? 0.0917 0.0187 0.0391 -0.0143 -0.0053 0.0096  121 VAL A CA  
1017 C  C   . VAL A 119 ? 0.0739 0.0256 0.0452 -0.0125 -0.0092 0.0141  121 VAL A C   
1018 O  O   . VAL A 119 ? 0.0955 0.0389 0.0510 -0.0027 -0.0232 0.0126  121 VAL A O   
1019 C  CB  . VAL A 119 ? 0.0840 0.0312 0.0598 -0.0115 -0.0084 0.0067  121 VAL A CB  
1020 C  CG1 . VAL A 119 ? 0.0847 0.0443 0.0757 -0.0260 -0.0027 0.0060  121 VAL A CG1 
1021 C  CG2 . VAL A 119 ? 0.1049 0.0405 0.0409 0.0109  -0.0073 0.0200  121 VAL A CG2 
1022 N  N   . HIS A 120 ? 0.0785 0.0241 0.0540 -0.0089 -0.0064 0.0063  122 HIS A N   
1023 C  CA  . HIS A 120 ? 0.0524 0.0249 0.0768 -0.0166 -0.0084 -0.0036 122 HIS A CA  
1024 C  C   . HIS A 120 ? 0.0725 0.0311 0.0600 -0.0118 -0.0287 0.0027  122 HIS A C   
1025 O  O   . HIS A 120 ? 0.0879 0.0309 0.0646 -0.0031 -0.0331 0.0104  122 HIS A O   
1026 C  CB  . HIS A 120 ? 0.0478 0.0496 0.0703 0.0041  -0.0040 0.0035  122 HIS A CB  
1027 C  CG  . HIS A 120 ? 0.0782 0.0303 0.0553 -0.0078 -0.0034 0.0233  122 HIS A CG  
1028 N  ND1 . HIS A 120 ? 0.0671 0.0319 0.0619 0.0027  -0.0106 0.0143  122 HIS A ND1 
1029 C  CD2 . HIS A 120 ? 0.0759 0.0584 0.0479 -0.0111 -0.0059 0.0086  122 HIS A CD2 
1030 C  CE1 . HIS A 120 ? 0.0469 0.0768 0.0765 -0.0001 -0.0017 -0.0062 122 HIS A CE1 
1031 N  NE2 . HIS A 120 ? 0.0757 0.0575 0.0628 -0.0044 -0.0182 0.0000  122 HIS A NE2 
1032 N  N   . TRP A 121 ? 0.0685 0.0260 0.0686 -0.0132 -0.0129 -0.0087 123 TRP A N   
1033 C  CA  . TRP A 121 ? 0.0589 0.0295 0.0653 -0.0111 -0.0155 -0.0082 123 TRP A CA  
1034 C  C   . TRP A 121 ? 0.0489 0.0346 0.0584 -0.0168 -0.0003 0.0042  123 TRP A C   
1035 O  O   . TRP A 121 ? 0.0732 0.0530 0.0894 -0.0004 -0.0264 -0.0110 123 TRP A O   
1036 C  CB  . TRP A 121 ? 0.0882 0.0822 0.0804 -0.0391 -0.0276 0.0242  123 TRP A CB  
1037 C  CG  . TRP A 121 ? 0.1011 0.0392 0.0803 -0.0182 -0.0190 0.0170  123 TRP A CG  
1038 C  CD1 . TRP A 121 ? 0.1500 0.0670 0.0750 -0.0398 -0.0226 0.0215  123 TRP A CD1 
1039 C  CD2 . TRP A 121 ? 0.1557 0.0300 0.0685 -0.0306 -0.0223 0.0243  123 TRP A CD2 
1040 N  NE1 . TRP A 121 ? 0.1561 0.0466 0.0898 -0.0189 -0.0153 0.0027  123 TRP A NE1 
1041 C  CE2 . TRP A 121 ? 0.1737 0.0505 0.0651 0.0010  -0.0217 0.0093  123 TRP A CE2 
1042 C  CE3 . TRP A 121 ? 0.2052 0.0387 0.1106 -0.0403 0.0064  0.0047  123 TRP A CE3 
1043 C  CZ2 . TRP A 121 ? 0.2733 0.0443 0.0829 0.0044  -0.0228 0.0186  123 TRP A CZ2 
1044 C  CZ3 . TRP A 121 ? 0.3209 0.0425 0.1084 -0.0272 -0.0222 -0.0083 123 TRP A CZ3 
1045 C  CH2 . TRP A 121 ? 0.3041 0.0574 0.0952 0.0012  -0.0066 0.0043  123 TRP A CH2 
1046 N  N   . ASN A 122 ? 0.0750 0.0381 0.0748 -0.0082 -0.0143 -0.0179 124 ASN A N   
1047 C  CA  . ASN A 122 ? 0.0835 0.0153 0.0813 0.0086  -0.0260 -0.0121 124 ASN A CA  
1048 C  C   . ASN A 122 ? 0.0969 0.0230 0.0797 0.0050  -0.0288 -0.0116 124 ASN A C   
1049 O  O   . ASN A 122 ? 0.1138 0.0369 0.0659 0.0043  -0.0138 -0.0069 124 ASN A O   
1050 C  CB  . ASN A 122 ? 0.0928 0.0544 0.0678 0.0047  -0.0181 -0.0060 124 ASN A CB  
1051 C  CG  . ASN A 122 ? 0.1313 0.0303 0.0794 0.0121  -0.0078 -0.0062 124 ASN A CG  
1052 O  OD1 . ASN A 122 ? 0.1298 0.0346 0.0946 0.0140  -0.0087 -0.0130 124 ASN A OD1 
1053 N  ND2 . ASN A 122 ? 0.1550 0.0408 0.0847 0.0008  -0.0233 -0.0049 124 ASN A ND2 
1054 N  N   . THR A 123 ? 0.1091 0.0260 0.0985 0.0221  -0.0497 -0.0138 125 THR A N   
1055 C  CA  . THR A 123 ? 0.1284 0.0329 0.1302 0.0182  -0.0530 0.0055  125 THR A CA  
1056 C  C   . THR A 123 ? 0.1377 0.0339 0.1194 0.0229  -0.0146 -0.0040 125 THR A C   
1057 O  O   . THR A 123 ? 0.1406 0.0363 0.1409 0.0185  -0.0311 0.0071  125 THR A O   
1058 C  CB  . THR A 123 ? 0.1539 0.0655 0.1625 0.0339  -0.1013 -0.0086 125 THR A CB  
1059 O  OG1 . THR A 123 ? 0.1718 0.1164 0.2681 0.0712  -0.0237 -0.0035 125 THR A OG1 
1060 C  CG2 . THR A 123 ? 0.2159 0.0820 0.1521 -0.0106 -0.0928 -0.0109 125 THR A CG2 
1061 N  N   A LYS A 124 ? 0.1525 0.0213 0.1013 0.0153  0.0105  -0.0190 126 LYS A N   
1062 N  N   B LYS A 124 ? 0.1535 0.0152 0.1007 0.0109  0.0006  -0.0225 126 LYS A N   
1063 C  CA  A LYS A 124 ? 0.1406 0.0303 0.1020 -0.0113 -0.0010 -0.0053 126 LYS A CA  
1064 C  CA  B LYS A 124 ? 0.1441 0.0364 0.0934 -0.0257 -0.0066 -0.0125 126 LYS A CA  
1065 C  C   A LYS A 124 ? 0.1294 0.0232 0.1084 0.0099  -0.0063 0.0135  126 LYS A C   
1066 C  C   B LYS A 124 ? 0.1320 0.0215 0.1040 0.0070  -0.0072 0.0130  126 LYS A C   
1067 O  O   A LYS A 124 ? 0.1489 0.0528 0.1464 -0.0044 -0.0054 -0.0238 126 LYS A O   
1068 O  O   B LYS A 124 ? 0.1610 0.0409 0.1302 -0.0075 -0.0020 -0.0074 126 LYS A O   
1069 C  CB  A LYS A 124 ? 0.1930 0.0601 0.1037 -0.0011 -0.0097 -0.0006 126 LYS A CB  
1070 C  CB  B LYS A 124 ? 0.2049 0.0750 0.0942 -0.0188 -0.0151 -0.0086 126 LYS A CB  
1071 C  CG  A LYS A 124 ? 0.2135 0.0673 0.0791 0.0241  0.0026  0.0151  126 LYS A CG  
1072 C  CG  B LYS A 124 ? 0.1589 0.1194 0.0610 -0.0398 -0.0335 -0.0064 126 LYS A CG  
1073 C  CD  A LYS A 124 ? 0.2458 0.0881 0.0703 -0.0166 -0.0024 0.0010  126 LYS A CD  
1074 C  CD  B LYS A 124 ? 0.1937 0.1539 0.0634 0.0026  -0.0244 0.0009  126 LYS A CD  
1075 C  CE  A LYS A 124 ? 0.3004 0.0889 0.1041 0.0217  -0.0228 -0.0187 126 LYS A CE  
1076 C  CE  B LYS A 124 ? 0.1356 0.1966 0.1044 0.0326  0.0265  0.0073  126 LYS A CE  
1077 N  NZ  A LYS A 124 ? 0.3005 0.1324 0.1776 -0.0467 0.0137  0.0690  126 LYS A NZ  
1078 N  NZ  B LYS A 124 ? 0.2240 0.1586 0.1093 0.0666  0.0140  0.0356  126 LYS A NZ  
1079 N  N   . TYR A 125 ? 0.1233 0.0392 0.0933 0.0038  -0.0008 0.0063  127 TYR A N   
1080 C  CA  . TYR A 125 ? 0.1160 0.0714 0.0908 0.0070  -0.0209 0.0086  127 TYR A CA  
1081 C  C   . TYR A 125 ? 0.1338 0.0405 0.0847 0.0107  -0.0076 -0.0185 127 TYR A C   
1082 O  O   . TYR A 125 ? 0.1593 0.0662 0.0882 0.0021  0.0139  -0.0092 127 TYR A O   
1083 C  CB  . TYR A 125 ? 0.1392 0.0540 0.0891 0.0019  0.0097  0.0153  127 TYR A CB  
1084 C  CG  . TYR A 125 ? 0.1190 0.0384 0.0700 0.0137  -0.0070 -0.0137 127 TYR A CG  
1085 C  CD1 . TYR A 125 ? 0.1467 0.0519 0.0803 -0.0110 0.0097  -0.0209 127 TYR A CD1 
1086 C  CD2 . TYR A 125 ? 0.1093 0.0506 0.0819 0.0024  -0.0021 -0.0073 127 TYR A CD2 
1087 C  CE1 . TYR A 125 ? 0.1615 0.0538 0.0812 0.0104  -0.0039 -0.0131 127 TYR A CE1 
1088 C  CE2 . TYR A 125 ? 0.0908 0.0952 0.0593 0.0184  -0.0151 -0.0321 127 TYR A CE2 
1089 C  CZ  . TYR A 125 ? 0.1306 0.0582 0.0653 0.0168  -0.0009 -0.0187 127 TYR A CZ  
1090 O  OH  . TYR A 125 ? 0.1938 0.1106 0.0591 0.0129  -0.0102 -0.0348 127 TYR A OH  
1091 N  N   . GLY A 126 ? 0.1431 0.0357 0.0864 -0.0097 -0.0201 0.0041  128 GLY A N   
1092 C  CA  . GLY A 126 ? 0.2304 0.0176 0.0826 -0.0104 0.0323  0.0075  128 GLY A CA  
1093 C  C   . GLY A 126 ? 0.2168 0.0346 0.0635 0.0126  -0.0091 0.0079  128 GLY A C   
1094 O  O   . GLY A 126 ? 0.2698 0.0513 0.0725 0.0211  -0.0277 0.0183  128 GLY A O   
1095 N  N   A ASP A 127 ? 0.2449 0.0141 0.0773 0.0206  0.0095  0.0048  129 ASP A N   
1096 N  N   B ASP A 127 ? 0.2228 0.0729 0.1007 0.0217  -0.0139 -0.0072 129 ASP A N   
1097 C  CA  A ASP A 127 ? 0.2045 0.0065 0.0937 0.0004  0.0298  -0.0036 129 ASP A CA  
1098 C  CA  B ASP A 127 ? 0.1773 0.0555 0.0801 -0.0026 0.0004  0.0109  129 ASP A CA  
1099 C  C   A ASP A 127 ? 0.1891 0.0400 0.0882 0.0184  0.0335  0.0041  129 ASP A C   
1100 C  C   B ASP A 127 ? 0.2017 0.0689 0.0554 0.0011  -0.0323 0.0094  129 ASP A C   
1101 O  O   A ASP A 127 ? 0.1488 0.0621 0.0953 0.0157  0.0326  0.0166  129 ASP A O   
1102 O  O   B ASP A 127 ? 0.1208 0.0761 0.0378 0.0063  0.0055  -0.0029 129 ASP A O   
1103 C  CB  A ASP A 127 ? 0.1862 0.0272 0.1240 -0.0117 0.0221  0.0336  129 ASP A CB  
1104 C  CB  B ASP A 127 ? 0.1172 0.0750 0.0653 0.0047  -0.0223 0.0094  129 ASP A CB  
1105 C  CG  A ASP A 127 ? 0.1954 0.0073 0.1201 -0.0138 0.0296  -0.0025 129 ASP A CG  
1106 C  CG  B ASP A 127 ? 0.0942 0.1023 0.1029 0.0298  -0.0002 0.0091  129 ASP A CG  
1107 O  OD1 A ASP A 127 ? 0.1870 0.0591 0.1539 -0.0136 -0.0133 -0.0469 129 ASP A OD1 
1108 O  OD1 B ASP A 127 ? 0.0822 0.1453 0.1041 0.0222  -0.0299 0.0269  129 ASP A OD1 
1109 O  OD2 A ASP A 127 ? 0.2466 0.0566 0.1280 -0.0209 0.0425  0.0230  129 ASP A OD2 
1110 O  OD2 B ASP A 127 ? 0.1251 0.1058 0.1970 0.0212  0.0062  0.0196  129 ASP A OD2 
1111 N  N   . PHE A 128 ? 0.2261 0.0557 0.0715 0.0425  0.0044  -0.0015 130 PHE A N   
1112 C  CA  . PHE A 128 ? 0.1791 0.0558 0.0765 0.0398  -0.0298 -0.0289 130 PHE A CA  
1113 C  C   . PHE A 128 ? 0.1586 0.0496 0.0540 0.0015  0.0256  -0.0027 130 PHE A C   
1114 O  O   . PHE A 128 ? 0.1345 0.0601 0.0582 -0.0201 -0.0052 -0.0109 130 PHE A O   
1115 C  CB  . PHE A 128 ? 0.1841 0.0510 0.0917 0.0215  -0.0190 -0.0362 130 PHE A CB  
1116 C  CG  . PHE A 128 ? 0.1439 0.0346 0.1012 -0.0065 0.0000  -0.0229 130 PHE A CG  
1117 C  CD1 . PHE A 128 ? 0.1550 0.0398 0.1036 -0.0300 -0.0170 -0.0240 130 PHE A CD1 
1118 C  CD2 . PHE A 128 ? 0.1593 0.0704 0.1124 -0.0006 0.0063  -0.0089 130 PHE A CD2 
1119 C  CE1 . PHE A 128 ? 0.1775 0.0425 0.1208 -0.0156 -0.0062 -0.0339 130 PHE A CE1 
1120 C  CE2 . PHE A 128 ? 0.1852 0.0786 0.1313 0.0270  0.0352  -0.0109 130 PHE A CE2 
1121 C  CZ  . PHE A 128 ? 0.1848 0.0890 0.1177 0.0004  0.0024  -0.0208 130 PHE A CZ  
1122 N  N   . GLY A 129 ? 0.2134 0.0750 0.0822 -0.0397 0.0314  -0.0003 131 GLY A N   
1123 C  CA  . GLY A 129 ? 0.1844 0.1101 0.0888 -0.0431 0.0510  -0.0052 131 GLY A CA  
1124 C  C   . GLY A 129 ? 0.1646 0.1102 0.0993 -0.0722 0.0594  -0.0012 131 GLY A C   
1125 O  O   . GLY A 129 ? 0.1622 0.0874 0.1636 -0.0225 0.0512  -0.0420 131 GLY A O   
1126 N  N   . LYS A 130 ? 0.1733 0.0759 0.0982 -0.0655 0.0405  0.0089  132 LYS A N   
1127 C  CA  . LYS A 130 ? 0.1526 0.0294 0.1090 -0.0491 0.0223  -0.0066 132 LYS A CA  
1128 C  C   . LYS A 130 ? 0.1238 0.0436 0.0879 -0.0353 0.0153  -0.0050 132 LYS A C   
1129 O  O   . LYS A 130 ? 0.1288 0.0678 0.0863 -0.0392 0.0043  -0.0197 132 LYS A O   
1130 C  CB  . LYS A 130 ? 0.1646 0.0537 0.1150 -0.0176 0.0117  -0.0126 132 LYS A CB  
1131 C  CG  . LYS A 130 ? 0.1894 0.1240 0.2307 -0.0846 -0.0193 0.0350  132 LYS A CG  
1132 C  CD  . LYS A 130 ? 0.2601 0.0345 0.4839 -0.0604 -0.0380 0.0793  132 LYS A CD  
1133 C  CE  . LYS A 130 ? 0.3711 0.2354 0.3743 -0.0050 -0.0054 0.0750  132 LYS A CE  
1134 N  NZ  . LYS A 130 ? 0.6060 0.1526 0.7734 0.0494  0.0556  0.0582  132 LYS A NZ  
1135 N  N   . ALA A 131 ? 0.1132 0.0557 0.0934 -0.0416 0.0269  -0.0065 133 ALA A N   
1136 C  CA  . ALA A 131 ? 0.0979 0.0576 0.0917 -0.0348 0.0091  0.0053  133 ALA A CA  
1137 C  C   . ALA A 131 ? 0.1004 0.0540 0.0757 -0.0370 0.0054  -0.0079 133 ALA A C   
1138 O  O   . ALA A 131 ? 0.0885 0.0820 0.0725 -0.0178 0.0051  -0.0051 133 ALA A O   
1139 C  CB  . ALA A 131 ? 0.1120 0.0364 0.0662 -0.0429 0.0013  -0.0041 133 ALA A CB  
1140 N  N   . VAL A 132 ? 0.0980 0.0567 0.0898 -0.0229 0.0105  -0.0146 134 VAL A N   
1141 C  CA  . VAL A 132 ? 0.1248 0.0756 0.0757 -0.0067 -0.0041 -0.0064 134 VAL A CA  
1142 C  C   . VAL A 132 ? 0.1089 0.0696 0.0811 -0.0252 0.0092  0.0107  134 VAL A C   
1143 O  O   . VAL A 132 ? 0.1154 0.1023 0.0907 -0.0106 0.0186  0.0075  134 VAL A O   
1144 C  CB  . VAL A 132 ? 0.1510 0.0979 0.0946 -0.0347 0.0461  -0.0113 134 VAL A CB  
1145 C  CG1 . VAL A 132 ? 0.1536 0.1073 0.1309 -0.0297 0.0181  -0.0006 134 VAL A CG1 
1146 C  CG2 . VAL A 132 ? 0.1302 0.0856 0.1215 -0.0383 0.0328  -0.0093 134 VAL A CG2 
1147 N  N   . GLN A 133 ? 0.1065 0.0724 0.0731 -0.0253 0.0153  -0.0064 135 GLN A N   
1148 C  CA  . GLN A 133 ? 0.1172 0.0946 0.1016 -0.0463 0.0079  -0.0150 135 GLN A CA  
1149 C  C   . GLN A 133 ? 0.0810 0.0980 0.0775 -0.0211 -0.0248 0.0041  135 GLN A C   
1150 O  O   . GLN A 133 ? 0.1023 0.1521 0.1111 -0.0522 -0.0271 -0.0214 135 GLN A O   
1151 C  CB  . GLN A 133 ? 0.1446 0.0964 0.1212 -0.0681 0.0024  -0.0177 135 GLN A CB  
1152 C  CG  . GLN A 133 ? 0.1995 0.1507 0.1287 -0.0680 0.0269  0.0110  135 GLN A CG  
1153 C  CD  . GLN A 133 ? 0.2922 0.1779 0.2347 -0.1075 0.0201  -0.0039 135 GLN A CD  
1154 O  OE1 . GLN A 133 ? 0.3257 0.2710 0.3980 -0.1374 -0.0610 0.0208  135 GLN A OE1 
1155 N  NE2 . GLN A 133 ? 0.2322 0.2572 0.2991 -0.0558 0.0399  0.0910  135 GLN A NE2 
1156 N  N   A GLN A 134 ? 0.0882 0.0697 0.0685 -0.0111 0.0254  -0.0182 136 GLN A N   
1157 N  N   B GLN A 134 ? 0.0951 0.0788 0.0731 -0.0168 0.0262  -0.0100 136 GLN A N   
1158 C  CA  A GLN A 134 ? 0.0829 0.0779 0.0427 0.0041  0.0018  -0.0137 136 GLN A CA  
1159 C  CA  B GLN A 134 ? 0.1049 0.0973 0.0522 -0.0113 0.0066  -0.0131 136 GLN A CA  
1160 C  C   A GLN A 134 ? 0.0826 0.0732 0.0603 0.0067  -0.0085 -0.0166 136 GLN A C   
1161 C  C   B GLN A 134 ? 0.1291 0.0872 0.0739 0.0200  0.0022  -0.0052 136 GLN A C   
1162 O  O   A GLN A 134 ? 0.0299 0.0445 0.0372 0.0104  -0.0178 0.0095  136 GLN A O   
1163 O  O   B GLN A 134 ? 0.1163 0.0925 0.0865 0.0034  -0.0120 -0.0164 136 GLN A O   
1164 C  CB  A GLN A 134 ? 0.0831 0.0864 0.0495 0.0012  -0.0029 0.0089  136 GLN A CB  
1165 C  CB  B GLN A 134 ? 0.1072 0.1005 0.0527 -0.0143 -0.0077 0.0024  136 GLN A CB  
1166 C  CG  A GLN A 134 ? 0.1467 0.0619 0.0800 0.0046  0.0522  -0.0201 136 GLN A CG  
1167 C  CG  B GLN A 134 ? 0.1801 0.0979 0.1074 -0.0225 -0.0207 0.0250  136 GLN A CG  
1168 C  CD  A GLN A 134 ? 0.0773 0.0470 0.2017 0.0040  0.0053  0.0261  136 GLN A CD  
1169 C  CD  B GLN A 134 ? 0.1438 0.0889 0.2279 0.0129  -0.0278 -0.0134 136 GLN A CD  
1170 O  OE1 A GLN A 134 ? 0.2220 0.1020 0.1988 -0.0050 -0.0996 -0.0697 136 GLN A OE1 
1171 O  OE1 B GLN A 134 ? 0.2273 0.1801 0.2614 -0.0244 -0.0763 -0.1442 136 GLN A OE1 
1172 N  NE2 A GLN A 134 ? 0.2579 0.1241 0.3001 -0.0643 0.0140  0.1086  136 GLN A NE2 
1173 N  NE2 B GLN A 134 ? 0.2257 0.1967 0.2602 -0.0020 0.0447  0.0484  136 GLN A NE2 
1174 N  N   A PRO A 135 ? 0.0732 0.0757 0.0617 0.0093  -0.0032 -0.0108 137 PRO A N   
1175 N  N   B PRO A 135 ? 0.1102 0.0856 0.0705 -0.0067 -0.0044 -0.0124 137 PRO A N   
1176 C  CA  A PRO A 135 ? 0.0750 0.0831 0.0443 0.0109  -0.0250 -0.0008 137 PRO A CA  
1177 C  CA  B PRO A 135 ? 0.0883 0.0901 0.0576 0.0106  -0.0335 0.0055  137 PRO A CA  
1178 C  C   A PRO A 135 ? 0.0793 0.0881 0.0694 -0.0042 -0.0162 -0.0119 137 PRO A C   
1179 C  C   B PRO A 135 ? 0.0949 0.0950 0.0812 -0.0049 -0.0435 -0.0108 137 PRO A C   
1180 O  O   A PRO A 135 ? 0.0978 0.0812 0.0803 -0.0039 -0.0022 0.0001  137 PRO A O   
1181 O  O   B PRO A 135 ? 0.1344 0.0732 0.0908 0.0297  -0.0410 -0.0119 137 PRO A O   
1182 C  CB  A PRO A 135 ? 0.1056 0.1077 0.0401 0.0188  -0.0079 -0.0288 137 PRO A CB  
1183 C  CB  B PRO A 135 ? 0.1712 0.1320 0.0556 0.0023  -0.0387 0.0100  137 PRO A CB  
1184 C  CG  A PRO A 135 ? 0.0590 0.1083 0.0633 0.0120  -0.0285 -0.0237 137 PRO A CG  
1185 C  CG  B PRO A 135 ? 0.2036 0.1696 0.1152 -0.0340 -0.0238 0.0111  137 PRO A CG  
1186 C  CD  A PRO A 135 ? 0.0759 0.1337 0.0678 -0.0042 0.0031  -0.0392 137 PRO A CD  
1187 C  CD  B PRO A 135 ? 0.1241 0.1435 0.0627 -0.0108 -0.0181 -0.0325 137 PRO A CD  
1188 N  N   . ASP A 136 ? 0.0740 0.0856 0.0544 -0.0013 -0.0049 -0.0158 138 ASP A N   
1189 C  CA  . ASP A 136 ? 0.0718 0.1076 0.0660 -0.0080 0.0018  0.0051  138 ASP A CA  
1190 C  C   . ASP A 136 ? 0.0655 0.0470 0.0625 -0.0155 -0.0103 -0.0120 138 ASP A C   
1191 O  O   . ASP A 136 ? 0.0836 0.0628 0.0740 0.0030  -0.0141 -0.0017 138 ASP A O   
1192 C  CB  . ASP A 136 ? 0.0882 0.0935 0.0955 0.0073  0.0079  -0.0075 138 ASP A CB  
1193 C  CG  . ASP A 136 ? 0.1204 0.1004 0.0856 0.0161  -0.0083 -0.0190 138 ASP A CG  
1194 O  OD1 . ASP A 136 ? 0.1309 0.0813 0.0944 0.0203  -0.0147 -0.0104 138 ASP A OD1 
1195 O  OD2 . ASP A 136 ? 0.1854 0.1111 0.1198 0.0295  0.0177  -0.0380 138 ASP A OD2 
1196 N  N   . GLY A 137 ? 0.0725 0.0493 0.0539 -0.0096 -0.0122 -0.0126 139 GLY A N   
1197 C  CA  . GLY A 137 ? 0.0935 0.0527 0.0562 -0.0291 -0.0292 -0.0043 139 GLY A CA  
1198 C  C   . GLY A 137 ? 0.0588 0.0294 0.0557 -0.0244 -0.0163 0.0055  139 GLY A C   
1199 O  O   . GLY A 137 ? 0.0962 0.0335 0.0628 -0.0038 -0.0249 0.0093  139 GLY A O   
1200 N  N   . LEU A 138 ? 0.0496 0.0293 0.0566 -0.0092 -0.0130 -0.0083 140 LEU A N   
1201 C  CA  . LEU A 138 ? 0.0705 0.0233 0.0549 -0.0156 -0.0032 -0.0132 140 LEU A CA  
1202 C  C   . LEU A 138 ? 0.0653 0.0286 0.0469 -0.0089 -0.0067 -0.0063 140 LEU A C   
1203 O  O   . LEU A 138 ? 0.0785 0.0348 0.0484 -0.0022 -0.0135 -0.0060 140 LEU A O   
1204 C  CB  . LEU A 138 ? 0.0721 0.0379 0.0558 0.0030  -0.0034 0.0013  140 LEU A CB  
1205 C  CG  . LEU A 138 ? 0.0662 0.0398 0.0849 0.0020  0.0085  0.0057  140 LEU A CG  
1206 C  CD1 . LEU A 138 ? 0.0766 0.0607 0.0795 0.0021  0.0062  -0.0168 140 LEU A CD1 
1207 C  CD2 . LEU A 138 ? 0.1090 0.0621 0.0986 0.0149  -0.0068 0.0174  140 LEU A CD2 
1208 N  N   . ALA A 139 ? 0.0609 0.0238 0.0703 -0.0145 -0.0129 0.0037  141 ALA A N   
1209 C  CA  . ALA A 139 ? 0.0610 0.0223 0.0590 -0.0179 -0.0111 -0.0017 141 ALA A CA  
1210 C  C   . ALA A 139 ? 0.0686 0.0477 0.0320 -0.0107 -0.0237 0.0070  141 ALA A C   
1211 O  O   . ALA A 139 ? 0.0804 0.0478 0.0335 -0.0150 -0.0308 0.0046  141 ALA A O   
1212 C  CB  . ALA A 139 ? 0.0557 0.0662 0.0584 -0.0187 0.0023  0.0141  141 ALA A CB  
1213 N  N   . VAL A 140 ? 0.0564 0.0399 0.0354 -0.0152 -0.0147 -0.0075 142 VAL A N   
1214 C  CA  . VAL A 140 ? 0.0599 0.0434 0.0197 -0.0072 -0.0034 -0.0026 142 VAL A CA  
1215 C  C   . VAL A 140 ? 0.0557 0.0337 0.0311 0.0005  -0.0105 0.0117  142 VAL A C   
1216 O  O   . VAL A 140 ? 0.0671 0.0401 0.0269 -0.0072 -0.0078 0.0098  142 VAL A O   
1217 C  CB  . VAL A 140 ? 0.0567 0.0651 0.0276 -0.0016 -0.0146 0.0009  142 VAL A CB  
1218 C  CG1 . VAL A 140 ? 0.0864 0.1120 0.0269 0.0373  -0.0184 -0.0301 142 VAL A CG1 
1219 C  CG2 . VAL A 140 ? 0.0533 0.1212 0.0469 -0.0238 0.0012  0.0228  142 VAL A CG2 
1220 N  N   . LEU A 141 ? 0.0539 0.0312 0.0477 -0.0071 -0.0109 -0.0061 143 LEU A N   
1221 C  CA  . LEU A 141 ? 0.0522 0.0387 0.0547 -0.0115 -0.0193 -0.0044 143 LEU A CA  
1222 C  C   . LEU A 141 ? 0.0636 0.0355 0.0232 -0.0140 -0.0094 0.0067  143 LEU A C   
1223 O  O   . LEU A 141 ? 0.0995 0.0452 0.0242 -0.0159 -0.0054 0.0041  143 LEU A O   
1224 C  CB  . LEU A 141 ? 0.0659 0.0562 0.0756 -0.0086 -0.0305 0.0223  143 LEU A CB  
1225 C  CG  . LEU A 141 ? 0.0691 0.0637 0.0952 -0.0113 -0.0105 0.0279  143 LEU A CG  
1226 C  CD1 . LEU A 141 ? 0.0872 0.1187 0.1040 -0.0136 -0.0244 0.0549  143 LEU A CD1 
1227 C  CD2 . LEU A 141 ? 0.0829 0.1177 0.0892 0.0139  -0.0166 0.0153  143 LEU A CD2 
1228 N  N   . GLY A 142 ? 0.0593 0.0240 0.0422 -0.0091 -0.0053 0.0071  144 GLY A N   
1229 C  CA  . GLY A 142 ? 0.0601 0.0294 0.0267 -0.0127 -0.0023 0.0002  144 GLY A CA  
1230 C  C   . GLY A 142 ? 0.0484 0.0234 0.0311 -0.0039 -0.0100 0.0005  144 GLY A C   
1231 O  O   . GLY A 142 ? 0.0734 0.0527 0.0355 -0.0193 0.0026  -0.0024 144 GLY A O   
1232 N  N   . ILE A 143 ? 0.0572 0.0234 0.0354 -0.0076 -0.0175 -0.0025 145 ILE A N   
1233 C  CA  . ILE A 143 ? 0.0449 0.0272 0.0440 -0.0064 -0.0179 0.0026  145 ILE A CA  
1234 C  C   . ILE A 143 ? 0.0390 0.0286 0.0495 -0.0095 -0.0158 0.0036  145 ILE A C   
1235 O  O   . ILE A 143 ? 0.0715 0.0544 0.0408 -0.0044 -0.0108 -0.0022 145 ILE A O   
1236 C  CB  . ILE A 143 ? 0.0469 0.0443 0.0610 -0.0048 -0.0278 0.0009  145 ILE A CB  
1237 C  CG1 . ILE A 143 ? 0.0661 0.0555 0.0891 0.0248  -0.0357 0.0006  145 ILE A CG1 
1238 C  CG2 . ILE A 143 ? 0.0583 0.0628 0.1074 -0.0172 -0.0236 -0.0184 145 ILE A CG2 
1239 C  CD1 . ILE A 143 ? 0.0563 0.0593 0.0731 0.0006  -0.0277 0.0239  145 ILE A CD1 
1240 N  N   . PHE A 144 ? 0.0531 0.0223 0.0413 -0.0017 -0.0208 0.0000  146 PHE A N   
1241 C  CA  . PHE A 144 ? 0.0680 0.0265 0.0478 0.0137  -0.0212 0.0102  146 PHE A CA  
1242 C  C   . PHE A 144 ? 0.0589 0.0282 0.0513 -0.0053 -0.0069 0.0081  146 PHE A C   
1243 O  O   . PHE A 144 ? 0.0601 0.0458 0.0715 -0.0043 -0.0125 -0.0038 146 PHE A O   
1244 C  CB  . PHE A 144 ? 0.0770 0.0242 0.0389 -0.0119 -0.0296 0.0064  146 PHE A CB  
1245 C  CG  . PHE A 144 ? 0.0557 0.0232 0.0422 -0.0066 -0.0223 0.0026  146 PHE A CG  
1246 C  CD1 . PHE A 144 ? 0.0564 0.0417 0.0459 0.0026  -0.0280 0.0106  146 PHE A CD1 
1247 C  CD2 . PHE A 144 ? 0.0882 0.0241 0.0441 -0.0052 -0.0156 0.0069  146 PHE A CD2 
1248 C  CE1 . PHE A 144 ? 0.0480 0.0442 0.0445 0.0131  -0.0285 0.0076  146 PHE A CE1 
1249 C  CE2 . PHE A 144 ? 0.0566 0.0330 0.0557 -0.0097 -0.0095 0.0164  146 PHE A CE2 
1250 C  CZ  . PHE A 144 ? 0.0521 0.0381 0.0619 -0.0001 -0.0089 0.0168  146 PHE A CZ  
1251 N  N   . LEU A 145 ? 0.0685 0.0457 0.0485 -0.0106 -0.0061 -0.0158 147 LEU A N   
1252 C  CA  . LEU A 145 ? 0.1037 0.0388 0.0346 -0.0166 -0.0131 -0.0042 147 LEU A CA  
1253 C  C   . LEU A 145 ? 0.0865 0.0414 0.0463 -0.0201 -0.0057 -0.0042 147 LEU A C   
1254 O  O   . LEU A 145 ? 0.0829 0.0584 0.0565 -0.0160 -0.0177 0.0006  147 LEU A O   
1255 C  CB  . LEU A 145 ? 0.1141 0.0488 0.0382 -0.0052 -0.0087 0.0012  147 LEU A CB  
1256 C  CG  . LEU A 145 ? 0.1240 0.0291 0.0558 -0.0096 -0.0172 -0.0048 147 LEU A CG  
1257 C  CD1 . LEU A 145 ? 0.1525 0.0364 0.0487 -0.0212 -0.0189 -0.0064 147 LEU A CD1 
1258 C  CD2 . LEU A 145 ? 0.1381 0.0730 0.0556 -0.0074 -0.0160 0.0047  147 LEU A CD2 
1259 N  N   . LYS A 146 ? 0.0973 0.0233 0.0662 -0.0216 -0.0190 -0.0070 148 LYS A N   
1260 C  CA  . LYS A 146 ? 0.1049 0.0214 0.0697 -0.0216 -0.0308 0.0083  148 LYS A CA  
1261 C  C   . LYS A 146 ? 0.1076 0.0400 0.0882 -0.0085 -0.0392 -0.0081 148 LYS A C   
1262 O  O   . LYS A 146 ? 0.1302 0.0741 0.0779 0.0081  -0.0460 -0.0016 148 LYS A O   
1263 C  CB  . LYS A 146 ? 0.1134 0.0795 0.0812 -0.0270 -0.0270 0.0269  148 LYS A CB  
1264 C  CG  . LYS A 146 ? 0.1259 0.1255 0.0978 -0.0125 0.0108  0.0107  148 LYS A CG  
1265 C  CD  . LYS A 146 ? 0.2024 0.2521 0.1704 -0.0398 0.0447  0.0730  148 LYS A CD  
1266 C  CE  . LYS A 146 ? 0.2253 0.3944 0.2106 -0.0303 0.0710  0.0713  148 LYS A CE  
1267 N  NZ  . LYS A 146 ? 0.4347 0.6511 0.2666 -0.3037 0.0577  0.1531  148 LYS A NZ  
1268 N  N   . VAL A 147 ? 0.1423 0.0215 0.0802 -0.0139 -0.0283 0.0017  149 VAL A N   
1269 C  CA  . VAL A 147 ? 0.1428 0.0496 0.0935 -0.0106 -0.0273 -0.0194 149 VAL A CA  
1270 C  C   . VAL A 147 ? 0.1421 0.0502 0.0988 -0.0077 -0.0266 -0.0181 149 VAL A C   
1271 O  O   . VAL A 147 ? 0.1884 0.0713 0.1309 -0.0114 -0.0532 0.0082  149 VAL A O   
1272 C  CB  . VAL A 147 ? 0.1223 0.0952 0.0941 0.0021  -0.0379 -0.0206 149 VAL A CB  
1273 C  CG1 . VAL A 147 ? 0.1733 0.1442 0.0943 -0.0068 -0.0252 -0.0455 149 VAL A CG1 
1274 C  CG2 . VAL A 147 ? 0.1180 0.1449 0.1280 -0.0204 0.0009  -0.0253 149 VAL A CG2 
1275 N  N   . GLY A 148 ? 0.1316 0.0813 0.0988 -0.0421 -0.0381 -0.0132 150 GLY A N   
1276 C  CA  . GLY A 148 ? 0.1582 0.1108 0.1428 -0.0695 -0.0635 0.0264  150 GLY A CA  
1277 C  C   . GLY A 148 ? 0.1266 0.0937 0.1203 -0.0600 -0.0444 0.0066  150 GLY A C   
1278 O  O   . GLY A 148 ? 0.1629 0.1216 0.1172 -0.0611 -0.0423 -0.0103 150 GLY A O   
1279 N  N   A SER A 149 ? 0.1640 0.0786 0.1374 -0.0324 -0.0438 0.0074  151 SER A N   
1280 N  N   B SER A 149 ? 0.1564 0.0664 0.1513 -0.0359 -0.0445 0.0085  151 SER A N   
1281 C  CA  A SER A 149 ? 0.1855 0.0926 0.1446 -0.0064 -0.0516 0.0161  151 SER A CA  
1282 C  CA  B SER A 149 ? 0.1518 0.0953 0.1496 -0.0084 -0.0513 -0.0033 151 SER A CA  
1283 C  C   A SER A 149 ? 0.1532 0.0874 0.1028 -0.0157 -0.0630 -0.0144 151 SER A C   
1284 C  C   B SER A 149 ? 0.1496 0.0836 0.1058 0.0021  -0.0613 -0.0190 151 SER A C   
1285 O  O   A SER A 149 ? 0.1672 0.0876 0.0809 -0.0406 -0.0204 -0.0124 151 SER A O   
1286 O  O   B SER A 149 ? 0.1456 0.1067 0.0752 0.0055  -0.0414 -0.0279 151 SER A O   
1287 C  CB  A SER A 149 ? 0.2103 0.1999 0.2404 -0.0363 -0.0133 -0.0362 151 SER A CB  
1288 C  CB  B SER A 149 ? 0.1320 0.1269 0.2613 -0.0710 -0.0234 -0.0440 151 SER A CB  
1289 O  OG  A SER A 149 ? 0.2697 0.1887 0.2702 -0.0088 -0.0132 -0.0496 151 SER A OG  
1290 O  OG  B SER A 149 ? 0.1084 0.1765 0.3004 -0.0216 -0.0518 0.1005  151 SER A OG  
1291 N  N   . ALA A 150 ? 0.1719 0.1049 0.1050 0.0032  -0.0528 0.0006  152 ALA A N   
1292 C  CA  . ALA A 150 ? 0.1528 0.0935 0.0759 0.0244  -0.0341 -0.0173 152 ALA A CA  
1293 C  C   . ALA A 150 ? 0.1391 0.0908 0.0995 0.0192  -0.0501 -0.0243 152 ALA A C   
1294 O  O   . ALA A 150 ? 0.1370 0.1334 0.1546 0.0315  -0.0230 -0.0211 152 ALA A O   
1295 C  CB  . ALA A 150 ? 0.2297 0.1116 0.0779 0.0176  -0.0523 -0.0394 152 ALA A CB  
1296 N  N   . LYS A 151 ? 0.1812 0.0856 0.1190 -0.0019 -0.0398 -0.0062 153 LYS A N   
1297 C  CA  . LYS A 151 ? 0.1550 0.0840 0.1306 0.0178  -0.0400 0.0164  153 LYS A CA  
1298 C  C   . LYS A 151 ? 0.1367 0.0926 0.1177 0.0026  -0.0417 0.0008  153 LYS A C   
1299 O  O   . LYS A 151 ? 0.1220 0.1116 0.0978 -0.0133 -0.0615 -0.0215 153 LYS A O   
1300 C  CB  . LYS A 151 ? 0.1689 0.0786 0.1229 0.0110  -0.0672 0.0278  153 LYS A CB  
1301 C  CG  . LYS A 151 ? 0.2243 0.1023 0.1862 0.0020  -0.0769 -0.0124 153 LYS A CG  
1302 C  CD  . LYS A 151 ? 0.3640 0.0399 0.2006 -0.0223 -0.0019 -0.0434 153 LYS A CD  
1303 C  CE  . LYS A 151 ? 0.4889 0.1230 0.1870 0.0603  -0.0848 -0.0768 153 LYS A CE  
1304 N  NZ  . LYS A 151 ? 0.4459 0.4014 0.1503 0.0450  -0.0491 -0.0451 153 LYS A NZ  
1305 N  N   . PRO A 152 ? 0.1388 0.0861 0.1769 0.0095  -0.0547 0.0192  154 PRO A N   
1306 C  CA  . PRO A 152 ? 0.1238 0.1478 0.2055 -0.0048 -0.0836 0.0385  154 PRO A CA  
1307 C  C   . PRO A 152 ? 0.1525 0.1295 0.1291 0.0006  -0.1059 0.0067  154 PRO A C   
1308 O  O   . PRO A 152 ? 0.1956 0.1543 0.1413 0.0099  -0.0906 0.0116  154 PRO A O   
1309 C  CB  . PRO A 152 ? 0.1248 0.1248 0.2734 0.0293  -0.0396 0.0326  154 PRO A CB  
1310 C  CG  . PRO A 152 ? 0.2217 0.2401 0.2372 0.0137  -0.0546 0.0973  154 PRO A CG  
1311 C  CD  . PRO A 152 ? 0.1769 0.1725 0.1902 -0.0214 -0.0032 0.0143  154 PRO A CD  
1312 N  N   . GLY A 153 ? 0.1526 0.1111 0.1643 0.0326  -0.0794 -0.0166 155 GLY A N   
1313 C  CA  . GLY A 153 ? 0.1539 0.1312 0.1841 0.0156  -0.0630 0.0050  155 GLY A CA  
1314 C  C   . GLY A 153 ? 0.1549 0.0891 0.0988 0.0011  -0.0518 0.0247  155 GLY A C   
1315 O  O   . GLY A 153 ? 0.1927 0.1170 0.2311 -0.0145 -0.0401 0.0392  155 GLY A O   
1316 N  N   . LEU A 154 ? 0.1241 0.1327 0.1280 0.0152  -0.0613 0.0006  156 LEU A N   
1317 C  CA  . LEU A 154 ? 0.1301 0.0993 0.0650 0.0117  -0.0684 -0.0023 156 LEU A CA  
1318 C  C   . LEU A 154 ? 0.1676 0.0989 0.0741 -0.0320 -0.0611 -0.0219 156 LEU A C   
1319 O  O   . LEU A 154 ? 0.1779 0.0901 0.0619 -0.0242 -0.0623 0.0013  156 LEU A O   
1320 C  CB  . LEU A 154 ? 0.1507 0.1099 0.0829 -0.0135 -0.0653 0.0348  156 LEU A CB  
1321 C  CG  . LEU A 154 ? 0.1416 0.1076 0.0837 -0.0291 -0.0526 0.0025  156 LEU A CG  
1322 C  CD1 . LEU A 154 ? 0.2247 0.1135 0.0729 -0.0515 -0.0745 -0.0019 156 LEU A CD1 
1323 C  CD2 . LEU A 154 ? 0.1337 0.1238 0.1244 0.0144  -0.0658 0.0053  156 LEU A CD2 
1324 N  N   . GLN A 155 ? 0.1718 0.1040 0.0770 -0.0318 -0.0727 -0.0127 157 GLN A N   
1325 C  CA  . GLN A 155 ? 0.1453 0.1331 0.0768 -0.0414 -0.0517 -0.0182 157 GLN A CA  
1326 C  C   . GLN A 155 ? 0.1557 0.1242 0.0759 -0.0147 -0.0640 -0.0084 157 GLN A C   
1327 O  O   . GLN A 155 ? 0.1974 0.1050 0.0653 -0.0377 -0.0501 -0.0111 157 GLN A O   
1328 C  CB  . GLN A 155 ? 0.1905 0.1388 0.0818 -0.0653 -0.0802 -0.0173 157 GLN A CB  
1329 C  CG  . GLN A 155 ? 0.2319 0.1424 0.1248 -0.0019 -0.0743 -0.0271 157 GLN A CG  
1330 C  CD  . GLN A 155 ? 0.2264 0.1194 0.0847 -0.0075 -0.0524 0.0015  157 GLN A CD  
1331 O  OE1 . GLN A 155 ? 0.2612 0.1049 0.0747 -0.0193 -0.0480 -0.0106 157 GLN A OE1 
1332 N  NE2 . GLN A 155 ? 0.2369 0.1295 0.1172 -0.0647 -0.0497 -0.0494 157 GLN A NE2 
1333 N  N   . LYS A 156 ? 0.2114 0.1277 0.0673 -0.0100 -0.0910 0.0003  158 LYS A N   
1334 C  CA  . LYS A 156 ? 0.1664 0.1137 0.1266 -0.0122 -0.0881 0.0111  158 LYS A CA  
1335 C  C   . LYS A 156 ? 0.1729 0.1266 0.0838 -0.0260 -0.0615 -0.0127 158 LYS A C   
1336 O  O   . LYS A 156 ? 0.1859 0.1791 0.0758 -0.0346 -0.0610 -0.0034 158 LYS A O   
1337 C  CB  . LYS A 156 ? 0.1991 0.1150 0.1520 0.0042  -0.0715 0.0266  158 LYS A CB  
1338 C  CG  . LYS A 156 ? 0.2588 0.2635 0.2462 -0.0431 -0.1001 0.0197  158 LYS A CG  
1339 N  N   . VAL A 157 ? 0.1622 0.1100 0.0916 -0.0120 -0.0832 -0.0316 159 VAL A N   
1340 C  CA  . VAL A 157 ? 0.1553 0.1005 0.0558 -0.0172 -0.0488 -0.0048 159 VAL A CA  
1341 C  C   . VAL A 157 ? 0.1808 0.1125 0.0768 -0.0042 -0.0427 -0.0253 159 VAL A C   
1342 O  O   . VAL A 157 ? 0.1704 0.1005 0.0846 0.0026  -0.0531 -0.0158 159 VAL A O   
1343 C  CB  . VAL A 157 ? 0.1865 0.1111 0.0588 0.0048  -0.0696 0.0083  159 VAL A CB  
1344 C  CG1 . VAL A 157 ? 0.1740 0.1222 0.0891 -0.0132 -0.0528 -0.0042 159 VAL A CG1 
1345 C  CG2 . VAL A 157 ? 0.2336 0.1428 0.0803 0.0044  -0.0597 -0.0406 159 VAL A CG2 
1346 N  N   . VAL A 158 ? 0.1769 0.0917 0.0609 -0.0093 -0.0553 -0.0323 160 VAL A N   
1347 C  CA  . VAL A 158 ? 0.1973 0.1259 0.0951 -0.0070 -0.0392 -0.0403 160 VAL A CA  
1348 C  C   . VAL A 158 ? 0.2152 0.1118 0.1005 -0.0267 -0.0505 -0.0466 160 VAL A C   
1349 O  O   . VAL A 158 ? 0.2225 0.1054 0.0898 -0.0414 -0.0154 -0.0075 160 VAL A O   
1350 C  CB  . VAL A 158 ? 0.3532 0.0777 0.0935 0.0278  0.0245  0.0322  160 VAL A CB  
1351 C  CG1 . VAL A 158 ? 0.2597 0.1679 0.1816 -0.0220 -0.0661 -0.0678 160 VAL A CG1 
1352 C  CG2 . VAL A 158 ? 0.3729 0.1258 0.1047 0.0463  0.0152  0.0167  160 VAL A CG2 
1353 N  N   . ASP A 159 ? 0.2110 0.1574 0.0646 -0.0480 -0.0619 -0.0294 161 ASP A N   
1354 C  CA  . ASP A 159 ? 0.2754 0.1532 0.0653 -0.0668 -0.0796 0.0013  161 ASP A CA  
1355 C  C   . ASP A 159 ? 0.2714 0.1786 0.0801 -0.0778 -0.0580 -0.0032 161 ASP A C   
1356 O  O   . ASP A 159 ? 0.4160 0.2401 0.1011 -0.1715 0.0100  -0.0115 161 ASP A O   
1357 C  CB  . ASP A 159 ? 0.2949 0.1852 0.0917 -0.0708 -0.0994 -0.0311 161 ASP A CB  
1358 C  CG  . ASP A 159 ? 0.2517 0.1755 0.0627 -0.0499 -0.0091 -0.0357 161 ASP A CG  
1359 O  OD1 . ASP A 159 ? 0.2800 0.2042 0.1923 -0.0495 -0.0248 -0.0424 161 ASP A OD1 
1360 O  OD2 . ASP A 159 ? 0.2852 0.3445 0.1342 -0.0340 -0.0649 -0.0474 161 ASP A OD2 
1361 N  N   . VAL A 160 ? 0.2710 0.1234 0.0840 -0.0490 -0.0744 0.0147  162 VAL A N   
1362 C  CA  . VAL A 160 ? 0.2389 0.1456 0.1146 -0.0391 -0.0858 0.0203  162 VAL A CA  
1363 C  C   . VAL A 160 ? 0.2178 0.1049 0.0588 -0.0309 -0.0133 0.0120  162 VAL A C   
1364 O  O   . VAL A 160 ? 0.2694 0.1629 0.0417 -0.0619 -0.0137 0.0189  162 VAL A O   
1365 C  CB  . VAL A 160 ? 0.2897 0.1392 0.1406 -0.0199 -0.0748 0.0232  162 VAL A CB  
1366 C  CG1 . VAL A 160 ? 0.3197 0.1298 0.1586 -0.0165 -0.1092 -0.0065 162 VAL A CG1 
1367 C  CG2 . VAL A 160 ? 0.2714 0.2828 0.1690 -0.0616 -0.0544 0.0809  162 VAL A CG2 
1368 N  N   . LEU A 161 ? 0.2368 0.1176 0.0847 -0.0310 -0.0398 0.0085  163 LEU A N   
1369 C  CA  . LEU A 161 ? 0.2182 0.1053 0.0601 0.0039  0.0058  -0.0040 163 LEU A CA  
1370 C  C   . LEU A 161 ? 0.2569 0.1287 0.0914 0.0207  0.0164  -0.0460 163 LEU A C   
1371 O  O   . LEU A 161 ? 0.2653 0.1313 0.0624 -0.0012 -0.0013 0.0152  163 LEU A O   
1372 C  CB  . LEU A 161 ? 0.2454 0.0831 0.0564 -0.0098 -0.0125 -0.0216 163 LEU A CB  
1373 C  CG  . LEU A 161 ? 0.2067 0.0768 0.0432 0.0072  -0.0215 0.0020  163 LEU A CG  
1374 C  CD1 . LEU A 161 ? 0.2322 0.0871 0.1076 -0.0245 -0.0239 0.0358  163 LEU A CD1 
1375 C  CD2 . LEU A 161 ? 0.2570 0.0926 0.0513 -0.0122 -0.0118 0.0006  163 LEU A CD2 
1376 N  N   . ASP A 162 ? 0.4005 0.1055 0.0671 -0.0225 -0.0009 -0.0024 164 ASP A N   
1377 C  CA  . ASP A 162 ? 0.4354 0.1507 0.0829 -0.0138 0.0287  -0.0653 164 ASP A CA  
1378 C  C   . ASP A 162 ? 0.3669 0.2053 0.1129 -0.0228 -0.0153 -0.0051 164 ASP A C   
1379 O  O   . ASP A 162 ? 0.5429 0.1926 0.1830 0.0609  0.1174  -0.0294 164 ASP A O   
1380 C  CB  . ASP A 162 ? 0.5940 0.2261 0.1248 -0.1014 -0.0860 -0.1016 164 ASP A CB  
1381 C  CG  . ASP A 162 ? 0.5500 0.4722 0.2487 -0.0610 0.0241  0.0408  164 ASP A CG  
1382 O  OD1 . ASP A 162 ? 0.5426 0.4805 0.3028 -0.1725 0.0551  -0.0214 164 ASP A OD1 
1383 O  OD2 . ASP A 162 ? 0.7120 0.6474 0.2261 -0.0602 0.1483  -0.0661 164 ASP A OD2 
1384 N  N   . SER A 163 ? 0.3583 0.2121 0.0417 -0.0153 -0.0332 0.0164  165 SER A N   
1385 C  CA  . SER A 163 ? 0.3483 0.2178 0.0379 -0.0324 -0.0100 -0.0075 165 SER A CA  
1386 C  C   . SER A 163 ? 0.3051 0.1503 0.0206 -0.0170 -0.0016 0.0190  165 SER A C   
1387 O  O   . SER A 163 ? 0.3785 0.1531 0.0553 -0.0119 0.0304  0.0323  165 SER A O   
1388 C  CB  . SER A 163 ? 0.4300 0.2757 0.1137 0.0001  0.0771  0.0643  165 SER A CB  
1389 O  OG  . SER A 163 ? 0.3307 0.2293 0.1625 0.0198  0.0342  0.0660  165 SER A OG  
1390 N  N   . ILE A 164 ? 0.2858 0.1128 0.0197 -0.0209 -0.0171 0.0046  166 ILE A N   
1391 C  CA  . ILE A 164 ? 0.2606 0.1080 0.0695 -0.0221 0.0148  -0.0079 166 ILE A CA  
1392 C  C   . ILE A 164 ? 0.2095 0.1164 0.0691 -0.0188 0.0270  -0.0166 166 ILE A C   
1393 O  O   . ILE A 164 ? 0.1985 0.1125 0.0660 -0.0190 0.0211  0.0107  166 ILE A O   
1394 C  CB  . ILE A 164 ? 0.2238 0.0812 0.0558 -0.0236 0.0141  0.0036  166 ILE A CB  
1395 C  CG1 . ILE A 164 ? 0.2631 0.0989 0.0250 -0.0337 0.0025  0.0243  166 ILE A CG1 
1396 C  CG2 . ILE A 164 ? 0.2354 0.0908 0.0812 -0.0100 0.0088  0.0160  166 ILE A CG2 
1397 C  CD1 . ILE A 164 ? 0.2211 0.1014 0.0601 -0.0072 0.0385  -0.0149 166 ILE A CD1 
1398 N  N   . LYS A 165 ? 0.2309 0.0932 0.0697 -0.0347 0.0151  -0.0082 167 LYS A N   
1399 C  CA  . LYS A 165 ? 0.1798 0.1185 0.0633 -0.0263 0.0117  -0.0259 167 LYS A CA  
1400 C  C   . LYS A 165 ? 0.1898 0.1059 0.0566 -0.0325 0.0347  -0.0126 167 LYS A C   
1401 O  O   . LYS A 165 ? 0.2127 0.1164 0.0538 -0.0652 0.0133  -0.0152 167 LYS A O   
1402 C  CB  . LYS A 165 ? 0.2383 0.1242 0.0443 -0.0290 0.0174  -0.0203 167 LYS A CB  
1403 C  CG  . LYS A 165 ? 0.2236 0.1489 0.1058 -0.0259 0.0201  -0.0201 167 LYS A CG  
1404 C  CD  . LYS A 165 ? 0.3582 0.2416 0.1823 0.0216  -0.0675 -0.1315 167 LYS A CD  
1405 C  CE  . LYS A 165 ? 0.4554 0.2829 0.2577 0.0625  -0.0136 -0.1223 167 LYS A CE  
1406 N  NZ  . LYS A 165 ? 0.4246 0.3167 0.3762 -0.0114 0.0522  -0.2015 167 LYS A NZ  
1407 N  N   . THR A 166 ? 0.1962 0.0962 0.1154 -0.0258 0.0526  0.0040  168 THR A N   
1408 C  CA  . THR A 166 ? 0.1883 0.1081 0.0838 -0.0158 0.0458  -0.0022 168 THR A CA  
1409 C  C   . THR A 166 ? 0.2067 0.1316 0.0274 -0.0080 0.0486  0.0126  168 THR A C   
1410 O  O   . THR A 166 ? 0.2010 0.1036 0.0716 -0.0242 0.0288  -0.0003 168 THR A O   
1411 C  CB  . THR A 166 ? 0.2514 0.1152 0.0803 -0.0436 0.0587  -0.0234 168 THR A CB  
1412 O  OG1 . THR A 166 ? 0.2848 0.1701 0.0549 -0.0651 0.0310  -0.0040 168 THR A OG1 
1413 C  CG2 . THR A 166 ? 0.3104 0.1011 0.0589 -0.0429 0.0820  -0.0151 168 THR A CG2 
1414 N  N   . LYS A 167 ? 0.2375 0.1453 0.0748 -0.0950 0.0610  -0.0044 169 LYS A N   
1415 C  CA  . LYS A 167 ? 0.2383 0.1064 0.0809 -0.0703 0.0272  0.0109  169 LYS A CA  
1416 C  C   . LYS A 167 ? 0.2178 0.1238 0.0783 -0.0585 0.0485  0.0301  169 LYS A C   
1417 O  O   . LYS A 167 ? 0.2612 0.1744 0.0804 -0.0905 0.0568  -0.0035 169 LYS A O   
1418 C  CB  . LYS A 167 ? 0.2185 0.1453 0.1197 -0.0520 0.0295  -0.0118 169 LYS A CB  
1419 C  CG  . LYS A 167 ? 0.2250 0.1089 0.1205 -0.0387 0.0284  0.0145  169 LYS A CG  
1420 C  CD  . LYS A 167 ? 0.2335 0.1553 0.1363 -0.0506 0.0190  -0.0212 169 LYS A CD  
1421 C  CE  . LYS A 167 ? 0.2225 0.3194 0.2820 0.0182  0.0575  -0.0042 169 LYS A CE  
1422 N  NZ  . LYS A 167 ? 0.3365 0.3922 0.2182 0.0679  -0.0142 -0.0048 169 LYS A NZ  
1423 N  N   . GLY A 168 ? 0.2643 0.0961 0.0897 -0.0449 0.0104  0.0241  170 GLY A N   
1424 C  CA  . GLY A 168 ? 0.2449 0.1298 0.1617 -0.0592 -0.0147 0.0854  170 GLY A CA  
1425 C  C   . GLY A 168 ? 0.2644 0.1199 0.1463 -0.0237 0.0008  0.0309  170 GLY A C   
1426 O  O   . GLY A 168 ? 0.3198 0.1172 0.2426 -0.0513 0.0000  0.0683  170 GLY A O   
1427 N  N   . LYS A 169 ? 0.2603 0.1107 0.0812 -0.0348 0.0538  0.0341  171 LYS A N   
1428 C  CA  . LYS A 169 ? 0.2672 0.1203 0.0818 -0.0219 0.0407  0.0290  171 LYS A CA  
1429 C  C   . LYS A 169 ? 0.2730 0.1385 0.0346 0.0093  0.0197  0.0185  171 LYS A C   
1430 O  O   . LYS A 169 ? 0.2725 0.1568 0.0477 -0.0416 0.0129  0.0333  171 LYS A O   
1431 C  CB  . LYS A 169 ? 0.2690 0.1076 0.1381 -0.0508 0.0442  0.0141  171 LYS A CB  
1432 C  CG  . LYS A 169 ? 0.2613 0.1694 0.1442 0.0093  0.0230  -0.0322 171 LYS A CG  
1433 C  CD  . LYS A 169 ? 0.3285 0.3286 0.1044 -0.0193 -0.0207 -0.0706 171 LYS A CD  
1434 C  CE  . LYS A 169 ? 0.2988 0.2861 0.1342 -0.0103 -0.0098 -0.0152 171 LYS A CE  
1435 N  NZ  . LYS A 169 ? 0.4925 0.2006 0.1852 -0.0787 0.0858  -0.0231 171 LYS A NZ  
1436 N  N   . SER A 170 ? 0.2603 0.1561 0.0885 -0.0062 0.0156  0.0464  172 SER A N   
1437 C  CA  . SER A 170 ? 0.2836 0.1684 0.0987 0.0054  0.0242  -0.0178 172 SER A CA  
1438 C  C   . SER A 170 ? 0.2337 0.2458 0.0389 0.0317  0.0476  0.0583  172 SER A C   
1439 O  O   . SER A 170 ? 0.2967 0.3167 0.0250 0.0809  0.0145  0.0606  172 SER A O   
1440 C  CB  . SER A 170 ? 0.2838 0.1467 0.0810 -0.0236 0.0314  0.0361  172 SER A CB  
1441 O  OG  . SER A 170 ? 0.4547 0.2156 0.2016 0.0671  0.1191  0.1407  172 SER A OG  
1442 N  N   . ALA A 171 ? 0.1941 0.2480 0.0942 0.0750  -0.0077 0.0108  173 ALA A N   
1443 C  CA  . ALA A 171 ? 0.2049 0.2658 0.0847 0.0567  -0.0149 0.0508  173 ALA A CA  
1444 C  C   . ALA A 171 ? 0.2736 0.2522 0.0505 0.0974  -0.0513 0.0006  173 ALA A C   
1445 O  O   . ALA A 171 ? 0.2552 0.2332 0.0417 0.0726  -0.0189 0.0469  173 ALA A O   
1446 C  CB  . ALA A 171 ? 0.3173 0.2192 0.0864 0.1150  -0.0383 0.0067  173 ALA A CB  
1447 N  N   . ASP A 172 ? 0.2383 0.2827 0.0871 0.0664  -0.0287 0.0939  174 ASP A N   
1448 C  CA  . ASP A 172 ? 0.2718 0.2604 0.0743 0.0528  0.0019  0.0618  174 ASP A CA  
1449 C  C   . ASP A 172 ? 0.3131 0.2597 0.0486 0.0172  -0.0644 0.0517  174 ASP A C   
1450 O  O   . ASP A 172 ? 0.2980 0.2843 0.1039 0.0095  0.0119  0.0211  174 ASP A O   
1451 C  CB  . ASP A 172 ? 0.1513 0.2746 0.1514 0.0241  -0.0225 0.0552  174 ASP A CB  
1452 C  CG  . ASP A 172 ? 0.3794 0.3177 0.2222 -0.0069 -0.0427 0.1148  174 ASP A CG  
1453 O  OD1 . ASP A 172 ? 0.3835 0.4451 0.2046 0.0161  -0.0992 0.0505  174 ASP A OD1 
1454 O  OD2 . ASP A 172 ? 0.2103 0.3332 0.1888 -0.0066 0.0070  0.0858  174 ASP A OD2 
1455 N  N   . PHE A 173 ? 0.1729 0.2430 0.0891 0.0214  -0.0147 0.0559  175 PHE A N   
1456 C  CA  . PHE A 173 ? 0.2358 0.2376 0.0916 0.0272  -0.0238 0.0946  175 PHE A CA  
1457 C  C   . PHE A 173 ? 0.2206 0.1905 0.0840 -0.0117 -0.0558 0.0447  175 PHE A C   
1458 O  O   . PHE A 173 ? 0.2985 0.1963 0.0906 0.0472  -0.0771 0.0185  175 PHE A O   
1459 C  CB  . PHE A 173 ? 0.2523 0.1362 0.0882 0.0309  -0.0447 0.0337  175 PHE A CB  
1460 C  CG  . PHE A 173 ? 0.2680 0.1134 0.1077 0.0559  -0.0269 0.0270  175 PHE A CG  
1461 C  CD1 . PHE A 173 ? 0.3124 0.1611 0.1084 -0.0015 -0.0302 0.0000  175 PHE A CD1 
1462 C  CD2 . PHE A 173 ? 0.2498 0.1381 0.0980 0.0260  -0.0455 0.0145  175 PHE A CD2 
1463 C  CE1 . PHE A 173 ? 0.3901 0.1446 0.1242 0.0303  0.0162  0.0030  175 PHE A CE1 
1464 C  CE2 . PHE A 173 ? 0.2615 0.1084 0.1208 0.0363  -0.0444 0.0255  175 PHE A CE2 
1465 C  CZ  . PHE A 173 ? 0.3024 0.1801 0.1273 0.0449  -0.0274 -0.0195 175 PHE A CZ  
1466 N  N   . THR A 174 ? 0.2343 0.1959 0.0775 0.0372  -0.0564 0.0275  176 THR A N   
1467 C  CA  . THR A 174 ? 0.1876 0.1661 0.1093 0.0176  -0.0455 0.0649  176 THR A CA  
1468 C  C   . THR A 174 ? 0.1625 0.1428 0.0502 -0.0043 -0.0583 0.0160  176 THR A C   
1469 O  O   . THR A 174 ? 0.2606 0.1482 0.0566 -0.0141 -0.0737 0.0336  176 THR A O   
1470 C  CB  . THR A 174 ? 0.2803 0.1967 0.1136 -0.0306 -0.1306 0.0766  176 THR A CB  
1471 O  OG1 . THR A 174 ? 0.4394 0.2289 0.0856 0.0428  -0.1084 0.0456  176 THR A OG1 
1472 C  CG2 . THR A 174 ? 0.2780 0.3995 0.2549 -0.0477 -0.1021 0.2174  176 THR A CG2 
1473 N  N   . ASN A 175 ? 0.2095 0.1319 0.0480 0.0097  -0.0611 0.0306  177 ASN A N   
1474 C  CA  . ASN A 175 ? 0.2357 0.1392 0.1047 -0.0192 -0.0780 0.0631  177 ASN A CA  
1475 C  C   . ASN A 175 ? 0.2153 0.1381 0.0618 -0.0230 -0.0700 0.0586  177 ASN A C   
1476 O  O   . ASN A 175 ? 0.2494 0.1654 0.2189 -0.0549 -0.1395 0.1067  177 ASN A O   
1477 C  CB  . ASN A 175 ? 0.2195 0.1241 0.1360 0.0182  -0.1016 0.0313  177 ASN A CB  
1478 C  CG  . ASN A 175 ? 0.2867 0.1622 0.0847 0.0630  -0.0895 0.0414  177 ASN A CG  
1479 O  OD1 . ASN A 175 ? 0.2425 0.1521 0.1905 0.0293  0.0039  0.0598  177 ASN A OD1 
1480 N  ND2 . ASN A 175 ? 0.2275 0.1657 0.0935 0.0054  -0.0886 0.0394  177 ASN A ND2 
1481 N  N   . PHE A 176 ? 0.2497 0.1005 0.0434 0.0155  -0.0773 0.0284  178 PHE A N   
1482 C  CA  . PHE A 176 ? 0.2200 0.1137 0.0641 0.0173  -0.0328 0.0495  178 PHE A CA  
1483 C  C   . PHE A 176 ? 0.1661 0.1171 0.0655 -0.0023 -0.0529 0.0070  178 PHE A C   
1484 O  O   . PHE A 176 ? 0.1956 0.1168 0.0673 -0.0058 -0.0585 0.0135  178 PHE A O   
1485 C  CB  . PHE A 176 ? 0.2340 0.1198 0.0777 0.0221  -0.0320 0.0438  178 PHE A CB  
1486 C  CG  . PHE A 176 ? 0.1970 0.1135 0.0741 -0.0096 -0.0478 0.0461  178 PHE A CG  
1487 C  CD1 . PHE A 176 ? 0.2177 0.0998 0.1036 0.0394  -0.0232 0.0209  178 PHE A CD1 
1488 C  CD2 . PHE A 176 ? 0.1248 0.1894 0.0662 -0.0037 -0.0227 0.0474  178 PHE A CD2 
1489 C  CE1 . PHE A 176 ? 0.2504 0.1014 0.0700 0.0231  -0.0455 0.0047  178 PHE A CE1 
1490 C  CE2 . PHE A 176 ? 0.1266 0.1306 0.1111 -0.0034 -0.0335 0.0219  178 PHE A CE2 
1491 C  CZ  . PHE A 176 ? 0.1866 0.1464 0.0617 0.0143  -0.0359 0.0344  178 PHE A CZ  
1492 N  N   . ASP A 177 ? 0.1658 0.1460 0.0718 -0.0038 -0.0652 0.0447  179 ASP A N   
1493 C  CA  . ASP A 177 ? 0.1298 0.1650 0.0619 0.0027  -0.0695 0.0284  179 ASP A CA  
1494 C  C   . ASP A 177 ? 0.0985 0.0900 0.0662 -0.0081 -0.0364 0.0159  179 ASP A C   
1495 O  O   . ASP A 177 ? 0.1345 0.1029 0.0952 -0.0211 -0.0495 0.0013  179 ASP A O   
1496 C  CB  . ASP A 177 ? 0.1320 0.1489 0.1366 0.0124  -0.0348 0.0487  179 ASP A CB  
1497 C  CG  . ASP A 177 ? 0.1031 0.2072 0.1564 -0.0174 -0.0350 0.0334  179 ASP A CG  
1498 O  OD1 . ASP A 177 ? 0.1518 0.1252 0.1441 0.0086  -0.0529 0.0413  179 ASP A OD1 
1499 O  OD2 . ASP A 177 ? 0.1023 0.4028 0.2606 0.0187  -0.0524 0.0000  179 ASP A OD2 
1500 N  N   . PRO A 178 ? 0.1208 0.0944 0.0688 0.0013  -0.0528 0.0127  180 PRO A N   
1501 C  CA  . PRO A 178 ? 0.0840 0.1194 0.0801 -0.0054 -0.0497 0.0266  180 PRO A CA  
1502 C  C   . PRO A 178 ? 0.1146 0.1155 0.0510 -0.0006 -0.0369 0.0024  180 PRO A C   
1503 O  O   . PRO A 178 ? 0.1453 0.0980 0.0608 -0.0061 -0.0434 0.0077  180 PRO A O   
1504 C  CB  . PRO A 178 ? 0.1108 0.1270 0.0988 -0.0204 -0.0384 0.0035  180 PRO A CB  
1505 C  CG  . PRO A 178 ? 0.1514 0.1120 0.0822 -0.0421 -0.0633 0.0372  180 PRO A CG  
1506 C  CD  . PRO A 178 ? 0.1295 0.0988 0.0818 -0.0088 -0.0532 0.0077  180 PRO A CD  
1507 N  N   . ARG A 179 ? 0.0994 0.1084 0.0713 -0.0115 -0.0268 0.0185  181 ARG A N   
1508 C  CA  . ARG A 179 ? 0.0910 0.1106 0.0910 0.0064  -0.0154 0.0126  181 ARG A CA  
1509 C  C   . ARG A 179 ? 0.1345 0.1269 0.1154 -0.0073 -0.0666 0.0190  181 ARG A C   
1510 O  O   . ARG A 179 ? 0.1403 0.1241 0.1410 -0.0108 -0.0630 0.0359  181 ARG A O   
1511 C  CB  . ARG A 179 ? 0.1014 0.1198 0.1485 0.0172  -0.0446 0.0162  181 ARG A CB  
1512 C  CG  . ARG A 179 ? 0.1514 0.1164 0.1467 0.0063  -0.0242 0.0133  181 ARG A CG  
1513 C  CD  . ARG A 179 ? 0.1671 0.1671 0.1593 0.0506  -0.0149 0.0346  181 ARG A CD  
1514 N  NE  . ARG A 179 ? 0.1489 0.1453 0.1808 0.0111  -0.0350 0.0491  181 ARG A NE  
1515 C  CZ  . ARG A 179 ? 0.1769 0.2896 0.1819 0.1020  -0.0053 0.0832  181 ARG A CZ  
1516 N  NH1 . ARG A 179 ? 0.2490 0.3762 0.3194 0.1486  0.0629  0.0627  181 ARG A NH1 
1517 N  NH2 . ARG A 179 ? 0.1941 0.3576 0.2045 0.0888  -0.0379 0.1338  181 ARG A NH2 
1518 N  N   . GLY A 180 ? 0.1270 0.0898 0.1101 0.0065  -0.0781 0.0285  182 GLY A N   
1519 C  CA  . GLY A 180 ? 0.1567 0.0861 0.1363 -0.0188 -0.0942 0.0312  182 GLY A CA  
1520 C  C   . GLY A 180 ? 0.1381 0.0784 0.1270 0.0073  -0.0609 -0.0150 182 GLY A C   
1521 O  O   . GLY A 180 ? 0.2113 0.0910 0.2091 0.0144  -0.1333 -0.0409 182 GLY A O   
1522 N  N   . LEU A 181 ? 0.1377 0.1040 0.0864 -0.0086 -0.0666 0.0033  183 LEU A N   
1523 C  CA  . LEU A 181 ? 0.1618 0.0874 0.0829 -0.0061 -0.0662 0.0134  183 LEU A CA  
1524 C  C   . LEU A 181 ? 0.1316 0.0562 0.0803 0.0089  -0.0591 0.0023  183 LEU A C   
1525 O  O   . LEU A 181 ? 0.1338 0.1040 0.1049 0.0188  -0.0574 0.0266  183 LEU A O   
1526 C  CB  . LEU A 181 ? 0.1373 0.1187 0.0584 0.0272  -0.0150 0.0223  183 LEU A CB  
1527 C  CG  . LEU A 181 ? 0.1636 0.1100 0.0531 0.0192  -0.0227 0.0140  183 LEU A CG  
1528 C  CD1 . LEU A 181 ? 0.1374 0.1834 0.0899 0.0241  -0.0187 0.0356  183 LEU A CD1 
1529 C  CD2 . LEU A 181 ? 0.2785 0.1337 0.1309 0.0551  -0.0188 -0.0176 183 LEU A CD2 
1530 N  N   . LEU A 182 ? 0.1349 0.0873 0.0970 0.0018  -0.0283 0.0027  184 LEU A N   
1531 C  CA  . LEU A 182 ? 0.1169 0.1097 0.0979 -0.0303 -0.0396 0.0233  184 LEU A CA  
1532 C  C   . LEU A 182 ? 0.1773 0.1022 0.1040 -0.0595 -0.0754 0.0266  184 LEU A C   
1533 O  O   . LEU A 182 ? 0.2701 0.1851 0.2017 -0.1321 -0.1694 0.0855  184 LEU A O   
1534 C  CB  . LEU A 182 ? 0.1120 0.0917 0.1027 -0.0223 -0.0345 0.0314  184 LEU A CB  
1535 C  CG  . LEU A 182 ? 0.0626 0.1007 0.1046 -0.0106 -0.0369 0.0370  184 LEU A CG  
1536 C  CD1 . LEU A 182 ? 0.0849 0.1776 0.1091 0.0288  -0.0280 0.0219  184 LEU A CD1 
1537 C  CD2 . LEU A 182 ? 0.0792 0.1360 0.1635 -0.0003 -0.0749 0.0539  184 LEU A CD2 
1538 N  N   . PRO A 183 ? 0.0861 0.0883 0.1374 -0.0140 -0.0475 0.0441  185 PRO A N   
1539 C  CA  . PRO A 183 ? 0.1233 0.1032 0.1306 -0.0132 -0.0267 0.0671  185 PRO A CA  
1540 C  C   . PRO A 183 ? 0.1016 0.0916 0.1597 -0.0314 -0.0556 0.0507  185 PRO A C   
1541 O  O   . PRO A 183 ? 0.0610 0.0891 0.2977 -0.0091 -0.0581 0.0656  185 PRO A O   
1542 C  CB  . PRO A 183 ? 0.1073 0.0861 0.1156 -0.0078 -0.0156 0.0466  185 PRO A CB  
1543 C  CG  . PRO A 183 ? 0.1076 0.0840 0.1098 0.0017  -0.0161 0.0342  185 PRO A CG  
1544 C  CD  . PRO A 183 ? 0.0944 0.0962 0.0846 -0.0096 -0.0337 0.0171  185 PRO A CD  
1545 N  N   A GLU A 184 ? 0.1032 0.0935 0.1549 -0.0425 -0.0467 0.0388  186 GLU A N   
1546 N  N   B GLU A 184 ? 0.0845 0.1118 0.1503 -0.0245 -0.0207 0.0545  186 GLU A N   
1547 C  CA  A GLU A 184 ? 0.0785 0.1316 0.1733 -0.0681 -0.0457 0.0471  186 GLU A CA  
1548 C  CA  B GLU A 184 ? 0.0597 0.1503 0.1439 -0.0577 -0.0254 0.0771  186 GLU A CA  
1549 C  C   A GLU A 184 ? 0.0766 0.0944 0.1781 -0.0403 -0.0589 0.0549  186 GLU A C   
1550 C  C   B GLU A 184 ? 0.0293 0.1072 0.1704 -0.0264 -0.0283 0.0648  186 GLU A C   
1551 O  O   A GLU A 184 ? 0.0522 0.1198 0.2749 -0.0219 -0.0187 0.0557  186 GLU A O   
1552 O  O   B GLU A 184 ? 0.0256 0.1234 0.1833 -0.0168 -0.0248 0.0534  186 GLU A O   
1553 C  CB  A GLU A 184 ? 0.1190 0.1560 0.2575 -0.1081 -0.0847 0.0744  186 GLU A CB  
1554 C  CB  B GLU A 184 ? 0.0724 0.1395 0.1920 -0.0494 -0.0247 0.0414  186 GLU A CB  
1555 C  CG  A GLU A 184 ? 0.1762 0.1586 0.2243 -0.0983 -0.0906 0.0499  186 GLU A CG  
1556 C  CG  B GLU A 184 ? 0.0952 0.1503 0.1629 -0.0206 -0.0073 0.0581  186 GLU A CG  
1557 C  CD  A GLU A 184 ? 0.1248 0.1664 0.2583 -0.0891 -0.0534 0.0439  186 GLU A CD  
1558 C  CD  B GLU A 184 ? 0.0531 0.1714 0.1305 -0.0194 -0.0192 0.0844  186 GLU A CD  
1559 O  OE1 A GLU A 184 ? 0.2024 0.2467 0.2667 -0.0089 -0.0624 -0.0279 186 GLU A OE1 
1560 O  OE1 B GLU A 184 ? 0.0979 0.1722 0.2339 -0.0065 -0.0465 0.0312  186 GLU A OE1 
1561 O  OE2 A GLU A 184 ? 0.1956 0.1855 0.2547 -0.0939 -0.0563 0.0432  186 GLU A OE2 
1562 O  OE2 B GLU A 184 ? 0.1442 0.1963 0.1992 0.0100  0.0688  0.1025  186 GLU A OE2 
1563 N  N   . SER A 185 ? 0.0401 0.1128 0.1654 -0.0247 -0.0465 0.0372  187 SER A N   
1564 C  CA  . SER A 185 ? 0.0706 0.0908 0.1848 -0.0124 -0.0190 0.0198  187 SER A CA  
1565 C  C   . SER A 185 ? 0.0547 0.0828 0.1597 -0.0033 -0.0091 0.0114  187 SER A C   
1566 O  O   . SER A 185 ? 0.0677 0.1205 0.1549 -0.0175 0.0006  0.0009  187 SER A O   
1567 C  CB  . SER A 185 ? 0.0926 0.1607 0.1410 -0.0083 -0.0314 0.0319  187 SER A CB  
1568 O  OG  . SER A 185 ? 0.1253 0.1284 0.1459 -0.0417 -0.0260 0.0234  187 SER A OG  
1569 N  N   . LEU A 186 ? 0.0557 0.0619 0.1794 -0.0156 -0.0253 0.0120  188 LEU A N   
1570 C  CA  . LEU A 186 ? 0.0662 0.0812 0.1531 -0.0245 -0.0257 -0.0031 188 LEU A CA  
1571 C  C   . LEU A 186 ? 0.0409 0.1155 0.1467 -0.0055 -0.0050 -0.0118 188 LEU A C   
1572 O  O   . LEU A 186 ? 0.0696 0.1410 0.1388 -0.0152 -0.0194 -0.0092 188 LEU A O   
1573 C  CB  . LEU A 186 ? 0.1076 0.1036 0.1948 -0.0050 -0.0282 0.0196  188 LEU A CB  
1574 C  CG  . LEU A 186 ? 0.0806 0.1560 0.2272 0.0134  -0.0247 0.0569  188 LEU A CG  
1575 C  CD1 . LEU A 186 ? 0.1625 0.1324 0.3057 -0.0085 -0.0263 0.0960  188 LEU A CD1 
1576 C  CD2 . LEU A 186 ? 0.0703 0.3023 0.1787 0.0118  -0.0402 0.0479  188 LEU A CD2 
1577 N  N   . ASP A 187 ? 0.0642 0.1305 0.1221 0.0234  -0.0107 -0.0088 189 ASP A N   
1578 C  CA  . ASP A 187 ? 0.0432 0.1514 0.1055 -0.0438 -0.0020 -0.0089 189 ASP A CA  
1579 C  C   . ASP A 187 ? 0.0387 0.0987 0.0989 -0.0130 -0.0098 -0.0122 189 ASP A C   
1580 O  O   . ASP A 187 ? 0.0528 0.0872 0.0881 -0.0137 -0.0017 -0.0100 189 ASP A O   
1581 C  CB  . ASP A 187 ? 0.0950 0.1895 0.1002 -0.0632 0.0085  0.0329  189 ASP A CB  
1582 C  CG  . ASP A 187 ? 0.1119 0.3035 0.1729 -0.0648 0.0306  0.0139  189 ASP A CG  
1583 O  OD1 . ASP A 187 ? 0.1007 0.4291 0.1992 -0.0132 0.0776  0.0175  189 ASP A OD1 
1584 O  OD2 . ASP A 187 ? 0.1884 0.4232 0.1884 -0.1265 0.0159  0.0851  189 ASP A OD2 
1585 N  N   . TYR A 188 ? 0.0373 0.0885 0.0820 -0.0159 -0.0016 -0.0067 190 TYR A N   
1586 C  CA  . TYR A 188 ? 0.0449 0.0873 0.0743 -0.0396 -0.0076 0.0058  190 TYR A CA  
1587 C  C   . TYR A 188 ? 0.0759 0.0706 0.0431 -0.0048 0.0057  0.0083  190 TYR A C   
1588 O  O   . TYR A 188 ? 0.0786 0.0934 0.0522 -0.0040 0.0198  -0.0041 190 TYR A O   
1589 C  CB  . TYR A 188 ? 0.0837 0.0874 0.0637 -0.0138 0.0006  0.0150  190 TYR A CB  
1590 C  CG  . TYR A 188 ? 0.0689 0.0917 0.0688 -0.0220 -0.0002 0.0144  190 TYR A CG  
1591 C  CD1 . TYR A 188 ? 0.0861 0.0786 0.0846 -0.0311 -0.0027 0.0091  190 TYR A CD1 
1592 C  CD2 . TYR A 188 ? 0.0907 0.1028 0.0812 -0.0001 0.0252  -0.0002 190 TYR A CD2 
1593 C  CE1 . TYR A 188 ? 0.0697 0.0901 0.1003 -0.0100 -0.0012 0.0142  190 TYR A CE1 
1594 C  CE2 . TYR A 188 ? 0.1031 0.0994 0.0743 -0.0139 0.0012  -0.0105 190 TYR A CE2 
1595 C  CZ  . TYR A 188 ? 0.0791 0.0822 0.0862 -0.0064 -0.0011 0.0000  190 TYR A CZ  
1596 O  OH  . TYR A 188 ? 0.1277 0.0926 0.1126 0.0122  -0.0222 -0.0155 190 TYR A OH  
1597 N  N   . TRP A 189 ? 0.0732 0.0469 0.0636 -0.0044 -0.0053 0.0066  191 TRP A N   
1598 C  CA  . TRP A 189 ? 0.0635 0.0449 0.0566 -0.0092 0.0069  0.0053  191 TRP A CA  
1599 C  C   . TRP A 189 ? 0.0616 0.0479 0.0266 -0.0121 -0.0003 -0.0050 191 TRP A C   
1600 O  O   . TRP A 189 ? 0.1102 0.0706 0.0309 -0.0095 -0.0018 0.0047  191 TRP A O   
1601 C  CB  . TRP A 189 ? 0.0797 0.0434 0.0700 -0.0019 0.0085  -0.0073 191 TRP A CB  
1602 C  CG  . TRP A 189 ? 0.0917 0.0506 0.0538 0.0067  -0.0076 0.0107  191 TRP A CG  
1603 C  CD1 . TRP A 189 ? 0.0942 0.0673 0.0641 0.0130  0.0138  0.0154  191 TRP A CD1 
1604 C  CD2 . TRP A 189 ? 0.0566 0.0650 0.0712 0.0118  -0.0121 -0.0033 191 TRP A CD2 
1605 N  NE1 . TRP A 189 ? 0.1170 0.0697 0.0803 0.0076  -0.0078 0.0212  191 TRP A NE1 
1606 C  CE2 . TRP A 189 ? 0.1134 0.0750 0.0797 0.0041  -0.0104 0.0067  191 TRP A CE2 
1607 C  CE3 . TRP A 189 ? 0.0662 0.0996 0.0759 0.0243  -0.0199 -0.0198 191 TRP A CE3 
1608 C  CZ2 . TRP A 189 ? 0.1181 0.0653 0.1144 0.0052  -0.0186 0.0160  191 TRP A CZ2 
1609 C  CZ3 . TRP A 189 ? 0.0478 0.0882 0.1080 0.0067  0.0029  -0.0178 191 TRP A CZ3 
1610 C  CH2 . TRP A 189 ? 0.0687 0.0998 0.1146 0.0044  -0.0233 0.0005  191 TRP A CH2 
1611 N  N   . THR A 190 ? 0.0601 0.0549 0.0346 -0.0139 -0.0088 -0.0046 192 THR A N   
1612 C  CA  . THR A 190 ? 0.0558 0.0513 0.0285 -0.0025 0.0012  -0.0005 192 THR A CA  
1613 C  C   . THR A 190 ? 0.0530 0.0519 0.0267 -0.0065 0.0055  0.0068  192 THR A C   
1614 O  O   . THR A 190 ? 0.0784 0.0750 0.0247 -0.0039 -0.0013 0.0071  192 THR A O   
1615 C  CB  . THR A 190 ? 0.0496 0.0531 0.0418 0.0004  0.0130  0.0076  192 THR A CB  
1616 O  OG1 . THR A 190 ? 0.0563 0.0480 0.0680 -0.0024 0.0037  0.0114  192 THR A OG1 
1617 C  CG2 . THR A 190 ? 0.0668 0.0641 0.0489 0.0121  0.0225  0.0044  192 THR A CG2 
1618 N  N   . TYR A 191 ? 0.0467 0.0571 0.0415 -0.0105 -0.0023 0.0036  193 TYR A N   
1619 C  CA  . TYR A 191 ? 0.0413 0.0522 0.0364 -0.0002 0.0030  -0.0040 193 TYR A CA  
1620 C  C   . TYR A 191 ? 0.0573 0.0441 0.0259 0.0027  -0.0078 -0.0063 193 TYR A C   
1621 O  O   . TYR A 191 ? 0.0584 0.0621 0.0283 0.0018  -0.0109 0.0011  193 TYR A O   
1622 C  CB  . TYR A 191 ? 0.0890 0.0469 0.0441 0.0087  0.0072  -0.0118 193 TYR A CB  
1623 C  CG  . TYR A 191 ? 0.0600 0.0294 0.0422 0.0021  -0.0015 -0.0066 193 TYR A CG  
1624 C  CD1 . TYR A 191 ? 0.0685 0.0344 0.0378 0.0149  -0.0151 -0.0013 193 TYR A CD1 
1625 C  CD2 . TYR A 191 ? 0.0538 0.0564 0.0470 0.0063  -0.0099 0.0003  193 TYR A CD2 
1626 C  CE1 . TYR A 191 ? 0.0618 0.0418 0.0390 -0.0002 0.0037  0.0098  193 TYR A CE1 
1627 C  CE2 . TYR A 191 ? 0.0635 0.0452 0.0399 0.0144  -0.0175 -0.0010 193 TYR A CE2 
1628 C  CZ  . TYR A 191 ? 0.0511 0.0505 0.0256 0.0067  -0.0075 0.0042  193 TYR A CZ  
1629 O  OH  . TYR A 191 ? 0.0597 0.0440 0.0363 -0.0022 0.0046  0.0013  193 TYR A OH  
1630 N  N   . PRO A 192 ? 0.0457 0.0643 0.0232 -0.0057 -0.0030 -0.0052 194 PRO A N   
1631 C  CA  . PRO A 192 ? 0.0522 0.0487 0.0417 0.0001  0.0009  -0.0085 194 PRO A CA  
1632 C  C   . PRO A 192 ? 0.0441 0.0557 0.0328 0.0044  -0.0154 -0.0109 194 PRO A C   
1633 O  O   . PRO A 192 ? 0.0652 0.0712 0.0355 0.0183  -0.0122 -0.0027 194 PRO A O   
1634 C  CB  . PRO A 192 ? 0.0890 0.0897 0.0318 0.0067  -0.0031 -0.0216 194 PRO A CB  
1635 C  CG  . PRO A 192 ? 0.1093 0.0831 0.0400 -0.0282 0.0052  -0.0087 194 PRO A CG  
1636 C  CD  . PRO A 192 ? 0.0776 0.1032 0.0230 -0.0142 -0.0027 -0.0159 194 PRO A CD  
1637 N  N   . GLY A 193 ? 0.0427 0.0434 0.0357 -0.0044 0.0002  -0.0111 195 GLY A N   
1638 C  CA  . GLY A 193 ? 0.0443 0.0487 0.0330 0.0073  -0.0008 0.0071  195 GLY A CA  
1639 C  C   . GLY A 193 ? 0.0364 0.0325 0.0440 -0.0067 0.0020  -0.0033 195 GLY A C   
1640 O  O   . GLY A 193 ? 0.0610 0.0320 0.0443 -0.0043 -0.0085 -0.0012 195 GLY A O   
1641 N  N   . SER A 194 ? 0.0497 0.0381 0.0318 -0.0068 -0.0050 -0.0026 196 SER A N   
1642 C  CA  . SER A 194 ? 0.0423 0.0518 0.0370 0.0000  0.0047  -0.0070 196 SER A CA  
1643 C  C   . SER A 194 ? 0.0285 0.0381 0.0399 0.0048  -0.0102 0.0022  196 SER A C   
1644 O  O   . SER A 194 ? 0.0364 0.0555 0.0469 -0.0071 0.0027  -0.0097 196 SER A O   
1645 C  CB  . SER A 194 ? 0.0466 0.0390 0.0518 0.0089  -0.0078 -0.0093 196 SER A CB  
1646 O  OG  . SER A 194 ? 0.0382 0.0339 0.0685 0.0010  -0.0060 -0.0099 196 SER A OG  
1647 N  N   . LEU A 195 ? 0.0461 0.0466 0.0233 0.0076  -0.0120 0.0001  197 LEU A N   
1648 C  CA  . LEU A 195 ? 0.0497 0.0479 0.0378 -0.0068 0.0050  -0.0161 197 LEU A CA  
1649 C  C   . LEU A 195 ? 0.0408 0.0450 0.0470 -0.0138 0.0000  -0.0104 197 LEU A C   
1650 O  O   . LEU A 195 ? 0.0477 0.0567 0.0566 -0.0016 -0.0027 -0.0060 197 LEU A O   
1651 C  CB  . LEU A 195 ? 0.0785 0.0637 0.0678 -0.0162 0.0110  0.0015  197 LEU A CB  
1652 C  CG  . LEU A 195 ? 0.0907 0.0847 0.1058 0.0140  0.0268  0.0394  197 LEU A CG  
1653 C  CD1 . LEU A 195 ? 0.0924 0.1388 0.2059 -0.0030 0.0655  0.0862  197 LEU A CD1 
1654 C  CD2 . LEU A 195 ? 0.0723 0.0953 0.1280 0.0070  0.0221  0.0252  197 LEU A CD2 
1655 N  N   . THR A 196 ? 0.0524 0.0373 0.0337 -0.0052 -0.0064 -0.0064 198 THR A N   
1656 C  CA  . THR A 196 ? 0.0512 0.0431 0.0528 -0.0038 0.0083  -0.0111 198 THR A CA  
1657 C  C   . THR A 196 ? 0.0555 0.0518 0.0388 0.0017  -0.0003 -0.0011 198 THR A C   
1658 O  O   . THR A 196 ? 0.0443 0.0574 0.0637 0.0031  -0.0051 -0.0026 198 THR A O   
1659 C  CB  . THR A 196 ? 0.0617 0.0487 0.0153 -0.0100 -0.0030 -0.0021 198 THR A CB  
1660 O  OG1 . THR A 196 ? 0.0566 0.0553 0.0239 -0.0084 -0.0116 0.0038  198 THR A OG1 
1661 C  CG2 . THR A 196 ? 0.0575 0.0549 0.0379 -0.0034 0.0098  -0.0220 198 THR A CG2 
1662 N  N   . THR A 197 ? 0.0556 0.0601 0.0521 -0.0219 0.0079  0.0025  199 THR A N   
1663 C  CA  . THR A 197 ? 0.0643 0.0582 0.0496 -0.0172 0.0080  -0.0093 199 THR A CA  
1664 C  C   . THR A 197 ? 0.0644 0.0619 0.0756 -0.0201 0.0110  -0.0008 199 THR A C   
1665 O  O   . THR A 197 ? 0.0651 0.0584 0.0695 -0.0255 0.0026  -0.0168 199 THR A O   
1666 C  CB  . THR A 197 ? 0.0652 0.0476 0.0661 -0.0095 -0.0026 -0.0015 199 THR A CB  
1667 O  OG1 . THR A 197 ? 0.0855 0.0642 0.0794 0.0061  -0.0052 0.0098  199 THR A OG1 
1668 C  CG2 . THR A 197 ? 0.0653 0.0752 0.0601 -0.0256 -0.0060 0.0021  199 THR A CG2 
1669 N  N   . PRO A 198 ? 0.0688 0.0619 0.0838 -0.0110 0.0206  -0.0061 200 PRO A N   
1670 C  CA  . PRO A 198 ? 0.0618 0.0671 0.0900 -0.0200 0.0181  0.0100  200 PRO A CA  
1671 C  C   . PRO A 198 ? 0.0910 0.0820 0.0731 -0.0085 0.0013  0.0069  200 PRO A C   
1672 O  O   . PRO A 198 ? 0.0968 0.0944 0.0785 -0.0241 0.0088  -0.0006 200 PRO A O   
1673 C  CB  . PRO A 198 ? 0.0478 0.0910 0.0916 -0.0110 0.0031  -0.0118 200 PRO A CB  
1674 C  CG  . PRO A 198 ? 0.0653 0.0952 0.0855 -0.0050 0.0175  -0.0116 200 PRO A CG  
1675 C  CD  . PRO A 198 ? 0.0625 0.0908 0.0813 -0.0001 0.0142  -0.0251 200 PRO A CD  
1676 N  N   . PRO A 199 ? 0.0677 0.0882 0.0926 -0.0097 0.0083  0.0040  201 PRO A N   
1677 C  CA  . PRO A 199 ? 0.0958 0.0739 0.0882 -0.0296 0.0023  0.0118  201 PRO A CA  
1678 C  C   . PRO A 199 ? 0.0540 0.0891 0.0854 -0.0190 0.0106  -0.0010 201 PRO A C   
1679 O  O   . PRO A 199 ? 0.0847 0.0838 0.1045 -0.0342 0.0005  0.0015  201 PRO A O   
1680 C  CB  . PRO A 199 ? 0.1111 0.0715 0.1247 -0.0296 0.0080  0.0115  201 PRO A CB  
1681 C  CG  . PRO A 199 ? 0.1223 0.0706 0.1342 0.0044  -0.0193 -0.0136 201 PRO A CG  
1682 C  CD  . PRO A 199 ? 0.1273 0.0601 0.0888 -0.0044 0.0162  0.0081  201 PRO A CD  
1683 N  N   . LEU A 200 ? 0.0399 0.0713 0.0680 -0.0092 0.0049  0.0033  202 LEU A N   
1684 C  CA  . LEU A 200 ? 0.0554 0.0487 0.0732 0.0089  0.0054  -0.0006 202 LEU A CA  
1685 C  C   . LEU A 200 ? 0.0427 0.0519 0.0713 -0.0093 -0.0065 -0.0107 202 LEU A C   
1686 O  O   . LEU A 200 ? 0.0495 0.0610 0.0671 -0.0053 -0.0204 -0.0058 202 LEU A O   
1687 C  CB  . LEU A 200 ? 0.0478 0.0770 0.0688 0.0134  -0.0062 -0.0212 202 LEU A CB  
1688 C  CG  . LEU A 200 ? 0.0250 0.0718 0.0864 0.0069  -0.0024 -0.0232 202 LEU A CG  
1689 C  CD1 . LEU A 200 ? 0.0169 0.1198 0.1309 0.0143  0.0009  -0.0160 202 LEU A CD1 
1690 C  CD2 . LEU A 200 ? 0.0601 0.0831 0.0777 -0.0160 0.0068  -0.0162 202 LEU A CD2 
1691 N  N   . LEU A 201 ? 0.0373 0.0522 0.0994 0.0064  0.0011  -0.0155 203 LEU A N   
1692 C  CA  . LEU A 201 ? 0.0479 0.0434 0.0838 -0.0065 0.0061  -0.0091 203 LEU A CA  
1693 C  C   . LEU A 201 ? 0.0434 0.0436 0.0707 -0.0073 -0.0008 -0.0147 203 LEU A C   
1694 O  O   . LEU A 201 ? 0.0635 0.0521 0.0636 -0.0195 -0.0173 -0.0145 203 LEU A O   
1695 C  CB  . LEU A 201 ? 0.0971 0.0510 0.1102 -0.0013 0.0139  0.0216  203 LEU A CB  
1696 C  CG  . LEU A 201 ? 0.0969 0.0732 0.1181 -0.0012 0.0254  -0.0015 203 LEU A CG  
1697 C  CD1 . LEU A 201 ? 0.1284 0.1076 0.1489 0.0104  0.0266  0.0367  203 LEU A CD1 
1698 C  CD2 . LEU A 201 ? 0.0765 0.1350 0.2546 -0.0266 -0.0055 0.0357  203 LEU A CD2 
1699 N  N   . GLU A 202 ? 0.0650 0.0724 0.0633 -0.0128 -0.0133 -0.0091 204 GLU A N   
1700 C  CA  . GLU A 202 ? 0.0637 0.0734 0.0467 -0.0049 -0.0269 -0.0121 204 GLU A CA  
1701 C  C   . GLU A 202 ? 0.0653 0.0584 0.0575 -0.0048 -0.0277 -0.0195 204 GLU A C   
1702 O  O   . GLU A 202 ? 0.0950 0.0892 0.0715 0.0088  -0.0247 -0.0352 204 GLU A O   
1703 C  CB  . GLU A 202 ? 0.0461 0.0670 0.0776 0.0047  -0.0422 -0.0068 204 GLU A CB  
1704 C  CG  . GLU A 202 ? 0.0406 0.0804 0.1005 0.0141  -0.0326 -0.0215 204 GLU A CG  
1705 C  CD  . GLU A 202 ? 0.0820 0.0829 0.0898 -0.0148 -0.0412 0.0075  204 GLU A CD  
1706 O  OE1 . GLU A 202 ? 0.0995 0.1179 0.1345 0.0049  -0.0564 -0.0398 204 GLU A OE1 
1707 O  OE2 . GLU A 202 ? 0.0603 0.0968 0.0901 -0.0055 -0.0274 -0.0062 204 GLU A OE2 
1708 N  N   . CYS A 203 ? 0.0433 0.0513 0.0750 -0.0062 -0.0272 -0.0099 205 CYS A N   
1709 C  CA  . CYS A 203 ? 0.0480 0.0442 0.0651 -0.0034 -0.0132 0.0059  205 CYS A CA  
1710 C  C   . CYS A 203 ? 0.0454 0.0373 0.0521 -0.0009 -0.0022 -0.0053 205 CYS A C   
1711 O  O   . CYS A 203 ? 0.0732 0.0418 0.0827 0.0079  -0.0245 -0.0050 205 CYS A O   
1712 C  CB  . CYS A 203 ? 0.0793 0.0556 0.0601 -0.0156 0.0098  -0.0022 205 CYS A CB  
1713 S  SG  . CYS A 203 ? 0.0961 0.0592 0.0625 -0.0061 -0.0160 -0.0013 205 CYS A SG  
1714 N  N   . VAL A 204 ? 0.0503 0.0449 0.0538 -0.0132 -0.0157 0.0036  206 VAL A N   
1715 C  CA  . VAL A 204 ? 0.0463 0.0321 0.0496 -0.0050 -0.0210 0.0011  206 VAL A CA  
1716 C  C   . VAL A 204 ? 0.0486 0.0390 0.0443 -0.0030 -0.0221 0.0000  206 VAL A C   
1717 O  O   . VAL A 204 ? 0.0706 0.0610 0.0643 0.0085  -0.0142 0.0206  206 VAL A O   
1718 C  CB  . VAL A 204 ? 0.0494 0.0311 0.0477 -0.0188 -0.0100 0.0018  206 VAL A CB  
1719 C  CG1 . VAL A 204 ? 0.0496 0.0558 0.0494 -0.0152 -0.0242 -0.0192 206 VAL A CG1 
1720 C  CG2 . VAL A 204 ? 0.0716 0.0664 0.0399 -0.0010 -0.0038 -0.0013 206 VAL A CG2 
1721 N  N   . THR A 205 ? 0.0496 0.0326 0.0513 -0.0104 -0.0057 -0.0111 207 THR A N   
1722 C  CA  . THR A 205 ? 0.0457 0.0357 0.0497 -0.0115 -0.0010 -0.0134 207 THR A CA  
1723 C  C   . THR A 205 ? 0.0537 0.0292 0.0303 -0.0039 -0.0160 -0.0008 207 THR A C   
1724 O  O   . THR A 205 ? 0.0680 0.0459 0.0260 -0.0116 -0.0201 0.0036  207 THR A O   
1725 C  CB  . THR A 205 ? 0.0597 0.0391 0.0545 0.0006  0.0000  -0.0073 207 THR A CB  
1726 O  OG1 . THR A 205 ? 0.0873 0.0390 0.0818 -0.0100 -0.0069 -0.0104 207 THR A OG1 
1727 C  CG2 . THR A 205 ? 0.0734 0.0716 0.0837 0.0019  0.0155  0.0214  207 THR A CG2 
1728 N  N   . TRP A 206 ? 0.0505 0.0276 0.0319 -0.0027 -0.0106 -0.0004 208 TRP A N   
1729 C  CA  . TRP A 206 ? 0.0449 0.0284 0.0434 -0.0010 -0.0065 -0.0087 208 TRP A CA  
1730 C  C   . TRP A 206 ? 0.0400 0.0372 0.0325 0.0049  -0.0107 -0.0020 208 TRP A C   
1731 O  O   . TRP A 206 ? 0.0573 0.0408 0.0355 0.0054  -0.0018 -0.0044 208 TRP A O   
1732 C  CB  . TRP A 206 ? 0.0461 0.0479 0.0433 0.0088  0.0067  0.0044  208 TRP A CB  
1733 C  CG  . TRP A 206 ? 0.0339 0.0267 0.0277 0.0068  -0.0070 0.0075  208 TRP A CG  
1734 C  CD1 . TRP A 206 ? 0.0466 0.0400 0.0380 -0.0055 -0.0036 0.0076  208 TRP A CD1 
1735 C  CD2 . TRP A 206 ? 0.0472 0.0223 0.0337 -0.0055 -0.0107 0.0015  208 TRP A CD2 
1736 N  NE1 . TRP A 206 ? 0.0495 0.0487 0.0336 -0.0004 -0.0048 -0.0037 208 TRP A NE1 
1737 C  CE2 . TRP A 206 ? 0.0478 0.0269 0.0392 0.0024  -0.0087 0.0032  208 TRP A CE2 
1738 C  CE3 . TRP A 206 ? 0.0566 0.0241 0.0250 0.0121  -0.0230 -0.0089 208 TRP A CE3 
1739 C  CZ2 . TRP A 206 ? 0.0553 0.0362 0.0399 0.0151  -0.0122 -0.0027 208 TRP A CZ2 
1740 C  CZ3 . TRP A 206 ? 0.0712 0.0348 0.0255 -0.0020 -0.0064 0.0036  208 TRP A CZ3 
1741 C  CH2 . TRP A 206 ? 0.0608 0.0397 0.0408 0.0081  -0.0122 -0.0015 208 TRP A CH2 
1742 N  N   . ILE A 207 ? 0.0363 0.0303 0.0400 -0.0036 -0.0111 -0.0018 209 ILE A N   
1743 C  CA  . ILE A 207 ? 0.0345 0.0432 0.0470 -0.0032 -0.0064 -0.0099 209 ILE A CA  
1744 C  C   . ILE A 207 ? 0.0488 0.0382 0.0346 0.0013  0.0004  -0.0031 209 ILE A C   
1745 O  O   . ILE A 207 ? 0.0800 0.0487 0.0336 -0.0025 -0.0044 -0.0042 209 ILE A O   
1746 C  CB  . ILE A 207 ? 0.0544 0.0371 0.0923 0.0061  -0.0010 -0.0054 209 ILE A CB  
1747 C  CG1 . ILE A 207 ? 0.0584 0.0327 0.1338 0.0239  -0.0031 -0.0185 209 ILE A CG1 
1748 C  CG2 . ILE A 207 ? 0.0454 0.0547 0.0935 0.0041  -0.0085 0.0079  209 ILE A CG2 
1749 C  CD1 . ILE A 207 ? 0.0496 0.0627 0.1242 0.0291  -0.0107 -0.0097 209 ILE A CD1 
1750 N  N   . VAL A 208 ? 0.0487 0.0334 0.0463 -0.0124 0.0022  -0.0042 210 VAL A N   
1751 C  CA  . VAL A 208 ? 0.0434 0.0348 0.0294 0.0041  -0.0033 -0.0017 210 VAL A CA  
1752 C  C   . VAL A 208 ? 0.0478 0.0335 0.0381 0.0067  -0.0004 0.0036  210 VAL A C   
1753 O  O   . VAL A 208 ? 0.0756 0.0470 0.0375 -0.0171 0.0048  0.0011  210 VAL A O   
1754 C  CB  . VAL A 208 ? 0.0396 0.0392 0.0479 0.0038  -0.0093 -0.0025 210 VAL A CB  
1755 C  CG1 . VAL A 208 ? 0.0706 0.0415 0.0610 0.0129  -0.0062 -0.0100 210 VAL A CG1 
1756 C  CG2 . VAL A 208 ? 0.0608 0.0644 0.0671 -0.0208 -0.0048 -0.0027 210 VAL A CG2 
1757 N  N   . LEU A 209 ? 0.0531 0.0531 0.0584 -0.0059 -0.0147 0.0002  211 LEU A N   
1758 C  CA  . LEU A 209 ? 0.0655 0.0459 0.0563 -0.0187 -0.0125 0.0064  211 LEU A CA  
1759 C  C   . LEU A 209 ? 0.0546 0.0460 0.0510 -0.0173 -0.0093 0.0066  211 LEU A C   
1760 O  O   . LEU A 209 ? 0.0644 0.0680 0.0573 -0.0099 -0.0039 -0.0037 211 LEU A O   
1761 C  CB  . LEU A 209 ? 0.0489 0.0644 0.0732 -0.0174 -0.0183 0.0054  211 LEU A CB  
1762 C  CG  . LEU A 209 ? 0.0761 0.0741 0.0593 0.0020  -0.0243 0.0085  211 LEU A CG  
1763 C  CD1 . LEU A 209 ? 0.0625 0.1332 0.0883 -0.0052 -0.0365 0.0260  211 LEU A CD1 
1764 C  CD2 . LEU A 209 ? 0.0761 0.0935 0.0901 -0.0011 0.0023  -0.0050 211 LEU A CD2 
1765 N  N   . LYS A 210 ? 0.0741 0.0686 0.0549 -0.0250 -0.0092 0.0238  212 LYS A N   
1766 C  CA  . LYS A 210 ? 0.1047 0.0616 0.0488 -0.0037 -0.0013 0.0150  212 LYS A CA  
1767 C  C   . LYS A 210 ? 0.0636 0.0575 0.0619 -0.0018 -0.0103 0.0188  212 LYS A C   
1768 O  O   . LYS A 210 ? 0.0785 0.0575 0.1151 0.0019  -0.0373 0.0137  212 LYS A O   
1769 C  CB  . LYS A 210 ? 0.1341 0.1011 0.0770 -0.0422 0.0176  0.0128  212 LYS A CB  
1770 C  CG  . LYS A 210 ? 0.1672 0.1198 0.1320 -0.0271 0.0012  0.0480  212 LYS A CG  
1771 C  CD  . LYS A 210 ? 0.3088 0.1805 0.1694 -0.1404 0.0605  0.0131  212 LYS A CD  
1772 C  CE  . LYS A 210 ? 0.3820 0.2235 0.2272 -0.0625 0.1235  0.0988  212 LYS A CE  
1773 N  N   A GLU A 211 ? 0.0589 0.0566 0.0573 -0.0162 -0.0168 0.0128  213 GLU A N   
1774 N  N   B GLU A 211 ? 0.0608 0.0558 0.0636 -0.0080 -0.0137 0.0212  213 GLU A N   
1775 C  CA  A GLU A 211 ? 0.0723 0.0558 0.0743 -0.0264 -0.0113 0.0004  213 GLU A CA  
1776 C  CA  B GLU A 211 ? 0.0619 0.0544 0.0829 -0.0110 -0.0127 0.0095  213 GLU A CA  
1777 C  C   A GLU A 211 ? 0.0624 0.0452 0.0606 -0.0197 -0.0254 0.0036  213 GLU A C   
1778 C  C   B GLU A 211 ? 0.0671 0.0461 0.0715 -0.0061 -0.0217 0.0140  213 GLU A C   
1779 O  O   A GLU A 211 ? 0.0615 0.0565 0.0662 -0.0150 -0.0145 0.0154  213 GLU A O   
1780 O  O   B GLU A 211 ? 0.0619 0.0557 0.0747 -0.0025 -0.0158 0.0240  213 GLU A O   
1781 C  CB  A GLU A 211 ? 0.0659 0.0937 0.0773 -0.0253 -0.0069 -0.0272 213 GLU A CB  
1782 C  CB  B GLU A 211 ? 0.0697 0.0576 0.0908 0.0059  -0.0226 0.0212  213 GLU A CB  
1783 C  CG  A GLU A 211 ? 0.0995 0.0901 0.0978 -0.0375 -0.0279 -0.0205 213 GLU A CG  
1784 C  CG  B GLU A 211 ? 0.0544 0.0980 0.1137 -0.0156 -0.0344 0.0098  213 GLU A CG  
1785 C  CD  A GLU A 211 ? 0.1084 0.1037 0.1356 -0.0236 -0.0295 -0.0357 213 GLU A CD  
1786 C  CD  B GLU A 211 ? 0.0575 0.0671 0.1266 -0.0140 -0.0399 0.0210  213 GLU A CD  
1787 O  OE1 A GLU A 211 ? 0.1234 0.0937 0.1471 -0.0199 -0.0154 -0.0221 213 GLU A OE1 
1788 O  OE1 B GLU A 211 ? 0.0409 0.0989 0.1081 -0.0004 -0.0274 0.0131  213 GLU A OE1 
1789 O  OE2 A GLU A 211 ? 0.1837 0.1449 0.1553 -0.0353 -0.0789 0.0009  213 GLU A OE2 
1790 O  OE2 B GLU A 211 ? 0.0767 0.0788 0.2092 -0.0436 -0.0418 0.0006  213 GLU A OE2 
1791 N  N   A PRO A 212 ? 0.0603 0.0479 0.0488 -0.0157 -0.0237 0.0089  214 PRO A N   
1792 N  N   B PRO A 212 ? 0.0713 0.0449 0.0610 -0.0039 -0.0164 0.0228  214 PRO A N   
1793 C  CA  A PRO A 212 ? 0.0689 0.0519 0.0461 -0.0147 -0.0237 -0.0046 214 PRO A CA  
1794 C  CA  B PRO A 212 ? 0.0844 0.0584 0.0591 -0.0003 -0.0177 0.0052  214 PRO A CA  
1795 C  C   A PRO A 212 ? 0.0592 0.0682 0.0627 -0.0204 -0.0280 -0.0146 214 PRO A C   
1796 C  C   B PRO A 212 ? 0.0723 0.0697 0.0756 -0.0046 -0.0204 -0.0024 214 PRO A C   
1797 O  O   A PRO A 212 ? 0.0612 0.0653 0.0761 -0.0308 -0.0379 -0.0109 214 PRO A O   
1798 O  O   B PRO A 212 ? 0.0944 0.0599 0.0960 -0.0148 0.0040  0.0122  214 PRO A O   
1799 C  CB  A PRO A 212 ? 0.0594 0.0460 0.0616 -0.0184 -0.0149 0.0001  214 PRO A CB  
1800 C  CB  B PRO A 212 ? 0.0838 0.0540 0.1056 0.0004  -0.0049 0.0041  214 PRO A CB  
1801 C  CG  A PRO A 212 ? 0.0610 0.0400 0.0624 -0.0183 -0.0205 0.0005  214 PRO A CG  
1802 C  CG  B PRO A 212 ? 0.1187 0.1076 0.1058 0.0071  0.0158  0.0010  214 PRO A CG  
1803 C  CD  A PRO A 212 ? 0.0831 0.0391 0.0557 -0.0117 -0.0218 0.0002  214 PRO A CD  
1804 C  CD  B PRO A 212 ? 0.1053 0.0102 0.1045 -0.0050 0.0018  0.0085  214 PRO A CD  
1805 N  N   . ILE A 213 ? 0.0697 0.0838 0.0636 -0.0089 -0.0200 -0.0119 215 ILE A N   
1806 C  CA  . ILE A 213 ? 0.0880 0.0637 0.0773 -0.0057 -0.0411 -0.0125 215 ILE A CA  
1807 C  C   . ILE A 213 ? 0.0784 0.0679 0.0791 -0.0095 -0.0089 -0.0048 215 ILE A C   
1808 O  O   . ILE A 213 ? 0.0898 0.0636 0.1023 0.0044  -0.0179 -0.0129 215 ILE A O   
1809 C  CB  . ILE A 213 ? 0.1084 0.0506 0.1212 0.0077  -0.0271 -0.0009 215 ILE A CB  
1810 C  CG1 . ILE A 213 ? 0.1199 0.0831 0.0890 -0.0132 -0.0400 0.0230  215 ILE A CG1 
1811 C  CG2 . ILE A 213 ? 0.1221 0.0721 0.1230 0.0298  -0.0653 -0.0227 215 ILE A CG2 
1812 C  CD1 . ILE A 213 ? 0.1668 0.0655 0.1119 -0.0085 -0.0424 0.0261  215 ILE A CD1 
1813 N  N   A SER A 214 ? 0.1187 0.0480 0.0818 -0.0130 -0.0249 -0.0111 216 SER A N   
1814 N  N   B SER A 214 ? 0.1076 0.0697 0.0908 -0.0132 -0.0234 -0.0177 216 SER A N   
1815 C  CA  A SER A 214 ? 0.1341 0.0510 0.0820 -0.0149 -0.0057 -0.0081 216 SER A CA  
1816 C  CA  B SER A 214 ? 0.1208 0.0668 0.0910 -0.0229 0.0012  -0.0113 216 SER A CA  
1817 C  C   A SER A 214 ? 0.1252 0.0144 0.0741 -0.0073 -0.0420 -0.0106 216 SER A C   
1818 C  C   B SER A 214 ? 0.1170 0.0357 0.0838 -0.0271 -0.0348 -0.0286 216 SER A C   
1819 O  O   A SER A 214 ? 0.1370 0.0635 0.0891 0.0072  -0.0518 0.0057  216 SER A O   
1820 O  O   B SER A 214 ? 0.1135 0.0664 0.1005 -0.0201 -0.0231 -0.0147 216 SER A O   
1821 C  CB  A SER A 214 ? 0.1860 0.0099 0.1005 -0.0195 -0.0076 0.0124  216 SER A CB  
1822 C  CB  B SER A 214 ? 0.1499 0.0571 0.1665 -0.0335 -0.0326 0.0223  216 SER A CB  
1823 O  OG  A SER A 214 ? 0.1352 0.0838 0.0732 -0.0402 -0.0282 0.0149  216 SER A OG  
1824 O  OG  B SER A 214 ? 0.1622 0.1102 0.2307 -0.0273 -0.0321 -0.0144 216 SER A OG  
1825 N  N   . VAL A 215 ? 0.1306 0.0610 0.0750 -0.0252 -0.0165 -0.0279 217 VAL A N   
1826 C  CA  . VAL A 215 ? 0.1199 0.0607 0.0743 -0.0163 -0.0168 -0.0244 217 VAL A CA  
1827 C  C   . VAL A 215 ? 0.1283 0.0417 0.0732 -0.0197 -0.0525 -0.0038 217 VAL A C   
1828 O  O   . VAL A 215 ? 0.1291 0.0566 0.0741 -0.0154 -0.0427 -0.0010 217 VAL A O   
1829 C  CB  . VAL A 215 ? 0.1240 0.0637 0.1065 -0.0273 -0.0518 -0.0175 217 VAL A CB  
1830 C  CG1 . VAL A 215 ? 0.1496 0.0748 0.0785 -0.0209 -0.0532 -0.0220 217 VAL A CG1 
1831 C  CG2 . VAL A 215 ? 0.1255 0.0557 0.1574 -0.0350 -0.0683 -0.0027 217 VAL A CG2 
1832 N  N   . SER A 216 ? 0.1208 0.0687 0.0734 -0.0174 -0.0370 -0.0306 218 SER A N   
1833 C  CA  . SER A 216 ? 0.1266 0.0562 0.1002 -0.0073 -0.0324 -0.0155 218 SER A CA  
1834 C  C   . SER A 216 ? 0.1428 0.0427 0.1057 -0.0116 -0.0273 -0.0012 218 SER A C   
1835 O  O   . SER A 216 ? 0.1406 0.0594 0.0882 -0.0226 -0.0334 -0.0089 218 SER A O   
1836 C  CB  . SER A 216 ? 0.2163 0.0664 0.0856 -0.0201 -0.0480 -0.0163 218 SER A CB  
1837 O  OG  . SER A 216 ? 0.1866 0.0968 0.0885 -0.0179 -0.0402 -0.0111 218 SER A OG  
1838 N  N   A SER A 217 ? 0.1449 0.0488 0.1120 0.0022  -0.0372 -0.0147 219 SER A N   
1839 N  N   B SER A 217 ? 0.1338 0.0502 0.1180 0.0013  -0.0364 -0.0210 219 SER A N   
1840 C  CA  A SER A 217 ? 0.1492 0.0540 0.1316 -0.0005 -0.0355 -0.0012 219 SER A CA  
1841 C  CA  B SER A 217 ? 0.1342 0.0475 0.1410 -0.0035 -0.0355 0.0027  219 SER A CA  
1842 C  C   A SER A 217 ? 0.1643 0.0589 0.1525 -0.0179 -0.0201 -0.0004 219 SER A C   
1843 C  C   B SER A 217 ? 0.1428 0.0549 0.1526 -0.0355 -0.0135 -0.0083 219 SER A C   
1844 O  O   A SER A 217 ? 0.1790 0.0337 0.1690 -0.0263 -0.0209 -0.0296 219 SER A O   
1845 O  O   B SER A 217 ? 0.1345 0.0743 0.2046 -0.0245 0.0277  0.0179  219 SER A O   
1846 C  CB  A SER A 217 ? 0.1805 0.0545 0.1783 -0.0057 -0.0556 0.0099  219 SER A CB  
1847 C  CB  B SER A 217 ? 0.1384 0.0487 0.1510 -0.0033 -0.0628 -0.0297 219 SER A CB  
1848 O  OG  A SER A 217 ? 0.1956 0.0635 0.1615 -0.0013 -0.0453 -0.0031 219 SER A OG  
1849 O  OG  B SER A 217 ? 0.1410 0.0610 0.1676 0.0110  -0.0588 -0.0076 219 SER A OG  
1850 N  N   . GLU A 218 ? 0.1937 0.0646 0.1076 -0.0012 -0.0167 -0.0159 220 GLU A N   
1851 C  CA  . GLU A 218 ? 0.2405 0.0820 0.1102 -0.0141 -0.0152 -0.0147 220 GLU A CA  
1852 C  C   . GLU A 218 ? 0.1988 0.0873 0.0610 -0.0165 0.0009  -0.0176 220 GLU A C   
1853 O  O   . GLU A 218 ? 0.2337 0.1084 0.0995 -0.0111 0.0325  -0.0201 220 GLU A O   
1854 C  CB  . GLU A 218 ? 0.2812 0.1102 0.1156 -0.0278 -0.0337 -0.0725 220 GLU A CB  
1855 C  CG  . GLU A 218 ? 0.3569 0.1053 0.1844 -0.0237 -0.0575 -0.0707 220 GLU A CG  
1856 C  CD  . GLU A 218 ? 0.3775 0.1294 0.2917 -0.0307 -0.0138 -0.1263 220 GLU A CD  
1857 O  OE1 . GLU A 218 ? 0.2506 0.1320 0.2414 -0.0747 0.0043  -0.0577 220 GLU A OE1 
1858 O  OE2 . GLU A 218 ? 0.4623 0.2736 0.4160 -0.2181 0.1077  -0.2223 220 GLU A OE2 
1859 N  N   . GLN A 219 ? 0.1574 0.0567 0.0671 -0.0073 -0.0165 -0.0055 221 GLN A N   
1860 C  CA  . GLN A 219 ? 0.1478 0.0634 0.1230 -0.0144 -0.0201 -0.0076 221 GLN A CA  
1861 C  C   . GLN A 219 ? 0.1535 0.0478 0.0943 -0.0100 -0.0147 -0.0013 221 GLN A C   
1862 O  O   . GLN A 219 ? 0.1485 0.0838 0.0743 -0.0335 -0.0038 -0.0087 221 GLN A O   
1863 C  CB  . GLN A 219 ? 0.1535 0.0738 0.0879 -0.0280 -0.0348 -0.0247 221 GLN A CB  
1864 C  CG  . GLN A 219 ? 0.1403 0.0908 0.0734 -0.0164 -0.0226 -0.0099 221 GLN A CG  
1865 C  CD  . GLN A 219 ? 0.1751 0.0610 0.0653 -0.0241 -0.0264 -0.0117 221 GLN A CD  
1866 O  OE1 . GLN A 219 ? 0.1654 0.0677 0.0626 0.0083  -0.0242 0.0034  221 GLN A OE1 
1867 N  NE2 . GLN A 219 ? 0.1238 0.0802 0.0985 -0.0258 -0.0297 -0.0041 221 GLN A NE2 
1868 N  N   . VAL A 220 ? 0.1525 0.0748 0.0795 -0.0166 -0.0388 0.0061  222 VAL A N   
1869 C  CA  . VAL A 220 ? 0.1492 0.0698 0.0899 -0.0211 -0.0188 0.0100  222 VAL A CA  
1870 C  C   . VAL A 220 ? 0.1464 0.0713 0.1344 -0.0392 -0.0074 0.0118  222 VAL A C   
1871 O  O   . VAL A 220 ? 0.1360 0.1032 0.0865 -0.0359 0.0027  0.0245  222 VAL A O   
1872 C  CB  . VAL A 220 ? 0.1532 0.1076 0.1263 -0.0228 -0.0594 0.0485  222 VAL A CB  
1873 C  CG1 . VAL A 220 ? 0.2092 0.1136 0.1848 -0.0648 -0.0268 0.0230  222 VAL A CG1 
1874 C  CG2 . VAL A 220 ? 0.1668 0.1377 0.1525 -0.0212 -0.0560 -0.0022 222 VAL A CG2 
1875 N  N   . LEU A 221 ? 0.1722 0.0770 0.1116 -0.0077 0.0110  -0.0068 223 LEU A N   
1876 C  CA  . LEU A 221 ? 0.2090 0.0662 0.1640 0.0068  0.0265  -0.0260 223 LEU A CA  
1877 C  C   . LEU A 221 ? 0.1650 0.1146 0.1230 -0.0254 -0.0227 -0.0196 223 LEU A C   
1878 O  O   . LEU A 221 ? 0.1625 0.1291 0.1622 -0.0142 0.0171  -0.0187 223 LEU A O   
1879 C  CB  . LEU A 221 ? 0.2329 0.0864 0.1791 -0.0138 0.0185  -0.0405 223 LEU A CB  
1880 C  CG  . LEU A 221 ? 0.2802 0.1212 0.2486 -0.0377 0.0656  -0.0011 223 LEU A CG  
1881 C  CD1 . LEU A 221 ? 0.3346 0.1829 0.2538 -0.0555 0.0409  -0.0469 223 LEU A CD1 
1882 C  CD2 . LEU A 221 ? 0.2523 0.2020 0.3733 -0.0347 0.1188  -0.0924 223 LEU A CD2 
1883 N  N   . LYS A 222 ? 0.1640 0.1222 0.0900 -0.0182 -0.0187 -0.0018 224 LYS A N   
1884 C  CA  . LYS A 222 ? 0.1696 0.1694 0.0835 -0.0173 -0.0406 0.0188  224 LYS A CA  
1885 C  C   . LYS A 222 ? 0.1611 0.1216 0.0488 0.0000  -0.0047 0.0093  224 LYS A C   
1886 O  O   . LYS A 222 ? 0.1862 0.1622 0.0540 -0.0183 0.0043  0.0117  224 LYS A O   
1887 C  CB  . LYS A 222 ? 0.1653 0.2028 0.1082 -0.0107 -0.0179 0.0389  224 LYS A CB  
1888 C  CG  . LYS A 222 ? 0.2236 0.3590 0.1147 -0.0662 -0.0600 0.0049  224 LYS A CG  
1889 C  CD  . LYS A 222 ? 0.2275 0.3679 0.3349 -0.0277 -0.0815 -0.1075 224 LYS A CD  
1890 C  CE  . LYS A 222 ? 0.3290 0.3306 0.2586 -0.0546 -0.1086 -0.0785 224 LYS A CE  
1891 N  NZ  . LYS A 222 ? 0.2951 0.3097 0.3209 0.0077  0.0279  -0.0254 224 LYS A NZ  
1892 N  N   . PHE A 223 ? 0.1388 0.0924 0.0436 -0.0034 -0.0201 0.0032  225 PHE A N   
1893 C  CA  . PHE A 223 ? 0.1172 0.0908 0.0610 -0.0164 -0.0030 0.0175  225 PHE A CA  
1894 C  C   . PHE A 223 ? 0.1474 0.0847 0.0670 -0.0088 0.0047  0.0022  225 PHE A C   
1895 O  O   . PHE A 223 ? 0.1439 0.0888 0.0564 -0.0172 0.0099  -0.0153 225 PHE A O   
1896 C  CB  . PHE A 223 ? 0.1858 0.0925 0.0557 0.0049  -0.0124 -0.0010 225 PHE A CB  
1897 C  CG  . PHE A 223 ? 0.1593 0.0527 0.0803 -0.0337 0.0020  -0.0149 225 PHE A CG  
1898 C  CD1 . PHE A 223 ? 0.1866 0.1471 0.1084 0.0194  0.0114  0.0013  225 PHE A CD1 
1899 C  CD2 . PHE A 223 ? 0.2253 0.1135 0.0943 -0.0068 0.0002  -0.0629 225 PHE A CD2 
1900 C  CE1 . PHE A 223 ? 0.2049 0.1617 0.1244 0.0186  0.0283  -0.0162 225 PHE A CE1 
1901 C  CE2 . PHE A 223 ? 0.2042 0.1273 0.1629 0.0047  -0.0188 -0.0895 225 PHE A CE2 
1902 C  CZ  . PHE A 223 ? 0.1913 0.1007 0.1463 -0.0118 0.0003  -0.0491 225 PHE A CZ  
1903 N  N   . ARG A 224 ? 0.1388 0.0881 0.0553 -0.0030 -0.0038 0.0091  226 ARG A N   
1904 C  CA  . ARG A 224 ? 0.1514 0.0813 0.0644 0.0046  0.0111  -0.0008 226 ARG A CA  
1905 C  C   . ARG A 224 ? 0.1406 0.0926 0.0689 -0.0303 0.0022  -0.0089 226 ARG A C   
1906 O  O   . ARG A 224 ? 0.1539 0.1107 0.0937 -0.0003 0.0047  0.0027  226 ARG A O   
1907 C  CB  . ARG A 224 ? 0.1694 0.0818 0.0716 0.0165  0.0179  0.0083  226 ARG A CB  
1908 C  CG  . ARG A 224 ? 0.1640 0.0786 0.0632 -0.0146 0.0055  0.0023  226 ARG A CG  
1909 C  CD  . ARG A 224 ? 0.1998 0.0680 0.0636 -0.0350 -0.0096 -0.0161 226 ARG A CD  
1910 N  NE  . ARG A 224 ? 0.1916 0.0801 0.0496 -0.0579 -0.0266 0.0037  226 ARG A NE  
1911 C  CZ  . ARG A 224 ? 0.1841 0.0871 0.0678 -0.0581 -0.0158 -0.0159 226 ARG A CZ  
1912 N  NH1 . ARG A 224 ? 0.2426 0.1004 0.1090 -0.0682 -0.0122 -0.0444 226 ARG A NH1 
1913 N  NH2 . ARG A 224 ? 0.1757 0.1295 0.0723 -0.0544 -0.0059 0.0164  226 ARG A NH2 
1914 N  N   . LYS A 225 ? 0.1615 0.0820 0.0433 -0.0350 -0.0079 -0.0105 227 LYS A N   
1915 C  CA  . LYS A 225 ? 0.1801 0.1058 0.0572 -0.0412 0.0100  -0.0131 227 LYS A CA  
1916 C  C   . LYS A 225 ? 0.1805 0.0891 0.0417 -0.0172 0.0243  -0.0089 227 LYS A C   
1917 O  O   . LYS A 225 ? 0.2161 0.1471 0.0451 -0.0220 0.0431  -0.0259 227 LYS A O   
1918 C  CB  . LYS A 225 ? 0.1934 0.1597 0.0689 -0.0324 -0.0120 -0.0243 227 LYS A CB  
1919 C  CG  . LYS A 225 ? 0.2849 0.1694 0.1014 -0.0568 0.0139  -0.0228 227 LYS A CG  
1920 C  CD  . LYS A 225 ? 0.3771 0.2893 0.1294 -0.1001 -0.0358 -0.1081 227 LYS A CD  
1921 C  CE  . LYS A 225 ? 0.3844 0.4476 0.2192 -0.2044 0.0477  -0.0344 227 LYS A CE  
1922 N  NZ  . LYS A 225 ? 0.5899 0.5847 0.4717 -0.0662 -0.1965 -0.1367 227 LYS A NZ  
1923 N  N   . LEU A 226 ? 0.1920 0.0697 0.0709 -0.0286 0.0126  -0.0204 228 LEU A N   
1924 C  CA  . LEU A 226 ? 0.1700 0.0741 0.0679 -0.0249 0.0442  -0.0171 228 LEU A CA  
1925 C  C   . LEU A 226 ? 0.2013 0.0748 0.0381 -0.0234 0.0407  -0.0315 228 LEU A C   
1926 O  O   . LEU A 226 ? 0.1553 0.0952 0.0653 -0.0182 0.0368  -0.0190 228 LEU A O   
1927 C  CB  . LEU A 226 ? 0.2010 0.0865 0.0466 -0.0285 0.0230  -0.0268 228 LEU A CB  
1928 C  CG  . LEU A 226 ? 0.2103 0.1032 0.0468 -0.0234 0.0245  -0.0096 228 LEU A CG  
1929 C  CD1 . LEU A 226 ? 0.1945 0.1164 0.0706 -0.0128 0.0223  -0.0365 228 LEU A CD1 
1930 C  CD2 . LEU A 226 ? 0.2850 0.1226 0.0743 0.0075  0.0417  0.0184  228 LEU A CD2 
1931 N  N   . ASN A 227 ? 0.1737 0.1212 0.0555 -0.0482 0.0283  0.0004  229 ASN A N   
1932 C  CA  . ASN A 227 ? 0.1542 0.1266 0.0480 -0.0316 0.0301  -0.0178 229 ASN A CA  
1933 C  C   . ASN A 227 ? 0.1708 0.1203 0.0698 -0.0299 0.0652  -0.0120 229 ASN A C   
1934 O  O   . ASN A 227 ? 0.1945 0.1164 0.0818 -0.0325 0.0303  -0.0226 229 ASN A O   
1935 C  CB  . ASN A 227 ? 0.2035 0.1198 0.0470 -0.0135 0.0339  -0.0064 229 ASN A CB  
1936 C  CG  . ASN A 227 ? 0.1894 0.1456 0.0506 -0.0475 0.0333  -0.0227 229 ASN A CG  
1937 O  OD1 . ASN A 227 ? 0.2899 0.1781 0.0591 -0.0337 0.0648  -0.0141 229 ASN A OD1 
1938 N  ND2 . ASN A 227 ? 0.2064 0.1119 0.0601 -0.0365 0.0433  -0.0231 229 ASN A ND2 
1939 N  N   . PHE A 228 ? 0.1452 0.1240 0.0761 -0.0858 0.0489  -0.0258 230 PHE A N   
1940 C  CA  . PHE A 228 ? 0.1208 0.1146 0.1059 -0.0652 0.0339  -0.0243 230 PHE A CA  
1941 C  C   . PHE A 228 ? 0.1891 0.1229 0.1120 -0.0710 0.0627  -0.0270 230 PHE A C   
1942 O  O   . PHE A 228 ? 0.1812 0.1198 0.1049 -0.0859 0.0384  0.0030  230 PHE A O   
1943 C  CB  . PHE A 228 ? 0.1744 0.1266 0.0941 -0.0575 0.0309  -0.0189 230 PHE A CB  
1944 C  CG  . PHE A 228 ? 0.1629 0.0844 0.1054 -0.0586 0.0425  -0.0321 230 PHE A CG  
1945 C  CD1 . PHE A 228 ? 0.1689 0.0964 0.0646 -0.0159 0.0106  -0.0207 230 PHE A CD1 
1946 C  CD2 . PHE A 228 ? 0.1970 0.0835 0.0861 -0.0445 0.0396  -0.0355 230 PHE A CD2 
1947 C  CE1 . PHE A 228 ? 0.1944 0.0800 0.0986 -0.0736 0.0260  -0.0143 230 PHE A CE1 
1948 C  CE2 . PHE A 228 ? 0.2117 0.0864 0.0828 -0.0446 0.0270  -0.0248 230 PHE A CE2 
1949 C  CZ  . PHE A 228 ? 0.1876 0.0865 0.1032 -0.0476 0.0135  -0.0397 230 PHE A CZ  
1950 N  N   . ASN A 229 ? 0.2099 0.1500 0.0716 -0.0661 0.0547  -0.0326 231 ASN A N   
1951 C  CA  . ASN A 229 ? 0.1816 0.1234 0.1234 -0.0693 0.0578  -0.0288 231 ASN A CA  
1952 C  C   . ASN A 229 ? 0.1970 0.1503 0.0536 -0.0573 0.0532  -0.0328 231 ASN A C   
1953 O  O   . ASN A 229 ? 0.2102 0.1298 0.1171 -0.0402 0.0584  -0.0279 231 ASN A O   
1954 C  CB  . ASN A 229 ? 0.2207 0.1581 0.1223 -0.0463 0.0772  -0.0401 231 ASN A CB  
1955 C  CG  . ASN A 229 ? 0.2055 0.1252 0.1084 -0.0326 0.0632  -0.0143 231 ASN A CG  
1956 O  OD1 . ASN A 229 ? 0.2785 0.1242 0.1159 -0.0568 0.0800  -0.0221 231 ASN A OD1 
1957 N  ND2 . ASN A 229 ? 0.2388 0.1744 0.0819 -0.0188 0.0413  -0.0494 231 ASN A ND2 
1958 N  N   . GLY A 230 ? 0.2293 0.1136 0.1561 -0.0406 0.0928  -0.0212 232 GLY A N   
1959 C  CA  . GLY A 230 ? 0.2418 0.1324 0.1683 -0.0296 0.0889  -0.0053 232 GLY A CA  
1960 C  C   . GLY A 230 ? 0.2250 0.1324 0.1829 -0.0324 0.0168  -0.0049 232 GLY A C   
1961 O  O   . GLY A 230 ? 0.2444 0.1949 0.0928 0.0103  0.0810  0.0157  232 GLY A O   
1962 N  N   . GLU A 231 ? 0.2235 0.1574 0.1064 -0.0358 0.0640  -0.0286 233 GLU A N   
1963 C  CA  . GLU A 231 ? 0.1959 0.1617 0.1032 0.0205  0.0249  -0.0242 233 GLU A CA  
1964 C  C   . GLU A 231 ? 0.1948 0.2398 0.1234 0.0458  0.0174  -0.0516 233 GLU A C   
1965 O  O   . GLU A 231 ? 0.2307 0.2679 0.1212 -0.0164 0.0729  -0.0133 233 GLU A O   
1966 C  CB  . GLU A 231 ? 0.1858 0.1715 0.1176 0.0197  0.0280  0.0078  233 GLU A CB  
1967 C  CG  . GLU A 231 ? 0.2141 0.2042 0.0978 -0.0766 0.0482  0.0297  233 GLU A CG  
1968 C  CD  . GLU A 231 ? 0.3113 0.3019 0.2442 0.0221  -0.0512 -0.0084 233 GLU A CD  
1969 O  OE1 . GLU A 231 ? 0.3721 0.2433 0.1568 -0.0957 0.0666  0.0176  233 GLU A OE1 
1970 O  OE2 . GLU A 231 ? 0.2625 0.2653 0.2095 -0.0324 -0.0319 -0.0138 233 GLU A OE2 
1971 N  N   . GLY A 232 ? 0.2867 0.2181 0.1313 0.0651  0.0597  -0.0258 234 GLY A N   
1972 C  CA  . GLY A 232 ? 0.3078 0.4105 0.1172 0.1190  0.0395  -0.0653 234 GLY A CA  
1973 C  C   . GLY A 232 ? 0.2717 0.4507 0.1636 0.0605  0.0161  0.0696  234 GLY A C   
1974 O  O   . GLY A 232 ? 0.4012 0.7465 0.2048 0.1249  0.1565  0.0312  234 GLY A O   
1975 N  N   . GLU A 233 ? 0.2243 0.2479 0.1661 -0.0036 0.0268  -0.0306 235 GLU A N   
1976 C  CA  . GLU A 233 ? 0.2109 0.1682 0.1808 -0.0118 0.0078  -0.0406 235 GLU A CA  
1977 C  C   . GLU A 233 ? 0.2533 0.2370 0.1798 -0.0052 0.1584  -0.0128 235 GLU A C   
1978 O  O   . GLU A 233 ? 0.2711 0.2845 0.1859 0.0052  0.1136  -0.0031 235 GLU A O   
1979 C  CB  . GLU A 233 ? 0.2207 0.1665 0.1851 -0.0321 0.0421  -0.0285 235 GLU A CB  
1980 C  CG  . GLU A 233 ? 0.2319 0.1801 0.2852 -0.0650 0.1050  -0.0547 235 GLU A CG  
1981 C  CD  . GLU A 233 ? 0.4184 0.2153 0.2503 -0.1295 0.1908  -0.0458 235 GLU A CD  
1982 O  OE1 . GLU A 233 ? 0.2963 0.2662 0.2404 -0.1270 0.1335  -0.0467 235 GLU A OE1 
1983 O  OE2 . GLU A 233 ? 0.5995 0.2285 0.5316 -0.1935 0.1976  -0.0405 235 GLU A OE2 
1984 N  N   . PRO A 234 ? 0.2339 0.1762 0.2160 -0.0319 0.1430  0.0119  236 PRO A N   
1985 C  CA  . PRO A 234 ? 0.2278 0.1877 0.2390 -0.0111 0.1723  0.0087  236 PRO A CA  
1986 C  C   . PRO A 234 ? 0.2337 0.2038 0.0953 -0.0987 0.1071  -0.0443 236 PRO A C   
1987 O  O   . PRO A 234 ? 0.2449 0.2178 0.1442 -0.0531 0.0956  -0.0615 236 PRO A O   
1988 C  CB  . PRO A 234 ? 0.1931 0.3025 0.2623 0.0001  0.1759  -0.0186 236 PRO A CB  
1989 C  CG  . PRO A 234 ? 0.2653 0.2321 0.3976 0.0070  0.1093  0.1645  236 PRO A CG  
1990 C  CD  . PRO A 234 ? 0.2720 0.1794 0.3276 -0.0471 0.1800  0.0446  236 PRO A CD  
1991 N  N   . GLU A 235 ? 0.1834 0.1790 0.1826 -0.0596 0.0713  -0.0165 237 GLU A N   
1992 C  CA  . GLU A 235 ? 0.1891 0.2533 0.1147 -0.0718 0.0714  -0.0523 237 GLU A CA  
1993 C  C   . GLU A 235 ? 0.1909 0.1794 0.1428 -0.0359 0.0665  -0.0533 237 GLU A C   
1994 O  O   . GLU A 235 ? 0.1715 0.1816 0.1266 -0.0309 0.0190  -0.0405 237 GLU A O   
1995 C  CB  . GLU A 235 ? 0.1948 0.1532 0.1532 -0.0089 -0.0109 -0.0351 237 GLU A CB  
1996 C  CG  . GLU A 235 ? 0.2451 0.2372 0.2031 -0.0417 0.0209  -0.0819 237 GLU A CG  
1997 C  CD  . GLU A 235 ? 0.1654 0.2260 0.1646 -0.0002 0.0715  -0.1193 237 GLU A CD  
1998 O  OE1 . GLU A 235 ? 0.2716 0.2293 0.4569 0.0444  -0.0579 -0.1509 237 GLU A OE1 
1999 O  OE2 . GLU A 235 ? 0.2176 0.1604 0.1413 -0.0259 0.0395  -0.0574 237 GLU A OE2 
2000 N  N   . GLU A 236 ? 0.2176 0.1125 0.0908 -0.0798 0.0649  -0.0400 238 GLU A N   
2001 C  CA  . GLU A 236 ? 0.1622 0.2517 0.0979 -0.0903 0.0486  -0.0315 238 GLU A CA  
2002 C  C   . GLU A 236 ? 0.1640 0.1647 0.0497 -0.0570 0.0522  -0.0421 238 GLU A C   
2003 O  O   . GLU A 236 ? 0.2781 0.1313 0.0958 -0.0455 0.0515  -0.0148 238 GLU A O   
2004 C  CB  . GLU A 236 ? 0.2115 0.2199 0.1241 -0.0754 0.0390  -0.0288 238 GLU A CB  
2005 C  CG  . GLU A 236 ? 0.1751 0.1927 0.2437 0.0518  0.0221  -0.0546 238 GLU A CG  
2006 C  CD  . GLU A 236 ? 0.3035 0.3727 0.3036 -0.0550 -0.0106 -0.1276 238 GLU A CD  
2007 O  OE1 . GLU A 236 ? 0.3146 0.7153 0.4354 -0.3962 0.2654  -0.2955 238 GLU A OE1 
2008 O  OE2 . GLU A 236 ? 0.2861 0.2922 0.3199 0.0430  0.0065  -0.0559 238 GLU A OE2 
2009 N  N   . LEU A 237 ? 0.1434 0.1428 0.0538 -0.0343 0.0435  -0.0171 239 LEU A N   
2010 C  CA  . LEU A 237 ? 0.1395 0.1150 0.0885 -0.0388 0.0679  -0.0451 239 LEU A CA  
2011 C  C   . LEU A 237 ? 0.1162 0.1134 0.0644 -0.0042 0.0464  -0.0217 239 LEU A C   
2012 O  O   . LEU A 237 ? 0.1446 0.1164 0.0828 -0.0181 0.0309  -0.0113 239 LEU A O   
2013 C  CB  . LEU A 237 ? 0.1367 0.0867 0.1064 -0.0027 0.0351  -0.0331 239 LEU A CB  
2014 C  CG  . LEU A 237 ? 0.1205 0.1040 0.1367 -0.0042 0.0122  -0.0536 239 LEU A CG  
2015 C  CD1 . LEU A 237 ? 0.1747 0.0862 0.3034 -0.0042 -0.0522 -0.0178 239 LEU A CD1 
2016 C  CD2 . LEU A 237 ? 0.1991 0.1080 0.1526 0.0217  0.0071  -0.0135 239 LEU A CD2 
2017 N  N   . MET A 238 ? 0.1482 0.0891 0.0627 0.0050  0.0594  -0.0280 240 MET A N   
2018 C  CA  . MET A 238 ? 0.1819 0.0806 0.0461 -0.0003 0.0614  -0.0170 240 MET A CA  
2019 C  C   . MET A 238 ? 0.1356 0.0741 0.0353 -0.0398 0.0013  -0.0308 240 MET A C   
2020 O  O   . MET A 238 ? 0.1313 0.0883 0.0562 -0.0157 0.0086  -0.0176 240 MET A O   
2021 C  CB  . MET A 238 ? 0.1822 0.0540 0.0970 -0.0024 0.0647  -0.0268 240 MET A CB  
2022 C  CG  . MET A 238 ? 0.1855 0.0865 0.0697 -0.0080 0.0663  -0.0259 240 MET A CG  
2023 S  SD  . MET A 238 ? 0.1969 0.0743 0.0853 -0.0108 0.0452  -0.0078 240 MET A SD  
2024 C  CE  . MET A 238 ? 0.2795 0.0889 0.0662 -0.0355 0.0926  0.0195  240 MET A CE  
2025 N  N   . VAL A 239 ? 0.1478 0.0734 0.0346 -0.0192 0.0114  -0.0127 241 VAL A N   
2026 C  CA  . VAL A 239 ? 0.1253 0.0689 0.0248 -0.0086 0.0167  -0.0170 241 VAL A CA  
2027 C  C   . VAL A 239 ? 0.1027 0.0575 0.0364 -0.0005 0.0199  -0.0204 241 VAL A C   
2028 O  O   . VAL A 239 ? 0.1153 0.1003 0.0540 -0.0238 0.0317  -0.0166 241 VAL A O   
2029 C  CB  . VAL A 239 ? 0.1045 0.0662 0.0661 -0.0374 0.0049  -0.0127 241 VAL A CB  
2030 C  CG1 . VAL A 239 ? 0.1399 0.0612 0.0768 -0.0125 -0.0093 -0.0281 241 VAL A CG1 
2031 C  CG2 . VAL A 239 ? 0.1223 0.0891 0.0926 -0.0161 0.0274  -0.0292 241 VAL A CG2 
2032 N  N   . ASP A 240 ? 0.1118 0.0522 0.0281 -0.0050 0.0208  -0.0244 242 ASP A N   
2033 C  CA  . ASP A 240 ? 0.1076 0.0441 0.0469 0.0085  0.0053  -0.0270 242 ASP A CA  
2034 C  C   . ASP A 240 ? 0.0822 0.0549 0.0326 -0.0138 0.0192  -0.0026 242 ASP A C   
2035 O  O   . ASP A 240 ? 0.0907 0.0619 0.0786 -0.0173 0.0033  -0.0255 242 ASP A O   
2036 C  CB  . ASP A 240 ? 0.1138 0.0506 0.0773 0.0134  0.0179  -0.0043 242 ASP A CB  
2037 C  CG  . ASP A 240 ? 0.0986 0.0616 0.0564 0.0013  0.0072  -0.0313 242 ASP A CG  
2038 O  OD1 . ASP A 240 ? 0.1040 0.0632 0.0797 0.0087  0.0270  -0.0150 242 ASP A OD1 
2039 O  OD2 . ASP A 240 ? 0.1171 0.0662 0.1076 0.0075  0.0218  -0.0427 242 ASP A OD2 
2040 N  N   . ASN A 241 ? 0.1039 0.0417 0.0258 0.0008  0.0201  -0.0170 243 ASN A N   
2041 C  CA  . ASN A 241 ? 0.1168 0.0415 0.0364 -0.0026 0.0108  -0.0138 243 ASN A CA  
2042 C  C   . ASN A 241 ? 0.0767 0.0597 0.0337 -0.0042 0.0088  -0.0048 243 ASN A C   
2043 O  O   . ASN A 241 ? 0.1128 0.0697 0.0309 0.0119  0.0192  0.0107  243 ASN A O   
2044 C  CB  . ASN A 241 ? 0.0882 0.0761 0.0215 -0.0076 0.0204  -0.0048 243 ASN A CB  
2045 C  CG  . ASN A 241 ? 0.0961 0.0722 0.0487 -0.0187 0.0209  -0.0006 243 ASN A CG  
2046 O  OD1 . ASN A 241 ? 0.1120 0.0706 0.0636 -0.0131 0.0222  0.0100  243 ASN A OD1 
2047 N  ND2 . ASN A 241 ? 0.1388 0.1816 0.1568 -0.0422 -0.0207 0.1034  243 ASN A ND2 
2048 N  N   . TRP A 242 ? 0.0752 0.0503 0.0312 -0.0242 0.0031  -0.0038 244 TRP A N   
2049 C  CA  . TRP A 242 ? 0.0644 0.0547 0.0321 0.0013  -0.0001 -0.0040 244 TRP A CA  
2050 C  C   . TRP A 242 ? 0.0671 0.0599 0.0335 0.0040  -0.0012 0.0003  244 TRP A C   
2051 O  O   . TRP A 242 ? 0.0572 0.0662 0.0603 -0.0034 -0.0013 -0.0163 244 TRP A O   
2052 C  CB  . TRP A 242 ? 0.0894 0.0284 0.0406 0.0040  0.0117  -0.0099 244 TRP A CB  
2053 C  CG  . TRP A 242 ? 0.0725 0.0405 0.0544 0.0163  0.0150  -0.0031 244 TRP A CG  
2054 C  CD1 . TRP A 242 ? 0.1023 0.0488 0.0557 0.0086  0.0294  -0.0085 244 TRP A CD1 
2055 C  CD2 . TRP A 242 ? 0.0583 0.0653 0.0408 0.0142  0.0079  -0.0049 244 TRP A CD2 
2056 N  NE1 . TRP A 242 ? 0.0846 0.0565 0.0547 0.0132  0.0162  0.0060  244 TRP A NE1 
2057 C  CE2 . TRP A 242 ? 0.0688 0.0470 0.0653 0.0062  0.0087  0.0067  244 TRP A CE2 
2058 C  CE3 . TRP A 242 ? 0.0776 0.0906 0.0470 0.0025  -0.0131 0.0097  244 TRP A CE3 
2059 C  CZ2 . TRP A 242 ? 0.0882 0.0598 0.0687 0.0109  -0.0066 0.0107  244 TRP A CZ2 
2060 C  CZ3 . TRP A 242 ? 0.0932 0.0960 0.0806 0.0232  0.0088  0.0227  244 TRP A CZ3 
2061 C  CH2 . TRP A 242 ? 0.1144 0.1115 0.0653 0.0110  -0.0008 0.0106  244 TRP A CH2 
2062 N  N   . ARG A 243 ? 0.0650 0.0554 0.0346 -0.0062 -0.0008 -0.0009 245 ARG A N   
2063 C  CA  . ARG A 243 ? 0.0549 0.0461 0.0513 -0.0041 -0.0068 -0.0118 245 ARG A CA  
2064 C  C   . ARG A 243 ? 0.0576 0.0597 0.0452 0.0104  -0.0044 -0.0118 245 ARG A C   
2065 O  O   . ARG A 243 ? 0.0617 0.0607 0.0653 0.0027  0.0071  -0.0069 245 ARG A O   
2066 C  CB  . ARG A 243 ? 0.0425 0.0480 0.0488 -0.0002 -0.0148 -0.0099 245 ARG A CB  
2067 C  CG  . ARG A 243 ? 0.0459 0.0593 0.0497 -0.0080 -0.0118 -0.0234 245 ARG A CG  
2068 C  CD  . ARG A 243 ? 0.0531 0.0659 0.0653 0.0003  -0.0139 -0.0286 245 ARG A CD  
2069 N  NE  . ARG A 243 ? 0.0549 0.0743 0.0554 -0.0236 -0.0050 -0.0228 245 ARG A NE  
2070 C  CZ  . ARG A 243 ? 0.0328 0.0698 0.0431 -0.0280 0.0076  -0.0174 245 ARG A CZ  
2071 N  NH1 . ARG A 243 ? 0.0565 0.0809 0.0722 -0.0005 0.0091  -0.0003 245 ARG A NH1 
2072 N  NH2 . ARG A 243 ? 0.0353 0.0923 0.1072 -0.0269 -0.0108 -0.0005 245 ARG A NH2 
2073 N  N   A PRO A 244 ? 0.0567 0.0533 0.0427 0.0082  0.0048  -0.0059 246 PRO A N   
2074 N  N   B PRO A 244 ? 0.0697 0.0635 0.0506 0.0079  -0.0033 0.0044  246 PRO A N   
2075 C  CA  A PRO A 244 ? 0.0642 0.0564 0.0418 0.0062  0.0040  -0.0038 246 PRO A CA  
2076 C  CA  B PRO A 244 ? 0.0732 0.0723 0.0380 0.0133  -0.0021 0.0035  246 PRO A CA  
2077 C  C   A PRO A 244 ? 0.0707 0.0478 0.0362 0.0145  -0.0124 -0.0016 246 PRO A C   
2078 C  C   B PRO A 244 ? 0.0707 0.0584 0.0339 0.0160  -0.0189 0.0071  246 PRO A C   
2079 O  O   A PRO A 244 ? 0.0926 0.0522 0.0436 0.0119  -0.0157 -0.0104 246 PRO A O   
2080 O  O   B PRO A 244 ? 0.0898 0.0698 0.0478 0.0037  -0.0237 0.0041  246 PRO A O   
2081 C  CB  A PRO A 244 ? 0.0715 0.0576 0.0724 0.0133  0.0036  -0.0098 246 PRO A CB  
2082 C  CB  B PRO A 244 ? 0.0706 0.0982 0.1056 0.0230  -0.0074 -0.0006 246 PRO A CB  
2083 C  CG  A PRO A 244 ? 0.0636 0.0524 0.0800 0.0060  0.0149  -0.0158 246 PRO A CG  
2084 C  CG  B PRO A 244 ? 0.0738 0.0952 0.1187 0.0328  -0.0100 0.0328  246 PRO A CG  
2085 C  CD  A PRO A 244 ? 0.0478 0.0732 0.0575 0.0218  -0.0113 -0.0141 246 PRO A CD  
2086 C  CD  B PRO A 244 ? 0.0714 0.0891 0.0734 0.0370  -0.0092 0.0008  246 PRO A CD  
2087 N  N   . ALA A 245 ? 0.0871 0.0689 0.0423 0.0089  -0.0015 0.0037  247 ALA A N   
2088 C  CA  . ALA A 245 ? 0.0978 0.0698 0.0285 0.0132  -0.0094 0.0105  247 ALA A CA  
2089 C  C   . ALA A 245 ? 0.0813 0.0829 0.0488 0.0216  -0.0059 0.0017  247 ALA A C   
2090 O  O   . ALA A 245 ? 0.0797 0.0784 0.0662 0.0200  -0.0166 -0.0010 247 ALA A O   
2091 C  CB  . ALA A 245 ? 0.1190 0.1023 0.0636 0.0073  0.0274  0.0168  247 ALA A CB  
2092 N  N   . GLN A 246 ? 0.0793 0.0608 0.0527 -0.0063 -0.0039 0.0104  248 GLN A N   
2093 C  CA  . GLN A 246 ? 0.0603 0.0775 0.0795 0.0032  -0.0156 0.0094  248 GLN A CA  
2094 C  C   . GLN A 246 ? 0.0641 0.0741 0.0827 0.0099  -0.0244 -0.0018 248 GLN A C   
2095 O  O   . GLN A 246 ? 0.0801 0.0806 0.0759 0.0089  -0.0211 0.0128  248 GLN A O   
2096 C  CB  . GLN A 246 ? 0.1066 0.0739 0.0633 -0.0011 -0.0281 0.0093  248 GLN A CB  
2097 C  CG  . GLN A 246 ? 0.0820 0.0910 0.0659 -0.0068 -0.0151 -0.0025 248 GLN A CG  
2098 C  CD  . GLN A 246 ? 0.0827 0.1306 0.0641 -0.0153 -0.0060 -0.0087 248 GLN A CD  
2099 O  OE1 . GLN A 246 ? 0.0980 0.1679 0.1107 -0.0253 -0.0201 -0.0215 248 GLN A OE1 
2100 N  NE2 . GLN A 246 ? 0.1247 0.1169 0.0557 0.0121  0.0066  0.0013  248 GLN A NE2 
2101 N  N   . PRO A 247 ? 0.0812 0.1248 0.0653 0.0306  -0.0330 -0.0100 249 PRO A N   
2102 C  CA  . PRO A 247 ? 0.0812 0.1650 0.0724 0.0494  -0.0066 0.0083  249 PRO A CA  
2103 C  C   . PRO A 247 ? 0.0794 0.0944 0.0469 0.0252  -0.0330 -0.0072 249 PRO A C   
2104 O  O   . PRO A 247 ? 0.0979 0.1116 0.0696 0.0248  -0.0133 0.0240  249 PRO A O   
2105 C  CB  . PRO A 247 ? 0.1071 0.1980 0.1215 0.0690  -0.0585 -0.0281 249 PRO A CB  
2106 C  CG  . PRO A 247 ? 0.1153 0.3267 0.0861 0.0219  -0.0632 -0.0644 249 PRO A CG  
2107 C  CD  . PRO A 247 ? 0.0761 0.2114 0.1146 0.0403  -0.0366 -0.0120 249 PRO A CD  
2108 N  N   . LEU A 248 ? 0.1003 0.1111 0.0556 0.0299  -0.0084 -0.0030 250 LEU A N   
2109 C  CA  . LEU A 248 ? 0.1037 0.1040 0.0575 0.0116  0.0111  -0.0179 250 LEU A CA  
2110 C  C   . LEU A 248 ? 0.0694 0.0951 0.0589 0.0280  -0.0166 -0.0002 250 LEU A C   
2111 O  O   . LEU A 248 ? 0.0856 0.0882 0.0786 0.0335  -0.0400 -0.0016 250 LEU A O   
2112 C  CB  . LEU A 248 ? 0.1463 0.1011 0.0831 0.0013  0.0150  0.0065  250 LEU A CB  
2113 C  CG  . LEU A 248 ? 0.1385 0.1223 0.0820 -0.0129 0.0195  -0.0146 250 LEU A CG  
2114 C  CD1 . LEU A 248 ? 0.1132 0.1819 0.0949 -0.0020 -0.0249 -0.0462 250 LEU A CD1 
2115 C  CD2 . LEU A 248 ? 0.2110 0.1453 0.1744 -0.0439 0.0606  -0.0044 250 LEU A CD2 
2116 N  N   . LYS A 249 ? 0.1002 0.1306 0.0686 0.0323  -0.0455 -0.0086 251 LYS A N   
2117 C  CA  . LYS A 249 ? 0.1005 0.1399 0.0894 0.0359  -0.0483 -0.0100 251 LYS A CA  
2118 C  C   . LYS A 249 ? 0.1014 0.1500 0.1259 0.0268  -0.0406 -0.0223 251 LYS A C   
2119 O  O   . LYS A 249 ? 0.1514 0.2283 0.1172 -0.0017 -0.0049 -0.0022 251 LYS A O   
2120 C  CB  . LYS A 249 ? 0.1377 0.1373 0.1338 -0.0005 -0.0272 -0.0370 251 LYS A CB  
2121 C  CG  . LYS A 249 ? 0.1366 0.1870 0.1951 -0.0258 0.0245  -0.0488 251 LYS A CG  
2122 C  CD  . LYS A 249 ? 0.1467 0.1905 0.2020 -0.0250 0.0150  -0.0249 251 LYS A CD  
2123 C  CE  . LYS A 249 ? 0.1367 0.2329 0.4503 0.0134  0.0846  0.0245  251 LYS A CE  
2124 N  NZ  . LYS A 249 ? 0.1762 0.2322 0.4876 -0.0092 0.0343  0.0622  251 LYS A NZ  
2125 N  N   . ASN A 250 ? 0.1618 0.1528 0.0680 0.0473  -0.0450 -0.0359 252 ASN A N   
2126 C  CA  . ASN A 250 ? 0.1653 0.3189 0.1155 0.0397  -0.0293 -0.0732 252 ASN A CA  
2127 C  C   . ASN A 250 ? 0.1528 0.2159 0.2074 0.0779  -0.0132 -0.0458 252 ASN A C   
2128 O  O   . ASN A 250 ? 0.2412 0.2279 0.2419 0.0384  0.0012  -0.0590 252 ASN A O   
2129 C  CB  . ASN A 250 ? 0.3143 0.3924 0.1701 -0.0854 -0.0290 -0.1141 252 ASN A CB  
2130 C  CG  . ASN A 250 ? 0.3605 0.4158 0.1743 -0.0392 -0.0058 -0.0282 252 ASN A CG  
2131 O  OD1 . ASN A 250 ? 0.5262 0.5427 0.2189 -0.0548 0.0614  0.0889  252 ASN A OD1 
2132 N  ND2 . ASN A 250 ? 0.2920 0.4429 0.3179 -0.1088 -0.0528 -0.0362 252 ASN A ND2 
2133 N  N   . ARG A 251 ? 0.1235 0.2913 0.0743 0.0253  0.0008  -0.0022 253 ARG A N   
2134 C  CA  . ARG A 251 ? 0.0988 0.1471 0.0513 0.0031  0.0130  -0.0124 253 ARG A CA  
2135 C  C   . ARG A 251 ? 0.1208 0.1063 0.0786 0.0125  0.0367  -0.0286 253 ARG A C   
2136 O  O   . ARG A 251 ? 0.2189 0.1453 0.2698 0.0752  0.1329  0.0482  253 ARG A O   
2137 C  CB  . ARG A 251 ? 0.1118 0.0847 0.0433 0.0164  0.0000  0.0024  253 ARG A CB  
2138 C  CG  . ARG A 251 ? 0.1471 0.0847 0.0181 -0.0021 -0.0152 -0.0077 253 ARG A CG  
2139 C  CD  . ARG A 251 ? 0.1107 0.0581 0.0206 0.0248  -0.0051 0.0016  253 ARG A CD  
2140 N  NE  . ARG A 251 ? 0.0803 0.0641 0.0388 0.0164  -0.0138 -0.0021 253 ARG A NE  
2141 C  CZ  . ARG A 251 ? 0.0373 0.0775 0.0327 0.0096  -0.0131 0.0033  253 ARG A CZ  
2142 N  NH1 . ARG A 251 ? 0.0364 0.0758 0.0522 -0.0044 -0.0366 0.0081  253 ARG A NH1 
2143 N  NH2 . ARG A 251 ? 0.0584 0.0703 0.0337 0.0092  -0.0163 -0.0040 253 ARG A NH2 
2144 N  N   . GLN A 252 ? 0.0949 0.1536 0.0715 0.0055  -0.0068 -0.0621 254 GLN A N   
2145 C  CA  . GLN A 252 ? 0.0996 0.1755 0.0765 0.0064  -0.0199 -0.0585 254 GLN A CA  
2146 C  C   . GLN A 252 ? 0.1234 0.1161 0.0882 -0.0132 -0.0383 -0.0210 254 GLN A C   
2147 O  O   . GLN A 252 ? 0.1992 0.1345 0.1381 -0.0122 -0.0751 -0.0059 254 GLN A O   
2148 C  CB  . GLN A 252 ? 0.1726 0.3195 0.0855 -0.0334 0.0212  -0.1198 254 GLN A CB  
2149 C  CG  . GLN A 252 ? 0.3251 0.4198 0.1309 0.0230  0.0653  -0.0595 254 GLN A CG  
2150 C  CD  . GLN A 252 ? 0.4567 0.6742 0.3333 -0.0638 -0.0027 0.2096  254 GLN A CD  
2151 O  OE1 . GLN A 252 ? 0.4818 0.7868 0.4310 0.2848  0.1468  -0.1190 254 GLN A OE1 
2152 N  NE2 . GLN A 252 ? 0.4656 0.5316 0.3551 -0.0556 0.1794  0.0475  254 GLN A NE2 
2153 N  N   . ILE A 253 ? 0.1071 0.0961 0.0598 -0.0047 -0.0193 -0.0025 255 ILE A N   
2154 C  CA  . ILE A 253 ? 0.0907 0.0952 0.0364 0.0146  0.0017  -0.0110 255 ILE A CA  
2155 C  C   . ILE A 253 ? 0.0926 0.0653 0.0644 0.0204  0.0211  0.0094  255 ILE A C   
2156 O  O   . ILE A 253 ? 0.1241 0.1097 0.0739 0.0266  0.0222  0.0353  255 ILE A O   
2157 C  CB  . ILE A 253 ? 0.1099 0.0917 0.0480 0.0266  -0.0025 -0.0130 255 ILE A CB  
2158 C  CG1 . ILE A 253 ? 0.1068 0.0747 0.1020 0.0533  0.0070  -0.0160 255 ILE A CG1 
2159 C  CG2 . ILE A 253 ? 0.1217 0.1220 0.0677 0.0348  -0.0175 -0.0072 255 ILE A CG2 
2160 C  CD1 . ILE A 253 ? 0.1162 0.0855 0.1076 0.0008  0.0154  -0.0394 255 ILE A CD1 
2161 N  N   . LYS A 254 ? 0.0741 0.0905 0.0741 0.0139  0.0043  0.0120  256 LYS A N   
2162 C  CA  . LYS A 254 ? 0.0706 0.1058 0.0531 0.0139  -0.0035 -0.0098 256 LYS A CA  
2163 C  C   . LYS A 254 ? 0.0576 0.1102 0.0355 0.0049  0.0109  0.0115  256 LYS A C   
2164 O  O   . LYS A 254 ? 0.1313 0.1424 0.0310 -0.0474 0.0084  0.0054  256 LYS A O   
2165 C  CB  . LYS A 254 ? 0.1005 0.1240 0.0828 0.0396  0.0053  -0.0013 256 LYS A CB  
2166 C  CG  . LYS A 254 ? 0.1492 0.2150 0.1132 -0.0160 0.0239  -0.0411 256 LYS A CG  
2167 C  CD  . LYS A 254 ? 0.3482 0.3837 0.1664 0.0110  -0.0278 0.0326  256 LYS A CD  
2168 N  N   . ALA A 255 ? 0.0829 0.1071 0.0480 -0.0111 0.0322  0.0032  257 ALA A N   
2169 C  CA  . ALA A 255 ? 0.0943 0.1298 0.0571 -0.0095 0.0066  0.0066  257 ALA A CA  
2170 C  C   . ALA A 255 ? 0.0891 0.1066 0.0488 -0.0205 0.0196  -0.0209 257 ALA A C   
2171 O  O   . ALA A 255 ? 0.1089 0.1442 0.0504 -0.0013 0.0275  -0.0227 257 ALA A O   
2172 C  CB  . ALA A 255 ? 0.1187 0.1320 0.1005 -0.0215 0.0230  0.0106  257 ALA A CB  
2173 N  N   . SER A 256 ? 0.0838 0.1334 0.0768 -0.0203 0.0025  0.0004  258 SER A N   
2174 C  CA  . SER A 256 ? 0.0881 0.1647 0.0901 -0.0132 0.0150  -0.0039 258 SER A CA  
2175 C  C   . SER A 256 ? 0.1106 0.1750 0.0917 -0.0255 0.0439  -0.0102 258 SER A C   
2176 O  O   . SER A 256 ? 0.1194 0.3338 0.1726 0.0185  0.0510  -0.0100 258 SER A O   
2177 C  CB  . SER A 256 ? 0.1442 0.0989 0.0897 -0.0079 0.0030  0.0031  258 SER A CB  
2178 O  OG  . SER A 256 ? 0.0960 0.1324 0.0971 -0.0066 0.0188  -0.0149 258 SER A OG  
2179 N  N   . PHE A 257 ? 0.1229 0.1808 0.1180 -0.0518 0.0412  -0.0190 259 PHE A N   
2180 C  CA  . PHE A 257 ? 0.1170 0.2128 0.1298 -0.0721 0.0145  0.0149  259 PHE A CA  
2181 C  C   . PHE A 257 ? 0.2265 0.3655 0.1144 -0.0735 0.0568  0.0879  259 PHE A C   
2182 O  O   . PHE A 257 ? 0.3129 0.2125 0.1787 -0.0862 -0.0233 0.0917  259 PHE A O   
2183 C  CB  . PHE A 257 ? 0.1145 0.2182 0.1538 -0.0775 0.0363  -0.0190 259 PHE A CB  
2184 C  CG  . PHE A 257 ? 0.1204 0.1683 0.1668 -0.0525 0.0033  0.0388  259 PHE A CG  
2185 C  CD1 . PHE A 257 ? 0.1013 0.1553 0.0907 -0.0433 -0.0041 -0.0003 259 PHE A CD1 
2186 C  CD2 . PHE A 257 ? 0.2354 0.1564 0.2415 -0.0179 0.0179  0.0092  259 PHE A CD2 
2187 C  CE1 . PHE A 257 ? 0.1298 0.1697 0.1571 -0.0216 0.0157  -0.0075 259 PHE A CE1 
2188 C  CE2 . PHE A 257 ? 0.1586 0.1905 0.3106 -0.0576 -0.0552 0.0656  259 PHE A CE2 
2189 C  CZ  . PHE A 257 ? 0.2267 0.1733 0.2038 -0.0424 0.0165  -0.0155 259 PHE A CZ  
2190 N  N   . LYS A 258 ? 0.3111 0.4295 0.2117 -0.1339 0.0854  0.1182  260 LYS A N   
2191 C  CA  . LYS A 258 ? 0.4378 0.6293 0.2794 0.0047  0.1463  0.2980  260 LYS A CA  
2192 C  C   . LYS A 258 ? 0.5466 0.6893 0.3727 -0.0679 0.1228  0.1826  260 LYS A C   
2193 O  O   . LYS A 258 ? 0.3653 0.7935 0.8088 -0.2276 -0.0691 0.3389  260 LYS A O   
2194 C  CB  . LYS A 258 ? 0.5333 0.6457 0.3894 0.0679  0.0502  0.0851  260 LYS A CB  
2195 C  CG  . LYS A 258 ? 1.2388 0.3547 0.5713 -0.5021 0.3098  0.1384  260 LYS A CG  
2196 O  OXT . LYS A 258 ? 0.4709 1.0616 0.6966 -0.0107 0.4446  0.2198  260 LYS A OXT 
2197 ZN ZN  . ZN  B .   ? 0.0715 0.0400 0.0258 -0.0109 -0.0088 -0.0012 301 ZN  A ZN  
2198 NA NA  . NA  C .   ? 0.5087 0.2328 0.2561 -0.0688 0.0029  -0.0322 302 NA  A NA  
2199 NA NA  . NA  D .   ? 0.4397 0.3983 0.4756 0.0279  0.0575  0.0916  303 NA  A NA  
2200 NA NA  . NA  E .   ? 0.6324 0.3629 0.6603 -0.0110 -0.0284 0.1041  304 NA  A NA  
2201 NA NA  . NA  F .   ? 0.5324 0.4878 0.5224 -0.0027 -0.0384 0.0013  305 NA  A NA  
2202 N  N1  A BCN G .   ? 0.2702 0.2689 0.2480 -0.0592 -0.0183 -0.0013 306 BCN A N1  
2203 N  N1  B BCN G .   ? 0.2949 0.2887 0.2709 -0.0318 -0.0197 -0.0074 306 BCN A N1  
2204 C  C1  A BCN G .   ? 0.2072 0.2992 0.2526 -0.0853 -0.0309 0.0649  306 BCN A C1  
2205 C  C1  B BCN G .   ? 0.2060 0.2999 0.2525 -0.0840 -0.0358 0.0631  306 BCN A C1  
2206 C  C2  A BCN G .   ? 0.2352 0.2653 0.2451 -0.0384 0.0282  0.0421  306 BCN A C2  
2207 C  C2  B BCN G .   ? 0.2491 0.2728 0.2498 -0.0342 0.0259  0.0430  306 BCN A C2  
2208 O  O21 A BCN G .   ? 0.4337 0.3628 0.3071 -0.1664 -0.0937 0.1632  306 BCN A O21 
2209 O  O21 B BCN G .   ? 0.4234 0.3823 0.3165 -0.1694 -0.0983 0.1489  306 BCN A O21 
2210 O  O22 A BCN G .   ? 0.2940 0.4014 0.2956 -0.1338 -0.0110 0.0652  306 BCN A O22 
2211 O  O22 B BCN G .   ? 0.2953 0.4009 0.2954 -0.1355 -0.0091 0.0621  306 BCN A O22 
2212 C  C3  A BCN G .   ? 0.2041 0.1255 0.1597 -0.0719 0.0029  0.0658  306 BCN A C3  
2213 C  C3  B BCN G .   ? 0.2346 0.1502 0.1798 -0.0884 -0.0359 0.0592  306 BCN A C3  
2214 C  C4  A BCN G .   ? 0.4426 0.5737 0.2243 -0.2247 -0.1603 -0.0648 306 BCN A C4  
2215 C  C4  B BCN G .   ? 0.4967 0.6646 0.3678 -0.0514 0.1029  0.1075  306 BCN A C4  
2216 O  O4  A BCN G .   ? 0.3823 0.2822 0.1912 -0.3078 0.0074  0.0600  306 BCN A O4  
2217 O  O4  B BCN G .   ? 0.3455 0.3289 0.1023 -0.2958 -0.0293 0.1032  306 BCN A O4  
2218 C  C5  A BCN G .   ? 0.2187 0.2049 0.2256 -0.0647 0.0002  0.0505  306 BCN A C5  
2219 C  C5  B BCN G .   ? 0.2139 0.1988 0.2261 -0.0598 0.0030  0.0458  306 BCN A C5  
2220 C  C6  A BCN G .   ? 0.6110 0.4252 0.4051 0.0373  0.1267  -0.2325 306 BCN A C6  
2221 C  C6  B BCN G .   ? 0.6480 0.4225 0.4318 0.0221  0.1248  -0.2193 306 BCN A C6  
2222 O  O6  A BCN G .   ? 0.2621 0.2311 0.3361 -0.0281 0.0564  -0.0301 306 BCN A O6  
2223 O  O6  B BCN G .   ? 0.2676 0.2455 0.3492 -0.0324 0.0436  -0.0297 306 BCN A O6  
2224 S  S   . DMS H .   ? 0.2797 0.4433 0.4575 0.0319  0.0617  0.0644  307 DMS A S   
2225 O  O   . DMS H .   ? 0.6064 0.5450 1.0555 0.4114  0.4794  -0.0847 307 DMS A O   
2226 C  C1  . DMS H .   ? 0.1449 0.3009 0.6702 -0.0571 -0.0594 0.2960  307 DMS A C1  
2227 C  C2  . DMS H .   ? 0.2010 0.2080 0.3679 0.0967  0.0664  -0.0037 307 DMS A C2  
2228 O  O18 . 84Z I .   ? 0.2017 0.0705 0.0644 0.0013  -0.0049 0.0111  308 84Z A O18 
2229 S  S16 . 84Z I .   ? 0.1398 0.0627 0.0743 -0.0034 -0.0031 0.0127  308 84Z A S16 
2230 O  O17 . 84Z I .   ? 0.1313 0.0761 0.1050 -0.0001 -0.0015 0.0129  308 84Z A O17 
2231 C  C19 . 84Z I .   ? 0.1385 0.0249 0.1434 -0.0024 0.0036  0.0290  308 84Z A C19 
2232 C  C24 . 84Z I .   ? 0.1526 0.1023 0.1862 -0.0345 0.0421  0.0573  308 84Z A C24 
2233 C  C23 . 84Z I .   ? 0.1635 0.1242 0.2480 -0.0193 0.0116  0.0480  308 84Z A C23 
2234 C  C22 . 84Z I .   ? 0.1683 0.1291 0.2303 -0.0407 -0.0463 0.0849  308 84Z A C22 
2235 C  C21 . 84Z I .   ? 0.1773 0.1050 0.1967 -0.0236 -0.0370 0.0431  308 84Z A C21 
2236 C  C20 . 84Z I .   ? 0.1679 0.0489 0.1665 -0.0055 -0.0149 0.0070  308 84Z A C20 
2237 C  C3  . 84Z I .   ? 0.1098 0.0478 0.0601 -0.0109 -0.0161 0.0049  308 84Z A C3  
2238 C  C2  . 84Z I .   ? 0.0973 0.0547 0.0768 -0.0100 -0.0175 -0.0055 308 84Z A C2  
2239 C  C4  . 84Z I .   ? 0.1004 0.0423 0.0651 -0.0175 -0.0013 0.0051  308 84Z A C4  
2240 C  C12 . 84Z I .   ? 0.1273 0.0496 0.0777 -0.0077 0.0074  0.0173  308 84Z A C12 
2241 O  O14 . 84Z I .   ? 0.1283 0.0761 0.0950 -0.0057 0.0339  0.0153  308 84Z A O14 
2242 C  C15 . 84Z I .   ? 0.1880 0.1536 0.0872 -0.0158 0.0719  0.0303  308 84Z A C15 
2243 O  O13 . 84Z I .   ? 0.1370 0.0777 0.0804 -0.0106 0.0135  -0.0052 308 84Z A O13 
2244 C  C5  . 84Z I .   ? 0.1046 0.0486 0.0549 -0.0188 -0.0105 0.0055  308 84Z A C5  
2245 C  C6  . 84Z I .   ? 0.0652 0.0399 0.0673 -0.0118 -0.0194 0.0035  308 84Z A C6  
2246 C  C1  . 84Z I .   ? 0.0888 0.0554 0.0549 0.0111  -0.0128 -0.0084 308 84Z A C1  
2247 CL CL1 . 84Z I .   ? 0.0812 0.0513 0.0917 0.0026  -0.0021 -0.0212 308 84Z A CL1 
2248 S  S7  . 84Z I .   ? 0.0697 0.0400 0.0417 -0.0082 -0.0114 -0.0097 308 84Z A S7  
2249 O  O8  . 84Z I .   ? 0.0625 0.0445 0.0467 -0.0139 -0.0036 -0.0150 308 84Z A O8  
2250 O  O9  . 84Z I .   ? 0.0664 0.0531 0.0369 -0.0004 -0.0129 -0.0032 308 84Z A O9  
2251 N  N10 . 84Z I .   ? 0.0506 0.0346 0.0425 -0.0108 -0.0118 -0.0121 308 84Z A N10 
2252 O  O   . HOH J .   ? 0.2910 0.1643 0.2591 -0.0739 -0.0767 0.0258  401 HOH A O   
2253 O  O   . HOH J .   ? 0.1628 0.2242 0.3664 -0.0177 -0.0726 0.0328  402 HOH A O   
2254 O  O   . HOH J .   ? 0.3782 0.2937 0.3865 -0.0072 -0.0613 0.0189  403 HOH A O   
2255 O  O   . HOH J .   ? 0.2498 0.6276 0.2062 0.0352  0.0075  -0.0718 404 HOH A O   
2256 O  O   . HOH J .   ? 0.4103 0.4160 0.2006 -0.0345 0.0900  -0.0436 405 HOH A O   
2257 O  O   . HOH J .   ? 0.4352 0.1844 0.5056 -0.0609 0.1385  0.0135  406 HOH A O   
2258 O  O   . HOH J .   ? 0.4311 0.2752 0.4806 -0.0794 -0.3339 -0.0478 407 HOH A O   
2259 O  O   . HOH J .   ? 0.5583 0.4641 0.3667 -0.0785 0.0242  0.1257  408 HOH A O   
2260 O  O   . HOH J .   ? 0.7336 0.2437 0.1714 -0.2132 0.1092  -0.0577 409 HOH A O   
2261 O  O   . HOH J .   ? 0.7108 0.5984 0.3855 -0.1038 -0.0403 -0.0794 410 HOH A O   
2262 O  O   . HOH J .   ? 0.0641 0.0626 0.0472 -0.0041 0.0060  -0.0072 411 HOH A O   
2263 O  O   . HOH J .   ? 0.4697 0.2727 0.2776 -0.0915 0.1187  -0.1717 412 HOH A O   
2264 O  O   . HOH J .   ? 0.3800 0.2697 0.0670 0.0251  0.0013  0.0283  413 HOH A O   
2265 O  O   . HOH J .   ? 0.2872 0.2225 0.6154 -0.0073 0.0089  -0.1861 414 HOH A O   
2266 O  O   . HOH J .   ? 0.3017 0.4500 0.5271 0.0873  0.1436  -0.1056 415 HOH A O   
2267 O  O   . HOH J .   ? 0.3058 0.4137 0.8559 0.0436  0.0370  -0.0935 416 HOH A O   
2268 O  O   . HOH J .   ? 0.3085 0.4462 0.1963 -0.0886 -0.0158 0.0867  417 HOH A O   
2269 O  O   . HOH J .   ? 0.3993 0.3146 0.2643 0.0265  -0.0509 -0.0351 418 HOH A O   
2270 O  O   . HOH J .   ? 0.3309 0.2301 0.2568 0.0241  0.0334  0.0618  419 HOH A O   
2271 O  O   . HOH J .   ? 0.1934 0.1429 0.2542 0.0055  -0.0092 -0.0380 420 HOH A O   
2272 O  O   . HOH J .   ? 0.3258 0.4074 0.5438 0.0019  0.2538  0.1206  421 HOH A O   
2273 O  O   . HOH J .   ? 0.5845 0.4669 0.2232 0.2388  -0.0342 -0.0364 422 HOH A O   
2274 O  O   . HOH J .   ? 0.2473 0.5880 0.4821 0.0140  0.0873  0.3500  423 HOH A O   
2275 O  O   . HOH J .   ? 0.4745 0.2332 0.3040 -0.0832 0.0433  -0.0766 424 HOH A O   
2276 O  O   . HOH J .   ? 0.1363 0.3319 0.4562 -0.0190 -0.0076 0.0803  425 HOH A O   
2277 O  O   . HOH J .   ? 0.2275 0.2552 0.3023 -0.0681 0.0794  -0.1266 426 HOH A O   
2278 O  O   . HOH J .   ? 0.4078 0.3341 0.4637 0.0054  -0.2825 0.1096  427 HOH A O   
2279 O  O   . HOH J .   ? 0.2696 0.4126 0.1909 0.1685  0.0061  -0.1078 428 HOH A O   
2280 O  O   . HOH J .   ? 0.2557 0.3700 0.3865 -0.0651 -0.0819 0.0027  429 HOH A O   
2281 O  O   . HOH J .   ? 0.1808 0.3641 0.3265 0.0070  -0.0885 -0.0078 430 HOH A O   
2282 O  O   . HOH J .   ? 0.4231 0.1905 0.4965 -0.2032 -0.0175 0.0891  431 HOH A O   
2283 O  O   . HOH J .   ? 0.1614 0.0927 0.0068 -0.0335 -0.0060 -0.0036 432 HOH A O   
2284 O  O   . HOH J .   ? 0.1787 0.2109 0.1618 0.0168  -0.0429 0.0097  433 HOH A O   
2285 O  O   . HOH J .   ? 0.2515 0.2024 0.2301 -0.0089 -0.0457 0.0577  434 HOH A O   
2286 O  O   . HOH J .   ? 0.3016 0.3209 0.8414 0.0474  -0.2791 -0.0930 435 HOH A O   
2287 O  O   . HOH J .   ? 0.2423 0.4490 0.4588 0.0396  0.0064  0.1773  436 HOH A O   
2288 O  O   . HOH J .   ? 0.3180 0.7513 0.7047 0.1358  0.1646  0.2929  437 HOH A O   
2289 O  O   . HOH J .   ? 0.3844 0.4620 0.1801 -0.1371 0.0346  0.0498  438 HOH A O   
2290 O  O   . HOH J .   ? 0.2483 0.2473 0.3755 -0.0399 -0.0914 0.2072  439 HOH A O   
2291 O  O   . HOH J .   ? 0.3792 0.4412 0.2878 -0.1362 -0.0495 0.0545  440 HOH A O   
2292 O  O   . HOH J .   ? 0.1694 0.1403 0.1783 0.0134  0.0087  0.0411  441 HOH A O   
2293 O  O   . HOH J .   ? 0.3034 0.6779 0.1238 -0.0556 0.0535  -0.0722 442 HOH A O   
2294 O  O   . HOH J .   ? 0.4077 0.3392 0.5868 -0.0471 0.1103  -0.0560 443 HOH A O   
2295 O  O   . HOH J .   ? 0.1402 0.6681 0.3758 0.0682  -0.0469 -0.3186 444 HOH A O   
2296 O  O   . HOH J .   ? 0.2725 0.2020 0.3042 -0.0688 0.1433  -0.0911 445 HOH A O   
2297 O  O   . HOH J .   ? 0.1719 0.6545 0.5248 -0.0194 0.1179  0.1796  446 HOH A O   
2298 O  O   . HOH J .   ? 0.4459 0.2487 0.6322 -0.1276 0.0657  0.0665  447 HOH A O   
2299 O  O   . HOH J .   ? 0.4331 0.1908 0.3197 0.0817  0.0316  0.0330  448 HOH A O   
2300 O  O   . HOH J .   ? 0.2882 0.4919 0.4835 -0.0567 0.0783  0.0846  449 HOH A O   
2301 O  O   . HOH J .   ? 0.2311 0.2206 0.2363 0.0372  -0.0205 -0.0493 450 HOH A O   
2302 O  O   . HOH J .   ? 0.3976 0.2218 0.7747 0.0189  -0.3327 -0.0358 451 HOH A O   
2303 O  O   . HOH J .   ? 0.3720 0.4447 0.2956 0.1285  0.1518  -0.0160 452 HOH A O   
2304 O  O   . HOH J .   ? 0.1744 0.1460 0.1877 -0.0124 -0.1328 0.0005  453 HOH A O   
2305 O  O   . HOH J .   ? 0.1794 0.2731 0.1707 -0.0350 0.0370  -0.0079 454 HOH A O   
2306 O  O   . HOH J .   ? 0.1102 0.0487 0.0686 -0.0203 -0.0069 -0.0034 455 HOH A O   
2307 O  O   . HOH J .   ? 0.2092 0.2865 0.3235 0.0269  -0.1240 -0.1996 456 HOH A O   
2308 O  O   . HOH J .   ? 0.2382 0.1510 0.1410 -0.0615 -0.0346 -0.0049 457 HOH A O   
2309 O  O   . HOH J .   ? 0.4031 0.4281 0.2178 0.1335  -0.0120 0.1104  458 HOH A O   
2310 O  O   . HOH J .   ? 0.2615 0.6602 0.2261 -0.0106 -0.0177 -0.0023 459 HOH A O   
2311 O  O   . HOH J .   ? 0.3833 0.1898 0.1658 -0.1191 0.1072  -0.0732 460 HOH A O   
2312 O  O   . HOH J .   ? 0.6052 0.1858 0.1162 0.0153  -0.0192 -0.0031 461 HOH A O   
2313 O  O   . HOH J .   ? 0.3527 0.1284 0.1349 0.0565  -0.1215 0.0137  462 HOH A O   
2314 O  O   . HOH J .   ? 0.3313 0.1683 0.0891 -0.0307 -0.0716 -0.0009 463 HOH A O   
2315 O  O   . HOH J .   ? 0.2739 0.2433 0.2550 -0.1055 -0.0515 -0.0557 464 HOH A O   
2316 O  O   . HOH J .   ? 0.3185 0.2271 0.1927 -0.0543 -0.0864 -0.0111 465 HOH A O   
2317 O  O   . HOH J .   ? 0.3177 0.2983 0.1600 0.0798  -0.0021 -0.1036 466 HOH A O   
2318 O  O   . HOH J .   ? 0.2569 0.1255 0.1080 -0.0373 0.0550  0.0118  467 HOH A O   
2319 O  O   . HOH J .   ? 0.3143 0.4064 0.3976 -0.1100 -0.1367 0.0783  468 HOH A O   
2320 O  O   . HOH J .   ? 0.0873 0.0770 0.0716 -0.0176 0.0026  -0.0011 469 HOH A O   
2321 O  O   . HOH J .   ? 0.1945 0.2412 0.2451 0.0381  0.0240  0.0391  470 HOH A O   
2322 O  O   . HOH J .   ? 0.2412 0.2326 0.2812 -0.0241 0.1221  0.0238  471 HOH A O   
2323 O  O   . HOH J .   ? 0.5299 0.2066 0.1126 -0.1391 -0.0195 0.0534  472 HOH A O   
2324 O  O   . HOH J .   ? 0.2055 0.2174 0.2013 -0.0127 -0.0199 0.0242  473 HOH A O   
2325 O  O   . HOH J .   ? 0.2293 0.5309 0.3966 -0.0796 -0.0368 -0.0530 474 HOH A O   
2326 O  O   . HOH J .   ? 0.2652 0.3812 0.2222 -0.0163 -0.0425 0.0017  475 HOH A O   
2327 O  O   . HOH J .   ? 0.4082 0.3703 0.3146 -0.1283 -0.0750 -0.0197 476 HOH A O   
2328 O  O   . HOH J .   ? 0.2020 0.1435 0.1198 0.0298  0.0566  -0.0248 477 HOH A O   
2329 O  O   . HOH J .   ? 0.0632 0.0632 0.0694 -0.0085 0.0040  0.0042  478 HOH A O   
2330 O  O   . HOH J .   ? 0.2141 0.2229 0.2297 0.0227  -0.0302 0.0757  479 HOH A O   
2331 O  O   . HOH J .   ? 0.6043 0.4962 0.4859 -0.1089 -0.1089 0.0243  480 HOH A O   
2332 O  O   . HOH J .   ? 0.3753 0.3362 0.3869 0.0677  -0.0838 -0.2242 481 HOH A O   
2333 O  O   . HOH J .   ? 0.2722 0.3005 0.6492 0.0947  0.1824  0.0134  482 HOH A O   
2334 O  O   . HOH J .   ? 0.1492 0.2581 0.3842 0.0489  0.0026  -0.0104 483 HOH A O   
2335 O  O   . HOH J .   ? 0.2231 0.1362 0.1586 0.0087  -0.0526 0.0000  484 HOH A O   
2336 O  O   . HOH J .   ? 0.2582 0.1877 0.2182 -0.0091 0.0047  0.0716  485 HOH A O   
2337 O  O   . HOH J .   ? 0.6054 0.3375 0.4207 0.1569  -0.2870 -0.0108 486 HOH A O   
2338 O  O   . HOH J .   ? 0.0802 0.1049 0.0732 0.0096  -0.0294 0.0159  487 HOH A O   
2339 O  O   . HOH J .   ? 0.1221 0.0761 0.0944 -0.0127 -0.0059 0.0168  488 HOH A O   
2340 O  O   . HOH J .   ? 0.3141 0.7227 0.2698 0.1263  -0.0926 -0.0185 489 HOH A O   
2341 O  O   . HOH J .   ? 0.5276 0.4691 0.4072 0.1485  -0.2270 -0.1802 490 HOH A O   
2342 O  O   . HOH J .   ? 0.1855 0.0961 0.1406 -0.0500 -0.0277 -0.0083 491 HOH A O   
2343 O  O   . HOH J .   ? 0.2938 0.2931 0.2860 0.0885  -0.1644 -0.1629 492 HOH A O   
2344 O  O   . HOH J .   ? 0.0979 0.0589 0.0529 0.0086  -0.0122 -0.0104 493 HOH A O   
2345 O  O   . HOH J .   ? 0.2584 0.3001 0.2115 0.0586  0.0589  -0.0829 494 HOH A O   
2346 O  O   . HOH J .   ? 0.3100 0.2364 0.1640 -0.0431 0.0961  -0.0994 495 HOH A O   
2347 O  O   . HOH J .   ? 0.4163 0.3244 0.1733 -0.0972 -0.0296 -0.0229 496 HOH A O   
2348 O  O   . HOH J .   ? 0.0801 0.0897 0.0633 0.0201  0.0073  0.0069  497 HOH A O   
2349 O  O   . HOH J .   ? 0.2839 0.1747 0.2157 -0.0513 0.0148  -0.0369 498 HOH A O   
2350 O  O   . HOH J .   ? 0.1776 0.0926 0.0853 -0.0013 0.0057  -0.0067 499 HOH A O   
2351 O  O   . HOH J .   ? 0.1884 0.2751 0.1520 -0.0266 -0.0069 -0.0795 500 HOH A O   
2352 O  O   . HOH J .   ? 0.4839 0.2907 0.4237 0.0033  -0.0439 -0.0217 501 HOH A O   
2353 O  O   . HOH J .   ? 0.0829 0.1127 0.0792 0.0148  -0.0144 0.0177  502 HOH A O   
2354 O  O   . HOH J .   ? 0.3159 0.1564 0.1981 0.0494  -0.1005 -0.0312 503 HOH A O   
2355 O  O   . HOH J .   ? 0.1773 0.1032 0.2329 -0.0433 -0.0348 0.0664  504 HOH A O   
2356 O  O   . HOH J .   ? 0.0840 0.1280 0.1816 -0.0167 0.0065  0.0176  505 HOH A O   
2357 O  O   . HOH J .   ? 0.5605 0.4885 0.1435 0.0086  0.0362  0.0564  506 HOH A O   
2358 O  O   . HOH J .   ? 0.1172 0.2414 0.2347 0.0149  0.0190  0.0148  507 HOH A O   
2359 O  O   . HOH J .   ? 0.6260 0.2333 0.1076 0.0648  0.0402  0.0855  508 HOH A O   
2360 O  O   . HOH J .   ? 0.2451 0.1878 0.2791 -0.0330 -0.0032 -0.0302 509 HOH A O   
2361 O  O   . HOH J .   ? 0.1664 0.2567 0.1464 0.0144  -0.0820 -0.0218 510 HOH A O   
2362 O  O   . HOH J .   ? 0.5398 0.5533 0.4165 0.0680  -0.2713 -0.0516 511 HOH A O   
2363 O  O   . HOH J .   ? 0.2447 0.3095 0.3477 -0.0768 0.1419  -0.0495 512 HOH A O   
2364 O  O   . HOH J .   ? 0.1880 0.2518 0.1521 -0.0187 -0.0540 -0.0253 513 HOH A O   
2365 O  O   . HOH J .   ? 0.8285 0.2268 0.4983 -0.2599 0.2408  -0.0750 514 HOH A O   
2366 O  O   . HOH J .   ? 0.4185 0.2764 0.3065 0.1138  -0.0595 -0.0886 515 HOH A O   
2367 O  O   . HOH J .   ? 0.6077 0.3078 0.4775 -0.1920 -0.0836 -0.0411 516 HOH A O   
2368 O  O   . HOH J .   ? 0.5633 0.2956 0.3304 -0.0085 0.0111  -0.1395 517 HOH A O   
2369 O  O   . HOH J .   ? 0.2658 0.3624 0.1190 -0.0506 -0.1054 0.0932  518 HOH A O   
2370 O  O   . HOH J .   ? 0.5085 0.4458 0.1737 -0.1826 -0.0050 0.1251  519 HOH A O   
2371 O  O   . HOH J .   ? 0.1528 0.1306 0.1862 -0.0372 -0.0352 -0.0142 520 HOH A O   
2372 O  O   . HOH J .   ? 0.1170 0.1053 0.1076 0.0120  -0.0037 0.0134  521 HOH A O   
2373 O  O   . HOH J .   ? 0.4310 0.4852 0.3240 -0.1198 0.0746  -0.2024 522 HOH A O   
2374 O  O   . HOH J .   ? 0.2656 0.1661 0.1084 0.0176  0.0031  -0.0267 523 HOH A O   
2375 O  O   . HOH J .   ? 0.0673 0.1156 0.1589 -0.0003 -0.0170 -0.0313 524 HOH A O   
2376 O  O   . HOH J .   ? 0.1679 0.1860 0.1216 0.0099  0.0069  -0.0005 525 HOH A O   
2377 O  O   . HOH J .   ? 0.1004 0.1413 0.2437 -0.0341 -0.0499 0.0197  526 HOH A O   
2378 O  O   . HOH J .   ? 0.5450 0.2328 0.1309 0.0917  -0.0293 0.0647  527 HOH A O   
2379 O  O   . HOH J .   ? 0.2229 0.2730 0.1156 -0.0559 0.0143  -0.0124 528 HOH A O   
2380 O  O   . HOH J .   ? 0.3336 0.1471 0.2418 0.1272  -0.0581 0.0100  529 HOH A O   
2381 O  O   . HOH J .   ? 0.3136 0.1646 0.3718 0.0055  -0.0697 -0.0019 530 HOH A O   
2382 O  O   . HOH J .   ? 0.2777 0.1834 0.1046 -0.0052 -0.0743 0.0392  531 HOH A O   
2383 O  O   . HOH J .   ? 0.1712 0.1302 0.1180 -0.0078 -0.0331 0.0071  532 HOH A O   
2384 O  O   . HOH J .   ? 0.2261 0.0759 0.1287 0.0150  0.0093  0.0019  533 HOH A O   
2385 O  O   . HOH J .   ? 0.1120 0.1027 0.1180 0.0286  0.0064  0.0158  534 HOH A O   
2386 O  O   . HOH J .   ? 0.3072 0.3942 0.1288 0.1692  -0.1167 -0.0702 535 HOH A O   
2387 O  O   . HOH J .   ? 0.0506 0.1435 0.1524 0.0000  -0.0040 -0.0233 536 HOH A O   
2388 O  O   . HOH J .   ? 0.3712 0.3096 0.4252 -0.0177 -0.1779 0.0271  537 HOH A O   
2389 O  O   . HOH J .   ? 0.4931 0.3046 0.2477 -0.1161 0.0641  -0.1098 538 HOH A O   
2390 O  O   . HOH J .   ? 0.2566 0.3829 0.2401 -0.1856 -0.0403 -0.0392 539 HOH A O   
2391 O  O   . HOH J .   ? 0.5924 0.4189 0.3129 0.0057  -0.0197 0.0998  540 HOH A O   
2392 O  O   . HOH J .   ? 0.2832 0.2956 0.3397 -0.1982 -0.0455 0.0455  541 HOH A O   
2393 O  O   . HOH J .   ? 0.2902 0.1980 0.2222 0.0549  0.0760  0.0060  542 HOH A O   
2394 O  O   . HOH J .   ? 0.2708 0.2365 0.3098 0.0688  -0.0500 0.0098  543 HOH A O   
2395 O  O   . HOH J .   ? 0.1640 0.1199 0.1155 0.0197  -0.0073 0.0098  544 HOH A O   
2396 O  O   . HOH J .   ? 0.2645 0.1546 0.2265 -0.0114 -0.0198 -0.0228 545 HOH A O   
2397 O  O   . HOH J .   ? 0.2975 0.0646 0.1729 0.0410  -0.0908 -0.0144 546 HOH A O   
2398 O  O   . HOH J .   ? 0.3486 0.3992 0.2024 -0.1236 0.0674  0.1046  547 HOH A O   
2399 O  O   . HOH J .   ? 0.5419 0.2760 0.5750 0.0094  -0.0024 -0.1643 548 HOH A O   
2400 O  O   . HOH J .   ? 0.2354 0.2271 0.1732 -0.0076 0.0309  -0.0441 549 HOH A O   
2401 O  O   . HOH J .   ? 0.2770 0.4181 0.2732 -0.0048 0.0030  0.0329  550 HOH A O   
2402 O  O   . HOH J .   ? 0.1524 0.1888 0.2257 -0.0309 -0.0285 0.0156  551 HOH A O   
2403 O  O   . HOH J .   ? 0.6503 0.2735 0.4333 0.2150  -0.2940 -0.1169 552 HOH A O   
2404 O  O   . HOH J .   ? 0.0803 0.4053 0.2049 0.0100  -0.0211 0.1311  553 HOH A O   
2405 O  O   . HOH J .   ? 0.2893 0.3373 0.4604 -0.0347 0.0612  -0.1133 554 HOH A O   
2406 O  O   . HOH J .   ? 0.6281 0.5041 0.2358 0.1316  -0.0760 -0.1340 555 HOH A O   
2407 O  O   . HOH J .   ? 0.7875 0.1676 0.3741 0.0440  0.3208  0.0827  556 HOH A O   
2408 O  O   . HOH J .   ? 0.1521 0.2194 0.2383 -0.0067 -0.0174 0.0126  557 HOH A O   
2409 O  O   . HOH J .   ? 0.1159 0.2550 0.2340 -0.0348 -0.0130 0.0348  558 HOH A O   
2410 O  O   . HOH J .   ? 0.1410 0.0906 0.1399 -0.0006 0.0270  0.0038  559 HOH A O   
2411 O  O   . HOH J .   ? 0.4365 0.6964 0.2376 -0.4225 -0.0539 -0.0958 560 HOH A O   
2412 O  O   . HOH J .   ? 0.4984 0.4720 0.3065 -0.1918 0.1687  -0.0386 561 HOH A O   
2413 O  O   . HOH J .   ? 0.3677 0.1658 0.3778 -0.0754 0.0284  -0.0954 562 HOH A O   
2414 O  O   . HOH J .   ? 0.3076 0.5113 0.4985 0.1494  0.0858  0.1123  563 HOH A O   
2415 O  O   . HOH J .   ? 0.1524 0.1020 0.1080 -0.0212 -0.0273 0.0093  564 HOH A O   
2416 O  O   . HOH J .   ? 0.2268 0.2067 0.2655 -0.0058 0.0089  -0.0267 565 HOH A O   
2417 O  O   . HOH J .   ? 0.2074 0.1586 0.1305 0.0515  -0.0160 -0.0095 566 HOH A O   
2418 O  O   . HOH J .   ? 0.2300 0.2340 0.3792 0.0052  0.0142  -0.1059 567 HOH A O   
2419 O  O   . HOH J .   ? 0.2658 0.2620 0.2617 -0.0174 0.0000  0.0491  568 HOH A O   
2420 O  O   . HOH J .   ? 0.4426 0.1273 0.1334 -0.0719 -0.0441 -0.0568 569 HOH A O   
2421 O  O   . HOH J .   ? 0.1891 0.1269 0.2796 0.0009  0.0314  -0.0614 570 HOH A O   
2422 O  O   . HOH J .   ? 0.3631 0.2103 0.4503 -0.0335 0.0484  0.0462  571 HOH A O   
2423 O  O   . HOH J .   ? 0.4782 0.3105 0.3432 -0.1766 -0.1893 -0.0186 572 HOH A O   
2424 O  O   . HOH J .   ? 0.3082 0.2742 0.1388 0.1406  -0.0387 0.0205  573 HOH A O   
2425 O  O   . HOH J .   ? 0.2092 0.5147 0.2311 0.0195  -0.0725 0.1168  574 HOH A O   
2426 O  O   . HOH J .   ? 0.1068 0.3182 0.3868 0.0248  -0.0260 0.1351  575 HOH A O   
2427 O  O   . HOH J .   ? 0.2966 0.1884 0.2449 0.0232  0.0917  -0.0938 576 HOH A O   
2428 O  O   . HOH J .   ? 0.1661 0.0944 0.2558 -0.0724 -0.0477 -0.0198 577 HOH A O   
2429 O  O   . HOH J .   ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  578 HOH A O   
2430 O  O   . HOH J .   ? 0.1611 0.2139 0.3568 0.0490  0.0556  0.0730  579 HOH A O   
2431 O  O   . HOH J .   ? 0.4588 0.4954 0.2838 -0.1210 0.1673  -0.0788 580 HOH A O   
2432 O  O   . HOH J .   ? 0.2472 0.5297 0.3497 -0.0995 0.0330  -0.0013 581 HOH A O   
2433 O  O   . HOH J .   ? 0.4445 0.3073 0.1877 -0.1007 -0.0370 0.0139  582 HOH A O   
2434 O  O   . HOH J .   ? 0.2145 0.2073 0.2228 0.0079  -0.0004 -0.0499 583 HOH A O   
2435 O  O   . HOH J .   ? 0.2949 0.1518 0.3407 -0.0065 0.1333  0.0099  584 HOH A O   
2436 O  O   . HOH J .   ? 0.2964 0.1549 0.2390 0.0318  -0.0422 -0.0046 585 HOH A O   
2437 O  O   . HOH J .   ? 0.3820 0.3899 0.1327 0.0541  -0.0325 0.0385  586 HOH A O   
2438 O  O   . HOH J .   ? 0.3615 0.2128 0.1561 -0.0704 -0.0942 -0.0143 587 HOH A O   
2439 O  O   . HOH J .   ? 0.1456 0.3041 0.2304 0.1218  -0.0952 -0.0882 588 HOH A O   
2440 O  O   . HOH J .   ? 0.3991 0.2400 0.2218 0.0413  -0.0162 0.0983  589 HOH A O   
2441 O  O   . HOH J .   ? 0.4848 0.3093 0.1366 -0.0881 -0.0047 -0.0697 590 HOH A O   
2442 O  O   . HOH J .   ? 0.3459 0.5599 0.4925 -0.0263 0.0616  0.2884  591 HOH A O   
2443 O  O   . HOH J .   ? 0.5251 0.5946 0.2419 0.0293  0.0323  -0.2665 592 HOH A O   
2444 O  O   . HOH J .   ? 0.2319 0.1224 0.1636 -0.0024 0.0323  0.0812  593 HOH A O   
2445 O  O   . HOH J .   ? 0.6380 0.3683 0.1859 0.1726  -0.1926 -0.0668 594 HOH A O   
2446 O  O   . HOH J .   ? 0.1526 0.1460 0.2419 -0.0131 -0.0121 -0.0299 595 HOH A O   
2447 O  O   . HOH J .   ? 0.2929 0.3387 0.8277 0.0982  0.0025  0.0785  596 HOH A O   
2448 O  O   . HOH J .   ? 0.7083 0.2430 0.3418 0.1670  0.0880  -0.0608 597 HOH A O   
2449 O  O   . HOH J .   ? 0.4031 0.2036 0.4863 -0.0385 -0.1986 -0.0859 598 HOH A O   
2450 O  O   . HOH J .   ? 0.1021 0.1931 0.0784 -0.0080 -0.0474 0.0558  599 HOH A O   
2451 O  O   . HOH J .   ? 0.3274 0.1729 0.2010 0.1098  -0.1201 -0.0359 600 HOH A O   
2452 O  O   . HOH J .   ? 0.3332 0.1360 0.2546 0.0763  0.0469  0.0992  601 HOH A O   
2453 O  O   . HOH J .   ? 0.3547 0.8663 0.5796 0.1132  0.0668  0.4149  602 HOH A O   
2454 O  O   . HOH J .   ? 0.5994 0.2782 0.2142 -0.1000 0.0841  -0.0543 603 HOH A O   
2455 O  O   . HOH J .   ? 0.2225 0.1525 0.1765 0.0069  -0.0412 -0.0575 604 HOH A O   
2456 O  O   . HOH J .   ? 0.2737 0.2293 0.5723 -0.1113 0.0257  0.0591  605 HOH A O   
2457 O  O   . HOH J .   ? 0.5655 0.2046 0.5358 -0.0566 -0.2545 0.0417  606 HOH A O   
2458 O  O   . HOH J .   ? 0.4538 0.2347 0.1507 0.1435  0.0403  0.0198  607 HOH A O   
2459 O  O   . HOH J .   ? 0.1539 0.8102 0.2249 0.0617  0.0068  0.0478  608 HOH A O   
2460 O  O   . HOH J .   ? 0.3161 0.2010 0.3415 0.0771  0.0060  -0.0249 609 HOH A O   
2461 O  O   . HOH J .   ? 0.2157 0.1482 0.1302 0.0549  -0.0265 0.0398  610 HOH A O   
2462 O  O   . HOH J .   ? 0.0910 0.0493 0.0964 0.0036  -0.0100 0.0003  611 HOH A O   
2463 O  O   . HOH J .   ? 0.4593 0.5750 0.2979 0.2426  0.0655  -0.0635 612 HOH A O   
2464 O  O   . HOH J .   ? 0.3346 0.3952 0.4100 -0.0424 -0.0967 0.0456  613 HOH A O   
2465 O  O   . HOH J .   ? 0.2196 0.1593 0.1646 0.0251  0.0082  -0.0303 614 HOH A O   
2466 O  O   . HOH J .   ? 0.3265 0.3472 0.2764 -0.0587 -0.0819 0.1430  615 HOH A O   
2467 O  O   . HOH J .   ? 0.8181 0.2703 0.3274 -0.2350 -0.0496 0.0346  616 HOH A O   
2468 O  O   . HOH J .   ? 0.4826 0.2317 0.1927 -0.0170 0.1010  0.1036  617 HOH A O   
2469 O  O   . HOH J .   ? 0.2441 0.1495 0.2430 0.0573  0.0585  0.0403  618 HOH A O   
2470 O  O   . HOH J .   ? 0.4623 0.6225 0.3377 0.0650  0.0336  0.0923  619 HOH A O   
2471 O  O   . HOH J .   ? 0.2386 0.1650 0.3655 0.0788  0.0807  0.0826  620 HOH A O   
2472 O  O   . HOH J .   ? 0.1912 0.0519 0.1625 0.0222  -0.0084 -0.0129 621 HOH A O   
2473 O  O   . HOH J .   ? 0.4215 0.4253 0.1118 -0.0708 0.0373  0.0889  622 HOH A O   
2474 O  O   . HOH J .   ? 0.1478 0.1895 0.0873 0.0051  -0.0026 -0.0148 623 HOH A O   
2475 O  O   . HOH J .   ? 0.4712 0.2960 0.0970 0.2017  -0.0562 0.0038  624 HOH A O   
2476 O  O   . HOH J .   ? 0.2576 0.1916 0.3747 0.0411  0.0827  0.0805  625 HOH A O   
2477 O  O   . HOH J .   ? 0.0853 0.1411 0.2358 -0.0172 0.0000  -0.0009 626 HOH A O   
2478 O  O   . HOH J .   ? 0.4026 0.5620 0.3188 0.1129  -0.1025 0.1928  627 HOH A O   
2479 O  O   . HOH J .   ? 0.2814 0.2694 0.4038 -0.0440 -0.0454 -0.0335 628 HOH A O   
2480 O  O   . HOH J .   ? 0.3963 0.3820 0.3193 0.0027  -0.1670 -0.0847 629 HOH A O   
2481 O  O   . HOH J .   ? 0.2656 0.1941 0.1733 -0.0873 -0.0395 0.0564  630 HOH A O   
2482 O  O   . HOH J .   ? 0.3555 0.1811 0.4773 -0.0877 -0.0041 0.1199  631 HOH A O   
2483 O  O   . HOH J .   ? 0.3600 0.4458 0.2135 0.2298  0.0064  0.0454  632 HOH A O   
2484 O  O   . HOH J .   ? 0.1327 0.5898 0.5098 -0.0710 0.0340  0.2683  633 HOH A O   
2485 O  O   . HOH J .   ? 0.3433 0.2787 1.2061 -0.2639 0.2953  0.0171  634 HOH A O   
2486 O  O   . HOH J .   ? 0.1665 0.1737 0.3283 0.0776  -0.0176 -0.0049 635 HOH A O   
2487 O  O   . HOH J .   ? 0.4565 0.2632 0.5826 0.0626  0.1211  0.1197  636 HOH A O   
2488 O  O   . HOH J .   ? 0.2752 0.9265 0.3912 0.0334  -0.0019 -0.0930 637 HOH A O   
2489 O  O   . HOH J .   ? 0.4496 0.4906 0.5123 0.4522  -0.2741 -0.1923 638 HOH A O   
2490 O  O   . HOH J .   ? 0.5139 0.3146 0.7766 0.0721  0.2158  -0.1571 639 HOH A O   
2491 O  O   . HOH J .   ? 0.3973 0.3805 0.2146 -0.0122 0.0075  -0.0153 640 HOH A O   
2492 O  O   . HOH J .   ? 0.2964 0.4979 0.3959 0.1860  -0.0889 -0.1839 641 HOH A O   
2493 O  O   . HOH J .   ? 0.2365 0.3930 0.3714 -0.0465 0.1004  -0.1116 642 HOH A O   
2494 O  O   . HOH J .   ? 0.5834 0.2893 0.3648 0.0637  0.2433  0.0433  643 HOH A O   
2495 O  O   . HOH J .   ? 0.4619 0.2568 0.4522 -0.0421 0.2306  -0.0176 644 HOH A O   
2496 O  O   . HOH J .   ? 0.4684 0.3730 0.1632 -0.0127 -0.0388 -0.0917 645 HOH A O   
2497 O  O   . HOH J .   ? 0.5362 0.2268 0.2640 -0.1953 0.0315  0.0351  646 HOH A O   
2498 O  O   . HOH J .   ? 0.1860 0.3771 0.2194 0.0407  -0.0255 0.0339  647 HOH A O   
2499 O  O   . HOH J .   ? 0.5425 0.4848 0.3878 -0.1276 0.1051  -0.1515 648 HOH A O   
2500 O  O   . HOH J .   ? 0.3494 0.3720 0.3773 -0.0214 -0.0053 -0.0726 649 HOH A O   
2501 O  O   . HOH J .   ? 0.6546 0.2388 0.4321 0.0880  0.3115  0.0741  650 HOH A O   
2502 O  O   . HOH J .   ? 0.3218 0.3520 0.6901 -0.0680 -0.0534 -0.0713 651 HOH A O   
2503 O  O   . HOH J .   ? 0.4352 0.2495 0.3503 -0.0052 -0.0205 0.0140  652 HOH A O   
2504 O  O   . HOH J .   ? 0.3030 0.2523 0.1858 -0.0013 -0.0414 -0.0183 653 HOH A O   
2505 O  O   . HOH J .   ? 0.5843 0.5819 0.2326 0.3132  -0.0527 -0.0466 654 HOH A O   
2506 O  O   . HOH J .   ? 0.4828 0.2297 0.3195 0.0567  -0.0254 -0.0082 655 HOH A O   
2507 O  O   . HOH J .   ? 0.1302 0.0721 0.1046 0.0015  -0.0168 -0.0117 656 HOH A O   
2508 O  O   . HOH J .   ? 0.2340 0.5127 0.3955 -0.0946 -0.0232 0.0018  657 HOH A O   
2509 O  O   . HOH J .   ? 0.1574 0.2676 0.2912 0.0113  0.0484  -0.0643 658 HOH A O   
2510 O  O   . HOH J .   ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  659 HOH A O   
2511 O  O   . HOH J .   ? 0.3761 0.4409 0.2422 0.0237  0.0232  0.1459  660 HOH A O   
2512 O  O   . HOH J .   ? 0.5752 0.4371 0.2274 -0.0605 0.0157  -0.1274 661 HOH A O   
2513 O  O   . HOH J .   ? 0.2836 0.1981 0.3499 0.0023  0.1138  -0.0363 662 HOH A O   
2514 O  O   . HOH J .   ? 0.6039 0.3295 0.2146 0.2340  0.0270  -0.0660 663 HOH A O   
2515 O  O   . HOH J .   ? 0.4705 0.4826 0.2859 0.1425  0.0276  -0.0834 664 HOH A O   
2516 O  O   . HOH J .   ? 0.5116 0.5035 0.3911 0.0410  -0.0288 -0.0206 665 HOH A O   
2517 O  O   . HOH J .   ? 0.3776 0.2662 0.3679 0.0355  0.1058  -0.0908 666 HOH A O   
2518 O  O   . HOH J .   ? 0.2006 0.6346 0.5792 0.0545  -0.0100 -0.2034 667 HOH A O   
2519 O  O   . HOH J .   ? 0.3828 0.6293 0.3131 0.2887  0.1876  0.2070  668 HOH A O   
2520 O  O   . HOH J .   ? 0.2691 0.4203 0.5043 0.1764  0.1426  0.3065  669 HOH A O   
2521 O  O   . HOH J .   ? 0.3980 0.2958 0.2231 0.0214  0.1241  -0.0103 670 HOH A O   
2522 O  O   . HOH J .   ? 0.3098 0.1952 0.3510 0.0655  -0.2210 -0.0186 671 HOH A O   
2523 O  O   . HOH J .   ? 0.3736 0.4421 0.3301 0.1101  -0.0185 0.0243  672 HOH A O   
2524 O  O   . HOH J .   ? 0.3292 0.2319 0.1977 0.0315  -0.1023 -0.0655 673 HOH A O   
2525 O  O   . HOH J .   ? 0.3537 0.3124 0.2933 0.0314  -0.0146 0.0727  674 HOH A O   
2526 O  O   . HOH J .   ? 0.5343 0.3350 0.3204 -0.0740 -0.0095 -0.0012 675 HOH A O   
2527 O  O   . HOH J .   ? 0.5721 0.6504 0.2805 0.3371  -0.1669 0.0211  676 HOH A O   
2528 O  O   . HOH J .   ? 0.3840 0.8389 0.2530 -0.2270 -0.0060 0.2516  677 HOH A O   
2529 O  O   . HOH J .   ? 0.3174 0.7604 0.1931 0.1398  0.0502  0.0118  678 HOH A O   
2530 O  O   . HOH J .   ? 0.5123 0.7940 0.2153 0.0206  -0.3251 -0.0091 679 HOH A O   
2531 O  O   . HOH J .   ? 0.2006 0.2016 0.2455 0.0067  -0.0457 0.0172  680 HOH A O   
2532 O  O   . HOH J .   ? 0.2149 0.5802 0.2159 -0.0463 -0.0593 0.0485  681 HOH A O   
2533 O  O   . HOH J .   ? 0.3184 0.1847 0.5716 0.1022  -0.1177 -0.0908 682 HOH A O   
2534 O  O   . HOH J .   ? 0.3549 0.3509 0.5109 0.0149  -0.0283 0.0145  683 HOH A O   
2535 O  O   . HOH J .   ? 0.2230 0.3383 0.5861 0.0248  -0.0099 0.0357  684 HOH A O   
2536 O  O   . HOH J .   ? 0.2999 0.4056 0.2596 0.1158  0.0229  -0.0208 685 HOH A O   
2537 O  O   . HOH J .   ? 0.1621 0.3549 0.5110 0.0195  -0.0500 0.1921  686 HOH A O   
2538 O  O   . HOH J .   ? 0.3154 0.7293 0.1920 0.0700  0.0086  0.1012  687 HOH A O   
2539 O  O   . HOH J .   ? 0.3019 0.3170 0.2717 0.1678  -0.1039 -0.0570 688 HOH A O   
2540 O  O   . HOH J .   ? 0.1963 0.2509 0.2297 -0.0117 -0.0493 -0.0424 689 HOH A O   
2541 O  O   . HOH J .   ? 0.2683 0.5725 0.4027 -0.0381 0.0883  0.1029  690 HOH A O   
2542 O  O   . HOH J .   ? 0.1016 0.2099 0.3357 0.0731  0.0675  0.0329  691 HOH A O   
2543 O  O   . HOH J .   ? 0.3398 0.7027 0.1377 -0.0575 0.0299  0.0592  692 HOH A O   
2544 O  O   . HOH J .   ? 0.5097 0.4307 0.3617 0.0818  0.1368  0.0121  693 HOH A O   
2545 O  O   . HOH J .   ? 0.4284 0.2064 0.3656 -0.0268 0.1156  -0.0749 694 HOH A O   
2546 O  O   . HOH J .   ? 0.1895 0.3682 0.3101 -0.0114 -0.0062 -0.0469 695 HOH A O   
2547 O  O   . HOH J .   ? 0.3858 0.2563 0.6494 0.0974  0.0065  -0.0271 696 HOH A O   
2548 O  O   . HOH J .   ? 0.3238 0.3739 0.5438 0.1190  0.0473  0.0907  697 HOH A O   
2549 O  O   . HOH J .   ? 0.4706 0.3078 0.2340 -0.0433 0.0895  -0.0179 698 HOH A O   
2550 O  O   . HOH J .   ? 0.2081 0.2994 0.3345 -0.0829 -0.0132 0.0411  699 HOH A O   
2551 O  O   . HOH J .   ? 0.2601 0.4789 0.2056 0.0201  0.0023  0.0880  700 HOH A O   
2552 O  O   . HOH J .   ? 0.2339 0.3773 0.6225 0.0285  -0.0958 -0.0785 701 HOH A O   
2553 O  O   . HOH J .   ? 0.6943 0.3608 0.3131 0.1132  -0.1234 0.0343  702 HOH A O   
2554 O  O   . HOH J .   ? 0.5488 0.4000 0.1923 -0.0133 -0.0740 0.0203  703 HOH A O   
2555 O  O   . HOH J .   ? 0.1866 0.3980 0.6120 0.0302  0.0464  -0.0587 704 HOH A O   
2556 O  O   . HOH J .   ? 0.2256 0.2238 0.3035 0.0228  0.0000  0.0127  705 HOH A O   
2557 O  O   . HOH J .   ? 0.7670 0.2088 0.3876 0.1064  -0.1202 -0.0737 706 HOH A O   
2558 O  O   . HOH J .   ? 0.4206 0.3096 0.3107 0.0250  0.1123  -0.1186 707 HOH A O   
2559 O  O   . HOH J .   ? 0.2981 0.2511 0.1999 0.0322  0.0583  -0.0025 708 HOH A O   
2560 O  O   . HOH J .   ? 0.2728 0.2398 0.1543 0.0264  -0.0113 -0.0541 709 HOH A O   
2561 O  O   . HOH J .   ? 0.5456 0.5416 0.2705 -0.2522 -0.2111 0.1702  710 HOH A O   
2562 O  O   . HOH J .   ? 0.3066 0.4760 0.3186 -0.0469 -0.1714 -0.0343 711 HOH A O   
2563 O  O   . HOH J .   ? 0.4023 0.2837 0.4303 0.0688  -0.1008 -0.0959 712 HOH A O   
2564 O  O   . HOH J .   ? 0.2077 0.3995 0.3545 -0.0268 0.0083  0.0782  713 HOH A O   
2565 O  O   . HOH J .   ? 0.5355 0.2103 0.2451 0.0700  -0.1049 -0.0030 714 HOH A O   
2566 O  O   . HOH J .   ? 0.1901 0.2599 0.2642 -0.0212 -0.0424 0.0381  715 HOH A O   
2567 O  O   . HOH J .   ? 0.3467 0.8151 0.4332 0.1333  -0.0127 -0.0016 716 HOH A O   
2568 O  O   . HOH J .   ? 0.2006 0.4480 0.4066 -0.0067 -0.0321 0.0528  717 HOH A O   
2569 O  O   . HOH J .   ? 0.5207 0.1855 0.2911 -0.0135 0.1059  -0.0316 718 HOH A O   
2570 O  O   . HOH J .   ? 0.3624 0.3153 0.3842 0.0851  -0.0510 0.0381  719 HOH A O   
2571 O  O   . HOH J .   ? 0.6016 0.2398 0.5007 -0.1674 0.1992  -0.1047 720 HOH A O   
2572 O  O   . HOH J .   ? 0.4877 0.2910 0.2473 -0.1482 -0.1615 -0.0290 721 HOH A O   
2573 O  O   . HOH J .   ? 0.3698 0.4149 0.4631 -0.0209 -0.0372 -0.0040 722 HOH A O   
2574 O  O   . HOH J .   ? 0.3103 0.3885 0.6160 0.1421  -0.1298 -0.0250 723 HOH A O   
2575 O  O   . HOH J .   ? 0.3597 0.2182 0.1683 -0.0128 0.0108  -0.0471 724 HOH A O   
2576 O  O   . HOH J .   ? 0.1622 0.1295 0.1870 0.0079  -0.0461 0.0423  725 HOH A O   
2577 O  O   . HOH J .   ? 0.3380 0.2110 0.5478 0.0458  0.1635  0.0467  726 HOH A O   
2578 O  O   . HOH J .   ? 0.2437 0.0962 0.1453 0.0211  -0.0715 -0.0111 727 HOH A O   
2579 O  O   . HOH J .   ? 0.3303 0.2363 0.3077 -0.0063 -0.0173 0.0683  728 HOH A O   
2580 O  O   . HOH J .   ? 0.2838 0.5035 0.3438 -0.1128 -0.0518 0.0517  729 HOH A O   
2581 O  O   . HOH J .   ? 0.4214 0.3204 0.4641 0.0145  0.0103  0.1564  730 HOH A O   
2582 O  O   . HOH J .   ? 0.5060 0.4478 0.5055 -0.0666 -0.3599 0.0463  731 HOH A O   
2583 O  O   . HOH J .   ? 0.2462 0.3082 0.4947 0.0362  0.0442  0.1592  732 HOH A O   
2584 O  O   . HOH J .   ? 0.2602 0.3162 0.6338 -0.1190 -0.1737 0.0606  733 HOH A O   
2585 O  O   . HOH J .   ? 0.6417 0.4088 0.4471 0.0094  0.0337  -0.1323 734 HOH A O   
2586 O  O   . HOH J .   ? 0.4546 0.3368 0.4429 -0.2063 -0.0554 0.1766  735 HOH A O   
2587 O  O   . HOH J .   ? 0.2679 0.3226 0.5158 0.0580  0.1410  0.0176  736 HOH A O   
2588 O  O   . HOH J .   ? 0.5092 0.2770 0.2214 -0.1665 0.1082  -0.0027 737 HOH A O   
2589 O  O   . HOH J .   ? 0.5156 0.2599 0.1992 0.0067  0.0455  0.0013  738 HOH A O   
2590 O  O   . HOH J .   ? 0.4304 0.3376 0.2749 0.1285  0.0220  -0.0402 739 HOH A O   
2591 O  O   . HOH J .   ? 0.3780 0.2778 0.1830 -0.0021 -0.0642 -0.1178 740 HOH A O   
2592 O  O   . HOH J .   ? 0.2658 0.0883 0.3923 -0.0129 0.1204  -0.0262 741 HOH A O   
2593 O  O   . HOH J .   ? 0.3901 0.5090 0.4311 -0.0220 0.0605  -0.0959 742 HOH A O   
2594 O  O   . HOH J .   ? 0.1647 0.3772 0.4655 -0.0381 -0.0372 -0.1345 743 HOH A O   
2595 O  O   . HOH J .   ? 0.3414 0.7962 0.5225 -0.1753 0.1342  0.1956  744 HOH A O   
2596 O  O   . HOH J .   ? 0.1639 0.4991 0.3750 -0.0167 -0.0357 -0.0010 745 HOH A O   
2597 O  O   . HOH J .   ? 0.2495 0.2764 0.3675 -0.1059 0.0160  -0.0791 746 HOH A O   
2598 O  O   . HOH J .   ? 0.4810 0.3848 0.3404 0.0505  -0.1262 0.1045  747 HOH A O   
2599 O  O   . HOH J .   ? 0.5268 0.3369 0.2958 -0.0268 0.0069  0.0576  748 HOH A O   
2600 O  O   . HOH J .   ? 0.0840 0.4073 0.8894 -0.1301 -0.2479 0.2846  749 HOH A O   
# 
