data_4WW6
# 
_entry.id   4WW6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_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   4WW6         pdb_00004ww6 10.2210/pdb4ww6/pdb 
WWPDB D_1000204618 ?            ?                   
# 
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 2015-07-01 
2 'Structure model' 1 1 2018-03-07 
3 'Structure model' 1 2 2024-01-10 
# 
_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' 'Data collection'        
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 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' diffrn_source                 
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' database_2                    
5 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' '_diffrn_source.pdbx_synchrotron_site' 
2 3 'Structure model' '_database_2.pdbx_DOI'                 
3 3 'Structure model' '_database_2.pdbx_database_accession'  
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        4WW6 
_pdbx_database_status.recvd_initial_deposition_date   2014-11-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 4WR7 unspecified 
PDB . 4WUP unspecified 
PDB . 4WUQ unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_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                   NE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biophys.Chem. 
_citation.journal_id_ASTM           BICIAZ 
_citation.journal_id_CSD            0829 
_citation.journal_id_ISSN           0301-4622 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            205 
_citation.language                  ? 
_citation.page_first                51 
_citation.page_last                 65 
_citation.title                     
;Intrinsic thermodynamics of 4-substituted-2,3,5,6-tetrafluorobenzenesulfonamide binding to carbonic anhydrases by isothermal titration calorimetry.
;
_citation.year                      2015 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bpc.2015.05.009 
_citation.pdbx_database_id_PubMed   26079542 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zubriene, A.'      1  ? 
primary 'Smirnoviene, J.'   2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Morkunaite, V.'    4  ? 
primary 'Michailoviene, V.' 5  ? 
primary 'Jachno, J.'        6  ? 
primary 'Juozapaitiene, V.' 7  ? 
primary 'Norvaisas, P.'     8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Matulis, D.'       11 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                     29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                 65.409    1   ?       ? 
'2,3,5,6-Tetrafluoro-4-(propylthio)benzenesulfonamide' ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                       78.133    1   ?       ? 'ZINC ION' ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                     195.237   1   ?       ? BICINE ? 
5 non-polymer syn 'MALONIC ACID'                                             104.061   1   ?       ? 
'2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                 ? 
6 non-polymer syn BICINE                                                     163.172   1   ?       ? 'DIMETHYL SULFOXIDE' ? 
7 non-polymer syn '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 303.297   2   ?       ? 'MALONIC ACID' ? 
8 water       nat water                                                      18.015    268 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                 ZN  
3 'DIMETHYL SULFOXIDE'                                       DMS 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                     MES 
5 'MALONIC ACID'                                             MLA 
6 BICINE                                                     BCN 
7 '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 3TV 
8 water                                                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               pET15b 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
3TV non-polymer         . '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' ? 'C9 H9 F4 N O2 S2' 303.297 
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                     ? 'C6 H13 N O4 S'    195.237 
MET 'L-peptide linking' y METHIONINE                                                 ? 'C5 H11 N O2 S'    149.211 
MLA non-polymer         . 'MALONIC ACID'                                             
'DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID; METHANEDICARBOXYLIC ACID' 'C3 H4 O4'         104.061 
PHE 'L-peptide linking' y PHENYLALANINE                                              ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                    ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                     ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                  ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                 ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                   ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                                     ? 'C5 H11 N O2'      117.146 
ZN  non-polymer         . 'ZINC ION'                                                 ? 'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 MES 1   303 2   MES MES A . 
E 5 MLA 1   304 3   MLA DXX A . 
F 6 BCN 1   305 4   BCN BCN A . 
G 7 3TV 1   306 1   3TV 3TV A . 
H 7 3TV 1   307 2   3TV 3TV A . 
I 8 HOH 1   401 102 HOH HOH A . 
I 8 HOH 2   402 120 HOH HOH A . 
I 8 HOH 3   403 220 HOH HOH A . 
I 8 HOH 4   404 67  HOH HOH A . 
I 8 HOH 5   405 83  HOH HOH A . 
I 8 HOH 6   406 233 HOH HOH A . 
I 8 HOH 7   407 195 HOH HOH A . 
I 8 HOH 8   408 30  HOH HOH A . 
I 8 HOH 9   409 231 HOH HOH A . 
I 8 HOH 10  410 190 HOH HOH A . 
I 8 HOH 11  411 108 HOH HOH A . 
I 8 HOH 12  412 153 HOH HOH A . 
I 8 HOH 13  413 264 HOH HOH A . 
I 8 HOH 14  414 213 HOH HOH A . 
I 8 HOH 15  415 194 HOH HOH A . 
I 8 HOH 16  416 186 HOH HOH A . 
I 8 HOH 17  417 216 HOH HOH A . 
I 8 HOH 18  418 189 HOH HOH A . 
I 8 HOH 19  419 55  HOH HOH A . 
I 8 HOH 20  420 149 HOH HOH A . 
I 8 HOH 21  421 184 HOH HOH A . 
I 8 HOH 22  422 171 HOH HOH A . 
I 8 HOH 23  423 125 HOH HOH A . 
I 8 HOH 24  424 222 HOH HOH A . 
I 8 HOH 25  425 147 HOH HOH A . 
I 8 HOH 26  426 185 HOH HOH A . 
I 8 HOH 27  427 229 HOH HOH A . 
I 8 HOH 28  428 167 HOH HOH A . 
I 8 HOH 29  429 215 HOH HOH A . 
I 8 HOH 30  430 208 HOH HOH A . 
I 8 HOH 31  431 191 HOH HOH A . 
I 8 HOH 32  432 142 HOH HOH A . 
I 8 HOH 33  433 243 HOH HOH A . 
I 8 HOH 34  434 197 HOH HOH A . 
I 8 HOH 35  435 61  HOH HOH A . 
I 8 HOH 36  436 187 HOH HOH A . 
I 8 HOH 37  437 42  HOH HOH A . 
I 8 HOH 38  438 248 HOH HOH A . 
I 8 HOH 39  439 29  HOH HOH A . 
I 8 HOH 40  440 259 HOH HOH A . 
I 8 HOH 41  441 254 HOH HOH A . 
I 8 HOH 42  442 244 HOH HOH A . 
I 8 HOH 43  443 72  HOH HOH A . 
I 8 HOH 44  444 114 HOH HOH A . 
I 8 HOH 45  445 65  HOH HOH A . 
I 8 HOH 46  446 232 HOH HOH A . 
I 8 HOH 47  447 168 HOH HOH A . 
I 8 HOH 48  448 162 HOH HOH A . 
I 8 HOH 49  449 107 HOH HOH A . 
I 8 HOH 50  450 105 HOH HOH A . 
I 8 HOH 51  451 27  HOH HOH A . 
I 8 HOH 52  452 54  HOH HOH A . 
I 8 HOH 53  453 18  HOH HOH A . 
I 8 HOH 54  454 156 HOH HOH A . 
I 8 HOH 55  455 172 HOH HOH A . 
I 8 HOH 56  456 101 HOH HOH A . 
I 8 HOH 57  457 78  HOH HOH A . 
I 8 HOH 58  458 217 HOH HOH A . 
I 8 HOH 59  459 127 HOH HOH A . 
I 8 HOH 60  460 40  HOH HOH A . 
I 8 HOH 61  461 75  HOH HOH A . 
I 8 HOH 62  462 80  HOH HOH A . 
I 8 HOH 63  463 87  HOH HOH A . 
I 8 HOH 64  464 170 HOH HOH A . 
I 8 HOH 65  465 151 HOH HOH A . 
I 8 HOH 66  466 4   HOH HOH A . 
I 8 HOH 67  467 68  HOH HOH A . 
I 8 HOH 68  468 139 HOH HOH A . 
I 8 HOH 69  469 250 HOH HOH A . 
I 8 HOH 70  470 57  HOH HOH A . 
I 8 HOH 71  471 2   HOH HOH A . 
I 8 HOH 72  472 165 HOH HOH A . 
I 8 HOH 73  473 249 HOH HOH A . 
I 8 HOH 74  474 173 HOH HOH A . 
I 8 HOH 75  475 38  HOH HOH A . 
I 8 HOH 76  476 77  HOH HOH A . 
I 8 HOH 77  477 128 HOH HOH A . 
I 8 HOH 78  478 234 HOH HOH A . 
I 8 HOH 79  479 85  HOH HOH A . 
I 8 HOH 80  480 179 HOH HOH A . 
I 8 HOH 81  481 123 HOH HOH A . 
I 8 HOH 82  482 53  HOH HOH A . 
I 8 HOH 83  483 116 HOH HOH A . 
I 8 HOH 84  484 141 HOH HOH A . 
I 8 HOH 85  485 99  HOH HOH A . 
I 8 HOH 86  486 158 HOH HOH A . 
I 8 HOH 87  487 148 HOH HOH A . 
I 8 HOH 88  488 60  HOH HOH A . 
I 8 HOH 89  489 76  HOH HOH A . 
I 8 HOH 90  490 131 HOH HOH A . 
I 8 HOH 91  491 132 HOH HOH A . 
I 8 HOH 92  492 79  HOH HOH A . 
I 8 HOH 93  493 176 HOH HOH A . 
I 8 HOH 94  494 45  HOH HOH A . 
I 8 HOH 95  495 41  HOH HOH A . 
I 8 HOH 96  496 121 HOH HOH A . 
I 8 HOH 97  497 159 HOH HOH A . 
I 8 HOH 98  498 251 HOH HOH A . 
I 8 HOH 99  499 119 HOH HOH A . 
I 8 HOH 100 500 166 HOH HOH A . 
I 8 HOH 101 501 221 HOH HOH A . 
I 8 HOH 102 502 211 HOH HOH A . 
I 8 HOH 103 503 175 HOH HOH A . 
I 8 HOH 104 504 209 HOH HOH A . 
I 8 HOH 105 505 115 HOH HOH A . 
I 8 HOH 106 506 174 HOH HOH A . 
I 8 HOH 107 507 177 HOH HOH A . 
I 8 HOH 108 508 134 HOH HOH A . 
I 8 HOH 109 509 135 HOH HOH A . 
I 8 HOH 110 510 169 HOH HOH A . 
I 8 HOH 111 511 247 HOH HOH A . 
I 8 HOH 112 512 95  HOH HOH A . 
I 8 HOH 113 513 92  HOH HOH A . 
I 8 HOH 114 514 253 HOH HOH A . 
I 8 HOH 115 515 252 HOH HOH A . 
I 8 HOH 116 516 37  HOH HOH A . 
I 8 HOH 117 517 32  HOH HOH A . 
I 8 HOH 118 518 180 HOH HOH A . 
I 8 HOH 119 519 161 HOH HOH A . 
I 8 HOH 120 520 181 HOH HOH A . 
I 8 HOH 121 521 49  HOH HOH A . 
I 8 HOH 122 522 237 HOH HOH A . 
I 8 HOH 123 523 201 HOH HOH A . 
I 8 HOH 124 524 238 HOH HOH A . 
I 8 HOH 125 525 227 HOH HOH A . 
I 8 HOH 126 526 146 HOH HOH A . 
I 8 HOH 127 527 126 HOH HOH A . 
I 8 HOH 128 528 199 HOH HOH A . 
I 8 HOH 129 529 255 HOH HOH A . 
I 8 HOH 130 530 155 HOH HOH A . 
I 8 HOH 131 531 212 HOH HOH A . 
I 8 HOH 132 532 256 HOH HOH A . 
I 8 HOH 133 533 137 HOH HOH A . 
I 8 HOH 134 534 210 HOH HOH A . 
I 8 HOH 135 535 204 HOH HOH A . 
I 8 HOH 136 536 206 HOH HOH A . 
I 8 HOH 137 537 202 HOH HOH A . 
I 8 HOH 138 538 240 HOH HOH A . 
I 8 HOH 139 539 230 HOH HOH A . 
I 8 HOH 140 540 203 HOH HOH A . 
I 8 HOH 141 541 94  HOH HOH A . 
I 8 HOH 142 542 1   HOH HOH A . 
I 8 HOH 143 543 3   HOH HOH A . 
I 8 HOH 144 544 5   HOH HOH A . 
I 8 HOH 145 545 6   HOH HOH A . 
I 8 HOH 146 546 7   HOH HOH A . 
I 8 HOH 147 547 8   HOH HOH A . 
I 8 HOH 148 548 9   HOH HOH A . 
I 8 HOH 149 549 10  HOH HOH A . 
I 8 HOH 150 550 11  HOH HOH A . 
I 8 HOH 151 551 12  HOH HOH A . 
I 8 HOH 152 552 13  HOH HOH A . 
I 8 HOH 153 553 14  HOH HOH A . 
I 8 HOH 154 554 15  HOH HOH A . 
I 8 HOH 155 555 16  HOH HOH A . 
I 8 HOH 156 556 17  HOH HOH A . 
I 8 HOH 157 557 19  HOH HOH A . 
I 8 HOH 158 558 20  HOH HOH A . 
I 8 HOH 159 559 21  HOH HOH A . 
I 8 HOH 160 560 22  HOH HOH A . 
I 8 HOH 161 561 23  HOH HOH A . 
I 8 HOH 162 562 24  HOH HOH A . 
I 8 HOH 163 563 25  HOH HOH A . 
I 8 HOH 164 564 26  HOH HOH A . 
I 8 HOH 165 565 28  HOH HOH A . 
I 8 HOH 166 566 31  HOH HOH A . 
I 8 HOH 167 567 33  HOH HOH A . 
I 8 HOH 168 568 34  HOH HOH A . 
I 8 HOH 169 569 35  HOH HOH A . 
I 8 HOH 170 570 36  HOH HOH A . 
I 8 HOH 171 571 39  HOH HOH A . 
I 8 HOH 172 572 43  HOH HOH A . 
I 8 HOH 173 573 44  HOH HOH A . 
I 8 HOH 174 574 46  HOH HOH A . 
I 8 HOH 175 575 47  HOH HOH A . 
I 8 HOH 176 576 48  HOH HOH A . 
I 8 HOH 177 577 50  HOH HOH A . 
I 8 HOH 178 578 51  HOH HOH A . 
I 8 HOH 179 579 52  HOH HOH A . 
I 8 HOH 180 580 56  HOH HOH A . 
I 8 HOH 181 581 58  HOH HOH A . 
I 8 HOH 182 582 59  HOH HOH A . 
I 8 HOH 183 583 62  HOH HOH A . 
I 8 HOH 184 584 63  HOH HOH A . 
I 8 HOH 185 585 64  HOH HOH A . 
I 8 HOH 186 586 66  HOH HOH A . 
I 8 HOH 187 587 69  HOH HOH A . 
I 8 HOH 188 588 70  HOH HOH A . 
I 8 HOH 189 589 71  HOH HOH A . 
I 8 HOH 190 590 73  HOH HOH A . 
I 8 HOH 191 591 74  HOH HOH A . 
I 8 HOH 192 592 81  HOH HOH A . 
I 8 HOH 193 593 82  HOH HOH A . 
I 8 HOH 194 594 84  HOH HOH A . 
I 8 HOH 195 595 86  HOH HOH A . 
I 8 HOH 196 596 88  HOH HOH A . 
I 8 HOH 197 597 89  HOH HOH A . 
I 8 HOH 198 598 90  HOH HOH A . 
I 8 HOH 199 599 91  HOH HOH A . 
I 8 HOH 200 600 93  HOH HOH A . 
I 8 HOH 201 601 96  HOH HOH A . 
I 8 HOH 202 602 97  HOH HOH A . 
I 8 HOH 203 603 98  HOH HOH A . 
I 8 HOH 204 604 100 HOH HOH A . 
I 8 HOH 205 605 103 HOH HOH A . 
I 8 HOH 206 606 104 HOH HOH A . 
I 8 HOH 207 607 106 HOH HOH A . 
I 8 HOH 208 608 109 HOH HOH A . 
I 8 HOH 209 609 110 HOH HOH A . 
I 8 HOH 210 610 111 HOH HOH A . 
I 8 HOH 211 611 112 HOH HOH A . 
I 8 HOH 212 612 113 HOH HOH A . 
I 8 HOH 213 613 117 HOH HOH A . 
I 8 HOH 214 614 118 HOH HOH A . 
I 8 HOH 215 615 122 HOH HOH A . 
I 8 HOH 216 616 124 HOH HOH A . 
I 8 HOH 217 617 129 HOH HOH A . 
I 8 HOH 218 618 130 HOH HOH A . 
I 8 HOH 219 619 133 HOH HOH A . 
I 8 HOH 220 620 136 HOH HOH A . 
I 8 HOH 221 621 138 HOH HOH A . 
I 8 HOH 222 622 140 HOH HOH A . 
I 8 HOH 223 623 143 HOH HOH A . 
I 8 HOH 224 624 144 HOH HOH A . 
I 8 HOH 225 625 145 HOH HOH A . 
I 8 HOH 226 626 150 HOH HOH A . 
I 8 HOH 227 627 152 HOH HOH A . 
I 8 HOH 228 628 154 HOH HOH A . 
I 8 HOH 229 629 157 HOH HOH A . 
I 8 HOH 230 630 160 HOH HOH A . 
I 8 HOH 231 631 163 HOH HOH A . 
I 8 HOH 232 632 164 HOH HOH A . 
I 8 HOH 233 633 178 HOH HOH A . 
I 8 HOH 234 634 182 HOH HOH A . 
I 8 HOH 235 635 183 HOH HOH A . 
I 8 HOH 236 636 188 HOH HOH A . 
I 8 HOH 237 637 192 HOH HOH A . 
I 8 HOH 238 638 193 HOH HOH A . 
I 8 HOH 239 639 196 HOH HOH A . 
I 8 HOH 240 640 198 HOH HOH A . 
I 8 HOH 241 641 200 HOH HOH A . 
I 8 HOH 242 642 205 HOH HOH A . 
I 8 HOH 243 643 207 HOH HOH A . 
I 8 HOH 244 644 214 HOH HOH A . 
I 8 HOH 245 645 218 HOH HOH A . 
I 8 HOH 246 646 219 HOH HOH A . 
I 8 HOH 247 647 223 HOH HOH A . 
I 8 HOH 248 648 224 HOH HOH A . 
I 8 HOH 249 649 225 HOH HOH A . 
I 8 HOH 250 650 226 HOH HOH A . 
I 8 HOH 251 651 228 HOH HOH A . 
I 8 HOH 252 652 235 HOH HOH A . 
I 8 HOH 253 653 236 HOH HOH A . 
I 8 HOH 254 654 239 HOH HOH A . 
I 8 HOH 255 655 241 HOH HOH A . 
I 8 HOH 256 656 242 HOH HOH A . 
I 8 HOH 257 657 245 HOH HOH A . 
I 8 HOH 258 658 246 HOH HOH A . 
I 8 HOH 259 659 257 HOH HOH A . 
I 8 HOH 260 660 258 HOH HOH A . 
I 8 HOH 261 661 260 HOH HOH A . 
I 8 HOH 262 662 261 HOH HOH A . 
I 8 HOH 263 663 262 HOH HOH A . 
I 8 HOH 264 664 263 HOH HOH A . 
I 8 HOH 265 665 265 HOH HOH A . 
I 8 HOH 266 666 266 HOH HOH A . 
I 8 HOH 267 667 267 HOH HOH A . 
I 8 HOH 268 668 268 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   ? CB  ? A LYS 9   CB  
2  1 Y 1 A LYS 9   ? CG  ? A LYS 9   CG  
3  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
4  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
5  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
6  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
7  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
8  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
9  1 Y 1 A LYS 172 ? CE  ? A LYS 171 CE  
10 1 Y 1 A LYS 172 ? NZ  ? A LYS 171 NZ  
11 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
12 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
13 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
14 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
15 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
16 1 N 1 A MES 303 ? S   ? D MES 1   S   
17 1 N 1 A MES 303 ? O1S ? D MES 1   O1S 
18 1 N 1 A MES 303 ? O2S ? D MES 1   O2S 
19 1 N 1 A MES 303 ? O3S ? D MES 1   O3S 
# 
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 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.006    2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .        3 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.290 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     4WW6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.214 
_cell.length_a_esd                 ? 
_cell.length_b                     41.026 
_cell.length_b_esd                 ? 
_cell.length_c                     71.774 
_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                         4WW6 
_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                   4WW6 
_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            2.0 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.2 
_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              7.0 
_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 was 0.1M sodium BICINE, pH 9, 0.25 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_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_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         2013-05-22 
# 
_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   0.826606 
_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        0.826606 
_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            8.784 
_reflns.entry_id                         4WW6 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.060 
_reflns.d_resolution_low                 69.554 
_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                       102717 
_reflns.number_obs                       102717 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             95.400 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.600 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.041 
_reflns.pdbx_netI_over_av_sigmaI         6.933 
_reflns.pdbx_netI_over_sigmaI            17.900 
_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                  0.050 
_reflns.pdbx_Rpim_I_all                  0.019 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         676004 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
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_R_split 
1.06 1.12  ? 2.2  75329 ? ? 12952 ? 83.00 ? ? ? 0.428 0.350 ? ? ? ? ? ? ? ? 5.80 0.350 ? ? 4.10  0.43 0.17 ? 1  1 ? ? 
1.12 1.19  ? 3.3  89091 ? ? 13968 ? 94.60 ? ? ? 0.283 0.233 ? ? ? ? ? ? ? ? 6.40 0.233 ? ? 6.30  0.28 0.11 ? 2  ? ? ? 
1.19 1.27  ? 4.6  90220 ? ? 13449 ? 96.60 ? ? ? 0.200 0.166 ? ? ? ? ? ? ? ? 6.70 0.166 ? ? 8.50  0.20 0.08 ? 3  ? ? ? 
1.27 1.37  ? 6.5  81656 ? ? 12624 ? 97.10 ? ? ? 0.144 0.116 ? ? ? ? ? ? ? ? 6.50 0.116 ? ? 11.20 0.14 0.05 ? 4  ? ? ? 
1.37 1.50  ? 9.2  81100 ? ? 11733 ? 98.40 ? ? ? 0.103 0.081 ? ? ? ? ? ? ? ? 6.90 0.081 ? ? 15.50 0.10 0.04 ? 5  ? ? ? 
1.50 1.68  ? 12.9 69678 ? ? 10615 ? 98.20 ? ? ? 0.074 0.056 ? ? ? ? ? ? ? ? 6.60 0.056 ? ? 21.00 0.07 0.03 ? 6  ? ? ? 
1.68 1.94  ? 16.3 67457 ? ? 9531  ? 99.50 ? ? ? 0.054 0.041 ? ? ? ? ? ? ? ? 7.10 0.041 ? ? 30.00 0.05 0.02 ? 7  ? ? ? 
1.94 2.37  ? 18.7 52941 ? ? 8013  ? 98.80 ? ? ? 0.045 0.035 ? ? ? ? ? ? ? ? 6.60 0.035 ? ? 37.50 0.05 0.02 ? 8  ? ? ? 
2.37 3.35  ? 18.8 44797 ? ? 6296  ? 99.70 ? ? ? 0.040 0.032 ? ? ? ? ? ? ? ? 7.10 0.032 ? ? 44.90 0.04 0.01 ? 9  ? ? ? 
3.35 69.55 ? 16.8 23735 ? ? 3536  ? 99.20 ? ? ? 0.037 0.031 ? ? ? ? ? ? ? ? 6.70 0.031 ? ? 48.20 0.04 0.01 ? 10 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.020 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.100 
_refine.aniso_B[2][2]                            -0.270 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.210 
_refine.B_iso_max                                105.69 
_refine.B_iso_mean                               15.737 
_refine.B_iso_min                                6.39 
_refine.correlation_coeff_Fo_to_Fc               0.981 
_refine.correlation_coeff_Fo_to_Fc_free          0.977 
_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                                 4WW6 
_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                            1.060 
_refine.ls_d_res_low                             40.910 
_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                     102697 
_refine.ls_number_reflns_R_free                  10363 
_refine.ls_number_reflns_R_work                  92334 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.170 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.131 
_refine.ls_R_factor_R_free                       0.151 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.128 
_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                      0.155 
_refine.ls_wR_factor_R_work                      0.130 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          0.00 
_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                      3HLJ 
_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                       0.028 
_refine.pdbx_overall_ESU_R_Free                  0.028 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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             0.028 
_refine.overall_SU_R_free                        0.028 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.937 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_refine_hist.number_atoms_solvent             268 
_refine_hist.number_atoms_total               2384 
_refine_hist.d_res_high                       1.060 
_refine_hist.d_res_low                        40.910 
# 
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' ? 0.024  0.020  2396 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.417  1.978  3282 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.167  5.000  303  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.618 24.815 108  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 11.976 15.000 383  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 20.597 15.000 9    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.162  0.200  331  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.021  1913 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 8.835  3.000  2396 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 20.884 5.000  269  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 9.795  5.000  2316 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.060 
_refine_ls_shell.d_res_low                        1.088 
_refine_ls_shell.number_reflns_all                5817 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             595 
_refine_ls_shell.number_reflns_R_work             5222 
_refine_ls_shell.percent_reflns_obs               73.240 
_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                  0.215 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.192 
_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_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                     4WW6 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme II with 2,3,5,6-Tetrafluoro-4-(propylthio)benzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        4WW6 
_struct_keywords.text            'drug design, lyase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 7 ? 
I N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4WW6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1130  ? 
1 MORE         6     ? 
1 'SSA (A^2)'  11250 ? 
# 
_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 
# 
_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 
# 
_struct_biol.details                      'biological unit is the same as asym.' 
_struct_biol.id                           1 
_struct_biol.pdbx_parent_biol_id          ? 
_struct_biol.pdbx_formula_weight          ? 
_struct_biol.pdbx_formula_weight_method   ? 
_struct_biol.pdbx_aggregation_state       ? 
_struct_biol.pdbx_assembly_method         ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 G 3TV . N2 ? ? A ZN  301 A 3TV 306 1_555 ? ? ? ? ? ? ? 1.916 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.9 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 113.0 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.3  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? G 3TV .   ? A 3TV 306 ? 1_555 112.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? G 3TV .   ? A 3TV 306 ? 1_555 115.7 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? G 3TV .   ? A 3TV 306 ? 1_555 111.3 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.60 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.20  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 3  'binding site for residue DMS A 302' 
AC3 Software A MES 303 ? 5  'binding site for residue MES A 303' 
AC4 Software A MLA 304 ? 10 'binding site for residue MLA A 304' 
AC5 Software A BCN 305 ? 8  'binding site for residue BCN A 305' 
AC6 Software A 3TV 306 ? 13 'binding site for residue 3TV A 306' 
AC7 Software A 3TV 307 ? 14 'binding site for residue 3TV A 307' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  3TV G .   ? 3TV A 306 . ? 1_555 ? 
5  AC2 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
6  AC2 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
7  AC2 3  HOH I .   ? HOH A 642 . ? 1_555 ? 
8  AC3 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
9  AC3 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
10 AC3 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
11 AC3 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
12 AC3 5  HOH I .   ? HOH A 472 . ? 1_555 ? 
13 AC4 10 GLY A 6   ? GLY A 6   . ? 1_555 ? 
14 AC4 10 TYR A 7   ? TYR A 7   . ? 1_555 ? 
15 AC4 10 GLY A 8   ? GLY A 8   . ? 1_555 ? 
16 AC4 10 ASN A 11  ? ASN A 11  . ? 1_555 ? 
17 AC4 10 PHE A 230 ? PHE A 231 . ? 1_555 ? 
18 AC4 10 GLU A 238 ? GLU A 239 . ? 1_555 ? 
19 AC4 10 HOH I .   ? HOH A 586 . ? 1_555 ? 
20 AC4 10 HOH I .   ? HOH A 605 . ? 1_555 ? 
21 AC4 10 HOH I .   ? HOH A 652 . ? 1_555 ? 
22 AC4 10 HOH I .   ? HOH A 668 . ? 1_555 ? 
23 AC5 8  LYS A 148 ? LYS A 149 . ? 1_555 ? 
24 AC5 8  LYS A 212 ? LYS A 213 . ? 1_555 ? 
25 AC5 8  GLU A 213 ? GLU A 214 . ? 1_555 ? 
26 AC5 8  PRO A 214 ? PRO A 215 . ? 1_555 ? 
27 AC5 8  HOH I .   ? HOH A 416 . ? 1_555 ? 
28 AC5 8  HOH I .   ? HOH A 607 . ? 1_555 ? 
29 AC5 8  HOH I .   ? HOH A 643 . ? 1_555 ? 
30 AC5 8  HOH I .   ? HOH A 659 . ? 1_555 ? 
31 AC6 13 HIS A 94  ? HIS A 94  . ? 1_555 ? 
32 AC6 13 HIS A 96  ? HIS A 96  . ? 1_555 ? 
33 AC6 13 HIS A 119 ? HIS A 119 . ? 1_555 ? 
34 AC6 13 VAL A 121 ? VAL A 121 . ? 1_555 ? 
35 AC6 13 PHE A 130 ? PHE A 131 . ? 1_555 ? 
36 AC6 13 VAL A 142 ? VAL A 143 . ? 1_555 ? 
37 AC6 13 LEU A 197 ? LEU A 198 . ? 1_555 ? 
38 AC6 13 THR A 198 ? THR A 199 . ? 1_555 ? 
39 AC6 13 THR A 199 ? THR A 200 . ? 1_555 ? 
40 AC6 13 TRP A 208 ? TRP A 209 . ? 1_555 ? 
41 AC6 13 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
42 AC6 13 HOH I .   ? HOH A 565 . ? 1_555 ? 
43 AC6 13 HOH I .   ? HOH A 603 . ? 1_555 ? 
44 AC7 14 HIS A 4   ? HIS A 4   . ? 1_555 ? 
45 AC7 14 TRP A 5   ? TRP A 5   . ? 1_555 ? 
46 AC7 14 HIS A 10  ? HIS A 10  . ? 1_555 ? 
47 AC7 14 ASN A 11  ? ASN A 11  . ? 1_555 ? 
48 AC7 14 HIS A 15  ? HIS A 15  . ? 1_555 ? 
49 AC7 14 TRP A 16  ? TRP A 16  . ? 1_555 ? 
50 AC7 14 ASP A 19  ? ASP A 19  . ? 1_555 ? 
51 AC7 14 ASP A 179 ? ASP A 180 . ? 1_655 ? 
52 AC7 14 ARG A 181 ? ARG A 182 . ? 1_655 ? 
53 AC7 14 GLY A 182 ? GLY A 183 . ? 1_655 ? 
54 AC7 14 HOH I .   ? HOH A 420 . ? 1_555 ? 
55 AC7 14 HOH I .   ? HOH A 435 . ? 1_655 ? 
56 AC7 14 HOH I .   ? HOH A 451 . ? 1_655 ? 
57 AC7 14 HOH I .   ? HOH A 459 . ? 1_555 ? 
# 
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 634 ? ? O   A HOH 661 ? ? 1.73 
2 1 OE2 A GLU 214 ? B O   A HOH 401 ? ? 1.84 
3 1 OD1 A ASP 75  ? ? NH2 A ARG 89  ? B 2.18 
4 1 O22 A BCN 305 ? ? O   A HOH 643 ? ? 2.19 
5 1 O   A SER 152 ? A O   A HOH 613 ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            ASP 
_pdbx_validate_rmsd_bond.auth_seq_id_1             34 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            B 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            ASP 
_pdbx_validate_rmsd_bond.auth_seq_id_2             34 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.345 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            0.116 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.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  ? ? -142.94 23.21   
2 1 ARG A 27  ? ? -141.65 56.04   
3 1 LYS A 76  ? A -99.71  -92.56  
4 1 GLU A 106 ? ? -90.89  -61.65  
5 1 LYS A 111 ? ? 74.46   -3.32   
6 1 PHE A 176 ? ? -151.88 64.47   
7 1 ASN A 244 ? ? -94.41  48.94   
8 1 LYS A 252 ? B 48.48   -134.09 
9 1 ASN A 253 ? B -105.03 63.34   
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
3TV F18  F  N N 1   
3TV C7   C  Y N 2   
3TV C6   C  Y N 3   
3TV F17  F  N N 4   
3TV C8   C  Y N 5   
3TV S11  S  N N 6   
3TV C12  C  N N 7   
3TV C13  C  N N 8   
3TV C14  C  N N 9   
3TV C9   C  Y N 10  
3TV F15  F  N N 11  
3TV C10  C  Y N 12  
3TV F16  F  N N 13  
3TV C5   C  Y N 14  
3TV S1   S  N N 15  
3TV O3   O  N N 16  
3TV O4   O  N N 17  
3TV N2   N  N N 18  
3TV H1   H  N N 19  
3TV H2   H  N N 20  
3TV H3   H  N N 21  
3TV H4   H  N N 22  
3TV H5   H  N N 23  
3TV H6   H  N N 24  
3TV H7   H  N N 25  
3TV H8   H  N N 26  
3TV H9   H  N N 27  
ALA N    N  N N 28  
ALA CA   C  N S 29  
ALA C    C  N N 30  
ALA O    O  N N 31  
ALA CB   C  N N 32  
ALA OXT  O  N N 33  
ALA H    H  N N 34  
ALA H2   H  N N 35  
ALA HA   H  N N 36  
ALA HB1  H  N N 37  
ALA HB2  H  N N 38  
ALA HB3  H  N N 39  
ALA HXT  H  N N 40  
ARG N    N  N N 41  
ARG CA   C  N S 42  
ARG C    C  N N 43  
ARG O    O  N N 44  
ARG CB   C  N N 45  
ARG CG   C  N N 46  
ARG CD   C  N N 47  
ARG NE   N  N N 48  
ARG CZ   C  N N 49  
ARG NH1  N  N N 50  
ARG NH2  N  N N 51  
ARG OXT  O  N N 52  
ARG H    H  N N 53  
ARG H2   H  N N 54  
ARG HA   H  N N 55  
ARG HB2  H  N N 56  
ARG HB3  H  N N 57  
ARG HG2  H  N N 58  
ARG HG3  H  N N 59  
ARG HD2  H  N N 60  
ARG HD3  H  N N 61  
ARG HE   H  N N 62  
ARG HH11 H  N N 63  
ARG HH12 H  N N 64  
ARG HH21 H  N N 65  
ARG HH22 H  N N 66  
ARG HXT  H  N N 67  
ASN N    N  N N 68  
ASN CA   C  N S 69  
ASN C    C  N N 70  
ASN O    O  N N 71  
ASN CB   C  N N 72  
ASN CG   C  N N 73  
ASN OD1  O  N N 74  
ASN ND2  N  N N 75  
ASN OXT  O  N N 76  
ASN H    H  N N 77  
ASN H2   H  N N 78  
ASN HA   H  N N 79  
ASN HB2  H  N N 80  
ASN HB3  H  N N 81  
ASN HD21 H  N N 82  
ASN HD22 H  N N 83  
ASN HXT  H  N N 84  
ASP N    N  N N 85  
ASP CA   C  N S 86  
ASP C    C  N N 87  
ASP O    O  N N 88  
ASP CB   C  N N 89  
ASP CG   C  N N 90  
ASP OD1  O  N N 91  
ASP OD2  O  N N 92  
ASP OXT  O  N N 93  
ASP H    H  N N 94  
ASP H2   H  N N 95  
ASP HA   H  N N 96  
ASP HB2  H  N N 97  
ASP HB3  H  N N 98  
ASP HD2  H  N N 99  
ASP HXT  H  N N 100 
BCN N1   N  N N 101 
BCN C1   C  N N 102 
BCN C2   C  N N 103 
BCN O21  O  N N 104 
BCN O22  O  N N 105 
BCN C3   C  N N 106 
BCN C4   C  N N 107 
BCN O4   O  N N 108 
BCN C5   C  N N 109 
BCN C6   C  N N 110 
BCN O6   O  N N 111 
BCN H11  H  N N 112 
BCN H12  H  N N 113 
BCN HO2  H  N N 114 
BCN H31  H  N N 115 
BCN H32  H  N N 116 
BCN H41  H  N N 117 
BCN H42  H  N N 118 
BCN HO4  H  N N 119 
BCN H51  H  N N 120 
BCN H52  H  N N 121 
BCN H61  H  N N 122 
BCN H62  H  N N 123 
BCN HO6  H  N N 124 
CYS N    N  N N 125 
CYS CA   C  N R 126 
CYS C    C  N N 127 
CYS O    O  N N 128 
CYS CB   C  N N 129 
CYS SG   S  N N 130 
CYS OXT  O  N N 131 
CYS H    H  N N 132 
CYS H2   H  N N 133 
CYS HA   H  N N 134 
CYS HB2  H  N N 135 
CYS HB3  H  N N 136 
CYS HG   H  N N 137 
CYS HXT  H  N N 138 
DMS S    S  N N 139 
DMS O    O  N N 140 
DMS C1   C  N N 141 
DMS C2   C  N N 142 
DMS H11  H  N N 143 
DMS H12  H  N N 144 
DMS H13  H  N N 145 
DMS H21  H  N N 146 
DMS H22  H  N N 147 
DMS H23  H  N N 148 
GLN N    N  N N 149 
GLN CA   C  N S 150 
GLN C    C  N N 151 
GLN O    O  N N 152 
GLN CB   C  N N 153 
GLN CG   C  N N 154 
GLN CD   C  N N 155 
GLN OE1  O  N N 156 
GLN NE2  N  N N 157 
GLN OXT  O  N N 158 
GLN H    H  N N 159 
GLN H2   H  N N 160 
GLN HA   H  N N 161 
GLN HB2  H  N N 162 
GLN HB3  H  N N 163 
GLN HG2  H  N N 164 
GLN HG3  H  N N 165 
GLN HE21 H  N N 166 
GLN HE22 H  N N 167 
GLN HXT  H  N N 168 
GLU N    N  N N 169 
GLU CA   C  N S 170 
GLU C    C  N N 171 
GLU O    O  N N 172 
GLU CB   C  N N 173 
GLU CG   C  N N 174 
GLU CD   C  N N 175 
GLU OE1  O  N N 176 
GLU OE2  O  N N 177 
GLU OXT  O  N N 178 
GLU H    H  N N 179 
GLU H2   H  N N 180 
GLU HA   H  N N 181 
GLU HB2  H  N N 182 
GLU HB3  H  N N 183 
GLU HG2  H  N N 184 
GLU HG3  H  N N 185 
GLU HE2  H  N N 186 
GLU HXT  H  N N 187 
GLY N    N  N N 188 
GLY CA   C  N N 189 
GLY C    C  N N 190 
GLY O    O  N N 191 
GLY OXT  O  N N 192 
GLY H    H  N N 193 
GLY H2   H  N N 194 
GLY HA2  H  N N 195 
GLY HA3  H  N N 196 
GLY HXT  H  N N 197 
HIS N    N  N N 198 
HIS CA   C  N S 199 
HIS C    C  N N 200 
HIS O    O  N N 201 
HIS CB   C  N N 202 
HIS CG   C  Y N 203 
HIS ND1  N  Y N 204 
HIS CD2  C  Y N 205 
HIS CE1  C  Y N 206 
HIS NE2  N  Y N 207 
HIS OXT  O  N N 208 
HIS H    H  N N 209 
HIS H2   H  N N 210 
HIS HA   H  N N 211 
HIS HB2  H  N N 212 
HIS HB3  H  N N 213 
HIS HD1  H  N N 214 
HIS HD2  H  N N 215 
HIS HE1  H  N N 216 
HIS HE2  H  N N 217 
HIS HXT  H  N N 218 
HOH O    O  N N 219 
HOH H1   H  N N 220 
HOH H2   H  N N 221 
ILE N    N  N N 222 
ILE CA   C  N S 223 
ILE C    C  N N 224 
ILE O    O  N N 225 
ILE CB   C  N S 226 
ILE CG1  C  N N 227 
ILE CG2  C  N N 228 
ILE CD1  C  N N 229 
ILE OXT  O  N N 230 
ILE H    H  N N 231 
ILE H2   H  N N 232 
ILE HA   H  N N 233 
ILE HB   H  N N 234 
ILE HG12 H  N N 235 
ILE HG13 H  N N 236 
ILE HG21 H  N N 237 
ILE HG22 H  N N 238 
ILE HG23 H  N N 239 
ILE HD11 H  N N 240 
ILE HD12 H  N N 241 
ILE HD13 H  N N 242 
ILE HXT  H  N N 243 
LEU N    N  N N 244 
LEU CA   C  N S 245 
LEU C    C  N N 246 
LEU O    O  N N 247 
LEU CB   C  N N 248 
LEU CG   C  N N 249 
LEU CD1  C  N N 250 
LEU CD2  C  N N 251 
LEU OXT  O  N N 252 
LEU H    H  N N 253 
LEU H2   H  N N 254 
LEU HA   H  N N 255 
LEU HB2  H  N N 256 
LEU HB3  H  N N 257 
LEU HG   H  N N 258 
LEU HD11 H  N N 259 
LEU HD12 H  N N 260 
LEU HD13 H  N N 261 
LEU HD21 H  N N 262 
LEU HD22 H  N N 263 
LEU HD23 H  N N 264 
LEU HXT  H  N N 265 
LYS N    N  N N 266 
LYS CA   C  N S 267 
LYS C    C  N N 268 
LYS O    O  N N 269 
LYS CB   C  N N 270 
LYS CG   C  N N 271 
LYS CD   C  N N 272 
LYS CE   C  N N 273 
LYS NZ   N  N N 274 
LYS OXT  O  N N 275 
LYS H    H  N N 276 
LYS H2   H  N N 277 
LYS HA   H  N N 278 
LYS HB2  H  N N 279 
LYS HB3  H  N N 280 
LYS HG2  H  N N 281 
LYS HG3  H  N N 282 
LYS HD2  H  N N 283 
LYS HD3  H  N N 284 
LYS HE2  H  N N 285 
LYS HE3  H  N N 286 
LYS HZ1  H  N N 287 
LYS HZ2  H  N N 288 
LYS HZ3  H  N N 289 
LYS HXT  H  N N 290 
MES O1   O  N N 291 
MES C2   C  N N 292 
MES C3   C  N N 293 
MES N4   N  N N 294 
MES C5   C  N N 295 
MES C6   C  N N 296 
MES C7   C  N N 297 
MES C8   C  N N 298 
MES S    S  N N 299 
MES O1S  O  N N 300 
MES O2S  O  N N 301 
MES O3S  O  N N 302 
MES H21  H  N N 303 
MES H22  H  N N 304 
MES H31  H  N N 305 
MES H32  H  N N 306 
MES HN4  H  N N 307 
MES H51  H  N N 308 
MES H52  H  N N 309 
MES H61  H  N N 310 
MES H62  H  N N 311 
MES H71  H  N N 312 
MES H72  H  N N 313 
MES H81  H  N N 314 
MES H82  H  N N 315 
MET N    N  N N 316 
MET CA   C  N S 317 
MET C    C  N N 318 
MET O    O  N N 319 
MET CB   C  N N 320 
MET CG   C  N N 321 
MET SD   S  N N 322 
MET CE   C  N N 323 
MET OXT  O  N N 324 
MET H    H  N N 325 
MET H2   H  N N 326 
MET HA   H  N N 327 
MET HB2  H  N N 328 
MET HB3  H  N N 329 
MET HG2  H  N N 330 
MET HG3  H  N N 331 
MET HE1  H  N N 332 
MET HE2  H  N N 333 
MET HE3  H  N N 334 
MET HXT  H  N N 335 
MLA C1   C  N N 336 
MLA O1A  O  N N 337 
MLA O1B  O  N N 338 
MLA C2   C  N N 339 
MLA C3   C  N N 340 
MLA O3A  O  N N 341 
MLA O3B  O  N N 342 
MLA H1A  H  N N 343 
MLA HC21 H  N N 344 
MLA HC22 H  N N 345 
MLA H3B  H  N N 346 
PHE N    N  N N 347 
PHE CA   C  N S 348 
PHE C    C  N N 349 
PHE O    O  N N 350 
PHE CB   C  N N 351 
PHE CG   C  Y N 352 
PHE CD1  C  Y N 353 
PHE CD2  C  Y N 354 
PHE CE1  C  Y N 355 
PHE CE2  C  Y N 356 
PHE CZ   C  Y N 357 
PHE OXT  O  N N 358 
PHE H    H  N N 359 
PHE H2   H  N N 360 
PHE HA   H  N N 361 
PHE HB2  H  N N 362 
PHE HB3  H  N N 363 
PHE HD1  H  N N 364 
PHE HD2  H  N N 365 
PHE HE1  H  N N 366 
PHE HE2  H  N N 367 
PHE HZ   H  N N 368 
PHE HXT  H  N N 369 
PRO N    N  N N 370 
PRO CA   C  N S 371 
PRO C    C  N N 372 
PRO O    O  N N 373 
PRO CB   C  N N 374 
PRO CG   C  N N 375 
PRO CD   C  N N 376 
PRO OXT  O  N N 377 
PRO H    H  N N 378 
PRO HA   H  N N 379 
PRO HB2  H  N N 380 
PRO HB3  H  N N 381 
PRO HG2  H  N N 382 
PRO HG3  H  N N 383 
PRO HD2  H  N N 384 
PRO HD3  H  N N 385 
PRO HXT  H  N N 386 
SER N    N  N N 387 
SER CA   C  N S 388 
SER C    C  N N 389 
SER O    O  N N 390 
SER CB   C  N N 391 
SER OG   O  N N 392 
SER OXT  O  N N 393 
SER H    H  N N 394 
SER H2   H  N N 395 
SER HA   H  N N 396 
SER HB2  H  N N 397 
SER HB3  H  N N 398 
SER HG   H  N N 399 
SER HXT  H  N N 400 
THR N    N  N N 401 
THR CA   C  N S 402 
THR C    C  N N 403 
THR O    O  N N 404 
THR CB   C  N R 405 
THR OG1  O  N N 406 
THR CG2  C  N N 407 
THR OXT  O  N N 408 
THR H    H  N N 409 
THR H2   H  N N 410 
THR HA   H  N N 411 
THR HB   H  N N 412 
THR HG1  H  N N 413 
THR HG21 H  N N 414 
THR HG22 H  N N 415 
THR HG23 H  N N 416 
THR HXT  H  N N 417 
TRP N    N  N N 418 
TRP CA   C  N S 419 
TRP C    C  N N 420 
TRP O    O  N N 421 
TRP CB   C  N N 422 
TRP CG   C  Y N 423 
TRP CD1  C  Y N 424 
TRP CD2  C  Y N 425 
TRP NE1  N  Y N 426 
TRP CE2  C  Y N 427 
TRP CE3  C  Y N 428 
TRP CZ2  C  Y N 429 
TRP CZ3  C  Y N 430 
TRP CH2  C  Y N 431 
TRP OXT  O  N N 432 
TRP H    H  N N 433 
TRP H2   H  N N 434 
TRP HA   H  N N 435 
TRP HB2  H  N N 436 
TRP HB3  H  N N 437 
TRP HD1  H  N N 438 
TRP HE1  H  N N 439 
TRP HE3  H  N N 440 
TRP HZ2  H  N N 441 
TRP HZ3  H  N N 442 
TRP HH2  H  N N 443 
TRP HXT  H  N N 444 
TYR N    N  N N 445 
TYR CA   C  N S 446 
TYR C    C  N N 447 
TYR O    O  N N 448 
TYR CB   C  N N 449 
TYR CG   C  Y N 450 
TYR CD1  C  Y N 451 
TYR CD2  C  Y N 452 
TYR CE1  C  Y N 453 
TYR CE2  C  Y N 454 
TYR CZ   C  Y N 455 
TYR OH   O  N N 456 
TYR OXT  O  N N 457 
TYR H    H  N N 458 
TYR H2   H  N N 459 
TYR HA   H  N N 460 
TYR HB2  H  N N 461 
TYR HB3  H  N N 462 
TYR HD1  H  N N 463 
TYR HD2  H  N N 464 
TYR HE1  H  N N 465 
TYR HE2  H  N N 466 
TYR HH   H  N N 467 
TYR HXT  H  N N 468 
VAL N    N  N N 469 
VAL CA   C  N S 470 
VAL C    C  N N 471 
VAL O    O  N N 472 
VAL CB   C  N N 473 
VAL CG1  C  N N 474 
VAL CG2  C  N N 475 
VAL OXT  O  N N 476 
VAL H    H  N N 477 
VAL H2   H  N N 478 
VAL HA   H  N N 479 
VAL HB   H  N N 480 
VAL HG11 H  N N 481 
VAL HG12 H  N N 482 
VAL HG13 H  N N 483 
VAL HG21 H  N N 484 
VAL HG22 H  N N 485 
VAL HG23 H  N N 486 
VAL HXT  H  N N 487 
ZN  ZN   ZN N N 488 
# 
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 
3TV C14 C13  sing N N 1   
3TV C13 C12  sing N N 2   
3TV S11 C12  sing N N 3   
3TV S11 C8   sing N N 4   
3TV F18 C7   sing N N 5   
3TV C8  C7   doub Y N 6   
3TV C8  C9   sing Y N 7   
3TV C7  C6   sing Y N 8   
3TV F15 C9   sing N N 9   
3TV C9  C10  doub Y N 10  
3TV C6  F17  sing N N 11  
3TV C6  C5   doub Y N 12  
3TV C10 C5   sing Y N 13  
3TV C10 F16  sing N N 14  
3TV C5  S1   sing N N 15  
3TV N2  S1   sing N N 16  
3TV S1  O4   doub N N 17  
3TV S1  O3   doub N N 18  
3TV C12 H1   sing N N 19  
3TV C12 H2   sing N N 20  
3TV C13 H3   sing N N 21  
3TV C13 H4   sing N N 22  
3TV C14 H5   sing N N 23  
3TV C14 H6   sing N N 24  
3TV C14 H7   sing N N 25  
3TV N2  H8   sing N N 26  
3TV N2  H9   sing N N 27  
ALA N   CA   sing N N 28  
ALA N   H    sing N N 29  
ALA N   H2   sing N N 30  
ALA CA  C    sing N N 31  
ALA CA  CB   sing N N 32  
ALA CA  HA   sing N N 33  
ALA C   O    doub N N 34  
ALA C   OXT  sing N N 35  
ALA CB  HB1  sing N N 36  
ALA CB  HB2  sing N N 37  
ALA CB  HB3  sing N N 38  
ALA OXT HXT  sing N N 39  
ARG N   CA   sing N N 40  
ARG N   H    sing N N 41  
ARG N   H2   sing N N 42  
ARG CA  C    sing N N 43  
ARG CA  CB   sing N N 44  
ARG CA  HA   sing N N 45  
ARG C   O    doub N N 46  
ARG C   OXT  sing N N 47  
ARG CB  CG   sing N N 48  
ARG CB  HB2  sing N N 49  
ARG CB  HB3  sing N N 50  
ARG CG  CD   sing N N 51  
ARG CG  HG2  sing N N 52  
ARG CG  HG3  sing N N 53  
ARG CD  NE   sing N N 54  
ARG CD  HD2  sing N N 55  
ARG CD  HD3  sing N N 56  
ARG NE  CZ   sing N N 57  
ARG NE  HE   sing N N 58  
ARG CZ  NH1  sing N N 59  
ARG CZ  NH2  doub N N 60  
ARG NH1 HH11 sing N N 61  
ARG NH1 HH12 sing N N 62  
ARG NH2 HH21 sing N N 63  
ARG NH2 HH22 sing N N 64  
ARG OXT HXT  sing N N 65  
ASN N   CA   sing N N 66  
ASN N   H    sing N N 67  
ASN N   H2   sing N N 68  
ASN CA  C    sing N N 69  
ASN CA  CB   sing N N 70  
ASN CA  HA   sing N N 71  
ASN C   O    doub N N 72  
ASN C   OXT  sing N N 73  
ASN CB  CG   sing N N 74  
ASN CB  HB2  sing N N 75  
ASN CB  HB3  sing N N 76  
ASN CG  OD1  doub N N 77  
ASN CG  ND2  sing N N 78  
ASN ND2 HD21 sing N N 79  
ASN ND2 HD22 sing N N 80  
ASN OXT HXT  sing N N 81  
ASP N   CA   sing N N 82  
ASP N   H    sing N N 83  
ASP N   H2   sing N N 84  
ASP CA  C    sing N N 85  
ASP CA  CB   sing N N 86  
ASP CA  HA   sing N N 87  
ASP C   O    doub N N 88  
ASP C   OXT  sing N N 89  
ASP CB  CG   sing N N 90  
ASP CB  HB2  sing N N 91  
ASP CB  HB3  sing N N 92  
ASP CG  OD1  doub N N 93  
ASP CG  OD2  sing N N 94  
ASP OD2 HD2  sing N N 95  
ASP OXT HXT  sing N N 96  
BCN N1  C1   sing N N 97  
BCN N1  C3   sing N N 98  
BCN N1  C5   sing N N 99  
BCN C1  C2   sing N N 100 
BCN C1  H11  sing N N 101 
BCN C1  H12  sing N N 102 
BCN C2  O21  doub N N 103 
BCN C2  O22  sing N N 104 
BCN O22 HO2  sing N N 105 
BCN C3  C4   sing N N 106 
BCN C3  H31  sing N N 107 
BCN C3  H32  sing N N 108 
BCN C4  O4   sing N N 109 
BCN C4  H41  sing N N 110 
BCN C4  H42  sing N N 111 
BCN O4  HO4  sing N N 112 
BCN C5  C6   sing N N 113 
BCN C5  H51  sing N N 114 
BCN C5  H52  sing N N 115 
BCN C6  O6   sing N N 116 
BCN C6  H61  sing N N 117 
BCN C6  H62  sing N N 118 
BCN O6  HO6  sing N N 119 
CYS N   CA   sing N N 120 
CYS N   H    sing N N 121 
CYS N   H2   sing N N 122 
CYS CA  C    sing N N 123 
CYS CA  CB   sing N N 124 
CYS CA  HA   sing N N 125 
CYS C   O    doub N N 126 
CYS C   OXT  sing N N 127 
CYS CB  SG   sing N N 128 
CYS CB  HB2  sing N N 129 
CYS CB  HB3  sing N N 130 
CYS SG  HG   sing N N 131 
CYS OXT HXT  sing N N 132 
DMS S   O    doub N N 133 
DMS S   C1   sing N N 134 
DMS S   C2   sing N N 135 
DMS C1  H11  sing N N 136 
DMS C1  H12  sing N N 137 
DMS C1  H13  sing N N 138 
DMS C2  H21  sing N N 139 
DMS C2  H22  sing N N 140 
DMS C2  H23  sing N N 141 
GLN N   CA   sing N N 142 
GLN N   H    sing N N 143 
GLN N   H2   sing N N 144 
GLN CA  C    sing N N 145 
GLN CA  CB   sing N N 146 
GLN CA  HA   sing N N 147 
GLN C   O    doub N N 148 
GLN C   OXT  sing N N 149 
GLN CB  CG   sing N N 150 
GLN CB  HB2  sing N N 151 
GLN CB  HB3  sing N N 152 
GLN CG  CD   sing N N 153 
GLN CG  HG2  sing N N 154 
GLN CG  HG3  sing N N 155 
GLN CD  OE1  doub N N 156 
GLN CD  NE2  sing N N 157 
GLN NE2 HE21 sing N N 158 
GLN NE2 HE22 sing N N 159 
GLN OXT HXT  sing N N 160 
GLU N   CA   sing N N 161 
GLU N   H    sing N N 162 
GLU N   H2   sing N N 163 
GLU CA  C    sing N N 164 
GLU CA  CB   sing N N 165 
GLU CA  HA   sing N N 166 
GLU C   O    doub N N 167 
GLU C   OXT  sing N N 168 
GLU CB  CG   sing N N 169 
GLU CB  HB2  sing N N 170 
GLU CB  HB3  sing N N 171 
GLU CG  CD   sing N N 172 
GLU CG  HG2  sing N N 173 
GLU CG  HG3  sing N N 174 
GLU CD  OE1  doub N N 175 
GLU CD  OE2  sing N N 176 
GLU OE2 HE2  sing N N 177 
GLU OXT HXT  sing N N 178 
GLY N   CA   sing N N 179 
GLY N   H    sing N N 180 
GLY N   H2   sing N N 181 
GLY CA  C    sing N N 182 
GLY CA  HA2  sing N N 183 
GLY CA  HA3  sing N N 184 
GLY C   O    doub N N 185 
GLY C   OXT  sing N N 186 
GLY OXT HXT  sing N N 187 
HIS N   CA   sing N N 188 
HIS N   H    sing N N 189 
HIS N   H2   sing N N 190 
HIS CA  C    sing N N 191 
HIS CA  CB   sing N N 192 
HIS CA  HA   sing N N 193 
HIS C   O    doub N N 194 
HIS C   OXT  sing N N 195 
HIS CB  CG   sing N N 196 
HIS CB  HB2  sing N N 197 
HIS CB  HB3  sing N N 198 
HIS CG  ND1  sing Y N 199 
HIS CG  CD2  doub Y N 200 
HIS ND1 CE1  doub Y N 201 
HIS ND1 HD1  sing N N 202 
HIS CD2 NE2  sing Y N 203 
HIS CD2 HD2  sing N N 204 
HIS CE1 NE2  sing Y N 205 
HIS CE1 HE1  sing N N 206 
HIS NE2 HE2  sing N N 207 
HIS OXT HXT  sing N N 208 
HOH O   H1   sing N N 209 
HOH O   H2   sing N N 210 
ILE N   CA   sing N N 211 
ILE N   H    sing N N 212 
ILE N   H2   sing N N 213 
ILE CA  C    sing N N 214 
ILE CA  CB   sing N N 215 
ILE CA  HA   sing N N 216 
ILE C   O    doub N N 217 
ILE C   OXT  sing N N 218 
ILE CB  CG1  sing N N 219 
ILE CB  CG2  sing N N 220 
ILE CB  HB   sing N N 221 
ILE CG1 CD1  sing N N 222 
ILE CG1 HG12 sing N N 223 
ILE CG1 HG13 sing N N 224 
ILE CG2 HG21 sing N N 225 
ILE CG2 HG22 sing N N 226 
ILE CG2 HG23 sing N N 227 
ILE CD1 HD11 sing N N 228 
ILE CD1 HD12 sing N N 229 
ILE CD1 HD13 sing N N 230 
ILE OXT HXT  sing N N 231 
LEU N   CA   sing N N 232 
LEU N   H    sing N N 233 
LEU N   H2   sing N N 234 
LEU CA  C    sing N N 235 
LEU CA  CB   sing N N 236 
LEU CA  HA   sing N N 237 
LEU C   O    doub N N 238 
LEU C   OXT  sing N N 239 
LEU CB  CG   sing N N 240 
LEU CB  HB2  sing N N 241 
LEU CB  HB3  sing N N 242 
LEU CG  CD1  sing N N 243 
LEU CG  CD2  sing N N 244 
LEU CG  HG   sing N N 245 
LEU CD1 HD11 sing N N 246 
LEU CD1 HD12 sing N N 247 
LEU CD1 HD13 sing N N 248 
LEU CD2 HD21 sing N N 249 
LEU CD2 HD22 sing N N 250 
LEU CD2 HD23 sing N N 251 
LEU OXT HXT  sing N N 252 
LYS N   CA   sing N N 253 
LYS N   H    sing N N 254 
LYS N   H2   sing N N 255 
LYS CA  C    sing N N 256 
LYS CA  CB   sing N N 257 
LYS CA  HA   sing N N 258 
LYS C   O    doub N N 259 
LYS C   OXT  sing N N 260 
LYS CB  CG   sing N N 261 
LYS CB  HB2  sing N N 262 
LYS CB  HB3  sing N N 263 
LYS CG  CD   sing N N 264 
LYS CG  HG2  sing N N 265 
LYS CG  HG3  sing N N 266 
LYS CD  CE   sing N N 267 
LYS CD  HD2  sing N N 268 
LYS CD  HD3  sing N N 269 
LYS CE  NZ   sing N N 270 
LYS CE  HE2  sing N N 271 
LYS CE  HE3  sing N N 272 
LYS NZ  HZ1  sing N N 273 
LYS NZ  HZ2  sing N N 274 
LYS NZ  HZ3  sing N N 275 
LYS OXT HXT  sing N N 276 
MES O1  C2   sing N N 277 
MES O1  C6   sing N N 278 
MES C2  C3   sing N N 279 
MES C2  H21  sing N N 280 
MES C2  H22  sing N N 281 
MES C3  N4   sing N N 282 
MES C3  H31  sing N N 283 
MES C3  H32  sing N N 284 
MES N4  C5   sing N N 285 
MES N4  C7   sing N N 286 
MES N4  HN4  sing N N 287 
MES C5  C6   sing N N 288 
MES C5  H51  sing N N 289 
MES C5  H52  sing N N 290 
MES C6  H61  sing N N 291 
MES C6  H62  sing N N 292 
MES C7  C8   sing N N 293 
MES C7  H71  sing N N 294 
MES C7  H72  sing N N 295 
MES C8  S    sing N N 296 
MES C8  H81  sing N N 297 
MES C8  H82  sing N N 298 
MES S   O1S  doub N N 299 
MES S   O2S  doub N N 300 
MES S   O3S  sing N N 301 
MET N   CA   sing N N 302 
MET N   H    sing N N 303 
MET N   H2   sing N N 304 
MET CA  C    sing N N 305 
MET CA  CB   sing N N 306 
MET CA  HA   sing N N 307 
MET C   O    doub N N 308 
MET C   OXT  sing N N 309 
MET CB  CG   sing N N 310 
MET CB  HB2  sing N N 311 
MET CB  HB3  sing N N 312 
MET CG  SD   sing N N 313 
MET CG  HG2  sing N N 314 
MET CG  HG3  sing N N 315 
MET SD  CE   sing N N 316 
MET CE  HE1  sing N N 317 
MET CE  HE2  sing N N 318 
MET CE  HE3  sing N N 319 
MET OXT HXT  sing N N 320 
MLA C1  O1A  sing N N 321 
MLA C1  O1B  doub N N 322 
MLA C1  C2   sing N N 323 
MLA O1A H1A  sing N N 324 
MLA C2  C3   sing N N 325 
MLA C2  HC21 sing N N 326 
MLA C2  HC22 sing N N 327 
MLA C3  O3A  doub N N 328 
MLA C3  O3B  sing N N 329 
MLA O3B H3B  sing N N 330 
PHE N   CA   sing N N 331 
PHE N   H    sing N N 332 
PHE N   H2   sing N N 333 
PHE CA  C    sing N N 334 
PHE CA  CB   sing N N 335 
PHE CA  HA   sing N N 336 
PHE C   O    doub N N 337 
PHE C   OXT  sing N N 338 
PHE CB  CG   sing N N 339 
PHE CB  HB2  sing N N 340 
PHE CB  HB3  sing N N 341 
PHE CG  CD1  doub Y N 342 
PHE CG  CD2  sing Y N 343 
PHE CD1 CE1  sing Y N 344 
PHE CD1 HD1  sing N N 345 
PHE CD2 CE2  doub Y N 346 
PHE CD2 HD2  sing N N 347 
PHE CE1 CZ   doub Y N 348 
PHE CE1 HE1  sing N N 349 
PHE CE2 CZ   sing Y N 350 
PHE CE2 HE2  sing N N 351 
PHE CZ  HZ   sing N N 352 
PHE OXT HXT  sing N N 353 
PRO N   CA   sing N N 354 
PRO N   CD   sing N N 355 
PRO N   H    sing N N 356 
PRO CA  C    sing N N 357 
PRO CA  CB   sing N N 358 
PRO CA  HA   sing N N 359 
PRO C   O    doub N N 360 
PRO C   OXT  sing N N 361 
PRO CB  CG   sing N N 362 
PRO CB  HB2  sing N N 363 
PRO CB  HB3  sing N N 364 
PRO CG  CD   sing N N 365 
PRO CG  HG2  sing N N 366 
PRO CG  HG3  sing N N 367 
PRO CD  HD2  sing N N 368 
PRO CD  HD3  sing N N 369 
PRO OXT HXT  sing N N 370 
SER N   CA   sing N N 371 
SER N   H    sing N N 372 
SER N   H2   sing N N 373 
SER CA  C    sing N N 374 
SER CA  CB   sing N N 375 
SER CA  HA   sing N N 376 
SER C   O    doub N N 377 
SER C   OXT  sing N N 378 
SER CB  OG   sing N N 379 
SER CB  HB2  sing N N 380 
SER CB  HB3  sing N N 381 
SER OG  HG   sing N N 382 
SER OXT HXT  sing N N 383 
THR N   CA   sing N N 384 
THR N   H    sing N N 385 
THR N   H2   sing N N 386 
THR CA  C    sing N N 387 
THR CA  CB   sing N N 388 
THR CA  HA   sing N N 389 
THR C   O    doub N N 390 
THR C   OXT  sing N N 391 
THR CB  OG1  sing N N 392 
THR CB  CG2  sing N N 393 
THR CB  HB   sing N N 394 
THR OG1 HG1  sing N N 395 
THR CG2 HG21 sing N N 396 
THR CG2 HG22 sing N N 397 
THR CG2 HG23 sing N N 398 
THR OXT HXT  sing N N 399 
TRP N   CA   sing N N 400 
TRP N   H    sing N N 401 
TRP N   H2   sing N N 402 
TRP CA  C    sing N N 403 
TRP CA  CB   sing N N 404 
TRP CA  HA   sing N N 405 
TRP C   O    doub N N 406 
TRP C   OXT  sing N N 407 
TRP CB  CG   sing N N 408 
TRP CB  HB2  sing N N 409 
TRP CB  HB3  sing N N 410 
TRP CG  CD1  doub Y N 411 
TRP CG  CD2  sing Y N 412 
TRP CD1 NE1  sing Y N 413 
TRP CD1 HD1  sing N N 414 
TRP CD2 CE2  doub Y N 415 
TRP CD2 CE3  sing Y N 416 
TRP NE1 CE2  sing Y N 417 
TRP NE1 HE1  sing N N 418 
TRP CE2 CZ2  sing Y N 419 
TRP CE3 CZ3  doub Y N 420 
TRP CE3 HE3  sing N N 421 
TRP CZ2 CH2  doub Y N 422 
TRP CZ2 HZ2  sing N N 423 
TRP CZ3 CH2  sing Y N 424 
TRP CZ3 HZ3  sing N N 425 
TRP CH2 HH2  sing N N 426 
TRP OXT HXT  sing N N 427 
TYR N   CA   sing N N 428 
TYR N   H    sing N N 429 
TYR N   H2   sing N N 430 
TYR CA  C    sing N N 431 
TYR CA  CB   sing N N 432 
TYR CA  HA   sing N N 433 
TYR C   O    doub N N 434 
TYR C   OXT  sing N N 435 
TYR CB  CG   sing N N 436 
TYR CB  HB2  sing N N 437 
TYR CB  HB3  sing N N 438 
TYR CG  CD1  doub Y N 439 
TYR CG  CD2  sing Y N 440 
TYR CD1 CE1  sing Y N 441 
TYR CD1 HD1  sing N N 442 
TYR CD2 CE2  doub Y N 443 
TYR CD2 HD2  sing N N 444 
TYR CE1 CZ   doub Y N 445 
TYR CE1 HE1  sing N N 446 
TYR CE2 CZ   sing Y N 447 
TYR CE2 HE2  sing N N 448 
TYR CZ  OH   sing N N 449 
TYR OH  HH   sing N N 450 
TYR OXT HXT  sing N N 451 
VAL N   CA   sing N N 452 
VAL N   H    sing N N 453 
VAL N   H2   sing N N 454 
VAL CA  C    sing N N 455 
VAL CA  CB   sing N N 456 
VAL CA  HA   sing N N 457 
VAL C   O    doub N N 458 
VAL C   OXT  sing N N 459 
VAL CB  CG1  sing N N 460 
VAL CB  CG2  sing N N 461 
VAL CB  HB   sing N N 462 
VAL CG1 HG11 sing N N 463 
VAL CG1 HG12 sing N N 464 
VAL CG1 HG13 sing N N 465 
VAL CG2 HG21 sing N N 466 
VAL CG2 HG22 sing N N 467 
VAL CG2 HG23 sing N N 468 
VAL OXT HXT  sing N N 469 
# 
_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   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    4WW6 
_atom_sites.fract_transf_matrix[1][1]   0.023689 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006032 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024375 
_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]   0.014377 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 30.380  3.673   8.897   1.00 32.37  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 30.553  2.251   8.402   1.00 21.86  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.165  1.168   9.412   1.00 17.93  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.526  -0.013  9.323   1.00 22.11  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 31.951  1.980   8.004   1.00 29.36  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 32.066  1.494   6.607   1.00 39.54  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 33.107  1.815   5.816   1.00 75.46  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 31.213  0.684   5.840   1.00 58.47  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 32.943  1.241   4.601   1.00 101.86 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 31.781  0.552   4.616   1.00 105.69 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.347  1.530   10.353  1.00 15.46  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.739  0.516   11.223  1.00 12.99  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.676  -0.280  10.407  1.00 12.54  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.124  0.180   9.413   1.00 13.74  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.063  1.212   12.415  1.00 12.69  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 26.847  2.037   12.042  1.00 11.86  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 26.792  3.373   11.812  1.00 13.46  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.502  1.575   12.032  1.00 11.65  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.540  3.788   11.553  1.00 13.65  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.694  2.691   11.676  1.00 12.61  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 24.902  0.338   12.249  1.00 11.49  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.311  2.598   11.592  1.00 13.11  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.500  0.240   12.121  1.00 12.28  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.762  1.360   11.767  1.00 12.98  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.426  -1.490  10.937  1.00 11.75  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.388  -2.302  10.297  1.00 12.02  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.050  -3.445  11.230  1.00 11.32  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.057  -3.330  12.455  1.00 11.60  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.723  -4.559  10.579  1.00 12.59  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.236  -5.757  11.303  1.00 13.21  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.100  -6.988  10.968  1.00 15.67  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 25.700  -8.119  11.251  1.00 20.19  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 23.773  -6.040  11.050  1.00 12.27  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 22.944  -4.936  11.633  1.00 10.41  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.599  -4.987  13.026  1.00 10.66  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.467  -3.919  10.855  1.00 11.49  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.759  -3.990  13.533  1.00 9.71   ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.646  -2.947  11.390  1.00 10.83  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.281  -2.999  12.739  1.00 9.52   ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.439  -2.036  13.209  1.00 10.42  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.254  -6.762  10.355  1.00 16.15  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.105  -7.852  9.957   1.00 20.48  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.043  -8.229  11.071  1.00 15.35  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.109  -7.578  12.107  1.00 22.87  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 29.756  -9.315  10.845  1.00 26.85  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 30.843  -9.755  11.747  1.00 26.14  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 31.865  -8.679  12.008  1.00 29.44  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.404  -8.622  13.086  1.00 25.49  ? 9   LYS A O   1 
ATOM   49   N  N   . HIS A 1 10  ? 32.161  -7.863  11.034  1.00 17.42  ? 10  HIS A N   1 
ATOM   50   C  CA  . HIS A 1 10  ? 33.240  -6.926  11.214  1.00 15.25  ? 10  HIS A CA  1 
ATOM   51   C  C   . HIS A 1 10  ? 32.807  -5.571  11.682  1.00 15.72  ? 10  HIS A C   1 
ATOM   52   O  O   . HIS A 1 10  ? 33.612  -4.771  12.100  1.00 18.24  ? 10  HIS A O   1 
ATOM   53   C  CB  . HIS A 1 10  ? 34.141  -6.881  9.980   1.00 16.62  ? 10  HIS A CB  1 
ATOM   54   C  CG  . HIS A 1 10  ? 34.687  -8.254  9.609   1.00 17.27  ? 10  HIS A CG  1 
ATOM   55   N  ND1 . HIS A 1 10  ? 35.578  -8.880  10.412  1.00 17.51  ? 10  HIS A ND1 1 
ATOM   56   C  CD2 . HIS A 1 10  ? 34.318  -9.153  8.612   1.00 18.99  ? 10  HIS A CD2 1 
ATOM   57   C  CE1 . HIS A 1 10  ? 35.862  -10.120 9.918   1.00 16.24  ? 10  HIS A CE1 1 
ATOM   58   N  NE2 . HIS A 1 10  ? 35.085  -10.270 8.762   1.00 20.87  ? 10  HIS A NE2 1 
ATOM   59   N  N   . ASN A 1 11  ? 31.482  -5.256  11.632  1.00 13.91  ? 11  ASN A N   1 
ATOM   60   C  CA  . ASN A 1 11  ? 31.045  -3.917  11.960  1.00 13.50  ? 11  ASN A CA  1 
ATOM   61   C  C   . ASN A 1 11  ? 29.727  -3.947  12.704  1.00 11.69  ? 11  ASN A C   1 
ATOM   62   O  O   . ASN A 1 11  ? 29.070  -2.908  12.811  1.00 13.46  ? 11  ASN A O   1 
ATOM   63   C  CB  . ASN A 1 11  ? 30.859  -3.115  10.712  1.00 14.33  ? 11  ASN A CB  1 
ATOM   64   C  CG  . ASN A 1 11  ? 29.801  -3.645  9.736   1.00 13.69  ? 11  ASN A CG  1 
ATOM   65   O  OD1 . ASN A 1 11  ? 29.224  -4.684  9.989   1.00 15.59  ? 11  ASN A OD1 1 
ATOM   66   N  ND2 . ASN A 1 11  ? 29.492  -2.914  8.703   1.00 17.99  ? 11  ASN A ND2 1 
ATOM   67   N  N   . GLY A 1 12  ? 29.421  -5.050  13.338  1.00 12.41  ? 12  GLY A N   1 
ATOM   68   C  CA  . GLY A 1 12  ? 28.157  -5.201  14.048  1.00 13.11  ? 12  GLY A CA  1 
ATOM   69   C  C   . GLY A 1 12  ? 28.137  -4.730  15.463  1.00 11.49  ? 12  GLY A C   1 
ATOM   70   O  O   . GLY A 1 12  ? 29.043  -4.025  15.906  1.00 11.61  ? 12  GLY A O   1 
ATOM   71   N  N   . PRO A 1 13  ? 27.069  -4.986  16.186  1.00 11.28  ? 13  PRO A N   1 
ATOM   72   C  CA  . PRO A 1 13  ? 26.811  -4.391  17.493  1.00 11.01  ? 13  PRO A CA  1 
ATOM   73   C  C   . PRO A 1 13  ? 27.938  -4.431  18.442  1.00 10.92  ? 13  PRO A C   1 
ATOM   74   O  O   . PRO A 1 13  ? 28.128  -3.464  19.232  1.00 11.96  ? 13  PRO A O   1 
ATOM   75   C  CB  . PRO A 1 13  ? 25.622  -5.220  17.974  1.00 11.96  ? 13  PRO A CB  1 
ATOM   76   C  CG  . PRO A 1 13  ? 24.830  -5.455  16.746  1.00 12.10  ? 13  PRO A CG  1 
ATOM   77   C  CD  . PRO A 1 13  ? 25.869  -5.727  15.669  1.00 11.75  ? 13  PRO A CD  1 
ATOM   78   N  N   . GLU A 1 14  ? 28.755  -5.492  18.481  1.00 12.28  ? 14  GLU A N   1 
ATOM   79   C  CA  . GLU A 1 14  ? 29.850  -5.554  19.427  1.00 14.04  ? 14  GLU A CA  1 
ATOM   80   C  C   . GLU A 1 14  ? 30.994  -4.586  19.082  1.00 12.65  ? 14  GLU A C   1 
ATOM   81   O  O   . GLU A 1 14  ? 31.872  -4.374  19.931  1.00 14.13  ? 14  GLU A O   1 
ATOM   82   C  CB  . GLU A 1 14  ? 30.311  -7.014  19.531  1.00 19.69  ? 14  GLU A CB  1 
ATOM   83   C  CG  . GLU A 1 14  ? 30.945  -7.553  18.257  1.00 20.29  ? 14  GLU A CG  1 
ATOM   84   C  CD  . GLU A 1 14  ? 30.147  -8.141  17.022  1.00 25.91  ? 14  GLU A CD  1 
ATOM   85   O  OE1 . GLU A 1 14  ? 28.956  -7.799  16.863  1.00 22.36  ? 14  GLU A OE1 1 
ATOM   86   O  OE2 . GLU A 1 14  ? 30.745  -8.920  16.249  1.00 27.80  ? 14  GLU A OE2 1 
ATOM   87   N  N   . HIS A 1 15  ? 30.993  -4.020  17.876  1.00 11.35  ? 15  HIS A N   1 
ATOM   88   C  CA  . HIS A 1 15  ? 32.005  -3.080  17.487  1.00 11.43  ? 15  HIS A CA  1 
ATOM   89   C  C   . HIS A 1 15  ? 31.587  -1.633  17.664  1.00 11.05  ? 15  HIS A C   1 
ATOM   90   O  O   . HIS A 1 15  ? 32.416  -0.716  17.583  1.00 11.56  ? 15  HIS A O   1 
ATOM   91   C  CB  . HIS A 1 15  ? 32.331  -3.279  16.003  1.00 12.95  ? 15  HIS A CB  1 
ATOM   92   C  CG  . HIS A 1 15  ? 33.031  -4.564  15.727  1.00 14.80  ? 15  HIS A CG  1 
ATOM   93   N  ND1 . HIS A 1 15  ? 34.389  -4.712  15.880  1.00 17.40  ? 15  HIS A ND1 1 
ATOM   94   C  CD2 . HIS A 1 15  ? 32.521  -5.785  15.330  1.00 17.20  ? 15  HIS A CD2 1 
ATOM   95   C  CE1 . HIS A 1 15  ? 34.609  -6.027  15.729  1.00 19.01  ? 15  HIS A CE1 1 
ATOM   96   N  NE2 . HIS A 1 15  ? 33.562  -6.642  15.243  1.00 20.92  ? 15  HIS A NE2 1 
ATOM   97   N  N   . TRP A 1 16  ? 30.290  -1.354  17.809  1.00 10.32  ? 16  TRP A N   1 
ATOM   98   C  CA  . TRP A 1 16  ? 29.793  0.010   17.723  1.00 10.09  ? 16  TRP A CA  1 
ATOM   99   C  C   . TRP A 1 16  ? 30.395  0.964   18.751  1.00 10.23  ? 16  TRP A C   1 
ATOM   100  O  O   . TRP A 1 16  ? 30.524  2.156   18.464  1.00 10.60  ? 16  TRP A O   1 
ATOM   101  C  CB  . TRP A 1 16  ? 28.253  -0.006  17.884  1.00 10.40  ? 16  TRP A CB  1 
ATOM   102  C  CG  . TRP A 1 16  ? 27.543  -0.673  16.744  1.00 9.54   ? 16  TRP A CG  1 
ATOM   103  C  CD1 . TRP A 1 16  ? 28.030  -1.102  15.537  1.00 10.35  ? 16  TRP A CD1 1 
ATOM   104  C  CD2 . TRP A 1 16  ? 26.135  -0.970  16.744  1.00 9.24   ? 16  TRP A CD2 1 
ATOM   105  N  NE1 . TRP A 1 16  ? 27.064  -1.651  14.772  1.00 10.20  ? 16  TRP A NE1 1 
ATOM   106  C  CE2 . TRP A 1 16  ? 25.859  -1.579  15.458  1.00 9.43   ? 16  TRP A CE2 1 
ATOM   107  C  CE3 . TRP A 1 16  ? 25.120  -0.809  17.652  1.00 9.20   ? 16  TRP A CE3 1 
ATOM   108  C  CZ2 . TRP A 1 16  ? 24.590  -2.030  15.117  1.00 9.22   ? 16  TRP A CZ2 1 
ATOM   109  C  CZ3 . TRP A 1 16  ? 23.844  -1.238  17.315  1.00 9.27   ? 16  TRP A CZ3 1 
ATOM   110  C  CH2 . TRP A 1 16  ? 23.591  -1.816  16.055  1.00 9.44   ? 16  TRP A CH2 1 
ATOM   111  N  N   . HIS A 1 17  ? 30.728  0.438   19.915  1.00 10.25  ? 17  HIS A N   1 
ATOM   112  C  CA  . HIS A 1 17  ? 31.271  1.275   20.966  1.00 11.10  ? 17  HIS A CA  1 
ATOM   113  C  C   . HIS A 1 17  ? 32.523  2.028   20.551  1.00 11.65  ? 17  HIS A C   1 
ATOM   114  O  O   . HIS A 1 17  ? 32.806  3.079   21.134  1.00 12.44  ? 17  HIS A O   1 
ATOM   115  C  CB  . HIS A 1 17  ? 31.537  0.489   22.232  1.00 11.83  ? 17  HIS A CB  1 
ATOM   116  C  CG  . HIS A 1 17  ? 32.749  -0.398  22.111  1.00 12.35  ? 17  HIS A CG  1 
ATOM   117  N  ND1 . HIS A 1 17  ? 33.959  -0.007  22.595  1.00 15.42  ? 17  HIS A ND1 1 
ATOM   118  C  CD2 . HIS A 1 17  ? 32.903  -1.589  21.499  1.00 13.19  ? 17  HIS A CD2 1 
ATOM   119  C  CE1 . HIS A 1 17  ? 34.823  -0.965  22.326  1.00 15.24  ? 17  HIS A CE1 1 
ATOM   120  N  NE2 . HIS A 1 17  ? 34.262  -1.930  21.660  1.00 14.79  ? 17  HIS A NE2 1 
ATOM   121  N  N   . LYS A 1 18  ? 33.270  1.501   19.575  1.00 11.61  ? 18  LYS A N   1 
ATOM   122  C  CA  . LYS A 1 18  ? 34.520  2.203   19.209  1.00 13.23  ? 18  LYS A CA  1 
ATOM   123  C  C   . LYS A 1 18  ? 34.249  3.523   18.509  1.00 13.60  ? 18  LYS A C   1 
ATOM   124  O  O   . LYS A 1 18  ? 35.066  4.418   18.558  1.00 17.56  ? 18  LYS A O   1 
ATOM   125  C  CB  . LYS A 1 18  ? 35.332  1.272   18.289  1.00 14.13  ? 18  LYS A CB  1 
ATOM   126  C  CG  . LYS A 1 18  ? 35.837  0.048   19.006  1.00 14.65  ? 18  LYS A CG  1 
ATOM   127  C  CD  . LYS A 1 18  ? 36.590  -0.870  18.085  1.00 15.08  ? 18  LYS A CD  1 
ATOM   128  C  CE  . LYS A 1 18  ? 35.648  -1.816  17.370  1.00 15.79  ? 18  LYS A CE  1 
ATOM   129  N  NZ  . LYS A 1 18  ? 36.312  -2.580  16.264  1.00 15.73  ? 18  LYS A NZ  1 
ATOM   130  N  N   . ASP A 1 19  ? 33.143  3.661   17.798  1.00 11.60  ? 19  ASP A N   1 
ATOM   131  C  CA  . ASP A 1 19  ? 32.750  4.934   17.231  1.00 13.31  ? 19  ASP A CA  1 
ATOM   132  C  C   . ASP A 1 19  ? 31.670  5.655   17.991  1.00 12.11  ? 19  ASP A C   1 
ATOM   133  O  O   . ASP A 1 19  ? 31.534  6.854   17.830  1.00 14.25  ? 19  ASP A O   1 
ATOM   134  C  CB  . ASP A 1 19  ? 32.371  4.787   15.756  1.00 14.91  ? 19  ASP A CB  1 
ATOM   135  C  CG  . ASP A 1 19  ? 33.636  4.493   14.920  1.00 17.97  ? 19  ASP A CG  1 
ATOM   136  O  OD1 . ASP A 1 19  ? 34.354  5.481   14.666  1.00 20.73  ? 19  ASP A OD1 1 
ATOM   137  O  OD2 . ASP A 1 19  ? 34.007  3.283   14.768  1.00 18.40  ? 19  ASP A OD2 1 
ATOM   138  N  N   . PHE A 1 20  ? 30.931  4.942   18.863  1.00 11.59  ? 20  PHE A N   1 
ATOM   139  C  CA  . PHE A 1 20  ? 29.804  5.508   19.545  1.00 11.73  ? 20  PHE A CA  1 
ATOM   140  C  C   . PHE A 1 20  ? 29.907  5.027   20.973  1.00 11.94  ? 20  PHE A C   1 
ATOM   141  O  O   . PHE A 1 20  ? 29.255  4.030   21.391  1.00 11.57  ? 20  PHE A O   1 
ATOM   142  C  CB  . PHE A 1 20  ? 28.497  5.013   18.892  1.00 11.71  ? 20  PHE A CB  1 
ATOM   143  C  CG  . PHE A 1 20  ? 28.426  5.373   17.487  1.00 11.34  ? 20  PHE A CG  1 
ATOM   144  C  CD1 . PHE A 1 20  ? 28.038  6.632   17.101  1.00 13.53  ? 20  PHE A CD1 1 
ATOM   145  C  CD2 . PHE A 1 20  ? 28.821  4.439   16.463  1.00 13.08  ? 20  PHE A CD2 1 
ATOM   146  C  CE1 . PHE A 1 20  ? 28.049  6.996   15.747  1.00 14.21  ? 20  PHE A CE1 1 
ATOM   147  C  CE2 . PHE A 1 20  ? 28.855  4.775   15.136  1.00 13.46  ? 20  PHE A CE2 1 
ATOM   148  C  CZ  . PHE A 1 20  ? 28.446  6.056   14.760  1.00 14.37  ? 20  PHE A CZ  1 
ATOM   149  N  N   . PRO A 1 21  ? 30.782  5.617   21.826  1.00 13.04  ? 21  PRO A N   1 
ATOM   150  C  CA  . PRO A 1 21  ? 31.031  5.098   23.135  1.00 13.44  ? 21  PRO A CA  1 
ATOM   151  C  C   . PRO A 1 21  ? 29.820  5.009   24.074  1.00 11.87  ? 21  PRO A C   1 
ATOM   152  O  O   . PRO A 1 21  ? 29.864  4.234   25.037  1.00 12.88  ? 21  PRO A O   1 
ATOM   153  C  CB  . PRO A 1 21  ? 32.153  6.057   23.742  1.00 17.90  ? 21  PRO A CB  1 
ATOM   154  C  CG  . PRO A 1 21  ? 32.291  7.115   22.783  1.00 23.32  ? 21  PRO A CG  1 
ATOM   155  C  CD  . PRO A 1 21  ? 31.745  6.680   21.469  1.00 15.19  ? 21  PRO A CD  1 
ATOM   156  N  N   A ILE A 1 22  ? 28.756  5.787   23.860  0.50 11.47  ? 22  ILE A N   1 
ATOM   157  N  N   B ILE A 1 22  ? 28.780  5.792   23.748  0.50 11.37  ? 22  ILE A N   1 
ATOM   158  C  CA  A ILE A 1 22  ? 27.528  5.621   24.682  0.50 10.68  ? 22  ILE A CA  1 
ATOM   159  C  CA  B ILE A 1 22  ? 27.485  5.722   24.461  0.50 10.67  ? 22  ILE A CA  1 
ATOM   160  C  C   A ILE A 1 22  ? 26.920  4.254   24.475  0.50 10.37  ? 22  ILE A C   1 
ATOM   161  C  C   B ILE A 1 22  ? 26.893  4.308   24.412  0.50 10.60  ? 22  ILE A C   1 
ATOM   162  O  O   A ILE A 1 22  ? 25.997  3.913   25.196  0.50 11.10  ? 22  ILE A O   1 
ATOM   163  O  O   B ILE A 1 22  ? 26.021  3.958   25.232  0.50 11.24  ? 22  ILE A O   1 
ATOM   164  C  CB  A ILE A 1 22  ? 26.527  6.678   24.253  0.50 10.12  ? 22  ILE A CB  1 
ATOM   165  C  CB  B ILE A 1 22  ? 26.571  6.865   23.964  0.50 10.96  ? 22  ILE A CB  1 
ATOM   166  C  CG1 A ILE A 1 22  ? 25.438  6.966   25.276  0.50 9.97   ? 22  ILE A CG1 1 
ATOM   167  C  CG1 B ILE A 1 22  ? 25.460  7.195   24.966  0.50 12.30  ? 22  ILE A CG1 1 
ATOM   168  C  CG2 A ILE A 1 22  ? 25.841  6.260   22.954  0.50 10.96  ? 22  ILE A CG2 1 
ATOM   169  C  CG2 B ILE A 1 22  ? 25.952  6.571   22.599  0.50 10.28  ? 22  ILE A CG2 1 
ATOM   170  C  CD1 A ILE A 1 22  ? 24.618  8.162   24.802  0.50 11.25  ? 22  ILE A CD1 1 
ATOM   171  C  CD1 B ILE A 1 22  ? 25.921  7.461   26.391  0.50 17.58  ? 22  ILE A CD1 1 
ATOM   172  N  N   . ALA A 1 23  ? 27.429  3.448   23.518  1.00 10.64  ? 23  ALA A N   1 
ATOM   173  C  CA  . ALA A 1 23  ? 26.964  2.054   23.420  1.00 10.05  ? 23  ALA A CA  1 
ATOM   174  C  C   . ALA A 1 23  ? 27.070  1.342   24.747  1.00 11.62  ? 23  ALA A C   1 
ATOM   175  O  O   . ALA A 1 23  ? 26.358  0.345   24.946  1.00 11.50  ? 23  ALA A O   1 
ATOM   176  C  CB  . ALA A 1 23  ? 27.818  1.304   22.415  1.00 11.02  ? 23  ALA A CB  1 
ATOM   177  N  N   . LYS A 1 24  ? 28.016  1.778   25.642  1.00 11.48  ? 24  LYS A N   1 
ATOM   178  C  CA  . LYS A 1 24  ? 28.217  1.181   26.961  1.00 12.46  ? 24  LYS A CA  1 
ATOM   179  C  C   . LYS A 1 24  ? 27.557  2.050   28.014  1.00 13.03  ? 24  LYS A C   1 
ATOM   180  O  O   . LYS A 1 24  ? 27.944  1.961   29.183  1.00 15.45  ? 24  LYS A O   1 
ATOM   181  C  CB  . LYS A 1 24  ? 29.676  0.913   27.253  1.00 13.20  ? 24  LYS A CB  1 
ATOM   182  C  CG  . LYS A 1 24  ? 30.314  -0.060  26.256  1.00 15.03  ? 24  LYS A CG  1 
ATOM   183  C  CD  . LYS A 1 24  ? 31.771  -0.272  26.565  1.00 19.59  ? 24  LYS A CD  1 
ATOM   184  C  CE  . LYS A 1 24  ? 32.493  -1.267  25.664  1.00 21.68  ? 24  LYS A CE  1 
ATOM   185  N  NZ  . LYS A 1 24  ? 32.113  -2.655  25.985  1.00 28.74  ? 24  LYS A NZ  1 
ATOM   186  N  N   . GLY A 1 25  ? 26.561  2.842   27.674  1.00 12.76  ? 25  GLY A N   1 
ATOM   187  C  CA  . GLY A 1 25  ? 25.932  3.793   28.578  1.00 14.15  ? 25  GLY A CA  1 
ATOM   188  C  C   . GLY A 1 25  ? 24.972  3.167   29.579  1.00 12.45  ? 25  GLY A C   1 
ATOM   189  O  O   . GLY A 1 25  ? 24.776  1.990   29.673  1.00 13.43  ? 25  GLY A O   1 
ATOM   190  N  N   . GLU A 1 26  ? 24.334  4.071   30.312  1.00 13.17  ? 26  GLU A N   1 
ATOM   191  C  CA  . GLU A 1 26  ? 23.468  3.729   31.433  1.00 13.75  ? 26  GLU A CA  1 
ATOM   192  C  C   . GLU A 1 26  ? 22.054  3.444   31.025  1.00 12.17  ? 26  GLU A C   1 
ATOM   193  O  O   . GLU A 1 26  ? 21.315  2.902   31.877  1.00 13.76  ? 26  GLU A O   1 
ATOM   194  C  CB  . GLU A 1 26  ? 23.488  4.864   32.473  1.00 18.60  ? 26  GLU A CB  1 
ATOM   195  C  CG  . GLU A 1 26  ? 24.915  5.080   33.010  1.00 21.86  ? 26  GLU A CG  1 
ATOM   196  C  CD  . GLU A 1 26  ? 25.454  3.763   33.694  1.00 29.69  ? 26  GLU A CD  1 
ATOM   197  O  OE1 . GLU A 1 26  ? 24.775  3.207   34.621  1.00 32.86  ? 26  GLU A OE1 1 
ATOM   198  O  OE2 . GLU A 1 26  ? 26.532  3.226   33.260  1.00 37.38  ? 26  GLU A OE2 1 
ATOM   199  N  N   . ARG A 1 27  ? 21.609  3.775   29.821  1.00 10.31  ? 27  ARG A N   1 
ATOM   200  C  CA  . ARG A 1 27  ? 20.242  3.539   29.428  1.00 9.42   ? 27  ARG A CA  1 
ATOM   201  C  C   . ARG A 1 27  ? 20.160  3.091   27.973  1.00 8.65   ? 27  ARG A C   1 
ATOM   202  O  O   . ARG A 1 27  ? 19.441  3.702   27.154  1.00 9.26   ? 27  ARG A O   1 
ATOM   203  C  CB  . ARG A 1 27  ? 19.338  4.756   29.763  1.00 12.61  ? 27  ARG A CB  1 
ATOM   204  C  CG  . ARG A 1 27  ? 19.609  6.071   29.175  1.00 15.20  ? 27  ARG A CG  1 
ATOM   205  C  CD  . ARG A 1 27  ? 18.578  7.237   29.370  1.00 19.94  ? 27  ARG A CD  1 
ATOM   206  N  NE  . ARG A 1 27  ? 17.418  7.152   28.479  1.00 15.34  ? 27  ARG A NE  1 
ATOM   207  C  CZ  . ARG A 1 27  ? 16.550  8.142   28.282  1.00 13.42  ? 27  ARG A CZ  1 
ATOM   208  N  NH1 . ARG A 1 27  ? 16.701  9.298   28.907  1.00 15.20  ? 27  ARG A NH1 1 
ATOM   209  N  NH2 . ARG A 1 27  ? 15.524  7.971   27.456  1.00 14.01  ? 27  ARG A NH2 1 
ATOM   210  N  N   . GLN A 1 28  ? 20.866  2.036   27.678  1.00 8.23   ? 28  GLN A N   1 
ATOM   211  C  CA  . GLN A 1 28  ? 20.886  1.502   26.308  1.00 8.17   ? 28  GLN A CA  1 
ATOM   212  C  C   . GLN A 1 28  ? 19.728  0.541   26.060  1.00 7.73   ? 28  GLN A C   1 
ATOM   213  O  O   . GLN A 1 28  ? 19.220  -0.139  26.949  1.00 9.05   ? 28  GLN A O   1 
ATOM   214  C  CB  . GLN A 1 28  ? 22.240  0.835   26.054  1.00 8.72   ? 28  GLN A CB  1 
ATOM   215  C  CG  . GLN A 1 28  ? 23.368  1.869   25.958  1.00 9.45   ? 28  GLN A CG  1 
ATOM   216  C  CD  . GLN A 1 28  ? 23.244  2.672   24.697  1.00 8.44   ? 28  GLN A CD  1 
ATOM   217  O  OE1 . GLN A 1 28  ? 23.439  2.129   23.599  1.00 8.80   ? 28  GLN A OE1 1 
ATOM   218  N  NE2 . GLN A 1 28  ? 22.938  3.950   24.813  1.00 8.99   ? 28  GLN A NE2 1 
ATOM   219  N  N   . SER A 1 29  ? 19.357  0.465   24.796  1.00 7.19   ? 29  SER A N   1 
ATOM   220  C  CA  . SER A 1 29  ? 18.286  -0.407  24.318  1.00 7.23   ? 29  SER A CA  1 
ATOM   221  C  C   . SER A 1 29  ? 18.808  -1.277  23.193  1.00 6.93   ? 29  SER A C   1 
ATOM   222  O  O   . SER A 1 29  ? 19.770  -0.911  22.495  1.00 7.58   ? 29  SER A O   1 
ATOM   223  C  CB  . SER A 1 29  ? 17.142  0.455   23.796  1.00 7.20   ? 29  SER A CB  1 
ATOM   224  O  OG  . SER A 1 29  ? 16.529  1.180   24.863  1.00 7.43   ? 29  SER A OG  1 
ATOM   225  N  N   . PRO A 1 30  ? 18.155  -2.412  22.921  1.00 6.65   ? 30  PRO A N   1 
ATOM   226  C  CA  . PRO A 1 30  ? 16.994  -2.953  23.635  1.00 6.82   ? 30  PRO A CA  1 
ATOM   227  C  C   . PRO A 1 30  ? 17.420  -3.624  24.938  1.00 6.84   ? 30  PRO A C   1 
ATOM   228  O  O   . PRO A 1 30  ? 18.601  -3.662  25.284  1.00 7.57   ? 30  PRO A O   1 
ATOM   229  C  CB  . PRO A 1 30  ? 16.467  -3.988  22.639  1.00 7.30   ? 30  PRO A CB  1 
ATOM   230  C  CG  . PRO A 1 30  ? 17.763  -4.535  22.027  1.00 7.54   ? 30  PRO A CG  1 
ATOM   231  C  CD  . PRO A 1 30  ? 18.650  -3.340  21.879  1.00 7.52   ? 30  PRO A CD  1 
ATOM   232  N  N   . VAL A 1 31  ? 16.421  -4.176  25.630  1.00 7.35   ? 31  VAL A N   1 
ATOM   233  C  CA  . VAL A 1 31  ? 16.604  -4.929  26.857  1.00 7.72   ? 31  VAL A CA  1 
ATOM   234  C  C   . VAL A 1 31  ? 15.722  -6.144  26.793  1.00 7.84   ? 31  VAL A C   1 
ATOM   235  O  O   . VAL A 1 31  ? 14.761  -6.211  26.042  1.00 8.09   ? 31  VAL A O   1 
ATOM   236  C  CB  . VAL A 1 31  ? 16.289  -4.091  28.112  1.00 8.40   ? 31  VAL A CB  1 
ATOM   237  C  CG1 . VAL A 1 31  ? 17.218  -2.891  28.199  1.00 9.53   ? 31  VAL A CG1 1 
ATOM   238  C  CG2 . VAL A 1 31  ? 14.829  -3.678  28.158  1.00 9.26   ? 31  VAL A CG2 1 
ATOM   239  N  N   . ASP A 1 32  ? 16.045  -7.137  27.646  1.00 8.21   ? 32  ASP A N   1 
ATOM   240  C  CA  . ASP A 1 32  ? 15.133  -8.219  27.932  1.00 8.76   ? 32  ASP A CA  1 
ATOM   241  C  C   . ASP A 1 32  ? 14.079  -7.700  28.915  1.00 8.75   ? 32  ASP A C   1 
ATOM   242  O  O   . ASP A 1 32  ? 14.391  -7.063  29.920  1.00 10.41  ? 32  ASP A O   1 
ATOM   243  C  CB  . ASP A 1 32  ? 15.870  -9.401  28.535  1.00 9.88   ? 32  ASP A CB  1 
ATOM   244  C  CG  . ASP A 1 32  ? 14.920  -10.552 28.836  1.00 10.14  ? 32  ASP A CG  1 
ATOM   245  O  OD1 . ASP A 1 32  ? 14.224  -11.015 27.906  1.00 9.99   ? 32  ASP A OD1 1 
ATOM   246  O  OD2 . ASP A 1 32  ? 14.886  -10.988 30.011  1.00 13.48  ? 32  ASP A OD2 1 
ATOM   247  N  N   . ILE A 1 33  ? 12.829  -7.993  28.591  1.00 8.76   ? 33  ILE A N   1 
ATOM   248  C  CA  . ILE A 1 33  ? 11.677  -7.643  29.453  1.00 9.08   ? 33  ILE A CA  1 
ATOM   249  C  C   . ILE A 1 33  ? 11.390  -8.874  30.286  1.00 10.14  ? 33  ILE A C   1 
ATOM   250  O  O   . ILE A 1 33  ? 10.822  -9.853  29.794  1.00 10.51  ? 33  ILE A O   1 
ATOM   251  C  CB  . ILE A 1 33  ? 10.501  -7.201  28.616  1.00 9.76   ? 33  ILE A CB  1 
ATOM   252  C  CG1 . ILE A 1 33  ? 10.882  -5.992  27.780  1.00 10.14  ? 33  ILE A CG1 1 
ATOM   253  C  CG2 . ILE A 1 33  ? 9.312   -6.941  29.554  1.00 11.34  ? 33  ILE A CG2 1 
ATOM   254  C  CD1 . ILE A 1 33  ? 9.835   -5.683  26.673  1.00 11.51  ? 33  ILE A CD1 1 
ATOM   255  N  N   A ASP A 1 34  ? 11.845  -8.766  31.561  0.50 11.98  ? 34  ASP A N   1 
ATOM   256  N  N   B ASP A 1 34  ? 11.694  -8.873  31.573  0.50 10.38  ? 34  ASP A N   1 
ATOM   257  C  CA  A ASP A 1 34  ? 11.543  -9.762  32.599  0.50 11.35  ? 34  ASP A CA  1 
ATOM   258  C  CA  B ASP A 1 34  ? 11.385  -10.034 32.386  0.50 10.73  ? 34  ASP A CA  1 
ATOM   259  C  C   A ASP A 1 34  ? 10.007  -9.590  33.000  0.50 12.09  ? 34  ASP A C   1 
ATOM   260  C  C   B ASP A 1 34  ? 10.103  -9.632  33.010  0.50 12.57  ? 34  ASP A C   1 
ATOM   261  O  O   A ASP A 1 34  ? 9.600   -8.682  33.682  0.50 12.10  ? 34  ASP A O   1 
ATOM   262  O  O   B ASP A 1 34  ? 10.057  -8.617  33.891  0.50 12.68  ? 34  ASP A O   1 
ATOM   263  C  CB  A ASP A 1 34  ? 12.571  -9.716  33.758  0.50 12.58  ? 34  ASP A CB  1 
ATOM   264  C  CB  B ASP A 1 34  ? 12.424  -10.124 33.458  0.50 11.71  ? 34  ASP A CB  1 
ATOM   265  C  CG  A ASP A 1 34  ? 12.279  -10.814 34.763  0.50 14.50  ? 34  ASP A CG  1 
ATOM   266  C  CG  B ASP A 1 34  ? 12.208  -11.306 34.341  0.50 15.01  ? 34  ASP A CG  1 
ATOM   267  O  OD1 A ASP A 1 34  ? 11.117  -11.332 34.881  0.50 13.55  ? 34  ASP A OD1 1 
ATOM   268  O  OD1 B ASP A 1 34  ? 12.634  -12.397 33.965  0.50 18.98  ? 34  ASP A OD1 1 
ATOM   269  O  OD2 A ASP A 1 34  ? 13.216  -11.196 35.431  0.50 21.63  ? 34  ASP A OD2 1 
ATOM   270  O  OD2 B ASP A 1 34  ? 11.725  -11.106 35.436  0.50 18.55  ? 34  ASP A OD2 1 
ATOM   271  N  N   . THR A 1 35  ? 9.091   -10.387 32.531  1.00 13.05  ? 35  THR A N   1 
ATOM   272  C  CA  . THR A 1 35  ? 7.723   -10.095 32.763  1.00 14.19  ? 35  THR A CA  1 
ATOM   273  C  C   . THR A 1 35  ? 7.314   -10.207 34.175  1.00 13.18  ? 35  THR A C   1 
ATOM   274  O  O   . THR A 1 35  ? 6.419   -9.499  34.620  1.00 16.56  ? 35  THR A O   1 
ATOM   275  C  CB  . THR A 1 35  ? 6.785   -10.939 31.953  1.00 16.17  ? 35  THR A CB  1 
ATOM   276  O  OG1 . THR A 1 35  ? 6.903   -12.261 32.406  1.00 16.72  ? 35  THR A OG1 1 
ATOM   277  C  CG2 . THR A 1 35  ? 7.068   -10.839 30.456  1.00 17.59  ? 35  THR A CG2 1 
ATOM   278  N  N   . HIS A 1 36  ? 7.958   -11.098 34.915  1.00 15.10  ? 36  HIS A N   1 
ATOM   279  C  CA  . HIS A 1 36  ? 7.648   -11.294 36.296  1.00 16.59  ? 36  HIS A CA  1 
ATOM   280  C  C   . HIS A 1 36  ? 8.166   -10.141 37.107  1.00 18.44  ? 36  HIS A C   1 
ATOM   281  O  O   . HIS A 1 36  ? 7.500   -9.843  38.154  1.00 19.96  ? 36  HIS A O   1 
ATOM   282  C  CB  . HIS A 1 36  ? 8.145   -12.680 36.701  1.00 18.98  ? 36  HIS A CB  1 
ATOM   283  C  CG  . HIS A 1 36  ? 7.226   -13.760 36.186  1.00 17.10  ? 36  HIS A CG  1 
ATOM   284  N  ND1 . HIS A 1 36  ? 5.960   -13.822 36.553  1.00 23.68  ? 36  HIS A ND1 1 
ATOM   285  C  CD2 . HIS A 1 36  ? 7.397   -14.735 35.237  1.00 20.73  ? 36  HIS A CD2 1 
ATOM   286  C  CE1 . HIS A 1 36  ? 5.365   -14.821 35.922  1.00 22.87  ? 36  HIS A CE1 1 
ATOM   287  N  NE2 . HIS A 1 36  ? 6.237   -15.355 35.101  1.00 30.72  ? 36  HIS A NE2 1 
ATOM   288  N  N   . THR A 1 37  ? 9.278   -9.468  36.739  1.00 17.93  ? 37  THR A N   1 
ATOM   289  C  CA  . THR A 1 37  ? 9.827   -8.355  37.534  1.00 17.92  ? 37  THR A CA  1 
ATOM   290  C  C   . THR A 1 37  ? 9.344   -6.964  37.061  1.00 16.19  ? 37  THR A C   1 
ATOM   291  O  O   . THR A 1 37  ? 9.568   -5.995  37.787  1.00 19.43  ? 37  THR A O   1 
ATOM   292  C  CB  . THR A 1 37  ? 11.309  -8.313  37.723  1.00 25.63  ? 37  THR A CB  1 
ATOM   293  O  OG1 . THR A 1 37  ? 11.864  -8.488  36.490  1.00 24.91  ? 37  THR A OG1 1 
ATOM   294  C  CG2 . THR A 1 37  ? 11.803  -9.585  38.384  1.00 32.69  ? 37  THR A CG2 1 
ATOM   295  N  N   . ALA A 1 38  ? 8.714   -6.880  35.913  1.00 15.71  ? 38  ALA A N   1 
ATOM   296  C  CA  . ALA A 1 38  ? 8.121   -5.641  35.497  1.00 13.65  ? 38  ALA A CA  1 
ATOM   297  C  C   . ALA A 1 38  ? 7.107   -5.236  36.555  1.00 14.79  ? 38  ALA A C   1 
ATOM   298  O  O   . ALA A 1 38  ? 6.506   -6.053  37.151  1.00 19.85  ? 38  ALA A O   1 
ATOM   299  C  CB  . ALA A 1 38  ? 7.531   -5.743  34.107  1.00 14.43  ? 38  ALA A CB  1 
ATOM   300  N  N   . LYS A 1 39  ? 7.014   -3.982  36.876  1.00 13.53  ? 39  LYS A N   1 
ATOM   301  C  CA  . LYS A 1 39  ? 6.105   -3.469  37.878  1.00 15.09  ? 39  LYS A CA  1 
ATOM   302  C  C   . LYS A 1 39  ? 4.823   -2.922  37.241  1.00 13.79  ? 39  LYS A C   1 
ATOM   303  O  O   . LYS A 1 39  ? 4.854   -1.994  36.488  1.00 13.07  ? 39  LYS A O   1 
ATOM   304  C  CB  . LYS A 1 39  ? 6.839   -2.290  38.604  1.00 18.83  ? 39  LYS A CB  1 
ATOM   305  C  CG  . LYS A 1 39  ? 6.100   -1.391  39.598  1.00 19.53  ? 39  LYS A CG  1 
ATOM   306  C  CD  . LYS A 1 39  ? 5.884   -2.106  40.955  1.00 19.93  ? 39  LYS A CD  1 
ATOM   307  C  CE  . LYS A 1 39  ? 5.174   -1.230  41.940  1.00 23.19  ? 39  LYS A CE  1 
ATOM   308  N  NZ  . LYS A 1 39  ? 4.852   -2.076  43.084  1.00 26.21  ? 39  LYS A NZ  1 
ATOM   309  N  N   . TYR A 1 40  ? 3.671   -3.493  37.644  1.00 15.87  ? 40  TYR A N   1 
ATOM   310  C  CA  . TYR A 1 40  ? 2.413   -2.924  37.259  1.00 14.94  ? 40  TYR A CA  1 
ATOM   311  C  C   . TYR A 1 40  ? 2.274   -1.530  37.847  1.00 13.96  ? 40  TYR A C   1 
ATOM   312  O  O   . TYR A 1 40  ? 2.452   -1.385  39.094  1.00 17.11  ? 40  TYR A O   1 
ATOM   313  C  CB  . TYR A 1 40  ? 1.269   -3.841  37.653  1.00 19.84  ? 40  TYR A CB  1 
ATOM   314  C  CG  . TYR A 1 40  ? -0.049  -3.195  37.524  1.00 17.61  ? 40  TYR A CG  1 
ATOM   315  C  CD1 . TYR A 1 40  ? -0.542  -2.793  36.268  1.00 18.49  ? 40  TYR A CD1 1 
ATOM   316  C  CD2 . TYR A 1 40  ? -0.905  -3.016  38.612  1.00 25.16  ? 40  TYR A CD2 1 
ATOM   317  C  CE1 . TYR A 1 40  ? -1.765  -2.182  36.127  1.00 19.43  ? 40  TYR A CE1 1 
ATOM   318  C  CE2 . TYR A 1 40  ? -2.139  -2.385  38.453  1.00 31.47  ? 40  TYR A CE2 1 
ATOM   319  C  CZ  . TYR A 1 40  ? -2.577  -1.976  37.246  1.00 26.75  ? 40  TYR A CZ  1 
ATOM   320  O  OH  . TYR A 1 40  ? -3.815  -1.373  37.075  1.00 32.60  ? 40  TYR A OH  1 
ATOM   321  N  N   . ASP A 1 41  ? 1.979   -0.533  37.064  1.00 13.63  ? 41  ASP A N   1 
ATOM   322  C  CA  . ASP A 1 41  ? 1.821   0.821   37.542  1.00 15.65  ? 41  ASP A CA  1 
ATOM   323  C  C   . ASP A 1 41  ? 0.432   1.230   37.210  1.00 16.82  ? 41  ASP A C   1 
ATOM   324  O  O   . ASP A 1 41  ? 0.115   1.565   36.093  1.00 17.93  ? 41  ASP A O   1 
ATOM   325  C  CB  . ASP A 1 41  ? 2.822   1.738   36.868  1.00 19.33  ? 41  ASP A CB  1 
ATOM   326  C  CG  . ASP A 1 41  ? 2.761   3.159   37.399  1.00 22.81  ? 41  ASP A CG  1 
ATOM   327  O  OD1 . ASP A 1 41  ? 1.775   3.491   38.086  1.00 26.87  ? 41  ASP A OD1 1 
ATOM   328  O  OD2 . ASP A 1 41  ? 3.660   3.945   37.084  1.00 33.72  ? 41  ASP A OD2 1 
ATOM   329  N  N   . PRO A 1 42  ? -0.432  1.255   38.237  1.00 22.61  ? 42  PRO A N   1 
ATOM   330  C  CA  . PRO A 1 42  ? -1.877  1.499   37.962  1.00 24.94  ? 42  PRO A CA  1 
ATOM   331  C  C   . PRO A 1 42  ? -2.122  2.917   37.565  1.00 26.04  ? 42  PRO A C   1 
ATOM   332  O  O   . PRO A 1 42  ? -3.204  3.247   37.049  1.00 34.60  ? 42  PRO A O   1 
ATOM   333  C  CB  . PRO A 1 42  ? -2.547  1.138   39.297  1.00 36.19  ? 42  PRO A CB  1 
ATOM   334  C  CG  . PRO A 1 42  ? -1.502  1.573   40.271  1.00 34.87  ? 42  PRO A CG  1 
ATOM   335  C  CD  . PRO A 1 42  ? -0.231  0.946   39.679  1.00 27.42  ? 42  PRO A CD  1 
ATOM   336  N  N   . SER A 1 43  ? -1.109  3.769   37.714  1.00 21.99  ? 43  SER A N   1 
ATOM   337  C  CA  . SER A 1 43  ? -1.250  5.145   37.336  1.00 30.56  ? 43  SER A CA  1 
ATOM   338  C  C   . SER A 1 43  ? -0.840  5.429   35.847  1.00 25.75  ? 43  SER A C   1 
ATOM   339  O  O   . SER A 1 43  ? -1.052  6.563   35.303  1.00 32.31  ? 43  SER A O   1 
ATOM   340  C  CB  . SER A 1 43  ? -0.476  5.990   38.297  1.00 35.19  ? 43  SER A CB  1 
ATOM   341  O  OG  . SER A 1 43  ? 0.871   6.133   37.868  1.00 31.49  ? 43  SER A OG  1 
ATOM   342  N  N   . LEU A 1 44  ? -0.321  4.415   35.152  1.00 21.96  ? 44  LEU A N   1 
ATOM   343  C  CA  . LEU A 1 44  ? -0.054  4.526   33.681  1.00 18.49  ? 44  LEU A CA  1 
ATOM   344  C  C   . LEU A 1 44  ? -1.386  4.637   32.981  1.00 19.35  ? 44  LEU A C   1 
ATOM   345  O  O   . LEU A 1 44  ? -2.311  3.914   33.257  1.00 25.86  ? 44  LEU A O   1 
ATOM   346  C  CB  . LEU A 1 44  ? 0.706   3.331   33.166  1.00 16.58  ? 44  LEU A CB  1 
ATOM   347  C  CG  . LEU A 1 44  ? 2.180   3.363   33.459  1.00 15.31  ? 44  LEU A CG  1 
ATOM   348  C  CD1 . LEU A 1 44  ? 2.730   1.982   33.076  1.00 16.07  ? 44  LEU A CD1 1 
ATOM   349  C  CD2 . LEU A 1 44  ? 2.957   4.456   32.749  1.00 17.46  ? 44  LEU A CD2 1 
ATOM   350  N  N   . LYS A 1 45  ? -1.416  5.518   32.011  1.00 18.95  ? 45  LYS A N   1 
ATOM   351  C  CA  . LYS A 1 45  ? -2.686  5.762   31.240  1.00 17.33  ? 45  LYS A CA  1 
ATOM   352  C  C   . LYS A 1 45  ? -2.691  4.854   30.018  1.00 15.82  ? 45  LYS A C   1 
ATOM   353  O  O   . LYS A 1 45  ? -1.655  4.382   29.536  1.00 16.40  ? 45  LYS A O   1 
ATOM   354  C  CB  . LYS A 1 45  ? -2.724  7.190   30.773  1.00 19.38  ? 45  LYS A CB  1 
ATOM   355  C  CG  . LYS A 1 45  ? -2.695  8.211   31.860  1.00 26.03  ? 45  LYS A CG  1 
ATOM   356  C  CD  . LYS A 1 45  ? -2.610  9.634   31.314  1.00 32.91  ? 45  LYS A CD  1 
ATOM   357  N  N   . PRO A 1 46  ? -3.883  4.653   29.443  1.00 15.22  ? 46  PRO A N   1 
ATOM   358  C  CA  . PRO A 1 46  ? -3.942  4.010   28.148  1.00 15.01  ? 46  PRO A CA  1 
ATOM   359  C  C   . PRO A 1 46  ? -3.154  4.811   27.133  1.00 12.60  ? 46  PRO A C   1 
ATOM   360  O  O   . PRO A 1 46  ? -3.092  5.996   27.186  1.00 13.76  ? 46  PRO A O   1 
ATOM   361  C  CB  . PRO A 1 46  ? -5.448  4.059   27.805  1.00 18.16  ? 46  PRO A CB  1 
ATOM   362  C  CG  . PRO A 1 46  ? -6.168  4.215   29.107  1.00 24.92  ? 46  PRO A CG  1 
ATOM   363  C  CD  . PRO A 1 46  ? -5.218  5.016   29.967  1.00 20.12  ? 46  PRO A CD  1 
ATOM   364  N  N   . LEU A 1 47  ? -2.547  4.056   26.225  1.00 13.56  ? 47  LEU A N   1 
ATOM   365  C  CA  . LEU A 1 47  ? -1.852  4.691   25.149  1.00 13.55  ? 47  LEU A CA  1 
ATOM   366  C  C   . LEU A 1 47  ? -2.897  5.317   24.186  1.00 14.56  ? 47  LEU A C   1 
ATOM   367  O  O   . LEU A 1 47  ? -3.912  4.674   23.919  1.00 18.35  ? 47  LEU A O   1 
ATOM   368  C  CB  . LEU A 1 47  ? -1.022  3.678   24.422  1.00 17.09  ? 47  LEU A CB  1 
ATOM   369  C  CG  . LEU A 1 47  ? 0.036   4.043   23.512  1.00 17.74  ? 47  LEU A CG  1 
ATOM   370  C  CD1 . LEU A 1 47  ? 1.076   4.879   24.305  1.00 19.62  ? 47  LEU A CD1 1 
ATOM   371  C  CD2 . LEU A 1 47  ? 0.636   2.747   22.906  1.00 18.97  ? 47  LEU A CD2 1 
ATOM   372  N  N   . SER A 1 48  ? -2.648  6.483   23.662  1.00 12.94  ? 48  SER A N   1 
ATOM   373  C  CA  . SER A 1 48  ? -3.467  7.149   22.642  1.00 13.50  ? 48  SER A CA  1 
ATOM   374  C  C   . SER A 1 48  ? -2.717  7.133   21.348  1.00 13.17  ? 48  SER A C   1 
ATOM   375  O  O   . SER A 1 48  ? -1.693  7.874   21.197  1.00 14.42  ? 48  SER A O   1 
ATOM   376  C  CB  . SER A 1 48  ? -3.797  8.550   23.096  1.00 15.62  ? 48  SER A CB  1 
ATOM   377  O  OG  . SER A 1 48  ? -4.452  9.285   22.064  1.00 20.08  ? 48  SER A OG  1 
ATOM   378  N  N   . VAL A 1 49  ? -3.113  6.314   20.421  1.00 14.29  ? 49  VAL A N   1 
ATOM   379  C  CA  . VAL A 1 49  ? -2.542  6.264   19.115  1.00 14.88  ? 49  VAL A CA  1 
ATOM   380  C  C   . VAL A 1 49  ? -3.502  6.896   18.133  1.00 16.89  ? 49  VAL A C   1 
ATOM   381  O  O   . VAL A 1 49  ? -4.604  6.393   17.932  1.00 19.57  ? 49  VAL A O   1 
ATOM   382  C  CB  . VAL A 1 49  ? -2.255  4.787   18.734  1.00 17.45  ? 49  VAL A CB  1 
ATOM   383  C  CG1 . VAL A 1 49  ? -1.586  4.745   17.352  1.00 23.96  ? 49  VAL A CG1 1 
ATOM   384  C  CG2 . VAL A 1 49  ? -1.425  4.113   19.827  1.00 20.08  ? 49  VAL A CG2 1 
ATOM   385  N  N   . SER A 1 50  ? -3.154  8.012   17.556  1.00 14.46  ? 50  SER A N   1 
ATOM   386  C  CA  . SER A 1 50  ? -4.069  8.763   16.686  1.00 16.54  ? 50  SER A CA  1 
ATOM   387  C  C   . SER A 1 50  ? -3.446  8.840   15.358  1.00 13.88  ? 50  SER A C   1 
ATOM   388  O  O   . SER A 1 50  ? -2.744  9.793   15.054  1.00 15.91  ? 50  SER A O   1 
ATOM   389  C  CB  . SER A 1 50  ? -4.461  10.182  17.249  1.00 21.47  ? 50  SER A CB  1 
ATOM   390  O  OG  . SER A 1 50  ? -5.140  10.083  18.492  1.00 27.63  ? 50  SER A OG  1 
ATOM   391  N  N   . TYR A 1 51  ? -3.704  7.845   14.514  1.00 14.34  ? 51  TYR A N   1 
ATOM   392  C  CA  . TYR A 1 51  ? -3.112  7.727   13.223  1.00 13.35  ? 51  TYR A CA  1 
ATOM   393  C  C   . TYR A 1 51  ? -4.135  7.981   12.085  1.00 15.20  ? 51  TYR A C   1 
ATOM   394  O  O   . TYR A 1 51  ? -3.757  7.811   10.968  1.00 15.75  ? 51  TYR A O   1 
ATOM   395  C  CB  . TYR A 1 51  ? -2.489  6.345   13.043  1.00 14.52  ? 51  TYR A CB  1 
ATOM   396  C  CG  . TYR A 1 51  ? -1.227  6.058   13.823  1.00 12.69  ? 51  TYR A CG  1 
ATOM   397  C  CD1 . TYR A 1 51  ? -0.493  7.047   14.509  1.00 13.46  ? 51  TYR A CD1 1 
ATOM   398  C  CD2 . TYR A 1 51  ? -0.747  4.761   13.873  1.00 12.54  ? 51  TYR A CD2 1 
ATOM   399  C  CE1 . TYR A 1 51  ? 0.692   6.734   15.175  1.00 11.36  ? 51  TYR A CE1 1 
ATOM   400  C  CE2 . TYR A 1 51  ? 0.423   4.426   14.515  1.00 11.59  ? 51  TYR A CE2 1 
ATOM   401  C  CZ  . TYR A 1 51  ? 1.165   5.420   15.170  1.00 11.06  ? 51  TYR A CZ  1 
ATOM   402  O  OH  . TYR A 1 51  ? 2.308   5.055   15.816  1.00 11.54  ? 51  TYR A OH  1 
ATOM   403  N  N   A ASP A 1 52  ? -5.366  8.372   12.395  0.50 16.88  ? 52  ASP A N   1 
ATOM   404  N  N   B ASP A 1 52  ? -5.376  8.372   12.370  0.50 16.73  ? 52  ASP A N   1 
ATOM   405  C  CA  A ASP A 1 52  ? -6.368  8.626   11.377  0.50 16.99  ? 52  ASP A CA  1 
ATOM   406  C  CA  B ASP A 1 52  ? -6.368  8.620   11.316  0.50 19.56  ? 52  ASP A CA  1 
ATOM   407  C  C   A ASP A 1 52  ? -6.004  9.625   10.267  0.50 17.02  ? 52  ASP A C   1 
ATOM   408  C  C   B ASP A 1 52  ? -5.814  9.496   10.196  0.50 19.33  ? 52  ASP A C   1 
ATOM   409  O  O   A ASP A 1 52  ? -6.515  9.523   9.138   0.50 19.32  ? 52  ASP A O   1 
ATOM   410  O  O   B ASP A 1 52  ? -6.025  9.190   8.996   0.50 25.12  ? 52  ASP A O   1 
ATOM   411  C  CB  A ASP A 1 52  ? -7.705  9.023   12.018  0.50 18.68  ? 52  ASP A CB  1 
ATOM   412  C  CB  B ASP A 1 52  ? -7.608  9.286   11.917  0.50 23.68  ? 52  ASP A CB  1 
ATOM   413  C  CG  A ASP A 1 52  ? -7.533  9.965   13.191  0.50 27.31  ? 52  ASP A CG  1 
ATOM   414  C  CG  B ASP A 1 52  ? -8.729  9.441   10.914  0.50 23.32  ? 52  ASP A CG  1 
ATOM   415  O  OD1 A ASP A 1 52  ? -6.762  9.633   14.115  0.50 24.92  ? 52  ASP A OD1 1 
ATOM   416  O  OD1 B ASP A 1 52  ? -9.212  8.414   10.395  0.50 23.45  ? 52  ASP A OD1 1 
ATOM   417  O  OD2 A ASP A 1 52  ? -8.172  11.038  13.191  0.50 34.63  ? 52  ASP A OD2 1 
ATOM   418  O  OD2 B ASP A 1 52  ? -9.129  10.595  10.650  0.50 31.74  ? 52  ASP A OD2 1 
ATOM   419  N  N   . GLN A 1 53  ? -5.139  10.565  10.588  1.00 20.01  ? 53  GLN A N   1 
ATOM   420  C  CA  . GLN A 1 53  ? -4.717  11.556  9.550   1.00 21.35  ? 53  GLN A CA  1 
ATOM   421  C  C   . GLN A 1 53  ? -3.303  11.308  9.027   1.00 17.25  ? 53  GLN A C   1 
ATOM   422  O  O   . GLN A 1 53  ? -2.706  12.217  8.436   1.00 18.45  ? 53  GLN A O   1 
ATOM   423  C  CB  . GLN A 1 53  ? -4.906  12.992  10.043  1.00 25.15  ? 53  GLN A CB  1 
ATOM   424  C  CG  . GLN A 1 53  ? -6.418  13.293  10.270  1.00 34.10  ? 53  GLN A CG  1 
ATOM   425  C  CD  . GLN A 1 53  ? -7.227  13.300  8.950   1.00 34.62  ? 53  GLN A CD  1 
ATOM   426  O  OE1 . GLN A 1 53  ? -6.691  13.806  7.857   1.00 46.68  ? 53  GLN A OE1 1 
ATOM   427  N  NE2 . GLN A 1 53  ? -8.396  12.651  8.949   1.00 58.30  ? 53  GLN A NE2 1 
ATOM   428  N  N   . ALA A 1 54  ? -2.756  10.128  9.221   1.00 15.93  ? 54  ALA A N   1 
ATOM   429  C  CA  . ALA A 1 54  ? -1.398  9.900   8.820   1.00 13.88  ? 54  ALA A CA  1 
ATOM   430  C  C   . ALA A 1 54  ? -1.232  10.106  7.335   1.00 14.88  ? 54  ALA A C   1 
ATOM   431  O  O   . ALA A 1 54  ? -2.095  9.697   6.542   1.00 18.89  ? 54  ALA A O   1 
ATOM   432  C  CB  . ALA A 1 54  ? -0.925  8.518   9.205   1.00 16.00  ? 54  ALA A CB  1 
ATOM   433  N  N   . THR A 1 55  ? -0.089  10.639  6.953   1.00 13.01  ? 55  THR A N   1 
ATOM   434  C  CA  . THR A 1 55  ? 0.307   10.828  5.577   1.00 13.29  ? 55  THR A CA  1 
ATOM   435  C  C   . THR A 1 55  ? 1.641   10.193  5.326   1.00 11.28  ? 55  THR A C   1 
ATOM   436  O  O   . THR A 1 55  ? 2.658   10.789  5.598   1.00 12.13  ? 55  THR A O   1 
ATOM   437  C  CB  . THR A 1 55  ? 0.426   12.349  5.174   1.00 16.27  ? 55  THR A CB  1 
ATOM   438  O  OG1 . THR A 1 55  ? -0.821  12.982  5.321   1.00 20.90  ? 55  THR A OG1 1 
ATOM   439  C  CG2 . THR A 1 55  ? 0.932   12.512  3.702   1.00 18.35  ? 55  THR A CG2 1 
ATOM   440  N  N   . SER A 1 56  ? 1.629   8.967   4.817   1.00 11.99  ? 56  SER A N   1 
ATOM   441  C  CA  . SER A 1 56  ? 2.874   8.364   4.401   1.00 11.92  ? 56  SER A CA  1 
ATOM   442  C  C   . SER A 1 56  ? 3.292   9.021   3.142   1.00 11.90  ? 56  SER A C   1 
ATOM   443  O  O   . SER A 1 56  ? 2.486   9.472   2.345   1.00 13.50  ? 56  SER A O   1 
ATOM   444  C  CB  . SER A 1 56  ? 2.786   6.842   4.235   1.00 11.97  ? 56  SER A CB  1 
ATOM   445  O  OG  . SER A 1 56  ? 1.881   6.497   3.153   1.00 13.80  ? 56  SER A OG  1 
ATOM   446  N  N   . LEU A 1 57  ? 4.590   9.028   2.910   1.00 11.28  ? 57  LEU A N   1 
ATOM   447  C  CA  . LEU A 1 57  ? 5.130   9.678   1.725   1.00 12.69  ? 57  LEU A CA  1 
ATOM   448  C  C   . LEU A 1 57  ? 5.967   8.741   0.871   1.00 11.96  ? 57  LEU A C   1 
ATOM   449  O  O   . LEU A 1 57  ? 5.894   8.781   -0.365  1.00 13.52  ? 57  LEU A O   1 
ATOM   450  C  CB  . LEU A 1 57  ? 6.004   10.816  2.178   1.00 14.86  ? 57  LEU A CB  1 
ATOM   451  C  CG  . LEU A 1 57  ? 5.161   12.011  2.790   1.00 18.21  ? 57  LEU A CG  1 
ATOM   452  C  CD1 . LEU A 1 57  ? 6.118   13.072  3.354   1.00 21.37  ? 57  LEU A CD1 1 
ATOM   453  C  CD2 . LEU A 1 57  ? 4.114   12.655  1.811   1.00 20.71  ? 57  LEU A CD2 1 
ATOM   454  N  N   . ARG A 1 58  ? 6.864   7.968   1.484   1.00 12.02  ? 58  ARG A N   1 
ATOM   455  C  CA  . ARG A 1 58  ? 7.953   7.343   0.755   1.00 12.68  ? 58  ARG A CA  1 
ATOM   456  C  C   . ARG A 1 58  ? 8.442   6.151   1.571   1.00 10.79  ? 58  ARG A C   1 
ATOM   457  O  O   . ARG A 1 58  ? 8.339   6.157   2.799   1.00 11.17  ? 58  ARG A O   1 
ATOM   458  C  CB  . ARG A 1 58  ? 9.070   8.357   0.531   1.00 13.89  ? 58  ARG A CB  1 
ATOM   459  C  CG  . ARG A 1 58  ? 10.109  7.931   -0.374  1.00 14.43  ? 58  ARG A CG  1 
ATOM   460  C  CD  . ARG A 1 58  ? 11.181  8.969   -0.580  1.00 16.64  ? 58  ARG A CD  1 
ATOM   461  N  NE  . ARG A 1 58  ? 12.027  9.075   0.580   1.00 14.65  ? 58  ARG A NE  1 
ATOM   462  C  CZ  . ARG A 1 58  ? 13.357  9.238   0.562   1.00 13.69  ? 58  ARG A CZ  1 
ATOM   463  N  NH1 . ARG A 1 58  ? 14.005  9.481   -0.558  1.00 16.81  ? 58  ARG A NH1 1 
ATOM   464  N  NH2 . ARG A 1 58  ? 14.009  9.222   1.724   1.00 14.57  ? 58  ARG A NH2 1 
ATOM   465  N  N   . ILE A 1 59  ? 9.075   5.201   0.903   1.00 10.55  ? 59  ILE A N   1 
ATOM   466  C  CA  . ILE A 1 59  ? 9.750   4.093   1.546   1.00 11.31  ? 59  ILE A CA  1 
ATOM   467  C  C   . ILE A 1 59  ? 11.173  4.081   1.039   1.00 10.52  ? 59  ILE A C   1 
ATOM   468  O  O   . ILE A 1 59  ? 11.414  4.233   -0.179  1.00 12.49  ? 59  ILE A O   1 
ATOM   469  C  CB  . ILE A 1 59  ? 9.009   2.771   1.299   1.00 11.02  ? 59  ILE A CB  1 
ATOM   470  C  CG1 . ILE A 1 59  ? 9.582   1.634   2.203   1.00 11.21  ? 59  ILE A CG1 1 
ATOM   471  C  CG2 . ILE A 1 59  ? 8.913   2.337   -0.181  1.00 12.47  ? 59  ILE A CG2 1 
ATOM   472  C  CD1 . ILE A 1 59  ? 8.710   0.404   2.111   1.00 12.28  ? 59  ILE A CD1 1 
ATOM   473  N  N   . LEU A 1 60  ? 12.136  3.912   1.962   1.00 10.57  ? 60  LEU A N   1 
ATOM   474  C  CA  . LEU A 1 60  ? 13.520  4.027   1.668   1.00 10.37  ? 60  LEU A CA  1 
ATOM   475  C  C   . LEU A 1 60  ? 14.314  2.859   2.204   1.00 9.76   ? 60  LEU A C   1 
ATOM   476  O  O   . LEU A 1 60  ? 14.159  2.517   3.392   1.00 10.74  ? 60  LEU A O   1 
ATOM   477  C  CB  . LEU A 1 60  ? 14.076  5.322   2.393   1.00 11.75  ? 60  LEU A CB  1 
ATOM   478  C  CG  . LEU A 1 60  ? 15.583  5.478   2.324   1.00 12.56  ? 60  LEU A CG  1 
ATOM   479  C  CD1 . LEU A 1 60  ? 16.117  5.741   0.929   1.00 13.64  ? 60  LEU A CD1 1 
ATOM   480  C  CD2 . LEU A 1 60  ? 16.050  6.555   3.337   1.00 14.22  ? 60  LEU A CD2 1 
ATOM   481  N  N   . ASN A 1 61  ? 15.175  2.241   1.425   1.00 10.13  ? 61  ASN A N   1 
ATOM   482  C  CA  . ASN A 1 61  ? 16.193  1.317   1.879   1.00 10.68  ? 61  ASN A CA  1 
ATOM   483  C  C   . ASN A 1 61  ? 17.443  2.113   2.255   1.00 10.71  ? 61  ASN A C   1 
ATOM   484  O  O   . ASN A 1 61  ? 18.020  2.676   1.367   1.00 13.17  ? 61  ASN A O   1 
ATOM   485  C  CB  . ASN A 1 61  ? 16.507  0.260   0.819   1.00 11.30  ? 61  ASN A CB  1 
ATOM   486  C  CG  . ASN A 1 61  ? 17.573  -0.714  1.223   1.00 11.07  ? 61  ASN A CG  1 
ATOM   487  O  OD1 . ASN A 1 61  ? 18.462  -0.440  2.099   1.00 12.34  ? 61  ASN A OD1 1 
ATOM   488  N  ND2 . ASN A 1 61  ? 17.550  -1.920  0.636   1.00 12.65  ? 61  ASN A ND2 1 
ATOM   489  N  N   . ASN A 1 62  ? 17.719  2.225   3.567   1.00 11.50  ? 62  ASN A N   1 
ATOM   490  C  CA  . ASN A 1 62  ? 18.808  3.061   3.998   1.00 13.67  ? 62  ASN A CA  1 
ATOM   491  C  C   . ASN A 1 62  ? 20.089  2.239   4.189   1.00 12.78  ? 62  ASN A C   1 
ATOM   492  O  O   . ASN A 1 62  ? 21.131  2.721   4.797   1.00 16.84  ? 62  ASN A O   1 
ATOM   493  C  CB  . ASN A 1 62  ? 18.453  3.859   5.325   1.00 16.09  ? 62  ASN A CB  1 
ATOM   494  C  CG  . ASN A 1 62  ? 18.332  2.946   6.495   1.00 14.86  ? 62  ASN A CG  1 
ATOM   495  O  OD1 . ASN A 1 62  ? 18.542  1.772   6.462   1.00 14.31  ? 62  ASN A OD1 1 
ATOM   496  N  ND2 . ASN A 1 62  ? 18.105  3.531   7.683   1.00 21.14  ? 62  ASN A ND2 1 
ATOM   497  N  N   . GLY A 1 63  ? 20.124  0.970   3.780   1.00 12.20  ? 63  GLY A N   1 
ATOM   498  C  CA  . GLY A 1 63  ? 21.234  0.157   3.984   1.00 12.92  ? 63  GLY A CA  1 
ATOM   499  C  C   . GLY A 1 63  ? 21.340  -0.554  5.324   1.00 12.20  ? 63  GLY A C   1 
ATOM   500  O  O   . GLY A 1 63  ? 22.261  -1.359  5.518   1.00 14.20  ? 63  GLY A O   1 
ATOM   501  N  N   . HIS A 1 64  ? 20.389  -0.294  6.198   1.00 11.32  ? 64  HIS A N   1 
ATOM   502  C  CA  . HIS A 1 64  ? 20.293  -0.946  7.539   1.00 11.63  ? 64  HIS A CA  1 
ATOM   503  C  C   . HIS A 1 64  ? 18.918  -1.596  7.691   1.00 11.01  ? 64  HIS A C   1 
ATOM   504  O  O   . HIS A 1 64  ? 18.888  -2.707  8.229   1.00 18.22  ? 64  HIS A O   1 
ATOM   505  C  CB  . HIS A 1 64  ? 20.523  0.094   8.682   1.00 12.52  ? 64  HIS A CB  1 
ATOM   506  C  CG  . HIS A 1 64  ? 21.819  0.847   8.501   1.00 13.21  ? 64  HIS A CG  1 
ATOM   507  N  ND1 . HIS A 1 64  ? 23.053  0.233   8.588   1.00 14.81  ? 64  HIS A ND1 1 
ATOM   508  C  CD2 . HIS A 1 64  ? 22.012  2.167   8.306   1.00 15.34  ? 64  HIS A CD2 1 
ATOM   509  C  CE1 . HIS A 1 64  ? 24.023  1.215   8.487   1.00 15.93  ? 64  HIS A CE1 1 
ATOM   510  N  NE2 . HIS A 1 64  ? 23.382  2.391   8.277   1.00 16.97  ? 64  HIS A NE2 1 
ATOM   511  N  N   . ALA A 1 65  ? 17.887  -0.979  7.206   1.00 10.38  ? 65  ALA A N   1 
ATOM   512  C  CA  . ALA A 1 65  ? 16.540  -1.455  7.218   1.00 10.24  ? 65  ALA A CA  1 
ATOM   513  C  C   . ALA A 1 65  ? 15.803  -0.701  6.097   1.00 9.39   ? 65  ALA A C   1 
ATOM   514  O  O   . ALA A 1 65  ? 16.466  -0.033  5.266   1.00 11.24  ? 65  ALA A O   1 
ATOM   515  C  CB  . ALA A 1 65  ? 15.917  -1.240  8.609   1.00 12.05  ? 65  ALA A CB  1 
ATOM   516  N  N   . PHE A 1 66  ? 14.505  -0.729  6.096   1.00 9.65   ? 66  PHE A N   1 
ATOM   517  C  CA  . PHE A 1 66  ? 13.729  0.200   5.282   1.00 9.94   ? 66  PHE A CA  1 
ATOM   518  C  C   . PHE A 1 66  ? 12.843  1.062   6.171   1.00 9.09   ? 66  PHE A C   1 
ATOM   519  O  O   . PHE A 1 66  ? 12.284  0.581   7.154   1.00 9.84   ? 66  PHE A O   1 
ATOM   520  C  CB  . PHE A 1 66  ? 12.925  -0.505  4.182   1.00 11.35  ? 66  PHE A CB  1 
ATOM   521  C  CG  . PHE A 1 66  ? 11.867  -1.442  4.687   1.00 10.61  ? 66  PHE A CG  1 
ATOM   522  C  CD1 . PHE A 1 66  ? 10.633  -0.964  5.029   1.00 11.15  ? 66  PHE A CD1 1 
ATOM   523  C  CD2 . PHE A 1 66  ? 12.132  -2.810  4.838   1.00 11.36  ? 66  PHE A CD2 1 
ATOM   524  C  CE1 . PHE A 1 66  ? 9.663   -1.811  5.506   1.00 11.78  ? 66  PHE A CE1 1 
ATOM   525  C  CE2 . PHE A 1 66  ? 11.135  -3.670  5.352   1.00 11.67  ? 66  PHE A CE2 1 
ATOM   526  C  CZ  . PHE A 1 66  ? 9.883   -3.181  5.666   1.00 11.30  ? 66  PHE A CZ  1 
ATOM   527  N  N   . ASN A 1 67  ? 12.757  2.337   5.830   1.00 9.98   ? 67  ASN A N   1 
ATOM   528  C  CA  . ASN A 1 67  ? 11.917  3.278   6.548   1.00 9.04   ? 67  ASN A CA  1 
ATOM   529  C  C   . ASN A 1 67  ? 10.683  3.638   5.756   1.00 8.74   ? 67  ASN A C   1 
ATOM   530  O  O   . ASN A 1 67  ? 10.844  4.055   4.558   1.00 11.00  ? 67  ASN A O   1 
ATOM   531  C  CB  . ASN A 1 67  ? 12.677  4.552   6.867   1.00 10.82  ? 67  ASN A CB  1 
ATOM   532  C  CG  . ASN A 1 67  ? 13.870  4.361   7.716   1.00 11.43  ? 67  ASN A CG  1 
ATOM   533  O  OD1 . ASN A 1 67  ? 13.995  3.367   8.450   1.00 12.27  ? 67  ASN A OD1 1 
ATOM   534  N  ND2 . ASN A 1 67  ? 14.765  5.359   7.687   1.00 13.99  ? 67  ASN A ND2 1 
ATOM   535  N  N   . VAL A 1 68  ? 9.535   3.556   6.315   1.00 9.00   ? 68  VAL A N   1 
ATOM   536  C  CA  . VAL A 1 68  ? 8.319   4.158   5.756   1.00 9.88   ? 68  VAL A CA  1 
ATOM   537  C  C   . VAL A 1 68  ? 8.172   5.501   6.409   1.00 10.17  ? 68  VAL A C   1 
ATOM   538  O  O   . VAL A 1 68  ? 8.077   5.606   7.643   1.00 9.84   ? 68  VAL A O   1 
ATOM   539  C  CB  . VAL A 1 68  ? 7.055   3.291   5.954   1.00 10.55  ? 68  VAL A CB  1 
ATOM   540  C  CG1 . VAL A 1 68  ? 5.813   4.063   5.524   1.00 12.03  ? 68  VAL A CG1 1 
ATOM   541  C  CG2 . VAL A 1 68  ? 7.212   2.012   5.194   1.00 10.93  ? 68  VAL A CG2 1 
ATOM   542  N  N   . GLU A 1 69  ? 8.210   6.568   5.634   1.00 10.25  ? 69  GLU A N   1 
ATOM   543  C  CA  . GLU A 1 69  ? 8.317   7.941   6.087   1.00 10.82  ? 69  GLU A CA  1 
ATOM   544  C  C   . GLU A 1 69  ? 6.984   8.628   6.072   1.00 10.16  ? 69  GLU A C   1 
ATOM   545  O  O   . GLU A 1 69  ? 6.181   8.374   5.105   1.00 11.99  ? 69  GLU A O   1 
ATOM   546  C  CB  . GLU A 1 69  ? 9.205   8.677   5.162   1.00 12.03  ? 69  GLU A CB  1 
ATOM   547  C  CG  . GLU A 1 69  ? 10.599  8.116   5.191   1.00 12.42  ? 69  GLU A CG  1 
ATOM   548  C  CD  . GLU A 1 69  ? 11.453  8.576   4.032   1.00 13.58  ? 69  GLU A CD  1 
ATOM   549  O  OE1 . GLU A 1 69  ? 10.938  9.323   3.165   1.00 14.23  ? 69  GLU A OE1 1 
ATOM   550  O  OE2 . GLU A 1 69  ? 12.673  8.239   3.976   1.00 14.60  ? 69  GLU A OE2 1 
ATOM   551  N  N   . PHE A 1 70  ? 6.742   9.532   7.013   1.00 10.38  ? 70  PHE A N   1 
ATOM   552  C  CA  . PHE A 1 70  ? 5.502   10.242  7.113   1.00 10.49  ? 70  PHE A CA  1 
ATOM   553  C  C   . PHE A 1 70  ? 5.718   11.737  7.091   1.00 11.17  ? 70  PHE A C   1 
ATOM   554  O  O   . PHE A 1 70  ? 6.823   12.226  7.465   1.00 12.30  ? 70  PHE A O   1 
ATOM   555  C  CB  . PHE A 1 70  ? 4.786   9.866   8.420   1.00 11.09  ? 70  PHE A CB  1 
ATOM   556  C  CG  . PHE A 1 70  ? 4.258   8.472   8.390   1.00 10.55  ? 70  PHE A CG  1 
ATOM   557  C  CD1 . PHE A 1 70  ? 5.080   7.372   8.575   1.00 10.74  ? 70  PHE A CD1 1 
ATOM   558  C  CD2 . PHE A 1 70  ? 2.927   8.267   8.074   1.00 10.50  ? 70  PHE A CD2 1 
ATOM   559  C  CE1 . PHE A 1 70  ? 4.588   6.102   8.431   1.00 11.46  ? 70  PHE A CE1 1 
ATOM   560  C  CE2 . PHE A 1 70  ? 2.448   6.980   7.899   1.00 11.60  ? 70  PHE A CE2 1 
ATOM   561  C  CZ  . PHE A 1 70  ? 3.294   5.877   8.109   1.00 12.50  ? 70  PHE A CZ  1 
ATOM   562  N  N   . ASP A 1 71  ? 4.714   12.472  6.670   1.00 12.33  ? 71  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 71  ? 4.752   13.942  6.825   1.00 12.59  ? 71  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 71  ? 4.591   14.255  8.268   1.00 12.01  ? 71  ASP A C   1 
ATOM   565  O  O   . ASP A 1 71  ? 3.513   14.028  8.832   1.00 16.46  ? 71  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 71  ? 3.597   14.521  6.021   1.00 14.62  ? 71  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 71  ? 3.419   16.040  6.266   1.00 15.38  ? 71  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 71  ? 4.392   16.670  6.765   1.00 16.49  ? 71  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 71  ? 2.316   16.564  5.958   1.00 21.72  ? 71  ASP A OD2 1 
ATOM   570  N  N   . ASP A 1 72  ? 5.640   14.789  8.887   1.00 11.89  ? 72  ASP A N   1 
ATOM   571  C  CA  . ASP A 1 72  ? 5.631   15.155  10.294  1.00 12.08  ? 72  ASP A CA  1 
ATOM   572  C  C   . ASP A 1 72  ? 5.679   16.690  10.446  1.00 13.86  ? 72  ASP A C   1 
ATOM   573  O  O   . ASP A 1 72  ? 6.157   17.173  11.460  1.00 16.18  ? 72  ASP A O   1 
ATOM   574  C  CB  . ASP A 1 72  ? 6.744   14.484  11.053  1.00 12.70  ? 72  ASP A CB  1 
ATOM   575  C  CG  . ASP A 1 72  ? 8.077   14.981  10.636  1.00 13.64  ? 72  ASP A CG  1 
ATOM   576  O  OD1 . ASP A 1 72  ? 8.137   15.675  9.534   1.00 16.62  ? 72  ASP A OD1 1 
ATOM   577  O  OD2 . ASP A 1 72  ? 9.066   14.752  11.349  1.00 16.02  ? 72  ASP A OD2 1 
ATOM   578  N  N   . SER A 1 73  ? 5.160   17.414  9.460   1.00 14.27  ? 73  SER A N   1 
ATOM   579  C  CA  . SER A 1 73  ? 5.226   18.886  9.514   1.00 16.20  ? 73  SER A CA  1 
ATOM   580  C  C   . SER A 1 73  ? 3.900   19.451  10.157  1.00 15.87  ? 73  SER A C   1 
ATOM   581  O  O   . SER A 1 73  ? 3.779   20.677  10.236  1.00 16.95  ? 73  SER A O   1 
ATOM   582  C  CB  . SER A 1 73  ? 5.515   19.413  8.135   1.00 17.71  ? 73  SER A CB  1 
ATOM   583  O  OG  . SER A 1 73  ? 4.370   19.283  7.326   1.00 16.38  ? 73  SER A OG  1 
ATOM   584  N  N   . GLN A 1 74  ? 2.966   18.586  10.572  1.00 16.59  ? 74  GLN A N   1 
ATOM   585  C  CA  . GLN A 1 74  ? 1.798   18.946  11.379  1.00 19.37  ? 74  GLN A CA  1 
ATOM   586  C  C   . GLN A 1 74  ? 1.450   17.788  12.208  1.00 18.12  ? 74  GLN A C   1 
ATOM   587  O  O   . GLN A 1 74  ? 1.968   16.729  11.945  1.00 17.55  ? 74  GLN A O   1 
ATOM   588  C  CB  . GLN A 1 74  ? 0.551   19.132  10.505  1.00 21.06  ? 74  GLN A CB  1 
ATOM   589  C  CG  . GLN A 1 74  ? 0.666   20.236  9.533   1.00 23.96  ? 74  GLN A CG  1 
ATOM   590  C  CD  . GLN A 1 74  ? -0.646  20.419  8.861   1.00 29.94  ? 74  GLN A CD  1 
ATOM   591  O  OE1 . GLN A 1 74  ? -1.562  21.029  9.445   1.00 35.52  ? 74  GLN A OE1 1 
ATOM   592  N  NE2 . GLN A 1 74  ? -0.777  19.913  7.657   1.00 26.47  ? 74  GLN A NE2 1 
ATOM   593  N  N   . ASP A 1 75  ? 0.545   17.993  13.214  1.00 22.77  ? 75  ASP A N   1 
ATOM   594  C  CA  . ASP A 1 75  ? 0.091   16.937  14.098  1.00 24.85  ? 75  ASP A CA  1 
ATOM   595  C  C   . ASP A 1 75  ? -0.924  16.180  13.315  1.00 21.22  ? 75  ASP A C   1 
ATOM   596  O  O   . ASP A 1 75  ? -2.126  16.534  13.343  1.00 38.84  ? 75  ASP A O   1 
ATOM   597  C  CB  . ASP A 1 75  ? -0.545  17.414  15.409  1.00 27.62  ? 75  ASP A CB  1 
ATOM   598  C  CG  . ASP A 1 75  ? 0.457   18.019  16.354  1.00 26.46  ? 75  ASP A CG  1 
ATOM   599  O  OD1 . ASP A 1 75  ? 1.646   17.914  16.137  1.00 33.66  ? 75  ASP A OD1 1 
ATOM   600  O  OD2 . ASP A 1 75  ? 0.062   18.574  17.381  1.00 37.00  ? 75  ASP A OD2 1 
ATOM   601  N  N   A LYS A 1 76  ? -0.490  15.248  12.534  0.50 19.65  ? 76  LYS A N   1 
ATOM   602  N  N   B LYS A 1 76  ? -0.480  15.137  12.590  0.50 18.42  ? 76  LYS A N   1 
ATOM   603  C  CA  A LYS A 1 76  ? -1.394  14.340  11.969  0.50 20.52  ? 76  LYS A CA  1 
ATOM   604  C  CA  B LYS A 1 76  ? -1.230  14.227  11.693  0.50 15.85  ? 76  LYS A CA  1 
ATOM   605  C  C   A LYS A 1 76  ? -1.283  13.113  12.835  0.50 20.49  ? 76  LYS A C   1 
ATOM   606  C  C   B LYS A 1 76  ? -1.316  12.798  12.165  0.50 13.50  ? 76  LYS A C   1 
ATOM   607  O  O   A LYS A 1 76  ? -1.999  13.005  13.818  0.50 27.78  ? 76  LYS A O   1 
ATOM   608  O  O   B LYS A 1 76  ? -2.319  12.062  11.960  0.50 15.64  ? 76  LYS A O   1 
ATOM   609  C  CB  A LYS A 1 76  ? -0.930  14.140  10.545  0.50 21.66  ? 76  LYS A CB  1 
ATOM   610  C  CB  B LYS A 1 76  ? -0.534  14.178  10.349  0.50 17.07  ? 76  LYS A CB  1 
ATOM   611  C  CG  A LYS A 1 76  ? -1.227  15.337  9.659   0.50 30.84  ? 76  LYS A CG  1 
ATOM   612  C  CG  B LYS A 1 76  ? -0.843  15.364  9.487   0.50 18.87  ? 76  LYS A CG  1 
ATOM   613  C  CD  A LYS A 1 76  ? -0.463  15.282  8.341   0.50 30.50  ? 76  LYS A CD  1 
ATOM   614  C  CD  B LYS A 1 76  ? -0.181  15.161  8.151   0.50 18.91  ? 76  LYS A CD  1 
ATOM   615  C  CE  A LYS A 1 76  ? -1.167  16.150  7.329   0.50 26.93  ? 76  LYS A CE  1 
ATOM   616  C  CE  B LYS A 1 76  ? -0.717  16.170  7.187   0.50 20.72  ? 76  LYS A CE  1 
ATOM   617  N  NZ  A LYS A 1 76  ? -0.633  15.992  5.959   0.50 29.96  ? 76  LYS A NZ  1 
ATOM   618  N  NZ  B LYS A 1 76  ? -0.321  15.732  5.847   0.50 19.59  ? 76  LYS A NZ  1 
ATOM   619  N  N   A ALA A 1 77  ? -0.435  12.161  12.490  0.50 18.46  ? 77  ALA A N   1 
ATOM   620  N  N   B ALA A 1 77  ? -0.297  12.411  12.882  0.50 13.86  ? 77  ALA A N   1 
ATOM   621  C  CA  A ALA A 1 77  ? -0.362  10.925  13.322  0.50 15.99  ? 77  ALA A CA  1 
ATOM   622  C  CA  B ALA A 1 77  ? -0.144  10.998  13.319  0.50 14.25  ? 77  ALA A CA  1 
ATOM   623  C  C   A ALA A 1 77  ? 0.471   11.229  14.582  0.50 13.30  ? 77  ALA A C   1 
ATOM   624  C  C   B ALA A 1 77  ? 0.585   11.063  14.641  0.50 13.58  ? 77  ALA A C   1 
ATOM   625  O  O   A ALA A 1 77  ? 1.620   11.679  14.470  0.50 14.92  ? 77  ALA A O   1 
ATOM   626  O  O   B ALA A 1 77  ? 1.784   11.158  14.650  0.50 14.91  ? 77  ALA A O   1 
ATOM   627  C  CB  A ALA A 1 77  ? 0.210   9.787   12.470  0.50 17.99  ? 77  ALA A CB  1 
ATOM   628  C  CB  B ALA A 1 77  ? 0.688   10.287  12.245  0.50 14.24  ? 77  ALA A CB  1 
ATOM   629  N  N   . VAL A 1 78  ? -0.124  11.007  15.738  1.00 12.99  ? 78  VAL A N   1 
ATOM   630  C  CA  . VAL A 1 78  ? 0.521   11.305  16.994  1.00 12.96  ? 78  VAL A CA  1 
ATOM   631  C  C   . VAL A 1 78  ? 0.292   10.207  18.017  1.00 13.34  ? 78  VAL A C   1 
ATOM   632  O  O   . VAL A 1 78  ? -0.732  9.512   17.991  1.00 15.01  ? 78  VAL A O   1 
ATOM   633  C  CB  . VAL A 1 78  ? 0.145   12.653  17.520  1.00 16.84  ? 78  VAL A CB  1 
ATOM   634  C  CG1 . VAL A 1 78  ? 0.494   13.817  16.644  1.00 17.50  ? 78  VAL A CG1 1 
ATOM   635  C  CG2 . VAL A 1 78  ? -1.283  12.641  17.854  1.00 20.47  ? 78  VAL A CG2 1 
ATOM   636  N  N   . LEU A 1 79  ? 1.237   10.115  18.920  1.00 11.85  ? 79  LEU A N   1 
ATOM   637  C  CA  . LEU A 1 79  ? 1.185   9.249   20.083  1.00 12.50  ? 79  LEU A CA  1 
ATOM   638  C  C   . LEU A 1 79  ? 1.177   10.139  21.283  1.00 12.09  ? 79  LEU A C   1 
ATOM   639  O  O   . LEU A 1 79  ? 2.021   11.088  21.407  1.00 13.74  ? 79  LEU A O   1 
ATOM   640  C  CB  . LEU A 1 79  ? 2.437   8.342   20.046  1.00 13.40  ? 79  LEU A CB  1 
ATOM   641  C  CG  . LEU A 1 79  ? 2.547   7.276   21.057  1.00 13.74  ? 79  LEU A CG  1 
ATOM   642  C  CD1 . LEU A 1 79  ? 1.492   6.234   20.877  1.00 17.97  ? 79  LEU A CD1 1 
ATOM   643  C  CD2 . LEU A 1 79  ? 3.942   6.631   20.998  1.00 13.72  ? 79  LEU A CD2 1 
ATOM   644  N  N   A LYS A 1 80  ? 0.365   9.775   22.260  0.50 12.72  ? 80  LYS A N   1 
ATOM   645  N  N   B LYS A 1 80  ? 0.239   9.863   22.183  0.50 13.05  ? 80  LYS A N   1 
ATOM   646  C  CA  A LYS A 1 80  ? 0.370   10.484  23.532  0.50 12.96  ? 80  LYS A CA  1 
ATOM   647  C  CA  B LYS A 1 80  ? 0.080   10.587  23.461  0.50 13.10  ? 80  LYS A CA  1 
ATOM   648  C  C   A LYS A 1 80  ? -0.269  9.577   24.538  0.50 13.31  ? 80  LYS A C   1 
ATOM   649  C  C   B LYS A 1 80  ? -0.297  9.583   24.516  0.50 13.41  ? 80  LYS A C   1 
ATOM   650  O  O   A LYS A 1 80  ? -0.590  8.425   24.262  0.50 13.45  ? 80  LYS A O   1 
ATOM   651  O  O   B LYS A 1 80  ? -0.524  8.401   24.239  0.50 13.22  ? 80  LYS A O   1 
ATOM   652  C  CB  A LYS A 1 80  ? -0.306  11.853  23.400  0.50 16.04  ? 80  LYS A CB  1 
ATOM   653  C  CB  B LYS A 1 80  ? -1.030  11.662  23.406  0.50 16.97  ? 80  LYS A CB  1 
ATOM   654  C  CG  A LYS A 1 80  ? -1.815  11.711  23.067  0.50 16.59  ? 80  LYS A CG  1 
ATOM   655  C  CG  B LYS A 1 80  ? -1.012  12.638  22.219  0.50 18.04  ? 80  LYS A CG  1 
ATOM   656  C  CD  A LYS A 1 80  ? -2.498  13.058  22.925  0.50 20.27  ? 80  LYS A CD  1 
ATOM   657  C  CD  B LYS A 1 80  ? -2.277  13.505  22.168  0.50 21.15  ? 80  LYS A CD  1 
ATOM   658  C  CE  A LYS A 1 80  ? -2.015  13.788  21.654  0.50 28.50  ? 80  LYS A CE  1 
ATOM   659  C  CE  B LYS A 1 80  ? -2.970  13.561  23.530  0.50 29.99  ? 80  LYS A CE  1 
ATOM   660  N  N   . GLY A 1 81  ? -0.450  10.084  25.739  1.00 14.18  ? 81  GLY A N   1 
ATOM   661  C  CA  . GLY A 1 81  ? -0.951  9.250   26.810  1.00 15.58  ? 81  GLY A CA  1 
ATOM   662  C  C   . GLY A 1 81  ? 0.069   8.208   27.149  1.00 13.61  ? 81  GLY A C   1 
ATOM   663  O  O   . GLY A 1 81  ? 1.284   8.428   27.013  1.00 13.78  ? 81  GLY A O   1 
ATOM   664  N  N   . GLY A 1 82  ? -0.406  7.079   27.636  1.00 15.93  ? 82  GLY A N   1 
ATOM   665  C  CA  . GLY A 1 82  ? 0.494   6.085   28.052  1.00 18.17  ? 82  GLY A CA  1 
ATOM   666  C  C   . GLY A 1 82  ? 1.414   6.689   29.179  1.00 16.72  ? 82  GLY A C   1 
ATOM   667  O  O   . GLY A 1 82  ? 0.932   7.385   30.105  1.00 20.83  ? 82  GLY A O   1 
ATOM   668  N  N   . PRO A 1 83  ? 2.716   6.485   29.064  1.00 14.92  ? 83  PRO A N   1 
ATOM   669  C  CA  . PRO A 1 83  ? 3.626   7.065   30.050  1.00 14.95  ? 83  PRO A CA  1 
ATOM   670  C  C   . PRO A 1 83  ? 4.068   8.482   29.689  1.00 16.34  ? 83  PRO A C   1 
ATOM   671  O  O   . PRO A 1 83  ? 4.849   9.047   30.428  1.00 18.98  ? 83  PRO A O   1 
ATOM   672  C  CB  . PRO A 1 83  ? 4.828   6.128   29.989  1.00 17.56  ? 83  PRO A CB  1 
ATOM   673  C  CG  . PRO A 1 83  ? 4.854   5.667   28.570  1.00 15.22  ? 83  PRO A CG  1 
ATOM   674  C  CD  . PRO A 1 83  ? 3.428   5.641   28.086  1.00 14.31  ? 83  PRO A CD  1 
ATOM   675  N  N   . LEU A 1 84  ? 3.611   9.031   28.576  1.00 13.80  ? 84  LEU A N   1 
ATOM   676  C  CA  . LEU A 1 84  ? 4.196   10.226  27.980  1.00 13.88  ? 84  LEU A CA  1 
ATOM   677  C  C   . LEU A 1 84  ? 3.531   11.477  28.535  1.00 15.83  ? 84  LEU A C   1 
ATOM   678  O  O   . LEU A 1 84  ? 2.332   11.504  28.828  1.00 19.08  ? 84  LEU A O   1 
ATOM   679  C  CB  . LEU A 1 84  ? 3.933   10.219  26.494  1.00 12.23  ? 84  LEU A CB  1 
ATOM   680  C  CG  . LEU A 1 84  ? 4.526   8.967   25.775  1.00 11.74  ? 84  LEU A CG  1 
ATOM   681  C  CD1 . LEU A 1 84  ? 4.070   8.917   24.339  1.00 12.77  ? 84  LEU A CD1 1 
ATOM   682  C  CD2 . LEU A 1 84  ? 6.064   8.935   25.913  1.00 12.29  ? 84  LEU A CD2 1 
ATOM   683  N  N   A ASP A 1 85  ? 4.330   12.545  28.531  0.50 19.27  ? 85  ASP A N   1 
ATOM   684  N  N   B ASP A 1 85  ? 4.268   12.555  28.612  0.50 17.08  ? 85  ASP A N   1 
ATOM   685  C  CA  A ASP A 1 85  ? 3.924   13.966  28.663  0.50 23.32  ? 85  ASP A CA  1 
ATOM   686  C  CA  B ASP A 1 85  ? 3.705   13.793  29.123  0.50 17.33  ? 85  ASP A CA  1 
ATOM   687  C  C   A ASP A 1 85  ? 3.851   14.629  27.351  0.50 17.67  ? 85  ASP A C   1 
ATOM   688  C  C   B ASP A 1 85  ? 3.508   14.754  28.000  0.50 16.77  ? 85  ASP A C   1 
ATOM   689  O  O   A ASP A 1 85  ? 4.773   14.585  26.568  0.50 20.16  ? 85  ASP A O   1 
ATOM   690  O  O   B ASP A 1 85  ? 3.295   15.912  28.278  0.50 19.72  ? 85  ASP A O   1 
ATOM   691  C  CB  A ASP A 1 85  ? 5.016   14.759  29.352  0.50 29.82  ? 85  ASP A CB  1 
ATOM   692  C  CB  B ASP A 1 85  ? 4.734   14.437  30.086  0.50 19.14  ? 85  ASP A CB  1 
ATOM   693  C  CG  A ASP A 1 85  ? 4.920   14.656  30.776  0.50 34.14  ? 85  ASP A CG  1 
ATOM   694  C  CG  B ASP A 1 85  ? 4.676   13.865  31.481  0.50 24.61  ? 85  ASP A CG  1 
ATOM   695  O  OD1 A ASP A 1 85  ? 3.776   14.297  31.205  0.50 40.55  ? 85  ASP A OD1 1 
ATOM   696  O  OD1 B ASP A 1 85  ? 3.657   13.208  31.795  0.50 25.01  ? 85  ASP A OD1 1 
ATOM   697  O  OD2 A ASP A 1 85  ? 5.976   14.904  31.434  0.50 34.19  ? 85  ASP A OD2 1 
ATOM   698  O  OD2 B ASP A 1 85  ? 5.647   14.067  32.294  0.50 30.49  ? 85  ASP A OD2 1 
ATOM   699  N  N   A GLY A 1 86  ? 2.765   15.288  27.064  0.50 19.51  ? 86  GLY A N   1 
ATOM   700  N  N   B GLY A 1 86  ? 3.551   14.364  26.759  0.50 15.57  ? 86  GLY A N   1 
ATOM   701  C  CA  A GLY A 1 86  ? 2.742   15.912  25.786  0.50 19.01  ? 86  GLY A CA  1 
ATOM   702  C  CA  B GLY A 1 86  ? 3.683   15.288  25.689  0.50 19.59  ? 86  GLY A CA  1 
ATOM   703  C  C   A GLY A 1 86  ? 2.476   14.998  24.554  0.50 21.64  ? 86  GLY A C   1 
ATOM   704  C  C   B GLY A 1 86  ? 3.083   14.621  24.465  0.50 18.65  ? 86  GLY A C   1 
ATOM   705  O  O   A GLY A 1 86  ? 1.857   13.922  24.658  0.50 24.94  ? 86  GLY A O   1 
ATOM   706  O  O   B GLY A 1 86  ? 2.580   13.479  24.546  0.50 20.80  ? 86  GLY A O   1 
ATOM   707  N  N   . THR A 1 87  ? 3.003   15.394  23.374  1.00 15.86  ? 87  THR A N   1 
ATOM   708  C  CA  . THR A 1 87  ? 2.553   14.852  22.117  1.00 16.70  ? 87  THR A CA  1 
ATOM   709  C  C   . THR A 1 87  ? 3.737   14.529  21.273  1.00 13.06  ? 87  THR A C   1 
ATOM   710  O  O   . THR A 1 87  ? 4.662   15.347  21.164  1.00 13.65  ? 87  THR A O   1 
ATOM   711  C  CB  . THR A 1 87  ? 1.695   15.933  21.358  1.00 20.25  ? 87  THR A CB  1 
ATOM   712  O  OG1 . THR A 1 87  ? 0.545   16.239  22.141  1.00 26.87  ? 87  THR A OG1 1 
ATOM   713  C  CG2 . THR A 1 87  ? 1.277   15.482  19.948  1.00 20.57  ? 87  THR A CG2 1 
ATOM   714  N  N   . TYR A 1 88  ? 3.695   13.370  20.681  1.00 11.59  ? 88  TYR A N   1 
ATOM   715  C  CA  . TYR A 1 88  ? 4.849   12.897  19.868  1.00 10.85  ? 88  TYR A CA  1 
ATOM   716  C  C   . TYR A 1 88  ? 4.340   12.589  18.483  1.00 10.87  ? 88  TYR A C   1 
ATOM   717  O  O   . TYR A 1 88  ? 3.399   11.836  18.280  1.00 13.60  ? 88  TYR A O   1 
ATOM   718  C  CB  . TYR A 1 88  ? 5.457   11.656  20.469  1.00 11.46  ? 88  TYR A CB  1 
ATOM   719  C  CG  . TYR A 1 88  ? 6.176   11.889  21.785  1.00 10.23  ? 88  TYR A CG  1 
ATOM   720  C  CD1 . TYR A 1 88  ? 5.484   12.200  22.962  1.00 11.29  ? 88  TYR A CD1 1 
ATOM   721  C  CD2 . TYR A 1 88  ? 7.570   11.742  21.862  1.00 10.24  ? 88  TYR A CD2 1 
ATOM   722  C  CE1 . TYR A 1 88  ? 6.203   12.377  24.140  1.00 11.04  ? 88  TYR A CE1 1 
ATOM   723  C  CE2 . TYR A 1 88  ? 8.278   11.870  23.040  1.00 9.28   ? 88  TYR A CE2 1 
ATOM   724  C  CZ  . TYR A 1 88  ? 7.588   12.169  24.205  1.00 10.10  ? 88  TYR A CZ  1 
ATOM   725  O  OH  . TYR A 1 88  ? 8.283   12.276  25.370  1.00 10.31  ? 88  TYR A OH  1 
ATOM   726  N  N   A ARG A 1 89  ? 4.994   13.122  17.476  0.50 10.46  ? 89  ARG A N   1 
ATOM   727  N  N   B ARG A 1 89  ? 5.021   13.097  17.500  0.50 10.63  ? 89  ARG A N   1 
ATOM   728  C  CA  A ARG A 1 89  ? 4.576   12.984  16.061  0.50 11.56  ? 89  ARG A CA  1 
ATOM   729  C  CA  B ARG A 1 89  ? 4.591   12.988  16.135  0.50 11.33  ? 89  ARG A CA  1 
ATOM   730  C  C   A ARG A 1 89  ? 5.316   11.861  15.419  0.50 8.87   ? 89  ARG A C   1 
ATOM   731  C  C   B ARG A 1 89  ? 5.324   11.870  15.412  0.50 8.87   ? 89  ARG A C   1 
ATOM   732  O  O   A ARG A 1 89  ? 6.551   11.749  15.492  0.50 8.73   ? 89  ARG A O   1 
ATOM   733  O  O   B ARG A 1 89  ? 6.552   11.733  15.486  0.50 8.73   ? 89  ARG A O   1 
ATOM   734  C  CB  A ARG A 1 89  ? 4.969   14.225  15.224  0.50 13.64  ? 89  ARG A CB  1 
ATOM   735  C  CB  B ARG A 1 89  ? 4.928   14.321  15.496  0.50 14.70  ? 89  ARG A CB  1 
ATOM   736  C  CG  A ARG A 1 89  ? 4.147   15.450  15.414  0.50 17.03  ? 89  ARG A CG  1 
ATOM   737  C  CG  B ARG A 1 89  ? 4.200   14.428  14.238  0.50 14.80  ? 89  ARG A CG  1 
ATOM   738  C  CD  A ARG A 1 89  ? 4.481   16.438  14.333  0.50 21.61  ? 89  ARG A CD  1 
ATOM   739  C  CD  B ARG A 1 89  ? 4.442   15.831  13.684  0.50 14.52  ? 89  ARG A CD  1 
ATOM   740  N  NE  A ARG A 1 89  ? 3.752   17.628  14.734  0.50 21.61  ? 89  ARG A NE  1 
ATOM   741  N  NE  B ARG A 1 89  ? 3.814   16.792  14.539  0.50 16.08  ? 89  ARG A NE  1 
ATOM   742  C  CZ  A ARG A 1 89  ? 4.061   18.875  14.381  0.50 22.34  ? 89  ARG A CZ  1 
ATOM   743  C  CZ  B ARG A 1 89  ? 3.925   18.087  14.403  0.50 12.82  ? 89  ARG A CZ  1 
ATOM   744  N  NH1 A ARG A 1 89  ? 5.071   19.086  13.509  0.50 20.23  ? 89  ARG A NH1 1 
ATOM   745  N  NH1 B ARG A 1 89  ? 4.595   18.614  13.449  0.50 18.31  ? 89  ARG A NH1 1 
ATOM   746  N  NH2 A ARG A 1 89  ? 3.318   19.901  14.871  0.50 23.90  ? 89  ARG A NH2 1 
ATOM   747  N  NH2 B ARG A 1 89  ? 3.319   18.945  15.195  0.50 16.58  ? 89  ARG A NH2 1 
ATOM   748  N  N   . LEU A 1 90  ? 4.542   11.041  14.674  1.00 9.44   ? 90  LEU A N   1 
ATOM   749  C  CA  . LEU A 1 90  ? 5.123   9.924   13.888  1.00 9.30   ? 90  LEU A CA  1 
ATOM   750  C  C   . LEU A 1 90  ? 5.969   10.472  12.745  1.00 9.56   ? 90  LEU A C   1 
ATOM   751  O  O   . LEU A 1 90  ? 5.471   11.270  11.919  1.00 11.42  ? 90  LEU A O   1 
ATOM   752  C  CB  . LEU A 1 90  ? 4.020   9.073   13.348  1.00 10.16  ? 90  LEU A CB  1 
ATOM   753  C  CG  . LEU A 1 90  ? 4.446   7.894   12.459  1.00 10.74  ? 90  LEU A CG  1 
ATOM   754  C  CD1 . LEU A 1 90  ? 5.226   6.838   13.271  1.00 10.89  ? 90  LEU A CD1 1 
ATOM   755  C  CD2 . LEU A 1 90  ? 3.218   7.218   11.844  1.00 12.30  ? 90  LEU A CD2 1 
ATOM   756  N  N   . ILE A 1 91  ? 7.226   10.062  12.669  1.00 8.80   ? 91  ILE A N   1 
ATOM   757  C  CA  . ILE A 1 91  ? 8.109   10.400  11.560  1.00 9.15   ? 91  ILE A CA  1 
ATOM   758  C  C   . ILE A 1 91  ? 8.342   9.242   10.643  1.00 7.98   ? 91  ILE A C   1 
ATOM   759  O  O   . ILE A 1 91  ? 8.446   9.451   9.420   1.00 8.91   ? 91  ILE A O   1 
ATOM   760  C  CB  . ILE A 1 91  ? 9.414   11.066  12.071  1.00 9.72   ? 91  ILE A CB  1 
ATOM   761  C  CG1 . ILE A 1 91  ? 10.334  11.447  10.907  1.00 11.82  ? 91  ILE A CG1 1 
ATOM   762  C  CG2 . ILE A 1 91  ? 10.135  10.240  13.132  1.00 10.24  ? 91  ILE A CG2 1 
ATOM   763  C  CD1 . ILE A 1 91  ? 11.437  12.358  11.343  1.00 13.60  ? 91  ILE A CD1 1 
ATOM   764  N  N   . GLN A 1 92  ? 8.514   8.017   11.161  1.00 8.24   ? 92  GLN A N   1 
ATOM   765  C  CA  . GLN A 1 92  ? 8.783   6.878   10.311  1.00 8.03   ? 92  GLN A CA  1 
ATOM   766  C  C   . GLN A 1 92  ? 8.539   5.636   11.071  1.00 7.72   ? 92  GLN A C   1 
ATOM   767  O  O   . GLN A 1 92  ? 8.504   5.657   12.320  1.00 8.19   ? 92  GLN A O   1 
ATOM   768  C  CB  . GLN A 1 92  ? 10.225  6.885   9.819   1.00 9.57   ? 92  GLN A CB  1 
ATOM   769  C  CG  . GLN A 1 92  ? 11.322  6.986   10.938  1.00 10.11  ? 92  GLN A CG  1 
ATOM   770  C  CD  . GLN A 1 92  ? 12.088  5.717   11.129  1.00 8.90   ? 92  GLN A CD  1 
ATOM   771  O  OE1 . GLN A 1 92  ? 11.549  4.613   11.188  1.00 9.46   ? 92  GLN A OE1 1 
ATOM   772  N  NE2 . GLN A 1 92  ? 13.377  5.836   11.270  1.00 11.98  ? 92  GLN A NE2 1 
ATOM   773  N  N   . PHE A 1 93  ? 8.369   4.520   10.366  1.00 7.80   ? 93  PHE A N   1 
ATOM   774  C  CA  . PHE A 1 93  ? 8.501   3.235   10.985  1.00 7.92   ? 93  PHE A CA  1 
ATOM   775  C  C   . PHE A 1 93  ? 9.474   2.400   10.189  1.00 7.59   ? 93  PHE A C   1 
ATOM   776  O  O   . PHE A 1 93  ? 9.721   2.593   8.979   1.00 8.61   ? 93  PHE A O   1 
ATOM   777  C  CB  . PHE A 1 93  ? 7.176   2.508   11.223  1.00 8.46   ? 93  PHE A CB  1 
ATOM   778  C  CG  . PHE A 1 93  ? 6.427   2.021   10.016  1.00 8.32   ? 93  PHE A CG  1 
ATOM   779  C  CD1 . PHE A 1 93  ? 6.792   0.896   9.315   1.00 9.14   ? 93  PHE A CD1 1 
ATOM   780  C  CD2 . PHE A 1 93  ? 5.302   2.728   9.557   1.00 9.07   ? 93  PHE A CD2 1 
ATOM   781  C  CE1 . PHE A 1 93  ? 6.088   0.464   8.198   1.00 9.56   ? 93  PHE A CE1 1 
ATOM   782  C  CE2 . PHE A 1 93  ? 4.594   2.264   8.449   1.00 10.22  ? 93  PHE A CE2 1 
ATOM   783  C  CZ  . PHE A 1 93  ? 4.988   1.147   7.771   1.00 10.35  ? 93  PHE A CZ  1 
ATOM   784  N  N   . HIS A 1 94  ? 10.042  1.376   10.870  1.00 7.55   ? 94  HIS A N   1 
ATOM   785  C  CA  . HIS A 1 94  ? 10.935  0.408   10.295  1.00 7.79   ? 94  HIS A CA  1 
ATOM   786  C  C   . HIS A 1 94  ? 10.851  -0.860  11.102  1.00 7.11   ? 94  HIS A C   1 
ATOM   787  O  O   . HIS A 1 94  ? 10.230  -0.889  12.154  1.00 7.60   ? 94  HIS A O   1 
ATOM   788  C  CB  . HIS A 1 94  ? 12.391  0.931   10.212  1.00 8.52   ? 94  HIS A CB  1 
ATOM   789  C  CG  . HIS A 1 94  ? 12.912  1.199   11.610  1.00 7.36   ? 94  HIS A CG  1 
ATOM   790  N  ND1 . HIS A 1 94  ? 12.682  2.361   12.277  1.00 7.50   ? 94  HIS A ND1 1 
ATOM   791  C  CD2 . HIS A 1 94  ? 13.554  0.364   12.474  1.00 7.38   ? 94  HIS A CD2 1 
ATOM   792  C  CE1 . HIS A 1 94  ? 13.184  2.234   13.509  1.00 7.31   ? 94  HIS A CE1 1 
ATOM   793  N  NE2 . HIS A 1 94  ? 13.711  1.014   13.677  1.00 7.25   ? 94  HIS A NE2 1 
ATOM   794  N  N   . PHE A 1 95  ? 11.515  -1.899  10.621  1.00 7.45   ? 95  PHE A N   1 
ATOM   795  C  CA  . PHE A 1 95  ? 11.592  -3.192  11.279  1.00 7.44   ? 95  PHE A CA  1 
ATOM   796  C  C   . PHE A 1 95  ? 12.993  -3.624  11.497  1.00 7.38   ? 95  PHE A C   1 
ATOM   797  O  O   . PHE A 1 95  ? 13.924  -3.175  10.820  1.00 8.42   ? 95  PHE A O   1 
ATOM   798  C  CB  . PHE A 1 95  ? 10.837  -4.285  10.450  1.00 8.26   ? 95  PHE A CB  1 
ATOM   799  C  CG  . PHE A 1 95  ? 9.412   -3.998  10.125  1.00 7.48   ? 95  PHE A CG  1 
ATOM   800  C  CD1 . PHE A 1 95  ? 9.102   -3.140  9.069   1.00 9.08   ? 95  PHE A CD1 1 
ATOM   801  C  CD2 . PHE A 1 95  ? 8.380   -4.634  10.795  1.00 8.64   ? 95  PHE A CD2 1 
ATOM   802  C  CE1 . PHE A 1 95  ? 7.752   -2.947  8.743   1.00 9.74   ? 95  PHE A CE1 1 
ATOM   803  C  CE2 . PHE A 1 95  ? 7.065   -4.451  10.455  1.00 9.38   ? 95  PHE A CE2 1 
ATOM   804  C  CZ  . PHE A 1 95  ? 6.754   -3.575  9.407   1.00 9.35   ? 95  PHE A CZ  1 
ATOM   805  N  N   . HIS A 1 96  ? 13.164  -4.608  12.398  1.00 7.08   ? 96  HIS A N   1 
ATOM   806  C  CA  . HIS A 1 96  ? 14.354  -5.408  12.568  1.00 7.40   ? 96  HIS A CA  1 
ATOM   807  C  C   . HIS A 1 96  ? 13.928  -6.848  12.423  1.00 7.11   ? 96  HIS A C   1 
ATOM   808  O  O   . HIS A 1 96  ? 12.850  -7.206  12.932  1.00 7.87   ? 96  HIS A O   1 
ATOM   809  C  CB  . HIS A 1 96  ? 15.012  -5.178  13.949  1.00 7.67   ? 96  HIS A CB  1 
ATOM   810  C  CG  . HIS A 1 96  ? 15.278  -3.752  14.224  1.00 7.71   ? 96  HIS A CG  1 
ATOM   811  N  ND1 . HIS A 1 96  ? 16.516  -3.190  14.092  1.00 9.00   ? 96  HIS A ND1 1 
ATOM   812  C  CD2 . HIS A 1 96  ? 14.474  -2.729  14.620  1.00 7.09   ? 96  HIS A CD2 1 
ATOM   813  C  CE1 . HIS A 1 96  ? 16.427  -1.863  14.392  1.00 8.52   ? 96  HIS A CE1 1 
ATOM   814  N  NE2 . HIS A 1 96  ? 15.190  -1.580  14.701  1.00 6.84   ? 96  HIS A NE2 1 
ATOM   815  N  N   . TRP A 1 97  ? 14.682  -7.691  11.767  1.00 7.11   ? 97  TRP A N   1 
ATOM   816  C  CA  . TRP A 1 97  ? 14.310  -9.061  11.565  1.00 8.00   ? 97  TRP A CA  1 
ATOM   817  C  C   . TRP A 1 97  ? 15.475  -9.962  11.427  1.00 7.45   ? 97  TRP A C   1 
ATOM   818  O  O   . TRP A 1 97  ? 16.648  -9.540  11.340  1.00 8.35   ? 97  TRP A O   1 
ATOM   819  C  CB  . TRP A 1 97  ? 13.375  -9.164  10.302  1.00 8.29   ? 97  TRP A CB  1 
ATOM   820  C  CG  . TRP A 1 97  ? 14.023  -8.774  9.022   1.00 8.41   ? 97  TRP A CG  1 
ATOM   821  C  CD1 . TRP A 1 97  ? 14.676  -9.598  8.168   1.00 8.80   ? 97  TRP A CD1 1 
ATOM   822  C  CD2 . TRP A 1 97  ? 14.087  -7.488  8.460   1.00 8.30   ? 97  TRP A CD2 1 
ATOM   823  N  NE1 . TRP A 1 97  ? 15.110  -8.876  7.061   1.00 9.76   ? 97  TRP A NE1 1 
ATOM   824  C  CE2 . TRP A 1 97  ? 14.763  -7.576  7.236   1.00 9.01   ? 97  TRP A CE2 1 
ATOM   825  C  CE3 . TRP A 1 97  ? 13.595  -6.210  8.861   1.00 8.38   ? 97  TRP A CE3 1 
ATOM   826  C  CZ2 . TRP A 1 97  ? 14.923  -6.472  6.392   1.00 10.06  ? 97  TRP A CZ2 1 
ATOM   827  C  CZ3 . TRP A 1 97  ? 13.830  -5.123  8.047   1.00 9.25   ? 97  TRP A CZ3 1 
ATOM   828  C  CH2 . TRP A 1 97  ? 14.464  -5.240  6.801   1.00 9.51   ? 97  TRP A CH2 1 
ATOM   829  N  N   . GLY A 1 98  ? 15.207  -11.281 11.429  1.00 8.06   ? 98  GLY A N   1 
ATOM   830  C  CA  . GLY A 1 98  ? 16.232  -12.271 11.471  1.00 8.82   ? 98  GLY A CA  1 
ATOM   831  C  C   . GLY A 1 98  ? 16.462  -12.965 10.145  1.00 9.07   ? 98  GLY A C   1 
ATOM   832  O  O   . GLY A 1 98  ? 15.705  -12.813 9.179   1.00 10.42  ? 98  GLY A O   1 
ATOM   833  N  N   . SER A 1 99  ? 17.465  -13.822 10.156  1.00 9.85   ? 99  SER A N   1 
ATOM   834  C  CA  . SER A 1 99  ? 17.704  -14.788 9.045   1.00 11.61  ? 99  SER A CA  1 
ATOM   835  C  C   . SER A 1 99  ? 16.828  -16.017 9.153   1.00 12.91  ? 99  SER A C   1 
ATOM   836  O  O   . SER A 1 99  ? 16.742  -16.770 8.188   1.00 14.52  ? 99  SER A O   1 
ATOM   837  C  CB  . SER A 1 99  ? 19.130  -15.126 9.012   1.00 12.94  ? 99  SER A CB  1 
ATOM   838  O  OG  . SER A 1 99  ? 19.595  -15.635 10.260  1.00 12.72  ? 99  SER A OG  1 
ATOM   839  N  N   . LEU A 1 100 ? 16.221  -16.240 10.343  1.00 11.47  ? 100 LEU A N   1 
ATOM   840  C  CA  . LEU A 1 100 ? 15.427  -17.406 10.719  1.00 13.45  ? 100 LEU A CA  1 
ATOM   841  C  C   . LEU A 1 100 ? 14.296  -16.928 11.526  1.00 11.49  ? 100 LEU A C   1 
ATOM   842  O  O   . LEU A 1 100 ? 14.445  -15.897 12.216  1.00 11.55  ? 100 LEU A O   1 
ATOM   843  C  CB  . LEU A 1 100 ? 16.285  -18.327 11.704  1.00 17.42  ? 100 LEU A CB  1 
ATOM   844  C  CG  . LEU A 1 100 ? 17.526  -18.776 11.051  1.00 19.28  ? 100 LEU A CG  1 
ATOM   845  C  CD1 . LEU A 1 100 ? 18.617  -19.194 12.030  1.00 28.36  ? 100 LEU A CD1 1 
ATOM   846  C  CD2 . LEU A 1 100 ? 17.165  -19.853 10.046  1.00 25.88  ? 100 LEU A CD2 1 
ATOM   847  N  N   . ASP A 1 101 ? 13.206  -17.666 11.567  1.00 12.17  ? 101 ASP A N   1 
ATOM   848  C  CA  . ASP A 1 101 ? 12.031  -17.205 12.305  1.00 11.82  ? 101 ASP A CA  1 
ATOM   849  C  C   . ASP A 1 101 ? 12.301  -17.113 13.803  1.00 11.60  ? 101 ASP A C   1 
ATOM   850  O  O   . ASP A 1 101 ? 11.598  -16.413 14.459  1.00 14.19  ? 101 ASP A O   1 
ATOM   851  C  CB  . ASP A 1 101 ? 10.813  -18.088 12.067  1.00 12.52  ? 101 ASP A CB  1 
ATOM   852  C  CG  . ASP A 1 101 ? 10.297  -18.106 10.644  1.00 13.43  ? 101 ASP A CG  1 
ATOM   853  O  OD1 . ASP A 1 101 ? 10.675  -17.251 9.807   1.00 14.40  ? 101 ASP A OD1 1 
ATOM   854  O  OD2 . ASP A 1 101 ? 9.487   -18.984 10.358  1.00 19.70  ? 101 ASP A OD2 1 
ATOM   855  N  N   . GLY A 1 102 ? 13.282  -17.856 14.311  1.00 12.81  ? 102 GLY A N   1 
ATOM   856  C  CA  . GLY A 1 102 ? 13.606  -17.871 15.720  1.00 14.78  ? 102 GLY A CA  1 
ATOM   857  C  C   . GLY A 1 102 ? 14.398  -16.689 16.266  1.00 11.56  ? 102 GLY A C   1 
ATOM   858  O  O   . GLY A 1 102 ? 14.733  -16.697 17.455  1.00 13.11  ? 102 GLY A O   1 
ATOM   859  N  N   A GLN A 1 103 ? 14.457  -15.621 15.486  0.50 9.21   ? 103 GLN A N   1 
ATOM   860  N  N   B GLN A 1 103 ? 14.885  -15.742 15.447  0.50 9.40   ? 103 GLN A N   1 
ATOM   861  C  CA  A GLN A 1 103 ? 15.211  -14.486 15.865  0.50 8.39   ? 103 GLN A CA  1 
ATOM   862  C  CA  B GLN A 1 103 ? 15.546  -14.538 15.990  0.50 9.08   ? 103 GLN A CA  1 
ATOM   863  C  C   A GLN A 1 103 ? 14.869  -13.333 15.021  0.50 7.15   ? 103 GLN A C   1 
ATOM   864  C  C   B GLN A 1 103 ? 15.158  -13.380 15.084  0.50 8.31   ? 103 GLN A C   1 
ATOM   865  O  O   A GLN A 1 103 ? 14.281  -13.513 13.924  0.50 7.31   ? 103 GLN A O   1 
ATOM   866  O  O   B GLN A 1 103 ? 14.731  -13.589 13.985  0.50 9.15   ? 103 GLN A O   1 
ATOM   867  C  CB  A GLN A 1 103 ? 16.739  -14.766 15.798  0.50 9.03   ? 103 GLN A CB  1 
ATOM   868  C  CB  B GLN A 1 103 ? 17.074  -14.691 16.125  0.50 9.49   ? 103 GLN A CB  1 
ATOM   869  C  CG  A GLN A 1 103 ? 17.322  -15.027 14.384  0.50 10.09  ? 103 GLN A CG  1 
ATOM   870  C  CG  B GLN A 1 103 ? 17.609  -14.925 14.770  0.50 9.71   ? 103 GLN A CG  1 
ATOM   871  C  CD  A GLN A 1 103 ? 18.735  -15.696 14.465  0.50 11.34  ? 103 GLN A CD  1 
ATOM   872  C  CD  B GLN A 1 103 ? 19.027  -15.405 14.765  0.50 11.96  ? 103 GLN A CD  1 
ATOM   873  O  OE1 A GLN A 1 103 ? 18.799  -16.759 15.094  0.50 13.32  ? 103 GLN A OE1 1 
ATOM   874  O  OE1 B GLN A 1 103 ? 19.495  -16.022 15.724  0.50 16.38  ? 103 GLN A OE1 1 
ATOM   875  N  NE2 A GLN A 1 103 ? 19.836  -14.991 14.072  0.50 12.27  ? 103 GLN A NE2 1 
ATOM   876  N  NE2 B GLN A 1 103 ? 19.674  -15.153 13.632  0.50 12.24  ? 103 GLN A NE2 1 
ATOM   877  N  N   . GLY A 1 104 ? 15.318  -12.155 15.527  1.00 8.22   ? 104 GLY A N   1 
ATOM   878  C  CA  . GLY A 1 104 ? 15.053  -10.956 14.746  1.00 7.86   ? 104 GLY A CA  1 
ATOM   879  C  C   . GLY A 1 104 ? 14.621  -9.777  15.591  1.00 7.60   ? 104 GLY A C   1 
ATOM   880  O  O   . GLY A 1 104 ? 14.874  -8.650  15.245  1.00 8.36   ? 104 GLY A O   1 
ATOM   881  N  N   . SER A 1 105 ? 13.886  -10.041 16.693  1.00 7.62   ? 105 SER A N   1 
ATOM   882  C  CA  . SER A 1 105 ? 13.512  -8.942  17.543  1.00 7.54   ? 105 SER A CA  1 
ATOM   883  C  C   . SER A 1 105 ? 14.702  -8.389  18.318  1.00 6.83   ? 105 SER A C   1 
ATOM   884  O  O   . SER A 1 105 ? 15.707  -9.067  18.540  1.00 8.26   ? 105 SER A O   1 
ATOM   885  C  CB  . SER A 1 105 ? 12.376  -9.297  18.477  1.00 7.93   ? 105 SER A CB  1 
ATOM   886  O  OG  . SER A 1 105 ? 12.714  -10.260 19.476  1.00 8.20   ? 105 SER A OG  1 
ATOM   887  N  N   . GLU A 1 106 ? 14.560  -7.148  18.713  1.00 7.01   ? 106 GLU A N   1 
ATOM   888  C  CA  . GLU A 1 106 ? 15.567  -6.442  19.534  1.00 7.37   ? 106 GLU A CA  1 
ATOM   889  C  C   . GLU A 1 106 ? 15.231  -6.646  21.015  1.00 6.96   ? 106 GLU A C   1 
ATOM   890  O  O   . GLU A 1 106 ? 16.022  -7.203  21.773  1.00 7.49   ? 106 GLU A O   1 
ATOM   891  C  CB  . GLU A 1 106 ? 15.627  -4.972  19.106  1.00 7.06   ? 106 GLU A CB  1 
ATOM   892  C  CG  . GLU A 1 106 ? 16.084  -4.841  17.687  1.00 8.97   ? 106 GLU A CG  1 
ATOM   893  C  CD  . GLU A 1 106 ? 16.755  -3.570  17.418  1.00 7.37   ? 106 GLU A CD  1 
ATOM   894  O  OE1 . GLU A 1 106 ? 16.157  -2.489  17.649  1.00 7.60   ? 106 GLU A OE1 1 
ATOM   895  O  OE2 . GLU A 1 106 ? 17.914  -3.594  16.935  1.00 8.88   ? 106 GLU A OE2 1 
ATOM   896  N  N   . HIS A 1 107 ? 14.050  -6.170  21.436  1.00 6.83   ? 107 HIS A N   1 
ATOM   897  C  CA  . HIS A 1 107 ? 13.591  -6.571  22.737  1.00 7.01   ? 107 HIS A CA  1 
ATOM   898  C  C   . HIS A 1 107 ? 13.306  -8.063  22.736  1.00 6.94   ? 107 HIS A C   1 
ATOM   899  O  O   . HIS A 1 107 ? 12.969  -8.665  21.717  1.00 7.76   ? 107 HIS A O   1 
ATOM   900  C  CB  . HIS A 1 107 ? 12.330  -5.760  23.100  1.00 7.31   ? 107 HIS A CB  1 
ATOM   901  C  CG  . HIS A 1 107 ? 12.640  -4.329  23.281  1.00 6.99   ? 107 HIS A CG  1 
ATOM   902  N  ND1 . HIS A 1 107 ? 12.597  -3.413  22.253  1.00 7.25   ? 107 HIS A ND1 1 
ATOM   903  C  CD2 . HIS A 1 107 ? 13.122  -3.615  24.352  1.00 7.07   ? 107 HIS A CD2 1 
ATOM   904  C  CE1 . HIS A 1 107 ? 13.019  -2.239  22.715  1.00 7.52   ? 107 HIS A CE1 1 
ATOM   905  N  NE2 . HIS A 1 107 ? 13.351  -2.314  23.989  1.00 7.38   ? 107 HIS A NE2 1 
ATOM   906  N  N   . THR A 1 108 ? 13.416  -8.643  23.932  1.00 7.89   ? 108 THR A N   1 
ATOM   907  C  CA  . THR A 1 108 ? 13.027  -10.007 24.183  1.00 8.08   ? 108 THR A CA  1 
ATOM   908  C  C   . THR A 1 108 ? 12.077  -10.014 25.374  1.00 8.00   ? 108 THR A C   1 
ATOM   909  O  O   . THR A 1 108 ? 12.059  -9.055  26.160  1.00 8.53   ? 108 THR A O   1 
ATOM   910  C  CB  . THR A 1 108 ? 14.262  -10.944 24.392  1.00 8.66   ? 108 THR A CB  1 
ATOM   911  O  OG1 . THR A 1 108 ? 15.074  -10.448 25.452  1.00 9.10   ? 108 THR A OG1 1 
ATOM   912  C  CG2 . THR A 1 108 ? 15.047  -10.985 23.135  1.00 9.56   ? 108 THR A CG2 1 
ATOM   913  N  N   . VAL A 1 109 ? 11.306  -11.092 25.508  1.00 8.66   ? 109 VAL A N   1 
ATOM   914  C  CA  . VAL A 1 109 ? 10.314  -11.185 26.599  1.00 9.12   ? 109 VAL A CA  1 
ATOM   915  C  C   . VAL A 1 109 ? 10.627  -12.476 27.326  1.00 9.93   ? 109 VAL A C   1 
ATOM   916  O  O   . VAL A 1 109 ? 10.464  -13.580 26.763  1.00 10.42  ? 109 VAL A O   1 
ATOM   917  C  CB  . VAL A 1 109 ? 8.882   -11.197 26.017  1.00 10.98  ? 109 VAL A CB  1 
ATOM   918  C  CG1 . VAL A 1 109 ? 7.875   -11.310 27.166  1.00 12.39  ? 109 VAL A CG1 1 
ATOM   919  C  CG2 . VAL A 1 109 ? 8.625   -9.946  25.221  1.00 10.65  ? 109 VAL A CG2 1 
ATOM   920  N  N   . ASP A 1 110 ? 11.104  -12.377 28.549  1.00 10.39  ? 110 ASP A N   1 
ATOM   921  C  CA  . ASP A 1 110 ? 11.577  -13.584 29.261  1.00 12.05  ? 110 ASP A CA  1 
ATOM   922  C  C   . ASP A 1 110 ? 12.526  -14.403 28.380  1.00 10.50  ? 110 ASP A C   1 
ATOM   923  O  O   . ASP A 1 110 ? 12.463  -15.629 28.347  1.00 11.47  ? 110 ASP A O   1 
ATOM   924  C  CB  . ASP A 1 110 ? 10.383  -14.440 29.737  1.00 13.36  ? 110 ASP A CB  1 
ATOM   925  C  CG  . ASP A 1 110 ? 9.522   -13.650 30.747  1.00 14.43  ? 110 ASP A CG  1 
ATOM   926  O  OD1 . ASP A 1 110 ? 10.081  -12.819 31.459  1.00 14.93  ? 110 ASP A OD1 1 
ATOM   927  O  OD2 . ASP A 1 110 ? 8.340   -13.940 30.832  1.00 16.92  ? 110 ASP A OD2 1 
ATOM   928  N  N   . LYS A 1 111 ? 13.415  -13.654 27.713  1.00 9.96   ? 111 LYS A N   1 
ATOM   929  C  CA  . LYS A 1 111 ? 14.465  -14.198 26.838  1.00 10.51  ? 111 LYS A CA  1 
ATOM   930  C  C   . LYS A 1 111 ? 13.898  -14.706 25.487  1.00 10.32  ? 111 LYS A C   1 
ATOM   931  O  O   . LYS A 1 111 ? 14.690  -15.046 24.610  1.00 11.91  ? 111 LYS A O   1 
ATOM   932  C  CB  . LYS A 1 111 ? 15.365  -15.257 27.459  1.00 12.54  ? 111 LYS A CB  1 
ATOM   933  C  CG  . LYS A 1 111 ? 15.972  -14.802 28.745  1.00 16.41  ? 111 LYS A CG  1 
ATOM   934  C  CD  . LYS A 1 111 ? 16.931  -13.682 28.549  1.00 19.96  ? 111 LYS A CD  1 
ATOM   935  C  CE  . LYS A 1 111 ? 17.610  -13.250 29.841  1.00 28.41  ? 111 LYS A CE  1 
ATOM   936  N  NZ  . LYS A 1 111 ? 19.012  -13.655 29.841  1.00 36.25  ? 111 LYS A NZ  1 
ATOM   937  N  N   . LYS A 1 112 ? 12.613  -14.677 25.274  1.00 9.96   ? 112 LYS A N   1 
ATOM   938  C  CA  . LYS A 1 112 ? 12.072  -15.058 23.999  1.00 10.51  ? 112 LYS A CA  1 
ATOM   939  C  C   . LYS A 1 112 ? 12.370  -14.034 22.922  1.00 9.30   ? 112 LYS A C   1 
ATOM   940  O  O   . LYS A 1 112 ? 12.095  -12.853 23.115  1.00 9.37   ? 112 LYS A O   1 
ATOM   941  C  CB  . LYS A 1 112 ? 10.522  -15.176 24.093  1.00 12.76  ? 112 LYS A CB  1 
ATOM   942  C  CG  . LYS A 1 112 ? 9.832   -15.562 22.757  1.00 14.34  ? 112 LYS A CG  1 
ATOM   943  C  CD  . LYS A 1 112 ? 8.297   -15.551 22.863  1.00 17.33  ? 112 LYS A CD  1 
ATOM   944  C  CE  . LYS A 1 112 ? 7.732   -15.718 21.493  1.00 21.50  ? 112 LYS A CE  1 
ATOM   945  N  NZ  . LYS A 1 112 ? 7.935   -17.011 21.019  1.00 21.34  ? 112 LYS A NZ  1 
ATOM   946  N  N   A LYS A 1 113 ? 12.751  -14.527 21.758  0.50 8.20   ? 113 LYS A N   1 
ATOM   947  N  N   B LYS A 1 113 ? 13.065  -14.450 21.854  0.50 9.62   ? 113 LYS A N   1 
ATOM   948  C  CA  A LYS A 1 113 ? 12.931  -13.723 20.592  0.50 8.29   ? 113 LYS A CA  1 
ATOM   949  C  CA  B LYS A 1 113 ? 13.246  -13.673 20.572  0.50 9.26   ? 113 LYS A CA  1 
ATOM   950  C  C   A LYS A 1 113 ? 11.805  -13.965 19.701  0.50 8.60   ? 113 LYS A C   1 
ATOM   951  C  C   B LYS A 1 113 ? 12.100  -13.924 19.560  0.50 8.65   ? 113 LYS A C   1 
ATOM   952  O  O   A LYS A 1 113 ? 11.328  -15.056 19.563  0.50 10.46  ? 113 LYS A O   1 
ATOM   953  O  O   B LYS A 1 113 ? 11.792  -15.063 19.229  0.50 8.37   ? 113 LYS A O   1 
ATOM   954  C  CB  A LYS A 1 113 ? 14.226  -14.117 19.904  0.50 8.99   ? 113 LYS A CB  1 
ATOM   955  C  CB  B LYS A 1 113 ? 14.578  -14.021 19.894  0.50 10.21  ? 113 LYS A CB  1 
ATOM   956  C  CG  A LYS A 1 113 ? 15.498  -13.732 20.631  0.50 10.74  ? 113 LYS A CG  1 
ATOM   957  C  CG  B LYS A 1 113 ? 15.811  -13.786 20.742  0.50 10.40  ? 113 LYS A CG  1 
ATOM   958  C  CD  A LYS A 1 113 ? 16.771  -14.475 20.191  0.50 11.60  ? 113 LYS A CD  1 
ATOM   959  C  CD  B LYS A 1 113 ? 17.016  -14.246 19.966  0.50 10.50  ? 113 LYS A CD  1 
ATOM   960  C  CE  A LYS A 1 113 ? 17.956  -13.849 20.872  0.50 14.22  ? 113 LYS A CE  1 
ATOM   961  C  CE  B LYS A 1 113 ? 18.282  -13.720 20.594  0.50 13.50  ? 113 LYS A CE  1 
ATOM   962  N  NZ  A LYS A 1 113 ? 19.280  -14.476 20.627  0.50 16.66  ? 113 LYS A NZ  1 
ATOM   963  N  NZ  B LYS A 1 113 ? 18.527  -14.502 21.838  0.50 13.30  ? 113 LYS A NZ  1 
ATOM   964  N  N   . TYR A 1 114 ? 11.413  -12.847 19.113  1.00 8.84   ? 114 TYR A N   1 
ATOM   965  C  CA  . TYR A 1 114 ? 10.420  -12.889 18.061  1.00 8.66   ? 114 TYR A CA  1 
ATOM   966  C  C   . TYR A 1 114 ? 11.109  -12.849 16.673  1.00 7.98   ? 114 TYR A C   1 
ATOM   967  O  O   . TYR A 1 114 ? 12.298  -12.545 16.564  1.00 8.97   ? 114 TYR A O   1 
ATOM   968  C  CB  . TYR A 1 114 ? 9.362   -11.801 18.207  1.00 8.81   ? 114 TYR A CB  1 
ATOM   969  C  CG  . TYR A 1 114 ? 8.402   -12.024 19.344  1.00 9.01   ? 114 TYR A CG  1 
ATOM   970  C  CD1 . TYR A 1 114 ? 8.702   -11.603 20.637  1.00 10.36  ? 114 TYR A CD1 1 
ATOM   971  C  CD2 . TYR A 1 114 ? 7.193   -12.653 19.123  1.00 10.20  ? 114 TYR A CD2 1 
ATOM   972  C  CE1 . TYR A 1 114 ? 7.811   -11.801 21.674  1.00 12.61  ? 114 TYR A CE1 1 
ATOM   973  C  CE2 . TYR A 1 114 ? 6.301   -12.859 20.153  1.00 12.99  ? 114 TYR A CE2 1 
ATOM   974  C  CZ  . TYR A 1 114 ? 6.613   -12.426 21.423  1.00 13.90  ? 114 TYR A CZ  1 
ATOM   975  O  OH  . TYR A 1 114 ? 5.729   -12.629 22.461  1.00 20.77  ? 114 TYR A OH  1 
ATOM   976  N  N   . ALA A 1 115 ? 10.333  -13.143 15.626  1.00 8.54   ? 115 ALA A N   1 
ATOM   977  C  CA  . ALA A 1 115 ? 10.892  -13.164 14.278  1.00 8.98   ? 115 ALA A CA  1 
ATOM   978  C  C   . ALA A 1 115 ? 11.261  -11.753 13.772  1.00 7.88   ? 115 ALA A C   1 
ATOM   979  O  O   . ALA A 1 115 ? 12.116  -11.611 12.929  1.00 8.75   ? 115 ALA A O   1 
ATOM   980  C  CB  . ALA A 1 115 ? 9.860   -13.748 13.339  1.00 10.68  ? 115 ALA A CB  1 
ATOM   981  N  N   . ALA A 1 116 ? 10.604  -10.734 14.312  1.00 8.24   ? 116 ALA A N   1 
ATOM   982  C  CA  . ALA A 1 116 ? 10.879  -9.368  13.896  1.00 7.95   ? 116 ALA A CA  1 
ATOM   983  C  C   . ALA A 1 116 ? 10.282  -8.435  14.922  1.00 7.45   ? 116 ALA A C   1 
ATOM   984  O  O   . ALA A 1 116 ? 9.542   -8.849  15.831  1.00 7.70   ? 116 ALA A O   1 
ATOM   985  C  CB  . ALA A 1 116 ? 10.350  -9.091  12.492  1.00 8.95   ? 116 ALA A CB  1 
ATOM   986  N  N   . GLU A 1 117 ? 10.605  -7.152  14.779  1.00 7.14   ? 117 GLU A N   1 
ATOM   987  C  CA  . GLU A 1 117 ? 10.080  -6.125  15.654  1.00 6.85   ? 117 GLU A CA  1 
ATOM   988  C  C   . GLU A 1 117 ? 9.887   -4.878  14.821  1.00 7.33   ? 117 GLU A C   1 
ATOM   989  O  O   . GLU A 1 117 ? 10.821  -4.457  14.110  1.00 8.55   ? 117 GLU A O   1 
ATOM   990  C  CB  . GLU A 1 117 ? 11.038  -5.875  16.837  1.00 7.58   ? 117 GLU A CB  1 
ATOM   991  C  CG  . GLU A 1 117 ? 10.515  -4.955  17.893  1.00 8.11   ? 117 GLU A CG  1 
ATOM   992  C  CD  . GLU A 1 117 ? 11.437  -4.867  19.131  1.00 7.29   ? 117 GLU A CD  1 
ATOM   993  O  OE1 . GLU A 1 117 ? 12.128  -5.886  19.407  1.00 7.95   ? 117 GLU A OE1 1 
ATOM   994  O  OE2 . GLU A 1 117 ? 11.444  -3.816  19.801  1.00 8.27   ? 117 GLU A OE2 1 
ATOM   995  N  N   . LEU A 1 118 ? 8.706   -4.290  14.932  1.00 7.27   ? 118 LEU A N   1 
ATOM   996  C  CA  . LEU A 1 118 ? 8.312   -3.031  14.281  1.00 6.75   ? 118 LEU A CA  1 
ATOM   997  C  C   . LEU A 1 118 ? 8.543   -1.918  15.266  1.00 6.67   ? 118 LEU A C   1 
ATOM   998  O  O   . LEU A 1 118 ? 8.118   -1.985  16.416  1.00 6.91   ? 118 LEU A O   1 
ATOM   999  C  CB  . LEU A 1 118 ? 6.838   -3.153  13.934  1.00 7.83   ? 118 LEU A CB  1 
ATOM   1000 C  CG  . LEU A 1 118 ? 6.095   -1.852  13.550  1.00 7.97   ? 118 LEU A CG  1 
ATOM   1001 C  CD1 . LEU A 1 118 ? 6.672   -1.188  12.340  1.00 8.65   ? 118 LEU A CD1 1 
ATOM   1002 C  CD2 . LEU A 1 118 ? 4.639   -2.202  13.292  1.00 9.53   ? 118 LEU A CD2 1 
ATOM   1003 N  N   . HIS A 1 119 ? 9.166   -0.838  14.768  1.00 6.62   ? 119 HIS A N   1 
ATOM   1004 C  CA  . HIS A 1 119 ? 9.388   0.383   15.548  1.00 6.72   ? 119 HIS A CA  1 
ATOM   1005 C  C   . HIS A 1 119 ? 8.696   1.551   14.862  1.00 6.57   ? 119 HIS A C   1 
ATOM   1006 O  O   . HIS A 1 119 ? 9.123   1.920   13.744  1.00 7.55   ? 119 HIS A O   1 
ATOM   1007 C  CB  . HIS A 1 119 ? 10.889  0.651   15.660  1.00 7.35   ? 119 HIS A CB  1 
ATOM   1008 C  CG  . HIS A 1 119 ? 11.575  -0.317  16.551  1.00 6.70   ? 119 HIS A CG  1 
ATOM   1009 N  ND1 . HIS A 1 119 ? 12.927  -0.562  16.521  1.00 6.87   ? 119 HIS A ND1 1 
ATOM   1010 C  CD2 . HIS A 1 119 ? 11.046  -1.121  17.507  1.00 7.21   ? 119 HIS A CD2 1 
ATOM   1011 C  CE1 . HIS A 1 119 ? 13.188  -1.478  17.438  1.00 7.04   ? 119 HIS A CE1 1 
ATOM   1012 N  NE2 . HIS A 1 119 ? 12.072  -1.835  18.054  1.00 7.26   ? 119 HIS A NE2 1 
ATOM   1013 N  N   . LEU A 1 120 ? 7.722   2.126   15.513  1.00 6.96   ? 120 LEU A N   1 
ATOM   1014 C  CA  . LEU A 1 120 ? 7.045   3.368   15.078  1.00 7.42   ? 120 LEU A CA  1 
ATOM   1015 C  C   . LEU A 1 120 ? 7.684   4.484   15.855  1.00 6.92   ? 120 LEU A C   1 
ATOM   1016 O  O   . LEU A 1 120 ? 7.567   4.547   17.087  1.00 6.92   ? 120 LEU A O   1 
ATOM   1017 C  CB  . LEU A 1 120 ? 5.565   3.259   15.295  1.00 8.22   ? 120 LEU A CB  1 
ATOM   1018 C  CG  . LEU A 1 120 ? 4.872   2.200   14.406  1.00 8.79   ? 120 LEU A CG  1 
ATOM   1019 C  CD1 . LEU A 1 120 ? 4.011   1.280   15.225  1.00 12.76  ? 120 LEU A CD1 1 
ATOM   1020 C  CD2 . LEU A 1 120 ? 4.056   2.863   13.312  1.00 11.64  ? 120 LEU A CD2 1 
ATOM   1021 N  N   . VAL A 1 121 ? 8.429   5.357   15.150  1.00 7.39   ? 121 VAL A N   1 
ATOM   1022 C  CA  . VAL A 1 121 ? 9.260   6.373   15.787  1.00 7.41   ? 121 VAL A CA  1 
ATOM   1023 C  C   . VAL A 1 121 ? 8.537   7.718   15.807  1.00 7.18   ? 121 VAL A C   1 
ATOM   1024 O  O   . VAL A 1 121 ? 8.111   8.182   14.743  1.00 7.99   ? 121 VAL A O   1 
ATOM   1025 C  CB  . VAL A 1 121 ? 10.588  6.500   14.999  1.00 7.83   ? 121 VAL A CB  1 
ATOM   1026 C  CG1 . VAL A 1 121 ? 11.503  7.556   15.600  1.00 8.61   ? 121 VAL A CG1 1 
ATOM   1027 C  CG2 . VAL A 1 121 ? 11.302  5.151   14.868  1.00 8.87   ? 121 VAL A CG2 1 
ATOM   1028 N  N   . HIS A 1 122 ? 8.483   8.314   16.981  1.00 7.17   ? 122 HIS A N   1 
ATOM   1029 C  CA  . HIS A 1 122 ? 7.784   9.574   17.182  1.00 7.79   ? 122 HIS A CA  1 
ATOM   1030 C  C   . HIS A 1 122 ? 8.658   10.556  17.924  1.00 7.77   ? 122 HIS A C   1 
ATOM   1031 O  O   . HIS A 1 122 ? 9.426   10.136  18.820  1.00 8.52   ? 122 HIS A O   1 
ATOM   1032 C  CB  . HIS A 1 122 ? 6.502   9.392   17.993  1.00 8.01   ? 122 HIS A CB  1 
ATOM   1033 C  CG  . HIS A 1 122 ? 5.626   8.266   17.580  1.00 7.94   ? 122 HIS A CG  1 
ATOM   1034 N  ND1 . HIS A 1 122 ? 5.933   6.959   17.852  1.00 7.90   ? 122 HIS A ND1 1 
ATOM   1035 C  CD2 . HIS A 1 122 ? 4.412   8.219   16.939  1.00 8.54   ? 122 HIS A CD2 1 
ATOM   1036 C  CE1 . HIS A 1 122 ? 4.940   6.181   17.406  1.00 8.63   ? 122 HIS A CE1 1 
ATOM   1037 N  NE2 . HIS A 1 122 ? 3.992   6.928   16.836  1.00 8.99   ? 122 HIS A NE2 1 
ATOM   1038 N  N   . TRP A 1 123 ? 8.582   11.835  17.602  1.00 7.76   ? 123 TRP A N   1 
ATOM   1039 C  CA  . TRP A 1 123 ? 9.389   12.839  18.292  1.00 7.72   ? 123 TRP A CA  1 
ATOM   1040 C  C   . TRP A 1 123 ? 8.508   13.828  19.023  1.00 8.19   ? 123 TRP A C   1 
ATOM   1041 O  O   . TRP A 1 123 ? 7.395   14.183  18.600  1.00 9.01   ? 123 TRP A O   1 
ATOM   1042 C  CB  . TRP A 1 123 ? 10.353  13.544  17.332  1.00 9.37   ? 123 TRP A CB  1 
ATOM   1043 C  CG  . TRP A 1 123 ? 9.734   14.198  16.166  1.00 9.76   ? 123 TRP A CG  1 
ATOM   1044 C  CD1 . TRP A 1 123 ? 9.527   13.610  14.936  1.00 10.52  ? 123 TRP A CD1 1 
ATOM   1045 C  CD2 . TRP A 1 123 ? 9.294   15.544  16.059  1.00 9.95   ? 123 TRP A CD2 1 
ATOM   1046 N  NE1 . TRP A 1 123 ? 8.940   14.475  14.089  1.00 11.16  ? 123 TRP A NE1 1 
ATOM   1047 C  CE2 . TRP A 1 123 ? 8.783   15.695  14.717  1.00 11.64  ? 123 TRP A CE2 1 
ATOM   1048 C  CE3 . TRP A 1 123 ? 9.235   16.634  16.928  1.00 10.99  ? 123 TRP A CE3 1 
ATOM   1049 C  CZ2 . TRP A 1 123 ? 8.270   16.884  14.251  1.00 13.99  ? 123 TRP A CZ2 1 
ATOM   1050 C  CZ3 . TRP A 1 123 ? 8.689   17.839  16.439  1.00 12.77  ? 123 TRP A CZ3 1 
ATOM   1051 C  CH2 . TRP A 1 123 ? 8.232   17.935  15.124  1.00 13.14  ? 123 TRP A CH2 1 
ATOM   1052 N  N   . ASN A 1 124 ? 9.024   14.306  20.147  1.00 8.83   ? 124 ASN A N   1 
ATOM   1053 C  CA  . ASN A 1 124 ? 8.284   15.200  21.048  1.00 9.69   ? 124 ASN A CA  1 
ATOM   1054 C  C   . ASN A 1 124 ? 8.150   16.575  20.479  1.00 9.79   ? 124 ASN A C   1 
ATOM   1055 O  O   . ASN A 1 124 ? 9.171   17.252  20.200  1.00 9.87   ? 124 ASN A O   1 
ATOM   1056 C  CB  . ASN A 1 124 ? 9.067   15.241  22.360  1.00 9.46   ? 124 ASN A CB  1 
ATOM   1057 C  CG  . ASN A 1 124 ? 8.309   15.834  23.498  1.00 10.49  ? 124 ASN A CG  1 
ATOM   1058 O  OD1 . ASN A 1 124 ? 7.477   16.715  23.280  1.00 11.61  ? 124 ASN A OD1 1 
ATOM   1059 N  ND2 . ASN A 1 124 ? 8.591   15.395  24.694  1.00 12.22  ? 124 ASN A ND2 1 
ATOM   1060 N  N   . THR A 1 125 ? 6.917   17.002  20.257  1.00 9.96   ? 125 THR A N   1 
ATOM   1061 C  CA  . THR A 1 125 ? 6.688   18.276  19.554  1.00 11.66  ? 125 THR A CA  1 
ATOM   1062 C  C   . THR A 1 125 ? 7.258   19.469  20.334  1.00 12.23  ? 125 THR A C   1 
ATOM   1063 O  O   . THR A 1 125 ? 7.451   20.500  19.724  1.00 13.83  ? 125 THR A O   1 
ATOM   1064 C  CB  . THR A 1 125 ? 5.201   18.444  19.229  1.00 15.11  ? 125 THR A CB  1 
ATOM   1065 O  OG1 . THR A 1 125 ? 4.470   18.448  20.429  1.00 17.64  ? 125 THR A OG1 1 
ATOM   1066 C  CG2 . THR A 1 125 ? 4.740   17.338  18.237  1.00 17.04  ? 125 THR A CG2 1 
ATOM   1067 N  N   . LYS A 1 126 ? 7.488   19.320  21.627  1.00 12.27  ? 127 LYS A N   1 
ATOM   1068 C  CA  . LYS A 1 126 ? 8.071   20.464  22.329  1.00 14.47  ? 127 LYS A CA  1 
ATOM   1069 C  C   . LYS A 1 126 ? 9.478   20.821  21.854  1.00 12.54  ? 127 LYS A C   1 
ATOM   1070 O  O   . LYS A 1 126 ? 9.923   21.927  22.168  1.00 15.57  ? 127 LYS A O   1 
ATOM   1071 C  CB  . LYS A 1 126 ? 7.954   20.234  23.785  1.00 17.08  ? 127 LYS A CB  1 
ATOM   1072 C  CG  . LYS A 1 126 ? 9.009   19.386  24.327  1.00 17.01  ? 127 LYS A CG  1 
ATOM   1073 C  CD  . LYS A 1 126 ? 8.537   19.090  25.756  1.00 22.09  ? 127 LYS A CD  1 
ATOM   1074 C  CE  . LYS A 1 126 ? 9.628   18.418  26.457  1.00 21.35  ? 127 LYS A CE  1 
ATOM   1075 N  NZ  . LYS A 1 126 ? 9.229   17.878  27.760  1.00 30.34  ? 127 LYS A NZ  1 
ATOM   1076 N  N   . TYR A 1 127 ? 10.136  19.952  21.069  1.00 11.46  ? 128 TYR A N   1 
ATOM   1077 C  CA  . TYR A 1 127 ? 11.500  20.203  20.552  1.00 11.42  ? 128 TYR A CA  1 
ATOM   1078 C  C   . TYR A 1 127 ? 11.470  20.614  19.095  1.00 12.06  ? 128 TYR A C   1 
ATOM   1079 O  O   . TYR A 1 127 ? 12.572  20.858  18.550  1.00 12.33  ? 128 TYR A O   1 
ATOM   1080 C  CB  . TYR A 1 127 ? 12.426  19.043  20.844  1.00 11.98  ? 128 TYR A CB  1 
ATOM   1081 C  CG  . TYR A 1 127 ? 12.506  18.736  22.274  1.00 11.29  ? 128 TYR A CG  1 
ATOM   1082 C  CD1 . TYR A 1 127 ? 12.935  19.721  23.192  1.00 12.72  ? 128 TYR A CD1 1 
ATOM   1083 C  CD2 . TYR A 1 127 ? 12.185  17.500  22.784  1.00 11.25  ? 128 TYR A CD2 1 
ATOM   1084 C  CE1 . TYR A 1 127 ? 13.015  19.442  24.506  1.00 13.32  ? 128 TYR A CE1 1 
ATOM   1085 C  CE2 . TYR A 1 127 ? 12.297  17.184  24.131  1.00 11.78  ? 128 TYR A CE2 1 
ATOM   1086 C  CZ  . TYR A 1 127 ? 12.710  18.204  24.997  1.00 12.72  ? 128 TYR A CZ  1 
ATOM   1087 O  OH  . TYR A 1 127 ? 12.787  17.993  26.316  1.00 14.57  ? 128 TYR A OH  1 
ATOM   1088 N  N   . GLY A 1 128 ? 10.311  20.722  18.491  1.00 11.27  ? 129 GLY A N   1 
ATOM   1089 C  CA  . GLY A 1 128 ? 10.224  21.397  17.194  1.00 12.75  ? 129 GLY A CA  1 
ATOM   1090 C  C   . GLY A 1 128 ? 10.625  20.573  15.963  1.00 11.98  ? 129 GLY A C   1 
ATOM   1091 O  O   . GLY A 1 128 ? 10.003  20.708  14.922  1.00 14.08  ? 129 GLY A O   1 
ATOM   1092 N  N   A ASP A 1 129 ? 11.492  19.615  16.078  0.50 10.27  ? 130 ASP A N   1 
ATOM   1093 N  N   B ASP A 1 129 ? 11.814  19.848  16.021  0.50 11.63  ? 130 ASP A N   1 
ATOM   1094 C  CA  A ASP A 1 129 ? 11.631  18.722  14.984  0.50 9.79   ? 130 ASP A CA  1 
ATOM   1095 C  CA  B ASP A 1 129 ? 12.299  18.925  14.935  0.50 10.86  ? 130 ASP A CA  1 
ATOM   1096 C  C   A ASP A 1 129 ? 12.407  17.558  15.535  0.50 9.42   ? 130 ASP A C   1 
ATOM   1097 C  C   B ASP A 1 129 ? 12.982  17.661  15.452  0.50 11.49  ? 130 ASP A C   1 
ATOM   1098 O  O   A ASP A 1 129 ? 12.797  17.575  16.734  0.50 9.01   ? 130 ASP A O   1 
ATOM   1099 O  O   B ASP A 1 129 ? 13.516  17.638  16.611  0.50 8.91   ? 130 ASP A O   1 
ATOM   1100 C  CB  A ASP A 1 129 ? 12.281  19.389  13.773  0.50 11.17  ? 130 ASP A CB  1 
ATOM   1101 C  CB  B ASP A 1 129 ? 13.131  19.615  13.828  0.50 11.06  ? 130 ASP A CB  1 
ATOM   1102 C  CG  A ASP A 1 129 ? 13.731  19.806  13.982  0.50 10.43  ? 130 ASP A CG  1 
ATOM   1103 C  CG  B ASP A 1 129 ? 14.556  20.004  14.303  0.50 13.38  ? 130 ASP A CG  1 
ATOM   1104 O  OD1 A ASP A 1 129 ? 14.227  19.579  15.089  0.50 12.90  ? 130 ASP A OD1 1 
ATOM   1105 O  OD1 B ASP A 1 129 ? 15.381  19.157  14.644  0.50 15.36  ? 130 ASP A OD1 1 
ATOM   1106 O  OD2 A ASP A 1 129 ? 14.256  20.484  13.051  0.50 14.66  ? 130 ASP A OD2 1 
ATOM   1107 O  OD2 B ASP A 1 129 ? 14.858  21.196  14.455  0.50 18.06  ? 130 ASP A OD2 1 
ATOM   1108 N  N   . PHE A 1 130 ? 12.773  16.576  14.691  1.00 11.93  ? 131 PHE A N   1 
ATOM   1109 C  CA  . PHE A 1 130 ? 13.416  15.342  15.100  1.00 10.77  ? 131 PHE A CA  1 
ATOM   1110 C  C   . PHE A 1 130 ? 14.866  15.514  15.494  1.00 10.55  ? 131 PHE A C   1 
ATOM   1111 O  O   . PHE A 1 130 ? 15.323  14.937  16.489  1.00 10.86  ? 131 PHE A O   1 
ATOM   1112 C  CB  . PHE A 1 130 ? 13.246  14.354  13.942  1.00 11.07  ? 131 PHE A CB  1 
ATOM   1113 C  CG  . PHE A 1 130 ? 13.920  13.056  14.183  1.00 10.12  ? 131 PHE A CG  1 
ATOM   1114 C  CD1 . PHE A 1 130 ? 13.267  12.018  14.831  1.00 10.20  ? 131 PHE A CD1 1 
ATOM   1115 C  CD2 . PHE A 1 130 ? 15.275  12.814  13.878  1.00 13.86  ? 131 PHE A CD2 1 
ATOM   1116 C  CE1 . PHE A 1 130 ? 13.891  10.807  15.060  1.00 10.64  ? 131 PHE A CE1 1 
ATOM   1117 C  CE2 . PHE A 1 130 ? 15.839  11.617  14.075  1.00 16.88  ? 131 PHE A CE2 1 
ATOM   1118 C  CZ  . PHE A 1 130 ? 15.162  10.598  14.681  1.00 12.90  ? 131 PHE A CZ  1 
ATOM   1119 N  N   . GLY A 1 131 ? 15.613  16.291  14.705  1.00 12.21  ? 132 GLY A N   1 
ATOM   1120 C  CA  . GLY A 1 131 ? 17.022  16.417  15.019  1.00 14.29  ? 132 GLY A CA  1 
ATOM   1121 C  C   . GLY A 1 131 ? 17.311  17.078  16.346  1.00 13.47  ? 132 GLY A C   1 
ATOM   1122 O  O   . GLY A 1 131 ? 18.297  16.756  17.042  1.00 15.49  ? 132 GLY A O   1 
ATOM   1123 N  N   A LYS A 1 132 ? 16.477  18.003  16.803  0.50 12.60  ? 133 LYS A N   1 
ATOM   1124 N  N   B LYS A 1 132 ? 16.439  18.018  16.736  0.50 13.15  ? 133 LYS A N   1 
ATOM   1125 C  CA  A LYS A 1 132 ? 16.708  18.540  18.152  0.50 12.22  ? 133 LYS A CA  1 
ATOM   1126 C  CA  B LYS A 1 132 ? 16.554  18.623  18.077  0.50 13.28  ? 133 LYS A CA  1 
ATOM   1127 C  C   A LYS A 1 132 ? 16.087  17.614  19.189  0.50 11.43  ? 133 LYS A C   1 
ATOM   1128 C  C   B LYS A 1 132 ? 16.173  17.560  19.121  0.50 11.85  ? 133 LYS A C   1 
ATOM   1129 O  O   A LYS A 1 132 ? 16.506  17.612  20.310  0.50 10.11  ? 133 LYS A O   1 
ATOM   1130 O  O   B LYS A 1 132 ? 16.888  17.366  20.144  0.50 11.13  ? 133 LYS A O   1 
ATOM   1131 C  CB  A LYS A 1 132 ? 16.001  19.894  18.236  0.50 12.53  ? 133 LYS A CB  1 
ATOM   1132 C  CB  B LYS A 1 132 ? 15.659  19.885  18.170  0.50 14.19  ? 133 LYS A CB  1 
ATOM   1133 C  CG  A LYS A 1 132 ? 16.439  20.975  17.256  0.50 12.38  ? 133 LYS A CG  1 
ATOM   1134 C  CG  B LYS A 1 132 ? 15.631  20.449  19.607  0.50 17.50  ? 133 LYS A CG  1 
ATOM   1135 C  CD  A LYS A 1 132 ? 17.845  21.145  17.247  0.50 19.51  ? 133 LYS A CD  1 
ATOM   1136 C  CD  B LYS A 1 132 ? 16.582  21.595  20.025  0.50 25.21  ? 133 LYS A CD  1 
ATOM   1137 C  CE  A LYS A 1 132 ? 18.026  21.550  18.650  0.50 22.13  ? 133 LYS A CE  1 
ATOM   1138 C  CE  B LYS A 1 132 ? 16.313  22.252  21.449  0.50 13.69  ? 133 LYS A CE  1 
ATOM   1139 N  NZ  A LYS A 1 132 ? 17.979  22.992  19.066  0.50 37.16  ? 133 LYS A NZ  1 
ATOM   1140 N  NZ  B LYS A 1 132 ? 15.439  23.466  21.563  0.50 33.50  ? 133 LYS A NZ  1 
ATOM   1141 N  N   . ALA A 1 133 ? 15.048  16.859  18.842  1.00 10.65  ? 134 ALA A N   1 
ATOM   1142 C  CA  . ALA A 1 133 ? 14.484  15.910  19.828  1.00 10.21  ? 134 ALA A CA  1 
ATOM   1143 C  C   . ALA A 1 133 ? 15.489  14.834  20.212  1.00 9.72   ? 134 ALA A C   1 
ATOM   1144 O  O   . ALA A 1 133 ? 15.499  14.439  21.383  1.00 10.02  ? 134 ALA A O   1 
ATOM   1145 C  CB  . ALA A 1 133 ? 13.222  15.298  19.230  1.00 10.17  ? 134 ALA A CB  1 
ATOM   1146 N  N   . VAL A 1 134 ? 16.276  14.333  19.264  1.00 10.39  ? 135 VAL A N   1 
ATOM   1147 C  CA  . VAL A 1 134 ? 17.185  13.213  19.627  1.00 10.96  ? 135 VAL A CA  1 
ATOM   1148 C  C   . VAL A 1 134 ? 18.283  13.634  20.575  1.00 10.79  ? 135 VAL A C   1 
ATOM   1149 O  O   . VAL A 1 134 ? 18.960  12.790  21.150  1.00 11.70  ? 135 VAL A O   1 
ATOM   1150 C  CB  . VAL A 1 134 ? 17.818  12.534  18.436  1.00 12.08  ? 135 VAL A CB  1 
ATOM   1151 C  CG1 . VAL A 1 134 ? 16.763  11.852  17.591  1.00 14.46  ? 135 VAL A CG1 1 
ATOM   1152 C  CG2 . VAL A 1 134 ? 18.676  13.429  17.608  1.00 13.01  ? 135 VAL A CG2 1 
ATOM   1153 N  N   . GLN A 1 135 ? 18.435  14.965  20.775  1.00 10.92  ? 136 GLN A N   1 
ATOM   1154 C  CA  . GLN A 1 135 ? 19.406  15.483  21.743  1.00 12.45  ? 136 GLN A CA  1 
ATOM   1155 C  C   . GLN A 1 135 ? 18.866  15.596  23.116  1.00 11.27  ? 136 GLN A C   1 
ATOM   1156 O  O   . GLN A 1 135 ? 19.540  16.145  24.047  1.00 14.33  ? 136 GLN A O   1 
ATOM   1157 C  CB  . GLN A 1 135 ? 19.978  16.849  21.236  1.00 14.79  ? 136 GLN A CB  1 
ATOM   1158 C  CG  . GLN A 1 135 ? 20.629  16.670  19.878  1.00 18.97  ? 136 GLN A CG  1 
ATOM   1159 C  CD  . GLN A 1 135 ? 21.910  15.744  19.823  1.00 34.09  ? 136 GLN A CD  1 
ATOM   1160 O  OE1 . GLN A 1 135 ? 22.658  15.617  20.811  1.00 34.05  ? 136 GLN A OE1 1 
ATOM   1161 N  NE2 . GLN A 1 135 ? 22.163  15.088  18.631  1.00 35.84  ? 136 GLN A NE2 1 
ATOM   1162 N  N   . GLN A 1 136 ? 17.634  15.160  23.357  1.00 10.52  ? 137 GLN A N   1 
ATOM   1163 C  CA  . GLN A 1 136 ? 16.963  15.360  24.623  1.00 10.78  ? 137 GLN A CA  1 
ATOM   1164 C  C   . GLN A 1 136 ? 16.624  14.054  25.249  1.00 10.13  ? 137 GLN A C   1 
ATOM   1165 O  O   . GLN A 1 136 ? 16.233  13.106  24.558  1.00 10.31  ? 137 GLN A O   1 
ATOM   1166 C  CB  . GLN A 1 136 ? 15.684  16.159  24.461  1.00 11.83  ? 137 GLN A CB  1 
ATOM   1167 C  CG  . GLN A 1 136 ? 15.790  17.346  23.593  1.00 15.34  ? 137 GLN A CG  1 
ATOM   1168 C  CD  . GLN A 1 136 ? 16.734  18.281  24.035  1.00 17.87  ? 137 GLN A CD  1 
ATOM   1169 O  OE1 . GLN A 1 136 ? 17.034  18.457  25.264  1.00 17.23  ? 137 GLN A OE1 1 
ATOM   1170 N  NE2 . GLN A 1 136 ? 17.393  18.837  22.968  1.00 21.01  ? 137 GLN A NE2 1 
ATOM   1171 N  N   A PRO A 1 137 ? 16.534  14.116  26.575  0.50 10.64  ? 138 PRO A N   1 
ATOM   1172 N  N   B PRO A 1 137 ? 16.590  13.850  26.635  0.50 10.75  ? 138 PRO A N   1 
ATOM   1173 C  CA  A PRO A 1 137 ? 16.369  12.870  27.242  0.50 11.21  ? 138 PRO A CA  1 
ATOM   1174 C  CA  B PRO A 1 137 ? 16.295  12.491  27.193  0.50 11.24  ? 138 PRO A CA  1 
ATOM   1175 C  C   A PRO A 1 137 ? 14.951  12.260  27.066  0.50 10.18  ? 138 PRO A C   1 
ATOM   1176 C  C   B PRO A 1 137 ? 14.838  12.128  27.055  0.50 10.96  ? 138 PRO A C   1 
ATOM   1177 O  O   A PRO A 1 137 ? 14.807  11.049  27.241  0.50 13.05  ? 138 PRO A O   1 
ATOM   1178 O  O   B PRO A 1 137 ? 14.551  10.951  27.197  0.50 14.72  ? 138 PRO A O   1 
ATOM   1179 C  CB  A PRO A 1 137 ? 16.603  13.240  28.734  0.50 11.89  ? 138 PRO A CB  1 
ATOM   1180 C  CB  B PRO A 1 137 ? 16.622  12.619  28.708  0.50 13.20  ? 138 PRO A CB  1 
ATOM   1181 C  CG  A PRO A 1 137 ? 16.513  14.619  28.813  0.50 12.97  ? 138 PRO A CG  1 
ATOM   1182 C  CG  B PRO A 1 137 ? 17.386  13.859  28.831  0.50 15.88  ? 138 PRO A CG  1 
ATOM   1183 C  CD  A PRO A 1 137 ? 16.827  15.242  27.479  0.50 10.59  ? 138 PRO A CD  1 
ATOM   1184 C  CD  B PRO A 1 137 ? 17.236  14.716  27.620  0.50 11.14  ? 138 PRO A CD  1 
ATOM   1185 N  N   . ASP A 1 138 ? 13.945  13.072  26.767  1.00 10.52  ? 139 ASP A N   1 
ATOM   1186 C  CA  . ASP A 1 138 ? 12.559  12.754  26.484  1.00 10.31  ? 139 ASP A CA  1 
ATOM   1187 C  C   . ASP A 1 138 ? 12.200  13.164  25.057  1.00 9.29   ? 139 ASP A C   1 
ATOM   1188 O  O   . ASP A 1 138 ? 11.072  13.570  24.791  1.00 10.25  ? 139 ASP A O   1 
ATOM   1189 C  CB  . ASP A 1 138 ? 11.604  13.385  27.493  1.00 13.55  ? 139 ASP A CB  1 
ATOM   1190 C  CG  . ASP A 1 138 ? 11.717  14.840  27.512  1.00 13.39  ? 139 ASP A CG  1 
ATOM   1191 O  OD1 . ASP A 1 138 ? 12.671  15.448  26.944  1.00 13.85  ? 139 ASP A OD1 1 
ATOM   1192 O  OD2 . ASP A 1 138 ? 10.866  15.473  28.202  1.00 17.05  ? 139 ASP A OD2 1 
ATOM   1193 N  N   . GLY A 1 139 ? 13.156  13.036  24.131  1.00 8.36   ? 140 GLY A N   1 
ATOM   1194 C  CA  . GLY A 1 139 ? 12.922  13.492  22.802  1.00 8.73   ? 140 GLY A CA  1 
ATOM   1195 C  C   . GLY A 1 139 ? 12.065  12.575  21.928  1.00 7.63   ? 140 GLY A C   1 
ATOM   1196 O  O   . GLY A 1 139 ? 11.357  13.085  21.067  1.00 8.32   ? 140 GLY A O   1 
ATOM   1197 N  N   . LEU A 1 140 ? 12.188  11.260  22.101  1.00 7.41   ? 141 LEU A N   1 
ATOM   1198 C  CA  . LEU A 1 140 ? 11.493  10.301  21.250  1.00 7.33   ? 141 LEU A CA  1 
ATOM   1199 C  C   . LEU A 1 140 ? 10.642  9.397   22.040  1.00 7.08   ? 141 LEU A C   1 
ATOM   1200 O  O   . LEU A 1 140 ? 10.916  9.119   23.216  1.00 7.50   ? 141 LEU A O   1 
ATOM   1201 C  CB  . LEU A 1 140 ? 12.500  9.455   20.451  1.00 8.04   ? 141 LEU A CB  1 
ATOM   1202 C  CG  . LEU A 1 140 ? 13.432  10.095  19.417  1.00 10.49  ? 141 LEU A CG  1 
ATOM   1203 C  CD1 . LEU A 1 140 ? 14.095  9.024   18.565  1.00 9.39   ? 141 LEU A CD1 1 
ATOM   1204 C  CD2 . LEU A 1 140 ? 12.743  11.146  18.551  1.00 12.31  ? 141 LEU A CD2 1 
ATOM   1205 N  N   . ALA A 1 141 ? 9.606   8.882   21.395  1.00 7.30   ? 142 ALA A N   1 
ATOM   1206 C  CA  . ALA A 1 141 ? 8.808   7.745   21.910  1.00 7.75   ? 142 ALA A CA  1 
ATOM   1207 C  C   . ALA A 1 141 ? 8.760   6.757   20.796  1.00 6.96   ? 142 ALA A C   1 
ATOM   1208 O  O   . ALA A 1 141 ? 8.318   7.102   19.672  1.00 7.94   ? 142 ALA A O   1 
ATOM   1209 C  CB  . ALA A 1 141 ? 7.425   8.186   22.329  1.00 8.86   ? 142 ALA A CB  1 
ATOM   1210 N  N   . VAL A 1 142 ? 9.253   5.550   21.039  1.00 6.94   ? 143 VAL A N   1 
ATOM   1211 C  CA  . VAL A 1 142 ? 9.221   4.495   20.031  1.00 6.92   ? 143 VAL A CA  1 
ATOM   1212 C  C   . VAL A 1 142 ? 8.261   3.444   20.516  1.00 6.64   ? 143 VAL A C   1 
ATOM   1213 O  O   . VAL A 1 142 ? 8.387   2.928   21.628  1.00 7.16   ? 143 VAL A O   1 
ATOM   1214 C  CB  . VAL A 1 142 ? 10.610  3.941   19.669  1.00 7.31   ? 143 VAL A CB  1 
ATOM   1215 C  CG1 . VAL A 1 142 ? 10.457  2.911   18.576  1.00 7.90   ? 143 VAL A CG1 1 
ATOM   1216 C  CG2 . VAL A 1 142 ? 11.550  5.056   19.240  1.00 8.42   ? 143 VAL A CG2 1 
ATOM   1217 N  N   . LEU A 1 143 ? 7.257   3.171   19.667  1.00 6.99   ? 144 LEU A N   1 
ATOM   1218 C  CA  . LEU A 1 143 ? 6.283   2.125   19.909  1.00 7.31   ? 144 LEU A CA  1 
ATOM   1219 C  C   . LEU A 1 143 ? 6.807   0.871   19.220  1.00 6.96   ? 144 LEU A C   1 
ATOM   1220 O  O   . LEU A 1 143 ? 6.969   0.831   17.986  1.00 7.65   ? 144 LEU A O   1 
ATOM   1221 C  CB  . LEU A 1 143 ? 4.948   2.559   19.349  1.00 8.39   ? 144 LEU A CB  1 
ATOM   1222 C  CG  . LEU A 1 143 ? 3.782   1.599   19.512  1.00 9.06   ? 144 LEU A CG  1 
ATOM   1223 C  CD1 . LEU A 1 143 ? 3.563   1.267   20.942  1.00 11.43  ? 144 LEU A CD1 1 
ATOM   1224 C  CD2 . LEU A 1 143 ? 2.540   2.195   18.854  1.00 11.10  ? 144 LEU A CD2 1 
ATOM   1225 N  N   . GLY A 1 144 ? 7.100   -0.148  20.023  1.00 6.84   ? 145 GLY A N   1 
ATOM   1226 C  CA  . GLY A 1 144 ? 7.631   -1.401  19.527  1.00 7.37   ? 145 GLY A CA  1 
ATOM   1227 C  C   . GLY A 1 144 ? 6.590   -2.490  19.542  1.00 6.69   ? 145 GLY A C   1 
ATOM   1228 O  O   . GLY A 1 144 ? 5.857   -2.633  20.531  1.00 7.71   ? 145 GLY A O   1 
ATOM   1229 N  N   . ILE A 1 145 ? 6.516   -3.236  18.461  1.00 6.60   ? 146 ILE A N   1 
ATOM   1230 C  CA  . ILE A 1 145 ? 5.509   -4.294  18.283  1.00 7.16   ? 146 ILE A CA  1 
ATOM   1231 C  C   . ILE A 1 145 ? 6.236   -5.522  17.758  1.00 6.83   ? 146 ILE A C   1 
ATOM   1232 O  O   . ILE A 1 145 ? 6.924   -5.468  16.753  1.00 7.44   ? 146 ILE A O   1 
ATOM   1233 C  CB  . ILE A 1 145 ? 4.397   -3.816  17.293  1.00 7.76   ? 146 ILE A CB  1 
ATOM   1234 C  CG1 . ILE A 1 145 ? 3.808   -2.507  17.789  1.00 9.88   ? 146 ILE A CG1 1 
ATOM   1235 C  CG2 . ILE A 1 145 ? 3.393   -4.907  17.119  1.00 9.68   ? 146 ILE A CG2 1 
ATOM   1236 C  CD1 . ILE A 1 145 ? 2.743   -1.925  16.889  1.00 9.61   ? 146 ILE A CD1 1 
ATOM   1237 N  N   . PHE A 1 146 ? 6.072   -6.629  18.461  1.00 6.98   ? 147 PHE A N   1 
ATOM   1238 C  CA  . PHE A 1 146 ? 6.681   -7.870  18.045  1.00 7.17   ? 147 PHE A CA  1 
ATOM   1239 C  C   . PHE A 1 146 ? 5.905   -8.491  16.889  1.00 7.70   ? 147 PHE A C   1 
ATOM   1240 O  O   . PHE A 1 146 ? 4.676   -8.376  16.812  1.00 8.58   ? 147 PHE A O   1 
ATOM   1241 C  CB  . PHE A 1 146 ? 6.663   -8.844  19.211  1.00 7.70   ? 147 PHE A CB  1 
ATOM   1242 C  CG  . PHE A 1 146 ? 7.522   -8.380  20.353  1.00 7.06   ? 147 PHE A CG  1 
ATOM   1243 C  CD1 . PHE A 1 146 ? 8.874   -8.226  20.191  1.00 7.47   ? 147 PHE A CD1 1 
ATOM   1244 C  CD2 . PHE A 1 146 ? 6.990   -8.130  21.596  1.00 8.14   ? 147 PHE A CD2 1 
ATOM   1245 C  CE1 . PHE A 1 146 ? 9.709   -7.816  21.247  1.00 8.19   ? 147 PHE A CE1 1 
ATOM   1246 C  CE2 . PHE A 1 146 ? 7.800   -7.742  22.642  1.00 8.60   ? 147 PHE A CE2 1 
ATOM   1247 C  CZ  . PHE A 1 146 ? 9.162   -7.589  22.461  1.00 8.06   ? 147 PHE A CZ  1 
ATOM   1248 N  N   . LEU A 1 147 ? 6.636   -9.209  16.034  1.00 7.79   ? 148 LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 147 ? 6.066   -9.990  14.934  1.00 8.21   ? 148 LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 147 ? 6.397   -11.467 15.165  1.00 8.09   ? 148 LEU A C   1 
ATOM   1251 O  O   . LEU A 1 147 ? 7.559   -11.812 15.353  1.00 8.74   ? 148 LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 147 ? 6.649   -9.607  13.577  1.00 8.82   ? 148 LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 147 ? 6.115   -8.350  12.907  1.00 8.46   ? 148 LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 147 ? 6.325   -7.094  13.764  1.00 9.74   ? 148 LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 147 ? 6.732   -8.178  11.538  1.00 10.02  ? 148 LEU A CD2 1 
ATOM   1256 N  N   . LYS A 1 148 ? 5.363   -12.287 15.131  1.00 8.95   ? 149 LYS A N   1 
ATOM   1257 C  CA  . LYS A 1 148 ? 5.499   -13.742 15.125  1.00 9.54   ? 149 LYS A CA  1 
ATOM   1258 C  C   . LYS A 1 148 ? 5.040   -14.254 13.764  1.00 10.30  ? 149 LYS A C   1 
ATOM   1259 O  O   . LYS A 1 148 ? 4.230   -13.605 13.102  1.00 11.61  ? 149 LYS A O   1 
ATOM   1260 C  CB  . LYS A 1 148 ? 4.795   -14.415 16.244  1.00 11.73  ? 149 LYS A CB  1 
ATOM   1261 C  CG  . LYS A 1 148 ? 3.333   -14.294 16.178  1.00 13.24  ? 149 LYS A CG  1 
ATOM   1262 C  CD  . LYS A 1 148 ? 2.707   -14.985 17.399  1.00 20.07  ? 149 LYS A CD  1 
ATOM   1263 C  CE  . LYS A 1 148 ? 1.220   -14.992 17.294  1.00 28.89  ? 149 LYS A CE  1 
ATOM   1264 N  NZ  . LYS A 1 148 ? 0.660   -15.581 18.537  1.00 43.20  ? 149 LYS A NZ  1 
ATOM   1265 N  N   . VAL A 1 149 ? 5.539   -15.393 13.345  1.00 11.38  ? 150 VAL A N   1 
ATOM   1266 C  CA  . VAL A 1 149 ? 5.168   -15.994 12.072  1.00 11.04  ? 150 VAL A CA  1 
ATOM   1267 C  C   . VAL A 1 149 ? 3.943   -16.905 12.276  1.00 11.54  ? 150 VAL A C   1 
ATOM   1268 O  O   . VAL A 1 149 ? 4.007   -17.862 13.071  1.00 13.13  ? 150 VAL A O   1 
ATOM   1269 C  CB  . VAL A 1 149 ? 6.342   -16.696 11.440  1.00 11.43  ? 150 VAL A CB  1 
ATOM   1270 C  CG1 . VAL A 1 149 ? 5.964   -17.501 10.225  1.00 13.50  ? 150 VAL A CG1 1 
ATOM   1271 C  CG2 . VAL A 1 149 ? 7.444   -15.709 11.119  1.00 13.89  ? 150 VAL A CG2 1 
ATOM   1272 N  N   . GLY A 1 150 ? 2.914   -16.640 11.510  1.00 11.54  ? 151 GLY A N   1 
ATOM   1273 C  CA  . GLY A 1 150 ? 1.696   -17.478 11.546  1.00 13.45  ? 151 GLY A CA  1 
ATOM   1274 C  C   . GLY A 1 150 ? 0.826   -17.015 10.410  1.00 11.89  ? 151 GLY A C   1 
ATOM   1275 O  O   . GLY A 1 150 ? 1.201   -17.116 9.248   1.00 12.81  ? 151 GLY A O   1 
ATOM   1276 N  N   A SER A 1 151 ? -0.380  -16.509 10.728  0.50 13.22  ? 152 SER A N   1 
ATOM   1277 N  N   B SER A 1 151 ? -0.351  -16.510 10.768  0.50 13.69  ? 152 SER A N   1 
ATOM   1278 C  CA  A SER A 1 151 ? -1.285  -15.987 9.668   0.50 12.78  ? 152 SER A CA  1 
ATOM   1279 C  CA  B SER A 1 151 ? -1.216  -15.904 9.772   0.50 13.06  ? 152 SER A CA  1 
ATOM   1280 C  C   A SER A 1 151 ? -0.787  -14.646 9.211   0.50 11.30  ? 152 SER A C   1 
ATOM   1281 C  C   B SER A 1 151 ? -0.543  -14.686 9.124   0.50 11.78  ? 152 SER A C   1 
ATOM   1282 O  O   A SER A 1 151 ? -0.179  -13.906 10.012  0.50 10.00  ? 152 SER A O   1 
ATOM   1283 O  O   B SER A 1 151 ? 0.296   -13.992 9.709   0.50 9.95   ? 152 SER A O   1 
ATOM   1284 C  CB  A SER A 1 151 ? -2.680  -15.794 10.162  0.50 15.17  ? 152 SER A CB  1 
ATOM   1285 C  CB  B SER A 1 151 ? -2.533  -15.524 10.403  0.50 17.47  ? 152 SER A CB  1 
ATOM   1286 O  OG  A SER A 1 151 ? -2.696  -14.743 11.104  0.50 16.57  ? 152 SER A OG  1 
ATOM   1287 O  OG  B SER A 1 151 ? -3.196  -16.698 10.810  0.50 21.02  ? 152 SER A OG  1 
ATOM   1288 N  N   . ALA A 1 152 ? -0.955  -14.361 7.895   1.00 12.75  ? 153 ALA A N   1 
ATOM   1289 C  CA  . ALA A 1 152 ? -0.560  -13.105 7.314   1.00 11.84  ? 153 ALA A CA  1 
ATOM   1290 C  C   . ALA A 1 152 ? -1.179  -11.922 7.992   1.00 11.93  ? 153 ALA A C   1 
ATOM   1291 O  O   . ALA A 1 152 ? -2.272  -11.972 8.533   1.00 13.50  ? 153 ALA A O   1 
ATOM   1292 C  CB  . ALA A 1 152 ? -0.944  -13.089 5.837   1.00 15.31  ? 153 ALA A CB  1 
ATOM   1293 N  N   . LYS A 1 153 ? -0.462  -10.783 7.925   1.00 11.87  ? 154 LYS A N   1 
ATOM   1294 C  CA  . LYS A 1 153 ? -0.991  -9.500  8.386   1.00 12.24  ? 154 LYS A CA  1 
ATOM   1295 C  C   . LYS A 1 153 ? -1.432  -8.736  7.144   1.00 11.73  ? 154 LYS A C   1 
ATOM   1296 O  O   . LYS A 1 153 ? -0.611  -8.273  6.378   1.00 11.60  ? 154 LYS A O   1 
ATOM   1297 C  CB  . LYS A 1 153 ? 0.110   -8.723  9.125   1.00 12.31  ? 154 LYS A CB  1 
ATOM   1298 C  CG  . LYS A 1 153 ? -0.338  -7.498  9.857   1.00 13.50  ? 154 LYS A CG  1 
ATOM   1299 C  CD  . LYS A 1 153 ? -1.275  -7.811  10.995  1.00 14.30  ? 154 LYS A CD  1 
ATOM   1300 C  CE  . LYS A 1 153 ? -1.386  -6.652  11.952  1.00 13.75  ? 154 LYS A CE  1 
ATOM   1301 N  NZ  . LYS A 1 153 ? -2.367  -7.036  12.995  1.00 14.49  ? 154 LYS A NZ  1 
ATOM   1302 N  N   A PRO A 1 154 ? -2.678  -8.708  6.748   0.50 11.69  ? 155 PRO A N   1 
ATOM   1303 N  N   B PRO A 1 154 ? -2.796  -8.596  6.992   0.50 12.65  ? 155 PRO A N   1 
ATOM   1304 C  CA  A PRO A 1 154 ? -3.043  -8.063  5.473   0.50 12.71  ? 155 PRO A CA  1 
ATOM   1305 C  CA  B PRO A 1 154 ? -3.234  -8.011  5.706   0.50 13.40  ? 155 PRO A CA  1 
ATOM   1306 C  C   A PRO A 1 154 ? -2.682  -6.591  5.444   0.50 13.21  ? 155 PRO A C   1 
ATOM   1307 C  C   B PRO A 1 154 ? -2.593  -6.650  5.440   0.50 13.60  ? 155 PRO A C   1 
ATOM   1308 O  O   A PRO A 1 154 ? -2.456  -6.109  4.414   0.50 12.72  ? 155 PRO A O   1 
ATOM   1309 O  O   B PRO A 1 154 ? -2.030  -6.375  4.277   0.50 12.58  ? 155 PRO A O   1 
ATOM   1310 C  CB  A PRO A 1 154 ? -4.571  -8.241  5.432   0.50 13.80  ? 155 PRO A CB  1 
ATOM   1311 C  CB  B PRO A 1 154 ? -4.780  -7.992  5.854   0.50 12.91  ? 155 PRO A CB  1 
ATOM   1312 C  CG  A PRO A 1 154 ? -4.921  -9.223  6.524   0.50 13.45  ? 155 PRO A CG  1 
ATOM   1313 C  CG  B PRO A 1 154 ? -5.035  -8.192  7.277   0.50 17.82  ? 155 PRO A CG  1 
ATOM   1314 C  CD  A PRO A 1 154 ? -3.823  -9.264  7.482   0.50 13.28  ? 155 PRO A CD  1 
ATOM   1315 C  CD  B PRO A 1 154 ? -3.949  -9.009  7.848   0.50 14.28  ? 155 PRO A CD  1 
ATOM   1316 N  N   . GLY A 1 155 ? -2.586  -5.875  6.553   1.00 13.01  ? 156 GLY A N   1 
ATOM   1317 C  CA  . GLY A 1 155 ? -2.135  -4.486  6.520   1.00 14.98  ? 156 GLY A CA  1 
ATOM   1318 C  C   . GLY A 1 155 ? -0.677  -4.292  6.283   1.00 13.87  ? 156 GLY A C   1 
ATOM   1319 O  O   . GLY A 1 155 ? -0.238  -3.155  6.094   1.00 15.58  ? 156 GLY A O   1 
ATOM   1320 N  N   . LEU A 1 156 ? 0.081   -5.368  6.324   1.00 12.26  ? 157 LEU A N   1 
ATOM   1321 C  CA  . LEU A 1 156 ? 1.484   -5.337  5.983   1.00 11.38  ? 157 LEU A CA  1 
ATOM   1322 C  C   . LEU A 1 156 ? 1.774   -5.528  4.502   1.00 11.47  ? 157 LEU A C   1 
ATOM   1323 O  O   . LEU A 1 156 ? 2.872   -5.252  4.011   1.00 11.91  ? 157 LEU A O   1 
ATOM   1324 C  CB  . LEU A 1 156 ? 2.267   -6.374  6.808   1.00 12.49  ? 157 LEU A CB  1 
ATOM   1325 C  CG  . LEU A 1 156 ? 3.780   -6.475  6.644   1.00 11.62  ? 157 LEU A CG  1 
ATOM   1326 C  CD1 . LEU A 1 156 ? 4.495   -5.223  7.046   1.00 12.75  ? 157 LEU A CD1 1 
ATOM   1327 C  CD2 . LEU A 1 156 ? 4.308   -7.651  7.475   1.00 12.48  ? 157 LEU A CD2 1 
ATOM   1328 N  N   . GLN A 1 157 ? 0.812   -6.124  3.758   1.00 12.40  ? 158 GLN A N   1 
ATOM   1329 C  CA  . GLN A 1 157 ? 1.159   -6.614  2.399   1.00 12.88  ? 158 GLN A CA  1 
ATOM   1330 C  C   . GLN A 1 157 ? 1.550   -5.471  1.472   1.00 11.84  ? 158 GLN A C   1 
ATOM   1331 O  O   . GLN A 1 157 ? 2.387   -5.672  0.662   1.00 13.08  ? 158 GLN A O   1 
ATOM   1332 C  CB  . GLN A 1 157 ? 0.016   -7.431  1.843   1.00 14.11  ? 158 GLN A CB  1 
ATOM   1333 C  CG  . GLN A 1 157 ? 0.394   -8.133  0.581   1.00 15.04  ? 158 GLN A CG  1 
ATOM   1334 C  CD  . GLN A 1 157 ? 1.514   -9.130  0.781   1.00 13.48  ? 158 GLN A CD  1 
ATOM   1335 O  OE1 . GLN A 1 157 ? 1.683   -9.710  1.896   1.00 14.39  ? 158 GLN A OE1 1 
ATOM   1336 N  NE2 . GLN A 1 157 ? 2.321   -9.397  -0.262  1.00 17.12  ? 158 GLN A NE2 1 
ATOM   1337 N  N   . LYS A 1 158 ? 0.964   -4.256  1.617   1.00 13.06  ? 159 LYS A N   1 
ATOM   1338 C  CA  . LYS A 1 158 ? 1.352   -3.157  0.749   1.00 13.40  ? 159 LYS A CA  1 
ATOM   1339 C  C   . LYS A 1 158 ? 2.852   -2.838  0.908   1.00 12.90  ? 159 LYS A C   1 
ATOM   1340 O  O   . LYS A 1 158 ? 3.523   -2.473  -0.063  1.00 13.48  ? 159 LYS A O   1 
ATOM   1341 C  CB  . LYS A 1 158 ? 0.516   -1.909  1.016   1.00 15.68  ? 159 LYS A CB  1 
ATOM   1342 C  CG  . LYS A 1 158 ? 0.699   -0.668  0.196   1.00 25.92  ? 159 LYS A CG  1 
ATOM   1343 C  CD  . LYS A 1 158 ? -0.297  0.524   0.534   1.00 25.91  ? 159 LYS A CD  1 
ATOM   1344 C  CE  . LYS A 1 158 ? 0.073   1.885   -0.169  1.00 38.24  ? 159 LYS A CE  1 
ATOM   1345 N  NZ  . LYS A 1 158 ? -0.076  1.820   -1.691  1.00 34.64  ? 159 LYS A NZ  1 
ATOM   1346 N  N   . VAL A 1 159 ? 3.362   -2.958  2.146   1.00 12.21  ? 160 VAL A N   1 
ATOM   1347 C  CA  . VAL A 1 159 ? 4.803   -2.771  2.386   1.00 11.84  ? 160 VAL A CA  1 
ATOM   1348 C  C   . VAL A 1 159 ? 5.548   -3.887  1.711   1.00 11.67  ? 160 VAL A C   1 
ATOM   1349 O  O   . VAL A 1 159 ? 6.485   -3.648  0.975   1.00 12.66  ? 160 VAL A O   1 
ATOM   1350 C  CB  . VAL A 1 159 ? 5.106   -2.746  3.901   1.00 11.80  ? 160 VAL A CB  1 
ATOM   1351 C  CG1 . VAL A 1 159 ? 6.580   -2.746  4.172   1.00 13.66  ? 160 VAL A CG1 1 
ATOM   1352 C  CG2 . VAL A 1 159 ? 4.414   -1.572  4.540   1.00 13.70  ? 160 VAL A CG2 1 
ATOM   1353 N  N   . VAL A 1 160 ? 5.189   -5.133  1.940   1.00 11.72  ? 161 VAL A N   1 
ATOM   1354 C  CA  . VAL A 1 160 ? 5.881   -6.246  1.345   1.00 12.83  ? 161 VAL A CA  1 
ATOM   1355 C  C   . VAL A 1 160 ? 5.991   -6.134  -0.145  1.00 13.13  ? 161 VAL A C   1 
ATOM   1356 O  O   . VAL A 1 160 ? 7.033   -6.408  -0.716  1.00 15.27  ? 161 VAL A O   1 
ATOM   1357 C  CB  . VAL A 1 160 ? 5.175   -7.561  1.740   1.00 16.33  ? 161 VAL A CB  1 
ATOM   1358 C  CG1 . VAL A 1 160 ? 5.701   -8.733  0.929   1.00 17.53  ? 161 VAL A CG1 1 
ATOM   1359 C  CG2 . VAL A 1 160 ? 5.330   -7.810  3.235   1.00 16.42  ? 161 VAL A CG2 1 
ATOM   1360 N  N   . ASP A 1 161 ? 4.881   -5.744  -0.760  1.00 14.31  ? 162 ASP A N   1 
ATOM   1361 C  CA  . ASP A 1 161 ? 4.874   -5.765  -2.221  1.00 17.44  ? 162 ASP A CA  1 
ATOM   1362 C  C   . ASP A 1 161 ? 5.734   -4.715  -2.896  1.00 15.95  ? 162 ASP A C   1 
ATOM   1363 O  O   . ASP A 1 161 ? 6.029   -4.892  -4.060  1.00 22.38  ? 162 ASP A O   1 
ATOM   1364 C  CB  . ASP A 1 161 ? 3.441   -5.647  -2.649  1.00 19.49  ? 162 ASP A CB  1 
ATOM   1365 C  CG  . ASP A 1 161 ? 2.768   -7.033  -2.655  1.00 18.90  ? 162 ASP A CG  1 
ATOM   1366 O  OD1 . ASP A 1 161 ? 3.527   -8.113  -2.682  1.00 23.53  ? 162 ASP A OD1 1 
ATOM   1367 O  OD2 . ASP A 1 161 ? 1.557   -7.035  -2.437  1.00 22.99  ? 162 ASP A OD2 1 
ATOM   1368 N  N   . VAL A 1 162 ? 6.112   -3.649  -2.166  1.00 15.75  ? 163 VAL A N   1 
ATOM   1369 C  CA  . VAL A 1 162 ? 6.857   -2.592  -2.753  1.00 16.20  ? 163 VAL A CA  1 
ATOM   1370 C  C   . VAL A 1 162 ? 8.356   -2.902  -2.603  1.00 14.24  ? 163 VAL A C   1 
ATOM   1371 O  O   . VAL A 1 162 ? 9.225   -2.225  -3.159  1.00 15.46  ? 163 VAL A O   1 
ATOM   1372 C  CB  . VAL A 1 162 ? 6.474   -1.177  -2.150  1.00 15.79  ? 163 VAL A CB  1 
ATOM   1373 C  CG1 . VAL A 1 162 ? 7.178   -0.977  -0.851  1.00 16.87  ? 163 VAL A CG1 1 
ATOM   1374 C  CG2 . VAL A 1 162 ? 6.864   0.021   -3.041  1.00 18.49  ? 163 VAL A CG2 1 
ATOM   1375 N  N   . LEU A 1 163 ? 8.702   -3.890  -1.766  1.00 14.06  ? 164 LEU A N   1 
ATOM   1376 C  CA  . LEU A 1 163 ? 10.083  -4.086  -1.458  1.00 13.08  ? 164 LEU A CA  1 
ATOM   1377 C  C   . LEU A 1 163 ? 10.971  -4.390  -2.610  1.00 14.61  ? 164 LEU A C   1 
ATOM   1378 O  O   . LEU A 1 163 ? 12.171  -4.062  -2.601  1.00 14.84  ? 164 LEU A O   1 
ATOM   1379 C  CB  . LEU A 1 163 ? 10.318  -5.138  -0.332  1.00 13.73  ? 164 LEU A CB  1 
ATOM   1380 C  CG  . LEU A 1 163 ? 9.650   -4.804  1.003   1.00 13.16  ? 164 LEU A CG  1 
ATOM   1381 C  CD1 . LEU A 1 163 ? 9.890   -5.899  2.046   1.00 13.66  ? 164 LEU A CD1 1 
ATOM   1382 C  CD2 . LEU A 1 163 ? 10.144  -3.487  1.576   1.00 13.14  ? 164 LEU A CD2 1 
ATOM   1383 N  N   . ASP A 1 164 ? 10.473  -5.095  -3.612  1.00 17.60  ? 165 ASP A N   1 
ATOM   1384 C  CA  . ASP A 1 164 ? 11.370  -5.385  -4.772  1.00 20.18  ? 165 ASP A CA  1 
ATOM   1385 C  C   . ASP A 1 164 ? 11.782  -4.074  -5.466  1.00 19.99  ? 165 ASP A C   1 
ATOM   1386 O  O   . ASP A 1 164 ? 12.757  -4.194  -6.253  1.00 23.44  ? 165 ASP A O   1 
ATOM   1387 C  CB  . ASP A 1 164 ? 10.651  -6.322  -5.745  1.00 22.79  ? 165 ASP A CB  1 
ATOM   1388 C  CG  . ASP A 1 164 ? 9.606   -5.558  -6.486  1.00 27.65  ? 165 ASP A CG  1 
ATOM   1389 O  OD1 . ASP A 1 164 ? 8.624   -5.134  -5.882  1.00 32.61  ? 165 ASP A OD1 1 
ATOM   1390 O  OD2 . ASP A 1 164 ? 9.725   -5.270  -7.747  1.00 37.35  ? 165 ASP A OD2 1 
ATOM   1391 N  N   . SER A 1 165 ? 11.095  -2.947  -5.275  1.00 16.53  ? 166 SER A N   1 
ATOM   1392 C  CA  . SER A 1 165 ? 11.478  -1.680  -5.875  1.00 17.95  ? 166 SER A CA  1 
ATOM   1393 C  C   . SER A 1 165 ? 12.514  -0.941  -5.096  1.00 15.23  ? 166 SER A C   1 
ATOM   1394 O  O   . SER A 1 165 ? 13.038  0.055   -5.579  1.00 17.88  ? 166 SER A O   1 
ATOM   1395 C  CB  . SER A 1 165 ? 10.225  -0.842  -6.234  1.00 23.81  ? 166 SER A CB  1 
ATOM   1396 O  OG  . SER A 1 165 ? 9.757   -0.282  -5.064  1.00 21.91  ? 166 SER A OG  1 
ATOM   1397 N  N   . ILE A 1 166 ? 12.818  -1.426  -3.867  1.00 13.33  ? 167 ILE A N   1 
ATOM   1398 C  CA  . ILE A 1 166 ? 13.835  -0.775  -3.043  1.00 12.66  ? 167 ILE A CA  1 
ATOM   1399 C  C   . ILE A 1 166 ? 14.853  -1.808  -2.557  1.00 12.23  ? 167 ILE A C   1 
ATOM   1400 O  O   . ILE A 1 166 ? 15.252  -1.846  -1.394  1.00 12.48  ? 167 ILE A O   1 
ATOM   1401 C  CB  . ILE A 1 166 ? 13.229  0.038   -1.879  1.00 12.71  ? 167 ILE A CB  1 
ATOM   1402 C  CG1 . ILE A 1 166 ? 12.356  -0.832  -0.975  1.00 13.31  ? 167 ILE A CG1 1 
ATOM   1403 C  CG2 . ILE A 1 166 ? 12.472  1.235   -2.447  1.00 14.54  ? 167 ILE A CG2 1 
ATOM   1404 C  CD1 . ILE A 1 166 ? 12.361  -0.302  0.423   1.00 13.97  ? 167 ILE A CD1 1 
ATOM   1405 N  N   . LYS A 1 167 ? 15.248  -2.713  -3.461  1.00 13.09  ? 168 LYS A N   1 
ATOM   1406 C  CA  . LYS A 1 167 ? 16.010  -3.815  -3.020  1.00 13.27  ? 168 LYS A CA  1 
ATOM   1407 C  C   . LYS A 1 167 ? 17.320  -3.470  -2.365  1.00 12.53  ? 168 LYS A C   1 
ATOM   1408 O  O   . LYS A 1 167 ? 17.776  -4.153  -1.436  1.00 13.10  ? 168 LYS A O   1 
ATOM   1409 C  CB  . LYS A 1 167 ? 16.276  -4.811  -4.234  1.00 15.71  ? 168 LYS A CB  1 
ATOM   1410 C  CG  . LYS A 1 167 ? 17.034  -6.047  -3.817  1.00 15.34  ? 168 LYS A CG  1 
ATOM   1411 C  CD  . LYS A 1 167 ? 17.162  -7.002  -5.025  1.00 20.81  ? 168 LYS A CD  1 
ATOM   1412 C  CE  . LYS A 1 167 ? 18.019  -8.177  -4.703  1.00 27.68  ? 168 LYS A CE  1 
ATOM   1413 N  NZ  . LYS A 1 167 ? 18.253  -9.186  -5.811  1.00 37.82  ? 168 LYS A NZ  1 
ATOM   1414 N  N   . THR A 1 168 ? 17.958  -2.444  -2.887  1.00 13.03  ? 169 THR A N   1 
ATOM   1415 C  CA  . THR A 1 168 ? 19.309  -2.146  -2.512  1.00 13.60  ? 169 THR A CA  1 
ATOM   1416 C  C   . THR A 1 168 ? 19.442  -0.697  -1.842  1.00 11.15  ? 169 THR A C   1 
ATOM   1417 O  O   . THR A 1 168 ? 18.536  0.123   -1.965  1.00 12.99  ? 169 THR A O   1 
ATOM   1418 C  CB  . THR A 1 168 ? 20.243  -2.177  -3.762  1.00 14.70  ? 169 THR A CB  1 
ATOM   1419 O  OG1 . THR A 1 168 ? 19.658  -1.381  -4.790  1.00 14.88  ? 169 THR A OG1 1 
ATOM   1420 C  CG2 . THR A 1 168 ? 20.382  -3.602  -4.237  1.00 16.43  ? 169 THR A CG2 1 
ATOM   1421 N  N   . LYS A 1 169 ? 20.520  -0.577  -1.117  1.00 14.00  ? 170 LYS A N   1 
ATOM   1422 C  CA  . LYS A 1 169 ? 20.743  0.625   -0.364  1.00 13.38  ? 170 LYS A CA  1 
ATOM   1423 C  C   . LYS A 1 169 ? 20.688  1.902   -1.140  1.00 13.76  ? 170 LYS A C   1 
ATOM   1424 O  O   . LYS A 1 169 ? 21.249  1.989   -2.244  1.00 15.92  ? 170 LYS A O   1 
ATOM   1425 C  CB  . LYS A 1 169 ? 22.111  0.467   0.238   1.00 13.85  ? 170 LYS A CB  1 
ATOM   1426 C  CG  . LYS A 1 169 ? 22.605  1.683   1.029   1.00 15.83  ? 170 LYS A CG  1 
ATOM   1427 C  CD  . LYS A 1 169 ? 23.927  1.459   1.662   1.00 18.62  ? 170 LYS A CD  1 
ATOM   1428 C  CE  . LYS A 1 169 ? 24.976  0.994   0.688   1.00 31.00  ? 170 LYS A CE  1 
ATOM   1429 N  NZ  . LYS A 1 169 ? 26.314  0.929   1.350   1.00 42.22  ? 170 LYS A NZ  1 
ATOM   1430 N  N   . GLY A 1 170 ? 19.917  2.853   -0.637  1.00 14.86  ? 171 GLY A N   1 
ATOM   1431 C  CA  . GLY A 1 170 ? 19.705  4.115   -1.294  1.00 15.78  ? 171 GLY A CA  1 
ATOM   1432 C  C   . GLY A 1 170 ? 18.513  4.201   -2.201  1.00 16.08  ? 171 GLY A C   1 
ATOM   1433 O  O   . GLY A 1 170 ? 18.216  5.315   -2.643  1.00 19.08  ? 171 GLY A O   1 
ATOM   1434 N  N   . LYS A 1 171 ? 17.883  3.074   -2.559  1.00 13.89  ? 172 LYS A N   1 
ATOM   1435 C  CA  . LYS A 1 171 ? 16.668  3.122   -3.338  1.00 14.24  ? 172 LYS A CA  1 
ATOM   1436 C  C   . LYS A 1 171 ? 15.482  3.592   -2.509  1.00 12.14  ? 172 LYS A C   1 
ATOM   1437 O  O   . LYS A 1 171 ? 15.300  3.172   -1.340  1.00 13.16  ? 172 LYS A O   1 
ATOM   1438 C  CB  . LYS A 1 171 ? 16.444  1.818   -3.971  1.00 15.44  ? 172 LYS A CB  1 
ATOM   1439 C  CG  . LYS A 1 171 ? 17.493  1.364   -4.928  1.00 18.40  ? 172 LYS A CG  1 
ATOM   1440 C  CD  . LYS A 1 171 ? 17.007  0.309   -5.877  1.00 25.13  ? 172 LYS A CD  1 
ATOM   1441 N  N   . SER A 1 172 ? 14.615  4.371   -3.078  1.00 13.79  ? 173 SER A N   1 
ATOM   1442 C  CA  . SER A 1 172 ? 13.343  4.803   -2.513  1.00 14.27  ? 173 SER A CA  1 
ATOM   1443 C  C   . SER A 1 172 ? 12.185  4.655   -3.458  1.00 13.35  ? 173 SER A C   1 
ATOM   1444 O  O   . SER A 1 172 ? 12.391  4.609   -4.744  1.00 16.30  ? 173 SER A O   1 
ATOM   1445 C  CB  . SER A 1 172 ? 13.380  6.184   -1.981  1.00 14.67  ? 173 SER A CB  1 
ATOM   1446 O  OG  . SER A 1 172 ? 13.615  7.112   -3.006  1.00 19.48  ? 173 SER A OG  1 
ATOM   1447 N  N   . ALA A 1 173 ? 10.963  4.607   -2.993  1.00 14.62  ? 174 ALA A N   1 
ATOM   1448 C  CA  . ALA A 1 173 ? 9.793   4.614   -3.816  1.00 14.30  ? 174 ALA A CA  1 
ATOM   1449 C  C   . ALA A 1 173 ? 8.687   5.407   -3.218  1.00 13.33  ? 174 ALA A C   1 
ATOM   1450 O  O   . ALA A 1 173 ? 8.580   5.442   -1.979  1.00 12.85  ? 174 ALA A O   1 
ATOM   1451 C  CB  . ALA A 1 173 ? 9.345   3.184   -4.068  1.00 18.43  ? 174 ALA A CB  1 
ATOM   1452 N  N   . ASP A 1 174 ? 7.869   6.032   -4.015  1.00 15.08  ? 175 ASP A N   1 
ATOM   1453 C  CA  . ASP A 1 174 ? 6.684   6.735   -3.491  1.00 16.62  ? 175 ASP A CA  1 
ATOM   1454 C  C   . ASP A 1 174 ? 5.891   5.703   -2.748  1.00 14.66  ? 175 ASP A C   1 
ATOM   1455 O  O   . ASP A 1 174 ? 5.764   4.520   -3.119  1.00 17.74  ? 175 ASP A O   1 
ATOM   1456 C  CB  . ASP A 1 174 ? 5.874   7.240   -4.722  1.00 18.20  ? 175 ASP A CB  1 
ATOM   1457 C  CG  . ASP A 1 174 ? 6.604   8.326   -5.526  1.00 26.02  ? 175 ASP A CG  1 
ATOM   1458 O  OD1 . ASP A 1 174 ? 7.396   9.180   -4.937  1.00 34.70  ? 175 ASP A OD1 1 
ATOM   1459 O  OD2 . ASP A 1 174 ? 6.408   8.445   -6.770  1.00 23.89  ? 175 ASP A OD2 1 
ATOM   1460 N  N   . PHE A 1 175 ? 5.297   6.188   -1.615  1.00 13.97  ? 176 PHE A N   1 
ATOM   1461 C  CA  . PHE A 1 175 ? 4.597   5.276   -0.742  1.00 14.32  ? 176 PHE A CA  1 
ATOM   1462 C  C   . PHE A 1 175 ? 3.509   6.014   -0.019  1.00 13.21  ? 176 PHE A C   1 
ATOM   1463 O  O   . PHE A 1 175 ? 3.645   6.243   1.166   1.00 15.94  ? 176 PHE A O   1 
ATOM   1464 C  CB  . PHE A 1 175 ? 5.578   4.443   0.124   1.00 13.78  ? 176 PHE A CB  1 
ATOM   1465 C  CG  . PHE A 1 175 ? 4.978   3.198   0.655   1.00 13.02  ? 176 PHE A CG  1 
ATOM   1466 C  CD1 . PHE A 1 175 ? 4.685   2.143   -0.138  1.00 15.58  ? 176 PHE A CD1 1 
ATOM   1467 C  CD2 . PHE A 1 175 ? 4.614   3.095   1.998   1.00 14.58  ? 176 PHE A CD2 1 
ATOM   1468 C  CE1 . PHE A 1 175 ? 4.154   0.979   0.336   1.00 16.36  ? 176 PHE A CE1 1 
ATOM   1469 C  CE2 . PHE A 1 175 ? 4.115   1.901   2.509   1.00 14.43  ? 176 PHE A CE2 1 
ATOM   1470 C  CZ  . PHE A 1 175 ? 3.824   0.858   1.670   1.00 14.30  ? 176 PHE A CZ  1 
ATOM   1471 N  N   . THR A 1 176 ? 2.553   6.495   -0.721  1.00 12.99  ? 177 THR A N   1 
ATOM   1472 C  CA  . THR A 1 176 ? 1.465   7.284   -0.181  1.00 12.43  ? 177 THR A CA  1 
ATOM   1473 C  C   . THR A 1 176 ? 0.268   6.448   0.239   1.00 11.88  ? 177 THR A C   1 
ATOM   1474 O  O   . THR A 1 176 ? 0.096   5.280   -0.224  1.00 13.13  ? 177 THR A O   1 
ATOM   1475 C  CB  . THR A 1 176 ? 1.025   8.332   -1.221  1.00 13.89  ? 177 THR A CB  1 
ATOM   1476 O  OG1 . THR A 1 176 ? 0.726   7.725   -2.473  1.00 18.38  ? 177 THR A OG1 1 
ATOM   1477 C  CG2 . THR A 1 176 ? 2.146   9.420   -1.382  1.00 20.79  ? 177 THR A CG2 1 
ATOM   1478 N  N   . ASN A 1 177 ? -0.543  7.007   1.099   1.00 12.01  ? 178 ASN A N   1 
ATOM   1479 C  CA  . ASN A 1 177 ? -1.773  6.429   1.522   1.00 13.05  ? 178 ASN A CA  1 
ATOM   1480 C  C   . ASN A 1 177 ? -1.651  5.102   2.262   1.00 13.86  ? 178 ASN A C   1 
ATOM   1481 O  O   . ASN A 1 177 ? -2.559  4.301   2.209   1.00 19.25  ? 178 ASN A O   1 
ATOM   1482 C  CB  . ASN A 1 177 ? -2.720  6.312   0.318   1.00 13.94  ? 178 ASN A CB  1 
ATOM   1483 C  CG  . ASN A 1 177 ? -2.978  7.673   -0.271  1.00 15.36  ? 178 ASN A CG  1 
ATOM   1484 O  OD1 . ASN A 1 177 ? -3.619  8.533   0.334   1.00 18.37  ? 178 ASN A OD1 1 
ATOM   1485 N  ND2 . ASN A 1 177 ? -2.362  7.931   -1.436  1.00 15.13  ? 178 ASN A ND2 1 
ATOM   1486 N  N   . PHE A 1 178 ? -0.471  4.859   2.868   1.00 12.58  ? 179 PHE A N   1 
ATOM   1487 C  CA  . PHE A 1 178 ? -0.333  3.674   3.700   1.00 12.44  ? 179 PHE A CA  1 
ATOM   1488 C  C   . PHE A 1 178 ? -0.814  3.958   5.084   1.00 12.08  ? 179 PHE A C   1 
ATOM   1489 O  O   . PHE A 1 178 ? -0.475  4.977   5.699   1.00 13.45  ? 179 PHE A O   1 
ATOM   1490 C  CB  . PHE A 1 178 ? 1.086   3.245   3.783   1.00 12.75  ? 179 PHE A CB  1 
ATOM   1491 C  CG  . PHE A 1 178 ? 1.231   2.029   4.643   1.00 11.89  ? 179 PHE A CG  1 
ATOM   1492 C  CD1 . PHE A 1 178 ? 0.849   0.743   4.119   1.00 13.57  ? 179 PHE A CD1 1 
ATOM   1493 C  CD2 . PHE A 1 178 ? 1.650   2.092   5.975   1.00 11.65  ? 179 PHE A CD2 1 
ATOM   1494 C  CE1 . PHE A 1 178 ? 0.872   -0.357  4.938   1.00 13.00  ? 179 PHE A CE1 1 
ATOM   1495 C  CE2 . PHE A 1 178 ? 1.680   0.943   6.775   1.00 11.59  ? 179 PHE A CE2 1 
ATOM   1496 C  CZ  . PHE A 1 178 ? 1.278   -0.287  6.250   1.00 12.38  ? 179 PHE A CZ  1 
ATOM   1497 N  N   . ASP A 1 179 ? -1.690  3.087   5.614   1.00 12.65  ? 180 ASP A N   1 
ATOM   1498 C  CA  . ASP A 1 179 ? -2.326  3.303   6.886   1.00 12.64  ? 180 ASP A CA  1 
ATOM   1499 C  C   . ASP A 1 179 ? -1.633  2.467   7.984   1.00 11.26  ? 180 ASP A C   1 
ATOM   1500 O  O   . ASP A 1 179 ? -1.803  1.268   8.009   1.00 12.11  ? 180 ASP A O   1 
ATOM   1501 C  CB  . ASP A 1 179 ? -3.779  2.936   6.788   1.00 14.77  ? 180 ASP A CB  1 
ATOM   1502 C  CG  . ASP A 1 179 ? -4.557  3.350   7.992   1.00 16.17  ? 180 ASP A CG  1 
ATOM   1503 O  OD1 . ASP A 1 179 ? -3.979  3.602   9.088   1.00 14.77  ? 180 ASP A OD1 1 
ATOM   1504 O  OD2 . ASP A 1 179 ? -5.792  3.416   7.887   1.00 22.58  ? 180 ASP A OD2 1 
ATOM   1505 N  N   . PRO A 1 180 ? -0.842  3.114   8.875   1.00 11.03  ? 181 PRO A N   1 
ATOM   1506 C  CA  . PRO A 1 180 ? -0.124  2.294   9.870   1.00 11.23  ? 181 PRO A CA  1 
ATOM   1507 C  C   . PRO A 1 180 ? -1.008  1.682   10.903  1.00 11.01  ? 181 PRO A C   1 
ATOM   1508 O  O   . PRO A 1 180 ? -0.545  0.813   11.631  1.00 11.08  ? 181 PRO A O   1 
ATOM   1509 C  CB  . PRO A 1 180 ? 0.878   3.328   10.464  1.00 11.48  ? 181 PRO A CB  1 
ATOM   1510 C  CG  . PRO A 1 180 ? 0.170   4.661   10.283  1.00 12.20  ? 181 PRO A CG  1 
ATOM   1511 C  CD  . PRO A 1 180 ? -0.517  4.539   8.939   1.00 11.94  ? 181 PRO A CD  1 
ATOM   1512 N  N   . ARG A 1 181 ? -2.286  2.072   10.950  1.00 11.34  ? 182 ARG A N   1 
ATOM   1513 C  CA  . ARG A 1 181 ? -3.225  1.367   11.852  1.00 12.04  ? 182 ARG A CA  1 
ATOM   1514 C  C   . ARG A 1 181 ? -3.303  -0.116  11.516  1.00 11.68  ? 182 ARG A C   1 
ATOM   1515 O  O   . ARG A 1 181 ? -3.658  -0.912  12.394  1.00 13.42  ? 182 ARG A O   1 
ATOM   1516 C  CB  . ARG A 1 181 ? -4.573  2.009   11.816  1.00 12.35  ? 182 ARG A CB  1 
ATOM   1517 C  CG  . ARG A 1 181 ? -4.518  3.434   12.270  1.00 13.46  ? 182 ARG A CG  1 
ATOM   1518 C  CD  . ARG A 1 181 ? -5.888  4.108   12.286  1.00 15.88  ? 182 ARG A CD  1 
ATOM   1519 N  NE  . ARG A 1 181 ? -6.312  4.285   10.925  1.00 16.18  ? 182 ARG A NE  1 
ATOM   1520 C  CZ  . ARG A 1 181 ? -7.448  4.890   10.608  1.00 16.88  ? 182 ARG A CZ  1 
ATOM   1521 N  NH1 . ARG A 1 181 ? -8.176  5.433   11.575  1.00 20.53  ? 182 ARG A NH1 1 
ATOM   1522 N  NH2 . ARG A 1 181 ? -7.785  4.980   9.319   1.00 21.94  ? 182 ARG A NH2 1 
ATOM   1523 N  N   . GLY A 1 182 ? -3.024  -0.504  10.262  1.00 12.28  ? 183 GLY A N   1 
ATOM   1524 C  CA  . GLY A 1 182 ? -3.113  -1.898  9.883   1.00 13.12  ? 183 GLY A CA  1 
ATOM   1525 C  C   . GLY A 1 182 ? -1.936  -2.724  10.382  1.00 13.14  ? 183 GLY A C   1 
ATOM   1526 O  O   . GLY A 1 182 ? -1.897  -3.910  10.088  1.00 14.71  ? 183 GLY A O   1 
ATOM   1527 N  N   . LEU A 1 183 ? -0.990  -2.145  11.142  1.00 10.91  ? 184 LEU A N   1 
ATOM   1528 C  CA  . LEU A 1 183 ? 0.139   -2.861  11.704  1.00 11.48  ? 184 LEU A CA  1 
ATOM   1529 C  C   . LEU A 1 183 ? -0.012  -3.108  13.174  1.00 11.00  ? 184 LEU A C   1 
ATOM   1530 O  O   . LEU A 1 183 ? 0.870   -3.698  13.791  1.00 12.34  ? 184 LEU A O   1 
ATOM   1531 C  CB  . LEU A 1 183 ? 1.421   -2.144  11.421  1.00 11.34  ? 184 LEU A CB  1 
ATOM   1532 C  CG  . LEU A 1 183 ? 1.768   -2.012  9.914   1.00 13.41  ? 184 LEU A CG  1 
ATOM   1533 C  CD1 . LEU A 1 183 ? 3.018   -1.164  9.764   1.00 14.90  ? 184 LEU A CD1 1 
ATOM   1534 C  CD2 . LEU A 1 183 ? 1.863   -3.338  9.225   1.00 15.79  ? 184 LEU A CD2 1 
ATOM   1535 N  N   . LEU A 1 184 ? -1.095  -2.649  13.800  1.00 11.46  ? 185 LEU A N   1 
ATOM   1536 C  CA  . LEU A 1 184 ? -1.255  -2.755  15.220  1.00 10.97  ? 185 LEU A CA  1 
ATOM   1537 C  C   . LEU A 1 184 ? -1.927  -4.060  15.597  1.00 11.96  ? 185 LEU A C   1 
ATOM   1538 O  O   . LEU A 1 184 ? -2.676  -4.618  14.780  1.00 13.65  ? 185 LEU A O   1 
ATOM   1539 C  CB  . LEU A 1 184 ? -2.085  -1.562  15.746  1.00 11.59  ? 185 LEU A CB  1 
ATOM   1540 C  CG  . LEU A 1 184 ? -1.570  -0.136  15.392  1.00 11.89  ? 185 LEU A CG  1 
ATOM   1541 C  CD1 . LEU A 1 184 ? -2.500  0.944   15.894  1.00 14.36  ? 185 LEU A CD1 1 
ATOM   1542 C  CD2 . LEU A 1 184 ? -0.168  0.060   15.938  1.00 14.78  ? 185 LEU A CD2 1 
ATOM   1543 N  N   . PRO A 1 185 ? -1.670  -4.589  16.814  1.00 10.40  ? 186 PRO A N   1 
ATOM   1544 C  CA  . PRO A 1 185 ? -2.444  -5.727  17.341  1.00 11.78  ? 186 PRO A CA  1 
ATOM   1545 C  C   . PRO A 1 185 ? -3.745  -5.156  17.932  1.00 11.60  ? 186 PRO A C   1 
ATOM   1546 O  O   . PRO A 1 185 ? -3.963  -3.957  17.885  1.00 13.38  ? 186 PRO A O   1 
ATOM   1547 C  CB  . PRO A 1 185 ? -1.554  -6.270  18.429  1.00 11.10  ? 186 PRO A CB  1 
ATOM   1548 C  CG  . PRO A 1 185 ? -0.851  -5.019  18.946  1.00 10.57  ? 186 PRO A CG  1 
ATOM   1549 C  CD  . PRO A 1 185 ? -0.639  -4.134  17.739  1.00 9.81   ? 186 PRO A CD  1 
ATOM   1550 N  N   A GLU A 1 186 ? -4.531  -6.093  18.430  0.50 12.10  ? 187 GLU A N   1 
ATOM   1551 N  N   B GLU A 1 186 ? -4.614  -6.022  18.521  0.50 12.79  ? 187 GLU A N   1 
ATOM   1552 C  CA  A GLU A 1 186 ? -5.814  -5.731  18.962  0.50 14.08  ? 187 GLU A CA  1 
ATOM   1553 C  CA  B GLU A 1 186 ? -5.936  -5.555  19.163  0.50 12.62  ? 187 GLU A CA  1 
ATOM   1554 C  C   A GLU A 1 186 ? -5.674  -4.925  20.259  0.50 12.23  ? 187 GLU A C   1 
ATOM   1555 C  C   B GLU A 1 186 ? -5.700  -4.800  20.428  0.50 12.66  ? 187 GLU A C   1 
ATOM   1556 O  O   A GLU A 1 186 ? -6.286  -3.854  20.330  0.50 13.13  ? 187 GLU A O   1 
ATOM   1557 O  O   B GLU A 1 186 ? -6.322  -3.744  20.748  0.50 15.39  ? 187 GLU A O   1 
ATOM   1558 C  CB  A GLU A 1 186 ? -6.547  -7.022  19.120  0.50 12.35  ? 187 GLU A CB  1 
ATOM   1559 C  CB  B GLU A 1 186 ? -6.726  -6.762  19.572  0.50 16.57  ? 187 GLU A CB  1 
ATOM   1560 C  CG  A GLU A 1 186 ? -7.775  -6.814  20.017  0.50 15.29  ? 187 GLU A CG  1 
ATOM   1561 C  CG  B GLU A 1 186 ? -7.496  -7.331  18.398  0.50 18.84  ? 187 GLU A CG  1 
ATOM   1562 C  CD  A GLU A 1 186 ? -8.462  -8.103  20.419  0.50 19.29  ? 187 GLU A CD  1 
ATOM   1563 C  CD  B GLU A 1 186 ? -8.326  -8.534  18.805  0.50 22.31  ? 187 GLU A CD  1 
ATOM   1564 O  OE1 A GLU A 1 186 ? -8.304  -9.124  19.667  0.50 20.03  ? 187 GLU A OE1 1 
ATOM   1565 O  OE1 B GLU A 1 186 ? -8.423  -8.796  20.059  0.50 21.83  ? 187 GLU A OE1 1 
ATOM   1566 O  OE2 A GLU A 1 186 ? -9.209  -8.088  21.433  0.50 20.12  ? 187 GLU A OE2 1 
ATOM   1567 O  OE2 B GLU A 1 186 ? -8.891  -9.232  17.904  0.50 26.46  ? 187 GLU A OE2 1 
ATOM   1568 N  N   . SER A 1 187 ? -4.786  -5.351  21.207  1.00 11.34  ? 188 SER A N   1 
ATOM   1569 C  CA  . SER A 1 187 ? -4.594  -4.734  22.479  1.00 12.20  ? 188 SER A CA  1 
ATOM   1570 C  C   . SER A 1 187 ? -3.480  -3.686  22.505  1.00 11.72  ? 188 SER A C   1 
ATOM   1571 O  O   . SER A 1 187 ? -2.430  -3.904  21.842  1.00 12.87  ? 188 SER A O   1 
ATOM   1572 C  CB  . SER A 1 187 ? -4.189  -5.770  23.514  1.00 14.16  ? 188 SER A CB  1 
ATOM   1573 O  OG  . SER A 1 187 ? -3.935  -5.220  24.808  1.00 14.61  ? 188 SER A OG  1 
ATOM   1574 N  N   . LEU A 1 188 ? -3.634  -2.628  23.232  1.00 11.43  ? 189 LEU A N   1 
ATOM   1575 C  CA  . LEU A 1 188 ? -2.585  -1.640  23.465  1.00 12.25  ? 189 LEU A CA  1 
ATOM   1576 C  C   . LEU A 1 188 ? -1.984  -1.759  24.850  1.00 11.25  ? 189 LEU A C   1 
ATOM   1577 O  O   . LEU A 1 188 ? -1.316  -0.790  25.275  1.00 12.72  ? 189 LEU A O   1 
ATOM   1578 C  CB  . LEU A 1 188 ? -3.064  -0.203  23.158  1.00 13.08  ? 189 LEU A CB  1 
ATOM   1579 C  CG  . LEU A 1 188 ? -3.498  0.115   21.751  1.00 14.39  ? 189 LEU A CG  1 
ATOM   1580 C  CD1 . LEU A 1 188 ? -4.042  1.506   21.606  1.00 17.05  ? 189 LEU A CD1 1 
ATOM   1581 C  CD2 . LEU A 1 188 ? -2.357  -0.169  20.765  1.00 16.57  ? 189 LEU A CD2 1 
ATOM   1582 N  N   . ASP A 1 189 ? -2.097  -2.912  25.534  1.00 11.01  ? 190 ASP A N   1 
ATOM   1583 C  CA  . ASP A 1 189 ? -1.335  -3.097  26.769  1.00 11.71  ? 190 ASP A CA  1 
ATOM   1584 C  C   . ASP A 1 189 ? 0.165   -3.054  26.481  1.00 9.89   ? 190 ASP A C   1 
ATOM   1585 O  O   . ASP A 1 189 ? 0.608   -3.554  25.428  1.00 9.88   ? 190 ASP A O   1 
ATOM   1586 C  CB  . ASP A 1 189 ? -1.713  -4.433  27.340  1.00 13.38  ? 190 ASP A CB  1 
ATOM   1587 C  CG  . ASP A 1 189 ? -3.125  -4.501  28.016  1.00 18.12  ? 190 ASP A CG  1 
ATOM   1588 O  OD1 . ASP A 1 189 ? -3.694  -3.430  28.247  1.00 24.77  ? 190 ASP A OD1 1 
ATOM   1589 O  OD2 . ASP A 1 189 ? -3.549  -5.621  28.285  1.00 23.12  ? 190 ASP A OD2 1 
ATOM   1590 N  N   . TYR A 1 190 ? 0.948   -2.478  27.398  1.00 9.19   ? 191 TYR A N   1 
ATOM   1591 C  CA  . TYR A 1 190 ? 2.353   -2.249  27.086  1.00 9.11   ? 191 TYR A CA  1 
ATOM   1592 C  C   . TYR A 1 190 ? 3.230   -2.321  28.299  1.00 8.74   ? 191 TYR A C   1 
ATOM   1593 O  O   . TYR A 1 190 ? 2.789   -2.183  29.468  1.00 9.77   ? 191 TYR A O   1 
ATOM   1594 C  CB  . TYR A 1 190 ? 2.490   -0.835  26.405  1.00 9.64   ? 191 TYR A CB  1 
ATOM   1595 C  CG  . TYR A 1 190 ? 2.070   0.305   27.287  1.00 9.66   ? 191 TYR A CG  1 
ATOM   1596 C  CD1 . TYR A 1 190 ? 3.000   0.936   28.159  1.00 10.54  ? 191 TYR A CD1 1 
ATOM   1597 C  CD2 . TYR A 1 190 ? 0.771   0.811   27.241  1.00 10.57  ? 191 TYR A CD2 1 
ATOM   1598 C  CE1 . TYR A 1 190 ? 2.617   1.954   28.995  1.00 11.38  ? 191 TYR A CE1 1 
ATOM   1599 C  CE2 . TYR A 1 190 ? 0.373   1.870   28.067  1.00 11.60  ? 191 TYR A CE2 1 
ATOM   1600 C  CZ  . TYR A 1 190 ? 1.272   2.437   28.963  1.00 11.20  ? 191 TYR A CZ  1 
ATOM   1601 O  OH  . TYR A 1 190 ? 0.930   3.447   29.784  1.00 12.34  ? 191 TYR A OH  1 
ATOM   1602 N  N   . TRP A 1 191 ? 4.532   -2.470  28.000  1.00 8.29   ? 192 TRP A N   1 
ATOM   1603 C  CA  . TRP A 1 191 ? 5.623   -2.201  28.944  1.00 8.35   ? 192 TRP A CA  1 
ATOM   1604 C  C   . TRP A 1 191 ? 6.302   -0.917  28.533  1.00 7.73   ? 192 TRP A C   1 
ATOM   1605 O  O   . TRP A 1 191 ? 6.325   -0.540  27.354  1.00 8.64   ? 192 TRP A O   1 
ATOM   1606 C  CB  . TRP A 1 191 ? 6.665   -3.317  28.936  1.00 9.01   ? 192 TRP A CB  1 
ATOM   1607 C  CG  . TRP A 1 191 ? 6.167   -4.648  29.310  1.00 8.99   ? 192 TRP A CG  1 
ATOM   1608 C  CD1 . TRP A 1 191 ? 5.946   -5.103  30.591  1.00 10.07  ? 192 TRP A CD1 1 
ATOM   1609 C  CD2 . TRP A 1 191 ? 5.885   -5.772  28.442  1.00 9.06   ? 192 TRP A CD2 1 
ATOM   1610 N  NE1 . TRP A 1 191 ? 5.566   -6.417  30.558  1.00 10.85  ? 192 TRP A NE1 1 
ATOM   1611 C  CE2 . TRP A 1 191 ? 5.487   -6.863  29.266  1.00 10.26  ? 192 TRP A CE2 1 
ATOM   1612 C  CE3 . TRP A 1 191 ? 5.998   -5.969  27.052  1.00 9.64   ? 192 TRP A CE3 1 
ATOM   1613 C  CZ2 . TRP A 1 191 ? 5.230   -8.110  28.733  1.00 11.07  ? 192 TRP A CZ2 1 
ATOM   1614 C  CZ3 . TRP A 1 191 ? 5.713   -7.204  26.561  1.00 10.79  ? 192 TRP A CZ3 1 
ATOM   1615 C  CH2 . TRP A 1 191 ? 5.344   -8.259  27.390  1.00 12.23  ? 192 TRP A CH2 1 
ATOM   1616 N  N   . THR A 1 192 ? 6.925   -0.227  29.491  1.00 7.86   ? 193 THR A N   1 
ATOM   1617 C  CA  . THR A 1 192 ? 7.656   1.001   29.164  1.00 7.91   ? 193 THR A CA  1 
ATOM   1618 C  C   . THR A 1 192 ? 8.878   1.144   30.046  1.00 7.37   ? 193 THR A C   1 
ATOM   1619 O  O   . THR A 1 192 ? 8.889   0.750   31.216  1.00 8.64   ? 193 THR A O   1 
ATOM   1620 C  CB  . THR A 1 192 ? 6.703   2.206   29.286  1.00 8.31   ? 193 THR A CB  1 
ATOM   1621 O  OG1 . THR A 1 192 ? 7.397   3.393   28.869  1.00 8.44   ? 193 THR A OG1 1 
ATOM   1622 C  CG2 . THR A 1 192 ? 6.206   2.429   30.660  1.00 9.70   ? 193 THR A CG2 1 
ATOM   1623 N  N   . TYR A 1 193 ? 9.922   1.749   29.466  1.00 7.52   ? 194 TYR A N   1 
ATOM   1624 C  CA  . TYR A 1 193 ? 11.162  2.035   30.203  1.00 7.85   ? 194 TYR A CA  1 
ATOM   1625 C  C   . TYR A 1 193 ? 11.912  3.085   29.418  1.00 7.57   ? 194 TYR A C   1 
ATOM   1626 O  O   . TYR A 1 193 ? 11.706  3.257   28.215  1.00 7.83   ? 194 TYR A O   1 
ATOM   1627 C  CB  . TYR A 1 193 ? 11.990  0.751   30.405  1.00 8.47   ? 194 TYR A CB  1 
ATOM   1628 C  CG  . TYR A 1 193 ? 12.687  0.272   29.157  1.00 7.71   ? 194 TYR A CG  1 
ATOM   1629 C  CD1 . TYR A 1 193 ? 12.016  -0.466  28.153  1.00 7.89   ? 194 TYR A CD1 1 
ATOM   1630 C  CD2 . TYR A 1 193 ? 14.006  0.609   28.935  1.00 8.08   ? 194 TYR A CD2 1 
ATOM   1631 C  CE1 . TYR A 1 193 ? 12.653  -0.798  26.995  1.00 7.40   ? 194 TYR A CE1 1 
ATOM   1632 C  CE2 . TYR A 1 193 ? 14.661  0.252   27.761  1.00 7.94   ? 194 TYR A CE2 1 
ATOM   1633 C  CZ  . TYR A 1 193 ? 13.984  -0.431  26.762  1.00 7.18   ? 194 TYR A CZ  1 
ATOM   1634 O  OH  . TYR A 1 193 ? 14.644  -0.727  25.625  1.00 7.51   ? 194 TYR A OH  1 
ATOM   1635 N  N   . PRO A 1 194 ? 12.891  3.767   30.080  1.00 7.75   ? 195 PRO A N   1 
ATOM   1636 C  CA  . PRO A 1 194 ? 13.704  4.775   29.395  1.00 8.30   ? 195 PRO A CA  1 
ATOM   1637 C  C   . PRO A 1 194 ? 14.936  4.115   28.749  1.00 7.13   ? 195 PRO A C   1 
ATOM   1638 O  O   . PRO A 1 194 ? 15.635  3.325   29.423  1.00 8.57   ? 195 PRO A O   1 
ATOM   1639 C  CB  . PRO A 1 194 ? 14.193  5.699   30.538  1.00 10.03  ? 195 PRO A CB  1 
ATOM   1640 C  CG  . PRO A 1 194 ? 14.196  4.766   31.756  1.00 10.84  ? 195 PRO A CG  1 
ATOM   1641 C  CD  . PRO A 1 194 ? 13.072  3.792   31.554  1.00 9.45   ? 195 PRO A CD  1 
ATOM   1642 N  N   . GLY A 1 195 ? 15.168  4.408   27.499  1.00 7.32   ? 196 GLY A N   1 
ATOM   1643 C  CA  . GLY A 1 195 ? 16.285  3.805   26.791  1.00 7.67   ? 196 GLY A CA  1 
ATOM   1644 C  C   . GLY A 1 195 ? 16.828  4.673   25.716  1.00 7.00   ? 196 GLY A C   1 
ATOM   1645 O  O   . GLY A 1 195 ? 16.943  5.908   25.839  1.00 7.89   ? 196 GLY A O   1 
ATOM   1646 N  N   . SER A 1 196 ? 17.256  4.005   24.651  1.00 7.03   ? 197 SER A N   1 
ATOM   1647 C  CA  . SER A 1 196 ? 18.096  4.646   23.615  1.00 7.28   ? 197 SER A CA  1 
ATOM   1648 C  C   . SER A 1 196 ? 17.622  4.260   22.230  1.00 6.39   ? 197 SER A C   1 
ATOM   1649 O  O   . SER A 1 196 ? 16.876  3.290   22.049  1.00 6.97   ? 197 SER A O   1 
ATOM   1650 C  CB  . SER A 1 196 ? 19.568  4.244   23.780  1.00 7.97   ? 197 SER A CB  1 
ATOM   1651 O  OG  . SER A 1 196 ? 19.814  2.905   23.356  1.00 7.56   ? 197 SER A OG  1 
ATOM   1652 N  N   . LEU A 1 197 ? 18.169  4.939   21.240  1.00 7.20   ? 198 LEU A N   1 
ATOM   1653 C  CA  . LEU A 1 197 ? 18.178  4.389   19.866  1.00 6.97   ? 198 LEU A CA  1 
ATOM   1654 C  C   . LEU A 1 197 ? 18.898  3.073   19.917  1.00 7.10   ? 198 LEU A C   1 
ATOM   1655 O  O   . LEU A 1 197 ? 19.917  2.892   20.617  1.00 7.60   ? 198 LEU A O   1 
ATOM   1656 C  CB  . LEU A 1 197 ? 18.921  5.319   18.932  1.00 8.24   ? 198 LEU A CB  1 
ATOM   1657 C  CG  . LEU A 1 197 ? 18.425  6.730   18.843  1.00 8.45   ? 198 LEU A CG  1 
ATOM   1658 C  CD1 . LEU A 1 197 ? 19.344  7.570   17.926  1.00 11.19  ? 198 LEU A CD1 1 
ATOM   1659 C  CD2 . LEU A 1 197 ? 17.031  6.819   18.345  1.00 10.59  ? 198 LEU A CD2 1 
ATOM   1660 N  N   . THR A 1 198 ? 18.420  2.107   19.096  1.00 6.98   ? 199 THR A N   1 
ATOM   1661 C  CA  . THR A 1 198 ? 19.115  0.829   19.027  1.00 7.78   ? 199 THR A CA  1 
ATOM   1662 C  C   . THR A 1 198 ? 20.112  0.732   17.883  1.00 7.13   ? 199 THR A C   1 
ATOM   1663 O  O   . THR A 1 198 ? 20.728  -0.328  17.720  1.00 8.42   ? 199 THR A O   1 
ATOM   1664 C  CB  . THR A 1 198 ? 18.112  -0.345  18.901  1.00 7.31   ? 199 THR A CB  1 
ATOM   1665 O  OG1 . THR A 1 198 ? 17.539  -0.274  17.616  1.00 7.26   ? 199 THR A OG1 1 
ATOM   1666 C  CG2 . THR A 1 198 ? 17.065  -0.333  20.010  1.00 8.44   ? 199 THR A CG2 1 
ATOM   1667 N  N   . THR A 1 199 ? 20.253  1.802   17.109  1.00 8.39   ? 200 THR A N   1 
ATOM   1668 C  CA  . THR A 1 199 ? 21.282  1.919   16.123  1.00 9.11   ? 200 THR A CA  1 
ATOM   1669 C  C   . THR A 1 199 ? 22.130  3.108   16.477  1.00 8.97   ? 200 THR A C   1 
ATOM   1670 O  O   . THR A 1 199 ? 21.690  4.049   17.094  1.00 8.68   ? 200 THR A O   1 
ATOM   1671 C  CB  . THR A 1 199 ? 20.712  2.176   14.669  1.00 11.58  ? 200 THR A CB  1 
ATOM   1672 O  OG1 . THR A 1 199 ? 20.052  3.455   14.614  1.00 14.71  ? 200 THR A OG1 1 
ATOM   1673 C  CG2 . THR A 1 199 ? 19.751  1.115   14.259  1.00 11.03  ? 200 THR A CG2 1 
ATOM   1674 N  N   . PRO A 1 200 ? 23.417  3.126   16.001  1.00 9.23   ? 201 PRO A N   1 
ATOM   1675 C  CA  . PRO A 1 200 ? 24.153  4.368   16.044  1.00 9.34   ? 201 PRO A CA  1 
ATOM   1676 C  C   . PRO A 1 200 ? 23.312  5.496   15.528  1.00 9.30   ? 201 PRO A C   1 
ATOM   1677 O  O   . PRO A 1 200 ? 22.592  5.339   14.524  1.00 10.74  ? 201 PRO A O   1 
ATOM   1678 C  CB  . PRO A 1 200 ? 25.374  4.042   15.168  1.00 10.77  ? 201 PRO A CB  1 
ATOM   1679 C  CG  . PRO A 1 200 ? 25.588  2.573   15.410  1.00 11.31  ? 201 PRO A CG  1 
ATOM   1680 C  CD  . PRO A 1 200 ? 24.187  2.025   15.383  1.00 10.30  ? 201 PRO A CD  1 
ATOM   1681 N  N   . PRO A 1 201 ? 23.361  6.651   16.157  1.00 9.42   ? 202 PRO A N   1 
ATOM   1682 C  CA  . PRO A 1 201 ? 24.297  7.062   17.232  1.00 10.15  ? 202 PRO A CA  1 
ATOM   1683 C  C   . PRO A 1 201 ? 23.948  6.663   18.654  1.00 9.32   ? 202 PRO A C   1 
ATOM   1684 O  O   . PRO A 1 201 ? 24.654  7.080   19.570  1.00 10.18  ? 202 PRO A O   1 
ATOM   1685 C  CB  . PRO A 1 201 ? 24.307  8.604   17.077  1.00 12.34  ? 202 PRO A CB  1 
ATOM   1686 C  CG  . PRO A 1 201 ? 22.872  8.928   16.647  1.00 12.56  ? 202 PRO A CG  1 
ATOM   1687 C  CD  . PRO A 1 201 ? 22.579  7.831   15.669  1.00 11.91  ? 202 PRO A CD  1 
ATOM   1688 N  N   . LEU A 1 202 ? 22.938  5.798   18.851  1.00 8.60   ? 203 LEU A N   1 
ATOM   1689 C  CA  . LEU A 1 202 ? 22.726  5.160   20.161  1.00 8.30   ? 203 LEU A CA  1 
ATOM   1690 C  C   . LEU A 1 202 ? 22.340  6.157   21.243  1.00 8.45   ? 203 LEU A C   1 
ATOM   1691 O  O   . LEU A 1 202 ? 22.480  5.892   22.440  1.00 8.80   ? 203 LEU A O   1 
ATOM   1692 C  CB  . LEU A 1 202 ? 23.875  4.259   20.584  1.00 8.91   ? 203 LEU A CB  1 
ATOM   1693 C  CG  . LEU A 1 202 ? 24.183  3.113   19.632  1.00 8.79   ? 203 LEU A CG  1 
ATOM   1694 C  CD1 . LEU A 1 202 ? 25.500  2.436   20.048  1.00 10.55  ? 203 LEU A CD1 1 
ATOM   1695 C  CD2 . LEU A 1 202 ? 23.052  2.075   19.574  1.00 9.51   ? 203 LEU A CD2 1 
ATOM   1696 N  N   . LEU A 1 203 ? 21.788  7.298   20.852  1.00 8.72   ? 204 LEU A N   1 
ATOM   1697 C  CA  . LEU A 1 203 ? 21.496  8.386   21.785  1.00 9.11   ? 204 LEU A CA  1 
ATOM   1698 C  C   . LEU A 1 203 ? 20.423  7.961   22.760  1.00 8.55   ? 204 LEU A C   1 
ATOM   1699 O  O   . LEU A 1 203 ? 19.454  7.253   22.441  1.00 8.26   ? 204 LEU A O   1 
ATOM   1700 C  CB  . LEU A 1 203 ? 21.026  9.602   21.004  1.00 10.62  ? 204 LEU A CB  1 
ATOM   1701 C  CG  . LEU A 1 203 ? 22.085  10.201  20.066  1.00 12.24  ? 204 LEU A CG  1 
ATOM   1702 C  CD1 . LEU A 1 203 ? 21.485  11.238  19.151  1.00 13.66  ? 204 LEU A CD1 1 
ATOM   1703 C  CD2 . LEU A 1 203 ? 23.272  10.797  20.875  1.00 16.12  ? 204 LEU A CD2 1 
ATOM   1704 N  N   . GLU A 1 204 ? 20.563  8.425   23.998  1.00 8.78   ? 205 GLU A N   1 
ATOM   1705 C  CA  . GLU A 1 204 ? 19.737  8.037   25.115  1.00 8.84   ? 205 GLU A CA  1 
ATOM   1706 C  C   . GLU A 1 204 ? 18.565  9.011   25.221  1.00 8.51   ? 205 GLU A C   1 
ATOM   1707 O  O   . GLU A 1 204 ? 18.428  9.762   26.185  1.00 11.16  ? 205 GLU A O   1 
ATOM   1708 C  CB  . GLU A 1 204 ? 20.575  7.896   26.396  1.00 10.06  ? 205 GLU A CB  1 
ATOM   1709 C  CG  . GLU A 1 204 ? 21.465  6.690   26.267  1.00 9.94   ? 205 GLU A CG  1 
ATOM   1710 C  CD  . GLU A 1 204 ? 22.377  6.411   27.427  1.00 10.66  ? 205 GLU A CD  1 
ATOM   1711 O  OE1 . GLU A 1 204 ? 22.710  7.361   28.191  1.00 13.58  ? 205 GLU A OE1 1 
ATOM   1712 O  OE2 . GLU A 1 204 ? 22.812  5.235   27.578  1.00 10.69  ? 205 GLU A OE2 1 
ATOM   1713 N  N   . CYS A 1 205 ? 17.677  8.931   24.264  1.00 8.03   ? 206 CYS A N   1 
ATOM   1714 C  CA  . CYS A 1 205 ? 16.614  9.916   24.043  1.00 8.12   ? 206 CYS A CA  1 
ATOM   1715 C  C   . CYS A 1 205 ? 15.248  9.281   23.943  1.00 7.74   ? 206 CYS A C   1 
ATOM   1716 O  O   . CYS A 1 205 ? 14.317  10.001  23.563  1.00 9.50   ? 206 CYS A O   1 
ATOM   1717 C  CB  . CYS A 1 205 ? 16.915  10.749  22.793  1.00 9.08   ? 206 CYS A CB  1 
ATOM   1718 S  SG  . CYS A 1 205 ? 16.981  9.748   21.265  1.00 9.83   ? 206 CYS A SG  1 
ATOM   1719 N  N   . VAL A 1 206 ? 15.104  7.999   24.208  1.00 7.69   ? 207 VAL A N   1 
ATOM   1720 C  CA  . VAL A 1 206 ? 13.863  7.292   23.847  1.00 7.79   ? 207 VAL A CA  1 
ATOM   1721 C  C   . VAL A 1 206 ? 13.085  6.862   25.108  1.00 7.83   ? 207 VAL A C   1 
ATOM   1722 O  O   . VAL A 1 206 ? 13.652  6.180   25.972  1.00 8.70   ? 207 VAL A O   1 
ATOM   1723 C  CB  . VAL A 1 206 ? 14.167  6.028   23.014  1.00 8.00   ? 207 VAL A CB  1 
ATOM   1724 C  CG1 . VAL A 1 206 ? 12.856  5.320   22.677  1.00 8.00   ? 207 VAL A CG1 1 
ATOM   1725 C  CG2 . VAL A 1 206 ? 14.909  6.383   21.749  1.00 8.48   ? 207 VAL A CG2 1 
ATOM   1726 N  N   . THR A 1 207 ? 11.797  7.157   25.124  1.00 6.94   ? 208 THR A N   1 
ATOM   1727 C  CA  . THR A 1 207 ? 10.847  6.424   25.986  1.00 7.36   ? 208 THR A CA  1 
ATOM   1728 C  C   . THR A 1 207 ? 10.324  5.280   25.158  1.00 6.87   ? 208 THR A C   1 
ATOM   1729 O  O   . THR A 1 207 ? 9.637   5.476   24.138  1.00 7.73   ? 208 THR A O   1 
ATOM   1730 C  CB  . THR A 1 207 ? 9.684   7.309   26.435  1.00 8.28   ? 208 THR A CB  1 
ATOM   1731 O  OG1 . THR A 1 207 ? 10.182  8.439   27.179  1.00 9.55   ? 208 THR A OG1 1 
ATOM   1732 C  CG2 . THR A 1 207 ? 8.737   6.516   27.298  1.00 9.75   ? 208 THR A CG2 1 
ATOM   1733 N  N   . TRP A 1 208 ? 10.690  4.056   25.572  1.00 6.59   ? 209 TRP A N   1 
ATOM   1734 C  CA  . TRP A 1 208 ? 10.240  2.875   24.866  1.00 6.68   ? 209 TRP A CA  1 
ATOM   1735 C  C   . TRP A 1 208 ? 8.872   2.458   25.386  1.00 6.53   ? 209 TRP A C   1 
ATOM   1736 O  O   . TRP A 1 208 ? 8.631   2.411   26.597  1.00 7.10   ? 209 TRP A O   1 
ATOM   1737 C  CB  . TRP A 1 208 ? 11.240  1.704   25.082  1.00 6.96   ? 209 TRP A CB  1 
ATOM   1738 C  CG  . TRP A 1 208 ? 12.352  1.806   24.136  1.00 6.62   ? 209 TRP A CG  1 
ATOM   1739 C  CD1 . TRP A 1 208 ? 13.603  2.382   24.307  1.00 7.39   ? 209 TRP A CD1 1 
ATOM   1740 C  CD2 . TRP A 1 208 ? 12.295  1.407   22.760  1.00 6.64   ? 209 TRP A CD2 1 
ATOM   1741 N  NE1 . TRP A 1 208 ? 14.298  2.373   23.133  1.00 7.44   ? 209 TRP A NE1 1 
ATOM   1742 C  CE2 . TRP A 1 208 ? 13.542  1.785   22.156  1.00 6.95   ? 209 TRP A CE2 1 
ATOM   1743 C  CE3 . TRP A 1 208 ? 11.315  0.787   21.983  1.00 6.64   ? 209 TRP A CE3 1 
ATOM   1744 C  CZ2 . TRP A 1 208 ? 13.805  1.555   20.811  1.00 7.97   ? 209 TRP A CZ2 1 
ATOM   1745 C  CZ3 . TRP A 1 208 ? 11.595  0.528   20.672  1.00 7.68   ? 209 TRP A CZ3 1 
ATOM   1746 C  CH2 . TRP A 1 208 ? 12.828  0.907   20.080  1.00 8.39   ? 209 TRP A CH2 1 
ATOM   1747 N  N   . ILE A 1 209 ? 7.995   2.107   24.456  1.00 6.52   ? 210 ILE A N   1 
ATOM   1748 C  CA  . ILE A 1 209 ? 6.668   1.579   24.740  1.00 7.09   ? 210 ILE A CA  1 
ATOM   1749 C  C   . ILE A 1 209 ? 6.542   0.332   23.916  1.00 6.67   ? 210 ILE A C   1 
ATOM   1750 O  O   . ILE A 1 209 ? 6.494   0.413   22.674  1.00 7.91   ? 210 ILE A O   1 
ATOM   1751 C  CB  . ILE A 1 209 ? 5.588   2.618   24.403  1.00 7.81   ? 210 ILE A CB  1 
ATOM   1752 C  CG1 . ILE A 1 209 ? 5.780   3.889   25.208  1.00 9.11   ? 210 ILE A CG1 1 
ATOM   1753 C  CG2 . ILE A 1 209 ? 4.202   2.007   24.648  1.00 9.15   ? 210 ILE A CG2 1 
ATOM   1754 C  CD1 . ILE A 1 209 ? 4.946   5.078   24.736  1.00 10.48  ? 210 ILE A CD1 1 
ATOM   1755 N  N   . VAL A 1 210 ? 6.573   -0.835  24.530  1.00 7.02   ? 211 VAL A N   1 
ATOM   1756 C  CA  . VAL A 1 210 ? 6.607   -2.111  23.843  1.00 6.86   ? 211 VAL A CA  1 
ATOM   1757 C  C   . VAL A 1 210 ? 5.278   -2.807  24.096  1.00 7.20   ? 211 VAL A C   1 
ATOM   1758 O  O   . VAL A 1 210 ? 4.904   -3.070  25.240  1.00 7.84   ? 211 VAL A O   1 
ATOM   1759 C  CB  . VAL A 1 210 ? 7.797   -2.978  24.297  1.00 7.67   ? 211 VAL A CB  1 
ATOM   1760 C  CG1 . VAL A 1 210 ? 7.770   -4.325  23.592  1.00 8.63   ? 211 VAL A CG1 1 
ATOM   1761 C  CG2 . VAL A 1 210 ? 9.089   -2.229  24.006  1.00 8.53   ? 211 VAL A CG2 1 
ATOM   1762 N  N   . LEU A 1 211 ? 4.526   -3.103  23.027  1.00 7.60   ? 212 LEU A N   1 
ATOM   1763 C  CA  . LEU A 1 211 ? 3.210   -3.739  23.217  1.00 7.91   ? 212 LEU A CA  1 
ATOM   1764 C  C   . LEU A 1 211 ? 3.390   -5.180  23.606  1.00 7.90   ? 212 LEU A C   1 
ATOM   1765 O  O   . LEU A 1 211 ? 4.240   -5.913  23.101  1.00 8.68   ? 212 LEU A O   1 
ATOM   1766 C  CB  . LEU A 1 211 ? 2.411   -3.644  21.920  1.00 8.81   ? 212 LEU A CB  1 
ATOM   1767 C  CG  . LEU A 1 211 ? 2.048   -2.216  21.505  1.00 9.29   ? 212 LEU A CG  1 
ATOM   1768 C  CD1 . LEU A 1 211 ? 1.030   -2.274  20.306  1.00 11.08  ? 212 LEU A CD1 1 
ATOM   1769 C  CD2 . LEU A 1 211 ? 1.503   -1.374  22.627  1.00 9.92   ? 212 LEU A CD2 1 
ATOM   1770 N  N   . LYS A 1 212 ? 2.510   -5.643  24.521  1.00 9.27   ? 213 LYS A N   1 
ATOM   1771 C  CA  . LYS A 1 212 ? 2.541   -7.029  24.944  1.00 10.17  ? 213 LYS A CA  1 
ATOM   1772 C  C   . LYS A 1 212 ? 2.082   -7.982  23.852  1.00 8.99   ? 213 LYS A C   1 
ATOM   1773 O  O   . LYS A 1 212 ? 2.609   -9.095  23.776  1.00 11.29  ? 213 LYS A O   1 
ATOM   1774 C  CB  . LYS A 1 212 ? 1.686   -7.196  26.178  1.00 13.58  ? 213 LYS A CB  1 
ATOM   1775 C  CG  . LYS A 1 212 ? 1.248   -8.547  26.636  1.00 23.34  ? 213 LYS A CG  1 
ATOM   1776 C  CD  . LYS A 1 212 ? -0.018  -8.346  27.561  1.00 31.00  ? 213 LYS A CD  1 
ATOM   1777 C  CE  . LYS A 1 212 ? -1.444  -8.256  26.865  1.00 30.41  ? 213 LYS A CE  1 
ATOM   1778 N  NZ  . LYS A 1 212 ? -1.660  -7.669  25.442  1.00 23.59  ? 213 LYS A NZ  1 
ATOM   1779 N  N   A GLU A 1 213 ? 1.108   -7.593  23.081  0.50 9.01   ? 214 GLU A N   1 
ATOM   1780 N  N   B GLU A 1 213 ? 1.130   -7.621  23.027  0.50 9.04   ? 214 GLU A N   1 
ATOM   1781 C  CA  A GLU A 1 213 ? 0.515   -8.481  22.119  0.50 8.87   ? 214 GLU A CA  1 
ATOM   1782 C  CA  B GLU A 1 213 ? 0.572   -8.502  22.000  0.50 9.37   ? 214 GLU A CA  1 
ATOM   1783 C  C   A GLU A 1 213 ? 1.271   -8.408  20.816  0.50 8.55   ? 214 GLU A C   1 
ATOM   1784 C  C   B GLU A 1 213 ? 1.378   -8.419  20.725  0.50 9.10   ? 214 GLU A C   1 
ATOM   1785 O  O   A GLU A 1 213 ? 1.311   -7.336  20.216  0.50 8.59   ? 214 GLU A O   1 
ATOM   1786 O  O   B GLU A 1 213 ? 1.438   -7.357  20.118  0.50 9.23   ? 214 GLU A O   1 
ATOM   1787 C  CB  A GLU A 1 213 ? -0.966  -8.199  21.907  0.50 9.74   ? 214 GLU A CB  1 
ATOM   1788 C  CB  B GLU A 1 213 ? -0.899  -8.149  21.721  0.50 10.61  ? 214 GLU A CB  1 
ATOM   1789 C  CG  A GLU A 1 213 ? -1.571  -9.289  21.049  0.50 12.46  ? 214 GLU A CG  1 
ATOM   1790 C  CG  B GLU A 1 213 ? -1.646  -9.041  20.767  0.50 12.17  ? 214 GLU A CG  1 
ATOM   1791 C  CD  A GLU A 1 213 ? -3.058  -9.093  20.728  0.50 13.02  ? 214 GLU A CD  1 
ATOM   1792 C  CD  B GLU A 1 213 ? -3.127  -8.608  20.567  0.50 14.56  ? 214 GLU A CD  1 
ATOM   1793 O  OE1 A GLU A 1 213 ? -3.628  -8.000  20.966  0.50 11.70  ? 214 GLU A OE1 1 
ATOM   1794 O  OE1 B GLU A 1 213 ? -3.737  -8.054  21.541  0.50 13.24  ? 214 GLU A OE1 1 
ATOM   1795 O  OE2 A GLU A 1 213 ? -3.666  -9.983  20.133  0.50 15.44  ? 214 GLU A OE2 1 
ATOM   1796 O  OE2 B GLU A 1 213 ? -3.631  -8.766  19.406  0.50 18.21  ? 214 GLU A OE2 1 
ATOM   1797 N  N   A PRO A 1 214 ? 1.825   -9.525  20.316  0.50 8.72   ? 215 PRO A N   1 
ATOM   1798 N  N   B PRO A 1 214 ? 1.959   -9.515  20.284  0.50 8.86   ? 215 PRO A N   1 
ATOM   1799 C  CA  A PRO A 1 214 ? 2.470   -9.454  18.992  0.50 9.20   ? 215 PRO A CA  1 
ATOM   1800 C  CA  B PRO A 1 214 ? 2.600   -9.524  18.954  0.50 9.37   ? 215 PRO A CA  1 
ATOM   1801 C  C   A PRO A 1 214 ? 1.438   -9.355  17.909  0.50 8.80   ? 215 PRO A C   1 
ATOM   1802 C  C   B PRO A 1 214 ? 1.566   -9.528  17.834  0.50 9.60   ? 215 PRO A C   1 
ATOM   1803 O  O   A PRO A 1 214 ? 0.220   -9.616  18.186  0.50 10.34  ? 215 PRO A O   1 
ATOM   1804 O  O   B PRO A 1 214 ? 0.451   -10.033 17.980  0.50 9.27   ? 215 PRO A O   1 
ATOM   1805 C  CB  A PRO A 1 214 ? 3.210   -10.814 18.883  0.50 9.45   ? 215 PRO A CB  1 
ATOM   1806 C  CB  B PRO A 1 214 ? 3.409   -10.841 18.967  0.50 9.92   ? 215 PRO A CB  1 
ATOM   1807 C  CG  A PRO A 1 214 ? 2.388   -11.756 19.712  0.50 10.73  ? 215 PRO A CG  1 
ATOM   1808 C  CG  B PRO A 1 214 ? 3.407   -11.273 20.411  0.50 11.76  ? 215 PRO A CG  1 
ATOM   1809 C  CD  A PRO A 1 214 ? 1.771   -10.932 20.825  0.50 9.46   ? 215 PRO A CD  1 
ATOM   1810 C  CD  B PRO A 1 214 ? 2.174   -10.781 21.054  0.50 9.36   ? 215 PRO A CD  1 
ATOM   1811 N  N   . ILE A 1 215 ? 1.907   -9.005  16.697  1.00 9.09   ? 216 ILE A N   1 
ATOM   1812 C  CA  . ILE A 1 215 ? 1.129   -9.244  15.491  1.00 8.96   ? 216 ILE A CA  1 
ATOM   1813 C  C   . ILE A 1 215 ? 1.645   -10.506 14.833  1.00 9.15   ? 216 ILE A C   1 
ATOM   1814 O  O   . ILE A 1 215 ? 2.804   -10.877 14.993  1.00 10.66  ? 216 ILE A O   1 
ATOM   1815 C  CB  . ILE A 1 215 ? 1.136   -8.020  14.556  1.00 9.53   ? 216 ILE A CB  1 
ATOM   1816 C  CG1 . ILE A 1 215 ? 2.534   -7.676  14.056  1.00 10.36  ? 216 ILE A CG1 1 
ATOM   1817 C  CG2 . ILE A 1 215 ? 0.458   -6.835  15.211  1.00 10.76  ? 216 ILE A CG2 1 
ATOM   1818 C  CD1 . ILE A 1 215 ? 2.559   -6.729  12.875  1.00 12.32  ? 216 ILE A CD1 1 
ATOM   1819 N  N   A SER A 1 216 ? 0.680   -11.178 14.208  0.50 8.97   ? 217 SER A N   1 
ATOM   1820 N  N   B SER A 1 216 ? 0.884   -11.122 13.924  0.50 10.14  ? 217 SER A N   1 
ATOM   1821 C  CA  A SER A 1 216 ? 1.034   -12.242 13.250  0.50 9.45   ? 217 SER A CA  1 
ATOM   1822 C  CA  B SER A 1 216 ? 1.413   -12.341 13.290  0.50 10.69  ? 217 SER A CA  1 
ATOM   1823 C  C   A SER A 1 216 ? 1.371   -11.818 11.795  0.50 10.23  ? 217 SER A C   1 
ATOM   1824 C  C   B SER A 1 216 ? 1.353   -11.931 11.881  0.50 10.19  ? 217 SER A C   1 
ATOM   1825 O  O   A SER A 1 216 ? 0.645   -11.082 11.141  0.50 10.94  ? 217 SER A O   1 
ATOM   1826 O  O   B SER A 1 216 ? 0.383   -11.213 11.425  0.50 10.15  ? 217 SER A O   1 
ATOM   1827 C  CB  A SER A 1 216 ? -0.002  -13.347 13.267  0.50 10.98  ? 217 SER A CB  1 
ATOM   1828 C  CB  B SER A 1 216 ? 0.510   -13.520 13.583  0.50 13.11  ? 217 SER A CB  1 
ATOM   1829 O  OG  A SER A 1 216 ? -0.019  -13.995 14.505  0.50 14.70  ? 217 SER A OG  1 
ATOM   1830 O  OG  B SER A 1 216 ? -0.828  -13.229 13.169  0.50 15.36  ? 217 SER A OG  1 
ATOM   1831 N  N   . VAL A 1 217 ? 2.456   -12.316 11.225  1.00 10.24  ? 218 VAL A N   1 
ATOM   1832 C  CA  . VAL A 1 217 ? 2.733   -12.123 9.813   1.00 10.37  ? 218 VAL A CA  1 
ATOM   1833 C  C   . VAL A 1 217 ? 2.989   -13.483 9.213   1.00 10.09  ? 218 VAL A C   1 
ATOM   1834 O  O   . VAL A 1 217 ? 3.341   -14.434 9.925   1.00 11.37  ? 218 VAL A O   1 
ATOM   1835 C  CB  . VAL A 1 217 ? 3.927   -11.178 9.608   1.00 11.13  ? 218 VAL A CB  1 
ATOM   1836 C  CG1 . VAL A 1 217 ? 3.707   -9.862  10.253  1.00 11.43  ? 218 VAL A CG1 1 
ATOM   1837 C  CG2 . VAL A 1 217 ? 5.194   -11.807 10.109  1.00 13.50  ? 218 VAL A CG2 1 
ATOM   1838 N  N   . SER A 1 218 ? 2.871   -13.637 7.917   1.00 10.79  ? 219 SER A N   1 
ATOM   1839 C  CA  . SER A 1 218 ? 3.081   -14.966 7.345   1.00 11.62  ? 219 SER A CA  1 
ATOM   1840 C  C   . SER A 1 218 ? 4.551   -15.213 7.072   1.00 11.16  ? 219 SER A C   1 
ATOM   1841 O  O   . SER A 1 218 ? 5.360   -14.280 6.927   1.00 11.36  ? 219 SER A O   1 
ATOM   1842 C  CB  . SER A 1 218 ? 2.277   -15.132 6.064   1.00 12.44  ? 219 SER A CB  1 
ATOM   1843 O  OG  . SER A 1 218 ? 2.768   -14.260 5.071   1.00 13.00  ? 219 SER A OG  1 
ATOM   1844 N  N   A SER A 1 219 ? 4.819   -16.490 6.867   0.50 11.33  ? 220 SER A N   1 
ATOM   1845 N  N   B SER A 1 219 ? 4.932   -16.464 6.915   0.50 12.11  ? 220 SER A N   1 
ATOM   1846 C  CA  A SER A 1 219 ? 6.146   -16.867 6.520   0.50 12.04  ? 220 SER A CA  1 
ATOM   1847 C  CA  B SER A 1 219 ? 6.297   -16.768 6.564   0.50 13.50  ? 220 SER A CA  1 
ATOM   1848 C  C   A SER A 1 219 ? 6.570   -16.127 5.291   0.50 12.66  ? 220 SER A C   1 
ATOM   1849 C  C   B SER A 1 219 ? 6.637   -16.178 5.144   0.50 13.35  ? 220 SER A C   1 
ATOM   1850 O  O   A SER A 1 219 ? 7.726   -15.659 5.251   0.50 11.60  ? 220 SER A O   1 
ATOM   1851 O  O   B SER A 1 219 ? 7.738   -15.762 4.806   0.50 13.65  ? 220 SER A O   1 
ATOM   1852 C  CB  A SER A 1 219 ? 6.283   -18.381 6.288   0.50 12.90  ? 220 SER A CB  1 
ATOM   1853 C  CB  B SER A 1 219 ? 6.433   -18.289 6.688   0.50 13.77  ? 220 SER A CB  1 
ATOM   1854 O  OG  A SER A 1 219 ? 5.292   -18.920 5.500   0.50 12.25  ? 220 SER A OG  1 
ATOM   1855 O  OG  B SER A 1 219 ? 7.626   -18.688 6.131   0.50 16.85  ? 220 SER A OG  1 
ATOM   1856 N  N   . GLU A 1 220 ? 5.657   -16.066 4.296   1.00 12.80  ? 221 GLU A N   1 
ATOM   1857 C  CA  . GLU A 1 220 ? 5.957   -15.429 3.004   1.00 14.26  ? 221 GLU A CA  1 
ATOM   1858 C  C   . GLU A 1 220 ? 6.269   -13.934 3.167   1.00 12.49  ? 221 GLU A C   1 
ATOM   1859 O  O   . GLU A 1 220 ? 7.086   -13.395 2.447   1.00 14.35  ? 221 GLU A O   1 
ATOM   1860 C  CB  . GLU A 1 220 ? 4.807   -15.586 2.025   1.00 16.24  ? 221 GLU A CB  1 
ATOM   1861 C  CG  . GLU A 1 220 ? 4.677   -17.032 1.480   1.00 20.02  ? 221 GLU A CG  1 
ATOM   1862 C  CD  . GLU A 1 220 ? 3.701   -17.826 2.352   1.00 24.46  ? 221 GLU A CD  1 
ATOM   1863 O  OE1 . GLU A 1 220 ? 3.164   -17.312 3.367   1.00 20.11  ? 221 GLU A OE1 1 
ATOM   1864 O  OE2 . GLU A 1 220 ? 3.444   -18.967 2.036   1.00 60.55  ? 221 GLU A OE2 1 
ATOM   1865 N  N   . GLN A 1 221 ? 5.576   -13.284 4.044   1.00 12.10  ? 222 GLN A N   1 
ATOM   1866 C  CA  . GLN A 1 221 ? 5.822   -11.849 4.269   1.00 11.21  ? 222 GLN A CA  1 
ATOM   1867 C  C   . GLN A 1 221 ? 7.229   -11.649 4.799   1.00 11.84  ? 222 GLN A C   1 
ATOM   1868 O  O   . GLN A 1 221 ? 7.966   -10.789 4.294   1.00 12.33  ? 222 GLN A O   1 
ATOM   1869 C  CB  . GLN A 1 221 ? 4.772   -11.291 5.186   1.00 10.92  ? 222 GLN A CB  1 
ATOM   1870 C  CG  . GLN A 1 221 ? 3.411   -11.172 4.517   1.00 11.44  ? 222 GLN A CG  1 
ATOM   1871 C  CD  . GLN A 1 221 ? 2.308   -10.634 5.370   1.00 10.70  ? 222 GLN A CD  1 
ATOM   1872 O  OE1 . GLN A 1 221 ? 2.166   -10.986 6.565   1.00 11.26  ? 222 GLN A OE1 1 
ATOM   1873 N  NE2 . GLN A 1 221 ? 1.508   -9.759  4.804   1.00 11.59  ? 222 GLN A NE2 1 
ATOM   1874 N  N   A VAL A 1 222 ? 7.646   -12.398 5.821   0.50 11.88  ? 223 VAL A N   1 
ATOM   1875 N  N   B VAL A 1 222 ? 7.655   -12.400 5.826   0.50 12.44  ? 223 VAL A N   1 
ATOM   1876 C  CA  A VAL A 1 222 ? 8.977   -12.174 6.386   0.50 11.16  ? 223 VAL A CA  1 
ATOM   1877 C  CA  B VAL A 1 222 ? 9.019   -12.209 6.380   0.50 13.15  ? 223 VAL A CA  1 
ATOM   1878 C  C   A VAL A 1 222 ? 10.056  -12.672 5.382   0.50 12.24  ? 223 VAL A C   1 
ATOM   1879 C  C   B VAL A 1 222 ? 10.067  -12.663 5.362   0.50 13.55  ? 223 VAL A C   1 
ATOM   1880 O  O   A VAL A 1 222 ? 11.135  -12.088 5.301   0.50 12.56  ? 223 VAL A O   1 
ATOM   1881 O  O   B VAL A 1 222 ? 11.150  -12.085 5.284   0.50 13.67  ? 223 VAL A O   1 
ATOM   1882 C  CB  A VAL A 1 222 ? 9.082   -12.706 7.823   0.50 12.12  ? 223 VAL A CB  1 
ATOM   1883 C  CB  B VAL A 1 222 ? 9.262   -12.961 7.690   0.50 17.26  ? 223 VAL A CB  1 
ATOM   1884 C  CG1 A VAL A 1 222 ? 9.110   -14.198 7.823   0.50 11.79  ? 223 VAL A CG1 1 
ATOM   1885 C  CG1 B VAL A 1 222 ? 10.571  -12.498 8.283   0.50 23.96  ? 223 VAL A CG1 1 
ATOM   1886 C  CG2 A VAL A 1 222 ? 10.317  -12.137 8.504   0.50 13.38  ? 223 VAL A CG2 1 
ATOM   1887 C  CG2 B VAL A 1 222 ? 8.195   -12.591 8.655   0.50 17.49  ? 223 VAL A CG2 1 
ATOM   1888 N  N   . LEU A 1 223 ? 9.765   -13.691 4.591   1.00 13.79  ? 224 LEU A N   1 
ATOM   1889 C  CA  . LEU A 1 223 ? 10.687  -14.098 3.556   1.00 15.40  ? 224 LEU A CA  1 
ATOM   1890 C  C   . LEU A 1 223 ? 11.009  -12.956 2.617   1.00 14.60  ? 224 LEU A C   1 
ATOM   1891 O  O   . LEU A 1 223 ? 12.160  -12.838 2.148   1.00 15.80  ? 224 LEU A O   1 
ATOM   1892 C  CB  . LEU A 1 223 ? 10.210  -15.335 2.814   1.00 17.93  ? 224 LEU A CB  1 
ATOM   1893 C  CG  . LEU A 1 223 ? 10.485  -16.653 3.639   1.00 22.45  ? 224 LEU A CG  1 
ATOM   1894 C  CD1 . LEU A 1 223 ? 9.554   -17.785 3.125   1.00 27.51  ? 224 LEU A CD1 1 
ATOM   1895 C  CD2 . LEU A 1 223 ? 11.971  -17.038 3.614   1.00 26.52  ? 224 LEU A CD2 1 
ATOM   1896 N  N   . LYS A 1 224 ? 10.034  -12.106 2.307   1.00 13.13  ? 225 LYS A N   1 
ATOM   1897 C  CA  . LYS A 1 224 ? 10.264  -10.994 1.403   1.00 13.44  ? 225 LYS A CA  1 
ATOM   1898 C  C   . LYS A 1 224 ? 11.134  -9.934  2.055   1.00 11.96  ? 225 LYS A C   1 
ATOM   1899 O  O   . LYS A 1 224 ? 11.954  -9.345  1.390   1.00 13.09  ? 225 LYS A O   1 
ATOM   1900 C  CB  . LYS A 1 224 ? 8.953   -10.505 0.846   1.00 15.92  ? 225 LYS A CB  1 
ATOM   1901 C  CG  . LYS A 1 224 ? 8.369   -11.533 -0.170  1.00 19.77  ? 225 LYS A CG  1 
ATOM   1902 C  CD  . LYS A 1 224 ? 7.074   -11.212 -0.935  1.00 23.80  ? 225 LYS A CD  1 
ATOM   1903 C  CE  . LYS A 1 224 ? 6.423   -12.363 -1.795  1.00 26.46  ? 225 LYS A CE  1 
ATOM   1904 N  NZ  . LYS A 1 224 ? 5.058   -12.060 -2.466  1.00 29.79  ? 225 LYS A NZ  1 
ATOM   1905 N  N   . PHE A 1 225 ? 11.039  -9.726  3.379   1.00 11.70  ? 226 PHE A N   1 
ATOM   1906 C  CA  . PHE A 1 225 ? 11.937  -8.811  4.050   1.00 11.38  ? 226 PHE A CA  1 
ATOM   1907 C  C   . PHE A 1 225 ? 13.392  -9.311  3.842   1.00 11.25  ? 226 PHE A C   1 
ATOM   1908 O  O   . PHE A 1 225 ? 14.312  -8.524  3.646   1.00 11.82  ? 226 PHE A O   1 
ATOM   1909 C  CB  . PHE A 1 225 ? 11.772  -8.806  5.576   1.00 11.98  ? 226 PHE A CB  1 
ATOM   1910 C  CG  . PHE A 1 225 ? 10.583  -8.058  6.116   1.00 11.18  ? 226 PHE A CG  1 
ATOM   1911 C  CD1 . PHE A 1 225 ? 9.536   -7.626  5.319   1.00 15.04  ? 226 PHE A CD1 1 
ATOM   1912 C  CD2 . PHE A 1 225 ? 10.519  -7.829  7.481   1.00 16.05  ? 226 PHE A CD2 1 
ATOM   1913 C  CE1 . PHE A 1 225 ? 8.458   -6.959  5.886   1.00 15.29  ? 226 PHE A CE1 1 
ATOM   1914 C  CE2 . PHE A 1 225 ? 9.453   -7.170  8.051   1.00 15.64  ? 226 PHE A CE2 1 
ATOM   1915 C  CZ  . PHE A 1 225 ? 8.419   -6.732  7.253   1.00 14.67  ? 226 PHE A CZ  1 
ATOM   1916 N  N   . ARG A 1 226 ? 13.572  -10.643 3.889   1.00 11.16  ? 227 ARG A N   1 
ATOM   1917 C  CA  . ARG A 1 226 ? 14.901  -11.228 3.821   1.00 12.17  ? 227 ARG A CA  1 
ATOM   1918 C  C   . ARG A 1 226 ? 15.506  -11.256 2.422   1.00 12.97  ? 227 ARG A C   1 
ATOM   1919 O  O   . ARG A 1 226 ? 16.658  -11.633 2.281   1.00 14.14  ? 227 ARG A O   1 
ATOM   1920 C  CB  . ARG A 1 226 ? 14.861  -12.677 4.354   1.00 12.43  ? 227 ARG A CB  1 
ATOM   1921 C  CG  . ARG A 1 226 ? 14.441  -12.791 5.810   1.00 11.80  ? 227 ARG A CG  1 
ATOM   1922 C  CD  . ARG A 1 226 ? 14.535  -14.219 6.232   1.00 13.63  ? 227 ARG A CD  1 
ATOM   1923 N  NE  . ARG A 1 226 ? 13.964  -14.404 7.593   1.00 12.44  ? 227 ARG A NE  1 
ATOM   1924 C  CZ  . ARG A 1 226 ? 13.031  -15.252 7.948   1.00 11.92  ? 227 ARG A CZ  1 
ATOM   1925 N  NH1 . ARG A 1 226 ? 12.568  -16.153 7.084   1.00 17.52  ? 227 ARG A NH1 1 
ATOM   1926 N  NH2 . ARG A 1 226 ? 12.540  -15.243 9.141   1.00 13.10  ? 227 ARG A NH2 1 
ATOM   1927 N  N   . LYS A 1 227 ? 14.765  -10.790 1.431   1.00 12.02  ? 228 LYS A N   1 
ATOM   1928 C  CA  . LYS A 1 227 ? 15.277  -10.649 0.077   1.00 13.08  ? 228 LYS A CA  1 
ATOM   1929 C  C   . LYS A 1 227 ? 15.901  -9.270  -0.156  1.00 12.33  ? 228 LYS A C   1 
ATOM   1930 O  O   . LYS A 1 227 ? 16.597  -9.066  -1.150  1.00 14.02  ? 228 LYS A O   1 
ATOM   1931 C  CB  . LYS A 1 227 ? 14.167  -10.910 -0.942  1.00 15.32  ? 228 LYS A CB  1 
ATOM   1932 C  CG  . LYS A 1 227 ? 13.671  -12.347 -0.957  1.00 18.02  ? 228 LYS A CG  1 
ATOM   1933 C  CD  . LYS A 1 227 ? 12.577  -12.541 -1.993  1.00 23.04  ? 228 LYS A CD  1 
ATOM   1934 C  CE  . LYS A 1 227 ? 13.077  -12.211 -3.389  1.00 32.35  ? 228 LYS A CE  1 
ATOM   1935 N  NZ  . LYS A 1 227 ? 12.392  -13.032 -4.426  1.00 98.00  ? 228 LYS A NZ  1 
ATOM   1936 N  N   . LEU A 1 228 ? 15.657  -8.327  0.754   1.00 11.61  ? 229 LEU A N   1 
ATOM   1937 C  CA  . LEU A 1 228 ? 16.268  -7.047  0.646   1.00 11.55  ? 229 LEU A CA  1 
ATOM   1938 C  C   . LEU A 1 228 ? 17.746  -7.174  0.788   1.00 11.61  ? 229 LEU A C   1 
ATOM   1939 O  O   . LEU A 1 228 ? 18.316  -8.232  1.207   1.00 12.04  ? 229 LEU A O   1 
ATOM   1940 C  CB  . LEU A 1 228 ? 15.718  -6.080  1.740   1.00 11.79  ? 229 LEU A CB  1 
ATOM   1941 C  CG  . LEU A 1 228 ? 14.285  -5.639  1.542   1.00 12.43  ? 229 LEU A CG  1 
ATOM   1942 C  CD1 . LEU A 1 228 ? 13.859  -5.001  2.834   1.00 13.28  ? 229 LEU A CD1 1 
ATOM   1943 C  CD2 . LEU A 1 228 ? 14.260  -4.637  0.392   1.00 14.92  ? 229 LEU A CD2 1 
ATOM   1944 N  N   . ASN A 1 229 ? 18.496  -6.135  0.421   1.00 12.11  ? 230 ASN A N   1 
ATOM   1945 C  CA  . ASN A 1 229 ? 19.942  -6.158  0.454   1.00 11.80  ? 230 ASN A CA  1 
ATOM   1946 C  C   . ASN A 1 229 ? 20.496  -4.935  1.280   1.00 11.74  ? 230 ASN A C   1 
ATOM   1947 O  O   . ASN A 1 229 ? 19.997  -3.846  1.204   1.00 12.27  ? 230 ASN A O   1 
ATOM   1948 C  CB  . ASN A 1 229 ? 20.517  -5.935  -0.960  1.00 12.99  ? 230 ASN A CB  1 
ATOM   1949 C  CG  . ASN A 1 229 ? 20.476  -7.126  -1.918  1.00 13.95  ? 230 ASN A CG  1 
ATOM   1950 O  OD1 . ASN A 1 229 ? 20.975  -7.025  -3.043  1.00 16.51  ? 230 ASN A OD1 1 
ATOM   1951 N  ND2 . ASN A 1 229 ? 19.819  -8.247  -1.553  1.00 14.17  ? 230 ASN A ND2 1 
ATOM   1952 N  N   . PHE A 1 230 ? 21.550  -5.297  2.027   1.00 11.92  ? 231 PHE A N   1 
ATOM   1953 C  CA  . PHE A 1 230 ? 22.301  -4.208  2.708   1.00 11.97  ? 231 PHE A CA  1 
ATOM   1954 C  C   . PHE A 1 230 ? 23.144  -3.430  1.718   1.00 13.33  ? 231 PHE A C   1 
ATOM   1955 O  O   . PHE A 1 230 ? 23.440  -2.256  1.954   1.00 13.92  ? 231 PHE A O   1 
ATOM   1956 C  CB  . PHE A 1 230 ? 23.294  -4.801  3.723   1.00 13.13  ? 231 PHE A CB  1 
ATOM   1957 C  CG  . PHE A 1 230 ? 22.691  -5.369  4.994   1.00 11.57  ? 231 PHE A CG  1 
ATOM   1958 C  CD1 . PHE A 1 230 ? 21.929  -4.597  5.885   1.00 11.67  ? 231 PHE A CD1 1 
ATOM   1959 C  CD2 . PHE A 1 230 ? 23.016  -6.651  5.383   1.00 12.34  ? 231 PHE A CD2 1 
ATOM   1960 C  CE1 . PHE A 1 230 ? 21.494  -5.106  7.092   1.00 11.88  ? 231 PHE A CE1 1 
ATOM   1961 C  CE2 . PHE A 1 230 ? 22.546  -7.155  6.608   1.00 12.29  ? 231 PHE A CE2 1 
ATOM   1962 C  CZ  . PHE A 1 230 ? 21.845  -6.390  7.455   1.00 10.91  ? 231 PHE A CZ  1 
ATOM   1963 N  N   . ASN A 1 231 ? 23.665  -4.107  0.687   1.00 13.18  ? 232 ASN A N   1 
ATOM   1964 C  CA  . ASN A 1 231 ? 24.513  -3.496  -0.347  1.00 14.35  ? 232 ASN A CA  1 
ATOM   1965 C  C   . ASN A 1 231 ? 23.702  -2.652  -1.252  1.00 12.66  ? 232 ASN A C   1 
ATOM   1966 O  O   . ASN A 1 231 ? 22.498  -2.640  -1.415  1.00 15.02  ? 232 ASN A O   1 
ATOM   1967 C  CB  . ASN A 1 231 ? 25.174  -4.610  -1.160  1.00 15.97  ? 232 ASN A CB  1 
ATOM   1968 C  CG  . ASN A 1 231 ? 24.140  -5.506  -1.727  1.00 14.94  ? 232 ASN A CG  1 
ATOM   1969 O  OD1 . ASN A 1 231 ? 23.627  -6.351  -1.034  1.00 15.68  ? 232 ASN A OD1 1 
ATOM   1970 N  ND2 . ASN A 1 231 ? 23.773  -5.334  -3.039  1.00 16.63  ? 232 ASN A ND2 1 
ATOM   1971 N  N   . GLY A 1 232 ? 24.519  -1.726  -1.933  1.00 16.08  ? 233 GLY A N   1 
ATOM   1972 C  CA  . GLY A 1 232 ? 23.998  -0.918  -3.035  1.00 15.23  ? 233 GLY A CA  1 
ATOM   1973 C  C   . GLY A 1 232 ? 23.913  -1.703  -4.344  1.00 14.55  ? 233 GLY A C   1 
ATOM   1974 O  O   . GLY A 1 232 ? 24.493  -2.764  -4.446  1.00 16.33  ? 233 GLY A O   1 
ATOM   1975 N  N   . GLU A 1 233 ? 23.181  -1.142  -5.311  1.00 14.88  ? 234 GLU A N   1 
ATOM   1976 C  CA  . GLU A 1 233 ? 23.087  -1.716  -6.613  1.00 15.36  ? 234 GLU A CA  1 
ATOM   1977 C  C   . GLU A 1 233 ? 24.519  -1.828  -7.184  1.00 15.51  ? 234 GLU A C   1 
ATOM   1978 O  O   . GLU A 1 233 ? 25.331  -0.932  -7.031  1.00 18.29  ? 234 GLU A O   1 
ATOM   1979 C  CB  . GLU A 1 233 ? 22.232  -0.861  -7.490  1.00 15.54  ? 234 GLU A CB  1 
ATOM   1980 C  CG  . GLU A 1 233 ? 21.916  -1.433  -8.880  1.00 19.24  ? 234 GLU A CG  1 
ATOM   1981 C  CD  . GLU A 1 233 ? 21.101  -0.497  -9.730  1.00 24.57  ? 234 GLU A CD  1 
ATOM   1982 O  OE1 . GLU A 1 233 ? 20.826  0.636   -9.287  1.00 26.17  ? 234 GLU A OE1 1 
ATOM   1983 O  OE2 . GLU A 1 233 ? 20.737  -0.905  -10.848 1.00 26.21  ? 234 GLU A OE2 1 
ATOM   1984 N  N   . GLY A 1 234 ? 24.767  -2.938  -7.855  1.00 19.04  ? 235 GLY A N   1 
ATOM   1985 C  CA  . GLY A 1 234 ? 26.058  -3.126  -8.513  1.00 21.36  ? 235 GLY A CA  1 
ATOM   1986 C  C   . GLY A 1 234 ? 27.174  -3.526  -7.576  1.00 22.72  ? 235 GLY A C   1 
ATOM   1987 O  O   . GLY A 1 234 ? 28.389  -3.602  -7.974  1.00 29.09  ? 235 GLY A O   1 
ATOM   1988 N  N   . GLU A 1 235 ? 26.749  -3.935  -6.378  1.00 19.88  ? 236 GLU A N   1 
ATOM   1989 C  CA  . GLU A 1 235 ? 27.679  -4.566  -5.454  1.00 17.39  ? 236 GLU A CA  1 
ATOM   1990 C  C   . GLU A 1 235 ? 27.205  -5.967  -5.117  1.00 18.52  ? 236 GLU A C   1 
ATOM   1991 O  O   . GLU A 1 235 ? 26.037  -6.376  -5.341  1.00 20.29  ? 236 GLU A O   1 
ATOM   1992 C  CB  . GLU A 1 235 ? 27.686  -3.795  -4.127  1.00 19.58  ? 236 GLU A CB  1 
ATOM   1993 C  CG  . GLU A 1 235 ? 28.007  -2.319  -4.280  1.00 21.01  ? 236 GLU A CG  1 
ATOM   1994 C  CD  . GLU A 1 235 ? 28.003  -1.524  -2.968  1.00 30.05  ? 236 GLU A CD  1 
ATOM   1995 O  OE1 . GLU A 1 235 ? 27.344  -1.955  -1.993  1.00 24.05  ? 236 GLU A OE1 1 
ATOM   1996 O  OE2 . GLU A 1 235 ? 28.686  -0.466  -2.955  1.00 45.32  ? 236 GLU A OE2 1 
ATOM   1997 N  N   . PRO A 1 236 ? 28.118  -6.813  -4.647  1.00 18.83  ? 237 PRO A N   1 
ATOM   1998 C  CA  . PRO A 1 236 ? 27.759  -8.220  -4.430  1.00 20.38  ? 237 PRO A CA  1 
ATOM   1999 C  C   . PRO A 1 236 ? 26.660  -8.313  -3.359  1.00 15.25  ? 237 PRO A C   1 
ATOM   2000 O  O   . PRO A 1 236 ? 26.663  -7.488  -2.372  1.00 17.43  ? 237 PRO A O   1 
ATOM   2001 C  CB  . PRO A 1 236 ? 29.037  -8.776  -3.848  1.00 22.29  ? 237 PRO A CB  1 
ATOM   2002 C  CG  . PRO A 1 236 ? 30.154  -8.018  -4.616  1.00 24.37  ? 237 PRO A CG  1 
ATOM   2003 C  CD  . PRO A 1 236 ? 29.590  -6.624  -4.538  1.00 22.36  ? 237 PRO A CD  1 
ATOM   2004 N  N   . GLU A 1 237 ? 25.800  -9.305  -3.434  1.00 17.57  ? 238 GLU A N   1 
ATOM   2005 C  CA  . GLU A 1 237 ? 24.617  -9.314  -2.655  1.00 16.42  ? 238 GLU A CA  1 
ATOM   2006 C  C   . GLU A 1 237 ? 24.962  -9.653  -1.202  1.00 13.80  ? 238 GLU A C   1 
ATOM   2007 O  O   . GLU A 1 237 ? 25.597  -10.667 -0.914  1.00 15.67  ? 238 GLU A O   1 
ATOM   2008 C  CB  . GLU A 1 237 ? 23.629  -10.363 -3.131  1.00 18.32  ? 238 GLU A CB  1 
ATOM   2009 C  CG  . GLU A 1 237 ? 22.328  -10.330 -2.418  1.00 21.02  ? 238 GLU A CG  1 
ATOM   2010 C  CD  . GLU A 1 237 ? 21.295  -11.048 -3.137  1.00 21.08  ? 238 GLU A CD  1 
ATOM   2011 O  OE1 . GLU A 1 237 ? 21.589  -12.232 -3.576  1.00 28.69  ? 238 GLU A OE1 1 
ATOM   2012 O  OE2 . GLU A 1 237 ? 20.167  -10.524 -3.269  1.00 18.80  ? 238 GLU A OE2 1 
ATOM   2013 N  N   . GLU A 1 238 ? 24.447  -8.882  -0.256  1.00 13.62  ? 239 GLU A N   1 
ATOM   2014 C  CA  . GLU A 1 238 ? 24.499  -9.143  1.159   1.00 13.48  ? 239 GLU A CA  1 
ATOM   2015 C  C   . GLU A 1 238 ? 23.077  -9.002  1.660   1.00 11.99  ? 239 GLU A C   1 
ATOM   2016 O  O   . GLU A 1 238 ? 22.570  -7.930  1.762   1.00 14.53  ? 239 GLU A O   1 
ATOM   2017 C  CB  . GLU A 1 238 ? 25.384  -8.154  1.831   1.00 18.43  ? 239 GLU A CB  1 
ATOM   2018 C  CG  . GLU A 1 238 ? 25.769  -8.542  3.275   1.00 24.46  ? 239 GLU A CG  1 
ATOM   2019 C  CD  . GLU A 1 238 ? 26.633  -9.772  3.458   1.00 23.73  ? 239 GLU A CD  1 
ATOM   2020 O  OE1 . GLU A 1 238 ? 27.851  -9.680  3.078   1.00 41.56  ? 239 GLU A OE1 1 
ATOM   2021 O  OE2 . GLU A 1 238 ? 26.053  -10.814 3.964   1.00 25.35  ? 239 GLU A OE2 1 
ATOM   2022 N  N   . LEU A 1 239 ? 22.459  -10.200 1.913   1.00 13.30  ? 240 LEU A N   1 
ATOM   2023 C  CA  . LEU A 1 239 ? 21.069  -10.129 2.283   1.00 11.66  ? 240 LEU A CA  1 
ATOM   2024 C  C   . LEU A 1 239 ? 20.832  -9.297  3.530   1.00 10.74  ? 240 LEU A C   1 
ATOM   2025 O  O   . LEU A 1 239 ? 21.620  -9.472  4.497   1.00 12.22  ? 240 LEU A O   1 
ATOM   2026 C  CB  . LEU A 1 239 ? 20.484  -11.546 2.490   1.00 13.12  ? 240 LEU A CB  1 
ATOM   2027 C  CG  . LEU A 1 239 ? 20.445  -12.426 1.236   1.00 13.51  ? 240 LEU A CG  1 
ATOM   2028 C  CD1 . LEU A 1 239 ? 19.825  -13.783 1.725   1.00 17.38  ? 240 LEU A CD1 1 
ATOM   2029 C  CD2 . LEU A 1 239 ? 19.660  -11.806 0.155   1.00 14.67  ? 240 LEU A CD2 1 
ATOM   2030 N  N   . MET A 1 240 ? 19.803  -8.493  3.529   1.00 11.20  ? 241 MET A N   1 
ATOM   2031 C  CA  . MET A 1 240 ? 19.443  -7.678  4.713   1.00 11.08  ? 241 MET A CA  1 
ATOM   2032 C  C   . MET A 1 240 ? 18.651  -8.620  5.645   1.00 10.14  ? 241 MET A C   1 
ATOM   2033 O  O   . MET A 1 240 ? 17.492  -8.794  5.543   1.00 11.01  ? 241 MET A O   1 
ATOM   2034 C  CB  . MET A 1 240 ? 18.604  -6.534  4.264   1.00 11.42  ? 241 MET A CB  1 
ATOM   2035 C  CG  . MET A 1 240 ? 18.246  -5.568  5.436   1.00 11.45  ? 241 MET A CG  1 
ATOM   2036 S  SD  . MET A 1 240 ? 17.278  -4.158  4.918   1.00 11.80  ? 241 MET A SD  1 
ATOM   2037 C  CE  . MET A 1 240 ? 18.553  -3.095  4.272   1.00 12.41  ? 241 MET A CE  1 
ATOM   2038 N  N   . VAL A 1 241 ? 19.429  -9.226  6.557   1.00 10.34  ? 242 VAL A N   1 
ATOM   2039 C  CA  . VAL A 1 241 ? 18.924  -10.141 7.622   1.00 10.23  ? 242 VAL A CA  1 
ATOM   2040 C  C   . VAL A 1 241 ? 19.741  -9.892  8.874   1.00 9.47   ? 242 VAL A C   1 
ATOM   2041 O  O   . VAL A 1 241 ? 20.863  -9.465  8.821   1.00 10.16  ? 242 VAL A O   1 
ATOM   2042 C  CB  . VAL A 1 241 ? 19.028  -11.656 7.228   1.00 10.83  ? 242 VAL A CB  1 
ATOM   2043 C  CG1 . VAL A 1 241 ? 18.102  -11.950 6.063   1.00 12.76  ? 242 VAL A CG1 1 
ATOM   2044 C  CG2 . VAL A 1 241 ? 20.466  -12.076 6.984   1.00 12.61  ? 242 VAL A CG2 1 
ATOM   2045 N  N   . ASP A 1 242 ? 19.112  -10.212 10.023  1.00 9.09   ? 243 ASP A N   1 
ATOM   2046 C  CA  . ASP A 1 242 ? 19.804  -10.066 11.308  1.00 8.83   ? 243 ASP A CA  1 
ATOM   2047 C  C   . ASP A 1 242 ? 20.267  -8.648  11.552  1.00 8.64   ? 243 ASP A C   1 
ATOM   2048 O  O   . ASP A 1 242 ? 21.376  -8.403  12.042  1.00 10.09  ? 243 ASP A O   1 
ATOM   2049 C  CB  . ASP A 1 242 ? 20.891  -11.112 11.523  1.00 9.48   ? 243 ASP A CB  1 
ATOM   2050 C  CG  . ASP A 1 242 ? 20.343  -12.517 11.636  1.00 9.57   ? 243 ASP A CG  1 
ATOM   2051 O  OD1 . ASP A 1 242 ? 19.282  -12.691 12.287  1.00 9.77   ? 243 ASP A OD1 1 
ATOM   2052 O  OD2 . ASP A 1 242 ? 20.940  -13.439 11.050  1.00 11.84  ? 243 ASP A OD2 1 
ATOM   2053 N  N   . ASN A 1 243 ? 19.354  -7.712  11.267  1.00 8.34   ? 244 ASN A N   1 
ATOM   2054 C  CA  . ASN A 1 243 ? 19.615  -6.281  11.520  1.00 8.24   ? 244 ASN A CA  1 
ATOM   2055 C  C   . ASN A 1 243 ? 19.082  -5.851  12.859  1.00 7.80   ? 244 ASN A C   1 
ATOM   2056 O  O   . ASN A 1 243 ? 18.402  -4.825  12.968  1.00 9.14   ? 244 ASN A O   1 
ATOM   2057 C  CB  . ASN A 1 243 ? 19.082  -5.430  10.346  1.00 8.70   ? 244 ASN A CB  1 
ATOM   2058 C  CG  . ASN A 1 243 ? 17.625  -5.602  10.084  1.00 8.85   ? 244 ASN A CG  1 
ATOM   2059 O  OD1 . ASN A 1 243 ? 16.963  -6.469  10.672  1.00 9.42   ? 244 ASN A OD1 1 
ATOM   2060 N  ND2 . ASN A 1 243 ? 17.105  -4.802  9.208   1.00 14.56  ? 244 ASN A ND2 1 
ATOM   2061 N  N   . TRP A 1 244 ? 19.397  -6.616  13.901  1.00 7.73   ? 245 TRP A N   1 
ATOM   2062 C  CA  . TRP A 1 244 ? 18.973  -6.366  15.275  1.00 7.51   ? 245 TRP A CA  1 
ATOM   2063 C  C   . TRP A 1 244 ? 20.172  -6.261  16.185  1.00 7.54   ? 245 TRP A C   1 
ATOM   2064 O  O   . TRP A 1 244 ? 21.172  -6.971  16.037  1.00 8.92   ? 245 TRP A O   1 
ATOM   2065 C  CB  . TRP A 1 244 ? 17.985  -7.466  15.768  1.00 7.97   ? 245 TRP A CB  1 
ATOM   2066 C  CG  . TRP A 1 244 ? 18.472  -8.871  15.583  1.00 7.68   ? 245 TRP A CG  1 
ATOM   2067 C  CD1 . TRP A 1 244 ? 18.370  -9.611  14.442  1.00 8.27   ? 245 TRP A CD1 1 
ATOM   2068 C  CD2 . TRP A 1 244 ? 19.043  -9.729  16.565  1.00 7.96   ? 245 TRP A CD2 1 
ATOM   2069 N  NE1 . TRP A 1 244 ? 18.863  -10.866 14.621  1.00 8.43   ? 245 TRP A NE1 1 
ATOM   2070 C  CE2 . TRP A 1 244 ? 19.297  -10.981 15.919  1.00 8.29   ? 245 TRP A CE2 1 
ATOM   2071 C  CE3 . TRP A 1 244 ? 19.313  -9.600  17.926  1.00 8.75   ? 245 TRP A CE3 1 
ATOM   2072 C  CZ2 . TRP A 1 244 ? 19.846  -12.060 16.612  1.00 9.68   ? 245 TRP A CZ2 1 
ATOM   2073 C  CZ3 . TRP A 1 244 ? 19.853  -10.668 18.596  1.00 10.28  ? 245 TRP A CZ3 1 
ATOM   2074 C  CH2 . TRP A 1 244 ? 20.105  -11.896 17.925  1.00 10.41  ? 245 TRP A CH2 1 
ATOM   2075 N  N   . ARG A 1 245 ? 20.034  -5.395  17.177  1.00 7.84   ? 246 ARG A N   1 
ATOM   2076 C  CA  . ARG A 1 245 ? 20.943  -5.292  18.291  1.00 7.91   ? 246 ARG A CA  1 
ATOM   2077 C  C   . ARG A 1 245 ? 20.480  -6.215  19.398  1.00 7.73   ? 246 ARG A C   1 
ATOM   2078 O  O   . ARG A 1 245 ? 19.304  -6.203  19.735  1.00 8.49   ? 246 ARG A O   1 
ATOM   2079 C  CB  . ARG A 1 245 ? 21.014  -3.856  18.791  1.00 7.91   ? 246 ARG A CB  1 
ATOM   2080 C  CG  . ARG A 1 245 ? 22.119  -3.618  19.814  1.00 8.59   ? 246 ARG A CG  1 
ATOM   2081 C  CD  . ARG A 1 245 ? 22.060  -2.252  20.440  1.00 8.30   ? 246 ARG A CD  1 
ATOM   2082 N  NE  . ARG A 1 245 ? 23.276  -1.956  21.166  1.00 8.63   ? 246 ARG A NE  1 
ATOM   2083 C  CZ  . ARG A 1 245 ? 23.474  -0.922  21.972  1.00 8.19   ? 246 ARG A CZ  1 
ATOM   2084 N  NH1 . ARG A 1 245 ? 22.485  -0.162  22.358  1.00 8.82   ? 246 ARG A NH1 1 
ATOM   2085 N  NH2 . ARG A 1 245 ? 24.737  -0.690  22.415  1.00 10.36  ? 246 ARG A NH2 1 
ATOM   2086 N  N   . PRO A 1 246 ? 21.363  -6.987  20.016  1.00 8.41   ? 247 PRO A N   1 
ATOM   2087 C  CA  . PRO A 1 246 ? 20.945  -7.844  21.134  1.00 8.91   ? 247 PRO A CA  1 
ATOM   2088 C  C   . PRO A 1 246 ? 20.600  -7.012  22.394  1.00 8.43   ? 247 PRO A C   1 
ATOM   2089 O  O   . PRO A 1 246 ? 20.981  -5.828  22.518  1.00 8.81   ? 247 PRO A O   1 
ATOM   2090 C  CB  . PRO A 1 246 ? 22.162  -8.688  21.434  1.00 11.75  ? 247 PRO A CB  1 
ATOM   2091 C  CG  . PRO A 1 246 ? 22.990  -8.638  20.162  1.00 15.10  ? 247 PRO A CG  1 
ATOM   2092 C  CD  . PRO A 1 246 ? 22.799  -7.227  19.679  1.00 10.74  ? 247 PRO A CD  1 
ATOM   2093 N  N   . ALA A 1 247 ? 19.963  -7.667  23.349  1.00 9.14   ? 248 ALA A N   1 
ATOM   2094 C  CA  . ALA A 1 247 ? 19.613  -7.060  24.610  1.00 8.52   ? 248 ALA A CA  1 
ATOM   2095 C  C   . ALA A 1 247 ? 20.861  -6.552  25.350  1.00 8.72   ? 248 ALA A C   1 
ATOM   2096 O  O   . ALA A 1 247 ? 21.909  -7.204  25.375  1.00 10.32  ? 248 ALA A O   1 
ATOM   2097 C  CB  . ALA A 1 247 ? 18.888  -8.066  25.453  1.00 11.39  ? 248 ALA A CB  1 
ATOM   2098 N  N   . GLN A 1 248 ? 20.726  -5.365  25.928  1.00 8.73   ? 249 GLN A N   1 
ATOM   2099 C  CA  . GLN A 1 248 ? 21.746  -4.647  26.672  1.00 9.37   ? 249 GLN A CA  1 
ATOM   2100 C  C   . GLN A 1 248 ? 21.448  -4.661  28.130  1.00 9.53   ? 249 GLN A C   1 
ATOM   2101 O  O   . GLN A 1 248 ? 20.327  -4.875  28.560  1.00 10.83  ? 249 GLN A O   1 
ATOM   2102 C  CB  . GLN A 1 248 ? 21.829  -3.212  26.140  1.00 10.18  ? 249 GLN A CB  1 
ATOM   2103 C  CG  . GLN A 1 248 ? 22.135  -3.138  24.646  1.00 10.57  ? 249 GLN A CG  1 
ATOM   2104 C  CD  . GLN A 1 248 ? 23.431  -3.820  24.298  1.00 11.21  ? 249 GLN A CD  1 
ATOM   2105 O  OE1 . GLN A 1 248 ? 24.481  -3.515  24.905  1.00 13.64  ? 249 GLN A OE1 1 
ATOM   2106 N  NE2 . GLN A 1 248 ? 23.442  -4.729  23.335  1.00 12.16  ? 249 GLN A NE2 1 
ATOM   2107 N  N   . PRO A 1 249 ? 22.433  -4.365  28.979  1.00 11.28  ? 250 PRO A N   1 
ATOM   2108 C  CA  . PRO A 1 249 ? 22.238  -4.424  30.425  1.00 12.61  ? 250 PRO A CA  1 
ATOM   2109 C  C   . PRO A 1 249 ? 21.167  -3.411  30.866  1.00 10.41  ? 250 PRO A C   1 
ATOM   2110 O  O   . PRO A 1 249 ? 21.173  -2.244  30.511  1.00 11.22  ? 250 PRO A O   1 
ATOM   2111 C  CB  . PRO A 1 249 ? 23.648  -4.027  30.960  1.00 16.65  ? 250 PRO A CB  1 
ATOM   2112 C  CG  . PRO A 1 249 ? 24.616  -4.445  29.897  1.00 17.00  ? 250 PRO A CG  1 
ATOM   2113 C  CD  . PRO A 1 249 ? 23.850  -4.118  28.630  1.00 13.83  ? 250 PRO A CD  1 
ATOM   2114 N  N   . LEU A 1 250 ? 20.292  -3.894  31.733  1.00 11.68  ? 251 LEU A N   1 
ATOM   2115 C  CA  . LEU A 1 250 ? 19.233  -3.051  32.242  1.00 10.87  ? 251 LEU A CA  1 
ATOM   2116 C  C   . LEU A 1 250 ? 19.759  -1.964  33.168  1.00 11.05  ? 251 LEU A C   1 
ATOM   2117 O  O   . LEU A 1 250 ? 19.172  -0.872  33.267  1.00 11.23  ? 251 LEU A O   1 
ATOM   2118 C  CB  . LEU A 1 250 ? 18.192  -3.898  32.960  1.00 13.17  ? 251 LEU A CB  1 
ATOM   2119 C  CG  . LEU A 1 250 ? 16.903  -3.209  33.362  1.00 13.51  ? 251 LEU A CG  1 
ATOM   2120 C  CD1 . LEU A 1 250 ? 16.099  -2.643  32.170  1.00 13.93  ? 251 LEU A CD1 1 
ATOM   2121 C  CD2 . LEU A 1 250 ? 16.080  -4.227  34.163  1.00 17.72  ? 251 LEU A CD2 1 
ATOM   2122 N  N   A LYS A 1 251 ? 20.652  -2.371  34.041  0.50 11.89  ? 252 LYS A N   1 
ATOM   2123 N  N   B LYS A 1 251 ? 20.955  -2.135  33.771  0.50 10.66  ? 252 LYS A N   1 
ATOM   2124 C  CA  A LYS A 1 251 ? 21.366  -1.351  34.900  0.50 13.98  ? 252 LYS A CA  1 
ATOM   2125 C  CA  B LYS A 1 251 ? 21.529  -1.141  34.723  0.50 10.59  ? 252 LYS A CA  1 
ATOM   2126 C  C   A LYS A 1 251 ? 20.416  -0.520  35.788  0.50 12.63  ? 252 LYS A C   1 
ATOM   2127 C  C   B LYS A 1 251 ? 20.440  -0.762  35.757  0.50 14.23  ? 252 LYS A C   1 
ATOM   2128 O  O   A LYS A 1 251 ? 20.484  0.720   35.949  0.50 14.43  ? 252 LYS A O   1 
ATOM   2129 O  O   B LYS A 1 251 ? 19.756  -1.654  36.285  0.50 16.78  ? 252 LYS A O   1 
ATOM   2130 C  CB  A LYS A 1 251 ? 22.244  -0.441  34.092  0.50 13.25  ? 252 LYS A CB  1 
ATOM   2131 C  CB  B LYS A 1 251 ? 22.238  0.014   33.985  0.50 13.67  ? 252 LYS A CB  1 
ATOM   2132 C  CG  A LYS A 1 251 ? 23.318  -1.200  33.404  0.50 16.80  ? 252 LYS A CG  1 
ATOM   2133 C  CG  B LYS A 1 251 ? 23.332  -0.637  33.191  0.50 13.61  ? 252 LYS A CG  1 
ATOM   2134 C  CD  A LYS A 1 251 ? 24.227  -0.228  32.710  0.50 15.88  ? 252 LYS A CD  1 
ATOM   2135 C  CD  B LYS A 1 251 ? 24.407  0.295   32.660  0.50 15.88  ? 252 LYS A CD  1 
ATOM   2136 C  CE  A LYS A 1 251 ? 25.591  -0.831  32.589  0.50 22.17  ? 252 LYS A CE  1 
ATOM   2137 C  CE  B LYS A 1 251 ? 25.410  -0.545  31.929  0.50 18.66  ? 252 LYS A CE  1 
ATOM   2138 N  NZ  A LYS A 1 251 ? 26.446  0.227   31.985  0.50 24.09  ? 252 LYS A NZ  1 
ATOM   2139 N  NZ  B LYS A 1 251 ? 26.367  0.300   31.207  0.50 19.16  ? 252 LYS A NZ  1 
ATOM   2140 N  N   A ASN A 1 252 ? 19.532  -1.341  36.353  0.50 12.45  ? 253 ASN A N   1 
ATOM   2141 N  N   B ASN A 1 252 ? 20.296  0.526   36.015  0.50 12.59  ? 253 ASN A N   1 
ATOM   2142 C  CA  A ASN A 1 252 ? 18.654  -1.054  37.466  0.50 14.59  ? 253 ASN A CA  1 
ATOM   2143 C  CA  B ASN A 1 252 ? 19.561  1.097   37.067  0.50 14.81  ? 253 ASN A CA  1 
ATOM   2144 C  C   A ASN A 1 252 ? 17.509  -0.181  37.072  0.50 13.41  ? 253 ASN A C   1 
ATOM   2145 C  C   B ASN A 1 252 ? 18.279  1.665   36.490  0.50 12.56  ? 253 ASN A C   1 
ATOM   2146 O  O   A ASN A 1 252 ? 16.692  0.219   37.929  0.50 14.58  ? 253 ASN A O   1 
ATOM   2147 O  O   B ASN A 1 252 ? 18.124  2.922   36.393  0.50 14.01  ? 253 ASN A O   1 
ATOM   2148 C  CB  A ASN A 1 252 ? 19.397  -0.436  38.628  0.50 16.47  ? 253 ASN A CB  1 
ATOM   2149 C  CB  B ASN A 1 252 ? 20.298  2.249   37.701  0.50 16.74  ? 253 ASN A CB  1 
ATOM   2150 C  CG  A ASN A 1 252 ? 20.141  -1.428  39.457  0.50 17.94  ? 253 ASN A CG  1 
ATOM   2151 C  CG  B ASN A 1 252 ? 19.580  2.752   38.900  0.50 19.10  ? 253 ASN A CG  1 
ATOM   2152 O  OD1 A ASN A 1 252 ? 19.569  -2.405  39.936  0.50 28.00  ? 253 ASN A OD1 1 
ATOM   2153 O  OD1 B ASN A 1 252 ? 18.955  1.941   39.628  0.50 26.15  ? 253 ASN A OD1 1 
ATOM   2154 N  ND2 A ASN A 1 252 ? 21.387  -1.206  39.577  0.50 23.37  ? 253 ASN A ND2 1 
ATOM   2155 N  ND2 B ASN A 1 252 ? 19.602  4.053   39.105  0.50 19.04  ? 253 ASN A ND2 1 
ATOM   2156 N  N   A ARG A 1 253 ? 17.342  0.014   35.777  0.50 9.34   ? 254 ARG A N   1 
ATOM   2157 N  N   B ARG A 1 253 ? 17.460  0.755   35.949  0.50 9.90   ? 254 ARG A N   1 
ATOM   2158 C  CA  A ARG A 1 253 ? 16.097  0.573   35.327  0.50 9.58   ? 254 ARG A CA  1 
ATOM   2159 C  CA  B ARG A 1 253 ? 16.230  1.062   35.337  0.50 11.00  ? 254 ARG A CA  1 
ATOM   2160 C  C   A ARG A 1 253 ? 14.930  -0.344  35.698  0.50 10.99  ? 254 ARG A C   1 
ATOM   2161 C  C   B ARG A 1 253 ? 15.203  0.021   35.805  0.50 11.35  ? 254 ARG A C   1 
ATOM   2162 O  O   A ARG A 1 253 ? 15.044  -1.514  35.625  0.50 14.04  ? 254 ARG A O   1 
ATOM   2163 O  O   B ARG A 1 253 ? 15.545  -1.120  36.206  0.50 13.43  ? 254 ARG A O   1 
ATOM   2164 C  CB  A ARG A 1 253 ? 16.096  0.721   33.808  0.50 9.25   ? 254 ARG A CB  1 
ATOM   2165 C  CB  B ARG A 1 253 ? 16.359  1.071   33.795  0.50 10.03  ? 254 ARG A CB  1 
ATOM   2166 C  CG  A ARG A 1 253 ? 16.940  1.912   33.344  0.50 8.72   ? 254 ARG A CG  1 
ATOM   2167 C  CG  B ARG A 1 253 ? 17.250  2.192   33.292  0.50 10.62  ? 254 ARG A CG  1 
ATOM   2168 C  CD  A ARG A 1 253 ? 17.018  1.909   31.825  0.50 8.92   ? 254 ARG A CD  1 
ATOM   2169 C  CD  B ARG A 1 253 ? 17.411  2.178   31.773  0.50 8.76   ? 254 ARG A CD  1 
ATOM   2170 N  NE  A ARG A 1 253 ? 17.930  0.816   31.398  0.50 7.21   ? 254 ARG A NE  1 
ATOM   2171 N  NE  B ARG A 1 253 ? 18.230  1.045   31.325  0.50 9.18   ? 254 ARG A NE  1 
ATOM   2172 C  CZ  A ARG A 1 253 ? 18.221  0.585   30.119  0.50 7.47   ? 254 ARG A CZ  1 
ATOM   2173 C  CZ  B ARG A 1 253 ? 18.424  0.699   30.047  0.50 8.05   ? 254 ARG A CZ  1 
ATOM   2174 N  NH1 A ARG A 1 253 ? 17.634  1.311   29.158  0.50 7.70   ? 254 ARG A NH1 1 
ATOM   2175 N  NH1 B ARG A 1 253 ? 17.792  1.343   29.054  0.50 8.23   ? 254 ARG A NH1 1 
ATOM   2176 N  NH2 A ARG A 1 253 ? 19.042  -0.398  29.794  0.50 8.99   ? 254 ARG A NH2 1 
ATOM   2177 N  NH2 B ARG A 1 253 ? 19.267  -0.274  29.714  0.50 8.35   ? 254 ARG A NH2 1 
ATOM   2178 N  N   A GLN A 1 254 ? 13.790  0.260   35.949  0.50 12.85  ? 255 GLN A N   1 
ATOM   2179 N  N   B GLN A 1 254 ? 13.936  0.471   35.745  0.50 12.66  ? 255 GLN A N   1 
ATOM   2180 C  CA  A GLN A 1 254 ? 12.576  -0.471  36.189  0.50 15.26  ? 255 GLN A CA  1 
ATOM   2181 C  CA  B GLN A 1 254 ? 12.751  -0.358  36.042  0.50 13.56  ? 255 GLN A CA  1 
ATOM   2182 C  C   A GLN A 1 254 ? 11.792  -0.390  34.869  0.50 12.76  ? 255 GLN A C   1 
ATOM   2183 C  C   B GLN A 1 254 ? 11.775  -0.373  34.865  0.50 12.83  ? 255 GLN A C   1 
ATOM   2184 O  O   A GLN A 1 254 ? 11.746  0.693   34.154  0.50 16.84  ? 255 GLN A O   1 
ATOM   2185 O  O   B GLN A 1 254 ? 11.457  0.703   34.298  0.50 18.24  ? 255 GLN A O   1 
ATOM   2186 C  CB  A GLN A 1 254 ? 11.730  0.124   37.336  0.50 19.40  ? 255 GLN A CB  1 
ATOM   2187 C  CB  B GLN A 1 254 ? 11.961  0.162   37.225  0.50 17.93  ? 255 GLN A CB  1 
ATOM   2188 C  CG  A GLN A 1 254 ? 10.613  -0.790  37.760  0.50 24.21  ? 255 GLN A CG  1 
ATOM   2189 C  CG  B GLN A 1 254 ? 12.698  -0.006  38.537  0.50 21.59  ? 255 GLN A CG  1 
ATOM   2190 C  CD  A GLN A 1 254 ? 10.179  -0.818  39.224  0.50 31.20  ? 255 GLN A CD  1 
ATOM   2191 O  OE1 A GLN A 1 254 ? 9.103   -0.339  39.516  0.50 39.14  ? 255 GLN A OE1 1 
ATOM   2192 N  NE2 A GLN A 1 254 ? 10.930  -1.507  40.092  0.50 39.89  ? 255 GLN A NE2 1 
ATOM   2193 N  N   . ILE A 1 255 ? 11.336  -1.564  34.468  1.00 10.94  ? 256 ILE A N   1 
ATOM   2194 C  CA  . ILE A 1 255 ? 10.338  -1.685  33.399  1.00 10.32  ? 256 ILE A CA  1 
ATOM   2195 C  C   . ILE A 1 255 ? 8.984   -1.656  34.087  1.00 9.79   ? 256 ILE A C   1 
ATOM   2196 O  O   . ILE A 1 255 ? 8.758   -2.394  35.054  1.00 11.78  ? 256 ILE A O   1 
ATOM   2197 C  CB  . ILE A 1 255 ? 10.557  -2.878  32.563  1.00 10.53  ? 256 ILE A CB  1 
ATOM   2198 C  CG1 . ILE A 1 255 ? 12.009  -2.912  32.026  1.00 11.80  ? 256 ILE A CG1 1 
ATOM   2199 C  CG2 . ILE A 1 255 ? 9.504   -2.978  31.473  1.00 12.09  ? 256 ILE A CG2 1 
ATOM   2200 C  CD1 . ILE A 1 255 ? 12.338  -4.086  31.189  1.00 13.26  ? 256 ILE A CD1 1 
ATOM   2201 N  N   A LYS A 1 256 ? 8.075   -0.819  33.599  0.50 9.78   ? 257 LYS A N   1 
ATOM   2202 N  N   B LYS A 1 256 ? 8.075   -0.862  33.582  0.50 9.54   ? 257 LYS A N   1 
ATOM   2203 C  CA  A LYS A 1 256 ? 6.716   -0.643  34.124  0.50 10.15  ? 257 LYS A CA  1 
ATOM   2204 C  CA  B LYS A 1 256 ? 6.749   -0.801  34.102  0.50 9.73   ? 257 LYS A CA  1 
ATOM   2205 C  C   A LYS A 1 256 ? 5.690   -1.216  33.144  0.50 10.19  ? 257 LYS A C   1 
ATOM   2206 C  C   B LYS A 1 256 ? 5.798   -1.469  33.129  0.50 8.64   ? 257 LYS A C   1 
ATOM   2207 O  O   A LYS A 1 256 ? 5.811   -0.967  31.932  0.50 10.58  ? 257 LYS A O   1 
ATOM   2208 O  O   B LYS A 1 256 ? 6.065   -1.490  31.927  0.50 7.97   ? 257 LYS A O   1 
ATOM   2209 C  CB  A LYS A 1 256 ? 6.357   0.828   34.298  0.50 12.06  ? 257 LYS A CB  1 
ATOM   2210 C  CB  B LYS A 1 256 ? 6.372   0.662   34.407  0.50 11.21  ? 257 LYS A CB  1 
ATOM   2211 C  CG  A LYS A 1 256 ? 7.377   1.656   35.019  0.50 16.30  ? 257 LYS A CG  1 
ATOM   2212 C  CG  B LYS A 1 256 ? 7.218   1.210   35.543  0.50 13.91  ? 257 LYS A CG  1 
ATOM   2213 C  CD  A LYS A 1 256 ? 7.784   1.112   36.355  0.50 17.92  ? 257 LYS A CD  1 
ATOM   2214 C  CD  B LYS A 1 256 ? 7.041   2.672   35.909  0.50 18.71  ? 257 LYS A CD  1 
ATOM   2215 N  N   . ALA A 1 257 ? 4.709   -1.960  33.663  1.00 10.68  ? 258 ALA A N   1 
ATOM   2216 C  CA  . ALA A 1 257 ? 3.663   -2.564  32.899  1.00 10.62  ? 258 ALA A CA  1 
ATOM   2217 C  C   . ALA A 1 257 ? 2.340   -1.802  33.088  1.00 10.68  ? 258 ALA A C   1 
ATOM   2218 O  O   . ALA A 1 257 ? 2.004   -1.400  34.212  1.00 11.80  ? 258 ALA A O   1 
ATOM   2219 C  CB  . ALA A 1 257 ? 3.451   -4.041  33.267  1.00 12.91  ? 258 ALA A CB  1 
ATOM   2220 N  N   . SER A 1 258 ? 1.597   -1.613  32.000  1.00 10.66  ? 259 SER A N   1 
ATOM   2221 C  CA  . SER A 1 258 ? 0.294   -0.979  32.040  1.00 12.02  ? 259 SER A CA  1 
ATOM   2222 C  C   . SER A 1 258 ? -0.796  -1.966  32.444  1.00 12.83  ? 259 SER A C   1 
ATOM   2223 O  O   . SER A 1 258 ? -1.931  -1.518  32.586  1.00 16.39  ? 259 SER A O   1 
ATOM   2224 C  CB  . SER A 1 258 ? -0.037  -0.406  30.704  1.00 12.94  ? 259 SER A CB  1 
ATOM   2225 O  OG  . SER A 1 258 ? -0.419  -1.385  29.763  1.00 11.90  ? 259 SER A OG  1 
ATOM   2226 N  N   . PHE A 1 259 ? -0.499  -3.192  32.668  1.00 13.24  ? 260 PHE A N   1 
ATOM   2227 C  CA  . PHE A 1 259 ? -1.519  -4.241  32.816  1.00 15.25  ? 260 PHE A CA  1 
ATOM   2228 C  C   . PHE A 1 259 ? -0.964  -5.182  33.871  1.00 17.78  ? 260 PHE A C   1 
ATOM   2229 O  O   . PHE A 1 259 ? 0.287   -5.312  34.103  1.00 17.84  ? 260 PHE A O   1 
ATOM   2230 C  CB  . PHE A 1 259 ? -1.706  -4.960  31.482  1.00 16.12  ? 260 PHE A CB  1 
ATOM   2231 C  CG  . PHE A 1 259 ? -0.437  -5.676  31.018  1.00 14.69  ? 260 PHE A CG  1 
ATOM   2232 C  CD1 . PHE A 1 259 ? 0.559   -4.954  30.304  1.00 13.52  ? 260 PHE A CD1 1 
ATOM   2233 C  CD2 . PHE A 1 259 ? -0.196  -6.987  31.320  1.00 18.00  ? 260 PHE A CD2 1 
ATOM   2234 C  CE1 . PHE A 1 259 ? 1.758   -5.593  29.943  1.00 14.46  ? 260 PHE A CE1 1 
ATOM   2235 C  CE2 . PHE A 1 259 ? 0.987   -7.591  30.952  1.00 18.81  ? 260 PHE A CE2 1 
ATOM   2236 C  CZ  . PHE A 1 259 ? 1.968   -6.894  30.269  1.00 17.87  ? 260 PHE A CZ  1 
ATOM   2237 N  N   . LYS A 1 260 ? -1.944  -5.903  34.421  1.00 27.33  ? 261 LYS A N   1 
ATOM   2238 C  CA  . LYS A 1 260 ? -1.903  -7.092  35.327  1.00 40.39  ? 261 LYS A CA  1 
ATOM   2239 C  C   . LYS A 1 260 ? -1.729  -7.013  36.837  1.00 47.18  ? 261 LYS A C   1 
ATOM   2240 O  O   . LYS A 1 260 ? -2.548  -6.325  37.480  1.00 66.05  ? 261 LYS A O   1 
ATOM   2241 C  CB  . LYS A 1 260 ? -1.277  -8.305  34.648  1.00 38.12  ? 261 LYS A CB  1 
ATOM   2242 C  CG  . LYS A 1 260 ? -2.239  -8.876  33.611  1.00 42.32  ? 261 LYS A CG  1 
ATOM   2243 O  OXT . LYS A 1 260 ? -0.830  -7.621  37.433  1.00 90.49  ? 261 LYS A OXT 1 
HETATM 2244 ZN ZN  . ZN  B 2 .   ? 14.397  0.163   15.340  1.00 6.92   ? 301 ZN  A ZN  1 
HETATM 2245 S  S   . DMS C 3 .   ? 22.452  -9.820  14.907  1.00 16.54  ? 302 DMS A S   1 
HETATM 2246 O  O   . DMS C 3 .   ? 23.057  -11.125 14.508  1.00 20.63  ? 302 DMS A O   1 
HETATM 2247 C  C1  . DMS C 3 .   ? 22.707  -9.663  16.565  1.00 15.15  ? 302 DMS A C1  1 
HETATM 2248 C  C2  . DMS C 3 .   ? 23.497  -8.545  14.410  1.00 17.13  ? 302 DMS A C2  1 
HETATM 2249 O  O1  . MES D 4 .   ? 13.684  -7.337  -2.511  1.00 31.11  ? 303 MES A O1  1 
HETATM 2250 C  C2  . MES D 4 .   ? 12.639  -7.675  -1.568  1.00 25.36  ? 303 MES A C2  1 
HETATM 2251 C  C3  . MES D 4 .   ? 11.352  -8.425  -1.898  1.00 26.43  ? 303 MES A C3  1 
HETATM 2252 N  N4  . MES D 4 .   ? 11.302  -8.880  -3.363  1.00 31.39  ? 303 MES A N4  1 
HETATM 2253 C  C5  . MES D 4 .   ? 12.519  -8.816  -4.249  1.00 30.50  ? 303 MES A C5  1 
HETATM 2254 C  C6  . MES D 4 .   ? 13.779  -8.159  -3.713  1.00 25.17  ? 303 MES A C6  1 
HETATM 2255 C  C7  . MES D 4 .   ? 10.448  -10.000 -3.675  1.00 40.20  ? 303 MES A C7  1 
HETATM 2256 C  C8  . MES D 4 .   ? 9.046   -9.520  -3.318  1.00 29.39  ? 303 MES A C8  1 
HETATM 2257 C  C1  A MLA E 5 .   ? 26.367  -4.599  6.965   0.50 32.70  ? 304 MLA A C1  1 
HETATM 2258 C  C1  B MLA E 5 .   ? 26.386  -4.706  7.190   0.50 18.89  ? 304 MLA A C1  1 
HETATM 2259 O  O1A A MLA E 5 .   ? 25.372  -4.393  7.749   0.50 19.10  ? 304 MLA A O1A 1 
HETATM 2260 O  O1A B MLA E 5 .   ? 25.309  -4.468  7.826   0.50 17.81  ? 304 MLA A O1A 1 
HETATM 2261 O  O1B A MLA E 5 .   ? 27.264  -3.723  6.615   0.50 33.67  ? 304 MLA A O1B 1 
HETATM 2262 O  O1B B MLA E 5 .   ? 27.162  -3.776  6.689   0.50 20.24  ? 304 MLA A O1B 1 
HETATM 2263 C  C2  A MLA E 5 .   ? 26.510  -6.005  6.420   0.50 23.02  ? 304 MLA A C2  1 
HETATM 2264 C  C2  B MLA E 5 .   ? 26.849  -6.139  7.068   0.50 19.02  ? 304 MLA A C2  1 
HETATM 2265 C  C3  A MLA E 5 .   ? 27.951  -6.442  6.273   0.50 18.56  ? 304 MLA A C3  1 
HETATM 2266 C  C3  B MLA E 5 .   ? 25.794  -7.177  7.352   0.50 18.07  ? 304 MLA A C3  1 
HETATM 2267 O  O3A A MLA E 5 .   ? 28.113  -7.576  5.781   0.50 59.49  ? 304 MLA A O3A 1 
HETATM 2268 O  O3A B MLA E 5 .   ? 26.039  -8.421  7.116   0.50 22.99  ? 304 MLA A O3A 1 
HETATM 2269 O  O3B A MLA E 5 .   ? 28.949  -5.761  6.663   0.50 39.53  ? 304 MLA A O3B 1 
HETATM 2270 O  O3B B MLA E 5 .   ? 24.736  -6.651  7.765   0.50 29.82  ? 304 MLA A O3B 1 
HETATM 2271 N  N1  . BCN F 6 .   ? 0.392   -12.865 23.513  1.00 36.30  ? 305 BCN A N1  1 
HETATM 2272 C  C1  . BCN F 6 .   ? 1.222   -13.733 22.665  1.00 25.43  ? 305 BCN A C1  1 
HETATM 2273 C  C2  . BCN F 6 .   ? 0.958   -14.386 21.368  1.00 34.83  ? 305 BCN A C2  1 
HETATM 2274 O  O21 . BCN F 6 .   ? -0.153  -14.200 20.729  1.00 54.83  ? 305 BCN A O21 1 
HETATM 2275 O  O22 . BCN F 6 .   ? 1.945   -15.120 21.048  1.00 61.21  ? 305 BCN A O22 1 
HETATM 2276 C  C3  . BCN F 6 .   ? 1.330   -12.265 24.561  1.00 38.50  ? 305 BCN A C3  1 
HETATM 2277 C  C4  . BCN F 6 .   ? 1.444   -13.251 25.774  1.00 30.51  ? 305 BCN A C4  1 
HETATM 2278 O  O4  . BCN F 6 .   ? 0.430   -14.290 25.703  1.00 46.99  ? 305 BCN A O4  1 
HETATM 2279 C  C5  . BCN F 6 .   ? -0.617  -11.988 22.856  1.00 25.82  ? 305 BCN A C5  1 
HETATM 2280 C  C6  . BCN F 6 .   ? -1.757  -11.389 23.707  1.00 33.19  ? 305 BCN A C6  1 
HETATM 2281 O  O6  . BCN F 6 .   ? -1.344  -10.528 24.782  1.00 35.69  ? 305 BCN A O6  1 
HETATM 2282 F  F18 . 3TV G 7 .   ? 14.905  7.426   15.238  1.00 12.53  ? 306 3TV A F18 1 
HETATM 2283 C  C7  . 3TV G 7 .   ? 15.429  6.197   15.037  1.00 9.88   ? 306 3TV A C7  1 
HETATM 2284 C  C6  . 3TV G 7 .   ? 15.101  5.184   15.873  1.00 9.55   ? 306 3TV A C6  1 
HETATM 2285 F  F17 . 3TV G 7 .   ? 14.280  5.502   16.935  1.00 10.91  ? 306 3TV A F17 1 
HETATM 2286 C  C8  . 3TV G 7 .   ? 16.209  5.985   13.961  1.00 10.72  ? 306 3TV A C8  1 
HETATM 2287 S  S11 . 3TV G 7 .   ? 16.540  7.280   12.820  1.00 13.60  ? 306 3TV A S11 1 
HETATM 2288 C  C12 . 3TV G 7 .   ? 18.310  7.273   12.663  1.00 14.38  ? 306 3TV A C12 1 
HETATM 2289 C  C13 . 3TV G 7 .   ? 18.959  7.528   13.937  1.00 14.79  ? 306 3TV A C13 1 
HETATM 2290 C  C14 . 3TV G 7 .   ? 18.834  8.893   14.485  1.00 17.95  ? 306 3TV A C14 1 
HETATM 2291 C  C9  . 3TV G 7 .   ? 16.708  4.693   13.816  1.00 10.36  ? 306 3TV A C9  1 
HETATM 2292 F  F15 . 3TV G 7 .   ? 17.483  4.388   12.796  1.00 12.25  ? 306 3TV A F15 1 
HETATM 2293 C  C10 . 3TV G 7 .   ? 16.371  3.664   14.709  1.00 9.29   ? 306 3TV A C10 1 
HETATM 2294 F  F16 . 3TV G 7 .   ? 16.891  2.477   14.441  1.00 18.38  ? 306 3TV A F16 1 
HETATM 2295 C  C5  . 3TV G 7 .   ? 15.561  3.927   15.769  1.00 8.66   ? 306 3TV A C5  1 
HETATM 2296 S  S1  . 3TV G 7 .   ? 15.095  2.660   16.892  1.00 7.54   ? 306 3TV A S1  1 
HETATM 2297 O  O3  . 3TV G 7 .   ? 13.666  2.727   16.820  1.00 8.20   ? 306 3TV A O3  1 
HETATM 2298 O  O4  . 3TV G 7 .   ? 15.744  2.968   18.133  1.00 7.59   ? 306 3TV A O4  1 
HETATM 2299 N  N2  . 3TV G 7 .   ? 15.583  1.303   16.323  1.00 8.03   ? 306 3TV A N2  1 
HETATM 2300 F  F18 . 3TV H 7 .   ? 34.244  1.577   9.440   1.00 25.71  ? 307 3TV A F18 1 
HETATM 2301 C  C7  . 3TV H 7 .   ? 34.077  0.802   10.496  1.00 21.59  ? 307 3TV A C7  1 
HETATM 2302 C  C6  . 3TV H 7 .   ? 33.237  1.209   11.515  1.00 18.04  ? 307 3TV A C6  1 
HETATM 2303 F  F17 . 3TV H 7 .   ? 32.539  2.355   11.265  1.00 24.12  ? 307 3TV A F17 1 
HETATM 2304 C  C8  . 3TV H 7 .   ? 34.877  -0.361  10.682  1.00 17.11  ? 307 3TV A C8  1 
HETATM 2305 S  S11 . 3TV H 7 .   ? 35.936  -0.841  9.386   1.00 22.07  ? 307 3TV A S11 1 
HETATM 2306 C  C12 . 3TV H 7 .   ? 35.440  -2.555  9.032   1.00 26.25  ? 307 3TV A C12 1 
HETATM 2307 C  C13 . 3TV H 7 .   ? 36.024  -3.121  7.701   1.00 42.68  ? 307 3TV A C13 1 
HETATM 2308 C  C14 . 3TV H 7 .   ? 36.341  -4.612  7.702   1.00 40.39  ? 307 3TV A C14 1 
HETATM 2309 C  C9  . 3TV H 7 .   ? 34.681  -1.088  11.830  1.00 18.73  ? 307 3TV A C9  1 
HETATM 2310 F  F15 . 3TV H 7 .   ? 35.437  -2.190  11.968  1.00 21.91  ? 307 3TV A F15 1 
HETATM 2311 C  C10 . 3TV H 7 .   ? 33.774  -0.710  12.754  1.00 18.15  ? 307 3TV A C10 1 
HETATM 2312 F  F16 . 3TV H 7 .   ? 33.724  -1.480  13.829  1.00 21.76  ? 307 3TV A F16 1 
HETATM 2313 C  C5  . 3TV H 7 .   ? 32.987  0.433   12.640  1.00 17.50  ? 307 3TV A C5  1 
HETATM 2314 S  S1  . 3TV H 7 .   ? 31.764  0.841   13.857  1.00 17.17  ? 307 3TV A S1  1 
HETATM 2315 O  O3  . 3TV H 7 .   ? 31.023  -0.366  14.018  1.00 18.17  ? 307 3TV A O3  1 
HETATM 2316 O  O4  . 3TV H 7 .   ? 31.152  2.115   13.542  1.00 19.26  ? 307 3TV A O4  1 
HETATM 2317 N  N2  . 3TV H 7 .   ? 32.487  1.121   15.330  1.00 18.04  ? 307 3TV A N2  1 
HETATM 2318 O  O   . HOH I 8 .   ? -4.438  -8.783  17.752  1.00 21.38  ? 401 HOH A O   1 
HETATM 2319 O  O   . HOH I 8 .   ? 5.808   21.167  13.129  1.00 18.95  ? 402 HOH A O   1 
HETATM 2320 O  O   . HOH I 8 .   ? 20.548  -15.302 29.527  1.00 39.38  ? 403 HOH A O   1 
HETATM 2321 O  O   . HOH I 8 .   ? 7.237   -6.854  -5.283  1.00 23.71  ? 404 HOH A O   1 
HETATM 2322 O  O   . HOH I 8 .   ? 3.307   20.888  6.085   1.00 12.78  ? 405 HOH A O   1 
HETATM 2323 O  O   . HOH I 8 .   ? 19.811  -15.684 18.073  1.00 31.82  ? 406 HOH A O   1 
HETATM 2324 O  O   . HOH I 8 .   ? 8.371   14.914  31.767  1.00 56.65  ? 407 HOH A O   1 
HETATM 2325 O  O   . HOH I 8 .   ? 14.360  22.722  19.520  1.00 13.83  ? 408 HOH A O   1 
HETATM 2326 O  O   . HOH I 8 .   ? 14.933  -9.720  36.334  1.00 39.52  ? 409 HOH A O   1 
HETATM 2327 O  O   . HOH I 8 .   ? 9.928   -13.311 34.013  1.00 24.57  ? 410 HOH A O   1 
HETATM 2328 O  O   . HOH I 8 .   ? 2.203   22.126  15.001  1.00 37.15  ? 411 HOH A O   1 
HETATM 2329 O  O   . HOH I 8 .   ? 10.702  -3.799  38.277  1.00 28.26  ? 412 HOH A O   1 
HETATM 2330 O  O   . HOH I 8 .   ? 20.005  -4.161  36.470  1.00 26.20  ? 413 HOH A O   1 
HETATM 2331 O  O   . HOH I 8 .   ? -0.012  -5.086  -2.059  1.00 59.86  ? 414 HOH A O   1 
HETATM 2332 O  O   . HOH I 8 .   ? 5.533   -8.422  37.397  1.00 28.94  ? 415 HOH A O   1 
HETATM 2333 O  O   . HOH I 8 .   ? 4.170   -16.147 20.167  1.00 29.46  ? 416 HOH A O   1 
HETATM 2334 O  O   . HOH I 8 .   ? 4.046   -12.260 37.386  1.00 32.01  ? 417 HOH A O   1 
HETATM 2335 O  O   . HOH I 8 .   ? 11.939  7.764   29.024  1.00 19.31  ? 418 HOH A O   1 
HETATM 2336 O  O   . HOH I 8 .   ? 1.293   -14.977 3.001   1.00 24.01  ? 419 HOH A O   1 
HETATM 2337 O  O   . HOH I 8 .   ? 36.254  -5.050  12.213  1.00 28.79  ? 420 HOH A O   1 
HETATM 2338 O  O   . HOH I 8 .   ? 2.480   -10.414 -3.507  1.00 21.26  ? 421 HOH A O   1 
HETATM 2339 O  O   . HOH I 8 .   ? 10.449  -17.518 20.056  1.00 18.74  ? 422 HOH A O   1 
HETATM 2340 O  O   . HOH I 8 .   ? 20.864  2.954   34.549  1.00 24.12  ? 423 HOH A O   1 
HETATM 2341 O  O   . HOH I 8 .   ? 9.117   12.587  6.154   1.00 31.86  ? 424 HOH A O   1 
HETATM 2342 O  O   . HOH I 8 .   ? 14.395  -3.469  37.319  1.00 19.70  ? 425 HOH A O   1 
HETATM 2343 O  O   . HOH I 8 .   ? 23.077  9.979   27.836  1.00 31.60  ? 426 HOH A O   1 
HETATM 2344 O  O   . HOH I 8 .   ? -0.737  17.584  3.820   1.00 38.96  ? 427 HOH A O   1 
HETATM 2345 O  O   . HOH I 8 .   ? 4.506   6.987   -7.946  1.00 27.69  ? 428 HOH A O   1 
HETATM 2346 O  O   . HOH I 8 .   ? 8.288   -20.394 8.430   1.00 28.56  ? 429 HOH A O   1 
HETATM 2347 O  O   . HOH I 8 .   ? 32.262  -5.203  22.444  1.00 29.91  ? 430 HOH A O   1 
HETATM 2348 O  O   . HOH I 8 .   ? 36.451  2.247   15.107  1.00 27.78  ? 431 HOH A O   1 
HETATM 2349 O  O   . HOH I 8 .   ? 12.717  -13.410 36.851  1.00 30.71  ? 432 HOH A O   1 
HETATM 2350 O  O   . HOH I 8 .   ? 8.681   18.008  8.338   1.00 41.23  ? 433 HOH A O   1 
HETATM 2351 O  O   . HOH I 8 .   ? 28.579  -6.082  -1.138  1.00 27.39  ? 434 HOH A O   1 
HETATM 2352 O  O   . HOH I 8 .   ? -4.532  -3.277  13.391  1.00 23.72  ? 435 HOH A O   1 
HETATM 2353 O  O   . HOH I 8 .   ? 8.685   14.269  29.218  1.00 26.79  ? 436 HOH A O   1 
HETATM 2354 O  O   . HOH I 8 .   ? -0.170  9.616   1.896   1.00 15.03  ? 437 HOH A O   1 
HETATM 2355 O  O   . HOH I 8 .   ? 21.462  9.019   29.915  1.00 30.51  ? 438 HOH A O   1 
HETATM 2356 O  O   . HOH I 8 .   ? 14.096  7.836   6.234   1.00 15.38  ? 439 HOH A O   1 
HETATM 2357 O  O   . HOH I 8 .   ? -6.241  -5.746  26.120  1.00 35.51  ? 440 HOH A O   1 
HETATM 2358 O  O   . HOH I 8 .   ? 20.718  -18.606 14.622  1.00 37.76  ? 441 HOH A O   1 
HETATM 2359 O  O   . HOH I 8 .   ? 4.464   -13.369 32.801  1.00 46.07  ? 442 HOH A O   1 
HETATM 2360 O  O   . HOH I 8 .   ? 19.892  11.014  28.108  1.00 28.43  ? 443 HOH A O   1 
HETATM 2361 O  O   . HOH I 8 .   ? 1.635   -18.843 5.022   1.00 20.47  ? 444 HOH A O   1 
HETATM 2362 O  O   . HOH I 8 .   ? 23.551  -11.240 5.291   1.00 17.68  ? 445 HOH A O   1 
HETATM 2363 O  O   . HOH I 8 .   ? -4.834  9.744   6.520   1.00 28.77  ? 446 HOH A O   1 
HETATM 2364 O  O   . HOH I 8 .   ? 1.526   -2.511  41.415  1.00 35.65  ? 447 HOH A O   1 
HETATM 2365 O  O   . HOH I 8 .   ? 19.160  6.582   -4.883  1.00 36.43  ? 448 HOH A O   1 
HETATM 2366 O  O   . HOH I 8 .   ? 1.574   19.205  6.046   1.00 22.40  ? 449 HOH A O   1 
HETATM 2367 O  O   . HOH I 8 .   ? 6.450   -16.633 18.739  1.00 18.26  ? 450 HOH A O   1 
HETATM 2368 O  O   . HOH I 8 .   ? -3.616  -5.864  9.100   1.00 16.75  ? 451 HOH A O   1 
HETATM 2369 O  O   . HOH I 8 .   ? 10.713  -16.373 17.061  1.00 14.35  ? 452 HOH A O   1 
HETATM 2370 O  O   . HOH I 8 .   ? 3.190   -18.601 8.067   1.00 13.31  ? 453 HOH A O   1 
HETATM 2371 O  O   . HOH I 8 .   ? 2.594   -1.905  -2.591  1.00 29.33  ? 454 HOH A O   1 
HETATM 2372 O  O   . HOH I 8 .   ? -5.314  4.682   20.749  1.00 27.56  ? 455 HOH A O   1 
HETATM 2373 O  O   . HOH I 8 .   ? 5.374   10.802  -2.177  1.00 25.40  ? 456 HOH A O   1 
HETATM 2374 O  O   . HOH I 8 .   ? -5.139  5.430   15.394  1.00 21.79  ? 457 HOH A O   1 
HETATM 2375 O  O   . HOH I 8 .   ? 9.016   11.318  3.244   1.00 23.59  ? 458 HOH A O   1 
HETATM 2376 O  O   . HOH I 8 .   ? 30.501  4.311   11.978  1.00 24.60  ? 459 HOH A O   1 
HETATM 2377 O  O   . HOH I 8 .   ? 34.567  2.060   24.349  1.00 18.68  ? 460 HOH A O   1 
HETATM 2378 O  O   . HOH I 8 .   ? 36.645  -0.443  14.519  1.00 18.26  ? 461 HOH A O   1 
HETATM 2379 O  O   . HOH I 8 .   ? 7.040   16.104  27.136  1.00 23.42  ? 462 HOH A O   1 
HETATM 2380 O  O   . HOH I 8 .   ? 10.403  10.447  7.701   1.00 17.90  ? 463 HOH A O   1 
HETATM 2381 O  O   . HOH I 8 .   ? 13.360  -2.871  39.938  1.00 32.13  ? 464 HOH A O   1 
HETATM 2382 O  O   . HOH I 8 .   ? 19.395  0.605   -12.778 1.00 51.93  ? 465 HOH A O   1 
HETATM 2383 O  O   . HOH I 8 .   ? -0.912  7.575   4.761   1.00 15.40  ? 466 HOH A O   1 
HETATM 2384 O  O   . HOH I 8 .   ? 8.011   -14.945 26.629  1.00 17.19  ? 467 HOH A O   1 
HETATM 2385 O  O   . HOH I 8 .   ? 10.820  15.327  8.773   1.00 34.82  ? 468 HOH A O   1 
HETATM 2386 O  O   . HOH I 8 .   ? -8.694  8.619   7.607   1.00 42.39  ? 469 HOH A O   1 
HETATM 2387 O  O   . HOH I 8 .   ? -1.042  -16.453 13.588  1.00 23.10  ? 470 HOH A O   1 
HETATM 2388 O  O   . HOH I 8 .   ? 17.293  -13.993 24.383  1.00 13.49  ? 471 HOH A O   1 
HETATM 2389 O  O   . HOH I 8 .   ? 8.107   -6.959  -3.262  1.00 24.55  ? 472 HOH A O   1 
HETATM 2390 O  O   . HOH I 8 .   ? 9.213   -1.380  42.325  1.00 28.80  ? 473 HOH A O   1 
HETATM 2391 O  O   . HOH I 8 .   ? 37.582  -7.064  11.215  1.00 18.98  ? 474 HOH A O   1 
HETATM 2392 O  O   . HOH I 8 .   ? 13.094  -20.215 10.362  1.00 20.66  ? 475 HOH A O   1 
HETATM 2393 O  O   . HOH I 8 .   ? 6.129   21.888  17.650  1.00 22.15  ? 476 HOH A O   1 
HETATM 2394 O  O   . HOH I 8 .   ? 7.781   -16.574 14.605  1.00 17.20  ? 477 HOH A O   1 
HETATM 2395 O  O   . HOH I 8 .   ? -0.018  20.728  13.698  1.00 28.90  ? 478 HOH A O   1 
HETATM 2396 O  O   . HOH I 8 .   ? 2.504   5.719   -3.448  1.00 54.11  ? 479 HOH A O   1 
HETATM 2397 O  O   . HOH I 8 .   ? 20.742  2.931   -10.975 1.00 29.95  ? 480 HOH A O   1 
HETATM 2398 O  O   . HOH I 8 .   ? 22.476  -14.033 -1.540  1.00 31.15  ? 481 HOH A O   1 
HETATM 2399 O  O   . HOH I 8 .   ? 7.351   21.786  15.141  1.00 20.79  ? 482 HOH A O   1 
HETATM 2400 O  O   . HOH I 8 .   ? -5.848  -2.132  24.994  1.00 17.84  ? 483 HOH A O   1 
HETATM 2401 O  O   . HOH I 8 .   ? 22.612  -4.445  34.387  1.00 23.53  ? 484 HOH A O   1 
HETATM 2402 O  O   . HOH I 8 .   ? 14.904  -17.840 23.923  1.00 24.98  ? 485 HOH A O   1 
HETATM 2403 O  O   . HOH I 8 .   ? 12.546  -17.953 26.630  1.00 24.09  ? 486 HOH A O   1 
HETATM 2404 O  O   . HOH I 8 .   ? 3.866   -5.531  39.697  1.00 28.84  ? 487 HOH A O   1 
HETATM 2405 O  O   . HOH I 8 .   ? 11.153  16.620  12.125  1.00 17.18  ? 488 HOH A O   1 
HETATM 2406 O  O   . HOH I 8 .   ? 20.521  -6.687  32.514  1.00 24.68  ? 489 HOH A O   1 
HETATM 2407 O  O   . HOH I 8 .   ? 8.234   5.525   -6.865  1.00 23.80  ? 490 HOH A O   1 
HETATM 2408 O  O   . HOH I 8 .   ? 13.939  3.327   35.136  1.00 27.11  ? 491 HOH A O   1 
HETATM 2409 O  O   . HOH I 8 .   ? 34.182  -4.007  24.397  1.00 24.91  ? 492 HOH A O   1 
HETATM 2410 O  O   . HOH I 8 .   ? 8.437   -16.556 32.166  1.00 30.25  ? 493 HOH A O   1 
HETATM 2411 O  O   . HOH I 8 .   ? 17.819  5.820   40.636  1.00 21.62  ? 494 HOH A O   1 
HETATM 2412 O  O   . HOH I 8 .   ? 12.942  -17.469 21.683  1.00 15.06  ? 495 HOH A O   1 
HETATM 2413 O  O   . HOH I 8 .   ? -0.057  -17.640 6.618   1.00 23.39  ? 496 HOH A O   1 
HETATM 2414 O  O   . HOH I 8 .   ? 15.336  17.540  12.033  1.00 54.44  ? 497 HOH A O   1 
HETATM 2415 O  O   . HOH I 8 .   ? -3.656  13.872  6.160   1.00 29.17  ? 498 HOH A O   1 
HETATM 2416 O  O   . HOH I 8 .   ? 25.829  -11.267 -5.664  1.00 22.64  ? 499 HOH A O   1 
HETATM 2417 O  O   . HOH I 8 .   ? 23.846  -12.556 0.731   1.00 21.63  ? 500 HOH A O   1 
HETATM 2418 O  O   . HOH I 8 .   ? -3.390  1.602   1.247   1.00 35.85  ? 501 HOH A O   1 
HETATM 2419 O  O   . HOH I 8 .   ? 9.986   19.365  12.229  1.00 22.38  ? 502 HOH A O   1 
HETATM 2420 O  O   . HOH I 8 .   ? -10.561 6.894   12.734  1.00 33.43  ? 503 HOH A O   1 
HETATM 2421 O  O   . HOH I 8 .   ? 15.658  5.439   -5.712  1.00 26.48  ? 504 HOH A O   1 
HETATM 2422 O  O   . HOH I 8 .   ? -3.566  -7.594  1.915   1.00 22.72  ? 505 HOH A O   1 
HETATM 2423 O  O   . HOH I 8 .   ? 35.201  4.025   22.812  1.00 29.85  ? 506 HOH A O   1 
HETATM 2424 O  O   . HOH I 8 .   ? 3.992   2.103   -3.877  1.00 48.75  ? 507 HOH A O   1 
HETATM 2425 O  O   . HOH I 8 .   ? 31.495  8.544   15.235  1.00 36.70  ? 508 HOH A O   1 
HETATM 2426 O  O   . HOH I 8 .   ? 19.526  13.130  25.922  1.00 27.19  ? 509 HOH A O   1 
HETATM 2427 O  O   . HOH I 8 .   ? -4.392  6.081   3.997   1.00 40.98  ? 510 HOH A O   1 
HETATM 2428 O  O   . HOH I 8 .   ? 34.982  7.594   18.662  1.00 40.46  ? 511 HOH A O   1 
HETATM 2429 O  O   . HOH I 8 .   ? 3.320   21.608  17.554  1.00 26.58  ? 512 HOH A O   1 
HETATM 2430 O  O   . HOH I 8 .   ? 21.313  2.588   -6.817  1.00 26.58  ? 513 HOH A O   1 
HETATM 2431 O  O   . HOH I 8 .   ? -0.753  21.704  17.455  1.00 42.03  ? 514 HOH A O   1 
HETATM 2432 O  O   . HOH I 8 .   ? 10.652  7.829   -4.158  1.00 32.70  ? 515 HOH A O   1 
HETATM 2433 O  O   . HOH I 8 .   ? 8.245   -15.314 16.881  1.00 14.78  ? 516 HOH A O   1 
HETATM 2434 O  O   . HOH I 8 .   ? 3.302   8.188   38.588  1.00 36.19  ? 517 HOH A O   1 
HETATM 2435 O  O   . HOH I 8 .   ? 5.743   -14.355 25.278  1.00 36.70  ? 518 HOH A O   1 
HETATM 2436 O  O   . HOH I 8 .   ? 5.847   -18.154 23.394  1.00 41.17  ? 519 HOH A O   1 
HETATM 2437 O  O   . HOH I 8 .   ? 3.678   19.956  4.076   1.00 29.57  ? 520 HOH A O   1 
HETATM 2438 O  O   . HOH I 8 .   ? 18.462  -15.866 5.391   1.00 36.88  ? 521 HOH A O   1 
HETATM 2439 O  O   . HOH I 8 .   ? 31.198  -3.536  -5.744  1.00 37.54  ? 522 HOH A O   1 
HETATM 2440 O  O   . HOH I 8 .   ? 7.894   20.628  11.748  1.00 32.24  ? 523 HOH A O   1 
HETATM 2441 O  O   . HOH I 8 .   ? 20.225  -15.356 -2.073  1.00 36.61  ? 524 HOH A O   1 
HETATM 2442 O  O   . HOH I 8 .   ? 4.927   18.765  26.284  1.00 33.56  ? 525 HOH A O   1 
HETATM 2443 O  O   . HOH I 8 .   ? 18.965  -15.678 25.635  1.00 29.60  ? 526 HOH A O   1 
HETATM 2444 O  O   . HOH I 8 .   ? 36.467  0.588   25.891  1.00 18.78  ? 527 HOH A O   1 
HETATM 2445 O  O   . HOH I 8 .   ? 13.065  16.692  10.499  1.00 31.42  ? 528 HOH A O   1 
HETATM 2446 O  O   . HOH I 8 .   ? 14.931  -18.939 26.300  1.00 33.82  ? 529 HOH A O   1 
HETATM 2447 O  O   . HOH I 8 .   ? 11.867  4.907   34.837  1.00 29.03  ? 530 HOH A O   1 
HETATM 2448 O  O   . HOH I 8 .   ? 11.361  3.256   38.982  1.00 27.07  ? 531 HOH A O   1 
HETATM 2449 O  O   . HOH I 8 .   ? 10.567  -18.441 24.990  1.00 24.94  ? 532 HOH A O   1 
HETATM 2450 O  O   . HOH I 8 .   ? 12.876  9.367   8.161   1.00 21.50  ? 533 HOH A O   1 
HETATM 2451 O  O   . HOH I 8 .   ? 2.997   4.699   -6.564  1.00 44.54  ? 534 HOH A O   1 
HETATM 2452 O  O   . HOH I 8 .   ? 33.464  5.904   27.058  1.00 35.30  ? 535 HOH A O   1 
HETATM 2453 O  O   . HOH I 8 .   ? 8.154   -17.612 26.195  1.00 26.54  ? 536 HOH A O   1 
HETATM 2454 O  O   . HOH I 8 .   ? 19.589  4.972   -7.164  1.00 29.01  ? 537 HOH A O   1 
HETATM 2455 O  O   . HOH I 8 .   ? 35.248  0.402   28.427  1.00 28.49  ? 538 HOH A O   1 
HETATM 2456 O  O   . HOH I 8 .   ? 17.780  -18.188 27.353  1.00 41.49  ? 539 HOH A O   1 
HETATM 2457 O  O   . HOH I 8 .   ? 35.405  6.521   24.768  1.00 73.69  ? 540 HOH A O   1 
HETATM 2458 O  O   . HOH I 8 .   ? 14.070  -13.016 31.623  1.00 20.59  ? 541 HOH A O   1 
HETATM 2459 O  O   . HOH I 8 .   ? 4.067   -6.537  20.428  1.00 8.84   ? 542 HOH A O   1 
HETATM 2460 O  O   . HOH I 8 .   ? 19.826  -2.150  15.753  1.00 9.38   ? 543 HOH A O   1 
HETATM 2461 O  O   . HOH I 8 .   ? 18.579  -6.885  29.105  1.00 11.53  ? 544 HOH A O   1 
HETATM 2462 O  O   . HOH I 8 .   ? 16.548  -11.630 18.044  1.00 9.28   ? 545 HOH A O   1 
HETATM 2463 O  O   . HOH I 8 .   ? 17.115  5.498   9.657   1.00 19.63  ? 546 HOH A O   1 
HETATM 2464 O  O   . HOH I 8 .   ? -0.536  -5.220  23.526  1.00 12.16  ? 547 HOH A O   1 
HETATM 2465 O  O   . HOH I 8 .   ? 25.930  -2.956  20.974  1.00 12.98  ? 548 HOH A O   1 
HETATM 2466 O  O   . HOH I 8 .   ? 18.996  -10.428 22.901  1.00 10.52  ? 549 HOH A O   1 
HETATM 2467 O  O   . HOH I 8 .   ? -1.829  -9.651  14.059  1.00 15.58  ? 550 HOH A O   1 
HETATM 2468 O  O   . HOH I 8 .   ? 17.654  -11.396 25.205  1.00 11.48  ? 551 HOH A O   1 
HETATM 2469 O  O   . HOH I 8 .   ? 4.655   -8.070  32.852  1.00 17.70  ? 552 HOH A O   1 
HETATM 2470 O  O   . HOH I 8 .   ? 10.448  10.536  25.586  1.00 10.55  ? 553 HOH A O   1 
HETATM 2471 O  O   . HOH I 8 .   ? 24.752  6.871   29.847  1.00 19.68  ? 554 HOH A O   1 
HETATM 2472 O  O   . HOH I 8 .   ? 29.668  -1.956  21.039  1.00 13.41  ? 555 HOH A O   1 
HETATM 2473 O  O   . HOH I 8 .   ? 12.385  -1.934  7.902   1.00 8.85   ? 556 HOH A O   1 
HETATM 2474 O  O   . HOH I 8 .   ? 1.716   11.838  8.891   1.00 13.85  ? 557 HOH A O   1 
HETATM 2475 O  O   . HOH I 8 .   ? 21.120  0.842   -4.734  1.00 16.09  ? 558 HOH A O   1 
HETATM 2476 O  O   . HOH I 8 .   ? 13.156  -13.533 11.322  1.00 10.47  ? 559 HOH A O   1 
HETATM 2477 O  O   . HOH I 8 .   ? 18.526  -0.924  11.443  1.00 15.09  ? 560 HOH A O   1 
HETATM 2478 O  O   . HOH I 8 .   ? 17.574  -9.296  20.904  1.00 9.40   ? 561 HOH A O   1 
HETATM 2479 O  O   . HOH I 8 .   ? 22.327  0.239   29.464  1.00 13.63  ? 562 HOH A O   1 
HETATM 2480 O  O   . HOH I 8 .   ? -2.976  1.195   26.406  1.00 14.55  ? 563 HOH A O   1 
HETATM 2481 O  O   . HOH I 8 .   ? 7.081   12.232  27.865  1.00 20.11  ? 564 HOH A O   1 
HETATM 2482 O  O   . HOH I 8 .   ? 15.430  3.602   10.863  1.00 14.22  ? 565 HOH A O   1 
HETATM 2483 O  O   . HOH I 8 .   ? 14.375  8.474   10.266  1.00 20.89  ? 566 HOH A O   1 
HETATM 2484 O  O   . HOH I 8 .   ? 14.927  -2.656  -6.397  1.00 24.44  ? 567 HOH A O   1 
HETATM 2485 O  O   . HOH I 8 .   ? 22.292  10.664  24.441  1.00 16.74  ? 568 HOH A O   1 
HETATM 2486 O  O   . HOH I 8 .   ? -1.702  -4.016  2.837   1.00 20.12  ? 569 HOH A O   1 
HETATM 2487 O  O   . HOH I 8 .   ? 3.099   12.405  11.329  1.00 16.99  ? 570 HOH A O   1 
HETATM 2488 O  O   . HOH I 8 .   ? 0.663   12.612  26.581  1.00 19.12  ? 571 HOH A O   1 
HETATM 2489 O  O   . HOH I 8 .   ? 25.469  -0.654  28.991  1.00 25.26  ? 572 HOH A O   1 
HETATM 2490 O  O   . HOH I 8 .   ? 29.777  -2.825  23.642  1.00 24.36  ? 573 HOH A O   1 
HETATM 2491 O  O   . HOH I 8 .   ? 22.494  -9.893  25.042  1.00 22.56  ? 574 HOH A O   1 
HETATM 2492 O  O   . HOH I 8 .   ? -2.124  -1.198  6.644   1.00 17.23  ? 575 HOH A O   1 
HETATM 2493 O  O   . HOH I 8 .   ? 26.599  8.947   20.229  1.00 17.25  ? 576 HOH A O   1 
HETATM 2494 O  O   . HOH I 8 .   ? 28.735  7.938   21.735  1.00 15.55  ? 577 HOH A O   1 
HETATM 2495 O  O   . HOH I 8 .   ? 9.106   4.687   30.786  1.00 20.85  ? 578 HOH A O   1 
HETATM 2496 O  O   . HOH I 8 .   ? 19.479  -11.322 27.268  1.00 26.31  ? 579 HOH A O   1 
HETATM 2497 O  O   . HOH I 8 .   ? 19.915  -9.259  28.970  1.00 18.27  ? 580 HOH A O   1 
HETATM 2498 O  O   . HOH I 8 .   ? 9.985   -17.396 7.071   1.00 24.51  ? 581 HOH A O   1 
HETATM 2499 O  O   . HOH I 8 .   ? -2.786  1.065   3.920   1.00 21.33  ? 582 HOH A O   1 
HETATM 2500 O  O   . HOH I 8 .   ? 21.192  -13.376 26.488  1.00 43.50  ? 583 HOH A O   1 
HETATM 2501 O  O   . HOH I 8 .   ? 11.504  -6.099  34.114  1.00 20.98  ? 584 HOH A O   1 
HETATM 2502 O  O   . HOH I 8 .   ? 17.443  -11.046 -2.851  1.00 21.88  ? 585 HOH A O   1 
HETATM 2503 O  O   . HOH I 8 .   ? 23.681  -2.297  7.871   1.00 16.20  ? 586 HOH A O   1 
HETATM 2504 O  O   . HOH I 8 .   ? 23.616  -9.369  9.528   1.00 19.34  ? 587 HOH A O   1 
HETATM 2505 O  O   . HOH I 8 .   ? 24.215  2.884   -1.890  1.00 35.90  ? 588 HOH A O   1 
HETATM 2506 O  O   . HOH I 8 .   ? 16.310  -10.132 32.115  1.00 20.85  ? 589 HOH A O   1 
HETATM 2507 O  O   . HOH I 8 .   ? 20.592  12.657  23.403  1.00 16.32  ? 590 HOH A O   1 
HETATM 2508 O  O   . HOH I 8 .   ? 11.944  -4.010  35.863  1.00 18.08  ? 591 HOH A O   1 
HETATM 2509 O  O   . HOH I 8 .   ? -3.079  10.544  20.164  1.00 20.63  ? 592 HOH A O   1 
HETATM 2510 O  O   . HOH I 8 .   ? 16.483  -14.068 0.775   1.00 25.25  ? 593 HOH A O   1 
HETATM 2511 O  O   . HOH I 8 .   ? 26.251  -5.342  22.356  1.00 29.37  ? 594 HOH A O   1 
HETATM 2512 O  O   . HOH I 8 .   ? 3.215   -10.253 31.669  1.00 29.87  ? 595 HOH A O   1 
HETATM 2513 O  O   . HOH I 8 .   ? 25.472  -1.603  26.497  1.00 16.53  ? 596 HOH A O   1 
HETATM 2514 O  O   . HOH I 8 .   ? 4.990   -10.462 24.413  1.00 15.75  ? 597 HOH A O   1 
HETATM 2515 O  O   . HOH I 8 .   ? 32.409  3.202   25.912  1.00 21.04  ? 598 HOH A O   1 
HETATM 2516 O  O   . HOH I 8 .   ? 18.972  -10.357 31.353  1.00 33.57  ? 599 HOH A O   1 
HETATM 2517 O  O   . HOH I 8 .   ? 24.782  11.806  23.824  1.00 26.17  ? 600 HOH A O   1 
HETATM 2518 O  O   . HOH I 8 .   ? 13.642  -6.868  32.615  1.00 16.15  ? 601 HOH A O   1 
HETATM 2519 O  O   . HOH I 8 .   ? -4.102  6.413   8.604   1.00 27.27  ? 602 HOH A O   1 
HETATM 2520 O  O   . HOH I 8 .   ? 19.851  3.338   11.522  1.00 23.51  ? 603 HOH A O   1 
HETATM 2521 O  O   . HOH I 8 .   ? 4.916   17.684  23.622  1.00 18.18  ? 604 HOH A O   1 
HETATM 2522 O  O   . HOH I 8 .   ? 26.970  -0.900  6.852   1.00 25.69  ? 605 HOH A O   1 
HETATM 2523 O  O   . HOH I 8 .   ? -2.837  -5.285  0.315   1.00 29.16  ? 606 HOH A O   1 
HETATM 2524 O  O   . HOH I 8 .   ? 4.223   -12.091 26.318  1.00 22.16  ? 607 HOH A O   1 
HETATM 2525 O  O   . HOH I 8 .   ? 24.901  -0.165  5.113   1.00 30.35  ? 608 HOH A O   1 
HETATM 2526 O  O   . HOH I 8 .   ? 16.831  -6.683  31.182  1.00 18.23  ? 609 HOH A O   1 
HETATM 2527 O  O   . HOH I 8 .   ? -5.269  -5.564  30.487  1.00 35.75  ? 610 HOH A O   1 
HETATM 2528 O  O   . HOH I 8 .   ? 20.842  -12.428 22.208  1.00 22.39  ? 611 HOH A O   1 
HETATM 2529 O  O   . HOH I 8 .   ? 12.336  2.531   -6.547  1.00 25.05  ? 612 HOH A O   1 
HETATM 2530 O  O   . HOH I 8 .   ? -1.518  -12.493 11.014  1.00 19.16  ? 613 HOH A O   1 
HETATM 2531 O  O   . HOH I 8 .   ? 16.783  -2.909  11.274  1.00 16.89  ? 614 HOH A O   1 
HETATM 2532 O  O   . HOH I 8 .   ? 23.643  -7.858  29.723  1.00 49.75  ? 615 HOH A O   1 
HETATM 2533 O  O   . HOH I 8 .   ? 29.423  4.896   27.624  1.00 29.54  ? 616 HOH A O   1 
HETATM 2534 O  O   . HOH I 8 .   ? 24.676  4.769   8.266   1.00 30.12  ? 617 HOH A O   1 
HETATM 2535 O  O   . HOH I 8 .   ? 17.858  1.773   10.549  1.00 20.77  ? 618 HOH A O   1 
HETATM 2536 O  O   . HOH I 8 .   ? -4.600  11.376  13.335  1.00 29.89  ? 619 HOH A O   1 
HETATM 2537 O  O   . HOH I 8 .   ? 22.968  -13.708 9.288   1.00 19.51  ? 620 HOH A O   1 
HETATM 2538 O  O   . HOH I 8 .   ? 0.323   10.149  29.924  1.00 32.66  ? 621 HOH A O   1 
HETATM 2539 O  O   . HOH I 8 .   ? 8.280   9.718   28.875  1.00 25.10  ? 622 HOH A O   1 
HETATM 2540 O  O   . HOH I 8 .   ? 13.954  -14.905 1.533   1.00 19.86  ? 623 HOH A O   1 
HETATM 2541 O  O   . HOH I 8 .   ? -4.890  8.022   26.990  1.00 25.07  ? 624 HOH A O   1 
HETATM 2542 O  O   . HOH I 8 .   ? 27.482  7.247   28.757  1.00 35.80  ? 625 HOH A O   1 
HETATM 2543 O  O   . HOH I 8 .   ? 17.132  -13.660 -2.148  1.00 32.31  ? 626 HOH A O   1 
HETATM 2544 O  O   . HOH I 8 .   ? 23.904  -11.447 8.090   1.00 21.51  ? 627 HOH A O   1 
HETATM 2545 O  O   . HOH I 8 .   ? 22.108  6.510   12.089  1.00 22.77  ? 628 HOH A O   1 
HETATM 2546 O  O   . HOH I 8 .   ? 26.598  10.985  21.960  1.00 29.70  ? 629 HOH A O   1 
HETATM 2547 O  O   . HOH I 8 .   ? 2.417   -7.258  34.377  1.00 24.24  ? 630 HOH A O   1 
HETATM 2548 O  O   . HOH I 8 .   ? 6.176   11.177  31.634  1.00 36.77  ? 631 HOH A O   1 
HETATM 2549 O  O   . HOH I 8 .   ? -2.152  1.149   34.347  1.00 25.33  ? 632 HOH A O   1 
HETATM 2550 O  O   . HOH I 8 .   ? 24.535  6.404   10.723  1.00 28.24  ? 633 HOH A O   1 
HETATM 2551 O  O   . HOH I 8 .   ? -3.097  -1.799  29.728  1.00 24.47  ? 634 HOH A O   1 
HETATM 2552 O  O   . HOH I 8 .   ? 27.513  -3.401  27.303  1.00 33.44  ? 635 HOH A O   1 
HETATM 2553 O  O   . HOH I 8 .   ? 22.861  14.284  22.795  1.00 29.05  ? 636 HOH A O   1 
HETATM 2554 O  O   . HOH I 8 .   ? 26.758  -10.745 11.655  1.00 37.05  ? 637 HOH A O   1 
HETATM 2555 O  O   . HOH I 8 .   ? 1.032   -0.333  43.091  1.00 40.35  ? 638 HOH A O   1 
HETATM 2556 O  O   . HOH I 8 .   ? 20.143  5.305   10.077  1.00 36.38  ? 639 HOH A O   1 
HETATM 2557 O  O   . HOH I 8 .   ? -2.754  -1.622  4.028   1.00 30.02  ? 640 HOH A O   1 
HETATM 2558 O  O   . HOH I 8 .   ? 23.147  -12.299 20.745  1.00 34.61  ? 641 HOH A O   1 
HETATM 2559 O  O   . HOH I 8 .   ? 24.449  -11.744 12.218  1.00 31.62  ? 642 HOH A O   1 
HETATM 2560 O  O   . HOH I 8 .   ? 3.782   -14.414 22.005  1.00 25.95  ? 643 HOH A O   1 
HETATM 2561 O  O   . HOH I 8 .   ? 9.297   12.647  0.779   1.00 26.58  ? 644 HOH A O   1 
HETATM 2562 O  O   . HOH I 8 .   ? -4.563  -1.477  31.782  1.00 33.31  ? 645 HOH A O   1 
HETATM 2563 O  O   . HOH I 8 .   ? 20.621  15.810  16.062  1.00 26.63  ? 646 HOH A O   1 
HETATM 2564 O  O   . HOH I 8 .   ? 26.810  -11.995 8.524   1.00 35.59  ? 647 HOH A O   1 
HETATM 2565 O  O   . HOH I 8 .   ? 2.060   19.405  18.925  1.00 27.99  ? 648 HOH A O   1 
HETATM 2566 O  O   . HOH I 8 .   ? 18.959  -2.682  -7.015  1.00 28.08  ? 649 HOH A O   1 
HETATM 2567 O  O   . HOH I 8 .   ? 25.065  -9.939  23.487  1.00 39.76  ? 650 HOH A O   1 
HETATM 2568 O  O   . HOH I 8 .   ? 25.925  -1.554  2.937   1.00 27.36  ? 651 HOH A O   1 
HETATM 2569 O  O   . HOH I 8 .   ? 31.273  -6.610  8.251   1.00 31.28  ? 652 HOH A O   1 
HETATM 2570 O  O   . HOH I 8 .   ? 16.823  8.098   9.390   1.00 27.85  ? 653 HOH A O   1 
HETATM 2571 O  O   . HOH I 8 .   ? 27.645  10.326  18.097  1.00 31.19  ? 654 HOH A O   1 
HETATM 2572 O  O   . HOH I 8 .   ? -6.115  -8.932  22.644  1.00 36.91  ? 655 HOH A O   1 
HETATM 2573 O  O   . HOH I 8 .   ? 2.204   14.037  13.036  1.00 23.19  ? 656 HOH A O   1 
HETATM 2574 O  O   . HOH I 8 .   ? 26.966  2.850   8.560   1.00 23.21  ? 657 HOH A O   1 
HETATM 2575 O  O   . HOH I 8 .   ? 27.225  -9.129  15.452  1.00 39.51  ? 658 HOH A O   1 
HETATM 2576 O  O   . HOH I 8 .   ? -0.787  -12.263 18.790  1.00 32.36  ? 659 HOH A O   1 
HETATM 2577 O  O   . HOH I 8 .   ? 7.448   0.981   -6.218  1.00 34.04  ? 660 HOH A O   1 
HETATM 2578 O  O   . HOH I 8 .   ? -2.948  -0.364  28.777  1.00 24.32  ? 661 HOH A O   1 
HETATM 2579 O  O   . HOH I 8 .   ? -2.181  -9.420  17.060  1.00 28.96  ? 662 HOH A O   1 
HETATM 2580 O  O   . HOH I 8 .   ? 21.432  -7.552  -5.476  1.00 52.47  ? 663 HOH A O   1 
HETATM 2581 O  O   . HOH I 8 .   ? 20.667  -5.310  -7.410  1.00 46.56  ? 664 HOH A O   1 
HETATM 2582 O  O   . HOH I 8 .   ? 23.063  -4.951  -8.134  1.00 39.08  ? 665 HOH A O   1 
HETATM 2583 O  O   . HOH I 8 .   ? 16.594  -4.058  -8.131  1.00 37.77  ? 666 HOH A O   1 
HETATM 2584 O  O   . HOH I 8 .   ? 24.708  -7.059  25.688  1.00 33.74  ? 667 HOH A O   1 
HETATM 2585 O  O   . HOH I 8 .   ? 27.285  -3.589  3.840   1.00 35.76  ? 668 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 4   ? 0.4332 0.3034 0.4930 -0.0353 0.1190  0.1238  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.2606 0.3036 0.2662 -0.0366 0.1425  0.0174  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.2292 0.2114 0.2405 -0.0306 0.0975  -0.0091 4   HIS A C   
4    O  O   . HIS A 4   ? 0.2477 0.3127 0.2795 0.0298  0.1271  0.0432  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.2721 0.5440 0.2992 -0.0082 0.1115  0.1054  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.5634 0.5328 0.4059 -0.0340 -0.2476 -0.0355 4   HIS A CG  
7    N  ND1 . HIS A 4   ? 1.0628 0.9192 0.8851 -0.4298 0.1217  0.0122  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.5375 0.9544 0.7296 -0.2992 -0.3705 0.0364  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 1.5557 1.2487 1.0656 -0.2829 0.1395  -0.1977 4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 1.4412 1.4019 1.1726 -0.1753 0.1968  -0.4483 4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.1713 0.1994 0.2164 -0.0450 0.0461  -0.0021 5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1469 0.1597 0.1867 -0.0272 0.0449  -0.0054 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1475 0.1599 0.1688 -0.0024 0.0370  -0.0023 5   TRP A C   
14   O  O   . TRP A 5   ? 0.1695 0.1775 0.1749 -0.0082 0.0295  0.0148  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1381 0.1542 0.1896 -0.0088 0.0181  -0.0206 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1422 0.1477 0.1605 -0.0185 0.0383  -0.0140 5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.1768 0.1527 0.1818 -0.0091 0.0493  0.0142  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1388 0.1834 0.1202 -0.0135 0.0197  -0.0017 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.1938 0.1764 0.1483 0.0063  0.0381  0.0137  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1589 0.1855 0.1347 0.0258  0.0136  0.0062  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1208 0.1702 0.1456 -0.0227 0.0284  -0.0216 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1713 0.2125 0.1141 0.0220  0.0160  -0.0110 5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1260 0.2055 0.1351 -0.0096 0.0264  -0.0414 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1509 0.2120 0.1300 0.0062  0.0052  -0.0485 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1425 0.1489 0.1550 -0.0073 0.0447  -0.0155 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1527 0.1420 0.1621 -0.0221 0.0211  -0.0148 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1239 0.1508 0.1553 -0.0062 0.0412  -0.0210 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1218 0.1679 0.1508 -0.0068 0.0271  -0.0096 6   GLY A O   
29   N  N   . TYR A 7   ? 0.1583 0.1458 0.1740 -0.0027 0.0482  -0.0253 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1421 0.1424 0.2173 -0.0010 0.0355  -0.0133 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.1489 0.1485 0.2978 0.0013  0.0614  -0.0098 7   TYR A C   
32   O  O   . TYR A 7   ? 0.2035 0.1794 0.3840 0.0098  0.0760  0.0020  7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1319 0.1494 0.1845 -0.0066 0.0315  -0.0209 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1146 0.1395 0.1414 -0.0152 0.0258  -0.0263 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1112 0.1347 0.1590 -0.0302 0.0140  -0.0143 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1359 0.1334 0.1670 -0.0164 0.0292  -0.0131 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1148 0.1227 0.1313 -0.0206 0.0212  -0.0142 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1407 0.1442 0.1264 -0.0307 0.0154  -0.0143 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1096 0.1222 0.1297 -0.0165 0.0092  -0.0076 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1421 0.1306 0.1229 -0.0051 0.0094  -0.0126 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.1649 0.1779 0.2709 -0.0001 0.0649  -0.0513 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.2561 0.2049 0.3169 -0.0176 0.0615  -0.0603 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.1693 0.1737 0.2401 0.0151  0.0461  -0.0401 8   GLY A C   
44   O  O   . GLY A 8   ? 0.2379 0.2973 0.3339 0.0348  0.0755  -0.0082 8   GLY A O   
45   N  N   . LYS A 9   ? 0.2678 0.1923 0.5600 0.0666  0.0881  0.0012  9   LYS A N   
46   C  CA  . LYS A 9   ? 0.2657 0.2092 0.5181 0.0083  0.0189  0.0313  9   LYS A CA  
47   C  C   . LYS A 9   ? 0.2056 0.4857 0.4269 -0.1403 0.0299  0.1058  9   LYS A C   
48   O  O   . LYS A 9   ? 0.2680 0.3082 0.3923 0.0709  0.0247  -0.0509 9   LYS A O   
49   N  N   . HIS A 10  ? 0.1353 0.2208 0.3055 0.0094  0.0802  -0.0223 10  HIS A N   
50   C  CA  . HIS A 10  ? 0.1198 0.2372 0.2223 0.0147  0.0174  -0.0395 10  HIS A CA  
51   C  C   . HIS A 10  ? 0.1444 0.2148 0.2380 0.0038  0.0262  -0.0060 10  HIS A C   
52   O  O   . HIS A 10  ? 0.0996 0.2998 0.2937 0.0263  0.0142  -0.0829 10  HIS A O   
53   C  CB  . HIS A 10  ? 0.1641 0.2351 0.2324 0.0078  0.0447  -0.0679 10  HIS A CB  
54   C  CG  . HIS A 10  ? 0.1613 0.2694 0.2255 -0.0196 0.0178  -0.0551 10  HIS A CG  
55   N  ND1 . HIS A 10  ? 0.1932 0.2459 0.2261 -0.0003 0.0223  0.0098  10  HIS A ND1 
56   C  CD2 . HIS A 10  ? 0.2304 0.2314 0.2594 0.0060  0.0357  -0.0662 10  HIS A CD2 
57   C  CE1 . HIS A 10  ? 0.1712 0.1870 0.2585 -0.0019 0.0249  -0.0482 10  HIS A CE1 
58   N  NE2 . HIS A 10  ? 0.2230 0.2712 0.2985 -0.0137 0.0313  -0.0684 10  HIS A NE2 
59   N  N   . ASN A 11  ? 0.1363 0.1906 0.2013 0.0136  0.0509  -0.0194 11  ASN A N   
60   C  CA  . ASN A 11  ? 0.1397 0.1828 0.1904 0.0243  0.0469  -0.0178 11  ASN A CA  
61   C  C   . ASN A 11  ? 0.1288 0.1506 0.1648 0.0076  0.0271  -0.0186 11  ASN A C   
62   O  O   . ASN A 11  ? 0.1530 0.1787 0.1796 0.0115  0.0535  -0.0059 11  ASN A O   
63   C  CB  . ASN A 11  ? 0.1420 0.2137 0.1885 0.0057  0.0627  -0.0040 11  ASN A CB  
64   C  CG  . ASN A 11  ? 0.1510 0.1828 0.1861 0.0219  0.0346  -0.0166 11  ASN A CG  
65   O  OD1 . ASN A 11  ? 0.1658 0.2263 0.2002 -0.0068 0.0244  -0.0163 11  ASN A OD1 
66   N  ND2 . ASN A 11  ? 0.1949 0.2687 0.2198 0.0252  0.0603  0.0252  11  ASN A ND2 
67   N  N   . GLY A 12  ? 0.1356 0.1737 0.1623 0.0070  0.0496  -0.0003 12  GLY A N   
68   C  CA  . GLY A 12  ? 0.1187 0.2028 0.1764 0.0160  0.0505  -0.0104 12  GLY A CA  
69   C  C   . GLY A 12  ? 0.1350 0.1432 0.1582 0.0041  0.0222  0.0070  12  GLY A C   
70   O  O   . GLY A 12  ? 0.1157 0.1580 0.1674 0.0199  0.0178  0.0040  12  GLY A O   
71   N  N   . PRO A 13  ? 0.1245 0.1421 0.1617 0.0057  0.0397  -0.0091 13  PRO A N   
72   C  CA  . PRO A 13  ? 0.1181 0.1279 0.1722 -0.0010 0.0340  -0.0109 13  PRO A CA  
73   C  C   . PRO A 13  ? 0.1385 0.1366 0.1398 0.0055  0.0377  -0.0041 13  PRO A C   
74   O  O   . PRO A 13  ? 0.1184 0.1666 0.1694 -0.0052 0.0260  -0.0200 13  PRO A O   
75   C  CB  . PRO A 13  ? 0.1375 0.1457 0.1711 -0.0221 0.0439  -0.0023 13  PRO A CB  
76   C  CG  . PRO A 13  ? 0.1405 0.1542 0.1648 -0.0148 0.0251  -0.0109 13  PRO A CG  
77   C  CD  . PRO A 13  ? 0.1175 0.1729 0.1560 -0.0057 0.0421  0.0031  13  PRO A CD  
78   N  N   . GLU A 14  ? 0.1529 0.1377 0.1758 0.0068  0.0116  0.0173  14  GLU A N   
79   C  CA  . GLU A 14  ? 0.1938 0.1473 0.1924 0.0114  0.0245  0.0230  14  GLU A CA  
80   C  C   . GLU A 14  ? 0.1293 0.1771 0.1743 0.0557  -0.0060 0.0044  14  GLU A C   
81   O  O   . GLU A 14  ? 0.1607 0.1796 0.1962 0.0504  -0.0032 0.0181  14  GLU A O   
82   C  CB  . GLU A 14  ? 0.3079 0.1871 0.2531 0.0362  -0.0222 0.0483  14  GLU A CB  
83   C  CG  . GLU A 14  ? 0.2102 0.2703 0.2901 0.0054  -0.0136 0.0288  14  GLU A CG  
84   C  CD  . GLU A 14  ? 0.3237 0.2834 0.3772 0.0883  -0.0366 -0.0034 14  GLU A CD  
85   O  OE1 . GLU A 14  ? 0.2759 0.2184 0.3551 0.0697  -0.0604 -0.1120 14  GLU A OE1 
86   O  OE2 . GLU A 14  ? 0.5051 0.2204 0.3307 0.0185  0.0302  -0.0351 14  GLU A OE2 
87   N  N   . HIS A 15  ? 0.1202 0.1354 0.1753 0.0186  0.0203  0.0093  15  HIS A N   
88   C  CA  . HIS A 15  ? 0.1121 0.1590 0.1629 0.0192  0.0062  0.0020  15  HIS A CA  
89   C  C   . HIS A 15  ? 0.0992 0.1401 0.1807 0.0167  0.0120  0.0010  15  HIS A C   
90   O  O   . HIS A 15  ? 0.0856 0.1583 0.1949 0.0170  0.0144  0.0137  15  HIS A O   
91   C  CB  . HIS A 15  ? 0.1094 0.1763 0.2062 0.0357  0.0103  0.0052  15  HIS A CB  
92   C  CG  . HIS A 15  ? 0.1495 0.2014 0.2110 0.0447  0.0125  0.0100  15  HIS A CG  
93   N  ND1 . HIS A 15  ? 0.1471 0.2748 0.2393 0.0883  0.0063  -0.0351 15  HIS A ND1 
94   C  CD2 . HIS A 15  ? 0.2222 0.1811 0.2500 0.0851  0.0196  -0.0052 15  HIS A CD2 
95   C  CE1 . HIS A 15  ? 0.1992 0.2754 0.2475 0.0923  0.0196  -0.0676 15  HIS A CE1 
96   N  NE2 . HIS A 15  ? 0.2448 0.2451 0.3046 0.1238  -0.0015 -0.0621 15  HIS A NE2 
97   N  N   . TRP A 16  ? 0.0819 0.1412 0.1692 0.0182  0.0164  0.0148  16  TRP A N   
98   C  CA  . TRP A 16  ? 0.0782 0.1328 0.1720 0.0073  0.0052  -0.0043 16  TRP A CA  
99   C  C   . TRP A 16  ? 0.0711 0.1457 0.1717 0.0096  0.0038  0.0113  16  TRP A C   
100  O  O   . TRP A 16  ? 0.0864 0.1367 0.1796 -0.0048 -0.0119 0.0030  16  TRP A O   
101  C  CB  . TRP A 16  ? 0.0696 0.1480 0.1773 0.0120  0.0020  -0.0087 16  TRP A CB  
102  C  CG  . TRP A 16  ? 0.0974 0.1200 0.1448 0.0010  -0.0010 -0.0070 16  TRP A CG  
103  C  CD1 . TRP A 16  ? 0.1118 0.1430 0.1386 0.0131  0.0040  0.0003  16  TRP A CD1 
104  C  CD2 . TRP A 16  ? 0.0861 0.1148 0.1500 0.0005  0.0163  0.0020  16  TRP A CD2 
105  N  NE1 . TRP A 16  ? 0.0976 0.1403 0.1493 -0.0012 0.0262  -0.0096 16  TRP A NE1 
106  C  CE2 . TRP A 16  ? 0.0996 0.1186 0.1402 0.0098  0.0167  0.0035  16  TRP A CE2 
107  C  CE3 . TRP A 16  ? 0.0803 0.1200 0.1491 -0.0015 0.0194  0.0007  16  TRP A CE3 
108  C  CZ2 . TRP A 16  ? 0.0979 0.1168 0.1356 -0.0017 0.0120  -0.0038 16  TRP A CZ2 
109  C  CZ3 . TRP A 16  ? 0.0896 0.1196 0.1429 -0.0076 0.0166  -0.0012 16  TRP A CZ3 
110  C  CH2 . TRP A 16  ? 0.0908 0.1218 0.1460 -0.0081 0.0166  0.0007  16  TRP A CH2 
111  N  N   . HIS A 17  ? 0.0767 0.1469 0.1659 -0.0012 -0.0013 -0.0035 17  HIS A N   
112  C  CA  . HIS A 17  ? 0.0856 0.1465 0.1895 0.0093  -0.0015 0.0057  17  HIS A CA  
113  C  C   . HIS A 17  ? 0.1024 0.1589 0.1811 -0.0070 -0.0091 0.0055  17  HIS A C   
114  O  O   . HIS A 17  ? 0.0957 0.1814 0.1952 -0.0012 -0.0193 0.0006  17  HIS A O   
115  C  CB  . HIS A 17  ? 0.0777 0.1890 0.1825 0.0070  0.0017  0.0098  17  HIS A CB  
116  C  CG  . HIS A 17  ? 0.1028 0.1856 0.1807 0.0038  -0.0121 0.0289  17  HIS A CG  
117  N  ND1 . HIS A 17  ? 0.1164 0.2256 0.2436 0.0037  -0.0293 0.0302  17  HIS A ND1 
118  C  CD2 . HIS A 17  ? 0.1203 0.1847 0.1960 0.0328  -0.0063 0.0226  17  HIS A CD2 
119  C  CE1 . HIS A 17  ? 0.1265 0.2294 0.2231 0.0357  -0.0138 0.0167  17  HIS A CE1 
120  N  NE2 . HIS A 17  ? 0.1379 0.1955 0.2285 0.0373  0.0023  0.0423  17  HIS A NE2 
121  N  N   . LYS A 18  ? 0.0763 0.1776 0.1870 0.0003  -0.0020 0.0076  18  LYS A N   
122  C  CA  . LYS A 18  ? 0.0791 0.2196 0.2037 0.0026  -0.0026 0.0247  18  LYS A CA  
123  C  C   . LYS A 18  ? 0.1106 0.1846 0.2214 -0.0161 -0.0313 0.0136  18  LYS A C   
124  O  O   . LYS A 18  ? 0.1187 0.2432 0.3052 -0.0573 -0.0461 0.0441  18  LYS A O   
125  C  CB  . LYS A 18  ? 0.0910 0.2134 0.2322 0.0171  0.0068  0.0351  18  LYS A CB  
126  C  CG  . LYS A 18  ? 0.1328 0.2269 0.1968 0.0460  0.0076  0.0328  18  LYS A CG  
127  C  CD  . LYS A 18  ? 0.1395 0.2240 0.2094 0.0579  -0.0027 0.0381  18  LYS A CD  
128  C  CE  . LYS A 18  ? 0.1441 0.2337 0.2220 0.0215  -0.0082 0.0324  18  LYS A CE  
129  N  NZ  . LYS A 18  ? 0.1067 0.2469 0.2436 0.0627  0.0146  0.0344  18  LYS A NZ  
130  N  N   . ASP A 19  ? 0.0860 0.1661 0.1886 -0.0024 0.0003  0.0088  19  ASP A N   
131  C  CA  . ASP A 19  ? 0.1216 0.1705 0.2134 -0.0110 0.0071  0.0232  19  ASP A CA  
132  C  C   . ASP A 19  ? 0.1010 0.1430 0.2161 -0.0017 0.0146  0.0102  19  ASP A C   
133  O  O   . ASP A 19  ? 0.1411 0.1553 0.2448 -0.0085 0.0348  0.0267  19  ASP A O   
134  C  CB  . ASP A 19  ? 0.1405 0.2264 0.1996 0.0215  -0.0181 0.0333  19  ASP A CB  
135  C  CG  . ASP A 19  ? 0.2457 0.1811 0.2558 0.0097  0.0414  0.0092  19  ASP A CG  
136  O  OD1 . ASP A 19  ? 0.2263 0.2266 0.3346 0.0034  0.0197  0.0441  19  ASP A OD1 
137  O  OD2 . ASP A 19  ? 0.1888 0.2469 0.2633 0.0089  0.0288  -0.0024 19  ASP A OD2 
138  N  N   . PHE A 20  ? 0.0780 0.1557 0.2064 -0.0148 0.0003  0.0076  20  PHE A N   
139  C  CA  . PHE A 20  ? 0.0943 0.1545 0.1967 -0.0125 0.0024  -0.0062 20  PHE A CA  
140  C  C   . PHE A 20  ? 0.0771 0.1702 0.2064 -0.0085 0.0125  -0.0013 20  PHE A C   
141  O  O   . PHE A 20  ? 0.1089 0.1450 0.1855 -0.0089 0.0027  0.0000  20  PHE A O   
142  C  CB  . PHE A 20  ? 0.0820 0.1611 0.2019 -0.0118 0.0043  0.0062  20  PHE A CB  
143  C  CG  . PHE A 20  ? 0.0766 0.1529 0.2011 -0.0186 0.0035  0.0164  20  PHE A CG  
144  C  CD1 . PHE A 20  ? 0.1207 0.1801 0.2131 -0.0077 -0.0005 0.0238  20  PHE A CD1 
145  C  CD2 . PHE A 20  ? 0.1175 0.1863 0.1931 -0.0164 0.0035  0.0017  20  PHE A CD2 
146  C  CE1 . PHE A 20  ? 0.1049 0.2134 0.2215 -0.0130 0.0013  0.0329  20  PHE A CE1 
147  C  CE2 . PHE A 20  ? 0.1103 0.1942 0.2066 -0.0144 0.0037  0.0076  20  PHE A CE2 
148  C  CZ  . PHE A 20  ? 0.1011 0.2384 0.2063 -0.0288 0.0205  0.0241  20  PHE A CZ  
149  N  N   . PRO A 21  ? 0.1096 0.1764 0.2093 -0.0204 -0.0040 0.0196  21  PRO A N   
150  C  CA  . PRO A 21  ? 0.1046 0.2020 0.2037 -0.0275 -0.0255 0.0017  21  PRO A CA  
151  C  C   . PRO A 21  ? 0.1030 0.1563 0.1915 -0.0152 -0.0197 -0.0141 21  PRO A C   
152  O  O   . PRO A 21  ? 0.1071 0.1836 0.1985 -0.0097 -0.0366 -0.0097 21  PRO A O   
153  C  CB  . PRO A 21  ? 0.1141 0.2879 0.2779 -0.0957 -0.0326 0.0340  21  PRO A CB  
154  C  CG  . PRO A 21  ? 0.2815 0.2861 0.3183 -0.1336 -0.0706 0.0199  21  PRO A CG  
155  C  CD  . PRO A 21  ? 0.1204 0.2267 0.2296 -0.0568 -0.0093 0.0289  21  PRO A CD  
156  N  N   A ILE A 22  ? 0.0957 0.1480 0.1918 -0.0129 -0.0114 -0.0102 22  ILE A N   
157  N  N   B ILE A 22  ? 0.0989 0.1474 0.1855 -0.0182 -0.0297 -0.0197 22  ILE A N   
158  C  CA  A ILE A 22  ? 0.0813 0.1476 0.1766 -0.0082 0.0074  -0.0087 22  ILE A CA  
159  C  CA  B ILE A 22  ? 0.1074 0.1516 0.1464 -0.0129 -0.0065 -0.0265 22  ILE A CA  
160  C  C   A ILE A 22  ? 0.0948 0.1477 0.1513 -0.0089 -0.0263 -0.0172 22  ILE A C   
161  C  C   B ILE A 22  ? 0.1005 0.1420 0.1599 -0.0046 -0.0236 -0.0175 22  ILE A C   
162  O  O   A ILE A 22  ? 0.0879 0.1465 0.1872 -0.0087 -0.0010 -0.0119 22  ILE A O   
163  O  O   B ILE A 22  ? 0.0866 0.1495 0.1908 -0.0104 -0.0038 -0.0161 22  ILE A O   
164  C  CB  A ILE A 22  ? 0.0912 0.1324 0.1607 -0.0333 -0.0160 0.0017  22  ILE A CB  
165  C  CB  B ILE A 22  ? 0.1159 0.1613 0.1391 -0.0098 -0.0206 0.0006  22  ILE A CB  
166  C  CG1 A ILE A 22  ? 0.0912 0.1393 0.1484 0.0054  -0.0124 -0.0184 22  ILE A CG1 
167  C  CG1 B ILE A 22  ? 0.1357 0.1521 0.1796 -0.0126 0.0027  -0.0237 22  ILE A CG1 
168  C  CG2 A ILE A 22  ? 0.0944 0.1598 0.1620 -0.0109 -0.0183 0.0164  22  ILE A CG2 
169  C  CG2 B ILE A 22  ? 0.1212 0.1362 0.1331 -0.0551 -0.0292 0.0153  22  ILE A CG2 
170  C  CD1 A ILE A 22  ? 0.1075 0.1325 0.1871 0.0051  -0.0071 -0.0122 22  ILE A CD1 
171  C  CD1 B ILE A 22  ? 0.1655 0.2702 0.2322 0.0074  -0.0136 -0.0313 22  ILE A CD1 
172  N  N   . ALA A 23  ? 0.1067 0.1362 0.1612 -0.0119 -0.0223 -0.0110 23  ALA A N   
173  C  CA  . ALA A 23  ? 0.1032 0.1257 0.1527 -0.0049 -0.0027 -0.0129 23  ALA A CA  
174  C  C   . ALA A 23  ? 0.1071 0.1425 0.1916 0.0052  -0.0086 -0.0174 23  ALA A C   
175  O  O   . ALA A 23  ? 0.1090 0.1469 0.1807 -0.0140 -0.0054 -0.0076 23  ALA A O   
176  C  CB  . ALA A 23  ? 0.0986 0.1383 0.1817 -0.0097 -0.0054 -0.0164 23  ALA A CB  
177  N  N   . LYS A 24  ? 0.1227 0.1568 0.1565 -0.0023 -0.0055 -0.0046 24  LYS A N   
178  C  CA  . LYS A 24  ? 0.1066 0.1877 0.1790 -0.0077 -0.0055 0.0109  24  LYS A CA  
179  C  C   . LYS A 24  ? 0.1447 0.1931 0.1571 -0.0188 -0.0285 -0.0038 24  LYS A C   
180  O  O   . LYS A 24  ? 0.1513 0.2440 0.1914 -0.0051 -0.0348 -0.0142 24  LYS A O   
181  C  CB  . LYS A 24  ? 0.1118 0.1942 0.1952 0.0060  -0.0148 0.0125  24  LYS A CB  
182  C  CG  . LYS A 24  ? 0.1498 0.2372 0.1841 0.0310  -0.0146 0.0237  24  LYS A CG  
183  C  CD  . LYS A 24  ? 0.1553 0.3027 0.2861 0.0485  0.0131  0.0046  24  LYS A CD  
184  C  CE  . LYS A 24  ? 0.1985 0.3269 0.2980 0.0784  0.0181  0.0339  24  LYS A CE  
185  N  NZ  . LYS A 24  ? 0.3328 0.3206 0.4384 -0.0173 0.0417  -0.0496 24  LYS A NZ  
186  N  N   . GLY A 25  ? 0.1356 0.1731 0.1762 0.0052  -0.0185 -0.0153 25  GLY A N   
187  C  CA  . GLY A 25  ? 0.1333 0.2067 0.1973 -0.0216 -0.0063 -0.0494 25  GLY A CA  
188  C  C   . GLY A 25  ? 0.1234 0.1925 0.1570 -0.0054 -0.0273 -0.0196 25  GLY A C   
189  O  O   . GLY A 25  ? 0.1359 0.2118 0.1624 -0.0020 -0.0242 -0.0147 25  GLY A O   
190  N  N   . GLU A 26  ? 0.1307 0.2240 0.1457 0.0019  -0.0423 -0.0362 26  GLU A N   
191  C  CA  . GLU A 26  ? 0.1622 0.2396 0.1207 -0.0091 -0.0216 -0.0353 26  GLU A CA  
192  C  C   . GLU A 26  ? 0.1590 0.1701 0.1331 0.0074  -0.0183 -0.0232 26  GLU A C   
193  O  O   . GLU A 26  ? 0.1808 0.2226 0.1193 -0.0015 -0.0401 -0.0015 26  GLU A O   
194  C  CB  . GLU A 26  ? 0.1993 0.3219 0.1855 -0.0379 -0.0571 -0.1098 26  GLU A CB  
195  C  CG  . GLU A 26  ? 0.2773 0.3684 0.1845 -0.0331 -0.0362 -0.0778 26  GLU A CG  
196  C  CD  . GLU A 26  ? 0.4399 0.4528 0.2351 -0.0333 -0.1064 -0.0083 26  GLU A CD  
197  O  OE1 . GLU A 26  ? 0.3943 0.5080 0.3461 0.0248  -0.0967 0.0410  26  GLU A OE1 
198  O  OE2 . GLU A 26  ? 0.4176 0.5209 0.4819 0.0068  -0.1449 0.0372  26  GLU A OE2 
199  N  N   . ARG A 27  ? 0.1225 0.1490 0.1202 -0.0021 -0.0256 -0.0209 27  ARG A N   
200  C  CA  . ARG A 27  ? 0.1044 0.1351 0.1184 0.0031  -0.0162 -0.0176 27  ARG A CA  
201  C  C   . ARG A 27  ? 0.1066 0.1202 0.1018 -0.0031 -0.0082 -0.0173 27  ARG A C   
202  O  O   . ARG A 27  ? 0.1083 0.1316 0.1119 0.0081  -0.0131 -0.0160 27  ARG A O   
203  C  CB  . ARG A 27  ? 0.1850 0.1731 0.1208 0.0087  -0.0225 -0.0386 27  ARG A CB  
204  C  CG  . ARG A 27  ? 0.1777 0.2360 0.1635 -0.0137 0.0027  -0.0233 27  ARG A CG  
205  C  CD  . ARG A 27  ? 0.2901 0.2946 0.1728 0.0386  -0.0310 -0.0355 27  ARG A CD  
206  N  NE  . ARG A 27  ? 0.2263 0.1978 0.1588 0.0237  0.0208  -0.0143 27  ARG A NE  
207  C  CZ  . ARG A 27  ? 0.1733 0.2017 0.1349 0.0390  0.0219  0.0178  27  ARG A CZ  
208  N  NH1 . ARG A 27  ? 0.1765 0.2041 0.1968 0.0219  -0.0100 -0.1178 27  ARG A NH1 
209  N  NH2 . ARG A 27  ? 0.1792 0.1659 0.1870 -0.0114 -0.0017 -0.0304 27  ARG A NH2 
210  N  N   . GLN A 28  ? 0.0996 0.1155 0.0973 -0.0041 -0.0115 -0.0178 28  GLN A N   
211  C  CA  . GLN A 28  ? 0.0975 0.1116 0.1010 -0.0024 -0.0074 -0.0104 28  GLN A CA  
212  C  C   . GLN A 28  ? 0.0956 0.0983 0.0997 -0.0082 -0.0076 -0.0043 28  GLN A C   
213  O  O   . GLN A 28  ? 0.1187 0.1268 0.0983 -0.0137 -0.0156 -0.0034 28  GLN A O   
214  C  CB  . GLN A 28  ? 0.0886 0.1271 0.1157 -0.0020 -0.0094 -0.0129 28  GLN A CB  
215  C  CG  . GLN A 28  ? 0.0979 0.1331 0.1280 -0.0052 -0.0108 -0.0255 28  GLN A CG  
216  C  CD  . GLN A 28  ? 0.0802 0.1162 0.1240 -0.0102 -0.0136 -0.0177 28  GLN A CD  
217  O  OE1 . GLN A 28  ? 0.0983 0.1148 0.1212 -0.0099 0.0013  -0.0203 28  GLN A OE1 
218  N  NE2 . GLN A 28  ? 0.0829 0.1178 0.1407 -0.0046 -0.0126 -0.0183 28  GLN A NE2 
219  N  N   . SER A 29  ? 0.0887 0.0951 0.0891 0.0031  -0.0041 -0.0156 29  SER A N   
220  C  CA  . SER A 29  ? 0.0842 0.0887 0.1017 -0.0020 -0.0060 -0.0091 29  SER A CA  
221  C  C   . SER A 29  ? 0.0872 0.0923 0.0838 0.0027  -0.0051 0.0046  29  SER A C   
222  O  O   . SER A 29  ? 0.0874 0.0961 0.1044 -0.0057 0.0031  -0.0086 29  SER A O   
223  C  CB  . SER A 29  ? 0.0861 0.0913 0.0961 0.0074  0.0012  -0.0105 29  SER A CB  
224  O  OG  . SER A 29  ? 0.0833 0.0926 0.1062 0.0031  0.0012  -0.0155 29  SER A OG  
225  N  N   . PRO A 30  ? 0.0773 0.0873 0.0879 -0.0041 -0.0008 -0.0063 30  PRO A N   
226  C  CA  . PRO A 30  ? 0.0751 0.0869 0.0970 -0.0068 -0.0043 0.0015  30  PRO A CA  
227  C  C   . PRO A 30  ? 0.0803 0.0883 0.0912 0.0043  0.0003  -0.0041 30  PRO A C   
228  O  O   . PRO A 30  ? 0.0861 0.1006 0.1008 0.0041  -0.0066 -0.0026 30  PRO A O   
229  C  CB  . PRO A 30  ? 0.0917 0.0952 0.0903 0.0017  -0.0015 -0.0129 30  PRO A CB  
230  C  CG  . PRO A 30  ? 0.0935 0.0936 0.0991 -0.0037 0.0000  -0.0041 30  PRO A CG  
231  C  CD  . PRO A 30  ? 0.0966 0.0909 0.0982 0.0024  -0.0012 -0.0127 30  PRO A CD  
232  N  N   . VAL A 31  ? 0.0925 0.0927 0.0938 0.0043  0.0015  0.0024  31  VAL A N   
233  C  CA  . VAL A 31  ? 0.1085 0.0931 0.0914 0.0116  -0.0001 0.0104  31  VAL A CA  
234  C  C   . VAL A 31  ? 0.1024 0.0982 0.0970 0.0179  -0.0060 0.0007  31  VAL A C   
235  O  O   . VAL A 31  ? 0.1026 0.1023 0.1024 0.0001  -0.0017 0.0114  31  VAL A O   
236  C  CB  . VAL A 31  ? 0.1123 0.1114 0.0954 0.0052  0.0015  -0.0030 31  VAL A CB  
237  C  CG1 . VAL A 31  ? 0.1398 0.1053 0.1168 -0.0121 0.0020  -0.0125 31  VAL A CG1 
238  C  CG2 . VAL A 31  ? 0.1133 0.1239 0.1146 0.0070  0.0174  -0.0024 31  VAL A CG2 
239  N  N   . ASP A 32  ? 0.1152 0.1002 0.0965 0.0060  -0.0006 0.0096  32  ASP A N   
240  C  CA  . ASP A 32  ? 0.1278 0.0997 0.1050 0.0102  0.0086  0.0122  32  ASP A CA  
241  C  C   . ASP A 32  ? 0.1349 0.1061 0.0913 0.0017  0.0027  0.0044  32  ASP A C   
242  O  O   . ASP A 32  ? 0.1307 0.1475 0.1171 -0.0031 0.0043  -0.0113 32  ASP A O   
243  C  CB  . ASP A 32  ? 0.1442 0.1020 0.1290 0.0163  -0.0015 0.0241  32  ASP A CB  
244  C  CG  . ASP A 32  ? 0.1515 0.1202 0.1136 0.0125  -0.0065 0.0278  32  ASP A CG  
245  O  OD1 . ASP A 32  ? 0.1439 0.1150 0.1206 0.0063  -0.0043 0.0217  32  ASP A OD1 
246  O  OD2 . ASP A 32  ? 0.2240 0.1595 0.1283 -0.0244 -0.0129 0.0439  32  ASP A OD2 
247  N  N   . ILE A 33  ? 0.1234 0.1080 0.1014 0.0114  0.0121  0.0166  33  ILE A N   
248  C  CA  . ILE A 33  ? 0.1238 0.1190 0.1022 0.0080  0.0157  0.0091  33  ILE A CA  
249  C  C   . ILE A 33  ? 0.1402 0.1177 0.1273 0.0192  0.0223  0.0116  33  ILE A C   
250  O  O   . ILE A 33  ? 0.1512 0.1240 0.1240 0.0000  0.0214  0.0263  33  ILE A O   
251  C  CB  . ILE A 33  ? 0.1218 0.1238 0.1250 0.0159  0.0209  0.0149  33  ILE A CB  
252  C  CG1 . ILE A 33  ? 0.1280 0.1163 0.1407 0.0143  -0.0074 0.0273  33  ILE A CG1 
253  C  CG2 . ILE A 33  ? 0.1323 0.1530 0.1456 0.0137  0.0304  0.0163  33  ILE A CG2 
254  C  CD1 . ILE A 33  ? 0.1177 0.1500 0.1694 0.0087  -0.0027 0.0243  33  ILE A CD1 
255  N  N   A ASP A 34  ? 0.1886 0.1657 0.1008 0.0377  0.0255  0.0239  34  ASP A N   
256  N  N   B ASP A 34  ? 0.1582 0.1281 0.1078 0.0099  0.0164  0.0183  34  ASP A N   
257  C  CA  A ASP A 34  ? 0.1711 0.1392 0.1208 0.0261  0.0143  0.0238  34  ASP A CA  
258  C  CA  B ASP A 34  ? 0.1641 0.1480 0.0954 0.0249  0.0270  0.0465  34  ASP A CA  
259  C  C   A ASP A 34  ? 0.1929 0.1598 0.1063 0.0390  0.0289  0.0496  34  ASP A C   
260  C  C   B ASP A 34  ? 0.1944 0.1624 0.1206 0.0480  0.0370  0.0436  34  ASP A C   
261  O  O   A ASP A 34  ? 0.1530 0.1754 0.1314 0.0223  0.0476  0.0154  34  ASP A O   
262  O  O   B ASP A 34  ? 0.1451 0.1912 0.1454 0.0320  0.0174  0.0249  34  ASP A O   
263  C  CB  A ASP A 34  ? 0.2239 0.1477 0.1061 -0.0030 -0.0020 0.0173  34  ASP A CB  
264  C  CB  B ASP A 34  ? 0.1784 0.1482 0.1181 0.0137  0.0241  0.0023  34  ASP A CB  
265  C  CG  A ASP A 34  ? 0.2107 0.1782 0.1618 0.0289  0.0089  0.0315  34  ASP A CG  
266  C  CG  B ASP A 34  ? 0.2238 0.1823 0.1641 0.0230  0.0132  0.0447  34  ASP A CG  
267  O  OD1 A ASP A 34  ? 0.2119 0.1729 0.1298 0.0219  0.0140  0.0659  34  ASP A OD1 
268  O  OD1 B ASP A 34  ? 0.3140 0.2213 0.1855 0.0842  0.0299  0.0657  34  ASP A OD1 
269  O  OD2 A ASP A 34  ? 0.2664 0.3120 0.2434 0.0068  -0.0505 0.1501  34  ASP A OD2 
270  O  OD2 B ASP A 34  ? 0.2716 0.2414 0.1917 0.0179  0.0427  0.0275  34  ASP A OD2 
271  N  N   . THR A 35  ? 0.1787 0.1714 0.1456 0.0350  0.0520  0.0538  35  THR A N   
272  C  CA  . THR A 35  ? 0.1697 0.1988 0.1704 0.0469  0.0537  0.0746  35  THR A CA  
273  C  C   . THR A 35  ? 0.1890 0.1547 0.1568 0.0472  0.0562  0.0331  35  THR A C   
274  O  O   . THR A 35  ? 0.2203 0.2090 0.1997 0.0706  0.0577  0.0313  35  THR A O   
275  C  CB  . THR A 35  ? 0.1937 0.2046 0.2159 0.0401  0.0292  0.0746  35  THR A CB  
276  O  OG1 . THR A 35  ? 0.2145 0.2240 0.1967 0.0348  0.0625  0.0628  35  THR A OG1 
277  C  CG2 . THR A 35  ? 0.2267 0.2339 0.2073 0.0687  0.0412  0.0741  35  THR A CG2 
278  N  N   . HIS A 36  ? 0.2490 0.1738 0.1507 0.0505  0.0645  0.0667  36  HIS A N   
279  C  CA  . HIS A 36  ? 0.2815 0.2125 0.1361 0.0253  0.0538  0.0615  36  HIS A CA  
280  C  C   . HIS A 36  ? 0.3217 0.2606 0.1184 -0.0122 0.0700  0.0478  36  HIS A C   
281  O  O   . HIS A 36  ? 0.2752 0.3300 0.1532 0.0935  0.0104  0.0546  36  HIS A O   
282  C  CB  . HIS A 36  ? 0.3314 0.2477 0.1416 0.0121  0.0244  0.1071  36  HIS A CB  
283  C  CG  . HIS A 36  ? 0.3084 0.1844 0.1565 0.0081  -0.0232 0.0553  36  HIS A CG  
284  N  ND1 . HIS A 36  ? 0.4004 0.2287 0.2707 0.0087  -0.0962 0.1010  36  HIS A ND1 
285  C  CD2 . HIS A 36  ? 0.3034 0.2698 0.2143 -0.0230 -0.0107 0.0685  36  HIS A CD2 
286  C  CE1 . HIS A 36  ? 0.3264 0.2436 0.2989 0.0346  -0.0342 0.0688  36  HIS A CE1 
287  N  NE2 . HIS A 36  ? 0.5188 0.3016 0.3465 -0.0364 -0.0452 0.0860  36  HIS A NE2 
288  N  N   . THR A 37  ? 0.3152 0.1763 0.1896 0.0571  0.0839  0.0460  37  THR A N   
289  C  CA  . THR A 37  ? 0.2777 0.2515 0.1515 0.0873  0.0450  0.0626  37  THR A CA  
290  C  C   . THR A 37  ? 0.2185 0.2132 0.1833 0.0768  0.0445  0.0038  37  THR A C   
291  O  O   . THR A 37  ? 0.3054 0.2333 0.1994 0.0668  -0.0113 0.0131  37  THR A O   
292  C  CB  . THR A 37  ? 0.3795 0.3740 0.2202 0.1385  -0.0298 0.0148  37  THR A CB  
293  O  OG1 . THR A 37  ? 0.4041 0.3197 0.2228 0.0945  0.0060  0.0630  37  THR A OG1 
294  C  CG2 . THR A 37  ? 0.5454 0.2890 0.4075 0.2108  -0.1388 -0.0702 37  THR A CG2 
295  N  N   . ALA A 38  ? 0.2739 0.1879 0.1350 0.0653  0.0450  0.0460  38  ALA A N   
296  C  CA  . ALA A 38  ? 0.2119 0.1756 0.1310 0.0463  0.0465  0.0366  38  ALA A CA  
297  C  C   . ALA A 38  ? 0.1952 0.1693 0.1974 0.0225  0.0661  0.0507  38  ALA A C   
298  O  O   . ALA A 38  ? 0.3052 0.1984 0.2506 0.0185  0.0974  0.0430  38  ALA A O   
299  C  CB  . ALA A 38  ? 0.2041 0.1925 0.1515 0.0403  0.0313  0.0109  38  ALA A CB  
300  N  N   . LYS A 39  ? 0.1850 0.1909 0.1381 0.0441  0.0126  0.0159  39  LYS A N   
301  C  CA  . LYS A 39  ? 0.2221 0.2340 0.1171 0.0702  0.0241  0.0076  39  LYS A CA  
302  C  C   . LYS A 39  ? 0.1912 0.1791 0.1536 0.0483  0.0579  0.0184  39  LYS A C   
303  O  O   . LYS A 39  ? 0.1764 0.2011 0.1189 0.0377  0.0153  0.0156  39  LYS A O   
304  C  CB  . LYS A 39  ? 0.2816 0.2795 0.1542 0.0662  -0.0256 -0.0131 39  LYS A CB  
305  C  CG  . LYS A 39  ? 0.2522 0.2894 0.2002 0.0381  0.0331  0.0109  39  LYS A CG  
306  C  CD  . LYS A 39  ? 0.1947 0.3341 0.2284 0.0564  0.0073  0.0131  39  LYS A CD  
307  C  CE  . LYS A 39  ? 0.3287 0.3400 0.2125 0.0397  0.0276  0.0102  39  LYS A CE  
308  N  NZ  . LYS A 39  ? 0.2554 0.4490 0.2915 0.0873  0.0194  0.1349  39  LYS A NZ  
309  N  N   . TYR A 40  ? 0.2415 0.2309 0.1305 0.0511  0.0342  0.0432  40  TYR A N   
310  C  CA  . TYR A 40  ? 0.1952 0.2173 0.1551 0.0210  0.0494  0.0298  40  TYR A CA  
311  C  C   . TYR A 40  ? 0.1691 0.2238 0.1375 0.0088  0.0434  0.0208  40  TYR A C   
312  O  O   . TYR A 40  ? 0.2295 0.3010 0.1193 0.0690  0.0315  -0.0015 40  TYR A O   
313  C  CB  . TYR A 40  ? 0.2549 0.2852 0.2134 -0.0142 0.0537  0.0610  40  TYR A CB  
314  C  CG  . TYR A 40  ? 0.2329 0.2583 0.1775 -0.0226 0.0579  0.0223  40  TYR A CG  
315  C  CD1 . TYR A 40  ? 0.2216 0.2657 0.2151 -0.0057 0.0421  0.0208  40  TYR A CD1 
316  C  CD2 . TYR A 40  ? 0.3201 0.4605 0.1752 0.0028  0.0870  0.0427  40  TYR A CD2 
317  C  CE1 . TYR A 40  ? 0.2400 0.3037 0.1946 -0.0038 0.0553  0.0177  40  TYR A CE1 
318  C  CE2 . TYR A 40  ? 0.3312 0.6349 0.2293 0.0627  0.1194  0.0248  40  TYR A CE2 
319  C  CZ  . TYR A 40  ? 0.1784 0.5457 0.2919 0.0253  0.0803  0.0083  40  TYR A CZ  
320  O  OH  . TYR A 40  ? 0.2759 0.5953 0.3675 0.1088  0.0821  0.0178  40  TYR A OH  
321  N  N   . ASP A 41  ? 0.1796 0.1912 0.1472 0.0324  0.0249  -0.0006 41  ASP A N   
322  C  CA  . ASP A 41  ? 0.2169 0.1943 0.1832 0.0412  -0.0170 -0.0168 41  ASP A CA  
323  C  C   . ASP A 41  ? 0.2212 0.2450 0.1728 0.0480  0.0151  -0.0379 41  ASP A C   
324  O  O   . ASP A 41  ? 0.2136 0.2861 0.1811 0.0665  0.0149  -0.0063 41  ASP A O   
325  C  CB  . ASP A 41  ? 0.2655 0.2222 0.2466 0.0040  -0.0038 -0.0199 41  ASP A CB  
326  C  CG  . ASP A 41  ? 0.3280 0.2818 0.2569 -0.0311 -0.0355 -0.0450 41  ASP A CG  
327  O  OD1 . ASP A 41  ? 0.4338 0.3104 0.2766 0.0926  -0.0311 -0.0900 41  ASP A OD1 
328  O  OD2 . ASP A 41  ? 0.5221 0.2996 0.4593 -0.1344 -0.0997 -0.0003 41  ASP A OD2 
329  N  N   . PRO A 42  ? 0.2728 0.3779 0.2081 0.1314  0.0560  0.0086  42  PRO A N   
330  C  CA  . PRO A 42  ? 0.2827 0.3928 0.2720 0.1121  0.0553  0.0156  42  PRO A CA  
331  C  C   . PRO A 42  ? 0.3537 0.3889 0.2466 0.0773  0.0997  -0.0305 42  PRO A C   
332  O  O   . PRO A 42  ? 0.3646 0.5798 0.3700 0.1930  0.0952  0.0750  42  PRO A O   
333  C  CB  . PRO A 42  ? 0.3844 0.6808 0.3098 0.1301  0.1350  0.0878  42  PRO A CB  
334  C  CG  . PRO A 42  ? 0.4117 0.6693 0.2436 0.1712  0.0702  0.0070  42  PRO A CG  
335  C  CD  . PRO A 42  ? 0.4381 0.4277 0.1759 0.1548  0.1089  0.0138  42  PRO A CD  
336  N  N   . SER A 43  ? 0.3156 0.3136 0.2062 0.1238  0.0306  -0.0414 43  SER A N   
337  C  CA  . SER A 43  ? 0.6323 0.2842 0.2447 0.0772  0.0439  -0.0868 43  SER A CA  
338  C  C   . SER A 43  ? 0.4499 0.3068 0.2214 0.1150  -0.0140 -0.0593 43  SER A C   
339  O  O   . SER A 43  ? 0.5716 0.3260 0.3300 0.2301  -0.0555 -0.0362 43  SER A O   
340  C  CB  . SER A 43  ? 0.4805 0.2808 0.5756 0.1076  -0.0441 -0.0681 43  SER A CB  
341  O  OG  . SER A 43  ? 0.5475 0.3391 0.3097 -0.0148 -0.0031 -0.0549 43  SER A OG  
342  N  N   . LEU A 44  ? 0.3237 0.3167 0.1938 0.1094  -0.0118 -0.0719 44  LEU A N   
343  C  CA  . LEU A 44  ? 0.2630 0.2552 0.1841 0.0656  -0.0233 -0.0073 44  LEU A CA  
344  C  C   . LEU A 44  ? 0.2266 0.2777 0.2309 0.0373  0.0076  0.0148  44  LEU A C   
345  O  O   . LEU A 44  ? 0.2178 0.4422 0.3226 0.0581  0.0344  0.1102  44  LEU A O   
346  C  CB  . LEU A 44  ? 0.2079 0.2587 0.1633 0.0386  0.0110  -0.0199 44  LEU A CB  
347  C  CG  . LEU A 44  ? 0.1693 0.2353 0.1770 0.0208  -0.0038 0.0098  44  LEU A CG  
348  C  CD1 . LEU A 44  ? 0.1921 0.2407 0.1776 0.0161  0.0359  -0.0142 44  LEU A CD1 
349  C  CD2 . LEU A 44  ? 0.2689 0.2055 0.1889 -0.0097 -0.0227 0.0138  44  LEU A CD2 
350  N  N   . LYS A 45  ? 0.2144 0.2585 0.2468 0.0515  -0.0357 0.0161  45  LYS A N   
351  C  CA  . LYS A 45  ? 0.1941 0.2305 0.2337 0.0498  0.0000  -0.0465 45  LYS A CA  
352  C  C   . LYS A 45  ? 0.1747 0.2037 0.2224 0.0511  0.0031  -0.0226 45  LYS A C   
353  O  O   . LYS A 45  ? 0.1697 0.2234 0.2298 0.0520  0.0265  -0.0179 45  LYS A O   
354  C  CB  . LYS A 45  ? 0.2524 0.2198 0.2639 0.0835  -0.0118 -0.0264 45  LYS A CB  
355  C  CG  . LYS A 45  ? 0.3833 0.2910 0.3147 0.0399  -0.0264 -0.0663 45  LYS A CG  
356  C  CD  . LYS A 45  ? 0.4934 0.3501 0.4066 0.0582  0.0738  -0.1039 45  LYS A CD  
357  N  N   . PRO A 46  ? 0.1421 0.2249 0.2113 0.0252  0.0289  0.0103  46  PRO A N   
358  C  CA  . PRO A 46  ? 0.1482 0.2249 0.1974 -0.0085 0.0214  -0.0070 46  PRO A CA  
359  C  C   . PRO A 46  ? 0.1177 0.1701 0.1909 0.0207  0.0110  -0.0005 46  PRO A C   
360  O  O   . PRO A 46  ? 0.1428 0.1789 0.2011 0.0237  0.0046  0.0046  46  PRO A O   
361  C  CB  . PRO A 46  ? 0.1500 0.2743 0.2657 -0.0201 0.0096  0.0328  46  PRO A CB  
362  C  CG  . PRO A 46  ? 0.1585 0.4383 0.3501 0.0447  0.0469  -0.0577 46  PRO A CG  
363  C  CD  . PRO A 46  ? 0.1404 0.3192 0.3046 0.0390  0.0151  -0.0163 46  PRO A CD  
364  N  N   . LEU A 47  ? 0.1312 0.1964 0.1876 0.0152  0.0070  0.0066  47  LEU A N   
365  C  CA  . LEU A 47  ? 0.1236 0.2037 0.1877 0.0174  0.0116  -0.0026 47  LEU A CA  
366  C  C   . LEU A 47  ? 0.1229 0.2069 0.2234 -0.0304 -0.0080 0.0248  47  LEU A C   
367  O  O   . LEU A 47  ? 0.1404 0.2565 0.3003 -0.0533 -0.0553 0.0648  47  LEU A O   
368  C  CB  . LEU A 47  ? 0.1975 0.2125 0.2393 -0.0055 0.0474  -0.0241 47  LEU A CB  
369  C  CG  . LEU A 47  ? 0.1710 0.2588 0.2443 -0.0126 0.0093  -0.0362 47  LEU A CG  
370  C  CD1 . LEU A 47  ? 0.1254 0.3125 0.3075 -0.0458 0.0201  -0.0791 47  LEU A CD1 
371  C  CD2 . LEU A 47  ? 0.1456 0.2768 0.2980 0.0383  0.0311  -0.0520 47  LEU A CD2 
372  N  N   . SER A 48  ? 0.1155 0.1951 0.1809 -0.0252 -0.0074 0.0184  48  SER A N   
373  C  CA  . SER A 48  ? 0.1421 0.1956 0.1753 -0.0040 -0.0043 0.0031  48  SER A CA  
374  C  C   . SER A 48  ? 0.1291 0.1912 0.1799 -0.0307 0.0122  0.0023  48  SER A C   
375  O  O   . SER A 48  ? 0.1492 0.2105 0.1881 -0.0395 0.0166  -0.0148 48  SER A O   
376  C  CB  . SER A 48  ? 0.1498 0.2143 0.2293 0.0049  -0.0119 0.0215  48  SER A CB  
377  O  OG  . SER A 48  ? 0.2037 0.2750 0.2840 0.0320  -0.0132 0.0266  48  SER A OG  
378  N  N   . VAL A 49  ? 0.1664 0.1991 0.1775 -0.0482 -0.0074 0.0126  49  VAL A N   
379  C  CA  . VAL A 49  ? 0.1662 0.2052 0.1939 -0.0640 0.0065  0.0035  49  VAL A CA  
380  C  C   . VAL A 49  ? 0.1771 0.2418 0.2229 -0.0808 -0.0275 0.0044  49  VAL A C   
381  O  O   . VAL A 49  ? 0.1775 0.3000 0.2657 -0.1011 -0.0441 0.0320  49  VAL A O   
382  C  CB  . VAL A 49  ? 0.2329 0.2232 0.2067 -0.0524 0.0147  -0.0285 49  VAL A CB  
383  C  CG1 . VAL A 49  ? 0.3855 0.2894 0.2355 -0.1309 0.0675  -0.0562 49  VAL A CG1 
384  C  CG2 . VAL A 49  ? 0.2125 0.2748 0.2752 -0.0763 0.0445  -0.0153 49  VAL A CG2 
385  N  N   . SER A 50  ? 0.1647 0.2057 0.1788 -0.0582 -0.0126 -0.0062 50  SER A N   
386  C  CA  . SER A 50  ? 0.1721 0.2266 0.2295 -0.0120 -0.0143 -0.0255 50  SER A CA  
387  C  C   . SER A 50  ? 0.1160 0.1925 0.2187 -0.0037 -0.0237 0.0131  50  SER A C   
388  O  O   . SER A 50  ? 0.1721 0.2143 0.2178 -0.0297 -0.0092 0.0256  50  SER A O   
389  C  CB  . SER A 50  ? 0.2386 0.2976 0.2793 -0.0557 0.0416  -0.0718 50  SER A CB  
390  O  OG  . SER A 50  ? 0.2809 0.4436 0.3249 -0.0021 -0.0035 -0.0688 50  SER A OG  
391  N  N   . TYR A 51  ? 0.1379 0.1907 0.2159 -0.0129 -0.0280 -0.0098 51  TYR A N   
392  C  CA  . TYR A 51  ? 0.1247 0.1852 0.1970 -0.0080 -0.0392 0.0100  51  TYR A CA  
393  C  C   . TYR A 51  ? 0.1541 0.1949 0.2285 -0.0210 -0.0154 0.0219  51  TYR A C   
394  O  O   . TYR A 51  ? 0.1789 0.2035 0.2160 0.0160  -0.0297 0.0329  51  TYR A O   
395  C  CB  . TYR A 51  ? 0.1339 0.1894 0.2284 -0.0189 -0.0368 0.0057  51  TYR A CB  
396  C  CG  . TYR A 51  ? 0.1411 0.1674 0.1737 -0.0146 -0.0443 -0.0017 51  TYR A CG  
397  C  CD1 . TYR A 51  ? 0.1402 0.1573 0.2137 -0.0238 -0.0395 -0.0078 51  TYR A CD1 
398  C  CD2 . TYR A 51  ? 0.1484 0.1641 0.1638 -0.0214 -0.0289 -0.0109 51  TYR A CD2 
399  C  CE1 . TYR A 51  ? 0.1150 0.1456 0.1712 -0.0065 -0.0178 0.0160  51  TYR A CE1 
400  C  CE2 . TYR A 51  ? 0.1500 0.1280 0.1622 -0.0225 -0.0197 -0.0060 51  TYR A CE2 
401  C  CZ  . TYR A 51  ? 0.1159 0.1412 0.1630 -0.0219 -0.0219 0.0046  51  TYR A CZ  
402  O  OH  . TYR A 51  ? 0.1204 0.1422 0.1757 -0.0137 -0.0245 -0.0010 51  TYR A OH  
403  N  N   A ASP A 52  ? 0.1287 0.2479 0.2646 -0.0142 -0.0403 0.0447  52  ASP A N   
404  N  N   B ASP A 52  ? 0.1178 0.2498 0.2680 -0.0242 -0.0467 0.0595  52  ASP A N   
405  C  CA  A ASP A 52  ? 0.1353 0.2572 0.2529 -0.0144 -0.0212 0.0738  52  ASP A CA  
406  C  CA  B ASP A 52  ? 0.1808 0.2908 0.2714 -0.0209 -0.0658 0.0868  52  ASP A CA  
407  C  C   A ASP A 52  ? 0.1909 0.1745 0.2811 0.0131  -0.0287 0.0597  52  ASP A C   
408  C  C   B ASP A 52  ? 0.1336 0.2842 0.3165 -0.0141 -0.0489 0.0625  52  ASP A C   
409  O  O   A ASP A 52  ? 0.2100 0.2536 0.2703 0.0184  -0.0606 0.0649  52  ASP A O   
410  O  O   B ASP A 52  ? 0.2495 0.3456 0.3592 0.0710  -0.0988 0.0899  52  ASP A O   
411  C  CB  A ASP A 52  ? 0.0631 0.2831 0.3634 0.0200  -0.0461 0.0888  52  ASP A CB  
412  C  CB  B ASP A 52  ? 0.2673 0.3192 0.3133 -0.0027 0.0131  0.1570  52  ASP A CB  
413  C  CG  A ASP A 52  ? 0.1982 0.4377 0.4016 0.0458  -0.0118 -0.0417 52  ASP A CG  
414  C  CG  B ASP A 52  ? 0.1518 0.3258 0.4084 -0.0811 0.0443  0.0553  52  ASP A CG  
415  O  OD1 A ASP A 52  ? 0.2078 0.3195 0.4196 -0.0076 0.0571  0.0520  52  ASP A OD1 
416  O  OD1 B ASP A 52  ? 0.2190 0.3136 0.3583 0.0254  -0.1111 0.0706  52  ASP A OD1 
417  O  OD2 A ASP A 52  ? 0.2960 0.3921 0.6276 -0.0720 -0.0815 0.1528  52  ASP A OD2 
418  O  OD2 B ASP A 52  ? 0.4785 0.3824 0.3447 0.0529  0.1018  0.0829  52  ASP A OD2 
419  N  N   . GLN A 53  ? 0.1497 0.2387 0.3716 0.0080  -0.0065 0.0628  53  GLN A N   
420  C  CA  . GLN A 53  ? 0.1970 0.2242 0.3898 0.0109  0.0357  0.0423  53  GLN A CA  
421  C  C   . GLN A 53  ? 0.2236 0.1805 0.2513 0.0097  0.0104  0.0152  53  GLN A C   
422  O  O   . GLN A 53  ? 0.2116 0.2013 0.2879 -0.0017 -0.0038 0.0326  53  GLN A O   
423  C  CB  . GLN A 53  ? 0.2325 0.2552 0.4677 0.0639  0.0688  0.0054  53  GLN A CB  
424  C  CG  . GLN A 53  ? 0.2881 0.4431 0.5643 0.1451  0.0540  0.0057  53  GLN A CG  
425  C  CD  . GLN A 53  ? 0.2703 0.5796 0.4654 0.2052  0.1260  0.2134  53  GLN A CD  
426  O  OE1 . GLN A 53  ? 0.3704 0.7434 0.6599 0.0931  0.0406  0.4338  53  GLN A OE1 
427  N  NE2 . GLN A 53  ? 0.4411 0.7476 1.0264 -0.0353 -0.3136 0.4235  53  GLN A NE2 
428  N  N   . ALA A 54  ? 0.1733 0.1726 0.2592 -0.0082 -0.0305 0.0167  54  ALA A N   
429  C  CA  . ALA A 54  ? 0.1794 0.1491 0.1987 0.0013  -0.0259 -0.0164 54  ALA A CA  
430  C  C   . ALA A 54  ? 0.1923 0.1713 0.2017 -0.0208 -0.0416 -0.0192 54  ALA A C   
431  O  O   . ALA A 54  ? 0.2117 0.2655 0.2402 -0.0368 -0.0768 -0.0228 54  ALA A O   
432  C  CB  . ALA A 54  ? 0.2058 0.1571 0.2450 -0.0135 -0.0115 -0.0074 54  ALA A CB  
433  N  N   . THR A 55  ? 0.1756 0.1548 0.1639 0.0164  -0.0306 0.0120  55  THR A N   
434  C  CA  . THR A 55  ? 0.1840 0.1533 0.1675 0.0168  -0.0331 0.0326  55  THR A CA  
435  C  C   . THR A 55  ? 0.1704 0.1404 0.1173 0.0000  -0.0403 0.0166  55  THR A C   
436  O  O   . THR A 55  ? 0.1782 0.1238 0.1588 -0.0052 -0.0289 0.0295  55  THR A O   
437  C  CB  . THR A 55  ? 0.2079 0.1665 0.2437 0.0260  -0.0406 0.0269  55  THR A CB  
438  O  OG1 . THR A 55  ? 0.2549 0.1911 0.3479 0.0144  -0.0930 0.0465  55  THR A OG1 
439  C  CG2 . THR A 55  ? 0.3077 0.1718 0.2177 0.0082  -0.0132 0.0513  55  THR A CG2 
440  N  N   . SER A 56  ? 0.1810 0.1357 0.1386 -0.0010 -0.0560 0.0183  56  SER A N   
441  C  CA  . SER A 56  ? 0.1957 0.1358 0.1215 -0.0109 -0.0471 0.0153  56  SER A CA  
442  C  C   . SER A 56  ? 0.1865 0.1372 0.1280 0.0078  -0.0465 0.0241  56  SER A C   
443  O  O   . SER A 56  ? 0.2056 0.1626 0.1445 0.0181  -0.0509 0.0313  56  SER A O   
444  C  CB  . SER A 56  ? 0.2054 0.1284 0.1208 -0.0044 -0.0527 0.0027  56  SER A CB  
445  O  OG  . SER A 56  ? 0.2299 0.1465 0.1481 -0.0102 -0.0702 0.0236  56  SER A OG  
446  N  N   . LEU A 57  ? 0.1861 0.1272 0.1151 0.0083  -0.0206 0.0212  57  LEU A N   
447  C  CA  . LEU A 57  ? 0.2158 0.1245 0.1420 0.0063  -0.0049 0.0266  57  LEU A CA  
448  C  C   . LEU A 57  ? 0.2069 0.1209 0.1266 0.0074  -0.0133 0.0262  57  LEU A C   
449  O  O   . LEU A 57  ? 0.2293 0.1571 0.1271 0.0182  -0.0322 0.0359  57  LEU A O   
450  C  CB  . LEU A 57  ? 0.2480 0.1412 0.1754 -0.0114 0.0229  0.0252  57  LEU A CB  
451  C  CG  . LEU A 57  ? 0.3120 0.1365 0.2433 -0.0076 -0.0103 -0.0253 57  LEU A CG  
452  C  CD1 . LEU A 57  ? 0.3578 0.1957 0.2585 -0.0571 0.0406  -0.0052 57  LEU A CD1 
453  C  CD2 . LEU A 57  ? 0.3456 0.1802 0.2610 0.0502  0.0096  0.0573  57  LEU A CD2 
454  N  N   . ARG A 58  ? 0.1736 0.1356 0.1475 0.0137  -0.0223 0.0214  58  ARG A N   
455  C  CA  . ARG A 58  ? 0.1961 0.1439 0.1418 -0.0008 -0.0240 0.0430  58  ARG A CA  
456  C  C   . ARG A 58  ? 0.1629 0.1385 0.1084 -0.0087 -0.0147 0.0250  58  ARG A C   
457  O  O   . ARG A 58  ? 0.1881 0.1306 0.1055 0.0087  -0.0043 0.0171  58  ARG A O   
458  C  CB  . ARG A 58  ? 0.2101 0.1491 0.1684 0.0083  -0.0003 0.0300  58  ARG A CB  
459  C  CG  . ARG A 58  ? 0.1764 0.1800 0.1917 -0.0215 -0.0063 0.0493  58  ARG A CG  
460  C  CD  . ARG A 58  ? 0.2148 0.2110 0.2064 -0.0315 -0.0370 0.0683  58  ARG A CD  
461  N  NE  . ARG A 58  ? 0.1776 0.2116 0.1675 -0.0269 -0.0159 0.0322  58  ARG A NE  
462  C  CZ  . ARG A 58  ? 0.1564 0.1891 0.1743 -0.0132 0.0086  0.0245  58  ARG A CZ  
463  N  NH1 . ARG A 58  ? 0.2260 0.2255 0.1870 -0.0623 0.0353  0.0498  58  ARG A NH1 
464  N  NH2 . ARG A 58  ? 0.1981 0.1781 0.1773 -0.0234 0.0125  0.0285  58  ARG A NH2 
465  N  N   . ILE A 59  ? 0.1762 0.1263 0.0983 0.0062  -0.0152 0.0146  59  ILE A N   
466  C  CA  . ILE A 59  ? 0.1810 0.1330 0.1155 -0.0038 -0.0232 0.0241  59  ILE A CA  
467  C  C   . ILE A 59  ? 0.1741 0.1245 0.1010 0.0015  -0.0216 0.0212  59  ILE A C   
468  O  O   . ILE A 59  ? 0.1975 0.1888 0.0882 0.0152  -0.0098 0.0240  59  ILE A O   
469  C  CB  . ILE A 59  ? 0.1858 0.1224 0.1105 0.0038  -0.0179 0.0236  59  ILE A CB  
470  C  CG1 . ILE A 59  ? 0.1949 0.1222 0.1087 -0.0015 -0.0179 0.0172  59  ILE A CG1 
471  C  CG2 . ILE A 59  ? 0.2281 0.1395 0.1061 -0.0028 -0.0432 0.0165  59  ILE A CG2 
472  C  CD1 . ILE A 59  ? 0.2185 0.1330 0.1150 -0.0141 -0.0359 0.0103  59  ILE A CD1 
473  N  N   . LEU A 60  ? 0.1483 0.1363 0.1169 -0.0088 -0.0109 0.0181  60  LEU A N   
474  C  CA  . LEU A 60  ? 0.1573 0.1336 0.1031 -0.0015 -0.0054 0.0219  60  LEU A CA  
475  C  C   . LEU A 60  ? 0.1455 0.1212 0.1040 -0.0077 0.0010  0.0207  60  LEU A C   
476  O  O   . LEU A 60  ? 0.1623 0.1445 0.1014 -0.0048 0.0071  0.0230  60  LEU A O   
477  C  CB  . LEU A 60  ? 0.1603 0.1155 0.1706 -0.0120 -0.0087 0.0226  60  LEU A CB  
478  C  CG  . LEU A 60  ? 0.2003 0.1313 0.1455 -0.0160 -0.0104 0.0305  60  LEU A CG  
479  C  CD1 . LEU A 60  ? 0.2076 0.1557 0.1548 -0.0265 0.0156  0.0287  60  LEU A CD1 
480  C  CD2 . LEU A 60  ? 0.2052 0.1296 0.2054 -0.0335 -0.0104 0.0065  60  LEU A CD2 
481  N  N   . ASN A 61  ? 0.1597 0.1152 0.1098 -0.0026 0.0093  0.0183  61  ASN A N   
482  C  CA  . ASN A 61  ? 0.1641 0.1367 0.1050 -0.0187 0.0188  -0.0091 61  ASN A CA  
483  C  C   . ASN A 61  ? 0.1595 0.1287 0.1186 -0.0210 0.0057  0.0122  61  ASN A C   
484  O  O   . ASN A 61  ? 0.1912 0.1543 0.1547 -0.0176 0.0217  0.0467  61  ASN A O   
485  C  CB  . ASN A 61  ? 0.1808 0.1467 0.1014 -0.0063 0.0243  0.0131  61  ASN A CB  
486  C  CG  . ASN A 61  ? 0.1710 0.1457 0.1036 -0.0171 0.0111  -0.0035 61  ASN A CG  
487  O  OD1 . ASN A 61  ? 0.1824 0.1571 0.1292 -0.0253 0.0195  0.0122  61  ASN A OD1 
488  N  ND2 . ASN A 61  ? 0.2020 0.1439 0.1344 -0.0001 0.0250  -0.0020 61  ASN A ND2 
489  N  N   . ASN A 62  ? 0.1886 0.1216 0.1268 -0.0207 -0.0021 0.0087  62  ASN A N   
490  C  CA  . ASN A 62  ? 0.2029 0.1203 0.1961 -0.0211 -0.0253 -0.0027 62  ASN A CA  
491  C  C   . ASN A 62  ? 0.1711 0.1627 0.1517 -0.0549 -0.0080 0.0116  62  ASN A C   
492  O  O   . ASN A 62  ? 0.2354 0.1914 0.2129 -0.0746 -0.0160 0.0197  62  ASN A O   
493  C  CB  . ASN A 62  ? 0.2361 0.1141 0.2612 -0.0096 -0.0465 -0.0291 62  ASN A CB  
494  C  CG  . ASN A 62  ? 0.2179 0.1932 0.1533 0.0093  -0.0509 -0.0241 62  ASN A CG  
495  O  OD1 . ASN A 62  ? 0.2104 0.1816 0.1517 -0.0060 0.0164  -0.0071 62  ASN A OD1 
496  N  ND2 . ASN A 62  ? 0.3411 0.2414 0.2205 -0.0088 0.0068  -0.0454 62  ASN A ND2 
497  N  N   . GLY A 63  ? 0.1837 0.1494 0.1304 -0.0259 0.0120  0.0249  63  GLY A N   
498  C  CA  . GLY A 63  ? 0.1914 0.1753 0.1242 -0.0419 0.0168  0.0248  63  GLY A CA  
499  C  C   . GLY A 63  ? 0.1559 0.1640 0.1437 -0.0126 0.0094  0.0010  63  GLY A C   
500  O  O   . GLY A 63  ? 0.1846 0.1969 0.1578 -0.0006 0.0269  0.0017  63  GLY A O   
501  N  N   . HIS A 64  ? 0.1596 0.1436 0.1268 -0.0263 0.0255  0.0114  64  HIS A N   
502  C  CA  . HIS A 64  ? 0.1448 0.1590 0.1379 -0.0231 0.0159  0.0182  64  HIS A CA  
503  C  C   . HIS A 64  ? 0.1534 0.1323 0.1326 -0.0285 0.0182  0.0261  64  HIS A C   
504  O  O   . HIS A 64  ? 0.1404 0.2243 0.3273 -0.0234 -0.0065 0.1430  64  HIS A O   
505  C  CB  . HIS A 64  ? 0.1625 0.1808 0.1323 -0.0366 0.0062  0.0017  64  HIS A CB  
506  C  CG  . HIS A 64  ? 0.1854 0.1905 0.1260 -0.0125 0.0071  0.0043  64  HIS A CG  
507  N  ND1 . HIS A 64  ? 0.1861 0.2206 0.1559 -0.0264 0.0147  -0.0220 64  HIS A ND1 
508  C  CD2 . HIS A 64  ? 0.2080 0.2131 0.1618 -0.0637 0.0103  0.0021  64  HIS A CD2 
509  C  CE1 . HIS A 64  ? 0.1935 0.2379 0.1736 -0.0207 0.0146  -0.0160 64  HIS A CE1 
510  N  NE2 . HIS A 64  ? 0.2012 0.2350 0.2083 -0.0416 0.0359  0.0131  64  HIS A NE2 
511  N  N   . ALA A 65  ? 0.1400 0.1322 0.1221 -0.0100 0.0048  0.0142  65  ALA A N   
512  C  CA  . ALA A 65  ? 0.1509 0.1290 0.1089 -0.0243 0.0148  0.0196  65  ALA A CA  
513  C  C   . ALA A 65  ? 0.1532 0.1155 0.0878 -0.0065 0.0062  0.0038  65  ALA A C   
514  O  O   . ALA A 65  ? 0.1717 0.1415 0.1137 -0.0296 0.0165  0.0130  65  ALA A O   
515  C  CB  . ALA A 65  ? 0.1560 0.1803 0.1212 -0.0179 0.0068  0.0201  65  ALA A CB  
516  N  N   . PHE A 66  ? 0.1467 0.1181 0.1017 -0.0093 0.0037  0.0057  66  PHE A N   
517  C  CA  . PHE A 66  ? 0.1659 0.1184 0.0934 -0.0038 -0.0068 0.0196  66  PHE A CA  
518  C  C   . PHE A 66  ? 0.1405 0.1169 0.0877 -0.0137 -0.0089 0.0041  66  PHE A C   
519  O  O   . PHE A 66  ? 0.1708 0.1142 0.0887 -0.0055 0.0001  0.0152  66  PHE A O   
520  C  CB  . PHE A 66  ? 0.1833 0.1573 0.0907 -0.0127 -0.0094 0.0052  66  PHE A CB  
521  C  CG  . PHE A 66  ? 0.1882 0.1296 0.0854 -0.0109 -0.0142 -0.0035 66  PHE A CG  
522  C  CD1 . PHE A 66  ? 0.1650 0.1614 0.0970 -0.0115 -0.0254 -0.0046 66  PHE A CD1 
523  C  CD2 . PHE A 66  ? 0.1944 0.1458 0.0910 -0.0057 -0.0144 -0.0217 66  PHE A CD2 
524  C  CE1 . PHE A 66  ? 0.1878 0.1504 0.1094 -0.0173 -0.0403 -0.0035 66  PHE A CE1 
525  C  CE2 . PHE A 66  ? 0.1899 0.1409 0.1124 -0.0242 -0.0272 -0.0049 66  PHE A CE2 
526  C  CZ  . PHE A 66  ? 0.1641 0.1572 0.1076 -0.0189 -0.0318 -0.0065 66  PHE A CZ  
527  N  N   . ASN A 67  ? 0.1494 0.1207 0.1089 -0.0126 -0.0051 0.0260  67  ASN A N   
528  C  CA  . ASN A 67  ? 0.1354 0.1081 0.0998 -0.0065 -0.0040 0.0041  67  ASN A CA  
529  C  C   . ASN A 67  ? 0.1419 0.1013 0.0887 -0.0057 -0.0193 0.0087  67  ASN A C   
530  O  O   . ASN A 67  ? 0.1717 0.1456 0.1004 -0.0107 -0.0151 0.0297  67  ASN A O   
531  C  CB  . ASN A 67  ? 0.1676 0.1288 0.1146 -0.0215 -0.0125 0.0091  67  ASN A CB  
532  C  CG  . ASN A 67  ? 0.1606 0.1304 0.1433 -0.0272 -0.0030 0.0162  67  ASN A CG  
533  O  OD1 . ASN A 67  ? 0.1650 0.1611 0.1398 -0.0351 -0.0285 0.0215  67  ASN A OD1 
534  N  ND2 . ASN A 67  ? 0.2034 0.1611 0.1671 -0.0485 -0.0357 0.0212  67  ASN A ND2 
535  N  N   . VAL A 68  ? 0.1404 0.1027 0.0986 0.0023  -0.0111 0.0115  68  VAL A N   
536  C  CA  . VAL A 68  ? 0.1596 0.1204 0.0952 0.0168  -0.0161 0.0073  68  VAL A CA  
537  C  C   . VAL A 68  ? 0.1704 0.1203 0.0956 0.0054  -0.0086 0.0093  68  VAL A C   
538  O  O   . VAL A 68  ? 0.1712 0.1071 0.0956 0.0088  -0.0115 0.0133  68  VAL A O   
539  C  CB  . VAL A 68  ? 0.1498 0.1261 0.1248 -0.0043 -0.0403 0.0043  68  VAL A CB  
540  C  CG1 . VAL A 68  ? 0.1552 0.1603 0.1416 0.0074  -0.0366 0.0027  68  VAL A CG1 
541  C  CG2 . VAL A 68  ? 0.1404 0.1392 0.1356 -0.0140 -0.0152 -0.0144 68  VAL A CG2 
542  N  N   . GLU A 69  ? 0.1728 0.1033 0.1133 0.0087  -0.0100 0.0172  69  GLU A N   
543  C  CA  . GLU A 69  ? 0.1757 0.1148 0.1204 0.0049  -0.0027 0.0096  69  GLU A CA  
544  C  C   . GLU A 69  ? 0.1680 0.1171 0.1008 0.0161  -0.0176 0.0297  69  GLU A C   
545  O  O   . GLU A 69  ? 0.1909 0.1321 0.1323 0.0063  -0.0359 0.0137  69  GLU A O   
546  C  CB  . GLU A 69  ? 0.1594 0.1348 0.1630 0.0015  0.0258  0.0296  69  GLU A CB  
547  C  CG  . GLU A 69  ? 0.1617 0.1684 0.1418 -0.0195 0.0055  0.0295  69  GLU A CG  
548  C  CD  . GLU A 69  ? 0.1661 0.1651 0.1844 0.0071  0.0146  0.0383  69  GLU A CD  
549  O  OE1 . GLU A 69  ? 0.1897 0.1671 0.1837 -0.0015 0.0074  0.0277  69  GLU A OE1 
550  O  OE2 . GLU A 69  ? 0.1861 0.1820 0.1863 -0.0104 0.0114  0.0261  69  GLU A OE2 
551  N  N   . PHE A 70  ? 0.1685 0.1166 0.1090 0.0041  -0.0151 0.0081  70  PHE A N   
552  C  CA  . PHE A 70  ? 0.1618 0.0952 0.1413 0.0108  -0.0227 0.0225  70  PHE A CA  
553  C  C   . PHE A 70  ? 0.1649 0.1327 0.1265 0.0089  -0.0269 0.0098  70  PHE A C   
554  O  O   . PHE A 70  ? 0.1821 0.1182 0.1669 0.0055  -0.0296 0.0255  70  PHE A O   
555  C  CB  . PHE A 70  ? 0.1865 0.1173 0.1173 -0.0060 -0.0241 0.0114  70  PHE A CB  
556  C  CG  . PHE A 70  ? 0.1629 0.1024 0.1356 0.0087  -0.0405 0.0205  70  PHE A CG  
557  C  CD1 . PHE A 70  ? 0.1782 0.1121 0.1177 0.0096  0.0032  0.0329  70  PHE A CD1 
558  C  CD2 . PHE A 70  ? 0.1652 0.1137 0.1199 0.0043  -0.0274 0.0233  70  PHE A CD2 
559  C  CE1 . PHE A 70  ? 0.1771 0.1115 0.1466 0.0118  0.0048  0.0326  70  PHE A CE1 
560  C  CE2 . PHE A 70  ? 0.1728 0.1260 0.1421 0.0024  -0.0103 0.0292  70  PHE A CE2 
561  C  CZ  . PHE A 70  ? 0.2011 0.1101 0.1636 -0.0041 -0.0153 0.0126  70  PHE A CZ  
562  N  N   . ASP A 71  ? 0.1928 0.1061 0.1696 0.0121  -0.0544 0.0250  71  ASP A N   
563  C  CA  . ASP A 71  ? 0.1850 0.1031 0.1902 0.0068  -0.0296 0.0348  71  ASP A CA  
564  C  C   . ASP A 71  ? 0.1678 0.1090 0.1792 0.0032  0.0001  0.0231  71  ASP A C   
565  O  O   . ASP A 71  ? 0.2117 0.1695 0.2441 -0.0359 -0.0041 -0.0113 71  ASP A O   
566  C  CB  . ASP A 71  ? 0.2249 0.1184 0.2120 0.0105  -0.0666 0.0405  71  ASP A CB  
567  C  CG  . ASP A 71  ? 0.2150 0.1347 0.2344 0.0168  -0.0476 0.0487  71  ASP A CG  
568  O  OD1 . ASP A 71  ? 0.2461 0.1298 0.2508 0.0063  -0.0641 0.0450  71  ASP A OD1 
569  O  OD2 . ASP A 71  ? 0.2741 0.1675 0.3835 0.0265  -0.0811 0.0318  71  ASP A OD2 
570  N  N   . ASP A 72  ? 0.1580 0.1001 0.1934 -0.0078 -0.0197 0.0225  72  ASP A N   
571  C  CA  . ASP A 72  ? 0.1714 0.1030 0.1844 -0.0124 -0.0066 0.0006  72  ASP A CA  
572  C  C   . ASP A 72  ? 0.2052 0.1200 0.2013 -0.0197 -0.0399 0.0155  72  ASP A C   
573  O  O   . ASP A 72  ? 0.2632 0.1191 0.2325 -0.0219 -0.0342 0.0096  72  ASP A O   
574  C  CB  . ASP A 72  ? 0.1847 0.1168 0.1808 0.0013  0.0027  0.0294  72  ASP A CB  
575  C  CG  . ASP A 72  ? 0.1911 0.1583 0.1688 -0.0017 -0.0172 0.0242  72  ASP A CG  
576  O  OD1 . ASP A 72  ? 0.2220 0.2150 0.1946 -0.0328 -0.0276 0.0559  72  ASP A OD1 
577  O  OD2 . ASP A 72  ? 0.2296 0.2084 0.1705 -0.0092 -0.0443 0.0187  72  ASP A OD2 
578  N  N   . SER A 73  ? 0.2100 0.1032 0.2287 -0.0120 -0.0253 0.0322  73  SER A N   
579  C  CA  . SER A 73  ? 0.2475 0.1059 0.2621 -0.0283 -0.0421 0.0239  73  SER A CA  
580  C  C   . SER A 73  ? 0.2282 0.1166 0.2581 -0.0085 -0.0399 -0.0119 73  SER A C   
581  O  O   . SER A 73  ? 0.2849 0.1046 0.2545 -0.0057 -0.0366 0.0007  73  SER A O   
582  C  CB  . SER A 73  ? 0.2451 0.1529 0.2748 -0.0329 -0.0496 0.0516  73  SER A CB  
583  O  OG  . SER A 73  ? 0.2689 0.1218 0.2316 -0.0028 -0.0163 0.0287  73  SER A OG  
584  N  N   . GLN A 74  ? 0.2561 0.1281 0.2461 -0.0063 -0.0269 -0.0020 74  GLN A N   
585  C  CA  . GLN A 74  ? 0.2560 0.1727 0.3070 0.0507  -0.0366 0.0210  74  GLN A CA  
586  C  C   . GLN A 74  ? 0.2538 0.2031 0.2314 0.0015  -0.0731 -0.0262 74  GLN A C   
587  O  O   . GLN A 74  ? 0.2177 0.1862 0.2630 -0.0289 -0.0430 -0.0055 74  GLN A O   
588  C  CB  . GLN A 74  ? 0.3479 0.2020 0.2502 0.0296  -0.0436 0.0162  74  GLN A CB  
589  C  CG  . GLN A 74  ? 0.2971 0.2754 0.3377 -0.0046 -0.0656 0.0357  74  GLN A CG  
590  C  CD  . GLN A 74  ? 0.3461 0.3835 0.4081 0.0487  -0.0741 0.1120  74  GLN A CD  
591  O  OE1 . GLN A 74  ? 0.4190 0.4965 0.4338 -0.0843 -0.1358 -0.0450 74  GLN A OE1 
592  N  NE2 . GLN A 74  ? 0.3197 0.3016 0.3842 -0.0344 -0.0267 0.0273  74  GLN A NE2 
593  N  N   . ASP A 75  ? 0.3192 0.2827 0.2633 0.0051  -0.0515 -0.0206 75  ASP A N   
594  C  CA  . ASP A 75  ? 0.3010 0.3037 0.3391 -0.0366 -0.0390 -0.0432 75  ASP A CA  
595  C  C   . ASP A 75  ? 0.2099 0.3411 0.2551 -0.0144 -0.0546 -0.0207 75  ASP A C   
596  O  O   . ASP A 75  ? 0.2700 0.6617 0.5439 -0.0073 -0.0588 -0.2328 75  ASP A O   
597  C  CB  . ASP A 75  ? 0.4375 0.2718 0.3402 0.0984  -0.1368 -0.0632 75  ASP A CB  
598  C  CG  . ASP A 75  ? 0.3300 0.3716 0.3037 -0.0799 0.0454  -0.0425 75  ASP A CG  
599  O  OD1 . ASP A 75  ? 0.4059 0.5802 0.2926 0.0718  -0.0644 -0.1465 75  ASP A OD1 
600  O  OD2 . ASP A 75  ? 0.5691 0.4833 0.3533 0.1203  0.1598  0.0010  75  ASP A OD2 
601  N  N   A LYS A 76  ? 0.2416 0.1821 0.3228 -0.0196 -0.0551 0.0909  76  LYS A N   
602  N  N   B LYS A 76  ? 0.2108 0.2287 0.2603 -0.0080 -0.0646 0.0342  76  LYS A N   
603  C  CA  A LYS A 76  ? 0.2881 0.1764 0.3149 -0.0791 0.0425  0.0564  76  LYS A CA  
604  C  CA  B LYS A 76  ? 0.1824 0.1635 0.2560 0.0320  -0.0746 0.0265  76  LYS A CA  
605  C  C   A LYS A 76  ? 0.3174 0.2028 0.2581 0.0017  -0.0342 0.0559  76  LYS A C   
606  C  C   B LYS A 76  ? 0.1579 0.1715 0.1833 -0.0243 -0.0617 0.0229  76  LYS A C   
607  O  O   A LYS A 76  ? 0.3528 0.4156 0.2870 0.0890  0.0172  0.1254  76  LYS A O   
608  O  O   B LYS A 76  ? 0.1501 0.2008 0.2433 -0.0174 -0.0617 0.0245  76  LYS A O   
609  C  CB  A LYS A 76  ? 0.2725 0.2718 0.2784 -0.1300 0.0023  0.0643  76  LYS A CB  
610  C  CB  B LYS A 76  ? 0.1984 0.1437 0.3064 0.0203  -0.0502 0.0388  76  LYS A CB  
611  C  CG  A LYS A 76  ? 0.4607 0.3116 0.3993 -0.0093 -0.0099 0.0671  76  LYS A CG  
612  C  CG  B LYS A 76  ? 0.2286 0.1879 0.3003 0.0294  -0.0595 0.0447  76  LYS A CG  
613  C  CD  A LYS A 76  ? 0.5602 0.2870 0.3116 -0.0584 -0.0041 0.1208  76  LYS A CD  
614  C  CD  B LYS A 76  ? 0.2635 0.1798 0.2752 0.0021  -0.0207 0.0241  76  LYS A CD  
615  C  CE  A LYS A 76  ? 0.4733 0.2703 0.2795 -0.0452 -0.0705 -0.0132 76  LYS A CE  
616  C  CE  B LYS A 76  ? 0.3010 0.2529 0.2329 0.0000  -0.0636 0.0229  76  LYS A CE  
617  N  NZ  A LYS A 76  ? 0.4492 0.3095 0.3797 -0.0445 0.0388  -0.0641 76  LYS A NZ  
618  N  NZ  B LYS A 76  ? 0.3271 0.1468 0.2703 0.0292  -0.0302 0.0604  76  LYS A NZ  
619  N  N   A ALA A 77  ? 0.2294 0.2301 0.2418 0.0027  -0.0872 0.0527  77  ALA A N   
620  N  N   B ALA A 77  ? 0.1475 0.1882 0.1906 0.0160  -0.0568 0.0097  77  ALA A N   
621  C  CA  A ALA A 77  ? 0.1618 0.1958 0.2498 -0.0173 -0.0527 0.0443  77  ALA A CA  
622  C  CA  B ALA A 77  ? 0.1524 0.1659 0.2231 -0.0144 -0.0723 0.0196  77  ALA A CA  
623  C  C   A ALA A 77  ? 0.1074 0.1615 0.2362 -0.0023 -0.0570 0.0469  77  ALA A C   
624  C  C   B ALA A 77  ? 0.1322 0.1662 0.2175 -0.0219 -0.0723 0.0076  77  ALA A C   
625  O  O   A ALA A 77  ? 0.1208 0.2146 0.2313 -0.0211 0.0021  0.0817  77  ALA A O   
626  O  O   B ALA A 77  ? 0.1305 0.1763 0.2599 0.0116  -0.0675 -0.0326 77  ALA A O   
627  C  CB  A ALA A 77  ? 0.1952 0.2804 0.2079 0.0135  -0.0432 0.0000  77  ALA A CB  
628  C  CB  B ALA A 77  ? 0.1996 0.1712 0.1703 -0.0326 -0.0359 0.0130  77  ALA A CB  
629  N  N   . VAL A 78  ? 0.1579 0.1553 0.1803 -0.0174 -0.0370 0.0015  78  VAL A N   
630  C  CA  . VAL A 78  ? 0.1761 0.1403 0.1758 -0.0291 -0.0337 0.0104  78  VAL A CA  
631  C  C   . VAL A 78  ? 0.1651 0.1414 0.2000 -0.0281 -0.0210 0.0126  78  VAL A C   
632  O  O   . VAL A 78  ? 0.1661 0.1701 0.2340 -0.0540 -0.0557 0.0337  78  VAL A O   
633  C  CB  . VAL A 78  ? 0.2210 0.1826 0.2361 -0.0051 -0.0423 -0.0104 78  VAL A CB  
634  C  CG1 . VAL A 78  ? 0.2178 0.1747 0.2723 0.0208  -0.0410 0.0228  78  VAL A CG1 
635  C  CG2 . VAL A 78  ? 0.2372 0.2281 0.3122 0.0160  0.0006  -0.0230 78  VAL A CG2 
636  N  N   . LEU A 79  ? 0.1431 0.1404 0.1665 -0.0175 -0.0222 0.0094  79  LEU A N   
637  C  CA  . LEU A 79  ? 0.1620 0.1361 0.1767 -0.0026 -0.0157 0.0027  79  LEU A CA  
638  C  C   . LEU A 79  ? 0.1618 0.1462 0.1511 -0.0153 -0.0057 -0.0023 79  LEU A C   
639  O  O   . LEU A 79  ? 0.1600 0.1733 0.1887 -0.0377 0.0024  -0.0167 79  LEU A O   
640  C  CB  . LEU A 79  ? 0.1551 0.1594 0.1944 -0.0167 -0.0186 0.0034  79  LEU A CB  
641  C  CG  . LEU A 79  ? 0.1671 0.1565 0.1984 0.0046  0.0008  0.0037  79  LEU A CG  
642  C  CD1 . LEU A 79  ? 0.1564 0.1791 0.3470 0.0037  0.0164  0.0535  79  LEU A CD1 
643  C  CD2 . LEU A 79  ? 0.1446 0.1820 0.1947 0.0111  0.0048  -0.0003 79  LEU A CD2 
644  N  N   A LYS A 80  ? 0.1394 0.1762 0.1676 -0.0071 0.0119  0.0000  80  LYS A N   
645  N  N   B LYS A 80  ? 0.1410 0.1756 0.1791 -0.0296 -0.0027 -0.0131 80  LYS A N   
646  C  CA  A LYS A 80  ? 0.1656 0.1383 0.1887 0.0164  0.0156  0.0034  80  LYS A CA  
647  C  CA  B LYS A 80  ? 0.1552 0.1621 0.1803 -0.0111 0.0057  -0.0027 80  LYS A CA  
648  C  C   A LYS A 80  ? 0.1243 0.1687 0.2127 0.0102  0.0205  0.0019  80  LYS A C   
649  C  C   B LYS A 80  ? 0.1274 0.1694 0.2126 0.0080  0.0186  0.0013  80  LYS A C   
650  O  O   A LYS A 80  ? 0.1446 0.1648 0.2014 -0.0074 -0.0132 0.0130  80  LYS A O   
651  O  O   B LYS A 80  ? 0.1271 0.1656 0.2096 -0.0057 -0.0175 0.0124  80  LYS A O   
652  C  CB  A LYS A 80  ? 0.1705 0.1520 0.2867 0.0381  0.0135  0.0098  80  LYS A CB  
653  C  CB  B LYS A 80  ? 0.2265 0.1940 0.2243 0.0163  -0.0189 0.0234  80  LYS A CB  
654  C  CG  A LYS A 80  ? 0.1666 0.2054 0.2581 0.0348  0.0226  0.0108  80  LYS A CG  
655  C  CG  B LYS A 80  ? 0.2405 0.2003 0.2444 0.0010  0.0063  0.0421  80  LYS A CG  
656  C  CD  A LYS A 80  ? 0.2025 0.2270 0.3406 0.0241  0.0250  -0.0230 80  LYS A CD  
657  C  CD  B LYS A 80  ? 0.2372 0.2655 0.3009 -0.0035 0.0099  0.0820  80  LYS A CD  
658  C  CE  A LYS A 80  ? 0.2533 0.4259 0.4032 0.0252  0.1332  -0.0480 80  LYS A CE  
659  C  CE  B LYS A 80  ? 0.3512 0.4104 0.3776 0.1533  0.0727  0.0769  80  LYS A CE  
660  N  N   . GLY A 81  ? 0.1588 0.1881 0.1917 0.0015  0.0225  -0.0097 81  GLY A N   
661  C  CA  . GLY A 81  ? 0.1729 0.2101 0.2087 0.0126  0.0500  0.0326  81  GLY A CA  
662  C  C   . GLY A 81  ? 0.1482 0.1806 0.1885 0.0085  0.0196  0.0043  81  GLY A C   
663  O  O   . GLY A 81  ? 0.1474 0.1834 0.1929 -0.0070 0.0046  -0.0098 81  GLY A O   
664  N  N   . GLY A 82  ? 0.1819 0.1984 0.2247 -0.0272 0.0272  0.0087  82  GLY A N   
665  C  CA  . GLY A 82  ? 0.2020 0.2172 0.2709 -0.0222 -0.0068 0.0436  82  GLY A CA  
666  C  C   . GLY A 82  ? 0.1788 0.2117 0.2444 0.0394  0.0496  0.0181  82  GLY A C   
667  O  O   . GLY A 82  ? 0.2316 0.3194 0.2405 0.0692  0.0537  -0.0007 82  GLY A O   
668  N  N   . PRO A 83  ? 0.1757 0.1772 0.2140 0.0105  0.0274  0.0155  83  PRO A N   
669  C  CA  . PRO A 83  ? 0.2002 0.1805 0.1872 0.0608  0.0054  0.0035  83  PRO A CA  
670  C  C   . PRO A 83  ? 0.1851 0.2421 0.1934 0.0560  -0.0205 -0.0366 83  PRO A C   
671  O  O   . PRO A 83  ? 0.2397 0.2578 0.2236 0.0294  -0.0461 -0.0120 83  PRO A O   
672  C  CB  . PRO A 83  ? 0.2252 0.2281 0.2137 0.0706  -0.0096 -0.0054 83  PRO A CB  
673  C  CG  . PRO A 83  ? 0.1909 0.1953 0.1920 0.0397  0.0055  0.0012  83  PRO A CG  
674  C  CD  . PRO A 83  ? 0.1703 0.1606 0.2127 0.0091  0.0485  -0.0052 83  PRO A CD  
675  N  N   . LEU A 84  ? 0.1784 0.1641 0.1817 0.0373  0.0008  -0.0024 84  LEU A N   
676  C  CA  . LEU A 84  ? 0.2029 0.1456 0.1789 0.0285  0.0035  -0.0252 84  LEU A CA  
677  C  C   . LEU A 84  ? 0.1991 0.1730 0.2293 0.0366  0.0154  -0.0434 84  LEU A C   
678  O  O   . LEU A 84  ? 0.2448 0.1846 0.2955 0.0496  0.0395  -0.0702 84  LEU A O   
679  C  CB  . LEU A 84  ? 0.1503 0.1422 0.1720 0.0195  0.0110  -0.0168 84  LEU A CB  
680  C  CG  . LEU A 84  ? 0.1229 0.1280 0.1949 0.0119  0.0164  -0.0194 84  LEU A CG  
681  C  CD1 . LEU A 84  ? 0.1569 0.1482 0.1801 0.0296  0.0028  -0.0120 84  LEU A CD1 
682  C  CD2 . LEU A 84  ? 0.1253 0.1389 0.2025 0.0000  0.0177  -0.0215 84  LEU A CD2 
683  N  N   A ASP A 85  ? 0.2682 0.1923 0.2714 -0.0037 -0.0052 -0.0873 85  ASP A N   
684  N  N   B ASP A 85  ? 0.2290 0.1581 0.2617 0.0324  0.0118  -0.0646 85  ASP A N   
685  C  CA  A ASP A 85  ? 0.3806 0.1881 0.3170 -0.0157 0.0170  -0.0364 85  ASP A CA  
686  C  CA  B ASP A 85  ? 0.3537 0.1275 0.1771 0.0197  -0.0108 -0.0621 85  ASP A CA  
687  C  C   A ASP A 85  ? 0.2599 0.1671 0.2441 -0.0035 0.0252  -0.1023 85  ASP A C   
688  C  C   B ASP A 85  ? 0.2570 0.1966 0.1834 0.0077  -0.0315 -0.0776 85  ASP A C   
689  O  O   A ASP A 85  ? 0.2594 0.2208 0.2856 0.0043  0.0825  -0.0847 85  ASP A O   
690  O  O   B ASP A 85  ? 0.3098 0.1996 0.2397 0.0331  -0.0142 -0.0697 85  ASP A O   
691  C  CB  A ASP A 85  ? 0.5540 0.1877 0.3912 -0.1263 0.0166  -0.0406 85  ASP A CB  
692  C  CB  B ASP A 85  ? 0.3937 0.1412 0.1921 0.0672  -0.0161 -0.0604 85  ASP A CB  
693  C  CG  A ASP A 85  ? 0.5482 0.3644 0.3846 -0.0392 -0.0846 0.0182  85  ASP A CG  
694  C  CG  B ASP A 85  ? 0.3134 0.3021 0.3194 0.0703  -0.0416 0.1074  85  ASP A CG  
695  O  OD1 A ASP A 85  ? 0.5576 0.2136 0.7692 -0.0575 -0.1002 -0.0024 85  ASP A OD1 
696  O  OD1 B ASP A 85  ? 0.3987 0.2921 0.2592 -0.0684 0.0198  -0.0276 85  ASP A OD1 
697  O  OD2 A ASP A 85  ? 0.5026 0.3014 0.4950 0.1004  -0.0676 -0.1365 85  ASP A OD2 
698  O  OD2 B ASP A 85  ? 0.4345 0.3316 0.3921 -0.0166 -0.0848 0.1383  85  ASP A OD2 
699  N  N   A GLY A 86  ? 0.3039 0.1793 0.2578 -0.0066 -0.0540 0.0138  86  GLY A N   
700  N  N   B GLY A 86  ? 0.2155 0.1908 0.1850 -0.0010 0.0725  -0.0430 86  GLY A N   
701  C  CA  A GLY A 86  ? 0.2308 0.2551 0.2362 -0.0102 0.0527  -0.0024 86  GLY A CA  
702  C  CA  B GLY A 86  ? 0.3391 0.2469 0.1582 -0.0340 0.0094  -0.0136 86  GLY A CA  
703  C  C   A GLY A 86  ? 0.3271 0.1560 0.3391 -0.0182 0.1360  -0.0663 86  GLY A C   
704  C  C   B GLY A 86  ? 0.2486 0.2078 0.2524 -0.0560 0.0028  -0.0518 86  GLY A C   
705  O  O   A GLY A 86  ? 0.3648 0.2540 0.3287 -0.1400 0.1298  -0.1084 86  GLY A O   
706  O  O   B GLY A 86  ? 0.2781 0.2128 0.2992 -0.0318 0.1155  -0.0810 86  GLY A O   
707  N  N   . THR A 87  ? 0.1938 0.1644 0.2443 -0.0135 0.0310  -0.0423 87  THR A N   
708  C  CA  . THR A 87  ? 0.1906 0.1898 0.2538 0.0249  0.0348  -0.0654 87  THR A CA  
709  C  C   . THR A 87  ? 0.1520 0.1157 0.2284 -0.0043 0.0065  -0.0273 87  THR A C   
710  O  O   . THR A 87  ? 0.1633 0.1198 0.2355 -0.0015 0.0088  -0.0307 87  THR A O   
711  C  CB  . THR A 87  ? 0.1733 0.3115 0.2845 0.1066  -0.0026 -0.0810 87  THR A CB  
712  O  OG1 . THR A 87  ? 0.2400 0.3526 0.4282 0.0910  0.0375  -0.0838 87  THR A OG1 
713  C  CG2 . THR A 87  ? 0.2034 0.2748 0.3034 0.0807  -0.0173 -0.0083 87  THR A CG2 
714  N  N   . TYR A 88  ? 0.1277 0.1184 0.1941 0.0113  0.0021  -0.0287 88  TYR A N   
715  C  CA  . TYR A 88  ? 0.1264 0.1234 0.1622 0.0024  -0.0013 -0.0221 88  TYR A CA  
716  C  C   . TYR A 88  ? 0.1173 0.1209 0.1746 0.0154  -0.0155 -0.0203 88  TYR A C   
717  O  O   . TYR A 88  ? 0.1391 0.1756 0.2020 -0.0392 -0.0328 0.0015  88  TYR A O   
718  C  CB  . TYR A 88  ? 0.1449 0.1076 0.1826 0.0131  -0.0208 -0.0318 88  TYR A CB  
719  C  CG  . TYR A 88  ? 0.1305 0.0974 0.1607 0.0109  0.0138  -0.0166 88  TYR A CG  
720  C  CD1 . TYR A 88  ? 0.1422 0.1195 0.1671 0.0046  0.0000  -0.0141 88  TYR A CD1 
721  C  CD2 . TYR A 88  ? 0.1357 0.0904 0.1627 0.0125  0.0003  -0.0172 88  TYR A CD2 
722  C  CE1 . TYR A 88  ? 0.1253 0.1229 0.1710 0.0177  0.0273  -0.0085 88  TYR A CE1 
723  C  CE2 . TYR A 88  ? 0.1263 0.0922 0.1340 -0.0010 0.0070  -0.0010 88  TYR A CE2 
724  C  CZ  . TYR A 88  ? 0.1386 0.0956 0.1494 -0.0052 -0.0068 -0.0217 88  TYR A CZ  
725  O  OH  . TYR A 88  ? 0.1297 0.1099 0.1518 -0.0026 0.0144  -0.0227 88  TYR A OH  
726  N  N   A ARG A 89  ? 0.1067 0.1204 0.1701 0.0119  -0.0151 -0.0317 89  ARG A N   
727  N  N   B ARG A 89  ? 0.1121 0.1191 0.1726 0.0136  -0.0131 -0.0274 89  ARG A N   
728  C  CA  A ARG A 89  ? 0.1446 0.1080 0.1864 0.0126  -0.0491 -0.0126 89  ARG A CA  
729  C  CA  B ARG A 89  ? 0.1467 0.0958 0.1879 0.0187  -0.0388 0.0074  89  ARG A CA  
730  C  C   A ARG A 89  ? 0.1208 0.0855 0.1307 -0.0093 -0.0229 0.0189  89  ARG A C   
731  C  C   B ARG A 89  ? 0.1199 0.0847 0.1323 -0.0092 -0.0228 0.0193  89  ARG A C   
732  O  O   A ARG A 89  ? 0.1089 0.0934 0.1293 -0.0038 -0.0146 0.0097  89  ARG A O   
733  O  O   B ARG A 89  ? 0.1083 0.0939 0.1292 -0.0049 -0.0149 0.0098  89  ARG A O   
734  C  CB  A ARG A 89  ? 0.1662 0.0957 0.2561 0.0046  -0.0992 0.0127  89  ARG A CB  
735  C  CB  B ARG A 89  ? 0.2267 0.0692 0.2626 0.0206  -0.0405 0.0215  89  ARG A CB  
736  C  CG  A ARG A 89  ? 0.2273 0.1753 0.2443 0.0619  -0.0537 -0.0401 89  ARG A CG  
737  C  CG  B ARG A 89  ? 0.2896 0.0850 0.1876 0.0135  -0.0322 0.0124  89  ARG A CG  
738  C  CD  A ARG A 89  ? 0.3253 0.2307 0.2648 0.1266  -0.0619 0.0189  89  ARG A CD  
739  C  CD  B ARG A 89  ? 0.2472 0.1622 0.1423 0.0401  0.0114  0.0388  89  ARG A CD  
740  N  NE  A ARG A 89  ? 0.3079 0.2419 0.2711 0.1023  -0.1486 -0.0588 89  ARG A NE  
741  N  NE  B ARG A 89  ? 0.3883 0.0693 0.1534 0.0192  -0.0285 0.0142  89  ARG A NE  
742  C  CZ  A ARG A 89  ? 0.3204 0.2852 0.2429 0.0860  -0.0935 -0.0410 89  ARG A CZ  
743  C  CZ  B ARG A 89  ? 0.2436 0.0816 0.1617 -0.0174 0.0083  0.0287  89  ARG A CZ  
744  N  NH1 A ARG A 89  ? 0.4399 0.1068 0.2217 0.0265  -0.1727 -0.0255 89  ARG A NH1 
745  N  NH1 B ARG A 89  ? 0.2978 0.1333 0.2644 -0.0304 0.0390  0.0811  89  ARG A NH1 
746  N  NH2 A ARG A 89  ? 0.4041 0.1872 0.3167 0.0412  -0.0720 -0.0913 89  ARG A NH2 
747  N  NH2 B ARG A 89  ? 0.3422 0.0899 0.1977 0.0439  0.0520  0.0361  89  ARG A NH2 
748  N  N   . LEU A 90  ? 0.1222 0.1026 0.1339 -0.0054 -0.0273 0.0073  90  LEU A N   
749  C  CA  . LEU A 90  ? 0.1368 0.0958 0.1206 -0.0124 -0.0167 0.0091  90  LEU A CA  
750  C  C   . LEU A 90  ? 0.1480 0.0993 0.1159 -0.0097 -0.0342 0.0144  90  LEU A C   
751  O  O   . LEU A 90  ? 0.1571 0.1317 0.1449 0.0006  -0.0270 0.0406  90  LEU A O   
752  C  CB  . LEU A 90  ? 0.1393 0.1119 0.1347 -0.0185 -0.0226 -0.0044 90  LEU A CB  
753  C  CG  . LEU A 90  ? 0.1587 0.1145 0.1350 -0.0253 -0.0264 0.0000  90  LEU A CG  
754  C  CD1 . LEU A 90  ? 0.1611 0.1094 0.1430 -0.0175 -0.0210 0.0001  90  LEU A CD1 
755  C  CD2 . LEU A 90  ? 0.1509 0.1533 0.1630 -0.0254 -0.0377 -0.0031 90  LEU A CD2 
756  N  N   . ILE A 91  ? 0.1402 0.0882 0.1058 -0.0049 -0.0121 0.0035  91  ILE A N   
757  C  CA  . ILE A 91  ? 0.1430 0.0859 0.1187 -0.0125 -0.0151 0.0116  91  ILE A CA  
758  C  C   . ILE A 91  ? 0.1234 0.0790 0.1009 -0.0074 -0.0103 0.0082  91  ILE A C   
759  O  O   . ILE A 91  ? 0.1433 0.0942 0.1010 -0.0140 -0.0153 0.0132  91  ILE A O   
760  C  CB  . ILE A 91  ? 0.1624 0.0948 0.1119 -0.0137 -0.0049 -0.0026 91  ILE A CB  
761  C  CG1 . ILE A 91  ? 0.1703 0.1431 0.1356 -0.0577 -0.0126 0.0105  91  ILE A CG1 
762  C  CG2 . ILE A 91  ? 0.1581 0.1116 0.1193 -0.0216 -0.0192 0.0093  91  ILE A CG2 
763  C  CD1 . ILE A 91  ? 0.1959 0.1697 0.1510 -0.0675 0.0078  0.0038  91  ILE A CD1 
764  N  N   . GLN A 92  ? 0.1326 0.0766 0.1036 -0.0091 -0.0152 0.0149  92  GLN A N   
765  C  CA  . GLN A 92  ? 0.1331 0.0769 0.0948 0.0020  -0.0108 0.0104  92  GLN A CA  
766  C  C   . GLN A 92  ? 0.1164 0.0811 0.0957 -0.0100 -0.0148 0.0048  92  GLN A C   
767  O  O   . GLN A 92  ? 0.1342 0.0826 0.0939 -0.0035 -0.0078 0.0082  92  GLN A O   
768  C  CB  . GLN A 92  ? 0.1555 0.0984 0.1094 -0.0003 -0.0156 0.0146  92  GLN A CB  
769  C  CG  . GLN A 92  ? 0.1501 0.0925 0.1413 -0.0065 -0.0199 0.0060  92  GLN A CG  
770  C  CD  . GLN A 92  ? 0.1315 0.1042 0.1022 -0.0153 -0.0164 0.0021  92  GLN A CD  
771  O  OE1 . GLN A 92  ? 0.1455 0.0934 0.1204 -0.0125 -0.0151 0.0109  92  GLN A OE1 
772  N  NE2 . GLN A 92  ? 0.1512 0.1429 0.1609 -0.0093 -0.0174 0.0296  92  GLN A NE2 
773  N  N   . PHE A 93  ? 0.1277 0.0731 0.0954 -0.0032 -0.0096 0.0054  93  PHE A N   
774  C  CA  . PHE A 93  ? 0.1286 0.0776 0.0947 -0.0070 -0.0136 0.0046  93  PHE A CA  
775  C  C   . PHE A 93  ? 0.1245 0.0807 0.0830 -0.0120 -0.0131 0.0124  93  PHE A C   
776  O  O   . PHE A 93  ? 0.1415 0.0939 0.0914 -0.0044 -0.0154 0.0115  93  PHE A O   
777  C  CB  . PHE A 93  ? 0.1272 0.0917 0.1024 -0.0091 -0.0291 0.0142  93  PHE A CB  
778  C  CG  . PHE A 93  ? 0.1198 0.0830 0.1130 -0.0155 -0.0276 0.0074  93  PHE A CG  
779  C  CD1 . PHE A 93  ? 0.1471 0.0992 0.1010 -0.0071 -0.0229 0.0032  93  PHE A CD1 
780  C  CD2 . PHE A 93  ? 0.1253 0.1046 0.1146 -0.0126 -0.0322 0.0138  93  PHE A CD2 
781  C  CE1 . PHE A 93  ? 0.1361 0.1009 0.1262 -0.0049 -0.0362 0.0041  93  PHE A CE1 
782  C  CE2 . PHE A 93  ? 0.1503 0.1101 0.1278 -0.0041 -0.0428 0.0088  93  PHE A CE2 
783  C  CZ  . PHE A 93  ? 0.1585 0.1089 0.1256 -0.0043 -0.0553 -0.0020 93  PHE A CZ  
784  N  N   . HIS A 94  ? 0.1202 0.0820 0.0844 -0.0065 -0.0121 0.0008  94  HIS A N   
785  C  CA  . HIS A 94  ? 0.1272 0.0865 0.0820 -0.0142 -0.0126 0.0063  94  HIS A CA  
786  C  C   . HIS A 94  ? 0.1080 0.0816 0.0803 -0.0099 -0.0114 -0.0031 94  HIS A C   
787  O  O   . HIS A 94  ? 0.1209 0.0864 0.0813 -0.0021 0.0024  0.0107  94  HIS A O   
788  C  CB  . HIS A 94  ? 0.1350 0.0939 0.0949 -0.0179 -0.0113 0.0074  94  HIS A CB  
789  C  CG  . HIS A 94  ? 0.1178 0.0822 0.0794 -0.0147 0.0003  0.0021  94  HIS A CG  
790  N  ND1 . HIS A 94  ? 0.1130 0.0822 0.0895 -0.0186 -0.0030 0.0057  94  HIS A ND1 
791  C  CD2 . HIS A 94  ? 0.1137 0.0988 0.0678 -0.0132 -0.0051 0.0015  94  HIS A CD2 
792  C  CE1 . HIS A 94  ? 0.1017 0.0835 0.0925 -0.0168 -0.0063 0.0076  94  HIS A CE1 
793  N  NE2 . HIS A 94  ? 0.1045 0.0798 0.0909 -0.0172 -0.0076 0.0035  94  HIS A NE2 
794  N  N   . PHE A 95  ? 0.1141 0.0820 0.0866 -0.0165 -0.0074 0.0073  95  PHE A N   
795  C  CA  . PHE A 95  ? 0.1114 0.0822 0.0888 -0.0055 -0.0104 0.0071  95  PHE A CA  
796  C  C   . PHE A 95  ? 0.1145 0.0847 0.0812 -0.0110 0.0021  -0.0008 95  PHE A C   
797  O  O   . PHE A 95  ? 0.1168 0.1014 0.1017 -0.0129 0.0006  0.0133  95  PHE A O   
798  C  CB  . PHE A 95  ? 0.1227 0.0872 0.1039 -0.0135 -0.0130 -0.0007 95  PHE A CB  
799  C  CG  . PHE A 95  ? 0.1173 0.0812 0.0855 -0.0113 -0.0098 -0.0019 95  PHE A CG  
800  C  CD1 . PHE A 95  ? 0.1435 0.0956 0.1058 0.0031  -0.0170 -0.0082 95  PHE A CD1 
801  C  CD2 . PHE A 95  ? 0.1218 0.1000 0.1064 -0.0137 -0.0104 -0.0122 95  PHE A CD2 
802  C  CE1 . PHE A 95  ? 0.1460 0.1124 0.1114 -0.0027 -0.0266 -0.0109 95  PHE A CE1 
803  C  CE2 . PHE A 95  ? 0.1376 0.1027 0.1160 -0.0066 -0.0174 -0.0258 95  PHE A CE2 
804  C  CZ  . PHE A 95  ? 0.1300 0.1099 0.1150 0.0057  -0.0270 -0.0212 95  PHE A CZ  
805  N  N   . HIS A 96  ? 0.1048 0.0803 0.0838 -0.0055 -0.0038 -0.0023 96  HIS A N   
806  C  CA  . HIS A 96  ? 0.1045 0.0857 0.0907 -0.0132 0.0049  -0.0005 96  HIS A CA  
807  C  C   . HIS A 96  ? 0.1005 0.0851 0.0844 -0.0063 0.0066  0.0015  96  HIS A C   
808  O  O   . HIS A 96  ? 0.1101 0.0903 0.0984 -0.0074 0.0066  -0.0063 96  HIS A O   
809  C  CB  . HIS A 96  ? 0.1106 0.0812 0.0996 -0.0043 -0.0131 -0.0052 96  HIS A CB  
810  C  CG  . HIS A 96  ? 0.1000 0.0988 0.0942 -0.0046 -0.0035 -0.0043 96  HIS A CG  
811  N  ND1 . HIS A 96  ? 0.1119 0.0904 0.1397 -0.0043 -0.0043 -0.0125 96  HIS A ND1 
812  C  CD2 . HIS A 96  ? 0.1064 0.0842 0.0786 -0.0105 -0.0024 -0.0063 96  HIS A CD2 
813  C  CE1 . HIS A 96  ? 0.0993 0.0976 0.1268 0.0044  -0.0070 -0.0125 96  HIS A CE1 
814  N  NE2 . HIS A 96  ? 0.0922 0.0768 0.0909 -0.0021 -0.0030 -0.0007 96  HIS A NE2 
815  N  N   . TRP A 97  ? 0.1032 0.0839 0.0829 -0.0032 0.0055  -0.0013 97  TRP A N   
816  C  CA  . TRP A 97  ? 0.1157 0.0885 0.0996 -0.0089 -0.0007 -0.0113 97  TRP A CA  
817  C  C   . TRP A 97  ? 0.1076 0.0900 0.0856 0.0000  0.0034  -0.0070 97  TRP A C   
818  O  O   . TRP A 97  ? 0.1209 0.0925 0.1036 -0.0028 0.0131  -0.0093 97  TRP A O   
819  C  CB  . TRP A 97  ? 0.1243 0.0976 0.0930 -0.0149 -0.0008 -0.0085 97  TRP A CB  
820  C  CG  . TRP A 97  ? 0.1325 0.1001 0.0865 -0.0171 -0.0083 -0.0126 97  TRP A CG  
821  C  CD1 . TRP A 97  ? 0.1393 0.1058 0.0892 -0.0092 0.0126  -0.0148 97  TRP A CD1 
822  C  CD2 . TRP A 97  ? 0.1416 0.0923 0.0812 -0.0166 -0.0020 -0.0032 97  TRP A CD2 
823  N  NE1 . TRP A 97  ? 0.1615 0.1098 0.0992 -0.0070 0.0144  -0.0092 97  TRP A NE1 
824  C  CE2 . TRP A 97  ? 0.1471 0.1027 0.0925 -0.0217 0.0065  -0.0116 97  TRP A CE2 
825  C  CE3 . TRP A 97  ? 0.1279 0.0960 0.0944 -0.0104 -0.0216 -0.0046 97  TRP A CE3 
826  C  CZ2 . TRP A 97  ? 0.1559 0.1227 0.1036 -0.0125 0.0015  0.0019  97  TRP A CZ2 
827  C  CZ3 . TRP A 97  ? 0.1571 0.1014 0.0930 -0.0107 -0.0048 0.0003  97  TRP A CZ3 
828  C  CH2 . TRP A 97  ? 0.1571 0.1142 0.0898 -0.0096 -0.0068 -0.0057 97  TRP A CH2 
829  N  N   . GLY A 98  ? 0.1207 0.0905 0.0948 -0.0065 0.0087  -0.0130 98  GLY A N   
830  C  CA  . GLY A 98  ? 0.1221 0.1071 0.1058 0.0013  0.0148  -0.0057 98  GLY A CA  
831  C  C   . GLY A 98  ? 0.1279 0.0998 0.1166 -0.0032 0.0107  -0.0148 98  GLY A C   
832  O  O   . GLY A 98  ? 0.1624 0.1049 0.1284 -0.0091 0.0008  -0.0208 98  GLY A O   
833  N  N   . SER A 99  ? 0.1473 0.1048 0.1220 -0.0005 0.0164  -0.0209 99  SER A N   
834  C  CA  . SER A 99  ? 0.1775 0.1231 0.1404 -0.0043 0.0142  -0.0524 99  SER A CA  
835  C  C   . SER A 99  ? 0.2048 0.1071 0.1784 0.0124  -0.0173 -0.0522 99  SER A C   
836  O  O   . SER A 99  ? 0.2365 0.1402 0.1748 -0.0065 -0.0116 -0.0524 99  SER A O   
837  C  CB  . SER A 99  ? 0.1850 0.1397 0.1668 0.0044  0.0284  -0.0406 99  SER A CB  
838  O  OG  . SER A 99  ? 0.1652 0.1239 0.1941 0.0208  0.0192  -0.0240 99  SER A OG  
839  N  N   . LEU A 100 ? 0.1456 0.1182 0.1718 -0.0019 0.0135  -0.0329 100 LEU A N   
840  C  CA  . LEU A 100 ? 0.1939 0.0948 0.2222 0.0176  0.0201  -0.0310 100 LEU A CA  
841  C  C   . LEU A 100 ? 0.1623 0.0917 0.1825 -0.0073 0.0054  -0.0151 100 LEU A C   
842  O  O   . LEU A 100 ? 0.1675 0.0969 0.1746 -0.0046 0.0080  -0.0203 100 LEU A O   
843  C  CB  . LEU A 100 ? 0.2545 0.1542 0.2531 0.0529  0.0568  0.0057  100 LEU A CB  
844  C  CG  . LEU A 100 ? 0.2813 0.1962 0.2547 0.0608  0.0318  -0.0214 100 LEU A CG  
845  C  CD1 . LEU A 100 ? 0.2545 0.4052 0.4176 0.1620  0.0515  0.0355  100 LEU A CD1 
846  C  CD2 . LEU A 100 ? 0.3835 0.2648 0.3350 0.0302  0.1255  -0.1316 100 LEU A CD2 
847  N  N   . ASP A 101 ? 0.1572 0.0980 0.2069 -0.0133 -0.0003 -0.0211 101 ASP A N   
848  C  CA  . ASP A 101 ? 0.1844 0.0980 0.1666 -0.0118 0.0070  0.0028  101 ASP A CA  
849  C  C   . ASP A 101 ? 0.1704 0.0816 0.1886 -0.0032 0.0147  -0.0100 101 ASP A C   
850  O  O   . ASP A 101 ? 0.2405 0.1277 0.1709 0.0027  0.0194  -0.0076 101 ASP A O   
851  C  CB  . ASP A 101 ? 0.1695 0.1118 0.1942 -0.0124 0.0071  0.0071  101 ASP A CB  
852  C  CG  . ASP A 101 ? 0.1780 0.1189 0.2134 -0.0278 0.0088  0.0037  101 ASP A CG  
853  O  OD1 . ASP A 101 ? 0.2152 0.1536 0.1782 -0.0342 0.0110  -0.0142 101 ASP A OD1 
854  O  OD2 . ASP A 101 ? 0.2705 0.1957 0.2822 -0.1004 -0.0147 0.0114  101 ASP A OD2 
855  N  N   . GLY A 102 ? 0.1870 0.1041 0.1955 -0.0272 -0.0164 0.0308  102 GLY A N   
856  C  CA  . GLY A 102 ? 0.2280 0.1264 0.2071 -0.0353 -0.0142 0.0465  102 GLY A CA  
857  C  C   . GLY A 102 ? 0.1706 0.1157 0.1527 -0.0049 0.0076  0.0208  102 GLY A C   
858  O  O   . GLY A 102 ? 0.2019 0.1321 0.1642 -0.0060 0.0089  0.0318  102 GLY A O   
859  N  N   A GLN A 103 ? 0.1177 0.0908 0.1415 -0.0131 0.0000  0.0105  103 GLN A N   
860  N  N   B GLN A 103 ? 0.1172 0.0907 0.1492 0.0000  0.0198  0.0104  103 GLN A N   
861  C  CA  A GLN A 103 ? 0.1202 0.0993 0.0988 -0.0063 0.0065  0.0007  103 GLN A CA  
862  C  CA  B GLN A 103 ? 0.1212 0.1022 0.1215 0.0146  0.0013  0.0000  103 GLN A CA  
863  C  C   A GLN A 103 ? 0.0824 0.0813 0.1076 0.0049  0.0163  0.0008  103 GLN A C   
864  C  C   B GLN A 103 ? 0.0983 0.0891 0.1282 -0.0055 -0.0012 -0.0030 103 GLN A C   
865  O  O   A GLN A 103 ? 0.0837 0.0860 0.1080 0.0024  0.0046  -0.0133 103 GLN A O   
866  O  O   B GLN A 103 ? 0.1190 0.0983 0.1301 -0.0032 -0.0184 -0.0086 103 GLN A O   
867  C  CB  A GLN A 103 ? 0.1380 0.0916 0.1132 0.0006  -0.0076 -0.0130 103 GLN A CB  
868  C  CB  B GLN A 103 ? 0.1193 0.1365 0.1046 0.0111  -0.0108 0.0057  103 GLN A CB  
869  C  CG  A GLN A 103 ? 0.1458 0.1218 0.1155 0.0211  0.0120  -0.0060 103 GLN A CG  
870  C  CG  B GLN A 103 ? 0.1190 0.1221 0.1279 0.0048  0.0082  -0.0077 103 GLN A CG  
871  C  CD  A GLN A 103 ? 0.1446 0.1110 0.1753 0.0115  0.0114  0.0017  103 GLN A CD  
872  C  CD  B GLN A 103 ? 0.1363 0.1264 0.1914 0.0267  0.0160  0.0137  103 GLN A CD  
873  O  OE1 A GLN A 103 ? 0.1674 0.1292 0.2093 0.0452  0.0366  0.0305  103 GLN A OE1 
874  O  OE1 B GLN A 103 ? 0.1800 0.2058 0.2362 0.0606  0.0239  0.0595  103 GLN A OE1 
875  N  NE2 A GLN A 103 ? 0.1489 0.1412 0.1758 0.0078  0.0043  0.0010  103 GLN A NE2 
876  N  NE2 B GLN A 103 ? 0.1702 0.1563 0.1386 0.0432  0.0238  -0.0032 103 GLN A NE2 
877  N  N   . GLY A 104 ? 0.1177 0.0876 0.1071 -0.0027 0.0109  -0.0046 104 GLY A N   
878  C  CA  . GLY A 104 ? 0.1092 0.0882 0.1013 -0.0051 -0.0005 -0.0026 104 GLY A CA  
879  C  C   . GLY A 104 ? 0.1036 0.0834 0.1018 -0.0049 -0.0017 0.0024  104 GLY A C   
880  O  O   . GLY A 104 ? 0.1112 0.0930 0.1132 -0.0115 0.0074  0.0034  104 GLY A O   
881  N  N   . SER A 105 ? 0.1036 0.0917 0.0942 -0.0008 0.0046  -0.0074 105 SER A N   
882  C  CA  . SER A 105 ? 0.1089 0.0844 0.0930 -0.0051 0.0035  -0.0057 105 SER A CA  
883  C  C   . SER A 105 ? 0.0927 0.0819 0.0847 -0.0024 0.0076  0.0043  105 SER A C   
884  O  O   . SER A 105 ? 0.1177 0.0834 0.1128 0.0015  -0.0087 -0.0078 105 SER A O   
885  C  CB  . SER A 105 ? 0.1119 0.0855 0.1040 -0.0052 0.0026  0.0087  105 SER A CB  
886  O  OG  . SER A 105 ? 0.1121 0.0869 0.1123 -0.0054 0.0060  0.0031  105 SER A OG  
887  N  N   . GLU A 106 ? 0.0974 0.0754 0.0935 -0.0074 0.0030  -0.0035 106 GLU A N   
888  C  CA  . GLU A 106 ? 0.1046 0.0857 0.0894 -0.0122 0.0035  -0.0070 106 GLU A CA  
889  C  C   . GLU A 106 ? 0.0966 0.0806 0.0872 0.0006  -0.0066 0.0020  106 GLU A C   
890  O  O   . GLU A 106 ? 0.0930 0.0952 0.0962 0.0000  0.0031  0.0049  106 GLU A O   
891  C  CB  . GLU A 106 ? 0.1002 0.0891 0.0789 -0.0085 0.0028  0.0017  106 GLU A CB  
892  C  CG  . GLU A 106 ? 0.1439 0.0939 0.1027 -0.0105 0.0186  -0.0020 106 GLU A CG  
893  C  CD  . GLU A 106 ? 0.0939 0.0954 0.0904 -0.0027 0.0083  -0.0091 106 GLU A CD  
894  O  OE1 . GLU A 106 ? 0.0896 0.0886 0.1105 -0.0060 -0.0001 -0.0013 106 GLU A OE1 
895  O  OE2 . GLU A 106 ? 0.1009 0.1141 0.1222 0.0000  0.0081  -0.0081 106 GLU A OE2 
896  N  N   . HIS A 107 ? 0.0940 0.0810 0.0844 0.0012  0.0049  0.0046  107 HIS A N   
897  C  CA  . HIS A 107 ? 0.1040 0.0788 0.0834 -0.0003 -0.0023 0.0003  107 HIS A CA  
898  C  C   . HIS A 107 ? 0.0926 0.0869 0.0838 0.0015  0.0054  0.0093  107 HIS A C   
899  O  O   . HIS A 107 ? 0.1101 0.0872 0.0974 -0.0006 -0.0048 0.0035  107 HIS A O   
900  C  CB  . HIS A 107 ? 0.1010 0.0851 0.0913 0.0017  0.0034  -0.0008 107 HIS A CB  
901  C  CG  . HIS A 107 ? 0.0848 0.0904 0.0903 0.0085  0.0023  0.0010  107 HIS A CG  
902  N  ND1 . HIS A 107 ? 0.0996 0.0803 0.0952 0.0027  -0.0010 0.0060  107 HIS A ND1 
903  C  CD2 . HIS A 107 ? 0.0851 0.0882 0.0952 0.0113  0.0044  -0.0044 107 HIS A CD2 
904  C  CE1 . HIS A 107 ? 0.1062 0.0813 0.0979 0.0063  0.0006  0.0000  107 HIS A CE1 
905  N  NE2 . HIS A 107 ? 0.1020 0.0916 0.0866 0.0087  -0.0024 -0.0066 107 HIS A NE2 
906  N  N   . THR A 108 ? 0.1078 0.0901 0.1017 -0.0041 0.0060  0.0116  108 THR A N   
907  C  CA  . THR A 108 ? 0.1198 0.0815 0.1057 0.0006  0.0105  0.0174  108 THR A CA  
908  C  C   . THR A 108 ? 0.1155 0.0860 0.1023 0.0100  -0.0087 0.0165  108 THR A C   
909  O  O   . THR A 108 ? 0.1186 0.0973 0.1080 0.0001  0.0040  0.0074  108 THR A O   
910  C  CB  . THR A 108 ? 0.1227 0.1005 0.1058 0.0146  0.0012  0.0052  108 THR A CB  
911  O  OG1 . THR A 108 ? 0.1331 0.0991 0.1133 0.0160  -0.0030 0.0024  108 THR A OG1 
912  C  CG2 . THR A 108 ? 0.1388 0.1071 0.1172 0.0118  0.0097  0.0031  108 THR A CG2 
913  N  N   . VAL A 109 ? 0.1224 0.1008 0.1057 0.0024  0.0046  0.0142  109 VAL A N   
914  C  CA  . VAL A 109 ? 0.1327 0.1005 0.1130 -0.0021 0.0121  0.0231  109 VAL A CA  
915  C  C   . VAL A 109 ? 0.1222 0.1127 0.1421 -0.0035 0.0119  0.0195  109 VAL A C   
916  O  O   . VAL A 109 ? 0.1481 0.1035 0.1442 -0.0065 0.0205  0.0304  109 VAL A O   
917  C  CB  . VAL A 109 ? 0.1368 0.1238 0.1562 0.0010  0.0082  0.0331  109 VAL A CB  
918  C  CG1 . VAL A 109 ? 0.1518 0.1488 0.1700 -0.0059 0.0280  0.0478  109 VAL A CG1 
919  C  CG2 . VAL A 109 ? 0.1284 0.1356 0.1404 0.0015  -0.0093 0.0296  109 VAL A CG2 
920  N  N   . ASP A 110 ? 0.1588 0.1046 0.1314 0.0063  0.0129  0.0335  110 ASP A N   
921  C  CA  . ASP A 110 ? 0.1911 0.1193 0.1473 0.0168  0.0283  0.0445  110 ASP A CA  
922  C  C   . ASP A 110 ? 0.1713 0.1049 0.1225 0.0032  0.0052  0.0281  110 ASP A C   
923  O  O   . ASP A 110 ? 0.1875 0.1057 0.1425 0.0126  0.0127  0.0364  110 ASP A O   
924  C  CB  . ASP A 110 ? 0.2060 0.1365 0.1652 0.0118  0.0469  0.0432  110 ASP A CB  
925  C  CG  . ASP A 110 ? 0.1978 0.1670 0.1832 -0.0035 0.0298  0.0745  110 ASP A CG  
926  O  OD1 . ASP A 110 ? 0.2090 0.1831 0.1749 0.0187  0.0478  0.0450  110 ASP A OD1 
927  O  OD2 . ASP A 110 ? 0.2100 0.2319 0.2006 0.0156  0.0500  0.0465  110 ASP A OD2 
928  N  N   . LYS A 111 ? 0.1427 0.1089 0.1266 0.0093  -0.0054 0.0205  111 LYS A N   
929  C  CA  . LYS A 111 ? 0.1634 0.1121 0.1236 0.0184  0.0010  0.0181  111 LYS A CA  
930  C  C   . LYS A 111 ? 0.1657 0.1053 0.1209 0.0012  0.0088  0.0230  111 LYS A C   
931  O  O   . LYS A 111 ? 0.1643 0.1386 0.1494 0.0091  0.0065  0.0031  111 LYS A O   
932  C  CB  . LYS A 111 ? 0.1740 0.1544 0.1480 0.0333  0.0035  0.0288  111 LYS A CB  
933  C  CG  . LYS A 111 ? 0.2275 0.2181 0.1776 0.0683  -0.0346 0.0001  111 LYS A CG  
934  C  CD  . LYS A 111 ? 0.2291 0.2998 0.2294 0.0416  -0.0750 -0.0465 111 LYS A CD  
935  C  CE  . LYS A 111 ? 0.3244 0.4514 0.3034 0.0851  -0.0908 -0.1203 111 LYS A CE  
936  N  NZ  . LYS A 111 ? 0.2910 0.5971 0.4891 0.0469  -0.1462 0.1381  111 LYS A NZ  
937  N  N   . LYS A 112 ? 0.1536 0.1013 0.1236 -0.0028 0.0020  0.0212  112 LYS A N   
938  C  CA  . LYS A 112 ? 0.1599 0.1148 0.1245 -0.0080 0.0052  0.0115  112 LYS A CA  
939  C  C   . LYS A 112 ? 0.1347 0.0891 0.1296 -0.0008 -0.0024 0.0151  112 LYS A C   
940  O  O   . LYS A 112 ? 0.1360 0.0986 0.1215 -0.0043 0.0057  0.0034  112 LYS A O   
941  C  CB  . LYS A 112 ? 0.1699 0.1556 0.1591 -0.0408 0.0187  0.0152  112 LYS A CB  
942  C  CG  . LYS A 112 ? 0.1749 0.1865 0.1832 -0.0428 0.0124  -0.0241 112 LYS A CG  
943  C  CD  . LYS A 112 ? 0.1788 0.2567 0.2230 -0.0306 -0.0124 0.0328  112 LYS A CD  
944  C  CE  . LYS A 112 ? 0.3057 0.2479 0.2633 -0.0308 -0.0533 -0.0208 112 LYS A CE  
945  N  NZ  . LYS A 112 ? 0.2858 0.2522 0.2728 -0.0295 -0.0631 0.0324  112 LYS A NZ  
946  N  N   A LYS A 113 ? 0.1098 0.0842 0.1177 0.0099  0.0038  0.0038  113 LYS A N   
947  N  N   B LYS A 113 ? 0.1146 0.1216 0.1293 0.0015  0.0098  0.0027  113 LYS A N   
948  C  CA  A LYS A 113 ? 0.1143 0.0795 0.1209 0.0057  0.0094  0.0188  113 LYS A CA  
949  C  CA  B LYS A 113 ? 0.1307 0.1071 0.1141 0.0026  -0.0063 0.0093  113 LYS A CA  
950  C  C   A LYS A 113 ? 0.1268 0.0734 0.1265 0.0116  0.0245  0.0148  113 LYS A C   
951  C  C   B LYS A 113 ? 0.1254 0.0819 0.1215 0.0144  0.0168  -0.0021 113 LYS A C   
952  O  O   A LYS A 113 ? 0.1472 0.0731 0.1772 -0.0052 0.0183  0.0027  113 LYS A O   
953  O  O   B LYS A 113 ? 0.1215 0.0768 0.1198 0.0074  0.0199  -0.0007 113 LYS A O   
954  C  CB  A LYS A 113 ? 0.1083 0.1094 0.1238 -0.0116 0.0007  0.0115  113 LYS A CB  
955  C  CB  B LYS A 113 ? 0.1229 0.1190 0.1462 0.0141  -0.0109 -0.0157 113 LYS A CB  
956  C  CG  A LYS A 113 ? 0.1245 0.1662 0.1171 0.0031  0.0066  0.0073  113 LYS A CG  
957  C  CG  B LYS A 113 ? 0.1175 0.1500 0.1274 0.0273  -0.0052 0.0113  113 LYS A CG  
958  C  CD  A LYS A 113 ? 0.1213 0.1614 0.1580 0.0020  0.0274  0.0111  113 LYS A CD  
959  C  CD  B LYS A 113 ? 0.1341 0.1053 0.1594 0.0170  0.0247  0.0206  113 LYS A CD  
960  C  CE  A LYS A 113 ? 0.1634 0.1544 0.2222 -0.0068 -0.0102 0.0465  113 LYS A CE  
961  C  CE  B LYS A 113 ? 0.1089 0.2362 0.1677 0.0171  0.0375  0.0087  113 LYS A CE  
962  N  NZ  A LYS A 113 ? 0.1676 0.2072 0.2581 0.0048  0.0317  -0.0262 113 LYS A NZ  
963  N  NZ  B LYS A 113 ? 0.1370 0.1835 0.1844 0.0135  -0.0049 -0.0331 113 LYS A NZ  
964  N  N   . TYR A 114 ? 0.1225 0.0837 0.1296 -0.0013 0.0020  0.0040  114 TYR A N   
965  C  CA  . TYR A 114 ? 0.1037 0.0890 0.1361 -0.0027 -0.0049 0.0052  114 TYR A CA  
966  C  C   . TYR A 114 ? 0.1116 0.0724 0.1191 -0.0080 0.0000  0.0001  114 TYR A C   
967  O  O   . TYR A 114 ? 0.1182 0.0961 0.1265 -0.0048 0.0097  -0.0054 114 TYR A O   
968  C  CB  . TYR A 114 ? 0.1175 0.0967 0.1203 -0.0052 0.0156  0.0049  114 TYR A CB  
969  C  CG  . TYR A 114 ? 0.1280 0.0835 0.1306 0.0049  -0.0104 0.0118  114 TYR A CG  
970  C  CD1 . TYR A 114 ? 0.1489 0.1017 0.1430 0.0065  0.0015  0.0105  114 TYR A CD1 
971  C  CD2 . TYR A 114 ? 0.1162 0.1175 0.1536 -0.0109 0.0126  0.0241  114 TYR A CD2 
972  C  CE1 . TYR A 114 ? 0.1918 0.1406 0.1466 0.0379  0.0105  0.0204  114 TYR A CE1 
973  C  CE2 . TYR A 114 ? 0.1561 0.1431 0.1943 0.0068  0.0351  0.0055  114 TYR A CE2 
974  C  CZ  . TYR A 114 ? 0.1916 0.1704 0.1659 -0.0038 0.0626  0.0318  114 TYR A CZ  
975  O  OH  . TYR A 114 ? 0.2822 0.2811 0.2257 0.0308  0.1173  0.0540  114 TYR A OH  
976  N  N   . ALA A 115 ? 0.1208 0.0800 0.1236 -0.0141 -0.0088 0.0003  115 ALA A N   
977  C  CA  . ALA A 115 ? 0.1298 0.0807 0.1307 -0.0141 -0.0065 -0.0174 115 ALA A CA  
978  C  C   . ALA A 115 ? 0.1089 0.0864 0.1039 -0.0108 0.0000  -0.0043 115 ALA A C   
979  O  O   . ALA A 115 ? 0.1171 0.0848 0.1303 -0.0063 0.0092  -0.0096 115 ALA A O   
980  C  CB  . ALA A 115 ? 0.1615 0.0970 0.1473 -0.0229 -0.0137 -0.0121 115 ALA A CB  
981  N  N   . ALA A 116 ? 0.1186 0.0776 0.1166 -0.0024 -0.0001 -0.0024 116 ALA A N   
982  C  CA  . ALA A 116 ? 0.1216 0.0799 0.1005 -0.0070 -0.0062 -0.0007 116 ALA A CA  
983  C  C   . ALA A 116 ? 0.1028 0.0816 0.0984 -0.0005 -0.0065 0.0003  116 ALA A C   
984  O  O   . ALA A 116 ? 0.1081 0.0824 0.1018 -0.0088 0.0000  0.0048  116 ALA A O   
985  C  CB  . ALA A 116 ? 0.1342 0.1015 0.1042 -0.0076 -0.0059 -0.0076 116 ALA A CB  
986  N  N   . GLU A 117 ? 0.1067 0.0694 0.0948 0.0007  -0.0024 0.0031  117 GLU A N   
987  C  CA  . GLU A 117 ? 0.1001 0.0736 0.0864 -0.0001 0.0003  0.0048  117 GLU A CA  
988  C  C   . GLU A 117 ? 0.1064 0.0914 0.0806 -0.0108 -0.0032 -0.0015 117 GLU A C   
989  O  O   . GLU A 117 ? 0.1211 0.1020 0.1018 0.0076  0.0041  0.0148  117 GLU A O   
990  C  CB  . GLU A 117 ? 0.1087 0.0886 0.0905 0.0076  -0.0046 0.0010  117 GLU A CB  
991  C  CG  . GLU A 117 ? 0.1247 0.0971 0.0864 -0.0006 -0.0052 0.0085  117 GLU A CG  
992  C  CD  . GLU A 117 ? 0.1040 0.0843 0.0882 0.0021  0.0038  0.0049  117 GLU A CD  
993  O  OE1 . GLU A 117 ? 0.1008 0.1039 0.0973 0.0026  -0.0082 0.0010  117 GLU A OE1 
994  O  OE2 . GLU A 117 ? 0.1263 0.0960 0.0918 -0.0003 -0.0147 0.0055  117 GLU A OE2 
995  N  N   . LEU A 118 ? 0.1080 0.0777 0.0903 -0.0048 -0.0152 0.0034  118 LEU A N   
996  C  CA  . LEU A 118 ? 0.0996 0.0672 0.0894 -0.0046 -0.0126 0.0006  118 LEU A CA  
997  C  C   . LEU A 118 ? 0.1023 0.0697 0.0812 -0.0023 -0.0028 0.0034  118 LEU A C   
998  O  O   . LEU A 118 ? 0.1017 0.0777 0.0832 -0.0087 -0.0043 -0.0003 118 LEU A O   
999  C  CB  . LEU A 118 ? 0.1173 0.0841 0.0958 -0.0019 -0.0208 0.0028  118 LEU A CB  
1000 C  CG  . LEU A 118 ? 0.1039 0.0964 0.1026 0.0010  -0.0206 0.0093  118 LEU A CG  
1001 C  CD1 . LEU A 118 ? 0.1309 0.0929 0.1048 -0.0034 -0.0291 0.0086  118 LEU A CD1 
1002 C  CD2 . LEU A 118 ? 0.1083 0.1262 0.1275 -0.0017 -0.0320 0.0104  118 LEU A CD2 
1003 N  N   . HIS A 119 ? 0.0947 0.0697 0.0870 -0.0096 -0.0155 -0.0003 119 HIS A N   
1004 C  CA  . HIS A 119 ? 0.1015 0.0681 0.0854 -0.0032 -0.0136 0.0057  119 HIS A CA  
1005 C  C   . HIS A 119 ? 0.0970 0.0744 0.0781 -0.0173 -0.0100 0.0041  119 HIS A C   
1006 O  O   . HIS A 119 ? 0.1118 0.0894 0.0857 0.0027  -0.0052 0.0110  119 HIS A O   
1007 C  CB  . HIS A 119 ? 0.1066 0.0772 0.0956 0.0031  -0.0032 0.0041  119 HIS A CB  
1008 C  CG  . HIS A 119 ? 0.0887 0.0852 0.0803 -0.0156 -0.0037 -0.0065 119 HIS A CG  
1009 N  ND1 . HIS A 119 ? 0.0885 0.0844 0.0882 -0.0091 -0.0020 0.0013  119 HIS A ND1 
1010 C  CD2 . HIS A 119 ? 0.1032 0.0800 0.0905 -0.0031 -0.0102 0.0041  119 HIS A CD2 
1011 C  CE1 . HIS A 119 ? 0.0948 0.0918 0.0806 -0.0102 -0.0038 -0.0024 119 HIS A CE1 
1012 N  NE2 . HIS A 119 ? 0.0962 0.0907 0.0886 0.0012  -0.0068 0.0060  119 HIS A NE2 
1013 N  N   . LEU A 120 ? 0.1001 0.0760 0.0882 -0.0003 -0.0060 0.0012  120 LEU A N   
1014 C  CA  . LEU A 120 ? 0.1070 0.0688 0.1059 -0.0006 -0.0187 0.0068  120 LEU A CA  
1015 C  C   . LEU A 120 ? 0.0927 0.0756 0.0944 0.0074  -0.0041 0.0077  120 LEU A C   
1016 O  O   . LEU A 120 ? 0.0954 0.0759 0.0917 -0.0041 -0.0107 0.0026  120 LEU A O   
1017 C  CB  . LEU A 120 ? 0.0975 0.0961 0.1187 -0.0087 -0.0269 0.0013  120 LEU A CB  
1018 C  CG  . LEU A 120 ? 0.1248 0.1027 0.1064 -0.0100 -0.0263 -0.0035 120 LEU A CG  
1019 C  CD1 . LEU A 120 ? 0.1911 0.1322 0.1615 -0.0637 -0.0093 0.0021  120 LEU A CD1 
1020 C  CD2 . LEU A 120 ? 0.1351 0.1518 0.1553 0.0110  -0.0540 -0.0078 120 LEU A CD2 
1021 N  N   . VAL A 121 ? 0.1093 0.0786 0.0929 -0.0085 -0.0100 0.0091  121 VAL A N   
1022 C  CA  . VAL A 121 ? 0.1136 0.0728 0.0952 -0.0043 -0.0063 0.0046  121 VAL A CA  
1023 C  C   . VAL A 121 ? 0.0991 0.0756 0.0979 -0.0076 -0.0080 0.0007  121 VAL A C   
1024 O  O   . VAL A 121 ? 0.1196 0.0878 0.0961 -0.0013 -0.0153 0.0066  121 VAL A O   
1025 C  CB  . VAL A 121 ? 0.1154 0.0754 0.1064 -0.0013 -0.0086 0.0037  121 VAL A CB  
1026 C  CG1 . VAL A 121 ? 0.1200 0.0948 0.1121 -0.0120 -0.0023 0.0000  121 VAL A CG1 
1027 C  CG2 . VAL A 121 ? 0.1365 0.0917 0.1089 0.0048  0.0089  0.0023  121 VAL A CG2 
1028 N  N   . HIS A 122 ? 0.1011 0.0731 0.0980 -0.0051 -0.0133 0.0024  122 HIS A N   
1029 C  CA  . HIS A 122 ? 0.1177 0.0676 0.1106 -0.0074 -0.0076 0.0041  122 HIS A CA  
1030 C  C   . HIS A 122 ? 0.1102 0.0763 0.1085 0.0006  -0.0121 -0.0040 122 HIS A C   
1031 O  O   . HIS A 122 ? 0.1256 0.0798 0.1182 -0.0141 -0.0152 0.0073  122 HIS A O   
1032 C  CB  . HIS A 122 ? 0.1105 0.0790 0.1148 0.0013  -0.0071 0.0012  122 HIS A CB  
1033 C  CG  . HIS A 122 ? 0.1101 0.0810 0.1106 0.0040  -0.0055 0.0055  122 HIS A CG  
1034 N  ND1 . HIS A 122 ? 0.1040 0.0798 0.1163 -0.0006 0.0028  -0.0020 122 HIS A ND1 
1035 C  CD2 . HIS A 122 ? 0.1010 0.1028 0.1203 -0.0057 -0.0135 0.0010  122 HIS A CD2 
1036 C  CE1 . HIS A 122 ? 0.1004 0.1019 0.1255 -0.0032 -0.0038 -0.0097 122 HIS A CE1 
1037 N  NE2 . HIS A 122 ? 0.1036 0.1052 0.1325 -0.0049 -0.0126 0.0000  122 HIS A NE2 
1038 N  N   . TRP A 123 ? 0.1084 0.0785 0.1080 -0.0020 -0.0043 -0.0076 123 TRP A N   
1039 C  CA  . TRP A 123 ? 0.1027 0.0788 0.1120 -0.0037 -0.0010 -0.0085 123 TRP A CA  
1040 C  C   . TRP A 123 ? 0.1132 0.0859 0.1119 0.0000  -0.0147 0.0032  123 TRP A C   
1041 O  O   . TRP A 123 ? 0.1164 0.0883 0.1374 0.0034  -0.0133 -0.0083 123 TRP A O   
1042 C  CB  . TRP A 123 ? 0.1251 0.1096 0.1211 -0.0173 0.0003  -0.0044 123 TRP A CB  
1043 C  CG  . TRP A 123 ? 0.1422 0.1018 0.1268 -0.0214 0.0000  0.0031  123 TRP A CG  
1044 C  CD1 . TRP A 123 ? 0.1712 0.1054 0.1229 -0.0189 -0.0171 0.0043  123 TRP A CD1 
1045 C  CD2 . TRP A 123 ? 0.1644 0.0890 0.1245 -0.0226 -0.0107 0.0017  123 TRP A CD2 
1046 N  NE1 . TRP A 123 ? 0.1877 0.0913 0.1449 -0.0172 -0.0188 -0.0008 123 TRP A NE1 
1047 C  CE2 . TRP A 123 ? 0.1961 0.0899 0.1561 -0.0198 -0.0271 0.0049  123 TRP A CE2 
1048 C  CE3 . TRP A 123 ? 0.1977 0.0790 0.1406 -0.0355 -0.0104 0.0057  123 TRP A CE3 
1049 C  CZ2 . TRP A 123 ? 0.2662 0.0971 0.1682 -0.0163 -0.0222 0.0074  123 TRP A CZ2 
1050 C  CZ3 . TRP A 123 ? 0.2380 0.0886 0.1583 -0.0271 -0.0068 0.0131  123 TRP A CZ3 
1051 C  CH2 . TRP A 123 ? 0.2267 0.0952 0.1771 -0.0063 -0.0230 0.0098  123 TRP A CH2 
1052 N  N   . ASN A 124 ? 0.1177 0.0926 0.1251 0.0035  -0.0003 -0.0120 124 ASN A N   
1053 C  CA  . ASN A 124 ? 0.1354 0.0964 0.1361 0.0115  0.0019  -0.0157 124 ASN A CA  
1054 C  C   . ASN A 124 ? 0.1227 0.1010 0.1480 0.0100  -0.0057 -0.0302 124 ASN A C   
1055 O  O   . ASN A 124 ? 0.1324 0.0970 0.1455 0.0020  -0.0007 -0.0146 124 ASN A O   
1056 C  CB  . ASN A 124 ? 0.1402 0.0991 0.1200 -0.0054 0.0020  -0.0074 124 ASN A CB  
1057 C  CG  . ASN A 124 ? 0.1597 0.0976 0.1411 -0.0085 0.0238  -0.0149 124 ASN A CG  
1058 O  OD1 . ASN A 124 ? 0.1631 0.1168 0.1612 0.0152  0.0234  -0.0281 124 ASN A OD1 
1059 N  ND2 . ASN A 124 ? 0.1997 0.1132 0.1511 0.0038  0.0066  -0.0243 124 ASN A ND2 
1060 N  N   . THR A 125 ? 0.1289 0.0926 0.1567 0.0100  -0.0057 -0.0173 125 THR A N   
1061 C  CA  . THR A 125 ? 0.1460 0.0988 0.1978 0.0141  -0.0086 0.0000  125 THR A CA  
1062 C  C   . THR A 125 ? 0.1691 0.0910 0.2046 0.0260  0.0043  0.0052  125 THR A C   
1063 O  O   . THR A 125 ? 0.1770 0.1083 0.2401 0.0160  -0.0034 0.0087  125 THR A O   
1064 C  CB  . THR A 125 ? 0.1816 0.1468 0.2455 0.0148  -0.0381 0.0222  125 THR A CB  
1065 O  OG1 . THR A 125 ? 0.1826 0.1779 0.3097 0.0472  0.0097  -0.0159 125 THR A OG1 
1066 C  CG2 . THR A 125 ? 0.2154 0.1632 0.2685 -0.0082 -0.0776 -0.0098 125 THR A CG2 
1067 N  N   . LYS A 126 ? 0.1861 0.0948 0.1850 0.0144  0.0151  -0.0348 127 LYS A N   
1068 C  CA  . LYS A 126 ? 0.2076 0.1327 0.2091 -0.0082 0.0178  -0.0419 127 LYS A CA  
1069 C  C   . LYS A 126 ? 0.1985 0.0914 0.1863 -0.0068 0.0104  -0.0241 127 LYS A C   
1070 O  O   . LYS A 126 ? 0.2340 0.1092 0.2480 -0.0320 0.0242  -0.0566 127 LYS A O   
1071 C  CB  . LYS A 126 ? 0.2443 0.1806 0.2240 -0.0373 0.0185  -0.0627 127 LYS A CB  
1072 C  CG  . LYS A 126 ? 0.2372 0.2057 0.2031 -0.0428 0.0118  -0.0474 127 LYS A CG  
1073 C  CD  . LYS A 126 ? 0.3073 0.2851 0.2469 -0.0443 -0.0007 -0.0649 127 LYS A CD  
1074 C  CE  . LYS A 126 ? 0.2689 0.2851 0.2570 -0.0089 0.0252  -0.0243 127 LYS A CE  
1075 N  NZ  . LYS A 126 ? 0.4961 0.4483 0.2081 0.1269  0.0496  0.0414  127 LYS A NZ  
1076 N  N   . TYR A 127 ? 0.1785 0.0947 0.1620 -0.0046 -0.0118 -0.0211 128 TYR A N   
1077 C  CA  . TYR A 127 ? 0.1641 0.1055 0.1642 -0.0229 -0.0093 -0.0076 128 TYR A CA  
1078 C  C   . TYR A 127 ? 0.1747 0.1011 0.1823 -0.0127 -0.0010 -0.0167 128 TYR A C   
1079 O  O   . TYR A 127 ? 0.1733 0.1105 0.1844 -0.0108 0.0013  -0.0074 128 TYR A O   
1080 C  CB  . TYR A 127 ? 0.1720 0.1070 0.1762 -0.0059 0.0113  -0.0063 128 TYR A CB  
1081 C  CG  . TYR A 127 ? 0.1545 0.1142 0.1601 -0.0071 -0.0027 -0.0175 128 TYR A CG  
1082 C  CD1 . TYR A 127 ? 0.1772 0.1304 0.1757 -0.0102 -0.0136 -0.0311 128 TYR A CD1 
1083 C  CD2 . TYR A 127 ? 0.1440 0.1157 0.1674 -0.0162 -0.0008 -0.0147 128 TYR A CD2 
1084 C  CE1 . TYR A 127 ? 0.1965 0.1334 0.1759 0.0077  -0.0168 -0.0388 128 TYR A CE1 
1085 C  CE2 . TYR A 127 ? 0.1692 0.1173 0.1611 0.0062  -0.0006 -0.0348 128 TYR A CE2 
1086 C  CZ  . TYR A 127 ? 0.1806 0.1393 0.1634 0.0038  -0.0006 -0.0296 128 TYR A CZ  
1087 O  OH  . TYR A 127 ? 0.2289 0.1502 0.1745 0.0205  -0.0222 -0.0544 128 TYR A OH  
1088 N  N   . GLY A 128 ? 0.1589 0.0986 0.1705 -0.0108 -0.0190 -0.0043 129 GLY A N   
1089 C  CA  . GLY A 128 ? 0.1900 0.0979 0.1961 -0.0054 0.0155  0.0146  129 GLY A CA  
1090 C  C   . GLY A 128 ? 0.1825 0.1141 0.1582 -0.0013 -0.0124 0.0276  129 GLY A C   
1091 O  O   . GLY A 128 ? 0.2415 0.1116 0.1818 0.0043  -0.0196 0.0264  129 GLY A O   
1092 N  N   A ASP A 129 ? 0.1693 0.0945 0.1263 -0.0078 0.0049  0.0013  130 ASP A N   
1093 N  N   B ASP A 129 ? 0.1944 0.0886 0.1586 -0.0062 -0.0040 -0.0108 130 ASP A N   
1094 C  CA  A ASP A 129 ? 0.1365 0.0904 0.1448 -0.0098 0.0228  0.0098  130 ASP A CA  
1095 C  CA  B ASP A 129 ? 0.1439 0.1275 0.1411 -0.0031 -0.0186 0.0065  130 ASP A CA  
1096 C  C   A ASP A 129 ? 0.1404 0.0961 0.1215 -0.0049 0.0099  0.0153  130 ASP A C   
1097 C  C   B ASP A 129 ? 0.1500 0.1199 0.1664 -0.0196 -0.0318 -0.0003 130 ASP A C   
1098 O  O   A ASP A 129 ? 0.1184 0.0966 0.1272 0.0040  0.0030  -0.0019 130 ASP A O   
1099 O  O   B ASP A 129 ? 0.1089 0.1018 0.1274 0.0094  -0.0037 0.0000  130 ASP A O   
1100 C  CB  A ASP A 129 ? 0.1627 0.1225 0.1391 0.0010  0.0190  0.0226  130 ASP A CB  
1101 C  CB  B ASP A 129 ? 0.1510 0.1238 0.1451 0.0096  0.0001  0.0154  130 ASP A CB  
1102 C  CG  A ASP A 129 ? 0.1594 0.0920 0.1448 -0.0104 0.0130  0.0024  130 ASP A CG  
1103 C  CG  B ASP A 129 ? 0.1606 0.1659 0.1817 0.0195  0.0359  0.0230  130 ASP A CG  
1104 O  OD1 A ASP A 129 ? 0.1872 0.1340 0.1689 -0.0270 0.0214  -0.0097 130 ASP A OD1 
1105 O  OD1 B ASP A 129 ? 0.2301 0.1741 0.1791 0.0203  -0.0223 0.0368  130 ASP A OD1 
1106 O  OD2 A ASP A 129 ? 0.2357 0.1313 0.1898 -0.0162 0.0566  0.0265  130 ASP A OD2 
1107 O  OD2 B ASP A 129 ? 0.1986 0.1872 0.3000 -0.0166 -0.0227 0.0676  130 ASP A OD2 
1108 N  N   . PHE A 130 ? 0.2196 0.1020 0.1314 0.0093  -0.0088 0.0015  131 PHE A N   
1109 C  CA  . PHE A 130 ? 0.1957 0.0869 0.1268 0.0076  -0.0068 0.0000  131 PHE A CA  
1110 C  C   . PHE A 130 ? 0.1730 0.1032 0.1243 0.0019  0.0234  0.0071  131 PHE A C   
1111 O  O   . PHE A 130 ? 0.1820 0.1220 0.1084 -0.0176 0.0130  0.0077  131 PHE A O   
1112 C  CB  . PHE A 130 ? 0.1846 0.1080 0.1279 0.0006  0.0078  -0.0031 131 PHE A CB  
1113 C  CG  . PHE A 130 ? 0.1564 0.0942 0.1340 -0.0015 0.0076  -0.0099 131 PHE A CG  
1114 C  CD1 . PHE A 130 ? 0.1577 0.1050 0.1247 -0.0203 -0.0031 -0.0082 131 PHE A CD1 
1115 C  CD2 . PHE A 130 ? 0.2082 0.1013 0.2171 -0.0141 0.0465  0.0138  131 PHE A CD2 
1116 C  CE1 . PHE A 130 ? 0.1544 0.1142 0.1352 -0.0208 -0.0013 -0.0054 131 PHE A CE1 
1117 C  CE2 . PHE A 130 ? 0.2425 0.1255 0.2730 -0.0015 0.0469  0.0258  131 PHE A CE2 
1118 C  CZ  . PHE A 130 ? 0.1898 0.1014 0.1986 -0.0098 0.0013  0.0103  131 PHE A CZ  
1119 N  N   . GLY A 131 ? 0.1931 0.1307 0.1400 -0.0199 0.0222  0.0172  132 GLY A N   
1120 C  CA  . GLY A 131 ? 0.2249 0.1613 0.1565 -0.0335 0.0537  0.0340  132 GLY A CA  
1121 C  C   . GLY A 131 ? 0.1789 0.1503 0.1825 -0.0439 0.0372  0.0177  132 GLY A C   
1122 O  O   . GLY A 131 ? 0.1916 0.1662 0.2305 -0.0200 0.0425  -0.0219 132 GLY A O   
1123 N  N   A LYS A 132 ? 0.1774 0.1247 0.1765 -0.0333 0.0137  0.0130  133 LYS A N   
1124 N  N   B LYS A 132 ? 0.1948 0.1236 0.1809 -0.0375 0.0259  0.0204  133 LYS A N   
1125 C  CA  A LYS A 132 ? 0.1984 0.0944 0.1715 -0.0244 -0.0159 0.0186  133 LYS A CA  
1126 C  CA  B LYS A 132 ? 0.1934 0.1159 0.1952 -0.0390 0.0065  -0.0038 133 LYS A CA  
1127 C  C   A LYS A 132 ? 0.1750 0.1023 0.1569 -0.0408 -0.0034 -0.0032 133 LYS A C   
1128 C  C   B LYS A 132 ? 0.1747 0.1137 0.1616 -0.0388 -0.0065 -0.0098 133 LYS A C   
1129 O  O   A LYS A 132 ? 0.1202 0.1160 0.1476 -0.0230 0.0124  -0.0215 133 LYS A O   
1130 O  O   B LYS A 132 ? 0.1431 0.1195 0.1598 -0.0238 0.0059  -0.0357 133 LYS A O   
1131 C  CB  A LYS A 132 ? 0.1600 0.1141 0.2017 -0.0223 0.0082  0.0104  133 LYS A CB  
1132 C  CB  B LYS A 132 ? 0.2140 0.1024 0.2228 -0.0317 -0.0174 -0.0405 133 LYS A CB  
1133 C  CG  A LYS A 132 ? 0.1525 0.1023 0.2157 0.0188  0.0110  0.0153  133 LYS A CG  
1134 C  CG  B LYS A 132 ? 0.2867 0.1953 0.1826 0.0174  0.0384  0.0241  133 LYS A CG  
1135 C  CD  A LYS A 132 ? 0.2081 0.1447 0.3883 -0.0201 -0.0527 0.1067  133 LYS A CD  
1136 C  CD  B LYS A 132 ? 0.3652 0.4291 0.1635 -0.0813 0.0452  -0.0153 133 LYS A CD  
1137 C  CE  A LYS A 132 ? 0.3463 0.1653 0.3289 -0.0782 0.0286  0.1169  133 LYS A CE  
1138 C  CE  B LYS A 132 ? 0.1983 0.1321 0.1898 -0.0177 -0.0758 0.0122  133 LYS A CE  
1139 N  NZ  A LYS A 132 ? 0.5935 0.2768 0.5417 0.0766  0.0428  -0.1076 133 LYS A NZ  
1140 N  NZ  B LYS A 132 ? 0.4451 0.3450 0.4824 0.0930  0.0425  -0.0496 133 LYS A NZ  
1141 N  N   . ALA A 133 ? 0.1624 0.1045 0.1375 -0.0408 0.0070  -0.0038 134 ALA A N   
1142 C  CA  . ALA A 133 ? 0.1412 0.1204 0.1263 -0.0348 -0.0087 0.0003  134 ALA A CA  
1143 C  C   . ALA A 133 ? 0.1449 0.1105 0.1137 -0.0293 0.0059  -0.0017 134 ALA A C   
1144 O  O   . ALA A 133 ? 0.1202 0.1418 0.1186 -0.0172 0.0041  -0.0046 134 ALA A O   
1145 C  CB  . ALA A 133 ? 0.1415 0.1166 0.1280 -0.0300 -0.0083 -0.0035 134 ALA A CB  
1146 N  N   . VAL A 134 ? 0.1421 0.1245 0.1280 -0.0351 0.0162  -0.0003 135 VAL A N   
1147 C  CA  . VAL A 134 ? 0.1670 0.1221 0.1272 -0.0241 0.0198  0.0126  135 VAL A CA  
1148 C  C   . VAL A 134 ? 0.1454 0.1292 0.1351 -0.0131 0.0299  0.0012  135 VAL A C   
1149 O  O   . VAL A 134 ? 0.1381 0.1474 0.1590 0.0000  0.0258  0.0015  135 VAL A O   
1150 C  CB  . VAL A 134 ? 0.1677 0.1274 0.1635 -0.0282 0.0315  -0.0057 135 VAL A CB  
1151 C  CG1 . VAL A 134 ? 0.2017 0.1682 0.1797 -0.0331 0.0262  -0.0247 135 VAL A CG1 
1152 C  CG2 . VAL A 134 ? 0.1737 0.1523 0.1685 -0.0296 0.0377  -0.0037 135 VAL A CG2 
1153 N  N   . GLN A 135 ? 0.1289 0.1330 0.1527 -0.0217 0.0107  -0.0030 136 GLN A N   
1154 C  CA  . GLN A 135 ? 0.1571 0.1507 0.1652 -0.0329 0.0020  0.0003  136 GLN A CA  
1155 C  C   . GLN A 135 ? 0.1243 0.1431 0.1606 -0.0157 -0.0129 -0.0221 136 GLN A C   
1156 O  O   . GLN A 135 ? 0.1507 0.1992 0.1946 -0.0399 -0.0215 -0.0243 136 GLN A O   
1157 C  CB  . GLN A 135 ? 0.1644 0.1860 0.2114 -0.0635 0.0074  0.0151  136 GLN A CB  
1158 C  CG  . GLN A 135 ? 0.2477 0.2319 0.2409 -0.1039 0.0595  0.0364  136 GLN A CG  
1159 C  CD  . GLN A 135 ? 0.3551 0.4872 0.4528 -0.0785 0.0535  0.0252  136 GLN A CD  
1160 O  OE1 . GLN A 135 ? 0.3436 0.5001 0.4499 -0.0542 0.0436  0.0841  136 GLN A OE1 
1161 N  NE2 . GLN A 135 ? 0.5266 0.3314 0.5037 -0.1902 0.1023  -0.0120 136 GLN A NE2 
1162 N  N   . GLN A 136 ? 0.1233 0.1336 0.1427 -0.0155 0.0055  -0.0153 137 GLN A N   
1163 C  CA  . GLN A 136 ? 0.1388 0.1407 0.1298 -0.0015 -0.0187 -0.0283 137 GLN A CA  
1164 C  C   . GLN A 136 ? 0.1331 0.1380 0.1137 0.0087  0.0023  -0.0215 137 GLN A C   
1165 O  O   . GLN A 136 ? 0.1604 0.1236 0.1075 -0.0066 0.0008  -0.0182 137 GLN A O   
1166 C  CB  . GLN A 136 ? 0.1730 0.1200 0.1562 -0.0040 -0.0083 -0.0173 137 GLN A CB  
1167 C  CG  . GLN A 136 ? 0.2270 0.1772 0.1783 0.0060  0.0275  -0.0094 137 GLN A CG  
1168 C  CD  . GLN A 136 ? 0.2184 0.2344 0.2261 0.0043  0.0344  0.0401  137 GLN A CD  
1169 O  OE1 . GLN A 136 ? 0.2393 0.1587 0.2565 -0.0136 0.0038  -0.0592 137 GLN A OE1 
1170 N  NE2 . GLN A 136 ? 0.2757 0.2894 0.2328 -0.0414 0.0161  0.0008  137 GLN A NE2 
1171 N  N   A PRO A 137 ? 0.1416 0.1563 0.1062 0.0137  -0.0263 -0.0220 138 PRO A N   
1172 N  N   B PRO A 137 ? 0.1448 0.1520 0.1115 0.0082  -0.0027 -0.0331 138 PRO A N   
1173 C  CA  A PRO A 137 ? 0.1759 0.1649 0.0851 0.0189  0.0020  -0.0229 138 PRO A CA  
1174 C  CA  B PRO A 137 ? 0.1630 0.1623 0.1017 -0.0038 -0.0110 0.0126  138 PRO A CA  
1175 C  C   A PRO A 137 ? 0.1432 0.1616 0.0816 0.0096  0.0147  -0.0103 138 PRO A C   
1176 C  C   B PRO A 137 ? 0.1393 0.1606 0.1164 0.0100  -0.0019 -0.0144 138 PRO A C   
1177 O  O   A PRO A 137 ? 0.1800 0.1631 0.1527 0.0060  0.0137  0.0307  138 PRO A O   
1178 O  O   B PRO A 137 ? 0.1800 0.1757 0.2034 0.0034  -0.0120 0.0412  138 PRO A O   
1179 C  CB  A PRO A 137 ? 0.1879 0.1791 0.0847 -0.0221 -0.0335 0.0000  138 PRO A CB  
1180 C  CB  B PRO A 137 ? 0.2347 0.1305 0.1363 0.0126  0.0006  -0.0006 138 PRO A CB  
1181 C  CG  A PRO A 137 ? 0.1948 0.1868 0.1112 0.0173  -0.0176 -0.0381 138 PRO A CG  
1182 C  CG  B PRO A 137 ? 0.2369 0.2398 0.1265 -0.0127 -0.0006 -0.0168 138 PRO A CG  
1183 C  CD  A PRO A 137 ? 0.1168 0.1596 0.1261 0.0038  -0.0353 -0.0313 138 PRO A CD  
1184 C  CD  B PRO A 137 ? 0.1225 0.1740 0.1266 0.0136  -0.0242 -0.0220 138 PRO A CD  
1185 N  N   . ASP A 138 ? 0.1508 0.1431 0.1058 0.0054  0.0024  -0.0071 139 ASP A N   
1186 C  CA  . ASP A 138 ? 0.1465 0.1394 0.1058 -0.0055 0.0065  -0.0142 139 ASP A CA  
1187 C  C   . ASP A 138 ? 0.1279 0.1107 0.1142 -0.0087 -0.0006 -0.0116 139 ASP A C   
1188 O  O   . ASP A 138 ? 0.1357 0.1233 0.1303 0.0063  0.0073  -0.0048 139 ASP A O   
1189 C  CB  . ASP A 138 ? 0.1914 0.1968 0.1265 -0.0057 0.0328  -0.0185 139 ASP A CB  
1190 C  CG  . ASP A 138 ? 0.1568 0.2020 0.1498 0.0087  0.0070  -0.0335 139 ASP A CG  
1191 O  OD1 . ASP A 138 ? 0.1862 0.1614 0.1785 0.0073  0.0052  -0.0586 139 ASP A OD1 
1192 O  OD2 . ASP A 138 ? 0.2214 0.2238 0.2025 0.0219  0.0416  -0.0626 139 ASP A OD2 
1193 N  N   . GLY A 139 ? 0.1136 0.1090 0.0948 -0.0126 -0.0010 -0.0165 140 GLY A N   
1194 C  CA  . GLY A 139 ? 0.1290 0.1045 0.0979 -0.0140 -0.0118 -0.0070 140 GLY A CA  
1195 C  C   . GLY A 139 ? 0.1019 0.0904 0.0974 -0.0043 0.0024  -0.0048 140 GLY A C   
1196 O  O   . GLY A 139 ? 0.1166 0.0883 0.1110 0.0006  -0.0068 -0.0021 140 GLY A O   
1197 N  N   . LEU A 140 ? 0.0939 0.0832 0.1042 -0.0068 0.0003  -0.0043 141 LEU A N   
1198 C  CA  . LEU A 140 ? 0.0983 0.0816 0.0983 -0.0076 0.0030  -0.0093 141 LEU A CA  
1199 C  C   . LEU A 140 ? 0.0951 0.0811 0.0927 0.0051  -0.0059 -0.0074 141 LEU A C   
1200 O  O   . LEU A 140 ? 0.1014 0.0843 0.0992 -0.0041 -0.0017 -0.0043 141 LEU A O   
1201 C  CB  . LEU A 140 ? 0.1096 0.0944 0.1014 -0.0063 0.0153  -0.0100 141 LEU A CB  
1202 C  CG  . LEU A 140 ? 0.1481 0.1010 0.1493 0.0196  0.0399  0.0076  141 LEU A CG  
1203 C  CD1 . LEU A 140 ? 0.1162 0.1191 0.1212 0.0168  0.0183  0.0007  141 LEU A CD1 
1204 C  CD2 . LEU A 140 ? 0.1827 0.1206 0.1643 0.0251  0.0355  0.0227  141 LEU A CD2 
1205 N  N   . ALA A 141 ? 0.0936 0.0799 0.1037 -0.0068 0.0027  -0.0046 142 ALA A N   
1206 C  CA  . ALA A 141 ? 0.1014 0.0769 0.1162 -0.0060 0.0031  -0.0035 142 ALA A CA  
1207 C  C   . ALA A 141 ? 0.0922 0.0784 0.0936 -0.0143 -0.0082 -0.0031 142 ALA A C   
1208 O  O   . ALA A 141 ? 0.1112 0.0826 0.1078 -0.0017 -0.0127 0.0041  142 ALA A O   
1209 C  CB  . ALA A 141 ? 0.1071 0.1096 0.1196 -0.0102 0.0054  -0.0052 142 ALA A CB  
1210 N  N   . VAL A 142 ? 0.0876 0.0742 0.1018 -0.0034 -0.0020 -0.0003 143 VAL A N   
1211 C  CA  . VAL A 142 ? 0.0873 0.0826 0.0930 0.0019  -0.0074 0.0000  143 VAL A CA  
1212 C  C   . VAL A 142 ? 0.0874 0.0798 0.0847 0.0000  -0.0006 -0.0032 143 VAL A C   
1213 O  O   . VAL A 142 ? 0.0960 0.0838 0.0922 -0.0038 -0.0068 0.0049  143 VAL A O   
1214 C  CB  . VAL A 142 ? 0.0886 0.0996 0.0895 -0.0012 -0.0052 0.0031  143 VAL A CB  
1215 C  CG1 . VAL A 142 ? 0.1076 0.1032 0.0891 0.0010  -0.0082 -0.0113 143 VAL A CG1 
1216 C  CG2 . VAL A 142 ? 0.1045 0.1198 0.0953 -0.0113 0.0017  0.0115  143 VAL A CG2 
1217 N  N   . LEU A 143 ? 0.0926 0.0746 0.0983 -0.0068 -0.0051 0.0049  144 LEU A N   
1218 C  CA  . LEU A 143 ? 0.0882 0.0804 0.1089 -0.0065 -0.0144 0.0057  144 LEU A CA  
1219 C  C   . LEU A 143 ? 0.0922 0.0842 0.0881 -0.0120 -0.0059 0.0030  144 LEU A C   
1220 O  O   . LEU A 143 ? 0.1105 0.0885 0.0916 -0.0030 0.0019  0.0037  144 LEU A O   
1221 C  CB  . LEU A 143 ? 0.0974 0.1089 0.1124 0.0008  -0.0020 0.0093  144 LEU A CB  
1222 C  CG  . LEU A 143 ? 0.0898 0.1137 0.1405 -0.0074 -0.0043 -0.0044 144 LEU A CG  
1223 C  CD1 . LEU A 143 ? 0.1268 0.1520 0.1553 -0.0237 -0.0028 0.0219  144 LEU A CD1 
1224 C  CD2 . LEU A 143 ? 0.0900 0.1570 0.1747 -0.0027 -0.0041 0.0057  144 LEU A CD2 
1225 N  N   . GLY A 144 ? 0.0954 0.0741 0.0904 -0.0020 -0.0031 -0.0030 145 GLY A N   
1226 C  CA  . GLY A 144 ? 0.1002 0.0812 0.0987 -0.0027 0.0031  0.0003  145 GLY A CA  
1227 C  C   . GLY A 144 ? 0.0864 0.0825 0.0852 0.0031  -0.0023 0.0071  145 GLY A C   
1228 O  O   . GLY A 144 ? 0.1057 0.0907 0.0964 -0.0094 0.0038  -0.0044 145 GLY A O   
1229 N  N   . ILE A 145 ? 0.0900 0.0759 0.0848 -0.0038 -0.0013 -0.0013 146 ILE A N   
1230 C  CA  . ILE A 145 ? 0.0926 0.0780 0.1015 -0.0122 -0.0065 0.0038  146 ILE A CA  
1231 C  C   . ILE A 145 ? 0.0939 0.0777 0.0876 -0.0115 -0.0083 0.0000  146 ILE A C   
1232 O  O   . ILE A 145 ? 0.0988 0.0847 0.0988 -0.0082 0.0038  -0.0012 146 ILE A O   
1233 C  CB  . ILE A 145 ? 0.1040 0.0920 0.0987 -0.0006 -0.0142 0.0065  146 ILE A CB  
1234 C  CG1 . ILE A 145 ? 0.1286 0.1067 0.1400 0.0184  -0.0262 -0.0021 146 ILE A CG1 
1235 C  CG2 . ILE A 145 ? 0.0962 0.1080 0.1635 -0.0060 -0.0359 -0.0037 146 ILE A CG2 
1236 C  CD1 . ILE A 145 ? 0.1137 0.1098 0.1418 0.0008  -0.0207 0.0109  146 ILE A CD1 
1237 N  N   . PHE A 146 ? 0.0958 0.0772 0.0920 0.0012  -0.0085 0.0005  147 PHE A N   
1238 C  CA  . PHE A 146 ? 0.1008 0.0737 0.0979 -0.0031 -0.0126 0.0021  147 PHE A CA  
1239 C  C   . PHE A 146 ? 0.1108 0.0795 0.1022 -0.0046 -0.0068 0.0023  147 PHE A C   
1240 O  O   . PHE A 146 ? 0.1115 0.0995 0.1148 0.0000  -0.0172 -0.0094 147 PHE A O   
1241 C  CB  . PHE A 146 ? 0.1114 0.0838 0.0974 -0.0131 -0.0122 0.0076  147 PHE A CB  
1242 C  CG  . PHE A 146 ? 0.0920 0.0794 0.0967 -0.0054 -0.0032 0.0076  147 PHE A CG  
1243 C  CD1 . PHE A 146 ? 0.1032 0.0886 0.0920 0.0003  0.0003  -0.0085 147 PHE A CD1 
1244 C  CD2 . PHE A 146 ? 0.1163 0.0834 0.1096 -0.0068 -0.0076 0.0184  147 PHE A CD2 
1245 C  CE1 . PHE A 146 ? 0.1216 0.0909 0.0983 0.0010  -0.0030 0.0074  147 PHE A CE1 
1246 C  CE2 . PHE A 146 ? 0.1146 0.0995 0.1123 0.0006  0.0010  0.0115  147 PHE A CE2 
1247 C  CZ  . PHE A 146 ? 0.1049 0.1009 0.1005 -0.0005 -0.0043 0.0103  147 PHE A CZ  
1248 N  N   . LEU A 147 ? 0.1033 0.0833 0.1094 -0.0126 -0.0093 0.0027  148 LEU A N   
1249 C  CA  . LEU A 147 ? 0.1209 0.0835 0.1072 -0.0104 -0.0193 -0.0080 148 LEU A CA  
1250 C  C   . LEU A 147 ? 0.1116 0.0833 0.1123 -0.0129 -0.0091 -0.0010 148 LEU A C   
1251 O  O   . LEU A 147 ? 0.1128 0.0930 0.1262 -0.0074 0.0000  0.0008  148 LEU A O   
1252 C  CB  . LEU A 147 ? 0.1292 0.0907 0.1152 -0.0121 -0.0031 0.0063  148 LEU A CB  
1253 C  CG  . LEU A 147 ? 0.1319 0.0847 0.1045 -0.0181 -0.0142 -0.0044 148 LEU A CG  
1254 C  CD1 . LEU A 147 ? 0.1574 0.0934 0.1193 -0.0077 -0.0249 -0.0052 148 LEU A CD1 
1255 C  CD2 . LEU A 147 ? 0.1467 0.1148 0.1189 -0.0082 -0.0196 0.0066  148 LEU A CD2 
1256 N  N   . LYS A 148 ? 0.1289 0.0793 0.1316 -0.0156 -0.0162 0.0010  149 LYS A N   
1257 C  CA  . LYS A 148 ? 0.1377 0.0855 0.1391 -0.0170 -0.0137 0.0006  149 LYS A CA  
1258 C  C   . LYS A 148 ? 0.1501 0.0969 0.1441 -0.0024 -0.0302 -0.0001 149 LYS A C   
1259 O  O   . LYS A 148 ? 0.1656 0.1308 0.1445 0.0113  -0.0397 -0.0163 149 LYS A O   
1260 C  CB  . LYS A 148 ? 0.1688 0.1146 0.1620 -0.0335 -0.0263 0.0130  149 LYS A CB  
1261 C  CG  . LYS A 148 ? 0.1791 0.1413 0.1826 -0.0295 -0.0030 0.0412  149 LYS A CG  
1262 C  CD  . LYS A 148 ? 0.2567 0.2316 0.2739 -0.0377 0.0372  0.0566  149 LYS A CD  
1263 C  CE  . LYS A 148 ? 0.3066 0.3754 0.4154 0.0102  0.1097  0.1377  149 LYS A CE  
1264 N  NZ  . LYS A 148 ? 0.5909 0.6610 0.3894 -0.2494 0.1437  0.1185  149 LYS A NZ  
1265 N  N   . VAL A 149 ? 0.1718 0.0988 0.1617 -0.0013 -0.0303 -0.0109 150 VAL A N   
1266 C  CA  . VAL A 149 ? 0.1525 0.0970 0.1699 -0.0065 -0.0304 -0.0294 150 VAL A CA  
1267 C  C   . VAL A 149 ? 0.1583 0.1105 0.1695 -0.0068 -0.0186 -0.0120 150 VAL A C   
1268 O  O   . VAL A 149 ? 0.1763 0.1366 0.1859 -0.0104 -0.0339 0.0082  150 VAL A O   
1269 C  CB  . VAL A 149 ? 0.1652 0.1040 0.1647 -0.0030 -0.0081 -0.0035 150 VAL A CB  
1270 C  CG1 . VAL A 149 ? 0.1764 0.1658 0.1705 0.0043  -0.0256 -0.0276 150 VAL A CG1 
1271 C  CG2 . VAL A 149 ? 0.1594 0.1480 0.2204 -0.0164 -0.0097 -0.0129 150 VAL A CG2 
1272 N  N   . GLY A 150 ? 0.1541 0.1200 0.1644 -0.0220 -0.0313 -0.0055 151 GLY A N   
1273 C  CA  . GLY A 150 ? 0.1728 0.1696 0.1685 -0.0439 -0.0379 0.0254  151 GLY A CA  
1274 C  C   . GLY A 150 ? 0.1614 0.1191 0.1713 -0.0355 -0.0273 -0.0001 151 GLY A C   
1275 O  O   . GLY A 150 ? 0.1761 0.1280 0.1825 -0.0195 -0.0184 -0.0201 151 GLY A O   
1276 N  N   A SER A 151 ? 0.1745 0.1421 0.1855 -0.0469 -0.0379 0.0044  152 SER A N   
1277 N  N   B SER A 151 ? 0.1741 0.1429 0.2030 -0.0518 -0.0351 0.0020  152 SER A N   
1278 C  CA  A SER A 151 ? 0.1744 0.1299 0.1812 -0.0248 -0.0362 -0.0026 152 SER A CA  
1279 C  CA  B SER A 151 ? 0.1652 0.1378 0.1930 -0.0331 -0.0403 -0.0288 152 SER A CA  
1280 C  C   A SER A 151 ? 0.1729 0.1106 0.1456 -0.0201 -0.0024 -0.0313 152 SER A C   
1281 C  C   B SER A 151 ? 0.1727 0.1236 0.1511 -0.0199 -0.0443 -0.0126 152 SER A C   
1282 O  O   A SER A 151 ? 0.1271 0.1146 0.1383 -0.0262 -0.0046 -0.0154 152 SER A O   
1283 O  O   B SER A 151 ? 0.1220 0.1305 0.1256 -0.0153 -0.0085 -0.0197 152 SER A O   
1284 C  CB  A SER A 151 ? 0.1817 0.1588 0.2357 -0.0408 -0.0209 0.0083  152 SER A CB  
1285 C  CB  B SER A 151 ? 0.1958 0.1981 0.2700 -0.0498 0.0241  -0.0348 152 SER A CB  
1286 O  OG  A SER A 151 ? 0.2230 0.2043 0.2023 -0.0138 -0.0335 0.0082  152 SER A OG  
1287 O  OG  B SER A 151 ? 0.1606 0.2660 0.3718 -0.0307 -0.0104 0.0895  152 SER A OG  
1288 N  N   . ALA A 152 ? 0.1987 0.1213 0.1642 -0.0185 -0.0581 -0.0116 153 ALA A N   
1289 C  CA  . ALA A 152 ? 0.1670 0.1281 0.1544 -0.0085 -0.0401 -0.0109 153 ALA A CA  
1290 C  C   . ALA A 152 ? 0.1914 0.1287 0.1331 -0.0051 -0.0313 -0.0131 153 ALA A C   
1291 O  O   . ALA A 152 ? 0.1821 0.1324 0.1983 -0.0070 -0.0320 -0.0113 153 ALA A O   
1292 C  CB  . ALA A 152 ? 0.2469 0.1684 0.1662 0.0074  -0.0588 -0.0186 153 ALA A CB  
1293 N  N   . LYS A 153 ? 0.1861 0.1114 0.1536 -0.0013 -0.0449 -0.0035 154 LYS A N   
1294 C  CA  . LYS A 153 ? 0.1753 0.1233 0.1662 -0.0055 -0.0355 -0.0044 154 LYS A CA  
1295 C  C   . LYS A 153 ? 0.1577 0.1304 0.1573 -0.0100 -0.0370 -0.0115 154 LYS A C   
1296 O  O   . LYS A 153 ? 0.1561 0.1296 0.1550 -0.0100 -0.0434 0.0000  154 LYS A O   
1297 C  CB  . LYS A 153 ? 0.1790 0.1220 0.1667 -0.0043 -0.0483 0.0062  154 LYS A CB  
1298 C  CG  . LYS A 153 ? 0.2125 0.1251 0.1754 -0.0054 -0.0412 -0.0078 154 LYS A CG  
1299 C  CD  . LYS A 153 ? 0.2141 0.1350 0.1941 0.0034  -0.0419 -0.0333 154 LYS A CD  
1300 C  CE  . LYS A 153 ? 0.1986 0.1735 0.1503 -0.0074 -0.0344 -0.0121 154 LYS A CE  
1301 N  NZ  . LYS A 153 ? 0.1810 0.1774 0.1918 0.0068  -0.0359 -0.0274 154 LYS A NZ  
1302 N  N   A PRO A 154 ? 0.1592 0.1324 0.1521 -0.0054 -0.0428 -0.0048 155 PRO A N   
1303 N  N   B PRO A 154 ? 0.1764 0.1333 0.1709 -0.0230 -0.0540 -0.0116 155 PRO A N   
1304 C  CA  A PRO A 154 ? 0.1557 0.1712 0.1559 -0.0183 -0.0386 0.0073  155 PRO A CA  
1305 C  CA  B PRO A 154 ? 0.1588 0.1652 0.1849 -0.0392 -0.0428 -0.0227 155 PRO A CA  
1306 C  C   A PRO A 154 ? 0.1592 0.1911 0.1513 -0.0135 -0.0771 0.0108  155 PRO A C   
1307 C  C   B PRO A 154 ? 0.1645 0.1881 0.1640 -0.0182 -0.0621 -0.0003 155 PRO A C   
1308 O  O   A PRO A 154 ? 0.1381 0.1696 0.1754 0.0204  -0.0236 0.0386  155 PRO A O   
1309 O  O   B PRO A 154 ? 0.1630 0.1509 0.1640 0.0021  -0.0540 -0.0049 155 PRO A O   
1310 C  CB  A PRO A 154 ? 0.1568 0.1880 0.1792 0.0008  -0.0148 -0.0311 155 PRO A CB  
1311 C  CB  B PRO A 154 ? 0.1354 0.1518 0.2030 0.0162  -0.0549 -0.0259 155 PRO A CB  
1312 C  CG  A PRO A 154 ? 0.1500 0.1455 0.2154 -0.0175 -0.0320 -0.0161 155 PRO A CG  
1313 C  CG  B PRO A 154 ? 0.1752 0.2825 0.2190 0.0049  -0.0133 -0.0197 155 PRO A CG  
1314 C  CD  A PRO A 154 ? 0.1635 0.1298 0.2109 -0.0017 -0.0335 -0.0197 155 PRO A CD  
1315 C  CD  B PRO A 154 ? 0.2142 0.1467 0.1816 -0.0006 -0.0170 -0.0013 155 PRO A CD  
1316 N  N   . GLY A 155 ? 0.1679 0.1418 0.1844 0.0185  -0.0588 0.0034  156 GLY A N   
1317 C  CA  . GLY A 155 ? 0.2074 0.1482 0.2134 -0.0068 -0.0513 0.0126  156 GLY A CA  
1318 C  C   . GLY A 155 ? 0.2135 0.1207 0.1926 -0.0313 -0.0434 0.0208  156 GLY A C   
1319 O  O   . GLY A 155 ? 0.1970 0.1406 0.2540 -0.0063 -0.0476 0.0339  156 GLY A O   
1320 N  N   . LEU A 156 ? 0.1689 0.1298 0.1671 -0.0137 -0.0412 0.0001  157 LEU A N   
1321 C  CA  . LEU A 156 ? 0.1816 0.1139 0.1367 -0.0217 -0.0306 0.0007  157 LEU A CA  
1322 C  C   . LEU A 156 ? 0.1648 0.1225 0.1485 -0.0015 -0.0463 -0.0129 157 LEU A C   
1323 O  O   . LEU A 156 ? 0.1748 0.1289 0.1485 -0.0243 -0.0491 -0.0005 157 LEU A O   
1324 C  CB  . LEU A 156 ? 0.1870 0.1377 0.1499 -0.0211 -0.0518 0.0088  157 LEU A CB  
1325 C  CG  . LEU A 156 ? 0.1689 0.1317 0.1405 -0.0299 -0.0326 0.0020  157 LEU A CG  
1326 C  CD1 . LEU A 156 ? 0.1747 0.1536 0.1557 -0.0315 -0.0436 -0.0013 157 LEU A CD1 
1327 C  CD2 . LEU A 156 ? 0.1578 0.1440 0.1722 -0.0210 -0.0388 0.0030  157 LEU A CD2 
1328 N  N   . GLN A 157 ? 0.1826 0.1362 0.1523 -0.0318 -0.0540 0.0028  158 GLN A N   
1329 C  CA  . GLN A 157 ? 0.2010 0.1475 0.1405 -0.0419 -0.0465 -0.0170 158 GLN A CA  
1330 C  C   . GLN A 157 ? 0.1720 0.1297 0.1482 -0.0348 -0.0570 -0.0086 158 GLN A C   
1331 O  O   . GLN A 157 ? 0.1996 0.1388 0.1582 -0.0266 -0.0496 -0.0099 158 GLN A O   
1332 C  CB  . GLN A 157 ? 0.2030 0.1601 0.1728 -0.0489 -0.0603 -0.0201 158 GLN A CB  
1333 C  CG  . GLN A 157 ? 0.2296 0.1626 0.1790 -0.0281 -0.0582 -0.0198 158 GLN A CG  
1334 C  CD  . GLN A 157 ? 0.2113 0.1314 0.1695 -0.0333 -0.0496 -0.0080 158 GLN A CD  
1335 O  OE1 . GLN A 157 ? 0.2477 0.1404 0.1583 -0.0230 -0.0381 -0.0082 158 GLN A OE1 
1336 N  NE2 . GLN A 157 ? 0.2804 0.1962 0.1738 -0.0763 -0.0164 -0.0548 158 GLN A NE2 
1337 N  N   . LYS A 158 ? 0.1895 0.1518 0.1551 -0.0340 -0.0737 -0.0003 159 LYS A N   
1338 C  CA  . LYS A 158 ? 0.2127 0.1366 0.1597 -0.0346 -0.0671 0.0098  159 LYS A CA  
1339 C  C   . LYS A 158 ? 0.1987 0.1459 0.1455 -0.0291 -0.0417 -0.0085 159 LYS A C   
1340 O  O   . LYS A 158 ? 0.2179 0.1474 0.1467 -0.0362 -0.0438 0.0017  159 LYS A O   
1341 C  CB  . LYS A 158 ? 0.2390 0.1509 0.2055 -0.0155 -0.0964 0.0289  159 LYS A CB  
1342 C  CG  . LYS A 158 ? 0.4395 0.2272 0.3183 -0.0020 -0.1483 0.0401  159 LYS A CG  
1343 C  CD  . LYS A 158 ? 0.4140 0.2964 0.2737 0.0439  -0.0953 0.0736  159 LYS A CD  
1344 C  CE  . LYS A 158 ? 0.5727 0.4061 0.4738 -0.0142 -0.1221 0.2228  159 LYS A CE  
1345 N  NZ  . LYS A 158 ? 0.3873 0.5236 0.4052 0.0421  -0.1450 0.1696  159 LYS A NZ  
1346 N  N   . VAL A 159 ? 0.2014 0.1303 0.1321 -0.0195 -0.0627 -0.0125 160 VAL A N   
1347 C  CA  . VAL A 159 ? 0.2017 0.1222 0.1260 -0.0233 -0.0414 -0.0020 160 VAL A CA  
1348 C  C   . VAL A 159 ? 0.1800 0.1290 0.1341 -0.0137 -0.0313 -0.0073 160 VAL A C   
1349 O  O   . VAL A 159 ? 0.1918 0.1337 0.1554 -0.0122 -0.0379 -0.0078 160 VAL A O   
1350 C  CB  . VAL A 159 ? 0.1879 0.1282 0.1322 -0.0225 -0.0443 0.0000  160 VAL A CB  
1351 C  CG1 . VAL A 159 ? 0.2034 0.1608 0.1547 -0.0271 -0.0344 0.0093  160 VAL A CG1 
1352 C  CG2 . VAL A 159 ? 0.2273 0.1543 0.1388 0.0046  -0.0394 -0.0214 160 VAL A CG2 
1353 N  N   . VAL A 160 ? 0.1965 0.1177 0.1309 -0.0216 -0.0397 -0.0125 161 VAL A N   
1354 C  CA  . VAL A 160 ? 0.2140 0.1352 0.1381 0.0001  -0.0104 -0.0054 161 VAL A CA  
1355 C  C   . VAL A 160 ? 0.2038 0.1298 0.1650 -0.0289 -0.0244 -0.0172 161 VAL A C   
1356 O  O   . VAL A 160 ? 0.2630 0.1492 0.1680 -0.0291 -0.0157 -0.0115 161 VAL A O   
1357 C  CB  . VAL A 160 ? 0.3043 0.1418 0.1745 -0.0041 0.0126  -0.0035 161 VAL A CB  
1358 C  CG1 . VAL A 160 ? 0.2655 0.1635 0.2368 -0.0612 -0.0379 -0.0215 161 VAL A CG1 
1359 C  CG2 . VAL A 160 ? 0.2644 0.1658 0.1937 0.0119  -0.0081 -0.0019 161 VAL A CG2 
1360 N  N   . ASP A 161 ? 0.2312 0.1667 0.1456 -0.0458 -0.0370 -0.0118 162 ASP A N   
1361 C  CA  . ASP A 161 ? 0.3009 0.2267 0.1349 -0.0626 -0.0617 -0.0115 162 ASP A CA  
1362 C  C   . ASP A 161 ? 0.2540 0.2263 0.1254 -0.0625 -0.0255 -0.0135 162 ASP A C   
1363 O  O   . ASP A 161 ? 0.4108 0.3113 0.1280 -0.0944 -0.0359 -0.0254 162 ASP A O   
1364 C  CB  . ASP A 161 ? 0.3459 0.2322 0.1622 -0.0604 -0.0511 -0.0260 162 ASP A CB  
1365 C  CG  . ASP A 161 ? 0.3420 0.2205 0.1556 -0.0185 -0.0370 -0.0329 162 ASP A CG  
1366 O  OD1 . ASP A 161 ? 0.3619 0.2576 0.2743 -0.0656 -0.0781 -0.0500 162 ASP A OD1 
1367 O  OD2 . ASP A 161 ? 0.3420 0.2619 0.2694 -0.0405 -0.0935 -0.0059 162 ASP A OD2 
1368 N  N   . VAL A 162 ? 0.2770 0.1916 0.1296 -0.0621 -0.0584 0.0000  163 VAL A N   
1369 C  CA  . VAL A 162 ? 0.2599 0.2204 0.1352 -0.0509 -0.0493 0.0253  163 VAL A CA  
1370 C  C   . VAL A 162 ? 0.2644 0.1661 0.1103 -0.0461 -0.0174 0.0237  163 VAL A C   
1371 O  O   . VAL A 162 ? 0.2718 0.1823 0.1331 -0.0262 -0.0063 0.0000  163 VAL A O   
1372 C  CB  . VAL A 162 ? 0.2217 0.1947 0.1834 -0.0208 -0.0284 0.0217  163 VAL A CB  
1373 C  CG1 . VAL A 162 ? 0.2858 0.1542 0.2008 -0.0138 -0.0460 -0.0043 163 VAL A CG1 
1374 C  CG2 . VAL A 162 ? 0.2685 0.2152 0.2188 -0.0041 0.0052  0.0531  163 VAL A CG2 
1375 N  N   . LEU A 163 ? 0.2265 0.1729 0.1345 -0.0322 -0.0361 -0.0010 164 LEU A N   
1376 C  CA  . LEU A 163 ? 0.2380 0.1437 0.1150 -0.0156 0.0060  0.0021  164 LEU A CA  
1377 C  C   . LEU A 163 ? 0.2368 0.1648 0.1536 0.0000  0.0086  -0.0183 164 LEU A C   
1378 O  O   . LEU A 163 ? 0.2547 0.1894 0.1198 0.0015  0.0063  0.0149  164 LEU A O   
1379 C  CB  . LEU A 163 ? 0.2326 0.1598 0.1292 -0.0297 -0.0071 0.0015  164 LEU A CB  
1380 C  CG  . LEU A 163 ? 0.2366 0.1456 0.1177 -0.0157 -0.0136 0.0038  164 LEU A CG  
1381 C  CD1 . LEU A 163 ? 0.2134 0.1459 0.1595 -0.0094 -0.0164 0.0324  164 LEU A CD1 
1382 C  CD2 . LEU A 163 ? 0.2074 0.1660 0.1257 -0.0063 -0.0353 -0.0048 164 LEU A CD2 
1383 N  N   . ASP A 164 ? 0.3567 0.1983 0.1136 -0.0395 -0.0044 -0.0315 165 ASP A N   
1384 C  CA  . ASP A 164 ? 0.3747 0.2491 0.1428 -0.0631 0.0507  -0.0593 165 ASP A CA  
1385 C  C   . ASP A 164 ? 0.3591 0.2660 0.1344 -0.0017 0.0151  -0.0099 165 ASP A C   
1386 O  O   . ASP A 164 ? 0.4133 0.2655 0.2116 0.0165  0.0731  -0.0273 165 ASP A O   
1387 C  CB  . ASP A 164 ? 0.4172 0.2772 0.1714 -0.0864 0.0252  -0.0518 165 ASP A CB  
1388 C  CG  . ASP A 164 ? 0.4492 0.3531 0.2481 -0.1648 -0.0463 -0.0842 165 ASP A CG  
1389 O  OD1 . ASP A 164 ? 0.6195 0.3916 0.2278 -0.1363 0.0326  -0.0208 165 ASP A OD1 
1390 O  OD2 . ASP A 164 ? 0.6830 0.5112 0.2248 -0.1703 0.0063  -0.0671 165 ASP A OD2 
1391 N  N   . SER A 165 ? 0.2687 0.2443 0.1150 -0.0167 -0.0201 0.0063  166 SER A N   
1392 C  CA  . SER A 165 ? 0.2962 0.2646 0.1211 -0.0152 -0.0294 0.0141  166 SER A CA  
1393 C  C   . SER A 165 ? 0.2567 0.2097 0.1123 -0.0088 0.0093  0.0188  166 SER A C   
1394 O  O   . SER A 165 ? 0.3036 0.2284 0.1474 -0.0259 -0.0275 0.0412  166 SER A O   
1395 C  CB  . SER A 165 ? 0.3986 0.3325 0.1733 -0.0148 0.0403  0.0654  166 SER A CB  
1396 O  OG  . SER A 165 ? 0.3194 0.2809 0.2319 -0.0035 -0.0208 0.0507  166 SER A OG  
1397 N  N   . ILE A 166 ? 0.2078 0.1926 0.1061 0.0094  -0.0185 0.0131  167 ILE A N   
1398 C  CA  . ILE A 166 ? 0.2041 0.1468 0.1298 -0.0065 0.0020  0.0119  167 ILE A CA  
1399 C  C   . ILE A 166 ? 0.1983 0.1605 0.1057 -0.0129 -0.0013 -0.0057 167 ILE A C   
1400 O  O   . ILE A 166 ? 0.2046 0.1536 0.1159 -0.0017 -0.0010 0.0019  167 ILE A O   
1401 C  CB  . ILE A 166 ? 0.2073 0.1469 0.1286 -0.0032 -0.0023 -0.0020 167 ILE A CB  
1402 C  CG1 . ILE A 166 ? 0.2090 0.1726 0.1240 -0.0237 0.0070  0.0020  167 ILE A CG1 
1403 C  CG2 . ILE A 166 ? 0.2085 0.1894 0.1544 0.0121  -0.0104 0.0328  167 ILE A CG2 
1404 C  CD1 . ILE A 166 ? 0.2284 0.1806 0.1216 -0.0131 0.0194  -0.0217 167 ILE A CD1 
1405 N  N   . LYS A 167 ? 0.2073 0.1594 0.1306 0.0226  0.0196  0.0046  168 LYS A N   
1406 C  CA  . LYS A 167 ? 0.2023 0.1921 0.1098 0.0109  -0.0013 -0.0252 168 LYS A CA  
1407 C  C   . LYS A 167 ? 0.1923 0.1645 0.1189 -0.0092 0.0100  0.0114  168 LYS A C   
1408 O  O   . LYS A 167 ? 0.2140 0.1486 0.1349 -0.0068 -0.0054 -0.0060 168 LYS A O   
1409 C  CB  . LYS A 167 ? 0.2675 0.1905 0.1386 0.0044  -0.0144 -0.0432 168 LYS A CB  
1410 C  CG  . LYS A 167 ? 0.2337 0.1940 0.1551 0.0208  0.0188  -0.0410 168 LYS A CG  
1411 C  CD  . LYS A 167 ? 0.3170 0.2099 0.2635 0.0302  -0.0051 -0.0775 168 LYS A CD  
1412 C  CE  . LYS A 167 ? 0.4052 0.3379 0.3084 0.0988  -0.0159 -0.0949 168 LYS A CE  
1413 N  NZ  . LYS A 167 ? 0.4366 0.5297 0.4706 0.1199  0.0148  -0.2058 168 LYS A NZ  
1414 N  N   . THR A 168 ? 0.1929 0.1651 0.1368 0.0130  0.0057  0.0083  169 THR A N   
1415 C  CA  . THR A 168 ? 0.1968 0.1972 0.1227 0.0096  0.0438  0.0188  169 THR A CA  
1416 C  C   . THR A 168 ? 0.1599 0.1604 0.1033 0.0041  0.0220  0.0198  169 THR A C   
1417 O  O   . THR A 168 ? 0.1923 0.1615 0.1394 -0.0141 0.0200  0.0225  169 THR A O   
1418 C  CB  . THR A 168 ? 0.2319 0.1782 0.1483 0.0173  0.0289  0.0198  169 THR A CB  
1419 O  OG1 . THR A 168 ? 0.2233 0.2066 0.1352 0.0162  0.0372  0.0110  169 THR A OG1 
1420 C  CG2 . THR A 168 ? 0.2615 0.1992 0.1635 0.0137  0.0469  -0.0076 169 THR A CG2 
1421 N  N   . LYS A 169 ? 0.2102 0.1867 0.1350 -0.0219 0.0329  0.0055  170 LYS A N   
1422 C  CA  . LYS A 169 ? 0.1767 0.1793 0.1523 -0.0102 0.0164  0.0230  170 LYS A CA  
1423 C  C   . LYS A 169 ? 0.1757 0.1932 0.1539 -0.0217 0.0381  0.0507  170 LYS A C   
1424 O  O   . LYS A 169 ? 0.2261 0.2270 0.1517 -0.0272 0.0461  0.0397  170 LYS A O   
1425 C  CB  . LYS A 169 ? 0.1982 0.1738 0.1543 -0.0055 0.0423  0.0138  170 LYS A CB  
1426 C  CG  . LYS A 169 ? 0.2085 0.2108 0.1818 -0.0286 0.0192  0.0291  170 LYS A CG  
1427 C  CD  . LYS A 169 ? 0.2594 0.2357 0.2123 -0.0015 0.0231  0.0377  170 LYS A CD  
1428 C  CE  . LYS A 169 ? 0.3298 0.4824 0.3655 -0.0019 0.0416  -0.0135 170 LYS A CE  
1429 N  NZ  . LYS A 169 ? 0.4717 0.7990 0.3334 -0.0907 -0.0776 0.0645  170 LYS A NZ  
1430 N  N   . GLY A 170 ? 0.2346 0.1615 0.1685 -0.0379 0.0223  0.0231  171 GLY A N   
1431 C  CA  . GLY A 170 ? 0.2028 0.1516 0.2451 -0.0155 -0.0161 0.0728  171 GLY A CA  
1432 C  C   . GLY A 170 ? 0.2322 0.1852 0.1934 -0.0172 0.0048  0.0674  171 GLY A C   
1433 O  O   . GLY A 170 ? 0.2477 0.1860 0.2913 -0.0540 -0.0189 0.0903  171 GLY A O   
1434 N  N   . LYS A 171 ? 0.1928 0.1601 0.1746 -0.0181 0.0287  0.0474  172 LYS A N   
1435 C  CA  . LYS A 171 ? 0.2061 0.1653 0.1696 -0.0174 0.0155  0.0375  172 LYS A CA  
1436 C  C   . LYS A 171 ? 0.1967 0.1485 0.1159 0.0126  0.0141  0.0222  172 LYS A C   
1437 O  O   . LYS A 171 ? 0.2067 0.1767 0.1163 0.0049  0.0184  0.0421  172 LYS A O   
1438 C  CB  . LYS A 171 ? 0.2707 0.1863 0.1293 -0.0275 0.0193  0.0219  172 LYS A CB  
1439 C  CG  . LYS A 171 ? 0.2856 0.2321 0.1812 0.0077  0.0126  -0.0063 172 LYS A CG  
1440 C  CD  . LYS A 171 ? 0.4156 0.2518 0.2872 0.0100  -0.0386 -0.0119 172 LYS A CD  
1441 N  N   . SER A 172 ? 0.2216 0.1685 0.1337 0.0017  -0.0040 0.0472  173 SER A N   
1442 C  CA  . SER A 172 ? 0.1908 0.1879 0.1632 0.0259  0.0131  0.0206  173 SER A CA  
1443 C  C   . SER A 172 ? 0.2008 0.1935 0.1128 0.0346  -0.0127 0.0384  173 SER A C   
1444 O  O   . SER A 172 ? 0.2402 0.2587 0.1203 0.0419  -0.0057 0.0296  173 SER A O   
1445 C  CB  . SER A 172 ? 0.2046 0.2122 0.1405 0.0183  0.0078  0.0307  173 SER A CB  
1446 O  OG  . SER A 172 ? 0.3384 0.2099 0.1915 0.0211  0.0006  0.0491  173 SER A OG  
1447 N  N   . ALA A 173 ? 0.1869 0.2240 0.1447 0.0555  -0.0183 0.0162  174 ALA A N   
1448 C  CA  . ALA A 173 ? 0.1852 0.2292 0.1288 0.0270  -0.0243 0.0381  174 ALA A CA  
1449 C  C   . ALA A 173 ? 0.1941 0.1953 0.1168 0.0294  -0.0260 0.0296  174 ALA A C   
1450 O  O   . ALA A 173 ? 0.1915 0.1796 0.1169 0.0252  -0.0157 0.0297  174 ALA A O   
1451 C  CB  . ALA A 173 ? 0.3030 0.2459 0.1512 0.0236  -0.0408 0.0120  174 ALA A CB  
1452 N  N   . ASP A 174 ? 0.2135 0.2371 0.1220 0.0218  -0.0166 0.0520  175 ASP A N   
1453 C  CA  . ASP A 174 ? 0.2465 0.2207 0.1641 0.0416  -0.0348 0.0617  175 ASP A CA  
1454 C  C   . ASP A 174 ? 0.2207 0.1747 0.1615 0.0305  -0.0579 0.0146  175 ASP A C   
1455 O  O   . ASP A 174 ? 0.2763 0.1976 0.2001 0.0220  -0.0087 -0.0205 175 ASP A O   
1456 C  CB  . ASP A 174 ? 0.2268 0.2619 0.2028 0.0423  -0.0406 0.0590  175 ASP A CB  
1457 C  CG  . ASP A 174 ? 0.3743 0.3619 0.2524 -0.0351 -0.1010 0.1572  175 ASP A CG  
1458 O  OD1 . ASP A 174 ? 0.4158 0.5454 0.3573 -0.1648 -0.1826 0.1310  175 ASP A OD1 
1459 O  OD2 . ASP A 174 ? 0.3319 0.3228 0.2531 -0.0597 -0.0474 0.1072  175 ASP A OD2 
1460 N  N   . PHE A 175 ? 0.2098 0.1764 0.1447 0.0098  -0.0226 -0.0060 176 PHE A N   
1461 C  CA  . PHE A 175 ? 0.2114 0.1796 0.1530 0.0206  -0.0430 0.0116  176 PHE A CA  
1462 C  C   . PHE A 175 ? 0.2012 0.1554 0.1451 -0.0082 -0.0410 0.0104  176 PHE A C   
1463 O  O   . PHE A 175 ? 0.2389 0.2123 0.1544 0.0496  -0.0728 -0.0203 176 PHE A O   
1464 C  CB  . PHE A 175 ? 0.2050 0.1439 0.1745 -0.0027 -0.0555 0.0167  176 PHE A CB  
1465 C  CG  . PHE A 175 ? 0.2146 0.1288 0.1512 -0.0006 -0.0432 0.0012  176 PHE A CG  
1466 C  CD1 . PHE A 175 ? 0.2766 0.1396 0.1755 -0.0006 -0.0412 -0.0154 176 PHE A CD1 
1467 C  CD2 . PHE A 175 ? 0.2515 0.1446 0.1578 -0.0105 -0.0679 0.0035  176 PHE A CD2 
1468 C  CE1 . PHE A 175 ? 0.2865 0.1543 0.1807 -0.0070 -0.0243 -0.0109 176 PHE A CE1 
1469 C  CE2 . PHE A 175 ? 0.2222 0.1668 0.1589 0.0068  -0.0434 0.0194  176 PHE A CE2 
1470 C  CZ  . PHE A 175 ? 0.2366 0.1413 0.1652 -0.0005 -0.0450 0.0046  176 PHE A CZ  
1471 N  N   . THR A 176 ? 0.1964 0.1808 0.1164 0.0175  -0.0348 0.0207  177 THR A N   
1472 C  CA  . THR A 176 ? 0.1780 0.1573 0.1368 0.0242  -0.0097 0.0449  177 THR A CA  
1473 C  C   . THR A 176 ? 0.1806 0.1370 0.1337 0.0147  -0.0397 0.0395  177 THR A C   
1474 O  O   . THR A 176 ? 0.2160 0.1384 0.1445 -0.0065 -0.0507 0.0162  177 THR A O   
1475 C  CB  . THR A 176 ? 0.2082 0.1666 0.1529 0.0097  -0.0379 0.0406  177 THR A CB  
1476 O  OG1 . THR A 176 ? 0.3492 0.2187 0.1306 0.0606  -0.0531 0.0491  177 THR A OG1 
1477 C  CG2 . THR A 176 ? 0.2423 0.2264 0.3212 -0.0132 -0.0097 0.1418  177 THR A CG2 
1478 N  N   . ASN A 177 ? 0.1782 0.1588 0.1193 0.0105  -0.0337 0.0212  178 ASN A N   
1479 C  CA  . ASN A 177 ? 0.1911 0.1652 0.1394 -0.0122 -0.0478 0.0313  178 ASN A CA  
1480 C  C   . ASN A 177 ? 0.2126 0.1645 0.1493 -0.0244 -0.0568 0.0368  178 ASN A C   
1481 O  O   . ASN A 177 ? 0.2673 0.2123 0.2518 -0.0306 -0.0964 0.1027  178 ASN A O   
1482 C  CB  . ASN A 177 ? 0.2018 0.1642 0.1636 0.0239  -0.0496 0.0346  178 ASN A CB  
1483 C  CG  . ASN A 177 ? 0.2251 0.1823 0.1762 0.0276  -0.0485 0.0280  178 ASN A CG  
1484 O  OD1 . ASN A 177 ? 0.2644 0.2073 0.2263 0.0397  -0.0093 0.0549  178 ASN A OD1 
1485 N  ND2 . ASN A 177 ? 0.2301 0.1783 0.1664 0.0175  -0.0522 0.0443  178 ASN A ND2 
1486 N  N   . PHE A 178 ? 0.2009 0.1513 0.1256 -0.0049 -0.0487 0.0254  179 PHE A N   
1487 C  CA  . PHE A 178 ? 0.2002 0.1372 0.1350 -0.0066 -0.0427 0.0359  179 PHE A CA  
1488 C  C   . PHE A 178 ? 0.1852 0.1456 0.1280 -0.0057 -0.0524 0.0208  179 PHE A C   
1489 O  O   . PHE A 178 ? 0.2260 0.1459 0.1388 -0.0188 -0.0461 0.0294  179 PHE A O   
1490 C  CB  . PHE A 178 ? 0.2111 0.1350 0.1381 0.0008  -0.0218 0.0267  179 PHE A CB  
1491 C  CG  . PHE A 178 ? 0.1832 0.1264 0.1421 -0.0019 -0.0335 0.0353  179 PHE A CG  
1492 C  CD1 . PHE A 178 ? 0.2213 0.1442 0.1498 -0.0130 -0.0438 0.0284  179 PHE A CD1 
1493 C  CD2 . PHE A 178 ? 0.1798 0.1323 0.1307 -0.0006 -0.0329 0.0259  179 PHE A CD2 
1494 C  CE1 . PHE A 178 ? 0.2029 0.1393 0.1516 -0.0104 -0.0423 0.0216  179 PHE A CE1 
1495 C  CE2 . PHE A 178 ? 0.1705 0.1350 0.1347 -0.0154 -0.0362 0.0302  179 PHE A CE2 
1496 C  CZ  . PHE A 178 ? 0.1990 0.1357 0.1357 -0.0038 -0.0346 0.0326  179 PHE A CZ  
1497 N  N   . ASP A 179 ? 0.1996 0.1489 0.1321 -0.0035 -0.0423 0.0394  180 ASP A N   
1498 C  CA  . ASP A 179 ? 0.1755 0.1678 0.1367 -0.0043 -0.0518 0.0296  180 ASP A CA  
1499 C  C   . ASP A 179 ? 0.1674 0.1271 0.1334 -0.0195 -0.0218 0.0182  180 ASP A C   
1500 O  O   . ASP A 179 ? 0.1886 0.1247 0.1467 -0.0087 -0.0377 0.0135  180 ASP A O   
1501 C  CB  . ASP A 179 ? 0.1653 0.2060 0.1898 -0.0032 -0.0663 0.0226  180 ASP A CB  
1502 C  CG  . ASP A 179 ? 0.1921 0.2089 0.2134 0.0165  -0.0542 0.0438  180 ASP A CG  
1503 O  OD1 . ASP A 179 ? 0.2122 0.1669 0.1820 0.0273  -0.0417 0.0478  180 ASP A OD1 
1504 O  OD2 . ASP A 179 ? 0.1938 0.3705 0.2935 -0.0126 -0.0436 0.0234  180 ASP A OD2 
1505 N  N   . PRO A 180 ? 0.1636 0.1151 0.1402 -0.0107 -0.0368 0.0171  181 PRO A N   
1506 C  CA  . PRO A 180 ? 0.1588 0.1356 0.1322 -0.0041 -0.0390 0.0233  181 PRO A CA  
1507 C  C   . PRO A 180 ? 0.1446 0.1251 0.1486 0.0077  -0.0326 0.0228  181 PRO A C   
1508 O  O   . PRO A 180 ? 0.1499 0.1332 0.1377 0.0035  -0.0331 0.0232  181 PRO A O   
1509 C  CB  . PRO A 180 ? 0.1240 0.1457 0.1664 -0.0185 -0.0226 0.0054  181 PRO A CB  
1510 C  CG  . PRO A 180 ? 0.1768 0.1423 0.1440 -0.0051 -0.0449 0.0142  181 PRO A CG  
1511 C  CD  . PRO A 180 ? 0.1815 0.1234 0.1488 -0.0109 -0.0388 0.0205  181 PRO A CD  
1512 N  N   . ARG A 181 ? 0.1474 0.1411 0.1422 -0.0020 -0.0329 0.0156  182 ARG A N   
1513 C  CA  . ARG A 181 ? 0.1455 0.1345 0.1773 -0.0137 -0.0351 0.0189  182 ARG A CA  
1514 C  C   . ARG A 181 ? 0.1281 0.1472 0.1682 0.0038  -0.0342 0.0331  182 ARG A C   
1515 O  O   . ARG A 181 ? 0.1665 0.1488 0.1946 -0.0019 -0.0381 0.0392  182 ARG A O   
1516 C  CB  . ARG A 181 ? 0.1481 0.1527 0.1685 0.0074  -0.0076 0.0340  182 ARG A CB  
1517 C  CG  . ARG A 181 ? 0.1600 0.1598 0.1914 0.0104  -0.0196 0.0062  182 ARG A CG  
1518 C  CD  . ARG A 181 ? 0.1846 0.1806 0.2380 0.0129  -0.0038 0.0221  182 ARG A CD  
1519 N  NE  . ARG A 181 ? 0.1611 0.2047 0.2486 0.0212  -0.0287 0.0599  182 ARG A NE  
1520 C  CZ  . ARG A 181 ? 0.1703 0.2630 0.2078 0.0114  0.0035  0.0737  182 ARG A CZ  
1521 N  NH1 . ARG A 181 ? 0.1983 0.2933 0.2885 0.0304  0.0259  0.0671  182 ARG A NH1 
1522 N  NH2 . ARG A 181 ? 0.1606 0.3926 0.2804 0.0450  -0.0115 0.0707  182 ARG A NH2 
1523 N  N   . GLY A 182 ? 0.1740 0.1313 0.1611 0.0021  -0.0505 0.0178  183 GLY A N   
1524 C  CA  . GLY A 182 ? 0.1719 0.1386 0.1879 -0.0140 -0.0697 0.0287  183 GLY A CA  
1525 C  C   . GLY A 182 ? 0.1967 0.1234 0.1792 0.0001  -0.0631 0.0102  183 GLY A C   
1526 O  O   . GLY A 182 ? 0.2299 0.1337 0.1951 -0.0124 -0.0894 0.0129  183 GLY A O   
1527 N  N   . LEU A 183 ? 0.1534 0.1266 0.1342 -0.0034 -0.0491 0.0162  184 LEU A N   
1528 C  CA  . LEU A 183 ? 0.1615 0.1315 0.1430 -0.0035 -0.0471 0.0215  184 LEU A CA  
1529 C  C   . LEU A 183 ? 0.1539 0.1218 0.1421 -0.0043 -0.0443 0.0080  184 LEU A C   
1530 O  O   . LEU A 183 ? 0.1708 0.1465 0.1513 0.0111  -0.0379 0.0231  184 LEU A O   
1531 C  CB  . LEU A 183 ? 0.1492 0.1324 0.1492 -0.0048 -0.0318 0.0136  184 LEU A CB  
1532 C  CG  . LEU A 183 ? 0.2020 0.1718 0.1356 0.0269  -0.0395 0.0267  184 LEU A CG  
1533 C  CD1 . LEU A 183 ? 0.1879 0.2222 0.1556 0.0057  -0.0443 0.0603  184 LEU A CD1 
1534 C  CD2 . LEU A 183 ? 0.2463 0.1938 0.1597 0.0240  -0.0196 0.0001  184 LEU A CD2 
1535 N  N   . LEU A 184 ? 0.1512 0.1368 0.1473 -0.0105 -0.0419 0.0182  185 LEU A N   
1536 C  CA  . LEU A 184 ? 0.1222 0.1444 0.1500 -0.0114 -0.0322 0.0163  185 LEU A CA  
1537 C  C   . LEU A 184 ? 0.1497 0.1405 0.1640 -0.0303 -0.0390 0.0093  185 LEU A C   
1538 O  O   . LEU A 184 ? 0.1649 0.1700 0.1836 -0.0303 -0.0625 0.0194  185 LEU A O   
1539 C  CB  . LEU A 184 ? 0.1353 0.1537 0.1512 -0.0270 -0.0227 0.0163  185 LEU A CB  
1540 C  CG  . LEU A 184 ? 0.1199 0.1554 0.1762 -0.0100 -0.0197 0.0173  185 LEU A CG  
1541 C  CD1 . LEU A 184 ? 0.1506 0.1793 0.2155 0.0109  -0.0074 -0.0142 185 LEU A CD1 
1542 C  CD2 . LEU A 184 ? 0.1289 0.1761 0.2563 -0.0085 -0.0452 0.0121  185 LEU A CD2 
1543 N  N   . PRO A 185 ? 0.1202 0.1262 0.1485 -0.0068 -0.0397 0.0147  186 PRO A N   
1544 C  CA  . PRO A 185 ? 0.1485 0.1347 0.1643 -0.0049 -0.0222 0.0298  186 PRO A CA  
1545 C  C   . PRO A 185 ? 0.1457 0.1212 0.1737 -0.0122 -0.0326 0.0261  186 PRO A C   
1546 O  O   . PRO A 185 ? 0.1001 0.1440 0.2640 -0.0054 -0.0342 0.0368  186 PRO A O   
1547 C  CB  . PRO A 185 ? 0.1387 0.1377 0.1450 0.0107  -0.0137 0.0264  186 PRO A CB  
1548 C  CG  . PRO A 185 ? 0.1148 0.1437 0.1430 0.0203  -0.0108 0.0119  186 PRO A CG  
1549 C  CD  . PRO A 185 ? 0.1137 0.1377 0.1211 -0.0001 -0.0208 0.0129  186 PRO A CD  
1550 N  N   A GLU A 186 ? 0.1199 0.1539 0.1860 -0.0249 -0.0322 0.0159  187 GLU A N   
1551 N  N   B GLU A 186 ? 0.1282 0.1528 0.2047 -0.0250 -0.0401 0.0384  187 GLU A N   
1552 C  CA  A GLU A 186 ? 0.1300 0.1955 0.2093 -0.0395 -0.0434 -0.0113 187 GLU A CA  
1553 C  CA  B GLU A 186 ? 0.1125 0.1631 0.2037 -0.0478 -0.0298 0.0023  187 GLU A CA  
1554 C  C   A GLU A 186 ? 0.0908 0.1625 0.2110 0.0146  -0.0027 0.0241  187 GLU A C   
1555 C  C   B GLU A 186 ? 0.1048 0.1525 0.2238 -0.0097 -0.0214 0.0264  187 GLU A C   
1556 O  O   A GLU A 186 ? 0.1148 0.1824 0.2017 0.0211  0.0225  0.0013  187 GLU A O   
1557 O  O   B GLU A 186 ? 0.0839 0.2048 0.2957 0.0121  -0.0307 0.0292  187 GLU A O   
1558 C  CB  A GLU A 186 ? 0.1177 0.1819 0.1694 0.0003  -0.0254 -0.0060 187 GLU A CB  
1559 C  CB  B GLU A 186 ? 0.1351 0.2050 0.2892 -0.0776 -0.0229 0.0122  187 GLU A CB  
1560 C  CG  A GLU A 186 ? 0.1145 0.2011 0.2653 0.0000  -0.0355 0.0111  187 GLU A CG  
1561 C  CG  B GLU A 186 ? 0.2466 0.1779 0.2912 -0.0615 -0.0865 0.0261  187 GLU A CG  
1562 C  CD  A GLU A 186 ? 0.1771 0.2515 0.3045 0.0035  0.0318  0.0193  187 GLU A CD  
1563 C  CD  B GLU A 186 ? 0.2136 0.3048 0.3289 -0.0873 0.0153  0.0392  187 GLU A CD  
1564 O  OE1 A GLU A 186 ? 0.2293 0.1737 0.3578 -0.0392 0.0052  0.0302  187 GLU A OE1 
1565 O  OE1 B GLU A 186 ? 0.1729 0.2958 0.3603 -0.0944 -0.0152 -0.0335 187 GLU A OE1 
1566 O  OE2 A GLU A 186 ? 0.2520 0.2113 0.3010 0.0480  0.0645  0.0690  187 GLU A OE2 
1567 O  OE2 B GLU A 186 ? 0.1489 0.3147 0.5417 -0.0800 0.0043  -0.0156 187 GLU A OE2 
1568 N  N   . SER A 187 ? 0.1001 0.1508 0.1798 -0.0093 -0.0157 -0.0003 188 SER A N   
1569 C  CA  . SER A 187 ? 0.1177 0.1458 0.1999 -0.0035 0.0252  0.0199  188 SER A CA  
1570 C  C   . SER A 187 ? 0.0909 0.1655 0.1888 -0.0088 0.0010  0.0000  188 SER A C   
1571 O  O   . SER A 187 ? 0.1023 0.1914 0.1952 -0.0177 0.0027  -0.0217 188 SER A O   
1572 C  CB  . SER A 187 ? 0.1482 0.2106 0.1791 -0.0153 0.0013  0.0137  188 SER A CB  
1573 O  OG  . SER A 187 ? 0.1516 0.2003 0.2031 -0.0232 0.0051  0.0228  188 SER A OG  
1574 N  N   . LEU A 188 ? 0.0995 0.1556 0.1791 -0.0157 -0.0093 -0.0017 189 LEU A N   
1575 C  CA  . LEU A 188 ? 0.1151 0.1622 0.1879 -0.0043 -0.0099 -0.0046 189 LEU A CA  
1576 C  C   . LEU A 188 ? 0.1010 0.1480 0.1784 -0.0098 0.0006  -0.0208 189 LEU A C   
1577 O  O   . LEU A 188 ? 0.1312 0.1631 0.1888 0.0006  -0.0138 -0.0140 189 LEU A O   
1578 C  CB  . LEU A 188 ? 0.1393 0.1594 0.1982 -0.0278 -0.0193 0.0086  189 LEU A CB  
1579 C  CG  . LEU A 188 ? 0.1441 0.1853 0.2171 -0.0028 -0.0185 0.0215  189 LEU A CG  
1580 C  CD1 . LEU A 188 ? 0.2094 0.1934 0.2448 -0.0253 -0.0302 0.0671  189 LEU A CD1 
1581 C  CD2 . LEU A 188 ? 0.1483 0.2854 0.1958 0.0041  -0.0260 0.0318  189 LEU A CD2 
1582 N  N   . ASP A 189 ? 0.0964 0.1668 0.1550 0.0024  0.0054  -0.0168 190 ASP A N   
1583 C  CA  . ASP A 189 ? 0.0979 0.1879 0.1590 -0.0241 0.0303  -0.0068 190 ASP A CA  
1584 C  C   . ASP A 189 ? 0.1041 0.1371 0.1344 -0.0198 0.0122  -0.0083 190 ASP A C   
1585 O  O   . ASP A 189 ? 0.1017 0.1421 0.1314 -0.0154 0.0120  -0.0098 190 ASP A O   
1586 C  CB  . ASP A 189 ? 0.1245 0.2080 0.1757 -0.0518 0.0272  0.0170  190 ASP A CB  
1587 C  CG  . ASP A 189 ? 0.1691 0.3084 0.2110 -0.0958 -0.0089 0.0082  190 ASP A CG  
1588 O  OD1 . ASP A 189 ? 0.1907 0.4311 0.3190 -0.0441 0.0954  -0.0282 190 ASP A OD1 
1589 O  OD2 . ASP A 189 ? 0.1884 0.4269 0.2628 -0.1246 0.0195  0.0465  190 ASP A OD2 
1590 N  N   . TYR A 190 ? 0.0922 0.1372 0.1194 0.0000  0.0103  0.0027  191 TYR A N   
1591 C  CA  . TYR A 190 ? 0.0913 0.1321 0.1227 -0.0131 0.0065  0.0104  191 TYR A CA  
1592 C  C   . TYR A 190 ? 0.1001 0.1187 0.1132 -0.0023 0.0217  0.0023  191 TYR A C   
1593 O  O   . TYR A 190 ? 0.1177 0.1432 0.1102 -0.0040 0.0228  -0.0013 191 TYR A O   
1594 C  CB  . TYR A 190 ? 0.1141 0.1412 0.1105 -0.0155 0.0085  0.0071  191 TYR A CB  
1595 C  CG  . TYR A 190 ? 0.1157 0.1326 0.1186 -0.0148 0.0131  0.0157  191 TYR A CG  
1596 C  CD1 . TYR A 190 ? 0.1238 0.1362 0.1403 -0.0125 0.0071  0.0015  191 TYR A CD1 
1597 C  CD2 . TYR A 190 ? 0.1190 0.1435 0.1393 0.0065  0.0149  0.0121  191 TYR A CD2 
1598 C  CE1 . TYR A 190 ? 0.1316 0.1388 0.1618 0.0006  -0.0082 0.0015  191 TYR A CE1 
1599 C  CE2 . TYR A 190 ? 0.1289 0.1492 0.1625 -0.0137 0.0085  0.0060  191 TYR A CE2 
1600 C  CZ  . TYR A 190 ? 0.1494 0.1352 0.1407 0.0146  0.0074  -0.0063 191 TYR A CZ  
1601 O  OH  . TYR A 190 ? 0.1552 0.1614 0.1521 0.0230  -0.0063 -0.0148 191 TYR A OH  
1602 N  N   . TRP A 191 ? 0.0926 0.1102 0.1119 -0.0013 0.0032  -0.0013 192 TRP A N   
1603 C  CA  . TRP A 191 ? 0.0952 0.1132 0.1087 -0.0010 0.0060  0.0063  192 TRP A CA  
1604 C  C   . TRP A 191 ? 0.0912 0.1211 0.0812 0.0054  0.0153  -0.0023 192 TRP A C   
1605 O  O   . TRP A 191 ? 0.1159 0.1182 0.0938 -0.0111 0.0087  0.0027  192 TRP A O   
1606 C  CB  . TRP A 191 ? 0.1105 0.1216 0.1103 0.0028  0.0164  0.0093  192 TRP A CB  
1607 C  CG  . TRP A 191 ? 0.1058 0.1193 0.1163 0.0099  0.0166  0.0131  192 TRP A CG  
1608 C  CD1 . TRP A 191 ? 0.1324 0.1307 0.1195 0.0093  0.0098  0.0089  192 TRP A CD1 
1609 C  CD2 . TRP A 191 ? 0.0971 0.1169 0.1299 0.0041  0.0037  0.0188  192 TRP A CD2 
1610 N  NE1 . TRP A 191 ? 0.1557 0.1253 0.1309 0.0104  0.0141  0.0163  192 TRP A NE1 
1611 C  CE2 . TRP A 191 ? 0.1227 0.1290 0.1379 -0.0028 0.0115  0.0032  192 TRP A CE2 
1612 C  CE3 . TRP A 191 ? 0.0988 0.1368 0.1306 0.0074  0.0057  0.0013  192 TRP A CE3 
1613 C  CZ2 . TRP A 191 ? 0.1430 0.1160 0.1614 0.0093  -0.0054 0.0019  192 TRP A CZ2 
1614 C  CZ3 . TRP A 191 ? 0.1128 0.1414 0.1555 -0.0010 0.0099  -0.0063 192 TRP A CZ3 
1615 C  CH2 . TRP A 191 ? 0.1433 0.1453 0.1761 -0.0006 -0.0151 -0.0097 192 TRP A CH2 
1616 N  N   . THR A 192 ? 0.0947 0.1133 0.0904 0.0000  0.0038  0.0003  193 THR A N   
1617 C  CA  . THR A 192 ? 0.0939 0.1155 0.0910 0.0078  0.0063  0.0068  193 THR A CA  
1618 C  C   . THR A 192 ? 0.0942 0.1027 0.0830 0.0038  0.0165  -0.0017 193 THR A C   
1619 O  O   . THR A 192 ? 0.1127 0.1283 0.0873 -0.0038 0.0091  0.0046  193 THR A O   
1620 C  CB  . THR A 192 ? 0.1083 0.1068 0.1004 0.0100  0.0151  -0.0006 193 THR A CB  
1621 O  OG1 . THR A 192 ? 0.1035 0.1093 0.1078 0.0063  0.0108  -0.0010 193 THR A OG1 
1622 C  CG2 . THR A 192 ? 0.1173 0.1438 0.1075 0.0113  0.0275  -0.0057 193 THR A CG2 
1623 N  N   . TYR A 193 ? 0.0876 0.1103 0.0877 0.0041  0.0037  -0.0027 194 TYR A N   
1624 C  CA  . TYR A 193 ? 0.0913 0.1198 0.0870 0.0020  0.0021  0.0038  194 TYR A CA  
1625 C  C   . TYR A 193 ? 0.0944 0.1118 0.0812 0.0099  0.0068  -0.0129 194 TYR A C   
1626 O  O   . TYR A 193 ? 0.1001 0.1118 0.0855 0.0026  -0.0030 -0.0041 194 TYR A O   
1627 C  CB  . TYR A 193 ? 0.1146 0.1254 0.0817 0.0057  0.0066  -0.0048 194 TYR A CB  
1628 C  CG  . TYR A 193 ? 0.1024 0.0970 0.0932 0.0015  -0.0028 0.0044  194 TYR A CG  
1629 C  CD1 . TYR A 193 ? 0.1083 0.1014 0.0900 0.0091  0.0035  0.0010  194 TYR A CD1 
1630 C  CD2 . TYR A 193 ? 0.0989 0.1027 0.1052 0.0027  -0.0024 0.0026  194 TYR A CD2 
1631 C  CE1 . TYR A 193 ? 0.0882 0.0979 0.0947 0.0040  -0.0126 0.0041  194 TYR A CE1 
1632 C  CE2 . TYR A 193 ? 0.0929 0.1039 0.1048 0.0049  -0.0015 -0.0040 194 TYR A CE2 
1633 C  CZ  . TYR A 193 ? 0.0984 0.0852 0.0888 0.0104  -0.0006 -0.0060 194 TYR A CZ  
1634 O  OH  . TYR A 193 ? 0.0971 0.0960 0.0922 0.0030  0.0024  -0.0044 194 TYR A OH  
1635 N  N   . PRO A 194 ? 0.0894 0.1195 0.0855 0.0049  -0.0020 -0.0110 195 PRO A N   
1636 C  CA  . PRO A 194 ? 0.0983 0.1089 0.1080 0.0099  -0.0006 -0.0259 195 PRO A CA  
1637 C  C   . PRO A 194 ? 0.0816 0.0883 0.1008 -0.0003 -0.0023 -0.0071 195 PRO A C   
1638 O  O   . PRO A 194 ? 0.1015 0.1247 0.0993 0.0109  -0.0087 -0.0110 195 PRO A O   
1639 C  CB  . PRO A 194 ? 0.1342 0.1460 0.1006 -0.0034 -0.0005 -0.0311 195 PRO A CB  
1640 C  CG  . PRO A 194 ? 0.1528 0.1544 0.1045 -0.0054 -0.0024 -0.0285 195 PRO A CG  
1641 C  CD  . PRO A 194 ? 0.1195 0.1551 0.0843 -0.0186 -0.0043 -0.0141 195 PRO A CD  
1642 N  N   . GLY A 195 ? 0.0859 0.1023 0.0899 -0.0040 0.0060  -0.0129 196 GLY A N   
1643 C  CA  . GLY A 195 ? 0.0892 0.0971 0.1050 0.0104  0.0038  -0.0055 196 GLY A CA  
1644 C  C   . GLY A 195 ? 0.0772 0.0905 0.0982 -0.0032 -0.0057 -0.0076 196 GLY A C   
1645 O  O   . GLY A 195 ? 0.1024 0.0948 0.1024 -0.0049 0.0000  -0.0130 196 GLY A O   
1646 N  N   . SER A 196 ? 0.0794 0.0952 0.0922 0.0020  -0.0017 -0.0086 197 SER A N   
1647 C  CA  . SER A 196 ? 0.0790 0.1015 0.0961 -0.0105 0.0027  -0.0001 197 SER A CA  
1648 C  C   . SER A 196 ? 0.0606 0.0834 0.0987 -0.0051 -0.0041 -0.0031 197 SER A C   
1649 O  O   . SER A 196 ? 0.0797 0.0899 0.0951 -0.0073 -0.0020 -0.0082 197 SER A O   
1650 C  CB  . SER A 196 ? 0.0958 0.1009 0.1058 -0.0017 -0.0070 -0.0031 197 SER A CB  
1651 O  OG  . SER A 196 ? 0.0785 0.0974 0.1112 0.0017  -0.0023 -0.0115 197 SER A OG  
1652 N  N   . LEU A 197 ? 0.0825 0.0938 0.0971 -0.0046 0.0082  -0.0107 198 LEU A N   
1653 C  CA  . LEU A 197 ? 0.0811 0.0913 0.0925 -0.0076 0.0046  -0.0088 198 LEU A CA  
1654 C  C   . LEU A 197 ? 0.0777 0.0930 0.0988 -0.0081 0.0071  -0.0035 198 LEU A C   
1655 O  O   . LEU A 197 ? 0.0808 0.1045 0.1035 -0.0054 -0.0040 -0.0113 198 LEU A O   
1656 C  CB  . LEU A 197 ? 0.0984 0.1041 0.1103 -0.0130 0.0059  0.0007  198 LEU A CB  
1657 C  CG  . LEU A 197 ? 0.1085 0.1030 0.1096 -0.0222 -0.0010 -0.0005 198 LEU A CG  
1658 C  CD1 . LEU A 197 ? 0.1191 0.1458 0.1600 -0.0252 0.0068  0.0181  198 LEU A CD1 
1659 C  CD2 . LEU A 197 ? 0.1076 0.1184 0.1764 0.0062  0.0104  0.0353  198 LEU A CD2 
1660 N  N   . THR A 198 ? 0.0820 0.0907 0.0925 -0.0038 -0.0008 -0.0103 199 THR A N   
1661 C  CA  . THR A 198 ? 0.0886 0.0957 0.1112 -0.0006 0.0049  -0.0108 199 THR A CA  
1662 C  C   . THR A 198 ? 0.0716 0.0944 0.1048 -0.0065 -0.0046 -0.0131 199 THR A C   
1663 O  O   . THR A 198 ? 0.0844 0.1120 0.1234 -0.0020 0.0015  -0.0119 199 THR A O   
1664 C  CB  . THR A 198 ? 0.0912 0.0926 0.0940 0.0007  0.0031  -0.0035 199 THR A CB  
1665 O  OG1 . THR A 198 ? 0.0874 0.0913 0.0970 -0.0063 -0.0035 -0.0015 199 THR A OG1 
1666 C  CG2 . THR A 198 ? 0.0908 0.1130 0.1168 -0.0005 0.0098  -0.0043 199 THR A CG2 
1667 N  N   . THR A 199 ? 0.0988 0.1171 0.1028 -0.0109 0.0063  -0.0093 200 THR A N   
1668 C  CA  . THR A 199 ? 0.1040 0.1317 0.1103 -0.0192 0.0177  -0.0043 200 THR A CA  
1669 C  C   . THR A 199 ? 0.0922 0.1247 0.1239 0.0006  0.0094  -0.0006 200 THR A C   
1670 O  O   . THR A 199 ? 0.0948 0.1118 0.1230 -0.0152 0.0030  -0.0152 200 THR A O   
1671 C  CB  . THR A 199 ? 0.1401 0.1835 0.1164 -0.0331 -0.0027 -0.0133 200 THR A CB  
1672 O  OG1 . THR A 199 ? 0.2008 0.1633 0.1948 -0.0346 -0.0511 0.0243  200 THR A OG1 
1673 C  CG2 . THR A 199 ? 0.1351 0.1678 0.1160 -0.0373 0.0132  -0.0226 200 THR A CG2 
1674 N  N   . PRO A 200 ? 0.1027 0.1300 0.1177 -0.0080 0.0154  -0.0019 201 PRO A N   
1675 C  CA  . PRO A 200 ? 0.1039 0.1218 0.1290 -0.0171 0.0168  -0.0041 201 PRO A CA  
1676 C  C   . PRO A 200 ? 0.1031 0.1328 0.1175 -0.0232 0.0124  0.0024  201 PRO A C   
1677 O  O   . PRO A 200 ? 0.1368 0.1362 0.1348 -0.0222 -0.0010 0.0093  201 PRO A O   
1678 C  CB  . PRO A 200 ? 0.1168 0.1468 0.1453 -0.0179 0.0198  -0.0065 201 PRO A CB  
1679 C  CG  . PRO A 200 ? 0.1004 0.1661 0.1632 -0.0024 0.0214  -0.0188 201 PRO A CG  
1680 C  CD  . PRO A 200 ? 0.1087 0.1473 0.1353 -0.0055 0.0138  -0.0162 201 PRO A CD  
1681 N  N   . PRO A 201 ? 0.0923 0.1289 0.1363 -0.0207 0.0132  0.0041  202 PRO A N   
1682 C  CA  . PRO A 201 ? 0.1115 0.1333 0.1407 -0.0251 0.0060  0.0006  202 PRO A CA  
1683 C  C   . PRO A 201 ? 0.0975 0.1207 0.1360 -0.0163 0.0008  -0.0059 202 PRO A C   
1684 O  O   . PRO A 201 ? 0.1136 0.1314 0.1418 -0.0263 0.0063  -0.0060 202 PRO A O   
1685 C  CB  . PRO A 201 ? 0.1601 0.1279 0.1808 -0.0361 0.0071  0.0181  202 PRO A CB  
1686 C  CG  . PRO A 201 ? 0.1559 0.1314 0.1900 -0.0098 0.0028  0.0012  202 PRO A CG  
1687 C  CD  . PRO A 201 ? 0.1616 0.1401 0.1507 -0.0154 -0.0104 0.0109  202 PRO A CD  
1688 N  N   . LEU A 202 ? 0.0930 0.1121 0.1216 -0.0094 0.0127  0.0060  203 LEU A N   
1689 C  CA  . LEU A 202 ? 0.0899 0.1014 0.1240 -0.0065 -0.0038 -0.0133 203 LEU A CA  
1690 C  C   . LEU A 202 ? 0.0935 0.1087 0.1186 -0.0216 0.0060  -0.0041 203 LEU A C   
1691 O  O   . LEU A 202 ? 0.0935 0.1096 0.1309 -0.0098 0.0003  -0.0148 203 LEU A O   
1692 C  CB  . LEU A 202 ? 0.0887 0.1172 0.1324 -0.0024 0.0005  -0.0125 203 LEU A CB  
1693 C  CG  . LEU A 202 ? 0.0835 0.1186 0.1315 0.0024  0.0105  -0.0136 203 LEU A CG  
1694 C  CD1 . LEU A 202 ? 0.0900 0.1464 0.1642 -0.0065 -0.0096 -0.0172 203 LEU A CD1 
1695 C  CD2 . LEU A 202 ? 0.1014 0.1220 0.1379 -0.0098 -0.0035 -0.0126 203 LEU A CD2 
1696 N  N   . LEU A 203 ? 0.0931 0.1083 0.1298 -0.0093 0.0114  -0.0065 204 LEU A N   
1697 C  CA  . LEU A 203 ? 0.0930 0.1112 0.1420 -0.0126 0.0068  -0.0162 204 LEU A CA  
1698 C  C   . LEU A 203 ? 0.0986 0.0954 0.1308 -0.0059 0.0026  -0.0192 204 LEU A C   
1699 O  O   . LEU A 203 ? 0.0975 0.1036 0.1127 -0.0104 -0.0046 -0.0116 204 LEU A O   
1700 C  CB  . LEU A 203 ? 0.1268 0.1092 0.1675 -0.0108 0.0186  0.0060  204 LEU A CB  
1701 C  CG  . LEU A 203 ? 0.1493 0.1377 0.1779 -0.0065 0.0423  0.0010  204 LEU A CG  
1702 C  CD1 . LEU A 203 ? 0.1682 0.1289 0.2221 0.0184  0.0313  0.0236  204 LEU A CD1 
1703 C  CD2 . LEU A 203 ? 0.1562 0.1784 0.2777 -0.0678 0.0085  0.0092  204 LEU A CD2 
1704 N  N   . GLU A 204 ? 0.0993 0.1115 0.1227 -0.0131 -0.0065 -0.0209 205 GLU A N   
1705 C  CA  . GLU A 204 ? 0.0961 0.1112 0.1282 -0.0017 -0.0118 -0.0276 205 GLU A CA  
1706 C  C   . GLU A 204 ? 0.1062 0.1023 0.1146 -0.0107 -0.0115 -0.0244 205 GLU A C   
1707 O  O   . GLU A 204 ? 0.1348 0.1534 0.1357 0.0255  -0.0259 -0.0355 205 GLU A O   
1708 C  CB  . GLU A 204 ? 0.1162 0.1341 0.1317 0.0052  -0.0428 -0.0262 205 GLU A CB  
1709 C  CG  . GLU A 204 ? 0.1089 0.1274 0.1412 0.0023  -0.0252 -0.0373 205 GLU A CG  
1710 C  CD  . GLU A 204 ? 0.1194 0.1454 0.1402 -0.0063 -0.0248 -0.0335 205 GLU A CD  
1711 O  OE1 . GLU A 204 ? 0.1571 0.1618 0.1967 0.0092  -0.0663 -0.0465 205 GLU A OE1 
1712 O  OE2 . GLU A 204 ? 0.1148 0.1405 0.1509 -0.0087 -0.0250 -0.0160 205 GLU A OE2 
1713 N  N   . CYS A 205 ? 0.0912 0.0971 0.1168 -0.0088 -0.0108 -0.0107 206 CYS A N   
1714 C  CA  . CYS A 205 ? 0.0964 0.0973 0.1150 -0.0068 -0.0013 -0.0131 206 CYS A CA  
1715 C  C   . CYS A 205 ? 0.0973 0.0926 0.1040 0.0038  -0.0113 -0.0081 206 CYS A C   
1716 O  O   . CYS A 205 ? 0.1132 0.0992 0.1483 -0.0041 -0.0274 -0.0054 206 CYS A O   
1717 C  CB  . CYS A 205 ? 0.1150 0.1121 0.1177 -0.0194 0.0006  -0.0054 206 CYS A CB  
1718 S  SG  . CYS A 205 ? 0.1367 0.1136 0.1231 -0.0041 -0.0035 -0.0060 206 CYS A SG  
1719 N  N   . VAL A 206 ? 0.0938 0.0892 0.1089 0.0019  -0.0030 -0.0026 207 VAL A N   
1720 C  CA  . VAL A 206 ? 0.0957 0.0891 0.1111 -0.0130 -0.0043 -0.0026 207 VAL A CA  
1721 C  C   . VAL A 206 ? 0.0945 0.0892 0.1137 0.0065  -0.0141 -0.0119 207 VAL A C   
1722 O  O   . VAL A 206 ? 0.0970 0.1137 0.1195 0.0065  -0.0048 0.0114  207 VAL A O   
1723 C  CB  . VAL A 206 ? 0.0973 0.0936 0.1130 -0.0017 -0.0006 -0.0086 207 VAL A CB  
1724 C  CG1 . VAL A 206 ? 0.0996 0.0912 0.1132 -0.0049 -0.0110 -0.0066 207 VAL A CG1 
1725 C  CG2 . VAL A 206 ? 0.1057 0.1067 0.1098 0.0062  0.0076  -0.0086 207 VAL A CG2 
1726 N  N   . THR A 207 ? 0.0829 0.0874 0.0930 0.0015  -0.0024 -0.0068 208 THR A N   
1727 C  CA  . THR A 207 ? 0.0996 0.0913 0.0886 -0.0019 0.0074  -0.0013 208 THR A CA  
1728 C  C   . THR A 207 ? 0.0860 0.0860 0.0888 -0.0052 0.0068  -0.0043 208 THR A C   
1729 O  O   . THR A 207 ? 0.1009 0.0896 0.1031 0.0028  -0.0086 0.0012  208 THR A O   
1730 C  CB  . THR A 207 ? 0.1114 0.0882 0.1150 0.0001  0.0001  -0.0138 208 THR A CB  
1731 O  OG1 . THR A 207 ? 0.1274 0.1055 0.1297 0.0000  0.0071  -0.0248 208 THR A OG1 
1732 C  CG2 . THR A 207 ? 0.1184 0.1108 0.1411 -0.0010 0.0126  -0.0113 208 THR A CG2 
1733 N  N   . TRP A 208 ? 0.0810 0.0835 0.0857 -0.0035 0.0027  -0.0017 209 TRP A N   
1734 C  CA  . TRP A 208 ? 0.0859 0.0847 0.0830 0.0013  0.0017  -0.0060 209 TRP A CA  
1735 C  C   . TRP A 208 ? 0.0764 0.0874 0.0842 0.0074  -0.0013 -0.0012 209 TRP A C   
1736 O  O   . TRP A 208 ? 0.0825 0.0992 0.0878 -0.0023 0.0087  -0.0035 209 TRP A O   
1737 C  CB  . TRP A 208 ? 0.0854 0.0900 0.0891 0.0043  -0.0024 0.0017  209 TRP A CB  
1738 C  CG  . TRP A 208 ? 0.0850 0.0772 0.0895 0.0051  -0.0043 0.0000  209 TRP A CG  
1739 C  CD1 . TRP A 208 ? 0.0970 0.0847 0.0987 0.0059  0.0028  -0.0005 209 TRP A CD1 
1740 C  CD2 . TRP A 208 ? 0.0820 0.0776 0.0926 0.0052  0.0015  -0.0043 209 TRP A CD2 
1741 N  NE1 . TRP A 208 ? 0.0842 0.0931 0.1053 -0.0038 0.0023  -0.0030 209 TRP A NE1 
1742 C  CE2 . TRP A 208 ? 0.0832 0.0784 0.1024 0.0107  0.0023  -0.0024 209 TRP A CE2 
1743 C  CE3 . TRP A 208 ? 0.0803 0.0804 0.0914 0.0043  -0.0066 -0.0015 209 TRP A CE3 
1744 C  CZ2 . TRP A 208 ? 0.1005 0.0917 0.1105 0.0232  0.0140  0.0007  209 TRP A CZ2 
1745 C  CZ3 . TRP A 208 ? 0.1011 0.0965 0.0939 0.0151  0.0013  0.0023  209 TRP A CZ3 
1746 C  CH2 . TRP A 208 ? 0.1193 0.0912 0.1080 0.0187  0.0031  0.0035  209 TRP A CH2 
1747 N  N   . ILE A 209 ? 0.0795 0.0802 0.0878 -0.0027 0.0010  0.0013  210 ILE A N   
1748 C  CA  . ILE A 209 ? 0.0800 0.0868 0.1026 -0.0032 -0.0034 -0.0070 210 ILE A CA  
1749 C  C   . ILE A 209 ? 0.0813 0.0839 0.0882 -0.0046 0.0113  -0.0012 210 ILE A C   
1750 O  O   . ILE A 209 ? 0.1215 0.0851 0.0939 -0.0057 -0.0006 0.0008  210 ILE A O   
1751 C  CB  . ILE A 209 ? 0.0817 0.0922 0.1225 0.0055  0.0019  -0.0049 210 ILE A CB  
1752 C  CG1 . ILE A 209 ? 0.0984 0.1057 0.1418 0.0151  -0.0104 -0.0199 210 ILE A CG1 
1753 C  CG2 . ILE A 209 ? 0.0763 0.1290 0.1421 0.0024  -0.0013 0.0041  210 ILE A CG2 
1754 C  CD1 . ILE A 209 ? 0.1107 0.1085 0.1789 0.0161  0.0000  -0.0049 210 ILE A CD1 
1755 N  N   . VAL A 210 ? 0.0848 0.0838 0.0980 -0.0012 0.0013  0.0003  211 VAL A N   
1756 C  CA  . VAL A 210 ? 0.0811 0.0923 0.0873 -0.0046 0.0049  -0.0013 211 VAL A CA  
1757 C  C   . VAL A 210 ? 0.0956 0.0855 0.0923 0.0071  0.0068  0.0031  211 VAL A C   
1758 O  O   . VAL A 210 ? 0.0944 0.1068 0.0966 -0.0089 0.0049  0.0041  211 VAL A O   
1759 C  CB  . VAL A 210 ? 0.0922 0.0942 0.1049 0.0003  0.0005  0.0027  211 VAL A CB  
1760 C  CG1 . VAL A 210 ? 0.1090 0.0934 0.1254 0.0017  0.0031  0.0005  211 VAL A CG1 
1761 C  CG2 . VAL A 210 ? 0.0945 0.1026 0.1269 -0.0031 0.0118  0.0087  211 VAL A CG2 
1762 N  N   . LEU A 211 ? 0.0851 0.1024 0.1010 -0.0111 0.0032  0.0000  212 LEU A N   
1763 C  CA  . LEU A 211 ? 0.0802 0.1068 0.1132 -0.0076 0.0005  -0.0051 212 LEU A CA  
1764 C  C   . LEU A 211 ? 0.0973 0.1053 0.0976 -0.0104 0.0048  -0.0096 212 LEU A C   
1765 O  O   . LEU A 211 ? 0.1050 0.1130 0.1115 -0.0082 0.0052  0.0035  212 LEU A O   
1766 C  CB  . LEU A 211 ? 0.0958 0.1150 0.1239 -0.0080 -0.0065 0.0010  212 LEU A CB  
1767 C  CG  . LEU A 211 ? 0.1048 0.1255 0.1224 -0.0046 -0.0052 0.0059  212 LEU A CG  
1768 C  CD1 . LEU A 211 ? 0.0944 0.1703 0.1562 -0.0092 -0.0148 0.0172  212 LEU A CD1 
1769 C  CD2 . LEU A 211 ? 0.1166 0.1216 0.1385 0.0044  0.0093  -0.0086 212 LEU A CD2 
1770 N  N   . LYS A 212 ? 0.1146 0.1272 0.1103 -0.0159 0.0057  0.0071  213 LYS A N   
1771 C  CA  . LYS A 212 ? 0.1342 0.1266 0.1255 -0.0310 -0.0007 0.0127  213 LYS A CA  
1772 C  C   . LYS A 212 ? 0.1148 0.1036 0.1230 -0.0198 -0.0059 0.0179  213 LYS A C   
1773 O  O   . LYS A 212 ? 0.1325 0.1243 0.1720 -0.0080 -0.0313 0.0174  213 LYS A O   
1774 C  CB  . LYS A 212 ? 0.1955 0.1858 0.1344 -0.0857 0.0205  0.0138  213 LYS A CB  
1775 C  CG  . LYS A 212 ? 0.4239 0.2797 0.1834 -0.1513 0.0146  0.0661  213 LYS A CG  
1776 C  CD  . LYS A 212 ? 0.4176 0.4618 0.2982 -0.2612 0.0894  -0.0206 213 LYS A CD  
1777 C  CE  . LYS A 212 ? 0.4476 0.3826 0.3249 -0.0724 0.0816  0.0623  213 LYS A CE  
1778 N  NZ  . LYS A 212 ? 0.2483 0.3041 0.3440 -0.0125 0.0054  0.0120  213 LYS A NZ  
1779 N  N   A GLU A 213 ? 0.0896 0.1229 0.1295 -0.0164 -0.0017 0.0116  214 GLU A N   
1780 N  N   B GLU A 213 ? 0.0912 0.1227 0.1293 -0.0148 -0.0071 0.0131  214 GLU A N   
1781 C  CA  A GLU A 213 ? 0.1054 0.1130 0.1184 -0.0031 0.0000  0.0003  214 GLU A CA  
1782 C  CA  B GLU A 213 ? 0.1120 0.1175 0.1263 -0.0122 -0.0092 0.0000  214 GLU A CA  
1783 C  C   A GLU A 213 ? 0.1080 0.1018 0.1150 -0.0110 -0.0114 0.0121  214 GLU A C   
1784 C  C   B GLU A 213 ? 0.0926 0.1159 0.1370 -0.0087 -0.0104 0.0196  214 GLU A C   
1785 O  O   A GLU A 213 ? 0.0970 0.1036 0.1255 -0.0035 0.0031  0.0120  214 GLU A O   
1786 O  O   B GLU A 213 ? 0.0992 0.1155 0.1359 -0.0006 -0.0081 0.0164  214 GLU A O   
1787 C  CB  A GLU A 213 ? 0.0952 0.1227 0.1523 -0.0153 -0.0068 0.0094  214 GLU A CB  
1788 C  CB  B GLU A 213 ? 0.0978 0.1518 0.1534 -0.0182 -0.0204 0.0093  214 GLU A CB  
1789 C  CG  A GLU A 213 ? 0.1221 0.1884 0.1627 -0.0208 -0.0355 -0.0063 214 GLU A CG  
1790 C  CG  B GLU A 213 ? 0.1489 0.1539 0.1595 -0.0449 -0.0287 0.0223  214 GLU A CG  
1791 C  CD  A GLU A 213 ? 0.1252 0.1606 0.2090 -0.0472 -0.0461 0.0135  214 GLU A CD  
1792 C  CD  B GLU A 213 ? 0.1709 0.1657 0.2166 -0.0328 -0.0097 -0.0099 214 GLU A CD  
1793 O  OE1 A GLU A 213 ? 0.1103 0.1732 0.1607 -0.0228 -0.0107 0.0013  214 GLU A OE1 
1794 O  OE1 B GLU A 213 ? 0.1387 0.1773 0.1870 -0.0368 -0.0043 0.0203  214 GLU A OE1 
1795 O  OE2 A GLU A 213 ? 0.1600 0.1623 0.2640 -0.0467 -0.0619 -0.0023 214 GLU A OE2 
1796 O  OE2 B GLU A 213 ? 0.2140 0.2065 0.2712 -0.0115 -0.0834 -0.0132 214 GLU A OE2 
1797 N  N   A PRO A 214 ? 0.1098 0.1010 0.1203 -0.0008 0.0008  0.0031  215 PRO A N   
1798 N  N   B PRO A 214 ? 0.1163 0.0929 0.1273 -0.0076 -0.0076 0.0164  215 PRO A N   
1799 C  CA  A PRO A 214 ? 0.1251 0.1084 0.1162 0.0040  -0.0041 0.0026  215 PRO A CA  
1800 C  CA  B PRO A 214 ? 0.1191 0.1194 0.1175 -0.0010 -0.0089 0.0120  215 PRO A CA  
1801 C  C   A PRO A 214 ? 0.1078 0.0929 0.1335 -0.0034 -0.0093 -0.0189 215 PRO A C   
1802 C  C   B PRO A 214 ? 0.1137 0.1071 0.1439 -0.0187 -0.0219 -0.0023 215 PRO A C   
1803 O  O   A PRO A 214 ? 0.1089 0.1456 0.1379 -0.0135 -0.0162 -0.0071 215 PRO A O   
1804 O  O   B PRO A 214 ? 0.1114 0.1146 0.1261 -0.0115 -0.0162 -0.0026 215 PRO A O   
1805 C  CB  A PRO A 214 ? 0.1111 0.1000 0.1481 -0.0010 -0.0032 0.0010  215 PRO A CB  
1806 C  CB  B PRO A 214 ? 0.1120 0.0970 0.1678 -0.0087 -0.0194 -0.0001 215 PRO A CB  
1807 C  CG  A PRO A 214 ? 0.1363 0.1284 0.1429 -0.0164 -0.0049 0.0148  215 PRO A CG  
1808 C  CG  B PRO A 214 ? 0.1483 0.1380 0.1605 0.0181  0.0087  0.0015  215 PRO A CG  
1809 C  CD  A PRO A 214 ? 0.1152 0.1093 0.1348 -0.0060 -0.0197 0.0131  215 PRO A CD  
1810 C  CD  B PRO A 214 ? 0.1178 0.0909 0.1466 -0.0074 0.0110  0.0186  215 PRO A CD  
1811 N  N   . ILE A 215 ? 0.1194 0.1114 0.1146 -0.0087 -0.0104 -0.0038 216 ILE A N   
1812 C  CA  . ILE A 215 ? 0.1154 0.1055 0.1194 -0.0041 -0.0162 -0.0129 216 ILE A CA  
1813 C  C   . ILE A 215 ? 0.1128 0.1045 0.1303 -0.0070 -0.0186 -0.0081 216 ILE A C   
1814 O  O   . ILE A 215 ? 0.1308 0.1118 0.1623 -0.0074 -0.0151 -0.0200 216 ILE A O   
1815 C  CB  . ILE A 215 ? 0.1193 0.1150 0.1274 0.0085  -0.0259 -0.0133 216 ILE A CB  
1816 C  CG1 . ILE A 215 ? 0.1389 0.1178 0.1366 0.0023  -0.0208 0.0085  216 ILE A CG1 
1817 C  CG2 . ILE A 215 ? 0.1430 0.1230 0.1425 0.0054  -0.0292 -0.0225 216 ILE A CG2 
1818 C  CD1 . ILE A 215 ? 0.1771 0.1340 0.1570 0.0137  -0.0115 0.0176  216 ILE A CD1 
1819 N  N   A SER A 216 ? 0.1005 0.1120 0.1284 -0.0136 -0.0043 -0.0081 217 SER A N   
1820 N  N   B SER A 216 ? 0.1255 0.1255 0.1340 -0.0097 -0.0218 -0.0160 217 SER A N   
1821 C  CA  A SER A 216 ? 0.1098 0.1075 0.1418 -0.0157 -0.0353 -0.0130 217 SER A CA  
1822 C  CA  B SER A 216 ? 0.1650 0.1123 0.1289 -0.0105 -0.0131 -0.0199 217 SER A CA  
1823 C  C   A SER A 216 ? 0.1430 0.1071 0.1386 -0.0032 -0.0255 -0.0172 217 SER A C   
1824 C  C   B SER A 216 ? 0.1536 0.0957 0.1377 0.0000  -0.0273 -0.0006 217 SER A C   
1825 O  O   A SER A 216 ? 0.1537 0.1312 0.1305 -0.0161 -0.0260 0.0078  217 SER A O   
1826 O  O   B SER A 216 ? 0.1198 0.1348 0.1308 0.0010  -0.0041 0.0077  217 SER A O   
1827 C  CB  A SER A 216 ? 0.1430 0.1067 0.1675 -0.0057 -0.0005 0.0041  217 SER A CB  
1828 C  CB  B SER A 216 ? 0.1726 0.1532 0.1723 -0.0176 -0.0165 -0.0340 217 SER A CB  
1829 O  OG  A SER A 216 ? 0.2149 0.1941 0.1494 -0.0476 0.0230  -0.0104 217 SER A OG  
1830 O  OG  B SER A 216 ? 0.1667 0.1709 0.2461 -0.0406 -0.0240 -0.0060 217 SER A OG  
1831 N  N   . VAL A 217 ? 0.1409 0.1068 0.1413 -0.0126 -0.0231 -0.0122 218 VAL A N   
1832 C  CA  . VAL A 217 ? 0.1544 0.0988 0.1405 -0.0121 -0.0256 -0.0081 218 VAL A CA  
1833 C  C   . VAL A 217 ? 0.1445 0.1040 0.1348 -0.0146 -0.0219 -0.0088 218 VAL A C   
1834 O  O   . VAL A 217 ? 0.1718 0.1036 0.1564 -0.0192 -0.0335 -0.0093 218 VAL A O   
1835 C  CB  . VAL A 217 ? 0.1404 0.1076 0.1747 -0.0212 -0.0326 -0.0096 218 VAL A CB  
1836 C  CG1 . VAL A 217 ? 0.1740 0.0979 0.1623 -0.0113 -0.0438 -0.0098 218 VAL A CG1 
1837 C  CG2 . VAL A 217 ? 0.1749 0.1314 0.2064 -0.0248 -0.0445 -0.0137 218 VAL A CG2 
1838 N  N   . SER A 218 ? 0.1635 0.1036 0.1427 -0.0225 -0.0241 -0.0187 219 SER A N   
1839 C  CA  . SER A 218 ? 0.1844 0.0873 0.1695 -0.0195 -0.0228 -0.0161 219 SER A CA  
1840 C  C   . SER A 218 ? 0.1807 0.0888 0.1544 -0.0195 -0.0109 -0.0063 219 SER A C   
1841 O  O   . SER A 218 ? 0.1806 0.1002 0.1507 -0.0115 -0.0227 -0.0052 219 SER A O   
1842 C  CB  . SER A 218 ? 0.2046 0.1220 0.1460 -0.0346 -0.0237 -0.0177 219 SER A CB  
1843 O  OG  . SER A 218 ? 0.1966 0.1363 0.1608 -0.0307 -0.0220 -0.0027 219 SER A OG  
1844 N  N   A SER A 219 ? 0.1750 0.0886 0.1667 -0.0130 -0.0060 -0.0007 220 SER A N   
1845 N  N   B SER A 219 ? 0.1916 0.0943 0.1741 -0.0082 -0.0034 0.0015  220 SER A N   
1846 C  CA  A SER A 219 ? 0.1700 0.0899 0.1975 -0.0223 -0.0103 0.0104  220 SER A CA  
1847 C  CA  B SER A 219 ? 0.1990 0.0966 0.2171 -0.0215 -0.0049 0.0020  220 SER A CA  
1848 C  C   A SER A 219 ? 0.1831 0.0993 0.1986 -0.0162 0.0034  -0.0001 220 SER A C   
1849 C  C   B SER A 219 ? 0.1879 0.1014 0.2180 0.0049  -0.0035 0.0019  220 SER A C   
1850 O  O   A SER A 219 ? 0.1711 0.1193 0.1504 -0.0104 0.0115  -0.0077 220 SER A O   
1851 O  O   B SER A 219 ? 0.2070 0.1182 0.1932 -0.0155 0.0193  0.0055  220 SER A O   
1852 C  CB  A SER A 219 ? 0.1974 0.1032 0.1896 0.0051  -0.0196 0.0196  220 SER A CB  
1853 C  CB  B SER A 219 ? 0.2078 0.1190 0.1965 -0.0405 -0.0188 -0.0008 220 SER A CB  
1854 O  OG  A SER A 219 ? 0.2075 0.0854 0.1723 -0.0027 -0.0049 -0.0127 220 SER A OG  
1855 O  OG  B SER A 219 ? 0.2382 0.1523 0.2497 -0.0322 0.0126  0.0035  220 SER A OG  
1856 N  N   . GLU A 220 ? 0.1921 0.1076 0.1864 -0.0130 0.0015  -0.0052 221 GLU A N   
1857 C  CA  . GLU A 220 ? 0.2225 0.1325 0.1865 -0.0200 0.0006  -0.0210 221 GLU A CA  
1858 C  C   . GLU A 220 ? 0.1999 0.1137 0.1607 -0.0063 0.0024  0.0062  221 GLU A C   
1859 O  O   . GLU A 220 ? 0.2328 0.1474 0.1649 -0.0031 0.0207  -0.0068 221 GLU A O   
1860 C  CB  . GLU A 220 ? 0.2640 0.1747 0.1783 -0.0342 -0.0194 -0.0355 221 GLU A CB  
1861 C  CG  . GLU A 220 ? 0.3240 0.2248 0.2119 -0.0305 -0.0538 -0.0890 221 GLU A CG  
1862 C  CD  . GLU A 220 ? 0.4255 0.2056 0.2980 -0.0663 0.0247  -0.0732 221 GLU A CD  
1863 O  OE1 . GLU A 220 ? 0.3055 0.1831 0.2754 -0.0597 0.0043  -0.0251 221 GLU A OE1 
1864 O  OE2 . GLU A 220 ? 1.1294 0.2118 0.9592 -0.2816 -0.0993 -0.1482 221 GLU A OE2 
1865 N  N   . GLN A 221 ? 0.1852 0.1062 0.1682 -0.0065 -0.0115 -0.0168 222 GLN A N   
1866 C  CA  . GLN A 221 ? 0.1837 0.0997 0.1421 -0.0197 -0.0097 -0.0026 222 GLN A CA  
1867 C  C   . GLN A 221 ? 0.1835 0.1115 0.1545 -0.0120 -0.0003 0.0086  222 GLN A C   
1868 O  O   . GLN A 221 ? 0.1819 0.1384 0.1479 -0.0214 -0.0054 0.0126  222 GLN A O   
1869 C  CB  . GLN A 221 ? 0.1661 0.1171 0.1316 -0.0098 -0.0137 -0.0104 222 GLN A CB  
1870 C  CG  . GLN A 221 ? 0.1785 0.1173 0.1386 -0.0217 -0.0238 -0.0046 222 GLN A CG  
1871 C  CD  . GLN A 221 ? 0.1624 0.1112 0.1328 -0.0243 -0.0274 -0.0085 222 GLN A CD  
1872 O  OE1 . GLN A 221 ? 0.1641 0.1206 0.1430 -0.0176 -0.0183 -0.0071 222 GLN A OE1 
1873 N  NE2 . GLN A 221 ? 0.1618 0.1177 0.1607 -0.0082 -0.0335 -0.0038 222 GLN A NE2 
1874 N  N   A VAL A 222 ? 0.1900 0.1162 0.1448 -0.0175 -0.0229 0.0155  223 VAL A N   
1875 N  N   B VAL A 222 ? 0.2040 0.1186 0.1500 -0.0173 -0.0236 0.0194  223 VAL A N   
1876 C  CA  A VAL A 222 ? 0.1632 0.1254 0.1354 -0.0214 -0.0175 0.0298  223 VAL A CA  
1877 C  CA  B VAL A 222 ? 0.1814 0.1574 0.1608 -0.0251 -0.0195 0.0177  223 VAL A CA  
1878 C  C   A VAL A 222 ? 0.1884 0.1327 0.1439 -0.0126 0.0144  0.0239  223 VAL A C   
1879 C  C   B VAL A 222 ? 0.2104 0.1433 0.1608 -0.0176 0.0153  0.0122  223 VAL A C   
1880 O  O   A VAL A 222 ? 0.1683 0.1391 0.1696 -0.0230 0.0017  0.0208  223 VAL A O   
1881 O  O   B VAL A 222 ? 0.1833 0.1489 0.1872 -0.0258 0.0017  0.0222  223 VAL A O   
1882 C  CB  A VAL A 222 ? 0.1597 0.1587 0.1421 -0.0217 -0.0173 0.0416  223 VAL A CB  
1883 C  CB  B VAL A 222 ? 0.2610 0.2337 0.1611 0.0205  0.0254  0.0379  223 VAL A CB  
1884 C  CG1 A VAL A 222 ? 0.1345 0.1486 0.1648 -0.0342 -0.0253 0.0425  223 VAL A CG1 
1885 C  CG1 B VAL A 222 ? 0.3125 0.3409 0.2567 0.0085  -0.0671 0.0772  223 VAL A CG1 
1886 C  CG2 A VAL A 222 ? 0.1738 0.1753 0.1592 -0.0175 -0.0344 -0.0006 223 VAL A CG2 
1887 C  CG2 B VAL A 222 ? 0.2238 0.2673 0.1735 -0.0172 -0.0005 0.0226  223 VAL A CG2 
1888 N  N   . LEU A 223 ? 0.1997 0.1386 0.1855 -0.0201 0.0035  0.0076  224 LEU A N   
1889 C  CA  . LEU A 223 ? 0.2246 0.1404 0.2199 -0.0205 0.0263  -0.0076 224 LEU A CA  
1890 C  C   . LEU A 223 ? 0.2038 0.1623 0.1885 -0.0216 0.0097  -0.0143 224 LEU A C   
1891 O  O   . LEU A 223 ? 0.2123 0.1685 0.2194 -0.0229 0.0188  -0.0041 224 LEU A O   
1892 C  CB  . LEU A 223 ? 0.2596 0.1483 0.2732 -0.0439 0.0465  -0.0110 224 LEU A CB  
1893 C  CG  . LEU A 223 ? 0.3567 0.1992 0.2969 -0.0131 0.0342  -0.0289 224 LEU A CG  
1894 C  CD1 . LEU A 223 ? 0.3935 0.2284 0.4232 -0.0733 -0.0062 -0.0254 224 LEU A CD1 
1895 C  CD2 . LEU A 223 ? 0.3388 0.2222 0.4465 0.0076  0.0288  -0.0927 224 LEU A CD2 
1896 N  N   . LYS A 224 ? 0.1861 0.1587 0.1538 -0.0187 0.0000  -0.0131 225 LYS A N   
1897 C  CA  . LYS A 224 ? 0.1887 0.1617 0.1599 -0.0144 0.0261  -0.0063 225 LYS A CA  
1898 C  C   . LYS A 224 ? 0.1869 0.1483 0.1191 -0.0165 0.0066  0.0140  225 LYS A C   
1899 O  O   . LYS A 224 ? 0.2055 0.1578 0.1339 -0.0186 0.0132  -0.0078 225 LYS A O   
1900 C  CB  . LYS A 224 ? 0.1908 0.2216 0.1923 -0.0046 -0.0073 0.0034  225 LYS A CB  
1901 C  CG  . LYS A 224 ? 0.2408 0.2664 0.2436 -0.0533 -0.0275 -0.0049 225 LYS A CG  
1902 C  CD  . LYS A 224 ? 0.3167 0.2754 0.3120 -0.0165 -0.0322 -0.0803 225 LYS A CD  
1903 C  CE  . LYS A 224 ? 0.4160 0.2928 0.2964 -0.0362 -0.0024 -0.1177 225 LYS A CE  
1904 N  NZ  . LYS A 224 ? 0.4268 0.3147 0.3903 0.0035  0.0373  -0.0401 225 LYS A NZ  
1905 N  N   . PHE A 225 ? 0.1888 0.1265 0.1289 0.0015  0.0096  0.0032  226 PHE A N   
1906 C  CA  . PHE A 225 ? 0.1894 0.1216 0.1212 -0.0094 0.0133  0.0034  226 PHE A CA  
1907 C  C   . PHE A 225 ? 0.1791 0.1360 0.1123 -0.0108 0.0099  -0.0044 226 PHE A C   
1908 O  O   . PHE A 225 ? 0.1930 0.1400 0.1160 -0.0183 0.0204  -0.0109 226 PHE A O   
1909 C  CB  . PHE A 225 ? 0.1912 0.1348 0.1289 -0.0052 0.0331  0.0054  226 PHE A CB  
1910 C  CG  . PHE A 225 ? 0.1699 0.1076 0.1473 -0.0299 0.0151  -0.0270 226 PHE A CG  
1911 C  CD1 . PHE A 225 ? 0.2069 0.1854 0.1791 0.0253  0.0263  0.0111  226 PHE A CD1 
1912 C  CD2 . PHE A 225 ? 0.2037 0.2180 0.1878 -0.0200 0.0248  -0.0646 226 PHE A CD2 
1913 C  CE1 . PHE A 225 ? 0.2307 0.1644 0.1856 0.0344  0.0353  0.0104  226 PHE A CE1 
1914 C  CE2 . PHE A 225 ? 0.1736 0.2340 0.1865 -0.0217 0.0017  -0.0839 226 PHE A CE2 
1915 C  CZ  . PHE A 225 ? 0.1843 0.1644 0.2085 -0.0121 0.0046  -0.0697 226 PHE A CZ  
1916 N  N   . ARG A 226 ? 0.1828 0.1266 0.1143 0.0037  0.0183  -0.0059 227 ARG A N   
1917 C  CA  . ARG A 226 ? 0.1905 0.1474 0.1243 -0.0133 0.0172  -0.0071 227 ARG A CA  
1918 C  C   . ARG A 226 ? 0.1903 0.1404 0.1620 -0.0181 0.0266  -0.0027 227 ARG A C   
1919 O  O   . ARG A 226 ? 0.2084 0.1729 0.1557 0.0082  0.0247  -0.0153 227 ARG A O   
1920 C  CB  . ARG A 226 ? 0.1965 0.1344 0.1412 0.0120  0.0176  0.0007  227 ARG A CB  
1921 C  CG  . ARG A 226 ? 0.1859 0.1265 0.1358 0.0019  0.0160  0.0000  227 ARG A CG  
1922 C  CD  . ARG A 226 ? 0.2472 0.1416 0.1289 -0.0043 -0.0043 0.0041  227 ARG A CD  
1923 N  NE  . ARG A 226 ? 0.1964 0.1315 0.1446 -0.0282 -0.0164 -0.0121 227 ARG A NE  
1924 C  CZ  . ARG A 226 ? 0.1731 0.1379 0.1415 -0.0236 -0.0173 -0.0263 227 ARG A CZ  
1925 N  NH1 . ARG A 226 ? 0.2619 0.1835 0.2199 -0.0504 -0.0355 -0.0671 227 ARG A NH1 
1926 N  NH2 . ARG A 226 ? 0.2002 0.1456 0.1519 -0.0472 0.0044  -0.0170 227 ARG A NH2 
1927 N  N   . LYS A 227 ? 0.1844 0.1460 0.1261 -0.0089 0.0241  -0.0211 228 LYS A N   
1928 C  CA  . LYS A 227 ? 0.2206 0.1613 0.1150 -0.0322 0.0397  -0.0293 228 LYS A CA  
1929 C  C   . LYS A 227 ? 0.2043 0.1559 0.1084 -0.0179 0.0182  -0.0197 228 LYS A C   
1930 O  O   . LYS A 227 ? 0.2400 0.1788 0.1139 -0.0355 0.0299  -0.0262 228 LYS A O   
1931 C  CB  . LYS A 227 ? 0.2333 0.2036 0.1450 -0.0494 0.0176  -0.0419 228 LYS A CB  
1932 C  CG  . LYS A 227 ? 0.2985 0.1975 0.1887 -0.0732 -0.0031 -0.0379 228 LYS A CG  
1933 C  CD  . LYS A 227 ? 0.3377 0.2896 0.2479 -0.1120 0.0070  -0.0815 228 LYS A CD  
1934 C  CE  . LYS A 227 ? 0.3492 0.5898 0.2903 -0.0491 0.0394  -0.0725 228 LYS A CE  
1935 N  NZ  . LYS A 227 ? 1.5231 1.1633 1.0371 0.2991  -0.7706 -0.4584 228 LYS A NZ  
1936 N  N   . LEU A 228 ? 0.1852 0.1335 0.1224 -0.0267 0.0164  -0.0151 229 LEU A N   
1937 C  CA  . LEU A 228 ? 0.1820 0.1508 0.1058 -0.0105 0.0076  -0.0252 229 LEU A CA  
1938 C  C   . LEU A 228 ? 0.2081 0.1326 0.1002 -0.0087 0.0251  -0.0041 229 LEU A C   
1939 O  O   . LEU A 228 ? 0.1865 0.1550 0.1157 -0.0026 0.0307  -0.0182 229 LEU A O   
1940 C  CB  . LEU A 228 ? 0.2025 0.1495 0.0960 -0.0113 0.0208  -0.0087 229 LEU A CB  
1941 C  CG  . LEU A 228 ? 0.1965 0.1614 0.1145 -0.0062 0.0105  -0.0100 229 LEU A CG  
1942 C  CD1 . LEU A 228 ? 0.2027 0.1684 0.1333 -0.0200 0.0175  -0.0258 229 LEU A CD1 
1943 C  CD2 . LEU A 228 ? 0.2383 0.1828 0.1456 0.0111  0.0219  0.0322  229 LEU A CD2 
1944 N  N   . ASN A 229 ? 0.1943 0.1460 0.1194 -0.0230 0.0190  -0.0135 230 ASN A N   
1945 C  CA  . ASN A 229 ? 0.1933 0.1600 0.0949 -0.0035 0.0196  -0.0137 230 ASN A CA  
1946 C  C   . ASN A 229 ? 0.1581 0.1644 0.1234 0.0295  0.0281  0.0109  230 ASN A C   
1947 O  O   . ASN A 229 ? 0.1815 0.1526 0.1321 -0.0017 0.0188  0.0007  230 ASN A O   
1948 C  CB  . ASN A 229 ? 0.2052 0.1676 0.1208 -0.0104 0.0250  -0.0111 230 ASN A CB  
1949 C  CG  . ASN A 229 ? 0.2284 0.1775 0.1239 0.0041  0.0218  -0.0173 230 ASN A CG  
1950 O  OD1 . ASN A 229 ? 0.2888 0.2197 0.1186 0.0001  0.0529  -0.0161 230 ASN A OD1 
1951 N  ND2 . ASN A 229 ? 0.2284 0.1729 0.1370 -0.0137 0.0320  -0.0285 230 ASN A ND2 
1952 N  N   . PHE A 230 ? 0.1720 0.1495 0.1313 -0.0167 0.0320  -0.0027 231 PHE A N   
1953 C  CA  . PHE A 230 ? 0.1708 0.1546 0.1293 -0.0094 0.0171  0.0099  231 PHE A CA  
1954 C  C   . PHE A 230 ? 0.2016 0.1582 0.1465 -0.0239 0.0203  -0.0010 231 PHE A C   
1955 O  O   . PHE A 230 ? 0.2023 0.1821 0.1442 -0.0443 0.0351  -0.0012 231 PHE A O   
1956 C  CB  . PHE A 230 ? 0.1835 0.1823 0.1328 -0.0182 0.0293  0.0020  231 PHE A CB  
1957 C  CG  . PHE A 230 ? 0.1694 0.1485 0.1215 -0.0115 0.0177  -0.0026 231 PHE A CG  
1958 C  CD1 . PHE A 230 ? 0.1750 0.1577 0.1105 -0.0015 0.0125  -0.0184 231 PHE A CD1 
1959 C  CD2 . PHE A 230 ? 0.1806 0.1733 0.1150 0.0238  0.0038  -0.0138 231 PHE A CD2 
1960 C  CE1 . PHE A 230 ? 0.1897 0.1430 0.1186 -0.0175 0.0302  -0.0021 231 PHE A CE1 
1961 C  CE2 . PHE A 230 ? 0.1763 0.1641 0.1263 0.0114  0.0028  -0.0019 231 PHE A CE2 
1962 C  CZ  . PHE A 230 ? 0.1366 0.1676 0.1101 -0.0103 0.0076  -0.0073 231 PHE A CZ  
1963 N  N   . ASN A 231 ? 0.1878 0.1859 0.1269 -0.0114 0.0375  0.0111  232 ASN A N   
1964 C  CA  . ASN A 231 ? 0.1966 0.2012 0.1474 -0.0035 0.0277  0.0048  232 ASN A CA  
1965 C  C   . ASN A 231 ? 0.1665 0.1992 0.1151 0.0306  0.0364  0.0127  232 ASN A C   
1966 O  O   . ASN A 231 ? 0.2196 0.2088 0.1421 0.0293  0.0353  -0.0003 232 ASN A O   
1967 C  CB  . ASN A 231 ? 0.2087 0.2186 0.1792 -0.0068 0.0891  -0.0071 232 ASN A CB  
1968 C  CG  . ASN A 231 ? 0.2123 0.2005 0.1546 0.0178  0.0313  0.0219  232 ASN A CG  
1969 O  OD1 . ASN A 231 ? 0.2249 0.1932 0.1774 0.0082  0.0553  -0.0071 232 ASN A OD1 
1970 N  ND2 . ASN A 231 ? 0.2382 0.2344 0.1591 0.0524  0.0403  0.0001  232 ASN A ND2 
1971 N  N   . GLY A 232 ? 0.2195 0.2058 0.1853 0.0059  0.0498  0.0331  233 GLY A N   
1972 C  CA  . GLY A 232 ? 0.2310 0.2026 0.1451 0.0057  0.0395  0.0189  233 GLY A CA  
1973 C  C   . GLY A 232 ? 0.1744 0.1895 0.1888 0.0511  0.0093  0.0340  233 GLY A C   
1974 O  O   . GLY A 232 ? 0.2248 0.2411 0.1546 0.0434  0.0590  0.0406  233 GLY A O   
1975 N  N   . GLU A 233 ? 0.2021 0.1975 0.1658 0.0251  0.0450  0.0153  234 GLU A N   
1976 C  CA  . GLU A 233 ? 0.2104 0.2252 0.1479 0.0344  0.0527  0.0099  234 GLU A CA  
1977 C  C   . GLU A 233 ? 0.2307 0.2081 0.1504 0.0337  0.0218  0.0089  234 GLU A C   
1978 O  O   . GLU A 233 ? 0.2583 0.2606 0.1758 0.0205  0.0564  0.0299  234 GLU A O   
1979 C  CB  . GLU A 233 ? 0.2140 0.2251 0.1513 0.0131  -0.0091 0.0283  234 GLU A CB  
1980 C  CG  . GLU A 233 ? 0.2608 0.2876 0.1826 -0.0351 0.0405  0.0507  234 GLU A CG  
1981 C  CD  . GLU A 233 ? 0.3016 0.3763 0.2554 0.0516  0.0170  -0.0196 234 GLU A CD  
1982 O  OE1 . GLU A 233 ? 0.3772 0.3499 0.2671 0.0293  0.0430  0.1042  234 GLU A OE1 
1983 O  OE2 . GLU A 233 ? 0.3427 0.3689 0.2842 -0.0485 -0.0406 -0.0094 234 GLU A OE2 
1984 N  N   . GLY A 234 ? 0.3032 0.2687 0.1517 0.0658  0.0518  0.0161  235 GLY A N   
1985 C  CA  . GLY A 234 ? 0.3213 0.3355 0.1546 0.0899  0.0566  0.0209  235 GLY A CA  
1986 C  C   . GLY A 234 ? 0.3411 0.3610 0.1608 0.1327  0.0723  0.0766  235 GLY A C   
1987 O  O   . GLY A 234 ? 0.3619 0.5002 0.2427 0.1259  0.1429  0.0763  235 GLY A O   
1988 N  N   . GLU A 235 ? 0.2567 0.2538 0.2448 0.0820  0.0767  0.0648  236 GLU A N   
1989 C  CA  . GLU A 235 ? 0.2484 0.1928 0.2194 0.0816  0.0408  0.0260  236 GLU A CA  
1990 C  C   . GLU A 235 ? 0.2709 0.2434 0.1890 0.0401  0.0529  0.0586  236 GLU A C   
1991 O  O   . GLU A 235 ? 0.2619 0.2849 0.2242 0.0467  0.0671  0.0208  236 GLU A O   
1992 C  CB  . GLU A 235 ? 0.2788 0.2382 0.2269 0.0348  0.0800  0.0242  236 GLU A CB  
1993 C  CG  . GLU A 235 ? 0.2901 0.2387 0.2693 0.0098  0.0803  0.0692  236 GLU A CG  
1994 C  CD  . GLU A 235 ? 0.4832 0.3939 0.2644 -0.0722 0.1712  0.0156  236 GLU A CD  
1995 O  OE1 . GLU A 235 ? 0.2755 0.3522 0.2858 -0.0307 0.0706  0.0408  236 GLU A OE1 
1996 O  OE2 . GLU A 235 ? 0.5763 0.5335 0.6119 -0.1891 0.1512  0.1116  236 GLU A OE2 
1997 N  N   . PRO A 236 ? 0.2175 0.2511 0.2466 0.0653  0.0829  0.0790  237 PRO A N   
1998 C  CA  . PRO A 236 ? 0.2745 0.2490 0.2509 0.1108  0.1062  0.0778  237 PRO A CA  
1999 C  C   . PRO A 236 ? 0.2192 0.2149 0.1451 0.0148  0.0529  0.0063  237 PRO A C   
2000 O  O   . PRO A 236 ? 0.2426 0.2229 0.1967 0.0179  0.0537  -0.0010 237 PRO A O   
2001 C  CB  . PRO A 236 ? 0.2118 0.3280 0.3068 0.0597  0.1013  0.0692  237 PRO A CB  
2002 C  CG  . PRO A 236 ? 0.2705 0.2881 0.3673 0.0394  0.0670  0.1587  237 PRO A CG  
2003 C  CD  . PRO A 236 ? 0.2447 0.3064 0.2985 0.0604  0.0614  0.1262  237 PRO A CD  
2004 N  N   . GLU A 237 ? 0.2475 0.2245 0.1953 0.0270  0.0653  -0.0020 238 GLU A N   
2005 C  CA  . GLU A 237 ? 0.2269 0.2241 0.1728 0.0285  0.0494  -0.0185 238 GLU A CA  
2006 C  C   . GLU A 237 ? 0.1775 0.1862 0.1605 0.0113  0.0511  0.0049  238 GLU A C   
2007 O  O   . GLU A 237 ? 0.2140 0.2205 0.1606 0.0452  0.0296  -0.0231 238 GLU A O   
2008 C  CB  . GLU A 237 ? 0.2364 0.2330 0.2265 0.0175  -0.0142 -0.0715 238 GLU A CB  
2009 C  CG  . GLU A 237 ? 0.2434 0.2976 0.2574 0.0131  0.0472  -0.1084 238 GLU A CG  
2010 C  CD  . GLU A 237 ? 0.3016 0.2533 0.2459 -0.0013 0.0100  -0.1004 238 GLU A CD  
2011 O  OE1 . GLU A 237 ? 0.3731 0.2874 0.4295 -0.0023 0.0024  -0.1107 238 GLU A OE1 
2012 O  OE2 . GLU A 237 ? 0.2800 0.2299 0.2046 -0.0080 0.0223  -0.0511 238 GLU A OE2 
2013 N  N   . GLU A 238 ? 0.1863 0.1856 0.1455 -0.0120 0.0388  -0.0177 239 GLU A N   
2014 C  CA  . GLU A 238 ? 0.1718 0.2027 0.1377 -0.0071 0.0436  -0.0100 239 GLU A CA  
2015 C  C   . GLU A 238 ? 0.1709 0.1677 0.1166 0.0240  0.0353  -0.0043 239 GLU A C   
2016 O  O   . GLU A 238 ? 0.2102 0.1594 0.1824 0.0087  0.0434  -0.0076 239 GLU A O   
2017 C  CB  . GLU A 238 ? 0.2432 0.2843 0.1726 -0.0693 0.0278  -0.0092 239 GLU A CB  
2018 C  CG  . GLU A 238 ? 0.3240 0.3190 0.2861 0.0790  0.0177  0.0137  239 GLU A CG  
2019 C  CD  . GLU A 238 ? 0.3472 0.2804 0.2737 -0.0161 -0.0766 -0.0434 239 GLU A CD  
2020 O  OE1 . GLU A 238 ? 0.2824 0.7222 0.5745 0.1972  0.0482  -0.0986 239 GLU A OE1 
2021 O  OE2 . GLU A 238 ? 0.2913 0.2890 0.3826 0.0623  0.0395  -0.0006 239 GLU A OE2 
2022 N  N   . LEU A 239 ? 0.1912 0.1754 0.1386 0.0013  0.0417  -0.0250 240 LEU A N   
2023 C  CA  . LEU A 239 ? 0.1642 0.1611 0.1177 -0.0071 0.0344  -0.0175 240 LEU A CA  
2024 C  C   . LEU A 239 ? 0.1543 0.1449 0.1089 -0.0140 0.0170  0.0108  240 LEU A C   
2025 O  O   . LEU A 239 ? 0.1624 0.1659 0.1359 0.0008  0.0392  0.0000  240 LEU A O   
2026 C  CB  . LEU A 239 ? 0.1975 0.1457 0.1553 0.0087  0.0240  -0.0188 240 LEU A CB  
2027 C  CG  . LEU A 239 ? 0.1773 0.1509 0.1852 -0.0140 0.0265  -0.0386 240 LEU A CG  
2028 C  CD1 . LEU A 239 ? 0.2649 0.1348 0.2606 0.0122  0.0142  -0.0274 240 LEU A CD1 
2029 C  CD2 . LEU A 239 ? 0.2113 0.1913 0.1547 -0.0044 0.0249  -0.0379 240 LEU A CD2 
2030 N  N   . MET A 240 ? 0.1614 0.1404 0.1236 0.0120  0.0386  -0.0074 241 MET A N   
2031 C  CA  . MET A 240 ? 0.1686 0.1454 0.1067 -0.0010 0.0441  -0.0124 241 MET A CA  
2032 C  C   . MET A 240 ? 0.1507 0.1322 0.1023 -0.0085 0.0086  -0.0175 241 MET A C   
2033 O  O   . MET A 240 ? 0.1648 0.1459 0.1076 -0.0104 0.0154  -0.0074 241 MET A O   
2034 C  CB  . MET A 240 ? 0.1895 0.1310 0.1132 0.0046  0.0228  -0.0055 241 MET A CB  
2035 C  CG  . MET A 240 ? 0.1745 0.1546 0.1059 -0.0146 0.0307  -0.0225 241 MET A CG  
2036 S  SD  . MET A 240 ? 0.1862 0.1331 0.1290 -0.0098 0.0266  -0.0063 241 MET A SD  
2037 C  CE  . MET A 240 ? 0.1914 0.1448 0.1352 -0.0201 0.0403  0.0129  241 MET A CE  
2038 N  N   . VAL A 241 ? 0.1599 0.1281 0.1046 -0.0074 0.0306  -0.0137 242 VAL A N   
2039 C  CA  . VAL A 241 ? 0.1613 0.1178 0.1094 -0.0077 0.0167  -0.0074 242 VAL A CA  
2040 C  C   . VAL A 241 ? 0.1308 0.1154 0.1136 -0.0021 0.0183  -0.0182 242 VAL A C   
2041 O  O   . VAL A 241 ? 0.1386 0.1366 0.1110 -0.0060 0.0216  -0.0122 242 VAL A O   
2042 C  CB  . VAL A 241 ? 0.1556 0.1295 0.1263 -0.0068 0.0148  -0.0346 242 VAL A CB  
2043 C  CG1 . VAL A 241 ? 0.2056 0.1495 0.1297 -0.0241 0.0116  -0.0406 242 VAL A CG1 
2044 C  CG2 . VAL A 241 ? 0.2021 0.1264 0.1503 0.0071  0.0366  -0.0219 242 VAL A CG2 
2045 N  N   . ASP A 242 ? 0.1404 0.1049 0.0998 -0.0034 0.0132  -0.0171 243 ASP A N   
2046 C  CA  . ASP A 242 ? 0.1251 0.0975 0.1128 0.0052  0.0057  -0.0148 243 ASP A CA  
2047 C  C   . ASP A 242 ? 0.1150 0.1166 0.0964 -0.0062 0.0161  -0.0098 243 ASP A C   
2048 O  O   . ASP A 242 ? 0.1260 0.1143 0.1430 -0.0068 0.0074  -0.0108 243 ASP A O   
2049 C  CB  . ASP A 242 ? 0.1291 0.1119 0.1190 -0.0019 0.0065  -0.0082 243 ASP A CB  
2050 C  CG  . ASP A 242 ? 0.1339 0.1116 0.1178 0.0041  0.0085  -0.0231 243 ASP A CG  
2051 O  OD1 . ASP A 242 ? 0.1299 0.1058 0.1356 0.0068  0.0116  -0.0118 243 ASP A OD1 
2052 O  OD2 . ASP A 242 ? 0.1643 0.1229 0.1623 0.0065  0.0285  -0.0291 243 ASP A OD2 
2053 N  N   . ASN A 243 ? 0.1225 0.0957 0.0983 -0.0076 0.0220  -0.0148 244 ASN A N   
2054 C  CA  . ASN A 243 ? 0.1172 0.0962 0.0993 -0.0024 0.0198  -0.0087 244 ASN A CA  
2055 C  C   . ASN A 243 ? 0.1028 0.0936 0.0996 -0.0140 0.0070  -0.0032 244 ASN A C   
2056 O  O   . ASN A 243 ? 0.1406 0.1059 0.1004 0.0086  0.0166  0.0000  244 ASN A O   
2057 C  CB  . ASN A 243 ? 0.1191 0.1125 0.0989 -0.0159 0.0164  0.0098  244 ASN A CB  
2058 C  CG  . ASN A 243 ? 0.1162 0.1062 0.1137 -0.0206 0.0068  0.0085  244 ASN A CG  
2059 O  OD1 . ASN A 243 ? 0.1243 0.1103 0.1233 -0.0167 0.0109  0.0062  244 ASN A OD1 
2060 N  ND2 . ASN A 243 ? 0.1580 0.1851 0.2099 -0.0353 -0.0163 0.0929  244 ASN A ND2 
2061 N  N   . TRP A 244 ? 0.1018 0.0966 0.0952 -0.0048 0.0021  -0.0094 245 TRP A N   
2062 C  CA  . TRP A 244 ? 0.0908 0.1014 0.0931 0.0052  0.0073  -0.0065 245 TRP A CA  
2063 C  C   . TRP A 244 ? 0.1071 0.0900 0.0891 0.0007  0.0115  -0.0055 245 TRP A C   
2064 O  O   . TRP A 244 ? 0.1033 0.1171 0.1184 0.0126  0.0006  -0.0186 245 TRP A O   
2065 C  CB  . TRP A 244 ? 0.1116 0.0870 0.1040 -0.0062 0.0186  -0.0048 245 TRP A CB  
2066 C  CG  . TRP A 244 ? 0.0943 0.0926 0.1046 -0.0041 0.0184  -0.0060 245 TRP A CG  
2067 C  CD1 . TRP A 244 ? 0.1115 0.0983 0.1045 -0.0024 0.0181  -0.0131 245 TRP A CD1 
2068 C  CD2 . TRP A 244 ? 0.0958 0.1022 0.1041 -0.0015 0.0151  -0.0109 245 TRP A CD2 
2069 N  NE1 . TRP A 244 ? 0.1227 0.0943 0.1033 -0.0074 0.0185  -0.0057 245 TRP A NE1 
2070 C  CE2 . TRP A 244 ? 0.1036 0.0954 0.1157 -0.0010 0.0144  -0.0023 245 TRP A CE2 
2071 C  CE3 . TRP A 244 ? 0.1221 0.1103 0.0998 0.0015  0.0103  0.0026  245 TRP A CE3 
2072 C  CZ2 . TRP A 244 ? 0.1233 0.1085 0.1360 0.0102  0.0137  -0.0052 245 TRP A CZ2 
2073 C  CZ3 . TRP A 244 ? 0.1380 0.1245 0.1280 0.0157  0.0035  0.0017  245 TRP A CZ3 
2074 C  CH2 . TRP A 244 ? 0.1381 0.1133 0.1439 0.0110  0.0041  0.0044  245 TRP A CH2 
2075 N  N   . ARG A 245 ? 0.0989 0.1014 0.0974 -0.0017 0.0131  -0.0165 246 ARG A N   
2076 C  CA  . ARG A 245 ? 0.0951 0.1033 0.1018 -0.0020 0.0074  -0.0094 246 ARG A CA  
2077 C  C   . ARG A 245 ? 0.0887 0.1023 0.1024 0.0038  0.0038  -0.0172 246 ARG A C   
2078 O  O   . ARG A 245 ? 0.1020 0.1076 0.1128 -0.0023 0.0083  -0.0126 246 ARG A O   
2079 C  CB  . ARG A 245 ? 0.0812 0.1148 0.1042 -0.0109 0.0006  -0.0170 246 ARG A CB  
2080 C  CG  . ARG A 245 ? 0.0979 0.1105 0.1178 0.0017  0.0028  -0.0149 246 ARG A CG  
2081 C  CD  . ARG A 245 ? 0.0812 0.1083 0.1259 -0.0140 0.0098  -0.0172 246 ARG A CD  
2082 N  NE  . ARG A 245 ? 0.0847 0.1191 0.1242 -0.0097 0.0041  -0.0178 246 ARG A NE  
2083 C  CZ  . ARG A 245 ? 0.0922 0.1169 0.1020 -0.0144 0.0073  -0.0100 246 ARG A CZ  
2084 N  NH1 . ARG A 245 ? 0.1023 0.1120 0.1206 -0.0178 0.0126  -0.0164 246 ARG A NH1 
2085 N  NH2 . ARG A 245 ? 0.0997 0.1559 0.1377 -0.0234 0.0007  -0.0230 246 ARG A NH2 
2086 N  N   . PRO A 246 ? 0.1128 0.1019 0.1045 0.0013  0.0109  -0.0038 247 PRO A N   
2087 C  CA  . PRO A 246 ? 0.1184 0.1172 0.1030 0.0177  0.0019  -0.0120 247 PRO A CA  
2088 C  C   . PRO A 246 ? 0.1130 0.1027 0.1045 0.0121  -0.0035 -0.0006 247 PRO A C   
2089 O  O   . PRO A 246 ? 0.1098 0.1103 0.1145 0.0086  -0.0027 -0.0065 247 PRO A O   
2090 C  CB  . PRO A 246 ? 0.1541 0.1358 0.1567 0.0386  0.0164  -0.0013 247 PRO A CB  
2091 C  CG  . PRO A 246 ? 0.1688 0.1833 0.2214 0.0533  0.0471  0.0482  247 PRO A CG  
2092 C  CD  . PRO A 246 ? 0.1125 0.1515 0.1440 0.0273  0.0091  0.0142  247 PRO A CD  
2093 N  N   . ALA A 247 ? 0.1225 0.1159 0.1085 0.0094  0.0107  0.0003  248 ALA A N   
2094 C  CA  . ALA A 247 ? 0.1063 0.1195 0.0976 0.0035  -0.0008 -0.0031 248 ALA A CA  
2095 C  C   . ALA A 247 ? 0.1102 0.1115 0.1094 0.0160  -0.0094 0.0159  248 ALA A C   
2096 O  O   . ALA A 247 ? 0.1231 0.1361 0.1325 0.0375  -0.0118 -0.0013 248 ALA A O   
2097 C  CB  . ALA A 247 ? 0.1653 0.1458 0.1213 -0.0027 0.0178  0.0126  248 ALA A CB  
2098 N  N   . GLN A 248 ? 0.1121 0.1124 0.1071 0.0062  -0.0086 0.0010  249 GLN A N   
2099 C  CA  . GLN A 248 ? 0.1053 0.1335 0.1169 0.0122  -0.0076 0.0013  249 GLN A CA  
2100 C  C   . GLN A 248 ? 0.1195 0.1236 0.1187 0.0144  -0.0234 0.0164  249 GLN A C   
2101 O  O   . GLN A 248 ? 0.1472 0.1407 0.1234 0.0109  -0.0006 0.0144  249 GLN A O   
2102 C  CB  . GLN A 248 ? 0.1283 0.1218 0.1366 0.0046  -0.0172 0.0060  249 GLN A CB  
2103 C  CG  . GLN A 248 ? 0.1477 0.1231 0.1307 -0.0104 -0.0046 0.0076  249 GLN A CG  
2104 C  CD  . GLN A 248 ? 0.1054 0.1574 0.1632 -0.0186 -0.0027 -0.0020 249 GLN A CD  
2105 O  OE1 . GLN A 248 ? 0.1252 0.2259 0.1670 -0.0329 0.0096  -0.0272 249 GLN A OE1 
2106 N  NE2 . GLN A 248 ? 0.1506 0.1685 0.1428 -0.0049 -0.0068 0.0013  249 GLN A NE2 
2107 N  N   . PRO A 249 ? 0.1300 0.1642 0.1342 0.0364  -0.0136 -0.0131 250 PRO A N   
2108 C  CA  . PRO A 249 ? 0.1603 0.1888 0.1298 0.0610  -0.0160 -0.0097 250 PRO A CA  
2109 C  C   . PRO A 249 ? 0.1485 0.1353 0.1115 0.0161  -0.0194 0.0024  250 PRO A C   
2110 O  O   . PRO A 249 ? 0.1348 0.1641 0.1274 0.0296  -0.0137 0.0066  250 PRO A O   
2111 C  CB  . PRO A 249 ? 0.1529 0.2858 0.1938 0.0810  -0.0549 -0.0684 250 PRO A CB  
2112 C  CG  . PRO A 249 ? 0.1572 0.2878 0.2008 0.0392  -0.0586 -0.0417 250 PRO A CG  
2113 C  CD  . PRO A 249 ? 0.1194 0.2257 0.1800 0.0362  -0.0527 -0.0188 250 PRO A CD  
2114 N  N   . LEU A 250 ? 0.1685 0.1547 0.1204 0.0421  -0.0234 0.0136  251 LEU A N   
2115 C  CA  . LEU A 250 ? 0.1439 0.1462 0.1229 0.0120  -0.0028 -0.0008 251 LEU A CA  
2116 C  C   . LEU A 250 ? 0.1476 0.1465 0.1255 0.0229  -0.0229 0.0120  251 LEU A C   
2117 O  O   . LEU A 250 ? 0.1493 0.1502 0.1268 0.0208  -0.0129 -0.0021 251 LEU A O   
2118 C  CB  . LEU A 250 ? 0.1993 0.1664 0.1344 0.0140  0.0065  0.0006  251 LEU A CB  
2119 C  CG  . LEU A 250 ? 0.2026 0.1863 0.1243 -0.0081 0.0335  -0.0088 251 LEU A CG  
2120 C  CD1 . LEU A 250 ? 0.1664 0.1990 0.1639 0.0057  -0.0023 -0.0179 251 LEU A CD1 
2121 C  CD2 . LEU A 250 ? 0.2741 0.1923 0.2065 -0.0258 0.0553  -0.0038 251 LEU A CD2 
2122 N  N   A LYS A 251 ? 0.1783 0.1807 0.0926 0.0531  -0.0133 0.0148  252 LYS A N   
2123 N  N   B LYS A 251 ? 0.1324 0.1565 0.1160 0.0060  -0.0162 0.0035  252 LYS A N   
2124 C  CA  A LYS A 251 ? 0.1715 0.2030 0.1562 0.0283  -0.0228 -0.0076 252 LYS A CA  
2125 C  CA  B LYS A 251 ? 0.1227 0.1588 0.1204 0.0198  -0.0266 0.0115  252 LYS A CA  
2126 C  C   A LYS A 251 ? 0.1639 0.1673 0.1488 0.0215  -0.0450 0.0057  252 LYS A C   
2127 C  C   B LYS A 251 ? 0.1736 0.2124 0.1547 0.0335  -0.0116 -0.0300 252 LYS A C   
2128 O  O   A LYS A 251 ? 0.2187 0.1972 0.1323 0.0350  -0.0295 -0.0293 252 LYS A O   
2129 O  O   B LYS A 251 ? 0.2412 0.2335 0.1627 0.0010  -0.0044 -0.0430 252 LYS A O   
2130 C  CB  A LYS A 251 ? 0.1506 0.1888 0.1641 -0.0046 -0.0702 -0.0364 252 LYS A CB  
2131 C  CB  B LYS A 251 ? 0.1784 0.1820 0.1588 -0.0074 0.0175  0.0077  252 LYS A CB  
2132 C  CG  A LYS A 251 ? 0.2280 0.1893 0.2211 0.0293  0.0074  -0.0068 252 LYS A CG  
2133 C  CG  B LYS A 251 ? 0.1704 0.2011 0.1456 0.0057  -0.0040 0.0052  252 LYS A CG  
2134 C  CD  A LYS A 251 ? 0.2291 0.1942 0.1799 0.0161  -0.0192 -0.0520 252 LYS A CD  
2135 C  CD  B LYS A 251 ? 0.2220 0.1867 0.1947 -0.0285 0.0034  0.0156  252 LYS A CD  
2136 C  CE  A LYS A 251 ? 0.2136 0.4210 0.2074 0.0790  -0.0130 -0.0096 252 LYS A CE  
2137 C  CE  B LYS A 251 ? 0.1442 0.2610 0.3036 0.0592  0.0060  0.0922  252 LYS A CE  
2138 N  NZ  A LYS A 251 ? 0.3262 0.3704 0.2185 0.0988  0.0038  -0.0146 252 LYS A NZ  
2139 N  NZ  B LYS A 251 ? 0.1878 0.3294 0.2108 0.0153  -0.0074 0.0799  252 LYS A NZ  
2140 N  N   A ASN A 252 ? 0.1691 0.1588 0.1450 0.0465  0.0031  0.0172  253 ASN A N   
2141 N  N   B ASN A 252 ? 0.1385 0.1890 0.1508 0.0164  -0.0305 -0.0282 253 ASN A N   
2142 C  CA  A ASN A 252 ? 0.1929 0.2590 0.1026 0.0467  0.0097  0.0252  253 ASN A CA  
2143 C  CA  B ASN A 252 ? 0.1435 0.2935 0.1255 0.0480  -0.0568 -0.0656 253 ASN A CA  
2144 C  C   A ASN A 252 ? 0.2093 0.1882 0.1116 0.0131  0.0253  0.0108  253 ASN A C   
2145 C  C   B ASN A 252 ? 0.1428 0.1852 0.1491 0.0308  0.0005  -0.0296 253 ASN A C   
2146 O  O   A ASN A 252 ? 0.1908 0.2608 0.1022 0.0237  0.0027  0.0054  253 ASN A O   
2147 O  O   B ASN A 252 ? 0.1949 0.1828 0.1545 0.0579  0.0116  -0.0120 253 ASN A O   
2148 C  CB  A ASN A 252 ? 0.2273 0.2651 0.1333 0.0368  -0.0082 0.0082  253 ASN A CB  
2149 C  CB  B ASN A 252 ? 0.2134 0.2404 0.1820 0.0658  -0.0723 -0.0988 253 ASN A CB  
2150 C  CG  A ASN A 252 ? 0.2773 0.2459 0.1583 0.0125  -0.0120 0.0249  253 ASN A CG  
2151 C  CG  B ASN A 252 ? 0.2027 0.2764 0.2463 -0.0163 -0.0003 -0.1027 253 ASN A CG  
2152 O  OD1 A ASN A 252 ? 0.5546 0.2847 0.2245 0.0472  0.0692  0.0679  253 ASN A OD1 
2153 O  OD1 B ASN A 252 ? 0.4300 0.3537 0.2098 0.0208  0.0702  -0.0584 253 ASN A OD1 
2154 N  ND2 A ASN A 252 ? 0.2570 0.4230 0.2075 0.0251  -0.0469 -0.0604 253 ASN A ND2 
2155 N  ND2 B ASN A 252 ? 0.2383 0.2712 0.2136 0.0181  -0.0129 -0.0887 253 ASN A ND2 
2156 N  N   A ARG A 253 ? 0.1314 0.1284 0.0948 0.0019  0.0063  -0.0008 254 ARG A N   
2157 N  N   B ARG A 253 ? 0.1360 0.1315 0.1087 0.0197  0.0125  0.0001  254 ARG A N   
2158 C  CA  A ARG A 253 ? 0.1333 0.1262 0.1044 0.0015  -0.0049 -0.0192 254 ARG A CA  
2159 C  CA  B ARG A 253 ? 0.1424 0.1511 0.1242 0.0249  -0.0121 0.0080  254 ARG A CA  
2160 C  C   A ARG A 253 ? 0.1503 0.1438 0.1231 0.0085  0.0141  0.0102  254 ARG A C   
2161 C  C   B ARG A 253 ? 0.1551 0.1676 0.1085 0.0291  0.0008  -0.0280 254 ARG A C   
2162 O  O   A ARG A 253 ? 0.1758 0.1660 0.1915 -0.0218 0.0597  -0.0168 254 ARG A O   
2163 O  O   B ARG A 253 ? 0.1536 0.1967 0.1600 0.0175  -0.0153 0.0063  254 ARG A O   
2164 C  CB  A ARG A 253 ? 0.1229 0.1326 0.0958 -0.0104 -0.0046 0.0007  254 ARG A CB  
2165 C  CB  B ARG A 253 ? 0.1369 0.1277 0.1164 -0.0093 0.0170  -0.0193 254 ARG A CB  
2166 C  CG  A ARG A 253 ? 0.1154 0.1177 0.0983 -0.0109 0.0013  -0.0038 254 ARG A CG  
2167 C  CG  B ARG A 253 ? 0.1378 0.1512 0.1143 -0.0296 0.0043  -0.0166 254 ARG A CG  
2168 C  CD  A ARG A 253 ? 0.1363 0.1067 0.0957 0.0024  0.0238  -0.0049 254 ARG A CD  
2169 C  CD  B ARG A 253 ? 0.1046 0.1279 0.1004 -0.0121 -0.0130 -0.0065 254 ARG A CD  
2170 N  NE  A ARG A 253 ? 0.0790 0.1001 0.0944 -0.0070 -0.0081 -0.0013 254 ARG A NE  
2171 N  NE  B ARG A 253 ? 0.1171 0.1298 0.1018 0.0083  -0.0052 0.0092  254 ARG A NE  
2172 C  CZ  A ARG A 253 ? 0.0860 0.1046 0.0929 -0.0097 0.0077  0.0003  254 ARG A CZ  
2173 C  CZ  B ARG A 253 ? 0.0991 0.1202 0.0865 -0.0097 -0.0153 0.0013  254 ARG A CZ  
2174 N  NH1 A ARG A 253 ? 0.0930 0.1171 0.0824 0.0035  0.0015  -0.0059 254 ARG A NH1 
2175 N  NH1 B ARG A 253 ? 0.0903 0.1123 0.1101 0.0028  -0.0159 0.0097  254 ARG A NH1 
2176 N  NH2 A ARG A 253 ? 0.1181 0.1154 0.1080 0.0144  -0.0133 -0.0013 254 ARG A NH2 
2177 N  NH2 B ARG A 253 ? 0.1001 0.1234 0.0938 0.0104  -0.0154 0.0000  254 ARG A NH2 
2178 N  N   A GLN A 254 ? 0.1513 0.1996 0.1369 0.0126  0.0000  -0.0351 255 GLN A N   
2179 N  N   B GLN A 254 ? 0.1280 0.2187 0.1344 0.0008  -0.0040 -0.0544 255 GLN A N   
2180 C  CA  A GLN A 254 ? 0.1509 0.2741 0.1546 -0.0227 0.0006  -0.0318 255 GLN A CA  
2181 C  CA  B GLN A 254 ? 0.1694 0.2549 0.0908 -0.0037 0.0096  -0.0113 255 GLN A CA  
2182 C  C   A GLN A 254 ? 0.1456 0.1835 0.1557 0.0097  -0.0043 -0.0087 255 GLN A C   
2183 C  C   B GLN A 254 ? 0.1500 0.1902 0.1471 0.0030  -0.0131 -0.0093 255 GLN A C   
2184 O  O   A GLN A 254 ? 0.2422 0.1993 0.1981 -0.0135 -0.0046 0.0105  255 GLN A O   
2185 O  O   B GLN A 254 ? 0.2637 0.1777 0.2513 0.0068  -0.1159 -0.0496 255 GLN A O   
2186 C  CB  A GLN A 254 ? 0.1869 0.3510 0.1991 -0.0026 -0.0063 -0.0838 255 GLN A CB  
2187 C  CB  B GLN A 254 ? 0.2072 0.3330 0.1410 -0.0108 0.0491  -0.0147 255 GLN A CB  
2188 C  CG  A GLN A 254 ? 0.2639 0.3605 0.2951 -0.0533 0.0839  -0.1295 255 GLN A CG  
2189 C  CG  B GLN A 254 ? 0.3070 0.3790 0.1342 0.0107  0.0397  0.1247  255 GLN A CG  
2190 C  CD  A GLN A 254 ? 0.3779 0.5084 0.2989 -0.1235 -0.0159 -0.1809 255 GLN A CD  
2191 O  OE1 A GLN A 254 ? 0.6079 0.6255 0.2536 0.0121  0.0467  -0.1864 255 GLN A OE1 
2192 N  NE2 A GLN A 254 ? 0.5529 0.4972 0.4656 0.1435  0.2378  -0.0333 255 GLN A NE2 
2193 N  N   . ILE A 255 ? 0.1403 0.1626 0.1128 0.0108  0.0052  0.0027  256 ILE A N   
2194 C  CA  . ILE A 255 ? 0.1357 0.1490 0.1072 0.0063  0.0000  0.0031  256 ILE A CA  
2195 C  C   . ILE A 255 ? 0.1359 0.1394 0.0965 0.0057  0.0219  0.0118  256 ILE A C   
2196 O  O   . ILE A 255 ? 0.1598 0.1621 0.1254 0.0194  0.0303  0.0351  256 ILE A O   
2197 C  CB  . ILE A 255 ? 0.1361 0.1395 0.1243 0.0186  0.0032  0.0003  256 ILE A CB  
2198 C  CG1 . ILE A 255 ? 0.1499 0.1544 0.1439 0.0196  0.0043  -0.0131 256 ILE A CG1 
2199 C  CG2 . ILE A 255 ? 0.1410 0.1854 0.1326 0.0140  -0.0074 0.0073  256 ILE A CG2 
2200 C  CD1 . ILE A 255 ? 0.1747 0.1754 0.1538 0.0070  0.0200  -0.0086 256 ILE A CD1 
2201 N  N   A LYS A 256 ? 0.1230 0.1475 0.1010 0.0087  0.0115  0.0115  257 LYS A N   
2202 N  N   B LYS A 256 ? 0.1184 0.1484 0.0956 0.0060  0.0093  0.0120  257 LYS A N   
2203 C  CA  A LYS A 256 ? 0.1203 0.1627 0.1023 -0.0007 0.0313  0.0229  257 LYS A CA  
2204 C  CA  B LYS A 256 ? 0.1132 0.1553 0.1011 0.0127  0.0234  0.0078  257 LYS A CA  
2205 C  C   A LYS A 256 ? 0.1134 0.1612 0.1124 0.0136  0.0109  0.0035  257 LYS A C   
2206 C  C   B LYS A 256 ? 0.1169 0.1263 0.0847 0.0087  0.0087  0.0103  257 LYS A C   
2207 O  O   A LYS A 256 ? 0.1442 0.1499 0.1076 0.0109  0.0289  0.0030  257 LYS A O   
2208 O  O   B LYS A 256 ? 0.1189 0.1006 0.0830 0.0048  0.0167  0.0063  257 LYS A O   
2209 C  CB  A LYS A 256 ? 0.1485 0.1553 0.1542 0.0177  0.0093  -0.0153 257 LYS A CB  
2210 C  CB  B LYS A 256 ? 0.1509 0.1524 0.1227 -0.0043 0.0065  0.0082  257 LYS A CB  
2211 C  CG  A LYS A 256 ? 0.2350 0.1796 0.2046 -0.0055 -0.0020 -0.0171 257 LYS A CG  
2212 C  CG  B LYS A 256 ? 0.2074 0.1747 0.1463 0.0057  -0.0156 0.0107  257 LYS A CG  
2213 C  CD  A LYS A 256 ? 0.2628 0.2233 0.1944 0.0241  -0.0208 -0.0439 257 LYS A CD  
2214 C  CD  B LYS A 256 ? 0.2808 0.1944 0.2357 0.0152  -0.0581 0.0093  257 LYS A CD  
2215 N  N   . ALA A 257 ? 0.1220 0.1744 0.1093 -0.0089 0.0244  0.0089  258 ALA A N   
2216 C  CA  . ALA A 257 ? 0.1186 0.1666 0.1184 0.0088  0.0206  0.0086  258 ALA A CA  
2217 C  C   . ALA A 257 ? 0.1242 0.1588 0.1227 -0.0043 0.0368  0.0015  258 ALA A C   
2218 O  O   . ALA A 257 ? 0.1379 0.1891 0.1211 0.0059  0.0377  -0.0054 258 ALA A O   
2219 C  CB  . ALA A 257 ? 0.1495 0.1682 0.1729 0.0031  0.0240  -0.0052 258 ALA A CB  
2220 N  N   . SER A 258 ? 0.1316 0.1537 0.1198 0.0054  0.0229  0.0051  259 SER A N   
2221 C  CA  . SER A 258 ? 0.1349 0.1808 0.1407 0.0057  0.0227  0.0006  259 SER A CA  
2222 C  C   . SER A 258 ? 0.1213 0.2011 0.1648 0.0023  0.0573  -0.0044 259 SER A C   
2223 O  O   . SER A 258 ? 0.1541 0.2664 0.2020 0.0130  0.0597  0.0239  259 SER A O   
2224 C  CB  . SER A 258 ? 0.1492 0.1732 0.1689 0.0003  0.0008  0.0068  259 SER A CB  
2225 O  OG  . SER A 258 ? 0.1189 0.1973 0.1359 -0.0015 0.0138  -0.0034 259 SER A OG  
2226 N  N   . PHE A 259 ? 0.1454 0.1896 0.1680 -0.0160 0.0436  0.0049  260 PHE A N   
2227 C  CA  . PHE A 259 ? 0.1630 0.2081 0.2081 -0.0329 0.0412  0.0250  260 PHE A CA  
2228 C  C   . PHE A 259 ? 0.2287 0.2477 0.1991 -0.0538 0.0759  0.0263  260 PHE A C   
2229 O  O   . PHE A 259 ? 0.2461 0.2177 0.2142 -0.0277 0.0478  0.0553  260 PHE A O   
2230 C  CB  . PHE A 259 ? 0.1611 0.2289 0.2224 -0.0344 0.0342  -0.0138 260 PHE A CB  
2231 C  CG  . PHE A 259 ? 0.1622 0.2012 0.1947 -0.0160 0.0364  0.0071  260 PHE A CG  
2232 C  CD1 . PHE A 259 ? 0.1494 0.1943 0.1696 -0.0294 0.0100  -0.0006 260 PHE A CD1 
2233 C  CD2 . PHE A 259 ? 0.2319 0.1861 0.2657 -0.0100 0.0266  0.0216  260 PHE A CD2 
2234 C  CE1 . PHE A 259 ? 0.1685 0.1955 0.1852 -0.0151 0.0238  0.0008  260 PHE A CE1 
2235 C  CE2 . PHE A 259 ? 0.2513 0.2092 0.2542 -0.0070 0.0494  0.0436  260 PHE A CE2 
2236 C  CZ  . PHE A 259 ? 0.2206 0.2061 0.2520 -0.0071 0.0102  0.0059  260 PHE A CZ  
2237 N  N   . LYS A 260 ? 0.3903 0.3776 0.2707 -0.1647 0.0657  0.0841  261 LYS A N   
2238 C  CA  . LYS A 260 ? 0.7858 0.4833 0.2655 -0.0179 0.1186  0.1437  261 LYS A CA  
2239 C  C   . LYS A 260 ? 1.0285 0.4744 0.2897 -0.1997 0.0940  0.1125  261 LYS A C   
2240 O  O   . LYS A 260 ? 0.8741 0.6754 0.9599 -0.0337 0.3161  0.2415  261 LYS A O   
2241 C  CB  . LYS A 260 ? 0.5200 0.4282 0.5001 -0.0408 0.1402  0.1455  261 LYS A CB  
2242 C  CG  . LYS A 260 ? 0.6075 0.3952 0.6051 -0.1585 0.0998  0.0842  261 LYS A CG  
2243 O  OXT . LYS A 260 ? 1.2308 0.9869 1.2206 0.0766  0.0264  0.2847  261 LYS A OXT 
2244 ZN ZN  . ZN  B .   ? 0.0926 0.0842 0.0860 -0.0068 -0.0043 -0.0034 301 ZN  A ZN  
2245 S  S   . DMS C .   ? 0.2075 0.2193 0.2014 -0.0208 0.0222  -0.0255 302 DMS A S   
2246 O  O   . DMS C .   ? 0.3043 0.2408 0.2383 0.0209  0.0544  -0.0586 302 DMS A O   
2247 C  C1  . DMS C .   ? 0.1863 0.1929 0.1964 0.0237  0.0469  -0.0087 302 DMS A C1  
2248 C  C2  . DMS C .   ? 0.2193 0.1808 0.2506 -0.0151 0.0208  -0.0024 302 DMS A C2  
2249 O  O1  . MES D .   ? 0.4436 0.4876 0.2504 -0.0680 -0.0366 -0.0401 303 MES A O1  
2250 C  C2  . MES D .   ? 0.4226 0.2375 0.3032 0.0195  -0.0144 -0.0421 303 MES A C2  
2251 C  C3  . MES D .   ? 0.3851 0.2292 0.3898 0.0317  -0.0192 0.0068  303 MES A C3  
2252 N  N4  . MES D .   ? 0.4327 0.3930 0.3668 -0.1017 -0.0147 -0.0513 303 MES A N4  
2253 C  C5  . MES D .   ? 0.5277 0.3939 0.2371 -0.0564 0.0768  -0.0693 303 MES A C5  
2254 C  C6  . MES D .   ? 0.4065 0.2693 0.2804 0.0115  0.0208  0.0377  303 MES A C6  
2255 C  C7  . MES D .   ? 0.4316 0.4395 0.6563 -0.1642 -0.0368 0.1685  303 MES A C7  
2256 C  C8  . MES D .   ? 0.5205 0.1990 0.3970 -0.0500 0.1033  -0.0008 303 MES A C8  
2257 C  C1  A MLA E .   ? 0.3662 0.3508 0.5252 -0.0035 0.1547  -0.0131 304 MLA A C1  
2258 C  C1  B MLA E .   ? 0.1612 0.2366 0.3197 -0.0513 -0.0463 -0.0685 304 MLA A C1  
2259 O  O1A A MLA E .   ? 0.2400 0.2567 0.2291 0.0355  0.0013  0.0088  304 MLA A O1A 
2260 O  O1A B MLA E .   ? 0.2305 0.2452 0.2009 0.0167  0.0263  -0.0129 304 MLA A O1A 
2261 O  O1B A MLA E .   ? 0.4401 0.4490 0.3901 -0.0549 0.1226  0.0414  304 MLA A O1B 
2262 O  O1B B MLA E .   ? 0.2325 0.3192 0.2175 -0.0461 -0.0423 -0.0104 304 MLA A O1B 
2263 C  C2  A MLA E .   ? 0.2502 0.2951 0.3294 0.0399  0.1510  0.0965  304 MLA A C2  
2264 C  C2  B MLA E .   ? 0.3192 0.2676 0.1356 -0.0142 0.0178  -0.0518 304 MLA A C2  
2265 C  C3  A MLA E .   ? 0.2294 0.2266 0.2490 -0.0328 0.1218  0.0087  304 MLA A C3  
2266 C  C3  B MLA E .   ? 0.1917 0.2718 0.2230 0.0307  -0.0318 -0.1001 304 MLA A C3  
2267 O  O3A A MLA E .   ? 0.6679 0.6046 0.9878 0.0086  -0.0593 -0.1040 304 MLA A O3A 
2268 O  O3A B MLA E .   ? 0.3098 0.2594 0.3041 0.0419  -0.0252 -0.0296 304 MLA A O3A 
2269 O  O3B A MLA E .   ? 0.2854 0.5667 0.6498 -0.1460 0.0573  -0.0147 304 MLA A O3B 
2270 O  O3B B MLA E .   ? 0.2333 0.5314 0.3684 0.0750  -0.0076 -0.0494 304 MLA A O3B 
2271 N  N1  . BCN F .   ? 0.4871 0.4602 0.4318 0.0439  0.0623  -0.0423 305 BCN A N1  
2272 C  C1  . BCN F .   ? 0.3801 0.2169 0.3691 -0.0555 0.0449  -0.0362 305 BCN A C1  
2273 C  C2  . BCN F .   ? 0.4090 0.4341 0.4801 -0.0852 0.0401  -0.0738 305 BCN A C2  
2274 O  O21 . BCN F .   ? 0.5304 0.6942 0.8586 -0.3199 -0.1377 0.1442  305 BCN A O21 
2275 O  O22 . BCN F .   ? 0.6741 0.6453 1.0060 0.1494  0.0790  -0.0430 305 BCN A O22 
2276 C  C3  . BCN F .   ? 0.4821 0.5345 0.4462 -0.0971 -0.0914 0.0948  305 BCN A C3  
2277 C  C4  . BCN F .   ? 0.3564 0.2890 0.5138 -0.0657 0.0693  0.0860  305 BCN A C4  
2278 O  O4  . BCN F .   ? 0.6219 0.5440 0.6193 -0.2542 0.0428  0.1274  305 BCN A O4  
2279 C  C5  . BCN F .   ? 0.3088 0.3082 0.3639 -0.0445 0.0405  -0.0159 305 BCN A C5  
2280 C  C6  . BCN F .   ? 0.5583 0.4083 0.2942 0.0377  0.0289  -0.0209 305 BCN A C6  
2281 O  O6  . BCN F .   ? 0.4914 0.3740 0.4905 -0.1010 0.0137  -0.0359 305 BCN A O6  
2282 F  F18 . 3TV G .   ? 0.1576 0.1076 0.2108 0.0021  0.0231  0.0146  306 3TV A F18 
2283 C  C7  . 3TV G .   ? 0.1314 0.0926 0.1513 -0.0008 -0.0082 0.0148  306 3TV A C7  
2284 C  C6  . 3TV G .   ? 0.1207 0.1028 0.1393 -0.0104 0.0054  -0.0015 306 3TV A C6  
2285 F  F17 . 3TV G .   ? 0.1437 0.1094 0.1615 -0.0093 0.0196  -0.0131 306 3TV A F17 
2286 C  C8  . 3TV G .   ? 0.1458 0.1159 0.1456 0.0008  -0.0063 0.0197  306 3TV A C8  
2287 S  S11 . 3TV G .   ? 0.1858 0.1597 0.1710 -0.0208 0.0031  0.0386  306 3TV A S11 
2288 C  C12 . 3TV G .   ? 0.1784 0.1578 0.2100 -0.0553 -0.0157 0.0261  306 3TV A C12 
2289 C  C13 . 3TV G .   ? 0.1965 0.1947 0.1705 -0.0494 -0.0082 0.0186  306 3TV A C13 
2290 C  C14 . 3TV G .   ? 0.2594 0.1677 0.2545 -0.0186 -0.0322 0.0161  306 3TV A C14 
2291 C  C9  . 3TV G .   ? 0.1253 0.1435 0.1250 -0.0120 0.0122  -0.0013 306 3TV A C9  
2292 F  F15 . 3TV G .   ? 0.1405 0.1785 0.1462 -0.0032 0.0156  0.0133  306 3TV A F15 
2293 C  C10 . 3TV G .   ? 0.1146 0.1081 0.1299 -0.0032 -0.0032 -0.0035 306 3TV A C10 
2294 F  F16 . 3TV G .   ? 0.2472 0.2043 0.2468 -0.0074 0.0088  0.0054  306 3TV A F16 
2295 C  C5  . 3TV G .   ? 0.1089 0.1039 0.1164 0.0006  0.0000  0.0001  306 3TV A C5  
2296 S  S1  . 3TV G .   ? 0.0956 0.0896 0.1013 -0.0032 -0.0126 -0.0076 306 3TV A S1  
2297 O  O3  . 3TV G .   ? 0.0982 0.0998 0.1132 0.0021  -0.0201 -0.0087 306 3TV A O3  
2298 O  O4  . 3TV G .   ? 0.0904 0.1024 0.0956 -0.0043 -0.0076 -0.0086 306 3TV A O4  
2299 N  N2  . 3TV G .   ? 0.1058 0.0891 0.1099 -0.0060 -0.0164 -0.0175 306 3TV A N2  
2300 F  F18 . 3TV H .   ? 0.3815 0.2847 0.3104 -0.0074 0.0987  0.0597  307 3TV A F18 
2301 C  C7  . 3TV H .   ? 0.2885 0.2658 0.2660 -0.0027 0.0614  0.0146  307 3TV A C7  
2302 C  C6  . 3TV H .   ? 0.1962 0.2454 0.2436 -0.0099 0.0401  0.0390  307 3TV A C6  
2303 F  F17 . 3TV H .   ? 0.3269 0.2937 0.2960 0.0463  0.0566  0.0531  307 3TV A F17 
2304 C  C8  . 3TV H .   ? 0.1669 0.2633 0.2196 -0.0511 -0.0208 0.0073  307 3TV A C8  
2305 S  S11 . 3TV H .   ? 0.2131 0.3526 0.2727 0.0137  0.0204  -0.0147 307 3TV A S11 
2306 C  C12 . 3TV H .   ? 0.2343 0.3644 0.3986 0.0076  -0.0427 -0.1397 307 3TV A C12 
2307 C  C13 . 3TV H .   ? 0.6383 0.5307 0.4523 0.1252  -0.0518 -0.2073 307 3TV A C13 
2308 C  C14 . 3TV H .   ? 0.4393 0.5220 0.5733 0.1932  -0.1731 -0.0017 307 3TV A C14 
2309 C  C9  . 3TV H .   ? 0.2224 0.2815 0.2078 0.0231  -0.0351 -0.0201 307 3TV A C9  
2310 F  F15 . 3TV H .   ? 0.2090 0.3152 0.3082 0.0533  0.0216  0.0046  307 3TV A F15 
2311 C  C10 . 3TV H .   ? 0.1959 0.2752 0.2184 0.0333  0.0068  0.0188  307 3TV A C10 
2312 F  F16 . 3TV H .   ? 0.2649 0.3181 0.2436 -0.0274 -0.0086 0.0542  307 3TV A F16 
2313 C  C5  . 3TV H .   ? 0.1861 0.2310 0.2479 -0.0390 -0.0005 0.0423  307 3TV A C5  
2314 S  S1  . 3TV H .   ? 0.1614 0.2536 0.2375 -0.0120 -0.0060 0.0215  307 3TV A S1  
2315 O  O3  . 3TV H .   ? 0.1694 0.2696 0.2513 -0.0877 0.0096  0.0013  307 3TV A O3  
2316 O  O4  . 3TV H .   ? 0.1791 0.2698 0.2825 0.0229  0.0049  0.0324  307 3TV A O4  
2317 N  N2  . 3TV H .   ? 0.1587 0.2675 0.2592 0.0015  -0.0015 0.0342  307 3TV A N2  
2318 O  O   . HOH I .   ? 0.2484 0.2213 0.3425 -0.0164 -0.0604 -0.0083 401 HOH A O   
2319 O  O   . HOH I .   ? 0.2809 0.1666 0.2723 0.0166  -0.0303 0.0226  402 HOH A O   
2320 O  O   . HOH I .   ? 0.4246 0.4736 0.5978 0.0190  -0.0645 0.1524  403 HOH A O   
2321 O  O   . HOH I .   ? 0.4334 0.2887 0.1787 -0.1498 0.0092  -0.0590 404 HOH A O   
2322 O  O   . HOH I .   ? 0.2143 0.1062 0.1648 -0.0122 -0.0272 -0.0052 405 HOH A O   
2323 O  O   . HOH I .   ? 0.5072 0.3242 0.3777 0.1664  -0.1049 -0.0666 406 HOH A O   
2324 O  O   . HOH I .   ? 0.7652 0.7732 0.6137 -0.6682 0.1935  -0.2745 407 HOH A O   
2325 O  O   . HOH I .   ? 0.1965 0.1545 0.1744 -0.0176 -0.0077 0.0071  408 HOH A O   
2326 O  O   . HOH I .   ? 0.7559 0.4803 0.2651 0.0662  -0.0125 0.0233  409 HOH A O   
2327 O  O   . HOH I .   ? 0.3630 0.2863 0.2840 0.0203  0.0533  0.0340  410 HOH A O   
2328 O  O   . HOH I .   ? 0.5795 0.3874 0.4445 -0.0980 -0.0923 0.2064  411 HOH A O   
2329 O  O   . HOH I .   ? 0.3582 0.4851 0.2302 -0.0194 0.0171  0.0164  412 HOH A O   
2330 O  O   . HOH I .   ? 0.4578 0.2829 0.2547 0.0601  0.0171  0.0324  413 HOH A O   
2331 O  O   . HOH I .   ? 1.0387 0.4018 0.8338 0.2231  0.0010  -0.1719 414 HOH A O   
2332 O  O   . HOH I .   ? 0.4517 0.2170 0.4305 0.0245  0.0958  0.0625  415 HOH A O   
2333 O  O   . HOH I .   ? 0.3648 0.4289 0.3255 -0.0373 0.0974  -0.0179 416 HOH A O   
2334 O  O   . HOH I .   ? 0.5059 0.4219 0.2883 -0.0619 0.0745  0.1067  417 HOH A O   
2335 O  O   . HOH I .   ? 0.2405 0.2551 0.2380 0.0140  -0.0472 0.0071  418 HOH A O   
2336 O  O   . HOH I .   ? 0.2854 0.4560 0.1708 -0.1497 -0.0878 0.0469  419 HOH A O   
2337 O  O   . HOH I .   ? 0.1712 0.3472 0.5752 0.0381  -0.1256 -0.2164 420 HOH A O   
2338 O  O   . HOH I .   ? 0.2876 0.2906 0.2293 -0.0500 -0.0742 0.0020  421 HOH A O   
2339 O  O   . HOH I .   ? 0.2948 0.1710 0.2462 -0.0109 0.0280  -0.0028 422 HOH A O   
2340 O  O   . HOH I .   ? 0.4668 0.3037 0.1456 -0.0102 0.0324  -0.0364 423 HOH A O   
2341 O  O   . HOH I .   ? 0.2838 0.3163 0.6105 -0.0071 0.2117  0.0078  424 HOH A O   
2342 O  O   . HOH I .   ? 0.2386 0.2991 0.2108 0.0320  0.0032  0.0303  425 HOH A O   
2343 O  O   . HOH I .   ? 0.5225 0.2198 0.4582 -0.0630 -0.0103 -0.0640 426 HOH A O   
2344 O  O   . HOH I .   ? 0.5904 0.4377 0.4521 0.0007  -0.2406 0.0803  427 HOH A O   
2345 O  O   . HOH I .   ? 0.2736 0.3443 0.4341 0.1084  -0.1299 -0.0386 428 HOH A O   
2346 O  O   . HOH I .   ? 0.4541 0.2475 0.3833 -0.0692 -0.1076 0.0057  429 HOH A O   
2347 O  O   . HOH I .   ? 0.4670 0.4002 0.2691 -0.0472 -0.1171 0.0833  430 HOH A O   
2348 O  O   . HOH I .   ? 0.3817 0.3966 0.2772 0.1342  0.0173  0.1181  431 HOH A O   
2349 O  O   . HOH I .   ? 0.3607 0.2949 0.5109 0.0154  0.0628  0.2066  432 HOH A O   
2350 O  O   . HOH I .   ? 0.5494 0.2132 0.8039 -0.0104 0.1941  0.1243  433 HOH A O   
2351 O  O   . HOH I .   ? 0.2592 0.3673 0.4140 -0.0046 -0.0098 0.1042  434 HOH A O   
2352 O  O   . HOH I .   ? 0.2394 0.2732 0.3887 -0.0454 -0.1124 0.0892  435 HOH A O   
2353 O  O   . HOH I .   ? 0.3061 0.4045 0.3070 -0.0869 0.1194  -0.1384 436 HOH A O   
2354 O  O   . HOH I .   ? 0.2351 0.1609 0.1750 0.0313  -0.0694 -0.0008 437 HOH A O   
2355 O  O   . HOH I .   ? 0.4286 0.3458 0.3849 -0.0060 -0.0430 -0.1402 438 HOH A O   
2356 O  O   . HOH I .   ? 0.1962 0.1752 0.2129 -0.0399 -0.0088 0.0379  439 HOH A O   
2357 O  O   . HOH I .   ? 0.3328 0.4539 0.5625 -0.1328 0.1661  -0.0570 440 HOH A O   
2358 O  O   . HOH I .   ? 0.4237 0.3278 0.6830 0.1274  0.0000  -0.0260 441 HOH A O   
2359 O  O   . HOH I .   ? 0.4065 0.8108 0.5329 -0.0754 -0.0772 0.2492  442 HOH A O   
2360 O  O   . HOH I .   ? 0.2840 0.3790 0.4169 0.0702  -0.1178 -0.2334 443 HOH A O   
2361 O  O   . HOH I .   ? 0.3063 0.1849 0.2865 -0.0182 -0.0231 -0.0076 444 HOH A O   
2362 O  O   . HOH I .   ? 0.2414 0.2064 0.2239 0.0379  0.0185  -0.0148 445 HOH A O   
2363 O  O   . HOH I .   ? 0.2644 0.4230 0.4054 0.0237  -0.0869 0.0879  446 HOH A O   
2364 O  O   . HOH I .   ? 0.5838 0.5663 0.2044 -0.0621 0.0566  0.0445  447 HOH A O   
2365 O  O   . HOH I .   ? 0.8802 0.2596 0.2443 -0.0908 0.1398  0.0687  448 HOH A O   
2366 O  O   . HOH I .   ? 0.2915 0.1923 0.3671 -0.0242 -0.0458 0.0370  449 HOH A O   
2367 O  O   . HOH I .   ? 0.2502 0.2104 0.2332 0.0074  -0.0248 0.0236  450 HOH A O   
2368 O  O   . HOH I .   ? 0.2398 0.1886 0.2081 -0.0076 -0.0705 -0.0219 451 HOH A O   
2369 O  O   . HOH I .   ? 0.2207 0.1247 0.1994 -0.0324 0.0051  0.0031  452 HOH A O   
2370 O  O   . HOH I .   ? 0.1925 0.1324 0.1806 -0.0203 -0.0186 -0.0010 453 HOH A O   
2371 O  O   . HOH I .   ? 0.3953 0.4993 0.2196 -0.0276 -0.1182 0.1037  454 HOH A O   
2372 O  O   . HOH I .   ? 0.3073 0.3860 0.3537 -0.2014 -0.0494 0.0685  455 HOH A O   
2373 O  O   . HOH I .   ? 0.3601 0.2951 0.3098 0.0315  -0.0083 0.1722  456 HOH A O   
2374 O  O   . HOH I .   ? 0.2266 0.3167 0.2847 -0.0948 -0.0027 -0.0104 457 HOH A O   
2375 O  O   . HOH I .   ? 0.2964 0.2423 0.3576 -0.0253 -0.0120 0.0732  458 HOH A O   
2376 O  O   . HOH I .   ? 0.2693 0.3133 0.3519 0.0274  0.0987  -0.0085 459 HOH A O   
2377 O  O   . HOH I .   ? 0.1270 0.2720 0.3109 -0.0142 -0.0403 0.0102  460 HOH A O   
2378 O  O   . HOH I .   ? 0.2056 0.2685 0.2194 0.0593  0.0076  0.0662  461 HOH A O   
2379 O  O   . HOH I .   ? 0.3840 0.3064 0.1992 -0.0961 0.1045  -0.0806 462 HOH A O   
2380 O  O   . HOH I .   ? 0.2473 0.2509 0.1818 -0.0329 0.0000  -0.0282 463 HOH A O   
2381 O  O   . HOH I .   ? 0.5521 0.3371 0.3314 0.1247  0.1204  0.1303  464 HOH A O   
2382 O  O   . HOH I .   ? 0.8604 0.6107 0.5019 -0.0436 -0.1158 0.0494  465 HOH A O   
2383 O  O   . HOH I .   ? 0.2357 0.1611 0.1885 -0.0131 -0.0546 0.0063  466 HOH A O   
2384 O  O   . HOH I .   ? 0.2081 0.1867 0.2583 -0.0248 0.0564  -0.0154 467 HOH A O   
2385 O  O   . HOH I .   ? 0.3962 0.5120 0.4146 0.0678  0.1152  0.1159  468 HOH A O   
2386 O  O   . HOH I .   ? 0.2608 0.6758 0.6740 -0.0847 -0.1334 0.1229  469 HOH A O   
2387 O  O   . HOH I .   ? 0.3481 0.2725 0.2569 -0.0577 0.0553  -0.0296 470 HOH A O   
2388 O  O   . HOH I .   ? 0.1810 0.1446 0.1870 0.0274  0.0068  0.0043  471 HOH A O   
2389 O  O   . HOH I .   ? 0.4650 0.2763 0.1914 -0.0909 0.0154  -0.0560 472 HOH A O   
2390 O  O   . HOH I .   ? 0.3066 0.4329 0.3546 0.0296  -0.0452 0.1046  473 HOH A O   
2391 O  O   . HOH I .   ? 0.1917 0.2469 0.2825 0.0366  -0.0353 -0.0109 474 HOH A O   
2392 O  O   . HOH I .   ? 0.3424 0.1870 0.2554 -0.0126 -0.0091 -0.0702 475 HOH A O   
2393 O  O   . HOH I .   ? 0.2883 0.2908 0.2623 -0.0394 -0.0700 0.0081  476 HOH A O   
2394 O  O   . HOH I .   ? 0.2536 0.1738 0.2261 0.0215  -0.0062 0.0263  477 HOH A O   
2395 O  O   . HOH I .   ? 0.3901 0.3217 0.3860 0.0131  -0.0099 -0.0328 478 HOH A O   
2396 O  O   . HOH I .   ? 0.7348 1.0031 0.3182 0.6380  -0.2978 -0.0076 479 HOH A O   
2397 O  O   . HOH I .   ? 0.3533 0.2926 0.4921 -0.1468 -0.1562 0.1261  480 HOH A O   
2398 O  O   . HOH I .   ? 0.3702 0.5066 0.3066 0.0467  0.0586  0.0329  481 HOH A O   
2399 O  O   . HOH I .   ? 0.3179 0.1643 0.3075 0.0124  -0.0991 0.0237  482 HOH A O   
2400 O  O   . HOH I .   ? 0.1801 0.2265 0.2712 0.0599  0.0531  0.0062  483 HOH A O   
2401 O  O   . HOH I .   ? 0.3878 0.2935 0.2127 0.1552  -0.0549 -0.0038 484 HOH A O   
2402 O  O   . HOH I .   ? 0.4250 0.2113 0.3129 0.0891  -0.0170 -0.0680 485 HOH A O   
2403 O  O   . HOH I .   ? 0.3630 0.1976 0.3544 0.0054  -0.0236 -0.0344 486 HOH A O   
2404 O  O   . HOH I .   ? 0.4086 0.3632 0.3240 0.0544  0.0878  0.1596  487 HOH A O   
2405 O  O   . HOH I .   ? 0.2834 0.2003 0.1688 0.0277  -0.0236 0.0274  488 HOH A O   
2406 O  O   . HOH I .   ? 0.4242 0.2008 0.3127 0.0627  0.0518  0.0458  489 HOH A O   
2407 O  O   . HOH I .   ? 0.3492 0.3675 0.1873 0.0423  -0.0425 -0.0175 490 HOH A O   
2408 O  O   . HOH I .   ? 0.4126 0.2980 0.3192 0.0458  0.0562  0.0331  491 HOH A O   
2409 O  O   . HOH I .   ? 0.2319 0.3219 0.3925 0.0285  0.0395  0.0285  492 HOH A O   
2410 O  O   . HOH I .   ? 0.3544 0.2517 0.5432 -0.0318 -0.0570 0.1402  493 HOH A O   
2411 O  O   . HOH I .   ? 0.2473 0.3348 0.2390 0.0568  0.0463  -0.0357 494 HOH A O   
2412 O  O   . HOH I .   ? 0.2257 0.1290 0.2171 0.0089  -0.0046 -0.0082 495 HOH A O   
2413 O  O   . HOH I .   ? 0.3107 0.2702 0.3079 -0.0024 -0.0401 -0.0458 496 HOH A O   
2414 O  O   . HOH I .   ? 0.9154 0.9124 0.2407 0.2245  0.1200  -0.0678 497 HOH A O   
2415 O  O   . HOH I .   ? 0.4797 0.3380 0.2904 -0.0364 -0.0057 0.0825  498 HOH A O   
2416 O  O   . HOH I .   ? 0.3607 0.2802 0.2190 0.1083  0.0412  -0.0335 499 HOH A O   
2417 O  O   . HOH I .   ? 0.2160 0.2104 0.3955 0.0560  0.0712  -0.0144 500 HOH A O   
2418 O  O   . HOH I .   ? 0.4875 0.4478 0.4268 0.0295  -0.1412 0.1598  501 HOH A O   
2419 O  O   . HOH I .   ? 0.3454 0.1818 0.3231 -0.0215 -0.0399 0.0057  502 HOH A O   
2420 O  O   . HOH I .   ? 0.2655 0.5286 0.4758 -0.0983 -0.0348 0.1058  503 HOH A O   
2421 O  O   . HOH I .   ? 0.3996 0.3935 0.2128 0.0282  0.0436  0.1512  504 HOH A O   
2422 O  O   . HOH I .   ? 0.3079 0.3118 0.2433 -0.0318 -0.0482 -0.0320 505 HOH A O   
2423 O  O   . HOH I .   ? 0.2987 0.3819 0.4533 0.1048  0.1096  0.0820  506 HOH A O   
2424 O  O   . HOH I .   ? 0.8001 0.5889 0.4629 0.2431  -0.1917 -0.0498 507 HOH A O   
2425 O  O   . HOH I .   ? 0.3456 0.3644 0.6840 -0.0671 0.0320  0.1080  508 HOH A O   
2426 O  O   . HOH I .   ? 0.2649 0.5026 0.2655 0.0604  0.0606  0.0109  509 HOH A O   
2427 O  O   . HOH I .   ? 0.5582 0.6614 0.3375 0.1022  0.0262  0.1660  510 HOH A O   
2428 O  O   . HOH I .   ? 0.3472 0.3943 0.7957 -0.1024 0.1588  -0.0782 511 HOH A O   
2429 O  O   . HOH I .   ? 0.3192 0.3546 0.3361 0.0693  -0.0010 0.0649  512 HOH A O   
2430 O  O   . HOH I .   ? 0.4388 0.2716 0.2996 -0.0092 0.1212  0.1058  513 HOH A O   
2431 O  O   . HOH I .   ? 0.5407 0.5831 0.4731 -0.0775 0.0006  0.0656  514 HOH A O   
2432 O  O   . HOH I .   ? 0.4724 0.4587 0.3111 0.1226  0.0680  0.1008  515 HOH A O   
2433 O  O   . HOH I .   ? 0.1928 0.1458 0.2230 -0.0152 -0.0368 -0.0125 516 HOH A O   
2434 O  O   . HOH I .   ? 0.5314 0.2651 0.5784 -0.0375 -0.1344 -0.0132 517 HOH A O   
2435 O  O   . HOH I .   ? 0.3345 0.4855 0.5745 0.1348  -0.1644 -0.1146 518 HOH A O   
2436 O  O   . HOH I .   ? 0.3174 0.3864 0.8601 0.0744  0.0278  0.1158  519 HOH A O   
2437 O  O   . HOH I .   ? 0.4436 0.3048 0.3749 -0.0126 -0.0518 0.0223  520 HOH A O   
2438 O  O   . HOH I .   ? 0.6037 0.3012 0.4963 0.0597  -0.0141 -0.0265 521 HOH A O   
2439 O  O   . HOH I .   ? 0.4564 0.3068 0.6632 0.0989  -0.0026 -0.0135 522 HOH A O   
2440 O  O   . HOH I .   ? 0.4101 0.2037 0.6108 -0.0732 0.1333  0.0172  523 HOH A O   
2441 O  O   . HOH I .   ? 0.6255 0.3298 0.4357 0.0096  0.0104  -0.1023 524 HOH A O   
2442 O  O   . HOH I .   ? 0.3671 0.4919 0.4162 0.1089  -0.0071 -0.1704 525 HOH A O   
2443 O  O   . HOH I .   ? 0.3625 0.3353 0.4268 0.1067  -0.0754 -0.0194 526 HOH A O   
2444 O  O   . HOH I .   ? 0.1966 0.2707 0.2461 -0.0021 -0.0012 0.0130  527 HOH A O   
2445 O  O   . HOH I .   ? 0.4216 0.5243 0.2479 0.0108  0.1466  0.0154  528 HOH A O   
2446 O  O   . HOH I .   ? 0.6176 0.2025 0.4647 0.0207  -0.0154 -0.0641 529 HOH A O   
2447 O  O   . HOH I .   ? 0.3786 0.4129 0.3115 0.0520  0.1006  -0.0582 530 HOH A O   
2448 O  O   . HOH I .   ? 0.5307 0.2903 0.2073 -0.0538 0.0287  -0.0913 531 HOH A O   
2449 O  O   . HOH I .   ? 0.4316 0.2301 0.2856 0.0553  -0.0939 -0.0121 532 HOH A O   
2450 O  O   . HOH I .   ? 0.2161 0.3395 0.2610 0.0308  -0.0019 0.0023  533 HOH A O   
2451 O  O   . HOH I .   ? 0.6715 0.5166 0.5040 0.1926  -0.1097 -0.1107 534 HOH A O   
2452 O  O   . HOH I .   ? 0.3607 0.5404 0.4402 -0.1810 -0.1059 0.0728  535 HOH A O   
2453 O  O   . HOH I .   ? 0.3425 0.1917 0.4740 -0.0395 0.1596  -0.0001 536 HOH A O   
2454 O  O   . HOH I .   ? 0.4785 0.3125 0.3109 -0.0164 0.0709  0.1155  537 HOH A O   
2455 O  O   . HOH I .   ? 0.2716 0.4058 0.4052 -0.0601 0.0487  0.0000  538 HOH A O   
2456 O  O   . HOH I .   ? 0.5529 0.3741 0.6492 0.1147  -0.1243 -0.0577 539 HOH A O   
2457 O  O   . HOH I .   ? 0.4582 1.0308 1.3108 0.0608  -0.1639 0.5138  540 HOH A O   
2458 O  O   . HOH I .   ? 0.3605 0.2132 0.2085 -0.0193 0.0174  0.0640  541 HOH A O   
2459 O  O   . HOH I .   ? 0.1063 0.1172 0.1123 -0.0024 0.0156  0.0005  542 HOH A O   
2460 O  O   . HOH I .   ? 0.1218 0.1200 0.1146 -0.0071 0.0100  -0.0127 543 HOH A O   
2461 O  O   . HOH I .   ? 0.1404 0.1578 0.1396 0.0167  -0.0251 0.0115  544 HOH A O   
2462 O  O   . HOH I .   ? 0.1295 0.1067 0.1164 0.0087  0.0008  -0.0066 545 HOH A O   
2463 O  O   . HOH I .   ? 0.2621 0.2924 0.1912 -0.0860 -0.0005 -0.0141 546 HOH A O   
2464 O  O   . HOH I .   ? 0.1067 0.1577 0.1975 -0.0076 -0.0077 -0.0362 547 HOH A O   
2465 O  O   . HOH I .   ? 0.1101 0.1997 0.1831 0.0114  0.0094  -0.0138 548 HOH A O   
2466 O  O   . HOH I .   ? 0.1404 0.1120 0.1473 0.0126  -0.0108 -0.0046 549 HOH A O   
2467 O  O   . HOH I .   ? 0.1538 0.1931 0.2451 0.0181  -0.0456 -0.0199 550 HOH A O   
2468 O  O   . HOH I .   ? 0.1555 0.1218 0.1585 0.0163  -0.0110 0.0148  551 HOH A O   
2469 O  O   . HOH I .   ? 0.2486 0.2003 0.2232 0.0368  0.0599  0.0904  552 HOH A O   
2470 O  O   . HOH I .   ? 0.1498 0.1172 0.1336 -0.0143 0.0175  -0.0137 553 HOH A O   
2471 O  O   . HOH I .   ? 0.2254 0.2171 0.3050 0.0060  -0.1421 -0.0533 554 HOH A O   
2472 O  O   . HOH I .   ? 0.1378 0.1703 0.2013 -0.0126 -0.0010 0.0010  555 HOH A O   
2473 O  O   . HOH I .   ? 0.1422 0.1114 0.0824 -0.0115 0.0013  0.0055  556 HOH A O   
2474 O  O   . HOH I .   ? 0.1864 0.1573 0.1821 -0.0057 -0.0529 0.0166  557 HOH A O   
2475 O  O   . HOH I .   ? 0.2357 0.2088 0.1669 0.0125  0.0555  0.0372  558 HOH A O   
2476 O  O   . HOH I .   ? 0.1506 0.1186 0.1287 -0.0044 0.0137  -0.0147 559 HOH A O   
2477 O  O   . HOH I .   ? 0.1608 0.2434 0.1688 -0.0247 -0.0020 0.0017  560 HOH A O   
2478 O  O   . HOH I .   ? 0.1152 0.1314 0.1105 0.0198  -0.0060 0.0020  561 HOH A O   
2479 O  O   . HOH I .   ? 0.1332 0.2312 0.1532 0.0110  -0.0280 0.0348  562 HOH A O   
2480 O  O   . HOH I .   ? 0.1466 0.1976 0.2083 0.0078  -0.0026 -0.0092 563 HOH A O   
2481 O  O   . HOH I .   ? 0.2657 0.2646 0.2337 -0.0318 0.0983  -0.0615 564 HOH A O   
2482 O  O   . HOH I .   ? 0.1869 0.2013 0.1519 -0.0247 -0.0153 0.0142  565 HOH A O   
2483 O  O   . HOH I .   ? 0.2976 0.2592 0.2366 -0.0969 -0.0568 0.0679  566 HOH A O   
2484 O  O   . HOH I .   ? 0.4203 0.3626 0.1455 0.0138  0.0007  0.0190  567 HOH A O   
2485 O  O   . HOH I .   ? 0.2185 0.1713 0.2461 -0.0696 -0.0238 -0.0324 568 HOH A O   
2486 O  O   . HOH I .   ? 0.2648 0.2069 0.2924 0.0040  -0.0263 0.0715  569 HOH A O   
2487 O  O   . HOH I .   ? 0.2220 0.2085 0.2151 0.0122  -0.0560 0.0185  570 HOH A O   
2488 O  O   . HOH I .   ? 0.2046 0.2234 0.2982 -0.0041 0.0293  -0.0238 571 HOH A O   
2489 O  O   . HOH I .   ? 0.3729 0.2994 0.2874 -0.0643 0.1098  -0.1064 572 HOH A O   
2490 O  O   . HOH I .   ? 0.3763 0.3018 0.2473 0.0194  -0.0974 -0.0197 573 HOH A O   
2491 O  O   . HOH I .   ? 0.3486 0.2061 0.3023 0.1076  -0.0318 -0.0041 574 HOH A O   
2492 O  O   . HOH I .   ? 0.2120 0.1843 0.2583 -0.0315 -0.0210 -0.0186 575 HOH A O   
2493 O  O   . HOH I .   ? 0.1679 0.1893 0.2980 -0.0603 -0.0551 0.0060  576 HOH A O   
2494 O  O   . HOH I .   ? 0.1207 0.2055 0.2646 -0.0147 -0.0057 0.0122  577 HOH A O   
2495 O  O   . HOH I .   ? 0.2825 0.2617 0.2477 -0.0252 -0.0555 -0.0810 578 HOH A O   
2496 O  O   . HOH I .   ? 0.4041 0.2190 0.3763 0.0538  -0.2178 -0.0065 579 HOH A O   
2497 O  O   . HOH I .   ? 0.2372 0.2089 0.2477 0.0278  -0.0617 0.0114  580 HOH A O   
2498 O  O   . HOH I .   ? 0.3192 0.3402 0.2716 -0.0904 0.0162  -0.1193 581 HOH A O   
2499 O  O   . HOH I .   ? 0.3632 0.2089 0.2382 -0.0560 -0.0776 -0.0155 582 HOH A O   
2500 O  O   . HOH I .   ? 0.5139 0.5418 0.5970 0.1697  -0.1046 -0.1325 583 HOH A O   
2501 O  O   . HOH I .   ? 0.3014 0.2220 0.2734 0.0700  0.0636  0.0326  584 HOH A O   
2502 O  O   . HOH I .   ? 0.3282 0.2944 0.2088 -0.0275 0.0782  -0.0886 585 HOH A O   
2503 O  O   . HOH I .   ? 0.2002 0.1849 0.2302 -0.0073 0.0204  -0.0253 586 HOH A O   
2504 O  O   . HOH I .   ? 0.1897 0.2416 0.3034 0.0186  0.0262  -0.0197 587 HOH A O   
2505 O  O   . HOH I .   ? 0.4440 0.5701 0.3501 -0.0208 0.1500  0.0284  588 HOH A O   
2506 O  O   . HOH I .   ? 0.3382 0.2727 0.1811 -0.0344 -0.0513 0.0030  589 HOH A O   
2507 O  O   . HOH I .   ? 0.2166 0.1923 0.2110 0.0041  -0.0275 -0.0223 590 HOH A O   
2508 O  O   . HOH I .   ? 0.2558 0.2511 0.1798 0.0264  -0.0098 0.0362  591 HOH A O   
2509 O  O   . HOH I .   ? 0.2484 0.2570 0.2781 0.0220  0.0164  0.0236  592 HOH A O   
2510 O  O   . HOH I .   ? 0.3063 0.2493 0.4038 -0.0217 0.0183  -0.1124 593 HOH A O   
2511 O  O   . HOH I .   ? 0.3610 0.4007 0.3540 0.1629  0.0663  0.0557  594 HOH A O   
2512 O  O   . HOH I .   ? 0.2982 0.2782 0.5582 0.0063  -0.0173 0.0260  595 HOH A O   
2513 O  O   . HOH I .   ? 0.2412 0.1858 0.2009 -0.0520 -0.0149 -0.0060 596 HOH A O   
2514 O  O   . HOH I .   ? 0.1626 0.2142 0.2216 0.0372  -0.0096 0.0048  597 HOH A O   
2515 O  O   . HOH I .   ? 0.1515 0.3160 0.3319 0.0399  -0.0204 0.0696  598 HOH A O   
2516 O  O   . HOH I .   ? 0.4368 0.5216 0.3170 0.0544  0.0270  0.1393  599 HOH A O   
2517 O  O   . HOH I .   ? 0.2372 0.3370 0.4201 -0.0993 0.0313  -0.0996 600 HOH A O   
2518 O  O   . HOH I .   ? 0.2257 0.2238 0.1641 0.0127  0.0126  -0.0126 601 HOH A O   
2519 O  O   . HOH I .   ? 0.4440 0.2347 0.3573 -0.0131 -0.0206 -0.0164 602 HOH A O   
2520 O  O   . HOH I .   ? 0.2632 0.3634 0.2664 0.0368  -0.0267 -0.0066 603 HOH A O   
2521 O  O   . HOH I .   ? 0.2213 0.1613 0.3080 0.0093  0.0342  -0.0381 604 HOH A O   
2522 O  O   . HOH I .   ? 0.3964 0.3441 0.2354 0.0227  0.0160  -0.0445 605 HOH A O   
2523 O  O   . HOH I .   ? 0.4593 0.3115 0.3370 -0.0310 -0.1474 -0.0080 606 HOH A O   
2524 O  O   . HOH I .   ? 0.2594 0.2454 0.3371 0.0156  0.0183  0.0542  607 HOH A O   
2525 O  O   . HOH I .   ? 0.2326 0.5584 0.3621 -0.0582 0.0148  0.1040  608 HOH A O   
2526 O  O   . HOH I .   ? 0.2143 0.2982 0.1800 -0.0063 0.0083  -0.0318 609 HOH A O   
2527 O  O   . HOH I .   ? 0.2114 0.7271 0.4196 -0.0163 0.0773  0.0829  610 HOH A O   
2528 O  O   . HOH I .   ? 0.2572 0.2284 0.3650 0.0879  -0.0223 -0.0555 611 HOH A O   
2529 O  O   . HOH I .   ? 0.4865 0.2834 0.1817 0.0364  -0.0006 0.0179  612 HOH A O   
2530 O  O   . HOH I .   ? 0.2556 0.2556 0.2168 -0.0480 -0.0491 -0.0130 613 HOH A O   
2531 O  O   . HOH I .   ? 0.2257 0.2061 0.2097 -0.0019 0.0043  0.0126  614 HOH A O   
2532 O  O   . HOH I .   ? 0.6995 0.3763 0.8141 0.0091  -0.3271 -0.0017 615 HOH A O   
2533 O  O   . HOH I .   ? 0.2940 0.4228 0.4052 0.0065  -0.0401 0.0210  616 HOH A O   
2534 O  O   . HOH I .   ? 0.4661 0.3345 0.3438 -0.0828 -0.0601 -0.0113 617 HOH A O   
2535 O  O   . HOH I .   ? 0.3273 0.2369 0.2249 0.0427  -0.0722 -0.0740 618 HOH A O   
2536 O  O   . HOH I .   ? 0.3409 0.3186 0.4760 0.0098  -0.1093 0.0228  619 HOH A O   
2537 O  O   . HOH I .   ? 0.2168 0.3052 0.2192 0.0227  0.0529  -0.0242 620 HOH A O   
2538 O  O   . HOH I .   ? 0.4262 0.3980 0.4165 0.1181  0.1736  -0.0273 621 HOH A O   
2539 O  O   . HOH I .   ? 0.2782 0.2971 0.3781 0.0441  0.0206  0.0107  622 HOH A O   
2540 O  O   . HOH I .   ? 0.2398 0.2224 0.2921 -0.0051 0.0096  -0.0450 623 HOH A O   
2541 O  O   . HOH I .   ? 0.1894 0.3125 0.4507 0.0781  -0.0218 0.0026  624 HOH A O   
2542 O  O   . HOH I .   ? 0.2721 0.4848 0.6033 -0.1248 -0.0899 -0.0030 625 HOH A O   
2543 O  O   . HOH I .   ? 0.4891 0.3034 0.4347 -0.0868 0.0820  -0.1260 626 HOH A O   
2544 O  O   . HOH I .   ? 0.2833 0.2917 0.2421 -0.0548 0.0044  0.0052  627 HOH A O   
2545 O  O   . HOH I .   ? 0.3327 0.3190 0.2134 0.0961  0.0339  0.0579  628 HOH A O   
2546 O  O   . HOH I .   ? 0.2759 0.3925 0.4600 -0.0718 0.0227  -0.2035 629 HOH A O   
2547 O  O   . HOH I .   ? 0.3097 0.2773 0.3339 0.0297  0.1006  0.0373  630 HOH A O   
2548 O  O   . HOH I .   ? 0.5231 0.3939 0.4799 0.0252  -0.0838 -0.1171 631 HOH A O   
2549 O  O   . HOH I .   ? 0.3427 0.3454 0.2743 0.0167  0.0062  0.0432  632 HOH A O   
2550 O  O   . HOH I .   ? 0.3603 0.3501 0.3625 0.0646  0.1001  0.1059  633 HOH A O   
2551 O  O   . HOH I .   ? 0.2282 0.3984 0.3030 0.0236  0.0368  -0.0288 634 HOH A O   
2552 O  O   . HOH I .   ? 0.3039 0.6130 0.3537 0.0706  -0.0131 0.1234  635 HOH A O   
2553 O  O   . HOH I .   ? 0.2750 0.3808 0.4476 -0.0843 0.0043  -0.0395 636 HOH A O   
2554 O  O   . HOH I .   ? 0.2894 0.4666 0.6517 0.0087  0.0799  0.1604  637 HOH A O   
2555 O  O   . HOH I .   ? 0.6341 0.5613 0.3373 0.1821  0.0932  0.0015  638 HOH A O   
2556 O  O   . HOH I .   ? 0.5338 0.4751 0.3731 0.1046  0.0619  -0.1048 639 HOH A O   
2557 O  O   . HOH I .   ? 0.4548 0.2125 0.4731 -0.0164 -0.0873 0.0463  640 HOH A O   
2558 O  O   . HOH I .   ? 0.4341 0.3646 0.5160 0.1106  0.0342  0.0608  641 HOH A O   
2559 O  O   . HOH I .   ? 0.2969 0.4620 0.4426 -0.0241 0.0636  -0.0467 642 HOH A O   
2560 O  O   . HOH I .   ? 0.2922 0.3140 0.3795 -0.0137 0.1017  0.1136  643 HOH A O   
2561 O  O   . HOH I .   ? 0.3869 0.3285 0.2942 0.0007  0.0070  0.1102  644 HOH A O   
2562 O  O   . HOH I .   ? 0.3799 0.5001 0.3856 0.0421  0.0086  -0.1659 645 HOH A O   
2563 O  O   . HOH I .   ? 0.2664 0.3824 0.3630 -0.0085 0.0947  0.0498  646 HOH A O   
2564 O  O   . HOH I .   ? 0.3698 0.4023 0.5799 0.0894  0.0148  -0.0751 647 HOH A O   
2565 O  O   . HOH I .   ? 0.3357 0.2917 0.4357 0.0487  -0.0659 -0.0399 648 HOH A O   
2566 O  O   . HOH I .   ? 0.4684 0.3828 0.2157 -0.1070 -0.0293 -0.0167 649 HOH A O   
2567 O  O   . HOH I .   ? 0.3623 0.5400 0.6082 0.2069  0.0436  0.0798  650 HOH A O   
2568 O  O   . HOH I .   ? 0.3461 0.3492 0.3440 -0.0949 -0.0776 0.0234  651 HOH A O   
2569 O  O   . HOH I .   ? 0.3091 0.5360 0.3433 0.0399  -0.0260 -0.0935 652 HOH A O   
2570 O  O   . HOH I .   ? 0.3052 0.4296 0.3231 -0.0186 0.0432  0.0983  653 HOH A O   
2571 O  O   . HOH I .   ? 0.3964 0.3296 0.4591 -0.1718 0.0209  0.0509  654 HOH A O   
2572 O  O   . HOH I .   ? 0.4393 0.3892 0.5740 -0.0960 0.0988  0.0842  655 HOH A O   
2573 O  O   . HOH I .   ? 0.3055 0.2205 0.3551 0.0070  -0.1140 -0.0020 656 HOH A O   
2574 O  O   . HOH I .   ? 0.2741 0.3115 0.2962 -0.0238 0.0168  -0.0234 657 HOH A O   
2575 O  O   . HOH I .   ? 0.3282 0.3817 0.7911 0.0326  -0.2246 -0.1474 658 HOH A O   
2576 O  O   . HOH I .   ? 0.4614 0.2858 0.4821 -0.1899 -0.0104 0.0136  659 HOH A O   
2577 O  O   . HOH I .   ? 0.5016 0.3458 0.4458 0.0702  -0.0183 -0.1324 660 HOH A O   
2578 O  O   . HOH I .   ? 0.2536 0.3790 0.2912 -0.0026 -0.0021 0.0199  661 HOH A O   
2579 O  O   . HOH I .   ? 0.3152 0.4672 0.3177 -0.1277 -0.1037 0.0661  662 HOH A O   
2580 O  O   . HOH I .   ? 0.6797 1.1324 0.1816 -0.2384 -0.1096 0.0119  663 HOH A O   
2581 O  O   . HOH I .   ? 0.8313 0.4539 0.4837 0.0817  0.1746  -0.0892 664 HOH A O   
2582 O  O   . HOH I .   ? 0.4363 0.4799 0.5685 -0.0006 -0.0529 -0.1688 665 HOH A O   
2583 O  O   . HOH I .   ? 0.3499 0.6114 0.4736 0.1756  0.0419  0.0277  666 HOH A O   
2584 O  O   . HOH I .   ? 0.2194 0.4257 0.6369 0.0406  -0.0322 0.1254  667 HOH A O   
2585 O  O   . HOH I .   ? 0.4893 0.4169 0.4524 -0.0390 0.1218  0.0900  668 HOH A O   
# 
