data_3S8X
# 
_entry.id   3S8X 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_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   3S8X         pdb_00003s8x 10.2210/pdb3s8x/pdb 
RCSB  RCSB065909   ?            ?                   
WWPDB D_1000065909 ?            ?                   
# 
_pdbx_database_status.entry_id                        3S8X 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2011-05-31 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'     1 
'Manakova, E.'     2 
'Tamulaitiene, G.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            51 
_citation.page_first                259 
_citation.page_last                 270 
_citation.year                      2012 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22440859 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2012.02.050 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1 ? 
primary 'Zubriene, A.'      2 ? 
primary 'Baranauskiene, L.' 3 ? 
primary 'Tamulaitiene, G.'  4 ? 
primary 'Manakova, E.'      5 ? 
primary 'Kairys, V.'        6 ? 
primary 'Grazulis, S.'      7 ? 
primary 'Tumkevicius, S.'   8 ? 
primary 'Matulis, D.'       9 ? 
# 
_cell.entry_id           3S8X 
_cell.length_a           42.208 
_cell.length_b           41.180 
_cell.length_c           71.918 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.290 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3S8X 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                             29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                         65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                               78.133    2   ?       ? ? ? 
4 non-polymer syn BICINE                                                                             163.172   1   ?       ? ? ? 
5 non-polymer syn '4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' 339.390   1   ?       ? ? ? 
6 water       nat water                                                                              18.015    248 ?       ? ? ? 
# 
_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_
_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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3S8X 
_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 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                            ? 'C3 H7 N O2'       
89.093  
ARG 'L-peptide linking' y ARGININE                                                                           ? 'C6 H15 N4 O2 1'   
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                         ? 'C4 H8 N2 O3'      
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                    ? 'C4 H7 N O4'       
133.103 
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  
E59 non-polymer         . '4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' ? 'C13 H13 N3 O4 S2' 
339.390 
GLN 'L-peptide linking' y GLUTAMINE                                                                          ? 'C5 H10 N2 O3'     
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                    ? 'C5 H9 N O4'       
147.129 
GLY 'peptide linking'   y GLYCINE                                                                            ? 'C2 H5 N O2'       
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                          ? 'C6 H10 N3 O2 1'   
156.162 
HOH non-polymer         . WATER                                                                              ? 'H2 O'             
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                         ? 'C6 H13 N O2'      
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                            ? 'C6 H13 N O2'      
131.173 
LYS 'L-peptide linking' y LYSINE                                                                             ? 'C6 H15 N2 O2 1'   
147.195 
MET 'L-peptide linking' y METHIONINE                                                                         ? 'C5 H11 N O2 S'    
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                      ? 'C9 H11 N O2'      
165.189 
PRO 'L-peptide linking' y PROLINE                                                                            ? 'C5 H9 N O2'       
115.130 
SER 'L-peptide linking' y SERINE                                                                             ? 'C3 H7 N O3'       
105.093 
THR 'L-peptide linking' y THREONINE                                                                          ? 'C4 H9 N O3'       
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                         ? 'C11 H12 N2 O2'    
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                           ? 'C9 H11 N O3'      
181.189 
VAL 'L-peptide linking' y VALINE                                                                             ? 'C5 H11 N O2'      
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                         ? 'Zn 2'             
65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3S8X 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   40.13 
_exptl_crystal.density_Matthews      2.07 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.pH              9 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    'Na-Bicine 0.1M pH 9, Na-Malonate 2.2M pH 7, VAPOR DIFFUSION, temperature 298K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMosaic, 225 mm' 
_diffrn_detector.pdbx_collection_date   2010-11-14 
_diffrn_detector.details                'Detector swing-out angle up to 30 degrees' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Double crystal Si(111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9748 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X12' 
_diffrn_source.pdbx_wavelength_list        0.9748 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X12 
# 
_reflns.entry_id                     3S8X 
_reflns.d_resolution_high            1.300 
_reflns.d_resolution_low             41.180 
_reflns.number_all                   ? 
_reflns.number_obs                   56499 
_reflns.pdbx_Rmerge_I_obs            0.064 
_reflns.pdbx_netI_over_sigmaI        26.200 
_reflns.pdbx_Rsym_value              0.064 
_reflns.pdbx_redundancy              7.600 
_reflns.percent_possible_obs         95.900 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        12.15 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.30 1.37  ? 62158 ? 0.380 2.0  0.380 ? 7.70 ? 8022 93.60 1  1 
1.37 1.45  ? 59218 ? 0.266 2.8  0.266 ? 7.70 ? 7642 94.30 2  1 
1.45 1.55  ? 55760 ? 0.178 4.2  0.178 ? 7.80 ? 7192 94.80 3  1 
1.55 1.68  ? 52476 ? 0.127 5.7  0.127 ? 7.70 ? 6781 95.60 4  1 
1.68 1.84  ? 48820 ? 0.092 7.6  0.092 ? 7.70 ? 6322 96.30 5  1 
1.84 2.06  ? 44025 ? 0.069 9.5  0.069 ? 7.70 ? 5743 96.90 6  1 
2.06 2.37  ? 38599 ? 0.060 10.7 0.060 ? 7.60 ? 5088 97.50 7  1 
2.37 2.91  ? 32735 ? 0.055 11.3 0.055 ? 7.50 ? 4367 98.20 8  1 
2.91 4.11  ? 24905 ? 0.048 12.1 0.048 ? 7.30 ? 3418 98.70 9  1 
4.11 41.18 ? 13292 ? 0.046 12.0 0.046 ? 6.90 ? 1924 98.40 10 1 
# 
_refine.entry_id                                 3S8X 
_refine.ls_d_res_high                            1.300 
_refine.ls_d_res_low                             39.840 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    95.530 
_refine.ls_number_reflns_obs                     56478 
_refine.ls_number_reflns_all                     56499 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_obs                          0.146 
_refine.ls_R_factor_R_work                       0.142 
_refine.ls_wR_factor_R_work                      0.141 
_refine.ls_R_factor_R_free                       0.179 
_refine.ls_wR_factor_R_free                      0.177 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  5694 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               16.210 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.560 
_refine.aniso_B[2][2]                            0.540 
_refine.aniso_B[3][3]                            0.020 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.966 
_refine.overall_SU_R_Cruickshank_DPI             0.057 
_refine.overall_SU_R_free                        0.054 
_refine.pdbx_overall_ESU_R_Free                  0.054 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          MR 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.903 
_refine.B_iso_max                                49.13 
_refine.B_iso_min                                6.36 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          0 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.ls_R_factor_all                          ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_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         42 
_refine_hist.number_atoms_solvent             248 
_refine_hist.number_atoms_total               2339 
_refine_hist.d_res_high                       1.300 
_refine_hist.d_res_low                        39.840 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d         2261 0.028  0.022  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      3081 2.348  1.976  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   275  6.606  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   103  35.159 24.951 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   370  12.968 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   7    22.139 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           315  0.191  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     1769 0.015  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            1064 0.226  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          1517 0.322  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    208  0.149  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      5    0.083  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   65   0.190  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 41   0.189  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              1341 2.928  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             2178 3.836  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              920  4.992  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             903  6.284  4.500  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr       2261 3.305  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free        249  15.581 3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded      2192 9.391  3.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.300 
_refine_ls_shell.d_res_low                        1.334 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               92.890 
_refine_ls_shell.number_reflns_R_work             3642 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.217 
_refine_ls_shell.R_factor_R_free                  0.298 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             398 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                4040 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3S8X 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 4-{[(4-methyl-6-oxo-1,6-dihydro-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3S8X 
_struct_keywords.text            'drug design, carbonic anhydrase, sulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'lyase/lyase inhibitor' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 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  262 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  262 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  262 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E59 . N22 B ? A ZN  262 A E59 266 1_555 ? ? ? ? ? ? ? 1.933 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E59 . N22 A ? A ZN  262 A E59 266 1_555 ? ? ? ? ? ? ? 1.934 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 -6.06 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 8.68  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 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 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 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 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 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 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 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  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A DMS 263 ? 3  'BINDING SITE FOR RESIDUE DMS A 263' 
AC3 Software A DMS 264 ? 8  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A BCN 265 ? 6  'BINDING SITE FOR RESIDUE BCN A 265' 
AC5 Software A E59 266 ? 18 'BINDING SITE FOR RESIDUE E59 A 266' 
# 
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  E59 F .   ? E59 A 266 . ? 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 G .   ? HOH A 473 . ? 1_555 ? 
8  AC3 8  HIS A 4   ? HIS A 4   . ? 1_555 ? 
9  AC3 8  TRP A 5   ? TRP A 5   . ? 1_555 ? 
10 AC3 8  ASN A 11  ? ASN A 11  . ? 1_555 ? 
11 AC3 8  HIS A 15  ? HIS A 15  . ? 1_555 ? 
12 AC3 8  TRP A 16  ? TRP A 16  . ? 1_555 ? 
13 AC3 8  ASP A 19  ? ASP A 19  . ? 1_555 ? 
14 AC3 8  PHE A 20  ? PHE A 20  . ? 1_555 ? 
15 AC3 8  HOH G .   ? HOH A 432 . ? 1_655 ? 
16 AC4 6  LYS A 148 ? LYS A 149 . ? 1_555 ? 
17 AC4 6  LYS A 212 ? LYS A 213 . ? 1_555 ? 
18 AC4 6  PRO A 214 ? PRO A 215 . ? 1_555 ? 
19 AC4 6  HOH G .   ? HOH A 353 . ? 1_555 ? 
20 AC4 6  HOH G .   ? HOH A 364 . ? 1_555 ? 
21 AC4 6  HOH G .   ? HOH A 468 . ? 1_555 ? 
22 AC5 18 GLN A 92  ? GLN A 92  . ? 1_555 ? 
23 AC5 18 HIS A 94  ? HIS A 94  . ? 1_555 ? 
24 AC5 18 HIS A 96  ? HIS A 96  . ? 1_555 ? 
25 AC5 18 HIS A 119 ? HIS A 119 . ? 1_555 ? 
26 AC5 18 VAL A 121 ? VAL A 121 . ? 1_555 ? 
27 AC5 18 PHE A 130 ? PHE A 131 . ? 1_555 ? 
28 AC5 18 VAL A 134 ? VAL A 135 . ? 1_555 ? 
29 AC5 18 VAL A 142 ? VAL A 143 . ? 1_555 ? 
30 AC5 18 LEU A 197 ? LEU A 198 . ? 1_555 ? 
31 AC5 18 THR A 198 ? THR A 199 . ? 1_555 ? 
32 AC5 18 THR A 199 ? THR A 200 . ? 1_555 ? 
33 AC5 18 PRO A 200 ? PRO A 201 . ? 1_555 ? 
34 AC5 18 PRO A 201 ? PRO A 202 . ? 1_555 ? 
35 AC5 18 LEU A 203 ? LEU A 204 . ? 1_555 ? 
36 AC5 18 TRP A 208 ? TRP A 209 . ? 1_555 ? 
37 AC5 18 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
38 AC5 18 HOH G .   ? HOH A 390 . ? 1_555 ? 
39 AC5 18 HOH G .   ? HOH A 461 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3S8X 
_atom_sites.fract_transf_matrix[1][1]   0.023692 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006034 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024284 
_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]   0.014349 
_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  
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   ? 9.187   1.217   8.216   1.00 32.60 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.068  0.120   8.716   1.00 29.49 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.239   -0.869  9.477   1.00 24.71 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.389   -2.038  9.233   1.00 25.16 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 11.257  0.617   9.617   1.00 33.46 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 12.157  -0.483  10.187  1.00 35.71 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 12.297  -0.702  11.551  1.00 37.67 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 12.972  -1.391  9.583   1.00 41.45 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 13.117  -1.732  11.751  1.00 42.76 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 13.546  -2.168  10.575  1.00 39.74 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.354   -0.437  10.369  1.00 19.96 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.699   -1.435  11.237  1.00 15.75 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.667   -2.235  10.465  1.00 15.21 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.112   -1.738  9.442   1.00 15.80 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.032   -0.730  12.418  1.00 15.35 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.857   0.148   12.084  1.00 15.68 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.857   1.536   11.817  1.00 16.41 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.488   -0.297  12.020  1.00 13.84 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.547   1.909   11.575  1.00 16.48 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.692   0.813   11.693  1.00 13.90 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.860   -1.545  12.287  1.00 13.93 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.303   0.717   11.548  1.00 17.32 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.473   -1.641  12.085  1.00 14.94 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.706   -0.474  11.779  1.00 15.87 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.371   -3.444  10.950  1.00 14.67 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.280   -4.205  10.276  1.00 14.16 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.013   -5.371  11.214  1.00 14.89 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.015   -5.259  12.454  1.00 15.23 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.730   -6.511  10.600  1.00 16.56 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.313   -7.683  11.384  1.00 17.14 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.161   -8.886  11.002  1.00 21.03 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 4.742   -10.006 11.284  1.00 25.33 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 2.846   -7.978  11.050  1.00 16.00 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 1.944   -6.888  11.660  1.00 13.40 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.581   -6.971  13.060  1.00 13.72 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.453   -5.841  10.856  1.00 13.21 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.699   -5.959  13.604  1.00 10.87 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.580   -4.917  11.386  1.00 12.35 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.195   -4.970  12.744  1.00 11.16 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.672  -4.017  13.278  1.00 11.82 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.339   -8.717  10.408  1.00 21.19 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.267   -9.939  10.087  1.00 21.57 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.241   -10.221 11.246  1.00 24.84 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.210   -9.537  12.269  1.00 27.84 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.111   -11.219 11.080  1.00 30.28 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.115  -11.643 12.130  1.00 31.35 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.053  -10.540 12.340  1.00 29.19 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.576  -10.384 13.506  1.00 30.63 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 10.990  -12.839 11.704  1.00 32.35 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.033  -13.384 12.765  1.00 33.80 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 12.617  -14.797 12.273  1.00 35.15 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 14.136  -15.118 12.613  1.00 38.24 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 15.024  -15.760 11.423  1.00 39.24 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 11.217  -9.744  11.252  1.00 23.43 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.261  -8.780  11.325  1.00 21.77 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 11.811  -7.426  11.804  1.00 21.13 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.633  -6.637  12.249  1.00 22.61 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.175  -8.795  10.036  1.00 20.62 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 13.707  -10.213 9.710   1.00 25.42 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 14.636  -10.853 10.515  1.00 26.83 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 13.405  -11.109 8.713   1.00 27.37 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 14.898  -12.081 10.043  1.00 21.32 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 14.162  -12.256 8.935   1.00 27.50 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.488  -7.158  11.673  1.00 17.77 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.033  -5.827  11.989  1.00 16.87 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.692   -5.864  12.730  1.00 15.30 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.094   -4.816  12.889  1.00 17.29 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 9.838   -5.028  10.693  1.00 16.77 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 8.797   -5.648  9.755   1.00 17.60 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.254   -6.698  10.084  1.00 20.28 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.488   -4.994  8.635   1.00 19.36 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.403   -6.998  13.374  1.00 15.31 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.094   -7.130  14.041  1.00 15.85 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.091   -6.587  15.469  1.00 14.23 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 7.990   -5.902  15.940  1.00 14.25 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.022   -6.905  16.205  1.00 11.52 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.789   -6.313  17.506  1.00 12.32 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 6.944   -6.315  18.497  1.00 11.93 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.061   -5.364  19.297  1.00 13.30 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.566   -7.133  18.009  1.00 13.57 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.775   -7.407  16.800  1.00 13.09 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.833   -7.646  15.729  1.00 14.18 ? 13  PRO A CD  1 
ATOM   83   N  N   A GLU A 1 14  ? 7.771   -7.355  18.425  0.50 12.25 ? 14  GLU A N   1 
ATOM   84   N  N   B GLU A 1 14  ? 7.795   -7.353  18.563  0.50 12.80 ? 14  GLU A N   1 
ATOM   85   C  CA  A GLU A 1 14  ? 8.829   -7.556  19.352  0.50 12.61 ? 14  GLU A CA  1 
ATOM   86   C  CA  B GLU A 1 14  ? 8.842   -7.331  19.590  0.50 14.34 ? 14  GLU A CA  1 
ATOM   87   C  C   A GLU A 1 14  ? 10.006  -6.582  19.077  0.50 12.61 ? 14  GLU A C   1 
ATOM   88   C  C   B GLU A 1 14  ? 9.961   -6.351  19.214  0.50 14.53 ? 14  GLU A C   1 
ATOM   89   O  O   A GLU A 1 14  ? 10.939  -6.486  19.868  0.50 12.91 ? 14  GLU A O   1 
ATOM   90   O  O   B GLU A 1 14  ? 10.817  -6.039  20.092  0.50 15.57 ? 14  GLU A O   1 
ATOM   91   C  CB  A GLU A 1 14  ? 9.293   -9.035  19.264  0.50 14.19 ? 14  GLU A CB  1 
ATOM   92   C  CB  B GLU A 1 14  ? 9.502   -8.696  19.831  0.50 16.92 ? 14  GLU A CB  1 
ATOM   93   C  CG  A GLU A 1 14  ? 10.021  -9.429  18.084  0.50 14.58 ? 14  GLU A CG  1 
ATOM   94   C  CG  B GLU A 1 14  ? 8.486   -9.839  20.102  0.50 17.04 ? 14  GLU A CG  1 
ATOM   95   C  CD  A GLU A 1 14  ? 9.190   -9.987  16.920  0.50 16.99 ? 14  GLU A CD  1 
ATOM   96   C  CD  B GLU A 1 14  ? 7.452   -9.473  21.193  0.50 23.98 ? 14  GLU A CD  1 
ATOM   97   O  OE1 A GLU A 1 14  ? 8.007   -9.528  16.727  0.50 15.11 ? 14  GLU A OE1 1 
ATOM   98   O  OE1 B GLU A 1 14  ? 7.954   -9.037  22.250  0.50 27.26 ? 14  GLU A OE1 1 
ATOM   99   O  OE2 A GLU A 1 14  ? 9.834   -10.858 16.182  0.50 17.22 ? 14  GLU A OE2 1 
ATOM   100  O  OE2 B GLU A 1 14  ? 6.147   -9.648  21.003  0.50 23.59 ? 14  GLU A OE2 1 
ATOM   101  N  N   . HIS A 1 15  ? 9.942   -5.871  17.942  1.00 13.65 ? 15  HIS A N   1 
ATOM   102  C  CA  . HIS A 1 15  ? 10.946  -4.907  17.499  1.00 14.06 ? 15  HIS A CA  1 
ATOM   103  C  C   . HIS A 1 15  ? 10.493  -3.461  17.666  1.00 13.86 ? 15  HIS A C   1 
ATOM   104  O  O   . HIS A 1 15  ? 11.346  -2.551  17.638  1.00 13.41 ? 15  HIS A O   1 
ATOM   105  C  CB  . HIS A 1 15  ? 11.307  -5.076  16.010  1.00 15.08 ? 15  HIS A CB  1 
ATOM   106  C  CG  . HIS A 1 15  ? 12.008  -6.331  15.759  1.00 16.70 ? 15  HIS A CG  1 
ATOM   107  N  ND1 . HIS A 1 15  ? 13.378  -6.435  15.897  1.00 19.40 ? 15  HIS A ND1 1 
ATOM   108  C  CD2 . HIS A 1 15  ? 11.538  -7.539  15.362  1.00 17.22 ? 15  HIS A CD2 1 
ATOM   109  C  CE1 . HIS A 1 15  ? 13.726  -7.687  15.651  1.00 23.98 ? 15  HIS A CE1 1 
ATOM   110  N  NE2 . HIS A 1 15  ? 12.653  -8.363  15.279  1.00 21.23 ? 15  HIS A NE2 1 
ATOM   111  N  N   . TRP A 1 16  ? 9.185   -3.229  17.852  1.00 11.58 ? 16  TRP A N   1 
ATOM   112  C  CA  . TRP A 1 16  ? 8.705   -1.843  17.774  1.00 12.18 ? 16  TRP A CA  1 
ATOM   113  C  C   . TRP A 1 16  ? 9.275   -0.895  18.810  1.00 12.30 ? 16  TRP A C   1 
ATOM   114  O  O   . TRP A 1 16  ? 9.394   0.324   18.555  1.00 12.67 ? 16  TRP A O   1 
ATOM   115  C  CB  . TRP A 1 16  ? 7.168   -1.875  17.911  1.00 11.69 ? 16  TRP A CB  1 
ATOM   116  C  CG  . TRP A 1 16  ? 6.471   -2.551  16.786  1.00 10.86 ? 16  TRP A CG  1 
ATOM   117  C  CD1 . TRP A 1 16  ? 6.999   -3.004  15.578  1.00 11.66 ? 16  TRP A CD1 1 
ATOM   118  C  CD2 . TRP A 1 16  ? 5.063   -2.890  16.764  1.00 10.88 ? 16  TRP A CD2 1 
ATOM   119  N  NE1 . TRP A 1 16  ? 6.008   -3.599  14.828  1.00 11.89 ? 16  TRP A NE1 1 
ATOM   120  C  CE2 . TRP A 1 16  ? 4.804   -3.502  15.505  1.00 10.51 ? 16  TRP A CE2 1 
ATOM   121  C  CE3 . TRP A 1 16  ? 4.005   -2.681  17.644  1.00 10.83 ? 16  TRP A CE3 1 
ATOM   122  C  CZ2 . TRP A 1 16  ? 3.527   -3.913  15.110  1.00 11.08 ? 16  TRP A CZ2 1 
ATOM   123  C  CZ3 . TRP A 1 16  ? 2.733   -3.182  17.280  1.00 10.87 ? 16  TRP A CZ3 1 
ATOM   124  C  CH2 . TRP A 1 16  ? 2.498   -3.732  16.017  1.00 10.29 ? 16  TRP A CH2 1 
ATOM   125  N  N   . HIS A 1 17  ? 9.650   -1.444  19.966  1.00 11.23 ? 17  HIS A N   1 
ATOM   126  C  CA  . HIS A 1 17  ? 10.125  -0.590  21.056  1.00 11.76 ? 17  HIS A CA  1 
ATOM   127  C  C   . HIS A 1 17  ? 11.402  0.163   20.664  1.00 14.54 ? 17  HIS A C   1 
ATOM   128  O  O   . HIS A 1 17  ? 11.694  1.212   21.279  1.00 14.52 ? 17  HIS A O   1 
ATOM   129  C  CB  . HIS A 1 17  ? 10.418  -1.402  22.348  1.00 13.30 ? 17  HIS A CB  1 
ATOM   130  C  CG  . HIS A 1 17  ? 11.609  -2.277  22.227  1.00 14.15 ? 17  HIS A CG  1 
ATOM   131  N  ND1 . HIS A 1 17  ? 12.847  -1.914  22.737  1.00 18.20 ? 17  HIS A ND1 1 
ATOM   132  C  CD2 . HIS A 1 17  ? 11.770  -3.470  21.611  1.00 14.33 ? 17  HIS A CD2 1 
ATOM   133  C  CE1 . HIS A 1 17  ? 13.721  -2.872  22.466  1.00 17.59 ? 17  HIS A CE1 1 
ATOM   134  N  NE2 . HIS A 1 17  ? 13.111  -3.833  21.783  1.00 16.48 ? 17  HIS A NE2 1 
ATOM   135  N  N   . LYS A 1 18  ? 12.138  -0.322  19.691  1.00 13.82 ? 18  LYS A N   1 
ATOM   136  C  CA  . LYS A 1 18  ? 13.409  0.361   19.355  1.00 16.15 ? 18  LYS A CA  1 
ATOM   137  C  C   . LYS A 1 18  ? 13.117  1.689   18.640  1.00 16.50 ? 18  LYS A C   1 
ATOM   138  O  O   . LYS A 1 18  ? 13.889  2.622   18.787  1.00 19.93 ? 18  LYS A O   1 
ATOM   139  C  CB  . LYS A 1 18  ? 14.265  -0.512  18.434  1.00 16.40 ? 18  LYS A CB  1 
ATOM   140  C  CG  . LYS A 1 18  ? 14.846  -1.714  19.169  1.00 17.18 ? 18  LYS A CG  1 
ATOM   141  C  CD  . LYS A 1 18  ? 15.554  -2.652  18.235  1.00 17.29 ? 18  LYS A CD  1 
ATOM   142  C  CE  . LYS A 1 18  ? 14.592  -3.629  17.540  1.00 15.76 ? 18  LYS A CE  1 
ATOM   143  N  NZ  . LYS A 1 18  ? 15.252  -4.506  16.496  1.00 16.60 ? 18  LYS A NZ  1 
ATOM   144  N  N   . ASP A 1 19  ? 12.040  1.828   17.859  1.00 14.65 ? 19  ASP A N   1 
ATOM   145  C  CA  . ASP A 1 19  ? 11.689  3.159   17.320  1.00 14.75 ? 19  ASP A CA  1 
ATOM   146  C  C   . ASP A 1 19  ? 10.593  3.836   18.121  1.00 15.16 ? 19  ASP A C   1 
ATOM   147  O  O   . ASP A 1 19  ? 10.479  5.047   17.984  1.00 17.00 ? 19  ASP A O   1 
ATOM   148  C  CB  . ASP A 1 19  ? 11.304  3.010   15.834  1.00 18.19 ? 19  ASP A CB  1 
ATOM   149  C  CG  . ASP A 1 19  ? 12.537  2.719   14.948  1.00 21.26 ? 19  ASP A CG  1 
ATOM   150  O  OD1 . ASP A 1 19  ? 13.269  3.727   14.768  1.00 23.04 ? 19  ASP A OD1 1 
ATOM   151  O  OD2 . ASP A 1 19  ? 12.915  1.500   14.748  1.00 29.74 ? 19  ASP A OD2 1 
ATOM   152  N  N   . PHE A 1 20  ? 9.841   3.064   18.924  1.00 13.60 ? 20  PHE A N   1 
ATOM   153  C  CA  . PHE A 1 20  ? 8.729   3.642   19.670  1.00 13.47 ? 20  PHE A CA  1 
ATOM   154  C  C   . PHE A 1 20  ? 8.809   3.192   21.096  1.00 12.98 ? 20  PHE A C   1 
ATOM   155  O  O   . PHE A 1 20  ? 8.158   2.180   21.464  1.00 12.54 ? 20  PHE A O   1 
ATOM   156  C  CB  . PHE A 1 20  ? 7.392   3.128   19.008  1.00 14.35 ? 20  PHE A CB  1 
ATOM   157  C  CG  . PHE A 1 20  ? 7.294   3.554   17.557  1.00 13.24 ? 20  PHE A CG  1 
ATOM   158  C  CD1 . PHE A 1 20  ? 6.971   4.857   17.180  1.00 15.91 ? 20  PHE A CD1 1 
ATOM   159  C  CD2 . PHE A 1 20  ? 7.732   2.649   16.524  1.00 15.06 ? 20  PHE A CD2 1 
ATOM   160  C  CE1 . PHE A 1 20  ? 6.975   5.194   15.778  1.00 15.61 ? 20  PHE A CE1 1 
ATOM   161  C  CE2 . PHE A 1 20  ? 7.770   2.988   15.203  1.00 17.08 ? 20  PHE A CE2 1 
ATOM   162  C  CZ  . PHE A 1 20  ? 7.388   4.249   14.826  1.00 17.38 ? 20  PHE A CZ  1 
ATOM   163  N  N   . PRO A 1 21  ? 9.699   3.782   21.922  1.00 14.30 ? 21  PRO A N   1 
ATOM   164  C  CA  . PRO A 1 21  ? 9.936   3.232   23.272  1.00 13.51 ? 21  PRO A CA  1 
ATOM   165  C  C   . PRO A 1 21  ? 8.711   3.147   24.153  1.00 13.00 ? 21  PRO A C   1 
ATOM   166  O  O   . PRO A 1 21  ? 8.725   2.370   25.138  1.00 13.68 ? 21  PRO A O   1 
ATOM   167  C  CB  . PRO A 1 21  ? 11.044  4.174   23.898  1.00 16.04 ? 21  PRO A CB  1 
ATOM   168  C  CG  . PRO A 1 21  ? 11.194  5.240   22.869  1.00 19.38 ? 21  PRO A CG  1 
ATOM   169  C  CD  . PRO A 1 21  ? 10.673  4.832   21.548  1.00 14.50 ? 21  PRO A CD  1 
ATOM   170  N  N   A ILE A 1 22  ? 7.629   3.913   23.879  0.50 11.85 ? 22  ILE A N   1 
ATOM   171  N  N   B ILE A 1 22  ? 7.661   3.905   23.792  0.50 11.96 ? 22  ILE A N   1 
ATOM   172  C  CA  A ILE A 1 22  ? 6.408   3.764   24.720  0.50 11.30 ? 22  ILE A CA  1 
ATOM   173  C  CA  B ILE A 1 22  ? 6.408   3.872   24.533  0.50 11.40 ? 22  ILE A CA  1 
ATOM   174  C  C   A ILE A 1 22  ? 5.853   2.344   24.557  0.50 10.61 ? 22  ILE A C   1 
ATOM   175  C  C   B ILE A 1 22  ? 5.773   2.464   24.412  0.50 10.65 ? 22  ILE A C   1 
ATOM   176  O  O   A ILE A 1 22  ? 4.997   1.941   25.369  0.50 9.69  ? 22  ILE A O   1 
ATOM   177  O  O   B ILE A 1 22  ? 4.791   2.199   25.108  0.50 12.37 ? 22  ILE A O   1 
ATOM   178  C  CB  A ILE A 1 22  ? 5.306   4.800   24.368  0.50 11.02 ? 22  ILE A CB  1 
ATOM   179  C  CB  B ILE A 1 22  ? 5.495   5.037   24.020  0.50 11.02 ? 22  ILE A CB  1 
ATOM   180  C  CG1 A ILE A 1 22  ? 4.286   4.931   25.516  0.50 13.48 ? 22  ILE A CG1 1 
ATOM   181  C  CG1 B ILE A 1 22  ? 4.408   5.377   25.057  0.50 10.75 ? 22  ILE A CG1 1 
ATOM   182  C  CG2 A ILE A 1 22  ? 4.634   4.445   23.032  0.50 11.63 ? 22  ILE A CG2 1 
ATOM   183  C  CG2 B ILE A 1 22  ? 4.963   4.668   22.607  0.50 11.21 ? 22  ILE A CG2 1 
ATOM   184  C  CD1 A ILE A 1 22  ? 4.853   5.826   26.601  0.50 17.94 ? 22  ILE A CD1 1 
ATOM   185  C  CD1 B ILE A 1 22  ? 3.378   6.380   24.784  0.50 11.44 ? 22  ILE A CD1 1 
ATOM   186  N  N   . ALA A 1 23  ? 6.342   1.580   23.557  1.00 11.56 ? 23  ALA A N   1 
ATOM   187  C  CA  . ALA A 1 23  ? 5.900   0.155   23.470  1.00 11.59 ? 23  ALA A CA  1 
ATOM   188  C  C   . ALA A 1 23  ? 5.981   -0.560  24.785  1.00 12.12 ? 23  ALA A C   1 
ATOM   189  O  O   . ALA A 1 23  ? 5.240   -1.565  25.020  1.00 12.01 ? 23  ALA A O   1 
ATOM   190  C  CB  . ALA A 1 23  ? 6.751   -0.606  22.454  1.00 12.76 ? 23  ALA A CB  1 
ATOM   191  N  N   . LYS A 1 24  ? 6.893   -0.108  25.668  1.00 13.28 ? 24  LYS A N   1 
ATOM   192  C  CA  . LYS A 1 24  ? 7.072   -0.738  26.968  1.00 13.27 ? 24  LYS A CA  1 
ATOM   193  C  C   . LYS A 1 24  ? 6.472   0.149   28.052  1.00 15.49 ? 24  LYS A C   1 
ATOM   194  O  O   . LYS A 1 24  ? 6.887   0.014   29.233  1.00 16.82 ? 24  LYS A O   1 
ATOM   195  C  CB  . LYS A 1 24  ? 8.559   -0.982  27.220  1.00 14.44 ? 24  LYS A CB  1 
ATOM   196  C  CG  . LYS A 1 24  ? 9.193   -1.977  26.268  1.00 17.62 ? 24  LYS A CG  1 
ATOM   197  C  CD  . LYS A 1 24  ? 10.588  -2.325  26.761  1.00 21.19 ? 24  LYS A CD  1 
ATOM   198  C  CE  . LYS A 1 24  ? 11.366  -3.210  25.794  1.00 25.57 ? 24  LYS A CE  1 
ATOM   199  N  NZ  . LYS A 1 24  ? 11.008  -4.587  26.104  1.00 29.80 ? 24  LYS A NZ  1 
ATOM   200  N  N   . GLY A 1 25  ? 5.450   0.954   27.710  1.00 13.28 ? 25  GLY A N   1 
ATOM   201  C  CA  . GLY A 1 25  ? 4.858   1.885   28.695  1.00 15.08 ? 25  GLY A CA  1 
ATOM   202  C  C   . GLY A 1 25  ? 3.891   1.270   29.664  1.00 13.40 ? 25  GLY A C   1 
ATOM   203  O  O   . GLY A 1 25  ? 3.713   0.032   29.751  1.00 14.73 ? 25  GLY A O   1 
ATOM   204  N  N   . GLU A 1 26  ? 3.219   2.194   30.355  1.00 14.49 ? 26  GLU A N   1 
ATOM   205  C  CA  . GLU A 1 26  ? 2.331   1.791   31.429  1.00 14.78 ? 26  GLU A CA  1 
ATOM   206  C  C   . GLU A 1 26  ? 0.901   1.555   31.050  1.00 13.32 ? 26  GLU A C   1 
ATOM   207  O  O   . GLU A 1 26  ? 0.125   1.075   31.916  1.00 13.79 ? 26  GLU A O   1 
ATOM   208  C  CB  . GLU A 1 26  ? 2.339   2.865   32.597  1.00 16.60 ? 26  GLU A CB  1 
ATOM   209  C  CG  . GLU A 1 26  ? 3.783   3.145   33.147  1.00 20.43 ? 26  GLU A CG  1 
ATOM   210  C  CD  . GLU A 1 26  ? 4.344   1.858   33.782  1.00 22.89 ? 26  GLU A CD  1 
ATOM   211  O  OE1 . GLU A 1 26  ? 3.647   1.264   34.652  1.00 27.52 ? 26  GLU A OE1 1 
ATOM   212  O  OE2 . GLU A 1 26  ? 5.441   1.431   33.346  1.00 29.16 ? 26  GLU A OE2 1 
ATOM   213  N  N   . ARG A 1 27  ? 0.493   1.897   29.804  1.00 11.34 ? 27  ARG A N   1 
ATOM   214  C  CA  . ARG A 1 27  ? -0.913  1.690   29.466  1.00 10.59 ? 27  ARG A CA  1 
ATOM   215  C  C   . ARG A 1 27  ? -0.970  1.240   27.993  1.00 9.99  ? 27  ARG A C   1 
ATOM   216  O  O   . ARG A 1 27  ? -1.657  1.827   27.137  1.00 9.64  ? 27  ARG A O   1 
ATOM   217  C  CB  . ARG A 1 27  ? -1.793  2.961   29.776  1.00 13.84 ? 27  ARG A CB  1 
ATOM   218  C  CG  . ARG A 1 27  ? -1.427  4.266   29.065  1.00 15.73 ? 27  ARG A CG  1 
ATOM   219  C  CD  . ARG A 1 27  ? -2.457  5.383   29.365  1.00 18.33 ? 27  ARG A CD  1 
ATOM   220  N  NE  . ARG A 1 27  ? -3.632  5.303   28.495  1.00 16.48 ? 27  ARG A NE  1 
ATOM   221  C  CZ  . ARG A 1 27  ? -4.550  6.257   28.360  1.00 14.23 ? 27  ARG A CZ  1 
ATOM   222  N  NH1 . ARG A 1 27  ? -4.448  7.397   29.034  1.00 16.95 ? 27  ARG A NH1 1 
ATOM   223  N  NH2 . ARG A 1 27  ? -5.574  6.075   27.541  1.00 13.79 ? 27  ARG A NH2 1 
ATOM   224  N  N   . GLN A 1 28  ? -0.225  0.160   27.699  1.00 9.50  ? 28  GLN A N   1 
ATOM   225  C  CA  . GLN A 1 28  ? -0.220  -0.387  26.342  1.00 8.93  ? 28  GLN A CA  1 
ATOM   226  C  C   . GLN A 1 28  ? -1.397  -1.331  26.067  1.00 8.38  ? 28  GLN A C   1 
ATOM   227  O  O   . GLN A 1 28  ? -1.888  -2.036  26.988  1.00 9.01  ? 28  GLN A O   1 
ATOM   228  C  CB  . GLN A 1 28  ? 1.128   -1.113  26.055  1.00 9.26  ? 28  GLN A CB  1 
ATOM   229  C  CG  . GLN A 1 28  ? 2.286   -0.024  26.016  1.00 9.58  ? 28  GLN A CG  1 
ATOM   230  C  CD  . GLN A 1 28  ? 2.179   0.846   24.746  1.00 10.43 ? 28  GLN A CD  1 
ATOM   231  O  OE1 . GLN A 1 28  ? 2.323   0.280   23.660  1.00 10.01 ? 28  GLN A OE1 1 
ATOM   232  N  NE2 . GLN A 1 28  ? 1.787   2.117   24.851  1.00 10.39 ? 28  GLN A NE2 1 
ATOM   233  N  N   . SER A 1 29  ? -1.752  -1.420  24.785  1.00 7.72  ? 29  SER A N   1 
ATOM   234  C  CA  . SER A 1 29  ? -2.828  -2.291  24.300  1.00 7.92  ? 29  SER A CA  1 
ATOM   235  C  C   . SER A 1 29  ? -2.257  -3.167  23.182  1.00 8.13  ? 29  SER A C   1 
ATOM   236  O  O   . SER A 1 29  ? -1.331  -2.777  22.492  1.00 8.33  ? 29  SER A O   1 
ATOM   237  C  CB  . SER A 1 29  ? -3.964  -1.423  23.746  1.00 7.67  ? 29  SER A CB  1 
ATOM   238  O  OG  . SER A 1 29  ? -4.573  -0.704  24.869  1.00 7.95  ? 29  SER A OG  1 
ATOM   239  N  N   . PRO A 1 30  ? -2.922  -4.315  22.870  1.00 7.37  ? 30  PRO A N   1 
ATOM   240  C  CA  . PRO A 1 30  ? -4.091  -4.853  23.615  1.00 7.45  ? 30  PRO A CA  1 
ATOM   241  C  C   . PRO A 1 30  ? -3.707  -5.514  24.959  1.00 7.54  ? 30  PRO A C   1 
ATOM   242  O  O   . PRO A 1 30  ? -2.474  -5.525  25.303  1.00 8.33  ? 30  PRO A O   1 
ATOM   243  C  CB  . PRO A 1 30  ? -4.631  -5.866  22.628  1.00 7.06  ? 30  PRO A CB  1 
ATOM   244  C  CG  . PRO A 1 30  ? -3.382  -6.459  22.037  1.00 8.21  ? 30  PRO A CG  1 
ATOM   245  C  CD  . PRO A 1 30  ? -2.430  -5.238  21.862  1.00 7.72  ? 30  PRO A CD  1 
ATOM   246  N  N   . VAL A 1 31  ? -4.695  -6.062  25.688  1.00 7.49  ? 31  VAL A N   1 
ATOM   247  C  CA  . VAL A 1 31  ? -4.492  -6.820  26.873  1.00 7.42  ? 31  VAL A CA  1 
ATOM   248  C  C   . VAL A 1 31  ? -5.385  -8.052  26.803  1.00 8.49  ? 31  VAL A C   1 
ATOM   249  O  O   . VAL A 1 31  ? -6.350  -8.117  26.057  1.00 8.46  ? 31  VAL A O   1 
ATOM   250  C  CB  . VAL A 1 31  ? -4.801  -6.014  28.154  1.00 9.33  ? 31  VAL A CB  1 
ATOM   251  C  CG1 . VAL A 1 31  ? -3.873  -4.782  28.224  1.00 11.09 ? 31  VAL A CG1 1 
ATOM   252  C  CG2 . VAL A 1 31  ? -6.254  -5.550  28.219  1.00 10.71 ? 31  VAL A CG2 1 
ATOM   253  N  N   . ASP A 1 32  ? -5.062  -9.018  27.695  1.00 8.99  ? 32  ASP A N   1 
ATOM   254  C  CA  . ASP A 1 32  ? -5.952  -10.096 27.982  1.00 8.87  ? 32  ASP A CA  1 
ATOM   255  C  C   . ASP A 1 32  ? -7.019  -9.614  28.945  1.00 8.98  ? 32  ASP A C   1 
ATOM   256  O  O   . ASP A 1 32  ? -6.723  -8.916  29.980  1.00 10.65 ? 32  ASP A O   1 
ATOM   257  C  CB  . ASP A 1 32  ? -5.200  -11.292 28.547  1.00 10.01 ? 32  ASP A CB  1 
ATOM   258  C  CG  . ASP A 1 32  ? -6.175  -12.475 28.870  1.00 9.95  ? 32  ASP A CG  1 
ATOM   259  O  OD1 . ASP A 1 32  ? -6.851  -12.902 27.957  1.00 9.90  ? 32  ASP A OD1 1 
ATOM   260  O  OD2 . ASP A 1 32  ? -6.191  -12.896 30.084  1.00 13.40 ? 32  ASP A OD2 1 
ATOM   261  N  N   . ILE A 1 33  ? -8.292  -9.908  28.612  1.00 8.44  ? 33  ILE A N   1 
ATOM   262  C  CA  . ILE A 1 33  ? -9.384  -9.509  29.494  1.00 9.28  ? 33  ILE A CA  1 
ATOM   263  C  C   . ILE A 1 33  ? -9.726  -10.741 30.367  1.00 11.27 ? 33  ILE A C   1 
ATOM   264  O  O   . ILE A 1 33  ? -10.234 -11.762 29.898  1.00 12.05 ? 33  ILE A O   1 
ATOM   265  C  CB  . ILE A 1 33  ? -10.606 -9.090  28.691  1.00 10.19 ? 33  ILE A CB  1 
ATOM   266  C  CG1 . ILE A 1 33  ? -10.212 -7.848  27.886  1.00 9.55  ? 33  ILE A CG1 1 
ATOM   267  C  CG2 . ILE A 1 33  ? -11.808 -8.806  29.649  1.00 11.15 ? 33  ILE A CG2 1 
ATOM   268  C  CD1 . ILE A 1 33  ? -11.272 -7.593  26.726  1.00 12.05 ? 33  ILE A CD1 1 
ATOM   269  N  N   . ASP A 1 34  ? -9.280  -10.698 31.591  1.00 11.24 ? 34  ASP A N   1 
ATOM   270  C  CA  . ASP A 1 34  ? -9.564  -11.778 32.552  1.00 12.93 ? 34  ASP A CA  1 
ATOM   271  C  C   . ASP A 1 34  ? -11.008 -11.535 33.063  1.00 13.15 ? 34  ASP A C   1 
ATOM   272  O  O   . ASP A 1 34  ? -11.251 -10.545 33.800  1.00 14.83 ? 34  ASP A O   1 
ATOM   273  C  CB  . ASP A 1 34  ? -8.509  -11.711 33.715  1.00 14.94 ? 34  ASP A CB  1 
ATOM   274  C  CG  . ASP A 1 34  ? -8.765  -12.727 34.810  1.00 18.74 ? 34  ASP A CG  1 
ATOM   275  O  OD1 . ASP A 1 34  ? -9.875  -13.129 35.057  1.00 20.94 ? 34  ASP A OD1 1 
ATOM   276  O  OD2 . ASP A 1 34  ? -7.787  -12.987 35.536  1.00 27.03 ? 34  ASP A OD2 1 
ATOM   277  N  N   . THR A 1 35  ? -11.991 -12.287 32.585  1.00 15.12 ? 35  THR A N   1 
ATOM   278  C  CA  . THR A 1 35  ? -13.368 -11.938 32.869  1.00 16.58 ? 35  THR A CA  1 
ATOM   279  C  C   . THR A 1 35  ? -13.744 -12.093 34.281  1.00 16.29 ? 35  THR A C   1 
ATOM   280  O  O   . THR A 1 35  ? -14.726 -11.434 34.754  1.00 18.59 ? 35  THR A O   1 
ATOM   281  C  CB  . THR A 1 35  ? -14.315 -12.855 32.051  1.00 17.35 ? 35  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 35  ? -14.178 -14.214 32.562  1.00 17.69 ? 35  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 35  ? -13.991 -12.822 30.554  1.00 17.10 ? 35  THR A CG2 1 
ATOM   284  N  N   . HIS A 1 36  ? -13.031 -12.940 35.029  1.00 18.29 ? 36  HIS A N   1 
ATOM   285  C  CA  . HIS A 1 36  ? -13.323 -13.084 36.480  1.00 17.63 ? 36  HIS A CA  1 
ATOM   286  C  C   . HIS A 1 36  ? -12.845 -11.983 37.300  1.00 20.29 ? 36  HIS A C   1 
ATOM   287  O  O   . HIS A 1 36  ? -13.603 -11.636 38.236  1.00 21.75 ? 36  HIS A O   1 
ATOM   288  C  CB  . HIS A 1 36  ? -12.696 -14.352 36.981  1.00 19.83 ? 36  HIS A CB  1 
ATOM   289  C  CG  . HIS A 1 36  ? -13.290 -15.485 36.310  1.00 21.78 ? 36  HIS A CG  1 
ATOM   290  N  ND1 . HIS A 1 36  ? -12.615 -16.131 35.274  1.00 26.50 ? 36  HIS A ND1 1 
ATOM   291  C  CD2 . HIS A 1 36  ? -14.566 -15.940 36.290  1.00 23.67 ? 36  HIS A CD2 1 
ATOM   292  C  CE1 . HIS A 1 36  ? -13.401 -17.036 34.751  1.00 21.25 ? 36  HIS A CE1 1 
ATOM   293  N  NE2 . HIS A 1 36  ? -14.589 -16.954 35.331  1.00 22.59 ? 36  HIS A NE2 1 
ATOM   294  N  N   . THR A 1 37  ? -11.757 -11.262 36.889  1.00 18.65 ? 37  THR A N   1 
ATOM   295  C  CA  . THR A 1 37  ? -11.293 -10.144 37.702  1.00 20.43 ? 37  THR A CA  1 
ATOM   296  C  C   . THR A 1 37  ? -11.720 -8.770  37.213  1.00 16.62 ? 37  THR A C   1 
ATOM   297  O  O   . THR A 1 37  ? -11.520 -7.783  37.963  1.00 20.03 ? 37  THR A O   1 
ATOM   298  C  CB  . THR A 1 37  ? -9.843  -10.081 37.959  1.00 22.48 ? 37  THR A CB  1 
ATOM   299  O  OG1 . THR A 1 37  ? -9.124  -10.023 36.772  1.00 27.02 ? 37  THR A OG1 1 
ATOM   300  C  CG2 . THR A 1 37  ? -9.357  -11.430 38.414  1.00 22.41 ? 37  THR A CG2 1 
ATOM   301  N  N   . ALA A 1 38  ? -12.365 -8.712  36.053  1.00 16.66 ? 38  ALA A N   1 
ATOM   302  C  CA  . ALA A 1 38  ? -12.943 -7.416  35.556  1.00 15.10 ? 38  ALA A CA  1 
ATOM   303  C  C   . ALA A 1 38  ? -14.043 -7.115  36.583  1.00 17.11 ? 38  ALA A C   1 
ATOM   304  O  O   . ALA A 1 38  ? -14.741 -8.006  37.054  1.00 22.07 ? 38  ALA A O   1 
ATOM   305  C  CB  . ALA A 1 38  ? -13.533 -7.606  34.165  1.00 15.31 ? 38  ALA A CB  1 
ATOM   306  N  N   . LYS A 1 39  ? -14.147 -5.858  36.983  1.00 17.29 ? 39  LYS A N   1 
ATOM   307  C  CA  . LYS A 1 39  ? -15.096 -5.436  38.016  1.00 18.51 ? 39  LYS A CA  1 
ATOM   308  C  C   . LYS A 1 39  ? -16.377 -4.899  37.322  1.00 15.58 ? 39  LYS A C   1 
ATOM   309  O  O   . LYS A 1 39  ? -16.311 -3.918  36.589  1.00 14.96 ? 39  LYS A O   1 
ATOM   310  C  CB  . LYS A 1 39  ? -14.373 -4.284  38.757  1.00 20.46 ? 39  LYS A CB  1 
ATOM   311  C  CG  . LYS A 1 39  ? -15.186 -3.494  39.716  1.00 24.18 ? 39  LYS A CG  1 
ATOM   312  C  CD  . LYS A 1 39  ? -15.291 -4.155  41.087  1.00 23.93 ? 39  LYS A CD  1 
ATOM   313  C  CE  . LYS A 1 39  ? -16.061 -3.240  41.986  1.00 29.39 ? 39  LYS A CE  1 
ATOM   314  N  NZ  . LYS A 1 39  ? -16.405 -3.861  43.258  1.00 29.15 ? 39  LYS A NZ  1 
ATOM   315  N  N   . TYR A 1 40  ? -17.519 -5.421  37.663  1.00 18.19 ? 40  TYR A N   1 
ATOM   316  C  CA  . TYR A 1 40  ? -18.768 -4.823  37.227  1.00 17.18 ? 40  TYR A CA  1 
ATOM   317  C  C   . TYR A 1 40  ? -18.870 -3.424  37.865  1.00 16.25 ? 40  TYR A C   1 
ATOM   318  O  O   . TYR A 1 40  ? -18.680 -3.195  39.082  1.00 17.29 ? 40  TYR A O   1 
ATOM   319  C  CB  . TYR A 1 40  ? -19.942 -5.689  37.691  1.00 18.99 ? 40  TYR A CB  1 
ATOM   320  C  CG  . TYR A 1 40  ? -21.274 -4.995  37.563  1.00 21.29 ? 40  TYR A CG  1 
ATOM   321  C  CD1 . TYR A 1 40  ? -21.702 -4.515  36.336  1.00 22.84 ? 40  TYR A CD1 1 
ATOM   322  C  CD2 . TYR A 1 40  ? -22.096 -4.790  38.665  1.00 28.23 ? 40  TYR A CD2 1 
ATOM   323  C  CE1 . TYR A 1 40  ? -22.918 -3.859  36.202  1.00 24.83 ? 40  TYR A CE1 1 
ATOM   324  C  CE2 . TYR A 1 40  ? -23.322 -4.133  38.538  1.00 27.86 ? 40  TYR A CE2 1 
ATOM   325  C  CZ  . TYR A 1 40  ? -23.726 -3.668  37.299  1.00 25.77 ? 40  TYR A CZ  1 
ATOM   326  O  OH  . TYR A 1 40  ? -24.934 -3.014  37.148  1.00 28.95 ? 40  TYR A OH  1 
ATOM   327  N  N   . ASP A 1 41  ? -19.170 -2.437  37.027  1.00 15.58 ? 41  ASP A N   1 
ATOM   328  C  CA  . ASP A 1 41  ? -19.241 -1.042  37.581  1.00 15.78 ? 41  ASP A CA  1 
ATOM   329  C  C   . ASP A 1 41  ? -20.662 -0.597  37.271  1.00 20.21 ? 41  ASP A C   1 
ATOM   330  O  O   . ASP A 1 41  ? -20.972 -0.274  36.112  1.00 18.83 ? 41  ASP A O   1 
ATOM   331  C  CB  . ASP A 1 41  ? -18.224 -0.167  36.852  1.00 18.73 ? 41  ASP A CB  1 
ATOM   332  C  CG  . ASP A 1 41  ? -18.214 1.257   37.379  1.00 23.34 ? 41  ASP A CG  1 
ATOM   333  O  OD1 . ASP A 1 41  ? -19.127 1.573   38.174  1.00 23.51 ? 41  ASP A OD1 1 
ATOM   334  O  OD2 . ASP A 1 41  ? -17.256 2.000   37.014  1.00 27.14 ? 41  ASP A OD2 1 
ATOM   335  N  N   . PRO A 1 42  ? -21.542 -0.554  38.298  1.00 22.76 ? 42  PRO A N   1 
ATOM   336  C  CA  . PRO A 1 42  ? -22.931 -0.171  38.047  1.00 25.05 ? 42  PRO A CA  1 
ATOM   337  C  C   . PRO A 1 42  ? -23.019 1.340   37.723  1.00 24.53 ? 42  PRO A C   1 
ATOM   338  O  O   . PRO A 1 42  ? -24.108 1.785   37.309  1.00 29.19 ? 42  PRO A O   1 
ATOM   339  C  CB  . PRO A 1 42  ? -23.646 -0.532  39.385  1.00 27.50 ? 42  PRO A CB  1 
ATOM   340  C  CG  . PRO A 1 42  ? -22.508 -0.166  40.466  1.00 25.76 ? 42  PRO A CG  1 
ATOM   341  C  CD  . PRO A 1 42  ? -21.261 -0.799  39.743  1.00 24.11 ? 42  PRO A CD  1 
ATOM   342  N  N   . SER A 1 43  ? -21.916 2.113   37.828  1.00 23.14 ? 43  SER A N   1 
ATOM   343  C  CA  . SER A 1 43  ? -21.912 3.567   37.442  1.00 25.27 ? 43  SER A CA  1 
ATOM   344  C  C   . SER A 1 43  ? -21.710 3.738   35.917  1.00 24.76 ? 43  SER A C   1 
ATOM   345  O  O   . SER A 1 43  ? -21.864 4.872   35.378  1.00 26.77 ? 43  SER A O   1 
ATOM   346  C  CB  . SER A 1 43  ? -20.810 4.401   38.186  1.00 26.24 ? 43  SER A CB  1 
ATOM   347  O  OG  . SER A 1 43  ? -19.501 4.201   37.691  1.00 30.59 ? 43  SER A OG  1 
ATOM   348  N  N   . LEU A 1 44  ? -21.327 2.655   35.215  1.00 24.26 ? 44  LEU A N   1 
ATOM   349  C  CA  . LEU A 1 44  ? -21.052 2.749   33.750  1.00 21.76 ? 44  LEU A CA  1 
ATOM   350  C  C   . LEU A 1 44  ? -22.387 2.887   33.039  1.00 23.63 ? 44  LEU A C   1 
ATOM   351  O  O   . LEU A 1 44  ? -23.360 2.299   33.475  1.00 25.53 ? 44  LEU A O   1 
ATOM   352  C  CB  . LEU A 1 44  ? -20.370 1.473   33.270  1.00 20.62 ? 44  LEU A CB  1 
ATOM   353  C  CG  . LEU A 1 44  ? -18.901 1.525   33.500  1.00 19.26 ? 44  LEU A CG  1 
ATOM   354  C  CD1 . LEU A 1 44  ? -18.405 0.151   32.987  1.00 17.64 ? 44  LEU A CD1 1 
ATOM   355  C  CD2 . LEU A 1 44  ? -18.157 2.646   32.769  1.00 18.77 ? 44  LEU A CD2 1 
ATOM   356  N  N   . LYS A 1 45  ? -22.441 3.681   31.955  1.00 22.01 ? 45  LYS A N   1 
ATOM   357  C  CA  . LYS A 1 45  ? -23.727 3.860   31.256  1.00 23.21 ? 45  LYS A CA  1 
ATOM   358  C  C   . LYS A 1 45  ? -23.783 2.996   30.044  1.00 19.69 ? 45  LYS A C   1 
ATOM   359  O  O   . LYS A 1 45  ? -22.720 2.499   29.614  1.00 20.56 ? 45  LYS A O   1 
ATOM   360  C  CB  . LYS A 1 45  ? -23.861 5.254   30.826  1.00 21.70 ? 45  LYS A CB  1 
ATOM   361  C  CG  . LYS A 1 45  ? -23.700 6.252   31.931  1.00 26.22 ? 45  LYS A CG  1 
ATOM   362  C  CD  . LYS A 1 45  ? -23.549 7.615   31.365  1.00 32.24 ? 45  LYS A CD  1 
ATOM   363  C  CE  . LYS A 1 45  ? -22.930 8.592   32.421  1.00 36.67 ? 45  LYS A CE  1 
ATOM   364  N  NZ  . LYS A 1 45  ? -23.869 8.712   33.591  1.00 39.43 ? 45  LYS A NZ  1 
ATOM   365  N  N   . PRO A 1 46  ? -25.010 2.764   29.527  1.00 18.96 ? 46  PRO A N   1 
ATOM   366  C  CA  . PRO A 1 46  ? -25.101 2.105   28.248  1.00 18.94 ? 46  PRO A CA  1 
ATOM   367  C  C   . PRO A 1 46  ? -24.264 2.873   27.243  1.00 17.09 ? 46  PRO A C   1 
ATOM   368  O  O   . PRO A 1 46  ? -24.216 4.132   27.311  1.00 17.12 ? 46  PRO A O   1 
ATOM   369  C  CB  . PRO A 1 46  ? -26.637 2.208   27.891  1.00 18.62 ? 46  PRO A CB  1 
ATOM   370  C  CG  . PRO A 1 46  ? -27.311 2.381   29.226  1.00 22.13 ? 46  PRO A CG  1 
ATOM   371  C  CD  . PRO A 1 46  ? -26.343 3.110   30.115  1.00 20.72 ? 46  PRO A CD  1 
ATOM   372  N  N   . LEU A 1 47  ? -23.628 2.164   26.314  1.00 18.73 ? 47  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 47  ? -22.941 2.835   25.270  1.00 16.03 ? 47  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 47  ? -24.019 3.480   24.340  1.00 16.52 ? 47  LEU A C   1 
ATOM   375  O  O   . LEU A 1 47  ? -25.061 2.837   24.043  1.00 19.54 ? 47  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 47  ? -22.198 1.727   24.544  1.00 20.93 ? 47  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 47  ? -21.114 2.105   23.662  1.00 21.86 ? 47  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 47  ? -20.058 3.097   24.406  1.00 23.93 ? 47  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 47  ? -20.535 0.724   23.173  1.00 20.84 ? 47  LEU A CD2 1 
ATOM   380  N  N   . SER A 1 48  ? -23.741 4.644   23.799  1.00 14.64 ? 48  SER A N   1 
ATOM   381  C  CA  . SER A 1 48  ? -24.566 5.242   22.768  1.00 15.18 ? 48  SER A CA  1 
ATOM   382  C  C   . SER A 1 48  ? -23.800 5.249   21.475  1.00 14.79 ? 48  SER A C   1 
ATOM   383  O  O   . SER A 1 48  ? -22.802 5.970   21.337  1.00 13.72 ? 48  SER A O   1 
ATOM   384  C  CB  . SER A 1 48  ? -24.947 6.700   23.189  1.00 15.77 ? 48  SER A CB  1 
ATOM   385  O  OG  . SER A 1 48  ? -25.548 7.407   22.098  1.00 19.43 ? 48  SER A OG  1 
ATOM   386  N  N   . VAL A 1 49  ? -24.227 4.480   20.517  1.00 16.03 ? 49  VAL A N   1 
ATOM   387  C  CA  . VAL A 1 49  ? -23.616 4.420   19.234  1.00 15.96 ? 49  VAL A CA  1 
ATOM   388  C  C   . VAL A 1 49  ? -24.612 5.016   18.238  1.00 17.69 ? 49  VAL A C   1 
ATOM   389  O  O   . VAL A 1 49  ? -25.680 4.434   18.009  1.00 19.57 ? 49  VAL A O   1 
ATOM   390  C  CB  . VAL A 1 49  ? -23.353 2.907   18.868  1.00 17.57 ? 49  VAL A CB  1 
ATOM   391  C  CG1 . VAL A 1 49  ? -22.581 2.828   17.548  1.00 20.30 ? 49  VAL A CG1 1 
ATOM   392  C  CG2 . VAL A 1 49  ? -22.593 2.262   19.997  1.00 19.03 ? 49  VAL A CG2 1 
ATOM   393  N  N   . SER A 1 50  ? -24.287 6.172   17.694  1.00 16.92 ? 50  SER A N   1 
ATOM   394  C  CA  . SER A 1 50  ? -25.205 6.882   16.806  1.00 18.23 ? 50  SER A CA  1 
ATOM   395  C  C   . SER A 1 50  ? -24.604 6.964   15.419  1.00 17.93 ? 50  SER A C   1 
ATOM   396  O  O   . SER A 1 50  ? -23.935 7.902   15.075  1.00 17.49 ? 50  SER A O   1 
ATOM   397  C  CB  . SER A 1 50  ? -25.552 8.271   17.370  1.00 20.21 ? 50  SER A CB  1 
ATOM   398  O  OG  . SER A 1 50  ? -26.201 8.108   18.596  1.00 27.16 ? 50  SER A OG  1 
ATOM   399  N  N   . TYR A 1 51  ? -24.832 5.907   14.611  1.00 17.19 ? 51  TYR A N   1 
ATOM   400  C  CA  . TYR A 1 51  ? -24.272 5.795   13.288  1.00 15.21 ? 51  TYR A CA  1 
ATOM   401  C  C   . TYR A 1 51  ? -25.258 6.040   12.145  1.00 17.33 ? 51  TYR A C   1 
ATOM   402  O  O   . TYR A 1 51  ? -24.853 5.848   10.972  1.00 16.73 ? 51  TYR A O   1 
ATOM   403  C  CB  . TYR A 1 51  ? -23.622 4.409   13.091  1.00 14.85 ? 51  TYR A CB  1 
ATOM   404  C  CG  . TYR A 1 51  ? -22.337 4.134   13.850  1.00 13.18 ? 51  TYR A CG  1 
ATOM   405  C  CD1 . TYR A 1 51  ? -21.641 5.127   14.532  1.00 13.91 ? 51  TYR A CD1 1 
ATOM   406  C  CD2 . TYR A 1 51  ? -21.873 2.813   13.956  1.00 12.52 ? 51  TYR A CD2 1 
ATOM   407  C  CE1 . TYR A 1 51  ? -20.413 4.858   15.218  1.00 11.82 ? 51  TYR A CE1 1 
ATOM   408  C  CE2 . TYR A 1 51  ? -20.695 2.547   14.571  1.00 10.98 ? 51  TYR A CE2 1 
ATOM   409  C  CZ  . TYR A 1 51  ? -19.969 3.536   15.244  1.00 11.92 ? 51  TYR A CZ  1 
ATOM   410  O  OH  . TYR A 1 51  ? -18.796 3.195   15.886  1.00 11.92 ? 51  TYR A OH  1 
ATOM   411  N  N   . ASP A 1 52  ? -26.486 6.497   12.458  1.00 18.10 ? 52  ASP A N   1 
ATOM   412  C  CA  . ASP A 1 52  ? -27.506 6.732   11.384  1.00 20.87 ? 52  ASP A CA  1 
ATOM   413  C  C   . ASP A 1 52  ? -27.056 7.664   10.261  1.00 21.79 ? 52  ASP A C   1 
ATOM   414  O  O   . ASP A 1 52  ? -27.434 7.472   9.080   1.00 22.56 ? 52  ASP A O   1 
ATOM   415  C  CB  . ASP A 1 52  ? -28.852 7.192   11.975  1.00 22.81 ? 52  ASP A CB  1 
ATOM   416  C  CG  . ASP A 1 52  ? -28.706 8.184   13.099  1.00 29.03 ? 52  ASP A CG  1 
ATOM   417  O  OD1 . ASP A 1 52  ? -28.155 7.880   14.218  1.00 38.75 ? 52  ASP A OD1 1 
ATOM   418  O  OD2 . ASP A 1 52  ? -29.175 9.320   12.863  1.00 40.24 ? 52  ASP A OD2 1 
ATOM   419  N  N   . GLN A 1 53  ? -26.200 8.629   10.550  1.00 19.58 ? 53  GLN A N   1 
ATOM   420  C  CA  . GLN A 1 53  ? -25.886 9.576   9.456   1.00 21.42 ? 53  GLN A CA  1 
ATOM   421  C  C   . GLN A 1 53  ? -24.428 9.418   9.020   1.00 17.31 ? 53  GLN A C   1 
ATOM   422  O  O   . GLN A 1 53  ? -23.823 10.305  8.461   1.00 19.33 ? 53  GLN A O   1 
ATOM   423  C  CB  . GLN A 1 53  ? -26.113 11.011  9.980   1.00 23.68 ? 53  GLN A CB  1 
ATOM   424  C  CG  . GLN A 1 53  ? -27.577 11.340  10.259  1.00 28.17 ? 53  GLN A CG  1 
ATOM   425  C  CD  . GLN A 1 53  ? -28.340 11.250  8.963   1.00 35.89 ? 53  GLN A CD  1 
ATOM   426  O  OE1 . GLN A 1 53  ? -27.839 11.708  7.873   1.00 40.47 ? 53  GLN A OE1 1 
ATOM   427  N  NE2 . GLN A 1 53  ? -29.526 10.633  9.016   1.00 33.81 ? 53  GLN A NE2 1 
ATOM   428  N  N   . ALA A 1 54  ? -23.829 8.293   9.351   1.00 16.56 ? 54  ALA A N   1 
ATOM   429  C  CA  . ALA A 1 54  ? -22.474 8.054   8.898   1.00 15.03 ? 54  ALA A CA  1 
ATOM   430  C  C   . ALA A 1 54  ? -22.294 8.206   7.391   1.00 17.25 ? 54  ALA A C   1 
ATOM   431  O  O   . ALA A 1 54  ? -23.179 7.804   6.572   1.00 21.22 ? 54  ALA A O   1 
ATOM   432  C  CB  . ALA A 1 54  ? -22.011 6.577   9.324   1.00 18.07 ? 54  ALA A CB  1 
ATOM   433  N  N   . THR A 1 55  ? -21.156 8.777   7.005   1.00 14.78 ? 55  THR A N   1 
ATOM   434  C  CA  . THR A 1 55  ? -20.759 8.979   5.596   1.00 16.42 ? 55  THR A CA  1 
ATOM   435  C  C   . THR A 1 55  ? -19.466 8.335   5.327   1.00 13.52 ? 55  THR A C   1 
ATOM   436  O  O   . THR A 1 55  ? -18.449 8.947   5.616   1.00 13.55 ? 55  THR A O   1 
ATOM   437  C  CB  . THR A 1 55  ? -20.598 10.518  5.236   1.00 18.24 ? 55  THR A CB  1 
ATOM   438  O  OG1 . THR A 1 55  ? -21.875 11.121  5.393   1.00 24.45 ? 55  THR A OG1 1 
ATOM   439  C  CG2 . THR A 1 55  ? -20.144 10.649  3.713   1.00 19.93 ? 55  THR A CG2 1 
ATOM   440  N  N   . SER A 1 56  ? -19.501 7.114   4.846   1.00 12.85 ? 56  SER A N   1 
ATOM   441  C  CA  . SER A 1 56  ? -18.239 6.495   4.452   1.00 14.00 ? 56  SER A CA  1 
ATOM   442  C  C   . SER A 1 56  ? -17.786 7.190   3.173   1.00 15.93 ? 56  SER A C   1 
ATOM   443  O  O   . SER A 1 56  ? -18.618 7.627   2.380   1.00 16.13 ? 56  SER A O   1 
ATOM   444  C  CB  . SER A 1 56  ? -18.291 4.933   4.302   1.00 14.03 ? 56  SER A CB  1 
ATOM   445  O  OG  . SER A 1 56  ? -19.137 4.651   3.165   1.00 15.58 ? 56  SER A OG  1 
ATOM   446  N  N   . LEU A 1 57  ? -16.472 7.216   2.964   1.00 13.33 ? 57  LEU A N   1 
ATOM   447  C  CA  . LEU A 1 57  ? -15.966 7.815   1.761   1.00 15.49 ? 57  LEU A CA  1 
ATOM   448  C  C   . LEU A 1 57  ? -15.108 6.870   0.920   1.00 14.34 ? 57  LEU A C   1 
ATOM   449  O  O   . LEU A 1 57  ? -15.138 6.931   -0.305  1.00 16.34 ? 57  LEU A O   1 
ATOM   450  C  CB  . LEU A 1 57  ? -15.067 8.988   2.163   1.00 16.93 ? 57  LEU A CB  1 
ATOM   451  C  CG  . LEU A 1 57  ? -15.899 10.192  2.728   1.00 19.90 ? 57  LEU A CG  1 
ATOM   452  C  CD1 . LEU A 1 57  ? -14.933 11.278  3.269   1.00 25.54 ? 57  LEU A CD1 1 
ATOM   453  C  CD2 . LEU A 1 57  ? -16.892 10.810  1.633   1.00 23.08 ? 57  LEU A CD2 1 
ATOM   454  N  N   . ARG A 1 58  ? -14.204 6.134   1.541   1.00 14.71 ? 58  ARG A N   1 
ATOM   455  C  CA  . ARG A 1 58  ? -13.148 5.463   0.792   1.00 12.76 ? 58  ARG A CA  1 
ATOM   456  C  C   . ARG A 1 58  ? -12.647 4.291   1.576   1.00 13.61 ? 58  ARG A C   1 
ATOM   457  O  O   . ARG A 1 58  ? -12.779 4.276   2.808   1.00 12.90 ? 58  ARG A O   1 
ATOM   458  C  CB  . ARG A 1 58  ? -11.986 6.458   0.626   1.00 14.88 ? 58  ARG A CB  1 
ATOM   459  C  CG  . ARG A 1 58  ? -10.885 6.045   -0.332  1.00 16.62 ? 58  ARG A CG  1 
ATOM   460  C  CD  . ARG A 1 58  ? -9.919  7.194   -0.534  1.00 20.45 ? 58  ARG A CD  1 
ATOM   461  N  NE  . ARG A 1 58  ? -9.047  7.221   0.634   1.00 17.44 ? 58  ARG A NE  1 
ATOM   462  C  CZ  . ARG A 1 58  ? -7.752  7.435   0.618   1.00 15.99 ? 58  ARG A CZ  1 
ATOM   463  N  NH1 . ARG A 1 58  ? -7.105  7.668   -0.520  1.00 19.60 ? 58  ARG A NH1 1 
ATOM   464  N  NH2 . ARG A 1 58  ? -7.079  7.410   1.749   1.00 17.87 ? 58  ARG A NH2 1 
ATOM   465  N  N   . ILE A 1 59  ? -12.008 3.357   0.878   1.00 12.65 ? 59  ILE A N   1 
ATOM   466  C  CA  . ILE A 1 59  ? -11.373 2.232   1.583   1.00 12.81 ? 59  ILE A CA  1 
ATOM   467  C  C   . ILE A 1 59  ? -9.908  2.193   1.075   1.00 11.28 ? 59  ILE A C   1 
ATOM   468  O  O   . ILE A 1 59  ? -9.641  2.382   -0.140  1.00 15.11 ? 59  ILE A O   1 
ATOM   469  C  CB  . ILE A 1 59  ? -12.138 0.885   1.360   1.00 12.16 ? 59  ILE A CB  1 
ATOM   470  C  CG1 . ILE A 1 59  ? -11.503 -0.222  2.205   1.00 12.77 ? 59  ILE A CG1 1 
ATOM   471  C  CG2 . ILE A 1 59  ? -12.086 0.468   -0.170  1.00 13.84 ? 59  ILE A CG2 1 
ATOM   472  C  CD1 . ILE A 1 59  ? -12.345 -1.545  2.082   1.00 13.61 ? 59  ILE A CD1 1 
ATOM   473  N  N   . LEU A 1 60  ? -8.938  2.047   2.025   1.00 12.57 ? 60  LEU A N   1 
ATOM   474  C  CA  . LEU A 1 60  ? -7.518  2.203   1.719   1.00 13.26 ? 60  LEU A CA  1 
ATOM   475  C  C   . LEU A 1 60  ? -6.719  0.992   2.270   1.00 13.02 ? 60  LEU A C   1 
ATOM   476  O  O   . LEU A 1 60  ? -6.954  0.618   3.436   1.00 11.45 ? 60  LEU A O   1 
ATOM   477  C  CB  . LEU A 1 60  ? -7.003  3.496   2.461   1.00 14.21 ? 60  LEU A CB  1 
ATOM   478  C  CG  . LEU A 1 60  ? -5.489  3.574   2.385   1.00 15.48 ? 60  LEU A CG  1 
ATOM   479  C  CD1 . LEU A 1 60  ? -4.957  3.833   0.948   1.00 16.80 ? 60  LEU A CD1 1 
ATOM   480  C  CD2 . LEU A 1 60  ? -4.954  4.746   3.354   1.00 14.68 ? 60  LEU A CD2 1 
ATOM   481  N  N   . ASN A 1 61  ? -5.856  0.348   1.428   1.00 11.58 ? 61  ASN A N   1 
ATOM   482  C  CA  . ASN A 1 61  ? -4.887  -0.605  1.972   1.00 12.40 ? 61  ASN A CA  1 
ATOM   483  C  C   . ASN A 1 61  ? -3.642  0.207   2.336   1.00 13.61 ? 61  ASN A C   1 
ATOM   484  O  O   . ASN A 1 61  ? -3.052  0.814   1.464   1.00 14.12 ? 61  ASN A O   1 
ATOM   485  C  CB  . ASN A 1 61  ? -4.543  -1.631  0.850   1.00 13.24 ? 61  ASN A CB  1 
ATOM   486  C  CG  . ASN A 1 61  ? -3.524  -2.649  1.281   1.00 12.71 ? 61  ASN A CG  1 
ATOM   487  O  OD1 . ASN A 1 61  ? -2.625  -2.332  2.115   1.00 14.38 ? 61  ASN A OD1 1 
ATOM   488  N  ND2 . ASN A 1 61  ? -3.524  -3.820  0.649   1.00 13.45 ? 61  ASN A ND2 1 
ATOM   489  N  N   . ASN A 1 62  ? -3.328  0.333   3.615   1.00 12.67 ? 62  ASN A N   1 
ATOM   490  C  CA  . ASN A 1 62  ? -2.284  1.191   4.067   1.00 13.37 ? 62  ASN A CA  1 
ATOM   491  C  C   . ASN A 1 62  ? -0.984  0.367   4.273   1.00 14.64 ? 62  ASN A C   1 
ATOM   492  O  O   . ASN A 1 62  ? 0.024   0.910   4.830   1.00 16.79 ? 62  ASN A O   1 
ATOM   493  C  CB  . ASN A 1 62  ? -2.627  1.991   5.361   1.00 13.88 ? 62  ASN A CB  1 
ATOM   494  C  CG  . ASN A 1 62  ? -2.810  1.058   6.541   1.00 14.45 ? 62  ASN A CG  1 
ATOM   495  O  OD1 . ASN A 1 62  ? -2.563  -0.152  6.469   1.00 16.12 ? 62  ASN A OD1 1 
ATOM   496  N  ND2 . ASN A 1 62  ? -3.081  1.625   7.658   1.00 18.41 ? 62  ASN A ND2 1 
ATOM   497  N  N   . GLY A 1 63  ? -0.920  -0.911  3.823   1.00 13.92 ? 63  GLY A N   1 
ATOM   498  C  CA  . GLY A 1 63  ? 0.213   -1.747  4.010   1.00 13.02 ? 63  GLY A CA  1 
ATOM   499  C  C   . GLY A 1 63  ? 0.243   -2.543  5.340   1.00 13.15 ? 63  GLY A C   1 
ATOM   500  O  O   . GLY A 1 63  ? 1.168   -3.352  5.537   1.00 14.81 ? 63  GLY A O   1 
ATOM   501  N  N   . HIS A 1 64  ? -0.677  -2.231  6.247   1.00 11.80 ? 64  HIS A N   1 
ATOM   502  C  CA  . HIS A 1 64  ? -0.778  -2.941  7.541   1.00 14.03 ? 64  HIS A CA  1 
ATOM   503  C  C   . HIS A 1 64  ? -2.131  -3.590  7.683   1.00 13.63 ? 64  HIS A C   1 
ATOM   504  O  O   . HIS A 1 64  ? -2.230  -4.676  8.215   1.00 16.53 ? 64  HIS A O   1 
ATOM   505  C  CB  . HIS A 1 64  ? -0.522  -1.923  8.705   1.00 14.29 ? 64  HIS A CB  1 
ATOM   506  C  CG  . HIS A 1 64  ? 0.748   -1.176  8.532   1.00 17.65 ? 64  HIS A CG  1 
ATOM   507  N  ND1 . HIS A 1 64  ? 1.992   -1.788  8.646   1.00 19.28 ? 64  HIS A ND1 1 
ATOM   508  C  CD2 . HIS A 1 64  ? 0.980   0.153   8.309   1.00 18.06 ? 64  HIS A CD2 1 
ATOM   509  C  CE1 . HIS A 1 64  ? 2.942   -0.861  8.490   1.00 23.36 ? 64  HIS A CE1 1 
ATOM   510  N  NE2 . HIS A 1 64  ? 2.363   0.318   8.257   1.00 22.34 ? 64  HIS A NE2 1 
ATOM   511  N  N   . ALA A 1 65  ? -3.174  -2.927  7.175   1.00 12.46 ? 65  ALA A N   1 
ATOM   512  C  CA  . ALA A 1 65  ? -4.576  -3.327  7.240   1.00 12.01 ? 65  ALA A CA  1 
ATOM   513  C  C   . ALA A 1 65  ? -5.305  -2.608  6.095   1.00 10.12 ? 65  ALA A C   1 
ATOM   514  O  O   . ALA A 1 65  ? -4.624  -1.981  5.256   1.00 12.06 ? 65  ALA A O   1 
ATOM   515  C  CB  . ALA A 1 65  ? -5.235  -3.117  8.621   1.00 12.21 ? 65  ALA A CB  1 
ATOM   516  N  N   . PHE A 1 66  ? -6.619  -2.668  6.131   1.00 11.37 ? 66  PHE A N   1 
ATOM   517  C  CA  . PHE A 1 66  ? -7.420  -1.721  5.284   1.00 11.08 ? 66  PHE A CA  1 
ATOM   518  C  C   . PHE A 1 66  ? -8.256  -0.869  6.191   1.00 10.97 ? 66  PHE A C   1 
ATOM   519  O  O   . PHE A 1 66  ? -8.882  -1.372  7.132   1.00 11.17 ? 66  PHE A O   1 
ATOM   520  C  CB  . PHE A 1 66  ? -8.229  -2.456  4.175   1.00 12.74 ? 66  PHE A CB  1 
ATOM   521  C  CG  . PHE A 1 66  ? -9.285  -3.385  4.694   1.00 12.07 ? 66  PHE A CG  1 
ATOM   522  C  CD1 . PHE A 1 66  ? -10.534 -2.938  5.024   1.00 12.79 ? 66  PHE A CD1 1 
ATOM   523  C  CD2 . PHE A 1 66  ? -8.991  -4.769  4.805   1.00 11.78 ? 66  PHE A CD2 1 
ATOM   524  C  CE1 . PHE A 1 66  ? -11.461 -3.778  5.582   1.00 13.14 ? 66  PHE A CE1 1 
ATOM   525  C  CE2 . PHE A 1 66  ? -9.957  -5.683  5.375   1.00 12.49 ? 66  PHE A CE2 1 
ATOM   526  C  CZ  . PHE A 1 66  ? -11.173 -5.195  5.676   1.00 11.80 ? 66  PHE A CZ  1 
ATOM   527  N  N   . ASN A 1 67  ? -8.355  0.421   5.798   1.00 10.25 ? 67  ASN A N   1 
ATOM   528  C  CA  . ASN A 1 67  ? -9.160  1.330   6.608   1.00 10.52 ? 67  ASN A CA  1 
ATOM   529  C  C   . ASN A 1 67  ? -10.393 1.722   5.780   1.00 9.81  ? 67  ASN A C   1 
ATOM   530  O  O   . ASN A 1 67  ? -10.231 2.144   4.582   1.00 11.81 ? 67  ASN A O   1 
ATOM   531  C  CB  . ASN A 1 67  ? -8.411  2.648   6.937   1.00 11.40 ? 67  ASN A CB  1 
ATOM   532  C  CG  . ASN A 1 67  ? -7.292  2.428   7.846   1.00 12.50 ? 67  ASN A CG  1 
ATOM   533  O  OD1 . ASN A 1 67  ? -7.160  1.363   8.513   1.00 14.60 ? 67  ASN A OD1 1 
ATOM   534  N  ND2 . ASN A 1 67  ? -6.430  3.448   7.920   1.00 17.34 ? 67  ASN A ND2 1 
ATOM   535  N  N   . VAL A 1 68  ? -11.602 1.661   6.370   1.00 10.82 ? 68  VAL A N   1 
ATOM   536  C  CA  . VAL A 1 68  ? -12.795 2.270   5.732   1.00 10.95 ? 68  VAL A CA  1 
ATOM   537  C  C   . VAL A 1 68  ? -12.953 3.632   6.419   1.00 12.40 ? 68  VAL A C   1 
ATOM   538  O  O   . VAL A 1 68  ? -13.057 3.711   7.693   1.00 11.68 ? 68  VAL A O   1 
ATOM   539  C  CB  . VAL A 1 68  ? -14.054 1.387   5.963   1.00 11.74 ? 68  VAL A CB  1 
ATOM   540  C  CG1 . VAL A 1 68  ? -15.321 2.199   5.478   1.00 12.36 ? 68  VAL A CG1 1 
ATOM   541  C  CG2 . VAL A 1 68  ? -13.915 0.083   5.152   1.00 12.08 ? 68  VAL A CG2 1 
ATOM   542  N  N   . GLU A 1 69  ? -12.846 4.698   5.625   1.00 12.91 ? 69  GLU A N   1 
ATOM   543  C  CA  . GLU A 1 69  ? -12.729 6.057   6.200   1.00 11.56 ? 69  GLU A CA  1 
ATOM   544  C  C   . GLU A 1 69  ? -14.080 6.752   6.114   1.00 12.21 ? 69  GLU A C   1 
ATOM   545  O  O   . GLU A 1 69  ? -14.846 6.519   5.123   1.00 13.64 ? 69  GLU A O   1 
ATOM   546  C  CB  . GLU A 1 69  ? -11.833 6.821   5.271   1.00 14.85 ? 69  GLU A CB  1 
ATOM   547  C  CG  . GLU A 1 69  ? -10.389 6.248   5.308   1.00 14.53 ? 69  GLU A CG  1 
ATOM   548  C  CD  . GLU A 1 69  ? -9.571  6.771   4.171   1.00 15.88 ? 69  GLU A CD  1 
ATOM   549  O  OE1 . GLU A 1 69  ? -10.114 7.453   3.243   1.00 17.40 ? 69  GLU A OE1 1 
ATOM   550  O  OE2 . GLU A 1 69  ? -8.367  6.406   4.130   1.00 18.63 ? 69  GLU A OE2 1 
ATOM   551  N  N   . PHE A 1 70  ? -14.317 7.675   7.075   1.00 12.44 ? 70  PHE A N   1 
ATOM   552  C  CA  . PHE A 1 70  ? -15.565 8.368   7.142   1.00 12.45 ? 70  PHE A CA  1 
ATOM   553  C  C   . PHE A 1 70  ? -15.292 9.872   7.082   1.00 12.84 ? 70  PHE A C   1 
ATOM   554  O  O   . PHE A 1 70  ? -14.227 10.374  7.473   1.00 13.43 ? 70  PHE A O   1 
ATOM   555  C  CB  . PHE A 1 70  ? -16.271 8.016   8.419   1.00 10.77 ? 70  PHE A CB  1 
ATOM   556  C  CG  . PHE A 1 70  ? -16.834 6.614   8.391   1.00 12.12 ? 70  PHE A CG  1 
ATOM   557  C  CD1 . PHE A 1 70  ? -15.998 5.514   8.604   1.00 13.17 ? 70  PHE A CD1 1 
ATOM   558  C  CD2 . PHE A 1 70  ? -18.130 6.414   8.047   1.00 12.22 ? 70  PHE A CD2 1 
ATOM   559  C  CE1 . PHE A 1 70  ? -16.503 4.212   8.478   1.00 12.80 ? 70  PHE A CE1 1 
ATOM   560  C  CE2 . PHE A 1 70  ? -18.642 5.129   7.897   1.00 13.05 ? 70  PHE A CE2 1 
ATOM   561  C  CZ  . PHE A 1 70  ? -17.795 4.043   8.104   1.00 12.51 ? 70  PHE A CZ  1 
ATOM   562  N  N   . ASP A 1 71  ? -16.310 10.577  6.573   1.00 13.42 ? 71  ASP A N   1 
ATOM   563  C  CA  . ASP A 1 71  ? -16.265 12.072  6.718   1.00 13.70 ? 71  ASP A CA  1 
ATOM   564  C  C   . ASP A 1 71  ? -16.505 12.438  8.176   1.00 14.74 ? 71  ASP A C   1 
ATOM   565  O  O   . ASP A 1 71  ? -17.589 12.203  8.691   1.00 19.74 ? 71  ASP A O   1 
ATOM   566  C  CB  . ASP A 1 71  ? -17.439 12.617  5.904   1.00 18.05 ? 71  ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 71  ? -17.636 14.195  6.124   1.00 20.65 ? 71  ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 71  ? -16.715 14.787  6.657   1.00 19.35 ? 71  ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 71  ? -18.751 14.684  5.836   1.00 24.49 ? 71  ASP A OD2 1 
ATOM   570  N  N   . ASP A 1 72  ? -15.495 12.955  8.901   1.00 14.59 ? 72  ASP A N   1 
ATOM   571  C  CA  . ASP A 1 72  ? -15.631 13.318  10.295  1.00 15.05 ? 72  ASP A CA  1 
ATOM   572  C  C   . ASP A 1 72  ? -15.530 14.858  10.426  1.00 19.05 ? 72  ASP A C   1 
ATOM   573  O  O   . ASP A 1 72  ? -15.101 15.353  11.459  1.00 18.82 ? 72  ASP A O   1 
ATOM   574  C  CB  . ASP A 1 72  ? -14.463 12.715  11.140  1.00 15.48 ? 72  ASP A CB  1 
ATOM   575  C  CG  . ASP A 1 72  ? -13.116 13.178  10.682  1.00 15.59 ? 72  ASP A CG  1 
ATOM   576  O  OD1 . ASP A 1 72  ? -12.985 13.888  9.590   1.00 19.56 ? 72  ASP A OD1 1 
ATOM   577  O  OD2 . ASP A 1 72  ? -12.103 12.926  11.394  1.00 16.44 ? 72  ASP A OD2 1 
ATOM   578  N  N   . SER A 1 73  ? -15.956 15.545  9.371   1.00 17.89 ? 73  SER A N   1 
ATOM   579  C  CA  . SER A 1 73  ? -15.931 17.090  9.418   1.00 18.54 ? 73  SER A CA  1 
ATOM   580  C  C   . SER A 1 73  ? -17.252 17.638  9.991   1.00 22.35 ? 73  SER A C   1 
ATOM   581  O  O   . SER A 1 73  ? -17.419 18.879  10.093  1.00 21.22 ? 73  SER A O   1 
ATOM   582  C  CB  . SER A 1 73  ? -15.645 17.630  8.028   1.00 23.52 ? 73  SER A CB  1 
ATOM   583  O  OG  . SER A 1 73  ? -16.808 17.427  7.215   1.00 22.32 ? 73  SER A OG  1 
ATOM   584  N  N   . GLN A 1 74  ? -18.174 16.766  10.392  1.00 21.69 ? 74  GLN A N   1 
ATOM   585  C  CA  . GLN A 1 74  ? -19.317 17.209  11.187  1.00 23.87 ? 74  GLN A CA  1 
ATOM   586  C  C   . GLN A 1 74  ? -19.747 16.128  12.093  1.00 22.83 ? 74  GLN A C   1 
ATOM   587  O  O   . GLN A 1 74  ? -19.239 15.024  11.926  1.00 22.08 ? 74  GLN A O   1 
ATOM   588  C  CB  . GLN A 1 74  ? -20.497 17.358  10.249  1.00 25.56 ? 74  GLN A CB  1 
ATOM   589  C  CG  . GLN A 1 74  ? -20.436 18.514  9.392   1.00 28.31 ? 74  GLN A CG  1 
ATOM   590  C  CD  . GLN A 1 74  ? -21.716 18.637  8.700   1.00 31.62 ? 74  GLN A CD  1 
ATOM   591  O  OE1 . GLN A 1 74  ? -21.887 18.136  7.548   1.00 34.25 ? 74  GLN A OE1 1 
ATOM   592  N  NE2 . GLN A 1 74  ? -22.689 19.241  9.413   1.00 35.25 ? 74  GLN A NE2 1 
ATOM   593  N  N   A ASP A 1 75  ? -20.706 16.333  13.047  0.50 24.38 ? 75  ASP A N   1 
ATOM   594  N  N   B ASP A 1 75  ? -20.694 16.495  12.944  0.50 23.77 ? 75  ASP A N   1 
ATOM   595  C  CA  A ASP A 1 75  ? -21.111 15.315  14.119  0.50 24.31 ? 75  ASP A CA  1 
ATOM   596  C  CA  B ASP A 1 75  ? -21.186 15.573  13.853  0.50 22.13 ? 75  ASP A CA  1 
ATOM   597  C  C   A ASP A 1 75  ? -22.107 14.159  13.672  0.50 23.01 ? 75  ASP A C   1 
ATOM   598  C  C   B ASP A 1 75  ? -22.144 14.624  13.130  0.50 21.35 ? 75  ASP A C   1 
ATOM   599  O  O   A ASP A 1 75  ? -23.207 13.859  14.237  0.50 25.61 ? 75  ASP A O   1 
ATOM   600  O  O   B ASP A 1 75  ? -23.340 14.963  13.045  0.50 20.19 ? 75  ASP A O   1 
ATOM   601  C  CB  A ASP A 1 75  ? -21.646 15.973  15.414  0.50 25.99 ? 75  ASP A CB  1 
ATOM   602  C  CB  B ASP A 1 75  ? -21.928 16.207  15.027  0.50 25.93 ? 75  ASP A CB  1 
ATOM   603  C  CG  A ASP A 1 75  ? -20.621 16.123  16.477  0.50 23.22 ? 75  ASP A CG  1 
ATOM   604  C  CG  B ASP A 1 75  ? -22.319 15.144  16.036  0.50 19.11 ? 75  ASP A CG  1 
ATOM   605  O  OD1 A ASP A 1 75  ? -19.516 15.583  16.352  0.50 26.35 ? 75  ASP A OD1 1 
ATOM   606  O  OD1 B ASP A 1 75  ? -22.103 13.951  15.711  0.50 29.89 ? 75  ASP A OD1 1 
ATOM   607  O  OD2 A ASP A 1 75  ? -20.945 16.788  17.486  0.50 27.36 ? 75  ASP A OD2 1 
ATOM   608  O  OD2 B ASP A 1 75  ? -22.728 15.465  17.170  0.50 32.00 ? 75  ASP A OD2 1 
ATOM   609  N  N   . LYS A 1 76  ? -21.652 13.445  12.701  1.00 20.40 ? 76  LYS A N   1 
ATOM   610  C  CA  . LYS A 1 76  ? -22.533 12.454  11.967  1.00 22.22 ? 76  LYS A CA  1 
ATOM   611  C  C   . LYS A 1 76  ? -22.617 10.982  12.418  1.00 24.41 ? 76  LYS A C   1 
ATOM   612  O  O   . LYS A 1 76  ? -23.574 10.185  12.086  1.00 28.51 ? 76  LYS A O   1 
ATOM   613  C  CB  . LYS A 1 76  ? -21.990 12.365  10.582  1.00 21.28 ? 76  LYS A CB  1 
ATOM   614  C  CG  . LYS A 1 76  ? -22.383 13.536  9.659   1.00 26.83 ? 76  LYS A CG  1 
ATOM   615  C  CD  . LYS A 1 76  ? -21.646 13.348  8.339   1.00 25.33 ? 76  LYS A CD  1 
ATOM   616  C  CE  . LYS A 1 76  ? -21.998 14.406  7.288   1.00 26.54 ? 76  LYS A CE  1 
ATOM   617  N  NZ  . LYS A 1 76  ? -21.544 13.959  5.941   1.00 25.63 ? 76  LYS A NZ  1 
ATOM   618  N  N   . ALA A 1 77  ? -21.527 10.507  12.914  1.00 20.69 ? 77  ALA A N   1 
ATOM   619  C  CA  . ALA A 1 77  ? -21.428 9.079   13.377  1.00 18.02 ? 77  ALA A CA  1 
ATOM   620  C  C   . ALA A 1 77  ? -20.674 9.258   14.694  1.00 16.51 ? 77  ALA A C   1 
ATOM   621  O  O   . ALA A 1 77  ? -19.441 9.482   14.691  1.00 19.96 ? 77  ALA A O   1 
ATOM   622  C  CB  . ALA A 1 77  ? -20.563 8.336   12.397  1.00 19.22 ? 77  ALA A CB  1 
ATOM   623  N  N   . VAL A 1 78  ? -21.352 9.162   15.826  1.00 14.50 ? 78  VAL A N   1 
ATOM   624  C  CA  . VAL A 1 78  ? -20.641 9.465   17.102  1.00 14.89 ? 78  VAL A CA  1 
ATOM   625  C  C   . VAL A 1 78  ? -20.908 8.425   18.163  1.00 13.70 ? 78  VAL A C   1 
ATOM   626  O  O   . VAL A 1 78  ? -21.959 7.728   18.237  1.00 15.48 ? 78  VAL A O   1 
ATOM   627  C  CB  . VAL A 1 78  ? -20.987 10.799  17.687  1.00 19.33 ? 78  VAL A CB  1 
ATOM   628  C  CG1 . VAL A 1 78  ? -20.760 11.976  16.768  1.00 20.63 ? 78  VAL A CG1 1 
ATOM   629  C  CG2 . VAL A 1 78  ? -22.370 10.818  18.055  1.00 19.66 ? 78  VAL A CG2 1 
ATOM   630  N  N   . LEU A 1 79  ? -19.909 8.280   19.015  1.00 12.31 ? 79  LEU A N   1 
ATOM   631  C  CA  . LEU A 1 79  ? -19.918 7.382   20.165  1.00 12.56 ? 79  LEU A CA  1 
ATOM   632  C  C   . LEU A 1 79  ? -19.944 8.287   21.372  1.00 12.35 ? 79  LEU A C   1 
ATOM   633  O  O   . LEU A 1 79  ? -19.117 9.226   21.461  1.00 14.32 ? 79  LEU A O   1 
ATOM   634  C  CB  . LEU A 1 79  ? -18.651 6.474   20.063  1.00 13.67 ? 79  LEU A CB  1 
ATOM   635  C  CG  . LEU A 1 79  ? -18.546 5.463   21.099  1.00 13.52 ? 79  LEU A CG  1 
ATOM   636  C  CD1 . LEU A 1 79  ? -19.591 4.397   20.877  1.00 17.85 ? 79  LEU A CD1 1 
ATOM   637  C  CD2 . LEU A 1 79  ? -17.169 4.763   21.083  1.00 14.01 ? 79  LEU A CD2 1 
ATOM   638  N  N   . LYS A 1 80  ? -20.781 7.919   22.295  1.00 13.35 ? 80  LYS A N   1 
ATOM   639  C  CA  . LYS A 1 80  ? -20.802 8.611   23.630  1.00 14.23 ? 80  LYS A CA  1 
ATOM   640  C  C   . LYS A 1 80  ? -21.407 7.703   24.680  1.00 14.14 ? 80  LYS A C   1 
ATOM   641  O  O   . LYS A 1 80  ? -21.708 6.543   24.374  1.00 14.71 ? 80  LYS A O   1 
ATOM   642  C  CB  . LYS A 1 80  ? -21.536 9.935   23.590  1.00 18.83 ? 80  LYS A CB  1 
ATOM   643  C  CG  . LYS A 1 80  ? -22.932 9.777   23.289  1.00 19.26 ? 80  LYS A CG  1 
ATOM   644  C  CD  . LYS A 1 80  ? -23.629 11.213  22.874  1.00 24.16 ? 80  LYS A CD  1 
ATOM   645  C  CE  . LYS A 1 80  ? -25.183 11.037  22.772  1.00 34.86 ? 80  LYS A CE  1 
ATOM   646  N  NZ  . LYS A 1 80  ? -25.839 10.413  23.987  1.00 41.11 ? 80  LYS A NZ  1 
ATOM   647  N  N   . GLY A 1 81  ? -21.472 8.229   25.900  1.00 14.56 ? 81  GLY A N   1 
ATOM   648  C  CA  . GLY A 1 81  ? -21.987 7.425   27.024  1.00 15.30 ? 81  GLY A CA  1 
ATOM   649  C  C   . GLY A 1 81  ? -21.004 6.343   27.336  1.00 15.67 ? 81  GLY A C   1 
ATOM   650  O  O   . GLY A 1 81  ? -19.797 6.508   27.121  1.00 15.02 ? 81  GLY A O   1 
ATOM   651  N  N   . GLY A 1 82  ? -21.466 5.229   27.860  1.00 17.19 ? 82  GLY A N   1 
ATOM   652  C  CA  . GLY A 1 82  ? -20.502 4.238   28.268  1.00 18.54 ? 82  GLY A CA  1 
ATOM   653  C  C   . GLY A 1 82  ? -19.616 4.829   29.368  1.00 16.90 ? 82  GLY A C   1 
ATOM   654  O  O   . GLY A 1 82  ? -20.089 5.540   30.271  1.00 22.01 ? 82  GLY A O   1 
ATOM   655  N  N   . PRO A 1 83  ? -18.251 4.635   29.281  1.00 16.55 ? 83  PRO A N   1 
ATOM   656  C  CA  . PRO A 1 83  ? -17.352 5.238   30.223  1.00 15.79 ? 83  PRO A CA  1 
ATOM   657  C  C   . PRO A 1 83  ? -16.912 6.675   29.806  1.00 17.50 ? 83  PRO A C   1 
ATOM   658  O  O   . PRO A 1 83  ? -16.099 7.259   30.519  1.00 20.19 ? 83  PRO A O   1 
ATOM   659  C  CB  . PRO A 1 83  ? -16.052 4.351   30.033  1.00 16.88 ? 83  PRO A CB  1 
ATOM   660  C  CG  . PRO A 1 83  ? -16.119 3.953   28.573  1.00 15.18 ? 83  PRO A CG  1 
ATOM   661  C  CD  . PRO A 1 83  ? -17.562 3.781   28.272  1.00 14.94 ? 83  PRO A CD  1 
ATOM   662  N  N   . LEU A 1 84  ? -17.395 7.190   28.661  1.00 14.02 ? 84  LEU A N   1 
ATOM   663  C  CA  . LEU A 1 84  ? -16.827 8.388   28.007  1.00 14.53 ? 84  LEU A CA  1 
ATOM   664  C  C   . LEU A 1 84  ? -17.481 9.628   28.604  1.00 17.48 ? 84  LEU A C   1 
ATOM   665  O  O   . LEU A 1 84  ? -18.708 9.612   28.876  1.00 18.00 ? 84  LEU A O   1 
ATOM   666  C  CB  . LEU A 1 84  ? -17.141 8.351   26.504  1.00 12.30 ? 84  LEU A CB  1 
ATOM   667  C  CG  . LEU A 1 84  ? -16.574 7.083   25.853  1.00 12.61 ? 84  LEU A CG  1 
ATOM   668  C  CD1 . LEU A 1 84  ? -17.033 7.035   24.368  1.00 13.68 ? 84  LEU A CD1 1 
ATOM   669  C  CD2 . LEU A 1 84  ? -14.978 7.083   25.946  1.00 11.60 ? 84  LEU A CD2 1 
ATOM   670  N  N   . ASP A 1 85  ? -16.710 10.674  28.632  1.00 18.30 ? 85  ASP A N   1 
ATOM   671  C  CA  . ASP A 1 85  ? -17.233 12.016  28.900  1.00 21.12 ? 85  ASP A CA  1 
ATOM   672  C  C   . ASP A 1 85  ? -17.238 12.680  27.513  1.00 19.72 ? 85  ASP A C   1 
ATOM   673  O  O   . ASP A 1 85  ? -16.234 12.664  26.797  1.00 23.49 ? 85  ASP A O   1 
ATOM   674  C  CB  . ASP A 1 85  ? -16.299 12.757  29.911  1.00 21.69 ? 85  ASP A CB  1 
ATOM   675  C  CG  . ASP A 1 85  ? -16.455 12.288  31.311  1.00 29.34 ? 85  ASP A CG  1 
ATOM   676  O  OD1 . ASP A 1 85  ? -17.567 11.770  31.672  1.00 33.82 ? 85  ASP A OD1 1 
ATOM   677  O  OD2 . ASP A 1 85  ? -15.464 12.472  32.105  1.00 35.18 ? 85  ASP A OD2 1 
ATOM   678  N  N   . GLY A 1 86  ? -18.305 13.320  27.093  1.00 23.69 ? 86  GLY A N   1 
ATOM   679  C  CA  . GLY A 1 86  ? -18.227 14.025  25.869  1.00 20.12 ? 86  GLY A CA  1 
ATOM   680  C  C   . GLY A 1 86  ? -18.477 13.087  24.647  1.00 19.26 ? 86  GLY A C   1 
ATOM   681  O  O   . GLY A 1 86  ? -18.990 11.963  24.745  1.00 23.05 ? 86  GLY A O   1 
ATOM   682  N  N   A THR A 1 87  ? -18.145 13.614  23.466  0.50 16.43 ? 87  THR A N   1 
ATOM   683  N  N   B THR A 1 87  ? -18.172 13.577  23.468  0.50 15.29 ? 87  THR A N   1 
ATOM   684  C  CA  A THR A 1 87  ? -18.581 13.062  22.180  0.50 17.27 ? 87  THR A CA  1 
ATOM   685  C  CA  B THR A 1 87  ? -18.605 12.899  22.279  0.50 15.64 ? 87  THR A CA  1 
ATOM   686  C  C   A THR A 1 87  ? -17.428 12.745  21.245  0.50 15.55 ? 87  THR A C   1 
ATOM   687  C  C   B THR A 1 87  ? -17.377 12.633  21.480  0.50 14.54 ? 87  THR A C   1 
ATOM   688  O  O   A THR A 1 87  ? -16.526 13.561  20.990  0.50 12.40 ? 87  THR A O   1 
ATOM   689  O  O   B THR A 1 87  ? -16.405 13.438  21.488  0.50 11.13 ? 87  THR A O   1 
ATOM   690  C  CB  A THR A 1 87  ? -19.713 13.950  21.509  0.50 20.72 ? 87  THR A CB  1 
ATOM   691  C  CB  B THR A 1 87  ? -19.523 13.819  21.491  0.50 18.46 ? 87  THR A CB  1 
ATOM   692  O  OG1 A THR A 1 87  ? -19.797 13.656  20.091  0.50 21.79 ? 87  THR A OG1 1 
ATOM   693  O  OG1 B THR A 1 87  ? -18.809 14.997  21.280  0.50 16.97 ? 87  THR A OG1 1 
ATOM   694  C  CG2 A THR A 1 87  ? -19.448 15.411  21.732  0.50 21.73 ? 87  THR A CG2 1 
ATOM   695  C  CG2 B THR A 1 87  ? -20.787 14.244  22.235  0.50 12.73 ? 87  THR A CG2 1 
ATOM   696  N  N   . TYR A 1 88  ? -17.421 11.512  20.768  1.00 12.71 ? 88  TYR A N   1 
ATOM   697  C  CA  . TYR A 1 88  ? -16.297 11.043  19.956  1.00 12.60 ? 88  TYR A CA  1 
ATOM   698  C  C   . TYR A 1 88  ? -16.773 10.722  18.560  1.00 11.49 ? 88  TYR A C   1 
ATOM   699  O  O   . TYR A 1 88  ? -17.783 10.031  18.414  1.00 15.17 ? 88  TYR A O   1 
ATOM   700  C  CB  . TYR A 1 88  ? -15.657 9.796   20.583  1.00 12.21 ? 88  TYR A CB  1 
ATOM   701  C  CG  . TYR A 1 88  ? -14.930 10.020  21.881  1.00 10.56 ? 88  TYR A CG  1 
ATOM   702  C  CD1 . TYR A 1 88  ? -15.601 10.398  23.057  1.00 11.62 ? 88  TYR A CD1 1 
ATOM   703  C  CD2 . TYR A 1 88  ? -13.524 9.879   21.914  1.00 10.29 ? 88  TYR A CD2 1 
ATOM   704  C  CE1 . TYR A 1 88  ? -14.896 10.568  24.242  1.00 11.00 ? 88  TYR A CE1 1 
ATOM   705  C  CE2 . TYR A 1 88  ? -12.802 10.008  23.101  1.00 9.41  ? 88  TYR A CE2 1 
ATOM   706  C  CZ  . TYR A 1 88  ? -13.501 10.343  24.252  1.00 10.25 ? 88  TYR A CZ  1 
ATOM   707  O  OH  . TYR A 1 88  ? -12.783 10.452  25.418  1.00 10.48 ? 88  TYR A OH  1 
ATOM   708  N  N   . ARG A 1 89  ? -16.104 11.249  17.565  1.00 10.93 ? 89  ARG A N   1 
ATOM   709  C  CA  . ARG A 1 89  ? -16.522 11.076  16.175  1.00 10.69 ? 89  ARG A CA  1 
ATOM   710  C  C   . ARG A 1 89  ? -15.799 9.987   15.436  1.00 9.58  ? 89  ARG A C   1 
ATOM   711  O  O   . ARG A 1 89  ? -14.611 9.877   15.535  1.00 9.26  ? 89  ARG A O   1 
ATOM   712  C  CB  . ARG A 1 89  ? -16.134 12.369  15.421  1.00 14.83 ? 89  ARG A CB  1 
ATOM   713  C  CG  . ARG A 1 89  ? -17.123 12.735  14.346  1.00 19.02 ? 89  ARG A CG  1 
ATOM   714  C  CD  . ARG A 1 89  ? -16.857 14.136  13.832  1.00 20.89 ? 89  ARG A CD  1 
ATOM   715  N  NE  . ARG A 1 89  ? -17.512 15.169  14.631  1.00 22.81 ? 89  ARG A NE  1 
ATOM   716  C  CZ  . ARG A 1 89  ? -17.317 16.473  14.461  1.00 18.73 ? 89  ARG A CZ  1 
ATOM   717  N  NH1 . ARG A 1 89  ? -16.485 16.903  13.523  1.00 21.81 ? 89  ARG A NH1 1 
ATOM   718  N  NH2 . ARG A 1 89  ? -17.955 17.347  15.225  1.00 24.67 ? 89  ARG A NH2 1 
ATOM   719  N  N   . LEU A 1 90  ? -16.566 9.171   14.689  1.00 9.70  ? 90  LEU A N   1 
ATOM   720  C  CA  . LEU A 1 90  ? -15.999 8.100   13.946  1.00 9.92  ? 90  LEU A CA  1 
ATOM   721  C  C   . LEU A 1 90  ? -15.136 8.608   12.830  1.00 9.95  ? 90  LEU A C   1 
ATOM   722  O  O   . LEU A 1 90  ? -15.649 9.402   11.991  1.00 11.79 ? 90  LEU A O   1 
ATOM   723  C  CB  . LEU A 1 90  ? -17.120 7.213   13.377  1.00 10.18 ? 90  LEU A CB  1 
ATOM   724  C  CG  . LEU A 1 90  ? -16.675 6.026   12.503  1.00 10.52 ? 90  LEU A CG  1 
ATOM   725  C  CD1 . LEU A 1 90  ? -15.887 4.983   13.291  1.00 11.55 ? 90  LEU A CD1 1 
ATOM   726  C  CD2 . LEU A 1 90  ? -17.946 5.368   11.898  1.00 12.23 ? 90  LEU A CD2 1 
ATOM   727  N  N   . ILE A 1 91  ? -13.875 8.175   12.708  1.00 9.61  ? 91  ILE A N   1 
ATOM   728  C  CA  . ILE A 1 91  ? -12.992 8.543   11.612  1.00 9.90  ? 91  ILE A CA  1 
ATOM   729  C  C   . ILE A 1 91  ? -12.704 7.369   10.637  1.00 9.39  ? 91  ILE A C   1 
ATOM   730  O  O   . ILE A 1 91  ? -12.665 7.565   9.466   1.00 10.03 ? 91  ILE A O   1 
ATOM   731  C  CB  . ILE A 1 91  ? -11.653 9.218   12.078  1.00 10.61 ? 91  ILE A CB  1 
ATOM   732  C  CG1 . ILE A 1 91  ? -10.803 9.545   10.904  1.00 14.03 ? 91  ILE A CG1 1 
ATOM   733  C  CG2 . ILE A 1 91  ? -10.973 8.375   13.155  1.00 11.99 ? 91  ILE A CG2 1 
ATOM   734  C  CD1 . ILE A 1 91  ? -9.570  10.476  11.324  1.00 14.49 ? 91  ILE A CD1 1 
ATOM   735  N  N   . GLN A 1 92  ? -12.570 6.119   11.186  1.00 9.18  ? 92  GLN A N   1 
ATOM   736  C  CA  . GLN A 1 92  ? -12.319 5.014   10.321  1.00 8.92  ? 92  GLN A CA  1 
ATOM   737  C  C   . GLN A 1 92  ? -12.580 3.747   11.114  1.00 9.16  ? 92  GLN A C   1 
ATOM   738  O  O   . GLN A 1 92  ? -12.588 3.774   12.315  1.00 9.36  ? 92  GLN A O   1 
ATOM   739  C  CB  . GLN A 1 92  ? -10.866 4.998   9.858   1.00 10.59 ? 92  GLN A CB  1 
ATOM   740  C  CG  . GLN A 1 92  ? -9.762  5.148   10.923  1.00 11.20 ? 92  GLN A CG  1 
ATOM   741  C  CD  . GLN A 1 92  ? -9.003  3.814   11.164  1.00 11.24 ? 92  GLN A CD  1 
ATOM   742  O  OE1 . GLN A 1 92  ? -9.581  2.732   11.196  1.00 10.92 ? 92  GLN A OE1 1 
ATOM   743  N  NE2 . GLN A 1 92  ? -7.769  3.919   11.553  1.00 12.83 ? 92  GLN A NE2 1 
ATOM   744  N  N   . PHE A 1 93  ? -12.723 2.631   10.374  1.00 9.22  ? 93  PHE A N   1 
ATOM   745  C  CA  . PHE A 1 93  ? -12.598 1.348   11.021  1.00 8.56  ? 93  PHE A CA  1 
ATOM   746  C  C   . PHE A 1 93  ? -11.663 0.472   10.197  1.00 7.92  ? 93  PHE A C   1 
ATOM   747  O  O   . PHE A 1 93  ? -11.434 0.667   9.024   1.00 9.67  ? 93  PHE A O   1 
ATOM   748  C  CB  . PHE A 1 93  ? -13.970 0.633   11.247  1.00 8.98  ? 93  PHE A CB  1 
ATOM   749  C  CG  . PHE A 1 93  ? -14.700 0.176   10.026  1.00 9.60  ? 93  PHE A CG  1 
ATOM   750  C  CD1 . PHE A 1 93  ? -14.317 -0.988  9.331   1.00 10.86 ? 93  PHE A CD1 1 
ATOM   751  C  CD2 . PHE A 1 93  ? -15.843 0.885   9.564   1.00 10.81 ? 93  PHE A CD2 1 
ATOM   752  C  CE1 . PHE A 1 93  ? -15.025 -1.421  8.240   1.00 9.77  ? 93  PHE A CE1 1 
ATOM   753  C  CE2 . PHE A 1 93  ? -16.526 0.421   8.469   1.00 9.62  ? 93  PHE A CE2 1 
ATOM   754  C  CZ  . PHE A 1 93  ? -16.135 -0.695  7.789   1.00 11.16 ? 93  PHE A CZ  1 
ATOM   755  N  N   . HIS A 1 94  ? -11.121 -0.556  10.916  1.00 8.38  ? 94  HIS A N   1 
ATOM   756  C  CA  . HIS A 1 94  ? -10.236 -1.495  10.261  1.00 7.86  ? 94  HIS A CA  1 
ATOM   757  C  C   . HIS A 1 94  ? -10.285 -2.770  11.100  1.00 8.69  ? 94  HIS A C   1 
ATOM   758  O  O   . HIS A 1 94  ? -10.920 -2.795  12.150  1.00 8.60  ? 94  HIS A O   1 
ATOM   759  C  CB  . HIS A 1 94  ? -8.783  -0.979  10.208  1.00 9.64  ? 94  HIS A CB  1 
ATOM   760  C  CG  . HIS A 1 94  ? -8.231  -0.684  11.570  1.00 8.53  ? 94  HIS A CG  1 
ATOM   761  N  ND1 . HIS A 1 94  ? -8.437  0.475   12.256  1.00 8.59  ? 94  HIS A ND1 1 
ATOM   762  C  CD2 . HIS A 1 94  ? -7.645  -1.542  12.469  1.00 9.18  ? 94  HIS A CD2 1 
ATOM   763  C  CE1 . HIS A 1 94  ? -7.913  0.370   13.462  1.00 8.02  ? 94  HIS A CE1 1 
ATOM   764  N  NE2 . HIS A 1 94  ? -7.393  -0.860  13.604  1.00 7.76  ? 94  HIS A NE2 1 
ATOM   765  N  N   . PHE A 1 95  ? -9.579  -3.824  10.604  1.00 8.55  ? 95  PHE A N   1 
ATOM   766  C  CA  . PHE A 1 95  ? -9.590  -5.118  11.345  1.00 7.99  ? 95  PHE A CA  1 
ATOM   767  C  C   . PHE A 1 95  ? -8.112  -5.542  11.517  1.00 8.26  ? 95  PHE A C   1 
ATOM   768  O  O   . PHE A 1 95  ? -7.212  -5.071  10.863  1.00 9.43  ? 95  PHE A O   1 
ATOM   769  C  CB  . PHE A 1 95  ? -10.253 -6.194  10.438  1.00 8.69  ? 95  PHE A CB  1 
ATOM   770  C  CG  . PHE A 1 95  ? -11.725 -5.914  10.160  1.00 8.36  ? 95  PHE A CG  1 
ATOM   771  C  CD1 . PHE A 1 95  ? -12.063 -5.052  9.121   1.00 9.60  ? 95  PHE A CD1 1 
ATOM   772  C  CD2 . PHE A 1 95  ? -12.743 -6.554  10.834  1.00 9.30  ? 95  PHE A CD2 1 
ATOM   773  C  CE1 . PHE A 1 95  ? -13.424 -4.869  8.762   1.00 9.88  ? 95  PHE A CE1 1 
ATOM   774  C  CE2 . PHE A 1 95  ? -14.042 -6.374  10.517  1.00 9.19  ? 95  PHE A CE2 1 
ATOM   775  C  CZ  . PHE A 1 95  ? -14.400 -5.507  9.455   1.00 9.50  ? 95  PHE A CZ  1 
ATOM   776  N  N   . HIS A 1 96  ? -7.967  -6.535  12.451  1.00 7.88  ? 96  HIS A N   1 
ATOM   777  C  CA  . HIS A 1 96  ? -6.728  -7.263  12.574  1.00 8.57  ? 96  HIS A CA  1 
ATOM   778  C  C   . HIS A 1 96  ? -7.183  -8.758  12.488  1.00 8.60  ? 96  HIS A C   1 
ATOM   779  O  O   . HIS A 1 96  ? -8.262  -9.105  12.980  1.00 8.63  ? 96  HIS A O   1 
ATOM   780  C  CB  . HIS A 1 96  ? -6.091  -7.089  13.976  1.00 9.97  ? 96  HIS A CB  1 
ATOM   781  C  CG  . HIS A 1 96  ? -5.808  -5.641  14.280  1.00 8.22  ? 96  HIS A CG  1 
ATOM   782  N  ND1 . HIS A 1 96  ? -4.572  -5.063  14.070  1.00 8.74  ? 96  HIS A ND1 1 
ATOM   783  C  CD2 . HIS A 1 96  ? -6.666  -4.614  14.639  1.00 8.63  ? 96  HIS A CD2 1 
ATOM   784  C  CE1 . HIS A 1 96  ? -4.661  -3.743  14.392  1.00 9.07  ? 96  HIS A CE1 1 
ATOM   785  N  NE2 . HIS A 1 96  ? -5.915  -3.450  14.726  1.00 9.45  ? 96  HIS A NE2 1 
ATOM   786  N  N   . TRP A 1 97  ? -6.384  -9.594  11.794  1.00 8.01  ? 97  TRP A N   1 
ATOM   787  C  CA  . TRP A 1 97  ? -6.822  -10.998 11.609  1.00 8.46  ? 97  TRP A CA  1 
ATOM   788  C  C   . TRP A 1 97  ? -5.631  -11.879 11.455  1.00 8.67  ? 97  TRP A C   1 
ATOM   789  O  O   . TRP A 1 97  ? -4.448  -11.460 11.373  1.00 9.20  ? 97  TRP A O   1 
ATOM   790  C  CB  . TRP A 1 97  ? -7.717  -11.091 10.316  1.00 9.24  ? 97  TRP A CB  1 
ATOM   791  C  CG  . TRP A 1 97  ? -7.087  -10.693 9.069   1.00 8.03  ? 97  TRP A CG  1 
ATOM   792  C  CD1 . TRP A 1 97  ? -6.404  -11.526 8.214   1.00 10.16 ? 97  TRP A CD1 1 
ATOM   793  C  CD2 . TRP A 1 97  ? -7.044  -9.378  8.481   1.00 10.10 ? 97  TRP A CD2 1 
ATOM   794  N  NE1 . TRP A 1 97  ? -5.963  -10.792 7.068   1.00 11.15 ? 97  TRP A NE1 1 
ATOM   795  C  CE2 . TRP A 1 97  ? -6.311  -9.463  7.264   1.00 11.28 ? 97  TRP A CE2 1 
ATOM   796  C  CE3 . TRP A 1 97  ? -7.547  -8.109  8.910   1.00 8.83  ? 97  TRP A CE3 1 
ATOM   797  C  CZ2 . TRP A 1 97  ? -6.141  -8.354  6.391   1.00 10.23 ? 97  TRP A CZ2 1 
ATOM   798  C  CZ3 . TRP A 1 97  ? -7.286  -7.029  8.055   1.00 10.60 ? 97  TRP A CZ3 1 
ATOM   799  C  CH2 . TRP A 1 97  ? -6.629  -7.156  6.855   1.00 10.66 ? 97  TRP A CH2 1 
ATOM   800  N  N   . GLY A 1 98  ? -5.915  -13.198 11.459  1.00 9.61  ? 98  GLY A N   1 
ATOM   801  C  CA  . GLY A 1 98  ? -4.857  -14.171 11.486  1.00 9.41  ? 98  GLY A CA  1 
ATOM   802  C  C   . GLY A 1 98  ? -4.602  -14.896 10.181  1.00 9.97  ? 98  GLY A C   1 
ATOM   803  O  O   . GLY A 1 98  ? -5.339  -14.733 9.213   1.00 10.76 ? 98  GLY A O   1 
ATOM   804  N  N   . SER A 1 99  ? -3.580  -15.771 10.163  1.00 11.40 ? 99  SER A N   1 
ATOM   805  C  CA  . SER A 1 99  ? -3.378  -16.651 9.027   1.00 12.20 ? 99  SER A CA  1 
ATOM   806  C  C   . SER A 1 99  ? -4.252  -17.917 9.171   1.00 12.47 ? 99  SER A C   1 
ATOM   807  O  O   . SER A 1 99  ? -4.358  -18.663 8.182   1.00 13.78 ? 99  SER A O   1 
ATOM   808  C  CB  . SER A 1 99  ? -1.913  -17.006 8.985   1.00 13.54 ? 99  SER A CB  1 
ATOM   809  O  OG  . SER A 1 99  ? -1.495  -17.533 10.266  1.00 13.88 ? 99  SER A OG  1 
ATOM   810  N  N   . LEU A 1 100 ? -4.828  -18.150 10.331  1.00 11.96 ? 100 LEU A N   1 
ATOM   811  C  CA  . LEU A 1 100 ? -5.647  -19.290 10.678  1.00 13.11 ? 100 LEU A CA  1 
ATOM   812  C  C   . LEU A 1 100 ? -6.806  -18.861 11.524  1.00 12.04 ? 100 LEU A C   1 
ATOM   813  O  O   . LEU A 1 100 ? -6.670  -17.822 12.185  1.00 12.38 ? 100 LEU A O   1 
ATOM   814  C  CB  . LEU A 1 100 ? -4.815  -20.302 11.590  1.00 18.24 ? 100 LEU A CB  1 
ATOM   815  C  CG  . LEU A 1 100 ? -3.476  -20.648 11.019  1.00 18.46 ? 100 LEU A CG  1 
ATOM   816  C  CD1 . LEU A 1 100 ? -2.593  -21.321 12.062  1.00 26.22 ? 100 LEU A CD1 1 
ATOM   817  C  CD2 . LEU A 1 100 ? -3.835  -21.719 9.869   1.00 24.34 ? 100 LEU A CD2 1 
ATOM   818  N  N   . ASP A 1 101 ? -7.903  -19.597 11.593  1.00 12.44 ? 101 ASP A N   1 
ATOM   819  C  CA  . ASP A 1 101 ? -9.063  -19.111 12.337  1.00 13.00 ? 101 ASP A CA  1 
ATOM   820  C  C   . ASP A 1 101 ? -8.753  -19.058 13.821  1.00 12.15 ? 101 ASP A C   1 
ATOM   821  O  O   . ASP A 1 101 ? -9.444  -18.317 14.541  1.00 13.87 ? 101 ASP A O   1 
ATOM   822  C  CB  . ASP A 1 101 ? -10.310 -20.003 12.090  1.00 13.70 ? 101 ASP A CB  1 
ATOM   823  C  CG  . ASP A 1 101 ? -10.793 -20.076 10.656  1.00 15.52 ? 101 ASP A CG  1 
ATOM   824  O  OD1 . ASP A 1 101 ? -10.476 -19.200 9.838   1.00 14.77 ? 101 ASP A OD1 1 
ATOM   825  O  OD2 . ASP A 1 101 ? -11.624 -20.952 10.446  1.00 20.95 ? 101 ASP A OD2 1 
ATOM   826  N  N   . GLY A 1 102 ? -7.764  -19.843 14.306  1.00 12.96 ? 102 GLY A N   1 
ATOM   827  C  CA  . GLY A 1 102 ? -7.496  -19.810 15.724  1.00 14.74 ? 102 GLY A CA  1 
ATOM   828  C  C   . GLY A 1 102 ? -6.683  -18.643 16.273  1.00 12.33 ? 102 GLY A C   1 
ATOM   829  O  O   . GLY A 1 102 ? -6.349  -18.632 17.448  1.00 13.19 ? 102 GLY A O   1 
ATOM   830  N  N   . GLN A 1 103 ? -6.395  -17.649 15.470  1.00 11.35 ? 103 GLN A N   1 
ATOM   831  C  CA  . GLN A 1 103 ? -5.736  -16.437 15.994  1.00 9.77  ? 103 GLN A CA  1 
ATOM   832  C  C   . GLN A 1 103 ? -6.037  -15.279 15.098  1.00 9.81  ? 103 GLN A C   1 
ATOM   833  O  O   . GLN A 1 103 ? -6.625  -15.461 14.028  1.00 10.34 ? 103 GLN A O   1 
ATOM   834  C  CB  . GLN A 1 103 ? -4.208  -16.627 15.966  1.00 12.10 ? 103 GLN A CB  1 
ATOM   835  C  CG  . GLN A 1 103 ? -3.661  -16.920 14.574  1.00 13.13 ? 103 GLN A CG  1 
ATOM   836  C  CD  . GLN A 1 103 ? -2.219  -17.459 14.697  1.00 15.52 ? 103 GLN A CD  1 
ATOM   837  O  OE1 . GLN A 1 103 ? -1.993  -18.407 15.507  1.00 25.69 ? 103 GLN A OE1 1 
ATOM   838  N  NE2 . GLN A 1 103 ? -1.301  -16.993 13.928  1.00 14.11 ? 103 GLN A NE2 1 
ATOM   839  N  N   . GLY A 1 104 ? -5.761  -14.041 15.617  1.00 9.35  ? 104 GLY A N   1 
ATOM   840  C  CA  . GLY A 1 104 ? -6.047  -12.853 14.758  1.00 8.39  ? 104 GLY A CA  1 
ATOM   841  C  C   . GLY A 1 104 ? -6.493  -11.719 15.645  1.00 9.33  ? 104 GLY A C   1 
ATOM   842  O  O   . GLY A 1 104 ? -6.244  -10.564 15.292  1.00 8.66  ? 104 GLY A O   1 
ATOM   843  N  N   . SER A 1 105 ? -7.238  -11.984 16.743  1.00 8.95  ? 105 SER A N   1 
ATOM   844  C  CA  . SER A 1 105 ? -7.635  -10.850 17.587  1.00 7.37  ? 105 SER A CA  1 
ATOM   845  C  C   . SER A 1 105 ? -6.407  -10.296 18.339  1.00 8.36  ? 105 SER A C   1 
ATOM   846  O  O   . SER A 1 105 ? -5.383  -10.997 18.548  1.00 8.47  ? 105 SER A O   1 
ATOM   847  C  CB  . SER A 1 105 ? -8.743  -11.199 18.538  1.00 8.37  ? 105 SER A CB  1 
ATOM   848  O  OG  . SER A 1 105 ? -8.381  -12.171 19.512  1.00 8.92  ? 105 SER A OG  1 
ATOM   849  N  N   . GLU A 1 106 ? -6.548  -9.027  18.734  1.00 7.31  ? 106 GLU A N   1 
ATOM   850  C  CA  . GLU A 1 106 ? -5.505  -8.368  19.554  1.00 7.60  ? 106 GLU A CA  1 
ATOM   851  C  C   . GLU A 1 106 ? -5.849  -8.540  21.041  1.00 7.09  ? 106 GLU A C   1 
ATOM   852  O  O   . GLU A 1 106 ? -5.085  -9.116  21.844  1.00 7.99  ? 106 GLU A O   1 
ATOM   853  C  CB  . GLU A 1 106 ? -5.493  -6.859  19.138  1.00 6.89  ? 106 GLU A CB  1 
ATOM   854  C  CG  . GLU A 1 106 ? -5.072  -6.750  17.726  1.00 9.27  ? 106 GLU A CG  1 
ATOM   855  C  CD  . GLU A 1 106 ? -4.381  -5.435  17.426  1.00 8.66  ? 106 GLU A CD  1 
ATOM   856  O  OE1 . GLU A 1 106 ? -4.978  -4.366  17.672  1.00 8.50  ? 106 GLU A OE1 1 
ATOM   857  O  OE2 . GLU A 1 106 ? -3.219  -5.505  17.011  1.00 9.32  ? 106 GLU A OE2 1 
ATOM   858  N  N   . HIS A 1 107 ? -7.043  -8.077  21.443  1.00 7.94  ? 107 HIS A N   1 
ATOM   859  C  CA  . HIS A 1 107 ? -7.524  -8.469  22.739  1.00 7.47  ? 107 HIS A CA  1 
ATOM   860  C  C   . HIS A 1 107 ? -7.813  -9.940  22.786  1.00 7.76  ? 107 HIS A C   1 
ATOM   861  O  O   . HIS A 1 107 ? -8.186  -10.552 21.771  1.00 8.04  ? 107 HIS A O   1 
ATOM   862  C  CB  . HIS A 1 107 ? -8.802  -7.646  23.156  1.00 7.91  ? 107 HIS A CB  1 
ATOM   863  C  CG  . HIS A 1 107 ? -8.448  -6.183  23.309  1.00 6.74  ? 107 HIS A CG  1 
ATOM   864  N  ND1 . HIS A 1 107 ? -8.504  -5.285  22.261  1.00 6.61  ? 107 HIS A ND1 1 
ATOM   865  C  CD2 . HIS A 1 107 ? -8.000  -5.467  24.388  1.00 7.15  ? 107 HIS A CD2 1 
ATOM   866  C  CE1 . HIS A 1 107 ? -8.079  -4.107  22.683  1.00 7.56  ? 107 HIS A CE1 1 
ATOM   867  N  NE2 . HIS A 1 107 ? -7.752  -4.160  23.984  1.00 7.60  ? 107 HIS A NE2 1 
ATOM   868  N  N   . THR A 1 108 ? -7.714  -10.539 23.978  1.00 7.81  ? 108 THR A N   1 
ATOM   869  C  CA  . THR A 1 108 ? -8.095  -11.917 24.210  1.00 8.98  ? 108 THR A CA  1 
ATOM   870  C  C   . THR A 1 108 ? -9.043  -11.929 25.381  1.00 8.16  ? 108 THR A C   1 
ATOM   871  O  O   . THR A 1 108 ? -9.072  -10.942 26.226  1.00 8.50  ? 108 THR A O   1 
ATOM   872  C  CB  . THR A 1 108 ? -6.877  -12.826 24.414  1.00 10.09 ? 108 THR A CB  1 
ATOM   873  O  OG1 . THR A 1 108 ? -6.022  -12.330 25.487  1.00 9.12  ? 108 THR A OG1 1 
ATOM   874  C  CG2 . THR A 1 108 ? -6.056  -12.875 23.157  1.00 10.34 ? 108 THR A CG2 1 
ATOM   875  N  N   . VAL A 1 109 ? -9.812  -13.026 25.548  1.00 9.19  ? 109 VAL A N   1 
ATOM   876  C  CA  . VAL A 1 109 ? -10.799 -13.095 26.662  1.00 9.80  ? 109 VAL A CA  1 
ATOM   877  C  C   . VAL A 1 109 ? -10.493 -14.396 27.417  1.00 11.37 ? 109 VAL A C   1 
ATOM   878  O  O   . VAL A 1 109 ? -10.617 -15.464 26.796  1.00 10.71 ? 109 VAL A O   1 
ATOM   879  C  CB  . VAL A 1 109 ? -12.235 -13.129 26.087  1.00 11.57 ? 109 VAL A CB  1 
ATOM   880  C  CG1 . VAL A 1 109 ? -13.287 -13.240 27.209  1.00 12.05 ? 109 VAL A CG1 1 
ATOM   881  C  CG2 . VAL A 1 109 ? -12.543 -11.796 25.284  1.00 11.24 ? 109 VAL A CG2 1 
ATOM   882  N  N   . ASP A 1 110 ? -9.944  -14.278 28.618  1.00 10.54 ? 110 ASP A N   1 
ATOM   883  C  CA  . ASP A 1 110 ? -9.465  -15.462 29.341  1.00 11.88 ? 110 ASP A CA  1 
ATOM   884  C  C   . ASP A 1 110 ? -8.539  -16.265 28.420  1.00 12.29 ? 110 ASP A C   1 
ATOM   885  O  O   . ASP A 1 110 ? -8.605  -17.521 28.391  1.00 12.73 ? 110 ASP A O   1 
ATOM   886  C  CB  . ASP A 1 110 ? -10.633 -16.318 29.829  1.00 13.55 ? 110 ASP A CB  1 
ATOM   887  C  CG  . ASP A 1 110 ? -11.481 -15.541 30.807  1.00 13.53 ? 110 ASP A CG  1 
ATOM   888  O  OD1 . ASP A 1 110 ? -10.901 -14.696 31.546  1.00 16.14 ? 110 ASP A OD1 1 
ATOM   889  O  OD2 . ASP A 1 110 ? -12.698 -15.839 30.971  1.00 18.20 ? 110 ASP A OD2 1 
ATOM   890  N  N   . LYS A 1 111 ? -7.653  -15.556 27.733  1.00 10.42 ? 111 LYS A N   1 
ATOM   891  C  CA  . LYS A 1 111 ? -6.613  -16.086 26.847  1.00 11.47 ? 111 LYS A CA  1 
ATOM   892  C  C   . LYS A 1 111 ? -7.179  -16.613 25.494  1.00 10.21 ? 111 LYS A C   1 
ATOM   893  O  O   . LYS A 1 111 ? -6.368  -16.982 24.638  1.00 12.38 ? 111 LYS A O   1 
ATOM   894  C  CB  . LYS A 1 111 ? -5.626  -17.121 27.541  1.00 14.75 ? 111 LYS A CB  1 
ATOM   895  C  CG  . LYS A 1 111 ? -5.013  -16.544 28.806  1.00 16.59 ? 111 LYS A CG  1 
ATOM   896  C  CD  . LYS A 1 111 ? -4.000  -15.431 28.342  1.00 22.05 ? 111 LYS A CD  1 
ATOM   897  C  CE  . LYS A 1 111 ? -3.191  -14.661 29.458  1.00 22.77 ? 111 LYS A CE  1 
ATOM   898  N  NZ  . LYS A 1 111 ? -2.105  -15.544 29.841  1.00 26.14 ? 111 LYS A NZ  1 
ATOM   899  N  N   . LYS A 1 112 ? -8.493  -16.604 25.315  1.00 9.34  ? 112 LYS A N   1 
ATOM   900  C  CA  . LYS A 1 112 ? -9.051  -16.972 24.029  1.00 11.05 ? 112 LYS A CA  1 
ATOM   901  C  C   . LYS A 1 112 ? -8.716  -15.942 22.914  1.00 8.94  ? 112 LYS A C   1 
ATOM   902  O  O   . LYS A 1 112 ? -8.996  -14.745 23.140  1.00 10.33 ? 112 LYS A O   1 
ATOM   903  C  CB  . LYS A 1 112 ? -10.577 -17.067 24.149  1.00 13.26 ? 112 LYS A CB  1 
ATOM   904  C  CG  . LYS A 1 112 ? -11.267 -17.459 22.833  1.00 14.79 ? 112 LYS A CG  1 
ATOM   905  C  CD  . LYS A 1 112 ? -12.843 -17.407 22.996  1.00 17.29 ? 112 LYS A CD  1 
ATOM   906  C  CE  . LYS A 1 112 ? -13.455 -17.594 21.643  1.00 16.71 ? 112 LYS A CE  1 
ATOM   907  N  NZ  . LYS A 1 112 ? -13.207 -18.893 21.056  1.00 18.77 ? 112 LYS A NZ  1 
ATOM   908  N  N   A LYS A 1 113 ? -8.079  -16.387 21.858  0.50 8.97  ? 113 LYS A N   1 
ATOM   909  N  N   B LYS A 1 113 ? -8.282  -16.474 21.797  0.50 8.66  ? 113 LYS A N   1 
ATOM   910  C  CA  A LYS A 1 113 ? -7.994  -15.528 20.669  0.50 9.34  ? 113 LYS A CA  1 
ATOM   911  C  CA  B LYS A 1 113 ? -7.988  -15.697 20.584  0.50 8.97  ? 113 LYS A CA  1 
ATOM   912  C  C   A LYS A 1 113 ? -9.188  -15.806 19.742  0.50 8.68  ? 113 LYS A C   1 
ATOM   913  C  C   B LYS A 1 113 ? -9.098  -15.850 19.543  0.50 8.88  ? 113 LYS A C   1 
ATOM   914  O  O   A LYS A 1 113 ? -9.620  -16.979 19.583  0.50 8.82  ? 113 LYS A O   1 
ATOM   915  O  O   B LYS A 1 113 ? -9.384  -16.976 19.108  0.50 9.25  ? 113 LYS A O   1 
ATOM   916  C  CB  A LYS A 1 113 ? -6.688  -15.759 19.874  0.50 9.44  ? 113 LYS A CB  1 
ATOM   917  C  CB  B LYS A 1 113 ? -6.652  -16.185 19.986  0.50 9.33  ? 113 LYS A CB  1 
ATOM   918  C  CG  A LYS A 1 113 ? -5.384  -15.477 20.627  0.50 10.32 ? 113 LYS A CG  1 
ATOM   919  C  CG  B LYS A 1 113 ? -5.484  -15.855 20.867  0.50 9.32  ? 113 LYS A CG  1 
ATOM   920  C  CD  A LYS A 1 113 ? -4.192  -16.129 19.891  0.50 9.59  ? 113 LYS A CD  1 
ATOM   921  C  CD  B LYS A 1 113 ? -4.215  -16.491 20.346  0.50 11.89 ? 113 LYS A CD  1 
ATOM   922  C  CE  A LYS A 1 113 ? -2.829  -15.753 20.507  0.50 12.56 ? 113 LYS A CE  1 
ATOM   923  C  CE  B LYS A 1 113 ? -3.029  -15.851 21.112  0.50 16.27 ? 113 LYS A CE  1 
ATOM   924  N  NZ  A LYS A 1 113 ? -2.581  -16.419 21.847  0.50 14.65 ? 113 LYS A NZ  1 
ATOM   925  N  NZ  B LYS A 1 113 ? -1.713  -16.397 20.659  0.50 16.40 ? 113 LYS A NZ  1 
ATOM   926  N  N   . TYR A 1 114 ? -9.720  -14.725 19.141  1.00 9.17  ? 114 TYR A N   1 
ATOM   927  C  CA  . TYR A 1 114 ? -10.677 -14.822 18.123  1.00 9.55  ? 114 TYR A CA  1 
ATOM   928  C  C   . TYR A 1 114 ? -10.063 -14.772 16.742  1.00 9.04  ? 114 TYR A C   1 
ATOM   929  O  O   . TYR A 1 114 ? -8.856  -14.474 16.615  1.00 9.57  ? 114 TYR A O   1 
ATOM   930  C  CB  . TYR A 1 114 ? -11.792 -13.687 18.244  1.00 9.07  ? 114 TYR A CB  1 
ATOM   931  C  CG  . TYR A 1 114 ? -12.702 -13.946 19.376  1.00 9.60  ? 114 TYR A CG  1 
ATOM   932  C  CD1 . TYR A 1 114 ? -12.386 -13.491 20.683  1.00 11.35 ? 114 TYR A CD1 1 
ATOM   933  C  CD2 . TYR A 1 114 ? -13.901 -14.575 19.161  1.00 10.31 ? 114 TYR A CD2 1 
ATOM   934  C  CE1 . TYR A 1 114 ? -13.283 -13.681 21.738  1.00 13.14 ? 114 TYR A CE1 1 
ATOM   935  C  CE2 . TYR A 1 114 ? -14.806 -14.768 20.220  1.00 12.52 ? 114 TYR A CE2 1 
ATOM   936  C  CZ  . TYR A 1 114 ? -14.492 -14.298 21.470  1.00 13.34 ? 114 TYR A CZ  1 
ATOM   937  O  OH  . TYR A 1 114 ? -15.363 -14.437 22.556  1.00 18.01 ? 114 TYR A OH  1 
ATOM   938  N  N   . ALA A 1 115 ? -10.846 -15.087 15.690  1.00 9.44  ? 115 ALA A N   1 
ATOM   939  C  CA  . ALA A 1 115 ? -10.291 -15.091 14.331  1.00 8.87  ? 115 ALA A CA  1 
ATOM   940  C  C   . ALA A 1 115 ? -9.889  -13.699 13.835  1.00 8.56  ? 115 ALA A C   1 
ATOM   941  O  O   . ALA A 1 115 ? -9.023  -13.532 13.007  1.00 9.49  ? 115 ALA A O   1 
ATOM   942  C  CB  . ALA A 1 115 ? -11.290 -15.692 13.344  1.00 10.57 ? 115 ALA A CB  1 
ATOM   943  N  N   . ALA A 1 116 ? -10.534 -12.659 14.403  1.00 9.36  ? 116 ALA A N   1 
ATOM   944  C  CA  . ALA A 1 116 ? -10.196 -11.294 13.914  1.00 8.93  ? 116 ALA A CA  1 
ATOM   945  C  C   . ALA A 1 116 ? -10.820 -10.349 14.978  1.00 8.10  ? 116 ALA A C   1 
ATOM   946  O  O   . ALA A 1 116 ? -11.560 -10.743 15.858  1.00 7.66  ? 116 ALA A O   1 
ATOM   947  C  CB  . ALA A 1 116 ? -10.780 -11.005 12.513  1.00 9.90  ? 116 ALA A CB  1 
ATOM   948  N  N   . GLU A 1 117 ? -10.503 -9.038  14.801  1.00 7.94  ? 117 GLU A N   1 
ATOM   949  C  CA  . GLU A 1 117 ? -11.070 -8.042  15.707  1.00 7.68  ? 117 GLU A CA  1 
ATOM   950  C  C   . GLU A 1 117 ? -11.232 -6.774  14.839  1.00 7.88  ? 117 GLU A C   1 
ATOM   951  O  O   . GLU A 1 117 ? -10.329 -6.342  14.142  1.00 8.91  ? 117 GLU A O   1 
ATOM   952  C  CB  . GLU A 1 117 ? -10.082 -7.785  16.851  1.00 8.17  ? 117 GLU A CB  1 
ATOM   953  C  CG  . GLU A 1 117 ? -10.600 -6.872  17.899  1.00 7.78  ? 117 GLU A CG  1 
ATOM   954  C  CD  . GLU A 1 117 ? -9.662  -6.767  19.076  1.00 7.81  ? 117 GLU A CD  1 
ATOM   955  O  OE1 . GLU A 1 117 ? -9.018  -7.790  19.414  1.00 8.44  ? 117 GLU A OE1 1 
ATOM   956  O  OE2 . GLU A 1 117 ? -9.637  -5.690  19.799  1.00 7.94  ? 117 GLU A OE2 1 
ATOM   957  N  N   . LEU A 1 118 ? -12.432 -6.169  14.982  1.00 8.28  ? 118 LEU A N   1 
ATOM   958  C  CA  . LEU A 1 118 ? -12.760 -4.938  14.269  1.00 7.67  ? 118 LEU A CA  1 
ATOM   959  C  C   . LEU A 1 118 ? -12.545 -3.779  15.272  1.00 8.42  ? 118 LEU A C   1 
ATOM   960  O  O   . LEU A 1 118 ? -12.964 -3.863  16.435  1.00 7.90  ? 118 LEU A O   1 
ATOM   961  C  CB  . LEU A 1 118 ? -14.290 -5.046  13.948  1.00 8.47  ? 118 LEU A CB  1 
ATOM   962  C  CG  . LEU A 1 118 ? -15.027 -3.730  13.591  1.00 9.43  ? 118 LEU A CG  1 
ATOM   963  C  CD1 . LEU A 1 118 ? -14.477 -3.071  12.384  1.00 10.39 ? 118 LEU A CD1 1 
ATOM   964  C  CD2 . LEU A 1 118 ? -16.499 -4.103  13.311  1.00 9.69  ? 118 LEU A CD2 1 
ATOM   965  N  N   . HIS A 1 119 ? -11.909 -2.701  14.744  1.00 7.16  ? 119 HIS A N   1 
ATOM   966  C  CA  . HIS A 1 119 ? -11.722 -1.482  15.550  1.00 7.36  ? 119 HIS A CA  1 
ATOM   967  C  C   . HIS A 1 119 ? -12.421 -0.321  14.870  1.00 6.46  ? 119 HIS A C   1 
ATOM   968  O  O   . HIS A 1 119 ? -12.014 0.047   13.766  1.00 7.76  ? 119 HIS A O   1 
ATOM   969  C  CB  . HIS A 1 119 ? -10.198 -1.223  15.621  1.00 7.42  ? 119 HIS A CB  1 
ATOM   970  C  CG  . HIS A 1 119 ? -9.545  -2.192  16.570  1.00 8.27  ? 119 HIS A CG  1 
ATOM   971  N  ND1 . HIS A 1 119 ? -8.187  -2.408  16.513  1.00 7.57  ? 119 HIS A ND1 1 
ATOM   972  C  CD2 . HIS A 1 119 ? -10.063 -3.027  17.487  1.00 8.00  ? 119 HIS A CD2 1 
ATOM   973  C  CE1 . HIS A 1 119 ? -7.867  -3.308  17.440  1.00 7.27  ? 119 HIS A CE1 1 
ATOM   974  N  NE2 . HIS A 1 119 ? -8.973  -3.720  18.063  1.00 8.16  ? 119 HIS A NE2 1 
ATOM   975  N  N   . LEU A 1 120 ? -13.423 0.225   15.583  1.00 7.11  ? 120 LEU A N   1 
ATOM   976  C  CA  . LEU A 1 120 ? -14.068 1.497   15.097  1.00 7.46  ? 120 LEU A CA  1 
ATOM   977  C  C   . LEU A 1 120 ? -13.440 2.640   15.899  1.00 6.79  ? 120 LEU A C   1 
ATOM   978  O  O   . LEU A 1 120 ? -13.555 2.653   17.105  1.00 7.50  ? 120 LEU A O   1 
ATOM   979  C  CB  . LEU A 1 120 ? -15.589 1.363   15.326  1.00 9.03  ? 120 LEU A CB  1 
ATOM   980  C  CG  . LEU A 1 120 ? -16.243 0.262   14.404  1.00 9.92  ? 120 LEU A CG  1 
ATOM   981  C  CD1 . LEU A 1 120 ? -17.192 -0.582  15.264  1.00 12.58 ? 120 LEU A CD1 1 
ATOM   982  C  CD2 . LEU A 1 120 ? -17.127 1.010   13.359  1.00 12.05 ? 120 LEU A CD2 1 
ATOM   983  N  N   . VAL A 1 121 ? -12.695 3.486   15.160  1.00 7.69  ? 121 VAL A N   1 
ATOM   984  C  CA  . VAL A 1 121 ? -11.858 4.488   15.805  1.00 8.42  ? 121 VAL A CA  1 
ATOM   985  C  C   . VAL A 1 121 ? -12.571 5.847   15.821  1.00 7.43  ? 121 VAL A C   1 
ATOM   986  O  O   . VAL A 1 121 ? -13.003 6.322   14.768  1.00 8.73  ? 121 VAL A O   1 
ATOM   987  C  CB  . VAL A 1 121 ? -10.531 4.590   14.965  1.00 7.98  ? 121 VAL A CB  1 
ATOM   988  C  CG1 . VAL A 1 121 ? -9.569  5.627   15.634  1.00 9.17  ? 121 VAL A CG1 1 
ATOM   989  C  CG2 . VAL A 1 121 ? -9.919  3.231   14.838  1.00 8.50  ? 121 VAL A CG2 1 
ATOM   990  N  N   . HIS A 1 122 ? -12.624 6.433   17.025  1.00 7.81  ? 122 HIS A N   1 
ATOM   991  C  CA  . HIS A 1 122 ? -13.326 7.695   17.202  1.00 7.85  ? 122 HIS A CA  1 
ATOM   992  C  C   . HIS A 1 122 ? -12.444 8.687   17.971  1.00 8.05  ? 122 HIS A C   1 
ATOM   993  O  O   . HIS A 1 122 ? -11.673 8.305   18.825  1.00 9.25  ? 122 HIS A O   1 
ATOM   994  C  CB  . HIS A 1 122 ? -14.594 7.506   18.057  1.00 9.91  ? 122 HIS A CB  1 
ATOM   995  C  CG  . HIS A 1 122 ? -15.481 6.387   17.626  1.00 9.23  ? 122 HIS A CG  1 
ATOM   996  N  ND1 . HIS A 1 122 ? -15.168 5.061   17.907  1.00 9.02  ? 122 HIS A ND1 1 
ATOM   997  C  CD2 . HIS A 1 122 ? -16.724 6.376   17.032  1.00 9.10  ? 122 HIS A CD2 1 
ATOM   998  C  CE1 . HIS A 1 122 ? -16.168 4.285   17.447  1.00 10.17 ? 122 HIS A CE1 1 
ATOM   999  N  NE2 . HIS A 1 122 ? -17.128 5.033   16.900  1.00 9.62  ? 122 HIS A NE2 1 
ATOM   1000 N  N   . TRP A 1 123 ? -12.577 9.987   17.642  1.00 8.68  ? 123 TRP A N   1 
ATOM   1001 C  CA  . TRP A 1 123 ? -11.785 10.985  18.358  1.00 8.93  ? 123 TRP A CA  1 
ATOM   1002 C  C   . TRP A 1 123 ? -12.647 12.002  19.091  1.00 8.44  ? 123 TRP A C   1 
ATOM   1003 O  O   . TRP A 1 123 ? -13.775 12.322  18.656  1.00 10.10 ? 123 TRP A O   1 
ATOM   1004 C  CB  . TRP A 1 123 ? -10.787 11.712  17.410  1.00 10.79 ? 123 TRP A CB  1 
ATOM   1005 C  CG  . TRP A 1 123 ? -11.428 12.324  16.190  1.00 11.76 ? 123 TRP A CG  1 
ATOM   1006 C  CD1 . TRP A 1 123 ? -11.640 11.739  14.960  1.00 10.53 ? 123 TRP A CD1 1 
ATOM   1007 C  CD2 . TRP A 1 123 ? -11.900 13.687  16.052  1.00 12.83 ? 123 TRP A CD2 1 
ATOM   1008 N  NE1 . TRP A 1 123 ? -12.228 12.638  14.086  1.00 12.33 ? 123 TRP A NE1 1 
ATOM   1009 C  CE2 . TRP A 1 123 ? -12.390 13.842  14.751  1.00 13.64 ? 123 TRP A CE2 1 
ATOM   1010 C  CE3 . TRP A 1 123 ? -11.929 14.781  16.930  1.00 12.82 ? 123 TRP A CE3 1 
ATOM   1011 C  CZ2 . TRP A 1 123 ? -12.929 15.033  14.282  1.00 15.13 ? 123 TRP A CZ2 1 
ATOM   1012 C  CZ3 . TRP A 1 123 ? -12.477 15.971  16.447  1.00 13.91 ? 123 TRP A CZ3 1 
ATOM   1013 C  CH2 . TRP A 1 123 ? -12.950 16.101  15.162  1.00 14.26 ? 123 TRP A CH2 1 
ATOM   1014 N  N   . ASN A 1 124 ? -12.098 12.472  20.233  1.00 9.82  ? 124 ASN A N   1 
ATOM   1015 C  CA  . ASN A 1 124 ? -12.855 13.352  21.135  1.00 9.14  ? 124 ASN A CA  1 
ATOM   1016 C  C   . ASN A 1 124 ? -12.979 14.733  20.522  1.00 11.00 ? 124 ASN A C   1 
ATOM   1017 O  O   . ASN A 1 124 ? -11.969 15.424  20.237  1.00 9.96  ? 124 ASN A O   1 
ATOM   1018 C  CB  . ASN A 1 124 ? -12.035 13.425  22.438  1.00 9.96  ? 124 ASN A CB  1 
ATOM   1019 C  CG  . ASN A 1 124 ? -12.784 14.033  23.529  1.00 10.81 ? 124 ASN A CG  1 
ATOM   1020 O  OD1 . ASN A 1 124 ? -13.643 14.913  23.290  1.00 12.06 ? 124 ASN A OD1 1 
ATOM   1021 N  ND2 . ASN A 1 124 ? -12.579 13.534  24.746  1.00 12.79 ? 124 ASN A ND2 1 
ATOM   1022 N  N   . THR A 1 125 ? -14.244 15.164  20.305  1.00 11.29 ? 125 THR A N   1 
ATOM   1023 C  CA  . THR A 1 125 ? -14.396 16.434  19.540  1.00 13.40 ? 125 THR A CA  1 
ATOM   1024 C  C   . THR A 1 125 ? -13.830 17.621  20.325  1.00 15.57 ? 125 THR A C   1 
ATOM   1025 O  O   . THR A 1 125 ? -13.711 18.677  19.751  1.00 13.95 ? 125 THR A O   1 
ATOM   1026 C  CB  . THR A 1 125 ? -15.906 16.633  19.201  1.00 14.90 ? 125 THR A CB  1 
ATOM   1027 O  OG1 . THR A 1 125 ? -16.665 16.626  20.423  1.00 18.32 ? 125 THR A OG1 1 
ATOM   1028 C  CG2 . THR A 1 125 ? -16.398 15.488  18.237  1.00 16.69 ? 125 THR A CG2 1 
ATOM   1029 N  N   . LYS A 1 126 ? -13.625 17.503  21.669  1.00 12.24 ? 127 LYS A N   1 
ATOM   1030 C  CA  . LYS A 1 126 ? -13.053 18.650  22.375  1.00 15.06 ? 127 LYS A CA  1 
ATOM   1031 C  C   . LYS A 1 126 ? -11.633 19.018  21.930  1.00 12.52 ? 127 LYS A C   1 
ATOM   1032 O  O   . LYS A 1 126 ? -11.132 20.129  22.281  1.00 17.67 ? 127 LYS A O   1 
ATOM   1033 C  CB  . LYS A 1 126 ? -13.162 18.414  23.843  1.00 16.42 ? 127 LYS A CB  1 
ATOM   1034 C  CG  . LYS A 1 126 ? -12.114 17.599  24.480  1.00 15.36 ? 127 LYS A CG  1 
ATOM   1035 C  CD  . LYS A 1 126 ? -12.552 17.113  25.909  1.00 21.86 ? 127 LYS A CD  1 
ATOM   1036 C  CE  . LYS A 1 126 ? -11.336 16.663  26.578  1.00 30.22 ? 127 LYS A CE  1 
ATOM   1037 N  NZ  . LYS A 1 126 ? -11.185 16.979  28.089  1.00 35.93 ? 127 LYS A NZ  1 
ATOM   1038 N  N   . TYR A 1 127 ? -11.031 18.109  21.156  1.00 11.55 ? 128 TYR A N   1 
ATOM   1039 C  CA  . TYR A 1 127 ? -9.685  18.412  20.606  1.00 11.95 ? 128 TYR A CA  1 
ATOM   1040 C  C   . TYR A 1 127 ? -9.648  18.781  19.143  1.00 12.06 ? 128 TYR A C   1 
ATOM   1041 O  O   . TYR A 1 127 ? -8.544  19.050  18.575  1.00 13.29 ? 128 TYR A O   1 
ATOM   1042 C  CB  . TYR A 1 127 ? -8.688  17.268  20.869  1.00 12.26 ? 128 TYR A CB  1 
ATOM   1043 C  CG  . TYR A 1 127 ? -8.607  16.920  22.342  1.00 12.07 ? 128 TYR A CG  1 
ATOM   1044 C  CD1 . TYR A 1 127 ? -8.202  17.892  23.306  1.00 12.91 ? 128 TYR A CD1 1 
ATOM   1045 C  CD2 . TYR A 1 127 ? -8.941  15.655  22.844  1.00 11.99 ? 128 TYR A CD2 1 
ATOM   1046 C  CE1 . TYR A 1 127 ? -8.115  17.600  24.638  1.00 13.84 ? 128 TYR A CE1 1 
ATOM   1047 C  CE2 . TYR A 1 127 ? -8.817  15.362  24.178  1.00 12.38 ? 128 TYR A CE2 1 
ATOM   1048 C  CZ  . TYR A 1 127 ? -8.438  16.393  25.083  1.00 11.84 ? 128 TYR A CZ  1 
ATOM   1049 O  OH  . TYR A 1 127 ? -8.395  16.142  26.380  1.00 15.60 ? 128 TYR A OH  1 
ATOM   1050 N  N   . GLY A 1 128 ? -10.837 18.909  18.533  1.00 12.10 ? 129 GLY A N   1 
ATOM   1051 C  CA  . GLY A 1 128 ? -10.827 19.619  17.220  1.00 12.96 ? 129 GLY A CA  1 
ATOM   1052 C  C   . GLY A 1 128 ? -10.538 18.729  15.976  1.00 12.45 ? 129 GLY A C   1 
ATOM   1053 O  O   . GLY A 1 128 ? -11.191 18.879  14.923  1.00 14.71 ? 129 GLY A O   1 
ATOM   1054 N  N   . ASP A 1 129 ? -9.527  17.861  16.086  1.00 13.88 ? 130 ASP A N   1 
ATOM   1055 C  CA  . ASP A 1 129 ? -9.263  16.946  15.009  1.00 14.17 ? 130 ASP A CA  1 
ATOM   1056 C  C   . ASP A 1 129 ? -8.498  15.762  15.543  1.00 14.04 ? 130 ASP A C   1 
ATOM   1057 O  O   . ASP A 1 129 ? -8.015  15.773  16.694  1.00 14.48 ? 130 ASP A O   1 
ATOM   1058 C  CB  . ASP A 1 129 ? -8.667  17.576  13.764  1.00 16.72 ? 130 ASP A CB  1 
ATOM   1059 C  CG  . ASP A 1 129 ? -7.260  18.057  13.960  1.00 14.61 ? 130 ASP A CG  1 
ATOM   1060 O  OD1 . ASP A 1 129 ? -6.608  17.748  14.982  1.00 22.59 ? 130 ASP A OD1 1 
ATOM   1061 O  OD2 . ASP A 1 129 ? -6.799  18.761  13.048  1.00 24.35 ? 130 ASP A OD2 1 
ATOM   1062 N  N   . PHE A 1 130 ? -8.414  14.743  14.699  1.00 14.59 ? 131 PHE A N   1 
ATOM   1063 C  CA  . PHE A 1 130 ? -7.763  13.493  15.137  1.00 12.71 ? 131 PHE A CA  1 
ATOM   1064 C  C   . PHE A 1 130 ? -6.288  13.701  15.478  1.00 13.44 ? 131 PHE A C   1 
ATOM   1065 O  O   . PHE A 1 130 ? -5.767  13.103  16.449  1.00 12.25 ? 131 PHE A O   1 
ATOM   1066 C  CB  . PHE A 1 130 ? -7.848  12.507  13.971  1.00 13.16 ? 131 PHE A CB  1 
ATOM   1067 C  CG  . PHE A 1 130 ? -7.221  11.142  14.250  1.00 11.00 ? 131 PHE A CG  1 
ATOM   1068 C  CD1 . PHE A 1 130 ? -7.917  10.172  14.950  1.00 10.68 ? 131 PHE A CD1 1 
ATOM   1069 C  CD2 . PHE A 1 130 ? -5.927  10.865  13.862  1.00 14.79 ? 131 PHE A CD2 1 
ATOM   1070 C  CE1 . PHE A 1 130 ? -7.373  8.935   15.208  1.00 14.09 ? 131 PHE A CE1 1 
ATOM   1071 C  CE2 . PHE A 1 130 ? -5.383  9.586   14.126  1.00 15.34 ? 131 PHE A CE2 1 
ATOM   1072 C  CZ  . PHE A 1 130 ? -6.165  8.649   14.804  1.00 16.90 ? 131 PHE A CZ  1 
ATOM   1073 N  N   . GLY A 1 131 ? -5.551  14.462  14.648  1.00 14.92 ? 132 GLY A N   1 
ATOM   1074 C  CA  . GLY A 1 131 ? -4.102  14.624  14.986  1.00 14.85 ? 132 GLY A CA  1 
ATOM   1075 C  C   . GLY A 1 131 ? -3.824  15.283  16.329  1.00 14.40 ? 132 GLY A C   1 
ATOM   1076 O  O   . GLY A 1 131 ? -2.807  14.965  17.005  1.00 15.68 ? 132 GLY A O   1 
ATOM   1077 N  N   . LYS A 1 132 ? -4.685  16.199  16.759  1.00 13.47 ? 133 LYS A N   1 
ATOM   1078 C  CA  . LYS A 1 132 ? -4.520  16.744  18.110  1.00 14.33 ? 133 LYS A CA  1 
ATOM   1079 C  C   . LYS A 1 132 ? -5.024  15.760  19.165  1.00 13.31 ? 133 LYS A C   1 
ATOM   1080 O  O   . LYS A 1 132 ? -4.470  15.657  20.266  1.00 13.28 ? 133 LYS A O   1 
ATOM   1081 C  CB  . LYS A 1 132 ? -5.324  18.088  18.195  1.00 15.13 ? 133 LYS A CB  1 
ATOM   1082 C  CG  . LYS A 1 132 ? -4.642  19.272  17.439  1.00 18.32 ? 133 LYS A CG  1 
ATOM   1083 C  CD  . LYS A 1 132 ? -3.256  19.614  18.120  1.00 24.80 ? 133 LYS A CD  1 
ATOM   1084 C  CE  . LYS A 1 132 ? -2.855  21.090  17.781  1.00 25.80 ? 133 LYS A CE  1 
ATOM   1085 N  NZ  . LYS A 1 132 ? -2.107  21.595  19.054  1.00 34.86 ? 133 LYS A NZ  1 
ATOM   1086 N  N   . ALA A 1 133 ? -6.120  15.042  18.867  1.00 11.83 ? 134 ALA A N   1 
ATOM   1087 C  CA  . ALA A 1 133 ? -6.620  14.112  19.839  1.00 11.20 ? 134 ALA A CA  1 
ATOM   1088 C  C   . ALA A 1 133 ? -5.662  13.024  20.239  1.00 10.54 ? 134 ALA A C   1 
ATOM   1089 O  O   . ALA A 1 133 ? -5.638  12.635  21.410  1.00 10.89 ? 134 ALA A O   1 
ATOM   1090 C  CB  . ALA A 1 133 ? -7.968  13.488  19.222  1.00 10.99 ? 134 ALA A CB  1 
ATOM   1091 N  N   . VAL A 1 134 ? -4.878  12.505  19.301  1.00 10.74 ? 135 VAL A N   1 
ATOM   1092 C  CA  . VAL A 1 134 ? -3.935  11.378  19.650  1.00 11.99 ? 135 VAL A CA  1 
ATOM   1093 C  C   . VAL A 1 134 ? -2.860  11.808  20.581  1.00 12.98 ? 135 VAL A C   1 
ATOM   1094 O  O   . VAL A 1 134 ? -2.168  10.965  21.156  1.00 13.09 ? 135 VAL A O   1 
ATOM   1095 C  CB  . VAL A 1 134 ? -3.248  10.696  18.449  1.00 14.11 ? 135 VAL A CB  1 
ATOM   1096 C  CG1 . VAL A 1 134 ? -4.251  10.010  17.591  1.00 15.67 ? 135 VAL A CG1 1 
ATOM   1097 C  CG2 . VAL A 1 134 ? -2.446  11.660  17.581  1.00 13.32 ? 135 VAL A CG2 1 
ATOM   1098 N  N   A GLN A 1 135 ? -2.689  13.135  20.776  0.50 12.48 ? 136 GLN A N   1 
ATOM   1099 N  N   B GLN A 1 135 ? -2.761  13.141  20.816  0.50 11.84 ? 136 GLN A N   1 
ATOM   1100 C  CA  A GLN A 1 135 ? -1.676  13.582  21.747  0.50 13.59 ? 136 GLN A CA  1 
ATOM   1101 C  CA  B GLN A 1 135 ? -1.775  13.686  21.775  0.50 12.73 ? 136 GLN A CA  1 
ATOM   1102 C  C   A GLN A 1 135 ? -2.304  13.825  23.138  0.50 12.95 ? 136 GLN A C   1 
ATOM   1103 C  C   B GLN A 1 135 ? -2.259  13.694  23.200  0.50 12.54 ? 136 GLN A C   1 
ATOM   1104 O  O   A GLN A 1 135 ? -1.713  14.526  24.029  0.50 14.02 ? 136 GLN A O   1 
ATOM   1105 O  O   B GLN A 1 135 ? -1.538  14.105  24.160  0.50 13.70 ? 136 GLN A O   1 
ATOM   1106 C  CB  A GLN A 1 135 ? -0.884  14.833  21.179  0.50 13.38 ? 136 GLN A CB  1 
ATOM   1107 C  CB  B GLN A 1 135 ? -1.329  15.117  21.310  0.50 11.89 ? 136 GLN A CB  1 
ATOM   1108 C  CG  A GLN A 1 135 ? -0.286  14.647  19.708  0.50 16.63 ? 136 GLN A CG  1 
ATOM   1109 C  CG  B GLN A 1 135 ? -0.686  14.998  19.988  0.50 14.60 ? 136 GLN A CG  1 
ATOM   1110 C  CD  A GLN A 1 135 ? 0.864   13.593  19.573  0.50 19.42 ? 136 GLN A CD  1 
ATOM   1111 C  CD  B GLN A 1 135 ? -0.115  16.257  19.453  0.50 18.04 ? 136 GLN A CD  1 
ATOM   1112 O  OE1 A GLN A 1 135 ? 1.620   13.363  20.524  0.50 27.26 ? 136 GLN A OE1 1 
ATOM   1113 O  OE1 B GLN A 1 135 ? 0.794   16.840  20.071  0.50 19.37 ? 136 GLN A OE1 1 
ATOM   1114 N  NE2 A GLN A 1 135 ? 1.036   13.018  18.361  0.50 25.23 ? 136 GLN A NE2 1 
ATOM   1115 N  NE2 B GLN A 1 135 ? -0.639  16.698  18.305  0.50 18.17 ? 136 GLN A NE2 1 
ATOM   1116 N  N   . GLN A 1 136 ? -3.494  13.269  23.396  1.00 11.70 ? 137 GLN A N   1 
ATOM   1117 C  CA  . GLN A 1 136 ? -4.168  13.513  24.696  1.00 11.38 ? 137 GLN A CA  1 
ATOM   1118 C  C   . GLN A 1 136 ? -4.537  12.165  25.317  1.00 11.57 ? 137 GLN A C   1 
ATOM   1119 O  O   . GLN A 1 136 ? -4.904  11.240  24.577  1.00 11.05 ? 137 GLN A O   1 
ATOM   1120 C  CB  . GLN A 1 136 ? -5.458  14.317  24.523  1.00 11.48 ? 137 GLN A CB  1 
ATOM   1121 C  CG  . GLN A 1 136 ? -5.275  15.579  23.677  1.00 16.35 ? 137 GLN A CG  1 
ATOM   1122 C  CD  . GLN A 1 136 ? -4.351  16.522  24.302  1.00 21.14 ? 137 GLN A CD  1 
ATOM   1123 O  OE1 . GLN A 1 136 ? -4.137  16.553  25.510  1.00 19.57 ? 137 GLN A OE1 1 
ATOM   1124 N  NE2 . GLN A 1 136 ? -3.758  17.375  23.451  1.00 28.65 ? 137 GLN A NE2 1 
ATOM   1125 N  N   . PRO A 1 137 ? -4.494  12.081  26.680  1.00 12.05 ? 138 PRO A N   1 
ATOM   1126 C  CA  . PRO A 1 137 ? -4.830  10.768  27.281  1.00 12.39 ? 138 PRO A CA  1 
ATOM   1127 C  C   . PRO A 1 137 ? -6.257  10.291  27.112  1.00 12.64 ? 138 PRO A C   1 
ATOM   1128 O  O   . PRO A 1 137 ? -6.495  9.084   27.193  1.00 14.91 ? 138 PRO A O   1 
ATOM   1129 C  CB  . PRO A 1 137 ? -4.453  10.922  28.757  1.00 14.59 ? 138 PRO A CB  1 
ATOM   1130 C  CG  . PRO A 1 137 ? -4.470  12.320  28.979  1.00 18.81 ? 138 PRO A CG  1 
ATOM   1131 C  CD  . PRO A 1 137 ? -4.060  13.087  27.683  1.00 14.29 ? 138 PRO A CD  1 
ATOM   1132 N  N   . ASP A 1 138 ? -7.197  11.225  26.787  1.00 10.89 ? 139 ASP A N   1 
ATOM   1133 C  CA  . ASP A 1 138 ? -8.599  10.898  26.549  1.00 11.12 ? 139 ASP A CA  1 
ATOM   1134 C  C   . ASP A 1 138 ? -8.936  11.300  25.126  1.00 10.09 ? 139 ASP A C   1 
ATOM   1135 O  O   . ASP A 1 138 ? -10.046 11.689  24.871  1.00 10.65 ? 139 ASP A O   1 
ATOM   1136 C  CB  . ASP A 1 138 ? -9.517  11.515  27.557  1.00 12.70 ? 139 ASP A CB  1 
ATOM   1137 C  CG  . ASP A 1 138 ? -9.414  13.033  27.601  1.00 13.36 ? 139 ASP A CG  1 
ATOM   1138 O  OD1 . ASP A 1 138 ? -8.445  13.599  26.994  1.00 13.75 ? 139 ASP A OD1 1 
ATOM   1139 O  OD2 . ASP A 1 138 ? -10.295 13.634  28.268  1.00 16.19 ? 139 ASP A OD2 1 
ATOM   1140 N  N   . GLY A 1 139 ? -7.966  11.183  24.212  1.00 9.42  ? 140 GLY A N   1 
ATOM   1141 C  CA  . GLY A 1 139 ? -8.184  11.677  22.829  1.00 9.75  ? 140 GLY A CA  1 
ATOM   1142 C  C   . GLY A 1 139 ? -9.048  10.763  21.957  1.00 8.17  ? 140 GLY A C   1 
ATOM   1143 O  O   . GLY A 1 139 ? -9.776  11.231  21.099  1.00 8.90  ? 140 GLY A O   1 
ATOM   1144 N  N   . LEU A 1 140 ? -8.935  9.451   22.149  1.00 7.71  ? 141 LEU A N   1 
ATOM   1145 C  CA  . LEU A 1 140 ? -9.619  8.497   21.274  1.00 7.23  ? 141 LEU A CA  1 
ATOM   1146 C  C   . LEU A 1 140 ? -10.509 7.532   22.038  1.00 7.55  ? 141 LEU A C   1 
ATOM   1147 O  O   . LEU A 1 140 ? -10.261 7.261   23.210  1.00 9.13  ? 141 LEU A O   1 
ATOM   1148 C  CB  . LEU A 1 140 ? -8.597  7.671   20.492  1.00 8.83  ? 141 LEU A CB  1 
ATOM   1149 C  CG  . LEU A 1 140 ? -7.646  8.340   19.502  1.00 11.95 ? 141 LEU A CG  1 
ATOM   1150 C  CD1 . LEU A 1 140 ? -6.999  7.293   18.605  1.00 10.48 ? 141 LEU A CD1 1 
ATOM   1151 C  CD2 . LEU A 1 140 ? -8.338  9.407   18.674  1.00 17.58 ? 141 LEU A CD2 1 
ATOM   1152 N  N   . ALA A 1 141 ? -11.525 6.993   21.363  1.00 7.96  ? 142 ALA A N   1 
ATOM   1153 C  CA  . ALA A 1 141 ? -12.304 5.874   21.949  1.00 7.95  ? 142 ALA A CA  1 
ATOM   1154 C  C   . ALA A 1 141 ? -12.347 4.883   20.803  1.00 9.32  ? 142 ALA A C   1 
ATOM   1155 O  O   . ALA A 1 141 ? -12.737 5.238   19.702  1.00 8.24  ? 142 ALA A O   1 
ATOM   1156 C  CB  . ALA A 1 141 ? -13.703 6.324   22.337  1.00 9.32  ? 142 ALA A CB  1 
ATOM   1157 N  N   . VAL A 1 142 ? -11.808 3.660   21.094  1.00 8.63  ? 143 VAL A N   1 
ATOM   1158 C  CA  . VAL A 1 142 ? -11.847 2.655   20.038  1.00 7.62  ? 143 VAL A CA  1 
ATOM   1159 C  C   . VAL A 1 142 ? -12.838 1.559   20.544  1.00 7.71  ? 143 VAL A C   1 
ATOM   1160 O  O   . VAL A 1 142 ? -12.726 1.049   21.647  1.00 7.07  ? 143 VAL A O   1 
ATOM   1161 C  CB  . VAL A 1 142 ? -10.458 2.057   19.669  1.00 7.40  ? 143 VAL A CB  1 
ATOM   1162 C  CG1 . VAL A 1 142 ? -10.661 1.029   18.543  1.00 8.56  ? 143 VAL A CG1 1 
ATOM   1163 C  CG2 . VAL A 1 142 ? -9.561  3.193   19.205  1.00 8.76  ? 143 VAL A CG2 1 
ATOM   1164 N  N   . LEU A 1 143 ? -13.827 1.299   19.657  1.00 7.38  ? 144 LEU A N   1 
ATOM   1165 C  CA  . LEU A 1 143 ? -14.823 0.250   19.966  1.00 8.57  ? 144 LEU A CA  1 
ATOM   1166 C  C   . LEU A 1 143 ? -14.275 -0.998  19.251  1.00 8.27  ? 144 LEU A C   1 
ATOM   1167 O  O   . LEU A 1 143 ? -14.166 -1.074  18.059  1.00 8.64  ? 144 LEU A O   1 
ATOM   1168 C  CB  . LEU A 1 143 ? -16.192 0.714   19.349  1.00 10.20 ? 144 LEU A CB  1 
ATOM   1169 C  CG  . LEU A 1 143 ? -17.335 -0.291  19.550  1.00 10.04 ? 144 LEU A CG  1 
ATOM   1170 C  CD1 . LEU A 1 143 ? -17.600 -0.587  21.015  1.00 13.22 ? 144 LEU A CD1 1 
ATOM   1171 C  CD2 . LEU A 1 143 ? -18.551 0.267   18.868  1.00 12.90 ? 144 LEU A CD2 1 
ATOM   1172 N  N   . GLY A 1 144 ? -14.008 -2.054  20.086  1.00 7.57  ? 145 GLY A N   1 
ATOM   1173 C  CA  . GLY A 1 144 ? -13.465 -3.288  19.528  1.00 8.31  ? 145 GLY A CA  1 
ATOM   1174 C  C   . GLY A 1 144 ? -14.526 -4.378  19.576  1.00 8.10  ? 145 GLY A C   1 
ATOM   1175 O  O   . GLY A 1 144 ? -15.252 -4.509  20.540  1.00 8.33  ? 145 GLY A O   1 
ATOM   1176 N  N   . ILE A 1 145 ? -14.552 -5.123  18.417  1.00 7.61  ? 146 ILE A N   1 
ATOM   1177 C  CA  . ILE A 1 145 ? -15.629 -6.184  18.314  1.00 7.84  ? 146 ILE A CA  1 
ATOM   1178 C  C   . ILE A 1 145 ? -14.912 -7.398  17.800  1.00 8.75  ? 146 ILE A C   1 
ATOM   1179 O  O   . ILE A 1 145 ? -14.189 -7.377  16.800  1.00 9.12  ? 146 ILE A O   1 
ATOM   1180 C  CB  . ILE A 1 145 ? -16.714 -5.655  17.322  1.00 8.92  ? 146 ILE A CB  1 
ATOM   1181 C  CG1 . ILE A 1 145 ? -17.316 -4.355  17.832  1.00 9.83  ? 146 ILE A CG1 1 
ATOM   1182 C  CG2 . ILE A 1 145 ? -17.786 -6.792  17.147  1.00 10.61 ? 146 ILE A CG2 1 
ATOM   1183 C  CD1 . ILE A 1 145 ? -18.376 -3.816  16.877  1.00 9.80  ? 146 ILE A CD1 1 
ATOM   1184 N  N   . PHE A 1 146 ? -15.118 -8.514  18.499  1.00 7.81  ? 147 PHE A N   1 
ATOM   1185 C  CA  . PHE A 1 146 ? -14.454 -9.806  18.059  1.00 7.88  ? 147 PHE A CA  1 
ATOM   1186 C  C   . PHE A 1 146 ? -15.228 -10.420 16.904  1.00 8.95  ? 147 PHE A C   1 
ATOM   1187 O  O   . PHE A 1 146 ? -16.464 -10.293 16.836  1.00 9.13  ? 147 PHE A O   1 
ATOM   1188 C  CB  . PHE A 1 146 ? -14.480 -10.750 19.240  1.00 7.43  ? 147 PHE A CB  1 
ATOM   1189 C  CG  . PHE A 1 146 ? -13.605 -10.289 20.369  1.00 7.79  ? 147 PHE A CG  1 
ATOM   1190 C  CD1 . PHE A 1 146 ? -12.227 -10.102 20.155  1.00 8.78  ? 147 PHE A CD1 1 
ATOM   1191 C  CD2 . PHE A 1 146 ? -14.110 -10.070 21.606  1.00 9.49  ? 147 PHE A CD2 1 
ATOM   1192 C  CE1 . PHE A 1 146 ? -11.364 -9.689  21.284  1.00 9.69  ? 147 PHE A CE1 1 
ATOM   1193 C  CE2 . PHE A 1 146 ? -13.328 -9.662  22.670  1.00 8.35  ? 147 PHE A CE2 1 
ATOM   1194 C  CZ  . PHE A 1 146 ? -11.958 -9.497  22.496  1.00 8.97  ? 147 PHE A CZ  1 
ATOM   1195 N  N   . LEU A 1 147 ? -14.482 -11.113 16.036  1.00 8.29  ? 148 LEU A N   1 
ATOM   1196 C  CA  . LEU A 1 147 ? -15.084 -11.881 14.925  1.00 9.25  ? 148 LEU A CA  1 
ATOM   1197 C  C   . LEU A 1 147 ? -14.723 -13.371 15.159  1.00 9.74  ? 148 LEU A C   1 
ATOM   1198 O  O   . LEU A 1 147 ? -13.576 -13.731 15.375  1.00 9.24  ? 148 LEU A O   1 
ATOM   1199 C  CB  . LEU A 1 147 ? -14.482 -11.515 13.588  1.00 10.16 ? 148 LEU A CB  1 
ATOM   1200 C  CG  . LEU A 1 147 ? -15.030 -10.258 12.910  1.00 10.48 ? 148 LEU A CG  1 
ATOM   1201 C  CD1 . LEU A 1 147 ? -14.837 -8.974  13.783  1.00 10.61 ? 148 LEU A CD1 1 
ATOM   1202 C  CD2 . LEU A 1 147 ? -14.434 -10.026 11.533  1.00 11.24 ? 148 LEU A CD2 1 
ATOM   1203 N  N   . LYS A 1 148 ? -15.759 -14.226 15.157  1.00 10.22 ? 149 LYS A N   1 
ATOM   1204 C  CA  . LYS A 1 148 ? -15.593 -15.681 15.086  1.00 10.01 ? 149 LYS A CA  1 
ATOM   1205 C  C   . LYS A 1 148 ? -16.087 -16.197 13.730  1.00 11.91 ? 149 LYS A C   1 
ATOM   1206 O  O   . LYS A 1 148 ? -16.904 -15.524 13.074  1.00 12.14 ? 149 LYS A O   1 
ATOM   1207 C  CB  . LYS A 1 148 ? -16.334 -16.378 16.227  1.00 12.03 ? 149 LYS A CB  1 
ATOM   1208 C  CG  . LYS A 1 148 ? -17.836 -16.247 16.136  1.00 14.10 ? 149 LYS A CG  1 
ATOM   1209 C  CD  . LYS A 1 148 ? -18.476 -16.913 17.401  1.00 18.14 ? 149 LYS A CD  1 
ATOM   1210 C  CE  . LYS A 1 148 ? -19.914 -17.187 17.112  1.00 25.90 ? 149 LYS A CE  1 
ATOM   1211 N  NZ  . LYS A 1 148 ? -20.519 -17.990 18.244  1.00 31.44 ? 149 LYS A NZ  1 
ATOM   1212 N  N   . VAL A 1 149 ? -15.565 -17.336 13.317  1.00 11.78 ? 150 VAL A N   1 
ATOM   1213 C  CA  . VAL A 1 149 ? -15.985 -17.859 12.051  1.00 12.51 ? 150 VAL A CA  1 
ATOM   1214 C  C   . VAL A 1 149 ? -17.212 -18.839 12.265  1.00 12.73 ? 150 VAL A C   1 
ATOM   1215 O  O   . VAL A 1 149 ? -17.167 -19.816 13.038  1.00 14.29 ? 150 VAL A O   1 
ATOM   1216 C  CB  . VAL A 1 149 ? -14.792 -18.638 11.423  1.00 11.98 ? 150 VAL A CB  1 
ATOM   1217 C  CG1 . VAL A 1 149 ? -15.199 -19.441 10.151  1.00 14.00 ? 150 VAL A CG1 1 
ATOM   1218 C  CG2 . VAL A 1 149 ? -13.686 -17.653 11.094  1.00 15.44 ? 150 VAL A CG2 1 
ATOM   1219 N  N   . GLY A 1 150 ? -18.237 -18.584 11.483  1.00 11.74 ? 151 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 150 ? -19.493 -19.375 11.573  1.00 14.09 ? 151 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 150 ? -20.354 -18.930 10.420  1.00 13.03 ? 151 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 150 ? -19.950 -19.025 9.243   1.00 13.54 ? 151 GLY A O   1 
ATOM   1223 N  N   A SER A 1 151 ? -21.571 -18.464 10.724  0.50 13.69 ? 152 SER A N   1 
ATOM   1224 N  N   B SER A 1 151 ? -21.536 -18.423 10.745  0.50 14.03 ? 152 SER A N   1 
ATOM   1225 C  CA  A SER A 1 151 ? -22.463 -17.906 9.661   0.50 13.61 ? 152 SER A CA  1 
ATOM   1226 C  CA  B SER A 1 151 ? -22.362 -17.834 9.688   0.50 13.86 ? 152 SER A CA  1 
ATOM   1227 C  C   A SER A 1 151 ? -21.913 -16.568 9.139   0.50 12.46 ? 152 SER A C   1 
ATOM   1228 C  C   B SER A 1 151 ? -21.708 -16.579 9.068   0.50 13.45 ? 152 SER A C   1 
ATOM   1229 O  O   A SER A 1 151 ? -21.277 -15.824 9.933   0.50 11.89 ? 152 SER A O   1 
ATOM   1230 O  O   B SER A 1 151 ? -20.820 -15.902 9.687   0.50 13.44 ? 152 SER A O   1 
ATOM   1231 C  CB  A SER A 1 151 ? -23.856 -17.623 10.230  0.50 16.88 ? 152 SER A CB  1 
ATOM   1232 C  CB  B SER A 1 151 ? -23.752 -17.471 10.222  0.50 17.17 ? 152 SER A CB  1 
ATOM   1233 O  OG  A SER A 1 151 ? -23.769 -16.584 11.192  0.50 17.54 ? 152 SER A OG  1 
ATOM   1234 O  OG  B SER A 1 151 ? -24.300 -18.620 10.835  0.50 18.10 ? 152 SER A OG  1 
ATOM   1235 N  N   . ALA A 1 152 ? -22.115 -16.272 7.835   1.00 13.34 ? 153 ALA A N   1 
ATOM   1236 C  CA  . ALA A 1 152 ? -21.718 -15.027 7.255   1.00 12.93 ? 153 ALA A CA  1 
ATOM   1237 C  C   . ALA A 1 152 ? -22.331 -13.804 7.961   1.00 12.61 ? 153 ALA A C   1 
ATOM   1238 O  O   . ALA A 1 152 ? -23.422 -13.872 8.488   1.00 14.57 ? 153 ALA A O   1 
ATOM   1239 C  CB  . ALA A 1 152 ? -22.078 -14.953 5.765   1.00 14.25 ? 153 ALA A CB  1 
ATOM   1240 N  N   . LYS A 1 153 ? -21.590 -12.678 7.899   1.00 13.39 ? 154 LYS A N   1 
ATOM   1241 C  CA  . LYS A 1 153 ? -22.132 -11.400 8.321   1.00 13.58 ? 154 LYS A CA  1 
ATOM   1242 C  C   . LYS A 1 153 ? -22.566 -10.616 7.091   1.00 12.80 ? 154 LYS A C   1 
ATOM   1243 O  O   . LYS A 1 153 ? -21.722 -10.168 6.323   1.00 12.05 ? 154 LYS A O   1 
ATOM   1244 C  CB  . LYS A 1 153 ? -21.053 -10.583 9.108   1.00 12.99 ? 154 LYS A CB  1 
ATOM   1245 C  CG  . LYS A 1 153 ? -21.619 -9.398  9.898   1.00 14.97 ? 154 LYS A CG  1 
ATOM   1246 C  CD  . LYS A 1 153 ? -22.554 -9.790  11.052  1.00 16.50 ? 154 LYS A CD  1 
ATOM   1247 C  CE  . LYS A 1 153 ? -22.719 -8.645  12.021  1.00 18.84 ? 154 LYS A CE  1 
ATOM   1248 N  NZ  . LYS A 1 153 ? -23.681 -9.018  13.038  1.00 20.00 ? 154 LYS A NZ  1 
ATOM   1249 N  N   . PRO A 1 154 ? -23.893 -10.523 6.847   1.00 14.01 ? 155 PRO A N   1 
ATOM   1250 C  CA  . PRO A 1 154 ? -24.272 -9.941  5.545   1.00 15.21 ? 155 PRO A CA  1 
ATOM   1251 C  C   . PRO A 1 154 ? -23.810 -8.500  5.434   1.00 15.58 ? 155 PRO A C   1 
ATOM   1252 O  O   . PRO A 1 154 ? -23.374 -8.122  4.331   1.00 16.81 ? 155 PRO A O   1 
ATOM   1253 C  CB  . PRO A 1 154 ? -25.817 -9.968  5.573   1.00 17.14 ? 155 PRO A CB  1 
ATOM   1254 C  CG  . PRO A 1 154 ? -26.114 -11.051 6.632   1.00 19.54 ? 155 PRO A CG  1 
ATOM   1255 C  CD  . PRO A 1 154 ? -25.021 -11.034 7.635   1.00 16.28 ? 155 PRO A CD  1 
ATOM   1256 N  N   . GLY A 1 155 ? -23.715 -7.748  6.536   1.00 14.43 ? 156 GLY A N   1 
ATOM   1257 C  CA  . GLY A 1 155 ? -23.283 -6.333  6.517   1.00 16.07 ? 156 GLY A CA  1 
ATOM   1258 C  C   . GLY A 1 155 ? -21.814 -6.190  6.261   1.00 15.47 ? 156 GLY A C   1 
ATOM   1259 O  O   . GLY A 1 155 ? -21.372 -5.062  5.994   1.00 17.38 ? 156 GLY A O   1 
ATOM   1260 N  N   . LEU A 1 156 ? -21.043 -7.248  6.281   1.00 14.20 ? 157 LEU A N   1 
ATOM   1261 C  CA  . LEU A 1 156 ? -19.608 -7.236  5.936   1.00 12.40 ? 157 LEU A CA  1 
ATOM   1262 C  C   . LEU A 1 156 ? -19.374 -7.501  4.476   1.00 13.45 ? 157 LEU A C   1 
ATOM   1263 O  O   . LEU A 1 156 ? -18.329 -7.146  3.949   1.00 12.94 ? 157 LEU A O   1 
ATOM   1264 C  CB  . LEU A 1 156 ? -18.841 -8.243  6.829   1.00 12.41 ? 157 LEU A CB  1 
ATOM   1265 C  CG  . LEU A 1 156 ? -17.314 -8.389  6.594   1.00 12.45 ? 157 LEU A CG  1 
ATOM   1266 C  CD1 . LEU A 1 156 ? -16.566 -7.101  6.999   1.00 14.20 ? 157 LEU A CD1 1 
ATOM   1267 C  CD2 . LEU A 1 156 ? -16.769 -9.538  7.447   1.00 12.20 ? 157 LEU A CD2 1 
ATOM   1268 N  N   . GLN A 1 157 ? -20.364 -8.011  3.706   1.00 13.71 ? 158 GLN A N   1 
ATOM   1269 C  CA  . GLN A 1 157 ? -20.031 -8.508  2.387   1.00 15.10 ? 158 GLN A CA  1 
ATOM   1270 C  C   . GLN A 1 157 ? -19.608 -7.375  1.461   1.00 14.00 ? 158 GLN A C   1 
ATOM   1271 O  O   . GLN A 1 157 ? -18.734 -7.575  0.633   1.00 14.67 ? 158 GLN A O   1 
ATOM   1272 C  CB  . GLN A 1 157 ? -21.212 -9.268  1.758   1.00 15.25 ? 158 GLN A CB  1 
ATOM   1273 C  CG  . GLN A 1 157 ? -20.777 -10.027 0.479   1.00 17.03 ? 158 GLN A CG  1 
ATOM   1274 C  CD  . GLN A 1 157 ? -19.605 -11.028 0.727   1.00 15.49 ? 158 GLN A CD  1 
ATOM   1275 O  OE1 . GLN A 1 157 ? -19.491 -11.633 1.838   1.00 16.47 ? 158 GLN A OE1 1 
ATOM   1276 N  NE2 . GLN A 1 157 ? -18.730 -11.248 -0.298  1.00 16.81 ? 158 GLN A NE2 1 
ATOM   1277 N  N   . LYS A 1 158 ? -20.174 -6.151  1.592   1.00 15.15 ? 159 LYS A N   1 
ATOM   1278 C  CA  . LYS A 1 158 ? -19.746 -5.061  0.715   1.00 14.63 ? 159 LYS A CA  1 
ATOM   1279 C  C   . LYS A 1 158 ? -18.260 -4.720  0.885   1.00 13.35 ? 159 LYS A C   1 
ATOM   1280 O  O   . LYS A 1 158 ? -17.574 -4.349  -0.055  1.00 14.83 ? 159 LYS A O   1 
ATOM   1281 C  CB  . LYS A 1 158 ? -20.646 -3.823  0.987   1.00 17.20 ? 159 LYS A CB  1 
ATOM   1282 C  CG  . LYS A 1 158 ? -21.977 -3.909  0.180   1.00 23.93 ? 159 LYS A CG  1 
ATOM   1283 C  CD  . LYS A 1 158 ? -21.805 -3.498  -1.271  0.01 20.75 ? 159 LYS A CD  1 
ATOM   1284 C  CE  . LYS A 1 158 ? -23.158 -3.452  -1.983  0.01 19.23 ? 159 LYS A CE  1 
ATOM   1285 N  NZ  . LYS A 1 158 ? -23.034 -2.824  -3.326  0.01 19.56 ? 159 LYS A NZ  1 
ATOM   1286 N  N   . VAL A 1 159 ? -17.794 -4.888  2.116   1.00 14.65 ? 160 VAL A N   1 
ATOM   1287 C  CA  . VAL A 1 159 ? -16.397 -4.627  2.370   1.00 13.23 ? 160 VAL A CA  1 
ATOM   1288 C  C   . VAL A 1 159 ? -15.581 -5.748  1.686   1.00 12.86 ? 160 VAL A C   1 
ATOM   1289 O  O   . VAL A 1 159 ? -14.614 -5.498  0.957   1.00 13.86 ? 160 VAL A O   1 
ATOM   1290 C  CB  . VAL A 1 159 ? -16.081 -4.591  3.839   1.00 13.69 ? 160 VAL A CB  1 
ATOM   1291 C  CG1 . VAL A 1 159 ? -14.526 -4.690  4.203   1.00 14.52 ? 160 VAL A CG1 1 
ATOM   1292 C  CG2 . VAL A 1 159 ? -16.780 -3.457  4.596   1.00 14.67 ? 160 VAL A CG2 1 
ATOM   1293 N  N   . VAL A 1 160 ? -15.959 -7.010  1.940   1.00 13.02 ? 161 VAL A N   1 
ATOM   1294 C  CA  . VAL A 1 160 ? -15.201 -8.076  1.341   1.00 15.68 ? 161 VAL A CA  1 
ATOM   1295 C  C   . VAL A 1 160 ? -15.071 -8.020  -0.158  1.00 15.95 ? 161 VAL A C   1 
ATOM   1296 O  O   . VAL A 1 160 ? -14.073 -8.308  -0.779  1.00 16.59 ? 161 VAL A O   1 
ATOM   1297 C  CB  . VAL A 1 160 ? -15.861 -9.426  1.760   1.00 17.01 ? 161 VAL A CB  1 
ATOM   1298 C  CG1 . VAL A 1 160 ? -15.368 -10.585 0.925   1.00 18.78 ? 161 VAL A CG1 1 
ATOM   1299 C  CG2 . VAL A 1 160 ? -15.658 -9.682  3.271   1.00 18.47 ? 161 VAL A CG2 1 
ATOM   1300 N  N   . ASP A 1 161 ? -16.172 -7.630  -0.771  1.00 16.59 ? 162 ASP A N   1 
ATOM   1301 C  CA  . ASP A 1 161 ? -16.201 -7.652  -2.261  1.00 17.98 ? 162 ASP A CA  1 
ATOM   1302 C  C   . ASP A 1 161 ? -15.390 -6.560  -2.921  1.00 19.10 ? 162 ASP A C   1 
ATOM   1303 O  O   . ASP A 1 161 ? -15.100 -6.723  -4.115  1.00 23.39 ? 162 ASP A O   1 
ATOM   1304 C  CB  . ASP A 1 161 ? -17.581 -7.625  -2.766  1.00 20.31 ? 162 ASP A CB  1 
ATOM   1305 C  CG  . ASP A 1 161 ? -18.189 -9.005  -2.698  1.00 22.48 ? 162 ASP A CG  1 
ATOM   1306 O  OD1 . ASP A 1 161 ? -17.460 -10.065 -2.788  1.00 23.42 ? 162 ASP A OD1 1 
ATOM   1307 O  OD2 . ASP A 1 161 ? -19.388 -9.010  -2.455  1.00 22.56 ? 162 ASP A OD2 1 
ATOM   1308 N  N   . VAL A 1 162 ? -14.960 -5.499  -2.177  1.00 15.95 ? 163 VAL A N   1 
ATOM   1309 C  CA  . VAL A 1 162 ? -14.158 -4.457  -2.772  1.00 17.04 ? 163 VAL A CA  1 
ATOM   1310 C  C   . VAL A 1 162 ? -12.663 -4.742  -2.579  1.00 15.77 ? 163 VAL A C   1 
ATOM   1311 O  O   . VAL A 1 162 ? -11.821 -4.093  -3.155  1.00 16.57 ? 163 VAL A O   1 
ATOM   1312 C  CB  . VAL A 1 162 ? -14.583 -3.045  -2.179  1.00 19.02 ? 163 VAL A CB  1 
ATOM   1313 C  CG1 . VAL A 1 162 ? -13.954 -2.799  -0.879  1.00 18.32 ? 163 VAL A CG1 1 
ATOM   1314 C  CG2 . VAL A 1 162 ? -14.277 -1.854  -3.081  1.00 18.78 ? 163 VAL A CG2 1 
ATOM   1315 N  N   . LEU A 1 163 ? -12.323 -5.752  -1.771  1.00 17.15 ? 164 LEU A N   1 
ATOM   1316 C  CA  . LEU A 1 163 ? -10.924 -5.971  -1.432  1.00 14.96 ? 164 LEU A CA  1 
ATOM   1317 C  C   . LEU A 1 163 ? -10.040 -6.309  -2.588  1.00 16.46 ? 164 LEU A C   1 
ATOM   1318 O  O   . LEU A 1 163 ? -8.872  -5.933  -2.621  1.00 16.47 ? 164 LEU A O   1 
ATOM   1319 C  CB  . LEU A 1 163 ? -10.734 -7.034  -0.308  1.00 14.79 ? 164 LEU A CB  1 
ATOM   1320 C  CG  . LEU A 1 163 ? -11.457 -6.670  1.000   1.00 14.08 ? 164 LEU A CG  1 
ATOM   1321 C  CD1 . LEU A 1 163 ? -11.182 -7.819  2.013   1.00 16.10 ? 164 LEU A CD1 1 
ATOM   1322 C  CD2 . LEU A 1 163 ? -10.881 -5.363  1.610   1.00 14.40 ? 164 LEU A CD2 1 
ATOM   1323 N  N   . ASP A 1 164 ? -10.579 -6.983  -3.606  1.00 18.87 ? 165 ASP A N   1 
ATOM   1324 C  CA  . ASP A 1 164 ? -9.687  -7.288  -4.767  1.00 21.59 ? 165 ASP A CA  1 
ATOM   1325 C  C   . ASP A 1 164 ? -9.277  -6.004  -5.533  1.00 22.15 ? 165 ASP A C   1 
ATOM   1326 O  O   . ASP A 1 164 ? -8.252  -6.053  -6.253  1.00 24.80 ? 165 ASP A O   1 
ATOM   1327 C  CB  . ASP A 1 164 ? -10.376 -8.225  -5.738  1.00 23.33 ? 165 ASP A CB  1 
ATOM   1328 C  CG  . ASP A 1 164 ? -11.337 -7.516  -6.543  1.00 29.11 ? 165 ASP A CG  1 
ATOM   1329 O  OD1 . ASP A 1 164 ? -12.363 -7.090  -5.964  1.00 32.64 ? 165 ASP A OD1 1 
ATOM   1330 O  OD2 . ASP A 1 164 ? -11.102 -7.369  -7.798  1.00 37.78 ? 165 ASP A OD2 1 
ATOM   1331 N  N   . SER A 1 165 ? -9.972  -4.871  -5.285  1.00 18.60 ? 166 SER A N   1 
ATOM   1332 C  CA  . SER A 1 165 ? -9.620  -3.579  -5.930  1.00 19.67 ? 166 SER A CA  1 
ATOM   1333 C  C   . SER A 1 165 ? -8.561  -2.858  -5.110  1.00 17.44 ? 166 SER A C   1 
ATOM   1334 O  O   . SER A 1 165 ? -7.988  -1.847  -5.618  1.00 19.38 ? 166 SER A O   1 
ATOM   1335 C  CB  . SER A 1 165 ? -10.842 -2.730  -6.198  1.00 23.54 ? 166 SER A CB  1 
ATOM   1336 O  OG  . SER A 1 165 ? -11.329 -2.204  -5.008  1.00 22.56 ? 166 SER A OG  1 
ATOM   1337 N  N   . ILE A 1 166 ? -8.312  -3.331  -3.851  1.00 15.83 ? 167 ILE A N   1 
ATOM   1338 C  CA  . ILE A 1 166 ? -7.267  -2.666  -3.054  1.00 14.94 ? 167 ILE A CA  1 
ATOM   1339 C  C   . ILE A 1 166 ? -6.228  -3.707  -2.557  1.00 14.09 ? 167 ILE A C   1 
ATOM   1340 O  O   . ILE A 1 166 ? -5.814  -3.700  -1.389  1.00 14.31 ? 167 ILE A O   1 
ATOM   1341 C  CB  . ILE A 1 166 ? -7.876  -1.832  -1.902  1.00 13.74 ? 167 ILE A CB  1 
ATOM   1342 C  CG1 . ILE A 1 166 ? -8.775  -2.707  -1.023  1.00 13.58 ? 167 ILE A CG1 1 
ATOM   1343 C  CG2 . ILE A 1 166 ? -8.605  -0.630  -2.469  1.00 15.82 ? 167 ILE A CG2 1 
ATOM   1344 C  CD1 . ILE A 1 166 ? -8.717  -2.160  0.412   1.00 15.68 ? 167 ILE A CD1 1 
ATOM   1345 N  N   . LYS A 1 167 ? -5.791  -4.593  -3.475  1.00 15.04 ? 168 LYS A N   1 
ATOM   1346 C  CA  . LYS A 1 167 ? -5.020  -5.710  -3.020  1.00 14.45 ? 168 LYS A CA  1 
ATOM   1347 C  C   . LYS A 1 167 ? -3.705  -5.320  -2.334  1.00 14.53 ? 168 LYS A C   1 
ATOM   1348 O  O   . LYS A 1 167 ? -3.221  -6.028  -1.427  1.00 14.37 ? 168 LYS A O   1 
ATOM   1349 C  CB  . LYS A 1 167 ? -4.748  -6.657  -4.247  1.00 15.99 ? 168 LYS A CB  1 
ATOM   1350 C  CG  . LYS A 1 167 ? -3.993  -7.914  -3.757  1.00 16.61 ? 168 LYS A CG  1 
ATOM   1351 C  CD  . LYS A 1 167 ? -3.946  -8.820  -4.983  1.00 24.26 ? 168 LYS A CD  1 
ATOM   1352 C  CE  . LYS A 1 167 ? -3.045  -9.951  -4.654  1.00 28.03 ? 168 LYS A CE  1 
ATOM   1353 N  NZ  . LYS A 1 167 ? -2.928  -10.911 -5.823  1.00 34.28 ? 168 LYS A NZ  1 
ATOM   1354 N  N   . THR A 1 168 ? -3.074  -4.265  -2.881  1.00 14.36 ? 169 THR A N   1 
ATOM   1355 C  CA  . THR A 1 168 ? -1.723  -3.991  -2.491  1.00 15.62 ? 169 THR A CA  1 
ATOM   1356 C  C   . THR A 1 168 ? -1.638  -2.566  -1.803  1.00 12.25 ? 169 THR A C   1 
ATOM   1357 O  O   . THR A 1 168 ? -2.538  -1.719  -1.919  1.00 14.77 ? 169 THR A O   1 
ATOM   1358 C  CB  . THR A 1 168 ? -0.763  -4.009  -3.741  1.00 16.68 ? 169 THR A CB  1 
ATOM   1359 O  OG1 . THR A 1 168 ? -1.386  -3.232  -4.754  1.00 16.95 ? 169 THR A OG1 1 
ATOM   1360 C  CG2 . THR A 1 168 ? -0.610  -5.511  -4.231  1.00 16.53 ? 169 THR A CG2 1 
ATOM   1361 N  N   . LYS A 1 169 ? -0.572  -2.438  -1.046  1.00 15.49 ? 170 LYS A N   1 
ATOM   1362 C  CA  . LYS A 1 169 ? -0.270  -1.241  -0.252  1.00 14.93 ? 170 LYS A CA  1 
ATOM   1363 C  C   . LYS A 1 169 ? -0.361  0.026   -1.047  1.00 15.57 ? 170 LYS A C   1 
ATOM   1364 O  O   . LYS A 1 169 ? 0.198   0.088   -2.196  1.00 18.84 ? 170 LYS A O   1 
ATOM   1365 C  CB  . LYS A 1 169 ? 1.150   -1.389  0.273   1.00 15.33 ? 170 LYS A CB  1 
ATOM   1366 C  CG  . LYS A 1 169 ? 1.623   -0.151  1.119   1.00 17.86 ? 170 LYS A CG  1 
ATOM   1367 C  CD  . LYS A 1 169 ? 2.953   -0.358  1.807   1.00 20.27 ? 170 LYS A CD  1 
ATOM   1368 C  CE  . LYS A 1 169 ? 3.549   0.972   2.424   1.00 29.73 ? 170 LYS A CE  1 
ATOM   1369 N  NZ  . LYS A 1 169 ? 5.046   0.881   2.938   1.00 33.21 ? 170 LYS A NZ  1 
ATOM   1370 N  N   . GLY A 1 170 ? -1.127  0.984   -0.533  1.00 16.17 ? 171 GLY A N   1 
ATOM   1371 C  CA  . GLY A 1 170 ? -1.281  2.284   -1.281  1.00 16.88 ? 171 GLY A CA  1 
ATOM   1372 C  C   . GLY A 1 170 ? -2.518  2.368   -2.180  1.00 19.38 ? 171 GLY A C   1 
ATOM   1373 O  O   . GLY A 1 170 ? -2.874  3.494   -2.655  1.00 22.46 ? 171 GLY A O   1 
ATOM   1374 N  N   . LYS A 1 171 ? -3.181  1.231   -2.496  1.00 15.72 ? 172 LYS A N   1 
ATOM   1375 C  CA  . LYS A 1 171 ? -4.403  1.297   -3.274  1.00 15.94 ? 172 LYS A CA  1 
ATOM   1376 C  C   . LYS A 1 171 ? -5.608  1.746   -2.479  1.00 15.30 ? 172 LYS A C   1 
ATOM   1377 O  O   . LYS A 1 171 ? -5.778  1.329   -1.319  1.00 14.97 ? 172 LYS A O   1 
ATOM   1378 C  CB  . LYS A 1 171 ? -4.681  -0.048  -3.937  1.00 17.11 ? 172 LYS A CB  1 
ATOM   1379 C  CG  . LYS A 1 171 ? -3.651  -0.538  -4.910  1.00 19.97 ? 172 LYS A CG  1 
ATOM   1380 C  CD  . LYS A 1 171 ? -4.289  -1.597  -5.831  1.00 25.53 ? 172 LYS A CD  1 
ATOM   1381 C  CE  . LYS A 1 171 ? -5.141  -1.051  -7.043  1.00 30.18 ? 172 LYS A CE  1 
ATOM   1382 N  NZ  . LYS A 1 171 ? -5.634  -2.245  -7.912  1.00 27.05 ? 172 LYS A NZ  1 
ATOM   1383 N  N   . SER A 1 172 ? -6.452  2.594   -3.043  1.00 15.78 ? 173 SER A N   1 
ATOM   1384 C  CA  . SER A 1 172 ? -7.706  3.003   -2.453  1.00 14.91 ? 173 SER A CA  1 
ATOM   1385 C  C   . SER A 1 172 ? -8.835  2.844   -3.487  1.00 15.71 ? 173 SER A C   1 
ATOM   1386 O  O   . SER A 1 172 ? -8.581  2.816   -4.759  1.00 18.34 ? 173 SER A O   1 
ATOM   1387 C  CB  . SER A 1 172 ? -7.632  4.458   -1.945  1.00 14.34 ? 173 SER A CB  1 
ATOM   1388 O  OG  . SER A 1 172 ? -7.395  5.357   -3.003  1.00 20.07 ? 173 SER A OG  1 
ATOM   1389 N  N   . ALA A 1 173 ? -10.060 2.836   -2.965  1.00 17.31 ? 174 ALA A N   1 
ATOM   1390 C  CA  . ALA A 1 173 ? -11.269 2.801   -3.830  1.00 16.25 ? 174 ALA A CA  1 
ATOM   1391 C  C   . ALA A 1 173 ? -12.423 3.574   -3.158  1.00 17.17 ? 174 ALA A C   1 
ATOM   1392 O  O   . ALA A 1 173 ? -12.519 3.661   -1.920  1.00 15.56 ? 174 ALA A O   1 
ATOM   1393 C  CB  . ALA A 1 173 ? -11.635 1.322   -4.132  1.00 18.66 ? 174 ALA A CB  1 
ATOM   1394 N  N   . ASP A 1 174 ? -13.263 4.203   -3.988  1.00 19.03 ? 175 ASP A N   1 
ATOM   1395 C  CA  . ASP A 1 174 ? -14.435 4.904   -3.456  1.00 17.87 ? 175 ASP A CA  1 
ATOM   1396 C  C   . ASP A 1 174 ? -15.223 3.863   -2.710  1.00 17.11 ? 175 ASP A C   1 
ATOM   1397 O  O   . ASP A 1 174 ? -15.281 2.671   -3.083  1.00 20.93 ? 175 ASP A O   1 
ATOM   1398 C  CB  . ASP A 1 174 ? -15.313 5.463   -4.628  1.00 21.07 ? 175 ASP A CB  1 
ATOM   1399 C  CG  . ASP A 1 174 ? -14.573 6.542   -5.433  1.00 27.45 ? 175 ASP A CG  1 
ATOM   1400 O  OD1 . ASP A 1 174 ? -13.793 7.384   -4.874  1.00 34.31 ? 175 ASP A OD1 1 
ATOM   1401 O  OD2 . ASP A 1 174 ? -14.785 6.615   -6.704  1.00 29.90 ? 175 ASP A OD2 1 
ATOM   1402 N  N   . PHE A 1 175 ? -15.782 4.303   -1.585  1.00 16.24 ? 176 PHE A N   1 
ATOM   1403 C  CA  . PHE A 1 175 ? -16.519 3.362   -0.725  1.00 14.65 ? 176 PHE A CA  1 
ATOM   1404 C  C   . PHE A 1 175 ? -17.562 4.138   0.014   1.00 15.13 ? 176 PHE A C   1 
ATOM   1405 O  O   . PHE A 1 175 ? -17.462 4.384   1.211   1.00 17.53 ? 176 PHE A O   1 
ATOM   1406 C  CB  . PHE A 1 175 ? -15.541 2.525   0.116   1.00 14.44 ? 176 PHE A CB  1 
ATOM   1407 C  CG  . PHE A 1 175 ? -16.162 1.283   0.690   1.00 14.66 ? 176 PHE A CG  1 
ATOM   1408 C  CD1 . PHE A 1 175 ? -16.434 0.221   -0.137  1.00 16.28 ? 176 PHE A CD1 1 
ATOM   1409 C  CD2 . PHE A 1 175 ? -16.468 1.182   2.038   1.00 14.72 ? 176 PHE A CD2 1 
ATOM   1410 C  CE1 . PHE A 1 175 ? -16.998 -0.891  0.368   1.00 19.63 ? 176 PHE A CE1 1 
ATOM   1411 C  CE2 . PHE A 1 175 ? -17.033 -0.013  2.548   1.00 16.34 ? 176 PHE A CE2 1 
ATOM   1412 C  CZ  . PHE A 1 175 ? -17.314 -1.040  1.694   1.00 16.48 ? 176 PHE A CZ  1 
ATOM   1413 N  N   . THR A 1 176 ? -18.547 4.617   -0.732  1.00 14.14 ? 177 THR A N   1 
ATOM   1414 C  CA  . THR A 1 176 ? -19.612 5.424   -0.144  1.00 15.49 ? 177 THR A CA  1 
ATOM   1415 C  C   . THR A 1 176 ? -20.787 4.623   0.277   1.00 13.60 ? 177 THR A C   1 
ATOM   1416 O  O   . THR A 1 176 ? -20.963 3.477   -0.201  1.00 15.05 ? 177 THR A O   1 
ATOM   1417 C  CB  . THR A 1 176 ? -20.086 6.461   -1.174  1.00 15.06 ? 177 THR A CB  1 
ATOM   1418 O  OG1 . THR A 1 176 ? -20.373 5.834   -2.407  1.00 20.17 ? 177 THR A OG1 1 
ATOM   1419 C  CG2 . THR A 1 176 ? -18.977 7.571   -1.362  1.00 19.31 ? 177 THR A CG2 1 
ATOM   1420 N  N   . ASN A 1 177 ? -21.622 5.200   1.139   1.00 13.68 ? 178 ASN A N   1 
ATOM   1421 C  CA  . ASN A 1 177 ? -22.879 4.620   1.544   1.00 14.59 ? 178 ASN A CA  1 
ATOM   1422 C  C   . ASN A 1 177 ? -22.727 3.301   2.309   1.00 14.11 ? 178 ASN A C   1 
ATOM   1423 O  O   . ASN A 1 177 ? -23.637 2.536   2.240   1.00 18.28 ? 178 ASN A O   1 
ATOM   1424 C  CB  . ASN A 1 177 ? -23.788 4.494   0.299   1.00 14.74 ? 178 ASN A CB  1 
ATOM   1425 C  CG  . ASN A 1 177 ? -24.064 5.893   -0.299  1.00 16.54 ? 178 ASN A CG  1 
ATOM   1426 O  OD1 . ASN A 1 177 ? -24.706 6.708   0.360   1.00 18.56 ? 178 ASN A OD1 1 
ATOM   1427 N  ND2 . ASN A 1 177 ? -23.446 6.172   -1.430  1.00 16.36 ? 178 ASN A ND2 1 
ATOM   1428 N  N   . PHE A 1 178 ? -21.569 3.070   2.954   1.00 13.98 ? 179 PHE A N   1 
ATOM   1429 C  CA  . PHE A 1 178 ? -21.449 1.855   3.722   1.00 14.94 ? 179 PHE A CA  1 
ATOM   1430 C  C   . PHE A 1 178 ? -21.985 2.128   5.114   1.00 13.40 ? 179 PHE A C   1 
ATOM   1431 O  O   . PHE A 1 178 ? -21.551 3.083   5.753   1.00 15.28 ? 179 PHE A O   1 
ATOM   1432 C  CB  . PHE A 1 178 ? -20.014 1.375   3.801   1.00 13.38 ? 179 PHE A CB  1 
ATOM   1433 C  CG  . PHE A 1 178 ? -19.909 0.146   4.663   1.00 13.28 ? 179 PHE A CG  1 
ATOM   1434 C  CD1 . PHE A 1 178 ? -20.271 -1.104  4.122   1.00 13.86 ? 179 PHE A CD1 1 
ATOM   1435 C  CD2 . PHE A 1 178 ? -19.483 0.252   5.977   1.00 12.91 ? 179 PHE A CD2 1 
ATOM   1436 C  CE1 . PHE A 1 178 ? -20.271 -2.206  4.935   1.00 14.40 ? 179 PHE A CE1 1 
ATOM   1437 C  CE2 . PHE A 1 178 ? -19.471 -0.953  6.773   1.00 12.64 ? 179 PHE A CE2 1 
ATOM   1438 C  CZ  . PHE A 1 178 ? -19.861 -2.153  6.231   1.00 14.25 ? 179 PHE A CZ  1 
ATOM   1439 N  N   . ASP A 1 179 ? -22.828 1.241   5.671   1.00 14.82 ? 180 ASP A N   1 
ATOM   1440 C  CA  . ASP A 1 179 ? -23.468 1.490   6.968   1.00 14.01 ? 180 ASP A CA  1 
ATOM   1441 C  C   . ASP A 1 179 ? -22.788 0.627   8.028   1.00 11.99 ? 180 ASP A C   1 
ATOM   1442 O  O   . ASP A 1 179 ? -22.987 -0.592  8.033   1.00 13.09 ? 180 ASP A O   1 
ATOM   1443 C  CB  . ASP A 1 179 ? -24.958 1.147   6.860   1.00 15.56 ? 180 ASP A CB  1 
ATOM   1444 C  CG  . ASP A 1 179 ? -25.723 1.554   8.078   1.00 19.00 ? 180 ASP A CG  1 
ATOM   1445 O  OD1 . ASP A 1 179 ? -25.116 1.724   9.170   1.00 15.72 ? 180 ASP A OD1 1 
ATOM   1446 O  OD2 . ASP A 1 179 ? -26.940 1.684   7.970   1.00 26.71 ? 180 ASP A OD2 1 
ATOM   1447 N  N   . PRO A 1 180 ? -21.971 1.233   8.920   1.00 11.83 ? 181 PRO A N   1 
ATOM   1448 C  CA  . PRO A 1 180 ? -21.248 0.377   9.868   1.00 11.56 ? 181 PRO A CA  1 
ATOM   1449 C  C   . PRO A 1 180 ? -22.174 -0.237  10.917  1.00 12.59 ? 181 PRO A C   1 
ATOM   1450 O  O   . PRO A 1 180 ? -21.739 -1.149  11.691  1.00 12.21 ? 181 PRO A O   1 
ATOM   1451 C  CB  . PRO A 1 180 ? -20.243 1.338   10.487  1.00 13.27 ? 181 PRO A CB  1 
ATOM   1452 C  CG  . PRO A 1 180 ? -20.930 2.743   10.379  1.00 12.75 ? 181 PRO A CG  1 
ATOM   1453 C  CD  . PRO A 1 180 ? -21.668 2.673   9.039   1.00 12.18 ? 181 PRO A CD  1 
ATOM   1454 N  N   . ARG A 1 181 ? -23.476 0.157   10.948  1.00 11.91 ? 182 ARG A N   1 
ATOM   1455 C  CA  . ARG A 1 181 ? -24.378 -0.528  11.906  1.00 12.68 ? 182 ARG A CA  1 
ATOM   1456 C  C   . ARG A 1 181 ? -24.470 -2.006  11.547  1.00 13.51 ? 182 ARG A C   1 
ATOM   1457 O  O   . ARG A 1 181 ? -24.786 -2.833  12.399  1.00 14.35 ? 182 ARG A O   1 
ATOM   1458 C  CB  . ARG A 1 181 ? -25.759 0.112   11.872  1.00 14.06 ? 182 ARG A CB  1 
ATOM   1459 C  CG  . ARG A 1 181 ? -25.668 1.570   12.432  1.00 15.14 ? 182 ARG A CG  1 
ATOM   1460 C  CD  . ARG A 1 181 ? -27.014 2.203   12.439  1.00 17.54 ? 182 ARG A CD  1 
ATOM   1461 N  NE  . ARG A 1 181 ? -27.407 2.434   11.037  1.00 16.95 ? 182 ARG A NE  1 
ATOM   1462 C  CZ  . ARG A 1 181 ? -28.525 3.065   10.721  1.00 18.39 ? 182 ARG A CZ  1 
ATOM   1463 N  NH1 . ARG A 1 181 ? -29.253 3.544   11.712  1.00 22.49 ? 182 ARG A NH1 1 
ATOM   1464 N  NH2 . ARG A 1 181 ? -28.853 3.216   9.426   1.00 21.91 ? 182 ARG A NH2 1 
ATOM   1465 N  N   . GLY A 1 182 ? -24.250 -2.366  10.294  1.00 13.78 ? 183 GLY A N   1 
ATOM   1466 C  CA  . GLY A 1 182 ? -24.291 -3.799  9.866   1.00 14.58 ? 183 GLY A CA  1 
ATOM   1467 C  C   . GLY A 1 182 ? -23.133 -4.667  10.439  1.00 14.68 ? 183 GLY A C   1 
ATOM   1468 O  O   . GLY A 1 182 ? -23.087 -5.840  10.119  1.00 15.54 ? 183 GLY A O   1 
ATOM   1469 N  N   . LEU A 1 183 ? -22.192 -4.078  11.181  1.00 13.51 ? 184 LEU A N   1 
ATOM   1470 C  CA  . LEU A 1 183 ? -21.048 -4.816  11.719  1.00 13.35 ? 184 LEU A CA  1 
ATOM   1471 C  C   . LEU A 1 183 ? -21.197 -5.023  13.233  1.00 11.46 ? 184 LEU A C   1 
ATOM   1472 O  O   . LEU A 1 183 ? -20.267 -5.580  13.873  1.00 13.09 ? 184 LEU A O   1 
ATOM   1473 C  CB  . LEU A 1 183 ? -19.740 -4.074  11.492  1.00 12.71 ? 184 LEU A CB  1 
ATOM   1474 C  CG  . LEU A 1 183 ? -19.460 -3.932  10.001  1.00 13.08 ? 184 LEU A CG  1 
ATOM   1475 C  CD1 . LEU A 1 183 ? -18.238 -3.119  9.752   1.00 16.52 ? 184 LEU A CD1 1 
ATOM   1476 C  CD2 . LEU A 1 183 ? -19.340 -5.262  9.225   1.00 16.53 ? 184 LEU A CD2 1 
ATOM   1477 N  N   . LEU A 1 184 ? -22.271 -4.519  13.850  1.00 12.79 ? 185 LEU A N   1 
ATOM   1478 C  CA  . LEU A 1 184 ? -22.463 -4.588  15.325  1.00 12.63 ? 185 LEU A CA  1 
ATOM   1479 C  C   . LEU A 1 184 ? -23.196 -5.859  15.763  1.00 13.12 ? 185 LEU A C   1 
ATOM   1480 O  O   . LEU A 1 184 ? -24.059 -6.409  15.007  1.00 19.09 ? 185 LEU A O   1 
ATOM   1481 C  CB  . LEU A 1 184 ? -23.287 -3.363  15.858  1.00 12.61 ? 185 LEU A CB  1 
ATOM   1482 C  CG  . LEU A 1 184 ? -22.716 -1.991  15.420  1.00 12.04 ? 185 LEU A CG  1 
ATOM   1483 C  CD1 . LEU A 1 184 ? -23.565 -0.889  15.945  1.00 14.96 ? 185 LEU A CD1 1 
ATOM   1484 C  CD2 . LEU A 1 184 ? -21.327 -1.867  15.897  1.00 14.51 ? 185 LEU A CD2 1 
ATOM   1485 N  N   . PRO A 1 185 ? -22.850 -6.409  16.916  1.00 11.10 ? 186 PRO A N   1 
ATOM   1486 C  CA  . PRO A 1 185 ? -23.603 -7.576  17.431  1.00 11.85 ? 186 PRO A CA  1 
ATOM   1487 C  C   . PRO A 1 185 ? -24.908 -7.028  18.046  1.00 11.76 ? 186 PRO A C   1 
ATOM   1488 O  O   . PRO A 1 185 ? -25.123 -5.818  18.111  1.00 14.19 ? 186 PRO A O   1 
ATOM   1489 C  CB  . PRO A 1 185 ? -22.668 -8.175  18.483  1.00 11.18 ? 186 PRO A CB  1 
ATOM   1490 C  CG  . PRO A 1 185 ? -21.947 -6.926  19.032  1.00 11.00 ? 186 PRO A CG  1 
ATOM   1491 C  CD  . PRO A 1 185 ? -21.703 -6.009  17.765  1.00 10.63 ? 186 PRO A CD  1 
ATOM   1492 N  N   A GLU A 1 186 ? -25.692 -7.973  18.568  0.50 12.95 ? 187 GLU A N   1 
ATOM   1493 N  N   B GLU A 1 186 ? -25.779 -7.926  18.549  0.50 13.53 ? 187 GLU A N   1 
ATOM   1494 C  CA  A GLU A 1 186 ? -26.948 -7.617  19.153  0.50 13.11 ? 187 GLU A CA  1 
ATOM   1495 C  CA  B GLU A 1 186 ? -27.006 -7.410  19.171  0.50 13.83 ? 187 GLU A CA  1 
ATOM   1496 C  C   A GLU A 1 186 ? -26.823 -6.855  20.469  0.50 11.53 ? 187 GLU A C   1 
ATOM   1497 C  C   B GLU A 1 186 ? -26.704 -6.695  20.429  0.50 12.41 ? 187 GLU A C   1 
ATOM   1498 O  O   A GLU A 1 186 ? -27.568 -5.888  20.737  0.50 13.67 ? 187 GLU A O   1 
ATOM   1499 O  O   B GLU A 1 186 ? -27.195 -5.549  20.592  0.50 14.14 ? 187 GLU A O   1 
ATOM   1500 C  CB  A GLU A 1 186 ? -27.704 -8.938  19.372  0.50 14.29 ? 187 GLU A CB  1 
ATOM   1501 C  CB  B GLU A 1 186 ? -27.981 -8.552  19.491  0.50 16.35 ? 187 GLU A CB  1 
ATOM   1502 C  CG  A GLU A 1 186 ? -28.959 -8.704  20.132  0.50 16.29 ? 187 GLU A CG  1 
ATOM   1503 C  CG  B GLU A 1 186 ? -28.472 -9.309  18.286  0.50 17.24 ? 187 GLU A CG  1 
ATOM   1504 C  CD  A GLU A 1 186 ? -29.536 -10.001 20.684  0.50 19.53 ? 187 GLU A CD  1 
ATOM   1505 C  CD  B GLU A 1 186 ? -29.348 -10.482 18.662  0.50 21.42 ? 187 GLU A CD  1 
ATOM   1506 O  OE1 A GLU A 1 186 ? -29.325 -11.060 20.042  0.50 22.97 ? 187 GLU A OE1 1 
ATOM   1507 O  OE1 B GLU A 1 186 ? -29.502 -10.757 19.864  0.50 15.51 ? 187 GLU A OE1 1 
ATOM   1508 O  OE2 A GLU A 1 186 ? -30.178 -9.931  21.739  0.50 20.36 ? 187 GLU A OE2 1 
ATOM   1509 O  OE2 B GLU A 1 186 ? -29.888 -11.071 17.717  0.50 22.49 ? 187 GLU A OE2 1 
ATOM   1510 N  N   . SER A 1 187 ? -25.898 -7.292  21.328  1.00 12.30 ? 188 SER A N   1 
ATOM   1511 C  CA  . SER A 1 187 ? -25.742 -6.666  22.608  1.00 12.19 ? 188 SER A CA  1 
ATOM   1512 C  C   . SER A 1 187 ? -24.597 -5.638  22.592  1.00 12.71 ? 188 SER A C   1 
ATOM   1513 O  O   . SER A 1 187 ? -23.538 -5.874  21.985  1.00 14.33 ? 188 SER A O   1 
ATOM   1514 C  CB  . SER A 1 187 ? -25.298 -7.755  23.621  1.00 14.35 ? 188 SER A CB  1 
ATOM   1515 O  OG  . SER A 1 187 ? -25.056 -7.182  24.903  1.00 14.94 ? 188 SER A OG  1 
ATOM   1516 N  N   . LEU A 1 188 ? -24.769 -4.596  23.383  1.00 12.60 ? 189 LEU A N   1 
ATOM   1517 C  CA  . LEU A 1 188 ? -23.681 -3.561  23.582  1.00 14.20 ? 189 LEU A CA  1 
ATOM   1518 C  C   . LEU A 1 188 ? -23.020 -3.709  24.927  1.00 12.50 ? 189 LEU A C   1 
ATOM   1519 O  O   . LEU A 1 188 ? -22.340 -2.784  25.399  1.00 14.03 ? 189 LEU A O   1 
ATOM   1520 C  CB  . LEU A 1 188 ? -24.187 -2.093  23.304  1.00 14.27 ? 189 LEU A CB  1 
ATOM   1521 C  CG  . LEU A 1 188 ? -24.608 -1.818  21.854  1.00 16.18 ? 189 LEU A CG  1 
ATOM   1522 C  CD1 . LEU A 1 188 ? -25.171 -0.335  21.804  1.00 16.61 ? 189 LEU A CD1 1 
ATOM   1523 C  CD2 . LEU A 1 188 ? -23.487 -2.045  20.808  1.00 19.74 ? 189 LEU A CD2 1 
ATOM   1524 N  N   . ASP A 1 189 ? -23.166 -4.885  25.596  1.00 13.34 ? 190 ASP A N   1 
ATOM   1525 C  CA  . ASP A 1 189 ? -22.406 -5.083  26.798  1.00 13.23 ? 190 ASP A CA  1 
ATOM   1526 C  C   . ASP A 1 189 ? -20.895 -5.028  26.521  1.00 10.52 ? 190 ASP A C   1 
ATOM   1527 O  O   . ASP A 1 189 ? -20.472 -5.523  25.489  1.00 10.29 ? 190 ASP A O   1 
ATOM   1528 C  CB  . ASP A 1 189 ? -22.716 -6.437  27.426  1.00 13.54 ? 190 ASP A CB  1 
ATOM   1529 C  CG  . ASP A 1 189 ? -24.114 -6.502  28.119  1.00 19.02 ? 190 ASP A CG  1 
ATOM   1530 O  OD1 . ASP A 1 189 ? -24.780 -5.470  28.267  1.00 23.37 ? 190 ASP A OD1 1 
ATOM   1531 O  OD2 . ASP A 1 189 ? -24.575 -7.623  28.427  1.00 25.64 ? 190 ASP A OD2 1 
ATOM   1532 N  N   . TYR A 1 190 ? -20.111 -4.457  27.455  1.00 10.24 ? 191 TYR A N   1 
ATOM   1533 C  CA  . TYR A 1 190 ? -18.707 -4.227  27.133  1.00 9.34  ? 191 TYR A CA  1 
ATOM   1534 C  C   . TYR A 1 190 ? -17.794 -4.268  28.318  1.00 9.47  ? 191 TYR A C   1 
ATOM   1535 O  O   . TYR A 1 190 ? -18.240 -4.136  29.491  1.00 10.58 ? 191 TYR A O   1 
ATOM   1536 C  CB  . TYR A 1 190 ? -18.577 -2.818  26.406  1.00 10.27 ? 191 TYR A CB  1 
ATOM   1537 C  CG  . TYR A 1 190 ? -18.954 -1.667  27.302  1.00 9.75  ? 191 TYR A CG  1 
ATOM   1538 C  CD1 . TYR A 1 190 ? -18.010 -1.072  28.179  1.00 10.17 ? 191 TYR A CD1 1 
ATOM   1539 C  CD2 . TYR A 1 190 ? -20.256 -1.123  27.277  1.00 10.47 ? 191 TYR A CD2 1 
ATOM   1540 C  CE1 . TYR A 1 190 ? -18.408 -0.028  29.052  1.00 10.69 ? 191 TYR A CE1 1 
ATOM   1541 C  CE2 . TYR A 1 190 ? -20.641 -0.020  28.058  1.00 11.36 ? 191 TYR A CE2 1 
ATOM   1542 C  CZ  . TYR A 1 190 ? -19.742 0.499   28.961  1.00 12.07 ? 191 TYR A CZ  1 
ATOM   1543 O  OH  . TYR A 1 190 ? -20.123 1.531   29.808  1.00 13.15 ? 191 TYR A OH  1 
ATOM   1544 N  N   . TRP A 1 191 ? -16.493 -4.412  28.024  1.00 8.41  ? 192 TRP A N   1 
ATOM   1545 C  CA  . TRP A 1 191 ? -15.438 -4.151  29.010  1.00 9.26  ? 192 TRP A CA  1 
ATOM   1546 C  C   . TRP A 1 191 ? -14.726 -2.834  28.599  1.00 8.38  ? 192 TRP A C   1 
ATOM   1547 O  O   . TRP A 1 191 ? -14.713 -2.500  27.433  1.00 9.32  ? 192 TRP A O   1 
ATOM   1548 C  CB  . TRP A 1 191 ? -14.375 -5.269  28.936  1.00 9.04  ? 192 TRP A CB  1 
ATOM   1549 C  CG  . TRP A 1 191 ? -14.921 -6.593  29.399  1.00 9.01  ? 192 TRP A CG  1 
ATOM   1550 C  CD1 . TRP A 1 191 ? -15.141 -7.025  30.683  1.00 11.03 ? 192 TRP A CD1 1 
ATOM   1551 C  CD2 . TRP A 1 191 ? -15.192 -7.710  28.541  1.00 9.03  ? 192 TRP A CD2 1 
ATOM   1552 N  NE1 . TRP A 1 191 ? -15.553 -8.357  30.661  1.00 11.42 ? 192 TRP A NE1 1 
ATOM   1553 C  CE2 . TRP A 1 191 ? -15.585 -8.770  29.360  1.00 10.82 ? 192 TRP A CE2 1 
ATOM   1554 C  CE3 . TRP A 1 191 ? -15.125 -7.910  27.164  1.00 10.33 ? 192 TRP A CE3 1 
ATOM   1555 C  CZ2 . TRP A 1 191 ? -15.930 -10.015 28.813  1.00 12.51 ? 192 TRP A CZ2 1 
ATOM   1556 C  CZ3 . TRP A 1 191 ? -15.402 -9.181  26.627  1.00 10.27 ? 192 TRP A CZ3 1 
ATOM   1557 C  CH2 . TRP A 1 191 ? -15.808 -10.176 27.477  1.00 12.14 ? 192 TRP A CH2 1 
ATOM   1558 N  N   . THR A 1 192 ? -14.172 -2.119  29.592  1.00 7.91  ? 193 THR A N   1 
ATOM   1559 C  CA  . THR A 1 192 ? -13.439 -0.898  29.178  1.00 8.34  ? 193 THR A CA  1 
ATOM   1560 C  C   . THR A 1 192 ? -12.200 -0.709  30.069  1.00 8.27  ? 193 THR A C   1 
ATOM   1561 O  O   . THR A 1 192 ? -12.182 -1.135  31.219  1.00 9.42  ? 193 THR A O   1 
ATOM   1562 C  CB  . THR A 1 192 ? -14.392 0.315   29.349  1.00 9.60  ? 193 THR A CB  1 
ATOM   1563 O  OG1 . THR A 1 192 ? -13.696 1.506   28.897  1.00 8.84  ? 193 THR A OG1 1 
ATOM   1564 C  CG2 . THR A 1 192 ? -14.938 0.578   30.785  1.00 10.82 ? 193 THR A CG2 1 
ATOM   1565 N  N   . TYR A 1 193 ? -11.147 -0.120  29.491  1.00 8.26  ? 194 TYR A N   1 
ATOM   1566 C  CA  . TYR A 1 193 ? -9.943  0.136   30.250  1.00 8.29  ? 194 TYR A CA  1 
ATOM   1567 C  C   . TYR A 1 193 ? -9.120  1.168   29.470  1.00 8.94  ? 194 TYR A C   1 
ATOM   1568 O  O   . TYR A 1 193 ? -9.390  1.388   28.283  1.00 8.55  ? 194 TYR A O   1 
ATOM   1569 C  CB  . TYR A 1 193 ? -9.087  -1.158  30.448  1.00 9.61  ? 194 TYR A CB  1 
ATOM   1570 C  CG  . TYR A 1 193 ? -8.391  -1.631  29.179  1.00 8.83  ? 194 TYR A CG  1 
ATOM   1571 C  CD1 . TYR A 1 193 ? -9.060  -2.368  28.179  1.00 8.52  ? 194 TYR A CD1 1 
ATOM   1572 C  CD2 . TYR A 1 193 ? -7.075  -1.283  28.942  1.00 9.18  ? 194 TYR A CD2 1 
ATOM   1573 C  CE1 . TYR A 1 193 ? -8.450  -2.708  26.996  1.00 8.43  ? 194 TYR A CE1 1 
ATOM   1574 C  CE2 . TYR A 1 193 ? -6.430  -1.631  27.771  1.00 9.18  ? 194 TYR A CE2 1 
ATOM   1575 C  CZ  . TYR A 1 193 ? -7.156  -2.302  26.813  1.00 8.30  ? 194 TYR A CZ  1 
ATOM   1576 O  OH  . TYR A 1 193 ? -6.469  -2.599  25.659  1.00 8.25  ? 194 TYR A OH  1 
ATOM   1577 N  N   . PRO A 1 194 ? -8.173  1.871   30.140  1.00 8.17  ? 195 PRO A N   1 
ATOM   1578 C  CA  . PRO A 1 194 ? -7.387  2.879   29.461  1.00 7.95  ? 195 PRO A CA  1 
ATOM   1579 C  C   . PRO A 1 194 ? -6.200  2.220   28.802  1.00 8.90  ? 195 PRO A C   1 
ATOM   1580 O  O   . PRO A 1 194 ? -5.444  1.420   29.451  1.00 9.29  ? 195 PRO A O   1 
ATOM   1581 C  CB  . PRO A 1 194 ? -6.901  3.779   30.601  1.00 9.79  ? 195 PRO A CB  1 
ATOM   1582 C  CG  . PRO A 1 194 ? -6.881  2.852   31.813  1.00 10.51 ? 195 PRO A CG  1 
ATOM   1583 C  CD  . PRO A 1 194 ? -8.080  1.923   31.620  1.00 10.35 ? 195 PRO A CD  1 
ATOM   1584 N  N   . GLY A 1 195 ? -5.957  2.555   27.554  1.00 7.84  ? 196 GLY A N   1 
ATOM   1585 C  CA  . GLY A 1 195 ? -4.869  1.931   26.838  1.00 7.26  ? 196 GLY A CA  1 
ATOM   1586 C  C   . GLY A 1 195 ? -4.263  2.764   25.706  1.00 6.75  ? 196 GLY A C   1 
ATOM   1587 O  O   . GLY A 1 195 ? -4.180  4.064   25.851  1.00 7.94  ? 196 GLY A O   1 
ATOM   1588 N  N   . SER A 1 196 ? -3.817  2.150   24.590  1.00 6.59  ? 197 SER A N   1 
ATOM   1589 C  CA  . SER A 1 196 ? -3.020  2.800   23.583  1.00 6.78  ? 197 SER A CA  1 
ATOM   1590 C  C   . SER A 1 196 ? -3.457  2.390   22.201  1.00 7.08  ? 197 SER A C   1 
ATOM   1591 O  O   . SER A 1 196 ? -4.230  1.439   22.039  1.00 7.50  ? 197 SER A O   1 
ATOM   1592 C  CB  . SER A 1 196 ? -1.553  2.383   23.785  1.00 9.20  ? 197 SER A CB  1 
ATOM   1593 O  OG  . SER A 1 196 ? -1.330  1.019   23.325  1.00 8.52  ? 197 SER A OG  1 
ATOM   1594 N  N   . LEU A 1 197 ? -2.922  3.093   21.199  1.00 7.30  ? 198 LEU A N   1 
ATOM   1595 C  CA  . LEU A 1 197 ? -2.944  2.529   19.860  1.00 7.45  ? 198 LEU A CA  1 
ATOM   1596 C  C   . LEU A 1 197 ? -2.230  1.201   19.881  1.00 7.54  ? 198 LEU A C   1 
ATOM   1597 O  O   . LEU A 1 197 ? -1.181  1.062   20.559  1.00 8.83  ? 198 LEU A O   1 
ATOM   1598 C  CB  . LEU A 1 197 ? -2.238  3.510   18.943  1.00 9.07  ? 198 LEU A CB  1 
ATOM   1599 C  CG  . LEU A 1 197 ? -2.722  4.963   18.823  1.00 8.92  ? 198 LEU A CG  1 
ATOM   1600 C  CD1 . LEU A 1 197 ? -1.828  5.712   17.830  1.00 10.94 ? 198 LEU A CD1 1 
ATOM   1601 C  CD2 . LEU A 1 197 ? -4.126  4.962   18.348  1.00 11.20 ? 198 LEU A CD2 1 
ATOM   1602 N  N   . THR A 1 198 ? -2.672  0.248   19.072  1.00 7.74  ? 199 THR A N   1 
ATOM   1603 C  CA  . THR A 1 198 ? -2.010  -1.053  19.022  1.00 8.80  ? 199 THR A CA  1 
ATOM   1604 C  C   . THR A 1 198 ? -0.988  -1.151  17.904  1.00 7.97  ? 199 THR A C   1 
ATOM   1605 O  O   . THR A 1 198 ? -0.404  -2.221  17.707  1.00 8.93  ? 199 THR A O   1 
ATOM   1606 C  CB  . THR A 1 198 ? -3.039  -2.203  18.908  1.00 8.85  ? 199 THR A CB  1 
ATOM   1607 O  OG1 . THR A 1 198 ? -3.638  -2.132  17.625  1.00 7.81  ? 199 THR A OG1 1 
ATOM   1608 C  CG2 . THR A 1 198 ? -4.021  -2.189  20.010  1.00 8.91  ? 199 THR A CG2 1 
ATOM   1609 N  N   . THR A 1 199 ? -0.804  -0.071  17.086  1.00 8.72  ? 200 THR A N   1 
ATOM   1610 C  CA  . THR A 1 199 ? 0.293   -0.050  16.130  1.00 10.05 ? 200 THR A CA  1 
ATOM   1611 C  C   . THR A 1 199 ? 1.110   1.221   16.423  1.00 10.60 ? 200 THR A C   1 
ATOM   1612 O  O   . THR A 1 199 ? 0.611   2.159   17.076  1.00 9.95  ? 200 THR A O   1 
ATOM   1613 C  CB  . THR A 1 199 ? -0.226  0.110   14.662  1.00 11.44 ? 200 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 199 ? -0.893  1.399   14.504  1.00 15.90 ? 200 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 199 ? -1.172  -1.018  14.284  1.00 13.85 ? 200 THR A CG2 1 
ATOM   1616 N  N   . PRO A 1 200 ? 2.385   1.256   16.000  1.00 9.67  ? 201 PRO A N   1 
ATOM   1617 C  CA  . PRO A 1 200 ? 3.109   2.507   16.080  1.00 11.03 ? 201 PRO A CA  1 
ATOM   1618 C  C   . PRO A 1 200 ? 2.264   3.659   15.526  1.00 10.84 ? 201 PRO A C   1 
ATOM   1619 O  O   . PRO A 1 200 ? 1.572   3.523   14.515  1.00 12.54 ? 201 PRO A O   1 
ATOM   1620 C  CB  . PRO A 1 200 ? 4.337   2.192   15.229  1.00 11.55 ? 201 PRO A CB  1 
ATOM   1621 C  CG  . PRO A 1 200 ? 4.593   0.705   15.458  1.00 12.29 ? 201 PRO A CG  1 
ATOM   1622 C  CD  . PRO A 1 200 ? 3.162   0.162   15.366  1.00 10.60 ? 201 PRO A CD  1 
ATOM   1623 N  N   . PRO A 1 201 ? 2.318   4.814   16.188  1.00 11.13 ? 202 PRO A N   1 
ATOM   1624 C  CA  . PRO A 1 201 ? 3.228   5.182   17.295  1.00 11.33 ? 202 PRO A CA  1 
ATOM   1625 C  C   . PRO A 1 201 ? 2.840   4.752   18.708  1.00 10.94 ? 202 PRO A C   1 
ATOM   1626 O  O   . PRO A 1 201 ? 3.509   5.213   19.637  1.00 11.76 ? 202 PRO A O   1 
ATOM   1627 C  CB  . PRO A 1 201 ? 3.287   6.698   17.141  1.00 13.31 ? 202 PRO A CB  1 
ATOM   1628 C  CG  . PRO A 1 201 ? 1.888   7.091   16.716  1.00 13.65 ? 202 PRO A CG  1 
ATOM   1629 C  CD  . PRO A 1 201 ? 1.540   5.976   15.639  1.00 13.15 ? 202 PRO A CD  1 
ATOM   1630 N  N   . LEU A 1 202 ? 1.812   3.904   18.865  1.00 9.18  ? 203 LEU A N   1 
ATOM   1631 C  CA  . LEU A 1 202 ? 1.603   3.258   20.174  1.00 9.88  ? 203 LEU A CA  1 
ATOM   1632 C  C   . LEU A 1 202 ? 1.200   4.298   21.249  1.00 9.49  ? 203 LEU A C   1 
ATOM   1633 O  O   . LEU A 1 202 ? 1.357   4.037   22.446  1.00 10.05 ? 203 LEU A O   1 
ATOM   1634 C  CB  . LEU A 1 202 ? 2.781   2.385   20.679  1.00 9.52  ? 203 LEU A CB  1 
ATOM   1635 C  CG  . LEU A 1 202 ? 3.062   1.241   19.659  1.00 9.85  ? 203 LEU A CG  1 
ATOM   1636 C  CD1 . LEU A 1 202 ? 4.362   0.570   20.097  1.00 12.18 ? 203 LEU A CD1 1 
ATOM   1637 C  CD2 . LEU A 1 202 ? 1.911   0.174   19.629  1.00 10.56 ? 203 LEU A CD2 1 
ATOM   1638 N  N   . LEU A 1 203 ? 0.655   5.452   20.818  1.00 9.40  ? 204 LEU A N   1 
ATOM   1639 C  CA  . LEU A 1 203 ? 0.367   6.537   21.780  1.00 9.65  ? 204 LEU A CA  1 
ATOM   1640 C  C   . LEU A 1 203 ? -0.706  6.085   22.780  1.00 9.32  ? 204 LEU A C   1 
ATOM   1641 O  O   . LEU A 1 203 ? -1.682  5.385   22.456  1.00 9.62  ? 204 LEU A O   1 
ATOM   1642 C  CB  . LEU A 1 203 ? -0.143  7.770   20.987  1.00 10.31 ? 204 LEU A CB  1 
ATOM   1643 C  CG  . LEU A 1 203 ? 0.908   8.321   20.015  1.00 12.79 ? 204 LEU A CG  1 
ATOM   1644 C  CD1 . LEU A 1 203 ? 0.301   9.434   19.184  1.00 14.41 ? 204 LEU A CD1 1 
ATOM   1645 C  CD2 . LEU A 1 203 ? 2.102   8.946   20.876  1.00 17.24 ? 204 LEU A CD2 1 
ATOM   1646 N  N   . GLU A 1 204 ? -0.557  6.592   24.033  1.00 10.17 ? 205 GLU A N   1 
ATOM   1647 C  CA  . GLU A 1 204 ? -1.374  6.163   25.135  1.00 9.67  ? 205 GLU A CA  1 
ATOM   1648 C  C   . GLU A 1 204 ? -2.568  7.143   25.228  1.00 9.34  ? 205 GLU A C   1 
ATOM   1649 O  O   . GLU A 1 204 ? -2.688  7.913   26.218  1.00 11.76 ? 205 GLU A O   1 
ATOM   1650 C  CB  . GLU A 1 204 ? -0.503  6.020   26.419  1.00 10.68 ? 205 GLU A CB  1 
ATOM   1651 C  CG  . GLU A 1 204 ? 0.383   4.789   26.231  1.00 11.08 ? 205 GLU A CG  1 
ATOM   1652 C  CD  . GLU A 1 204 ? 1.293   4.555   27.439  1.00 11.98 ? 205 GLU A CD  1 
ATOM   1653 O  OE1 . GLU A 1 204 ? 1.589   5.495   28.227  1.00 14.04 ? 205 GLU A OE1 1 
ATOM   1654 O  OE2 . GLU A 1 204 ? 1.713   3.365   27.600  1.00 11.40 ? 205 GLU A OE2 1 
ATOM   1655 N  N   . CYS A 1 205 ? -3.440  7.075   24.249  1.00 8.98  ? 206 CYS A N   1 
ATOM   1656 C  CA  . CYS A 1 205 ? -4.486  8.070   24.065  1.00 9.49  ? 206 CYS A CA  1 
ATOM   1657 C  C   . CYS A 1 205 ? -5.876  7.468   23.938  1.00 8.98  ? 206 CYS A C   1 
ATOM   1658 O  O   . CYS A 1 205 ? -6.827  8.152   23.565  1.00 9.71  ? 206 CYS A O   1 
ATOM   1659 C  CB  . CYS A 1 205 ? -4.220  8.885   22.829  1.00 9.62  ? 206 CYS A CB  1 
ATOM   1660 S  SG  . CYS A 1 205 ? -4.162  7.918   21.304  1.00 10.34 ? 206 CYS A SG  1 
ATOM   1661 N  N   . VAL A 1 206 ? -5.975  6.152   24.245  1.00 8.32  ? 207 VAL A N   1 
ATOM   1662 C  CA  . VAL A 1 206 ? -7.255  5.438   23.895  1.00 8.02  ? 207 VAL A CA  1 
ATOM   1663 C  C   . VAL A 1 206 ? -8.033  4.966   25.125  1.00 7.46  ? 207 VAL A C   1 
ATOM   1664 O  O   . VAL A 1 206 ? -7.471  4.318   26.016  1.00 9.31  ? 207 VAL A O   1 
ATOM   1665 C  CB  . VAL A 1 206 ? -6.954  4.180   23.017  1.00 8.53  ? 207 VAL A CB  1 
ATOM   1666 C  CG1 . VAL A 1 206 ? -8.288  3.475   22.676  1.00 8.04  ? 207 VAL A CG1 1 
ATOM   1667 C  CG2 . VAL A 1 206 ? -6.216  4.577   21.745  1.00 9.07  ? 207 VAL A CG2 1 
ATOM   1668 N  N   . THR A 1 207 ? -9.349  5.316   25.211  1.00 7.54  ? 208 THR A N   1 
ATOM   1669 C  CA  . THR A 1 207 ? -10.246 4.574   26.057  1.00 7.55  ? 208 THR A CA  1 
ATOM   1670 C  C   . THR A 1 207 ? -10.742 3.397   25.187  1.00 8.11  ? 208 THR A C   1 
ATOM   1671 O  O   . THR A 1 207 ? -11.459 3.598   24.200  1.00 7.77  ? 208 THR A O   1 
ATOM   1672 C  CB  . THR A 1 207 ? -11.473 5.432   26.482  1.00 8.76  ? 208 THR A CB  1 
ATOM   1673 O  OG1 . THR A 1 207 ? -10.926 6.568   27.227  1.00 9.22  ? 208 THR A OG1 1 
ATOM   1674 C  CG2 . THR A 1 207 ? -12.375 4.633   27.420  1.00 9.93  ? 208 THR A CG2 1 
ATOM   1675 N  N   . TRP A 1 208 ? -10.423 2.157   25.632  1.00 7.67  ? 209 TRP A N   1 
ATOM   1676 C  CA  . TRP A 1 208 ? -10.891 1.005   24.880  1.00 7.63  ? 209 TRP A CA  1 
ATOM   1677 C  C   . TRP A 1 208 ? -12.236 0.552   25.424  1.00 8.28  ? 209 TRP A C   1 
ATOM   1678 O  O   . TRP A 1 208 ? -12.468 0.524   26.616  1.00 8.19  ? 209 TRP A O   1 
ATOM   1679 C  CB  . TRP A 1 208 ? -9.851  -0.181  25.123  1.00 7.81  ? 209 TRP A CB  1 
ATOM   1680 C  CG  . TRP A 1 208 ? -8.773  -0.057  24.175  1.00 6.42  ? 209 TRP A CG  1 
ATOM   1681 C  CD1 . TRP A 1 208 ? -7.508  0.538   24.364  1.00 7.44  ? 209 TRP A CD1 1 
ATOM   1682 C  CD2 . TRP A 1 208 ? -8.825  -0.487  22.787  1.00 6.42  ? 209 TRP A CD2 1 
ATOM   1683 N  NE1 . TRP A 1 208 ? -6.815  0.542   23.167  1.00 7.87  ? 209 TRP A NE1 1 
ATOM   1684 C  CE2 . TRP A 1 208 ? -7.597  -0.055  22.187  1.00 6.72  ? 209 TRP A CE2 1 
ATOM   1685 C  CE3 . TRP A 1 208 ? -9.808  -1.099  22.003  1.00 7.56  ? 209 TRP A CE3 1 
ATOM   1686 C  CZ2 . TRP A 1 208 ? -7.300  -0.300  20.844  1.00 7.57  ? 209 TRP A CZ2 1 
ATOM   1687 C  CZ3 . TRP A 1 208 ? -9.526  -1.360  20.664  1.00 8.81  ? 209 TRP A CZ3 1 
ATOM   1688 C  CH2 . TRP A 1 208 ? -8.285  -0.966  20.071  1.00 7.67  ? 209 TRP A CH2 1 
ATOM   1689 N  N   . ILE A 1 209 ? -13.126 0.227   24.466  1.00 7.09  ? 210 ILE A N   1 
ATOM   1690 C  CA  . ILE A 1 209 ? -14.460 -0.314  24.835  1.00 7.79  ? 210 ILE A CA  1 
ATOM   1691 C  C   . ILE A 1 209 ? -14.556 -1.564  23.962  1.00 8.07  ? 210 ILE A C   1 
ATOM   1692 O  O   . ILE A 1 209 ? -14.645 -1.472  22.723  1.00 8.95  ? 210 ILE A O   1 
ATOM   1693 C  CB  . ILE A 1 209 ? -15.537 0.718   24.425  1.00 9.01  ? 210 ILE A CB  1 
ATOM   1694 C  CG1 . ILE A 1 209 ? -15.304 1.982   25.257  1.00 10.60 ? 210 ILE A CG1 1 
ATOM   1695 C  CG2 . ILE A 1 209 ? -16.962 0.097   24.745  1.00 9.48  ? 210 ILE A CG2 1 
ATOM   1696 C  CD1 . ILE A 1 209 ? -16.195 3.174   24.768  1.00 12.37 ? 210 ILE A CD1 1 
ATOM   1697 N  N   . VAL A 1 210 ? -14.545 -2.740  24.640  1.00 7.31  ? 211 VAL A N   1 
ATOM   1698 C  CA  . VAL A 1 210 ? -14.472 -4.042  23.877  1.00 7.62  ? 211 VAL A CA  1 
ATOM   1699 C  C   . VAL A 1 210 ? -15.813 -4.706  24.135  1.00 8.01  ? 211 VAL A C   1 
ATOM   1700 O  O   . VAL A 1 210 ? -16.151 -5.008  25.261  1.00 8.59  ? 211 VAL A O   1 
ATOM   1701 C  CB  . VAL A 1 210 ? -13.274 -4.877  24.355  1.00 8.26  ? 211 VAL A CB  1 
ATOM   1702 C  CG1 . VAL A 1 210 ? -13.290 -6.260  23.590  1.00 8.96  ? 211 VAL A CG1 1 
ATOM   1703 C  CG2 . VAL A 1 210 ? -11.939 -4.106  23.998  1.00 8.79  ? 211 VAL A CG2 1 
ATOM   1704 N  N   . LEU A 1 211 ? -16.578 -5.019  23.057  1.00 8.39  ? 212 LEU A N   1 
ATOM   1705 C  CA  . LEU A 1 211 ? -17.879 -5.644  23.267  1.00 9.60  ? 212 LEU A CA  1 
ATOM   1706 C  C   . LEU A 1 211 ? -17.671 -7.112  23.656  1.00 8.94  ? 212 LEU A C   1 
ATOM   1707 O  O   . LEU A 1 211 ? -16.828 -7.840  23.086  1.00 9.54  ? 212 LEU A O   1 
ATOM   1708 C  CB  . LEU A 1 211 ? -18.680 -5.556  21.918  1.00 10.00 ? 212 LEU A CB  1 
ATOM   1709 C  CG  . LEU A 1 211 ? -19.035 -4.093  21.543  1.00 9.46  ? 212 LEU A CG  1 
ATOM   1710 C  CD1 . LEU A 1 211 ? -20.126 -4.184  20.412  1.00 12.27 ? 212 LEU A CD1 1 
ATOM   1711 C  CD2 . LEU A 1 211 ? -19.549 -3.311  22.668  1.00 11.27 ? 212 LEU A CD2 1 
ATOM   1712 N  N   . LYS A 1 212 ? -18.555 -7.573  24.516  1.00 10.51 ? 213 LYS A N   1 
ATOM   1713 C  CA  . LYS A 1 212 ? -18.501 -9.007  24.906  1.00 10.62 ? 213 LYS A CA  1 
ATOM   1714 C  C   . LYS A 1 212 ? -18.984 -9.928  23.854  1.00 9.99  ? 213 LYS A C   1 
ATOM   1715 O  O   . LYS A 1 212 ? -18.432 -11.025 23.694  1.00 12.66 ? 213 LYS A O   1 
ATOM   1716 C  CB  . LYS A 1 212 ? -19.321 -9.207  26.152  1.00 13.58 ? 213 LYS A CB  1 
ATOM   1717 C  CG  . LYS A 1 212 ? -19.440 -10.673 26.593  1.00 18.10 ? 213 LYS A CG  1 
ATOM   1718 C  CD  . LYS A 1 212 ? -20.499 -10.717 27.725  1.00 25.36 ? 213 LYS A CD  1 
ATOM   1719 C  CE  . LYS A 1 212 ? -21.996 -10.227 27.232  1.00 32.02 ? 213 LYS A CE  1 
ATOM   1720 N  NZ  . LYS A 1 212 ? -23.338 -10.449 28.111  1.00 35.19 ? 213 LYS A NZ  1 
ATOM   1721 N  N   . GLU A 1 213 ? -20.009 -9.552  23.066  1.00 9.11  ? 214 GLU A N   1 
ATOM   1722 C  CA  . GLU A 1 213 ? -20.596 -10.472 22.076  1.00 11.70 ? 214 GLU A CA  1 
ATOM   1723 C  C   . GLU A 1 213 ? -19.837 -10.365 20.795  1.00 10.16 ? 214 GLU A C   1 
ATOM   1724 O  O   . GLU A 1 213 ? -19.774 -9.263  20.184  1.00 9.90  ? 214 GLU A O   1 
ATOM   1725 C  CB  . GLU A 1 213 ? -22.061 -10.141 21.863  1.00 11.66 ? 214 GLU A CB  1 
ATOM   1726 C  CG  . GLU A 1 213 ? -22.677 -11.065 20.870  1.00 13.60 ? 214 GLU A CG  1 
ATOM   1727 C  CD  . GLU A 1 213 ? -24.148 -10.924 20.683  1.00 19.63 ? 214 GLU A CD  1 
ATOM   1728 O  OE1 . GLU A 1 213 ? -24.785 -10.019 21.189  1.00 14.85 ? 214 GLU A OE1 1 
ATOM   1729 O  OE2 . GLU A 1 213 ? -24.720 -11.899 20.027  1.00 25.97 ? 214 GLU A OE2 1 
ATOM   1730 N  N   . PRO A 1 214 ? -19.233 -11.454 20.292  1.00 9.15  ? 215 PRO A N   1 
ATOM   1731 C  CA  . PRO A 1 214 ? -18.608 -11.384 18.977  1.00 10.05 ? 215 PRO A CA  1 
ATOM   1732 C  C   . PRO A 1 214 ? -19.638 -11.391 17.845  1.00 10.53 ? 215 PRO A C   1 
ATOM   1733 O  O   . PRO A 1 214 ? -20.816 -11.791 18.050  1.00 12.88 ? 215 PRO A O   1 
ATOM   1734 C  CB  . PRO A 1 214 ? -17.814 -12.754 18.869  1.00 10.06 ? 215 PRO A CB  1 
ATOM   1735 C  CG  . PRO A 1 214 ? -18.713 -13.646 19.707  1.00 16.08 ? 215 PRO A CG  1 
ATOM   1736 C  CD  . PRO A 1 214 ? -19.208 -12.814 20.896  1.00 10.98 ? 215 PRO A CD  1 
ATOM   1737 N  N   . ILE A 1 215 ? -19.250 -10.915 16.689  1.00 9.96  ? 216 ILE A N   1 
ATOM   1738 C  CA  . ILE A 1 215 ? -20.052 -11.155 15.487  1.00 10.66 ? 216 ILE A CA  1 
ATOM   1739 C  C   . ILE A 1 215 ? -19.479 -12.385 14.787  1.00 10.88 ? 216 ILE A C   1 
ATOM   1740 O  O   . ILE A 1 215 ? -18.326 -12.788 14.981  1.00 10.96 ? 216 ILE A O   1 
ATOM   1741 C  CB  . ILE A 1 215 ? -20.030 -9.975  14.492  1.00 10.39 ? 216 ILE A CB  1 
ATOM   1742 C  CG1 . ILE A 1 215 ? -18.580 -9.576  14.091  1.00 12.06 ? 216 ILE A CG1 1 
ATOM   1743 C  CG2 . ILE A 1 215 ? -20.682 -8.742  15.177  1.00 13.64 ? 216 ILE A CG2 1 
ATOM   1744 C  CD1 . ILE A 1 215 ? -18.578 -8.613  12.831  1.00 12.90 ? 216 ILE A CD1 1 
ATOM   1745 N  N   . SER A 1 216 ? -20.363 -13.040 14.035  1.00 11.25 ? 217 SER A N   1 
ATOM   1746 C  CA  . SER A 1 216 ? -19.969 -14.200 13.241  1.00 12.70 ? 217 SER A CA  1 
ATOM   1747 C  C   . SER A 1 216 ? -19.761 -13.764 11.802  1.00 10.89 ? 217 SER A C   1 
ATOM   1748 O  O   . SER A 1 216 ? -20.630 -13.067 11.266  1.00 12.84 ? 217 SER A O   1 
ATOM   1749 C  CB  . SER A 1 216 ? -21.151 -15.240 13.241  1.00 14.80 ? 217 SER A CB  1 
ATOM   1750 O  OG  . SER A 1 216 ? -21.105 -15.906 14.437  1.00 21.45 ? 217 SER A OG  1 
ATOM   1751 N  N   . VAL A 1 217 ? -18.660 -14.225 11.187  1.00 11.22 ? 218 VAL A N   1 
ATOM   1752 C  CA  . VAL A 1 217 ? -18.356 -14.038 9.785   1.00 11.63 ? 218 VAL A CA  1 
ATOM   1753 C  C   . VAL A 1 217 ? -18.117 -15.383 9.158   1.00 12.09 ? 218 VAL A C   1 
ATOM   1754 O  O   . VAL A 1 217 ? -17.758 -16.349 9.900   1.00 11.97 ? 218 VAL A O   1 
ATOM   1755 C  CB  . VAL A 1 217 ? -17.158 -13.093 9.532   1.00 12.31 ? 218 VAL A CB  1 
ATOM   1756 C  CG1 . VAL A 1 217 ? -17.444 -11.779 10.244  1.00 11.40 ? 218 VAL A CG1 1 
ATOM   1757 C  CG2 . VAL A 1 217 ? -15.880 -13.702 10.114  1.00 13.09 ? 218 VAL A CG2 1 
ATOM   1758 N  N   . SER A 1 218 ? -18.251 -15.527 7.837   1.00 11.41 ? 219 SER A N   1 
ATOM   1759 C  CA  . SER A 1 218 ? -18.078 -16.855 7.319   1.00 11.69 ? 219 SER A CA  1 
ATOM   1760 C  C   . SER A 1 218 ? -16.596 -17.109 7.023   1.00 13.06 ? 219 SER A C   1 
ATOM   1761 O  O   . SER A 1 218 ? -15.757 -16.166 6.889   1.00 12.31 ? 219 SER A O   1 
ATOM   1762 C  CB  . SER A 1 218 ? -18.861 -17.052 6.019   1.00 12.74 ? 219 SER A CB  1 
ATOM   1763 O  OG  . SER A 1 218 ? -18.396 -16.166 5.025   1.00 14.19 ? 219 SER A OG  1 
ATOM   1764 N  N   A SER A 1 219 ? -16.257 -18.378 6.885   0.50 11.91 ? 220 SER A N   1 
ATOM   1765 N  N   B SER A 1 219 ? -16.253 -18.390 6.857   0.50 12.23 ? 220 SER A N   1 
ATOM   1766 C  CA  A SER A 1 219 ? -14.924 -18.727 6.512   0.50 12.51 ? 220 SER A CA  1 
ATOM   1767 C  CA  B SER A 1 219 ? -14.899 -18.754 6.490   0.50 12.79 ? 220 SER A CA  1 
ATOM   1768 C  C   A SER A 1 219 ? -14.543 -18.066 5.197   0.50 14.15 ? 220 SER A C   1 
ATOM   1769 C  C   B SER A 1 219 ? -14.500 -18.094 5.124   0.50 14.67 ? 220 SER A C   1 
ATOM   1770 O  O   A SER A 1 219 ? -13.430 -17.537 5.132   0.50 13.48 ? 220 SER A O   1 
ATOM   1771 O  O   B SER A 1 219 ? -13.346 -17.645 4.908   0.50 14.09 ? 220 SER A O   1 
ATOM   1772 C  CB  A SER A 1 219 ? -14.808 -20.284 6.451   0.50 13.29 ? 220 SER A CB  1 
ATOM   1773 C  CB  B SER A 1 219 ? -14.774 -20.296 6.515   0.50 14.61 ? 220 SER A CB  1 
ATOM   1774 O  OG  A SER A 1 219 ? -15.736 -20.872 5.520   0.50 13.89 ? 220 SER A OG  1 
ATOM   1775 O  OG  B SER A 1 219 ? -13.433 -20.593 6.272   0.50 17.80 ? 220 SER A OG  1 
ATOM   1776 N  N   . GLU A 1 220 ? -15.465 -17.983 4.211   1.00 13.58 ? 221 GLU A N   1 
ATOM   1777 C  CA  . GLU A 1 220 ? -15.165 -17.337 2.932   1.00 13.68 ? 221 GLU A CA  1 
ATOM   1778 C  C   . GLU A 1 220 ? -14.889 -15.835 3.076   1.00 12.83 ? 221 GLU A C   1 
ATOM   1779 O  O   . GLU A 1 220 ? -14.027 -15.267 2.365   1.00 14.72 ? 221 GLU A O   1 
ATOM   1780 C  CB  . GLU A 1 220 ? -16.304 -17.582 1.943   1.00 16.37 ? 221 GLU A CB  1 
ATOM   1781 C  CG  . GLU A 1 220 ? -16.452 -19.037 1.541   1.00 19.17 ? 221 GLU A CG  1 
ATOM   1782 C  CD  . GLU A 1 220 ? -17.419 -19.774 2.430   1.00 24.41 ? 221 GLU A CD  1 
ATOM   1783 O  OE1 . GLU A 1 220 ? -17.844 -19.200 3.444   1.00 20.00 ? 221 GLU A OE1 1 
ATOM   1784 O  OE2 . GLU A 1 220 ? -17.763 -20.929 2.104   1.00 30.14 ? 221 GLU A OE2 1 
ATOM   1785 N  N   . GLN A 1 221 ? -15.595 -15.172 4.008   1.00 12.76 ? 222 GLN A N   1 
ATOM   1786 C  CA  . GLN A 1 221 ? -15.326 -13.714 4.220   1.00 12.53 ? 222 GLN A CA  1 
ATOM   1787 C  C   . GLN A 1 221 ? -13.881 -13.534 4.782   1.00 13.22 ? 222 GLN A C   1 
ATOM   1788 O  O   . GLN A 1 221 ? -13.163 -12.667 4.315   1.00 12.96 ? 222 GLN A O   1 
ATOM   1789 C  CB  . GLN A 1 221 ? -16.335 -13.193 5.155   1.00 12.41 ? 222 GLN A CB  1 
ATOM   1790 C  CG  . GLN A 1 221 ? -17.719 -13.049 4.440   1.00 11.92 ? 222 GLN A CG  1 
ATOM   1791 C  CD  . GLN A 1 221 ? -18.828 -12.526 5.330   1.00 12.34 ? 222 GLN A CD  1 
ATOM   1792 O  OE1 . GLN A 1 221 ? -18.965 -12.903 6.481   1.00 11.68 ? 222 GLN A OE1 1 
ATOM   1793 N  NE2 . GLN A 1 221 ? -19.661 -11.665 4.738   1.00 12.51 ? 222 GLN A NE2 1 
ATOM   1794 N  N   . VAL A 1 222 ? -13.497 -14.332 5.777   1.00 13.59 ? 223 VAL A N   1 
ATOM   1795 C  CA  . VAL A 1 222 ? -12.150 -14.075 6.316   1.00 13.66 ? 223 VAL A CA  1 
ATOM   1796 C  C   . VAL A 1 222 ? -11.061 -14.552 5.352   1.00 14.57 ? 223 VAL A C   1 
ATOM   1797 O  O   . VAL A 1 222 ? -9.979  -13.962 5.331   1.00 13.84 ? 223 VAL A O   1 
ATOM   1798 C  CB  . VAL A 1 222 ? -12.062 -14.663 7.778   1.00 15.83 ? 223 VAL A CB  1 
ATOM   1799 C  CG1 . VAL A 1 222 ? -12.039 -16.152 7.815   1.00 16.78 ? 223 VAL A CG1 1 
ATOM   1800 C  CG2 . VAL A 1 222 ? -10.782 -14.106 8.556   1.00 16.48 ? 223 VAL A CG2 1 
ATOM   1801 N  N   . LEU A 1 223 ? -11.354 -15.610 4.548   1.00 14.29 ? 224 LEU A N   1 
ATOM   1802 C  CA  . LEU A 1 223 ? -10.394 -15.957 3.541   1.00 16.35 ? 224 LEU A CA  1 
ATOM   1803 C  C   . LEU A 1 223 ? -10.097 -14.856 2.579   1.00 14.91 ? 224 LEU A C   1 
ATOM   1804 O  O   . LEU A 1 223 ? -8.947  -14.711 2.166   1.00 16.68 ? 224 LEU A O   1 
ATOM   1805 C  CB  . LEU A 1 223 ? -10.833 -17.186 2.757   1.00 19.88 ? 224 LEU A CB  1 
ATOM   1806 C  CG  . LEU A 1 223 ? -10.671 -18.425 3.664   1.00 23.13 ? 224 LEU A CG  1 
ATOM   1807 C  CD1 . LEU A 1 223 ? -11.665 -19.557 3.168   1.00 27.48 ? 224 LEU A CD1 1 
ATOM   1808 C  CD2 . LEU A 1 223 ? -9.197  -18.804 3.565   1.00 23.99 ? 224 LEU A CD2 1 
ATOM   1809 N  N   . LYS A 1 224 ? -11.075 -14.015 2.276   1.00 14.30 ? 225 LYS A N   1 
ATOM   1810 C  CA  . LYS A 1 224 ? -10.794 -12.870 1.405   1.00 16.11 ? 225 LYS A CA  1 
ATOM   1811 C  C   . LYS A 1 224 ? -9.969  -11.829 2.100   1.00 13.03 ? 225 LYS A C   1 
ATOM   1812 O  O   . LYS A 1 224 ? -9.171  -11.213 1.427   1.00 13.09 ? 225 LYS A O   1 
ATOM   1813 C  CB  . LYS A 1 224 ? -12.139 -12.345 0.840   1.00 17.30 ? 225 LYS A CB  1 
ATOM   1814 C  CG  . LYS A 1 224 ? -12.694 -13.376 -0.323  1.00 19.96 ? 225 LYS A CG  1 
ATOM   1815 C  CD  . LYS A 1 224 ? -14.053 -13.074 -0.866  1.00 24.61 ? 225 LYS A CD  1 
ATOM   1816 C  CE  . LYS A 1 224 ? -14.666 -14.315 -1.775  1.00 24.11 ? 225 LYS A CE  1 
ATOM   1817 N  NZ  . LYS A 1 224 ? -15.954 -13.876 -2.553  1.00 27.20 ? 225 LYS A NZ  1 
ATOM   1818 N  N   . PHE A 1 225 ? -10.093 -11.614 3.424   1.00 11.63 ? 226 PHE A N   1 
ATOM   1819 C  CA  . PHE A 1 225 ? -9.148  -10.738 4.095   1.00 11.19 ? 226 PHE A CA  1 
ATOM   1820 C  C   . PHE A 1 225 ? -7.721  -11.218 3.885   1.00 12.91 ? 226 PHE A C   1 
ATOM   1821 O  O   . PHE A 1 225 ? -6.793  -10.416 3.647   1.00 12.58 ? 226 PHE A O   1 
ATOM   1822 C  CB  . PHE A 1 225 ? -9.302  -10.711 5.613   1.00 11.38 ? 226 PHE A CB  1 
ATOM   1823 C  CG  . PHE A 1 225 ? -10.535 -9.992  6.159   1.00 11.97 ? 226 PHE A CG  1 
ATOM   1824 C  CD1 . PHE A 1 225 ? -11.583 -9.566  5.355   1.00 14.87 ? 226 PHE A CD1 1 
ATOM   1825 C  CD2 . PHE A 1 225 ? -10.643 -9.817  7.578   1.00 14.10 ? 226 PHE A CD2 1 
ATOM   1826 C  CE1 . PHE A 1 225 ? -12.700 -8.900  5.950   1.00 16.71 ? 226 PHE A CE1 1 
ATOM   1827 C  CE2 . PHE A 1 225 ? -11.692 -9.109  8.149   1.00 14.74 ? 226 PHE A CE2 1 
ATOM   1828 C  CZ  . PHE A 1 225 ? -12.711 -8.615  7.316   1.00 14.08 ? 226 PHE A CZ  1 
ATOM   1829 N  N   . ARG A 1 226 ? -7.505  -12.561 3.953   1.00 11.72 ? 227 ARG A N   1 
ATOM   1830 C  CA  . ARG A 1 226 ? -6.164  -13.134 3.842   1.00 13.30 ? 227 ARG A CA  1 
ATOM   1831 C  C   . ARG A 1 226 ? -5.586  -13.147 2.430   1.00 13.85 ? 227 ARG A C   1 
ATOM   1832 O  O   . ARG A 1 226 ? -4.411  -13.505 2.261   1.00 14.95 ? 227 ARG A O   1 
ATOM   1833 C  CB  . ARG A 1 226 ? -6.226  -14.623 4.348   1.00 13.05 ? 227 ARG A CB  1 
ATOM   1834 C  CG  . ARG A 1 226 ? -6.694  -14.654 5.848   1.00 12.00 ? 227 ARG A CG  1 
ATOM   1835 C  CD  . ARG A 1 226 ? -6.614  -16.137 6.285   1.00 15.18 ? 227 ARG A CD  1 
ATOM   1836 N  NE  . ARG A 1 226 ? -7.151  -16.308 7.642   1.00 12.40 ? 227 ARG A NE  1 
ATOM   1837 C  CZ  . ARG A 1 226 ? -8.081  -17.182 8.025   1.00 14.46 ? 227 ARG A CZ  1 
ATOM   1838 N  NH1 . ARG A 1 226 ? -8.488  -18.120 7.127   1.00 18.94 ? 227 ARG A NH1 1 
ATOM   1839 N  NH2 . ARG A 1 226 ? -8.608  -17.174 9.248   1.00 14.90 ? 227 ARG A NH2 1 
ATOM   1840 N  N   . LYS A 1 227 ? -6.362  -12.627 1.485   1.00 12.85 ? 228 LYS A N   1 
ATOM   1841 C  CA  . LYS A 1 227 ? -5.830  -12.521 0.152   1.00 15.43 ? 228 LYS A CA  1 
ATOM   1842 C  C   . LYS A 1 227 ? -5.208  -11.157 -0.119  1.00 13.84 ? 228 LYS A C   1 
ATOM   1843 O  O   . LYS A 1 227 ? -4.583  -10.957 -1.151  1.00 16.49 ? 228 LYS A O   1 
ATOM   1844 C  CB  . LYS A 1 227 ? -6.906  -12.761 -0.906  1.00 15.92 ? 228 LYS A CB  1 
ATOM   1845 C  CG  . LYS A 1 227 ? -7.303  -14.214 -1.078  1.00 19.86 ? 228 LYS A CG  1 
ATOM   1846 C  CD  . LYS A 1 227 ? -8.487  -14.320 -2.093  1.00 23.23 ? 228 LYS A CD  1 
ATOM   1847 C  CE  . LYS A 1 227 ? -8.067  -13.968 -3.533  1.00 31.66 ? 228 LYS A CE  1 
ATOM   1848 N  NZ  . LYS A 1 227 ? -8.744  -14.831 -4.617  1.00 39.34 ? 228 LYS A NZ  1 
ATOM   1849 N  N   . LEU A 1 228 ? -5.411  -10.220 0.824   1.00 13.68 ? 229 LEU A N   1 
ATOM   1850 C  CA  . LEU A 1 228 ? -4.788  -8.929  0.658   1.00 13.44 ? 229 LEU A CA  1 
ATOM   1851 C  C   . LEU A 1 228 ? -3.283  -9.103  0.790   1.00 14.66 ? 229 LEU A C   1 
ATOM   1852 O  O   . LEU A 1 228 ? -2.748  -10.149 1.233   1.00 13.97 ? 229 LEU A O   1 
ATOM   1853 C  CB  . LEU A 1 228 ? -5.303  -8.014  1.720   1.00 12.41 ? 229 LEU A CB  1 
ATOM   1854 C  CG  . LEU A 1 228 ? -6.766  -7.492  1.571   1.00 15.24 ? 229 LEU A CG  1 
ATOM   1855 C  CD1 . LEU A 1 228 ? -7.309  -6.881  2.883   1.00 14.78 ? 229 LEU A CD1 1 
ATOM   1856 C  CD2 . LEU A 1 228 ? -6.810  -6.434  0.444   1.00 15.93 ? 229 LEU A CD2 1 
ATOM   1857 N  N   . ASN A 1 229 ? -2.578  -8.041  0.408   1.00 13.84 ? 230 ASN A N   1 
ATOM   1858 C  CA  . ASN A 1 229 ? -1.151  -8.036  0.467   1.00 13.23 ? 230 ASN A CA  1 
ATOM   1859 C  C   . ASN A 1 229 ? -0.581  -6.881  1.333   1.00 13.91 ? 230 ASN A C   1 
ATOM   1860 O  O   . ASN A 1 229 ? -1.086  -5.760  1.248   1.00 14.43 ? 230 ASN A O   1 
ATOM   1861 C  CB  . ASN A 1 229 ? -0.537  -7.825  -0.957  1.00 14.51 ? 230 ASN A CB  1 
ATOM   1862 C  CG  . ASN A 1 229 ? -0.612  -8.994  -1.899  1.00 15.74 ? 230 ASN A CG  1 
ATOM   1863 O  OD1 . ASN A 1 229 ? -0.076  -8.874  -3.013  1.00 19.28 ? 230 ASN A OD1 1 
ATOM   1864 N  ND2 . ASN A 1 229 ? -1.154  -10.134 -1.486  1.00 17.21 ? 230 ASN A ND2 1 
ATOM   1865 N  N   . PHE A 1 230 ? 0.510   -7.189  2.061   1.00 13.78 ? 231 PHE A N   1 
ATOM   1866 C  CA  . PHE A 1 230 ? 1.196   -6.118  2.745   1.00 12.77 ? 231 PHE A CA  1 
ATOM   1867 C  C   . PHE A 1 230 ? 2.063   -5.298  1.777   1.00 15.65 ? 231 PHE A C   1 
ATOM   1868 O  O   . PHE A 1 230 ? 2.382   -4.149  2.008   1.00 16.18 ? 231 PHE A O   1 
ATOM   1869 C  CB  . PHE A 1 230 ? 2.203   -6.701  3.709   1.00 14.93 ? 231 PHE A CB  1 
ATOM   1870 C  CG  . PHE A 1 230 ? 1.626   -7.264  5.057   1.00 14.21 ? 231 PHE A CG  1 
ATOM   1871 C  CD1 . PHE A 1 230 ? 0.849   -6.493  5.926   1.00 13.48 ? 231 PHE A CD1 1 
ATOM   1872 C  CD2 . PHE A 1 230 ? 1.955   -8.562  5.436   1.00 13.68 ? 231 PHE A CD2 1 
ATOM   1873 C  CE1 . PHE A 1 230 ? 0.356   -7.020  7.175   1.00 14.74 ? 231 PHE A CE1 1 
ATOM   1874 C  CE2 . PHE A 1 230 ? 1.526   -9.115  6.632   1.00 13.86 ? 231 PHE A CE2 1 
ATOM   1875 C  CZ  . PHE A 1 230 ? 0.739   -8.343  7.526   1.00 13.34 ? 231 PHE A CZ  1 
ATOM   1876 N  N   . ASN A 1 231 ? 2.562   -5.943  0.765   1.00 14.53 ? 232 ASN A N   1 
ATOM   1877 C  CA  . ASN A 1 231 ? 3.458   -5.320  -0.250  1.00 16.41 ? 232 ASN A CA  1 
ATOM   1878 C  C   . ASN A 1 231 ? 2.708   -4.420  -1.195  1.00 16.61 ? 232 ASN A C   1 
ATOM   1879 O  O   . ASN A 1 231 ? 1.491   -4.528  -1.368  1.00 17.53 ? 232 ASN A O   1 
ATOM   1880 C  CB  . ASN A 1 231 ? 4.115   -6.427  -1.091  1.00 17.65 ? 232 ASN A CB  1 
ATOM   1881 C  CG  . ASN A 1 231 ? 3.087   -7.334  -1.689  1.00 16.18 ? 232 ASN A CG  1 
ATOM   1882 O  OD1 . ASN A 1 231 ? 2.598   -8.257  -1.001  1.00 18.32 ? 232 ASN A OD1 1 
ATOM   1883 N  ND2 . ASN A 1 231 ? 2.778   -7.171  -2.983  1.00 17.95 ? 232 ASN A ND2 1 
ATOM   1884 N  N   . GLY A 1 232 ? 3.524   -3.559  -1.877  1.00 16.78 ? 233 GLY A N   1 
ATOM   1885 C  CA  . GLY A 1 232 ? 2.991   -2.770  -2.984  1.00 18.03 ? 233 GLY A CA  1 
ATOM   1886 C  C   . GLY A 1 232 ? 2.862   -3.543  -4.268  1.00 18.12 ? 233 GLY A C   1 
ATOM   1887 O  O   . GLY A 1 232 ? 3.520   -4.554  -4.400  1.00 19.73 ? 233 GLY A O   1 
ATOM   1888 N  N   . GLU A 1 233 ? 2.130   -3.009  -5.253  1.00 19.07 ? 234 GLU A N   1 
ATOM   1889 C  CA  . GLU A 1 233 ? 2.088   -3.571  -6.602  1.00 17.24 ? 234 GLU A CA  1 
ATOM   1890 C  C   . GLU A 1 233 ? 3.480   -3.656  -7.203  1.00 18.57 ? 234 GLU A C   1 
ATOM   1891 O  O   . GLU A 1 233 ? 4.303   -2.789  -7.046  1.00 20.02 ? 234 GLU A O   1 
ATOM   1892 C  CB  . GLU A 1 233 ? 1.181   -2.742  -7.468  1.00 17.90 ? 234 GLU A CB  1 
ATOM   1893 C  CG  . GLU A 1 233 ? 0.898   -3.362  -8.821  1.00 19.30 ? 234 GLU A CG  1 
ATOM   1894 C  CD  . GLU A 1 233 ? 0.028   -2.458  -9.656  1.00 25.13 ? 234 GLU A CD  1 
ATOM   1895 O  OE1 . GLU A 1 233 ? -0.264  -1.248  -9.240  1.00 24.60 ? 234 GLU A OE1 1 
ATOM   1896 O  OE2 . GLU A 1 233 ? -0.322  -2.923  -10.742 1.00 27.94 ? 234 GLU A OE2 1 
ATOM   1897 N  N   . GLY A 1 234 ? 3.724   -4.789  -7.853  1.00 20.23 ? 235 GLY A N   1 
ATOM   1898 C  CA  . GLY A 1 234 ? 5.014   -5.068  -8.465  1.00 22.96 ? 235 GLY A CA  1 
ATOM   1899 C  C   . GLY A 1 234 ? 6.074   -5.559  -7.535  1.00 25.09 ? 235 GLY A C   1 
ATOM   1900 O  O   . GLY A 1 234 ? 7.264   -5.681  -7.959  1.00 29.12 ? 235 GLY A O   1 
ATOM   1901 N  N   . GLU A 1 235 ? 5.693   -5.839  -6.279  1.00 23.99 ? 236 GLU A N   1 
ATOM   1902 C  CA  . GLU A 1 235 ? 6.653   -6.393  -5.330  1.00 23.06 ? 236 GLU A CA  1 
ATOM   1903 C  C   . GLU A 1 235 ? 6.260   -7.817  -4.990  1.00 25.46 ? 236 GLU A C   1 
ATOM   1904 O  O   . GLU A 1 235 ? 5.100   -8.238  -5.258  1.00 24.89 ? 236 GLU A O   1 
ATOM   1905 C  CB  . GLU A 1 235 ? 6.662   -5.593  -3.998  1.00 24.83 ? 236 GLU A CB  1 
ATOM   1906 C  CG  . GLU A 1 235 ? 7.116   -4.141  -4.170  1.00 25.54 ? 236 GLU A CG  1 
ATOM   1907 C  CD  . GLU A 1 235 ? 6.884   -3.288  -2.935  1.00 27.38 ? 236 GLU A CD  1 
ATOM   1908 O  OE1 . GLU A 1 235 ? 6.291   -3.763  -1.924  1.00 29.89 ? 236 GLU A OE1 1 
ATOM   1909 O  OE2 . GLU A 1 235 ? 7.302   -2.117  -2.962  1.00 37.27 ? 236 GLU A OE2 1 
ATOM   1910 N  N   . PRO A 1 236 ? 7.229   -8.594  -4.440  1.00 24.98 ? 237 PRO A N   1 
ATOM   1911 C  CA  . PRO A 1 236 ? 7.015   -9.993  -4.079  1.00 26.58 ? 237 PRO A CA  1 
ATOM   1912 C  C   . PRO A 1 236 ? 5.791   -10.083 -3.141  1.00 23.59 ? 237 PRO A C   1 
ATOM   1913 O  O   . PRO A 1 236 ? 5.649   -9.244  -2.265  1.00 21.01 ? 237 PRO A O   1 
ATOM   1914 C  CB  . PRO A 1 236 ? 8.276   -10.315 -3.263  1.00 27.86 ? 237 PRO A CB  1 
ATOM   1915 C  CG  . PRO A 1 236 ? 9.336   -9.375  -3.800  1.00 28.98 ? 237 PRO A CG  1 
ATOM   1916 C  CD  . PRO A 1 236 ? 8.588   -8.120  -4.077  1.00 28.05 ? 237 PRO A CD  1 
ATOM   1917 N  N   . GLU A 1 237 ? 4.949   -11.099 -3.312  1.00 22.22 ? 238 GLU A N   1 
ATOM   1918 C  CA  . GLU A 1 237 ? 3.694   -11.104 -2.621  1.00 20.78 ? 238 GLU A CA  1 
ATOM   1919 C  C   . GLU A 1 237 ? 3.980   -11.548 -1.174  1.00 18.79 ? 238 GLU A C   1 
ATOM   1920 O  O   . GLU A 1 237 ? 4.570   -12.591 -0.947  1.00 18.30 ? 238 GLU A O   1 
ATOM   1921 C  CB  . GLU A 1 237 ? 2.695   -12.095 -3.279  1.00 20.78 ? 238 GLU A CB  1 
ATOM   1922 C  CG  . GLU A 1 237 ? 1.407   -12.144 -2.498  1.00 25.16 ? 238 GLU A CG  1 
ATOM   1923 C  CD  . GLU A 1 237 ? 0.298   -12.892 -3.215  1.00 25.61 ? 238 GLU A CD  1 
ATOM   1924 O  OE1 . GLU A 1 237 ? 0.596   -14.021 -3.787  1.00 33.04 ? 238 GLU A OE1 1 
ATOM   1925 O  OE2 . GLU A 1 237 ? -0.866  -12.414 -3.219  1.00 22.14 ? 238 GLU A OE2 1 
ATOM   1926 N  N   . GLU A 1 238 ? 3.492   -10.772 -0.231  1.00 16.23 ? 239 GLU A N   1 
ATOM   1927 C  CA  . GLU A 1 238 ? 3.506   -11.082 1.207   1.00 18.41 ? 239 GLU A CA  1 
ATOM   1928 C  C   . GLU A 1 238 ? 2.013   -10.959 1.615   1.00 13.94 ? 239 GLU A C   1 
ATOM   1929 O  O   . GLU A 1 238 ? 1.473   -9.866  1.620   1.00 17.18 ? 239 GLU A O   1 
ATOM   1930 C  CB  . GLU A 1 238 ? 4.264   -10.058 2.004   1.00 19.82 ? 239 GLU A CB  1 
ATOM   1931 C  CG  . GLU A 1 238 ? 5.630   -9.602  1.510   1.00 25.18 ? 239 GLU A CG  1 
ATOM   1932 C  CD  . GLU A 1 238 ? 6.042   -8.250  2.094   1.00 28.44 ? 239 GLU A CD  1 
ATOM   1933 O  OE1 . GLU A 1 238 ? 5.921   -8.070  3.325   1.00 38.24 ? 239 GLU A OE1 1 
ATOM   1934 O  OE2 . GLU A 1 238 ? 6.490   -7.381  1.315   1.00 38.62 ? 239 GLU A OE2 1 
ATOM   1935 N  N   . LEU A 1 239 ? 1.361   -12.089 1.938   1.00 14.96 ? 240 LEU A N   1 
ATOM   1936 C  CA  . LEU A 1 239 ? -0.025  -12.047 2.251   1.00 13.54 ? 240 LEU A CA  1 
ATOM   1937 C  C   . LEU A 1 239 ? -0.207  -11.219 3.550   1.00 13.11 ? 240 LEU A C   1 
ATOM   1938 O  O   . LEU A 1 239 ? 0.547   -11.394 4.541   1.00 13.86 ? 240 LEU A O   1 
ATOM   1939 C  CB  . LEU A 1 239 ? -0.603  -13.463 2.486   1.00 13.63 ? 240 LEU A CB  1 
ATOM   1940 C  CG  . LEU A 1 239 ? -0.656  -14.342 1.256   1.00 13.66 ? 240 LEU A CG  1 
ATOM   1941 C  CD1 . LEU A 1 239 ? -1.207  -15.714 1.751   1.00 19.28 ? 240 LEU A CD1 1 
ATOM   1942 C  CD2 . LEU A 1 239 ? -1.453  -13.709 0.146   1.00 16.12 ? 240 LEU A CD2 1 
ATOM   1943 N  N   . MET A 1 240 ? -1.280  -10.426 3.587   1.00 11.94 ? 241 MET A N   1 
ATOM   1944 C  CA  . MET A 1 240 ? -1.617  -9.608  4.759   1.00 11.60 ? 241 MET A CA  1 
ATOM   1945 C  C   . MET A 1 240 ? -2.365  -10.567 5.683   1.00 12.99 ? 241 MET A C   1 
ATOM   1946 O  O   . MET A 1 240 ? -3.590  -10.688 5.580   1.00 11.96 ? 241 MET A O   1 
ATOM   1947 C  CB  . MET A 1 240 ? -2.520  -8.472  4.281   1.00 12.64 ? 241 MET A CB  1 
ATOM   1948 C  CG  . MET A 1 240 ? -2.831  -7.456  5.489   1.00 12.21 ? 241 MET A CG  1 
ATOM   1949 S  SD  . MET A 1 240 ? -3.817  -6.070  4.941   1.00 13.72 ? 241 MET A SD  1 
ATOM   1950 C  CE  . MET A 1 240 ? -2.465  -4.997  4.348   1.00 14.49 ? 241 MET A CE  1 
ATOM   1951 N  N   . VAL A 1 241 ? -1.568  -11.150 6.614   1.00 11.14 ? 242 VAL A N   1 
ATOM   1952 C  CA  . VAL A 1 241 ? -2.174  -12.028 7.632   1.00 10.06 ? 242 VAL A CA  1 
ATOM   1953 C  C   . VAL A 1 241 ? -1.351  -11.786 8.906   1.00 11.74 ? 242 VAL A C   1 
ATOM   1954 O  O   . VAL A 1 241 ? -0.164  -11.362 8.885   1.00 10.90 ? 242 VAL A O   1 
ATOM   1955 C  CB  . VAL A 1 241 ? -2.068  -13.542 7.247   1.00 12.18 ? 242 VAL A CB  1 
ATOM   1956 C  CG1 . VAL A 1 241 ? -3.038  -13.853 6.009   1.00 13.40 ? 242 VAL A CG1 1 
ATOM   1957 C  CG2 . VAL A 1 241 ? -0.604  -13.981 6.970   1.00 13.41 ? 242 VAL A CG2 1 
ATOM   1958 N  N   . ASP A 1 242 ? -1.999  -12.118 10.050  1.00 10.41 ? 243 ASP A N   1 
ATOM   1959 C  CA  . ASP A 1 242 ? -1.307  -11.988 11.329  1.00 10.45 ? 243 ASP A CA  1 
ATOM   1960 C  C   . ASP A 1 242 ? -0.835  -10.548 11.549  1.00 9.60  ? 243 ASP A C   1 
ATOM   1961 O  O   . ASP A 1 242 ? 0.251   -10.301 12.083  1.00 10.30 ? 243 ASP A O   1 
ATOM   1962 C  CB  . ASP A 1 242 ? -0.171  -13.005 11.555  1.00 10.76 ? 243 ASP A CB  1 
ATOM   1963 C  CG  . ASP A 1 242 ? -0.729  -14.444 11.683  1.00 10.47 ? 243 ASP A CG  1 
ATOM   1964 O  OD1 . ASP A 1 242 ? -1.799  -14.594 12.277  1.00 10.59 ? 243 ASP A OD1 1 
ATOM   1965 O  OD2 . ASP A 1 242 ? -0.113  -15.354 11.038  1.00 12.20 ? 243 ASP A OD2 1 
ATOM   1966 N  N   . ASN A 1 243 ? -1.758  -9.628  11.280  1.00 10.10 ? 244 ASN A N   1 
ATOM   1967 C  CA  . ASN A 1 243 ? -1.464  -8.214  11.536  1.00 9.96  ? 244 ASN A CA  1 
ATOM   1968 C  C   . ASN A 1 243 ? -2.023  -7.760  12.894  1.00 9.92  ? 244 ASN A C   1 
ATOM   1969 O  O   . ASN A 1 243 ? -2.694  -6.721  12.999  1.00 10.14 ? 244 ASN A O   1 
ATOM   1970 C  CB  . ASN A 1 243 ? -1.991  -7.359  10.373  1.00 10.31 ? 244 ASN A CB  1 
ATOM   1971 C  CG  . ASN A 1 243 ? -3.463  -7.547  10.108  1.00 10.17 ? 244 ASN A CG  1 
ATOM   1972 O  OD1 . ASN A 1 243 ? -4.117  -8.357  10.728  1.00 10.39 ? 244 ASN A OD1 1 
ATOM   1973 N  ND2 . ASN A 1 243 ? -3.994  -6.738  9.219   1.00 15.05 ? 244 ASN A ND2 1 
ATOM   1974 N  N   . TRP A 1 244 ? -1.716  -8.554  13.930  1.00 8.39  ? 245 TRP A N   1 
ATOM   1975 C  CA  . TRP A 1 244 ? -2.149  -8.260  15.274  1.00 8.49  ? 245 TRP A CA  1 
ATOM   1976 C  C   . TRP A 1 244 ? -0.939  -8.173  16.233  1.00 8.64  ? 245 TRP A C   1 
ATOM   1977 O  O   . TRP A 1 244 ? 0.061   -8.893  16.048  1.00 9.18  ? 245 TRP A O   1 
ATOM   1978 C  CB  . TRP A 1 244 ? -3.110  -9.371  15.820  1.00 9.29  ? 245 TRP A CB  1 
ATOM   1979 C  CG  . TRP A 1 244 ? -2.616  -10.791 15.589  1.00 8.56  ? 245 TRP A CG  1 
ATOM   1980 C  CD1 . TRP A 1 244 ? -2.750  -11.508 14.501  1.00 9.54  ? 245 TRP A CD1 1 
ATOM   1981 C  CD2 . TRP A 1 244 ? -2.060  -11.644 16.601  1.00 8.92  ? 245 TRP A CD2 1 
ATOM   1982 N  NE1 . TRP A 1 244 ? -2.236  -12.794 14.668  1.00 9.93  ? 245 TRP A NE1 1 
ATOM   1983 C  CE2 . TRP A 1 244 ? -1.799  -12.888 15.974  1.00 9.53  ? 245 TRP A CE2 1 
ATOM   1984 C  CE3 . TRP A 1 244 ? -1.774  -11.477 17.924  1.00 11.00 ? 245 TRP A CE3 1 
ATOM   1985 C  CZ2 . TRP A 1 244 ? -1.236  -13.979 16.682  1.00 10.60 ? 245 TRP A CZ2 1 
ATOM   1986 C  CZ3 . TRP A 1 244 ? -1.214  -12.557 18.652  1.00 10.54 ? 245 TRP A CZ3 1 
ATOM   1987 C  CH2 . TRP A 1 244 ? -0.921  -13.785 17.961  1.00 11.07 ? 245 TRP A CH2 1 
ATOM   1988 N  N   . ARG A 1 245 ? -1.117  -7.322  17.213  1.00 8.72  ? 246 ARG A N   1 
ATOM   1989 C  CA  . ARG A 1 245 ? -0.133  -7.212  18.314  1.00 8.64  ? 246 ARG A CA  1 
ATOM   1990 C  C   . ARG A 1 245 ? -0.610  -8.154  19.431  1.00 8.62  ? 246 ARG A C   1 
ATOM   1991 O  O   . ARG A 1 245 ? -1.790  -8.151  19.739  1.00 9.44  ? 246 ARG A O   1 
ATOM   1992 C  CB  . ARG A 1 245 ? -0.073  -5.774  18.819  1.00 8.29  ? 246 ARG A CB  1 
ATOM   1993 C  CG  . ARG A 1 245 ? 1.064   -5.522  19.781  1.00 8.81  ? 246 ARG A CG  1 
ATOM   1994 C  CD  . ARG A 1 245 ? 0.923   -4.213  20.551  1.00 10.67 ? 246 ARG A CD  1 
ATOM   1995 N  NE  . ARG A 1 245 ? 2.202   -3.856  21.159  1.00 9.52  ? 246 ARG A NE  1 
ATOM   1996 C  CZ  . ARG A 1 245 ? 2.393   -2.853  22.012  1.00 8.21  ? 246 ARG A CZ  1 
ATOM   1997 N  NH1 . ARG A 1 245 ? 1.383   -2.076  22.385  1.00 9.60  ? 246 ARG A NH1 1 
ATOM   1998 N  NH2 . ARG A 1 245 ? 3.608   -2.630  22.494  1.00 10.00 ? 246 ARG A NH2 1 
ATOM   1999 N  N   . PRO A 1 246 ? 0.285   -8.885  20.057  1.00 9.33  ? 247 PRO A N   1 
ATOM   2000 C  CA  . PRO A 1 246 ? -0.153  -9.756  21.159  1.00 8.70  ? 247 PRO A CA  1 
ATOM   2001 C  C   . PRO A 1 246 ? -0.498  -8.923  22.416  1.00 8.77  ? 247 PRO A C   1 
ATOM   2002 O  O   . PRO A 1 246 ? -0.135  -7.734  22.563  1.00 9.74  ? 247 PRO A O   1 
ATOM   2003 C  CB  . PRO A 1 246 ? 1.066   -10.604 21.468  1.00 12.39 ? 247 PRO A CB  1 
ATOM   2004 C  CG  . PRO A 1 246 ? 2.016   -10.370 20.443  1.00 16.89 ? 247 PRO A CG  1 
ATOM   2005 C  CD  . PRO A 1 246 ? 1.709   -9.135  19.695  1.00 11.50 ? 247 PRO A CD  1 
ATOM   2006 N  N   . ALA A 1 247 ? -1.141  -9.611  23.386  1.00 8.71  ? 248 ALA A N   1 
ATOM   2007 C  CA  . ALA A 1 247 ? -1.472  -8.968  24.641  1.00 9.03  ? 248 ALA A CA  1 
ATOM   2008 C  C   . ALA A 1 247 ? -0.237  -8.471  25.368  1.00 9.65  ? 248 ALA A C   1 
ATOM   2009 O  O   . ALA A 1 247 ? 0.814   -9.123  25.385  1.00 11.23 ? 248 ALA A O   1 
ATOM   2010 C  CB  . ALA A 1 247 ? -2.253  -9.977  25.533  1.00 10.85 ? 248 ALA A CB  1 
ATOM   2011 N  N   . GLN A 1 248 ? -0.382  -7.251  25.955  1.00 8.24  ? 249 GLN A N   1 
ATOM   2012 C  CA  . GLN A 1 248 ? 0.665   -6.572  26.698  1.00 9.73  ? 249 GLN A CA  1 
ATOM   2013 C  C   . GLN A 1 248 ? 0.347   -6.565  28.193  1.00 9.73  ? 249 GLN A C   1 
ATOM   2014 O  O   . GLN A 1 248 ? -0.815  -6.751  28.625  1.00 10.78 ? 249 GLN A O   1 
ATOM   2015 C  CB  . GLN A 1 248 ? 0.705   -5.085  26.181  1.00 11.69 ? 249 GLN A CB  1 
ATOM   2016 C  CG  . GLN A 1 248 ? 0.996   -5.068  24.667  1.00 11.16 ? 249 GLN A CG  1 
ATOM   2017 C  CD  . GLN A 1 248 ? 2.358   -5.714  24.324  1.00 11.33 ? 249 GLN A CD  1 
ATOM   2018 O  OE1 . GLN A 1 248 ? 3.397   -5.339  24.888  1.00 13.87 ? 249 GLN A OE1 1 
ATOM   2019 N  NE2 . GLN A 1 248 ? 2.360   -6.690  23.400  1.00 12.05 ? 249 GLN A NE2 1 
ATOM   2020 N  N   . PRO A 1 249 ? 1.393   -6.281  29.034  1.00 11.84 ? 250 PRO A N   1 
ATOM   2021 C  CA  . PRO A 1 249 ? 1.179   -6.311  30.476  1.00 13.21 ? 250 PRO A CA  1 
ATOM   2022 C  C   . PRO A 1 249 ? 0.109   -5.306  30.924  1.00 10.69 ? 250 PRO A C   1 
ATOM   2023 O  O   . PRO A 1 249 ? 0.111   -4.119  30.529  1.00 12.68 ? 250 PRO A O   1 
ATOM   2024 C  CB  . PRO A 1 249 ? 2.588   -5.863  31.023  1.00 15.85 ? 250 PRO A CB  1 
ATOM   2025 C  CG  . PRO A 1 249 ? 3.536   -6.383  30.015  1.00 16.75 ? 250 PRO A CG  1 
ATOM   2026 C  CD  . PRO A 1 249 ? 2.792   -6.035  28.649  1.00 15.38 ? 250 PRO A CD  1 
ATOM   2027 N  N   . LEU A 1 250 ? -0.822  -5.767  31.749  1.00 11.59 ? 251 LEU A N   1 
ATOM   2028 C  CA  . LEU A 1 250 ? -1.859  -4.929  32.297  1.00 11.37 ? 251 LEU A CA  1 
ATOM   2029 C  C   . LEU A 1 250 ? -1.318  -3.818  33.199  1.00 10.98 ? 251 LEU A C   1 
ATOM   2030 O  O   . LEU A 1 250 ? -1.876  -2.736  33.331  1.00 12.13 ? 251 LEU A O   1 
ATOM   2031 C  CB  . LEU A 1 250 ? -2.927  -5.783  32.980  1.00 13.44 ? 251 LEU A CB  1 
ATOM   2032 C  CG  . LEU A 1 250 ? -4.194  -5.054  33.387  1.00 13.51 ? 251 LEU A CG  1 
ATOM   2033 C  CD1 . LEU A 1 250 ? -4.994  -4.485  32.196  1.00 14.60 ? 251 LEU A CD1 1 
ATOM   2034 C  CD2 . LEU A 1 250 ? -5.056  -6.084  34.229  1.00 15.26 ? 251 LEU A CD2 1 
ATOM   2035 N  N   . LYS A 1 251 ? -0.261  -4.179  33.958  1.00 13.45 ? 252 LYS A N   1 
ATOM   2036 C  CA  . LYS A 1 251 ? 0.395   -3.145  34.834  1.00 13.99 ? 252 LYS A CA  1 
ATOM   2037 C  C   . LYS A 1 251 ? -0.631  -2.572  35.825  1.00 15.93 ? 252 LYS A C   1 
ATOM   2038 O  O   . LYS A 1 251 ? -1.420  -3.375  36.371  1.00 18.52 ? 252 LYS A O   1 
ATOM   2039 C  CB  . LYS A 1 251 ? 1.137   -2.084  34.015  1.00 16.56 ? 252 LYS A CB  1 
ATOM   2040 C  CG  . LYS A 1 251 ? 2.293   -2.790  33.263  1.00 17.89 ? 252 LYS A CG  1 
ATOM   2041 C  CD  . LYS A 1 251 ? 3.253   -1.760  32.766  1.00 22.04 ? 252 LYS A CD  1 
ATOM   2042 C  CE  . LYS A 1 251 ? 4.432   -2.452  32.237  1.00 24.42 ? 252 LYS A CE  1 
ATOM   2043 N  NZ  . LYS A 1 251 ? 5.240   -1.488  31.445  1.00 30.19 ? 252 LYS A NZ  1 
ATOM   2044 N  N   . ASN A 1 252 ? -0.622  -1.268  36.055  1.00 14.71 ? 253 ASN A N   1 
ATOM   2045 C  CA  . ASN A 1 252 ? -1.470  -0.771  37.085  1.00 21.86 ? 253 ASN A CA  1 
ATOM   2046 C  C   . ASN A 1 252 ? -2.799  -0.315  36.480  1.00 19.91 ? 253 ASN A C   1 
ATOM   2047 O  O   . ASN A 1 252 ? -2.995  1.012   36.487  1.00 23.51 ? 253 ASN A O   1 
ATOM   2048 C  CB  . ASN A 1 252 ? -0.744  0.405   37.817  1.00 25.14 ? 253 ASN A CB  1 
ATOM   2049 C  CG  . ASN A 1 252 ? -1.486  0.841   39.115  1.00 32.59 ? 253 ASN A CG  1 
ATOM   2050 O  OD1 . ASN A 1 252 ? -1.890  -0.018  39.941  1.00 40.63 ? 253 ASN A OD1 1 
ATOM   2051 N  ND2 . ASN A 1 252 ? -1.673  2.178   39.299  1.00 35.39 ? 253 ASN A ND2 1 
ATOM   2052 N  N   . ARG A 1 253 ? -3.580  -1.346  35.912  1.00 16.16 ? 254 ARG A N   1 
ATOM   2053 C  CA  . ARG A 1 253 ? -4.896  -1.003  35.349  1.00 12.66 ? 254 ARG A CA  1 
ATOM   2054 C  C   . ARG A 1 253 ? -5.988  -1.941  35.796  1.00 14.22 ? 254 ARG A C   1 
ATOM   2055 O  O   . ARG A 1 253 ? -5.729  -3.148  36.005  1.00 17.24 ? 254 ARG A O   1 
ATOM   2056 C  CB  . ARG A 1 253 ? -4.826  -0.986  33.849  1.00 12.18 ? 254 ARG A CB  1 
ATOM   2057 C  CG  . ARG A 1 253 ? -3.903  0.137   33.336  1.00 11.71 ? 254 ARG A CG  1 
ATOM   2058 C  CD  . ARG A 1 253 ? -3.858  0.151   31.802  1.00 11.70 ? 254 ARG A CD  1 
ATOM   2059 N  NE  . ARG A 1 253 ? -3.002  -0.978  31.346  1.00 9.88  ? 254 ARG A NE  1 
ATOM   2060 C  CZ  . ARG A 1 253 ? -2.799  -1.240  30.076  1.00 9.45  ? 254 ARG A CZ  1 
ATOM   2061 N  NH1 . ARG A 1 253 ? -3.406  -0.520  29.111  1.00 9.08  ? 254 ARG A NH1 1 
ATOM   2062 N  NH2 . ARG A 1 253 ? -1.943  -2.230  29.726  1.00 9.67  ? 254 ARG A NH2 1 
ATOM   2063 N  N   A GLN A 1 254 ? -7.221  -1.422  35.773  0.50 12.58 ? 255 GLN A N   1 
ATOM   2064 N  N   B GLN A 1 254 ? -7.218  -1.437  35.940  0.50 14.08 ? 255 GLN A N   1 
ATOM   2065 C  CA  A GLN A 1 254 ? -8.441  -2.131  36.157  0.50 14.85 ? 255 GLN A CA  1 
ATOM   2066 C  CA  B GLN A 1 254 ? -8.390  -2.295  36.097  0.50 15.56 ? 255 GLN A CA  1 
ATOM   2067 C  C   A GLN A 1 254 ? -9.414  -2.199  35.000  0.50 12.63 ? 255 GLN A C   1 
ATOM   2068 C  C   B GLN A 1 254 ? -9.205  -2.238  34.820  0.50 13.66 ? 255 GLN A C   1 
ATOM   2069 O  O   A GLN A 1 254 ? -9.837  -1.154  34.490  0.50 14.34 ? 255 GLN A O   1 
ATOM   2070 O  O   B GLN A 1 254 ? -9.293  -1.212  34.060  0.50 14.00 ? 255 GLN A O   1 
ATOM   2071 C  CB  A GLN A 1 254 ? -9.123  -1.374  37.289  0.50 15.06 ? 255 GLN A CB  1 
ATOM   2072 C  CB  B GLN A 1 254 ? -9.284  -1.986  37.321  0.50 17.53 ? 255 GLN A CB  1 
ATOM   2073 C  CG  A GLN A 1 254 ? -8.526  -1.833  38.659  0.50 17.34 ? 255 GLN A CG  1 
ATOM   2074 C  CG  B GLN A 1 254 ? -9.109  -3.019  38.499  0.50 23.90 ? 255 GLN A CG  1 
ATOM   2075 C  CD  A GLN A 1 254 ? -9.285  -1.319  39.877  0.50 20.76 ? 255 GLN A CD  1 
ATOM   2076 C  CD  B GLN A 1 254 ? -10.351 -3.810  38.824  0.50 28.99 ? 255 GLN A CD  1 
ATOM   2077 O  OE1 A GLN A 1 254 ? -10.429 -0.848  39.758  0.50 25.25 ? 255 GLN A OE1 1 
ATOM   2078 O  OE1 B GLN A 1 254 ? -11.218 -3.307  39.588  0.50 29.20 ? 255 GLN A OE1 1 
ATOM   2079 N  NE2 A GLN A 1 254 ? -8.629  -1.369  41.065  0.50 20.93 ? 255 GLN A NE2 1 
ATOM   2080 N  NE2 B GLN A 1 254 ? -10.451 -5.098  38.303  0.50 27.81 ? 255 GLN A NE2 1 
ATOM   2081 N  N   . ILE A 1 255 ? -9.736  -3.407  34.513  1.00 11.52 ? 256 ILE A N   1 
ATOM   2082 C  CA  . ILE A 1 255 ? -10.734 -3.522  33.471  1.00 11.03 ? 256 ILE A CA  1 
ATOM   2083 C  C   . ILE A 1 255 ? -12.119 -3.573  34.129  1.00 10.94 ? 256 ILE A C   1 
ATOM   2084 O  O   . ILE A 1 255 ? -12.354 -4.289  35.089  1.00 12.88 ? 256 ILE A O   1 
ATOM   2085 C  CB  . ILE A 1 255 ? -10.484 -4.763  32.627  1.00 11.58 ? 256 ILE A CB  1 
ATOM   2086 C  CG1 . ILE A 1 255 ? -9.047  -4.740  32.059  1.00 12.39 ? 256 ILE A CG1 1 
ATOM   2087 C  CG2 . ILE A 1 255 ? -11.634 -4.909  31.537  1.00 12.38 ? 256 ILE A CG2 1 
ATOM   2088 C  CD1 . ILE A 1 255 ? -8.793  -6.003  31.259  1.00 13.55 ? 256 ILE A CD1 1 
ATOM   2089 N  N   . LYS A 1 256 ? -13.031 -2.723  33.615  1.00 10.70 ? 257 LYS A N   1 
ATOM   2090 C  CA  . LYS A 1 256 ? -14.375 -2.618  34.151  1.00 10.39 ? 257 LYS A CA  1 
ATOM   2091 C  C   . LYS A 1 256 ? -15.356 -3.243  33.183  1.00 10.57 ? 257 LYS A C   1 
ATOM   2092 O  O   . LYS A 1 256 ? -15.189 -3.114  31.954  1.00 12.02 ? 257 LYS A O   1 
ATOM   2093 C  CB  . LYS A 1 256 ? -14.719 -1.109  34.379  1.00 12.85 ? 257 LYS A CB  1 
ATOM   2094 C  CG  . LYS A 1 256 ? -13.795 -0.559  35.502  1.00 18.54 ? 257 LYS A CG  1 
ATOM   2095 C  CD  . LYS A 1 256 ? -14.221 0.797   35.923  1.00 29.02 ? 257 LYS A CD  1 
ATOM   2096 C  CE  . LYS A 1 256 ? -13.146 1.368   36.856  1.00 33.90 ? 257 LYS A CE  1 
ATOM   2097 N  NZ  . LYS A 1 256 ? -12.991 2.854   36.634  1.00 37.10 ? 257 LYS A NZ  1 
ATOM   2098 N  N   . ALA A 1 257 ? -16.390 -3.867  33.755  1.00 11.44 ? 258 ALA A N   1 
ATOM   2099 C  CA  . ALA A 1 257 ? -17.469 -4.482  32.959  1.00 12.98 ? 258 ALA A CA  1 
ATOM   2100 C  C   . ALA A 1 257 ? -18.772 -3.703  33.116  1.00 11.94 ? 258 ALA A C   1 
ATOM   2101 O  O   . ALA A 1 257 ? -19.113 -3.246  34.215  1.00 13.32 ? 258 ALA A O   1 
ATOM   2102 C  CB  . ALA A 1 257 ? -17.696 -6.014  33.352  1.00 14.23 ? 258 ALA A CB  1 
ATOM   2103 N  N   . SER A 1 258 ? -19.495 -3.532  32.006  1.00 11.82 ? 259 SER A N   1 
ATOM   2104 C  CA  . SER A 1 258 ? -20.768 -2.811  32.041  1.00 13.23 ? 259 SER A CA  1 
ATOM   2105 C  C   . SER A 1 258 ? -21.913 -3.696  32.478  1.00 14.50 ? 259 SER A C   1 
ATOM   2106 O  O   . SER A 1 258 ? -23.041 -3.195  32.560  1.00 19.00 ? 259 SER A O   1 
ATOM   2107 C  CB  . SER A 1 258 ? -21.088 -2.232  30.685  1.00 13.12 ? 259 SER A CB  1 
ATOM   2108 O  OG  . SER A 1 258 ? -21.512 -3.312  29.770  1.00 13.04 ? 259 SER A OG  1 
ATOM   2109 N  N   . PHE A 1 259 ? -21.650 -4.991  32.713  1.00 15.83 ? 260 PHE A N   1 
ATOM   2110 C  CA  . PHE A 1 259 ? -22.689 -5.995  32.887  1.00 16.33 ? 260 PHE A CA  1 
ATOM   2111 C  C   . PHE A 1 259 ? -22.237 -6.948  33.994  1.00 20.64 ? 260 PHE A C   1 
ATOM   2112 O  O   . PHE A 1 259 ? -21.011 -7.144  34.272  1.00 20.92 ? 260 PHE A O   1 
ATOM   2113 C  CB  . PHE A 1 259 ? -22.873 -6.799  31.561  1.00 16.79 ? 260 PHE A CB  1 
ATOM   2114 C  CG  . PHE A 1 259 ? -21.604 -7.541  31.116  1.00 17.11 ? 260 PHE A CG  1 
ATOM   2115 C  CD1 . PHE A 1 259 ? -20.565 -6.864  30.449  1.00 14.67 ? 260 PHE A CD1 1 
ATOM   2116 C  CD2 . PHE A 1 259 ? -21.399 -8.869  31.499  1.00 20.53 ? 260 PHE A CD2 1 
ATOM   2117 C  CE1 . PHE A 1 259 ? -19.348 -7.608  30.100  1.00 17.03 ? 260 PHE A CE1 1 
ATOM   2118 C  CE2 . PHE A 1 259 ? -20.215 -9.545  31.165  1.00 20.11 ? 260 PHE A CE2 1 
ATOM   2119 C  CZ  . PHE A 1 259 ? -19.196 -8.891  30.457  1.00 19.74 ? 260 PHE A CZ  1 
ATOM   2120 N  N   . LYS A 1 260 ? -23.288 -7.648  34.474  1.00 26.36 ? 261 LYS A N   1 
ATOM   2121 C  CA  . LYS A 1 260 ? -23.337 -8.715  35.532  1.00 34.65 ? 261 LYS A CA  1 
ATOM   2122 C  C   . LYS A 1 260 ? -22.823 -8.340  36.908  1.00 38.16 ? 261 LYS A C   1 
ATOM   2123 O  O   . LYS A 1 260 ? -23.496 -8.275  37.968  1.00 41.11 ? 261 LYS A O   1 
ATOM   2124 C  CB  . LYS A 1 260 ? -22.694 -10.012 35.062  1.00 34.32 ? 261 LYS A CB  1 
ATOM   2125 C  CG  . LYS A 1 260 ? -23.337 -10.632 33.850  1.00 36.49 ? 261 LYS A CG  1 
ATOM   2126 C  CD  . LYS A 1 260 ? -22.296 -11.630 33.224  1.00 43.35 ? 261 LYS A CD  1 
ATOM   2127 C  CE  . LYS A 1 260 ? -22.898 -12.356 32.052  1.00 46.11 ? 261 LYS A CE  1 
ATOM   2128 N  NZ  . LYS A 1 260 ? -23.995 -13.288 32.464  1.00 49.13 ? 261 LYS A NZ  1 
ATOM   2129 O  OXT . LYS A 1 260 ? -21.655 -7.967  36.915  1.00 43.02 ? 261 LYS A OXT 1 
HETATM 2130 ZN ZN  . ZN  B 2 .   ? -6.699  -1.677  15.327  1.00 8.13  ? 262 ZN  A ZN  1 
HETATM 2131 S  S   . DMS C 3 .   ? 1.338   -11.687 14.964  1.00 22.49 ? 263 DMS A S   1 
HETATM 2132 O  O   . DMS C 3 .   ? 2.017   -13.225 14.544  1.00 23.88 ? 263 DMS A O   1 
HETATM 2133 C  C1  . DMS C 3 .   ? 1.627   -11.442 16.689  1.00 18.12 ? 263 DMS A C1  1 
HETATM 2134 C  C2  . DMS C 3 .   ? 2.427   -10.488 14.196  1.00 23.58 ? 263 DMS A C2  1 
HETATM 2135 S  S   . DMS D 3 .   ? 10.773  -0.894  13.980  1.00 29.21 ? 264 DMS A S   1 
HETATM 2136 O  O   . DMS D 3 .   ? 10.002  0.603   13.575  1.00 28.57 ? 264 DMS A O   1 
HETATM 2137 C  C1  . DMS D 3 .   ? 11.477  -0.595  15.669  1.00 22.18 ? 264 DMS A C1  1 
HETATM 2138 C  C2  . DMS D 3 .   ? 9.861   -2.374  14.051  1.00 22.38 ? 264 DMS A C2  1 
HETATM 2139 N  N1  . BCN E 4 .   ? -20.401 -14.688 23.328  1.00 29.59 ? 265 BCN A N1  1 
HETATM 2140 C  C1  . BCN E 4 .   ? -19.838 -14.192 24.549  1.00 29.97 ? 265 BCN A C1  1 
HETATM 2141 C  C2  . BCN E 4 .   ? -19.963 -15.173 25.639  1.00 30.65 ? 265 BCN A C2  1 
HETATM 2142 O  O21 . BCN E 4 .   ? -20.906 -15.997 25.601  1.00 33.90 ? 265 BCN A O21 1 
HETATM 2143 O  O22 . BCN E 4 .   ? -19.167 -15.075 26.647  1.00 33.45 ? 265 BCN A O22 1 
HETATM 2144 C  C3  . BCN E 4 .   ? -20.051 -15.666 22.389  1.00 21.00 ? 265 BCN A C3  1 
HETATM 2145 C  C4  . BCN E 4 .   ? -20.634 -16.839 21.732  1.00 33.53 ? 265 BCN A C4  1 
HETATM 2146 O  O4  . BCN E 4 .   ? -20.718 -16.325 20.400  1.00 34.89 ? 265 BCN A O4  1 
HETATM 2147 C  C5  . BCN E 4 .   ? -21.609 -14.010 22.943  1.00 24.71 ? 265 BCN A C5  1 
HETATM 2148 C  C6  . BCN E 4 .   ? -22.377 -13.690 24.230  1.00 35.97 ? 265 BCN A C6  1 
HETATM 2149 O  O6  . BCN E 4 .   ? -22.383 -12.426 24.792  1.00 32.41 ? 265 BCN A O6  1 
HETATM 2150 N  N1  A E59 F 5 .   ? -1.989  7.779   12.539  0.50 19.73 ? 266 E59 A N1  1 
HETATM 2151 N  N1  B E59 F 5 .   ? -1.484  7.734   13.842  0.50 27.77 ? 266 E59 A N1  1 
HETATM 2152 C  C2  A E59 F 5 .   ? -2.006  9.079   12.285  0.50 24.52 ? 266 E59 A C2  1 
HETATM 2153 C  C2  B E59 F 5 .   ? -1.181  8.789   14.591  0.50 28.58 ? 266 E59 A C2  1 
HETATM 2154 C  C3  A E59 F 5 .   ? -1.459  9.961   13.208  0.50 22.21 ? 266 E59 A C3  1 
HETATM 2155 C  C3  B E59 F 5 .   ? -1.236  10.060  14.040  0.50 28.99 ? 266 E59 A C3  1 
HETATM 2156 C  C4  A E59 F 5 .   ? -0.908  9.431   14.364  0.50 21.62 ? 266 E59 A C4  1 
HETATM 2157 C  C4  B E59 F 5 .   ? -1.607  10.183  12.712  0.50 28.62 ? 266 E59 A C4  1 
HETATM 2158 N  N5  A E59 F 5 .   ? -0.919  8.121   14.558  0.50 21.59 ? 266 E59 A N5  1 
HETATM 2159 N  N5  B E59 F 5 .   ? -1.897  9.095   12.014  0.50 29.60 ? 266 E59 A N5  1 
HETATM 2160 C  C6  A E59 F 5 .   ? -1.452  7.304   13.657  0.50 19.28 ? 266 E59 A C6  1 
HETATM 2161 C  C6  B E59 F 5 .   ? -1.839  7.888   12.569  0.50 27.17 ? 266 E59 A C6  1 
HETATM 2162 O  O7  A E59 F 5 .   ? -2.513  9.488   11.238  0.50 24.56 ? 266 E59 A O7  1 
HETATM 2163 O  O7  B E59 F 5 .   ? -0.856  8.643   15.773  0.50 29.29 ? 266 E59 A O7  1 
HETATM 2164 C  C8  A E59 F 5 .   ? -0.295  10.321  15.400  0.50 20.86 ? 266 E59 A C8  1 
HETATM 2165 C  C8  B E59 F 5 .   ? -1.682  11.530  12.060  0.50 27.77 ? 266 E59 A C8  1 
HETATM 2166 S  S9  A E59 F 5 .   ? -1.455  5.543   13.941  0.50 19.76 ? 266 E59 A S9  1 
HETATM 2167 S  S9  B E59 F 5 .   ? -2.241  6.472   11.562  0.50 26.68 ? 266 E59 A S9  1 
HETATM 2168 C  C10 A E59 F 5 .   ? -2.778  5.119   12.824  0.50 14.46 ? 266 E59 A C10 1 
HETATM 2169 C  C10 B E59 F 5 .   ? -2.684  5.260   12.810  0.50 20.81 ? 266 E59 A C10 1 
HETATM 2170 C  C11 A E59 F 5 .   ? -4.138  5.383   13.365  0.50 15.27 ? 266 E59 A C11 1 
HETATM 2171 C  C11 B E59 F 5 .   ? -4.025  5.432   13.445  0.50 17.25 ? 266 E59 A C11 1 
HETATM 2172 O  O12 A E59 F 5 .   ? -4.812  6.392   13.113  0.50 14.50 ? 266 E59 A O12 1 
HETATM 2173 O  O12 B E59 F 5 .   ? -4.727  6.437   13.263  0.50 20.74 ? 266 E59 A O12 1 
HETATM 2174 C  C13 A E59 F 5 .   ? -4.613  4.313   14.231  0.50 14.34 ? 266 E59 A C13 1 
HETATM 2175 C  C13 B E59 F 5 .   ? -4.498  4.334   14.282  0.50 10.29 ? 266 E59 A C13 1 
HETATM 2176 C  C14 A E59 F 5 .   ? -5.904  4.295   14.723  0.50 11.38 ? 266 E59 A C14 1 
HETATM 2177 C  C14 B E59 F 5 .   ? -5.805  4.312   14.740  0.50 9.61  ? 266 E59 A C14 1 
HETATM 2178 C  C15 A E59 F 5 .   ? -6.301  3.241   15.532  0.50 9.68  ? 266 E59 A C15 1 
HETATM 2179 C  C15 B E59 F 5 .   ? -6.240  3.256   15.528  0.50 7.42  ? 266 E59 A C15 1 
HETATM 2180 C  C16 A E59 F 5 .   ? -5.407  2.224   15.838  0.50 9.50  ? 266 E59 A C16 1 
HETATM 2181 C  C16 B E59 F 5 .   ? -5.364  2.230   15.851  0.50 8.16  ? 266 E59 A C16 1 
HETATM 2182 C  C17 A E59 F 5 .   ? -4.115  2.236   15.341  0.50 11.28 ? 266 E59 A C17 1 
HETATM 2183 C  C17 B E59 F 5 .   ? -4.056  2.243   15.391  0.50 8.54  ? 266 E59 A C17 1 
HETATM 2184 C  C18 A E59 F 5 .   ? -3.718  3.290   14.534  0.50 13.18 ? 266 E59 A C18 1 
HETATM 2185 C  C18 B E59 F 5 .   ? -3.622  3.301   14.604  0.50 9.03  ? 266 E59 A C18 1 
HETATM 2186 S  S19 A E59 F 5 .   ? -5.924  0.888   16.854  0.50 9.30  ? 266 E59 A S19 1 
HETATM 2187 S  S19 B E59 F 5 .   ? -5.919  0.889   16.844  0.50 6.36  ? 266 E59 A S19 1 
HETATM 2188 O  O20 A E59 F 5 .   ? -7.438  0.878   16.825  0.50 7.85  ? 266 E59 A O20 1 
HETATM 2189 O  O20 B E59 F 5 .   ? -7.432  0.887   16.802  0.50 7.42  ? 266 E59 A O20 1 
HETATM 2190 O  O21 A E59 F 5 .   ? -5.388  1.058   18.258  0.50 10.01 ? 266 E59 A O21 1 
HETATM 2191 O  O21 B E59 F 5 .   ? -5.396  1.047   18.255  0.50 7.91  ? 266 E59 A O21 1 
HETATM 2192 N  N22 A E59 F 5 .   ? -5.331  -0.577  16.139  0.50 7.35  ? 266 E59 A N22 1 
HETATM 2193 N  N22 B E59 F 5 .   ? -5.328  -0.577  16.131  0.50 7.98  ? 266 E59 A N22 1 
HETATM 2194 O  O   . HOH G 6 .   ? -15.517 -16.448 25.617  1.00 30.94 ? 126 HOH A O   1 
HETATM 2195 O  O   . HOH G 6 .   ? -17.060 -8.436  20.435  1.00 9.90  ? 267 HOH A O   1 
HETATM 2196 O  O   . HOH G 6 .   ? -1.253  -4.107  15.776  1.00 9.71  ? 268 HOH A O   1 
HETATM 2197 O  O   . HOH G 6 .   ? -4.550  -13.539 18.103  1.00 9.73  ? 269 HOH A O   1 
HETATM 2198 O  O   . HOH G 6 .   ? -3.547  -11.175 20.920  1.00 10.42 ? 270 HOH A O   1 
HETATM 2199 O  O   . HOH G 6 .   ? -21.662 -7.209  23.640  1.00 12.38 ? 271 HOH A O   1 
HETATM 2200 O  O   . HOH G 6 .   ? -3.446  -13.292 25.215  1.00 12.08 ? 272 HOH A O   1 
HETATM 2201 O  O   . HOH G 6 .   ? -8.757  -3.853  7.938   1.00 10.25 ? 273 HOH A O   1 
HETATM 2202 O  O   . HOH G 6 .   ? -7.961  -15.474 11.354  1.00 11.25 ? 274 HOH A O   1 
HETATM 2203 O  O   . HOH G 6 .   ? 4.859   -4.918  21.010  1.00 14.18 ? 275 HOH A O   1 
HETATM 2204 O  O   . HOH G 6 .   ? -10.654 8.704   25.606  1.00 10.66 ? 276 HOH A O   1 
HETATM 2205 O  O   . HOH G 6 .   ? -3.817  -15.939 24.379  1.00 13.45 ? 277 HOH A O   1 
HETATM 2206 O  O   . HOH G 6 .   ? 1.230   -1.572  29.516  1.00 14.71 ? 278 HOH A O   1 
HETATM 2207 O  O   . HOH G 6 .   ? -2.098  -12.343 22.882  1.00 10.99 ? 279 HOH A O   1 
HETATM 2208 O  O   . HOH G 6 .   ? -2.542  -8.784  29.183  1.00 12.53 ? 280 HOH A O   1 
HETATM 2209 O  O   . HOH G 6 .   ? 8.546   -3.892  21.120  1.00 14.93 ? 281 HOH A O   1 
HETATM 2210 O  O   . HOH G 6 .   ? -22.006 5.684   4.816   1.00 16.38 ? 282 HOH A O   1 
HETATM 2211 O  O   . HOH G 6 .   ? -19.390 9.994   8.986   1.00 14.47 ? 283 HOH A O   1 
HETATM 2212 O  O   . HOH G 6 .   ? -10.362 -18.322 17.045  1.00 14.16 ? 284 HOH A O   1 
HETATM 2213 O  O   . HOH G 6 .   ? 3.559   4.971   29.963  1.00 20.32 ? 285 HOH A O   1 
HETATM 2214 O  O   . HOH G 6 .   ? -18.004 -20.519 8.070   1.00 15.86 ? 286 HOH A O   1 
HETATM 2215 O  O   . HOH G 6 .   ? -12.884 -17.241 16.911  1.00 14.72 ? 287 HOH A O   1 
HETATM 2216 O  O   . HOH G 6 .   ? -24.808 -7.743  9.050   1.00 18.31 ? 288 HOH A O   1 
HETATM 2217 O  O   . HOH G 6 .   ? -8.121  -19.393 21.721  1.00 15.35 ? 289 HOH A O   1 
HETATM 2218 O  O   . HOH G 6 .   ? -16.163 -12.318 24.457  1.00 14.88 ? 290 HOH A O   1 
HETATM 2219 O  O   . HOH G 6 .   ? -13.877 10.368  27.951  1.00 18.79 ? 291 HOH A O   1 
HETATM 2220 O  O   . HOH G 6 .   ? -23.001 -11.659 14.106  1.00 21.42 ? 292 HOH A O   1 
HETATM 2221 O  O   . HOH G 6 .   ? -24.169 8.630   20.232  1.00 21.17 ? 293 HOH A O   1 
HETATM 2222 O  O   . HOH G 6 .   ? -20.955 -12.763 -1.924  1.00 17.65 ? 294 HOH A O   1 
HETATM 2223 O  O   . HOH G 6 .   ? -16.387 -9.956  33.037  1.00 19.25 ? 295 HOH A O   1 
HETATM 2224 O  O   . HOH G 6 .   ? -17.969 10.627  11.388  1.00 16.95 ? 296 HOH A O   1 
HETATM 2225 O  O   . HOH G 6 .   ? -23.206 -3.077  6.844   1.00 20.69 ? 297 HOH A O   1 
HETATM 2226 O  O   . HOH G 6 .   ? -12.020 2.749   30.917  1.00 19.39 ? 298 HOH A O   1 
HETATM 2227 O  O   . HOH G 6 .   ? -24.074 -0.724  26.457  1.00 18.35 ? 299 HOH A O   1 
HETATM 2228 O  O   . HOH G 6 .   ? -6.808  -20.243 19.582  1.00 14.50 ? 300 HOH A O   1 
HETATM 2229 O  O   . HOH G 6 .   ? 5.411   7.069   20.330  1.00 17.29 ? 301 HOH A O   1 
HETATM 2230 O  O   . HOH G 6 .   ? -1.215  -11.166 29.023  1.00 17.40 ? 302 HOH A O   1 
HETATM 2231 O  O   . HOH G 6 .   ? -20.403 10.748  26.737  1.00 19.60 ? 303 HOH A O   1 
HETATM 2232 O  O   . HOH G 6 .   ? -9.625  -8.006  34.119  1.00 21.23 ? 304 HOH A O   1 
HETATM 2233 O  O   . HOH G 6 .   ? -6.100  -4.547  -6.416  1.00 25.80 ? 305 HOH A O   1 
HETATM 2234 O  O   . HOH G 6 .   ? 1.248   8.756   24.475  1.00 18.27 ? 306 HOH A O   1 
HETATM 2235 O  O   . HOH G 6 .   ? -17.729 -21.231 17.649  1.00 25.26 ? 307 HOH A O   1 
HETATM 2236 O  O   . HOH G 6 .   ? -13.097 -16.879 26.720  1.00 16.15 ? 308 HOH A O   1 
HETATM 2237 O  O   . HOH G 6 .   ? 4.376   -6.449  7.818   1.00 20.80 ? 309 HOH A O   1 
HETATM 2238 O  O   . HOH G 6 .   ? 7.626   6.066   21.767  1.00 17.99 ? 310 HOH A O   1 
HETATM 2239 O  O   . HOH G 6 .   ? -4.799  -12.021 32.147  1.00 18.99 ? 311 HOH A O   1 
HETATM 2240 O  O   . HOH G 6 .   ? -7.090  5.935   6.391   1.00 20.78 ? 312 HOH A O   1 
HETATM 2241 O  O   . HOH G 6 .   ? -1.425  1.924   11.616  1.00 23.35 ? 313 HOH A O   1 
HETATM 2242 O  O   . HOH G 6 .   ? -14.681 -18.602 18.750  1.00 17.68 ? 314 HOH A O   1 
HETATM 2243 O  O   . HOH G 6 .   ? -7.463  -8.688  32.645  1.00 16.96 ? 315 HOH A O   1 
HETATM 2244 O  O   . HOH G 6 .   ? -28.766 0.167   24.477  1.00 22.31 ? 316 HOH A O   1 
HETATM 2245 O  O   . HOH G 6 .   ? 1.389   -11.774 25.120  1.00 24.61 ? 317 HOH A O   1 
HETATM 2246 O  O   . HOH G 6 .   ? -8.003  -22.146 10.422  1.00 23.59 ? 318 HOH A O   1 
HETATM 2247 O  O   . HOH G 6 .   ? 2.627   -4.297  7.772   1.00 19.40 ? 319 HOH A O   1 
HETATM 2248 O  O   . HOH G 6 .   ? -26.263 3.522   15.465  1.00 22.04 ? 320 HOH A O   1 
HETATM 2249 O  O   . HOH G 6 .   ? -23.959 -0.812  3.947   1.00 21.13 ? 321 HOH A O   1 
HETATM 2250 O  O   . HOH G 6 .   ? -13.798 -21.237 15.104  1.00 20.71 ? 322 HOH A O   1 
HETATM 2251 O  O   . HOH G 6 .   ? -2.024  -17.510 25.578  1.00 25.30 ? 323 HOH A O   1 
HETATM 2252 O  O   . HOH G 6 .   ? -16.174 15.883  23.661  1.00 19.13 ? 324 HOH A O   1 
HETATM 2253 O  O   . HOH G 6 .   ? -9.146  -5.849  35.992  1.00 18.33 ? 325 HOH A O   1 
HETATM 2254 O  O   . HOH G 6 .   ? -22.850 -5.885  2.782   1.00 21.18 ? 326 HOH A O   1 
HETATM 2255 O  O   . HOH G 6 .   ? -13.421 -18.533 14.661  1.00 18.64 ? 327 HOH A O   1 
HETATM 2256 O  O   . HOH G 6 .   ? -2.562  -3.098  11.435  1.00 25.64 ? 328 HOH A O   1 
HETATM 2257 O  O   . HOH G 6 .   ? -30.999 1.206   25.959  1.00 24.29 ? 329 HOH A O   1 
HETATM 2258 O  O   . HOH G 6 .   ? -10.630 -19.460 20.097  1.00 18.85 ? 330 HOH A O   1 
HETATM 2259 O  O   . HOH G 6 .   ? -1.420  -13.116 27.124  1.00 24.48 ? 331 HOH A O   1 
HETATM 2260 O  O   . HOH G 6 .   ? 2.583   -11.306 9.514   1.00 21.24 ? 332 HOH A O   1 
HETATM 2261 O  O   . HOH G 6 .   ? -14.931 -21.094 17.640  1.00 18.79 ? 333 HOH A O   1 
HETATM 2262 O  O   . HOH G 6 .   ? -0.558  10.809  23.439  1.00 17.89 ? 334 HOH A O   1 
HETATM 2263 O  O   . HOH G 6 .   ? 4.239   -3.460  26.613  1.00 19.18 ? 335 HOH A O   1 
HETATM 2264 O  O   . HOH G 6 .   ? -4.773  1.016   43.393  1.00 23.95 ? 336 HOH A O   1 
HETATM 2265 O  O   . HOH G 6 .   ? -11.052 -19.475 7.133   1.00 29.15 ? 337 HOH A O   1 
HETATM 2266 O  O   . HOH G 6 .   ? -0.254  -14.326 22.277  1.00 22.06 ? 338 HOH A O   1 
HETATM 2267 O  O   . HOH G 6 .   ? -4.267  -8.526  31.192  1.00 18.99 ? 339 HOH A O   1 
HETATM 2268 O  O   . HOH G 6 .   ? 8.527   -4.757  23.701  1.00 23.52 ? 340 HOH A O   1 
HETATM 2269 O  O   . HOH G 6 .   ? -14.333 -16.622 29.044  1.00 24.00 ? 341 HOH A O   1 
HETATM 2270 O  O   . HOH G 6 .   ? -6.934  -14.936 31.646  1.00 23.55 ? 342 HOH A O   1 
HETATM 2271 O  O   . HOH G 6 .   ? 4.481   -2.649  29.130  1.00 23.08 ? 343 HOH A O   1 
HETATM 2272 O  O   . HOH G 6 .   ? -0.666  -8.574  32.576  1.00 23.18 ? 344 HOH A O   1 
HETATM 2273 O  O   . HOH G 6 .   ? -25.645 -10.707 17.740  1.00 22.78 ? 345 HOH A O   1 
HETATM 2274 O  O   . HOH G 6 .   ? -0.881  -17.485 18.090  1.00 32.67 ? 346 HOH A O   1 
HETATM 2275 O  O   . HOH G 6 .   ? -2.468  7.419   -5.225  1.00 21.26 ? 347 HOH A O   1 
HETATM 2276 O  O   . HOH G 6 .   ? -19.848 -16.911 2.934   1.00 23.82 ? 348 HOH A O   1 
HETATM 2277 O  O   . HOH G 6 .   ? -30.829 -7.201  22.357  1.00 28.05 ? 349 HOH A O   1 
HETATM 2278 O  O   . HOH G 6 .   ? -26.416 2.781   20.891  1.00 23.80 ? 350 HOH A O   1 
HETATM 2279 O  O   . HOH G 6 .   ? 0.128   -0.983  -4.686  1.00 18.22 ? 351 HOH A O   1 
HETATM 2280 O  O   . HOH G 6 .   ? -26.768 -2.449  14.560  1.00 23.52 ? 352 HOH A O   1 
HETATM 2281 O  O   . HOH G 6 .   ? -17.377 -16.224 22.167  1.00 25.00 ? 353 HOH A O   1 
HETATM 2282 O  O   . HOH G 6 .   ? -10.069 -26.369 12.177  1.00 19.11 ? 354 HOH A O   1 
HETATM 2283 O  O   . HOH G 6 .   ? -15.449 -21.812 13.189  1.00 19.32 ? 355 HOH A O   1 
HETATM 2284 O  O   . HOH G 6 .   ? -8.625  0.690   -6.542  1.00 27.30 ? 356 HOH A O   1 
HETATM 2285 O  O   . HOH G 6 .   ? -14.036 14.191  27.292  1.00 23.80 ? 357 HOH A O   1 
HETATM 2286 O  O   . HOH G 6 .   ? -22.176 -18.414 13.580  1.00 23.82 ? 358 HOH A O   1 
HETATM 2287 O  O   . HOH G 6 .   ? -11.112 15.338  32.263  1.00 19.14 ? 359 HOH A O   1 
HETATM 2288 O  O   . HOH G 6 .   ? -26.936 -4.029  25.108  1.00 22.19 ? 360 HOH A O   1 
HETATM 2289 O  O   . HOH G 6 .   ? -3.551  -12.982 -2.768  1.00 25.53 ? 361 HOH A O   1 
HETATM 2290 O  O   . HOH G 6 .   ? -29.167 -5.877  24.459  1.00 26.82 ? 362 HOH A O   1 
HETATM 2291 O  O   . HOH G 6 .   ? -2.989  -0.097  10.584  1.00 24.61 ? 363 HOH A O   1 
HETATM 2292 O  O   . HOH G 6 .   ? -16.936 -14.043 26.399  1.00 21.78 ? 364 HOH A O   1 
HETATM 2293 O  O   . HOH G 6 .   ? -18.515 -3.784  -2.612  1.00 27.48 ? 365 HOH A O   1 
HETATM 2294 O  O   . HOH G 6 .   ? -9.272  5.173   32.970  1.00 26.62 ? 366 HOH A O   1 
HETATM 2295 O  O   . HOH G 6 .   ? 5.043   -7.325  22.390  1.00 26.68 ? 367 HOH A O   1 
HETATM 2296 O  O   . HOH G 6 .   ? -4.430  4.178   10.042  1.00 29.23 ? 368 HOH A O   1 
HETATM 2297 O  O   . HOH G 6 .   ? -8.571  -14.718 40.651  1.00 19.64 ? 369 HOH A O   1 
HETATM 2298 O  O   . HOH G 6 .   ? -26.558 -11.650 2.109   1.00 26.85 ? 370 HOH A O   1 
HETATM 2299 O  O   . HOH G 6 .   ? 1.760   12.435  22.698  1.00 27.81 ? 371 HOH A O   1 
HETATM 2300 O  O   . HOH G 6 .   ? -18.569 -12.380 -3.588  1.00 23.34 ? 372 HOH A O   1 
HETATM 2301 O  O   . HOH G 6 .   ? -8.583  -19.869 26.703  1.00 23.15 ? 373 HOH A O   1 
HETATM 2302 O  O   . HOH G 6 .   ? -6.317  -19.760 23.900  1.00 24.91 ? 374 HOH A O   1 
HETATM 2303 O  O   . HOH G 6 .   ? -17.473 11.095  -1.994  1.00 24.99 ? 375 HOH A O   1 
HETATM 2304 O  O   . HOH G 6 .   ? -16.952 -17.891 20.107  1.00 25.23 ? 376 HOH A O   1 
HETATM 2305 O  O   . HOH G 6 .   ? -4.330  -4.706  11.214  1.00 25.68 ? 377 HOH A O   1 
HETATM 2306 O  O   . HOH G 6 .   ? -25.467 9.556   13.209  1.00 28.51 ? 378 HOH A O   1 
HETATM 2307 O  O   . HOH G 6 .   ? 3.732   9.848   23.889  1.00 27.78 ? 379 HOH A O   1 
HETATM 2308 O  O   . HOH G 6 .   ? -4.822  -7.373  37.854  1.00 27.51 ? 380 HOH A O   1 
HETATM 2309 O  O   . HOH G 6 .   ? -19.283 14.288  35.217  1.00 26.28 ? 381 HOH A O   1 
HETATM 2310 O  O   . HOH G 6 .   ? -2.137  -12.037 31.629  1.00 29.55 ? 382 HOH A O   1 
HETATM 2311 O  O   . HOH G 6 .   ? -11.004 -15.180 33.957  1.00 26.29 ? 383 HOH A O   1 
HETATM 2312 O  O   . HOH G 6 .   ? -7.221  -16.788 1.537   1.00 22.72 ? 384 HOH A O   1 
HETATM 2313 O  O   . HOH G 6 .   ? -23.400 -11.179 17.206  1.00 26.76 ? 385 HOH A O   1 
HETATM 2314 O  O   . HOH G 6 .   ? -17.766 -22.126 6.055   1.00 17.43 ? 386 HOH A O   1 
HETATM 2315 O  O   . HOH G 6 .   ? -20.984 0.964   -6.580  1.00 23.93 ? 387 HOH A O   1 
HETATM 2316 O  O   . HOH G 6 .   ? -17.937 6.307   38.669  1.00 30.16 ? 388 HOH A O   1 
HETATM 2317 O  O   . HOH G 6 .   ? -26.838 -1.289  26.064  1.00 23.33 ? 389 HOH A O   1 
HETATM 2318 O  O   . HOH G 6 .   ? -4.009  0.063   13.461  1.00 22.47 ? 390 HOH A O   1 
HETATM 2319 O  O   . HOH G 6 .   ? -12.376 12.478  29.239  1.00 24.67 ? 391 HOH A O   1 
HETATM 2320 O  O   . HOH G 6 .   ? -12.828 3.610   -6.865  1.00 25.37 ? 392 HOH A O   1 
HETATM 2321 O  O   . HOH G 6 .   ? -3.333  -23.146 21.394  1.00 24.37 ? 393 HOH A O   1 
HETATM 2322 O  O   . HOH G 6 .   ? -5.384  3.632   -5.657  1.00 26.12 ? 394 HOH A O   1 
HETATM 2323 O  O   . HOH G 6 .   ? 1.966   -15.657 9.244   1.00 21.30 ? 395 HOH A O   1 
HETATM 2324 O  O   . HOH G 6 .   ? -8.446  -17.516 34.747  1.00 24.85 ? 396 HOH A O   1 
HETATM 2325 O  O   . HOH G 6 .   ? -8.144  -26.365 10.525  1.00 29.81 ? 397 HOH A O   1 
HETATM 2326 O  O   . HOH G 6 .   ? -23.250 -13.604 11.232  1.00 26.90 ? 398 HOH A O   1 
HETATM 2327 O  O   . HOH G 6 .   ? 2.012   -14.230 20.574  1.00 28.53 ? 399 HOH A O   1 
HETATM 2328 O  O   . HOH G 6 .   ? -1.525  11.387  25.871  1.00 28.12 ? 400 HOH A O   1 
HETATM 2329 O  O   . HOH G 6 .   ? -15.343 -10.363 37.437  1.00 29.33 ? 401 HOH A O   1 
HETATM 2330 O  O   . HOH G 6 .   ? -23.359 -0.640  34.362  1.00 28.38 ? 402 HOH A O   1 
HETATM 2331 O  O   . HOH G 6 .   ? -24.895 4.587   8.431   1.00 32.65 ? 403 HOH A O   1 
HETATM 2332 O  O   . HOH G 6 .   ? -16.665 -15.093 32.918  1.00 32.24 ? 404 HOH A O   1 
HETATM 2333 O  O   . HOH G 6 .   ? -2.124  -4.600  -6.978  1.00 27.97 ? 405 HOH A O   1 
HETATM 2334 O  O   . HOH G 6 .   ? -5.057  2.127   37.386  1.00 29.44 ? 406 HOH A O   1 
HETATM 2335 O  O   . HOH G 6 .   ? -31.717 5.179   12.662  1.00 34.70 ? 407 HOH A O   1 
HETATM 2336 O  O   . HOH G 6 .   ? -25.939 6.174   27.026  1.00 25.82 ? 408 HOH A O   1 
HETATM 2337 O  O   . HOH G 6 .   ? -0.464  -19.837 6.652   1.00 29.95 ? 409 HOH A O   1 
HETATM 2338 O  O   . HOH G 6 .   ? -4.899  7.563   5.698   1.00 26.86 ? 410 HOH A O   1 
HETATM 2339 O  O   . HOH G 6 .   ? -1.223  9.200   28.137  1.00 25.11 ? 411 HOH A O   1 
HETATM 2340 O  O   . HOH G 6 .   ? 12.166  -9.907  -5.813  1.00 27.61 ? 412 HOH A O   1 
HETATM 2341 O  O   . HOH G 6 .   ? -7.164  -15.746 38.757  1.00 23.72 ? 413 HOH A O   1 
HETATM 2342 O  O   . HOH G 6 .   ? -16.527 5.279   -7.944  1.00 26.76 ? 414 HOH A O   1 
HETATM 2343 O  O   . HOH G 6 .   ? -17.901 -12.090 31.785  1.00 29.19 ? 415 HOH A O   1 
HETATM 2344 O  O   . HOH G 6 .   ? 4.222   -11.687 23.347  1.00 35.88 ? 416 HOH A O   1 
HETATM 2345 O  O   . HOH G 6 .   ? -25.805 -5.443  13.364  1.00 31.15 ? 417 HOH A O   1 
HETATM 2346 O  O   . HOH G 6 .   ? -10.682 -19.052 34.292  1.00 24.20 ? 418 HOH A O   1 
HETATM 2347 O  O   . HOH G 6 .   ? -31.795 6.640   15.323  1.00 32.77 ? 419 HOH A O   1 
HETATM 2348 O  O   . HOH G 6 .   ? -23.254 -17.166 3.484   1.00 29.78 ? 420 HOH A O   1 
HETATM 2349 O  O   . HOH G 6 .   ? -2.996  -19.274 1.943   1.00 36.55 ? 421 HOH A O   1 
HETATM 2350 O  O   . HOH G 6 .   ? 2.839   -14.480 0.979   1.00 26.84 ? 422 HOH A O   1 
HETATM 2351 O  O   . HOH G 6 .   ? -8.226  7.591   8.428   1.00 26.42 ? 423 HOH A O   1 
HETATM 2352 O  O   . HOH G 6 .   ? -10.661 8.525   7.724   1.00 23.39 ? 424 HOH A O   1 
HETATM 2353 O  O   . HOH G 6 .   ? -11.154 -23.660 12.262  1.00 22.21 ? 425 HOH A O   1 
HETATM 2354 O  O   . HOH G 6 .   ? -19.296 -20.828 5.127   1.00 25.76 ? 426 HOH A O   1 
HETATM 2355 O  O   . HOH G 6 .   ? -33.930 3.120   27.830  1.00 30.28 ? 427 HOH A O   1 
HETATM 2356 O  O   . HOH G 6 .   ? -6.075  -25.865 11.867  1.00 31.06 ? 428 HOH A O   1 
HETATM 2357 O  O   . HOH G 6 .   ? -3.279  -20.075 27.003  1.00 36.96 ? 429 HOH A O   1 
HETATM 2358 O  O   . HOH G 6 .   ? -29.240 11.640  3.184   1.00 28.80 ? 430 HOH A O   1 
HETATM 2359 O  O   . HOH G 6 .   ? -25.393 11.019  19.614  1.00 32.99 ? 431 HOH A O   1 
HETATM 2360 O  O   . HOH G 6 .   ? -32.777 2.121   12.030  1.00 30.11 ? 432 HOH A O   1 
HETATM 2361 O  O   . HOH G 6 .   ? 0.961   3.200   1.864   1.00 29.55 ? 433 HOH A O   1 
HETATM 2362 O  O   . HOH G 6 .   ? -28.040 2.177   23.246  1.00 33.80 ? 434 HOH A O   1 
HETATM 2363 O  O   . HOH G 6 .   ? -4.920  -12.659 40.739  1.00 23.45 ? 435 HOH A O   1 
HETATM 2364 O  O   . HOH G 6 .   ? -4.617  -15.957 0.922   1.00 27.59 ? 436 HOH A O   1 
HETATM 2365 O  O   . HOH G 6 .   ? 5.503   9.055   22.058  1.00 29.83 ? 437 HOH A O   1 
HETATM 2366 O  O   . HOH G 6 .   ? -18.737 -21.109 14.751  1.00 25.62 ? 438 HOH A O   1 
HETATM 2367 O  O   . HOH G 6 .   ? 12.052  -11.223 -3.240  1.00 22.16 ? 439 HOH A O   1 
HETATM 2368 O  O   . HOH G 6 .   ? -24.205 -3.296  29.481  1.00 30.11 ? 440 HOH A O   1 
HETATM 2369 O  O   . HOH G 6 .   ? -0.517  13.977  15.980  1.00 26.64 ? 441 HOH A O   1 
HETATM 2370 O  O   . HOH G 6 .   ? -17.721 -19.531 35.093  1.00 26.00 ? 442 HOH A O   1 
HETATM 2371 O  O   . HOH G 6 .   ? -9.668  -25.456 7.953   1.00 28.22 ? 443 HOH A O   1 
HETATM 2372 O  O   . HOH G 6 .   ? -4.867  -20.751 21.386  1.00 27.04 ? 444 HOH A O   1 
HETATM 2373 O  O   . HOH G 6 .   ? -6.001  -20.891 26.393  1.00 30.04 ? 445 HOH A O   1 
HETATM 2374 O  O   . HOH G 6 .   ? -0.243  1.055   -11.034 1.00 25.97 ? 446 HOH A O   1 
HETATM 2375 O  O   . HOH G 6 .   ? 1.998   8.044   27.969  1.00 28.07 ? 447 HOH A O   1 
HETATM 2376 O  O   . HOH G 6 .   ? -28.099 5.622   19.167  1.00 29.23 ? 448 HOH A O   1 
HETATM 2377 O  O   . HOH G 6 .   ? 1.524   -17.552 7.121   1.00 29.80 ? 449 HOH A O   1 
HETATM 2378 O  O   . HOH G 6 .   ? -2.838  7.172   -8.123  1.00 29.63 ? 450 HOH A O   1 
HETATM 2379 O  O   . HOH G 6 .   ? -1.627  -17.393 4.989   1.00 36.81 ? 451 HOH A O   1 
HETATM 2380 O  O   . HOH G 6 .   ? -12.931 -22.264 8.557   1.00 25.39 ? 452 HOH A O   1 
HETATM 2381 O  O   . HOH G 6 .   ? -10.083 1.526   39.136  1.00 29.49 ? 453 HOH A O   1 
HETATM 2382 O  O   . HOH G 6 .   ? -0.775  6.563   32.262  1.00 29.81 ? 454 HOH A O   1 
HETATM 2383 O  O   . HOH G 6 .   ? -18.655 -9.066  34.549  1.00 29.29 ? 455 HOH A O   1 
HETATM 2384 O  O   . HOH G 6 .   ? -26.362 -7.628  30.532  1.00 32.91 ? 456 HOH A O   1 
HETATM 2385 O  O   . HOH G 6 .   ? -27.327 -5.425  27.427  1.00 33.25 ? 457 HOH A O   1 
HETATM 2386 O  O   . HOH G 6 .   ? -28.000 -1.659  28.483  1.00 32.67 ? 458 HOH A O   1 
HETATM 2387 O  O   . HOH G 6 .   ? -19.895 -4.188  41.523  1.00 30.67 ? 459 HOH A O   1 
HETATM 2388 O  O   . HOH G 6 .   ? -5.449  1.972   11.711  1.00 24.58 ? 460 HOH A O   1 
HETATM 2389 O  O   . HOH G 6 .   ? -6.533  6.483   10.675  1.00 32.35 ? 461 HOH A O   1 
HETATM 2390 O  O   . HOH G 6 .   ? -2.830  4.512   7.721   1.00 37.59 ? 462 HOH A O   1 
HETATM 2391 O  O   . HOH G 6 .   ? 2.663   -14.420 -5.794  1.00 36.69 ? 463 HOH A O   1 
HETATM 2392 O  O   . HOH G 6 .   ? 6.630   -5.800  6.685   1.00 32.53 ? 464 HOH A O   1 
HETATM 2393 O  O   . HOH G 6 .   ? -25.707 -3.169  31.982  1.00 37.28 ? 465 HOH A O   1 
HETATM 2394 O  O   . HOH G 6 .   ? -20.928 -6.919  -2.054  1.00 29.96 ? 466 HOH A O   1 
HETATM 2395 O  O   . HOH G 6 .   ? 5.697   -12.387 11.819  1.00 37.56 ? 467 HOH A O   1 
HETATM 2396 O  O   . HOH G 6 .   ? -21.889 -14.240 18.634  1.00 32.05 ? 468 HOH A O   1 
HETATM 2397 O  O   . HOH G 6 .   ? -25.954 -9.887  15.009  1.00 32.85 ? 469 HOH A O   1 
HETATM 2398 O  O   . HOH G 6 .   ? -0.080  -15.311 27.086  1.00 32.42 ? 470 HOH A O   1 
HETATM 2399 O  O   . HOH G 6 .   ? -2.547  -19.138 21.588  1.00 28.95 ? 471 HOH A O   1 
HETATM 2400 O  O   . HOH G 6 .   ? -10.999 1.098   33.695  1.00 28.71 ? 472 HOH A O   1 
HETATM 2401 O  O   . HOH G 6 .   ? 3.490   -13.735 12.454  1.00 32.91 ? 473 HOH A O   1 
HETATM 2402 O  O   . HOH G 6 .   ? -13.471 -0.681  -6.191  1.00 29.99 ? 474 HOH A O   1 
HETATM 2403 O  O   . HOH G 6 .   ? -10.539 20.791  24.943  1.00 23.88 ? 475 HOH A O   1 
HETATM 2404 O  O   . HOH G 6 .   ? -20.329 13.881  29.067  1.00 34.42 ? 476 HOH A O   1 
HETATM 2405 O  O   . HOH G 6 .   ? -1.527  4.326   2.147   1.00 41.43 ? 477 HOH A O   1 
HETATM 2406 O  O   . HOH G 6 .   ? -26.342 2.409   39.438  1.00 45.09 ? 478 HOH A O   1 
HETATM 2407 O  O   . HOH G 6 .   ? -24.081 -7.152  0.272   1.00 29.90 ? 479 HOH A O   1 
HETATM 2408 O  O   . HOH G 6 .   ? -8.533  -14.985 33.424  1.00 32.77 ? 480 HOH A O   1 
HETATM 2409 O  O   . HOH G 6 .   ? -15.925 3.560   35.331  1.00 35.11 ? 481 HOH A O   1 
HETATM 2410 O  O   . HOH G 6 .   ? 1.034   14.661  24.307  1.00 33.44 ? 482 HOH A O   1 
HETATM 2411 O  O   . HOH G 6 .   ? -25.183 8.640   26.130  1.00 32.59 ? 483 HOH A O   1 
HETATM 2412 O  O   . HOH G 6 .   ? 11.939  -6.480  7.919   1.00 33.87 ? 484 HOH A O   1 
HETATM 2413 O  O   . HOH G 6 .   ? -15.278 -20.172 23.230  1.00 29.44 ? 485 HOH A O   1 
HETATM 2414 O  O   . HOH G 6 .   ? -23.950 -3.477  4.255   1.00 33.44 ? 486 HOH A O   1 
HETATM 2415 O  O   . HOH G 6 .   ? 6.497   -5.591  27.364  1.00 34.34 ? 487 HOH A O   1 
HETATM 2416 O  O   . HOH G 6 .   ? -24.752 11.867  6.212   1.00 28.33 ? 488 HOH A O   1 
HETATM 2417 O  O   . HOH G 6 .   ? -24.090 -0.203  1.146   1.00 32.35 ? 489 HOH A O   1 
HETATM 2418 O  O   . HOH G 6 .   ? -2.624  -14.885 32.894  1.00 27.37 ? 490 HOH A O   1 
HETATM 2419 O  O   . HOH G 6 .   ? -21.067 -0.373  -1.989  1.00 35.66 ? 491 HOH A O   1 
HETATM 2420 O  O   . HOH G 6 .   ? 5.964   -2.734  6.846   1.00 34.84 ? 492 HOH A O   1 
HETATM 2421 O  O   . HOH G 6 .   ? -14.241 3.593   33.298  1.00 26.15 ? 493 HOH A O   1 
HETATM 2422 O  O   . HOH G 6 .   ? -25.654 4.426   4.193   1.00 35.01 ? 494 HOH A O   1 
HETATM 2423 O  O   . HOH G 6 .   ? -21.230 0.575   0.344   1.00 33.79 ? 495 HOH A O   1 
HETATM 2424 O  O   . HOH G 6 .   ? -11.705 0.952   -7.772  1.00 32.82 ? 496 HOH A O   1 
HETATM 2425 O  O   . HOH G 6 .   ? -20.625 8.387   30.330  1.00 29.20 ? 497 HOH A O   1 
HETATM 2426 O  O   . HOH G 6 .   ? -0.343  13.985  27.203  1.00 35.23 ? 498 HOH A O   1 
HETATM 2427 O  O   . HOH G 6 .   ? -31.839 -8.517  8.270   1.00 33.35 ? 499 HOH A O   1 
HETATM 2428 O  O   . HOH G 6 .   ? -14.852 6.104   32.891  1.00 32.33 ? 500 HOH A O   1 
HETATM 2429 O  O   . HOH G 6 .   ? 5.860   -13.972 8.692   1.00 31.20 ? 501 HOH A O   1 
HETATM 2430 O  O   . HOH G 6 .   ? 0.104   3.503   10.194  1.00 34.97 ? 502 HOH A O   1 
HETATM 2431 O  O   . HOH G 6 .   ? 6.430   8.573   18.325  1.00 32.32 ? 503 HOH A O   1 
HETATM 2432 O  O   . HOH G 6 .   ? -19.429 -23.895 5.892   1.00 26.49 ? 504 HOH A O   1 
HETATM 2433 O  O   . HOH G 6 .   ? 15.084  -6.584  7.942   1.00 36.41 ? 505 HOH A O   1 
HETATM 2434 O  O   . HOH G 6 .   ? -2.538  -9.429  34.670  1.00 33.93 ? 506 HOH A O   1 
HETATM 2435 O  O   . HOH G 6 .   ? -0.389  -6.884  -7.480  1.00 35.08 ? 507 HOH A O   1 
HETATM 2436 O  O   . HOH G 6 .   ? -7.278  -10.200 -4.213  1.00 35.25 ? 508 HOH A O   1 
HETATM 2437 O  O   . HOH G 6 .   ? -7.478  -8.813  -2.368  1.00 31.54 ? 509 HOH A O   1 
HETATM 2438 O  O   . HOH G 6 .   ? -9.385  -10.091 -1.270  1.00 27.26 ? 510 HOH A O   1 
HETATM 2439 O  O   . HOH G 6 .   ? -5.193  -13.467 34.407  1.00 33.66 ? 511 HOH A O   1 
HETATM 2440 O  O   . HOH G 6 .   ? -5.027  0.494   9.951   1.00 25.02 ? 512 HOH A O   1 
HETATM 2441 O  O   . HOH G 6 .   ? 7.554   -7.870  -0.853  1.00 31.54 ? 513 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   ? 0.4072 0.4122 0.4190 -0.0204 0.0271  0.0370  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.3804 0.3403 0.3993 -0.0311 0.0331  0.0281  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.3165 0.2774 0.3446 -0.0294 0.0496  0.0040  4   HIS A C   
4    O  O   . HIS A 4   ? 0.3176 0.2872 0.3507 -0.0377 0.0653  0.0329  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.4345 0.3938 0.4429 -0.0234 0.0115  0.0283  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.4470 0.4569 0.4530 -0.0010 0.0065  0.0207  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.4713 0.5067 0.4530 0.0020  -0.0414 0.0282  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.5220 0.5332 0.5198 0.0245  -0.0104 -0.0086 4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.5320 0.5699 0.5225 0.0178  -0.0326 -0.0043 4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.4875 0.5566 0.4656 -0.0307 -0.0384 -0.0020 4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.2531 0.1993 0.3057 -0.0496 0.0414  0.0048  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.2191 0.1380 0.2414 -0.0333 0.0296  -0.0060 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1966 0.1376 0.2436 -0.0055 0.0249  -0.0108 5   TRP A C   
14   O  O   . TRP A 5   ? 0.2087 0.1474 0.2442 -0.0207 0.0207  -0.0071 5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1758 0.1555 0.2515 -0.0271 0.0441  -0.0126 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.2029 0.1658 0.2268 -0.0197 0.0406  -0.0060 5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2565 0.1547 0.2122 -0.0251 0.0303  0.0159  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1633 0.1298 0.2325 0.0082  0.0118  0.0333  5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2485 0.1545 0.2231 -0.0469 0.0458  0.0295  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1724 0.1546 0.2011 -0.0153 -0.0136 0.0207  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1941 0.1546 0.1803 -0.0302 0.0333  -0.0071 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.2217 0.2106 0.2257 -0.0146 0.0263  0.0102  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.2070 0.1722 0.1883 -0.0286 0.0359  -0.0125 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.2029 0.2022 0.1976 -0.0218 -0.0152 -0.0251 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.2016 0.1255 0.2302 -0.0007 0.0346  -0.0300 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1860 0.1138 0.2381 -0.0309 0.0113  -0.0315 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1722 0.1398 0.2536 -0.0107 0.0588  -0.0261 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1970 0.1616 0.2198 -0.0171 0.0553  -0.0015 6   GLY A O   
29   N  N   . TYR A 7   ? 0.2253 0.1298 0.2738 -0.0155 0.0489  -0.0326 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.2113 0.1384 0.3015 -0.0087 0.0772  -0.0216 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.2579 0.1520 0.3890 -0.0102 0.0762  -0.0250 7   TYR A C   
32   O  O   . TYR A 7   ? 0.2796 0.1774 0.5052 0.0054  0.0987  0.0102  7   TYR A O   
33   C  CB  . TYR A 7   ? 0.2170 0.1107 0.2799 -0.0182 0.0524  -0.0247 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1937 0.1079 0.2073 -0.0175 0.0163  -0.0104 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1547 0.1174 0.2492 -0.0542 0.0156  -0.0494 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.2088 0.1025 0.1907 -0.0198 0.0187  -0.0449 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1840 0.0682 0.1606 -0.0080 -0.0170 -0.0003 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1921 0.1359 0.1411 -0.0507 0.0425  -0.0337 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1598 0.1052 0.1587 -0.0364 0.0093  -0.0212 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1812 0.0989 0.1688 -0.0073 0.0263  -0.0132 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.2446 0.1590 0.4013 -0.0003 0.0882  -0.0428 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.2612 0.1459 0.4124 0.0133  0.1040  -0.0405 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.3198 0.2102 0.4135 0.0023  0.0768  -0.0226 8   GLY A C   
44   O  O   . GLY A 8   ? 0.3220 0.3008 0.4347 0.0212  0.1118  -0.0100 8   GLY A O   
45   N  N   . LYS A 9   ? 0.3635 0.3012 0.4855 0.0163  0.0559  -0.0049 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.3890 0.3309 0.4709 0.0124  0.0331  -0.0143 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.3338 0.3352 0.4398 0.0146  0.0527  0.0063  9   LYS A C   
48   O  O   . LYS A 9   ? 0.3421 0.3424 0.4792 -0.0052 0.0370  -0.0119 9   LYS A O   
49   C  CB  . LYS A 9   ? 0.3801 0.3619 0.4871 0.0401  0.0285  0.0104  9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.4185 0.3689 0.4966 0.0248  0.0219  0.0019  9   LYS A CG  
51   C  CD  . LYS A 9   ? 0.4228 0.3955 0.5173 0.0414  0.0212  -0.0126 9   LYS A CD  
52   C  CE  . LYS A 9   ? 0.4404 0.4549 0.5572 0.0315  0.0125  0.0000  9   LYS A CE  
53   N  NZ  . LYS A 9   ? 0.4692 0.4318 0.5896 0.0357  0.0333  -0.0052 9   LYS A NZ  
54   N  N   . HIS A 10  ? 0.2792 0.1966 0.4142 0.0430  0.0701  0.0083  10  HIS A N   
55   C  CA  . HIS A 10  ? 0.2342 0.2320 0.3608 0.0318  0.0627  -0.0355 10  HIS A CA  
56   C  C   . HIS A 10  ? 0.2379 0.2176 0.3474 0.0344  0.0573  -0.0081 10  HIS A C   
57   O  O   . HIS A 10  ? 0.2167 0.2700 0.3722 0.0372  0.0688  -0.0397 10  HIS A O   
58   C  CB  . HIS A 10  ? 0.2038 0.2239 0.3553 0.0242  0.0825  -0.0399 10  HIS A CB  
59   C  CG  . HIS A 10  ? 0.3271 0.2760 0.3625 0.0031  0.0493  -0.0617 10  HIS A CG  
60   N  ND1 . HIS A 10  ? 0.3819 0.2246 0.4128 0.0252  0.0597  -0.0080 10  HIS A ND1 
61   C  CD2 . HIS A 10  ? 0.3355 0.3133 0.3908 0.0267  0.0244  -0.0326 10  HIS A CD2 
62   C  CE1 . HIS A 10  ? 0.2551 0.2069 0.3481 0.0414  0.0542  -0.0220 10  HIS A CE1 
63   N  NE2 . HIS A 10  ? 0.3603 0.2806 0.4038 0.0253  0.0483  -0.0377 10  HIS A NE2 
64   N  N   . ASN A 11  ? 0.1948 0.1725 0.3075 0.0344  0.0706  0.0031  11  ASN A N   
65   C  CA  . ASN A 11  ? 0.2112 0.1697 0.2598 0.0337  0.0697  -0.0143 11  ASN A CA  
66   C  C   . ASN A 11  ? 0.1641 0.1573 0.2595 0.0057  0.0601  0.0091  11  ASN A C   
67   O  O   . ASN A 11  ? 0.2088 0.1775 0.2703 0.0245  0.0639  0.0248  11  ASN A O   
68   C  CB  . ASN A 11  ? 0.2332 0.1581 0.2454 0.0104  0.0553  0.0000  11  ASN A CB  
69   C  CG  . ASN A 11  ? 0.2699 0.1342 0.2644 0.0353  0.0604  -0.0493 11  ASN A CG  
70   O  OD1 . ASN A 11  ? 0.2483 0.2016 0.3205 -0.0199 0.0595  -0.0309 11  ASN A OD1 
71   N  ND2 . ASN A 11  ? 0.2689 0.2109 0.2556 -0.0276 0.0269  -0.0381 11  ASN A ND2 
72   N  N   . GLY A 12  ? 0.1962 0.1742 0.2110 0.0027  0.0615  0.0055  12  GLY A N   
73   C  CA  . GLY A 12  ? 0.1684 0.2138 0.2199 -0.0035 0.0295  -0.0175 12  GLY A CA  
74   C  C   . GLY A 12  ? 0.1541 0.1675 0.2189 0.0005  0.0403  0.0023  12  GLY A C   
75   O  O   . GLY A 12  ? 0.1347 0.1433 0.2631 0.0167  0.0102  0.0204  12  GLY A O   
76   N  N   . PRO A 13  ? 0.1420 0.1181 0.1774 0.0040  0.0430  -0.0003 13  PRO A N   
77   C  CA  . PRO A 13  ? 0.1562 0.0930 0.2187 0.0122  0.0372  -0.0103 13  PRO A CA  
78   C  C   . PRO A 13  ? 0.1736 0.0808 0.1984 0.0115  0.0351  0.0063  13  PRO A C   
79   O  O   . PRO A 13  ? 0.1817 0.0955 0.2281 0.0032  0.0055  -0.0129 13  PRO A O   
80   C  CB  . PRO A 13  ? 0.1676 0.1407 0.2073 -0.0326 0.0458  -0.0040 13  PRO A CB  
81   C  CG  . PRO A 13  ? 0.1658 0.1397 0.1915 -0.0154 0.0296  -0.0156 13  PRO A CG  
82   C  CD  . PRO A 13  ? 0.1588 0.1715 0.2083 0.0060  0.0195  -0.0237 13  PRO A CD  
83   N  N   A GLU A 14  ? 0.1731 0.0869 0.2052 0.0168  0.0076  0.0133  14  GLU A N   
84   N  N   B GLU A 14  ? 0.1714 0.0851 0.2295 0.0083  0.0208  0.0209  14  GLU A N   
85   C  CA  A GLU A 14  ? 0.1904 0.0894 0.1993 0.0253  -0.0065 0.0107  14  GLU A CA  
86   C  CA  B GLU A 14  ? 0.1977 0.1004 0.2467 0.0238  0.0043  0.0272  14  GLU A CA  
87   C  C   A GLU A 14  ? 0.1624 0.0961 0.2205 0.0379  0.0054  -0.0076 14  GLU A C   
88   C  C   B GLU A 14  ? 0.1790 0.1199 0.2531 0.0296  0.0114  0.0100  14  GLU A C   
89   O  O   A GLU A 14  ? 0.1840 0.0775 0.2292 0.0447  -0.0098 -0.0086 14  GLU A O   
90   O  O   B GLU A 14  ? 0.1986 0.1097 0.2829 0.0285  0.0136  0.0214  14  GLU A O   
91   C  CB  A GLU A 14  ? 0.2105 0.1145 0.2140 0.0372  -0.0291 0.0038  14  GLU A CB  
92   C  CB  B GLU A 14  ? 0.2354 0.1262 0.2809 0.0209  -0.0032 0.0395  14  GLU A CB  
93   C  CG  A GLU A 14  ? 0.1997 0.1536 0.2004 0.0017  -0.0241 0.0181  14  GLU A CG  
94   C  CG  B GLU A 14  ? 0.2062 0.1746 0.2664 -0.0208 0.0146  0.0551  14  GLU A CG  
95   C  CD  A GLU A 14  ? 0.2619 0.1363 0.2472 0.0241  -0.0220 -0.0059 14  GLU A CD  
96   C  CD  B GLU A 14  ? 0.2989 0.2975 0.3145 -0.0035 0.0046  -0.0020 14  GLU A CD  
97   O  OE1 A GLU A 14  ? 0.2025 0.1203 0.2513 0.0546  -0.0586 -0.1008 14  GLU A OE1 
98   O  OE1 B GLU A 14  ? 0.3291 0.3729 0.3337 -0.0012 -0.0222 -0.0092 14  GLU A OE1 
99   O  OE2 A GLU A 14  ? 0.3612 0.0894 0.2033 0.0450  0.0245  -0.0432 14  GLU A OE2 
100  O  OE2 B GLU A 14  ? 0.2843 0.3378 0.2741 0.0175  -0.0082 -0.0057 14  GLU A OE2 
101  N  N   . HIS A 15  ? 0.1693 0.1196 0.2295 0.0256  0.0120  0.0038  15  HIS A N   
102  C  CA  . HIS A 15  ? 0.1684 0.1149 0.2508 0.0282  -0.0076 0.0020  15  HIS A CA  
103  C  C   . HIS A 15  ? 0.1630 0.1289 0.2346 0.0199  -0.0063 -0.0032 15  HIS A C   
104  O  O   . HIS A 15  ? 0.1185 0.1183 0.2727 0.0049  0.0104  -0.0010 15  HIS A O   
105  C  CB  . HIS A 15  ? 0.1474 0.1473 0.2781 0.0366  -0.0019 -0.0041 15  HIS A CB  
106  C  CG  . HIS A 15  ? 0.1951 0.1815 0.2577 0.0210  0.0027  -0.0046 15  HIS A CG  
107  N  ND1 . HIS A 15  ? 0.1994 0.2098 0.3280 0.0754  -0.0221 -0.0403 15  HIS A ND1 
108  C  CD2 . HIS A 15  ? 0.1747 0.1699 0.3095 0.0709  0.0308  -0.0153 15  HIS A CD2 
109  C  CE1 . HIS A 15  ? 0.2695 0.2951 0.3461 0.0904  -0.0317 -0.0399 15  HIS A CE1 
110  N  NE2 . HIS A 15  ? 0.2526 0.1753 0.3786 0.0773  0.0531  -0.0584 15  HIS A NE2 
111  N  N   . TRP A 16  ? 0.1036 0.1041 0.2322 0.0219  0.0020  0.0137  16  TRP A N   
112  C  CA  . TRP A 16  ? 0.1304 0.1064 0.2257 0.0199  -0.0091 -0.0175 16  TRP A CA  
113  C  C   . TRP A 16  ? 0.1225 0.1460 0.1986 0.0207  -0.0020 0.0006  16  TRP A C   
114  O  O   . TRP A 16  ? 0.1332 0.0960 0.2520 0.0031  -0.0148 0.0038  16  TRP A O   
115  C  CB  . TRP A 16  ? 0.0996 0.1489 0.1958 0.0034  -0.0108 -0.0142 16  TRP A CB  
116  C  CG  . TRP A 16  ? 0.1392 0.0728 0.2004 0.0024  0.0080  0.0003  16  TRP A CG  
117  C  CD1 . TRP A 16  ? 0.1293 0.1163 0.1975 0.0026  0.0092  -0.0068 16  TRP A CD1 
118  C  CD2 . TRP A 16  ? 0.1192 0.0864 0.2077 0.0020  0.0228  -0.0062 16  TRP A CD2 
119  N  NE1 . TRP A 16  ? 0.1418 0.1072 0.2027 -0.0116 0.0013  -0.0140 16  TRP A NE1 
120  C  CE2 . TRP A 16  ? 0.1097 0.1001 0.1891 -0.0108 -0.0092 0.0265  16  TRP A CE2 
121  C  CE3 . TRP A 16  ? 0.1423 0.0644 0.2047 0.0037  0.0054  0.0057  16  TRP A CE3 
122  C  CZ2 . TRP A 16  ? 0.1365 0.0603 0.2239 -0.0051 0.0051  -0.0073 16  TRP A CZ2 
123  C  CZ3 . TRP A 16  ? 0.1076 0.1215 0.1840 -0.0175 0.0049  -0.0086 16  TRP A CZ3 
124  C  CH2 . TRP A 16  ? 0.1254 0.0925 0.1728 0.0131  0.0147  -0.0021 16  TRP A CH2 
125  N  N   . HIS A 17  ? 0.1216 0.1317 0.1731 0.0107  0.0093  -0.0124 17  HIS A N   
126  C  CA  . HIS A 17  ? 0.1122 0.1400 0.1944 -0.0043 -0.0070 0.0068  17  HIS A CA  
127  C  C   . HIS A 17  ? 0.1508 0.1649 0.2367 0.0003  -0.0093 0.0335  17  HIS A C   
128  O  O   . HIS A 17  ? 0.1210 0.1699 0.2606 -0.0170 -0.0245 0.0066  17  HIS A O   
129  C  CB  . HIS A 17  ? 0.1415 0.1518 0.2120 0.0310  -0.0065 0.0174  17  HIS A CB  
130  C  CG  . HIS A 17  ? 0.1086 0.1550 0.2737 0.0037  -0.0186 0.0252  17  HIS A CG  
131  N  ND1 . HIS A 17  ? 0.1664 0.2377 0.2872 0.0110  -0.0350 0.0766  17  HIS A ND1 
132  C  CD2 . HIS A 17  ? 0.1767 0.1140 0.2537 0.0315  -0.0031 0.0427  17  HIS A CD2 
133  C  CE1 . HIS A 17  ? 0.1774 0.1849 0.3061 0.0375  -0.0255 0.0740  17  HIS A CE1 
134  N  NE2 . HIS A 17  ? 0.1912 0.1485 0.2861 0.0386  -0.0155 0.0636  17  HIS A NE2 
135  N  N   . LYS A 18  ? 0.1250 0.1431 0.2569 -0.0031 -0.0118 0.0498  18  LYS A N   
136  C  CA  . LYS A 18  ? 0.1509 0.1923 0.2705 -0.0068 -0.0068 0.0504  18  LYS A CA  
137  C  C   . LYS A 18  ? 0.1438 0.1851 0.2978 -0.0153 -0.0124 0.0331  18  LYS A C   
138  O  O   . LYS A 18  ? 0.1586 0.2368 0.3618 -0.0432 -0.0531 0.0736  18  LYS A O   
139  C  CB  . LYS A 18  ? 0.1442 0.1871 0.2917 0.0114  -0.0222 0.0710  18  LYS A CB  
140  C  CG  . LYS A 18  ? 0.1697 0.1984 0.2845 0.0465  -0.0104 0.0575  18  LYS A CG  
141  C  CD  . LYS A 18  ? 0.1423 0.2299 0.2845 0.0467  0.0074  0.0785  18  LYS A CD  
142  C  CE  . LYS A 18  ? 0.1757 0.1586 0.2644 0.0184  0.0142  0.0786  18  LYS A CE  
143  N  NZ  . LYS A 18  ? 0.1393 0.2119 0.2795 0.0537  0.0129  0.0571  18  LYS A NZ  
144  N  N   . ASP A 19  ? 0.1201 0.1640 0.2723 0.0043  -0.0178 0.0401  19  ASP A N   
145  C  CA  . ASP A 19  ? 0.1396 0.1307 0.2899 0.0023  0.0021  0.0293  19  ASP A CA  
146  C  C   . ASP A 19  ? 0.1318 0.1350 0.3091 -0.0114 -0.0130 0.0243  19  ASP A C   
147  O  O   . ASP A 19  ? 0.1785 0.1007 0.3668 -0.0271 0.0141  0.0456  19  ASP A O   
148  C  CB  . ASP A 19  ? 0.1647 0.2181 0.3080 -0.0063 -0.0362 0.0270  19  ASP A CB  
149  C  CG  . ASP A 19  ? 0.2906 0.1588 0.3582 0.0264  0.0419  -0.0068 19  ASP A CG  
150  O  OD1 . ASP A 19  ? 0.2910 0.2169 0.3675 0.0375  0.0024  0.0012  19  ASP A OD1 
151  O  OD2 . ASP A 19  ? 0.3485 0.3270 0.4544 0.0944  0.0044  -0.0008 19  ASP A OD2 
152  N  N   . PHE A 20  ? 0.1169 0.1149 0.2847 -0.0098 0.0051  0.0313  20  PHE A N   
153  C  CA  . PHE A 20  ? 0.1321 0.1322 0.2476 -0.0082 -0.0068 0.0126  20  PHE A CA  
154  C  C   . PHE A 20  ? 0.1070 0.1552 0.2309 -0.0205 -0.0065 0.0192  20  PHE A C   
155  O  O   . PHE A 20  ? 0.1326 0.1156 0.2281 -0.0178 -0.0003 0.0165  20  PHE A O   
156  C  CB  . PHE A 20  ? 0.1389 0.1395 0.2667 -0.0214 -0.0171 0.0274  20  PHE A CB  
157  C  CG  . PHE A 20  ? 0.1327 0.1251 0.2451 -0.0308 -0.0087 0.0233  20  PHE A CG  
158  C  CD1 . PHE A 20  ? 0.1397 0.1682 0.2965 -0.0236 -0.0234 0.0590  20  PHE A CD1 
159  C  CD2 . PHE A 20  ? 0.1545 0.1557 0.2619 -0.0324 -0.0103 -0.0086 20  PHE A CD2 
160  C  CE1 . PHE A 20  ? 0.1640 0.2061 0.2228 -0.0175 -0.0114 0.0405  20  PHE A CE1 
161  C  CE2 . PHE A 20  ? 0.1201 0.2378 0.2910 -0.0038 -0.0421 0.0326  20  PHE A CE2 
162  C  CZ  . PHE A 20  ? 0.1331 0.2406 0.2865 -0.0183 -0.0051 0.0467  20  PHE A CZ  
163  N  N   . PRO A 21  ? 0.1437 0.1588 0.2407 -0.0370 -0.0135 0.0020  21  PRO A N   
164  C  CA  . PRO A 21  ? 0.1171 0.1715 0.2245 -0.0452 -0.0266 0.0094  21  PRO A CA  
165  C  C   . PRO A 21  ? 0.1422 0.1342 0.2176 -0.0187 -0.0208 -0.0260 21  PRO A C   
166  O  O   . PRO A 21  ? 0.1445 0.1237 0.2515 -0.0182 -0.0344 -0.0052 21  PRO A O   
167  C  CB  . PRO A 21  ? 0.1451 0.2094 0.2547 -0.0672 -0.0557 0.0275  21  PRO A CB  
168  C  CG  . PRO A 21  ? 0.2417 0.2047 0.2899 -0.0984 -0.0509 0.0153  21  PRO A CG  
169  C  CD  . PRO A 21  ? 0.1309 0.1500 0.2698 -0.0423 -0.0256 0.0379  21  PRO A CD  
170  N  N   A ILE A 22  ? 0.1066 0.1181 0.2255 -0.0186 -0.0247 -0.0186 22  ILE A N   
171  N  N   B ILE A 22  ? 0.1129 0.1201 0.2212 -0.0220 -0.0271 -0.0226 22  ILE A N   
172  C  CA  A ILE A 22  ? 0.1282 0.0932 0.2076 -0.0124 -0.0164 -0.0174 22  ILE A CA  
173  C  CA  B ILE A 22  ? 0.1446 0.0910 0.1975 -0.0093 -0.0237 -0.0159 22  ILE A CA  
174  C  C   A ILE A 22  ? 0.1289 0.0969 0.1772 -0.0063 -0.0262 -0.0109 22  ILE A C   
175  C  C   B ILE A 22  ? 0.1335 0.1077 0.1632 -0.0070 -0.0295 -0.0097 22  ILE A C   
176  O  O   A ILE A 22  ? 0.1011 0.0584 0.2083 0.0130  -0.0299 -0.0109 22  ILE A O   
177  O  O   B ILE A 22  ? 0.1363 0.1465 0.1869 0.0057  -0.0143 0.0040  22  ILE A O   
178  C  CB  A ILE A 22  ? 0.1215 0.1165 0.1807 -0.0012 -0.0038 -0.0097 22  ILE A CB  
179  C  CB  B ILE A 22  ? 0.1395 0.1058 0.1733 0.0178  -0.0190 -0.0207 22  ILE A CB  
180  C  CG1 A ILE A 22  ? 0.1057 0.1738 0.2325 0.0296  0.0103  -0.0269 22  ILE A CG1 
181  C  CG1 B ILE A 22  ? 0.1582 0.0727 0.1772 -0.0177 -0.0109 -0.0153 22  ILE A CG1 
182  C  CG2 A ILE A 22  ? 0.1018 0.1562 0.1835 -0.0138 -0.0118 -0.0005 22  ILE A CG2 
183  C  CG2 B ILE A 22  ? 0.1492 0.1165 0.1601 -0.0340 -0.0175 -0.0008 22  ILE A CG2 
184  C  CD1 A ILE A 22  ? 0.2338 0.2417 0.2059 -0.0214 -0.0070 -0.0120 22  ILE A CD1 
185  C  CD1 B ILE A 22  ? 0.1351 0.0969 0.2027 0.0083  -0.0344 -0.0059 22  ILE A CD1 
186  N  N   . ALA A 23  ? 0.1459 0.1005 0.1925 -0.0052 -0.0263 -0.0177 23  ALA A N   
187  C  CA  . ALA A 23  ? 0.1548 0.0937 0.1918 0.0044  -0.0240 0.0023  23  ALA A CA  
188  C  C   . ALA A 23  ? 0.1360 0.1298 0.1948 0.0127  -0.0296 -0.0031 23  ALA A C   
189  O  O   . ALA A 23  ? 0.1529 0.0937 0.2094 -0.0099 -0.0329 -0.0024 23  ALA A O   
190  C  CB  . ALA A 23  ? 0.1435 0.1246 0.2166 0.0154  -0.0254 -0.0076 23  ALA A CB  
191  N  N   . LYS A 24  ? 0.1502 0.1564 0.1977 0.0125  -0.0267 -0.0060 24  LYS A N   
192  C  CA  . LYS A 24  ? 0.1106 0.1731 0.2205 -0.0063 -0.0353 0.0055  24  LYS A CA  
193  C  C   . LYS A 24  ? 0.1665 0.1842 0.2379 -0.0098 -0.0388 -0.0256 24  LYS A C   
194  O  O   . LYS A 24  ? 0.1962 0.1948 0.2478 -0.0063 -0.0491 -0.0093 24  LYS A O   
195  C  CB  . LYS A 24  ? 0.1401 0.1668 0.2415 0.0230  -0.0076 0.0333  24  LYS A CB  
196  C  CG  . LYS A 24  ? 0.1662 0.2483 0.2547 0.0267  -0.0237 0.0088  24  LYS A CG  
197  C  CD  . LYS A 24  ? 0.2471 0.2302 0.3277 0.0549  -0.0126 0.0010  24  LYS A CD  
198  C  CE  . LYS A 24  ? 0.2709 0.3549 0.3457 0.0434  0.0425  -0.0077 24  LYS A CE  
199  N  NZ  . LYS A 24  ? 0.3478 0.3529 0.4314 0.0419  0.0143  0.0208  24  LYS A NZ  
200  N  N   . GLY A 25  ? 0.1587 0.1405 0.2054 0.0063  -0.0229 -0.0326 25  GLY A N   
201  C  CA  . GLY A 25  ? 0.1764 0.1875 0.2088 -0.0107 -0.0245 -0.0388 25  GLY A CA  
202  C  C   . GLY A 25  ? 0.1656 0.1837 0.1597 0.0054  -0.0456 -0.0449 25  GLY A C   
203  O  O   . GLY A 25  ? 0.1979 0.1861 0.1756 0.0115  -0.0581 -0.0469 25  GLY A O   
204  N  N   . GLU A 26  ? 0.1498 0.2275 0.1729 -0.0049 -0.0351 -0.0555 26  GLU A N   
205  C  CA  . GLU A 26  ? 0.1653 0.2320 0.1642 0.0010  -0.0399 -0.0379 26  GLU A CA  
206  C  C   . GLU A 26  ? 0.1700 0.1860 0.1499 0.0062  -0.0397 -0.0489 26  GLU A C   
207  O  O   . GLU A 26  ? 0.2027 0.1878 0.1333 -0.0138 -0.0540 -0.0013 26  GLU A O   
208  C  CB  . GLU A 26  ? 0.1903 0.2486 0.1918 -0.0052 -0.0781 -0.0649 26  GLU A CB  
209  C  CG  . GLU A 26  ? 0.2192 0.3343 0.2227 0.0040  -0.0364 -0.0089 26  GLU A CG  
210  C  CD  . GLU A 26  ? 0.2709 0.3537 0.2451 -0.0171 -0.0815 -0.0120 26  GLU A CD  
211  O  OE1 . GLU A 26  ? 0.2957 0.4408 0.3089 -0.0037 -0.0379 -0.0215 26  GLU A OE1 
212  O  OE2 . GLU A 26  ? 0.3161 0.4435 0.3479 0.0397  -0.0812 -0.0335 26  GLU A OE2 
213  N  N   . ARG A 27  ? 0.1839 0.0973 0.1497 0.0000  -0.0564 -0.0260 27  ARG A N   
214  C  CA  . ARG A 27  ? 0.1588 0.1149 0.1286 0.0100  -0.0476 -0.0386 27  ARG A CA  
215  C  C   . ARG A 27  ? 0.1395 0.0976 0.1423 -0.0122 -0.0308 -0.0217 27  ARG A C   
216  O  O   . ARG A 27  ? 0.1424 0.0755 0.1480 0.0028  -0.0443 -0.0081 27  ARG A O   
217  C  CB  . ARG A 27  ? 0.2047 0.1234 0.1976 -0.0167 -0.0259 -0.0203 27  ARG A CB  
218  C  CG  . ARG A 27  ? 0.1957 0.1948 0.2073 -0.0065 -0.0315 -0.0135 27  ARG A CG  
219  C  CD  . ARG A 27  ? 0.2725 0.2198 0.2038 0.0483  -0.0432 -0.0149 27  ARG A CD  
220  N  NE  . ARG A 27  ? 0.2450 0.1639 0.2173 0.0007  -0.0183 -0.0049 27  ARG A NE  
221  C  CZ  . ARG A 27  ? 0.2167 0.1548 0.1688 0.0087  -0.0140 0.0114  27  ARG A CZ  
222  N  NH1 . ARG A 27  ? 0.2077 0.1883 0.2479 0.0253  -0.0199 -0.1315 27  ARG A NH1 
223  N  NH2 . ARG A 27  ? 0.2173 0.1190 0.1875 -0.0350 0.0057  -0.0260 27  ARG A NH2 
224  N  N   . GLN A 28  ? 0.1406 0.0758 0.1444 -0.0076 -0.0381 -0.0233 28  GLN A N   
225  C  CA  . GLN A 28  ? 0.1421 0.0666 0.1303 -0.0099 -0.0216 -0.0113 28  GLN A CA  
226  C  C   . GLN A 28  ? 0.1174 0.0591 0.1418 0.0013  -0.0194 -0.0160 28  GLN A C   
227  O  O   . GLN A 28  ? 0.1518 0.0662 0.1243 -0.0074 -0.0243 -0.0125 28  GLN A O   
228  C  CB  . GLN A 28  ? 0.1140 0.0860 0.1518 -0.0057 -0.0156 -0.0099 28  GLN A CB  
229  C  CG  . GLN A 28  ? 0.1474 0.0816 0.1350 -0.0115 -0.0421 0.0040  28  GLN A CG  
230  C  CD  . GLN A 28  ? 0.1246 0.1269 0.1448 0.0077  -0.0449 -0.0326 28  GLN A CD  
231  O  OE1 . GLN A 28  ? 0.1425 0.0885 0.1493 -0.0176 -0.0310 -0.0019 28  GLN A OE1 
232  N  NE2 . GLN A 28  ? 0.1140 0.0732 0.2074 0.0127  -0.0405 -0.0148 28  GLN A NE2 
233  N  N   . SER A 29  ? 0.1324 0.0561 0.1046 0.0167  -0.0124 -0.0065 29  SER A N   
234  C  CA  . SER A 29  ? 0.1000 0.0631 0.1375 0.0019  -0.0024 -0.0204 29  SER A CA  
235  C  C   . SER A 29  ? 0.1067 0.0618 0.1404 0.0281  -0.0275 -0.0034 29  SER A C   
236  O  O   . SER A 29  ? 0.1083 0.0687 0.1395 -0.0124 -0.0024 -0.0120 29  SER A O   
237  C  CB  . SER A 29  ? 0.1278 0.0634 0.1001 0.0144  -0.0119 0.0096  29  SER A CB  
238  O  OG  . SER A 29  ? 0.1207 0.0507 0.1305 0.0041  -0.0015 -0.0221 29  SER A OG  
239  N  N   . PRO A 30  ? 0.1075 0.0486 0.1240 0.0097  -0.0216 0.0154  30  PRO A N   
240  C  CA  . PRO A 30  ? 0.1253 0.0566 0.1011 -0.0054 -0.0223 0.0175  30  PRO A CA  
241  C  C   . PRO A 30  ? 0.1468 0.0276 0.1122 0.0048  -0.0194 -0.0139 30  PRO A C   
242  O  O   . PRO A 30  ? 0.1403 0.0420 0.1342 0.0076  -0.0348 0.0000  30  PRO A O   
243  C  CB  . PRO A 30  ? 0.0962 0.0521 0.1199 -0.0020 -0.0015 -0.0226 30  PRO A CB  
244  C  CG  . PRO A 30  ? 0.1228 0.0697 0.1194 -0.0148 -0.0001 0.0141  30  PRO A CG  
245  C  CD  . PRO A 30  ? 0.1187 0.0513 0.1231 0.0081  0.0148  -0.0208 30  PRO A CD  
246  N  N   . VAL A 31  ? 0.1421 0.0326 0.1097 0.0060  -0.0070 0.0161  31  VAL A N   
247  C  CA  . VAL A 31  ? 0.1321 0.0300 0.1196 -0.0064 -0.0195 0.0208  31  VAL A CA  
248  C  C   . VAL A 31  ? 0.1309 0.0711 0.1204 0.0019  -0.0013 0.0098  31  VAL A C   
249  O  O   . VAL A 31  ? 0.1261 0.0561 0.1389 0.0000  -0.0289 0.0129  31  VAL A O   
250  C  CB  . VAL A 31  ? 0.1446 0.0584 0.1516 -0.0082 -0.0140 -0.0080 31  VAL A CB  
251  C  CG1 . VAL A 31  ? 0.1573 0.0937 0.1703 -0.0317 0.0020  -0.0222 31  VAL A CG1 
252  C  CG2 . VAL A 31  ? 0.1597 0.0864 0.1608 0.0046  0.0052  0.0183  31  VAL A CG2 
253  N  N   . ASP A 32  ? 0.1636 0.0543 0.1235 0.0032  -0.0196 0.0295  32  ASP A N   
254  C  CA  . ASP A 32  ? 0.1542 0.0689 0.1140 0.0326  0.0010  0.0230  32  ASP A CA  
255  C  C   . ASP A 32  ? 0.1650 0.0601 0.1158 0.0171  -0.0028 0.0337  32  ASP A C   
256  O  O   . ASP A 32  ? 0.1632 0.0869 0.1544 0.0015  -0.0115 -0.0015 32  ASP A O   
257  C  CB  . ASP A 32  ? 0.1738 0.0597 0.1465 0.0098  -0.0215 0.0307  32  ASP A CB  
258  C  CG  . ASP A 32  ? 0.1867 0.0838 0.1075 0.0157  -0.0125 0.0017  32  ASP A CG  
259  O  OD1 . ASP A 32  ? 0.1987 0.0772 0.1000 0.0129  -0.0373 -0.0059 32  ASP A OD1 
260  O  OD2 . ASP A 32  ? 0.2660 0.1102 0.1328 -0.0190 -0.0337 0.0247  32  ASP A OD2 
261  N  N   . ILE A 33  ? 0.1189 0.0743 0.1274 0.0144  0.0038  0.0212  33  ILE A N   
262  C  CA  . ILE A 33  ? 0.1676 0.0615 0.1233 0.0261  0.0038  0.0304  33  ILE A CA  
263  C  C   . ILE A 33  ? 0.1894 0.0736 0.1650 0.0176  -0.0132 0.0206  33  ILE A C   
264  O  O   . ILE A 33  ? 0.1898 0.0819 0.1860 0.0155  0.0132  0.0274  33  ILE A O   
265  C  CB  . ILE A 33  ? 0.1774 0.0811 0.1287 0.0297  0.0037  0.0113  33  ILE A CB  
266  C  CG1 . ILE A 33  ? 0.1441 0.0777 0.1407 0.0181  -0.0026 0.0425  33  ILE A CG1 
267  C  CG2 . ILE A 33  ? 0.1321 0.1304 0.1609 0.0302  0.0304  0.0292  33  ILE A CG2 
268  C  CD1 . ILE A 33  ? 0.1511 0.1189 0.1879 0.0242  -0.0355 0.0104  33  ILE A CD1 
269  N  N   . ASP A 34  ? 0.1964 0.0901 0.1404 0.0183  0.0037  0.0494  34  ASP A N   
270  C  CA  . ASP A 34  ? 0.2149 0.1165 0.1597 0.0276  0.0065  0.0337  34  ASP A CA  
271  C  C   . ASP A 34  ? 0.2364 0.1032 0.1599 0.0348  0.0241  0.0593  34  ASP A C   
272  O  O   . ASP A 34  ? 0.2681 0.1420 0.1532 0.0441  0.0410  0.0324  34  ASP A O   
273  C  CB  . ASP A 34  ? 0.2536 0.1262 0.1876 0.0052  -0.0052 0.0799  34  ASP A CB  
274  C  CG  . ASP A 34  ? 0.2576 0.2131 0.2410 0.0208  -0.0234 0.0430  34  ASP A CG  
275  O  OD1 . ASP A 34  ? 0.3033 0.2113 0.2807 0.0430  0.0337  0.0971  34  ASP A OD1 
276  O  OD2 . ASP A 34  ? 0.3865 0.2964 0.3439 0.0122  -0.0344 0.1362  34  ASP A OD2 
277  N  N   . THR A 35  ? 0.2264 0.1395 0.2083 0.0267  0.0211  0.0878  35  THR A N   
278  C  CA  . THR A 35  ? 0.2465 0.1779 0.2052 0.0399  0.0269  0.0590  35  THR A CA  
279  C  C   . THR A 35  ? 0.2811 0.1375 0.2002 0.0507  0.0392  0.0714  35  THR A C   
280  O  O   . THR A 35  ? 0.3073 0.1647 0.2343 0.0432  0.0781  0.0662  35  THR A O   
281  C  CB  . THR A 35  ? 0.2601 0.1670 0.2321 0.0285  0.0237  0.0736  35  THR A CB  
282  O  OG1 . THR A 35  ? 0.2720 0.1789 0.2210 0.0178  0.0401  0.0755  35  THR A OG1 
283  C  CG2 . THR A 35  ? 0.2541 0.1914 0.2038 0.0732  0.0233  0.0601  35  THR A CG2 
284  N  N   . HIS A 36  ? 0.3353 0.1674 0.1919 0.0489  0.0513  0.0548  36  HIS A N   
285  C  CA  . HIS A 36  ? 0.3446 0.1446 0.1807 0.0527  0.0324  0.0683  36  HIS A CA  
286  C  C   . HIS A 36  ? 0.3564 0.2293 0.1850 0.0504  0.0379  0.0227  36  HIS A C   
287  O  O   . HIS A 36  ? 0.3409 0.2713 0.2141 0.0740  0.0107  0.0129  36  HIS A O   
288  C  CB  . HIS A 36  ? 0.4027 0.1717 0.1790 0.0487  0.0149  0.0644  36  HIS A CB  
289  C  CG  . HIS A 36  ? 0.4214 0.2328 0.1732 0.0741  -0.0231 0.0399  36  HIS A CG  
290  N  ND1 . HIS A 36  ? 0.4706 0.3122 0.2239 0.0786  -0.0421 0.0359  36  HIS A ND1 
291  C  CD2 . HIS A 36  ? 0.4760 0.2210 0.2022 -0.0041 -0.0732 0.0606  36  HIS A CD2 
292  C  CE1 . HIS A 36  ? 0.3917 0.1571 0.2583 0.0635  -0.0817 0.1074  36  HIS A CE1 
293  N  NE2 . HIS A 36  ? 0.4817 0.1932 0.1833 0.1296  -0.0087 0.0364  36  HIS A NE2 
294  N  N   . THR A 37  ? 0.3435 0.1656 0.1994 0.0716  0.0472  0.0193  37  THR A N   
295  C  CA  . THR A 37  ? 0.3747 0.1826 0.2189 0.0741  0.0243  0.0476  37  THR A CA  
296  C  C   . THR A 37  ? 0.3163 0.1500 0.1650 0.0727  0.0172  0.0304  37  THR A C   
297  O  O   . THR A 37  ? 0.3870 0.1912 0.1826 0.0676  0.0065  -0.0013 37  THR A O   
298  C  CB  . THR A 37  ? 0.3794 0.2374 0.2372 0.0741  0.0125  0.0157  37  THR A CB  
299  O  OG1 . THR A 37  ? 0.4531 0.2930 0.2803 0.0942  0.0286  0.0790  37  THR A OG1 
300  C  CG2 . THR A 37  ? 0.3716 0.1817 0.2979 0.1048  0.0054  0.0140  37  THR A CG2 
301  N  N   . ALA A 38  ? 0.3129 0.1685 0.1517 0.0467  0.0212  0.0465  38  ALA A N   
302  C  CA  . ALA A 38  ? 0.2807 0.1354 0.1572 0.0619  0.0269  0.0329  38  ALA A CA  
303  C  C   . ALA A 38  ? 0.2687 0.1471 0.2343 0.0328  0.0333  0.0177  38  ALA A C   
304  O  O   . ALA A 38  ? 0.3399 0.1851 0.3136 0.0551  0.0817  0.0298  38  ALA A O   
305  C  CB  . ALA A 38  ? 0.2570 0.1306 0.1941 0.0178  -0.0121 0.0148  38  ALA A CB  
306  N  N   . LYS A 39  ? 0.2671 0.1696 0.2202 0.0737  0.0024  0.0043  39  LYS A N   
307  C  CA  . LYS A 39  ? 0.2551 0.2127 0.2354 0.0762  0.0030  0.0015  39  LYS A CA  
308  C  C   . LYS A 39  ? 0.2155 0.1954 0.1810 0.0434  0.0085  -0.0105 39  LYS A C   
309  O  O   . LYS A 39  ? 0.2217 0.2127 0.1339 0.0441  0.0104  -0.0031 39  LYS A O   
310  C  CB  . LYS A 39  ? 0.2831 0.2813 0.2128 0.0658  -0.0091 -0.0034 39  LYS A CB  
311  C  CG  . LYS A 39  ? 0.2896 0.3607 0.2680 0.0494  0.0019  0.0161  39  LYS A CG  
312  C  CD  . LYS A 39  ? 0.2821 0.3418 0.2849 0.1067  -0.0375 0.0723  39  LYS A CD  
313  C  CE  . LYS A 39  ? 0.3540 0.4359 0.3265 0.0390  -0.0105 -0.0010 39  LYS A CE  
314  N  NZ  . LYS A 39  ? 0.2692 0.4520 0.3859 0.0320  -0.0054 0.0557  39  LYS A NZ  
315  N  N   . TYR A 40  ? 0.2584 0.2298 0.2029 0.0266  -0.0046 0.0206  40  TYR A N   
316  C  CA  . TYR A 40  ? 0.2317 0.2070 0.2141 0.0082  0.0269  0.0043  40  TYR A CA  
317  C  C   . TYR A 40  ? 0.2360 0.2119 0.1693 0.0054  0.0131  -0.0092 40  TYR A C   
318  O  O   . TYR A 40  ? 0.2241 0.2756 0.1572 0.0359  0.0174  0.0015  40  TYR A O   
319  C  CB  . TYR A 40  ? 0.2712 0.2310 0.2194 -0.0236 0.0362  0.0140  40  TYR A CB  
320  C  CG  . TYR A 40  ? 0.2570 0.2933 0.2583 -0.0395 0.0162  -0.0020 40  TYR A CG  
321  C  CD1 . TYR A 40  ? 0.2803 0.3341 0.2534 -0.0538 -0.0001 0.0082  40  TYR A CD1 
322  C  CD2 . TYR A 40  ? 0.3285 0.3993 0.3445 -0.0189 0.0461  -0.0013 40  TYR A CD2 
323  C  CE1 . TYR A 40  ? 0.2954 0.3816 0.2663 0.0140  0.0032  -0.0200 40  TYR A CE1 
324  C  CE2 . TYR A 40  ? 0.3161 0.4247 0.3174 0.0010  0.0015  0.0060  40  TYR A CE2 
325  C  CZ  . TYR A 40  ? 0.2397 0.4070 0.3323 -0.0152 -0.0001 -0.0020 40  TYR A CZ  
326  O  OH  . TYR A 40  ? 0.3057 0.4467 0.3472 0.0340  0.0186  -0.0103 40  TYR A OH  
327  N  N   . ASP A 41  ? 0.2169 0.1715 0.2033 0.0242  0.0192  -0.0088 41  ASP A N   
328  C  CA  . ASP A 41  ? 0.2456 0.1688 0.1851 0.0275  -0.0023 -0.0083 41  ASP A CA  
329  C  C   . ASP A 41  ? 0.2779 0.2608 0.2289 0.0300  0.0013  -0.0215 41  ASP A C   
330  O  O   . ASP A 41  ? 0.2385 0.2418 0.2350 0.0261  -0.0063 -0.0026 41  ASP A O   
331  C  CB  . ASP A 41  ? 0.2993 0.1828 0.2293 0.0241  -0.0048 0.0020  41  ASP A CB  
332  C  CG  . ASP A 41  ? 0.3402 0.2536 0.2929 -0.0127 -0.0078 -0.0168 41  ASP A CG  
333  O  OD1 . ASP A 41  ? 0.3729 0.2313 0.2888 0.0305  -0.0057 -0.0524 41  ASP A OD1 
334  O  OD2 . ASP A 41  ? 0.3684 0.2738 0.3888 -0.0487 -0.0465 0.0107  41  ASP A OD2 
335  N  N   . PRO A 42  ? 0.2870 0.3348 0.2431 0.0597  0.0087  -0.0051 42  PRO A N   
336  C  CA  . PRO A 42  ? 0.3269 0.3479 0.2766 0.0614  0.0146  0.0020  42  PRO A CA  
337  C  C   . PRO A 42  ? 0.3220 0.3316 0.2782 0.0727  0.0233  -0.0074 42  PRO A C   
338  O  O   . PRO A 42  ? 0.3445 0.4059 0.3583 0.0890  0.0282  -0.0076 42  PRO A O   
339  C  CB  . PRO A 42  ? 0.3492 0.3998 0.2958 0.0460  0.0247  -0.0026 42  PRO A CB  
340  C  CG  . PRO A 42  ? 0.3276 0.3942 0.2566 0.0724  0.0353  -0.0291 42  PRO A CG  
341  C  CD  . PRO A 42  ? 0.3346 0.3542 0.2270 0.0623  0.0362  -0.0255 42  PRO A CD  
342  N  N   . SER A 43  ? 0.3195 0.2930 0.2666 0.0934  0.0236  -0.0182 43  SER A N   
343  C  CA  . SER A 43  ? 0.3671 0.3088 0.2842 0.0575  -0.0049 -0.0125 43  SER A CA  
344  C  C   . SER A 43  ? 0.3673 0.3008 0.2724 0.0689  -0.0052 -0.0115 43  SER A C   
345  O  O   . SER A 43  ? 0.4250 0.2858 0.3061 0.0693  -0.0195 -0.0103 43  SER A O   
346  C  CB  . SER A 43  ? 0.3508 0.3320 0.3140 0.0577  0.0024  -0.0219 43  SER A CB  
347  O  OG  . SER A 43  ? 0.4158 0.3603 0.3860 -0.0126 -0.0447 -0.0388 43  SER A OG  
348  N  N   . LEU A 44  ? 0.3363 0.3259 0.2594 0.0571  -0.0131 -0.0166 44  LEU A N   
349  C  CA  . LEU A 44  ? 0.2907 0.2946 0.2414 0.0384  -0.0346 0.0175  44  LEU A CA  
350  C  C   . LEU A 44  ? 0.2813 0.3273 0.2890 0.0166  -0.0140 0.0283  44  LEU A C   
351  O  O   . LEU A 44  ? 0.2692 0.3758 0.3249 -0.0071 -0.0129 0.0623  44  LEU A O   
352  C  CB  . LEU A 44  ? 0.2559 0.3084 0.2187 0.0412  -0.0089 -0.0104 44  LEU A CB  
353  C  CG  . LEU A 44  ? 0.2490 0.2379 0.2449 0.0208  -0.0200 0.0292  44  LEU A CG  
354  C  CD1 . LEU A 44  ? 0.2266 0.2547 0.1889 -0.0059 0.0306  0.0116  44  LEU A CD1 
355  C  CD2 . LEU A 44  ? 0.2594 0.2257 0.2278 -0.0239 -0.0364 0.0143  44  LEU A CD2 
356  N  N   . LYS A 45  ? 0.2730 0.2931 0.2700 0.0204  -0.0372 0.0237  45  LYS A N   
357  C  CA  . LYS A 45  ? 0.2917 0.2935 0.2965 0.0285  -0.0263 -0.0175 45  LYS A CA  
358  C  C   . LYS A 45  ? 0.2468 0.2322 0.2691 0.0324  -0.0082 -0.0074 45  LYS A C   
359  O  O   . LYS A 45  ? 0.2563 0.2389 0.2860 0.0038  0.0046  -0.0335 45  LYS A O   
360  C  CB  . LYS A 45  ? 0.2940 0.2637 0.2666 0.0599  -0.0065 0.0035  45  LYS A CB  
361  C  CG  . LYS A 45  ? 0.3206 0.3596 0.3159 0.0274  -0.0275 -0.0237 45  LYS A CG  
362  C  CD  . LYS A 45  ? 0.3980 0.4056 0.4212 -0.0302 -0.0304 -0.0116 45  LYS A CD  
363  C  CE  . LYS A 45  ? 0.4902 0.4485 0.4544 0.0105  -0.0027 -0.0450 45  LYS A CE  
364  N  NZ  . LYS A 45  ? 0.5231 0.4750 0.5001 0.0151  0.0253  0.0035  45  LYS A NZ  
365  N  N   . PRO A 46  ? 0.2227 0.2311 0.2663 0.0027  0.0010  -0.0068 46  PRO A N   
366  C  CA  . PRO A 46  ? 0.2169 0.2428 0.2599 -0.0001 -0.0081 0.0027  46  PRO A CA  
367  C  C   . PRO A 46  ? 0.1894 0.2243 0.2354 0.0057  0.0074  -0.0032 46  PRO A C   
368  O  O   . PRO A 46  ? 0.1695 0.2116 0.2694 -0.0256 -0.0375 0.0034  46  PRO A O   
369  C  CB  . PRO A 46  ? 0.2002 0.2669 0.2401 -0.0124 0.0020  0.0013  46  PRO A CB  
370  C  CG  . PRO A 46  ? 0.2184 0.3158 0.3065 -0.0028 -0.0051 -0.0298 46  PRO A CG  
371  C  CD  . PRO A 46  ? 0.2524 0.2750 0.2597 0.0395  -0.0115 -0.0551 46  PRO A CD  
372  N  N   . LEU A 47  ? 0.2171 0.2261 0.2680 0.0076  -0.0087 0.0265  47  LEU A N   
373  C  CA  . LEU A 47  ? 0.1720 0.2198 0.2171 -0.0130 0.0088  0.0274  47  LEU A CA  
374  C  C   . LEU A 47  ? 0.1743 0.1837 0.2695 -0.0295 -0.0304 0.0579  47  LEU A C   
375  O  O   . LEU A 47  ? 0.1828 0.2493 0.3104 -0.0621 -0.0511 0.0839  47  LEU A O   
376  C  CB  . LEU A 47  ? 0.2439 0.2619 0.2894 -0.0104 0.0081  0.0142  47  LEU A CB  
377  C  CG  . LEU A 47  ? 0.2417 0.2649 0.3237 -0.0476 -0.0049 -0.0551 47  LEU A CG  
378  C  CD1 . LEU A 47  ? 0.1936 0.3230 0.3924 -0.0546 -0.0529 -0.0640 47  LEU A CD1 
379  C  CD2 . LEU A 47  ? 0.1696 0.2419 0.3801 0.0137  0.0051  -0.0430 47  LEU A CD2 
380  N  N   . SER A 48  ? 0.1600 0.1483 0.2476 -0.0201 -0.0405 0.0557  48  SER A N   
381  C  CA  . SER A 48  ? 0.1671 0.1681 0.2414 -0.0186 -0.0269 0.0166  48  SER A CA  
382  C  C   . SER A 48  ? 0.1792 0.1621 0.2205 -0.0222 -0.0256 0.0051  48  SER A C   
383  O  O   . SER A 48  ? 0.1639 0.1333 0.2241 -0.0240 0.0019  -0.0046 48  SER A O   
384  C  CB  . SER A 48  ? 0.1993 0.1521 0.2474 -0.0027 -0.0395 0.0135  48  SER A CB  
385  O  OG  . SER A 48  ? 0.2509 0.2070 0.2799 0.0353  -0.0366 0.0417  48  SER A OG  
386  N  N   . VAL A 49  ? 0.2061 0.1642 0.2385 -0.0355 -0.0222 -0.0019 49  VAL A N   
387  C  CA  . VAL A 49  ? 0.2065 0.1482 0.2515 -0.0441 -0.0141 -0.0136 49  VAL A CA  
388  C  C   . VAL A 49  ? 0.2137 0.2008 0.2576 -0.0635 -0.0298 -0.0093 49  VAL A C   
389  O  O   . VAL A 49  ? 0.2182 0.2498 0.2752 -0.1001 -0.0423 -0.0120 49  VAL A O   
390  C  CB  . VAL A 49  ? 0.2831 0.1515 0.2328 -0.0322 0.0010  -0.0337 49  VAL A CB  
391  C  CG1 . VAL A 49  ? 0.3021 0.2177 0.2513 -0.0351 0.0205  -0.0410 49  VAL A CG1 
392  C  CG2 . VAL A 49  ? 0.2331 0.1560 0.3338 -0.0155 -0.0001 -0.0063 49  VAL A CG2 
393  N  N   . SER A 50  ? 0.2099 0.1710 0.2619 -0.0474 -0.0265 0.0098  50  SER A N   
394  C  CA  . SER A 50  ? 0.2037 0.1911 0.2978 -0.0083 -0.0428 -0.0137 50  SER A CA  
395  C  C   . SER A 50  ? 0.1887 0.1976 0.2946 -0.0210 -0.0627 0.0164  50  SER A C   
396  O  O   . SER A 50  ? 0.2137 0.1596 0.2912 -0.0298 -0.0520 0.0126  50  SER A O   
397  C  CB  . SER A 50  ? 0.2524 0.2101 0.3051 -0.0071 -0.0160 0.0074  50  SER A CB  
398  O  OG  . SER A 50  ? 0.3233 0.3201 0.3883 0.0120  -0.0229 -0.0153 50  SER A OG  
399  N  N   . TYR A 51  ? 0.2002 0.1697 0.2831 -0.0114 -0.0516 -0.0006 51  TYR A N   
400  C  CA  . TYR A 51  ? 0.1846 0.1410 0.2522 -0.0131 -0.0612 0.0297  51  TYR A CA  
401  C  C   . TYR A 51  ? 0.2020 0.1700 0.2861 0.0082  -0.0450 0.0329  51  TYR A C   
402  O  O   . TYR A 51  ? 0.2266 0.1659 0.2429 0.0005  -0.0771 0.0315  51  TYR A O   
403  C  CB  . TYR A 51  ? 0.1812 0.1529 0.2300 0.0147  -0.0570 -0.0021 51  TYR A CB  
404  C  CG  . TYR A 51  ? 0.1821 0.1210 0.1976 -0.0401 -0.0476 0.0209  51  TYR A CG  
405  C  CD1 . TYR A 51  ? 0.1750 0.1137 0.2399 -0.0054 -0.0368 0.0181  51  TYR A CD1 
406  C  CD2 . TYR A 51  ? 0.1869 0.1206 0.1679 -0.0076 -0.0241 0.0294  51  TYR A CD2 
407  C  CE1 . TYR A 51  ? 0.1483 0.0919 0.2087 0.0205  -0.0031 0.0264  51  TYR A CE1 
408  C  CE2 . TYR A 51  ? 0.1600 0.0808 0.1763 -0.0252 -0.0313 -0.0142 51  TYR A CE2 
409  C  CZ  . TYR A 51  ? 0.1661 0.1246 0.1620 -0.0217 -0.0218 -0.0085 51  TYR A CZ  
410  O  OH  . TYR A 51  ? 0.1613 0.0864 0.2052 -0.0165 -0.0542 -0.0092 51  TYR A OH  
411  N  N   . ASP A 52  ? 0.1747 0.2025 0.3102 -0.0120 -0.0537 0.0346  52  ASP A N   
412  C  CA  . ASP A 52  ? 0.2173 0.2743 0.3012 0.0041  -0.0335 0.0562  52  ASP A CA  
413  C  C   . ASP A 52  ? 0.2497 0.2576 0.3203 0.0074  -0.0496 0.0408  52  ASP A C   
414  O  O   . ASP A 52  ? 0.2881 0.2698 0.2992 0.0027  -0.0694 0.0513  52  ASP A O   
415  C  CB  . ASP A 52  ? 0.2295 0.3138 0.3233 0.0164  -0.0478 0.0566  52  ASP A CB  
416  C  CG  . ASP A 52  ? 0.3334 0.3658 0.4035 0.0228  -0.0263 0.0240  52  ASP A CG  
417  O  OD1 . ASP A 52  ? 0.4879 0.4936 0.4907 -0.0028 0.0030  0.0259  52  ASP A OD1 
418  O  OD2 . ASP A 52  ? 0.5223 0.4498 0.5568 0.0229  -0.0350 0.0419  52  ASP A OD2 
419  N  N   . GLN A 53  ? 0.2152 0.2047 0.3240 0.0175  -0.0454 0.0447  53  GLN A N   
420  C  CA  . GLN A 53  ? 0.2442 0.2242 0.3453 0.0078  -0.0318 0.0294  53  GLN A CA  
421  C  C   . GLN A 53  ? 0.2241 0.1541 0.2793 0.0164  -0.0193 0.0098  53  GLN A C   
422  O  O   . GLN A 53  ? 0.2429 0.1861 0.3052 -0.0107 -0.0458 0.0296  53  GLN A O   
423  C  CB  . GLN A 53  ? 0.2843 0.2421 0.3731 0.0186  -0.0044 0.0183  53  GLN A CB  
424  C  CG  . GLN A 53  ? 0.3187 0.3316 0.4199 0.0126  -0.0115 0.0309  53  GLN A CG  
425  C  CD  . GLN A 53  ? 0.4153 0.4815 0.4667 0.0096  -0.0307 0.0403  53  GLN A CD  
426  O  OE1 . GLN A 53  ? 0.4600 0.5525 0.5250 0.0331  -0.0160 0.0436  53  GLN A OE1 
427  N  NE2 . GLN A 53  ? 0.4097 0.4764 0.3984 0.0266  -0.0621 0.0693  53  GLN A NE2 
428  N  N   . ALA A 54  ? 0.2209 0.1280 0.2803 0.0017  -0.0653 0.0308  54  ALA A N   
429  C  CA  . ALA A 54  ? 0.2066 0.1319 0.2321 0.0143  -0.0529 0.0120  54  ALA A CA  
430  C  C   . ALA A 54  ? 0.2471 0.1718 0.2363 0.0027  -0.0586 -0.0240 54  ALA A C   
431  O  O   . ALA A 54  ? 0.2716 0.2832 0.2511 -0.0408 -0.0874 -0.0461 54  ALA A O   
432  C  CB  . ALA A 54  ? 0.2397 0.1326 0.3138 0.0195  -0.0340 0.0060  54  ALA A CB  
433  N  N   . THR A 55  ? 0.2173 0.1248 0.2192 0.0244  -0.0546 0.0368  55  THR A N   
434  C  CA  . THR A 55  ? 0.2475 0.1293 0.2469 0.0271  -0.0696 0.0419  55  THR A CA  
435  C  C   . THR A 55  ? 0.2288 0.0992 0.1854 0.0057  -0.0631 0.0306  55  THR A C   
436  O  O   . THR A 55  ? 0.2504 0.0756 0.1886 0.0065  -0.0520 0.0284  55  THR A O   
437  C  CB  . THR A 55  ? 0.2897 0.1273 0.2757 0.0230  -0.0361 0.0800  55  THR A CB  
438  O  OG1 . THR A 55  ? 0.3693 0.1792 0.3804 0.0179  -0.0904 0.0181  55  THR A OG1 
439  C  CG2 . THR A 55  ? 0.3233 0.1756 0.2583 0.0516  -0.0619 0.0414  55  THR A CG2 
440  N  N   . SER A 56  ? 0.2383 0.0870 0.1627 0.0133  -0.0681 0.0247  56  SER A N   
441  C  CA  . SER A 56  ? 0.2698 0.1014 0.1606 -0.0028 -0.0395 0.0023  56  SER A CA  
442  C  C   . SER A 56  ? 0.2809 0.1183 0.2058 -0.0001 -0.0566 0.0032  56  SER A C   
443  O  O   . SER A 56  ? 0.3011 0.1199 0.1914 0.0248  -0.0771 0.0138  56  SER A O   
444  C  CB  . SER A 56  ? 0.2824 0.1088 0.1418 -0.0005 -0.1005 0.0070  56  SER A CB  
445  O  OG  . SER A 56  ? 0.3082 0.1016 0.1821 -0.0237 -0.0888 0.0271  56  SER A OG  
446  N  N   . LEU A 57  ? 0.2609 0.0722 0.1731 0.0152  -0.0359 0.0194  57  LEU A N   
447  C  CA  . LEU A 57  ? 0.3145 0.0838 0.1903 0.0127  -0.0038 0.0223  57  LEU A CA  
448  C  C   . LEU A 57  ? 0.3023 0.0732 0.1692 0.0215  -0.0226 0.0076  57  LEU A C   
449  O  O   . LEU A 57  ? 0.3396 0.1110 0.1703 0.0355  -0.0480 0.0322  57  LEU A O   
450  C  CB  . LEU A 57  ? 0.3359 0.1235 0.1839 0.0100  -0.0187 0.0187  57  LEU A CB  
451  C  CG  . LEU A 57  ? 0.4011 0.1309 0.2239 0.0071  -0.0274 0.0038  57  LEU A CG  
452  C  CD1 . LEU A 57  ? 0.4092 0.2286 0.3324 -0.0570 -0.0274 0.0251  57  LEU A CD1 
453  C  CD2 . LEU A 57  ? 0.4494 0.1770 0.2504 0.0579  -0.0283 0.0593  57  LEU A CD2 
454  N  N   . ARG A 58  ? 0.2761 0.0886 0.1939 0.0333  -0.0261 0.0253  58  ARG A N   
455  C  CA  . ARG A 58  ? 0.2500 0.0720 0.1627 0.0111  -0.0130 0.0496  58  ARG A CA  
456  C  C   . ARG A 58  ? 0.2533 0.0895 0.1742 -0.0088 -0.0295 0.0173  58  ARG A C   
457  O  O   . ARG A 58  ? 0.2570 0.0863 0.1466 0.0200  -0.0203 0.0238  58  ARG A O   
458  C  CB  . ARG A 58  ? 0.2994 0.0752 0.1907 0.0114  -0.0195 0.0434  58  ARG A CB  
459  C  CG  . ARG A 58  ? 0.2615 0.1604 0.2095 -0.0535 0.0132  0.0575  58  ARG A CG  
460  C  CD  . ARG A 58  ? 0.3122 0.2271 0.2377 -0.0711 -0.0392 0.0417  58  ARG A CD  
461  N  NE  . ARG A 58  ? 0.2824 0.1608 0.2194 -0.0366 -0.0283 0.0515  58  ARG A NE  
462  C  CZ  . ARG A 58  ? 0.2106 0.1937 0.2031 -0.0513 -0.0201 0.0350  58  ARG A CZ  
463  N  NH1 . ARG A 58  ? 0.3265 0.1818 0.2361 -0.0807 0.0293  0.0463  58  ARG A NH1 
464  N  NH2 . ARG A 58  ? 0.2875 0.1401 0.2513 -0.0408 -0.0386 0.0614  58  ARG A NH2 
465  N  N   . ILE A 59  ? 0.2570 0.0679 0.1555 0.0034  -0.0305 0.0219  59  ILE A N   
466  C  CA  . ILE A 59  ? 0.2410 0.0904 0.1551 -0.0015 -0.0168 0.0192  59  ILE A CA  
467  C  C   . ILE A 59  ? 0.2377 0.0740 0.1169 -0.0156 -0.0300 0.0210  59  ILE A C   
468  O  O   . ILE A 59  ? 0.2725 0.1659 0.1357 -0.0005 -0.0232 0.0436  59  ILE A O   
469  C  CB  . ILE A 59  ? 0.2428 0.0905 0.1286 -0.0198 -0.0383 0.0040  59  ILE A CB  
470  C  CG1 . ILE A 59  ? 0.2508 0.0749 0.1592 0.0080  -0.0331 0.0342  59  ILE A CG1 
471  C  CG2 . ILE A 59  ? 0.2792 0.1052 0.1414 -0.0126 -0.0487 0.0156  59  ILE A CG2 
472  C  CD1 . ILE A 59  ? 0.2489 0.0961 0.1722 -0.0275 -0.0184 0.0142  59  ILE A CD1 
473  N  N   . LEU A 60  ? 0.2336 0.0962 0.1475 -0.0241 -0.0529 0.0131  60  LEU A N   
474  C  CA  . LEU A 60  ? 0.2379 0.0926 0.1731 0.0129  -0.0441 0.0294  60  LEU A CA  
475  C  C   . LEU A 60  ? 0.2490 0.0750 0.1704 -0.0144 -0.0185 0.0124  60  LEU A C   
476  O  O   . LEU A 60  ? 0.2029 0.1020 0.1300 -0.0164 -0.0043 0.0331  60  LEU A O   
477  C  CB  . LEU A 60  ? 0.2442 0.0720 0.2234 -0.0126 -0.0493 -0.0041 60  LEU A CB  
478  C  CG  . LEU A 60  ? 0.2695 0.1331 0.1854 -0.0190 -0.0674 0.0388  60  LEU A CG  
479  C  CD1 . LEU A 60  ? 0.3161 0.1007 0.2212 -0.0217 -0.0082 0.0328  60  LEU A CD1 
480  C  CD2 . LEU A 60  ? 0.2635 0.0904 0.2037 -0.0303 -0.0107 -0.0185 60  LEU A CD2 
481  N  N   . ASN A 61  ? 0.2474 0.0649 0.1275 -0.0133 0.0068  0.0187  61  ASN A N   
482  C  CA  . ASN A 61  ? 0.2415 0.0628 0.1667 -0.0188 -0.0028 0.0034  61  ASN A CA  
483  C  C   . ASN A 61  ? 0.2428 0.0993 0.1749 -0.0241 -0.0144 0.0148  61  ASN A C   
484  O  O   . ASN A 61  ? 0.2721 0.0922 0.1720 -0.0307 0.0063  0.0280  61  ASN A O   
485  C  CB  . ASN A 61  ? 0.2953 0.0584 0.1491 -0.0081 0.0054  0.0107  61  ASN A CB  
486  C  CG  . ASN A 61  ? 0.2465 0.0887 0.1477 -0.0148 -0.0060 0.0184  61  ASN A CG  
487  O  OD1 . ASN A 61  ? 0.2649 0.1088 0.1724 -0.0241 -0.0006 0.0186  61  ASN A OD1 
488  N  ND2 . ASN A 61  ? 0.2939 0.0811 0.1359 -0.0166 0.0161  -0.0220 61  ASN A ND2 
489  N  N   . ASN A 62  ? 0.2478 0.0768 0.1565 -0.0216 -0.0186 0.0228  62  ASN A N   
490  C  CA  . ASN A 62  ? 0.2442 0.1159 0.1477 -0.0254 -0.0178 0.0133  62  ASN A CA  
491  C  C   . ASN A 62  ? 0.2506 0.1336 0.1718 -0.0262 -0.0073 0.0041  62  ASN A C   
492  O  O   . ASN A 62  ? 0.2621 0.1562 0.2192 -0.0637 -0.0228 0.0178  62  ASN A O   
493  C  CB  . ASN A 62  ? 0.2824 0.0917 0.1528 -0.0263 0.0109  0.0110  62  ASN A CB  
494  C  CG  . ASN A 62  ? 0.2942 0.1544 0.1004 -0.0571 -0.0310 -0.0248 62  ASN A CG  
495  O  OD1 . ASN A 62  ? 0.3233 0.0854 0.2037 -0.0428 0.0098  -0.0116 62  ASN A OD1 
496  N  ND2 . ASN A 62  ? 0.3838 0.1301 0.1853 -0.0283 0.0533  0.0074  62  ASN A ND2 
497  N  N   . GLY A 63  ? 0.2460 0.1142 0.1685 -0.0416 0.0197  0.0059  63  GLY A N   
498  C  CA  . GLY A 63  ? 0.2228 0.1292 0.1424 -0.0421 0.0302  0.0270  63  GLY A CA  
499  C  C   . GLY A 63  ? 0.2140 0.1190 0.1666 -0.0405 0.0089  0.0006  63  GLY A C   
500  O  O   . GLY A 63  ? 0.2166 0.1617 0.1842 -0.0308 0.0007  -0.0031 63  GLY A O   
501  N  N   . HIS A 64  ? 0.2099 0.1059 0.1324 -0.0308 0.0230  0.0107  64  HIS A N   
502  C  CA  . HIS A 64  ? 0.2205 0.1463 0.1660 -0.0419 0.0041  0.0244  64  HIS A CA  
503  C  C   . HIS A 64  ? 0.2005 0.1137 0.2036 -0.0353 -0.0138 0.0456  64  HIS A C   
504  O  O   . HIS A 64  ? 0.2070 0.1704 0.2504 -0.0221 -0.0294 0.1030  64  HIS A O   
505  C  CB  . HIS A 64  ? 0.2063 0.1567 0.1800 -0.0637 -0.0010 -0.0040 64  HIS A CB  
506  C  CG  . HIS A 64  ? 0.2633 0.1488 0.2583 -0.0639 -0.0164 0.0175  64  HIS A CG  
507  N  ND1 . HIS A 64  ? 0.2730 0.2734 0.1861 -0.0272 -0.0071 -0.0544 64  HIS A ND1 
508  C  CD2 . HIS A 64  ? 0.3030 0.1632 0.2198 -0.0703 -0.0342 0.0245  64  HIS A CD2 
509  C  CE1 . HIS A 64  ? 0.2860 0.2878 0.3133 -0.0636 0.0102  -0.0076 64  HIS A CE1 
510  N  NE2 . HIS A 64  ? 0.2489 0.2899 0.3100 -0.0775 0.0141  0.0298  64  HIS A NE2 
511  N  N   . ALA A 65  ? 0.2049 0.1138 0.1544 -0.0212 -0.0076 0.0013  65  ALA A N   
512  C  CA  . ALA A 65  ? 0.2173 0.0813 0.1574 -0.0230 -0.0076 -0.0081 65  ALA A CA  
513  C  C   . ALA A 65  ? 0.2264 0.0497 0.1084 -0.0240 -0.0032 0.0165  65  ALA A C   
514  O  O   . ALA A 65  ? 0.2349 0.0732 0.1499 -0.0373 0.0062  0.0163  65  ALA A O   
515  C  CB  . ALA A 65  ? 0.2080 0.1251 0.1307 -0.0070 -0.0105 0.0113  65  ALA A CB  
516  N  N   . PHE A 66  ? 0.2131 0.0732 0.1456 0.0077  -0.0168 -0.0028 66  PHE A N   
517  C  CA  . PHE A 66  ? 0.2288 0.0777 0.1142 -0.0091 -0.0121 0.0126  66  PHE A CA  
518  C  C   . PHE A 66  ? 0.2045 0.0803 0.1321 -0.0148 -0.0237 0.0035  66  PHE A C   
519  O  O   . PHE A 66  ? 0.2210 0.0612 0.1420 -0.0052 -0.0149 0.0093  66  PHE A O   
520  C  CB  . PHE A 66  ? 0.2160 0.1334 0.1345 -0.0337 -0.0249 0.0245  66  PHE A CB  
521  C  CG  . PHE A 66  ? 0.2300 0.1045 0.1240 -0.0348 -0.0189 -0.0289 66  PHE A CG  
522  C  CD1 . PHE A 66  ? 0.2379 0.1464 0.1016 -0.0280 -0.0286 -0.0021 66  PHE A CD1 
523  C  CD2 . PHE A 66  ? 0.2191 0.1102 0.1183 -0.0035 -0.0126 -0.0071 66  PHE A CD2 
524  C  CE1 . PHE A 66  ? 0.2115 0.1438 0.1439 -0.0156 -0.0417 0.0021  66  PHE A CE1 
525  C  CE2 . PHE A 66  ? 0.2307 0.1128 0.1308 -0.0167 -0.0109 -0.0114 66  PHE A CE2 
526  C  CZ  . PHE A 66  ? 0.2149 0.1028 0.1303 -0.0500 -0.0500 0.0040  66  PHE A CZ  
527  N  N   . ASN A 67  ? 0.2106 0.0568 0.1219 -0.0097 -0.0212 0.0153  67  ASN A N   
528  C  CA  . ASN A 67  ? 0.2090 0.0750 0.1155 0.0015  -0.0190 -0.0024 67  ASN A CA  
529  C  C   . ASN A 67  ? 0.1946 0.0485 0.1298 -0.0040 -0.0335 0.0110  67  ASN A C   
530  O  O   . ASN A 67  ? 0.2325 0.0854 0.1308 -0.0182 -0.0171 0.0412  67  ASN A O   
531  C  CB  . ASN A 67  ? 0.2034 0.0930 0.1367 -0.0463 -0.0289 0.0007  67  ASN A CB  
532  C  CG  . ASN A 67  ? 0.2238 0.1274 0.1237 -0.0428 0.0062  0.0133  67  ASN A CG  
533  O  OD1 . ASN A 67  ? 0.2458 0.1463 0.1626 -0.0663 -0.0571 0.0537  67  ASN A OD1 
534  N  ND2 . ASN A 67  ? 0.2633 0.1499 0.2456 -0.0769 -0.0533 -0.0008 67  ASN A ND2 
535  N  N   . VAL A 68  ? 0.1922 0.0562 0.1625 0.0005  -0.0355 -0.0020 68  VAL A N   
536  C  CA  . VAL A 68  ? 0.2116 0.0595 0.1448 0.0303  -0.0472 0.0093  68  VAL A CA  
537  C  C   . VAL A 68  ? 0.2428 0.0876 0.1407 0.0322  -0.0203 0.0154  68  VAL A C   
538  O  O   . VAL A 68  ? 0.2399 0.0614 0.1421 0.0265  -0.0428 0.0125  68  VAL A O   
539  C  CB  . VAL A 68  ? 0.2067 0.0861 0.1532 0.0182  -0.0324 0.0052  68  VAL A CB  
540  C  CG1 . VAL A 68  ? 0.1904 0.1299 0.1491 0.0230  -0.0441 0.0083  68  VAL A CG1 
541  C  CG2 . VAL A 68  ? 0.2178 0.0729 0.1682 0.0098  -0.0245 -0.0273 68  VAL A CG2 
542  N  N   . GLU A 69  ? 0.2705 0.0594 0.1605 0.0239  -0.0116 0.0194  69  GLU A N   
543  C  CA  . GLU A 69  ? 0.2469 0.0700 0.1221 0.0110  -0.0031 0.0125  69  GLU A CA  
544  C  C   . GLU A 69  ? 0.2474 0.0667 0.1499 0.0214  -0.0269 0.0445  69  GLU A C   
545  O  O   . GLU A 69  ? 0.2827 0.0822 0.1530 0.0122  -0.0566 0.0174  69  GLU A O   
546  C  CB  . GLU A 69  ? 0.2374 0.1115 0.2152 0.0241  -0.0080 0.0335  69  GLU A CB  
547  C  CG  . GLU A 69  ? 0.2249 0.1115 0.2155 -0.0307 0.0355  0.0198  69  GLU A CG  
548  C  CD  . GLU A 69  ? 0.2818 0.0930 0.2285 -0.0057 0.0000  0.0417  69  GLU A CD  
549  O  OE1 . GLU A 69  ? 0.2694 0.1263 0.2652 -0.0214 -0.0166 0.0768  69  GLU A OE1 
550  O  OE2 . GLU A 69  ? 0.2827 0.1295 0.2955 -0.0008 0.0027  0.0531  69  GLU A OE2 
551  N  N   . PHE A 70  ? 0.2379 0.0700 0.1644 0.0031  -0.0199 0.0328  70  PHE A N   
552  C  CA  . PHE A 70  ? 0.2135 0.0688 0.1907 -0.0099 -0.0200 0.0170  70  PHE A CA  
553  C  C   . PHE A 70  ? 0.2202 0.1025 0.1652 -0.0035 -0.0381 -0.0057 70  PHE A C   
554  O  O   . PHE A 70  ? 0.2364 0.0779 0.1959 -0.0109 -0.0573 0.0258  70  PHE A O   
555  C  CB  . PHE A 70  ? 0.2020 0.0522 0.1548 -0.0103 -0.0242 0.0200  70  PHE A CB  
556  C  CG  . PHE A 70  ? 0.2027 0.0820 0.1757 0.0054  -0.0406 0.0315  70  PHE A CG  
557  C  CD1 . PHE A 70  ? 0.2407 0.0904 0.1691 0.0118  -0.0661 0.0311  70  PHE A CD1 
558  C  CD2 . PHE A 70  ? 0.2339 0.0779 0.1523 -0.0031 -0.0480 0.0278  70  PHE A CD2 
559  C  CE1 . PHE A 70  ? 0.2148 0.0944 0.1770 -0.0097 -0.0212 0.0174  70  PHE A CE1 
560  C  CE2 . PHE A 70  ? 0.2619 0.0712 0.1625 -0.0055 -0.0637 0.0302  70  PHE A CE2 
561  C  CZ  . PHE A 70  ? 0.2601 0.0729 0.1422 -0.0217 -0.0049 0.0131  70  PHE A CZ  
562  N  N   . ASP A 71  ? 0.2431 0.0538 0.2131 0.0038  -0.0570 0.0178  71  ASP A N   
563  C  CA  . ASP A 71  ? 0.2324 0.0637 0.2242 0.0093  -0.0476 0.0175  71  ASP A CA  
564  C  C   . ASP A 71  ? 0.2354 0.0576 0.2669 0.0094  -0.0190 -0.0024 71  ASP A C   
565  O  O   . ASP A 71  ? 0.2746 0.1101 0.3653 -0.0305 -0.0280 -0.0121 71  ASP A O   
566  C  CB  . ASP A 71  ? 0.2725 0.1451 0.2680 -0.0041 -0.0828 0.0294  71  ASP A CB  
567  C  CG  . ASP A 71  ? 0.2842 0.1676 0.3325 0.0085  -0.0962 0.0200  71  ASP A CG  
568  O  OD1 . ASP A 71  ? 0.2642 0.0858 0.3851 0.0372  -0.1064 0.0646  71  ASP A OD1 
569  O  OD2 . ASP A 71  ? 0.3021 0.1378 0.4903 -0.0271 -0.1371 0.0353  71  ASP A OD2 
570  N  N   . ASP A 72  ? 0.2273 0.0723 0.2547 -0.0006 -0.0384 0.0218  72  ASP A N   
571  C  CA  . ASP A 72  ? 0.2212 0.0937 0.2569 -0.0252 -0.0269 -0.0023 72  ASP A CA  
572  C  C   . ASP A 72  ? 0.2761 0.1585 0.2890 -0.0326 -0.0154 -0.0024 72  ASP A C   
573  O  O   . ASP A 72  ? 0.3033 0.0863 0.3255 -0.0208 -0.0476 -0.0137 72  ASP A O   
574  C  CB  . ASP A 72  ? 0.2299 0.1043 0.2537 -0.0401 -0.0094 0.0027  72  ASP A CB  
575  C  CG  . ASP A 72  ? 0.2169 0.1335 0.2417 -0.0237 -0.0275 -0.0060 72  ASP A CG  
576  O  OD1 . ASP A 72  ? 0.2562 0.2192 0.2676 -0.0627 -0.0397 0.0746  72  ASP A OD1 
577  O  OD2 . ASP A 72  ? 0.2619 0.1693 0.1933 -0.0234 -0.0293 0.0116  72  ASP A OD2 
578  N  N   . SER A 73  ? 0.2795 0.0680 0.3319 -0.0220 -0.0273 0.0006  73  SER A N   
579  C  CA  . SER A 73  ? 0.3041 0.0709 0.3292 -0.0073 -0.0137 -0.0062 73  SER A CA  
580  C  C   . SER A 73  ? 0.3025 0.1770 0.3697 -0.0222 -0.0076 -0.0138 73  SER A C   
581  O  O   . SER A 73  ? 0.3306 0.1275 0.3477 -0.0110 -0.0176 0.0080  73  SER A O   
582  C  CB  . SER A 73  ? 0.3510 0.1955 0.3468 -0.0083 -0.0141 -0.0093 73  SER A CB  
583  O  OG  . SER A 73  ? 0.3575 0.1395 0.3507 0.0063  -0.0085 0.0126  73  SER A OG  
584  N  N   . GLN A 74  ? 0.3009 0.1442 0.3787 0.0034  -0.0186 -0.0034 74  GLN A N   
585  C  CA  . GLN A 74  ? 0.3105 0.2460 0.3503 -0.0126 -0.0165 -0.0130 74  GLN A CA  
586  C  C   . GLN A 74  ? 0.2882 0.2421 0.3371 -0.0273 -0.0434 -0.0342 74  GLN A C   
587  O  O   . GLN A 74  ? 0.2732 0.2134 0.3521 -0.0307 -0.0688 -0.0159 74  GLN A O   
588  C  CB  . GLN A 74  ? 0.3330 0.2513 0.3865 0.0054  -0.0216 -0.0032 74  GLN A CB  
589  C  CG  . GLN A 74  ? 0.3495 0.3018 0.4243 -0.0076 -0.0034 -0.0013 74  GLN A CG  
590  C  CD  . GLN A 74  ? 0.3866 0.3619 0.4528 -0.0302 -0.0408 0.0087  74  GLN A CD  
591  O  OE1 . GLN A 74  ? 0.4890 0.3506 0.4616 -0.0147 -0.0093 -0.0283 74  GLN A OE1 
592  N  NE2 . GLN A 74  ? 0.4343 0.4314 0.4736 -0.0283 -0.0105 -0.0030 74  GLN A NE2 
593  N  N   A ASP A 75  ? 0.3140 0.2811 0.3310 -0.0244 -0.0427 -0.0258 75  ASP A N   
594  N  N   B ASP A 75  ? 0.3059 0.2677 0.3294 -0.0294 -0.0381 -0.0238 75  ASP A N   
595  C  CA  A ASP A 75  ? 0.3105 0.2811 0.3319 -0.0192 -0.0350 -0.0162 75  ASP A CA  
596  C  CA  B ASP A 75  ? 0.2900 0.2363 0.3143 -0.0304 -0.0372 -0.0098 75  ASP A CA  
597  C  C   A ASP A 75  ? 0.2971 0.2640 0.3129 -0.0120 -0.0471 0.0105  75  ASP A C   
598  C  C   B ASP A 75  ? 0.2788 0.2450 0.2871 -0.0282 -0.0515 -0.0055 75  ASP A C   
599  O  O   A ASP A 75  ? 0.3129 0.3177 0.3422 -0.0171 -0.0531 0.0006  75  ASP A O   
600  O  O   B ASP A 75  ? 0.2820 0.2004 0.2847 -0.0078 -0.0542 0.0318  75  ASP A O   
601  C  CB  A ASP A 75  ? 0.3465 0.3123 0.3283 -0.0129 -0.0302 -0.0060 75  ASP A CB  
602  C  CB  B ASP A 75  ? 0.3370 0.2957 0.3525 -0.0283 -0.0239 -0.0124 75  ASP A CB  
603  C  CG  A ASP A 75  ? 0.3000 0.2628 0.3192 -0.0162 -0.0181 -0.0181 75  ASP A CG  
604  C  CG  B ASP A 75  ? 0.2354 0.1547 0.3356 0.0328  -0.0416 0.0247  75  ASP A CG  
605  O  OD1 A ASP A 75  ? 0.3130 0.4143 0.2735 0.0110  -0.0740 -0.0626 75  ASP A OD1 
606  O  OD1 B ASP A 75  ? 0.3686 0.3582 0.4088 0.0062  -0.0030 -0.0111 75  ASP A OD1 
607  O  OD2 A ASP A 75  ? 0.3495 0.3496 0.3402 0.0017  0.0153  -0.0065 75  ASP A OD2 
608  O  OD2 B ASP A 75  ? 0.4135 0.3677 0.4344 0.0399  -0.0073 0.0155  75  ASP A OD2 
609  N  N   . LYS A 76  ? 0.2806 0.2128 0.2815 -0.0024 -0.0728 0.0399  76  LYS A N   
610  C  CA  . LYS A 76  ? 0.3082 0.2108 0.3252 -0.0256 -0.0502 0.0333  76  LYS A CA  
611  C  C   . LYS A 76  ? 0.3289 0.2572 0.3413 -0.0192 -0.0518 0.0340  76  LYS A C   
612  O  O   . LYS A 76  ? 0.3718 0.3140 0.3974 -0.0331 -0.0568 0.0227  76  LYS A O   
613  C  CB  . LYS A 76  ? 0.3274 0.1871 0.2937 -0.0283 -0.0612 0.0366  76  LYS A CB  
614  C  CG  . LYS A 76  ? 0.3999 0.2425 0.3770 0.0109  -0.0340 0.0357  76  LYS A CG  
615  C  CD  . LYS A 76  ? 0.4182 0.2081 0.3359 -0.0212 -0.0245 0.0192  76  LYS A CD  
616  C  CE  . LYS A 76  ? 0.3725 0.2889 0.3468 0.0423  -0.0575 0.0019  76  LYS A CE  
617  N  NZ  . LYS A 76  ? 0.3758 0.2440 0.3540 0.0544  -0.0318 -0.0020 76  LYS A NZ  
618  N  N   . ALA A 77  ? 0.2666 0.2164 0.3029 0.0122  -0.0882 0.0423  77  ALA A N   
619  C  CA  . ALA A 77  ? 0.2231 0.1993 0.2621 -0.0049 -0.0738 0.0284  77  ALA A CA  
620  C  C   . ALA A 77  ? 0.1905 0.1761 0.2605 -0.0093 -0.0817 -0.0041 77  ALA A C   
621  O  O   . ALA A 77  ? 0.2009 0.2680 0.2892 -0.0228 -0.0570 -0.0505 77  ALA A O   
622  C  CB  . ALA A 77  ? 0.2698 0.2235 0.2368 0.0154  -0.0846 -0.0074 77  ALA A CB  
623  N  N   . VAL A 78  ? 0.2221 0.1076 0.2213 -0.0130 -0.0812 0.0205  78  VAL A N   
624  C  CA  . VAL A 78  ? 0.2478 0.0863 0.2317 -0.0049 -0.0593 0.0372  78  VAL A CA  
625  C  C   . VAL A 78  ? 0.2059 0.0987 0.2158 -0.0093 -0.0452 0.0318  78  VAL A C   
626  O  O   . VAL A 78  ? 0.1858 0.1185 0.2835 -0.0377 -0.0795 0.0522  78  VAL A O   
627  C  CB  . VAL A 78  ? 0.2824 0.1539 0.2979 -0.0237 -0.0546 0.0153  78  VAL A CB  
628  C  CG1 . VAL A 78  ? 0.3198 0.1266 0.3370 -0.0038 -0.0397 0.0381  78  VAL A CG1 
629  C  CG2 . VAL A 78  ? 0.2695 0.1620 0.3154 0.0076  0.0000  0.0443  78  VAL A CG2 
630  N  N   . LEU A 79  ? 0.1932 0.0719 0.2022 0.0188  -0.0465 0.0103  79  LEU A N   
631  C  CA  . LEU A 79  ? 0.1815 0.0886 0.2070 0.0012  0.0035  -0.0005 79  LEU A CA  
632  C  C   . LEU A 79  ? 0.1749 0.0910 0.2034 -0.0007 0.0037  -0.0059 79  LEU A C   
633  O  O   . LEU A 79  ? 0.1933 0.1203 0.2302 -0.0320 0.0006  -0.0168 79  LEU A O   
634  C  CB  . LEU A 79  ? 0.1477 0.1235 0.2478 0.0043  -0.0401 0.0443  79  LEU A CB  
635  C  CG  . LEU A 79  ? 0.1742 0.1451 0.1943 -0.0208 -0.0181 0.0020  79  LEU A CG  
636  C  CD1 . LEU A 79  ? 0.1562 0.1366 0.3855 -0.0111 -0.0054 0.0544  79  LEU A CD1 
637  C  CD2 . LEU A 79  ? 0.1385 0.1563 0.2372 0.0167  -0.0085 -0.0068 79  LEU A CD2 
638  N  N   . LYS A 80  ? 0.1871 0.1416 0.1782 -0.0043 -0.0031 -0.0173 80  LYS A N   
639  C  CA  . LYS A 80  ? 0.2061 0.1176 0.2167 0.0097  0.0093  -0.0087 80  LYS A CA  
640  C  C   . LYS A 80  ? 0.1661 0.1445 0.2266 0.0346  0.0082  0.0041  80  LYS A C   
641  O  O   . LYS A 80  ? 0.2098 0.1019 0.2469 -0.0120 -0.0258 -0.0003 80  LYS A O   
642  C  CB  . LYS A 80  ? 0.2623 0.1970 0.2559 0.0432  -0.0105 0.0059  80  LYS A CB  
643  C  CG  . LYS A 80  ? 0.2421 0.1568 0.3327 0.0372  -0.0041 -0.0258 80  LYS A CG  
644  C  CD  . LYS A 80  ? 0.2953 0.2426 0.3797 0.0496  -0.0163 0.0017  80  LYS A CD  
645  C  CE  . LYS A 80  ? 0.3754 0.4250 0.5238 0.0483  0.0000  0.0245  80  LYS A CE  
646  N  NZ  . LYS A 80  ? 0.4848 0.5418 0.5353 0.0252  -0.0021 0.0194  80  LYS A NZ  
647  N  N   . GLY A 81  ? 0.1997 0.1437 0.2097 -0.0027 0.0236  0.0131  81  GLY A N   
648  C  CA  . GLY A 81  ? 0.1846 0.1467 0.2496 0.0214  0.0439  0.0344  81  GLY A CA  
649  C  C   . GLY A 81  ? 0.1900 0.1359 0.2695 0.0175  0.0375  0.0048  81  GLY A C   
650  O  O   . GLY A 81  ? 0.1743 0.1509 0.2454 0.0157  0.0170  -0.0076 81  GLY A O   
651  N  N   . GLY A 82  ? 0.2041 0.1581 0.2907 0.0003  0.0333  0.0377  82  GLY A N   
652  C  CA  . GLY A 82  ? 0.2210 0.1491 0.3341 -0.0003 0.0219  0.0383  82  GLY A CA  
653  C  C   . GLY A 82  ? 0.2080 0.1517 0.2825 0.0505  0.0214  0.0329  82  GLY A C   
654  O  O   . GLY A 82  ? 0.2512 0.2674 0.3173 0.0644  0.0835  0.0155  82  GLY A O   
655  N  N   . PRO A 83  ? 0.2011 0.1464 0.2811 0.0359  0.0248  0.0335  83  PRO A N   
656  C  CA  . PRO A 83  ? 0.2185 0.1409 0.2403 0.0505  0.0115  0.0171  83  PRO A CA  
657  C  C   . PRO A 83  ? 0.2472 0.1665 0.2509 0.0483  0.0109  -0.0109 83  PRO A C   
658  O  O   . PRO A 83  ? 0.2476 0.2422 0.2773 0.0291  -0.0116 -0.0077 83  PRO A O   
659  C  CB  . PRO A 83  ? 0.2522 0.1394 0.2497 0.0500  0.0052  0.0136  83  PRO A CB  
660  C  CG  . PRO A 83  ? 0.2059 0.1473 0.2232 0.0560  0.0350  -0.0093 83  PRO A CG  
661  C  CD  . PRO A 83  ? 0.1736 0.1199 0.2737 0.0348  0.0313  0.0227  83  PRO A CD  
662  N  N   . LEU A 84  ? 0.2026 0.1306 0.1994 0.0282  0.0073  -0.0320 84  LEU A N   
663  C  CA  . LEU A 84  ? 0.2396 0.0772 0.2350 0.0208  0.0140  -0.0265 84  LEU A CA  
664  C  C   . LEU A 84  ? 0.2404 0.1416 0.2820 0.0219  0.0136  -0.0438 84  LEU A C   
665  O  O   . LEU A 84  ? 0.2640 0.1334 0.2861 0.0264  0.0340  -0.0811 84  LEU A O   
666  C  CB  . LEU A 84  ? 0.2029 0.0548 0.2095 0.0105  0.0231  -0.0030 84  LEU A CB  
667  C  CG  . LEU A 84  ? 0.1677 0.0725 0.2388 0.0211  0.0142  -0.0289 84  LEU A CG  
668  C  CD1 . LEU A 84  ? 0.1633 0.1254 0.2307 0.0091  -0.0003 -0.0174 84  LEU A CD1 
669  C  CD2 . LEU A 84  ? 0.1515 0.0879 0.2012 0.0000  -0.0131 -0.0247 84  LEU A CD2 
670  N  N   . ASP A 85  ? 0.2713 0.1341 0.2897 0.0233  0.0313  -0.0703 85  ASP A N   
671  C  CA  . ASP A 85  ? 0.3107 0.1729 0.3184 0.0065  0.0071  -0.0531 85  ASP A CA  
672  C  C   . ASP A 85  ? 0.2700 0.1368 0.3421 0.0137  0.0160  -0.0333 85  ASP A C   
673  O  O   . ASP A 85  ? 0.3260 0.2084 0.3580 0.0313  0.0318  -0.0366 85  ASP A O   
674  C  CB  . ASP A 85  ? 0.3750 0.1219 0.3269 0.0282  -0.0043 -0.0644 85  ASP A CB  
675  C  CG  . ASP A 85  ? 0.3956 0.3095 0.4092 0.0048  0.0052  -0.0188 85  ASP A CG  
676  O  OD1 . ASP A 85  ? 0.4301 0.4180 0.4366 -0.0344 0.0046  0.0035  85  ASP A OD1 
677  O  OD2 . ASP A 85  ? 0.4210 0.4093 0.5060 -0.0300 -0.0103 -0.0472 85  ASP A OD2 
678  N  N   . GLY A 86  ? 0.3248 0.2336 0.3417 -0.0130 0.0003  -0.0167 86  GLY A N   
679  C  CA  . GLY A 86  ? 0.3076 0.1966 0.2599 -0.0328 0.0081  -0.0219 86  GLY A CA  
680  C  C   . GLY A 86  ? 0.2985 0.1639 0.2694 -0.0364 -0.0038 -0.0272 86  GLY A C   
681  O  O   . GLY A 86  ? 0.3377 0.2444 0.2933 -0.0888 0.0063  -0.0183 86  GLY A O   
682  N  N   A THR A 87  ? 0.2570 0.1335 0.2334 0.0024  0.0184  -0.0254 87  THR A N   
683  N  N   B THR A 87  ? 0.2368 0.1217 0.2223 -0.0007 0.0196  -0.0324 87  THR A N   
684  C  CA  A THR A 87  ? 0.2471 0.1580 0.2508 0.0068  0.0098  -0.0052 87  THR A CA  
685  C  CA  B THR A 87  ? 0.2095 0.1509 0.2338 0.0152  0.0110  -0.0208 87  THR A CA  
686  C  C   A THR A 87  ? 0.2081 0.1238 0.2587 0.0152  -0.0020 -0.0162 87  THR A C   
687  C  C   B THR A 87  ? 0.1861 0.1277 0.2388 0.0105  -0.0010 -0.0240 87  THR A C   
688  O  O   A THR A 87  ? 0.1855 0.0461 0.2393 0.0129  0.0085  -0.0087 87  THR A O   
689  O  O   B THR A 87  ? 0.1616 0.0449 0.2163 0.0119  -0.0041 -0.0239 87  THR A O   
690  C  CB  A THR A 87  ? 0.2907 0.2184 0.2781 0.0146  -0.0032 -0.0057 87  THR A CB  
691  C  CB  B THR A 87  ? 0.2363 0.2067 0.2581 0.0157  0.0046  -0.0173 87  THR A CB  
692  O  OG1 A THR A 87  ? 0.3036 0.2471 0.2770 0.0375  -0.0120 -0.0057 87  THR A OG1 
693  O  OG1 B THR A 87  ? 0.2178 0.1695 0.2576 0.0441  0.0055  0.0141  87  THR A OG1 
694  C  CG2 A THR A 87  ? 0.3072 0.2385 0.2799 0.0252  0.0171  0.0019  87  THR A CG2 
695  C  CG2 B THR A 87  ? 0.1482 0.1353 0.2002 0.0515  0.0092  -0.0656 87  THR A CG2 
696  N  N   . TYR A 88  ? 0.1756 0.0706 0.2364 0.0074  -0.0051 -0.0211 88  TYR A N   
697  C  CA  . TYR A 88  ? 0.1502 0.0952 0.2331 -0.0001 -0.0194 -0.0071 88  TYR A CA  
698  C  C   . TYR A 88  ? 0.1491 0.0786 0.2087 -0.0054 -0.0436 0.0225  88  TYR A C   
699  O  O   . TYR A 88  ? 0.1668 0.1455 0.2641 -0.0401 -0.0619 0.0351  88  TYR A O   
700  C  CB  . TYR A 88  ? 0.1702 0.0788 0.2148 -0.0059 -0.0269 0.0046  88  TYR A CB  
701  C  CG  . TYR A 88  ? 0.1606 0.0425 0.1979 0.0184  -0.0227 -0.0006 88  TYR A CG  
702  C  CD1 . TYR A 88  ? 0.1808 0.0785 0.1821 0.0228  -0.0244 -0.0209 88  TYR A CD1 
703  C  CD2 . TYR A 88  ? 0.1811 0.0349 0.1747 0.0063  -0.0335 0.0120  88  TYR A CD2 
704  C  CE1 . TYR A 88  ? 0.1513 0.0896 0.1767 0.0048  -0.0115 -0.0001 88  TYR A CE1 
705  C  CE2 . TYR A 88  ? 0.1592 0.0459 0.1525 0.0010  -0.0252 -0.0176 88  TYR A CE2 
706  C  CZ  . TYR A 88  ? 0.1641 0.0405 0.1847 0.0010  -0.0265 -0.0476 88  TYR A CZ  
707  O  OH  . TYR A 88  ? 0.1692 0.0648 0.1641 0.0052  -0.0138 -0.0359 88  TYR A OH  
708  N  N   . ARG A 89  ? 0.1829 0.0513 0.1810 0.0122  -0.0273 0.0082  89  ARG A N   
709  C  CA  . ARG A 89  ? 0.1964 0.0332 0.1764 0.0089  -0.0307 0.0281  89  ARG A CA  
710  C  C   . ARG A 89  ? 0.1565 0.0529 0.1544 0.0063  -0.0155 0.0194  89  ARG A C   
711  O  O   . ARG A 89  ? 0.1381 0.0542 0.1592 0.0043  -0.0166 0.0049  89  ARG A O   
712  C  CB  . ARG A 89  ? 0.2581 0.0995 0.2055 -0.0124 -0.0511 0.0390  89  ARG A CB  
713  C  CG  . ARG A 89  ? 0.3201 0.1510 0.2515 -0.0082 -0.0430 0.0666  89  ARG A CG  
714  C  CD  . ARG A 89  ? 0.3556 0.1412 0.2965 0.0249  -0.0277 0.0549  89  ARG A CD  
715  N  NE  . ARG A 89  ? 0.4149 0.2201 0.2317 0.0340  -0.0436 0.0844  89  ARG A NE  
716  C  CZ  . ARG A 89  ? 0.3560 0.1248 0.2306 -0.0454 -0.0113 0.0458  89  ARG A CZ  
717  N  NH1 . ARG A 89  ? 0.3923 0.1673 0.2688 0.0524  0.0299  0.0537  89  ARG A NH1 
718  N  NH2 . ARG A 89  ? 0.3406 0.2835 0.3129 0.0408  -0.0197 -0.0141 89  ARG A NH2 
719  N  N   . LEU A 90  ? 0.1782 0.0621 0.1281 -0.0052 -0.0219 0.0028  90  LEU A N   
720  C  CA  . LEU A 90  ? 0.1429 0.0693 0.1647 -0.0149 -0.0171 -0.0041 90  LEU A CA  
721  C  C   . LEU A 90  ? 0.1817 0.0594 0.1368 -0.0142 -0.0247 0.0366  90  LEU A C   
722  O  O   . LEU A 90  ? 0.1772 0.1018 0.1688 0.0055  -0.0351 0.0303  90  LEU A O   
723  C  CB  . LEU A 90  ? 0.1518 0.0689 0.1659 -0.0159 -0.0171 0.0157  90  LEU A CB  
724  C  CG  . LEU A 90  ? 0.2058 0.0592 0.1345 0.0146  -0.0502 0.0098  90  LEU A CG  
725  C  CD1 . LEU A 90  ? 0.1975 0.0794 0.1621 -0.0195 -0.0485 -0.0052 90  LEU A CD1 
726  C  CD2 . LEU A 90  ? 0.1710 0.1247 0.1688 -0.0181 -0.0645 -0.0165 90  LEU A CD2 
727  N  N   . ILE A 91  ? 0.1550 0.0414 0.1685 -0.0146 -0.0198 -0.0052 91  ILE A N   
728  C  CA  . ILE A 91  ? 0.1839 0.0487 0.1433 -0.0119 -0.0281 0.0057  91  ILE A CA  
729  C  C   . ILE A 91  ? 0.1597 0.0600 0.1368 -0.0003 -0.0120 0.0296  91  ILE A C   
730  O  O   . ILE A 91  ? 0.1959 0.0531 0.1318 -0.0081 -0.0474 0.0175  91  ILE A O   
731  C  CB  . ILE A 91  ? 0.1826 0.0768 0.1437 -0.0277 -0.0238 0.0049  91  ILE A CB  
732  C  CG1 . ILE A 91  ? 0.2005 0.1609 0.1713 -0.0747 0.0035  0.0115  91  ILE A CG1 
733  C  CG2 . ILE A 91  ? 0.2000 0.0718 0.1837 -0.0159 -0.0520 0.0144  91  ILE A CG2 
734  C  CD1 . ILE A 91  ? 0.2268 0.1409 0.1828 -0.0724 -0.0197 -0.0116 91  ILE A CD1 
735  N  N   . GLN A 92  ? 0.1846 0.0353 0.1289 -0.0093 -0.0272 0.0195  92  GLN A N   
736  C  CA  . GLN A 92  ? 0.1879 0.0265 0.1244 -0.0028 0.0141  0.0073  92  GLN A CA  
737  C  C   . GLN A 92  ? 0.1673 0.0667 0.1140 -0.0046 -0.0085 0.0013  92  GLN A C   
738  O  O   . GLN A 92  ? 0.1979 0.0373 0.1201 -0.0149 -0.0318 0.0057  92  GLN A O   
739  C  CB  . GLN A 92  ? 0.1810 0.0829 0.1384 -0.0055 -0.0197 0.0008  92  GLN A CB  
740  C  CG  . GLN A 92  ? 0.2110 0.0293 0.1852 0.0158  -0.0417 0.0163  92  GLN A CG  
741  C  CD  . GLN A 92  ? 0.1840 0.0724 0.1704 0.0001  -0.0258 0.0041  92  GLN A CD  
742  O  OE1 . GLN A 92  ? 0.2182 0.0399 0.1568 0.0008  -0.0375 0.0122  92  GLN A OE1 
743  N  NE2 . GLN A 92  ? 0.1645 0.0939 0.2286 0.0027  -0.0057 0.0251  92  GLN A NE2 
744  N  N   . PHE A 93  ? 0.1821 0.0310 0.1370 0.0048  -0.0305 0.0063  93  PHE A N   
745  C  CA  . PHE A 93  ? 0.1984 0.0259 0.1008 0.0028  -0.0078 0.0061  93  PHE A CA  
746  C  C   . PHE A 93  ? 0.1675 0.0543 0.0790 -0.0187 -0.0278 0.0000  93  PHE A C   
747  O  O   . PHE A 93  ? 0.2105 0.0551 0.1019 0.0037  -0.0329 0.0131  93  PHE A O   
748  C  CB  . PHE A 93  ? 0.1940 0.0393 0.1077 -0.0326 -0.0445 0.0060  93  PHE A CB  
749  C  CG  . PHE A 93  ? 0.2090 0.0446 0.1111 -0.0152 -0.0300 0.0215  93  PHE A CG  
750  C  CD1 . PHE A 93  ? 0.2447 0.0586 0.1092 -0.0164 -0.0434 -0.0020 93  PHE A CD1 
751  C  CD2 . PHE A 93  ? 0.1835 0.1045 0.1226 -0.0165 -0.0768 0.0507  93  PHE A CD2 
752  C  CE1 . PHE A 93  ? 0.1882 0.0567 0.1263 0.0146  -0.0263 0.0093  93  PHE A CE1 
753  C  CE2 . PHE A 93  ? 0.1901 0.0436 0.1316 0.0124  -0.0487 0.0035  93  PHE A CE2 
754  C  CZ  . PHE A 93  ? 0.2316 0.0419 0.1506 0.0076  -0.0621 0.0118  93  PHE A CZ  
755  N  N   . HIS A 94  ? 0.1673 0.0293 0.1219 0.0096  -0.0373 0.0100  94  HIS A N   
756  C  CA  . HIS A 94  ? 0.1543 0.0376 0.1068 0.0116  -0.0355 0.0176  94  HIS A CA  
757  C  C   . HIS A 94  ? 0.1530 0.0634 0.1134 0.0091  -0.0414 -0.0057 94  HIS A C   
758  O  O   . HIS A 94  ? 0.1562 0.0450 0.1254 -0.0038 -0.0164 0.0164  94  HIS A O   
759  C  CB  . HIS A 94  ? 0.1717 0.0716 0.1228 -0.0114 -0.0320 -0.0226 94  HIS A CB  
760  C  CG  . HIS A 94  ? 0.1810 0.0307 0.1122 -0.0153 -0.0078 -0.0052 94  HIS A CG  
761  N  ND1 . HIS A 94  ? 0.1633 0.0470 0.1159 -0.0200 -0.0164 -0.0102 94  HIS A ND1 
762  C  CD2 . HIS A 94  ? 0.1772 0.0432 0.1284 0.0006  0.0118  -0.0263 94  HIS A CD2 
763  C  CE1 . HIS A 94  ? 0.1507 0.0575 0.0966 -0.0173 -0.0226 -0.0024 94  HIS A CE1 
764  N  NE2 . HIS A 94  ? 0.1541 0.0284 0.1122 -0.0086 -0.0068 0.0119  94  HIS A NE2 
765  N  N   . PHE A 95  ? 0.1590 0.0295 0.1363 0.0015  -0.0206 0.0049  95  PHE A N   
766  C  CA  . PHE A 95  ? 0.1535 0.0322 0.1176 -0.0182 -0.0406 0.0186  95  PHE A CA  
767  C  C   . PHE A 95  ? 0.1675 0.0464 0.0998 -0.0269 -0.0207 -0.0005 95  PHE A C   
768  O  O   . PHE A 95  ? 0.1861 0.0489 0.1230 -0.0233 -0.0107 0.0088  95  PHE A O   
769  C  CB  . PHE A 95  ? 0.1733 0.0381 0.1187 -0.0136 -0.0287 -0.0013 95  PHE A CB  
770  C  CG  . PHE A 95  ? 0.1814 0.0341 0.1022 -0.0239 -0.0292 -0.0068 95  PHE A CG  
771  C  CD1 . PHE A 95  ? 0.1941 0.0652 0.1055 -0.0074 -0.0175 -0.0197 95  PHE A CD1 
772  C  CD2 . PHE A 95  ? 0.1492 0.0605 0.1433 -0.0241 -0.0461 -0.0219 95  PHE A CD2 
773  C  CE1 . PHE A 95  ? 0.1828 0.0703 0.1222 -0.0008 -0.0383 0.0105  95  PHE A CE1 
774  C  CE2 . PHE A 95  ? 0.1986 0.0341 0.1160 -0.0162 -0.0310 -0.0083 95  PHE A CE2 
775  C  CZ  . PHE A 95  ? 0.1715 0.0539 0.1354 -0.0010 -0.0193 -0.0230 95  PHE A CZ  
776  N  N   . HIS A 96  ? 0.1644 0.0363 0.0986 -0.0097 -0.0245 -0.0092 96  HIS A N   
777  C  CA  . HIS A 96  ? 0.1513 0.0280 0.1464 0.0095  -0.0332 -0.0173 96  HIS A CA  
778  C  C   . HIS A 96  ? 0.1553 0.0622 0.1092 -0.0010 -0.0287 0.0041  96  HIS A C   
779  O  O   . HIS A 96  ? 0.1643 0.0331 0.1303 0.0076  -0.0074 -0.0135 96  HIS A O   
780  C  CB  . HIS A 96  ? 0.1909 0.0403 0.1475 -0.0060 -0.0463 -0.0142 96  HIS A CB  
781  C  CG  . HIS A 96  ? 0.1524 0.0288 0.1310 0.0174  -0.0372 -0.0153 96  HIS A CG  
782  N  ND1 . HIS A 96  ? 0.1159 0.0597 0.1561 -0.0087 -0.0313 -0.0313 96  HIS A ND1 
783  C  CD2 . HIS A 96  ? 0.1622 0.0577 0.1079 0.0066  -0.0204 -0.0010 96  HIS A CD2 
784  C  CE1 . HIS A 96  ? 0.1745 0.0349 0.1351 -0.0210 -0.0187 -0.0057 96  HIS A CE1 
785  N  NE2 . HIS A 96  ? 0.1728 0.0401 0.1460 -0.0051 -0.0113 -0.0247 96  HIS A NE2 
786  N  N   . TRP A 97  ? 0.1582 0.0256 0.1205 -0.0002 -0.0216 -0.0050 97  TRP A N   
787  C  CA  . TRP A 97  ? 0.1750 0.0278 0.1185 0.0081  -0.0215 -0.0147 97  TRP A CA  
788  C  C   . TRP A 97  ? 0.1376 0.0551 0.1365 0.0088  -0.0318 -0.0156 97  TRP A C   
789  O  O   . TRP A 97  ? 0.1580 0.0417 0.1499 -0.0119 -0.0113 -0.0160 97  TRP A O   
790  C  CB  . TRP A 97  ? 0.1731 0.0637 0.1142 -0.0204 -0.0207 -0.0148 97  TRP A CB  
791  C  CG  . TRP A 97  ? 0.1685 0.0527 0.0838 -0.0267 -0.0030 0.0127  97  TRP A CG  
792  C  CD1 . TRP A 97  ? 0.1940 0.0846 0.1076 -0.0274 -0.0017 -0.0271 97  TRP A CD1 
793  C  CD2 . TRP A 97  ? 0.2002 0.0718 0.1115 -0.0359 -0.0346 -0.0294 97  TRP A CD2 
794  N  NE1 . TRP A 97  ? 0.2134 0.0722 0.1377 -0.0083 -0.0142 -0.0318 97  TRP A NE1 
795  C  CE2 . TRP A 97  ? 0.2213 0.0682 0.1387 -0.0157 -0.0024 -0.0172 97  TRP A CE2 
796  C  CE3 . TRP A 97  ? 0.1792 0.0689 0.0873 -0.0086 -0.0305 -0.0275 97  TRP A CE3 
797  C  CZ2 . TRP A 97  ? 0.2216 0.0615 0.1054 -0.0313 -0.0005 0.0206  97  TRP A CZ2 
798  C  CZ3 . TRP A 97  ? 0.2102 0.0741 0.1185 -0.0081 -0.0103 0.0110  97  TRP A CZ3 
799  C  CH2 . TRP A 97  ? 0.2292 0.0655 0.1102 -0.0032 0.0070  -0.0164 97  TRP A CH2 
800  N  N   . GLY A 98  ? 0.1954 0.0306 0.1391 0.0136  -0.0037 -0.0118 98  GLY A N   
801  C  CA  . GLY A 98  ? 0.1843 0.0386 0.1347 0.0237  0.0129  -0.0131 98  GLY A CA  
802  C  C   . GLY A 98  ? 0.1718 0.0539 0.1529 -0.0038 0.0087  -0.0252 98  GLY A C   
803  O  O   . GLY A 98  ? 0.2027 0.0540 0.1521 -0.0122 -0.0164 -0.0175 98  GLY A O   
804  N  N   . SER A 99  ? 0.2018 0.0511 0.1803 0.0218  0.0141  -0.0285 99  SER A N   
805  C  CA  . SER A 99  ? 0.2131 0.0560 0.1941 0.0026  0.0179  -0.0388 99  SER A CA  
806  C  C   . SER A 99  ? 0.2364 0.0505 0.1869 0.0124  -0.0035 -0.0311 99  SER A C   
807  O  O   . SER A 99  ? 0.2617 0.0860 0.1756 -0.0111 -0.0059 -0.0335 99  SER A O   
808  C  CB  . SER A 99  ? 0.2275 0.0907 0.1961 0.0472  -0.0052 -0.0476 99  SER A CB  
809  O  OG  . SER A 99  ? 0.2106 0.0886 0.2281 0.0282  0.0157  -0.0370 99  SER A OG  
810  N  N   . LEU A 100 ? 0.1862 0.0635 0.2045 -0.0200 0.0000  -0.0263 100 LEU A N   
811  C  CA  . LEU A 100 ? 0.2261 0.0585 0.2134 -0.0038 0.0162  -0.0041 100 LEU A CA  
812  C  C   . LEU A 100 ? 0.2110 0.0458 0.2006 0.0093  0.0071  0.0068  100 LEU A C   
813  O  O   . LEU A 100 ? 0.2372 0.0386 0.1941 -0.0038 -0.0125 -0.0126 100 LEU A O   
814  C  CB  . LEU A 100 ? 0.2767 0.1409 0.2754 0.0140  0.0209  0.0388  100 LEU A CB  
815  C  CG  . LEU A 100 ? 0.2960 0.1307 0.2746 0.0410  -0.0028 0.0003  100 LEU A CG  
816  C  CD1 . LEU A 100 ? 0.2903 0.2845 0.4212 0.0891  0.0093  0.0008  100 LEU A CD1 
817  C  CD2 . LEU A 100 ? 0.3973 0.1966 0.3309 0.0531  0.0678  -0.0991 100 LEU A CD2 
818  N  N   . ASP A 101 ? 0.1785 0.0750 0.2188 -0.0070 0.0041  -0.0034 101 ASP A N   
819  C  CA  . ASP A 101 ? 0.2081 0.0784 0.2074 -0.0156 -0.0137 0.0096  101 ASP A CA  
820  C  C   . ASP A 101 ? 0.2155 0.0430 0.2027 -0.0010 -0.0054 0.0200  101 ASP A C   
821  O  O   . ASP A 101 ? 0.2408 0.0680 0.2180 -0.0012 0.0031  0.0329  101 ASP A O   
822  C  CB  . ASP A 101 ? 0.2148 0.0872 0.2187 -0.0326 -0.0192 0.0513  101 ASP A CB  
823  C  CG  . ASP A 101 ? 0.2375 0.0987 0.2533 0.0043  -0.0249 0.0055  101 ASP A CG  
824  O  OD1 . ASP A 101 ? 0.2640 0.0865 0.2106 -0.0283 -0.0197 0.0076  101 ASP A OD1 
825  O  OD2 . ASP A 101 ? 0.3533 0.1571 0.2852 -0.0869 -0.0756 0.0163  101 ASP A OD2 
826  N  N   . GLY A 102 ? 0.2250 0.0591 0.2081 -0.0307 -0.0344 0.0348  102 GLY A N   
827  C  CA  . GLY A 102 ? 0.2400 0.0917 0.2281 -0.0264 -0.0340 0.0262  102 GLY A CA  
828  C  C   . GLY A 102 ? 0.1921 0.0673 0.2090 0.0226  -0.0105 -0.0017 102 GLY A C   
829  O  O   . GLY A 102 ? 0.2171 0.0907 0.1932 -0.0097 -0.0028 0.0377  102 GLY A O   
830  N  N   . GLN A 103 ? 0.1796 0.0465 0.2052 0.0005  -0.0028 0.0178  103 GLN A N   
831  C  CA  . GLN A 103 ? 0.1662 0.0411 0.1639 0.0038  -0.0236 -0.0077 103 GLN A CA  
832  C  C   . GLN A 103 ? 0.1703 0.0682 0.1341 -0.0024 -0.0185 -0.0046 103 GLN A C   
833  O  O   . GLN A 103 ? 0.1850 0.0463 0.1615 -0.0104 -0.0082 -0.0107 103 GLN A O   
834  C  CB  . GLN A 103 ? 0.2214 0.0549 0.1833 0.0126  0.0065  0.0131  103 GLN A CB  
835  C  CG  . GLN A 103 ? 0.2070 0.0761 0.2156 0.0351  0.0472  0.0104  103 GLN A CG  
836  C  CD  . GLN A 103 ? 0.2241 0.1244 0.2410 0.0317  0.0573  0.0719  103 GLN A CD  
837  O  OE1 . GLN A 103 ? 0.3446 0.2992 0.3321 0.1140  0.0881  0.1230  103 GLN A OE1 
838  N  NE2 . GLN A 103 ? 0.2067 0.1226 0.2069 0.0383  0.0228  0.0309  103 GLN A NE2 
839  N  N   . GLY A 104 ? 0.1640 0.0531 0.1381 0.0211  -0.0174 -0.0200 104 GLY A N   
840  C  CA  . GLY A 104 ? 0.1562 0.0405 0.1219 0.0054  0.0077  0.0131  104 GLY A CA  
841  C  C   . GLY A 104 ? 0.1395 0.0610 0.1539 -0.0001 -0.0282 0.0131  104 GLY A C   
842  O  O   . GLY A 104 ? 0.1366 0.0619 0.1304 -0.0171 -0.0020 0.0066  104 GLY A O   
843  N  N   . SER A 105 ? 0.1379 0.0644 0.1375 -0.0006 -0.0116 -0.0035 105 SER A N   
844  C  CA  . SER A 105 ? 0.1532 0.0450 0.0820 -0.0093 -0.0070 -0.0087 105 SER A CA  
845  C  C   . SER A 105 ? 0.1453 0.0594 0.1129 -0.0065 -0.0038 -0.0073 105 SER A C   
846  O  O   . SER A 105 ? 0.1538 0.0305 0.1375 0.0089  -0.0250 0.0000  105 SER A O   
847  C  CB  . SER A 105 ? 0.1527 0.0640 0.1013 -0.0049 0.0065  0.0331  105 SER A CB  
848  O  OG  . SER A 105 ? 0.1611 0.0361 0.1415 -0.0136 -0.0043 0.0108  105 SER A OG  
849  N  N   . GLU A 106 ? 0.1500 0.0280 0.0998 0.0054  -0.0207 -0.0111 106 GLU A N   
850  C  CA  . GLU A 106 ? 0.1365 0.0497 0.1025 -0.0178 -0.0165 0.0132  106 GLU A CA  
851  C  C   . GLU A 106 ? 0.1349 0.0456 0.0887 0.0052  -0.0024 -0.0262 106 GLU A C   
852  O  O   . GLU A 106 ? 0.1284 0.0533 0.1217 0.0019  -0.0234 -0.0041 106 GLU A O   
853  C  CB  . GLU A 106 ? 0.1401 0.0317 0.0900 -0.0142 -0.0100 0.0170  106 GLU A CB  
854  C  CG  . GLU A 106 ? 0.1817 0.0512 0.1194 -0.0331 0.0307  0.0066  106 GLU A CG  
855  C  CD  . GLU A 106 ? 0.1043 0.0916 0.1331 -0.0187 -0.0147 0.0491  106 GLU A CD  
856  O  OE1 . GLU A 106 ? 0.1149 0.0429 0.1650 0.0078  -0.0285 -0.0071 106 GLU A OE1 
857  O  OE2 . GLU A 106 ? 0.1389 0.0494 0.1659 -0.0073 -0.0013 -0.0107 106 GLU A OE2 
858  N  N   . HIS A 107 ? 0.1334 0.0464 0.1216 0.0038  0.0010  -0.0006 107 HIS A N   
859  C  CA  . HIS A 107 ? 0.1278 0.0255 0.1306 -0.0051 0.0083  -0.0001 107 HIS A CA  
860  C  C   . HIS A 107 ? 0.1485 0.0257 0.1207 -0.0052 -0.0108 0.0049  107 HIS A C   
861  O  O   . HIS A 107 ? 0.1219 0.0468 0.1367 0.0010  -0.0208 0.0175  107 HIS A O   
862  C  CB  . HIS A 107 ? 0.1305 0.0524 0.1176 0.0054  0.0040  -0.0188 107 HIS A CB  
863  C  CG  . HIS A 107 ? 0.1165 0.0271 0.1122 -0.0080 -0.0085 0.0000  107 HIS A CG  
864  N  ND1 . HIS A 107 ? 0.1254 0.0461 0.0794 0.0082  -0.0164 0.0068  107 HIS A ND1 
865  C  CD2 . HIS A 107 ? 0.1086 0.0416 0.1212 0.0198  -0.0164 -0.0265 107 HIS A CD2 
866  C  CE1 . HIS A 107 ? 0.1207 0.0357 0.1308 -0.0015 -0.0502 -0.0277 107 HIS A CE1 
867  N  NE2 . HIS A 107 ? 0.1270 0.0278 0.1336 0.0021  -0.0216 -0.0153 107 HIS A NE2 
868  N  N   . THR A 108 ? 0.1344 0.0472 0.1151 -0.0060 0.0013  0.0229  108 THR A N   
869  C  CA  . THR A 108 ? 0.1432 0.0430 0.1548 0.0000  -0.0021 0.0476  108 THR A CA  
870  C  C   . THR A 108 ? 0.1544 0.0447 0.1106 0.0096  -0.0192 0.0259  108 THR A C   
871  O  O   . THR A 108 ? 0.1560 0.0570 0.1098 0.0035  -0.0113 0.0098  108 THR A O   
872  C  CB  . THR A 108 ? 0.1700 0.0867 0.1266 0.0175  -0.0241 0.0265  108 THR A CB  
873  O  OG1 . THR A 108 ? 0.1611 0.0527 0.1327 0.0115  -0.0262 0.0120  108 THR A OG1 
874  C  CG2 . THR A 108 ? 0.1675 0.0707 0.1544 -0.0093 0.0074  0.0135  108 THR A CG2 
875  N  N   . VAL A 109 ? 0.1423 0.0395 0.1671 -0.0152 -0.0252 0.0313  109 VAL A N   
876  C  CA  . VAL A 109 ? 0.1641 0.0639 0.1445 -0.0024 -0.0038 0.0491  109 VAL A CA  
877  C  C   . VAL A 109 ? 0.1842 0.0761 0.1714 -0.0210 -0.0035 0.0289  109 VAL A C   
878  O  O   . VAL A 109 ? 0.1946 0.0571 0.1552 -0.0155 0.0120  0.0222  109 VAL A O   
879  C  CB  . VAL A 109 ? 0.1608 0.0803 0.1984 -0.0143 0.0030  0.0447  109 VAL A CB  
880  C  CG1 . VAL A 109 ? 0.1647 0.0939 0.1990 -0.0087 0.0248  0.0439  109 VAL A CG1 
881  C  CG2 . VAL A 109 ? 0.2018 0.0691 0.1560 0.0230  -0.0171 0.0461  109 VAL A CG2 
882  N  N   . ASP A 110 ? 0.2196 0.0509 0.1296 0.0212  0.0008  0.0326  110 ASP A N   
883  C  CA  . ASP A 110 ? 0.2263 0.0724 0.1527 0.0161  0.0288  0.0489  110 ASP A CA  
884  C  C   . ASP A 110 ? 0.2304 0.0649 0.1715 0.0346  0.0226  0.0096  110 ASP A C   
885  O  O   . ASP A 110 ? 0.2257 0.0582 0.1997 0.0227  -0.0186 0.0335  110 ASP A O   
886  C  CB  . ASP A 110 ? 0.2630 0.0799 0.1718 0.0227  0.0562  0.0588  110 ASP A CB  
887  C  CG  . ASP A 110 ? 0.2651 0.0944 0.1544 0.0208  0.0483  0.0724  110 ASP A CG  
888  O  OD1 . ASP A 110 ? 0.2678 0.1086 0.2367 0.0348  0.0428  0.0439  110 ASP A OD1 
889  O  OD2 . ASP A 110 ? 0.2542 0.1568 0.2802 0.0183  0.0478  0.0746  110 ASP A OD2 
890  N  N   . LYS A 111 ? 0.1905 0.0756 0.1298 0.0121  -0.0034 0.0320  111 LYS A N   
891  C  CA  . LYS A 111 ? 0.2171 0.0673 0.1512 0.0222  -0.0225 0.0231  111 LYS A CA  
892  C  C   . LYS A 111 ? 0.1918 0.0452 0.1508 0.0102  -0.0237 0.0259  111 LYS A C   
893  O  O   . LYS A 111 ? 0.1912 0.0856 0.1934 0.0141  0.0085  0.0136  111 LYS A O   
894  C  CB  . LYS A 111 ? 0.2512 0.0991 0.2099 0.0434  -0.0665 0.0494  111 LYS A CB  
895  C  CG  . LYS A 111 ? 0.2854 0.1359 0.2088 0.0542  -0.0527 0.0063  111 LYS A CG  
896  C  CD  . LYS A 111 ? 0.2666 0.2504 0.3206 -0.0052 -0.0595 -0.0390 111 LYS A CD  
897  C  CE  . LYS A 111 ? 0.3204 0.2498 0.2947 0.0333  -0.0628 0.0140  111 LYS A CE  
898  N  NZ  . LYS A 111 ? 0.3265 0.3095 0.3569 0.0348  -0.1086 0.0390  111 LYS A NZ  
899  N  N   . LYS A 112 ? 0.1599 0.0454 0.1492 0.0125  -0.0151 0.0223  112 LYS A N   
900  C  CA  . LYS A 112 ? 0.1914 0.0773 0.1508 0.0107  -0.0057 0.0060  112 LYS A CA  
901  C  C   . LYS A 112 ? 0.1605 0.0628 0.1162 0.0207  -0.0153 0.0005  112 LYS A C   
902  O  O   . LYS A 112 ? 0.1711 0.0490 0.1722 0.0155  -0.0207 -0.0211 112 LYS A O   
903  C  CB  . LYS A 112 ? 0.2115 0.1169 0.1754 -0.0295 -0.0250 -0.0015 112 LYS A CB  
904  C  CG  . LYS A 112 ? 0.2047 0.1431 0.2137 -0.0151 -0.0118 -0.0483 112 LYS A CG  
905  C  CD  . LYS A 112 ? 0.2239 0.1986 0.2345 -0.0008 -0.0324 -0.0089 112 LYS A CD  
906  C  CE  . LYS A 112 ? 0.2921 0.1286 0.2141 -0.0035 0.0149  -0.0054 112 LYS A CE  
907  N  NZ  . LYS A 112 ? 0.3467 0.1410 0.2255 -0.0027 -0.0706 0.0210  112 LYS A NZ  
908  N  N   A LYS A 113 ? 0.1729 0.0479 0.1201 0.0280  -0.0065 0.0088  113 LYS A N   
909  N  N   B LYS A 113 ? 0.1611 0.0558 0.1120 0.0098  -0.0078 0.0074  113 LYS A N   
910  C  CA  A LYS A 113 ? 0.1788 0.0640 0.1119 0.0157  0.0041  0.0100  113 LYS A CA  
911  C  CA  B LYS A 113 ? 0.1667 0.0320 0.1421 0.0087  -0.0028 0.0078  113 LYS A CA  
912  C  C   A LYS A 113 ? 0.1559 0.0336 0.1403 0.0052  0.0054  0.0087  113 LYS A C   
913  C  C   B LYS A 113 ? 0.1406 0.0474 0.1492 0.0097  -0.0024 0.0103  113 LYS A C   
914  O  O   A LYS A 113 ? 0.1853 0.0258 0.1238 -0.0041 0.0110  0.0058  113 LYS A O   
915  O  O   B LYS A 113 ? 0.1686 0.0335 0.1492 0.0109  -0.0054 0.0068  113 LYS A O   
916  C  CB  A LYS A 113 ? 0.1754 0.0335 0.1497 0.0097  0.0087  -0.0170 113 LYS A CB  
917  C  CB  B LYS A 113 ? 0.1295 0.0980 0.1269 0.0175  -0.0088 0.0390  113 LYS A CB  
918  C  CG  A LYS A 113 ? 0.1754 0.1102 0.1064 0.0171  -0.0108 0.0381  113 LYS A CG  
919  C  CG  B LYS A 113 ? 0.1374 0.0292 0.1876 0.0029  -0.0010 0.0247  113 LYS A CG  
920  C  CD  A LYS A 113 ? 0.1840 0.0485 0.1318 0.0293  0.0066  -0.0010 113 LYS A CD  
921  C  CD  B LYS A 113 ? 0.1233 0.1538 0.1746 0.0148  -0.0082 0.0063  113 LYS A CD  
922  C  CE  A LYS A 113 ? 0.1764 0.1310 0.1696 0.0289  0.0186  -0.0091 113 LYS A CE  
923  C  CE  B LYS A 113 ? 0.1803 0.2203 0.2173 -0.0129 -0.0309 -0.0074 113 LYS A CE  
924  N  NZ  A LYS A 113 ? 0.1738 0.1703 0.2124 0.0351  -0.0277 0.0000  113 LYS A NZ  
925  N  NZ  B LYS A 113 ? 0.1833 0.1700 0.2695 0.0132  -0.0274 0.0068  113 LYS A NZ  
926  N  N   . TYR A 114 ? 0.1614 0.0567 0.1304 0.0152  -0.0060 0.0071  114 TYR A N   
927  C  CA  . TYR A 114 ? 0.1546 0.0552 0.1529 0.0054  -0.0254 0.0073  114 TYR A CA  
928  C  C   . TYR A 114 ? 0.1472 0.0401 0.1561 0.0006  -0.0168 0.0115  114 TYR A C   
929  O  O   . TYR A 114 ? 0.1747 0.0427 0.1462 -0.0074 0.0026  -0.0168 114 TYR A O   
930  C  CB  . TYR A 114 ? 0.1298 0.0468 0.1682 -0.0035 0.0055  0.0040  114 TYR A CB  
931  C  CG  . TYR A 114 ? 0.1728 0.0399 0.1519 -0.0006 -0.0223 0.0168  114 TYR A CG  
932  C  CD1 . TYR A 114 ? 0.1964 0.0477 0.1871 -0.0082 0.0065  0.0441  114 TYR A CD1 
933  C  CD2 . TYR A 114 ? 0.1445 0.0493 0.1979 -0.0313 0.0107  0.0333  114 TYR A CD2 
934  C  CE1 . TYR A 114 ? 0.2446 0.0887 0.1659 -0.0065 -0.0157 0.0700  114 TYR A CE1 
935  C  CE2 . TYR A 114 ? 0.2070 0.0888 0.1797 -0.0276 0.0131  0.0121  114 TYR A CE2 
936  C  CZ  . TYR A 114 ? 0.2602 0.1074 0.1392 -0.0120 0.0436  0.0287  114 TYR A CZ  
937  O  OH  . TYR A 114 ? 0.3037 0.1614 0.2189 0.0164  0.0538  0.0293  114 TYR A OH  
938  N  N   . ALA A 115 ? 0.1893 0.0412 0.1281 -0.0209 -0.0168 0.0012  115 ALA A N   
939  C  CA  . ALA A 115 ? 0.1684 0.0266 0.1419 -0.0134 -0.0237 0.0007  115 ALA A CA  
940  C  C   . ALA A 115 ? 0.1621 0.0285 0.1345 -0.0117 -0.0094 0.0160  115 ALA A C   
941  O  O   . ALA A 115 ? 0.1632 0.0329 0.1643 -0.0165 -0.0120 0.0057  115 ALA A O   
942  C  CB  . ALA A 115 ? 0.2033 0.0567 0.1415 -0.0077 -0.0366 -0.0043 115 ALA A CB  
943  N  N   . ALA A 116 ? 0.1833 0.0346 0.1374 0.0008  -0.0340 -0.0161 116 ALA A N   
944  C  CA  . ALA A 116 ? 0.1897 0.0478 0.1018 -0.0060 0.0163  -0.0060 116 ALA A CA  
945  C  C   . ALA A 116 ? 0.1392 0.0526 0.1158 0.0027  -0.0066 0.0229  116 ALA A C   
946  O  O   . ALA A 116 ? 0.1379 0.0326 0.1203 -0.0097 -0.0249 -0.0038 116 ALA A O   
947  C  CB  . ALA A 116 ? 0.1891 0.0664 0.1203 -0.0035 -0.0346 -0.0086 116 ALA A CB  
948  N  N   . GLU A 117 ? 0.1679 0.0256 0.1080 -0.0016 -0.0133 0.0052  117 GLU A N   
949  C  CA  . GLU A 117 ? 0.1542 0.0255 0.1121 0.0048  -0.0192 -0.0010 117 GLU A CA  
950  C  C   . GLU A 117 ? 0.1468 0.0455 0.1068 -0.0206 -0.0308 0.0055  117 GLU A C   
951  O  O   . GLU A 117 ? 0.1642 0.0424 0.1319 0.0034  -0.0200 0.0137  117 GLU A O   
952  C  CB  . GLU A 117 ? 0.1544 0.0537 0.1020 0.0183  -0.0153 -0.0013 117 GLU A CB  
953  C  CG  . GLU A 117 ? 0.1448 0.0574 0.0931 0.0148  -0.0335 -0.0148 117 GLU A CG  
954  C  CD  . GLU A 117 ? 0.1444 0.0327 0.1196 0.0287  0.0102  -0.0013 117 GLU A CD  
955  O  OE1 . GLU A 117 ? 0.1195 0.0653 0.1356 0.0096  -0.0318 -0.0040 117 GLU A OE1 
956  O  OE2 . GLU A 117 ? 0.1510 0.0506 0.0998 0.0162  -0.0222 -0.0049 117 GLU A OE2 
957  N  N   . LEU A 118 ? 0.1369 0.0436 0.1340 0.0027  -0.0478 0.0170  118 LEU A N   
958  C  CA  . LEU A 118 ? 0.1659 0.0253 0.1001 0.0009  -0.0253 0.0005  118 LEU A CA  
959  C  C   . LEU A 118 ? 0.1392 0.0820 0.0987 -0.0019 -0.0098 0.0236  118 LEU A C   
960  O  O   . LEU A 118 ? 0.1450 0.0264 0.1287 -0.0029 -0.0320 0.0107  118 LEU A O   
961  C  CB  . LEU A 118 ? 0.1388 0.0322 0.1508 0.0088  -0.0339 0.0240  118 LEU A CB  
962  C  CG  . LEU A 118 ? 0.1695 0.0424 0.1464 0.0032  -0.0412 0.0421  118 LEU A CG  
963  C  CD1 . LEU A 118 ? 0.2124 0.0415 0.1409 -0.0054 -0.0286 0.0288  118 LEU A CD1 
964  C  CD2 . LEU A 118 ? 0.1485 0.0782 0.1412 0.0054  -0.0469 0.0115  118 LEU A CD2 
965  N  N   . HIS A 119 ? 0.1377 0.0258 0.1083 0.0015  -0.0224 0.0060  119 HIS A N   
966  C  CA  . HIS A 119 ? 0.1147 0.0535 0.1111 0.0024  -0.0277 -0.0087 119 HIS A CA  
967  C  C   . HIS A 119 ? 0.1271 0.0293 0.0887 -0.0073 -0.0133 0.0049  119 HIS A C   
968  O  O   . HIS A 119 ? 0.1447 0.0401 0.1098 0.0013  -0.0019 -0.0015 119 HIS A O   
969  C  CB  . HIS A 119 ? 0.1212 0.0511 0.1097 0.0088  -0.0295 0.0057  119 HIS A CB  
970  C  CG  . HIS A 119 ? 0.1275 0.0439 0.1428 -0.0001 -0.0471 0.0008  119 HIS A CG  
971  N  ND1 . HIS A 119 ? 0.1562 0.0314 0.1001 -0.0277 -0.0258 0.0091  119 HIS A ND1 
972  C  CD2 . HIS A 119 ? 0.1785 0.0309 0.0943 -0.0085 -0.0068 -0.0183 119 HIS A CD2 
973  C  CE1 . HIS A 119 ? 0.1291 0.0385 0.1086 -0.0233 -0.0270 -0.0017 119 HIS A CE1 
974  N  NE2 . HIS A 119 ? 0.1396 0.0441 0.1263 0.0065  -0.0329 -0.0082 119 HIS A NE2 
975  N  N   . LEU A 120 ? 0.1369 0.0327 0.1002 -0.0113 -0.0243 0.0008  120 LEU A N   
976  C  CA  . LEU A 120 ? 0.1475 0.0253 0.1104 -0.0012 -0.0331 0.0007  120 LEU A CA  
977  C  C   . LEU A 120 ? 0.1268 0.0336 0.0973 0.0175  -0.0281 -0.0048 120 LEU A C   
978  O  O   . LEU A 120 ? 0.1432 0.0277 0.1139 -0.0117 -0.0320 0.0129  120 LEU A O   
979  C  CB  . LEU A 120 ? 0.1368 0.0322 0.1742 0.0043  -0.0390 0.0098  120 LEU A CB  
980  C  CG  . LEU A 120 ? 0.1868 0.0578 0.1321 -0.0436 -0.0417 -0.0099 120 LEU A CG  
981  C  CD1 . LEU A 120 ? 0.2079 0.1043 0.1658 -0.0764 -0.0335 0.0264  120 LEU A CD1 
982  C  CD2 . LEU A 120 ? 0.1739 0.1309 0.1527 0.0071  -0.0913 0.0066  120 LEU A CD2 
983  N  N   . VAL A 121 ? 0.1364 0.0277 0.1282 -0.0109 -0.0326 0.0143  121 VAL A N   
984  C  CA  . VAL A 121 ? 0.1764 0.0357 0.1077 -0.0148 -0.0116 -0.0087 121 VAL A CA  
985  C  C   . VAL A 121 ? 0.1528 0.0300 0.0992 -0.0186 -0.0008 0.0120  121 VAL A C   
986  O  O   . VAL A 121 ? 0.1796 0.0458 0.1062 0.0034  -0.0342 -0.0024 121 VAL A O   
987  C  CB  . VAL A 121 ? 0.1466 0.0307 0.1256 -0.0147 -0.0118 -0.0021 121 VAL A CB  
988  C  CG1 . VAL A 121 ? 0.1507 0.0491 0.1485 -0.0175 -0.0120 -0.0060 121 VAL A CG1 
989  C  CG2 . VAL A 121 ? 0.1468 0.0567 0.1190 0.0096  -0.0208 0.0103  121 VAL A CG2 
990  N  N   . HIS A 122 ? 0.1521 0.0263 0.1181 -0.0080 -0.0154 -0.0058 122 HIS A N   
991  C  CA  . HIS A 122 ? 0.1385 0.0298 0.1298 -0.0176 -0.0300 -0.0082 122 HIS A CA  
992  C  C   . HIS A 122 ? 0.1551 0.0385 0.1122 -0.0131 -0.0097 0.0088  122 HIS A C   
993  O  O   . HIS A 122 ? 0.1688 0.0326 0.1501 -0.0142 -0.0432 0.0104  122 HIS A O   
994  C  CB  . HIS A 122 ? 0.1601 0.0436 0.1725 0.0116  -0.0074 0.0065  122 HIS A CB  
995  C  CG  . HIS A 122 ? 0.1567 0.0526 0.1413 -0.0469 -0.0303 0.0031  122 HIS A CG  
996  N  ND1 . HIS A 122 ? 0.1483 0.0344 0.1597 0.0038  -0.0102 0.0210  122 HIS A ND1 
997  C  CD2 . HIS A 122 ? 0.1587 0.0437 0.1432 -0.0010 -0.0346 0.0124  122 HIS A CD2 
998  C  CE1 . HIS A 122 ? 0.1314 0.0581 0.1968 0.0147  -0.0239 0.0015  122 HIS A CE1 
999  N  NE2 . HIS A 122 ? 0.1334 0.0631 0.1688 -0.0229 -0.0322 -0.0085 122 HIS A NE2 
1000 N  N   . TRP A 123 ? 0.1507 0.0335 0.1456 -0.0015 -0.0190 -0.0059 123 TRP A N   
1001 C  CA  . TRP A 123 ? 0.1709 0.0357 0.1327 0.0035  -0.0278 -0.0007 123 TRP A CA  
1002 C  C   . TRP A 123 ? 0.1590 0.0323 0.1290 -0.0077 -0.0076 0.0141  123 TRP A C   
1003 O  O   . TRP A 123 ? 0.1709 0.0430 0.1696 0.0015  -0.0362 -0.0017 123 TRP A O   
1004 C  CB  . TRP A 123 ? 0.1886 0.0576 0.1636 -0.0296 -0.0177 0.0065  123 TRP A CB  
1005 C  CG  . TRP A 123 ? 0.2070 0.0687 0.1711 -0.0124 -0.0242 0.0164  123 TRP A CG  
1006 C  CD1 . TRP A 123 ? 0.2173 0.0619 0.1210 -0.0390 -0.0136 0.0098  123 TRP A CD1 
1007 C  CD2 . TRP A 123 ? 0.2442 0.0804 0.1627 -0.0222 -0.0173 -0.0043 123 TRP A CD2 
1008 N  NE1 . TRP A 123 ? 0.2705 0.0526 0.1454 -0.0295 -0.0399 0.0027  123 TRP A NE1 
1009 C  CE2 . TRP A 123 ? 0.2737 0.0781 0.1664 -0.0160 -0.0627 0.0041  123 TRP A CE2 
1010 C  CE3 . TRP A 123 ? 0.2615 0.0419 0.1835 -0.0379 -0.0070 0.0408  123 TRP A CE3 
1011 C  CZ2 . TRP A 123 ? 0.3335 0.1104 0.1307 -0.0129 0.0089  0.0340  123 TRP A CZ2 
1012 C  CZ3 . TRP A 123 ? 0.3144 0.0505 0.1633 -0.0445 -0.0390 0.0114  123 TRP A CZ3 
1013 C  CH2 . TRP A 123 ? 0.3008 0.0351 0.2058 -0.0285 -0.0313 0.0126  123 TRP A CH2 
1014 N  N   . ASN A 124 ? 0.1658 0.0648 0.1423 -0.0104 -0.0328 -0.0162 124 ASN A N   
1015 C  CA  . ASN A 124 ? 0.1666 0.0261 0.1545 0.0088  -0.0162 -0.0063 124 ASN A CA  
1016 C  C   . ASN A 124 ? 0.1806 0.0474 0.1897 -0.0070 -0.0214 -0.0130 124 ASN A C   
1017 O  O   . ASN A 124 ? 0.1747 0.0513 0.1523 -0.0129 -0.0077 -0.0120 124 ASN A O   
1018 C  CB  . ASN A 124 ? 0.1711 0.0585 0.1486 0.0198  0.0083  -0.0043 124 ASN A CB  
1019 C  CG  . ASN A 124 ? 0.1767 0.0415 0.1923 -0.0144 -0.0023 -0.0012 124 ASN A CG  
1020 O  OD1 . ASN A 124 ? 0.2090 0.0355 0.2137 0.0381  0.0032  -0.0103 124 ASN A OD1 
1021 N  ND2 . ASN A 124 ? 0.2540 0.0561 0.1758 -0.0020 0.0032  -0.0076 124 ASN A ND2 
1022 N  N   . THR A 125 ? 0.1758 0.0533 0.1997 0.0192  -0.0168 0.0020  125 THR A N   
1023 C  CA  . THR A 125 ? 0.2070 0.0707 0.2314 0.0182  -0.0344 -0.0098 125 THR A CA  
1024 C  C   . THR A 125 ? 0.2349 0.1045 0.2519 0.0355  -0.0184 0.0010  125 THR A C   
1025 O  O   . THR A 125 ? 0.2508 0.0315 0.2478 0.0231  -0.0368 -0.0006 125 THR A O   
1026 C  CB  . THR A 125 ? 0.2045 0.1195 0.2422 0.0294  -0.0443 -0.0100 125 THR A CB  
1027 O  OG1 . THR A 125 ? 0.2515 0.1306 0.3138 0.0399  0.0057  -0.0071 125 THR A OG1 
1028 C  CG2 . THR A 125 ? 0.2410 0.1185 0.2742 0.0046  -0.0696 -0.0122 125 THR A CG2 
1029 N  N   . LYS A 126 ? 0.2173 0.0317 0.2162 0.0159  0.0107  -0.0251 127 LYS A N   
1030 C  CA  . LYS A 126 ? 0.2705 0.0998 0.2018 0.0003  0.0071  -0.0452 127 LYS A CA  
1031 C  C   . LYS A 126 ? 0.2281 0.0461 0.2012 0.0020  -0.0216 -0.0118 127 LYS A C   
1032 O  O   . LYS A 126 ? 0.2842 0.0824 0.3046 -0.0175 -0.0126 -0.0443 127 LYS A O   
1033 C  CB  . LYS A 126 ? 0.3102 0.0901 0.2234 -0.0035 -0.0071 -0.0377 127 LYS A CB  
1034 C  CG  . LYS A 126 ? 0.3046 0.0867 0.1921 -0.0007 -0.0013 -0.0118 127 LYS A CG  
1035 C  CD  . LYS A 126 ? 0.3981 0.2336 0.1987 -0.0799 -0.0209 -0.0231 127 LYS A CD  
1036 C  CE  . LYS A 126 ? 0.3876 0.4039 0.3565 0.0093  -0.0270 -0.0405 127 LYS A CE  
1037 N  NZ  . LYS A 126 ? 0.5526 0.4756 0.3370 -0.0144 0.0000  0.0007  127 LYS A NZ  
1038 N  N   . TYR A 127 ? 0.2144 0.0636 0.1606 0.0028  -0.0099 -0.0059 128 TYR A N   
1039 C  CA  . TYR A 127 ? 0.2346 0.0499 0.1693 0.0065  -0.0305 -0.0046 128 TYR A CA  
1040 C  C   . TYR A 127 ? 0.2356 0.0349 0.1873 0.0060  -0.0171 -0.0091 128 TYR A C   
1041 O  O   . TYR A 127 ? 0.2379 0.0630 0.2038 0.0184  -0.0362 -0.0021 128 TYR A O   
1042 C  CB  . TYR A 127 ? 0.2292 0.0433 0.1932 0.0092  -0.0142 -0.0351 128 TYR A CB  
1043 C  CG  . TYR A 127 ? 0.2381 0.0639 0.1565 0.0046  -0.0148 -0.0133 128 TYR A CG  
1044 C  CD1 . TYR A 127 ? 0.2415 0.0428 0.2062 0.0024  -0.0098 -0.0472 128 TYR A CD1 
1045 C  CD2 . TYR A 127 ? 0.1857 0.0731 0.1968 -0.0078 -0.0381 0.0164  128 TYR A CD2 
1046 C  CE1 . TYR A 127 ? 0.2718 0.0481 0.2055 -0.0062 -0.0577 0.0130  128 TYR A CE1 
1047 C  CE2 . TYR A 127 ? 0.2045 0.0822 0.1833 0.0260  -0.0281 -0.0250 128 TYR A CE2 
1048 C  CZ  . TYR A 127 ? 0.2019 0.0834 0.1643 0.0207  -0.0104 -0.0175 128 TYR A CZ  
1049 O  OH  . TYR A 127 ? 0.3226 0.1009 0.1691 0.0406  -0.0337 -0.0491 128 TYR A OH  
1050 N  N   . GLY A 128 ? 0.2257 0.0503 0.1835 -0.0010 -0.0281 0.0242  129 GLY A N   
1051 C  CA  . GLY A 128 ? 0.2699 0.0364 0.1858 -0.0094 -0.0003 0.0243  129 GLY A CA  
1052 C  C   . GLY A 128 ? 0.2624 0.0310 0.1794 -0.0086 -0.0148 0.0230  129 GLY A C   
1053 O  O   . GLY A 128 ? 0.3190 0.0650 0.1749 0.0186  -0.0454 0.0218  129 GLY A O   
1054 N  N   . ASP A 129 ? 0.2606 0.0759 0.1905 0.0141  -0.0214 -0.0017 130 ASP A N   
1055 C  CA  . ASP A 129 ? 0.3050 0.0436 0.1897 0.0205  -0.0074 0.0030  130 ASP A CA  
1056 C  C   . ASP A 129 ? 0.2797 0.0852 0.1684 0.0071  -0.0504 -0.0005 130 ASP A C   
1057 O  O   . ASP A 129 ? 0.3241 0.0605 0.1652 0.0136  -0.0370 0.0021  130 ASP A O   
1058 C  CB  . ASP A 129 ? 0.2990 0.1032 0.2328 0.0423  -0.0062 0.0140  130 ASP A CB  
1059 C  CG  . ASP A 129 ? 0.2789 0.0416 0.2343 0.0548  0.0270  0.0049  130 ASP A CG  
1060 O  OD1 . ASP A 129 ? 0.4520 0.1342 0.2720 -0.1059 -0.0666 0.0003  130 ASP A OD1 
1061 O  OD2 . ASP A 129 ? 0.3750 0.2209 0.3292 -0.0087 0.0966  0.0298  130 ASP A OD2 
1062 N  N   . PHE A 130 ? 0.3101 0.0710 0.1729 0.0120  -0.0108 -0.0013 131 PHE A N   
1063 C  CA  . PHE A 130 ? 0.2548 0.0661 0.1617 -0.0041 -0.0171 -0.0148 131 PHE A CA  
1064 C  C   . PHE A 130 ? 0.2558 0.0874 0.1670 -0.0153 0.0115  0.0010  131 PHE A C   
1065 O  O   . PHE A 130 ? 0.2446 0.0670 0.1539 -0.0275 0.0000  -0.0103 131 PHE A O   
1066 C  CB  . PHE A 130 ? 0.2688 0.0461 0.1849 0.0177  -0.0130 -0.0188 131 PHE A CB  
1067 C  CG  . PHE A 130 ? 0.2074 0.0591 0.1513 0.0031  -0.0057 -0.0242 131 PHE A CG  
1068 C  CD1 . PHE A 130 ? 0.1979 0.0816 0.1263 -0.0287 0.0030  -0.0126 131 PHE A CD1 
1069 C  CD2 . PHE A 130 ? 0.2781 0.0861 0.1975 -0.0144 0.0410  -0.0361 131 PHE A CD2 
1070 C  CE1 . PHE A 130 ? 0.2587 0.0912 0.1853 -0.0178 -0.0198 -0.0427 131 PHE A CE1 
1071 C  CE2 . PHE A 130 ? 0.2469 0.1274 0.2083 0.0472  0.0071  -0.0428 131 PHE A CE2 
1072 C  CZ  . PHE A 130 ? 0.2832 0.1221 0.2367 -0.0054 -0.0040 -0.0280 131 PHE A CZ  
1073 N  N   . GLY A 131 ? 0.2836 0.0874 0.1957 -0.0474 0.0263  -0.0030 132 GLY A N   
1074 C  CA  . GLY A 131 ? 0.2797 0.0910 0.1933 -0.0542 0.0373  0.0000  132 GLY A CA  
1075 C  C   . GLY A 131 ? 0.2540 0.1119 0.1811 -0.0388 0.0445  0.0251  132 GLY A C   
1076 O  O   . GLY A 131 ? 0.2381 0.1086 0.2486 -0.0132 0.0179  -0.0237 132 GLY A O   
1077 N  N   . LYS A 132 ? 0.2383 0.0606 0.2126 -0.0454 0.0417  0.0000  133 LYS A N   
1078 C  CA  . LYS A 132 ? 0.2551 0.0668 0.2224 -0.0423 0.0111  0.0041  133 LYS A CA  
1079 C  C   . LYS A 132 ? 0.2202 0.0772 0.2081 -0.0373 -0.0100 -0.0005 133 LYS A C   
1080 O  O   . LYS A 132 ? 0.2266 0.0901 0.1876 -0.0430 -0.0205 -0.0148 133 LYS A O   
1081 C  CB  . LYS A 132 ? 0.2541 0.0759 0.2446 -0.0329 -0.0066 -0.0003 133 LYS A CB  
1082 C  CG  . LYS A 132 ? 0.2939 0.1034 0.2986 -0.0188 -0.0183 0.0659  133 LYS A CG  
1083 C  CD  . LYS A 132 ? 0.3579 0.1510 0.4332 -0.0034 -0.0212 0.1064  133 LYS A CD  
1084 C  CE  . LYS A 132 ? 0.3716 0.1580 0.4506 -0.0714 -0.0348 0.0606  133 LYS A CE  
1085 N  NZ  . LYS A 132 ? 0.4944 0.3578 0.4721 0.0157  -0.0313 -0.0436 133 LYS A NZ  
1086 N  N   . ALA A 133 ? 0.1943 0.0684 0.1864 -0.0573 0.0015  -0.0130 134 ALA A N   
1087 C  CA  . ALA A 133 ? 0.2033 0.0698 0.1526 -0.0236 -0.0038 0.0176  134 ALA A CA  
1088 C  C   . ALA A 133 ? 0.1733 0.1011 0.1257 -0.0364 0.0020  0.0081  134 ALA A C   
1089 O  O   . ALA A 133 ? 0.1722 0.1000 0.1413 -0.0144 -0.0197 0.0041  134 ALA A O   
1090 C  CB  . ALA A 133 ? 0.1846 0.0861 0.1466 -0.0641 -0.0170 -0.0065 134 ALA A CB  
1091 N  N   . VAL A 134 ? 0.1941 0.0764 0.1374 -0.0430 0.0089  0.0115  135 VAL A N   
1092 C  CA  . VAL A 134 ? 0.2124 0.1004 0.1425 -0.0242 0.0000  0.0247  135 VAL A CA  
1093 C  C   . VAL A 134 ? 0.2011 0.1028 0.1890 -0.0331 0.0107  0.0176  135 VAL A C   
1094 O  O   . VAL A 134 ? 0.1914 0.1041 0.2019 -0.0241 0.0373  0.0162  135 VAL A O   
1095 C  CB  . VAL A 134 ? 0.2489 0.1351 0.1523 -0.0317 0.0130  0.0054  135 VAL A CB  
1096 C  CG1 . VAL A 134 ? 0.2559 0.1792 0.1600 -0.0670 -0.0189 -0.0026 135 VAL A CG1 
1097 C  CG2 . VAL A 134 ? 0.2368 0.1072 0.1621 -0.0390 0.0274  0.0096  135 VAL A CG2 
1098 N  N   A GLN A 135 ? 0.1923 0.0891 0.1928 -0.0315 0.0078  -0.0081 136 GLN A N   
1099 N  N   B GLN A 135 ? 0.1858 0.0904 0.1736 -0.0291 0.0133  -0.0174 136 GLN A N   
1100 C  CA  A GLN A 135 ? 0.1968 0.1077 0.2117 -0.0388 -0.0020 0.0074  136 GLN A CA  
1101 C  CA  B GLN A 135 ? 0.1904 0.1079 0.1851 -0.0333 0.0017  0.0000  136 GLN A CA  
1102 C  C   A GLN A 135 ? 0.1957 0.0895 0.2069 -0.0244 -0.0127 -0.0088 136 GLN A C   
1103 C  C   B GLN A 135 ? 0.1914 0.0932 0.1916 -0.0211 -0.0105 -0.0168 136 GLN A C   
1104 O  O   A GLN A 135 ? 0.1851 0.1031 0.2446 -0.0370 -0.0463 -0.0137 136 GLN A O   
1105 O  O   B GLN A 135 ? 0.1632 0.1349 0.2223 -0.0296 -0.0423 0.0006  136 GLN A O   
1106 C  CB  A GLN A 135 ? 0.1745 0.1104 0.2234 -0.0322 0.0041  0.0125  136 GLN A CB  
1107 C  CB  B GLN A 135 ? 0.1918 0.0886 0.1713 -0.0401 0.0156  -0.0254 136 GLN A CB  
1108 C  CG  A GLN A 135 ? 0.2206 0.1405 0.2706 -0.0604 0.0300  0.0491  136 GLN A CG  
1109 C  CG  B GLN A 135 ? 0.2347 0.1403 0.1794 -0.0277 0.0068  0.0073  136 GLN A CG  
1110 C  CD  A GLN A 135 ? 0.1958 0.2313 0.3105 -0.0777 -0.0023 0.0333  136 GLN A CD  
1111 C  CD  B GLN A 135 ? 0.2551 0.2073 0.2228 -0.0628 -0.0030 -0.0010 136 GLN A CD  
1112 O  OE1 A GLN A 135 ? 0.3731 0.3668 0.2955 -0.0689 -0.0038 0.0803  136 GLN A OE1 
1113 O  OE1 B GLN A 135 ? 0.2482 0.2137 0.2738 -0.0688 -0.0130 0.0188  136 GLN A OE1 
1114 N  NE2 A GLN A 135 ? 0.3258 0.2745 0.3582 -0.0328 0.0091  0.0653  136 GLN A NE2 
1115 N  NE2 B GLN A 135 ? 0.2209 0.1804 0.2890 -0.0697 0.0038  0.0216  136 GLN A NE2 
1116 N  N   . GLN A 136 ? 0.1652 0.0847 0.1946 -0.0070 0.0085  -0.0065 137 GLN A N   
1117 C  CA  . GLN A 136 ? 0.1714 0.0984 0.1622 0.0091  -0.0071 -0.0311 137 GLN A CA  
1118 C  C   . GLN A 136 ? 0.1692 0.1075 0.1627 0.0021  -0.0357 -0.0236 137 GLN A C   
1119 O  O   . GLN A 136 ? 0.1943 0.0958 0.1296 -0.0010 -0.0379 -0.0299 137 GLN A O   
1120 C  CB  . GLN A 136 ? 0.1908 0.0610 0.1840 0.0017  -0.0189 0.0000  137 GLN A CB  
1121 C  CG  . GLN A 136 ? 0.2658 0.1203 0.2352 0.0127  0.0183  0.0126  137 GLN A CG  
1122 C  CD  . GLN A 136 ? 0.2633 0.1961 0.3436 0.0000  0.0044  0.0579  137 GLN A CD  
1123 O  OE1 . GLN A 136 ? 0.3073 0.1335 0.3023 -0.0007 -0.0496 -0.0920 137 GLN A OE1 
1124 N  NE2 . GLN A 136 ? 0.3999 0.2243 0.4641 0.0229  0.0152  0.1383  137 GLN A NE2 
1125 N  N   . PRO A 137 ? 0.1781 0.1307 0.1489 0.0060  -0.0194 -0.0286 138 PRO A N   
1126 C  CA  . PRO A 137 ? 0.2011 0.1332 0.1365 0.0051  -0.0425 -0.0108 138 PRO A CA  
1127 C  C   . PRO A 137 ? 0.1828 0.1172 0.1801 -0.0059 -0.0373 -0.0152 138 PRO A C   
1128 O  O   . PRO A 137 ? 0.2471 0.0958 0.2234 0.0115  -0.0174 0.0194  138 PRO A O   
1129 C  CB  . PRO A 137 ? 0.2465 0.1652 0.1425 0.0447  -0.0197 -0.0231 138 PRO A CB  
1130 C  CG  . PRO A 137 ? 0.3113 0.2185 0.1847 -0.0239 -0.0253 -0.0244 138 PRO A CG  
1131 C  CD  . PRO A 137 ? 0.2109 0.1689 0.1627 -0.0397 -0.0631 -0.0436 138 PRO A CD  
1132 N  N   . ASP A 138 ? 0.1722 0.0969 0.1444 0.0059  -0.0373 -0.0168 139 ASP A N   
1133 C  CA  . ASP A 138 ? 0.1714 0.0982 0.1526 0.0160  0.0010  -0.0120 139 ASP A CA  
1134 C  C   . ASP A 138 ? 0.1704 0.0643 0.1483 -0.0031 -0.0089 -0.0115 139 ASP A C   
1135 O  O   . ASP A 138 ? 0.1555 0.0967 0.1521 0.0012  -0.0167 -0.0119 139 ASP A O   
1136 C  CB  . ASP A 138 ? 0.2081 0.1054 0.1688 0.0015  0.0120  -0.0160 139 ASP A CB  
1137 C  CG  . ASP A 138 ? 0.1911 0.1604 0.1561 0.0005  -0.0248 -0.0364 139 ASP A CG  
1138 O  OD1 . ASP A 138 ? 0.2282 0.1046 0.1894 0.0410  -0.0144 -0.0546 139 ASP A OD1 
1139 O  OD2 . ASP A 138 ? 0.2277 0.1731 0.2142 0.0527  0.0245  -0.0505 139 ASP A OD2 
1140 N  N   . GLY A 139 ? 0.1647 0.0646 0.1284 -0.0021 -0.0027 -0.0188 140 GLY A N   
1141 C  CA  . GLY A 139 ? 0.1817 0.0639 0.1246 -0.0195 -0.0237 -0.0096 140 GLY A CA  
1142 C  C   . GLY A 139 ? 0.1418 0.0488 0.1195 -0.0131 -0.0118 0.0026  140 GLY A C   
1143 O  O   . GLY A 139 ? 0.1682 0.0428 0.1270 0.0097  -0.0281 -0.0065 140 GLY A O   
1144 N  N   . LEU A 140 ? 0.1307 0.0280 0.1341 -0.0151 -0.0167 -0.0048 141 LEU A N   
1145 C  CA  . LEU A 140 ? 0.1297 0.0292 0.1158 -0.0192 -0.0100 -0.0034 141 LEU A CA  
1146 C  C   . LEU A 140 ? 0.1270 0.0278 0.1318 0.0085  0.0008  0.0043  141 LEU A C   
1147 O  O   . LEU A 140 ? 0.1625 0.0401 0.1439 -0.0071 -0.0333 -0.0038 141 LEU A O   
1148 C  CB  . LEU A 140 ? 0.1544 0.0468 0.1342 -0.0038 -0.0225 -0.0241 141 LEU A CB  
1149 C  CG  . LEU A 140 ? 0.1970 0.0930 0.1639 0.0269  0.0472  0.0247  141 LEU A CG  
1150 C  CD1 . LEU A 140 ? 0.1598 0.0855 0.1527 0.0087  0.0154  0.0031  141 LEU A CD1 
1151 C  CD2 . LEU A 140 ? 0.3190 0.0840 0.2648 0.0160  0.0436  0.0172  141 LEU A CD2 
1152 N  N   . ALA A 141 ? 0.1313 0.0344 0.1368 -0.0054 -0.0283 -0.0248 142 ALA A N   
1153 C  CA  . ALA A 141 ? 0.1393 0.0306 0.1323 -0.0238 0.0056  0.0041  142 ALA A CA  
1154 C  C   . ALA A 141 ? 0.1622 0.0670 0.1250 -0.0109 -0.0348 0.0138  142 ALA A C   
1155 O  O   . ALA A 141 ? 0.1613 0.0297 0.1219 0.0065  -0.0194 0.0111  142 ALA A O   
1156 C  CB  . ALA A 141 ? 0.1418 0.0648 0.1475 -0.0215 -0.0071 0.0125  142 ALA A CB  
1157 N  N   . VAL A 142 ? 0.1466 0.0339 0.1473 -0.0214 -0.0230 0.0027  143 VAL A N   
1158 C  CA  . VAL A 142 ? 0.1499 0.0295 0.1101 -0.0181 -0.0097 0.0051  143 VAL A CA  
1159 C  C   . VAL A 142 ? 0.1640 0.0278 0.1010 -0.0067 0.0112  0.0120  143 VAL A C   
1160 O  O   . VAL A 142 ? 0.1349 0.0301 0.1036 -0.0017 -0.0171 -0.0038 143 VAL A O   
1161 C  CB  . VAL A 142 ? 0.1331 0.0552 0.0926 0.0161  -0.0125 -0.0159 143 VAL A CB  
1162 C  CG1 . VAL A 142 ? 0.1616 0.0486 0.1149 0.0114  -0.0188 -0.0164 143 VAL A CG1 
1163 C  CG2 . VAL A 142 ? 0.1453 0.0991 0.0885 -0.0450 -0.0038 0.0175  143 VAL A CG2 
1164 N  N   . LEU A 143 ? 0.1220 0.0273 0.1310 -0.0136 -0.0228 0.0008  144 LEU A N   
1165 C  CA  . LEU A 143 ? 0.1436 0.0390 0.1430 0.0024  -0.0388 -0.0127 144 LEU A CA  
1166 C  C   . LEU A 143 ? 0.1361 0.0706 0.1076 -0.0261 -0.0065 -0.0113 144 LEU A C   
1167 O  O   . LEU A 143 ? 0.1532 0.0389 0.1362 -0.0077 -0.0186 0.0001  144 LEU A O   
1168 C  CB  . LEU A 143 ? 0.1438 0.0635 0.1801 0.0015  -0.0320 0.0044  144 LEU A CB  
1169 C  CG  . LEU A 143 ? 0.1377 0.0822 0.1613 -0.0038 -0.0305 0.0000  144 LEU A CG  
1170 C  CD1 . LEU A 143 ? 0.1521 0.1614 0.1886 -0.0313 -0.0362 0.0394  144 LEU A CD1 
1171 C  CD2 . LEU A 143 ? 0.1448 0.1106 0.2345 -0.0146 -0.0540 0.0171  144 LEU A CD2 
1172 N  N   . GLY A 144 ? 0.1353 0.0262 0.1260 -0.0061 -0.0177 -0.0064 145 GLY A N   
1173 C  CA  . GLY A 144 ? 0.1260 0.0287 0.1611 -0.0140 -0.0036 -0.0132 145 GLY A CA  
1174 C  C   . GLY A 144 ? 0.1001 0.0605 0.1467 0.0074  -0.0012 0.0114  145 GLY A C   
1175 O  O   . GLY A 144 ? 0.1340 0.0447 0.1376 -0.0104 -0.0137 -0.0076 145 GLY A O   
1176 N  N   . ILE A 145 ? 0.1396 0.0287 0.1208 0.0000  -0.0176 0.0068  146 ILE A N   
1177 C  CA  . ILE A 145 ? 0.1152 0.0403 0.1422 0.0024  -0.0465 0.0059  146 ILE A CA  
1178 C  C   . ILE A 145 ? 0.1265 0.0636 0.1421 -0.0140 -0.0241 0.0054  146 ILE A C   
1179 O  O   . ILE A 145 ? 0.1601 0.0320 0.1544 -0.0198 -0.0251 -0.0021 146 ILE A O   
1180 C  CB  . ILE A 145 ? 0.1448 0.0578 0.1363 -0.0143 -0.0281 -0.0077 146 ILE A CB  
1181 C  CG1 . ILE A 145 ? 0.1738 0.0417 0.1578 0.0233  -0.0370 -0.0121 146 ILE A CG1 
1182 C  CG2 . ILE A 145 ? 0.1582 0.0767 0.1682 -0.0013 -0.0410 -0.0105 146 ILE A CG2 
1183 C  CD1 . ILE A 145 ? 0.1714 0.0605 0.1403 0.0103  -0.0417 0.0206  146 ILE A CD1 
1184 N  N   . PHE A 146 ? 0.1422 0.0260 0.1285 0.0068  -0.0359 0.0028  147 PHE A N   
1185 C  CA  . PHE A 146 ? 0.1552 0.0327 0.1115 0.0126  -0.0362 -0.0017 147 PHE A CA  
1186 C  C   . PHE A 146 ? 0.1456 0.0403 0.1542 -0.0062 -0.0109 0.0174  147 PHE A C   
1187 O  O   . PHE A 146 ? 0.1351 0.0446 0.1670 -0.0038 -0.0217 -0.0152 147 PHE A O   
1188 C  CB  . PHE A 146 ? 0.1361 0.0287 0.1173 0.0000  -0.0269 0.0169  147 PHE A CB  
1189 C  CG  . PHE A 146 ? 0.1553 0.0340 0.1067 -0.0040 -0.0171 0.0208  147 PHE A CG  
1190 C  CD1 . PHE A 146 ? 0.1440 0.0311 0.1583 0.0029  -0.0072 0.0273  147 PHE A CD1 
1191 C  CD2 . PHE A 146 ? 0.1591 0.0625 0.1387 -0.0006 -0.0339 0.0324  147 PHE A CD2 
1192 C  CE1 . PHE A 146 ? 0.1907 0.0515 0.1261 -0.0089 -0.0399 -0.0008 147 PHE A CE1 
1193 C  CE2 . PHE A 146 ? 0.1273 0.0483 0.1413 -0.0185 -0.0176 0.0315  147 PHE A CE2 
1194 C  CZ  . PHE A 146 ? 0.1224 0.0522 0.1664 -0.0062 -0.0331 0.0322  147 PHE A CZ  
1195 N  N   . LEU A 147 ? 0.1554 0.0401 0.1192 -0.0037 0.0003  0.0008  148 LEU A N   
1196 C  CA  . LEU A 147 ? 0.1960 0.0265 0.1291 -0.0112 -0.0443 -0.0033 148 LEU A CA  
1197 C  C   . LEU A 147 ? 0.1721 0.0452 0.1525 -0.0147 -0.0364 0.0118  148 LEU A C   
1198 O  O   . LEU A 147 ? 0.1574 0.0417 0.1516 -0.0173 -0.0220 -0.0006 148 LEU A O   
1199 C  CB  . LEU A 147 ? 0.1916 0.0490 0.1454 0.0001  -0.0236 0.0074  148 LEU A CB  
1200 C  CG  . LEU A 147 ? 0.2117 0.0296 0.1569 -0.0173 -0.0458 0.0206  148 LEU A CG  
1201 C  CD1 . LEU A 147 ? 0.2403 0.0257 0.1369 -0.0011 -0.0321 -0.0067 148 LEU A CD1 
1202 C  CD2 . LEU A 147 ? 0.2268 0.0538 0.1462 -0.0258 -0.0571 0.0038  148 LEU A CD2 
1203 N  N   . LYS A 148 ? 0.1782 0.0372 0.1729 -0.0175 -0.0377 -0.0208 149 LYS A N   
1204 C  CA  . LYS A 148 ? 0.1804 0.0331 0.1666 -0.0065 -0.0427 -0.0141 149 LYS A CA  
1205 C  C   . LYS A 148 ? 0.1880 0.0786 0.1858 -0.0142 -0.0480 -0.0173 149 LYS A C   
1206 O  O   . LYS A 148 ? 0.2102 0.0779 0.1729 0.0137  -0.0472 -0.0267 149 LYS A O   
1207 C  CB  . LYS A 148 ? 0.1873 0.1004 0.1693 -0.0197 -0.0357 0.0286  149 LYS A CB  
1208 C  CG  . LYS A 148 ? 0.2196 0.0944 0.2217 -0.0060 -0.0043 0.0531  149 LYS A CG  
1209 C  CD  . LYS A 148 ? 0.2951 0.1343 0.2597 -0.0282 -0.0068 0.0381  149 LYS A CD  
1210 C  CE  . LYS A 148 ? 0.3418 0.3317 0.3104 -0.0621 0.0097  0.0932  149 LYS A CE  
1211 N  NZ  . LYS A 148 ? 0.4020 0.4243 0.3680 -0.0861 0.0275  0.0749  149 LYS A NZ  
1212 N  N   . VAL A 149 ? 0.2275 0.0442 0.1758 0.0034  -0.0516 -0.0260 150 VAL A N   
1213 C  CA  . VAL A 149 ? 0.1984 0.0819 0.1950 -0.0200 -0.0304 -0.0280 150 VAL A CA  
1214 C  C   . VAL A 149 ? 0.2099 0.0794 0.1941 -0.0132 -0.0364 -0.0263 150 VAL A C   
1215 O  O   . VAL A 149 ? 0.2460 0.0969 0.2001 -0.0214 -0.0474 0.0175  150 VAL A O   
1216 C  CB  . VAL A 149 ? 0.2020 0.0921 0.1611 -0.0052 -0.0104 -0.0129 150 VAL A CB  
1217 C  CG1 . VAL A 149 ? 0.2205 0.1151 0.1961 0.0109  -0.0516 -0.0153 150 VAL A CG1 
1218 C  CG2 . VAL A 149 ? 0.2108 0.1414 0.2343 -0.0384 -0.0197 -0.0175 150 VAL A CG2 
1219 N  N   . GLY A 150 ? 0.1858 0.0594 0.2009 -0.0172 -0.0670 -0.0303 151 GLY A N   
1220 C  CA  . GLY A 150 ? 0.1871 0.1150 0.2331 -0.0531 -0.0687 0.0043  151 GLY A CA  
1221 C  C   . GLY A 150 ? 0.1882 0.0955 0.2115 -0.0353 -0.0441 0.0020  151 GLY A C   
1222 O  O   . GLY A 150 ? 0.2091 0.0943 0.2108 -0.0304 -0.0527 -0.0211 151 GLY A O   
1223 N  N   A SER A 151 ? 0.1973 0.0969 0.2257 -0.0359 -0.0359 -0.0054 152 SER A N   
1224 N  N   B SER A 151 ? 0.2027 0.1028 0.2274 -0.0272 -0.0373 -0.0038 152 SER A N   
1225 C  CA  A SER A 151 ? 0.2051 0.0966 0.2152 -0.0163 -0.0293 0.0076  152 SER A CA  
1226 C  CA  B SER A 151 ? 0.2091 0.0962 0.2210 -0.0035 -0.0264 0.0208  152 SER A CA  
1227 C  C   A SER A 151 ? 0.2117 0.0740 0.1878 -0.0318 -0.0447 -0.0132 152 SER A C   
1228 C  C   B SER A 151 ? 0.2224 0.0840 0.2045 -0.0127 -0.0392 0.0024  152 SER A C   
1229 O  O   A SER A 151 ? 0.1647 0.1057 0.1815 -0.0223 -0.0463 -0.0476 152 SER A O   
1230 O  O   B SER A 151 ? 0.2141 0.1030 0.1936 0.0031  -0.0417 -0.0012 152 SER A O   
1231 C  CB  A SER A 151 ? 0.2235 0.1641 0.2536 -0.0441 -0.0189 -0.0046 152 SER A CB  
1232 C  CB  B SER A 151 ? 0.2289 0.1665 0.2566 -0.0276 -0.0138 0.0038  152 SER A CB  
1233 O  OG  A SER A 151 ? 0.2516 0.2025 0.2120 -0.0234 -0.0487 -0.0176 152 SER A OG  
1234 O  OG  B SER A 151 ? 0.2134 0.2054 0.2688 0.0020  -0.0239 0.0798  152 SER A OG  
1235 N  N   . ALA A 152 ? 0.2349 0.0903 0.1814 -0.0119 -0.0498 0.0015  153 ALA A N   
1236 C  CA  . ALA A 152 ? 0.2264 0.0930 0.1718 -0.0114 -0.0538 -0.0087 153 ALA A CA  
1237 C  C   . ALA A 152 ? 0.2040 0.0980 0.1770 -0.0124 -0.0421 -0.0188 153 ALA A C   
1238 O  O   . ALA A 152 ? 0.2238 0.0935 0.2363 -0.0071 -0.0244 -0.0214 153 ALA A O   
1239 C  CB  . ALA A 152 ? 0.2580 0.1213 0.1621 -0.0071 -0.0557 -0.0252 153 ALA A CB  
1240 N  N   . LYS A 153 ? 0.2338 0.0679 0.2069 -0.0188 -0.0698 -0.0094 154 LYS A N   
1241 C  CA  . LYS A 153 ? 0.2242 0.0964 0.1952 0.0085  -0.0522 -0.0019 154 LYS A CA  
1242 C  C   . LYS A 153 ? 0.1839 0.1176 0.1846 -0.0089 -0.0478 -0.0060 154 LYS A C   
1243 O  O   . LYS A 153 ? 0.1948 0.1002 0.1624 -0.0364 -0.0566 -0.0165 154 LYS A O   
1244 C  CB  . LYS A 153 ? 0.2345 0.0750 0.1840 -0.0038 -0.0737 -0.0149 154 LYS A CB  
1245 C  CG  . LYS A 153 ? 0.2465 0.1034 0.2187 -0.0281 -0.0754 -0.0220 154 LYS A CG  
1246 C  CD  . LYS A 153 ? 0.3098 0.0958 0.2212 -0.0037 -0.0329 -0.0285 154 LYS A CD  
1247 C  CE  . LYS A 153 ? 0.3510 0.1643 0.2002 0.0401  -0.0648 -0.0190 154 LYS A CE  
1248 N  NZ  . LYS A 153 ? 0.3389 0.1814 0.2395 0.0220  -0.0230 -0.0247 154 LYS A NZ  
1249 N  N   . PRO A 154 ? 0.2048 0.1160 0.2113 -0.0082 -0.0555 0.0057  155 PRO A N   
1250 C  CA  . PRO A 154 ? 0.2008 0.1361 0.2407 -0.0196 -0.0631 0.0233  155 PRO A CA  
1251 C  C   . PRO A 154 ? 0.2085 0.1527 0.2304 -0.0076 -0.0680 0.0142  155 PRO A C   
1252 O  O   . PRO A 154 ? 0.2518 0.1739 0.2128 -0.0065 -0.0573 0.0160  155 PRO A O   
1253 C  CB  . PRO A 154 ? 0.2009 0.1580 0.2921 -0.0046 -0.0654 0.0278  155 PRO A CB  
1254 C  CG  . PRO A 154 ? 0.2293 0.2309 0.2820 -0.0288 -0.0483 0.0551  155 PRO A CG  
1255 C  CD  . PRO A 154 ? 0.2187 0.1633 0.2363 -0.0026 -0.0373 0.0292  155 PRO A CD  
1256 N  N   . GLY A 155 ? 0.2135 0.1099 0.2246 -0.0007 -0.0507 -0.0109 156 GLY A N   
1257 C  CA  . GLY A 155 ? 0.2325 0.1255 0.2523 -0.0071 -0.0469 0.0065  156 GLY A CA  
1258 C  C   . GLY A 155 ? 0.2494 0.1108 0.2271 -0.0197 -0.0425 0.0184  156 GLY A C   
1259 O  O   . GLY A 155 ? 0.2858 0.0773 0.2971 -0.0048 -0.0546 0.0322  156 GLY A O   
1260 N  N   . LEU A 156 ? 0.2216 0.1143 0.2034 -0.0074 -0.0625 -0.0148 157 LEU A N   
1261 C  CA  . LEU A 156 ? 0.2266 0.0829 0.1613 -0.0211 -0.0625 0.0000  157 LEU A CA  
1262 C  C   . LEU A 156 ? 0.2426 0.0768 0.1914 -0.0162 -0.0579 -0.0135 157 LEU A C   
1263 O  O   . LEU A 156 ? 0.2419 0.0831 0.1665 -0.0381 -0.0766 0.0012  157 LEU A O   
1264 C  CB  . LEU A 156 ? 0.2140 0.0851 0.1724 -0.0147 -0.0741 0.0113  157 LEU A CB  
1265 C  CG  . LEU A 156 ? 0.1871 0.1048 0.1810 -0.0108 -0.0522 -0.0164 157 LEU A CG  
1266 C  CD1 . LEU A 156 ? 0.2493 0.1020 0.1882 -0.0300 -0.0658 -0.0019 157 LEU A CD1 
1267 C  CD2 . LEU A 156 ? 0.2213 0.0869 0.1553 0.0046  -0.0562 0.0226  157 LEU A CD2 
1268 N  N   . GLN A 157 ? 0.2515 0.0922 0.1770 -0.0337 -0.0759 -0.0130 158 GLN A N   
1269 C  CA  . GLN A 157 ? 0.2518 0.1349 0.1868 -0.0474 -0.0675 -0.0258 158 GLN A CA  
1270 C  C   . GLN A 157 ? 0.2460 0.1228 0.1632 -0.0275 -0.0747 -0.0326 158 GLN A C   
1271 O  O   . GLN A 157 ? 0.2549 0.1070 0.1954 -0.0254 -0.0802 -0.0078 158 GLN A O   
1272 C  CB  . GLN A 157 ? 0.2799 0.1124 0.1871 -0.0747 -0.0756 -0.0313 158 GLN A CB  
1273 C  CG  . GLN A 157 ? 0.3001 0.1334 0.2133 -0.0250 -0.0443 -0.0226 158 GLN A CG  
1274 C  CD  . GLN A 157 ? 0.2814 0.1016 0.2054 -0.0491 -0.0322 0.0012  158 GLN A CD  
1275 O  OE1 . GLN A 157 ? 0.3425 0.1005 0.1826 -0.0417 -0.0634 0.0046  158 GLN A OE1 
1276 N  NE2 . GLN A 157 ? 0.3054 0.1409 0.1925 -0.0460 -0.0366 -0.0331 158 GLN A NE2 
1277 N  N   . LYS A 158 ? 0.2475 0.1319 0.1959 -0.0520 -0.0763 -0.0126 159 LYS A N   
1278 C  CA  . LYS A 158 ? 0.2177 0.1309 0.2073 -0.0275 -0.0485 0.0032  159 LYS A CA  
1279 C  C   . LYS A 158 ? 0.2329 0.1111 0.1631 -0.0305 -0.0377 0.0104  159 LYS A C   
1280 O  O   . LYS A 158 ? 0.2662 0.1456 0.1517 -0.0478 -0.0454 0.0040  159 LYS A O   
1281 C  CB  . LYS A 158 ? 0.2444 0.1793 0.2298 0.0027  -0.0518 0.0122  159 LYS A CB  
1282 C  CG  . LYS A 158 ? 0.3411 0.2871 0.2807 -0.0285 -0.0610 0.0026  159 LYS A CG  
1283 C  CD  . LYS A 158 ? 0.2677 0.2547 0.2657 -0.0038 -0.0234 0.0000  159 LYS A CD  
1284 C  CE  . LYS A 158 ? 0.2545 0.2368 0.2390 -0.0013 -0.0230 0.0015  159 LYS A CE  
1285 N  NZ  . LYS A 158 ? 0.2516 0.2451 0.2462 0.0003  -0.0074 0.0035  159 LYS A NZ  
1286 N  N   . VAL A 159 ? 0.2595 0.1133 0.1836 -0.0006 -0.0744 -0.0177 160 VAL A N   
1287 C  CA  . VAL A 159 ? 0.2442 0.0967 0.1616 -0.0233 -0.0366 -0.0065 160 VAL A CA  
1288 C  C   . VAL A 159 ? 0.2544 0.1219 0.1122 -0.0104 -0.0394 -0.0059 160 VAL A C   
1289 O  O   . VAL A 159 ? 0.2644 0.0949 0.1671 -0.0146 -0.0586 -0.0175 160 VAL A O   
1290 C  CB  . VAL A 159 ? 0.2644 0.1092 0.1465 -0.0114 -0.0366 0.0089  160 VAL A CB  
1291 C  CG1 . VAL A 159 ? 0.2067 0.1533 0.1915 -0.0364 -0.0189 0.0031  160 VAL A CG1 
1292 C  CG2 . VAL A 159 ? 0.2853 0.0808 0.1912 0.0277  -0.0264 -0.0419 160 VAL A CG2 
1293 N  N   . VAL A 160 ? 0.2630 0.0700 0.1615 -0.0184 -0.0456 -0.0026 161 VAL A N   
1294 C  CA  . VAL A 160 ? 0.2849 0.1104 0.2001 -0.0003 -0.0166 0.0046  161 VAL A CA  
1295 C  C   . VAL A 160 ? 0.2831 0.1075 0.2155 -0.0258 -0.0221 -0.0122 161 VAL A C   
1296 O  O   . VAL A 160 ? 0.3203 0.1225 0.1875 -0.0502 -0.0094 -0.0288 161 VAL A O   
1297 C  CB  . VAL A 160 ? 0.3501 0.0873 0.2087 0.0073  0.0024  -0.0028 161 VAL A CB  
1298 C  CG1 . VAL A 160 ? 0.2867 0.1638 0.2630 -0.0679 -0.0465 -0.0007 161 VAL A CG1 
1299 C  CG2 . VAL A 160 ? 0.3288 0.1360 0.2370 0.0119  -0.0024 0.0203  161 VAL A CG2 
1300 N  N   . ASP A 161 ? 0.3077 0.1453 0.1772 -0.0313 -0.0491 -0.0077 162 ASP A N   
1301 C  CA  . ASP A 161 ? 0.3140 0.1722 0.1966 -0.0494 -0.0612 -0.0137 162 ASP A CA  
1302 C  C   . ASP A 161 ? 0.3447 0.2069 0.1739 -0.0560 -0.0571 0.0184  162 ASP A C   
1303 O  O   . ASP A 161 ? 0.3970 0.2374 0.2542 -0.0731 -0.0419 -0.0149 162 ASP A O   
1304 C  CB  . ASP A 161 ? 0.3438 0.2099 0.2178 -0.0331 -0.0454 0.0019  162 ASP A CB  
1305 C  CG  . ASP A 161 ? 0.3529 0.2203 0.2807 -0.0249 -0.0326 -0.0263 162 ASP A CG  
1306 O  OD1 . ASP A 161 ? 0.3823 0.2361 0.2712 -0.0419 -0.0680 -0.0603 162 ASP A OD1 
1307 O  OD2 . ASP A 161 ? 0.3955 0.2180 0.2436 -0.0146 -0.0656 -0.0566 162 ASP A OD2 
1308 N  N   . VAL A 162 ? 0.3022 0.1499 0.1539 -0.0610 -0.0684 0.0055  163 VAL A N   
1309 C  CA  . VAL A 162 ? 0.3087 0.1631 0.1756 -0.0406 -0.0483 0.0102  163 VAL A CA  
1310 C  C   . VAL A 162 ? 0.3041 0.1507 0.1440 -0.0280 -0.0305 0.0175  163 VAL A C   
1311 O  O   . VAL A 162 ? 0.3216 0.1620 0.1457 -0.0417 -0.0291 0.0043  163 VAL A O   
1312 C  CB  . VAL A 162 ? 0.3194 0.1804 0.2225 -0.0267 -0.0302 0.0049  163 VAL A CB  
1313 C  CG1 . VAL A 162 ? 0.3249 0.1231 0.2478 -0.0204 -0.0518 0.0230  163 VAL A CG1 
1314 C  CG2 . VAL A 162 ? 0.3252 0.1936 0.1944 -0.0284 -0.0080 -0.0100 163 VAL A CG2 
1315 N  N   . LEU A 163 ? 0.3237 0.1402 0.1876 -0.0269 -0.0480 -0.0055 164 LEU A N   
1316 C  CA  . LEU A 163 ? 0.2975 0.1049 0.1660 -0.0019 -0.0220 0.0021  164 LEU A CA  
1317 C  C   . LEU A 163 ? 0.3215 0.1447 0.1592 -0.0093 -0.0248 -0.0044 164 LEU A C   
1318 O  O   . LEU A 163 ? 0.3129 0.1523 0.1605 -0.0052 -0.0078 -0.0122 164 LEU A O   
1319 C  CB  . LEU A 163 ? 0.3101 0.0900 0.1618 0.0038  -0.0244 0.0024  164 LEU A CB  
1320 C  CG  . LEU A 163 ? 0.3206 0.0912 0.1228 -0.0126 -0.0282 0.0073  164 LEU A CG  
1321 C  CD1 . LEU A 163 ? 0.3029 0.1158 0.1930 0.0010  -0.0223 0.0116  164 LEU A CD1 
1322 C  CD2 . LEU A 163 ? 0.2734 0.1217 0.1520 -0.0375 -0.0500 -0.0055 164 LEU A CD2 
1323 N  N   . ASP A 164 ? 0.3736 0.1826 0.1606 -0.0350 -0.0096 -0.0284 165 ASP A N   
1324 C  CA  . ASP A 164 ? 0.3948 0.2153 0.2099 -0.0423 0.0020  -0.0243 165 ASP A CA  
1325 C  C   . ASP A 164 ? 0.3863 0.2462 0.2088 -0.0295 -0.0032 -0.0093 165 ASP A C   
1326 O  O   . ASP A 164 ? 0.4390 0.2598 0.2432 0.0003  0.0196  -0.0159 165 ASP A O   
1327 C  CB  . ASP A 164 ? 0.4417 0.2358 0.2087 -0.0432 -0.0127 -0.0289 165 ASP A CB  
1328 C  CG  . ASP A 164 ? 0.4505 0.3519 0.3036 -0.0381 -0.0214 -0.0414 165 ASP A CG  
1329 O  OD1 . ASP A 164 ? 0.5595 0.3592 0.3212 -0.0551 0.0287  -0.0307 165 ASP A OD1 
1330 O  OD2 . ASP A 164 ? 0.5674 0.5303 0.3375 -0.0516 0.0692  -0.0346 165 ASP A OD2 
1331 N  N   . SER A 165 ? 0.3482 0.1968 0.1616 -0.0329 -0.0373 0.0203  166 SER A N   
1332 C  CA  . SER A 165 ? 0.3501 0.2130 0.1840 -0.0133 -0.0295 0.0115  166 SER A CA  
1333 C  C   . SER A 165 ? 0.3417 0.1623 0.1587 -0.0260 -0.0186 0.0165  166 SER A C   
1334 O  O   . SER A 165 ? 0.3675 0.1862 0.1826 -0.0513 0.0104  0.0399  166 SER A O   
1335 C  CB  . SER A 165 ? 0.3819 0.2529 0.2594 -0.0211 -0.0005 0.0196  166 SER A CB  
1336 O  OG  . SER A 165 ? 0.3941 0.1986 0.2644 0.0129  -0.0421 0.0204  166 SER A OG  
1337 N  N   . ILE A 166 ? 0.3201 0.1473 0.1341 0.0060  -0.0355 0.0085  167 ILE A N   
1338 C  CA  . ILE A 166 ? 0.2971 0.1016 0.1689 -0.0055 0.0087  0.0154  167 ILE A CA  
1339 C  C   . ILE A 166 ? 0.2612 0.1213 0.1525 -0.0010 0.0071  -0.0006 167 ILE A C   
1340 O  O   . ILE A 166 ? 0.2450 0.1376 0.1609 -0.0204 0.0008  0.0083  167 ILE A O   
1341 C  CB  . ILE A 166 ? 0.2906 0.1212 0.1101 -0.0115 -0.0057 -0.0157 167 ILE A CB  
1342 C  CG1 . ILE A 166 ? 0.2518 0.1527 0.1113 -0.0326 0.0130  0.0167  167 ILE A CG1 
1343 C  CG2 . ILE A 166 ? 0.2962 0.1189 0.1857 0.0179  -0.0270 0.0198  167 ILE A CG2 
1344 C  CD1 . ILE A 166 ? 0.3288 0.1383 0.1286 -0.0060 0.0269  0.0073  167 ILE A CD1 
1345 N  N   . LYS A 167 ? 0.2734 0.1208 0.1771 0.0097  0.0164  0.0111  168 LYS A N   
1346 C  CA  . LYS A 167 ? 0.2583 0.1190 0.1718 0.0007  -0.0168 -0.0285 168 LYS A CA  
1347 C  C   . LYS A 167 ? 0.2442 0.1467 0.1611 0.0170  0.0159  -0.0182 168 LYS A C   
1348 O  O   . LYS A 167 ? 0.2716 0.1108 0.1632 -0.0041 -0.0135 -0.0041 168 LYS A O   
1349 C  CB  . LYS A 167 ? 0.3255 0.1077 0.1739 0.0044  -0.0035 -0.0359 168 LYS A CB  
1350 C  CG  . LYS A 167 ? 0.2856 0.1398 0.2055 -0.0010 -0.0102 -0.0351 168 LYS A CG  
1351 C  CD  . LYS A 167 ? 0.3962 0.2137 0.3116 0.0557  -0.0399 -0.0498 168 LYS A CD  
1352 C  CE  . LYS A 167 ? 0.3934 0.2429 0.4286 0.0724  -0.0015 -0.0854 168 LYS A CE  
1353 N  NZ  . LYS A 167 ? 0.4769 0.3973 0.4279 0.0131  -0.0071 -0.0696 168 LYS A NZ  
1354 N  N   . THR A 168 ? 0.2511 0.1261 0.1682 -0.0083 0.0118  0.0185  169 THR A N   
1355 C  CA  . THR A 168 ? 0.2583 0.1465 0.1885 0.0108  0.0241  0.0148  169 THR A CA  
1356 C  C   . THR A 168 ? 0.2169 0.1001 0.1482 0.0010  0.0174  0.0263  169 THR A C   
1357 O  O   . THR A 168 ? 0.2336 0.1272 0.2004 -0.0054 -0.0013 0.0443  169 THR A O   
1358 C  CB  . THR A 168 ? 0.2681 0.1458 0.2195 -0.0006 -0.0049 0.0094  169 THR A CB  
1359 O  OG1 . THR A 168 ? 0.3359 0.1724 0.1357 0.0364  0.0193  -0.0043 169 THR A OG1 
1360 C  CG2 . THR A 168 ? 0.3176 0.1298 0.1807 0.0267  0.0423  -0.0318 169 THR A CG2 
1361 N  N   . LYS A 169 ? 0.2670 0.1568 0.1645 -0.0381 0.0333  0.0154  170 LYS A N   
1362 C  CA  . LYS A 169 ? 0.2680 0.1251 0.1738 -0.0271 0.0051  0.0175  170 LYS A CA  
1363 C  C   . LYS A 169 ? 0.2489 0.1475 0.1950 -0.0286 0.0221  0.0294  170 LYS A C   
1364 O  O   . LYS A 169 ? 0.3163 0.2148 0.1846 -0.0269 0.0353  0.0035  170 LYS A O   
1365 C  CB  . LYS A 169 ? 0.2662 0.1386 0.1774 -0.0098 0.0114  0.0263  170 LYS A CB  
1366 C  CG  . LYS A 169 ? 0.2615 0.2015 0.2155 -0.0388 -0.0133 -0.0017 170 LYS A CG  
1367 C  CD  . LYS A 169 ? 0.3052 0.2246 0.2400 -0.0329 -0.0071 0.0001  170 LYS A CD  
1368 C  CE  . LYS A 169 ? 0.3754 0.3506 0.4035 -0.0500 -0.0630 -0.0410 170 LYS A CE  
1369 N  NZ  . LYS A 169 ? 0.3641 0.4532 0.4441 0.0082  -0.0568 -0.0280 170 LYS A NZ  
1370 N  N   . GLY A 170 ? 0.3028 0.1120 0.1993 -0.0351 0.0245  0.0285  171 GLY A N   
1371 C  CA  . GLY A 170 ? 0.2928 0.1342 0.2144 -0.0346 -0.0098 0.0649  171 GLY A CA  
1372 C  C   . GLY A 170 ? 0.3320 0.1685 0.2357 -0.0094 -0.0041 0.0452  171 GLY A C   
1373 O  O   . GLY A 170 ? 0.3695 0.1803 0.3036 -0.0392 -0.0063 0.0703  171 GLY A O   
1374 N  N   . LYS A 171 ? 0.3000 0.1097 0.1872 -0.0307 0.0248  0.0538  172 LYS A N   
1375 C  CA  . LYS A 171 ? 0.2919 0.1498 0.1638 -0.0071 0.0219  0.0304  172 LYS A CA  
1376 C  C   . LYS A 171 ? 0.2727 0.1257 0.1828 0.0085  0.0203  0.0219  172 LYS A C   
1377 O  O   . LYS A 171 ? 0.2748 0.1221 0.1717 0.0082  0.0154  0.0375  172 LYS A O   
1378 C  CB  . LYS A 171 ? 0.2881 0.1828 0.1790 -0.0221 0.0217  0.0342  172 LYS A CB  
1379 C  CG  . LYS A 171 ? 0.3267 0.2298 0.2020 0.0088  0.0168  -0.0074 172 LYS A CG  
1380 C  CD  . LYS A 171 ? 0.4480 0.2415 0.2803 0.0038  -0.0131 0.0244  172 LYS A CD  
1381 C  CE  . LYS A 171 ? 0.4678 0.3409 0.3378 -0.0068 -0.0546 0.0000  172 LYS A CE  
1382 N  NZ  . LYS A 171 ? 0.5044 0.2237 0.2994 -0.0046 0.0204  0.0015  172 LYS A NZ  
1383 N  N   . SER A 172 ? 0.2879 0.1481 0.1635 0.0046  0.0046  0.0337  173 SER A N   
1384 C  CA  . SER A 172 ? 0.2983 0.1512 0.1167 0.0109  0.0148  0.0218  173 SER A CA  
1385 C  C   . SER A 172 ? 0.2960 0.1603 0.1404 0.0194  0.0100  0.0445  173 SER A C   
1386 O  O   . SER A 172 ? 0.3235 0.2428 0.1304 0.0516  0.0119  0.0406  173 SER A O   
1387 C  CB  . SER A 172 ? 0.2584 0.1528 0.1333 0.0038  0.0092  0.0076  173 SER A CB  
1388 O  OG  . SER A 172 ? 0.3955 0.1677 0.1993 0.0087  0.0024  0.0524  173 SER A OG  
1389 N  N   . ALA A 173 ? 0.3000 0.1909 0.1668 0.0410  -0.0160 0.0141  174 ALA A N   
1390 C  CA  . ALA A 173 ? 0.2756 0.1882 0.1534 0.0549  -0.0302 0.0200  174 ALA A CA  
1391 C  C   . ALA A 173 ? 0.2709 0.2109 0.1702 0.0388  -0.0443 0.0020  174 ALA A C   
1392 O  O   . ALA A 173 ? 0.2867 0.1583 0.1458 0.0515  -0.0372 0.0040  174 ALA A O   
1393 C  CB  . ALA A 173 ? 0.3384 0.2029 0.1676 0.0397  -0.0282 0.0000  174 ALA A CB  
1394 N  N   . ASP A 174 ? 0.3039 0.2361 0.1831 0.0667  -0.0450 0.0493  175 ASP A N   
1395 C  CA  . ASP A 174 ? 0.3097 0.1836 0.1855 0.0480  -0.0430 0.0434  175 ASP A CA  
1396 C  C   . ASP A 174 ? 0.3016 0.1771 0.1713 0.0225  -0.0482 0.0491  175 ASP A C   
1397 O  O   . ASP A 174 ? 0.3409 0.2425 0.2117 0.0274  -0.0428 -0.0251 175 ASP A O   
1398 C  CB  . ASP A 174 ? 0.3224 0.2389 0.2389 0.0245  -0.0476 0.0670  175 ASP A CB  
1399 C  CG  . ASP A 174 ? 0.4203 0.3269 0.2957 -0.0032 -0.0493 0.0672  175 ASP A CG  
1400 O  OD1 . ASP A 174 ? 0.4660 0.4769 0.3607 -0.0214 -0.1005 0.0412  175 ASP A OD1 
1401 O  OD2 . ASP A 174 ? 0.4304 0.4193 0.2863 -0.0241 -0.0879 0.0683  175 ASP A OD2 
1402 N  N   . PHE A 175 ? 0.2714 0.1703 0.1752 0.0136  -0.0281 0.0249  176 PHE A N   
1403 C  CA  . PHE A 175 ? 0.2561 0.1536 0.1466 0.0286  -0.0445 0.0218  176 PHE A CA  
1404 C  C   . PHE A 175 ? 0.2827 0.1098 0.1819 0.0091  -0.0465 0.0006  176 PHE A C   
1405 O  O   . PHE A 175 ? 0.2961 0.1850 0.1846 0.0570  -0.0960 -0.0346 176 PHE A O   
1406 C  CB  . PHE A 175 ? 0.2936 0.0910 0.1641 0.0057  -0.0584 0.0249  176 PHE A CB  
1407 C  CG  . PHE A 175 ? 0.2735 0.0878 0.1958 -0.0023 -0.0414 0.0104  176 PHE A CG  
1408 C  CD1 . PHE A 175 ? 0.3366 0.0964 0.1853 -0.0038 -0.0137 -0.0377 176 PHE A CD1 
1409 C  CD2 . PHE A 175 ? 0.2540 0.1080 0.1969 -0.0317 -0.0794 0.0368  176 PHE A CD2 
1410 C  CE1 . PHE A 175 ? 0.3697 0.1518 0.2242 -0.0100 -0.0141 0.0052  176 PHE A CE1 
1411 C  CE2 . PHE A 175 ? 0.2820 0.1272 0.2113 0.0035  -0.0736 0.0174  176 PHE A CE2 
1412 C  CZ  . PHE A 175 ? 0.2908 0.1158 0.2195 0.0010  -0.0610 0.0059  176 PHE A CZ  
1413 N  N   . THR A 176 ? 0.2623 0.1097 0.1649 0.0350  -0.0516 0.0342  177 THR A N   
1414 C  CA  . THR A 176 ? 0.2853 0.1281 0.1750 0.0124  -0.0412 0.0476  177 THR A CA  
1415 C  C   . THR A 176 ? 0.2431 0.1174 0.1563 0.0200  -0.0568 0.0436  177 THR A C   
1416 O  O   . THR A 176 ? 0.2831 0.1147 0.1738 -0.0122 -0.0800 0.0498  177 THR A O   
1417 C  CB  . THR A 176 ? 0.2639 0.1526 0.1556 0.0099  -0.0496 0.0469  177 THR A CB  
1418 O  OG1 . THR A 176 ? 0.4106 0.1806 0.1749 0.0410  -0.0758 0.0249  177 THR A OG1 
1419 C  CG2 . THR A 176 ? 0.2763 0.1879 0.2694 0.0038  -0.0167 0.1076  177 THR A CG2 
1420 N  N   . ASN A 177 ? 0.2527 0.1099 0.1570 0.0019  -0.0644 0.0362  178 ASN A N   
1421 C  CA  . ASN A 177 ? 0.2649 0.1190 0.1703 0.0051  -0.0597 0.0439  178 ASN A CA  
1422 C  C   . ASN A 177 ? 0.2639 0.1025 0.1697 -0.0177 -0.0908 0.0249  178 ASN A C   
1423 O  O   . ASN A 177 ? 0.2732 0.1839 0.2372 -0.0127 -0.0931 0.0803  178 ASN A O   
1424 C  CB  . ASN A 177 ? 0.2757 0.0939 0.1904 -0.0148 -0.0945 0.0315  178 ASN A CB  
1425 C  CG  . ASN A 177 ? 0.2584 0.1581 0.2116 0.0263  -0.0474 0.0148  178 ASN A CG  
1426 O  OD1 . ASN A 177 ? 0.3058 0.1368 0.2623 0.0458  -0.0373 0.0505  178 ASN A OD1 
1427 N  ND2 . ASN A 177 ? 0.2530 0.1693 0.1991 0.0120  -0.0693 0.0518  178 ASN A ND2 
1428 N  N   . PHE A 178 ? 0.2698 0.0987 0.1625 -0.0087 -0.0715 0.0315  179 PHE A N   
1429 C  CA  . PHE A 178 ? 0.2917 0.1118 0.1641 -0.0093 -0.0520 0.0097  179 PHE A CA  
1430 C  C   . PHE A 178 ? 0.2888 0.0919 0.1284 -0.0115 -0.0791 0.0359  179 PHE A C   
1431 O  O   . PHE A 178 ? 0.3136 0.1034 0.1632 -0.0209 -0.0900 0.0238  179 PHE A O   
1432 C  CB  . PHE A 178 ? 0.2757 0.0797 0.1527 0.0130  -0.0421 0.0259  179 PHE A CB  
1433 C  CG  . PHE A 178 ? 0.2716 0.0714 0.1615 -0.0031 -0.0593 0.0359  179 PHE A CG  
1434 C  CD1 . PHE A 178 ? 0.2608 0.1007 0.1650 -0.0077 -0.0222 0.0166  179 PHE A CD1 
1435 C  CD2 . PHE A 178 ? 0.2164 0.1113 0.1625 -0.0021 -0.0593 0.0098  179 PHE A CD2 
1436 C  CE1 . PHE A 178 ? 0.2811 0.0919 0.1740 -0.0032 -0.0529 0.0013  179 PHE A CE1 
1437 C  CE2 . PHE A 178 ? 0.2187 0.1088 0.1527 -0.0174 -0.0432 0.0099  179 PHE A CE2 
1438 C  CZ  . PHE A 178 ? 0.2608 0.1323 0.1482 -0.0099 -0.0634 0.0320  179 PHE A CZ  
1439 N  N   . ASP A 179 ? 0.2620 0.1224 0.1785 0.0060  -0.0759 0.0320  180 ASP A N   
1440 C  CA  . ASP A 179 ? 0.2322 0.1187 0.1812 0.0127  -0.0681 0.0239  180 ASP A CA  
1441 C  C   . ASP A 179 ? 0.2055 0.0935 0.1565 -0.0024 -0.0590 0.0226  180 ASP A C   
1442 O  O   . ASP A 179 ? 0.2320 0.0824 0.1828 -0.0231 -0.0579 0.0186  180 ASP A O   
1443 C  CB  . ASP A 179 ? 0.2320 0.1561 0.2031 0.0263  -0.0715 0.0192  180 ASP A CB  
1444 C  CG  . ASP A 179 ? 0.2347 0.2213 0.2659 0.0284  -0.0432 0.0204  180 ASP A CG  
1445 O  OD1 . ASP A 179 ? 0.2461 0.1425 0.2083 0.0443  -0.0432 0.0296  180 ASP A OD1 
1446 O  OD2 . ASP A 179 ? 0.2388 0.4348 0.3413 0.0342  -0.0577 0.0176  180 ASP A OD2 
1447 N  N   . PRO A 180 ? 0.2155 0.0864 0.1475 -0.0021 -0.0590 0.0137  181 PRO A N   
1448 C  CA  . PRO A 180 ? 0.1905 0.1004 0.1482 -0.0126 -0.0575 0.0237  181 PRO A CA  
1449 C  C   . PRO A 180 ? 0.2142 0.1124 0.1515 -0.0194 -0.0491 0.0049  181 PRO A C   
1450 O  O   . PRO A 180 ? 0.2104 0.0851 0.1685 -0.0024 -0.0623 0.0253  181 PRO A O   
1451 C  CB  . PRO A 180 ? 0.1873 0.1246 0.1922 -0.0206 -0.0610 0.0041  181 PRO A CB  
1452 C  CG  . PRO A 180 ? 0.1919 0.1110 0.1812 -0.0057 -0.0438 0.0038  181 PRO A CG  
1453 C  CD  . PRO A 180 ? 0.2084 0.0851 0.1692 -0.0190 -0.0694 0.0173  181 PRO A CD  
1454 N  N   . ARG A 181 ? 0.1785 0.1016 0.1721 -0.0104 -0.0370 0.0252  182 ARG A N   
1455 C  CA  . ARG A 181 ? 0.1962 0.1140 0.1713 -0.0076 -0.0368 0.0024  182 ARG A CA  
1456 C  C   . ARG A 181 ? 0.2076 0.1124 0.1932 0.0088  -0.0601 0.0300  182 ARG A C   
1457 O  O   . ARG A 181 ? 0.2389 0.1208 0.1853 -0.0199 -0.0696 0.0309  182 ARG A O   
1458 C  CB  . ARG A 181 ? 0.1886 0.1388 0.2065 -0.0052 -0.0293 -0.0020 182 ARG A CB  
1459 C  CG  . ARG A 181 ? 0.2170 0.1293 0.2288 -0.0028 -0.0304 -0.0043 182 ARG A CG  
1460 C  CD  . ARG A 181 ? 0.2112 0.1803 0.2750 0.0285  -0.0394 0.0386  182 ARG A CD  
1461 N  NE  . ARG A 181 ? 0.1966 0.1324 0.3147 -0.0144 -0.0727 0.0612  182 ARG A NE  
1462 C  CZ  . ARG A 181 ? 0.2083 0.1930 0.2973 0.0262  -0.0003 0.0282  182 ARG A CZ  
1463 N  NH1 . ARG A 181 ? 0.2029 0.2773 0.3743 0.0913  0.0309  0.0657  182 ARG A NH1 
1464 N  NH2 . ARG A 181 ? 0.1908 0.3341 0.3075 0.0518  -0.0028 0.0650  182 ARG A NH2 
1465 N  N   . GLY A 182 ? 0.2267 0.0943 0.2025 0.0093  -0.0762 0.0162  183 GLY A N   
1466 C  CA  . GLY A 182 ? 0.2342 0.0987 0.2209 0.0076  -0.1000 0.0155  183 GLY A CA  
1467 C  C   . GLY A 182 ? 0.2289 0.1001 0.2285 0.0107  -0.0693 0.0260  183 GLY A C   
1468 O  O   . GLY A 182 ? 0.2727 0.0849 0.2328 0.0066  -0.1261 -0.0023 183 GLY A O   
1469 N  N   . LEU A 183 ? 0.2227 0.1149 0.1754 -0.0001 -0.0894 0.0302  184 LEU A N   
1470 C  CA  . LEU A 183 ? 0.2213 0.1397 0.1462 -0.0021 -0.0599 0.0120  184 LEU A CA  
1471 C  C   . LEU A 183 ? 0.2095 0.1004 0.1254 -0.0305 -0.0711 -0.0141 184 LEU A C   
1472 O  O   . LEU A 183 ? 0.2106 0.1253 0.1614 0.0043  -0.0644 0.0456  184 LEU A O   
1473 C  CB  . LEU A 183 ? 0.1998 0.1164 0.1668 -0.0001 -0.0684 0.0243  184 LEU A CB  
1474 C  CG  . LEU A 183 ? 0.1966 0.1046 0.1954 0.0262  -0.0478 0.0020  184 LEU A CG  
1475 C  CD1 . LEU A 183 ? 0.2173 0.2191 0.1911 0.0091  -0.0712 0.0555  184 LEU A CD1 
1476 C  CD2 . LEU A 183 ? 0.2889 0.1316 0.2076 0.0317  -0.0120 -0.0147 184 LEU A CD2 
1477 N  N   . LEU A 184 ? 0.2072 0.1030 0.1757 -0.0132 -0.0383 0.0098  185 LEU A N   
1478 C  CA  . LEU A 184 ? 0.1889 0.1041 0.1867 -0.0515 -0.0381 0.0313  185 LEU A CA  
1479 C  C   . LEU A 184 ? 0.2304 0.1185 0.1492 -0.0480 -0.0595 0.0450  185 LEU A C   
1480 O  O   . LEU A 184 ? 0.2847 0.1824 0.2581 -0.1030 -0.1482 0.0894  185 LEU A O   
1481 C  CB  . LEU A 184 ? 0.1668 0.1334 0.1788 -0.0417 -0.0414 0.0417  185 LEU A CB  
1482 C  CG  . LEU A 184 ? 0.1587 0.1210 0.1775 -0.0082 -0.0305 0.0192  185 LEU A CG  
1483 C  CD1 . LEU A 184 ? 0.1613 0.2070 0.2000 0.0167  -0.0200 0.0186  185 LEU A CD1 
1484 C  CD2 . LEU A 184 ? 0.1670 0.1596 0.2246 0.0057  -0.0763 -0.0130 185 LEU A CD2 
1485 N  N   . PRO A 185 ? 0.1588 0.1140 0.1490 -0.0253 -0.0452 0.0621  186 PRO A N   
1486 C  CA  . PRO A 185 ? 0.1611 0.1162 0.1729 -0.0111 -0.0207 0.0436  186 PRO A CA  
1487 C  C   . PRO A 185 ? 0.1474 0.1183 0.1811 -0.0233 -0.0412 0.0324  186 PRO A C   
1488 O  O   . PRO A 185 ? 0.1262 0.1058 0.3072 0.0041  -0.0546 0.0471  186 PRO A O   
1489 C  CB  . PRO A 185 ? 0.1609 0.0944 0.1695 -0.0063 -0.0239 0.0478  186 PRO A CB  
1490 C  CG  . PRO A 185 ? 0.1729 0.1041 0.1407 0.0113  -0.0434 0.0264  186 PRO A CG  
1491 C  CD  . PRO A 185 ? 0.1715 0.0931 0.1391 0.0074  -0.0597 -0.0132 186 PRO A CD  
1492 N  N   A GLU A 186 ? 0.1601 0.1235 0.2083 -0.0410 -0.0271 0.0522  187 GLU A N   
1493 N  N   B GLU A 186 ? 0.1721 0.1239 0.2177 -0.0392 -0.0248 0.0472  187 GLU A N   
1494 C  CA  A GLU A 186 ? 0.1525 0.1421 0.2036 -0.0348 -0.0276 0.0518  187 GLU A CA  
1495 C  CA  B GLU A 186 ? 0.1692 0.1330 0.2231 -0.0373 -0.0216 0.0368  187 GLU A CA  
1496 C  C   A GLU A 186 ? 0.1257 0.0849 0.2270 -0.0295 -0.0172 0.0368  187 GLU A C   
1497 C  C   B GLU A 186 ? 0.1548 0.0878 0.2289 -0.0272 -0.0160 0.0379  187 GLU A C   
1498 O  O   A GLU A 186 ? 0.1031 0.1456 0.2706 -0.0189 -0.0125 0.0410  187 GLU A O   
1499 O  O   B GLU A 186 ? 0.1494 0.0931 0.2946 -0.0179 -0.0242 0.0184  187 GLU A O   
1500 C  CB  A GLU A 186 ? 0.1488 0.1495 0.2446 -0.0414 -0.0209 0.0273  187 GLU A CB  
1501 C  CB  B GLU A 186 ? 0.1890 0.1664 0.2655 -0.0384 -0.0099 0.0339  187 GLU A CB  
1502 C  CG  A GLU A 186 ? 0.1800 0.1722 0.2663 -0.0388 -0.0031 0.0223  187 GLU A CG  
1503 C  CG  B GLU A 186 ? 0.2248 0.1325 0.2978 -0.0372 -0.0149 0.0249  187 GLU A CG  
1504 C  CD  A GLU A 186 ? 0.2569 0.2108 0.2742 -0.0152 0.0126  0.0331  187 GLU A CD  
1505 C  CD  B GLU A 186 ? 0.2637 0.2342 0.3158 -0.0487 -0.0111 0.0283  187 GLU A CD  
1506 O  OE1 A GLU A 186 ? 0.2853 0.2152 0.3722 -0.0108 0.0017  0.0410  187 GLU A OE1 
1507 O  OE1 B GLU A 186 ? 0.1254 0.1256 0.3380 -0.0522 -0.0377 0.0493  187 GLU A OE1 
1508 O  OE2 A GLU A 186 ? 0.2630 0.1731 0.3373 -0.0195 0.0502  0.0984  187 GLU A OE2 
1509 O  OE2 B GLU A 186 ? 0.2558 0.1948 0.4036 -0.0447 -0.0364 0.0221  187 GLU A OE2 
1510 N  N   . SER A 187 ? 0.1228 0.1264 0.2180 -0.0307 -0.0272 0.0419  188 SER A N   
1511 C  CA  . SER A 187 ? 0.1400 0.1133 0.2098 -0.0306 -0.0099 0.0364  188 SER A CA  
1512 C  C   . SER A 187 ? 0.1323 0.1301 0.2203 -0.0237 -0.0194 0.0228  188 SER A C   
1513 O  O   . SER A 187 ? 0.1493 0.1404 0.2544 -0.0256 -0.0091 -0.0057 188 SER A O   
1514 C  CB  . SER A 187 ? 0.1815 0.1442 0.2192 -0.0291 -0.0171 0.0430  188 SER A CB  
1515 O  OG  . SER A 187 ? 0.1842 0.1428 0.2406 -0.0295 -0.0303 0.0201  188 SER A OG  
1516 N  N   . LEU A 188 ? 0.1336 0.0984 0.2464 -0.0230 -0.0372 -0.0054 189 LEU A N   
1517 C  CA  . LEU A 188 ? 0.1509 0.1259 0.2624 -0.0148 -0.0328 -0.0068 189 LEU A CA  
1518 C  C   . LEU A 188 ? 0.1155 0.1441 0.2153 -0.0143 -0.0166 -0.0062 189 LEU A C   
1519 O  O   . LEU A 188 ? 0.1538 0.1411 0.2379 -0.0241 -0.0256 -0.0294 189 LEU A O   
1520 C  CB  . LEU A 188 ? 0.1565 0.1226 0.2628 -0.0219 -0.0261 0.0126  189 LEU A CB  
1521 C  CG  . LEU A 188 ? 0.1717 0.1776 0.2655 -0.0049 -0.0366 0.0088  189 LEU A CG  
1522 C  CD1 . LEU A 188 ? 0.1911 0.1455 0.2943 0.0059  -0.0141 0.0540  189 LEU A CD1 
1523 C  CD2 . LEU A 188 ? 0.1334 0.3036 0.3130 0.0137  -0.0285 0.0295  189 LEU A CD2 
1524 N  N   . ASP A 189 ? 0.1439 0.1553 0.2076 0.0024  -0.0103 -0.0300 190 ASP A N   
1525 C  CA  . ASP A 189 ? 0.1527 0.1580 0.1916 -0.0423 -0.0010 -0.0054 190 ASP A CA  
1526 C  C   . ASP A 189 ? 0.1176 0.1331 0.1491 -0.0230 -0.0024 -0.0115 190 ASP A C   
1527 O  O   . ASP A 189 ? 0.1412 0.0870 0.1624 -0.0160 -0.0068 -0.0054 190 ASP A O   
1528 C  CB  . ASP A 189 ? 0.1576 0.1641 0.1925 -0.0533 0.0318  0.0179  190 ASP A CB  
1529 C  CG  . ASP A 189 ? 0.2216 0.2824 0.2187 -0.0489 -0.0198 0.0188  190 ASP A CG  
1530 O  OD1 . ASP A 189 ? 0.1861 0.3337 0.3680 -0.0351 0.0423  -0.0285 190 ASP A OD1 
1531 O  OD2 . ASP A 189 ? 0.2153 0.3971 0.3616 -0.0989 0.0046  0.0588  190 ASP A OD2 
1532 N  N   . TYR A 190 ? 0.1334 0.1027 0.1527 -0.0071 -0.0133 0.0111  191 TYR A N   
1533 C  CA  . TYR A 190 ? 0.1068 0.0921 0.1561 -0.0149 -0.0240 0.0229  191 TYR A CA  
1534 C  C   . TYR A 190 ? 0.1493 0.0741 0.1360 0.0031  -0.0136 -0.0040 191 TYR A C   
1535 O  O   . TYR A 190 ? 0.1555 0.1010 0.1453 -0.0001 0.0074  -0.0035 191 TYR A O   
1536 C  CB  . TYR A 190 ? 0.1700 0.0785 0.1415 -0.0023 -0.0057 -0.0114 191 TYR A CB  
1537 C  CG  . TYR A 190 ? 0.1409 0.0837 0.1456 -0.0147 -0.0146 0.0366  191 TYR A CG  
1538 C  CD1 . TYR A 190 ? 0.1742 0.1005 0.1118 -0.0142 0.0027  0.0041  191 TYR A CD1 
1539 C  CD2 . TYR A 190 ? 0.1518 0.1203 0.1254 0.0208  0.0226  0.0267  191 TYR A CD2 
1540 C  CE1 . TYR A 190 ? 0.1345 0.0901 0.1815 -0.0038 0.0131  0.0226  191 TYR A CE1 
1541 C  CE2 . TYR A 190 ? 0.1731 0.1031 0.1553 -0.0160 -0.0085 -0.0126 191 TYR A CE2 
1542 C  CZ  . TYR A 190 ? 0.2187 0.0776 0.1622 -0.0015 -0.0007 0.0003  191 TYR A CZ  
1543 O  OH  . TYR A 190 ? 0.2099 0.0874 0.2020 0.0119  -0.0140 -0.0115 191 TYR A OH  
1544 N  N   . TRP A 191 ? 0.1298 0.0522 0.1374 -0.0048 -0.0281 0.0063  192 TRP A N   
1545 C  CA  . TRP A 191 ? 0.1492 0.0494 0.1530 -0.0154 -0.0111 0.0203  192 TRP A CA  
1546 C  C   . TRP A 191 ? 0.1395 0.0763 0.1023 -0.0026 0.0019  0.0035  192 TRP A C   
1547 O  O   . TRP A 191 ? 0.1548 0.0842 0.1151 -0.0103 -0.0087 -0.0062 192 TRP A O   
1548 C  CB  . TRP A 191 ? 0.1400 0.0512 0.1524 -0.0023 0.0041  0.0038  192 TRP A CB  
1549 C  CG  . TRP A 191 ? 0.1451 0.0682 0.1289 0.0138  -0.0164 0.0065  192 TRP A CG  
1550 C  CD1 . TRP A 191 ? 0.1718 0.0736 0.1736 0.0205  0.0041  0.0208  192 TRP A CD1 
1551 C  CD2 . TRP A 191 ? 0.1354 0.0693 0.1380 0.0071  -0.0165 0.0114  192 TRP A CD2 
1552 N  NE1 . TRP A 191 ? 0.1932 0.0664 0.1742 0.0109  0.0035  0.0187  192 TRP A NE1 
1553 C  CE2 . TRP A 191 ? 0.1825 0.0537 0.1749 0.0160  -0.0140 -0.0007 192 TRP A CE2 
1554 C  CE3 . TRP A 191 ? 0.1372 0.0962 0.1589 0.0007  -0.0238 -0.0052 192 TRP A CE3 
1555 C  CZ2 . TRP A 191 ? 0.1930 0.0903 0.1916 0.0010  -0.0222 0.0087  192 TRP A CZ2 
1556 C  CZ3 . TRP A 191 ? 0.1217 0.1025 0.1659 0.0080  0.0151  -0.0237 192 TRP A CZ3 
1557 C  CH2 . TRP A 191 ? 0.1598 0.1129 0.1882 -0.0170 -0.0353 -0.0119 192 TRP A CH2 
1558 N  N   . THR A 192 ? 0.1239 0.0661 0.1106 -0.0153 -0.0140 0.0006  193 THR A N   
1559 C  CA  . THR A 192 ? 0.1187 0.0578 0.1401 -0.0231 -0.0116 -0.0125 193 THR A CA  
1560 C  C   . THR A 192 ? 0.1372 0.0500 0.1266 -0.0054 -0.0030 0.0124  193 THR A C   
1561 O  O   . THR A 192 ? 0.1509 0.0637 0.1432 -0.0062 -0.0125 0.0114  193 THR A O   
1562 C  CB  . THR A 192 ? 0.1423 0.0606 0.1615 0.0152  -0.0068 0.0137  193 THR A CB  
1563 O  OG1 . THR A 192 ? 0.1530 0.0610 0.1217 0.0006  0.0041  0.0015  193 THR A OG1 
1564 C  CG2 . THR A 192 ? 0.1803 0.0754 0.1553 0.0104  0.0111  0.0152  193 THR A CG2 
1565 N  N   . TYR A 193 ? 0.1181 0.0556 0.1400 -0.0197 -0.0119 -0.0119 194 TYR A N   
1566 C  CA  . TYR A 193 ? 0.1147 0.0786 0.1217 -0.0108 -0.0108 -0.0020 194 TYR A CA  
1567 C  C   . TYR A 193 ? 0.1180 0.0843 0.1372 0.0093  -0.0141 -0.0032 194 TYR A C   
1568 O  O   . TYR A 193 ? 0.1395 0.0587 0.1264 -0.0048 -0.0406 0.0062  194 TYR A O   
1569 C  CB  . TYR A 193 ? 0.1587 0.0752 0.1310 0.0240  -0.0085 -0.0157 194 TYR A CB  
1570 C  CG  . TYR A 193 ? 0.1595 0.0456 0.1304 0.0111  -0.0210 0.0078  194 TYR A CG  
1571 C  CD1 . TYR A 193 ? 0.1623 0.0432 0.1183 0.0068  -0.0263 0.0093  194 TYR A CD1 
1572 C  CD2 . TYR A 193 ? 0.1397 0.0583 0.1507 0.0249  -0.0102 0.0068  194 TYR A CD2 
1573 C  CE1 . TYR A 193 ? 0.1235 0.0494 0.1473 -0.0003 0.0099  0.0044  194 TYR A CE1 
1574 C  CE2 . TYR A 193 ? 0.1640 0.0566 0.1282 -0.0030 -0.0309 -0.0093 194 TYR A CE2 
1575 C  CZ  . TYR A 193 ? 0.1550 0.0349 0.1254 0.0318  0.0067  -0.0115 194 TYR A CZ  
1576 O  OH  . TYR A 193 ? 0.1201 0.0389 0.1544 0.0060  -0.0164 -0.0043 194 TYR A OH  
1577 N  N   . PRO A 194 ? 0.1243 0.0734 0.1127 -0.0126 -0.0137 -0.0013 195 PRO A N   
1578 C  CA  . PRO A 194 ? 0.1484 0.0547 0.0989 0.0017  0.0168  -0.0204 195 PRO A CA  
1579 C  C   . PRO A 194 ? 0.1545 0.0494 0.1341 -0.0019 0.0096  -0.0234 195 PRO A C   
1580 O  O   . PRO A 194 ? 0.1632 0.0822 0.1075 0.0311  -0.0136 -0.0120 195 PRO A O   
1581 C  CB  . PRO A 194 ? 0.1842 0.0820 0.1057 -0.0120 0.0071  -0.0242 195 PRO A CB  
1582 C  CG  . PRO A 194 ? 0.1812 0.1016 0.1165 -0.0282 -0.0035 0.0037  195 PRO A CG  
1583 C  CD  . PRO A 194 ? 0.1700 0.1337 0.0892 -0.0263 -0.0115 0.0013  195 PRO A CD  
1584 N  N   . GLY A 195 ? 0.1240 0.0646 0.1092 -0.0121 0.0261  -0.0370 196 GLY A N   
1585 C  CA  . GLY A 195 ? 0.1501 0.0710 0.0544 -0.0043 0.0419  0.0027  196 GLY A CA  
1586 C  C   . GLY A 195 ? 0.0907 0.0863 0.0794 0.0065  0.0148  -0.0043 196 GLY A C   
1587 O  O   . GLY A 195 ? 0.1235 0.0524 0.1257 0.0020  -0.0149 -0.0170 196 GLY A O   
1588 N  N   . SER A 196 ? 0.1339 0.0640 0.0524 0.0089  -0.0041 -0.0132 197 SER A N   
1589 C  CA  . SER A 196 ? 0.1176 0.0874 0.0524 0.0003  0.0105  0.0054  197 SER A CA  
1590 C  C   . SER A 196 ? 0.0914 0.0599 0.1174 -0.0190 -0.0078 -0.0082 197 SER A C   
1591 O  O   . SER A 196 ? 0.1203 0.0441 0.1203 -0.0059 -0.0233 -0.0054 197 SER A O   
1592 C  CB  . SER A 196 ? 0.1124 0.0854 0.1518 0.0080  -0.0255 -0.0322 197 SER A CB  
1593 O  OG  . SER A 196 ? 0.1187 0.0561 0.1488 0.0103  -0.0126 -0.0156 197 SER A OG  
1594 N  N   . LEU A 197 ? 0.1240 0.0497 0.1034 0.0127  0.0126  0.0013  198 LEU A N   
1595 C  CA  . LEU A 197 ? 0.1357 0.0436 0.1036 -0.0046 0.0284  -0.0089 198 LEU A CA  
1596 C  C   . LEU A 197 ? 0.1356 0.0364 0.1145 -0.0186 -0.0129 -0.0054 198 LEU A C   
1597 O  O   . LEU A 197 ? 0.1367 0.0609 0.1377 -0.0013 -0.0364 -0.0148 198 LEU A O   
1598 C  CB  . LEU A 197 ? 0.1400 0.0745 0.1298 -0.0114 -0.0086 -0.0236 198 LEU A CB  
1599 C  CG  . LEU A 197 ? 0.1483 0.0464 0.1441 -0.0024 -0.0178 -0.0204 198 LEU A CG  
1600 C  CD1 . LEU A 197 ? 0.1736 0.0894 0.1524 -0.0505 0.0221  0.0138  198 LEU A CD1 
1601 C  CD2 . LEU A 197 ? 0.1277 0.0719 0.2257 0.0062  0.0074  0.0452  198 LEU A CD2 
1602 N  N   . THR A 198 ? 0.1343 0.0354 0.1244 -0.0074 -0.0282 -0.0172 199 THR A N   
1603 C  CA  . THR A 198 ? 0.1076 0.0582 0.1685 -0.0081 0.0085  -0.0093 199 THR A CA  
1604 C  C   . THR A 198 ? 0.1002 0.0691 0.1334 -0.0076 -0.0204 -0.0156 199 THR A C   
1605 O  O   . THR A 198 ? 0.1290 0.0574 0.1528 0.0013  -0.0097 -0.0043 199 THR A O   
1606 C  CB  . THR A 198 ? 0.1181 0.0460 0.1720 -0.0020 -0.0164 -0.0137 199 THR A CB  
1607 O  OG1 . THR A 198 ? 0.1272 0.0555 0.1140 0.0035  -0.0250 -0.0087 199 THR A OG1 
1608 C  CG2 . THR A 198 ? 0.1358 0.0581 0.1446 -0.0038 0.0241  -0.0076 199 THR A CG2 
1609 N  N   . THR A 199 ? 0.1254 0.0709 0.1350 -0.0320 -0.0109 0.0105  200 THR A N   
1610 C  CA  . THR A 199 ? 0.1546 0.0655 0.1617 -0.0277 -0.0141 0.0103  200 THR A CA  
1611 C  C   . THR A 199 ? 0.1324 0.0833 0.1869 -0.0239 -0.0008 0.0159  200 THR A C   
1612 O  O   . THR A 199 ? 0.1293 0.0786 0.1700 -0.0006 0.0055  -0.0141 200 THR A O   
1613 C  CB  . THR A 199 ? 0.1817 0.0797 0.1731 0.0074  -0.0192 0.0189  200 THR A CB  
1614 O  OG1 . THR A 199 ? 0.2712 0.1246 0.2084 0.0595  -0.0430 -0.0017 200 THR A OG1 
1615 C  CG2 . THR A 199 ? 0.2162 0.1154 0.1946 -0.0641 -0.0337 -0.0234 200 THR A CG2 
1616 N  N   . PRO A 200 ? 0.1325 0.0697 0.1651 -0.0096 0.0190  -0.0155 201 PRO A N   
1617 C  CA  . PRO A 200 ? 0.1244 0.0928 0.2016 -0.0326 0.0031  0.0124  201 PRO A CA  
1618 C  C   . PRO A 200 ? 0.1439 0.0883 0.1797 -0.0299 0.0020  -0.0104 201 PRO A C   
1619 O  O   . PRO A 200 ? 0.1810 0.1001 0.1950 -0.0119 -0.0142 -0.0204 201 PRO A O   
1620 C  CB  . PRO A 200 ? 0.1401 0.1124 0.1861 -0.0238 -0.0080 -0.0010 201 PRO A CB  
1621 C  CG  . PRO A 200 ? 0.1252 0.1225 0.2192 -0.0148 0.0052  -0.0248 201 PRO A CG  
1622 C  CD  . PRO A 200 ? 0.1541 0.0806 0.1679 0.0005  -0.0035 -0.0019 201 PRO A CD  
1623 N  N   . PRO A 201 ? 0.1362 0.1030 0.1836 -0.0236 -0.0230 0.0060  202 PRO A N   
1624 C  CA  . PRO A 201 ? 0.1722 0.0754 0.1825 -0.0326 -0.0136 0.0119  202 PRO A CA  
1625 C  C   . PRO A 201 ? 0.1331 0.0840 0.1984 -0.0024 -0.0147 0.0294  202 PRO A C   
1626 O  O   . PRO A 201 ? 0.1518 0.0849 0.2099 -0.0449 -0.0068 -0.0155 202 PRO A O   
1627 C  CB  . PRO A 201 ? 0.1753 0.0966 0.2338 -0.0463 -0.0219 0.0164  202 PRO A CB  
1628 C  CG  . PRO A 201 ? 0.1861 0.0883 0.2439 -0.0161 -0.0121 0.0028  202 PRO A CG  
1629 C  CD  . PRO A 201 ? 0.2055 0.1061 0.1879 0.0020  -0.0311 0.0054  202 PRO A CD  
1630 N  N   . LEU A 202 ? 0.1185 0.0652 0.1649 -0.0331 0.0195  -0.0104 203 LEU A N   
1631 C  CA  . LEU A 202 ? 0.1395 0.0436 0.1922 -0.0137 0.0020  0.0020  203 LEU A CA  
1632 C  C   . LEU A 202 ? 0.1216 0.0576 0.1812 -0.0228 -0.0175 -0.0125 203 LEU A C   
1633 O  O   . LEU A 202 ? 0.1336 0.0759 0.1720 -0.0023 -0.0254 -0.0082 203 LEU A O   
1634 C  CB  . LEU A 202 ? 0.1025 0.0736 0.1857 0.0255  -0.0060 -0.0331 203 LEU A CB  
1635 C  CG  . LEU A 202 ? 0.0975 0.0886 0.1879 0.0208  -0.0006 -0.0070 203 LEU A CG  
1636 C  CD1 . LEU A 202 ? 0.1296 0.1106 0.2223 0.0234  0.0046  -0.0216 203 LEU A CD1 
1637 C  CD2 . LEU A 202 ? 0.1324 0.0772 0.1918 -0.0057 -0.0148 -0.0097 203 LEU A CD2 
1638 N  N   . LEU A 203 ? 0.1270 0.0443 0.1858 -0.0119 -0.0097 -0.0074 204 LEU A N   
1639 C  CA  . LEU A 203 ? 0.1269 0.0834 0.1561 0.0007  -0.0044 -0.0198 204 LEU A CA  
1640 C  C   . LEU A 203 ? 0.1401 0.0601 0.1541 -0.0031 -0.0007 0.0024  204 LEU A C   
1641 O  O   . LEU A 203 ? 0.1400 0.0691 0.1565 -0.0060 -0.0421 -0.0151 204 LEU A O   
1642 C  CB  . LEU A 203 ? 0.1676 0.0644 0.1597 0.0031  -0.0078 0.0351  204 LEU A CB  
1643 C  CG  . LEU A 203 ? 0.1943 0.0899 0.2016 -0.0148 -0.0017 0.0087  204 LEU A CG  
1644 C  CD1 . LEU A 203 ? 0.1894 0.0870 0.2709 0.0032  0.0383  0.0551  204 LEU A CD1 
1645 C  CD2 . LEU A 203 ? 0.1946 0.1580 0.3025 -0.0825 0.0172  0.0109  204 LEU A CD2 
1646 N  N   . GLU A 204 ? 0.1617 0.0856 0.1391 -0.0100 -0.0142 -0.0324 205 GLU A N   
1647 C  CA  . GLU A 204 ? 0.1375 0.0628 0.1669 -0.0035 -0.0460 -0.0157 205 GLU A CA  
1648 C  C   . GLU A 204 ? 0.1455 0.0468 0.1624 -0.0216 -0.0186 -0.0115 205 GLU A C   
1649 O  O   . GLU A 204 ? 0.1879 0.0949 0.1638 0.0142  -0.0478 -0.0472 205 GLU A O   
1650 C  CB  . GLU A 204 ? 0.1535 0.0865 0.1659 -0.0076 -0.0370 -0.0373 205 GLU A CB  
1651 C  CG  . GLU A 204 ? 0.1298 0.1116 0.1792 0.0273  -0.0410 -0.0537 205 GLU A CG  
1652 C  CD  . GLU A 204 ? 0.1546 0.1264 0.1738 -0.0147 -0.0657 -0.0157 205 GLU A CD  
1653 O  OE1 . GLU A 204 ? 0.1796 0.1204 0.2332 -0.0010 -0.0931 -0.0447 205 GLU A OE1 
1654 O  OE2 . GLU A 204 ? 0.1599 0.0912 0.1817 -0.0035 -0.0714 -0.0086 205 GLU A OE2 
1655 N  N   . CYS A 205 ? 0.1208 0.0525 0.1677 -0.0129 -0.0441 -0.0226 206 CYS A N   
1656 C  CA  . CYS A 205 ? 0.1235 0.0722 0.1649 -0.0098 -0.0280 0.0021  206 CYS A CA  
1657 C  C   . CYS A 205 ? 0.1125 0.0594 0.1691 -0.0003 -0.0375 -0.0269 206 CYS A C   
1658 O  O   . CYS A 205 ? 0.1307 0.0548 0.1835 -0.0017 -0.0469 -0.0059 206 CYS A O   
1659 C  CB  . CYS A 205 ? 0.1624 0.0489 0.1542 -0.0175 0.0103  -0.0154 206 CYS A CB  
1660 S  SG  . CYS A 205 ? 0.1783 0.0648 0.1497 -0.0032 -0.0209 0.0003  206 CYS A SG  
1661 N  N   . VAL A 206 ? 0.1250 0.0533 0.1378 -0.0159 -0.0366 -0.0088 207 VAL A N   
1662 C  CA  . VAL A 206 ? 0.1279 0.0348 0.1420 -0.0017 -0.0148 -0.0167 207 VAL A CA  
1663 C  C   . VAL A 206 ? 0.1312 0.0273 0.1249 -0.0140 -0.0143 -0.0015 207 VAL A C   
1664 O  O   . VAL A 206 ? 0.1341 0.0790 0.1406 0.0087  -0.0001 0.0194  207 VAL A O   
1665 C  CB  . VAL A 206 ? 0.1331 0.0379 0.1532 -0.0109 -0.0020 -0.0130 207 VAL A CB  
1666 C  CG1 . VAL A 206 ? 0.1149 0.0585 0.1319 -0.0298 -0.0436 -0.0293 207 VAL A CG1 
1667 C  CG2 . VAL A 206 ? 0.1404 0.0636 0.1404 -0.0071 0.0027  -0.0055 207 VAL A CG2 
1668 N  N   . THR A 207 ? 0.1106 0.0516 0.1242 0.0019  -0.0142 -0.0065 208 THR A N   
1669 C  CA  . THR A 207 ? 0.1274 0.0422 0.1174 -0.0026 -0.0151 -0.0384 208 THR A CA  
1670 C  C   . THR A 207 ? 0.1286 0.0636 0.1159 0.0000  -0.0340 -0.0065 208 THR A C   
1671 O  O   . THR A 207 ? 0.1358 0.0355 0.1238 -0.0046 -0.0240 -0.0003 208 THR A O   
1672 C  CB  . THR A 207 ? 0.1492 0.0345 0.1492 0.0060  0.0096  -0.0138 208 THR A CB  
1673 O  OG1 . THR A 207 ? 0.1731 0.0454 0.1317 -0.0034 0.0077  -0.0259 208 THR A OG1 
1674 C  CG2 . THR A 207 ? 0.1563 0.0593 0.1615 -0.0270 0.0200  -0.0087 208 THR A CG2 
1675 N  N   . TRP A 208 ? 0.1070 0.0326 0.1518 -0.0060 -0.0190 -0.0096 209 TRP A N   
1676 C  CA  . TRP A 208 ? 0.1205 0.0299 0.1394 -0.0059 -0.0152 -0.0206 209 TRP A CA  
1677 C  C   . TRP A 208 ? 0.1299 0.0465 0.1379 -0.0043 -0.0253 -0.0143 209 TRP A C   
1678 O  O   . TRP A 208 ? 0.1207 0.0537 0.1366 -0.0137 -0.0108 0.0006  209 TRP A O   
1679 C  CB  . TRP A 208 ? 0.1453 0.0416 0.1097 -0.0013 -0.0043 0.0006  209 TRP A CB  
1680 C  CG  . TRP A 208 ? 0.1104 0.0262 0.1070 0.0023  -0.0062 0.0049  209 TRP A CG  
1681 C  CD1 . TRP A 208 ? 0.1187 0.0321 0.1319 -0.0052 0.0092  0.0256  209 TRP A CD1 
1682 C  CD2 . TRP A 208 ? 0.1190 0.0375 0.0872 0.0017  0.0206  0.0164  209 TRP A CD2 
1683 N  NE1 . TRP A 208 ? 0.1000 0.0434 0.1554 -0.0119 -0.0318 0.0104  209 TRP A NE1 
1684 C  CE2 . TRP A 208 ? 0.1188 0.0276 0.1088 0.0136  0.0004  0.0048  209 TRP A CE2 
1685 C  CE3 . TRP A 208 ? 0.1226 0.0424 0.1221 0.0013  -0.0337 -0.0162 209 TRP A CE3 
1686 C  CZ2 . TRP A 208 ? 0.1235 0.0353 0.1286 0.0281  0.0111  -0.0108 209 TRP A CZ2 
1687 C  CZ3 . TRP A 208 ? 0.1508 0.0434 0.1406 0.0098  -0.0153 0.0000  209 TRP A CZ3 
1688 C  CH2 . TRP A 208 ? 0.1446 0.0486 0.0982 0.0164  -0.0003 -0.0103 209 TRP A CH2 
1689 N  N   . ILE A 209 ? 0.1181 0.0295 0.1216 -0.0165 -0.0140 -0.0080 210 ILE A N   
1690 C  CA  . ILE A 209 ? 0.1128 0.0354 0.1477 -0.0232 -0.0196 -0.0049 210 ILE A CA  
1691 C  C   . ILE A 209 ? 0.1110 0.0700 0.1256 -0.0131 -0.0181 -0.0051 210 ILE A C   
1692 O  O   . ILE A 209 ? 0.1678 0.0491 0.1230 0.0035  -0.0249 0.0054  210 ILE A O   
1693 C  CB  . ILE A 209 ? 0.1259 0.0313 0.1849 0.0000  -0.0126 -0.0098 210 ILE A CB  
1694 C  CG1 . ILE A 209 ? 0.1392 0.0630 0.2002 0.0226  -0.0231 -0.0093 210 ILE A CG1 
1695 C  CG2 . ILE A 209 ? 0.1255 0.0682 0.1664 0.0041  -0.0189 0.0108  210 ILE A CG2 
1696 C  CD1 . ILE A 209 ? 0.1439 0.0907 0.2352 0.0140  -0.0381 -0.0093 210 ILE A CD1 
1697 N  N   . VAL A 210 ? 0.1307 0.0322 0.1149 -0.0044 -0.0052 0.0043  211 VAL A N   
1698 C  CA  . VAL A 210 ? 0.0967 0.0588 0.1340 -0.0003 0.0006  -0.0267 211 VAL A CA  
1699 C  C   . VAL A 210 ? 0.1240 0.0567 0.1235 0.0162  -0.0153 0.0073  211 VAL A C   
1700 O  O   . VAL A 210 ? 0.1524 0.0584 0.1155 -0.0178 -0.0026 0.0082  211 VAL A O   
1701 C  CB  . VAL A 210 ? 0.1104 0.0618 0.1414 0.0208  -0.0266 -0.0087 211 VAL A CB  
1702 C  CG1 . VAL A 210 ? 0.1612 0.0275 0.1516 0.0070  -0.0428 -0.0166 211 VAL A CG1 
1703 C  CG2 . VAL A 210 ? 0.1246 0.0585 0.1506 -0.0208 -0.0209 -0.0030 211 VAL A CG2 
1704 N  N   . LEU A 211 ? 0.1180 0.0725 0.1281 -0.0116 -0.0236 -0.0100 212 LEU A N   
1705 C  CA  . LEU A 211 ? 0.1298 0.0820 0.1529 -0.0299 -0.0320 0.0172  212 LEU A CA  
1706 C  C   . LEU A 211 ? 0.1210 0.0829 0.1358 -0.0259 -0.0136 0.0248  212 LEU A C   
1707 O  O   . LEU A 211 ? 0.1240 0.0917 0.1465 -0.0234 -0.0013 0.0041  212 LEU A O   
1708 C  CB  . LEU A 211 ? 0.1508 0.0966 0.1325 -0.0311 -0.0241 0.0000  212 LEU A CB  
1709 C  CG  . LEU A 211 ? 0.1435 0.0617 0.1544 -0.0132 -0.0274 0.0182  212 LEU A CG  
1710 C  CD1 . LEU A 211 ? 0.1282 0.1490 0.1887 -0.0163 -0.0340 0.0066  212 LEU A CD1 
1711 C  CD2 . LEU A 211 ? 0.1444 0.0987 0.1851 0.0225  -0.0074 -0.0225 212 LEU A CD2 
1712 N  N   . LYS A 212 ? 0.1444 0.0891 0.1659 -0.0233 -0.0276 0.0205  213 LYS A N   
1713 C  CA  . LYS A 212 ? 0.1631 0.0878 0.1527 -0.0254 -0.0164 0.0322  213 LYS A CA  
1714 C  C   . LYS A 212 ? 0.1592 0.0719 0.1483 -0.0164 -0.0280 0.0219  213 LYS A C   
1715 O  O   . LYS A 212 ? 0.1706 0.0921 0.2184 -0.0091 -0.0500 0.0155  213 LYS A O   
1716 C  CB  . LYS A 212 ? 0.2137 0.1183 0.1837 -0.0560 -0.0218 0.0205  213 LYS A CB  
1717 C  CG  . LYS A 212 ? 0.2800 0.1640 0.2437 -0.0562 -0.0221 0.0405  213 LYS A CG  
1718 C  CD  . LYS A 212 ? 0.3903 0.2282 0.3449 -0.1032 0.0251  0.0054  213 LYS A CD  
1719 C  CE  . LYS A 212 ? 0.4318 0.3755 0.4090 -0.0297 0.0335  0.0140  213 LYS A CE  
1720 N  NZ  . LYS A 212 ? 0.4221 0.4326 0.4824 -0.0610 0.0109  -0.0416 213 LYS A NZ  
1721 N  N   . GLU A 213 ? 0.1409 0.0759 0.1293 -0.0274 -0.0245 0.0194  214 GLU A N   
1722 C  CA  . GLU A 213 ? 0.1572 0.0930 0.1941 -0.0291 -0.0277 0.0099  214 GLU A CA  
1723 C  C   . GLU A 213 ? 0.1508 0.0698 0.1652 -0.0331 -0.0115 -0.0024 214 GLU A C   
1724 O  O   . GLU A 213 ? 0.1466 0.0576 0.1717 -0.0152 -0.0307 0.0208  214 GLU A O   
1725 C  CB  . GLU A 213 ? 0.1502 0.0974 0.1952 -0.0233 -0.0423 0.0077  214 GLU A CB  
1726 C  CG  . GLU A 213 ? 0.1430 0.1140 0.2597 -0.0307 -0.0703 -0.0156 214 GLU A CG  
1727 C  CD  . GLU A 213 ? 0.2274 0.1804 0.3377 -0.0423 -0.0135 -0.0346 214 GLU A CD  
1728 O  OE1 . GLU A 213 ? 0.1650 0.1142 0.2851 -0.0188 -0.0434 0.0384  214 GLU A OE1 
1729 O  OE2 . GLU A 213 ? 0.2860 0.2922 0.4083 -0.0746 -0.0755 -0.0778 214 GLU A OE2 
1730 N  N   . PRO A 214 ? 0.1634 0.0479 0.1361 -0.0126 -0.0176 0.0130  215 PRO A N   
1731 C  CA  . PRO A 214 ? 0.1709 0.0636 0.1474 -0.0156 -0.0193 0.0065  215 PRO A CA  
1732 C  C   . PRO A 214 ? 0.1609 0.0684 0.1706 -0.0109 -0.0291 0.0027  215 PRO A C   
1733 O  O   . PRO A 214 ? 0.1738 0.1208 0.1946 -0.0329 -0.0186 0.0223  215 PRO A O   
1734 C  CB  . PRO A 214 ? 0.1449 0.0478 0.1896 -0.0043 -0.0131 0.0052  215 PRO A CB  
1735 C  CG  . PRO A 214 ? 0.2700 0.1309 0.2099 0.0115  -0.0054 0.0357  215 PRO A CG  
1736 C  CD  . PRO A 214 ? 0.2059 0.0439 0.1670 -0.0071 0.0256  0.0232  215 PRO A CD  
1737 N  N   . ILE A 215 ? 0.1783 0.0640 0.1360 -0.0063 -0.0245 0.0076  216 ILE A N   
1738 C  CA  . ILE A 215 ? 0.1947 0.0822 0.1280 -0.0027 -0.0335 -0.0264 216 ILE A CA  
1739 C  C   . ILE A 215 ? 0.1681 0.0829 0.1624 -0.0093 -0.0155 0.0094  216 ILE A C   
1740 O  O   . ILE A 215 ? 0.1925 0.0579 0.1659 -0.0130 -0.0255 -0.0124 216 ILE A O   
1741 C  CB  . ILE A 215 ? 0.1801 0.0689 0.1456 0.0091  -0.0074 -0.0013 216 ILE A CB  
1742 C  CG1 . ILE A 215 ? 0.1941 0.0982 0.1659 -0.0062 -0.0093 0.0118  216 ILE A CG1 
1743 C  CG2 . ILE A 215 ? 0.1873 0.1296 0.2012 0.0152  -0.0458 -0.0432 216 ILE A CG2 
1744 C  CD1 . ILE A 215 ? 0.2367 0.0795 0.1739 0.0012  -0.0198 0.0149  216 ILE A CD1 
1745 N  N   . SER A 216 ? 0.2038 0.0671 0.1564 -0.0125 -0.0230 -0.0196 217 SER A N   
1746 C  CA  . SER A 216 ? 0.2029 0.0976 0.1817 -0.0159 -0.0248 -0.0114 217 SER A CA  
1747 C  C   . SER A 216 ? 0.1930 0.0447 0.1757 -0.0229 -0.0430 -0.0076 217 SER A C   
1748 O  O   . SER A 216 ? 0.1986 0.0811 0.2081 -0.0010 -0.0595 -0.0027 217 SER A O   
1749 C  CB  . SER A 216 ? 0.3064 0.0534 0.2023 -0.0368 0.0291  0.0017  217 SER A CB  
1750 O  OG  . SER A 216 ? 0.2906 0.2070 0.3172 -0.0300 -0.0489 0.0292  217 SER A OG  
1751 N  N   . VAL A 217 ? 0.2004 0.0710 0.1547 -0.0184 -0.0255 -0.0126 218 VAL A N   
1752 C  CA  . VAL A 217 ? 0.1915 0.0712 0.1790 -0.0241 -0.0230 -0.0121 218 VAL A CA  
1753 C  C   . VAL A 217 ? 0.2223 0.0731 0.1639 -0.0114 -0.0469 -0.0252 218 VAL A C   
1754 O  O   . VAL A 217 ? 0.2227 0.0552 0.1767 -0.0326 -0.0640 -0.0063 218 VAL A O   
1755 C  CB  . VAL A 217 ? 0.2058 0.0711 0.1905 -0.0320 -0.0326 -0.0192 218 VAL A CB  
1756 C  CG1 . VAL A 217 ? 0.2135 0.0372 0.1824 0.0040  -0.0516 -0.0278 218 VAL A CG1 
1757 C  CG2 . VAL A 217 ? 0.1579 0.1023 0.2372 -0.0210 -0.0551 -0.0397 218 VAL A CG2 
1758 N  N   . SER A 218 ? 0.2091 0.0798 0.1446 -0.0142 -0.0310 -0.0412 219 SER A N   
1759 C  CA  . SER A 218 ? 0.2163 0.0664 0.1611 -0.0115 -0.0230 -0.0292 219 SER A CA  
1760 C  C   . SER A 218 ? 0.2169 0.0826 0.1966 0.0043  -0.0264 -0.0098 219 SER A C   
1761 O  O   . SER A 218 ? 0.2232 0.0793 0.1650 -0.0070 -0.0456 0.0049  219 SER A O   
1762 C  CB  . SER A 218 ? 0.2511 0.0777 0.1551 -0.0269 -0.0263 -0.0163 219 SER A CB  
1763 O  OG  . SER A 218 ? 0.2587 0.0811 0.1993 -0.0221 -0.0129 -0.0445 219 SER A OG  
1764 N  N   A SER A 219 ? 0.2221 0.0509 0.1793 -0.0078 -0.0288 -0.0233 220 SER A N   
1765 N  N   B SER A 219 ? 0.2234 0.0549 0.1864 -0.0113 -0.0285 -0.0219 220 SER A N   
1766 C  CA  A SER A 219 ? 0.2185 0.0507 0.2059 -0.0078 -0.0226 -0.0057 220 SER A CA  
1767 C  CA  B SER A 219 ? 0.2209 0.0465 0.2184 -0.0138 -0.0200 0.0006  220 SER A CA  
1768 C  C   A SER A 219 ? 0.2224 0.1138 0.2013 0.0080  -0.0142 -0.0326 220 SER A C   
1769 C  C   B SER A 219 ? 0.2228 0.1225 0.2119 0.0118  -0.0148 -0.0223 220 SER A C   
1770 O  O   A SER A 219 ? 0.2277 0.0600 0.2245 -0.0122 0.0019  0.0068  220 SER A O   
1771 O  O   B SER A 219 ? 0.2167 0.0670 0.2516 0.0024  -0.0136 0.0055  220 SER A O   
1772 C  CB  A SER A 219 ? 0.2274 0.0601 0.2171 -0.0146 -0.0190 -0.0185 220 SER A CB  
1773 C  CB  B SER A 219 ? 0.2386 0.0828 0.2338 -0.0170 -0.0165 -0.0131 220 SER A CB  
1774 O  OG  A SER A 219 ? 0.2446 0.0807 0.2022 0.0114  -0.0300 -0.0040 220 SER A OG  
1775 O  OG  B SER A 219 ? 0.2684 0.1286 0.2793 -0.0093 -0.0288 0.0364  220 SER A OG  
1776 N  N   . GLU A 220 ? 0.2361 0.0860 0.1937 0.0007  -0.0020 -0.0096 221 GLU A N   
1777 C  CA  . GLU A 220 ? 0.2576 0.0666 0.1954 -0.0122 -0.0190 -0.0142 221 GLU A CA  
1778 C  C   . GLU A 220 ? 0.2368 0.0693 0.1810 -0.0140 -0.0315 -0.0041 221 GLU A C   
1779 O  O   . GLU A 220 ? 0.2601 0.1086 0.1905 0.0088  0.0102  -0.0294 221 GLU A O   
1780 C  CB  . GLU A 220 ? 0.3105 0.1304 0.1810 -0.0219 -0.0252 -0.0542 221 GLU A CB  
1781 C  CG  . GLU A 220 ? 0.3470 0.1351 0.2460 -0.0114 -0.0177 -0.0904 221 GLU A CG  
1782 C  CD  . GLU A 220 ? 0.3776 0.2569 0.2926 -0.0091 0.0054  -0.0239 221 GLU A CD  
1783 O  OE1 . GLU A 220 ? 0.3277 0.1432 0.2886 -0.0698 0.0081  -0.0654 221 GLU A OE1 
1784 O  OE2 . GLU A 220 ? 0.5321 0.1922 0.4205 -0.0776 0.0124  -0.1286 221 GLU A OE2 
1785 N  N   . GLN A 221 ? 0.2321 0.0822 0.1702 -0.0035 -0.0403 -0.0024 222 GLN A N   
1786 C  CA  . GLN A 221 ? 0.2177 0.0658 0.1923 -0.0148 -0.0357 -0.0171 222 GLN A CA  
1787 C  C   . GLN A 221 ? 0.2227 0.0842 0.1954 -0.0124 -0.0373 0.0159  222 GLN A C   
1788 O  O   . GLN A 221 ? 0.2241 0.0955 0.1729 -0.0373 -0.0288 0.0038  222 GLN A O   
1789 C  CB  . GLN A 221 ? 0.2219 0.0667 0.1826 -0.0256 -0.0252 -0.0066 222 GLN A CB  
1790 C  CG  . GLN A 221 ? 0.2031 0.1106 0.1389 -0.0215 -0.0297 -0.0306 222 GLN A CG  
1791 C  CD  . GLN A 221 ? 0.2327 0.0736 0.1624 -0.0206 -0.0379 0.0122  222 GLN A CD  
1792 O  OE1 . GLN A 221 ? 0.2023 0.0781 0.1631 -0.0108 -0.0502 0.0037  222 GLN A OE1 
1793 N  NE2 . GLN A 221 ? 0.1991 0.0736 0.2023 -0.0173 -0.0408 0.0024  222 GLN A NE2 
1794 N  N   . VAL A 222 ? 0.2451 0.0741 0.1969 0.0037  -0.0562 0.0234  223 VAL A N   
1795 C  CA  . VAL A 222 ? 0.2317 0.1050 0.1824 0.0070  -0.0436 0.0445  223 VAL A CA  
1796 C  C   . VAL A 222 ? 0.2469 0.1018 0.2047 -0.0121 -0.0313 0.0294  223 VAL A C   
1797 O  O   . VAL A 222 ? 0.2284 0.1120 0.1853 -0.0386 -0.0368 0.0219  223 VAL A O   
1798 C  CB  . VAL A 222 ? 0.2581 0.1387 0.2045 -0.0088 -0.0645 0.0582  223 VAL A CB  
1799 C  CG1 . VAL A 222 ? 0.2102 0.1666 0.2605 -0.0362 -0.0037 0.0439  223 VAL A CG1 
1800 C  CG2 . VAL A 222 ? 0.2069 0.1774 0.2418 0.0017  -0.0461 0.0264  223 VAL A CG2 
1801 N  N   . LEU A 223 ? 0.2639 0.0740 0.2049 -0.0155 -0.0218 -0.0104 224 LEU A N   
1802 C  CA  . LEU A 223 ? 0.2602 0.1118 0.2490 -0.0133 -0.0054 -0.0052 224 LEU A CA  
1803 C  C   . LEU A 223 ? 0.2572 0.1084 0.2009 -0.0136 -0.0147 -0.0417 224 LEU A C   
1804 O  O   . LEU A 223 ? 0.2399 0.1481 0.2456 -0.0071 -0.0062 -0.0187 224 LEU A O   
1805 C  CB  . LEU A 223 ? 0.3179 0.1720 0.2651 -0.0157 -0.0100 -0.0088 224 LEU A CB  
1806 C  CG  . LEU A 223 ? 0.3452 0.1897 0.3438 -0.0266 -0.0281 -0.0291 224 LEU A CG  
1807 C  CD1 . LEU A 223 ? 0.3772 0.2591 0.4074 -0.0194 -0.0322 0.0010  224 LEU A CD1 
1808 C  CD2 . LEU A 223 ? 0.3356 0.2149 0.3610 -0.0221 -0.0170 -0.0240 224 LEU A CD2 
1809 N  N   . LYS A 224 ? 0.2449 0.1172 0.1810 -0.0189 -0.0263 -0.0054 225 LYS A N   
1810 C  CA  . LYS A 224 ? 0.2570 0.1523 0.2026 -0.0097 -0.0208 -0.0160 225 LYS A CA  
1811 C  C   . LYS A 224 ? 0.2277 0.1095 0.1577 -0.0298 -0.0196 0.0068  225 LYS A C   
1812 O  O   . LYS A 224 ? 0.2558 0.1043 0.1370 -0.0167 -0.0027 0.0065  225 LYS A O   
1813 C  CB  . LYS A 224 ? 0.2674 0.1923 0.1973 -0.0044 -0.0300 0.0320  225 LYS A CB  
1814 C  CG  . LYS A 224 ? 0.2680 0.2457 0.2444 0.0062  -0.0366 -0.0269 225 LYS A CG  
1815 C  CD  . LYS A 224 ? 0.3353 0.2845 0.3149 -0.0127 -0.0467 -0.0355 225 LYS A CD  
1816 C  CE  . LYS A 224 ? 0.3521 0.2257 0.3384 -0.0333 -0.0696 -0.0432 225 LYS A CE  
1817 N  NZ  . LYS A 224 ? 0.3461 0.3043 0.3828 -0.0052 -0.0383 -0.0326 225 LYS A NZ  
1818 N  N   . PHE A 225 ? 0.2188 0.0989 0.1238 -0.0132 -0.0307 -0.0133 226 PHE A N   
1819 C  CA  . PHE A 225 ? 0.2141 0.0752 0.1358 -0.0141 -0.0137 -0.0043 226 PHE A CA  
1820 C  C   . PHE A 225 ? 0.2264 0.0949 0.1691 -0.0059 -0.0110 0.0099  226 PHE A C   
1821 O  O   . PHE A 225 ? 0.2270 0.0951 0.1556 -0.0035 -0.0062 -0.0105 226 PHE A O   
1822 C  CB  . PHE A 225 ? 0.2377 0.0718 0.1228 0.0074  0.0041  -0.0143 226 PHE A CB  
1823 C  CG  . PHE A 225 ? 0.2234 0.0716 0.1596 -0.0311 -0.0107 -0.0194 226 PHE A CG  
1824 C  CD1 . PHE A 225 ? 0.2773 0.1250 0.1627 -0.0078 0.0175  0.0054  226 PHE A CD1 
1825 C  CD2 . PHE A 225 ? 0.2295 0.1147 0.1914 -0.0073 0.0005  -0.0527 226 PHE A CD2 
1826 C  CE1 . PHE A 225 ? 0.2792 0.1429 0.2126 -0.0068 0.0131  0.0000  226 PHE A CE1 
1827 C  CE2 . PHE A 225 ? 0.2339 0.1445 0.1814 -0.0068 -0.0120 -0.0553 226 PHE A CE2 
1828 C  CZ  . PHE A 225 ? 0.2119 0.1133 0.2097 -0.0192 -0.0318 -0.0359 226 PHE A CZ  
1829 N  N   . ARG A 226 ? 0.2185 0.0612 0.1652 -0.0051 -0.0196 -0.0083 227 ARG A N   
1830 C  CA  . ARG A 226 ? 0.2504 0.1159 0.1388 0.0015  0.0096  -0.0005 227 ARG A CA  
1831 C  C   . ARG A 226 ? 0.2519 0.1032 0.1710 -0.0148 0.0136  -0.0088 227 ARG A C   
1832 O  O   . ARG A 226 ? 0.2282 0.1476 0.1919 0.0254  -0.0003 0.0066  227 ARG A O   
1833 C  CB  . ARG A 226 ? 0.2709 0.0898 0.1351 -0.0037 0.0162  0.0373  227 ARG A CB  
1834 C  CG  . ARG A 226 ? 0.2152 0.0764 0.1641 -0.0148 -0.0153 0.0320  227 ARG A CG  
1835 C  CD  . ARG A 226 ? 0.2935 0.0898 0.1932 0.0068  0.0144  0.0189  227 ARG A CD  
1836 N  NE  . ARG A 226 ? 0.2422 0.0867 0.1421 -0.0406 -0.0006 0.0292  227 ARG A NE  
1837 C  CZ  . ARG A 226 ? 0.2705 0.1228 0.1560 -0.0344 -0.0366 0.0188  227 ARG A CZ  
1838 N  NH1 . ARG A 226 ? 0.3183 0.1403 0.2612 -0.0359 -0.0527 -0.0482 227 ARG A NH1 
1839 N  NH2 . ARG A 226 ? 0.2613 0.0922 0.2126 -0.0608 -0.0043 0.0066  227 ARG A NH2 
1840 N  N   . LYS A 227 ? 0.2531 0.1210 0.1142 -0.0082 -0.0023 -0.0198 228 LYS A N   
1841 C  CA  . LYS A 227 ? 0.2930 0.1313 0.1616 -0.0388 -0.0038 -0.0111 228 LYS A CA  
1842 C  C   . LYS A 227 ? 0.2781 0.1070 0.1407 -0.0472 0.0074  0.0037  228 LYS A C   
1843 O  O   . LYS A 227 ? 0.3061 0.1456 0.1749 -0.0500 0.0166  -0.0395 228 LYS A O   
1844 C  CB  . LYS A 227 ? 0.3091 0.1615 0.1339 -0.0201 -0.0278 -0.0120 228 LYS A CB  
1845 C  CG  . LYS A 227 ? 0.3216 0.2030 0.2298 -0.0566 -0.0346 -0.0152 228 LYS A CG  
1846 C  CD  . LYS A 227 ? 0.3396 0.2638 0.2789 -0.0434 -0.0225 -0.0236 228 LYS A CD  
1847 C  CE  . LYS A 227 ? 0.3851 0.4595 0.3580 -0.0252 0.0054  0.0038  228 LYS A CE  
1848 N  NZ  . LYS A 227 ? 0.5067 0.5117 0.4761 -0.0264 -0.0395 -0.0408 228 LYS A NZ  
1849 N  N   . LEU A 228 ? 0.2651 0.0829 0.1718 -0.0269 0.0000  -0.0148 229 LEU A N   
1850 C  CA  . LEU A 228 ? 0.2458 0.0903 0.1746 -0.0237 0.0108  -0.0052 229 LEU A CA  
1851 C  C   . LEU A 228 ? 0.2750 0.1154 0.1667 -0.0313 0.0218  -0.0219 229 LEU A C   
1852 O  O   . LEU A 228 ? 0.2633 0.0969 0.1703 -0.0038 0.0151  -0.0170 229 LEU A O   
1853 C  CB  . LEU A 228 ? 0.2518 0.0770 0.1424 -0.0007 0.0125  -0.0124 229 LEU A CB  
1854 C  CG  . LEU A 228 ? 0.2505 0.1533 0.1750 -0.0111 -0.0120 -0.0063 229 LEU A CG  
1855 C  CD1 . LEU A 228 ? 0.2912 0.1293 0.1406 0.0000  0.0179  -0.0546 229 LEU A CD1 
1856 C  CD2 . LEU A 228 ? 0.3439 0.1251 0.1360 0.0124  0.0441  0.0216  229 LEU A CD2 
1857 N  N   . ASN A 229 ? 0.2444 0.1252 0.1562 -0.0445 0.0192  -0.0066 230 ASN A N   
1858 C  CA  . ASN A 229 ? 0.2361 0.1351 0.1313 -0.0210 0.0092  -0.0295 230 ASN A CA  
1859 C  C   . ASN A 229 ? 0.2476 0.1281 0.1527 -0.0177 0.0094  -0.0109 230 ASN A C   
1860 O  O   . ASN A 229 ? 0.2451 0.1185 0.1846 -0.0063 0.0149  0.0031  230 ASN A O   
1861 C  CB  . ASN A 229 ? 0.2692 0.1471 0.1349 -0.0078 0.0176  0.0063  230 ASN A CB  
1862 C  CG  . ASN A 229 ? 0.3043 0.1371 0.1567 0.0295  0.0099  0.0010  230 ASN A CG  
1863 O  OD1 . ASN A 229 ? 0.3944 0.1460 0.1918 -0.0410 0.0509  -0.0283 230 ASN A OD1 
1864 N  ND2 . ASN A 229 ? 0.3400 0.1322 0.1815 -0.0035 0.0375  -0.0313 230 ASN A ND2 
1865 N  N   . PHE A 230 ? 0.2374 0.1266 0.1594 -0.0399 0.0170  -0.0126 231 PHE A N   
1866 C  CA  . PHE A 230 ? 0.2196 0.1190 0.1465 -0.0439 0.0153  -0.0104 231 PHE A CA  
1867 C  C   . PHE A 230 ? 0.2476 0.1541 0.1928 -0.0151 0.0068  0.0012  231 PHE A C   
1868 O  O   . PHE A 230 ? 0.2777 0.1526 0.1844 -0.0648 0.0038  -0.0020 231 PHE A O   
1869 C  CB  . PHE A 230 ? 0.2561 0.1392 0.1720 -0.0379 -0.0110 0.0081  231 PHE A CB  
1870 C  CG  . PHE A 230 ? 0.2340 0.1106 0.1952 -0.0571 0.0344  0.0063  231 PHE A CG  
1871 C  CD1 . PHE A 230 ? 0.2458 0.1014 0.1649 -0.0111 -0.0120 -0.0230 231 PHE A CD1 
1872 C  CD2 . PHE A 230 ? 0.2675 0.1027 0.1493 0.0136  0.0304  -0.0142 231 PHE A CD2 
1873 C  CE1 . PHE A 230 ? 0.2641 0.0876 0.2081 -0.0482 -0.0013 -0.0081 231 PHE A CE1 
1874 C  CE2 . PHE A 230 ? 0.2569 0.0961 0.1736 -0.0153 0.0137  0.0010  231 PHE A CE2 
1875 C  CZ  . PHE A 230 ? 0.2153 0.1301 0.1612 -0.0193 -0.0179 -0.0542 231 PHE A CZ  
1876 N  N   . ASN A 231 ? 0.2598 0.1651 0.1270 -0.0230 0.0348  0.0098  232 ASN A N   
1877 C  CA  . ASN A 231 ? 0.2709 0.1735 0.1790 -0.0364 0.0364  0.0051  232 ASN A CA  
1878 C  C   . ASN A 231 ? 0.2456 0.2141 0.1713 -0.0109 0.0533  0.0083  232 ASN A C   
1879 O  O   . ASN A 231 ? 0.2864 0.1671 0.2124 -0.0171 0.0544  0.0168  232 ASN A O   
1880 C  CB  . ASN A 231 ? 0.2687 0.1861 0.2155 -0.0063 0.0549  0.0242  232 ASN A CB  
1881 C  CG  . ASN A 231 ? 0.2275 0.1779 0.2090 0.0146  -0.0107 0.0216  232 ASN A CG  
1882 O  OD1 . ASN A 231 ? 0.3475 0.1597 0.1889 -0.0339 0.0733  -0.0379 232 ASN A OD1 
1883 N  ND2 . ASN A 231 ? 0.2907 0.2331 0.1581 0.0062  0.0307  -0.0109 232 ASN A ND2 
1884 N  N   . GLY A 232 ? 0.2875 0.1754 0.1746 -0.0277 0.0504  0.0116  233 GLY A N   
1885 C  CA  . GLY A 232 ? 0.2933 0.1810 0.2106 0.0097  0.0423  0.0167  233 GLY A CA  
1886 C  C   . GLY A 232 ? 0.2883 0.1943 0.2058 0.0126  0.0295  0.0269  233 GLY A C   
1887 O  O   . GLY A 232 ? 0.2989 0.2261 0.2242 0.0324  0.0794  0.0252  233 GLY A O   
1888 N  N   . GLU A 233 ? 0.3082 0.2498 0.1664 0.0076  0.0353  0.0155  234 GLU A N   
1889 C  CA  . GLU A 233 ? 0.2788 0.1897 0.1865 0.0091  0.0178  0.0181  234 GLU A CA  
1890 C  C   . GLU A 233 ? 0.2849 0.2090 0.2116 0.0216  0.0208  0.0046  234 GLU A C   
1891 O  O   . GLU A 233 ? 0.3043 0.2313 0.2252 0.0190  0.0245  0.0340  234 GLU A O   
1892 C  CB  . GLU A 233 ? 0.2883 0.1982 0.1934 0.0116  0.0160  0.0467  234 GLU A CB  
1893 C  CG  . GLU A 233 ? 0.3163 0.2245 0.1923 -0.0148 0.0401  0.0209  234 GLU A CG  
1894 C  CD  . GLU A 233 ? 0.3737 0.2725 0.3084 0.0037  -0.0093 -0.0233 234 GLU A CD  
1895 O  OE1 . GLU A 233 ? 0.3582 0.2259 0.3506 -0.0322 0.0204  0.0070  234 GLU A OE1 
1896 O  OE2 . GLU A 233 ? 0.3953 0.3278 0.3382 -0.0564 -0.0515 -0.0483 234 GLU A OE2 
1897 N  N   . GLY A 234 ? 0.3041 0.2447 0.2198 0.0434  0.0592  -0.0021 235 GLY A N   
1898 C  CA  . GLY A 234 ? 0.3213 0.3027 0.2480 0.0557  0.0340  -0.0034 235 GLY A CA  
1899 C  C   . GLY A 234 ? 0.3305 0.3435 0.2792 0.0496  0.0395  0.0190  235 GLY A C   
1900 O  O   . GLY A 234 ? 0.3618 0.4246 0.3199 0.0701  0.0751  0.0141  235 GLY A O   
1901 N  N   . GLU A 235 ? 0.3287 0.3108 0.2717 0.0263  0.0445  0.0173  236 GLU A N   
1902 C  CA  . GLU A 235 ? 0.3263 0.2731 0.2766 0.0280  0.0317  0.0296  236 GLU A CA  
1903 C  C   . GLU A 235 ? 0.3409 0.3240 0.3022 0.0283  0.0445  0.0416  236 GLU A C   
1904 O  O   . GLU A 235 ? 0.3517 0.3003 0.2935 0.0683  0.0533  0.0428  236 GLU A O   
1905 C  CB  . GLU A 235 ? 0.3366 0.2978 0.3089 0.0255  0.0322  0.0220  236 GLU A CB  
1906 C  CG  . GLU A 235 ? 0.3549 0.3057 0.3097 0.0179  0.0643  0.0177  236 GLU A CG  
1907 C  CD  . GLU A 235 ? 0.4031 0.2996 0.3377 -0.0094 0.0265  0.0194  236 GLU A CD  
1908 O  OE1 . GLU A 235 ? 0.3605 0.3905 0.3844 -0.0392 0.0873  0.0141  236 GLU A OE1 
1909 O  OE2 . GLU A 235 ? 0.5171 0.3859 0.5130 -0.0627 0.0650  0.0566  236 GLU A OE2 
1910 N  N   . PRO A 236 ? 0.3204 0.3097 0.3190 0.0298  0.0463  0.0644  237 PRO A N   
1911 C  CA  . PRO A 236 ? 0.3377 0.3438 0.3281 0.0104  0.0533  0.0443  237 PRO A CA  
1912 C  C   . PRO A 236 ? 0.3058 0.3008 0.2893 0.0164  0.0546  0.0243  237 PRO A C   
1913 O  O   . PRO A 236 ? 0.3037 0.2511 0.2433 0.0267  0.0701  0.0203  237 PRO A O   
1914 C  CB  . PRO A 236 ? 0.3384 0.3680 0.3521 0.0267  0.0586  0.0494  237 PRO A CB  
1915 C  CG  . PRO A 236 ? 0.3668 0.3457 0.3883 0.0285  0.0226  0.0690  237 PRO A CG  
1916 C  CD  . PRO A 236 ? 0.3585 0.3540 0.3529 0.0344  0.0197  0.0623  237 PRO A CD  
1917 N  N   . GLU A 237 ? 0.2939 0.2840 0.2663 0.0199  0.0465  -0.0037 238 GLU A N   
1918 C  CA  . GLU A 237 ? 0.3007 0.2450 0.2440 0.0060  0.0533  -0.0116 238 GLU A CA  
1919 C  C   . GLU A 237 ? 0.2813 0.2006 0.2318 -0.0049 0.0553  -0.0161 238 GLU A C   
1920 O  O   . GLU A 237 ? 0.2845 0.2004 0.2104 0.0172  0.0388  -0.0315 238 GLU A O   
1921 C  CB  . GLU A 237 ? 0.3083 0.2426 0.2386 0.0143  0.0228  -0.0294 238 GLU A CB  
1922 C  CG  . GLU A 237 ? 0.3332 0.3163 0.3061 -0.0083 0.0141  -0.0285 238 GLU A CG  
1923 C  CD  . GLU A 237 ? 0.3730 0.2383 0.3616 0.0178  0.0179  -0.0612 238 GLU A CD  
1924 O  OE1 . GLU A 237 ? 0.4458 0.3348 0.4745 0.0148  0.0071  -0.1105 238 GLU A OE1 
1925 O  OE2 . GLU A 237 ? 0.3661 0.2058 0.2694 0.0118  0.0099  -0.0913 238 GLU A OE2 
1926 N  N   . GLU A 238 ? 0.2723 0.1589 0.1851 -0.0274 0.0606  -0.0288 239 GLU A N   
1927 C  CA  . GLU A 238 ? 0.2882 0.1918 0.2194 -0.0315 0.0351  -0.0188 239 GLU A CA  
1928 C  C   . GLU A 238 ? 0.2417 0.1310 0.1568 -0.0098 0.0432  -0.0203 239 GLU A C   
1929 O  O   . GLU A 238 ? 0.3018 0.1350 0.2160 -0.0164 0.0344  -0.0381 239 GLU A O   
1930 C  CB  . GLU A 238 ? 0.3123 0.1844 0.2560 -0.0447 0.0293  -0.0227 239 GLU A CB  
1931 C  CG  . GLU A 238 ? 0.3679 0.2763 0.3126 -0.0081 0.0049  -0.0199 239 GLU A CG  
1932 C  CD  . GLU A 238 ? 0.4088 0.3190 0.3528 -0.0797 0.0098  -0.0131 239 GLU A CD  
1933 O  OE1 . GLU A 238 ? 0.5370 0.4632 0.4526 -0.0799 0.0109  -0.0269 239 GLU A OE1 
1934 O  OE2 . GLU A 238 ? 0.5137 0.4325 0.5210 -0.0839 0.0307  0.0410  239 GLU A OE2 
1935 N  N   . LEU A 239 ? 0.2592 0.1468 0.1621 -0.0082 0.0395  -0.0203 240 LEU A N   
1936 C  CA  . LEU A 239 ? 0.2237 0.1299 0.1607 -0.0127 0.0406  -0.0278 240 LEU A CA  
1937 C  C   . LEU A 239 ? 0.2435 0.0876 0.1667 -0.0043 0.0093  -0.0077 240 LEU A C   
1938 O  O   . LEU A 239 ? 0.2307 0.1228 0.1731 -0.0043 0.0222  -0.0340 240 LEU A O   
1939 C  CB  . LEU A 239 ? 0.2461 0.1272 0.1444 0.0052  0.0133  -0.0073 240 LEU A CB  
1940 C  CG  . LEU A 239 ? 0.1993 0.1264 0.1932 0.0046  0.0337  -0.0447 240 LEU A CG  
1941 C  CD1 . LEU A 239 ? 0.3083 0.1328 0.2910 0.0110  -0.0068 -0.0086 240 LEU A CD1 
1942 C  CD2 . LEU A 239 ? 0.2842 0.1255 0.2025 0.0183  0.0100  -0.0375 240 LEU A CD2 
1943 N  N   . MET A 240 ? 0.2228 0.0939 0.1369 0.0109  0.0447  -0.0151 241 MET A N   
1944 C  CA  . MET A 240 ? 0.2440 0.0842 0.1122 0.0001  0.0196  0.0035  241 MET A CA  
1945 C  C   . MET A 240 ? 0.2407 0.1303 0.1222 -0.0182 0.0206  -0.0417 241 MET A C   
1946 O  O   . MET A 240 ? 0.2203 0.0834 0.1507 -0.0065 0.0068  -0.0006 241 MET A O   
1947 C  CB  . MET A 240 ? 0.2666 0.0797 0.1337 0.0034  0.0234  0.0000  241 MET A CB  
1948 C  CG  . MET A 240 ? 0.2173 0.1092 0.1371 0.0065  0.0153  -0.0212 241 MET A CG  
1949 S  SD  . MET A 240 ? 0.2745 0.0745 0.1721 -0.0074 0.0361  -0.0065 241 MET A SD  
1950 C  CE  . MET A 240 ? 0.2996 0.0894 0.1616 -0.0399 0.0803  0.0012  241 MET A CE  
1951 N  N   . VAL A 241 ? 0.2471 0.0715 0.1045 -0.0043 0.0003  -0.0096 242 VAL A N   
1952 C  CA  . VAL A 241 ? 0.2155 0.0535 0.1129 -0.0026 -0.0031 -0.0137 242 VAL A CA  
1953 C  C   . VAL A 241 ? 0.2134 0.0702 0.1624 0.0051  -0.0229 -0.0020 242 VAL A C   
1954 O  O   . VAL A 241 ? 0.2055 0.0834 0.1252 -0.0143 0.0152  -0.0197 242 VAL A O   
1955 C  CB  . VAL A 241 ? 0.2076 0.0828 0.1722 -0.0109 -0.0040 0.0003  242 VAL A CB  
1956 C  CG1 . VAL A 241 ? 0.2289 0.1124 0.1678 -0.0241 -0.0414 -0.0231 242 VAL A CG1 
1957 C  CG2 . VAL A 241 ? 0.2378 0.0930 0.1785 0.0157  -0.0019 -0.0105 242 VAL A CG2 
1958 N  N   . ASP A 242 ? 0.2022 0.0567 0.1368 -0.0086 -0.0023 -0.0035 243 ASP A N   
1959 C  CA  . ASP A 242 ? 0.1897 0.0619 0.1455 0.0264  -0.0173 -0.0263 243 ASP A CA  
1960 C  C   . ASP A 242 ? 0.1544 0.0612 0.1490 -0.0252 0.0096  -0.0077 243 ASP A C   
1961 O  O   . ASP A 242 ? 0.1699 0.0711 0.1501 -0.0057 0.0000  -0.0285 243 ASP A O   
1962 C  CB  . ASP A 242 ? 0.1681 0.0604 0.1801 -0.0031 -0.0089 -0.0066 243 ASP A CB  
1963 C  CG  . ASP A 242 ? 0.1622 0.0998 0.1358 0.0126  -0.0071 -0.0046 243 ASP A CG  
1964 O  OD1 . ASP A 242 ? 0.1718 0.0558 0.1746 0.0043  -0.0013 -0.0277 243 ASP A OD1 
1965 O  OD2 . ASP A 242 ? 0.2098 0.0543 0.1993 0.0133  0.0463  -0.0306 243 ASP A OD2 
1966 N  N   . ASN A 243 ? 0.1894 0.0401 0.1538 0.0242  -0.0105 -0.0395 244 ASN A N   
1967 C  CA  . ASN A 243 ? 0.1955 0.0480 0.1348 0.0137  -0.0089 -0.0199 244 ASN A CA  
1968 C  C   . ASN A 243 ? 0.1554 0.0498 0.1717 -0.0131 -0.0020 -0.0157 244 ASN A C   
1969 O  O   . ASN A 243 ? 0.1810 0.0497 0.1544 0.0010  -0.0054 0.0175  244 ASN A O   
1970 C  CB  . ASN A 243 ? 0.1735 0.0786 0.1397 -0.0052 0.0054  0.0109  244 ASN A CB  
1971 C  CG  . ASN A 243 ? 0.1731 0.0666 0.1466 -0.0161 0.0243  -0.0132 244 ASN A CG  
1972 O  OD1 . ASN A 243 ? 0.1720 0.0710 0.1516 -0.0149 -0.0115 0.0137  244 ASN A OD1 
1973 N  ND2 . ASN A 243 ? 0.2356 0.1119 0.2242 -0.0337 -0.0272 0.0812  244 ASN A ND2 
1974 N  N   . TRP A 244 ? 0.1519 0.0407 0.1259 -0.0167 0.0060  -0.0108 245 TRP A N   
1975 C  CA  . TRP A 244 ? 0.1394 0.0540 0.1290 0.0077  -0.0035 -0.0068 245 TRP A CA  
1976 C  C   . TRP A 244 ? 0.1485 0.0728 0.1066 -0.0021 0.0147  0.0199  245 TRP A C   
1977 O  O   . TRP A 244 ? 0.1396 0.0714 0.1377 0.0012  -0.0111 -0.0098 245 TRP A O   
1978 C  CB  . TRP A 244 ? 0.1756 0.0261 0.1513 0.0084  0.0278  -0.0048 245 TRP A CB  
1979 C  CG  . TRP A 244 ? 0.1369 0.0676 0.1206 -0.0030 -0.0157 -0.0052 245 TRP A CG  
1980 C  CD1 . TRP A 244 ? 0.1685 0.0318 0.1620 -0.0082 -0.0273 0.0093  245 TRP A CD1 
1981 C  CD2 . TRP A 244 ? 0.1401 0.0644 0.1342 0.0043  0.0092  -0.0012 245 TRP A CD2 
1982 N  NE1 . TRP A 244 ? 0.1576 0.0577 0.1618 -0.0082 -0.0068 0.0052  245 TRP A NE1 
1983 C  CE2 . TRP A 244 ? 0.1607 0.0693 0.1318 0.0162  0.0137  0.0230  245 TRP A CE2 
1984 C  CE3 . TRP A 244 ? 0.1659 0.1037 0.1480 -0.0057 -0.0388 0.0342  245 TRP A CE3 
1985 C  CZ2 . TRP A 244 ? 0.1731 0.0749 0.1546 0.0021  -0.0051 0.0140  245 TRP A CZ2 
1986 C  CZ3 . TRP A 244 ? 0.1581 0.0919 0.1501 0.0052  0.0153  -0.0001 245 TRP A CZ3 
1987 C  CH2 . TRP A 244 ? 0.1609 0.1067 0.1528 0.0221  -0.0082 0.0273  245 TRP A CH2 
1988 N  N   . ARG A 245 ? 0.1601 0.0706 0.1005 -0.0065 -0.0176 -0.0165 246 ARG A N   
1989 C  CA  . ARG A 245 ? 0.1416 0.0454 0.1410 -0.0151 -0.0091 -0.0133 246 ARG A CA  
1990 C  C   . ARG A 245 ? 0.1252 0.0653 0.1368 0.0034  -0.0263 -0.0219 246 ARG A C   
1991 O  O   . ARG A 245 ? 0.1310 0.0694 0.1580 0.0076  -0.0201 -0.0092 246 ARG A O   
1992 C  CB  . ARG A 245 ? 0.1154 0.0732 0.1264 -0.0017 -0.0201 -0.0263 246 ARG A CB  
1993 C  CG  . ARG A 245 ? 0.1286 0.0650 0.1411 -0.0200 -0.0193 -0.0306 246 ARG A CG  
1994 C  CD  . ARG A 245 ? 0.1312 0.0768 0.1973 -0.0041 -0.0184 -0.0531 246 ARG A CD  
1995 N  NE  . ARG A 245 ? 0.1405 0.0709 0.1500 -0.0315 -0.0291 -0.0384 246 ARG A NE  
1996 C  CZ  . ARG A 245 ? 0.1032 0.0802 0.1283 -0.0463 -0.0006 -0.0077 246 ARG A CZ  
1997 N  NH1 . ARG A 245 ? 0.1219 0.0813 0.1614 -0.0006 0.0131  -0.0046 246 ARG A NH1 
1998 N  NH2 . ARG A 245 ? 0.1174 0.0716 0.1909 -0.0182 -0.0077 -0.0059 246 ARG A NH2 
1999 N  N   . PRO A 246 ? 0.1386 0.0736 0.1421 -0.0003 -0.0091 0.0093  247 PRO A N   
2000 C  CA  . PRO A 246 ? 0.1217 0.0727 0.1359 0.0197  0.0140  -0.0019 247 PRO A CA  
2001 C  C   . PRO A 246 ? 0.1525 0.0614 0.1192 0.0419  -0.0040 -0.0006 247 PRO A C   
2002 O  O   . PRO A 246 ? 0.1616 0.0551 0.1533 0.0152  -0.0163 -0.0030 247 PRO A O   
2003 C  CB  . PRO A 246 ? 0.1599 0.1316 0.1789 0.0416  0.0401  0.0124  247 PRO A CB  
2004 C  CG  . PRO A 246 ? 0.1685 0.1871 0.2860 0.0443  0.0119  0.0900  247 PRO A CG  
2005 C  CD  . PRO A 246 ? 0.1588 0.0824 0.1958 0.0230  0.0000  0.0209  247 PRO A CD  
2006 N  N   . ALA A 247 ? 0.1631 0.0732 0.0946 0.0230  0.0008  0.0166  248 ALA A N   
2007 C  CA  . ALA A 247 ? 0.1513 0.0912 0.1005 0.0162  0.0021  -0.0031 248 ALA A CA  
2008 C  C   . ALA A 247 ? 0.1465 0.0725 0.1474 0.0077  0.0111  0.0031  248 ALA A C   
2009 O  O   . ALA A 247 ? 0.1749 0.0840 0.1676 0.0368  -0.0266 -0.0034 248 ALA A O   
2010 C  CB  . ALA A 247 ? 0.2167 0.0824 0.1131 0.0082  0.0355  0.0259  248 ALA A CB  
2011 N  N   . GLN A 248 ? 0.1319 0.0668 0.1142 0.0093  -0.0156 -0.0038 249 GLN A N   
2012 C  CA  . GLN A 248 ? 0.1527 0.0980 0.1189 0.0093  -0.0160 -0.0049 249 GLN A CA  
2013 C  C   . GLN A 248 ? 0.1509 0.0732 0.1456 0.0362  -0.0351 0.0035  249 GLN A C   
2014 O  O   . GLN A 248 ? 0.1439 0.0976 0.1679 0.0142  -0.0340 0.0087  249 GLN A O   
2015 C  CB  . GLN A 248 ? 0.1979 0.0738 0.1724 0.0087  -0.0281 0.0119  249 GLN A CB  
2016 C  CG  . GLN A 248 ? 0.1771 0.0974 0.1493 0.0052  0.0000  -0.0048 249 GLN A CG  
2017 C  CD  . GLN A 248 ? 0.1564 0.1014 0.1725 -0.0498 -0.0176 0.0068  249 GLN A CD  
2018 O  OE1 . GLN A 248 ? 0.1665 0.1557 0.2047 -0.0304 -0.0226 -0.0472 249 GLN A OE1 
2019 N  NE2 . GLN A 248 ? 0.1799 0.1253 0.1527 -0.0046 -0.0262 -0.0194 249 GLN A NE2 
2020 N  N   . PRO A 249 ? 0.1517 0.1441 0.1537 0.0310  -0.0296 -0.0154 250 PRO A N   
2021 C  CA  . PRO A 249 ? 0.1699 0.1727 0.1592 0.0575  -0.0131 -0.0063 250 PRO A CA  
2022 C  C   . PRO A 249 ? 0.1562 0.1061 0.1438 0.0302  -0.0454 -0.0076 250 PRO A C   
2023 O  O   . PRO A 249 ? 0.1847 0.1149 0.1821 0.0310  -0.0417 0.0100  250 PRO A O   
2024 C  CB  . PRO A 249 ? 0.1704 0.2590 0.1727 0.0760  -0.0527 -0.0182 250 PRO A CB  
2025 C  CG  . PRO A 249 ? 0.1919 0.2735 0.1710 0.0383  -0.0386 -0.0273 250 PRO A CG  
2026 C  CD  . PRO A 249 ? 0.1563 0.2187 0.2092 0.0414  -0.0476 -0.0020 250 PRO A CD  
2027 N  N   . LEU A 250 ? 0.1799 0.1194 0.1411 0.0315  -0.0178 -0.0010 251 LEU A N   
2028 C  CA  . LEU A 250 ? 0.1714 0.1250 0.1353 -0.0059 -0.0054 -0.0249 251 LEU A CA  
2029 C  C   . LEU A 250 ? 0.1792 0.0998 0.1379 0.0210  -0.0232 -0.0015 251 LEU A C   
2030 O  O   . LEU A 250 ? 0.1930 0.0860 0.1817 0.0267  -0.0562 -0.0020 251 LEU A O   
2031 C  CB  . LEU A 250 ? 0.2138 0.1192 0.1774 0.0104  0.0138  0.0078  251 LEU A CB  
2032 C  CG  . LEU A 250 ? 0.2346 0.1309 0.1474 -0.0092 0.0342  -0.0108 251 LEU A CG  
2033 C  CD1 . LEU A 250 ? 0.2264 0.1580 0.1703 0.0080  -0.0377 -0.0186 251 LEU A CD1 
2034 C  CD2 . LEU A 250 ? 0.2511 0.1436 0.1851 -0.0395 0.0299  0.0030  251 LEU A CD2 
2035 N  N   . LYS A 251 ? 0.2040 0.1685 0.1386 0.0311  -0.0559 0.0020  252 LYS A N   
2036 C  CA  . LYS A 251 ? 0.2117 0.1851 0.1344 0.0252  -0.0355 -0.0065 252 LYS A CA  
2037 C  C   . LYS A 251 ? 0.2087 0.1965 0.2001 0.0286  -0.0296 -0.0273 252 LYS A C   
2038 O  O   . LYS A 251 ? 0.2588 0.2343 0.2102 0.0032  0.0010  -0.0142 252 LYS A O   
2039 C  CB  . LYS A 251 ? 0.2486 0.1869 0.1937 -0.0083 -0.0379 -0.0242 252 LYS A CB  
2040 C  CG  . LYS A 251 ? 0.2464 0.2149 0.2181 -0.0432 0.0208  -0.0162 252 LYS A CG  
2041 C  CD  . LYS A 251 ? 0.2694 0.3149 0.2530 -0.0275 0.0226  0.0019  252 LYS A CD  
2042 C  CE  . LYS A 251 ? 0.2815 0.3396 0.3065 -0.0023 0.0001  -0.0421 252 LYS A CE  
2043 N  NZ  . LYS A 251 ? 0.3360 0.3693 0.4415 0.0259  0.0141  0.0078  252 LYS A NZ  
2044 N  N   . ASN A 252 ? 0.2113 0.1968 0.1508 0.0529  -0.0441 -0.0454 253 ASN A N   
2045 C  CA  . ASN A 252 ? 0.2615 0.3093 0.2595 0.0294  -0.0329 -0.0410 253 ASN A CA  
2046 C  C   . ASN A 252 ? 0.2322 0.2435 0.2804 0.0410  -0.0197 -0.0214 253 ASN A C   
2047 O  O   . ASN A 252 ? 0.3009 0.2753 0.3166 0.0423  -0.0197 -0.0287 253 ASN A O   
2048 C  CB  . ASN A 252 ? 0.2976 0.3384 0.3190 0.0082  -0.0416 -0.0531 253 ASN A CB  
2049 C  CG  . ASN A 252 ? 0.4242 0.4257 0.3880 0.0195  -0.0171 -0.0280 253 ASN A CG  
2050 O  OD1 . ASN A 252 ? 0.5236 0.5224 0.4975 0.0140  0.0456  0.0030  253 ASN A OD1 
2051 N  ND2 . ASN A 252 ? 0.4167 0.4286 0.4991 0.0313  -0.0432 -0.0108 253 ASN A ND2 
2052 N  N   . ARG A 253 ? 0.1921 0.2313 0.1907 0.0098  -0.0049 -0.0086 254 ARG A N   
2053 C  CA  . ARG A 253 ? 0.1706 0.1507 0.1596 0.0179  -0.0078 -0.0063 254 ARG A CA  
2054 C  C   . ARG A 253 ? 0.2070 0.1418 0.1914 0.0160  0.0015  -0.0266 254 ARG A C   
2055 O  O   . ARG A 253 ? 0.2421 0.1306 0.2821 0.0357  0.0494  0.0190  254 ARG A O   
2056 C  CB  . ARG A 253 ? 0.1926 0.1326 0.1374 0.0261  -0.0089 -0.0083 254 ARG A CB  
2057 C  CG  . ARG A 253 ? 0.2173 0.0982 0.1292 -0.0003 -0.0215 -0.0165 254 ARG A CG  
2058 C  CD  . ARG A 253 ? 0.2214 0.0960 0.1272 0.0278  -0.0083 -0.0408 254 ARG A CD  
2059 N  NE  . ARG A 253 ? 0.1706 0.0776 0.1271 0.0208  -0.0065 -0.0307 254 ARG A NE  
2060 C  CZ  . ARG A 253 ? 0.1576 0.0707 0.1307 -0.0066 0.0148  -0.0410 254 ARG A CZ  
2061 N  NH1 . ARG A 253 ? 0.1310 0.0946 0.1192 0.0167  -0.0260 0.0427  254 ARG A NH1 
2062 N  NH2 . ARG A 253 ? 0.1649 0.0608 0.1415 0.0155  -0.0223 -0.0177 254 ARG A NH2 
2063 N  N   A GLN A 254 ? 0.1662 0.1641 0.1476 0.0119  -0.0074 -0.0551 255 GLN A N   
2064 N  N   B GLN A 254 ? 0.1781 0.1835 0.1735 0.0046  -0.0048 -0.0417 255 GLN A N   
2065 C  CA  A GLN A 254 ? 0.2099 0.1793 0.1749 0.0085  -0.0164 -0.0408 255 GLN A CA  
2066 C  CA  B GLN A 254 ? 0.2134 0.2045 0.1731 0.0013  -0.0131 -0.0295 255 GLN A CA  
2067 C  C   A GLN A 254 ? 0.1871 0.1450 0.1477 0.0137  -0.0284 -0.0153 255 GLN A C   
2068 C  C   B GLN A 254 ? 0.1925 0.1659 0.1605 0.0089  -0.0217 0.0000  255 GLN A C   
2069 O  O   A GLN A 254 ? 0.1936 0.1278 0.2232 0.0010  -0.0454 -0.0306 255 GLN A O   
2070 O  O   B GLN A 254 ? 0.1993 0.1620 0.1704 0.0114  -0.0057 0.0057  255 GLN A O   
2071 C  CB  A GLN A 254 ? 0.2216 0.1907 0.1597 0.0121  -0.0120 -0.0641 255 GLN A CB  
2072 C  CB  B GLN A 254 ? 0.2415 0.2377 0.1865 -0.0052 -0.0103 -0.0234 255 GLN A CB  
2073 C  CG  A GLN A 254 ? 0.2766 0.1829 0.1991 -0.0020 -0.0080 -0.0035 255 GLN A CG  
2074 C  CG  B GLN A 254 ? 0.3506 0.3112 0.2460 0.0017  0.0127  -0.0221 255 GLN A CG  
2075 C  CD  A GLN A 254 ? 0.2838 0.2788 0.2260 0.0126  -0.0024 -0.0140 255 GLN A CD  
2076 C  CD  B GLN A 254 ? 0.3528 0.3860 0.3622 0.0000  0.0167  -0.0384 255 GLN A CD  
2077 O  OE1 A GLN A 254 ? 0.2800 0.3535 0.3256 -0.0109 0.0157  0.0103  255 GLN A OE1 
2078 O  OE1 B GLN A 254 ? 0.4266 0.4391 0.2436 -0.0071 0.0344  -0.0199 255 GLN A OE1 
2079 N  NE2 A GLN A 254 ? 0.3000 0.2735 0.2214 0.0026  -0.0164 -0.0653 255 GLN A NE2 
2080 N  NE2 B GLN A 254 ? 0.3677 0.4002 0.2885 0.0230  0.0284  -0.0485 255 GLN A NE2 
2081 N  N   . ILE A 255 ? 0.1688 0.1219 0.1467 -0.0093 -0.0204 -0.0088 256 ILE A N   
2082 C  CA  . ILE A 255 ? 0.1792 0.1108 0.1289 0.0200  -0.0060 -0.0013 256 ILE A CA  
2083 C  C   . ILE A 255 ? 0.1661 0.1032 0.1463 -0.0027 -0.0175 0.0205  256 ILE A C   
2084 O  O   . ILE A 255 ? 0.2061 0.1116 0.1715 0.0006  0.0114  0.0553  256 ILE A O   
2085 C  CB  . ILE A 255 ? 0.2119 0.1050 0.1228 0.0156  -0.0148 -0.0065 256 ILE A CB  
2086 C  CG1 . ILE A 255 ? 0.1851 0.1090 0.1764 0.0472  0.0098  -0.0329 256 ILE A CG1 
2087 C  CG2 . ILE A 255 ? 0.1889 0.1322 0.1490 0.0269  -0.0020 -0.0031 256 ILE A CG2 
2088 C  CD1 . ILE A 255 ? 0.2120 0.1611 0.1416 -0.0076 -0.0153 -0.0197 256 ILE A CD1 
2089 N  N   . LYS A 256 ? 0.1440 0.1129 0.1493 -0.0008 -0.0233 0.0170  257 LYS A N   
2090 C  CA  . LYS A 256 ? 0.1547 0.0998 0.1401 0.0010  -0.0065 0.0035  257 LYS A CA  
2091 C  C   . LYS A 256 ? 0.1463 0.1057 0.1497 -0.0006 -0.0115 0.0214  257 LYS A C   
2092 O  O   . LYS A 256 ? 0.1761 0.1519 0.1286 -0.0502 0.0076  0.0093  257 LYS A O   
2093 C  CB  . LYS A 256 ? 0.1742 0.1445 0.1693 0.0155  -0.0097 -0.0206 257 LYS A CB  
2094 C  CG  . LYS A 256 ? 0.3036 0.1600 0.2408 -0.0027 0.0082  -0.0577 257 LYS A CG  
2095 C  CD  . LYS A 256 ? 0.3837 0.3051 0.4138 0.0320  -0.0260 -0.0432 257 LYS A CD  
2096 C  CE  . LYS A 256 ? 0.4706 0.3629 0.4541 -0.0239 -0.0240 -0.0220 257 LYS A CE  
2097 N  NZ  . LYS A 256 ? 0.4689 0.3657 0.5748 -0.0092 -0.0138 0.0060  257 LYS A NZ  
2098 N  N   . ALA A 257 ? 0.1580 0.1101 0.1667 -0.0110 0.0082  0.0077  258 ALA A N   
2099 C  CA  . ALA A 257 ? 0.1570 0.1403 0.1958 0.0087  -0.0164 0.0126  258 ALA A CA  
2100 C  C   . ALA A 257 ? 0.1565 0.0953 0.2016 -0.0048 -0.0124 0.0157  258 ALA A C   
2101 O  O   . ALA A 257 ? 0.1749 0.1688 0.1621 0.0060  0.0000  -0.0163 258 ALA A O   
2102 C  CB  . ALA A 257 ? 0.1916 0.0987 0.2500 -0.0294 0.0214  0.0175  258 ALA A CB  
2103 N  N   . SER A 258 ? 0.1645 0.1238 0.1605 0.0031  0.0005  0.0041  259 SER A N   
2104 C  CA  . SER A 258 ? 0.1803 0.1436 0.1786 -0.0010 0.0211  0.0040  259 SER A CA  
2105 C  C   . SER A 258 ? 0.1824 0.1632 0.2055 -0.0077 0.0206  0.0082  259 SER A C   
2106 O  O   . SER A 258 ? 0.1991 0.2576 0.2652 -0.0012 0.0266  0.0204  259 SER A O   
2107 C  CB  . SER A 258 ? 0.1958 0.1279 0.1747 -0.0086 -0.0148 0.0109  259 SER A CB  
2108 O  OG  . SER A 258 ? 0.1858 0.1244 0.1853 -0.0057 0.0152  -0.0092 259 SER A OG  
2109 N  N   . PHE A 259 ? 0.1743 0.2001 0.2268 -0.0281 0.0130  -0.0043 260 PHE A N   
2110 C  CA  . PHE A 259 ? 0.2203 0.1670 0.2331 -0.0564 0.0142  0.0285  260 PHE A CA  
2111 C  C   . PHE A 259 ? 0.2602 0.2475 0.2763 -0.0663 0.0342  0.0395  260 PHE A C   
2112 O  O   . PHE A 259 ? 0.3222 0.2088 0.2638 -0.0674 0.0143  0.0640  260 PHE A O   
2113 C  CB  . PHE A 259 ? 0.2049 0.1889 0.2440 -0.0375 0.0196  0.0081  260 PHE A CB  
2114 C  CG  . PHE A 259 ? 0.2113 0.1756 0.2630 -0.0304 -0.0027 0.0303  260 PHE A CG  
2115 C  CD1 . PHE A 259 ? 0.2142 0.1604 0.1828 -0.0419 -0.0207 -0.0152 260 PHE A CD1 
2116 C  CD2 . PHE A 259 ? 0.2583 0.2295 0.2922 -0.0275 0.0170  0.0273  260 PHE A CD2 
2117 C  CE1 . PHE A 259 ? 0.2138 0.1818 0.2512 -0.0381 -0.0071 0.0181  260 PHE A CE1 
2118 C  CE2 . PHE A 259 ? 0.2498 0.2284 0.2856 -0.0081 0.0003  0.0168  260 PHE A CE2 
2119 C  CZ  . PHE A 259 ? 0.2442 0.2013 0.3046 -0.0154 -0.0085 -0.0153 260 PHE A CZ  
2120 N  N   . LYS A 260 ? 0.3495 0.3219 0.3301 -0.0932 0.0445  0.0447  261 LYS A N   
2121 C  CA  . LYS A 260 ? 0.4631 0.4352 0.4180 -0.0392 0.0148  0.0430  261 LYS A CA  
2122 C  C   . LYS A 260 ? 0.4810 0.5016 0.4670 -0.0428 0.0076  0.0287  261 LYS A C   
2123 O  O   . LYS A 260 ? 0.5090 0.5479 0.5049 -0.0377 0.0121  0.0362  261 LYS A O   
2124 C  CB  . LYS A 260 ? 0.4629 0.4260 0.4149 -0.0364 0.0255  0.0340  261 LYS A CB  
2125 C  CG  . LYS A 260 ? 0.5001 0.4401 0.4459 -0.0450 0.0193  0.0366  261 LYS A CG  
2126 C  CD  . LYS A 260 ? 0.5978 0.5386 0.5105 -0.0126 0.0176  0.0103  261 LYS A CD  
2127 C  CE  . LYS A 260 ? 0.6208 0.5594 0.5715 -0.0335 0.0015  -0.0160 261 LYS A CE  
2128 N  NZ  . LYS A 260 ? 0.6334 0.6223 0.6108 -0.0091 0.0245  0.0209  261 LYS A NZ  
2129 O  OXT . LYS A 260 ? 0.5230 0.5705 0.5408 -0.0263 -0.0006 0.0289  261 LYS A OXT 
2130 ZN ZN  . ZN  B .   ? 0.1497 0.0392 0.1199 -0.0097 -0.0219 -0.0015 262 ZN  A ZN  
2131 S  S   . DMS C .   ? 0.2809 0.2605 0.3133 -0.0093 0.0248  -0.0131 263 DMS A S   
2132 O  O   . DMS C .   ? 0.3319 0.2606 0.3145 0.0465  0.0529  -0.0496 263 DMS A O   
2133 C  C1  . DMS C .   ? 0.2458 0.1908 0.2518 0.0153  0.0333  -0.1097 263 DMS A C1  
2134 C  C2  . DMS C .   ? 0.2894 0.2367 0.3697 -0.0493 0.0252  0.0432  263 DMS A C2  
2135 S  S   . DMS D .   ? 0.3503 0.3428 0.4167 -0.0184 -0.0256 0.0428  264 DMS A S   
2136 O  O   . DMS D .   ? 0.3087 0.3343 0.4423 0.0175  -0.0131 0.0303  264 DMS A O   
2137 C  C1  . DMS D .   ? 0.2408 0.2406 0.3612 0.0384  -0.0252 0.0566  264 DMS A C1  
2138 C  C2  . DMS D .   ? 0.2353 0.2479 0.3669 -0.0740 0.0082  0.0772  264 DMS A C2  
2139 N  N1  . BCN E .   ? 0.4192 0.3273 0.3774 -0.0299 0.0030  0.0109  265 BCN A N1  
2140 C  C1  . BCN E .   ? 0.4107 0.3736 0.3542 -0.0392 -0.0285 0.0089  265 BCN A C1  
2141 C  C2  . BCN E .   ? 0.4047 0.3711 0.3887 -0.0571 0.0065  0.0254  265 BCN A C2  
2142 O  O21 . BCN E .   ? 0.4472 0.3750 0.4656 -0.0434 -0.0127 0.0223  265 BCN A O21 
2143 O  O22 . BCN E .   ? 0.4035 0.4315 0.4355 -0.0384 0.0062  0.0586  265 BCN A O22 
2144 C  C3  . BCN E .   ? 0.3567 0.1507 0.2904 -0.0452 0.0206  0.0108  265 BCN A C3  
2145 C  C4  . BCN E .   ? 0.5123 0.3357 0.4257 -0.0127 -0.0104 -0.0239 265 BCN A C4  
2146 O  O4  . BCN E .   ? 0.5640 0.3395 0.4219 -0.0571 0.0548  -0.0141 265 BCN A O4  
2147 C  C5  . BCN E .   ? 0.3694 0.1876 0.3815 -0.0165 -0.0161 0.0320  265 BCN A C5  
2148 C  C6  . BCN E .   ? 0.5110 0.3732 0.4821 -0.0087 0.0163  -0.0185 265 BCN A C6  
2149 O  O6  . BCN E .   ? 0.4163 0.2842 0.5310 -0.0403 0.0104  0.0020  265 BCN A O6  
2150 N  N1  A E59 F .   ? 0.2673 0.2146 0.2674 -0.0281 0.0000  0.0432  266 E59 A N1  
2151 N  N1  B E59 F .   ? 0.3783 0.3269 0.3496 -0.0136 0.0091  -0.0366 266 E59 A N1  
2152 C  C2  A E59 F .   ? 0.3406 0.2687 0.3222 -0.0038 -0.0210 0.0292  266 E59 A C2  
2153 C  C2  B E59 F .   ? 0.4039 0.3240 0.3579 -0.0189 0.0204  -0.0187 266 E59 A C2  
2154 C  C3  A E59 F .   ? 0.3238 0.2289 0.2911 0.0013  -0.0238 0.0048  266 E59 A C3  
2155 C  C3  B E59 F .   ? 0.4171 0.3273 0.3567 -0.0054 0.0098  -0.0086 266 E59 A C3  
2156 C  C4  A E59 F .   ? 0.3262 0.2407 0.2544 0.0017  0.0001  -0.0031 266 E59 A C4  
2157 C  C4  B E59 F .   ? 0.4193 0.3018 0.3664 -0.0190 0.0008  -0.0010 266 E59 A C4  
2158 N  N5  A E59 F .   ? 0.3082 0.2113 0.3008 0.0645  -0.0192 0.0215  266 E59 A N5  
2159 N  N5  B E59 F .   ? 0.4138 0.3360 0.3747 -0.0215 0.0115  0.0111  266 E59 A N5  
2160 C  C6  A E59 F .   ? 0.2185 0.1911 0.3227 0.0270  -0.0397 0.0302  266 E59 A C6  
2161 C  C6  B E59 F .   ? 0.3855 0.2806 0.3661 -0.0035 0.0044  0.0015  266 E59 A C6  
2162 O  O7  A E59 F .   ? 0.3274 0.3057 0.3000 -0.0156 -0.0326 0.0531  266 E59 A O7  
2163 O  O7  B E59 F .   ? 0.4207 0.3269 0.3650 -0.0041 0.0005  0.0017  266 E59 A O7  
2164 C  C8  A E59 F .   ? 0.2872 0.2396 0.2655 -0.0186 -0.0076 0.0103  266 E59 A C8  
2165 C  C8  B E59 F .   ? 0.3948 0.2888 0.3716 -0.0320 0.0006  -0.0168 266 E59 A C8  
2166 S  S9  A E59 F .   ? 0.2850 0.2235 0.2418 -0.0403 0.0178  0.0276  266 E59 A S9  
2167 S  S9  B E59 F .   ? 0.4236 0.2436 0.3461 -0.0527 0.0265  0.0271  266 E59 A S9  
2168 C  C10 A E59 F .   ? 0.2440 0.1080 0.1973 -0.0432 0.0207  0.0746  266 E59 A C10 
2169 C  C10 B E59 F .   ? 0.2754 0.2320 0.2831 -0.0581 0.0425  0.0535  266 E59 A C10 
2170 C  C11 A E59 F .   ? 0.2106 0.1419 0.2275 -0.0269 0.0077  0.0046  266 E59 A C11 
2171 C  C11 B E59 F .   ? 0.2180 0.1883 0.2489 -0.0164 0.0046  0.0023  266 E59 A C11 
2172 O  O12 A E59 F .   ? 0.2662 0.0900 0.1947 0.0020  -0.0104 0.0419  266 E59 A O12 
2173 O  O12 B E59 F .   ? 0.2486 0.1581 0.3810 0.0141  0.0177  0.0318  266 E59 A O12 
2174 C  C13 A E59 F .   ? 0.1977 0.1323 0.2145 0.0019  0.0384  0.0313  266 E59 A C13 
2175 C  C13 B E59 F .   ? 0.2090 0.0741 0.1077 -0.0081 -0.0384 -0.0149 266 E59 A C13 
2176 C  C14 A E59 F .   ? 0.1547 0.0939 0.1835 -0.0410 0.0043  -0.0149 266 E59 A C14 
2177 C  C14 B E59 F .   ? 0.1676 0.0498 0.1475 0.0065  0.0254  -0.0132 266 E59 A C14 
2178 C  C15 A E59 F .   ? 0.1850 0.0419 0.1407 0.0104  0.0005  -0.0427 266 E59 A C15 
2179 C  C15 B E59 F .   ? 0.1599 0.0276 0.0942 -0.0175 -0.0048 -0.0006 266 E59 A C15 
2180 C  C16 A E59 F .   ? 0.1219 0.1312 0.1077 0.0094  0.0300  -0.0003 266 E59 A C16 
2181 C  C16 B E59 F .   ? 0.1345 0.0630 0.1122 -0.0001 0.0192  -0.0057 266 E59 A C16 
2182 C  C17 A E59 F .   ? 0.1962 0.0953 0.1368 0.0215  0.0373  0.0491  266 E59 A C17 
2183 C  C17 B E59 F .   ? 0.1155 0.0618 0.1472 -0.0414 -0.0027 -0.0222 266 E59 A C17 
2184 C  C18 A E59 F .   ? 0.1533 0.1536 0.1937 -0.0007 0.0566  0.0298  266 E59 A C18 
2185 C  C18 B E59 F .   ? 0.1449 0.0562 0.1418 -0.0410 -0.0024 0.0062  266 E59 A C18 
2186 S  S19 A E59 F .   ? 0.1460 0.0258 0.1814 0.0031  0.0537  0.0024  266 E59 A S19 
2187 S  S19 B E59 F .   ? 0.1206 0.0485 0.0725 -0.0054 -0.0249 -0.0087 266 E59 A S19 
2188 O  O20 A E59 F .   ? 0.1240 0.0671 0.1070 0.0005  -0.0209 -0.0322 266 E59 A O20 
2189 O  O20 B E59 F .   ? 0.1598 0.0341 0.0878 -0.0046 0.0309  0.0207  266 E59 A O20 
2190 O  O21 A E59 F .   ? 0.1381 0.1079 0.1342 -0.0085 -0.0472 -0.0105 266 E59 A O21 
2191 O  O21 B E59 F .   ? 0.1312 0.0377 0.1316 -0.0326 -0.0445 0.0204  266 E59 A O21 
2192 N  N22 A E59 F .   ? 0.1036 0.0768 0.0986 -0.0478 -0.0013 -0.0395 266 E59 A N22 
2193 N  N22 B E59 F .   ? 0.1199 0.0795 0.1036 -0.0121 -0.0419 -0.0507 266 E59 A N22 
2194 O  O   . HOH G .   ? 0.4120 0.2745 0.4887 0.1115  -0.0355 -0.0395 126 HOH A O   
2195 O  O   . HOH G .   ? 0.1474 0.0644 0.1641 -0.0086 -0.0107 0.0157  267 HOH A O   
2196 O  O   . HOH G .   ? 0.1410 0.0791 0.1485 -0.0057 -0.0104 -0.0135 268 HOH A O   
2197 O  O   . HOH G .   ? 0.1908 0.0517 0.1269 0.0115  -0.0226 -0.0102 269 HOH A O   
2198 O  O   . HOH G .   ? 0.1650 0.0867 0.1440 0.0208  -0.0176 0.0093  270 HOH A O   
2199 O  O   . HOH G .   ? 0.1349 0.1185 0.2167 -0.0035 -0.0028 -0.0295 271 HOH A O   
2200 O  O   . HOH G .   ? 0.1720 0.1064 0.1803 0.0223  -0.0292 0.0274  272 HOH A O   
2201 O  O   . HOH G .   ? 0.2073 0.0621 0.1201 -0.0185 -0.0318 0.0000  273 HOH A O   
2202 O  O   . HOH G .   ? 0.1961 0.0738 0.1571 -0.0013 0.0046  -0.0366 274 HOH A O   
2203 O  O   . HOH G .   ? 0.1406 0.1530 0.2447 -0.0012 0.0035  -0.0124 275 HOH A O   
2204 O  O   . HOH G .   ? 0.1987 0.0411 0.1650 -0.0201 0.0015  -0.0093 276 HOH A O   
2205 O  O   . HOH G .   ? 0.2094 0.1104 0.1911 0.0211  -0.0110 0.0138  277 HOH A O   
2206 O  O   . HOH G .   ? 0.1635 0.2045 0.1908 -0.0010 -0.0498 0.0456  278 HOH A O   
2207 O  O   . HOH G .   ? 0.1509 0.0637 0.2027 0.0097  -0.0304 -0.0046 279 HOH A O   
2208 O  O   . HOH G .   ? 0.1544 0.1396 0.1817 -0.0031 -0.0516 0.0507  280 HOH A O   
2209 O  O   . HOH G .   ? 0.1510 0.1427 0.2732 -0.0152 -0.0065 0.0049  281 HOH A O   
2210 O  O   . HOH G .   ? 0.2975 0.1297 0.1950 -0.0250 -0.0738 -0.0006 282 HOH A O   
2211 O  O   . HOH G .   ? 0.2231 0.1098 0.2167 -0.0021 -0.0696 -0.0003 283 HOH A O   
2212 O  O   . HOH G .   ? 0.2435 0.0745 0.2198 -0.0175 -0.0115 0.0197  284 HOH A O   
2213 O  O   . HOH G .   ? 0.2720 0.1524 0.3476 0.0147  -0.1544 -0.0535 285 HOH A O   
2214 O  O   . HOH G .   ? 0.2576 0.1077 0.2371 -0.0340 -0.0627 0.0063  286 HOH A O   
2215 O  O   . HOH G .   ? 0.2167 0.0737 0.2688 0.0063  -0.0480 0.0010  287 HOH A O   
2216 O  O   . HOH G .   ? 0.3032 0.1383 0.2540 0.0395  -0.1134 0.0013  288 HOH A O   
2217 O  O   . HOH G .   ? 0.3019 0.0494 0.2317 0.0313  0.0054  0.0006  289 HOH A O   
2218 O  O   . HOH G .   ? 0.1864 0.1247 0.2538 0.0164  -0.0324 -0.0178 290 HOH A O   
2219 O  O   . HOH G .   ? 0.2806 0.2013 0.2318 0.0126  0.0824  -0.0564 291 HOH A O   
2220 O  O   . HOH G .   ? 0.2382 0.1767 0.3985 0.0434  -0.0593 -0.0099 292 HOH A O   
2221 O  O   . HOH G .   ? 0.2949 0.2134 0.2958 -0.0170 -0.0394 -0.0250 293 HOH A O   
2222 O  O   . HOH G .   ? 0.3477 0.0882 0.2346 -0.0218 -0.1102 -0.0176 294 HOH A O   
2223 O  O   . HOH G .   ? 0.3165 0.1665 0.2483 -0.0148 0.0392  0.0913  295 HOH A O   
2224 O  O   . HOH G .   ? 0.2407 0.1869 0.2162 0.0049  -0.0478 -0.0030 296 HOH A O   
2225 O  O   . HOH G .   ? 0.3129 0.1310 0.3418 -0.0217 -0.0030 -0.0401 297 HOH A O   
2226 O  O   . HOH G .   ? 0.2982 0.1638 0.2745 0.0046  -0.0478 -0.0722 298 HOH A O   
2227 O  O   . HOH G .   ? 0.2243 0.1871 0.2858 0.0275  -0.0601 -0.0588 299 HOH A O   
2228 O  O   . HOH G .   ? 0.2606 0.1151 0.1752 -0.0200 -0.0035 0.0245  300 HOH A O   
2229 O  O   . HOH G .   ? 0.1754 0.1339 0.3476 -0.0304 -0.0662 0.0147  301 HOH A O   
2230 O  O   . HOH G .   ? 0.3122 0.1215 0.2275 0.0214  -0.0516 0.0258  302 HOH A O   
2231 O  O   . HOH G .   ? 0.2513 0.1686 0.3248 0.0142  0.0024  -0.0392 303 HOH A O   
2232 O  O   . HOH G .   ? 0.3659 0.1500 0.2904 0.0674  0.0601  0.0397  304 HOH A O   
2233 O  O   . HOH G .   ? 0.5230 0.2770 0.1800 0.0199  0.0217  0.0359  305 HOH A O   
2234 O  O   . HOH G .   ? 0.2443 0.1401 0.3094 -0.0619 -0.0516 -0.0610 306 HOH A O   
2235 O  O   . HOH G .   ? 0.3040 0.2838 0.3716 0.0179  -0.0008 0.0152  307 HOH A O   
2236 O  O   . HOH G .   ? 0.2338 0.1014 0.2784 -0.0126 0.0350  -0.0054 308 HOH A O   
2237 O  O   . HOH G .   ? 0.3087 0.2238 0.2576 0.0251  0.0287  -0.0081 309 HOH A O   
2238 O  O   . HOH G .   ? 0.1850 0.1500 0.3483 -0.0020 -0.0408 -0.0071 310 HOH A O   
2239 O  O   . HOH G .   ? 0.3377 0.2052 0.1785 -0.0006 -0.0579 -0.0046 311 HOH A O   
2240 O  O   . HOH G .   ? 0.2487 0.1352 0.4053 -0.0450 -0.0724 0.0678  312 HOH A O   
2241 O  O   . HOH G .   ? 0.2951 0.2345 0.3574 0.0164  -0.0566 0.0089  313 HOH A O   
2242 O  O   . HOH G .   ? 0.2849 0.1357 0.2509 -0.0071 -0.0513 0.0062  314 HOH A O   
2243 O  O   . HOH G .   ? 0.3003 0.1570 0.1871 -0.0115 -0.0355 0.0010  315 HOH A O   
2244 O  O   . HOH G .   ? 0.1847 0.3118 0.3508 -0.0185 -0.0529 -0.0013 316 HOH A O   
2245 O  O   . HOH G .   ? 0.3908 0.1925 0.3517 0.0828  -0.0877 -0.0395 317 HOH A O   
2246 O  O   . HOH G .   ? 0.4241 0.1991 0.2728 -0.0240 -0.0127 -0.0419 318 HOH A O   
2247 O  O   . HOH G .   ? 0.2860 0.1674 0.2836 -0.0160 -0.0205 0.0119  319 HOH A O   
2248 O  O   . HOH G .   ? 0.2447 0.3255 0.2671 -0.0926 -0.0304 -0.0355 320 HOH A O   
2249 O  O   . HOH G .   ? 0.4045 0.1599 0.2382 -0.0800 -0.1048 -0.0186 321 HOH A O   
2250 O  O   . HOH G .   ? 0.3804 0.0943 0.3120 0.0465  -0.1295 -0.0198 322 HOH A O   
2251 O  O   . HOH G .   ? 0.3402 0.2913 0.3296 0.0995  -0.0456 0.0082  323 HOH A O   
2252 O  O   . HOH G .   ? 0.2786 0.1315 0.3167 0.0251  0.0351  -0.0390 324 HOH A O   
2253 O  O   . HOH G .   ? 0.2630 0.1977 0.2357 0.0522  -0.0208 0.0715  325 HOH A O   
2254 O  O   . HOH G .   ? 0.2913 0.2364 0.2768 0.0082  -0.0136 0.0834  326 HOH A O   
2255 O  O   . HOH G .   ? 0.2612 0.1528 0.2939 0.0419  -0.0489 0.0121  327 HOH A O   
2256 O  O   . HOH G .   ? 0.1968 0.5709 0.2063 -0.0074 0.0048  0.0046  328 HOH A O   
2257 O  O   . HOH G .   ? 0.1909 0.3266 0.4050 0.0296  -0.0549 0.1033  329 HOH A O   
2258 O  O   . HOH G .   ? 0.2996 0.1212 0.2953 -0.0071 0.0239  -0.0255 330 HOH A O   
2259 O  O   . HOH G .   ? 0.3517 0.2180 0.3603 0.0568  -0.1648 0.0092  331 HOH A O   
2260 O  O   . HOH G .   ? 0.2343 0.2381 0.3346 0.0057  -0.0038 0.0419  332 HOH A O   
2261 O  O   . HOH G .   ? 0.3209 0.1613 0.2317 0.0015  -0.0553 -0.0132 333 HOH A O   
2262 O  O   . HOH G .   ? 0.2566 0.1562 0.2666 0.0225  -0.0865 -0.0559 334 HOH A O   
2263 O  O   . HOH G .   ? 0.3434 0.1520 0.2331 -0.0894 -0.0472 -0.0135 335 HOH A O   
2264 O  O   . HOH G .   ? 0.3077 0.1403 0.4618 -0.0040 0.0544  0.0017  336 HOH A O   
2265 O  O   . HOH G .   ? 0.3707 0.3274 0.4093 -0.1076 -0.0212 -0.0921 337 HOH A O   
2266 O  O   . HOH G .   ? 0.2605 0.1897 0.3880 0.0883  -0.0124 0.0152  338 HOH A O   
2267 O  O   . HOH G .   ? 0.2681 0.2537 0.1994 -0.0163 -0.0092 -0.0603 339 HOH A O   
2268 O  O   . HOH G .   ? 0.3302 0.2723 0.2911 0.0172  -0.0546 -0.0665 340 HOH A O   
2269 O  O   . HOH G .   ? 0.3475 0.2942 0.2698 -0.0372 0.0537  0.0243  341 HOH A O   
2270 O  O   . HOH G .   ? 0.5005 0.1901 0.2040 -0.0592 0.0046  0.0414  342 HOH A O   
2271 O  O   . HOH G .   ? 0.3845 0.2133 0.2788 -0.0256 0.0432  -0.0719 343 HOH A O   
2272 O  O   . HOH G .   ? 0.3960 0.1404 0.3439 0.0806  0.0362  0.0443  344 HOH A O   
2273 O  O   . HOH G .   ? 0.2608 0.2537 0.3510 -0.0318 -0.0516 0.0078  345 HOH A O   
2274 O  O   . HOH G .   ? 0.5996 0.2400 0.4014 0.0733  -0.0046 -0.0076 346 HOH A O   
2275 O  O   . HOH G .   ? 0.3061 0.2361 0.2652 -0.0707 0.0157  0.0357  347 HOH A O   
2276 O  O   . HOH G .   ? 0.3057 0.3866 0.2127 -0.1186 -0.0754 0.0719  348 HOH A O   
2277 O  O   . HOH G .   ? 0.4339 0.3253 0.3062 -0.0143 -0.0071 0.0631  349 HOH A O   
2278 O  O   . HOH G .   ? 0.3039 0.2170 0.3833 -0.0766 -0.0454 0.0502  350 HOH A O   
2279 O  O   . HOH G .   ? 0.3007 0.1890 0.2025 -0.0270 0.0582  0.0489  351 HOH A O   
2280 O  O   . HOH G .   ? 0.2307 0.3737 0.2890 0.0768  -0.0108 0.1164  352 HOH A O   
2281 O  O   . HOH G .   ? 0.3762 0.2055 0.3682 0.0115  0.1076  0.0639  353 HOH A O   
2282 O  O   . HOH G .   ? 0.3460 0.1984 0.1815 0.0157  -0.0436 0.0076  354 HOH A O   
2283 O  O   . HOH G .   ? 0.3021 0.1433 0.2885 -0.0027 -0.0557 0.0137  355 HOH A O   
2284 O  O   . HOH G .   ? 0.5347 0.3004 0.2020 0.0217  0.0137  0.0850  356 HOH A O   
2285 O  O   . HOH G .   ? 0.4404 0.2009 0.2627 -0.0922 0.0886  -0.0690 357 HOH A O   
2286 O  O   . HOH G .   ? 0.4265 0.1727 0.3055 -0.0533 -0.0234 -0.0093 358 HOH A O   
2287 O  O   . HOH G .   ? 0.2821 0.2259 0.2189 -0.0274 -0.0005 -0.0024 359 HOH A O   
2288 O  O   . HOH G .   ? 0.1754 0.2415 0.4262 0.0690  0.0522  0.0154  360 HOH A O   
2289 O  O   . HOH G .   ? 0.4106 0.2460 0.3130 -0.0099 0.0326  -0.0907 361 HOH A O   
2290 O  O   . HOH G .   ? 0.2146 0.2967 0.5074 0.0062  0.0494  0.1050  362 HOH A O   
2291 O  O   . HOH G .   ? 0.3791 0.2368 0.3188 -0.0233 -0.0603 -0.0776 363 HOH A O   
2292 O  O   . HOH G .   ? 0.2892 0.2027 0.3355 -0.0160 -0.0066 0.1037  364 HOH A O   
2293 O  O   . HOH G .   ? 0.4114 0.4135 0.2192 0.0038  -0.0763 0.0825  365 HOH A O   
2294 O  O   . HOH G .   ? 0.3468 0.2296 0.4348 0.0035  -0.0035 -0.1595 366 HOH A O   
2295 O  O   . HOH G .   ? 0.3725 0.3177 0.3234 0.1324  0.0412  0.0615  367 HOH A O   
2296 O  O   . HOH G .   ? 0.3826 0.3091 0.4189 -0.1036 -0.0621 -0.0507 368 HOH A O   
2297 O  O   . HOH G .   ? 0.2836 0.2040 0.2583 0.0028  -0.0771 -0.0087 369 HOH A O   
2298 O  O   . HOH G .   ? 0.4153 0.2489 0.3557 0.0208  -0.0560 -0.1405 370 HOH A O   
2299 O  O   . HOH G .   ? 0.3156 0.3208 0.4199 -0.0593 0.0315  -0.0126 371 HOH A O   
2300 O  O   . HOH G .   ? 0.3898 0.2453 0.2516 -0.0640 -0.0864 -0.0262 372 HOH A O   
2301 O  O   . HOH G .   ? 0.4071 0.1539 0.3184 0.0083  -0.0414 0.0005  373 HOH A O   
2302 O  O   . HOH G .   ? 0.4092 0.1948 0.3421 0.0816  -0.0575 -0.0445 374 HOH A O   
2303 O  O   . HOH G .   ? 0.3980 0.2989 0.2523 0.0535  -0.0074 0.0207  375 HOH A O   
2304 O  O   . HOH G .   ? 0.3406 0.2919 0.3259 -0.0083 -0.0049 -0.0143 376 HOH A O   
2305 O  O   . HOH G .   ? 0.2857 0.2544 0.4354 0.0068  0.0254  -0.0089 377 HOH A O   
2306 O  O   . HOH G .   ? 0.4133 0.2327 0.4370 0.0390  -0.1324 0.0310  378 HOH A O   
2307 O  O   . HOH G .   ? 0.3317 0.2698 0.4538 -0.0559 -0.0305 -0.0882 379 HOH A O   
2308 O  O   . HOH G .   ? 0.4185 0.3506 0.2759 0.0741  0.0388  0.0635  380 HOH A O   
2309 O  O   . HOH G .   ? 0.4095 0.3524 0.2365 -0.1651 -0.0315 -0.0019 381 HOH A O   
2310 O  O   . HOH G .   ? 0.4632 0.4278 0.2314 0.0152  0.0041  0.0960  382 HOH A O   
2311 O  O   . HOH G .   ? 0.4354 0.2687 0.2946 -0.0160 0.0276  0.0608  383 HOH A O   
2312 O  O   . HOH G .   ? 0.3034 0.2134 0.3461 -0.0130 -0.0237 -0.0284 384 HOH A O   
2313 O  O   . HOH G .   ? 0.3048 0.3761 0.3355 -0.0856 -0.0623 -0.0114 385 HOH A O   
2314 O  O   . HOH G .   ? 0.3654 0.0561 0.2404 -0.0193 -0.0275 0.0020  386 HOH A O   
2315 O  O   . HOH G .   ? 0.2950 0.2985 0.3156 -0.0124 -0.0417 0.0026  387 HOH A O   
2316 O  O   . HOH G .   ? 0.3030 0.3089 0.5339 -0.0712 -0.0502 -0.0091 388 HOH A O   
2317 O  O   . HOH G .   ? 0.3533 0.2292 0.3039 0.0502  -0.0549 0.0076  389 HOH A O   
2318 O  O   . HOH G .   ? 0.3050 0.1696 0.3790 0.0260  0.1377  0.0264  390 HOH A O   
2319 O  O   . HOH G .   ? 0.3355 0.2814 0.3201 -0.0886 0.0851  -0.1017 391 HOH A O   
2320 O  O   . HOH G .   ? 0.3970 0.3661 0.2006 0.0612  -0.0040 0.0260  392 HOH A O   
2321 O  O   . HOH G .   ? 0.3716 0.1896 0.3644 0.0076  -0.0199 0.0373  393 HOH A O   
2322 O  O   . HOH G .   ? 0.4782 0.2882 0.2257 0.0203  0.0546  0.1330  394 HOH A O   
2323 O  O   . HOH G .   ? 0.3136 0.2637 0.2318 0.0221  0.0414  -0.0147 395 HOH A O   
2324 O  O   . HOH G .   ? 0.3500 0.2612 0.3327 -0.0183 0.0155  0.0865  396 HOH A O   
2325 O  O   . HOH G .   ? 0.3923 0.3759 0.3641 -0.0584 0.0425  -0.0027 397 HOH A O   
2326 O  O   . HOH G .   ? 0.3161 0.4796 0.2261 -0.2087 -0.1321 0.0738  398 HOH A O   
2327 O  O   . HOH G .   ? 0.3312 0.2964 0.4564 0.0683  -0.0121 0.0201  399 HOH A O   
2328 O  O   . HOH G .   ? 0.2784 0.4485 0.3414 0.0244  -0.0164 0.0063  400 HOH A O   
2329 O  O   . HOH G .   ? 0.4753 0.2243 0.4146 -0.0092 0.0469  0.0822  401 HOH A O   
2330 O  O   . HOH G .   ? 0.3463 0.3949 0.3368 0.0118  -0.0149 0.0872  402 HOH A O   
2331 O  O   . HOH G .   ? 0.4433 0.2642 0.5329 0.0054  -0.0812 -0.1042 403 HOH A O   
2332 O  O   . HOH G .   ? 0.3612 0.4804 0.3831 -0.0441 0.0195  0.0661  404 HOH A O   
2333 O  O   . HOH G .   ? 0.4377 0.3574 0.2675 -0.0988 -0.0303 -0.0147 405 HOH A O   
2334 O  O   . HOH G .   ? 0.3614 0.2756 0.4814 0.0303  -0.0303 -0.1054 406 HOH A O   
2335 O  O   . HOH G .   ? 0.4259 0.4146 0.4778 -0.0353 -0.0122 0.1040  407 HOH A O   
2336 O  O   . HOH G .   ? 0.2102 0.2820 0.4884 0.0463  -0.0428 -0.0199 408 HOH A O   
2337 O  O   . HOH G .   ? 0.4911 0.3147 0.3317 0.0588  0.0601  -0.0896 409 HOH A O   
2338 O  O   . HOH G .   ? 0.4293 0.2971 0.2940 -0.1287 0.0469  -0.0115 410 HOH A O   
2339 O  O   . HOH G .   ? 0.3217 0.2516 0.3804 0.0498  -0.1424 -0.1473 411 HOH A O   
2340 O  O   . HOH G .   ? 0.3418 0.2480 0.4591 -0.0098 0.0974  0.0166  412 HOH A O   
2341 O  O   . HOH G .   ? 0.3212 0.2443 0.3353 0.0447  -0.0546 0.0430  413 HOH A O   
2342 O  O   . HOH G .   ? 0.3136 0.2743 0.4286 0.0832  -0.1084 -0.0041 414 HOH A O   
2343 O  O   . HOH G .   ? 0.3101 0.2252 0.5734 -0.0187 0.0109  0.0024  415 HOH A O   
2344 O  O   . HOH G .   ? 0.3988 0.3697 0.5943 0.1423  -0.0082 0.0403  416 HOH A O   
2345 O  O   . HOH G .   ? 0.3357 0.5101 0.3377 0.0320  -0.0760 0.1068  417 HOH A O   
2346 O  O   . HOH G .   ? 0.3370 0.1714 0.4108 -0.0263 0.0762  -0.0292 418 HOH A O   
2347 O  O   . HOH G .   ? 0.3791 0.3197 0.5461 -0.0151 0.0118  0.0256  419 HOH A O   
2348 O  O   . HOH G .   ? 0.5568 0.3585 0.2160 -0.1171 -0.1696 -0.0043 420 HOH A O   
2349 O  O   . HOH G .   ? 0.4542 0.5476 0.3869 -0.0153 0.1494  -0.0119 421 HOH A O   
2350 O  O   . HOH G .   ? 0.2235 0.1420 0.6542 -0.0392 0.1193  -0.0439 422 HOH A O   
2351 O  O   . HOH G .   ? 0.3521 0.2652 0.3863 0.0233  -0.0006 0.0579  423 HOH A O   
2352 O  O   . HOH G .   ? 0.3332 0.2759 0.2795 -0.0582 -0.0012 -0.0632 424 HOH A O   
2353 O  O   . HOH G .   ? 0.3963 0.1569 0.2906 -0.0220 -0.0795 -0.0074 425 HOH A O   
2354 O  O   . HOH G .   ? 0.4110 0.1547 0.4128 -0.0542 0.0167  -0.0108 426 HOH A O   
2355 O  O   . HOH G .   ? 0.3676 0.4419 0.3409 -0.0108 -0.0153 0.0359  427 HOH A O   
2356 O  O   . HOH G .   ? 0.5982 0.3675 0.2142 -0.0337 0.0599  0.0874  428 HOH A O   
2357 O  O   . HOH G .   ? 0.4431 0.4955 0.4654 0.0259  -0.0401 0.0108  429 HOH A O   
2358 O  O   . HOH G .   ? 0.4933 0.3022 0.2985 0.0461  -0.0116 0.1454  430 HOH A O   
2359 O  O   . HOH G .   ? 0.4563 0.3453 0.4515 0.0274  -0.0121 0.0610  431 HOH A O   
2360 O  O   . HOH G .   ? 0.3968 0.3271 0.4200 -0.0324 0.0445  -0.0307 432 HOH A O   
2361 O  O   . HOH G .   ? 0.5210 0.2666 0.3352 0.0555  0.0059  0.0027  433 HOH A O   
2362 O  O   . HOH G .   ? 0.4343 0.3440 0.5055 0.1350  0.0489  0.1146  434 HOH A O   
2363 O  O   . HOH G .   ? 0.2615 0.1873 0.4419 -0.0522 0.0214  -0.0100 435 HOH A O   
2364 O  O   . HOH G .   ? 0.3198 0.2943 0.4338 -0.0160 0.0060  -0.0789 436 HOH A O   
2365 O  O   . HOH G .   ? 0.3715 0.2890 0.4727 -0.0573 -0.0324 -0.1423 437 HOH A O   
2366 O  O   . HOH G .   ? 0.4268 0.2088 0.3374 0.0137  0.0283  0.1108  438 HOH A O   
2367 O  O   . HOH G .   ? 0.3294 0.1912 0.3212 0.0342  -0.0300 -0.0384 439 HOH A O   
2368 O  O   . HOH G .   ? 0.1993 0.5364 0.4081 0.0331  -0.0308 -0.1667 440 HOH A O   
2369 O  O   . HOH G .   ? 0.3118 0.2990 0.4011 -0.0281 0.0868  0.1081  441 HOH A O   
2370 O  O   . HOH G .   ? 0.5381 0.2332 0.2164 0.0055  -0.0288 0.0000  442 HOH A O   
2371 O  O   . HOH G .   ? 0.3482 0.3513 0.3727 -0.0983 0.1102  -0.0474 443 HOH A O   
2372 O  O   . HOH G .   ? 0.3556 0.2110 0.4605 -0.0104 -0.1061 -0.0346 444 HOH A O   
2373 O  O   . HOH G .   ? 0.5162 0.2205 0.4045 -0.0126 -0.0538 0.0208  445 HOH A O   
2374 O  O   . HOH G .   ? 0.4002 0.2047 0.3816 -0.0719 -0.1185 0.0509  446 HOH A O   
2375 O  O   . HOH G .   ? 0.4990 0.1948 0.3725 -0.0653 -0.0627 -0.0557 447 HOH A O   
2376 O  O   . HOH G .   ? 0.3062 0.2558 0.5486 -0.0947 0.0351  0.0227  448 HOH A O   
2377 O  O   . HOH G .   ? 0.4824 0.2328 0.4168 0.0381  0.0003  -0.1125 449 HOH A O   
2378 O  O   . HOH G .   ? 0.3711 0.4158 0.3385 0.1062  0.0049  -0.0068 450 HOH A O   
2379 O  O   . HOH G .   ? 0.6595 0.3054 0.4337 0.0516  -0.0388 -0.0171 451 HOH A O   
2380 O  O   . HOH G .   ? 0.4485 0.2095 0.3064 -0.0553 -0.0342 0.0445  452 HOH A O   
2381 O  O   . HOH G .   ? 0.5404 0.3047 0.2753 -0.0652 -0.0698 -0.1172 453 HOH A O   
2382 O  O   . HOH G .   ? 0.3851 0.4038 0.3438 0.0303  0.0458  -0.0722 454 HOH A O   
2383 O  O   . HOH G .   ? 0.4347 0.2458 0.4322 0.0214  0.0802  0.0869  455 HOH A O   
2384 O  O   . HOH G .   ? 0.3357 0.4966 0.4178 -0.0322 0.0553  0.0688  456 HOH A O   
2385 O  O   . HOH G .   ? 0.3294 0.4300 0.5038 0.0487  -0.0310 0.0553  457 HOH A O   
2386 O  O   . HOH G .   ? 0.3345 0.4032 0.5034 0.0017  0.0052  -0.0082 458 HOH A O   
2387 O  O   . HOH G .   ? 0.5095 0.4253 0.2303 -0.0452 0.0419  0.0175  459 HOH A O   
2388 O  O   . HOH G .   ? 0.2332 0.1479 0.5526 0.0643  0.0794  0.1247  460 HOH A O   
2389 O  O   . HOH G .   ? 0.3707 0.2453 0.6129 -0.0273 0.0272  0.0236  461 HOH A O   
2390 O  O   . HOH G .   ? 0.5533 0.2352 0.6398 -0.0351 0.0520  -0.0197 462 HOH A O   
2391 O  O   . HOH G .   ? 0.4902 0.4174 0.4864 0.0869  -0.0379 -0.0258 463 HOH A O   
2392 O  O   . HOH G .   ? 0.4309 0.4196 0.3852 -0.0217 0.0170  0.0204  464 HOH A O   
2393 O  O   . HOH G .   ? 0.2967 0.5813 0.5382 0.0157  0.0237  -0.0157 465 HOH A O   
2394 O  O   . HOH G .   ? 0.4102 0.2802 0.4478 -0.0234 -0.1381 -0.1120 466 HOH A O   
2395 O  O   . HOH G .   ? 0.4315 0.4569 0.5386 0.0683  0.0195  0.0571  467 HOH A O   
2396 O  O   . HOH G .   ? 0.4248 0.2489 0.5440 -0.0619 0.0167  0.0472  468 HOH A O   
2397 O  O   . HOH G .   ? 0.5720 0.2763 0.3995 0.0903  0.0588  -0.0353 469 HOH A O   
2398 O  O   . HOH G .   ? 0.4138 0.3490 0.4688 0.0989  -0.0108 -0.0269 470 HOH A O   
2399 O  O   . HOH G .   ? 0.4156 0.2026 0.4818 0.0046  -0.1027 -0.0197 471 HOH A O   
2400 O  O   . HOH G .   ? 0.3973 0.1871 0.5062 -0.0161 0.1360  0.0110  472 HOH A O   
2401 O  O   . HOH G .   ? 0.3269 0.4011 0.5221 0.0454  0.0294  -0.0476 473 HOH A O   
2402 O  O   . HOH G .   ? 0.4563 0.2469 0.4358 0.0410  -0.0340 -0.0410 474 HOH A O   
2403 O  O   . HOH G .   ? 0.4067 0.1360 0.3643 0.0164  -0.0824 -0.0233 475 HOH A O   
2404 O  O   . HOH G .   ? 0.5207 0.3435 0.4433 0.0083  0.0546  0.0644  476 HOH A O   
2405 O  O   . HOH G .   ? 0.5242 0.4771 0.5727 0.0065  0.0208  -0.0276 477 HOH A O   
2406 O  O   . HOH G .   ? 0.6384 0.5386 0.5364 -0.0120 -0.0120 0.0027  478 HOH A O   
2407 O  O   . HOH G .   ? 0.4235 0.3023 0.4102 -0.0430 -0.1345 0.0671  479 HOH A O   
2408 O  O   . HOH G .   ? 0.4322 0.4732 0.3393 0.0608  -0.0683 0.2282  480 HOH A O   
2409 O  O   . HOH G .   ? 0.4459 0.3457 0.5422 -0.0825 -0.0218 -0.0375 481 HOH A O   
2410 O  O   . HOH G .   ? 0.3245 0.5027 0.4433 -0.0344 -0.0162 -0.0342 482 HOH A O   
2411 O  O   . HOH G .   ? 0.4049 0.4459 0.3871 0.0619  -0.0044 -0.0205 483 HOH A O   
2412 O  O   . HOH G .   ? 0.4498 0.4210 0.4160 -0.0046 0.1057  -0.0657 484 HOH A O   
2413 O  O   . HOH G .   ? 0.3810 0.2881 0.4494 0.0564  0.0302  0.0533  485 HOH A O   
2414 O  O   . HOH G .   ? 0.4521 0.2421 0.5763 0.0096  -0.0938 0.0208  486 HOH A O   
2415 O  O   . HOH G .   ? 0.3761 0.5698 0.3586 0.0013  -0.0171 -0.0015 487 HOH A O   
2416 O  O   . HOH G .   ? 0.4584 0.3316 0.2863 -0.0487 -0.0156 0.0820  488 HOH A O   
2417 O  O   . HOH G .   ? 0.4611 0.3851 0.3828 0.0628  -0.0746 0.0891  489 HOH A O   
2418 O  O   . HOH G .   ? 0.4161 0.2685 0.3550 0.0109  -0.0115 0.0359  490 HOH A O   
2419 O  O   . HOH G .   ? 0.4629 0.5212 0.3708 -0.0264 -0.0355 0.0275  491 HOH A O   
2420 O  O   . HOH G .   ? 0.4871 0.4133 0.4230 0.0575  -0.0066 0.0020  492 HOH A O   
2421 O  O   . HOH G .   ? 0.4545 0.2714 0.2675 0.0140  -0.0207 -0.0348 493 HOH A O   
2422 O  O   . HOH G .   ? 0.5023 0.4291 0.3986 0.0474  -0.0324 0.1036  494 HOH A O   
2423 O  O   . HOH G .   ? 0.5752 0.2953 0.4131 -0.0601 -0.0320 -0.0024 495 HOH A O   
2424 O  O   . HOH G .   ? 0.5605 0.4373 0.2493 0.0595  -0.0274 0.0657  496 HOH A O   
2425 O  O   . HOH G .   ? 0.3610 0.3641 0.3840 0.0384  0.0961  -0.0335 497 HOH A O   
2426 O  O   . HOH G .   ? 0.4835 0.3898 0.4650 -0.0077 -0.0157 -0.1040 498 HOH A O   
2427 O  O   . HOH G .   ? 0.3916 0.4322 0.4434 0.0131  0.0852  -0.0527 499 HOH A O   
2428 O  O   . HOH G .   ? 0.5005 0.3483 0.3794 0.0546  0.0465  -0.0553 500 HOH A O   
2429 O  O   . HOH G .   ? 0.3851 0.3995 0.4005 0.0502  0.0549  -0.0406 501 HOH A O   
2430 O  O   . HOH G .   ? 0.5432 0.4038 0.3815 0.0030  -0.0285 -0.0199 502 HOH A O   
2431 O  O   . HOH G .   ? 0.4498 0.3294 0.4487 -0.1537 -0.0195 0.0865  503 HOH A O   
2432 O  O   . HOH G .   ? 0.4570 0.1509 0.3984 0.0195  -0.0467 0.0381  504 HOH A O   
2433 O  O   . HOH G .   ? 0.3905 0.4745 0.5184 0.1316  0.0013  0.0027  505 HOH A O   
2434 O  O   . HOH G .   ? 0.5296 0.3222 0.4372 0.0649  0.0643  0.0176  506 HOH A O   
2435 O  O   . HOH G .   ? 0.5339 0.3840 0.4147 -0.0035 0.0502  -0.0410 507 HOH A O   
2436 O  O   . HOH G .   ? 0.4990 0.3607 0.4796 0.0502  -0.0156 -0.0114 508 HOH A O   
2437 O  O   . HOH G .   ? 0.4397 0.4490 0.3095 -0.0399 -0.0017 0.0351  509 HOH A O   
2438 O  O   . HOH G .   ? 0.5178 0.2045 0.3130 0.0680  0.0304  0.0140  510 HOH A O   
2439 O  O   . HOH G .   ? 0.4462 0.4699 0.3625 0.0608  -0.0913 0.0822  511 HOH A O   
2440 O  O   . HOH G .   ? 0.3262 0.3463 0.2779 0.0233  -0.0715 0.0302  512 HOH A O   
2441 O  O   . HOH G .   ? 0.3592 0.3506 0.4882 0.0017  0.0120  0.1036  513 HOH A O   
# 
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   262 1   ZN  ZN  A . 
C 3 DMS 1   263 1   DMS DMS A . 
D 3 DMS 1   264 2   DMS DMS A . 
E 4 BCN 1   265 1   BCN BCN A . 
F 5 E59 1   266 1   E59 E59 A . 
G 6 HOH 1   126 126 HOH HOH A . 
G 6 HOH 2   267 1   HOH HOH A . 
G 6 HOH 3   268 2   HOH HOH A . 
G 6 HOH 4   269 3   HOH HOH A . 
G 6 HOH 5   270 4   HOH HOH A . 
G 6 HOH 6   271 5   HOH HOH A . 
G 6 HOH 7   272 6   HOH HOH A . 
G 6 HOH 8   273 7   HOH HOH A . 
G 6 HOH 9   274 8   HOH HOH A . 
G 6 HOH 10  275 9   HOH HOH A . 
G 6 HOH 11  276 10  HOH HOH A . 
G 6 HOH 12  277 11  HOH HOH A . 
G 6 HOH 13  278 12  HOH HOH A . 
G 6 HOH 14  279 13  HOH HOH A . 
G 6 HOH 15  280 14  HOH HOH A . 
G 6 HOH 16  281 15  HOH HOH A . 
G 6 HOH 17  282 16  HOH HOH A . 
G 6 HOH 18  283 17  HOH HOH A . 
G 6 HOH 19  284 18  HOH HOH A . 
G 6 HOH 20  285 19  HOH HOH A . 
G 6 HOH 21  286 20  HOH HOH A . 
G 6 HOH 22  287 21  HOH HOH A . 
G 6 HOH 23  288 22  HOH HOH A . 
G 6 HOH 24  289 23  HOH HOH A . 
G 6 HOH 25  290 24  HOH HOH A . 
G 6 HOH 26  291 25  HOH HOH A . 
G 6 HOH 27  292 26  HOH HOH A . 
G 6 HOH 28  293 27  HOH HOH A . 
G 6 HOH 29  294 28  HOH HOH A . 
G 6 HOH 30  295 29  HOH HOH A . 
G 6 HOH 31  296 30  HOH HOH A . 
G 6 HOH 32  297 31  HOH HOH A . 
G 6 HOH 33  298 32  HOH HOH A . 
G 6 HOH 34  299 33  HOH HOH A . 
G 6 HOH 35  300 34  HOH HOH A . 
G 6 HOH 36  301 35  HOH HOH A . 
G 6 HOH 37  302 36  HOH HOH A . 
G 6 HOH 38  303 37  HOH HOH A . 
G 6 HOH 39  304 38  HOH HOH A . 
G 6 HOH 40  305 39  HOH HOH A . 
G 6 HOH 41  306 40  HOH HOH A . 
G 6 HOH 42  307 41  HOH HOH A . 
G 6 HOH 43  308 42  HOH HOH A . 
G 6 HOH 44  309 43  HOH HOH A . 
G 6 HOH 45  310 44  HOH HOH A . 
G 6 HOH 46  311 45  HOH HOH A . 
G 6 HOH 47  312 46  HOH HOH A . 
G 6 HOH 48  313 47  HOH HOH A . 
G 6 HOH 49  314 48  HOH HOH A . 
G 6 HOH 50  315 49  HOH HOH A . 
G 6 HOH 51  316 50  HOH HOH A . 
G 6 HOH 52  317 51  HOH HOH A . 
G 6 HOH 53  318 52  HOH HOH A . 
G 6 HOH 54  319 53  HOH HOH A . 
G 6 HOH 55  320 54  HOH HOH A . 
G 6 HOH 56  321 55  HOH HOH A . 
G 6 HOH 57  322 56  HOH HOH A . 
G 6 HOH 58  323 57  HOH HOH A . 
G 6 HOH 59  324 58  HOH HOH A . 
G 6 HOH 60  325 59  HOH HOH A . 
G 6 HOH 61  326 60  HOH HOH A . 
G 6 HOH 62  327 61  HOH HOH A . 
G 6 HOH 63  328 62  HOH HOH A . 
G 6 HOH 64  329 63  HOH HOH A . 
G 6 HOH 65  330 64  HOH HOH A . 
G 6 HOH 66  331 65  HOH HOH A . 
G 6 HOH 67  332 66  HOH HOH A . 
G 6 HOH 68  333 67  HOH HOH A . 
G 6 HOH 69  334 68  HOH HOH A . 
G 6 HOH 70  335 69  HOH HOH A . 
G 6 HOH 71  336 70  HOH HOH A . 
G 6 HOH 72  337 71  HOH HOH A . 
G 6 HOH 73  338 72  HOH HOH A . 
G 6 HOH 74  339 73  HOH HOH A . 
G 6 HOH 75  340 74  HOH HOH A . 
G 6 HOH 76  341 75  HOH HOH A . 
G 6 HOH 77  342 76  HOH HOH A . 
G 6 HOH 78  343 77  HOH HOH A . 
G 6 HOH 79  344 78  HOH HOH A . 
G 6 HOH 80  345 79  HOH HOH A . 
G 6 HOH 81  346 80  HOH HOH A . 
G 6 HOH 82  347 81  HOH HOH A . 
G 6 HOH 83  348 82  HOH HOH A . 
G 6 HOH 84  349 83  HOH HOH A . 
G 6 HOH 85  350 84  HOH HOH A . 
G 6 HOH 86  351 85  HOH HOH A . 
G 6 HOH 87  352 86  HOH HOH A . 
G 6 HOH 88  353 87  HOH HOH A . 
G 6 HOH 89  354 88  HOH HOH A . 
G 6 HOH 90  355 89  HOH HOH A . 
G 6 HOH 91  356 90  HOH HOH A . 
G 6 HOH 92  357 91  HOH HOH A . 
G 6 HOH 93  358 92  HOH HOH A . 
G 6 HOH 94  359 93  HOH HOH A . 
G 6 HOH 95  360 94  HOH HOH A . 
G 6 HOH 96  361 95  HOH HOH A . 
G 6 HOH 97  362 96  HOH HOH A . 
G 6 HOH 98  363 97  HOH HOH A . 
G 6 HOH 99  364 98  HOH HOH A . 
G 6 HOH 100 365 99  HOH HOH A . 
G 6 HOH 101 366 100 HOH HOH A . 
G 6 HOH 102 367 101 HOH HOH A . 
G 6 HOH 103 368 102 HOH HOH A . 
G 6 HOH 104 369 103 HOH HOH A . 
G 6 HOH 105 370 104 HOH HOH A . 
G 6 HOH 106 371 105 HOH HOH A . 
G 6 HOH 107 372 106 HOH HOH A . 
G 6 HOH 108 373 107 HOH HOH A . 
G 6 HOH 109 374 108 HOH HOH A . 
G 6 HOH 110 375 109 HOH HOH A . 
G 6 HOH 111 376 110 HOH HOH A . 
G 6 HOH 112 377 111 HOH HOH A . 
G 6 HOH 113 378 112 HOH HOH A . 
G 6 HOH 114 379 113 HOH HOH A . 
G 6 HOH 115 380 114 HOH HOH A . 
G 6 HOH 116 381 115 HOH HOH A . 
G 6 HOH 117 382 116 HOH HOH A . 
G 6 HOH 118 383 117 HOH HOH A . 
G 6 HOH 119 384 118 HOH HOH A . 
G 6 HOH 120 385 119 HOH HOH A . 
G 6 HOH 121 386 120 HOH HOH A . 
G 6 HOH 122 387 121 HOH HOH A . 
G 6 HOH 123 388 122 HOH HOH A . 
G 6 HOH 124 389 123 HOH HOH A . 
G 6 HOH 125 390 124 HOH HOH A . 
G 6 HOH 126 391 125 HOH HOH A . 
G 6 HOH 127 392 127 HOH HOH A . 
G 6 HOH 128 393 128 HOH HOH A . 
G 6 HOH 129 394 129 HOH HOH A . 
G 6 HOH 130 395 130 HOH HOH A . 
G 6 HOH 131 396 131 HOH HOH A . 
G 6 HOH 132 397 132 HOH HOH A . 
G 6 HOH 133 398 133 HOH HOH A . 
G 6 HOH 134 399 134 HOH HOH A . 
G 6 HOH 135 400 135 HOH HOH A . 
G 6 HOH 136 401 136 HOH HOH A . 
G 6 HOH 137 402 137 HOH HOH A . 
G 6 HOH 138 403 138 HOH HOH A . 
G 6 HOH 139 404 139 HOH HOH A . 
G 6 HOH 140 405 140 HOH HOH A . 
G 6 HOH 141 406 141 HOH HOH A . 
G 6 HOH 142 407 142 HOH HOH A . 
G 6 HOH 143 408 143 HOH HOH A . 
G 6 HOH 144 409 144 HOH HOH A . 
G 6 HOH 145 410 145 HOH HOH A . 
G 6 HOH 146 411 146 HOH HOH A . 
G 6 HOH 147 412 147 HOH HOH A . 
G 6 HOH 148 413 148 HOH HOH A . 
G 6 HOH 149 414 149 HOH HOH A . 
G 6 HOH 150 415 150 HOH HOH A . 
G 6 HOH 151 416 151 HOH HOH A . 
G 6 HOH 152 417 152 HOH HOH A . 
G 6 HOH 153 418 153 HOH HOH A . 
G 6 HOH 154 419 154 HOH HOH A . 
G 6 HOH 155 420 155 HOH HOH A . 
G 6 HOH 156 421 156 HOH HOH A . 
G 6 HOH 157 422 157 HOH HOH A . 
G 6 HOH 158 423 158 HOH HOH A . 
G 6 HOH 159 424 159 HOH HOH A . 
G 6 HOH 160 425 160 HOH HOH A . 
G 6 HOH 161 426 161 HOH HOH A . 
G 6 HOH 162 427 162 HOH HOH A . 
G 6 HOH 163 428 163 HOH HOH A . 
G 6 HOH 164 429 164 HOH HOH A . 
G 6 HOH 165 430 165 HOH HOH A . 
G 6 HOH 166 431 166 HOH HOH A . 
G 6 HOH 167 432 167 HOH HOH A . 
G 6 HOH 168 433 168 HOH HOH A . 
G 6 HOH 169 434 169 HOH HOH A . 
G 6 HOH 170 435 170 HOH HOH A . 
G 6 HOH 171 436 171 HOH HOH A . 
G 6 HOH 172 437 172 HOH HOH A . 
G 6 HOH 173 438 173 HOH HOH A . 
G 6 HOH 174 439 174 HOH HOH A . 
G 6 HOH 175 440 175 HOH HOH A . 
G 6 HOH 176 441 176 HOH HOH A . 
G 6 HOH 177 442 177 HOH HOH A . 
G 6 HOH 178 443 178 HOH HOH A . 
G 6 HOH 179 444 179 HOH HOH A . 
G 6 HOH 180 445 180 HOH HOH A . 
G 6 HOH 181 446 181 HOH HOH A . 
G 6 HOH 182 447 182 HOH HOH A . 
G 6 HOH 183 448 183 HOH HOH A . 
G 6 HOH 184 449 184 HOH HOH A . 
G 6 HOH 185 450 185 HOH HOH A . 
G 6 HOH 186 451 186 HOH HOH A . 
G 6 HOH 187 452 187 HOH HOH A . 
G 6 HOH 188 453 188 HOH HOH A . 
G 6 HOH 189 454 189 HOH HOH A . 
G 6 HOH 190 455 190 HOH HOH A . 
G 6 HOH 191 456 191 HOH HOH A . 
G 6 HOH 192 457 192 HOH HOH A . 
G 6 HOH 193 458 193 HOH HOH A . 
G 6 HOH 194 459 194 HOH HOH A . 
G 6 HOH 195 460 195 HOH HOH A . 
G 6 HOH 196 461 196 HOH HOH A . 
G 6 HOH 197 462 197 HOH HOH A . 
G 6 HOH 198 463 198 HOH HOH A . 
G 6 HOH 199 464 199 HOH HOH A . 
G 6 HOH 200 465 200 HOH HOH A . 
G 6 HOH 201 466 201 HOH HOH A . 
G 6 HOH 202 467 202 HOH HOH A . 
G 6 HOH 203 468 203 HOH HOH A . 
G 6 HOH 204 469 204 HOH HOH A . 
G 6 HOH 205 470 205 HOH HOH A . 
G 6 HOH 206 471 206 HOH HOH A . 
G 6 HOH 207 472 207 HOH HOH A . 
G 6 HOH 208 473 208 HOH HOH A . 
G 6 HOH 209 474 209 HOH HOH A . 
G 6 HOH 210 475 210 HOH HOH A . 
G 6 HOH 211 476 211 HOH HOH A . 
G 6 HOH 212 477 212 HOH HOH A . 
G 6 HOH 213 478 213 HOH HOH A . 
G 6 HOH 214 479 214 HOH HOH A . 
G 6 HOH 215 480 215 HOH HOH A . 
G 6 HOH 216 481 216 HOH HOH A . 
G 6 HOH 217 482 217 HOH HOH A . 
G 6 HOH 218 483 218 HOH HOH A . 
G 6 HOH 219 484 219 HOH HOH A . 
G 6 HOH 220 485 220 HOH HOH A . 
G 6 HOH 221 486 221 HOH HOH A . 
G 6 HOH 222 487 222 HOH HOH A . 
G 6 HOH 223 488 223 HOH HOH A . 
G 6 HOH 224 489 224 HOH HOH A . 
G 6 HOH 225 490 225 HOH HOH A . 
G 6 HOH 226 491 226 HOH HOH A . 
G 6 HOH 227 492 227 HOH HOH A . 
G 6 HOH 228 493 228 HOH HOH A . 
G 6 HOH 229 494 229 HOH HOH A . 
G 6 HOH 230 495 230 HOH HOH A . 
G 6 HOH 231 496 231 HOH HOH A . 
G 6 HOH 232 497 232 HOH HOH A . 
G 6 HOH 233 498 233 HOH HOH A . 
G 6 HOH 234 499 234 HOH HOH A . 
G 6 HOH 235 500 235 HOH HOH A . 
G 6 HOH 236 501 236 HOH HOH A . 
G 6 HOH 237 502 237 HOH HOH A . 
G 6 HOH 238 503 238 HOH HOH A . 
G 6 HOH 239 504 239 HOH HOH A . 
G 6 HOH 240 505 240 HOH HOH A . 
G 6 HOH 241 506 241 HOH HOH A . 
G 6 HOH 242 507 242 HOH HOH A . 
G 6 HOH 243 508 243 HOH HOH A . 
G 6 HOH 244 509 244 HOH HOH A . 
G 6 HOH 245 510 245 HOH HOH A . 
G 6 HOH 246 511 246 HOH HOH A . 
G 6 HOH 247 512 247 HOH HOH A . 
G 6 HOH 248 513 248 HOH HOH A . 
# 
_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 
# 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 262 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.4 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.9 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.1  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 B F E59 .   ? A E59 266 ? 1_555 111.5 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 B F E59 .   ? A E59 266 ? 1_555 110.3 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 B F E59 .   ? A E59 266 ? 1_555 118.7 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 A F E59 .   ? A E59 266 ? 1_555 111.7 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 A F E59 .   ? A E59 266 ? 1_555 110.4 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 A F E59 .   ? A E59 266 ? 1_555 118.4 ? 
10 N22 B F E59 .   ? A E59 266 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 A F E59 .   ? A E59 266 ? 1_555 0.3   ? 
# 
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 2012-04-11 
2 'Structure model' 1 1 2012-05-16 
3 'Structure model' 1 2 2017-11-08 
4 'Structure model' 1 3 2023-09-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Refinement description' 
3 4 'Structure model' 'Data collection'        
4 4 'Structure model' 'Database references'    
5 4 'Structure model' 'Derived calculations'   
6 4 '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 3 'Structure model' software                      
2 4 'Structure model' chem_comp_atom                
3 4 'Structure model' chem_comp_bond                
4 4 'Structure model' database_2                    
5 4 'Structure model' diffrn_source                 
6 4 'Structure model' pdbx_initial_refinement_model 
7 4 'Structure model' pdbx_struct_conn_angle        
8 4 'Structure model' struct_conn                   
9 4 'Structure model' struct_site                   
# 
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  3 'Structure model' '_software.name'                              
2  4 'Structure model' '_database_2.pdbx_DOI'                        
3  4 'Structure model' '_database_2.pdbx_database_accession'         
4  4 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
8  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
13 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
15 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
16 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
17 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
18 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
19 4 'Structure model' '_pdbx_struct_conn_angle.value'               
20 4 'Structure model' '_struct_conn.pdbx_dist_value'                
21 4 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
22 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
23 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
24 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
25 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
26 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
27 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
28 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
29 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
30 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
31 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
32 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
33 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
34 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
35 4 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .                              ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .                              ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19                         22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006                          'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345      'v. 0.10.22 on RedHat Linux 8' ?               ?       ?                    ?                        'data collection' 
?                                            ?          ? 5 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 N  A GLY 8  ? ? CA  A GLY 8  ? ? 1.568 1.456 0.112 0.015 N 
2 1 CD A GLU 14 ? B OE2 A GLU 14 ? B 1.330 1.252 0.078 0.011 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  ? ? -140.23 23.14   
2 1 ARG A 27  ? ? -143.34 55.09   
3 1 LYS A 111 ? ? 73.94   -3.73   
4 1 PHE A 176 ? ? -151.98 68.26   
5 1 ASN A 244 ? ? -96.93  49.66   
6 1 LYS A 252 ? ? 58.93   -138.39 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
E59 N1   N  N N 122 
E59 C2   C  N N 123 
E59 C3   C  N N 124 
E59 C4   C  N N 125 
E59 N5   N  N N 126 
E59 C6   C  N N 127 
E59 O7   O  N N 128 
E59 C8   C  N N 129 
E59 S9   S  N N 130 
E59 C10  C  N N 131 
E59 C11  C  N N 132 
E59 O12  O  N N 133 
E59 C13  C  Y N 134 
E59 C14  C  Y N 135 
E59 C15  C  Y N 136 
E59 C16  C  Y N 137 
E59 C17  C  Y N 138 
E59 C18  C  Y N 139 
E59 S19  S  N N 140 
E59 O20  O  N N 141 
E59 O21  O  N N 142 
E59 N22  N  N N 143 
E59 H1   H  N N 144 
E59 H3   H  N N 145 
E59 H8   H  N N 146 
E59 H8A  H  N N 147 
E59 H8B  H  N N 148 
E59 H10  H  N N 149 
E59 H10A H  N N 150 
E59 H14  H  N N 151 
E59 H15  H  N N 152 
E59 H17  H  N N 153 
E59 H18  H  N N 154 
E59 HN22 H  N N 155 
E59 HN2A H  N N 156 
GLN N    N  N N 157 
GLN CA   C  N S 158 
GLN C    C  N N 159 
GLN O    O  N N 160 
GLN CB   C  N N 161 
GLN CG   C  N N 162 
GLN CD   C  N N 163 
GLN OE1  O  N N 164 
GLN NE2  N  N N 165 
GLN OXT  O  N N 166 
GLN H    H  N N 167 
GLN H2   H  N N 168 
GLN HA   H  N N 169 
GLN HB2  H  N N 170 
GLN HB3  H  N N 171 
GLN HG2  H  N N 172 
GLN HG3  H  N N 173 
GLN HE21 H  N N 174 
GLN HE22 H  N N 175 
GLN HXT  H  N N 176 
GLU N    N  N N 177 
GLU CA   C  N S 178 
GLU C    C  N N 179 
GLU O    O  N N 180 
GLU CB   C  N N 181 
GLU CG   C  N N 182 
GLU CD   C  N N 183 
GLU OE1  O  N N 184 
GLU OE2  O  N N 185 
GLU OXT  O  N N 186 
GLU H    H  N N 187 
GLU H2   H  N N 188 
GLU HA   H  N N 189 
GLU HB2  H  N N 190 
GLU HB3  H  N N 191 
GLU HG2  H  N N 192 
GLU HG3  H  N N 193 
GLU HE2  H  N N 194 
GLU HXT  H  N N 195 
GLY N    N  N N 196 
GLY CA   C  N N 197 
GLY C    C  N N 198 
GLY O    O  N N 199 
GLY OXT  O  N N 200 
GLY H    H  N N 201 
GLY H2   H  N N 202 
GLY HA2  H  N N 203 
GLY HA3  H  N N 204 
GLY HXT  H  N N 205 
HIS N    N  N N 206 
HIS CA   C  N S 207 
HIS C    C  N N 208 
HIS O    O  N N 209 
HIS CB   C  N N 210 
HIS CG   C  Y N 211 
HIS ND1  N  Y N 212 
HIS CD2  C  Y N 213 
HIS CE1  C  Y N 214 
HIS NE2  N  Y N 215 
HIS OXT  O  N N 216 
HIS H    H  N N 217 
HIS H2   H  N N 218 
HIS HA   H  N N 219 
HIS HB2  H  N N 220 
HIS HB3  H  N N 221 
HIS HD1  H  N N 222 
HIS HD2  H  N N 223 
HIS HE1  H  N N 224 
HIS HE2  H  N N 225 
HIS HXT  H  N N 226 
HOH O    O  N N 227 
HOH H1   H  N N 228 
HOH H2   H  N N 229 
ILE N    N  N N 230 
ILE CA   C  N S 231 
ILE C    C  N N 232 
ILE O    O  N N 233 
ILE CB   C  N S 234 
ILE CG1  C  N N 235 
ILE CG2  C  N N 236 
ILE CD1  C  N N 237 
ILE OXT  O  N N 238 
ILE H    H  N N 239 
ILE H2   H  N N 240 
ILE HA   H  N N 241 
ILE HB   H  N N 242 
ILE HG12 H  N N 243 
ILE HG13 H  N N 244 
ILE HG21 H  N N 245 
ILE HG22 H  N N 246 
ILE HG23 H  N N 247 
ILE HD11 H  N N 248 
ILE HD12 H  N N 249 
ILE HD13 H  N N 250 
ILE HXT  H  N N 251 
LEU N    N  N N 252 
LEU CA   C  N S 253 
LEU C    C  N N 254 
LEU O    O  N N 255 
LEU CB   C  N N 256 
LEU CG   C  N N 257 
LEU CD1  C  N N 258 
LEU CD2  C  N N 259 
LEU OXT  O  N N 260 
LEU H    H  N N 261 
LEU H2   H  N N 262 
LEU HA   H  N N 263 
LEU HB2  H  N N 264 
LEU HB3  H  N N 265 
LEU HG   H  N N 266 
LEU HD11 H  N N 267 
LEU HD12 H  N N 268 
LEU HD13 H  N N 269 
LEU HD21 H  N N 270 
LEU HD22 H  N N 271 
LEU HD23 H  N N 272 
LEU HXT  H  N N 273 
LYS N    N  N N 274 
LYS CA   C  N S 275 
LYS C    C  N N 276 
LYS O    O  N N 277 
LYS CB   C  N N 278 
LYS CG   C  N N 279 
LYS CD   C  N N 280 
LYS CE   C  N N 281 
LYS NZ   N  N N 282 
LYS OXT  O  N N 283 
LYS H    H  N N 284 
LYS H2   H  N N 285 
LYS HA   H  N N 286 
LYS HB2  H  N N 287 
LYS HB3  H  N N 288 
LYS HG2  H  N N 289 
LYS HG3  H  N N 290 
LYS HD2  H  N N 291 
LYS HD3  H  N N 292 
LYS HE2  H  N N 293 
LYS HE3  H  N N 294 
LYS HZ1  H  N N 295 
LYS HZ2  H  N N 296 
LYS HZ3  H  N N 297 
LYS HXT  H  N N 298 
MET N    N  N N 299 
MET CA   C  N S 300 
MET C    C  N N 301 
MET O    O  N N 302 
MET CB   C  N N 303 
MET CG   C  N N 304 
MET SD   S  N N 305 
MET CE   C  N N 306 
MET OXT  O  N N 307 
MET H    H  N N 308 
MET H2   H  N N 309 
MET HA   H  N N 310 
MET HB2  H  N N 311 
MET HB3  H  N N 312 
MET HG2  H  N N 313 
MET HG3  H  N N 314 
MET HE1  H  N N 315 
MET HE2  H  N N 316 
MET HE3  H  N N 317 
MET HXT  H  N N 318 
PHE N    N  N N 319 
PHE CA   C  N S 320 
PHE C    C  N N 321 
PHE O    O  N N 322 
PHE CB   C  N N 323 
PHE CG   C  Y N 324 
PHE CD1  C  Y N 325 
PHE CD2  C  Y N 326 
PHE CE1  C  Y N 327 
PHE CE2  C  Y N 328 
PHE CZ   C  Y N 329 
PHE OXT  O  N N 330 
PHE H    H  N N 331 
PHE H2   H  N N 332 
PHE HA   H  N N 333 
PHE HB2  H  N N 334 
PHE HB3  H  N N 335 
PHE HD1  H  N N 336 
PHE HD2  H  N N 337 
PHE HE1  H  N N 338 
PHE HE2  H  N N 339 
PHE HZ   H  N N 340 
PHE HXT  H  N N 341 
PRO N    N  N N 342 
PRO CA   C  N S 343 
PRO C    C  N N 344 
PRO O    O  N N 345 
PRO CB   C  N N 346 
PRO CG   C  N N 347 
PRO CD   C  N N 348 
PRO OXT  O  N N 349 
PRO H    H  N N 350 
PRO HA   H  N N 351 
PRO HB2  H  N N 352 
PRO HB3  H  N N 353 
PRO HG2  H  N N 354 
PRO HG3  H  N N 355 
PRO HD2  H  N N 356 
PRO HD3  H  N N 357 
PRO HXT  H  N N 358 
SER N    N  N N 359 
SER CA   C  N S 360 
SER C    C  N N 361 
SER O    O  N N 362 
SER CB   C  N N 363 
SER OG   O  N N 364 
SER OXT  O  N N 365 
SER H    H  N N 366 
SER H2   H  N N 367 
SER HA   H  N N 368 
SER HB2  H  N N 369 
SER HB3  H  N N 370 
SER HG   H  N N 371 
SER HXT  H  N N 372 
THR N    N  N N 373 
THR CA   C  N S 374 
THR C    C  N N 375 
THR O    O  N N 376 
THR CB   C  N R 377 
THR OG1  O  N N 378 
THR CG2  C  N N 379 
THR OXT  O  N N 380 
THR H    H  N N 381 
THR H2   H  N N 382 
THR HA   H  N N 383 
THR HB   H  N N 384 
THR HG1  H  N N 385 
THR HG21 H  N N 386 
THR HG22 H  N N 387 
THR HG23 H  N N 388 
THR HXT  H  N N 389 
TRP N    N  N N 390 
TRP CA   C  N S 391 
TRP C    C  N N 392 
TRP O    O  N N 393 
TRP CB   C  N N 394 
TRP CG   C  Y N 395 
TRP CD1  C  Y N 396 
TRP CD2  C  Y N 397 
TRP NE1  N  Y N 398 
TRP CE2  C  Y N 399 
TRP CE3  C  Y N 400 
TRP CZ2  C  Y N 401 
TRP CZ3  C  Y N 402 
TRP CH2  C  Y N 403 
TRP OXT  O  N N 404 
TRP H    H  N N 405 
TRP H2   H  N N 406 
TRP HA   H  N N 407 
TRP HB2  H  N N 408 
TRP HB3  H  N N 409 
TRP HD1  H  N N 410 
TRP HE1  H  N N 411 
TRP HE3  H  N N 412 
TRP HZ2  H  N N 413 
TRP HZ3  H  N N 414 
TRP HH2  H  N N 415 
TRP HXT  H  N N 416 
TYR N    N  N N 417 
TYR CA   C  N S 418 
TYR C    C  N N 419 
TYR O    O  N N 420 
TYR CB   C  N N 421 
TYR CG   C  Y N 422 
TYR CD1  C  Y N 423 
TYR CD2  C  Y N 424 
TYR CE1  C  Y N 425 
TYR CE2  C  Y N 426 
TYR CZ   C  Y N 427 
TYR OH   O  N N 428 
TYR OXT  O  N N 429 
TYR H    H  N N 430 
TYR H2   H  N N 431 
TYR HA   H  N N 432 
TYR HB2  H  N N 433 
TYR HB3  H  N N 434 
TYR HD1  H  N N 435 
TYR HD2  H  N N 436 
TYR HE1  H  N N 437 
TYR HE2  H  N N 438 
TYR HH   H  N N 439 
TYR HXT  H  N N 440 
VAL N    N  N N 441 
VAL CA   C  N S 442 
VAL C    C  N N 443 
VAL O    O  N N 444 
VAL CB   C  N N 445 
VAL CG1  C  N N 446 
VAL CG2  C  N N 447 
VAL OXT  O  N N 448 
VAL H    H  N N 449 
VAL H2   H  N N 450 
VAL HA   H  N N 451 
VAL HB   H  N N 452 
VAL HG11 H  N N 453 
VAL HG12 H  N N 454 
VAL HG13 H  N N 455 
VAL HG21 H  N N 456 
VAL HG22 H  N N 457 
VAL HG23 H  N N 458 
VAL HXT  H  N N 459 
ZN  ZN   ZN N N 460 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
E59 N1  C6   sing N N 115 
E59 C2  N1   sing N N 116 
E59 C2  C3   sing N N 117 
E59 C3  C4   doub N N 118 
E59 C4  N5   sing N N 119 
E59 C4  C8   sing N N 120 
E59 C6  N5   doub N N 121 
E59 C6  S9   sing N N 122 
E59 O7  C2   doub N N 123 
E59 C10 S9   sing N N 124 
E59 C10 C11  sing N N 125 
E59 C11 C13  sing N N 126 
E59 O12 C11  doub N N 127 
E59 C13 C18  doub Y N 128 
E59 C13 C14  sing Y N 129 
E59 C14 C15  doub Y N 130 
E59 C15 C16  sing Y N 131 
E59 C16 S19  sing N N 132 
E59 C17 C16  doub Y N 133 
E59 C18 C17  sing Y N 134 
E59 S19 O21  doub N N 135 
E59 O20 S19  doub N N 136 
E59 N22 S19  sing N N 137 
E59 N1  H1   sing N N 138 
E59 C3  H3   sing N N 139 
E59 C8  H8   sing N N 140 
E59 C8  H8A  sing N N 141 
E59 C8  H8B  sing N N 142 
E59 C10 H10  sing N N 143 
E59 C10 H10A sing N N 144 
E59 C14 H14  sing N N 145 
E59 C15 H15  sing N N 146 
E59 C17 H17  sing N N 147 
E59 C18 H18  sing N N 148 
E59 N22 HN22 sing N N 149 
E59 N22 HN2A sing N N 150 
GLN N   CA   sing N N 151 
GLN N   H    sing N N 152 
GLN N   H2   sing N N 153 
GLN CA  C    sing N N 154 
GLN CA  CB   sing N N 155 
GLN CA  HA   sing N N 156 
GLN C   O    doub N N 157 
GLN C   OXT  sing N N 158 
GLN CB  CG   sing N N 159 
GLN CB  HB2  sing N N 160 
GLN CB  HB3  sing N N 161 
GLN CG  CD   sing N N 162 
GLN CG  HG2  sing N N 163 
GLN CG  HG3  sing N N 164 
GLN CD  OE1  doub N N 165 
GLN CD  NE2  sing N N 166 
GLN NE2 HE21 sing N N 167 
GLN NE2 HE22 sing N N 168 
GLN OXT HXT  sing N N 169 
GLU N   CA   sing N N 170 
GLU N   H    sing N N 171 
GLU N   H2   sing N N 172 
GLU CA  C    sing N N 173 
GLU CA  CB   sing N N 174 
GLU CA  HA   sing N N 175 
GLU C   O    doub N N 176 
GLU C   OXT  sing N N 177 
GLU CB  CG   sing N N 178 
GLU CB  HB2  sing N N 179 
GLU CB  HB3  sing N N 180 
GLU CG  CD   sing N N 181 
GLU CG  HG2  sing N N 182 
GLU CG  HG3  sing N N 183 
GLU CD  OE1  doub N N 184 
GLU CD  OE2  sing N N 185 
GLU OE2 HE2  sing N N 186 
GLU OXT HXT  sing N N 187 
GLY N   CA   sing N N 188 
GLY N   H    sing N N 189 
GLY N   H2   sing N N 190 
GLY CA  C    sing N N 191 
GLY CA  HA2  sing N N 192 
GLY CA  HA3  sing N N 193 
GLY C   O    doub N N 194 
GLY C   OXT  sing N N 195 
GLY OXT HXT  sing N N 196 
HIS N   CA   sing N N 197 
HIS N   H    sing N N 198 
HIS N   H2   sing N N 199 
HIS CA  C    sing N N 200 
HIS CA  CB   sing N N 201 
HIS CA  HA   sing N N 202 
HIS C   O    doub N N 203 
HIS C   OXT  sing N N 204 
HIS CB  CG   sing N N 205 
HIS CB  HB2  sing N N 206 
HIS CB  HB3  sing N N 207 
HIS CG  ND1  sing Y N 208 
HIS CG  CD2  doub Y N 209 
HIS ND1 CE1  doub Y N 210 
HIS ND1 HD1  sing N N 211 
HIS CD2 NE2  sing Y N 212 
HIS CD2 HD2  sing N N 213 
HIS CE1 NE2  sing Y N 214 
HIS CE1 HE1  sing N N 215 
HIS NE2 HE2  sing N N 216 
HIS OXT HXT  sing N N 217 
HOH O   H1   sing N N 218 
HOH O   H2   sing N N 219 
ILE N   CA   sing N N 220 
ILE N   H    sing N N 221 
ILE N   H2   sing N N 222 
ILE CA  C    sing N N 223 
ILE CA  CB   sing N N 224 
ILE CA  HA   sing N N 225 
ILE C   O    doub N N 226 
ILE C   OXT  sing N N 227 
ILE CB  CG1  sing N N 228 
ILE CB  CG2  sing N N 229 
ILE CB  HB   sing N N 230 
ILE CG1 CD1  sing N N 231 
ILE CG1 HG12 sing N N 232 
ILE CG1 HG13 sing N N 233 
ILE CG2 HG21 sing N N 234 
ILE CG2 HG22 sing N N 235 
ILE CG2 HG23 sing N N 236 
ILE CD1 HD11 sing N N 237 
ILE CD1 HD12 sing N N 238 
ILE CD1 HD13 sing N N 239 
ILE OXT HXT  sing N N 240 
LEU N   CA   sing N N 241 
LEU N   H    sing N N 242 
LEU N   H2   sing N N 243 
LEU CA  C    sing N N 244 
LEU CA  CB   sing N N 245 
LEU CA  HA   sing N N 246 
LEU C   O    doub N N 247 
LEU C   OXT  sing N N 248 
LEU CB  CG   sing N N 249 
LEU CB  HB2  sing N N 250 
LEU CB  HB3  sing N N 251 
LEU CG  CD1  sing N N 252 
LEU CG  CD2  sing N N 253 
LEU CG  HG   sing N N 254 
LEU CD1 HD11 sing N N 255 
LEU CD1 HD12 sing N N 256 
LEU CD1 HD13 sing N N 257 
LEU CD2 HD21 sing N N 258 
LEU CD2 HD22 sing N N 259 
LEU CD2 HD23 sing N N 260 
LEU OXT HXT  sing N N 261 
LYS N   CA   sing N N 262 
LYS N   H    sing N N 263 
LYS N   H2   sing N N 264 
LYS CA  C    sing N N 265 
LYS CA  CB   sing N N 266 
LYS CA  HA   sing N N 267 
LYS C   O    doub N N 268 
LYS C   OXT  sing N N 269 
LYS CB  CG   sing N N 270 
LYS CB  HB2  sing N N 271 
LYS CB  HB3  sing N N 272 
LYS CG  CD   sing N N 273 
LYS CG  HG2  sing N N 274 
LYS CG  HG3  sing N N 275 
LYS CD  CE   sing N N 276 
LYS CD  HD2  sing N N 277 
LYS CD  HD3  sing N N 278 
LYS CE  NZ   sing N N 279 
LYS CE  HE2  sing N N 280 
LYS CE  HE3  sing N N 281 
LYS NZ  HZ1  sing N N 282 
LYS NZ  HZ2  sing N N 283 
LYS NZ  HZ3  sing N N 284 
LYS OXT HXT  sing N N 285 
MET N   CA   sing N N 286 
MET N   H    sing N N 287 
MET N   H2   sing N N 288 
MET CA  C    sing N N 289 
MET CA  CB   sing N N 290 
MET CA  HA   sing N N 291 
MET C   O    doub N N 292 
MET C   OXT  sing N N 293 
MET CB  CG   sing N N 294 
MET CB  HB2  sing N N 295 
MET CB  HB3  sing N N 296 
MET CG  SD   sing N N 297 
MET CG  HG2  sing N N 298 
MET CG  HG3  sing N N 299 
MET SD  CE   sing N N 300 
MET CE  HE1  sing N N 301 
MET CE  HE2  sing N N 302 
MET CE  HE3  sing N N 303 
MET OXT HXT  sing N N 304 
PHE N   CA   sing N N 305 
PHE N   H    sing N N 306 
PHE N   H2   sing N N 307 
PHE CA  C    sing N N 308 
PHE CA  CB   sing N N 309 
PHE CA  HA   sing N N 310 
PHE C   O    doub N N 311 
PHE C   OXT  sing N N 312 
PHE CB  CG   sing N N 313 
PHE CB  HB2  sing N N 314 
PHE CB  HB3  sing N N 315 
PHE CG  CD1  doub Y N 316 
PHE CG  CD2  sing Y N 317 
PHE CD1 CE1  sing Y N 318 
PHE CD1 HD1  sing N N 319 
PHE CD2 CE2  doub Y N 320 
PHE CD2 HD2  sing N N 321 
PHE CE1 CZ   doub Y N 322 
PHE CE1 HE1  sing N N 323 
PHE CE2 CZ   sing Y N 324 
PHE CE2 HE2  sing N N 325 
PHE CZ  HZ   sing N N 326 
PHE OXT HXT  sing N N 327 
PRO N   CA   sing N N 328 
PRO N   CD   sing N N 329 
PRO N   H    sing N N 330 
PRO CA  C    sing N N 331 
PRO CA  CB   sing N N 332 
PRO CA  HA   sing N N 333 
PRO C   O    doub N N 334 
PRO C   OXT  sing N N 335 
PRO CB  CG   sing N N 336 
PRO CB  HB2  sing N N 337 
PRO CB  HB3  sing N N 338 
PRO CG  CD   sing N N 339 
PRO CG  HG2  sing N N 340 
PRO CG  HG3  sing N N 341 
PRO CD  HD2  sing N N 342 
PRO CD  HD3  sing N N 343 
PRO OXT HXT  sing N N 344 
SER N   CA   sing N N 345 
SER N   H    sing N N 346 
SER N   H2   sing N N 347 
SER CA  C    sing N N 348 
SER CA  CB   sing N N 349 
SER CA  HA   sing N N 350 
SER C   O    doub N N 351 
SER C   OXT  sing N N 352 
SER CB  OG   sing N N 353 
SER CB  HB2  sing N N 354 
SER CB  HB3  sing N N 355 
SER OG  HG   sing N N 356 
SER OXT HXT  sing N N 357 
THR N   CA   sing N N 358 
THR N   H    sing N N 359 
THR N   H2   sing N N 360 
THR CA  C    sing N N 361 
THR CA  CB   sing N N 362 
THR CA  HA   sing N N 363 
THR C   O    doub N N 364 
THR C   OXT  sing N N 365 
THR CB  OG1  sing N N 366 
THR CB  CG2  sing N N 367 
THR CB  HB   sing N N 368 
THR OG1 HG1  sing N N 369 
THR CG2 HG21 sing N N 370 
THR CG2 HG22 sing N N 371 
THR CG2 HG23 sing N N 372 
THR OXT HXT  sing N N 373 
TRP N   CA   sing N N 374 
TRP N   H    sing N N 375 
TRP N   H2   sing N N 376 
TRP CA  C    sing N N 377 
TRP CA  CB   sing N N 378 
TRP CA  HA   sing N N 379 
TRP C   O    doub N N 380 
TRP C   OXT  sing N N 381 
TRP CB  CG   sing N N 382 
TRP CB  HB2  sing N N 383 
TRP CB  HB3  sing N N 384 
TRP CG  CD1  doub Y N 385 
TRP CG  CD2  sing Y N 386 
TRP CD1 NE1  sing Y N 387 
TRP CD1 HD1  sing N N 388 
TRP CD2 CE2  doub Y N 389 
TRP CD2 CE3  sing Y N 390 
TRP NE1 CE2  sing Y N 391 
TRP NE1 HE1  sing N N 392 
TRP CE2 CZ2  sing Y N 393 
TRP CE3 CZ3  doub Y N 394 
TRP CE3 HE3  sing N N 395 
TRP CZ2 CH2  doub Y N 396 
TRP CZ2 HZ2  sing N N 397 
TRP CZ3 CH2  sing Y N 398 
TRP CZ3 HZ3  sing N N 399 
TRP CH2 HH2  sing N N 400 
TRP OXT HXT  sing N N 401 
TYR N   CA   sing N N 402 
TYR N   H    sing N N 403 
TYR N   H2   sing N N 404 
TYR CA  C    sing N N 405 
TYR CA  CB   sing N N 406 
TYR CA  HA   sing N N 407 
TYR C   O    doub N N 408 
TYR C   OXT  sing N N 409 
TYR CB  CG   sing N N 410 
TYR CB  HB2  sing N N 411 
TYR CB  HB3  sing N N 412 
TYR CG  CD1  doub Y N 413 
TYR CG  CD2  sing Y N 414 
TYR CD1 CE1  sing Y N 415 
TYR CD1 HD1  sing N N 416 
TYR CD2 CE2  doub Y N 417 
TYR CD2 HD2  sing N N 418 
TYR CE1 CZ   doub Y N 419 
TYR CE1 HE1  sing N N 420 
TYR CE2 CZ   sing Y N 421 
TYR CE2 HE2  sing N N 422 
TYR CZ  OH   sing N N 423 
TYR OH  HH   sing N N 424 
TYR OXT HXT  sing N N 425 
VAL N   CA   sing N N 426 
VAL N   H    sing N N 427 
VAL N   H2   sing N N 428 
VAL CA  C    sing N N 429 
VAL CA  CB   sing N N 430 
VAL CA  HA   sing N N 431 
VAL C   O    doub N N 432 
VAL C   OXT  sing N N 433 
VAL CB  CG1  sing N N 434 
VAL CB  CG2  sing N N 435 
VAL CB  HB   sing N N 436 
VAL CG1 HG11 sing N N 437 
VAL CG1 HG12 sing N N 438 
VAL CG1 HG13 sing N N 439 
VAL CG2 HG21 sing N N 440 
VAL CG2 HG22 sing N N 441 
VAL CG2 HG23 sing N N 442 
VAL OXT HXT  sing N N 443 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                         ZN  
3 'DIMETHYL SULFOXIDE'                                                               DMS 
4 BICINE                                                                             BCN 
5 '4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' E59 
6 water                                                                              HOH 
# 
_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          ? 
# 
