data_3MYQ
# 
_entry.id   3MYQ 
# 
_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   3MYQ         pdb_00003myq 10.2210/pdb3myq/pdb 
RCSB  RCSB059161   ?            ?                   
WWPDB D_1000059161 ?            ?                   
# 
_pdbx_database_status.entry_id                        3MYQ 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2010-05-11 
_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.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Indapamide-like benzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, and XIII.' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            18 
_citation.page_first                7357 
_citation.page_last                 7364 
_citation.year                      2010 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20926301 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2010.09.016 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Baranauskiene, L.' 1 ? 
primary 'Golovenko, D.'     2 ? 
primary 'Manakova, E.'      3 ? 
primary 'Grazulis, S.'      4 ? 
primary 'Tumkevicius, S.'   5 ? 
primary 'Matulis, D.'       6 ? 
# 
_cell.entry_id           3MYQ 
_cell.length_a           41.980 
_cell.length_b           40.910 
_cell.length_c           71.607 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.340 
_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                         3MYQ 
_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 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                          195.237   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                            78.133    2   ?       ? ? ? 
5 non-polymer syn '2-chloro-5-[(1H-imidazo[4,5-c]quinolin-2-ylsulfanyl)acetyl]benzenesulfonamide' 432.904   1   ?       ? ? ? 
6 water       nat water                                                                           18.015    253 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonic anhydrase II, CA-II, Carbonate dehydratase II, Carbonic anhydrase C, CAC' 
# 
_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     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               '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              3MYQ 
_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 
CYS 'L-peptide linking' y CYSTEINE                                                                        ? 'C3 H7 N O2 S'        
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                            ? 'C2 H6 O S'           
78.133  
E27 non-polymer         . '2-chloro-5-[(1H-imidazo[4,5-c]quinolin-2-ylsulfanyl)acetyl]benzenesulfonamide' ? 'C18 H13 Cl N4 O3 S2' 
432.904 
GLN 'L-peptide linking' y GLUTAMINE                                                                       ? 'C5 H10 N2 O3'        
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ? 'C5 H9 N O4'          
147.129 
GLY 'peptide linking'   y GLYCINE                                                                         ? 'C2 H5 N O2'          
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                       ? 'C6 H10 N3 O2 1'      
156.162 
HOH non-polymer         . WATER                                                                           ? 'H2 O'                
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2'         
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2'         
131.173 
LYS 'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1'      
147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                          ? 'C6 H13 N O4 S'       
195.237 
MET 'L-peptide linking' y METHIONINE                                                                      ? 'C5 H11 N O2 S'       
149.211 
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          3MYQ 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.53 
_exptl_crystal.density_Matthews      2.03 
_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, SITTING DROP' 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9.0, 0.2 M ammonium sulfate, and 2M sodium malonate, pH 7.0 made from 1M sodium BICINE and 3.4M sodium malonate, vapor diffusion, sitting drop, temperature 291K
;
_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 CCD' 
_diffrn_detector.pdbx_collection_date   2009-12-17 
_diffrn_detector.details                ? 
# 
_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   0.9443 
_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        0.9443 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X12 
# 
_reflns.entry_id                     3MYQ 
_reflns.d_resolution_high            1.350 
_reflns.d_resolution_low             28.843 
_reflns.number_all                   51791 
_reflns.number_obs                   50807 
_reflns.pdbx_Rmerge_I_obs            0.057 
_reflns.pdbx_netI_over_sigmaI        16.900 
_reflns.pdbx_Rsym_value              0.057 
_reflns.pdbx_redundancy              2.600 
_reflns.percent_possible_obs         98.100 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.B_iso_Wilson_estimate        13.44955 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.35 
_reflns_shell.d_res_low              1.42 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    18500 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.229 
_reflns_shell.meanI_over_sigI_obs    3.6 
_reflns_shell.pdbx_Rsym_value        0.229 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        2.60 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      7244 
_reflns_shell.percent_possible_all   97.00 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3MYQ 
_refine.ls_d_res_high                            1.350 
_refine.ls_d_res_low                             25.120 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.780 
_refine.ls_number_reflns_obs                     50792 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.143 
_refine.ls_R_factor_R_work                       0.139 
_refine.ls_wR_factor_R_work                      0.141 
_refine.ls_R_factor_R_free                       0.181 
_refine.ls_wR_factor_R_free                      0.188 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  5113 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               16.232 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.450 
_refine.aniso_B[2][2]                            0.340 
_refine.aniso_B[3][3]                            -1.010 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.450 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.974 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.overall_SU_R_Cruickshank_DPI             0.061 
_refine.overall_SU_R_free                        0.059 
_refine.pdbx_overall_ESU_R_Free                  0.059 
_refine.overall_SU_ML                            0.031 
_refine.overall_SU_B                             1.643 
_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                   0.907 
_refine.B_iso_max                                45.47 
_refine.B_iso_min                                3.34 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB entry 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_diffrn_id                           1 
_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         49 
_refine_hist.number_atoms_solvent             253 
_refine_hist.number_atoms_total               2351 
_refine_hist.d_res_high                       1.350 
_refine_hist.d_res_low                        25.120 
# 
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_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d       2255 0.024  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg    3077 2.187  1.971  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg 276  6.864  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg 103  34.484 24.854 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg 369  12.782 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg 7    25.261 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr         316  0.302  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined   1760 0.014  0.021  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it            1344 2.557  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it           2184 3.554  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it            911  4.476  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it           892  5.918  4.500  ? 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr     2255 2.734  3.000  ? 'X-RAY DIFFRACTION' ? 
r_sphericity_free      254  14.339 3.000  ? 'X-RAY DIFFRACTION' ? 
r_sphericity_bonded    2182 9.659  3.000  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.350 
_refine_ls_shell.d_res_low                        1.385 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               96.180 
_refine_ls_shell.number_reflns_R_work             3273 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.275 
_refine_ls_shell.R_factor_R_free                  0.316 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             352 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                3625 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3MYQ 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 2-chloro-5-[(1H-imidazo[4,5-c]quinolin-2-ylsulfanyl)acetyl]benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3MYQ 
_struct_keywords.text            'drug design, carbonic anhydrase, benzenesulfonamide, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 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 ? ? ? ? ? ? ? 1.962 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  262 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  262 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E27 . N28 ? ? A ZN  262 A E27 266 1_555 ? ? ? ? ? ? ? 1.880 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E27 . S24 ? ? A ZN  262 A E27 266 1_555 ? ? ? ? ? ? ? 2.985 ? ? 
# 
_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 -1.75 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.68  
# 
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 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
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 MES 263 ? 9  'BINDING SITE FOR RESIDUE MES A 263' 
AC3 Software A DMS 264 ? 2  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A DMS 265 ? 4  'BINDING SITE FOR RESIDUE DMS A 265' 
AC5 Software A E27 266 ? 18 'BINDING SITE FOR RESIDUE E27 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  E27 F .   ? E27 A 266 . ? 1_555 ? 
5  AC2 9  VAL A 160 ? VAL A 161 . ? 1_555 ? 
6  AC2 9  ASP A 161 ? ASP A 162 . ? 1_555 ? 
7  AC2 9  VAL A 162 ? VAL A 163 . ? 1_555 ? 
8  AC2 9  LEU A 163 ? LEU A 164 . ? 1_555 ? 
9  AC2 9  ASP A 164 ? ASP A 165 . ? 1_555 ? 
10 AC2 9  LYS A 224 ? LYS A 225 . ? 1_555 ? 
11 AC2 9  LYS A 227 ? LYS A 228 . ? 1_555 ? 
12 AC2 9  LEU A 228 ? LEU A 229 . ? 1_555 ? 
13 AC2 9  HOH G .   ? HOH A 430 . ? 1_555 ? 
14 AC3 2  ASP A 242 ? ASP A 243 . ? 1_555 ? 
15 AC3 2  TRP A 244 ? TRP A 245 . ? 1_555 ? 
16 AC4 4  GLN A 92  ? GLN A 92  . ? 1_555 ? 
17 AC4 4  PHE A 130 ? PHE A 131 . ? 1_555 ? 
18 AC4 4  E27 F .   ? E27 A 266 . ? 1_555 ? 
19 AC4 4  HOH G .   ? HOH A 506 . ? 1_555 ? 
20 AC5 18 ASN A 62  ? ASN A 62  . ? 1_555 ? 
21 AC5 18 HIS A 64  ? HIS A 64  . ? 1_555 ? 
22 AC5 18 ASN A 67  ? ASN A 67  . ? 1_555 ? 
23 AC5 18 GLN A 92  ? GLN A 92  . ? 1_555 ? 
24 AC5 18 HIS A 94  ? HIS A 94  . ? 1_555 ? 
25 AC5 18 HIS A 96  ? HIS A 96  . ? 1_555 ? 
26 AC5 18 HIS A 119 ? HIS A 119 . ? 1_555 ? 
27 AC5 18 LEU A 140 ? LEU A 141 . ? 1_555 ? 
28 AC5 18 VAL A 142 ? VAL A 143 . ? 1_555 ? 
29 AC5 18 LEU A 197 ? LEU A 198 . ? 1_555 ? 
30 AC5 18 THR A 198 ? THR A 199 . ? 1_555 ? 
31 AC5 18 THR A 199 ? THR A 200 . ? 1_555 ? 
32 AC5 18 PRO A 201 ? PRO A 202 . ? 1_555 ? 
33 AC5 18 TRP A 208 ? TRP A 209 . ? 1_555 ? 
34 AC5 18 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
35 AC5 18 DMS E .   ? DMS A 265 . ? 1_555 ? 
36 AC5 18 HOH G .   ? HOH A 303 . ? 1_555 ? 
37 AC5 18 HOH G .   ? HOH A 419 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3MYQ 
_atom_sites.fract_transf_matrix[1][1]   0.023821 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006088 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024444 
_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]   0.014414 
_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  
CL 
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   ? 9.169   1.129   8.247   1.00 28.37 ? 4   HIS A N    1 
ATOM   2    C  CA   . HIS A 1 4   ? 10.117  0.056   8.699   1.00 27.94 ? 4   HIS A CA   1 
ATOM   3    C  C    . HIS A 1 4   ? 9.358   -0.980  9.494   1.00 24.09 ? 4   HIS A C    1 
ATOM   4    O  O    . HIS A 1 4   ? 9.559   -2.184  9.291   1.00 24.94 ? 4   HIS A O    1 
ATOM   5    C  CB   . HIS A 1 4   ? 11.315  0.575   9.534   1.00 29.68 ? 4   HIS A CB   1 
ATOM   6    C  CG   . HIS A 1 4   ? 12.254  -0.515  9.958   1.00 35.13 ? 4   HIS A CG   1 
ATOM   7    N  ND1  . HIS A 1 4   ? 12.303  -0.979  11.260  1.00 39.04 ? 4   HIS A ND1  1 
ATOM   8    C  CD2  . HIS A 1 4   ? 13.125  -1.277  9.247   1.00 39.10 ? 4   HIS A CD2  1 
ATOM   9    C  CE1  . HIS A 1 4   ? 13.171  -1.981  11.334  1.00 41.10 ? 4   HIS A CE1  1 
ATOM   10   N  NE2  . HIS A 1 4   ? 13.691  -2.177  10.132  1.00 42.07 ? 4   HIS A NE2  1 
ATOM   11   N  N    . TRP A 1 5   ? 8.481   -0.522  10.365  1.00 22.19 ? 5   TRP A N    1 
ATOM   12   C  CA   . TRP A 1 5   ? 7.759   -1.447  11.237  1.00 17.24 ? 5   TRP A CA   1 
ATOM   13   C  C    . TRP A 1 5   ? 6.748   -2.278  10.447  1.00 18.02 ? 5   TRP A C    1 
ATOM   14   O  O    . TRP A 1 5   ? 6.228   -1.813  9.415   1.00 19.25 ? 5   TRP A O    1 
ATOM   15   C  CB   . TRP A 1 5   ? 7.055   -0.696  12.392  1.00 16.28 ? 5   TRP A CB   1 
ATOM   16   C  CG   . TRP A 1 5   ? 5.869   0.096   12.041  1.00 16.85 ? 5   TRP A CG   1 
ATOM   17   C  CD1  . TRP A 1 5   ? 5.843   1.405   11.717  1.00 19.48 ? 5   TRP A CD1  1 
ATOM   18   C  CD2  . TRP A 1 5   ? 4.503   -0.388  11.973  1.00 15.40 ? 5   TRP A CD2  1 
ATOM   19   N  NE1  . TRP A 1 5   ? 4.558   1.782   11.453  1.00 18.53 ? 5   TRP A NE1  1 
ATOM   20   C  CE2  . TRP A 1 5   ? 3.699   0.701   11.576  1.00 15.48 ? 5   TRP A CE2  1 
ATOM   21   C  CE3  . TRP A 1 5   ? 3.888   -1.641  12.215  1.00 14.52 ? 5   TRP A CE3  1 
ATOM   22   C  CZ2  . TRP A 1 5   ? 2.289   0.605   11.420  1.00 18.54 ? 5   TRP A CZ2  1 
ATOM   23   C  CZ3  . TRP A 1 5   ? 2.455   -1.725  12.075  1.00 15.12 ? 5   TRP A CZ3  1 
ATOM   24   C  CH2  . TRP A 1 5   ? 1.688   -0.597  11.702  1.00 15.30 ? 5   TRP A CH2  1 
ATOM   25   N  N    . GLY A 1 6   ? 6.446   -3.475  10.949  1.00 16.13 ? 6   GLY A N    1 
ATOM   26   C  CA   . GLY A 1 6   ? 5.416   -4.266  10.299  1.00 16.15 ? 6   GLY A CA   1 
ATOM   27   C  C    . GLY A 1 6   ? 5.084   -5.416  11.208  1.00 15.28 ? 6   GLY A C    1 
ATOM   28   O  O    . GLY A 1 6   ? 5.136   -5.299  12.432  1.00 14.87 ? 6   GLY A O    1 
ATOM   29   N  N    . TYR A 1 7   ? 4.787   -6.545  10.591  1.00 16.58 ? 7   TYR A N    1 
ATOM   30   C  CA   . TYR A 1 7   ? 4.427   -7.725  11.410  1.00 17.98 ? 7   TYR A CA   1 
ATOM   31   C  C    . TYR A 1 7   ? 5.292   -8.956  11.171  1.00 19.94 ? 7   TYR A C    1 
ATOM   32   O  O    . TYR A 1 7   ? 4.890   -10.088 11.574  1.00 24.87 ? 7   TYR A O    1 
ATOM   33   C  CB   . TYR A 1 7   ? 2.952   -8.085  11.202  1.00 16.02 ? 7   TYR A CB   1 
ATOM   34   C  CG   . TYR A 1 7   ? 2.037   -6.988  11.748  1.00 12.36 ? 7   TYR A CG   1 
ATOM   35   C  CD1  . TYR A 1 7   ? 1.607   -7.038  13.111  1.00 11.81 ? 7   TYR A CD1  1 
ATOM   36   C  CD2  . TYR A 1 7   ? 1.608   -5.937  10.932  1.00 12.09 ? 7   TYR A CD2  1 
ATOM   37   C  CE1  . TYR A 1 7   ? 0.757   -5.957  13.627  1.00 10.74 ? 7   TYR A CE1  1 
ATOM   38   C  CE2  . TYR A 1 7   ? 0.751   -4.949  11.430  1.00 12.84 ? 7   TYR A CE2  1 
ATOM   39   C  CZ   . TYR A 1 7   ? 0.366   -4.975  12.773  1.00 10.98 ? 7   TYR A CZ   1 
ATOM   40   O  OH   . TYR A 1 7   ? -0.486  -3.985  13.228  1.00 11.25 ? 7   TYR A OH   1 
ATOM   41   N  N    . GLY A 1 8   ? 6.459   -8.770  10.544  1.00 21.45 ? 8   GLY A N    1 
ATOM   42   C  CA   . GLY A 1 8   ? 7.427   -9.925  10.317  1.00 21.07 ? 8   GLY A CA   1 
ATOM   43   C  C    . GLY A 1 8   ? 8.398   -10.288 11.451  1.00 24.54 ? 8   GLY A C    1 
ATOM   44   O  O    . GLY A 1 8   ? 8.546   -9.616  12.510  1.00 27.06 ? 8   GLY A O    1 
ATOM   45   N  N    . LYS A 1 9   ? 9.238   -11.306 11.192  1.00 26.54 ? 9   LYS A N    1 
ATOM   46   C  CA   . LYS A 1 9   ? 10.307  -11.720 12.165  1.00 27.69 ? 9   LYS A CA   1 
ATOM   47   C  C    . LYS A 1 9   ? 11.204  -10.556 12.451  1.00 26.69 ? 9   LYS A C    1 
ATOM   48   O  O    . LYS A 1 9   ? 11.627  -10.383 13.624  1.00 26.69 ? 9   LYS A O    1 
ATOM   49   C  CB   . LYS A 1 9   ? 11.156  -12.896 11.637  1.00 28.51 ? 9   LYS A CB   1 
ATOM   50   C  CG   . LYS A 1 9   ? 12.076  -13.550 12.672  0.01 27.96 ? 9   LYS A CG   1 
ATOM   51   C  CD   . LYS A 1 9   ? 11.299  -14.391 13.679  0.01 27.74 ? 9   LYS A CD   1 
ATOM   52   C  CE   . LYS A 1 9   ? 12.219  -14.968 14.742  0.01 27.64 ? 9   LYS A CE   1 
ATOM   53   N  NZ   . LYS A 1 9   ? 11.466  -15.727 15.777  0.01 27.48 ? 9   LYS A NZ   1 
ATOM   54   N  N    . HIS A 1 10  ? 11.459  -9.746  11.414  1.00 22.40 ? 10  HIS A N    1 
ATOM   55   C  CA   . HIS A 1 10  ? 12.461  -8.789  11.609  1.00 23.33 ? 10  HIS A CA   1 
ATOM   56   C  C    . HIS A 1 10  ? 11.952  -7.432  11.973  1.00 20.58 ? 10  HIS A C    1 
ATOM   57   O  O    . HIS A 1 10  ? 12.775  -6.637  12.462  1.00 22.32 ? 10  HIS A O    1 
ATOM   58   C  CB   . HIS A 1 10  ? 13.479  -8.784  10.470  1.00 22.84 ? 10  HIS A CB   1 
ATOM   59   C  CG   . HIS A 1 10  ? 14.178  -10.118 10.333  1.00 26.26 ? 10  HIS A CG   1 
ATOM   60   N  ND1  . HIS A 1 10  ? 15.224  -10.519 11.153  1.00 27.52 ? 10  HIS A ND1  1 
ATOM   61   C  CD2  . HIS A 1 10  ? 13.933  -11.141 9.501   1.00 27.07 ? 10  HIS A CD2  1 
ATOM   62   C  CE1  . HIS A 1 10  ? 15.600  -11.737 10.813  1.00 27.29 ? 10  HIS A CE1  1 
ATOM   63   N  NE2  . HIS A 1 10  ? 14.802  -12.152 9.837   1.00 25.89 ? 10  HIS A NE2  1 
ATOM   64   N  N    . ASN A 1 11  ? 10.629  -7.135  11.798  1.00 18.59 ? 11  ASN A N    1 
ATOM   65   C  CA   . ASN A 1 11  ? 10.163  -5.788  12.081  1.00 16.98 ? 11  ASN A CA   1 
ATOM   66   C  C    . ASN A 1 11  ? 8.808   -5.843  12.786  1.00 16.99 ? 11  ASN A C    1 
ATOM   67   O  O    . ASN A 1 11  ? 8.134   -4.823  12.874  1.00 16.26 ? 11  ASN A O    1 
ATOM   68   C  CB   . ASN A 1 11  ? 10.002  -5.065  10.782  1.00 17.44 ? 11  ASN A CB   1 
ATOM   69   C  CG   . ASN A 1 11  ? 8.933   -5.690  9.837   1.00 18.16 ? 11  ASN A CG   1 
ATOM   70   O  OD1  . ASN A 1 11  ? 8.297   -6.707  10.145  1.00 20.51 ? 11  ASN A OD1  1 
ATOM   71   N  ND2  . ASN A 1 11  ? 8.677   -5.044  8.734   1.00 20.17 ? 11  ASN A ND2  1 
ATOM   72   N  N    . GLY A 1 12  ? 8.468   -6.983  13.377  1.00 17.06 ? 12  GLY A N    1 
ATOM   73   C  CA   . GLY A 1 12  ? 7.135   -7.189  14.003  1.00 16.24 ? 12  GLY A CA   1 
ATOM   74   C  C    . GLY A 1 12  ? 7.116   -6.619  15.411  1.00 14.75 ? 12  GLY A C    1 
ATOM   75   O  O    . GLY A 1 12  ? 8.035   -5.914  15.828  1.00 14.50 ? 12  GLY A O    1 
ATOM   76   N  N    . PRO A 1 13  ? 6.039   -6.856  16.160  1.00 12.81 ? 13  PRO A N    1 
ATOM   77   C  CA   . PRO A 1 13  ? 5.777   -6.286  17.436  1.00 13.34 ? 13  PRO A CA   1 
ATOM   78   C  C    . PRO A 1 13  ? 6.905   -6.296  18.426  1.00 12.12 ? 13  PRO A C    1 
ATOM   79   O  O    . PRO A 1 13  ? 7.051   -5.326  19.202  1.00 13.58 ? 13  PRO A O    1 
ATOM   80   C  CB   . PRO A 1 13  ? 4.549   -7.096  17.903  1.00 12.84 ? 13  PRO A CB   1 
ATOM   81   C  CG   . PRO A 1 13  ? 3.820   -7.366  16.657  1.00 14.18 ? 13  PRO A CG   1 
ATOM   82   C  CD   . PRO A 1 13  ? 4.914   -7.667  15.679  1.00 13.77 ? 13  PRO A CD   1 
ATOM   83   N  N    . GLU A 1 14  ? 7.741   -7.335  18.431  1.00 13.79 ? 14  GLU A N    1 
ATOM   84   C  CA   . GLU A 1 14  ? 8.795   -7.398  19.431  1.00 15.38 ? 14  GLU A CA   1 
ATOM   85   C  C    . GLU A 1 14  ? 9.953   -6.434  19.100  1.00 14.62 ? 14  GLU A C    1 
ATOM   86   O  O    . GLU A 1 14  ? 10.826  -6.223  19.934  1.00 16.58 ? 14  GLU A O    1 
ATOM   87   C  CB   . GLU A 1 14  ? 9.364   -8.819  19.474  1.00 19.69 ? 14  GLU A CB   1 
ATOM   88   C  CG   . GLU A 1 14  ? 9.975   -9.331  18.129  1.00 24.05 ? 14  GLU A CG   1 
ATOM   89   C  CD   . GLU A 1 14  ? 9.117   -9.925  16.926  1.00 29.02 ? 14  GLU A CD   1 
ATOM   90   O  OE1  . GLU A 1 14  ? 7.906   -9.529  16.681  1.00 24.26 ? 14  GLU A OE1  1 
ATOM   91   O  OE2  . GLU A 1 14  ? 9.799   -10.734 16.148  1.00 29.18 ? 14  GLU A OE2  1 
ATOM   92   N  N    . HIS A 1 15  ? 9.913   -5.830  17.919  1.00 13.31 ? 15  HIS A N    1 
ATOM   93   C  CA   . HIS A 1 15  ? 10.929  -4.874  17.515  1.00 13.50 ? 15  HIS A CA   1 
ATOM   94   C  C    . HIS A 1 15  ? 10.480  -3.457  17.681  1.00 12.42 ? 15  HIS A C    1 
ATOM   95   O  O    . HIS A 1 15  ? 11.319  -2.510  17.656  1.00 13.54 ? 15  HIS A O    1 
ATOM   96   C  CB   . HIS A 1 15  ? 11.237  -5.066  16.041  1.00 14.43 ? 15  HIS A CB   1 
ATOM   97   C  CG   . HIS A 1 15  ? 12.007  -6.295  15.800  1.00 15.26 ? 15  HIS A CG   1 
ATOM   98   N  ND1  . HIS A 1 15  ? 13.382  -6.354  15.921  1.00 17.70 ? 15  HIS A ND1  1 
ATOM   99   C  CD2  . HIS A 1 15  ? 11.580  -7.519  15.446  1.00 17.61 ? 15  HIS A CD2  1 
ATOM   100  C  CE1  . HIS A 1 15  ? 13.763  -7.598  15.698  1.00 19.78 ? 15  HIS A CE1  1 
ATOM   101  N  NE2  . HIS A 1 15  ? 12.705  -8.315  15.363  1.00 19.41 ? 15  HIS A NE2  1 
ATOM   102  N  N    . TRP A 1 16  ? 9.183   -3.193  17.835  1.00 12.26 ? 16  TRP A N    1 
ATOM   103  C  CA   . TRP A 1 16  ? 8.658   -1.823  17.699  1.00 11.45 ? 16  TRP A CA   1 
ATOM   104  C  C    . TRP A 1 16  ? 9.249   -0.881  18.751  1.00 11.79 ? 16  TRP A C    1 
ATOM   105  O  O    . TRP A 1 16  ? 9.347   0.310   18.510  1.00 12.69 ? 16  TRP A O    1 
ATOM   106  C  CB   . TRP A 1 16  ? 7.124   -1.824  17.856  1.00 10.87 ? 16  TRP A CB   1 
ATOM   107  C  CG   . TRP A 1 16  ? 6.439   -2.545  16.750  1.00 11.21 ? 16  TRP A CG   1 
ATOM   108  C  CD1  . TRP A 1 16  ? 7.009   -3.021  15.540  1.00 12.14 ? 16  TRP A CD1  1 
ATOM   109  C  CD2  . TRP A 1 16  ? 5.053   -2.888  16.680  1.00 10.30 ? 16  TRP A CD2  1 
ATOM   110  N  NE1  . TRP A 1 16  ? 6.020   -3.597  14.752  1.00 11.17 ? 16  TRP A NE1  1 
ATOM   111  C  CE2  . TRP A 1 16  ? 4.823   -3.503  15.413  1.00 10.19 ? 16  TRP A CE2  1 
ATOM   112  C  CE3  . TRP A 1 16  ? 3.984   -2.677  17.526  1.00 10.37 ? 16  TRP A CE3  1 
ATOM   113  C  CZ2  . TRP A 1 16  ? 3.555   -3.950  15.023  1.00 10.48 ? 16  TRP A CZ2  1 
ATOM   114  C  CZ3  . TRP A 1 16  ? 2.766   -3.106  17.159  1.00 11.02 ? 16  TRP A CZ3  1 
ATOM   115  C  CH2  . TRP A 1 16  ? 2.533   -3.711  15.936  1.00 11.79 ? 16  TRP A CH2  1 
ATOM   116  N  N    . HIS A 1 17  ? 9.612   -1.423  19.916  1.00 12.58 ? 17  HIS A N    1 
ATOM   117  C  CA   . HIS A 1 17  ? 10.104  -0.582  21.006  1.00 13.77 ? 17  HIS A CA   1 
ATOM   118  C  C    . HIS A 1 17  ? 11.336  0.199   20.603  1.00 14.27 ? 17  HIS A C    1 
ATOM   119  O  O    . HIS A 1 17  ? 11.595  1.235   21.203  1.00 14.95 ? 17  HIS A O    1 
ATOM   120  C  CB   . HIS A 1 17  ? 10.375  -1.362  22.303  1.00 13.23 ? 17  HIS A CB   1 
ATOM   121  C  CG   . HIS A 1 17  ? 11.556  -2.255  22.197  1.00 13.75 ? 17  HIS A CG   1 
ATOM   122  N  ND1  . HIS A 1 17  ? 12.795  -1.841  22.657  1.00 16.87 ? 17  HIS A ND1  1 
ATOM   123  C  CD2  . HIS A 1 17  ? 11.737  -3.437  21.584  1.00 14.86 ? 17  HIS A CD2  1 
ATOM   124  C  CE1  . HIS A 1 17  ? 13.681  -2.791  22.427  1.00 16.47 ? 17  HIS A CE1  1 
ATOM   125  N  NE2  . HIS A 1 17  ? 13.082  -3.762  21.754  1.00 16.61 ? 17  HIS A NE2  1 
ATOM   126  N  N    . LYS A 1 18  ? 12.133  -0.296  19.677  1.00 14.45 ? 18  LYS A N    1 
ATOM   127  C  CA   . LYS A 1 18  ? 13.364  0.455   19.305  1.00 14.87 ? 18  LYS A CA   1 
ATOM   128  C  C    . LYS A 1 18  ? 13.010  1.785   18.655  1.00 15.94 ? 18  LYS A C    1 
ATOM   129  O  O    . LYS A 1 18  ? 13.655  2.809   18.959  1.00 18.69 ? 18  LYS A O    1 
ATOM   130  C  CB   . LYS A 1 18  ? 14.210  -0.419  18.399  1.00 15.78 ? 18  LYS A CB   1 
ATOM   131  C  CG   . LYS A 1 18  ? 14.791  -1.633  19.117  1.00 15.99 ? 18  LYS A CG   1 
ATOM   132  C  CD   . LYS A 1 18  ? 15.459  -2.590  18.066  1.00 15.22 ? 18  LYS A CD   1 
ATOM   133  C  CE   . LYS A 1 18  ? 14.458  -3.561  17.508  1.00 14.86 ? 18  LYS A CE   1 
ATOM   134  N  NZ   . LYS A 1 18  ? 15.171  -4.375  16.484  1.00 15.78 ? 18  LYS A NZ   1 
ATOM   135  N  N    . ASP A 1 19  ? 12.024  1.834   17.765  1.00 14.92 ? 19  ASP A N    1 
ATOM   136  C  CA   . ASP A 1 19  ? 11.579  3.099   17.218  1.00 16.37 ? 19  ASP A CA   1 
ATOM   137  C  C    . ASP A 1 19  ? 10.604  3.831   18.096  1.00 15.46 ? 19  ASP A C    1 
ATOM   138  O  O    . ASP A 1 19  ? 10.474  5.026   17.939  1.00 17.44 ? 19  ASP A O    1 
ATOM   139  C  CB   . ASP A 1 19  ? 11.025  2.959   15.806  1.00 18.53 ? 19  ASP A CB   1 
ATOM   140  C  CG   . ASP A 1 19  ? 12.095  3.026   14.695  1.00 20.95 ? 19  ASP A CG   1 
ATOM   141  O  OD1  . ASP A 1 19  ? 13.185  3.588   14.922  1.00 24.39 ? 19  ASP A OD1  1 
ATOM   142  O  OD2  . ASP A 1 19  ? 11.808  2.536   13.562  1.00 32.99 ? 19  ASP A OD2  1 
ATOM   143  N  N    . PHE A 1 20  ? 9.800   3.059   18.842  1.00 14.46 ? 20  PHE A N    1 
ATOM   144  C  CA   . PHE A 1 20  ? 8.684   3.646   19.605  1.00 13.85 ? 20  PHE A CA   1 
ATOM   145  C  C    . PHE A 1 20  ? 8.788   3.142   21.033  1.00 13.16 ? 20  PHE A C    1 
ATOM   146  O  O    . PHE A 1 20  ? 8.127   2.146   21.392  1.00 13.24 ? 20  PHE A O    1 
ATOM   147  C  CB   . PHE A 1 20  ? 7.370   3.170   18.977  1.00 14.01 ? 20  PHE A CB   1 
ATOM   148  C  CG   . PHE A 1 20  ? 7.267   3.531   17.546  1.00 12.85 ? 20  PHE A CG   1 
ATOM   149  C  CD1  . PHE A 1 20  ? 6.920   4.864   17.175  1.00 16.09 ? 20  PHE A CD1  1 
ATOM   150  C  CD2  . PHE A 1 20  ? 7.639   2.612   16.522  1.00 15.05 ? 20  PHE A CD2  1 
ATOM   151  C  CE1  . PHE A 1 20  ? 6.916   5.231   15.828  1.00 17.00 ? 20  PHE A CE1  1 
ATOM   152  C  CE2  . PHE A 1 20  ? 7.618   2.987   15.172  1.00 17.62 ? 20  PHE A CE2  1 
ATOM   153  C  CZ   . PHE A 1 20  ? 7.242   4.309   14.836  1.00 16.64 ? 20  PHE A CZ   1 
ATOM   154  N  N    A PRO A 1 21  ? 9.643   3.763   21.888  0.50 13.35 ? 21  PRO A N    1 
ATOM   155  N  N    B PRO A 1 21  ? 9.688   3.753   21.816  0.50 13.08 ? 21  PRO A N    1 
ATOM   156  C  CA   A PRO A 1 21  ? 9.929   3.358   23.299  0.50 13.32 ? 21  PRO A CA   1 
ATOM   157  C  CA   B PRO A 1 21  ? 9.918   3.100   23.091  0.50 12.08 ? 21  PRO A CA   1 
ATOM   158  C  C    A PRO A 1 21  ? 8.765   3.148   24.284  0.50 12.04 ? 21  PRO A C    1 
ATOM   159  C  C    B PRO A 1 21  ? 8.609   3.153   23.923  0.50 10.76 ? 21  PRO A C    1 
ATOM   160  O  O    A PRO A 1 21  ? 8.869   2.347   25.227  0.50 13.25 ? 21  PRO A O    1 
ATOM   161  O  O    B PRO A 1 21  ? 8.462   2.369   24.856  0.50 11.47 ? 21  PRO A O    1 
ATOM   162  C  CB   A PRO A 1 21  ? 10.796  4.523   23.831  0.50 13.43 ? 21  PRO A CB   1 
ATOM   163  C  CB   B PRO A 1 21  ? 11.104  3.889   23.703  0.50 12.76 ? 21  PRO A CB   1 
ATOM   164  C  CG   A PRO A 1 21  ? 10.865  5.472   22.743  0.50 14.22 ? 21  PRO A CG   1 
ATOM   165  C  CG   B PRO A 1 21  ? 11.677  4.724   22.559  0.50 15.56 ? 21  PRO A CG   1 
ATOM   166  C  CD   A PRO A 1 21  ? 10.632  4.761   21.460  0.50 14.23 ? 21  PRO A CD   1 
ATOM   167  C  CD   B PRO A 1 21  ? 10.594  4.892   21.558  0.50 14.34 ? 21  PRO A CD   1 
ATOM   168  N  N    A ILE A 1 22  ? 7.673   3.889   24.065  0.50 11.12 ? 22  ILE A N    1 
ATOM   169  N  N    B ILE A 1 22  ? 7.609   3.973   23.522  0.50 9.08  ? 22  ILE A N    1 
ATOM   170  C  CA   A ILE A 1 22  ? 6.434   3.707   24.795  0.50 10.98 ? 22  ILE A CA   1 
ATOM   171  C  CA   B ILE A 1 22  ? 6.324   3.915   24.244  0.50 9.03  ? 22  ILE A CA   1 
ATOM   172  C  C    A ILE A 1 22  ? 5.855   2.306   24.525  0.50 11.14 ? 22  ILE A C    1 
ATOM   173  C  C    B ILE A 1 22  ? 5.710   2.477   24.237  0.50 10.87 ? 22  ILE A C    1 
ATOM   174  O  O    A ILE A 1 22  ? 4.951   1.907   25.306  0.50 10.70 ? 22  ILE A O    1 
ATOM   175  O  O    B ILE A 1 22  ? 4.734   2.200   24.937  0.50 11.29 ? 22  ILE A O    1 
ATOM   176  C  CB   A ILE A 1 22  ? 5.416   4.790   24.379  0.50 11.26 ? 22  ILE A CB   1 
ATOM   177  C  CB   B ILE A 1 22  ? 5.334   5.007   23.756  0.50 9.52  ? 22  ILE A CB   1 
ATOM   178  C  CG1  A ILE A 1 22  ? 4.328   4.999   25.446  0.50 13.78 ? 22  ILE A CG1  1 
ATOM   179  C  CG1  B ILE A 1 22  ? 4.343   5.347   24.876  0.50 8.39  ? 22  ILE A CG1  1 
ATOM   180  C  CG2  A ILE A 1 22  ? 4.850   4.409   23.025  0.50 11.91 ? 22  ILE A CG2  1 
ATOM   181  C  CG2  B ILE A 1 22  ? 4.722   4.573   22.431  0.50 10.77 ? 22  ILE A CG2  1 
ATOM   182  C  CD1  A ILE A 1 22  ? 4.755   5.888   26.514  0.50 14.83 ? 22  ILE A CD1  1 
ATOM   183  C  CD1  B ILE A 1 22  ? 3.370   6.355   24.582  0.50 10.23 ? 22  ILE A CD1  1 
ATOM   184  N  N    . ALA A 1 23  ? 6.309   1.571   23.465  1.00 11.41 ? 23  ALA A N    1 
ATOM   185  C  CA   . ALA A 1 23  ? 5.816   0.183   23.349  1.00 11.26 ? 23  ALA A CA   1 
ATOM   186  C  C    . ALA A 1 23  ? 5.933   -0.555  24.696  1.00 11.02 ? 23  ALA A C    1 
ATOM   187  O  O    . ALA A 1 23  ? 5.203   -1.536  24.885  1.00 12.74 ? 23  ALA A O    1 
ATOM   188  C  CB   . ALA A 1 23  ? 6.673   -0.540  22.366  1.00 12.41 ? 23  ALA A CB   1 
ATOM   189  N  N    . LYS A 1 24  ? 6.882   -0.137  25.571  1.00 12.52 ? 24  LYS A N    1 
ATOM   190  C  CA   . LYS A 1 24  ? 7.052   -0.738  26.895  1.00 13.84 ? 24  LYS A CA   1 
ATOM   191  C  C    . LYS A 1 24  ? 6.451   0.187   27.944  1.00 14.60 ? 24  LYS A C    1 
ATOM   192  O  O    . LYS A 1 24  ? 6.789   0.115   29.101  1.00 17.00 ? 24  LYS A O    1 
ATOM   193  C  CB   . LYS A 1 24  ? 8.546   -0.961  27.172  1.00 15.25 ? 24  LYS A CB   1 
ATOM   194  C  CG   . LYS A 1 24  ? 9.083   -1.968  26.237  1.00 16.79 ? 24  LYS A CG   1 
ATOM   195  C  CD   . LYS A 1 24  ? 10.505  -2.273  26.681  1.00 23.47 ? 24  LYS A CD   1 
ATOM   196  C  CE   . LYS A 1 24  ? 11.277  -3.168  25.714  1.00 25.44 ? 24  LYS A CE   1 
ATOM   197  N  NZ   . LYS A 1 24  ? 10.890  -4.564  25.897  1.00 30.33 ? 24  LYS A NZ   1 
ATOM   198  N  N    . GLY A 1 25  ? 5.422   0.933   27.558  1.00 14.01 ? 25  GLY A N    1 
ATOM   199  C  CA   . GLY A 1 25  ? 4.807   1.902   28.473  1.00 14.49 ? 25  GLY A CA   1 
ATOM   200  C  C    . GLY A 1 25  ? 3.819   1.330   29.485  1.00 13.48 ? 25  GLY A C    1 
ATOM   201  O  O    . GLY A 1 25  ? 3.621   0.089   29.607  1.00 14.58 ? 25  GLY A O    1 
ATOM   202  N  N    . GLU A 1 26  ? 3.174   2.252   30.194  1.00 14.50 ? 26  GLU A N    1 
ATOM   203  C  CA   . GLU A 1 26  ? 2.277   1.848   31.273  1.00 14.80 ? 26  GLU A CA   1 
ATOM   204  C  C    . GLU A 1 26  ? 0.847   1.589   30.900  1.00 13.05 ? 26  GLU A C    1 
ATOM   205  O  O    . GLU A 1 26  ? 0.102   1.100   31.718  1.00 15.33 ? 26  GLU A O    1 
ATOM   206  C  CB   . GLU A 1 26  ? 2.273   2.940   32.402  1.00 16.07 ? 26  GLU A CB   1 
ATOM   207  C  CG   . GLU A 1 26  ? 3.647   3.233   32.991  1.00 19.02 ? 26  GLU A CG   1 
ATOM   208  C  CD   . GLU A 1 26  ? 4.265   1.963   33.577  1.00 26.16 ? 26  GLU A CD   1 
ATOM   209  O  OE1  . GLU A 1 26  ? 3.602   1.301   34.426  1.00 29.37 ? 26  GLU A OE1  1 
ATOM   210  O  OE2  . GLU A 1 26  ? 5.388   1.617   33.113  1.00 34.32 ? 26  GLU A OE2  1 
ATOM   211  N  N    . ARG A 1 27  ? 0.469   1.922   29.687  1.00 11.56 ? 27  ARG A N    1 
ATOM   212  C  CA   . ARG A 1 27  ? -0.953  1.682   29.303  1.00 11.32 ? 27  ARG A CA   1 
ATOM   213  C  C    . ARG A 1 27  ? -1.026  1.243   27.827  1.00 9.49  ? 27  ARG A C    1 
ATOM   214  O  O    . ARG A 1 27  ? -1.700  1.860   26.992  1.00 10.54 ? 27  ARG A O    1 
ATOM   215  C  CB   . ARG A 1 27  ? -1.854  2.910   29.621  1.00 13.25 ? 27  ARG A CB   1 
ATOM   216  C  CG   . ARG A 1 27  ? -1.470  4.239   28.980  1.00 15.15 ? 27  ARG A CG   1 
ATOM   217  C  CD   . ARG A 1 27  ? -2.484  5.449   29.190  1.00 17.71 ? 27  ARG A CD   1 
ATOM   218  N  NE   . ARG A 1 27  ? -3.694  5.283   28.336  1.00 15.57 ? 27  ARG A NE   1 
ATOM   219  C  CZ   . ARG A 1 27  ? -4.600  6.220   28.231  1.00 13.26 ? 27  ARG A CZ   1 
ATOM   220  N  NH1  . ARG A 1 27  ? -4.540  7.431   28.897  1.00 15.62 ? 27  ARG A NH1  1 
ATOM   221  N  NH2  . ARG A 1 27  ? -5.539  6.029   27.375  1.00 15.41 ? 27  ARG A NH2  1 
ATOM   222  N  N    . GLN A 1 28  ? -0.233  0.184   27.529  1.00 9.35  ? 28  GLN A N    1 
ATOM   223  C  CA   . GLN A 1 28  ? -0.226  -0.346  26.165  1.00 8.94  ? 28  GLN A CA   1 
ATOM   224  C  C    . GLN A 1 28  ? -1.364  -1.329  25.915  1.00 7.62  ? 28  GLN A C    1 
ATOM   225  O  O    . GLN A 1 28  ? -1.854  -2.014  26.827  1.00 9.09  ? 28  GLN A O    1 
ATOM   226  C  CB   . GLN A 1 28  ? 1.090   -1.028  25.917  1.00 9.39  ? 28  GLN A CB   1 
ATOM   227  C  CG   . GLN A 1 28  ? 2.184   0.041   25.894  1.00 9.50  ? 28  GLN A CG   1 
ATOM   228  C  CD   . GLN A 1 28  ? 2.128   0.865   24.595  1.00 9.56  ? 28  GLN A CD   1 
ATOM   229  O  OE1  . GLN A 1 28  ? 2.354   0.284   23.503  1.00 9.98  ? 28  GLN A OE1  1 
ATOM   230  N  NE2  . GLN A 1 28  ? 1.743   2.149   24.682  1.00 9.84  ? 28  GLN A NE2  1 
ATOM   231  N  N    . SER A 1 29  ? -1.775  -1.378  24.642  1.00 8.02  ? 29  SER A N    1 
ATOM   232  C  CA   . SER A 1 29  ? -2.825  -2.268  24.178  1.00 7.44  ? 29  SER A CA   1 
ATOM   233  C  C    . SER A 1 29  ? -2.274  -3.151  23.073  1.00 7.33  ? 29  SER A C    1 
ATOM   234  O  O    . SER A 1 29  ? -1.332  -2.760  22.399  1.00 8.93  ? 29  SER A O    1 
ATOM   235  C  CB   . SER A 1 29  ? -3.966  -1.411  23.593  1.00 8.30  ? 29  SER A CB   1 
ATOM   236  O  OG   . SER A 1 29  ? -4.557  -0.693  24.688  1.00 8.38  ? 29  SER A OG   1 
ATOM   237  N  N    . PRO A 1 30  ? -2.890  -4.274  22.797  1.00 8.13  ? 30  PRO A N    1 
ATOM   238  C  CA   . PRO A 1 30  ? -4.103  -4.832  23.493  1.00 7.30  ? 30  PRO A CA   1 
ATOM   239  C  C    . PRO A 1 30  ? -3.684  -5.470  24.802  1.00 8.12  ? 30  PRO A C    1 
ATOM   240  O  O    . PRO A 1 30  ? -2.491  -5.502  25.150  1.00 8.41  ? 30  PRO A O    1 
ATOM   241  C  CB   . PRO A 1 30  ? -4.550  -5.846  22.483  1.00 7.93  ? 30  PRO A CB   1 
ATOM   242  C  CG   . PRO A 1 30  ? -3.310  -6.415  21.921  1.00 7.82  ? 30  PRO A CG   1 
ATOM   243  C  CD   . PRO A 1 30  ? -2.413  -5.200  21.749  1.00 8.47  ? 30  PRO A CD   1 
ATOM   244  N  N    . VAL A 1 31  ? -4.679  -6.046  25.496  1.00 7.75  ? 31  VAL A N    1 
ATOM   245  C  CA   . VAL A 1 31  ? -4.470  -6.807  26.715  1.00 7.83  ? 31  VAL A CA   1 
ATOM   246  C  C    . VAL A 1 31  ? -5.355  -8.038  26.688  1.00 7.97  ? 31  VAL A C    1 
ATOM   247  O  O    . VAL A 1 31  ? -6.305  -8.091  25.920  1.00 8.80  ? 31  VAL A O    1 
ATOM   248  C  CB   . VAL A 1 31  ? -4.801  -5.978  27.992  1.00 8.78  ? 31  VAL A CB   1 
ATOM   249  C  CG1  . VAL A 1 31  ? -3.855  -4.793  28.101  1.00 9.49  ? 31  VAL A CG1  1 
ATOM   250  C  CG2  . VAL A 1 31  ? -6.289  -5.517  28.012  1.00 9.90  ? 31  VAL A CG2  1 
ATOM   251  N  N    . ASP A 1 32  ? -4.991  -9.027  27.524  1.00 8.64  ? 32  ASP A N    1 
ATOM   252  C  CA   . ASP A 1 32  ? -5.913  -10.099 27.834  1.00 8.26  ? 32  ASP A CA   1 
ATOM   253  C  C    . ASP A 1 32  ? -6.999  -9.564  28.789  1.00 8.54  ? 32  ASP A C    1 
ATOM   254  O  O    . ASP A 1 32  ? -6.692  -8.947  29.795  1.00 10.69 ? 32  ASP A O    1 
ATOM   255  C  CB   . ASP A 1 32  ? -5.179  -11.276 28.419  1.00 10.44 ? 32  ASP A CB   1 
ATOM   256  C  CG   . ASP A 1 32  ? -6.129  -12.426 28.741  1.00 11.06 ? 32  ASP A CG   1 
ATOM   257  O  OD1  . ASP A 1 32  ? -6.781  -12.854 27.805  1.00 9.59  ? 32  ASP A OD1  1 
ATOM   258  O  OD2  . ASP A 1 32  ? -6.120  -12.887 29.940  1.00 14.36 ? 32  ASP A OD2  1 
ATOM   259  N  N    . ILE A 1 33  ? -8.263  -9.889  28.492  1.00 8.91  ? 33  ILE A N    1 
ATOM   260  C  CA   . ILE A 1 33  ? -9.340  -9.478  29.344  1.00 9.56  ? 33  ILE A CA   1 
ATOM   261  C  C    . ILE A 1 33  ? -9.625  -10.732 30.184  1.00 10.52 ? 33  ILE A C    1 
ATOM   262  O  O    . ILE A 1 33  ? -10.199 -11.719 29.698  1.00 11.37 ? 33  ILE A O    1 
ATOM   263  C  CB   . ILE A 1 33  ? -10.570 -9.061  28.552  1.00 9.87  ? 33  ILE A CB   1 
ATOM   264  C  CG1  . ILE A 1 33  ? -10.215 -7.846  27.688  1.00 10.05 ? 33  ILE A CG1  1 
ATOM   265  C  CG2  . ILE A 1 33  ? -11.801 -8.808  29.448  1.00 11.05 ? 33  ILE A CG2  1 
ATOM   266  C  CD1  . ILE A 1 33  ? -11.214 -7.543  26.584  1.00 12.03 ? 33  ILE A CD1  1 
ATOM   267  N  N    A ASP A 1 34  ? -9.237  -10.666 31.450  0.50 11.45 ? 34  ASP A N    1 
ATOM   268  N  N    B ASP A 1 34  ? -9.258  -10.695 31.443  0.50 11.28 ? 34  ASP A N    1 
ATOM   269  C  CA   A ASP A 1 34  ? -9.524  -11.720 32.449  0.50 12.84 ? 34  ASP A CA   1 
ATOM   270  C  CA   B ASP A 1 34  ? -9.534  -11.829 32.322  0.50 12.85 ? 34  ASP A CA   1 
ATOM   271  C  C    A ASP A 1 34  ? -10.967 -11.465 32.881  0.50 12.66 ? 34  ASP A C    1 
ATOM   272  C  C    B ASP A 1 34  ? -10.901 -11.546 32.898  0.50 12.83 ? 34  ASP A C    1 
ATOM   273  O  O    A ASP A 1 34  ? -11.290 -10.478 33.576  0.50 13.25 ? 34  ASP A O    1 
ATOM   274  O  O    B ASP A 1 34  ? -11.083 -10.627 33.722  0.50 14.87 ? 34  ASP A O    1 
ATOM   275  C  CB   A ASP A 1 34  ? -8.541  -11.599 33.621  0.50 13.88 ? 34  ASP A CB   1 
ATOM   276  C  CB   B ASP A 1 34  ? -8.490  -11.878 33.408  0.50 13.03 ? 34  ASP A CB   1 
ATOM   277  C  CG   A ASP A 1 34  ? -8.751  -12.661 34.669  0.50 15.13 ? 34  ASP A CG   1 
ATOM   278  C  CG   B ASP A 1 34  ? -8.649  -13.074 34.284  0.50 16.95 ? 34  ASP A CG   1 
ATOM   279  O  OD1  A ASP A 1 34  ? -9.894  -13.134 34.782  0.50 13.41 ? 34  ASP A OD1  1 
ATOM   280  O  OD1  B ASP A 1 34  ? -8.297  -14.177 33.844  0.50 19.09 ? 34  ASP A OD1  1 
ATOM   281  O  OD2  A ASP A 1 34  ? -7.773  -13.027 35.374  0.50 20.28 ? 34  ASP A OD2  1 
ATOM   282  O  OD2  B ASP A 1 34  ? -9.143  -12.890 35.405  0.50 18.03 ? 34  ASP A OD2  1 
ATOM   283  N  N    . THR A 1 35  ? -11.887 -12.280 32.417  1.00 13.87 ? 35  THR A N    1 
ATOM   284  C  CA   . THR A 1 35  ? -13.274 -11.929 32.681  1.00 14.56 ? 35  THR A CA   1 
ATOM   285  C  C    . THR A 1 35  ? -13.680 -12.039 34.107  1.00 15.50 ? 35  THR A C    1 
ATOM   286  O  O    . THR A 1 35  ? -14.618 -11.352 34.559  1.00 18.36 ? 35  THR A O    1 
ATOM   287  C  CB   . THR A 1 35  ? -14.191 -12.806 31.870  1.00 15.32 ? 35  THR A CB   1 
ATOM   288  O  OG1  . THR A 1 35  ? -14.113 -14.126 32.360  1.00 17.99 ? 35  THR A OG1  1 
ATOM   289  C  CG2  . THR A 1 35  ? -13.945 -12.763 30.401  1.00 16.97 ? 35  THR A CG2  1 
ATOM   290  N  N    . HIS A 1 36  ? -12.976 -12.857 34.871  1.00 16.43 ? 36  HIS A N    1 
ATOM   291  C  CA   . HIS A 1 36  ? -13.274 -13.073 36.249  1.00 17.41 ? 36  HIS A CA   1 
ATOM   292  C  C    . HIS A 1 36  ? -12.745 -11.925 37.097  1.00 18.09 ? 36  HIS A C    1 
ATOM   293  O  O    . HIS A 1 36  ? -13.463 -11.570 38.066  1.00 21.16 ? 36  HIS A O    1 
ATOM   294  C  CB   . HIS A 1 36  ? -12.804 -14.486 36.639  1.00 18.37 ? 36  HIS A CB   1 
ATOM   295  C  CG   . HIS A 1 36  ? -13.758 -15.540 36.148  1.00 21.22 ? 36  HIS A CG   1 
ATOM   296  N  ND1  . HIS A 1 36  ? -13.484 -16.447 35.137  1.00 24.43 ? 36  HIS A ND1  1 
ATOM   297  C  CD2  . HIS A 1 36  ? -15.078 -15.692 36.451  1.00 22.12 ? 36  HIS A CD2  1 
ATOM   298  C  CE1  . HIS A 1 36  ? -14.582 -17.147 34.897  1.00 23.36 ? 36  HIS A CE1  1 
ATOM   299  N  NE2  . HIS A 1 36  ? -15.548 -16.737 35.697  1.00 30.12 ? 36  HIS A NE2  1 
ATOM   300  N  N    A THR A 1 37  ? -11.622 -11.273 36.726  0.50 18.14 ? 37  THR A N    1 
ATOM   301  N  N    B THR A 1 37  ? -11.618 -11.299 36.685  0.50 17.16 ? 37  THR A N    1 
ATOM   302  C  CA   A THR A 1 37  ? -11.136 -10.131 37.502  0.50 18.37 ? 37  THR A CA   1 
ATOM   303  C  CA   B THR A 1 37  ? -11.004 -10.174 37.381  0.50 16.73 ? 37  THR A CA   1 
ATOM   304  C  C    A THR A 1 37  ? -11.536 -8.728  36.957  0.50 16.88 ? 37  THR A C    1 
ATOM   305  C  C    B THR A 1 37  ? -11.692 -8.815  37.041  0.50 15.64 ? 37  THR A C    1 
ATOM   306  O  O    A THR A 1 37  ? -11.162 -7.684  37.537  0.50 17.20 ? 37  THR A O    1 
ATOM   307  O  O    B THR A 1 37  ? -11.710 -7.905  37.867  0.50 15.94 ? 37  THR A O    1 
ATOM   308  C  CB   A THR A 1 37  ? -9.676  -10.209 37.746  0.50 19.45 ? 37  THR A CB   1 
ATOM   309  C  CB   B THR A 1 37  ? -9.522  -10.132 37.111  0.50 16.86 ? 37  THR A CB   1 
ATOM   310  O  OG1  A THR A 1 37  ? -8.981  -10.164 36.500  0.50 20.43 ? 37  THR A OG1  1 
ATOM   311  O  OG1  B THR A 1 37  ? -8.951  -11.316 37.653  0.50 19.85 ? 37  THR A OG1  1 
ATOM   312  C  CG2  A THR A 1 37  ? -9.349  -11.510 38.466  0.50 19.25 ? 37  THR A CG2  1 
ATOM   313  C  CG2  B THR A 1 37  ? -8.854  -8.917  37.789  0.50 15.26 ? 37  THR A CG2  1 
ATOM   314  N  N    . ALA A 1 38  ? -12.285 -8.721  35.855  1.00 16.13 ? 38  ALA A N    1 
ATOM   315  C  CA   . ALA A 1 38  ? -12.890 -7.463  35.388  1.00 14.59 ? 38  ALA A CA   1 
ATOM   316  C  C    . ALA A 1 38  ? -13.940 -7.102  36.433  1.00 16.94 ? 38  ALA A C    1 
ATOM   317  O  O    . ALA A 1 38  ? -14.655 -7.966  36.936  1.00 19.39 ? 38  ALA A O    1 
ATOM   318  C  CB   . ALA A 1 38  ? -13.485 -7.649  34.039  1.00 15.35 ? 38  ALA A CB   1 
ATOM   319  N  N    . LYS A 1 39  ? -13.991 -5.827  36.789  1.00 15.27 ? 39  LYS A N    1 
ATOM   320  C  CA   . LYS A 1 39  ? -14.883 -5.363  37.845  1.00 16.24 ? 39  LYS A CA   1 
ATOM   321  C  C    . LYS A 1 39  ? -16.197 -4.858  37.207  1.00 14.86 ? 39  LYS A C    1 
ATOM   322  O  O    . LYS A 1 39  ? -16.182 -3.959  36.410  1.00 14.20 ? 39  LYS A O    1 
ATOM   323  C  CB   . LYS A 1 39  ? -14.116 -4.231  38.529  1.00 18.96 ? 39  LYS A CB   1 
ATOM   324  C  CG   . LYS A 1 39  ? -14.910 -3.378  39.479  1.00 21.26 ? 39  LYS A CG   1 
ATOM   325  C  CD   . LYS A 1 39  ? -15.201 -4.089  40.775  1.00 20.04 ? 39  LYS A CD   1 
ATOM   326  C  CE   . LYS A 1 39  ? -16.125 -3.257  41.646  1.00 22.99 ? 39  LYS A CE   1 
ATOM   327  N  NZ   . LYS A 1 39  ? -16.301 -3.834  42.931  1.00 24.37 ? 39  LYS A NZ   1 
ATOM   328  N  N    . TYR A 1 40  ? -17.314 -5.430  37.576  1.00 16.88 ? 40  TYR A N    1 
ATOM   329  C  CA   . TYR A 1 40  ? -18.569 -4.866  37.150  1.00 17.35 ? 40  TYR A CA   1 
ATOM   330  C  C    . TYR A 1 40  ? -18.750 -3.483  37.767  1.00 16.97 ? 40  TYR A C    1 
ATOM   331  O  O    . TYR A 1 40  ? -18.653 -3.326  38.992  1.00 18.70 ? 40  TYR A O    1 
ATOM   332  C  CB   . TYR A 1 40  ? -19.742 -5.808  37.506  1.00 19.30 ? 40  TYR A CB   1 
ATOM   333  C  CG   . TYR A 1 40  ? -21.068 -5.166  37.395  1.00 21.71 ? 40  TYR A CG   1 
ATOM   334  C  CD1  . TYR A 1 40  ? -21.523 -4.687  36.170  1.00 23.95 ? 40  TYR A CD1  1 
ATOM   335  C  CD2  . TYR A 1 40  ? -21.917 -5.086  38.519  1.00 25.65 ? 40  TYR A CD2  1 
ATOM   336  C  CE1  . TYR A 1 40  ? -22.765 -4.082  36.030  1.00 23.43 ? 40  TYR A CE1  1 
ATOM   337  C  CE2  . TYR A 1 40  ? -23.194 -4.480  38.388  1.00 29.48 ? 40  TYR A CE2  1 
ATOM   338  C  CZ   . TYR A 1 40  ? -23.606 -4.011  37.141  1.00 26.35 ? 40  TYR A CZ   1 
ATOM   339  O  OH   . TYR A 1 40  ? -24.837 -3.396  37.021  1.00 31.69 ? 40  TYR A OH   1 
ATOM   340  N  N    . ASP A 1 41  ? -19.021 -2.486  36.910  1.00 16.20 ? 41  ASP A N    1 
ATOM   341  C  CA   . ASP A 1 41  ? -19.197 -1.088  37.384  1.00 18.77 ? 41  ASP A CA   1 
ATOM   342  C  C    . ASP A 1 41  ? -20.629 -0.679  37.095  1.00 21.47 ? 41  ASP A C    1 
ATOM   343  O  O    . ASP A 1 41  ? -20.942 -0.315  35.944  1.00 21.09 ? 41  ASP A O    1 
ATOM   344  C  CB   . ASP A 1 41  ? -18.213 -0.144  36.700  1.00 19.96 ? 41  ASP A CB   1 
ATOM   345  C  CG   . ASP A 1 41  ? -18.241 1.227   37.298  1.00 26.64 ? 41  ASP A CG   1 
ATOM   346  O  OD1  . ASP A 1 41  ? -19.201 1.513   38.035  1.00 27.91 ? 41  ASP A OD1  1 
ATOM   347  O  OD2  . ASP A 1 41  ? -17.291 1.981   37.011  1.00 31.18 ? 41  ASP A OD2  1 
ATOM   348  N  N    . PRO A 1 42  ? -21.522 -0.712  38.149  1.00 23.84 ? 42  PRO A N    1 
ATOM   349  C  CA   . PRO A 1 42  ? -22.903 -0.359  37.897  1.00 25.23 ? 42  PRO A CA   1 
ATOM   350  C  C    . PRO A 1 42  ? -23.043 1.117   37.514  1.00 26.67 ? 42  PRO A C    1 
ATOM   351  O  O    . PRO A 1 42  ? -24.057 1.480   36.934  1.00 30.31 ? 42  PRO A O    1 
ATOM   352  C  CB   . PRO A 1 42  ? -23.565 -0.620  39.243  1.00 26.70 ? 42  PRO A CB   1 
ATOM   353  C  CG   . PRO A 1 42  ? -22.454 -0.348  40.242  1.00 25.95 ? 42  PRO A CG   1 
ATOM   354  C  CD   . PRO A 1 42  ? -21.315 -1.082  39.561  1.00 23.40 ? 42  PRO A CD   1 
ATOM   355  N  N    . SER A 1 43  ? -22.008 1.932   37.729  1.00 25.58 ? 43  SER A N    1 
ATOM   356  C  CA   . SER A 1 43  ? -22.109 3.334   37.312  1.00 28.12 ? 43  SER A CA   1 
ATOM   357  C  C    . SER A 1 43  ? -21.759 3.561   35.808  1.00 26.69 ? 43  SER A C    1 
ATOM   358  O  O    . SER A 1 43  ? -21.852 4.709   35.260  1.00 29.20 ? 43  SER A O    1 
ATOM   359  C  CB   . SER A 1 43  ? -21.193 4.198   38.155  1.00 30.15 ? 43  SER A CB   1 
ATOM   360  O  OG   . SER A 1 43  ? -19.891 4.168   37.636  1.00 30.45 ? 43  SER A OG   1 
ATOM   361  N  N    . LEU A 1 44  ? -21.316 2.514   35.115  1.00 25.15 ? 44  LEU A N    1 
ATOM   362  C  CA   . LEU A 1 44  ? -21.031 2.659   33.694  1.00 22.09 ? 44  LEU A CA   1 
ATOM   363  C  C    . LEU A 1 44  ? -22.343 2.791   32.955  1.00 22.71 ? 44  LEU A C    1 
ATOM   364  O  O    . LEU A 1 44  ? -23.309 2.107   33.244  1.00 25.85 ? 44  LEU A O    1 
ATOM   365  C  CB   . LEU A 1 44  ? -20.278 1.432   33.154  1.00 21.90 ? 44  LEU A CB   1 
ATOM   366  C  CG   . LEU A 1 44  ? -18.782 1.403   33.412  1.00 18.48 ? 44  LEU A CG   1 
ATOM   367  C  CD1  . LEU A 1 44  ? -18.298 0.090   32.932  1.00 19.15 ? 44  LEU A CD1  1 
ATOM   368  C  CD2  . LEU A 1 44  ? -18.068 2.577   32.671  1.00 20.12 ? 44  LEU A CD2  1 
ATOM   369  N  N    . LYS A 1 45  ? -22.376 3.641   31.935  1.00 20.58 ? 45  LYS A N    1 
ATOM   370  C  CA   . LYS A 1 45  ? -23.658 3.855   31.214  1.00 22.56 ? 45  LYS A CA   1 
ATOM   371  C  C    . LYS A 1 45  ? -23.703 2.957   30.001  1.00 20.59 ? 45  LYS A C    1 
ATOM   372  O  O    . LYS A 1 45  ? -22.646 2.455   29.552  1.00 19.70 ? 45  LYS A O    1 
ATOM   373  C  CB   . LYS A 1 45  ? -23.751 5.273   30.796  1.00 21.29 ? 45  LYS A CB   1 
ATOM   374  C  CG   . LYS A 1 45  ? -23.634 6.321   31.906  1.00 25.98 ? 45  LYS A CG   1 
ATOM   375  C  CD   . LYS A 1 45  ? -23.556 7.747   31.286  1.00 32.38 ? 45  LYS A CD   1 
ATOM   376  C  CE   . LYS A 1 45  ? -22.647 8.693   32.114  1.00 38.16 ? 45  LYS A CE   1 
ATOM   377  N  NZ   . LYS A 1 45  ? -23.252 8.835   33.473  1.00 40.84 ? 45  LYS A NZ   1 
ATOM   378  N  N    . PRO A 1 46  ? -24.900 2.749   29.444  1.00 19.21 ? 46  PRO A N    1 
ATOM   379  C  CA   . PRO A 1 46  ? -24.967 2.077   28.148  1.00 18.44 ? 46  PRO A CA   1 
ATOM   380  C  C    . PRO A 1 46  ? -24.181 2.876   27.142  1.00 17.48 ? 46  PRO A C    1 
ATOM   381  O  O    . PRO A 1 46  ? -24.123 4.072   27.247  1.00 17.83 ? 46  PRO A O    1 
ATOM   382  C  CB   . PRO A 1 46  ? -26.441 2.173   27.780  1.00 18.20 ? 46  PRO A CB   1 
ATOM   383  C  CG   . PRO A 1 46  ? -27.153 2.600   29.019  1.00 22.75 ? 46  PRO A CG   1 
ATOM   384  C  CD   . PRO A 1 46  ? -26.219 3.109   30.010  1.00 20.96 ? 46  PRO A CD   1 
ATOM   385  N  N    . LEU A 1 47  ? -23.528 2.192   26.223  1.00 18.13 ? 47  LEU A N    1 
ATOM   386  C  CA   . LEU A 1 47  ? -22.834 2.841   25.153  1.00 16.74 ? 47  LEU A CA   1 
ATOM   387  C  C    . LEU A 1 47  ? -23.929 3.447   24.239  1.00 16.69 ? 47  LEU A C    1 
ATOM   388  O  O    . LEU A 1 47  ? -24.991 2.848   24.061  1.00 20.03 ? 47  LEU A O    1 
ATOM   389  C  CB   . LEU A 1 47  ? -22.076 1.732   24.434  1.00 20.33 ? 47  LEU A CB   1 
ATOM   390  C  CG   . LEU A 1 47  ? -20.984 2.128   23.538  1.00 21.38 ? 47  LEU A CG   1 
ATOM   391  C  CD1  . LEU A 1 47  ? -19.919 2.930   24.259  1.00 21.63 ? 47  LEU A CD1  1 
ATOM   392  C  CD2  . LEU A 1 47  ? -20.435 0.793   23.050  1.00 21.79 ? 47  LEU A CD2  1 
ATOM   393  N  N    . SER A 1 48  ? -23.670 4.629   23.693  1.00 14.08 ? 48  SER A N    1 
ATOM   394  C  CA   . SER A 1 48  ? -24.488 5.260   22.686  1.00 14.60 ? 48  SER A CA   1 
ATOM   395  C  C    . SER A 1 48  ? -23.703 5.252   21.365  1.00 13.72 ? 48  SER A C    1 
ATOM   396  O  O    . SER A 1 48  ? -22.720 5.990   21.212  1.00 15.14 ? 48  SER A O    1 
ATOM   397  C  CB   . SER A 1 48  ? -24.772 6.712   23.120  1.00 16.67 ? 48  SER A CB   1 
ATOM   398  O  OG   . SER A 1 48  ? -25.479 7.384   22.086  1.00 19.90 ? 48  SER A OG   1 
ATOM   399  N  N    . VAL A 1 49  ? -24.140 4.440   20.449  1.00 15.77 ? 49  VAL A N    1 
ATOM   400  C  CA   . VAL A 1 49  ? -23.589 4.382   19.131  1.00 17.03 ? 49  VAL A CA   1 
ATOM   401  C  C    . VAL A 1 49  ? -24.543 5.010   18.170  1.00 17.52 ? 49  VAL A C    1 
ATOM   402  O  O    . VAL A 1 49  ? -25.597 4.488   17.958  1.00 20.29 ? 49  VAL A O    1 
ATOM   403  C  CB   . VAL A 1 49  ? -23.396 2.938   18.739  1.00 18.72 ? 49  VAL A CB   1 
ATOM   404  C  CG1  . VAL A 1 49  ? -22.711 2.836   17.334  1.00 22.35 ? 49  VAL A CG1  1 
ATOM   405  C  CG2  . VAL A 1 49  ? -22.566 2.240   19.829  1.00 18.23 ? 49  VAL A CG2  1 
ATOM   406  N  N    . SER A 1 50  ? -24.229 6.138   17.604  1.00 17.76 ? 50  SER A N    1 
ATOM   407  C  CA   . SER A 1 50  ? -25.121 6.837   16.733  1.00 18.37 ? 50  SER A CA   1 
ATOM   408  C  C    . SER A 1 50  ? -24.569 6.933   15.401  1.00 15.71 ? 50  SER A C    1 
ATOM   409  O  O    . SER A 1 50  ? -23.822 7.824   15.120  1.00 16.96 ? 50  SER A O    1 
ATOM   410  C  CB   . SER A 1 50  ? -25.514 8.248   17.242  1.00 18.89 ? 50  SER A CB   1 
ATOM   411  O  OG   . SER A 1 50  ? -26.127 8.143   18.498  1.00 25.76 ? 50  SER A OG   1 
ATOM   412  N  N    . TYR A 1 51  ? -24.808 5.911   14.583  1.00 16.80 ? 51  TYR A N    1 
ATOM   413  C  CA   . TYR A 1 51  ? -24.213 5.820   13.276  1.00 15.79 ? 51  TYR A CA   1 
ATOM   414  C  C    . TYR A 1 51  ? -25.180 6.057   12.113  1.00 17.32 ? 51  TYR A C    1 
ATOM   415  O  O    . TYR A 1 51  ? -24.792 5.855   10.955  1.00 17.53 ? 51  TYR A O    1 
ATOM   416  C  CB   . TYR A 1 51  ? -23.552 4.425   13.110  1.00 15.56 ? 51  TYR A CB   1 
ATOM   417  C  CG   . TYR A 1 51  ? -22.271 4.146   13.881  1.00 13.77 ? 51  TYR A CG   1 
ATOM   418  C  CD1  . TYR A 1 51  ? -21.565 5.148   14.491  1.00 15.05 ? 51  TYR A CD1  1 
ATOM   419  C  CD2  . TYR A 1 51  ? -21.781 2.874   13.927  1.00 13.05 ? 51  TYR A CD2  1 
ATOM   420  C  CE1  . TYR A 1 51  ? -20.358 4.840   15.151  1.00 13.07 ? 51  TYR A CE1  1 
ATOM   421  C  CE2  . TYR A 1 51  ? -20.651 2.537   14.539  1.00 11.38 ? 51  TYR A CE2  1 
ATOM   422  C  CZ   . TYR A 1 51  ? -19.930 3.552   15.214  1.00 11.15 ? 51  TYR A CZ   1 
ATOM   423  O  OH   . TYR A 1 51  ? -18.742 3.181   15.798  1.00 12.47 ? 51  TYR A OH   1 
ATOM   424  N  N    . ASP A 1 52  ? -26.410 6.501   12.426  1.00 19.08 ? 52  ASP A N    1 
ATOM   425  C  CA   . ASP A 1 52  ? -27.402 6.743   11.366  1.00 21.07 ? 52  ASP A CA   1 
ATOM   426  C  C    . ASP A 1 52  ? -26.963 7.639   10.195  1.00 21.65 ? 52  ASP A C    1 
ATOM   427  O  O    . ASP A 1 52  ? -27.306 7.373   9.020   1.00 22.63 ? 52  ASP A O    1 
ATOM   428  C  CB   . ASP A 1 52  ? -28.689 7.269   11.967  1.00 22.06 ? 52  ASP A CB   1 
ATOM   429  C  CG   . ASP A 1 52  ? -28.473 8.183   13.149  1.00 28.90 ? 52  ASP A CG   1 
ATOM   430  O  OD1  . ASP A 1 52  ? -27.974 7.810   14.287  1.00 34.88 ? 52  ASP A OD1  1 
ATOM   431  O  OD2  . ASP A 1 52  ? -28.835 9.341   12.939  1.00 38.33 ? 52  ASP A OD2  1 
ATOM   432  N  N    . GLN A 1 53  ? -26.154 8.639   10.484  1.00 21.59 ? 53  GLN A N    1 
ATOM   433  C  CA   . GLN A 1 53  ? -25.797 9.621   9.429   1.00 22.23 ? 53  GLN A CA   1 
ATOM   434  C  C    . GLN A 1 53  ? -24.355 9.420   9.000   1.00 19.46 ? 53  GLN A C    1 
ATOM   435  O  O    . GLN A 1 53  ? -23.733 10.311  8.465   1.00 20.05 ? 53  GLN A O    1 
ATOM   436  C  CB   . GLN A 1 53  ? -25.954 11.066  9.955   1.00 23.56 ? 53  GLN A CB   1 
ATOM   437  C  CG   . GLN A 1 53  ? -27.420 11.515  10.098  1.00 29.07 ? 53  GLN A CG   1 
ATOM   438  C  CD   . GLN A 1 53  ? -28.125 11.295  8.790   1.00 34.41 ? 53  GLN A CD   1 
ATOM   439  O  OE1  . GLN A 1 53  ? -27.643 11.763  7.707   1.00 35.83 ? 53  GLN A OE1  1 
ATOM   440  N  NE2  . GLN A 1 53  ? -29.210 10.509  8.826   1.00 34.95 ? 53  GLN A NE2  1 
ATOM   441  N  N    . ALA A 1 54  ? -23.772 8.273   9.310   1.00 17.83 ? 54  ALA A N    1 
ATOM   442  C  CA   . ALA A 1 54  ? -22.408 8.004   8.883   1.00 15.44 ? 54  ALA A CA   1 
ATOM   443  C  C    . ALA A 1 54  ? -22.189 8.205   7.380   1.00 16.77 ? 54  ALA A C    1 
ATOM   444  O  O    . ALA A 1 54  ? -23.060 7.797   6.530   1.00 19.11 ? 54  ALA A O    1 
ATOM   445  C  CB   . ALA A 1 54  ? -21.989 6.612   9.274   1.00 16.12 ? 54  ALA A CB   1 
ATOM   446  N  N    . THR A 1 55  ? -21.053 8.787   7.014   1.00 14.72 ? 55  THR A N    1 
ATOM   447  C  CA   . THR A 1 55  ? -20.684 8.941   5.619   1.00 15.72 ? 55  THR A CA   1 
ATOM   448  C  C    . THR A 1 55  ? -19.351 8.306   5.342   1.00 13.89 ? 55  THR A C    1 
ATOM   449  O  O    . THR A 1 55  ? -18.344 8.897   5.606   1.00 14.08 ? 55  THR A O    1 
ATOM   450  C  CB   . THR A 1 55  ? -20.546 10.520  5.262   1.00 16.51 ? 55  THR A CB   1 
ATOM   451  O  OG1  . THR A 1 55  ? -21.805 11.102  5.346   1.00 21.30 ? 55  THR A OG1  1 
ATOM   452  C  CG2  . THR A 1 55  ? -20.024 10.645  3.788   1.00 20.46 ? 55  THR A CG2  1 
ATOM   453  N  N    . SER A 1 56  ? -19.376 7.081   4.859   1.00 14.65 ? 56  SER A N    1 
ATOM   454  C  CA   . SER A 1 56  ? -18.142 6.516   4.452   1.00 14.11 ? 56  SER A CA   1 
ATOM   455  C  C    . SER A 1 56  ? -17.659 7.158   3.160   1.00 16.40 ? 56  SER A C    1 
ATOM   456  O  O    . SER A 1 56  ? -18.466 7.638   2.350   1.00 16.19 ? 56  SER A O    1 
ATOM   457  C  CB   . SER A 1 56  ? -18.210 4.989   4.268   1.00 14.84 ? 56  SER A CB   1 
ATOM   458  O  OG   . SER A 1 56  ? -19.067 4.639   3.170   1.00 16.52 ? 56  SER A OG   1 
ATOM   459  N  N    . LEU A 1 57  ? -16.345 7.170   2.982   1.00 14.58 ? 57  LEU A N    1 
ATOM   460  C  CA   . LEU A 1 57  ? -15.796 7.817   1.818   1.00 16.23 ? 57  LEU A CA   1 
ATOM   461  C  C    . LEU A 1 57  ? -14.965 6.891   0.961   1.00 15.77 ? 57  LEU A C    1 
ATOM   462  O  O    . LEU A 1 57  ? -15.029 6.957   -0.260  1.00 16.70 ? 57  LEU A O    1 
ATOM   463  C  CB   . LEU A 1 57  ? -14.955 9.030   2.217   1.00 17.87 ? 57  LEU A CB   1 
ATOM   464  C  CG   . LEU A 1 57  ? -15.795 10.201  2.819   1.00 19.23 ? 57  LEU A CG   1 
ATOM   465  C  CD1  . LEU A 1 57  ? -14.828 11.289  3.204   1.00 23.87 ? 57  LEU A CD1  1 
ATOM   466  C  CD2  . LEU A 1 57  ? -16.834 10.773  1.847   1.00 22.39 ? 57  LEU A CD2  1 
ATOM   467  N  N    . ARG A 1 58  ? -14.087 6.114   1.587   1.00 14.48 ? 58  ARG A N    1 
ATOM   468  C  CA   . ARG A 1 58  ? -13.019 5.484   0.835   1.00 14.45 ? 58  ARG A CA   1 
ATOM   469  C  C    . ARG A 1 58  ? -12.518 4.315   1.649   1.00 14.38 ? 58  ARG A C    1 
ATOM   470  O  O    . ARG A 1 58  ? -12.671 4.316   2.869   1.00 13.81 ? 58  ARG A O    1 
ATOM   471  C  CB   . ARG A 1 58  ? -11.866 6.486   0.687   1.00 17.31 ? 58  ARG A CB   1 
ATOM   472  C  CG   . ARG A 1 58  ? -10.859 6.117   -0.221  1.00 19.46 ? 58  ARG A CG   1 
ATOM   473  C  CD   . ARG A 1 58  ? -9.949  7.281   -0.369  1.00 23.01 ? 58  ARG A CD   1 
ATOM   474  N  NE   . ARG A 1 58  ? -9.104  7.319   0.791   1.00 19.10 ? 58  ARG A NE   1 
ATOM   475  C  CZ   . ARG A 1 58  ? -7.794  7.448   0.738   1.00 17.37 ? 58  ARG A CZ   1 
ATOM   476  N  NH1  . ARG A 1 58  ? -7.172  7.740   -0.397  1.00 19.73 ? 58  ARG A NH1  1 
ATOM   477  N  NH2  . ARG A 1 58  ? -7.126  7.403   1.886   1.00 19.78 ? 58  ARG A NH2  1 
ATOM   478  N  N    . ILE A 1 59  ? -11.905 3.354   0.964   1.00 13.02 ? 59  ILE A N    1 
ATOM   479  C  CA   . ILE A 1 59  ? -11.268 2.206   1.597   1.00 12.55 ? 59  ILE A CA   1 
ATOM   480  C  C    . ILE A 1 59  ? -9.826  2.252   1.080   1.00 12.00 ? 59  ILE A C    1 
ATOM   481  O  O    . ILE A 1 59  ? -9.552  2.439   -0.123  1.00 15.28 ? 59  ILE A O    1 
ATOM   482  C  CB   . ILE A 1 59  ? -12.040 0.924   1.325   1.00 12.38 ? 59  ILE A CB   1 
ATOM   483  C  CG1  . ILE A 1 59  ? -11.450 -0.202  2.197   1.00 13.43 ? 59  ILE A CG1  1 
ATOM   484  C  CG2  . ILE A 1 59  ? -11.969 0.522   -0.168  1.00 15.25 ? 59  ILE A CG2  1 
ATOM   485  C  CD1  . ILE A 1 59  ? -12.281 -1.494  2.121   1.00 14.28 ? 59  ILE A CD1  1 
ATOM   486  N  N    . LEU A 1 60  ? -8.882  2.033   1.989   1.00 13.50 ? 60  LEU A N    1 
ATOM   487  C  CA   . LEU A 1 60  ? -7.454  2.185   1.708   1.00 13.63 ? 60  LEU A CA   1 
ATOM   488  C  C    . LEU A 1 60  ? -6.653  1.013   2.255   1.00 12.30 ? 60  LEU A C    1 
ATOM   489  O  O    . LEU A 1 60  ? -6.845  0.648   3.408   1.00 12.40 ? 60  LEU A O    1 
ATOM   490  C  CB   . LEU A 1 60  ? -6.950  3.513   2.441   1.00 15.29 ? 60  LEU A CB   1 
ATOM   491  C  CG   . LEU A 1 60  ? -5.425  3.635   2.447   1.00 15.95 ? 60  LEU A CG   1 
ATOM   492  C  CD1  . LEU A 1 60  ? -4.837  3.918   1.067   1.00 18.86 ? 60  LEU A CD1  1 
ATOM   493  C  CD2  . LEU A 1 60  ? -4.974  4.784   3.422   1.00 17.17 ? 60  LEU A CD2  1 
ATOM   494  N  N    . ASN A 1 61  ? -5.787  0.405   1.421   1.00 12.81 ? 61  ASN A N    1 
ATOM   495  C  CA   . ASN A 1 61  ? -4.799  -0.558  1.936   1.00 13.38 ? 61  ASN A CA   1 
ATOM   496  C  C    . ASN A 1 61  ? -3.599  0.261   2.343   1.00 13.77 ? 61  ASN A C    1 
ATOM   497  O  O    . ASN A 1 61  ? -2.983  0.884   1.481   1.00 15.69 ? 61  ASN A O    1 
ATOM   498  C  CB   . ASN A 1 61  ? -4.461  -1.583  0.843   1.00 13.88 ? 61  ASN A CB   1 
ATOM   499  C  CG   . ASN A 1 61  ? -3.375  -2.543  1.243   1.00 13.20 ? 61  ASN A CG   1 
ATOM   500  O  OD1  . ASN A 1 61  ? -2.536  -2.252  2.129   1.00 15.49 ? 61  ASN A OD1  1 
ATOM   501  N  ND2  . ASN A 1 61  ? -3.390  -3.752  0.649   1.00 15.19 ? 61  ASN A ND2  1 
ATOM   502  N  N    . ASN A 1 62  ? -3.322  0.344   3.642   1.00 12.93 ? 62  ASN A N    1 
ATOM   503  C  CA   . ASN A 1 62  ? -2.221  1.192   4.096   1.00 13.85 ? 62  ASN A CA   1 
ATOM   504  C  C    . ASN A 1 62  ? -0.942  0.420   4.319   1.00 15.40 ? 62  ASN A C    1 
ATOM   505  O  O    . ASN A 1 62  ? 0.097   0.968   4.842   1.00 18.53 ? 62  ASN A O    1 
ATOM   506  C  CB   . ASN A 1 62  ? -2.582  1.996   5.359   1.00 14.96 ? 62  ASN A CB   1 
ATOM   507  C  CG   . ASN A 1 62  ? -2.876  1.107   6.505   1.00 14.43 ? 62  ASN A CG   1 
ATOM   508  O  OD1  . ASN A 1 62  ? -2.479  -0.104  6.532   1.00 14.71 ? 62  ASN A OD1  1 
ATOM   509  N  ND2  . ASN A 1 62  ? -3.614  1.629   7.442   1.00 20.63 ? 62  ASN A ND2  1 
ATOM   510  N  N    . GLY A 1 63  ? -0.894  -0.836  3.871   1.00 15.30 ? 63  GLY A N    1 
ATOM   511  C  CA   . GLY A 1 63  ? 0.308   -1.634  4.050   1.00 15.04 ? 63  GLY A CA   1 
ATOM   512  C  C    . GLY A 1 63  ? 0.337   -2.442  5.339   1.00 15.28 ? 63  GLY A C    1 
ATOM   513  O  O    . GLY A 1 63  ? 1.191   -3.273  5.485   1.00 16.09 ? 63  GLY A O    1 
ATOM   514  N  N    . HIS A 1 64  ? -0.573  -2.174  6.272   1.00 13.15 ? 64  HIS A N    1 
ATOM   515  C  CA   A HIS A 1 64  ? -0.691  -2.876  7.573   0.50 14.07 ? 64  HIS A CA   1 
ATOM   516  C  CA   B HIS A 1 64  ? -0.672  -3.015  7.472   0.50 13.68 ? 64  HIS A CA   1 
ATOM   517  C  C    . HIS A 1 64  ? -2.076  -3.504  7.737   1.00 13.82 ? 64  HIS A C    1 
ATOM   518  O  O    . HIS A 1 64  ? -2.214  -4.527  8.347   1.00 17.20 ? 64  HIS A O    1 
ATOM   519  C  CB   A HIS A 1 64  ? -0.420  -1.879  8.728   0.50 14.69 ? 64  HIS A CB   1 
ATOM   520  C  CB   B HIS A 1 64  ? -0.045  -2.388  8.734   0.50 14.30 ? 64  HIS A CB   1 
ATOM   521  C  CG   A HIS A 1 64  ? 0.851   -1.119  8.534   0.50 16.49 ? 64  HIS A CG   1 
ATOM   522  C  CG   B HIS A 1 64  ? -0.632  -1.072  9.147   0.50 14.60 ? 64  HIS A CG   1 
ATOM   523  N  ND1  A HIS A 1 64  ? 0.885   0.220   8.204   0.50 17.82 ? 64  HIS A ND1  1 
ATOM   524  N  ND1  B HIS A 1 64  ? -0.170  0.152   8.692   0.50 15.41 ? 64  HIS A ND1  1 
ATOM   525  C  CD2  A HIS A 1 64  ? 2.136   -1.541  8.554   0.50 19.75 ? 64  HIS A CD2  1 
ATOM   526  C  CD2  B HIS A 1 64  ? -1.557  -0.783  10.086  0.50 15.84 ? 64  HIS A CD2  1 
ATOM   527  C  CE1  A HIS A 1 64  ? 2.144   0.585   8.007   0.50 17.63 ? 64  HIS A CE1  1 
ATOM   528  C  CE1  B HIS A 1 64  ? -0.829  1.132   9.294   0.50 14.79 ? 64  HIS A CE1  1 
ATOM   529  N  NE2  A HIS A 1 64  ? 2.924   -0.452  8.271   0.50 19.21 ? 64  HIS A NE2  1 
ATOM   530  N  NE2  B HIS A 1 64  ? -1.695  0.590   10.125  0.50 16.17 ? 64  HIS A NE2  1 
ATOM   531  N  N    . ALA A 1 65  ? -3.078  -2.850  7.225   1.00 12.53 ? 65  ALA A N    1 
ATOM   532  C  CA   . ALA A 1 65  ? -4.445  -3.288  7.278   1.00 11.90 ? 65  ALA A CA   1 
ATOM   533  C  C    . ALA A 1 65  ? -5.186  -2.554  6.160   1.00 11.21 ? 65  ALA A C    1 
ATOM   534  O  O    . ALA A 1 65  ? -4.518  -1.923  5.301   1.00 12.95 ? 65  ALA A O    1 
ATOM   535  C  CB   . ALA A 1 65  ? -5.101  -2.988  8.673   1.00 12.51 ? 65  ALA A CB   1 
ATOM   536  N  N    . PHE A 1 66  ? -6.518  -2.640  6.129   1.00 11.13 ? 66  PHE A N    1 
ATOM   537  C  CA   . PHE A 1 66  ? -7.249  -1.671  5.340   1.00 11.90 ? 66  PHE A CA   1 
ATOM   538  C  C    . PHE A 1 66  ? -8.150  -0.832  6.204   1.00 11.84 ? 66  PHE A C    1 
ATOM   539  O  O    . PHE A 1 66  ? -8.768  -1.322  7.162   1.00 12.97 ? 66  PHE A O    1 
ATOM   540  C  CB   . PHE A 1 66  ? -8.057  -2.327  4.180   1.00 13.34 ? 66  PHE A CB   1 
ATOM   541  C  CG   . PHE A 1 66  ? -9.111  -3.315  4.667   1.00 12.84 ? 66  PHE A CG   1 
ATOM   542  C  CD1  . PHE A 1 66  ? -10.393 -2.865  4.993   1.00 12.91 ? 66  PHE A CD1  1 
ATOM   543  C  CD2  . PHE A 1 66  ? -8.810  -4.667  4.820   1.00 13.39 ? 66  PHE A CD2  1 
ATOM   544  C  CE1  . PHE A 1 66  ? -11.353 -3.723  5.466   1.00 12.31 ? 66  PHE A CE1  1 
ATOM   545  C  CE2  . PHE A 1 66  ? -9.793  -5.554  5.343   1.00 13.19 ? 66  PHE A CE2  1 
ATOM   546  C  CZ   . PHE A 1 66  ? -11.036 -5.088  5.630   1.00 13.32 ? 66  PHE A CZ   1 
ATOM   547  N  N    . ASN A 1 67  ? -8.252  0.460   5.863   1.00 11.50 ? 67  ASN A N    1 
ATOM   548  C  CA   . ASN A 1 67  ? -9.118  1.363   6.624   1.00 12.21 ? 67  ASN A CA   1 
ATOM   549  C  C    . ASN A 1 67  ? -10.319 1.756   5.787   1.00 11.33 ? 67  ASN A C    1 
ATOM   550  O  O    . ASN A 1 67  ? -10.169 2.168   4.614   1.00 13.11 ? 67  ASN A O    1 
ATOM   551  C  CB   . ASN A 1 67  ? -8.395  2.681   6.959   1.00 12.80 ? 67  ASN A CB   1 
ATOM   552  C  CG   . ASN A 1 67  ? -7.321  2.519   7.884   1.00 15.43 ? 67  ASN A CG   1 
ATOM   553  O  OD1  . ASN A 1 67  ? -7.208  1.488   8.564   1.00 17.20 ? 67  ASN A OD1  1 
ATOM   554  N  ND2  . ASN A 1 67  ? -6.459  3.552   7.976   1.00 20.87 ? 67  ASN A ND2  1 
ATOM   555  N  N    . VAL A 1 68  ? -11.520 1.662   6.349   1.00 10.56 ? 68  VAL A N    1 
ATOM   556  C  CA   . VAL A 1 68  ? -12.713 2.292   5.762   1.00 11.29 ? 68  VAL A CA   1 
ATOM   557  C  C    . VAL A 1 68  ? -12.812 3.651   6.460   1.00 13.80 ? 68  VAL A C    1 
ATOM   558  O  O    . VAL A 1 68  ? -12.985 3.694   7.674   1.00 12.42 ? 68  VAL A O    1 
ATOM   559  C  CB   . VAL A 1 68  ? -13.981 1.390   5.941   1.00 13.17 ? 68  VAL A CB   1 
ATOM   560  C  CG1  . VAL A 1 68  ? -15.235 2.207   5.503   1.00 14.46 ? 68  VAL A CG1  1 
ATOM   561  C  CG2  . VAL A 1 68  ? -13.830 0.145   5.128   1.00 13.68 ? 68  VAL A CG2  1 
ATOM   562  N  N    . GLU A 1 69  ? -12.726 4.702   5.672   1.00 14.07 ? 69  GLU A N    1 
ATOM   563  C  CA   . GLU A 1 69  ? -12.652 6.041   6.208   1.00 13.90 ? 69  GLU A CA   1 
ATOM   564  C  C    . GLU A 1 69  ? -13.971 6.774   6.126   1.00 15.46 ? 69  GLU A C    1 
ATOM   565  O  O    . GLU A 1 69  ? -14.759 6.516   5.143   1.00 17.25 ? 69  GLU A O    1 
ATOM   566  C  CB   . GLU A 1 69  ? -11.700 6.829   5.360   1.00 16.22 ? 69  GLU A CB   1 
ATOM   567  C  CG   . GLU A 1 69  ? -10.331 6.265   5.379   1.00 16.70 ? 69  GLU A CG   1 
ATOM   568  C  CD   . GLU A 1 69  ? -9.555  6.765   4.223   1.00 18.37 ? 69  GLU A CD   1 
ATOM   569  O  OE1  . GLU A 1 69  ? -10.100 7.440   3.313   1.00 19.48 ? 69  GLU A OE1  1 
ATOM   570  O  OE2  . GLU A 1 69  ? -8.366  6.402   4.160   1.00 20.98 ? 69  GLU A OE2  1 
ATOM   571  N  N    . PHE A 1 70  ? -14.218 7.669   7.087   1.00 12.76 ? 70  PHE A N    1 
ATOM   572  C  CA   . PHE A 1 70  ? -15.483 8.382   7.143   1.00 12.38 ? 70  PHE A CA   1 
ATOM   573  C  C    . PHE A 1 70  ? -15.248 9.882   7.089   1.00 12.42 ? 70  PHE A C    1 
ATOM   574  O  O    . PHE A 1 70  ? -14.200 10.356  7.466   1.00 13.05 ? 70  PHE A O    1 
ATOM   575  C  CB   . PHE A 1 70  ? -16.179 8.016   8.437   1.00 11.20 ? 70  PHE A CB   1 
ATOM   576  C  CG   . PHE A 1 70  ? -16.728 6.604   8.374   1.00 11.96 ? 70  PHE A CG   1 
ATOM   577  C  CD1  . PHE A 1 70  ? -15.888 5.543   8.579   1.00 11.73 ? 70  PHE A CD1  1 
ATOM   578  C  CD2  . PHE A 1 70  ? -18.068 6.398   8.039   1.00 12.83 ? 70  PHE A CD2  1 
ATOM   579  C  CE1  . PHE A 1 70  ? -16.366 4.270   8.459   1.00 14.43 ? 70  PHE A CE1  1 
ATOM   580  C  CE2  . PHE A 1 70  ? -18.577 5.112   7.895   1.00 11.16 ? 70  PHE A CE2  1 
ATOM   581  C  CZ   . PHE A 1 70  ? -17.703 4.049   8.108   1.00 12.75 ? 70  PHE A CZ   1 
ATOM   582  N  N    . ASP A 1 71  ? -16.295 10.602  6.678   1.00 13.77 ? 71  ASP A N    1 
ATOM   583  C  CA   . ASP A 1 71  ? -16.238 12.040  6.823   1.00 14.09 ? 71  ASP A CA   1 
ATOM   584  C  C    . ASP A 1 71  ? -16.439 12.370  8.289   1.00 13.61 ? 71  ASP A C    1 
ATOM   585  O  O    . ASP A 1 71  ? -17.510 12.139  8.879   1.00 18.79 ? 71  ASP A O    1 
ATOM   586  C  CB   . ASP A 1 71  ? -17.345 12.625  5.995   1.00 15.97 ? 71  ASP A CB   1 
ATOM   587  C  CG   . ASP A 1 71  ? -17.525 14.097  6.249   1.00 17.30 ? 71  ASP A CG   1 
ATOM   588  O  OD1  . ASP A 1 71  ? -16.628 14.755  6.776   1.00 18.94 ? 71  ASP A OD1  1 
ATOM   589  O  OD2  . ASP A 1 71  ? -18.573 14.642  5.882   1.00 23.41 ? 71  ASP A OD2  1 
ATOM   590  N  N    . ASP A 1 72  ? -15.410 12.900  8.922   1.00 12.73 ? 72  ASP A N    1 
ATOM   591  C  CA   . ASP A 1 72  ? -15.477 13.254  10.323  1.00 12.90 ? 72  ASP A CA   1 
ATOM   592  C  C    . ASP A 1 72  ? -15.435 14.778  10.480  1.00 14.70 ? 72  ASP A C    1 
ATOM   593  O  O    . ASP A 1 72  ? -14.954 15.278  11.496  1.00 16.49 ? 72  ASP A O    1 
ATOM   594  C  CB   . ASP A 1 72  ? -14.303 12.618  11.105  1.00 12.99 ? 72  ASP A CB   1 
ATOM   595  C  CG   . ASP A 1 72  ? -12.956 13.095  10.632  1.00 13.99 ? 72  ASP A CG   1 
ATOM   596  O  OD1  . ASP A 1 72  ? -12.855 13.796  9.565   1.00 17.29 ? 72  ASP A OD1  1 
ATOM   597  O  OD2  . ASP A 1 72  ? -11.984 12.802  11.341  1.00 16.04 ? 72  ASP A OD2  1 
ATOM   598  N  N    . SER A 1 73  ? -15.963 15.484  9.483   1.00 15.53 ? 73  SER A N    1 
ATOM   599  C  CA   . SER A 1 73  ? -15.891 16.974  9.547   1.00 16.53 ? 73  SER A CA   1 
ATOM   600  C  C    . SER A 1 73  ? -17.178 17.555  10.141  1.00 18.14 ? 73  SER A C    1 
ATOM   601  O  O    . SER A 1 73  ? -17.308 18.782  10.201  1.00 18.49 ? 73  SER A O    1 
ATOM   602  C  CB   . SER A 1 73  ? -15.597 17.533  8.163   1.00 18.22 ? 73  SER A CB   1 
ATOM   603  O  OG   . SER A 1 73  ? -16.735 17.339  7.304   1.00 18.78 ? 73  SER A OG   1 
ATOM   604  N  N    . GLN A 1 74  ? -18.137 16.722  10.540  1.00 18.28 ? 74  GLN A N    1 
ATOM   605  C  CA   . GLN A 1 74  ? -19.341 17.062  11.323  1.00 20.25 ? 74  GLN A CA   1 
ATOM   606  C  C    . GLN A 1 74  ? -19.687 15.903  12.238  1.00 20.36 ? 74  GLN A C    1 
ATOM   607  O  O    . GLN A 1 74  ? -19.152 14.835  11.998  1.00 19.15 ? 74  GLN A O    1 
ATOM   608  C  CB   . GLN A 1 74  ? -20.566 17.176  10.388  1.00 22.03 ? 74  GLN A CB   1 
ATOM   609  C  CG   . GLN A 1 74  ? -20.469 18.310  9.463   1.00 25.22 ? 74  GLN A CG   1 
ATOM   610  C  CD   . GLN A 1 74  ? -21.790 18.499  8.751   1.00 27.17 ? 74  GLN A CD   1 
ATOM   611  O  OE1  . GLN A 1 74  ? -22.711 19.141  9.287   1.00 32.53 ? 74  GLN A OE1  1 
ATOM   612  N  NE2  . GLN A 1 74  ? -21.896 17.961  7.560   1.00 27.64 ? 74  GLN A NE2  1 
ATOM   613  N  N    . ASP A 1 75  ? -20.658 16.088  13.177  1.00 23.02 ? 75  ASP A N    1 
ATOM   614  C  CA   . ASP A 1 75  ? -21.064 15.025  14.122  1.00 25.23 ? 75  ASP A CA   1 
ATOM   615  C  C    . ASP A 1 75  ? -22.089 14.279  13.308  1.00 24.53 ? 75  ASP A C    1 
ATOM   616  O  O    . ASP A 1 75  ? -23.255 14.801  13.146  1.00 28.52 ? 75  ASP A O    1 
ATOM   617  C  CB   . ASP A 1 75  ? -21.733 15.484  15.443  1.00 27.68 ? 75  ASP A CB   1 
ATOM   618  C  CG   . ASP A 1 75  ? -20.714 16.032  16.441  1.00 30.52 ? 75  ASP A CG   1 
ATOM   619  O  OD1  . ASP A 1 75  ? -19.534 15.695  16.332  1.00 34.90 ? 75  ASP A OD1  1 
ATOM   620  O  OD2  . ASP A 1 75  ? -21.116 16.771  17.380  1.00 39.90 ? 75  ASP A OD2  1 
ATOM   621  N  N    . LYS A 1 76  ? -21.606 13.220  12.677  1.00 21.20 ? 76  LYS A N    1 
ATOM   622  C  CA   . LYS A 1 76  ? -22.417 12.298  11.854  1.00 20.10 ? 76  LYS A CA   1 
ATOM   623  C  C    . LYS A 1 76  ? -22.425 10.830  12.329  1.00 21.65 ? 76  LYS A C    1 
ATOM   624  O  O    . LYS A 1 76  ? -23.384 10.057  12.103  1.00 25.05 ? 76  LYS A O    1 
ATOM   625  C  CB   . LYS A 1 76  ? -21.827 12.238  10.470  1.00 20.00 ? 76  LYS A CB   1 
ATOM   626  C  CG   . LYS A 1 76  ? -22.084 13.435  9.608   1.00 22.93 ? 76  LYS A CG   1 
ATOM   627  C  CD   . LYS A 1 76  ? -21.305 13.233  8.323   1.00 21.89 ? 76  LYS A CD   1 
ATOM   628  C  CE   . LYS A 1 76  ? -21.895 14.177  7.259   1.00 23.15 ? 76  LYS A CE   1 
ATOM   629  N  NZ   . LYS A 1 76  ? -21.342 13.984  5.932   1.00 24.89 ? 76  LYS A NZ   1 
ATOM   630  N  N    . ALA A 1 77  ? -21.329 10.375  12.808  1.00 19.49 ? 77  ALA A N    1 
ATOM   631  C  CA   . ALA A 1 77  ? -21.233 8.974   13.333  1.00 17.69 ? 77  ALA A CA   1 
ATOM   632  C  C    . ALA A 1 77  ? -20.469 9.171   14.628  1.00 17.29 ? 77  ALA A C    1 
ATOM   633  O  O    . ALA A 1 77  ? -19.228 9.373   14.597  1.00 19.03 ? 77  ALA A O    1 
ATOM   634  C  CB   . ALA A 1 77  ? -20.490 8.126   12.332  1.00 19.06 ? 77  ALA A CB   1 
ATOM   635  N  N    . VAL A 1 78  ? -21.172 9.089   15.748  1.00 14.06 ? 78  VAL A N    1 
ATOM   636  C  CA   . VAL A 1 78  ? -20.573 9.388   17.038  1.00 15.67 ? 78  VAL A CA   1 
ATOM   637  C  C    . VAL A 1 78  ? -20.817 8.340   18.082  1.00 13.42 ? 78  VAL A C    1 
ATOM   638  O  O    . VAL A 1 78  ? -21.829 7.679   18.142  1.00 15.28 ? 78  VAL A O    1 
ATOM   639  C  CB   . VAL A 1 78  ? -20.955 10.760  17.630  1.00 18.29 ? 78  VAL A CB   1 
ATOM   640  C  CG1  . VAL A 1 78  ? -20.778 11.912  16.643  1.00 20.80 ? 78  VAL A CG1  1 
ATOM   641  C  CG2  . VAL A 1 78  ? -22.330 10.740  18.025  1.00 19.00 ? 78  VAL A CG2  1 
ATOM   642  N  N    . LEU A 1 79  ? -19.834 8.202   18.923  1.00 12.68 ? 79  LEU A N    1 
ATOM   643  C  CA   . LEU A 1 79  ? -19.871 7.360   20.056  1.00 13.12 ? 79  LEU A CA   1 
ATOM   644  C  C    . LEU A 1 79  ? -19.871 8.257   21.279  1.00 11.83 ? 79  LEU A C    1 
ATOM   645  O  O    . LEU A 1 79  ? -19.053 9.174   21.384  1.00 14.26 ? 79  LEU A O    1 
ATOM   646  C  CB   . LEU A 1 79  ? -18.618 6.465   20.004  1.00 13.47 ? 79  LEU A CB   1 
ATOM   647  C  CG   . LEU A 1 79  ? -18.471 5.419   21.044  1.00 13.85 ? 79  LEU A CG   1 
ATOM   648  C  CD1  . LEU A 1 79  ? -19.584 4.381   20.788  1.00 18.35 ? 79  LEU A CD1  1 
ATOM   649  C  CD2  . LEU A 1 79  ? -17.133 4.733   20.952  1.00 13.24 ? 79  LEU A CD2  1 
ATOM   650  N  N    . LYS A 1 80  ? -20.717 7.920   22.224  1.00 12.69 ? 80  LYS A N    1 
ATOM   651  C  CA   . LYS A 1 80  ? -20.816 8.624   23.537  1.00 14.79 ? 80  LYS A CA   1 
ATOM   652  C  C    . LYS A 1 80  ? -21.335 7.696   24.577  1.00 13.97 ? 80  LYS A C    1 
ATOM   653  O  O    . LYS A 1 80  ? -21.606 6.525   24.303  1.00 14.53 ? 80  LYS A O    1 
ATOM   654  C  CB   . LYS A 1 80  ? -21.737 9.813   23.547  1.00 20.22 ? 80  LYS A CB   1 
ATOM   655  C  CG   . LYS A 1 80  ? -21.263 10.814  22.703  1.00 26.84 ? 80  LYS A CG   1 
ATOM   656  C  CD   . LYS A 1 80  ? -22.196 10.811  21.633  1.00 28.67 ? 80  LYS A CD   1 
ATOM   657  C  CE   . LYS A 1 80  ? -23.386 11.656  22.035  1.00 29.17 ? 80  LYS A CE   1 
ATOM   658  N  NZ   . LYS A 1 80  ? -23.752 11.529  23.461  1.00 33.85 ? 80  LYS A NZ   1 
ATOM   659  N  N    . GLY A 1 81  ? -21.466 8.199   25.787  1.00 15.25 ? 81  GLY A N    1 
ATOM   660  C  CA   . GLY A 1 81  ? -21.908 7.362   26.859  1.00 14.68 ? 81  GLY A CA   1 
ATOM   661  C  C    . GLY A 1 81  ? -20.911 6.325   27.196  1.00 14.41 ? 81  GLY A C    1 
ATOM   662  O  O    . GLY A 1 81  ? -19.695 6.516   27.007  1.00 15.30 ? 81  GLY A O    1 
ATOM   663  N  N    . GLY A 1 82  ? -21.394 5.219   27.713  1.00 16.56 ? 82  GLY A N    1 
ATOM   664  C  CA   . GLY A 1 82  ? -20.426 4.223   28.098  1.00 16.95 ? 82  GLY A CA   1 
ATOM   665  C  C    . GLY A 1 82  ? -19.541 4.828   29.193  1.00 16.29 ? 82  GLY A C    1 
ATOM   666  O  O    . GLY A 1 82  ? -20.027 5.496   30.108  1.00 20.03 ? 82  GLY A O    1 
ATOM   667  N  N    . PRO A 1 83  ? -18.202 4.599   29.126  1.00 15.67 ? 83  PRO A N    1 
ATOM   668  C  CA   . PRO A 1 83  ? -17.286 5.216   30.077  1.00 14.23 ? 83  PRO A CA   1 
ATOM   669  C  C    . PRO A 1 83  ? -16.927 6.657   29.697  1.00 16.14 ? 83  PRO A C    1 
ATOM   670  O  O    . PRO A 1 83  ? -16.101 7.257   30.408  1.00 19.08 ? 83  PRO A O    1 
ATOM   671  C  CB   . PRO A 1 83  ? -16.018 4.324   29.921  1.00 16.48 ? 83  PRO A CB   1 
ATOM   672  C  CG   . PRO A 1 83  ? -16.054 3.933   28.458  1.00 13.66 ? 83  PRO A CG   1 
ATOM   673  C  CD   . PRO A 1 83  ? -17.514 3.734   28.134  1.00 14.07 ? 83  PRO A CD   1 
ATOM   674  N  N    . LEU A 1 84  ? -17.436 7.148   28.581  1.00 14.18 ? 84  LEU A N    1 
ATOM   675  C  CA   . LEU A 1 84  ? -16.840 8.326   27.935  1.00 14.38 ? 84  LEU A CA   1 
ATOM   676  C  C    . LEU A 1 84  ? -17.486 9.580   28.492  1.00 18.20 ? 84  LEU A C    1 
ATOM   677  O  O    . LEU A 1 84  ? -18.701 9.624   28.753  1.00 18.91 ? 84  LEU A O    1 
ATOM   678  C  CB   . LEU A 1 84  ? -17.094 8.307   26.449  1.00 12.40 ? 84  LEU A CB   1 
ATOM   679  C  CG   . LEU A 1 84  ? -16.503 7.036   25.792  1.00 11.70 ? 84  LEU A CG   1 
ATOM   680  C  CD1  . LEU A 1 84  ? -16.946 6.997   24.357  1.00 14.51 ? 84  LEU A CD1  1 
ATOM   681  C  CD2  . LEU A 1 84  ? -14.952 7.041   25.882  1.00 12.64 ? 84  LEU A CD2  1 
ATOM   682  N  N    . ASP A 1 85  ? -16.686 10.610  28.561  1.00 18.82 ? 85  ASP A N    1 
ATOM   683  C  CA   . ASP A 1 85  ? -17.237 11.980  28.769  1.00 22.33 ? 85  ASP A CA   1 
ATOM   684  C  C    . ASP A 1 85  ? -17.300 12.628  27.390  1.00 22.09 ? 85  ASP A C    1 
ATOM   685  O  O    . ASP A 1 85  ? -16.335 12.644  26.648  1.00 26.85 ? 85  ASP A O    1 
ATOM   686  C  CB   . ASP A 1 85  ? -16.344 12.737  29.781  1.00 24.63 ? 85  ASP A CB   1 
ATOM   687  C  CG   . ASP A 1 85  ? -16.453 12.196  31.207  1.00 31.53 ? 85  ASP A CG   1 
ATOM   688  O  OD1  . ASP A 1 85  ? -17.571 11.743  31.616  1.00 35.93 ? 85  ASP A OD1  1 
ATOM   689  O  OD2  . ASP A 1 85  ? -15.412 12.289  31.965  1.00 35.27 ? 85  ASP A OD2  1 
ATOM   690  N  N    . GLY A 1 86  ? -18.356 13.331  27.060  1.00 25.25 ? 86  GLY A N    1 
ATOM   691  C  CA   . GLY A 1 86  ? -18.340 13.988  25.759  1.00 23.82 ? 86  GLY A CA   1 
ATOM   692  C  C    . GLY A 1 86  ? -18.421 12.995  24.526  1.00 20.90 ? 86  GLY A C    1 
ATOM   693  O  O    . GLY A 1 86  ? -18.757 11.766  24.630  1.00 23.44 ? 86  GLY A O    1 
ATOM   694  N  N    . THR A 1 87  ? -18.064 13.496  23.341  1.00 17.63 ? 87  THR A N    1 
ATOM   695  C  CA   . THR A 1 87  ? -18.546 12.953  22.093  1.00 17.09 ? 87  THR A CA   1 
ATOM   696  C  C    . THR A 1 87  ? -17.362 12.638  21.262  1.00 13.56 ? 87  THR A C    1 
ATOM   697  O  O    . THR A 1 87  ? -16.389 13.417  21.164  1.00 13.68 ? 87  THR A O    1 
ATOM   698  C  CB   . THR A 1 87  ? -19.395 14.015  21.351  1.00 19.56 ? 87  THR A CB   1 
ATOM   699  O  OG1  . THR A 1 87  ? -20.606 14.262  22.084  1.00 24.87 ? 87  THR A OG1  1 
ATOM   700  C  CG2  . THR A 1 87  ? -19.758 13.577  19.852  1.00 21.85 ? 87  THR A CG2  1 
ATOM   701  N  N    . TYR A 1 88  ? -17.402 11.439  20.721  1.00 11.65 ? 88  TYR A N    1 
ATOM   702  C  CA   . TYR A 1 88  ? -16.314 10.967  19.903  1.00 11.80 ? 88  TYR A CA   1 
ATOM   703  C  C    . TYR A 1 88  ? -16.746 10.655  18.486  1.00 11.81 ? 88  TYR A C    1 
ATOM   704  O  O    . TYR A 1 88  ? -17.710 9.933   18.313  1.00 15.34 ? 88  TYR A O    1 
ATOM   705  C  CB   . TYR A 1 88  ? -15.634 9.746   20.481  1.00 11.36 ? 88  TYR A CB   1 
ATOM   706  C  CG   . TYR A 1 88  ? -14.864 9.962   21.779  1.00 10.11 ? 88  TYR A CG   1 
ATOM   707  C  CD1  . TYR A 1 88  ? -15.527 10.294  22.972  1.00 9.50  ? 88  TYR A CD1  1 
ATOM   708  C  CD2  . TYR A 1 88  ? -13.488 9.799   21.807  1.00 10.80 ? 88  TYR A CD2  1 
ATOM   709  C  CE1  . TYR A 1 88  ? -14.883 10.480  24.124  1.00 11.27 ? 88  TYR A CE1  1 
ATOM   710  C  CE2  . TYR A 1 88  ? -12.796 9.955   23.014  1.00 10.62 ? 88  TYR A CE2  1 
ATOM   711  C  CZ   . TYR A 1 88  ? -13.492 10.271  24.153  1.00 10.26 ? 88  TYR A CZ   1 
ATOM   712  O  OH   . TYR A 1 88  ? -12.796 10.383  25.326  1.00 11.08 ? 88  TYR A OH   1 
ATOM   713  N  N    . ARG A 1 89  ? -16.066 11.204  17.491  1.00 11.10 ? 89  ARG A N    1 
ATOM   714  C  CA   . ARG A 1 89  ? -16.479 11.059  16.085  1.00 11.94 ? 89  ARG A CA   1 
ATOM   715  C  C    . ARG A 1 89  ? -15.734 9.944   15.403  1.00 8.90  ? 89  ARG A C    1 
ATOM   716  O  O    . ARG A 1 89  ? -14.488 9.833   15.479  1.00 9.86  ? 89  ARG A O    1 
ATOM   717  C  CB   . ARG A 1 89  ? -16.073 12.324  15.369  1.00 14.47 ? 89  ARG A CB   1 
ATOM   718  C  CG   . ARG A 1 89  ? -16.977 13.376  15.396  1.00 21.10 ? 89  ARG A CG   1 
ATOM   719  C  CD   . ARG A 1 89  ? -16.761 14.265  14.205  1.00 19.33 ? 89  ARG A CD   1 
ATOM   720  N  NE   . ARG A 1 89  ? -17.403 15.392  14.699  1.00 19.52 ? 89  ARG A NE   1 
ATOM   721  C  CZ   . ARG A 1 89  ? -17.147 16.631  14.409  1.00 19.98 ? 89  ARG A CZ   1 
ATOM   722  N  NH1  . ARG A 1 89  ? -16.208 16.999  13.510  1.00 23.36 ? 89  ARG A NH1  1 
ATOM   723  N  NH2  . ARG A 1 89  ? -17.858 17.549  15.037  1.00 26.49 ? 89  ARG A NH2  1 
ATOM   724  N  N    . LEU A 1 90  ? -16.536 9.120   14.700  1.00 10.32 ? 90  LEU A N    1 
ATOM   725  C  CA   . LEU A 1 90  ? -15.926 8.026   13.915  1.00 10.10 ? 90  LEU A CA   1 
ATOM   726  C  C    . LEU A 1 90  ? -15.047 8.574   12.789  1.00 9.93  ? 90  LEU A C    1 
ATOM   727  O  O    . LEU A 1 90  ? -15.550 9.339   11.942  1.00 12.54 ? 90  LEU A O    1 
ATOM   728  C  CB   . LEU A 1 90  ? -17.018 7.136   13.345  1.00 10.72 ? 90  LEU A CB   1 
ATOM   729  C  CG   . LEU A 1 90  ? -16.556 5.988   12.454  1.00 9.90  ? 90  LEU A CG   1 
ATOM   730  C  CD1  . LEU A 1 90  ? -15.860 4.935   13.271  1.00 12.34 ? 90  LEU A CD1  1 
ATOM   731  C  CD2  . LEU A 1 90  ? -17.802 5.269   11.889  1.00 13.27 ? 90  LEU A CD2  1 
ATOM   732  N  N    . ILE A 1 91  ? -13.800 8.137   12.716  1.00 9.47  ? 91  ILE A N    1 
ATOM   733  C  CA   . ILE A 1 91  ? -12.928 8.513   11.612  1.00 10.19 ? 91  ILE A CA   1 
ATOM   734  C  C    . ILE A 1 91  ? -12.694 7.343   10.662  1.00 9.71  ? 91  ILE A C    1 
ATOM   735  O  O    . ILE A 1 91  ? -12.620 7.524   9.457   1.00 9.81  ? 91  ILE A O    1 
ATOM   736  C  CB   . ILE A 1 91  ? -11.624 9.175   12.072  1.00 10.06 ? 91  ILE A CB   1 
ATOM   737  C  CG1  . ILE A 1 91  ? -10.760 9.553   10.873  1.00 11.74 ? 91  ILE A CG1  1 
ATOM   738  C  CG2  . ILE A 1 91  ? -10.930 8.361   13.143  1.00 10.74 ? 91  ILE A CG2  1 
ATOM   739  C  CD1  . ILE A 1 91  ? -9.543  10.430  11.238  1.00 14.45 ? 91  ILE A CD1  1 
ATOM   740  N  N    . GLN A 1 92  ? -12.521 6.106   11.202  1.00 9.45  ? 92  GLN A N    1 
ATOM   741  C  CA   . GLN A 1 92  ? -12.238 4.967   10.291  1.00 9.04  ? 92  GLN A CA   1 
ATOM   742  C  C    . GLN A 1 92  ? -12.500 3.726   11.099  1.00 8.60  ? 92  GLN A C    1 
ATOM   743  O  O    . GLN A 1 92  ? -12.543 3.748   12.300  1.00 8.24  ? 92  GLN A O    1 
ATOM   744  C  CB   . GLN A 1 92  ? -10.801 4.981   9.825   1.00 10.46 ? 92  GLN A CB   1 
ATOM   745  C  CG   . GLN A 1 92  ? -9.749  5.057   10.926  1.00 11.08 ? 92  GLN A CG   1 
ATOM   746  C  CD   . GLN A 1 92  ? -8.952  3.783   11.134  1.00 10.70 ? 92  GLN A CD   1 
ATOM   747  O  OE1  . GLN A 1 92  ? -9.549  2.725   11.163  1.00 11.73 ? 92  GLN A OE1  1 
ATOM   748  N  NE2  . GLN A 1 92  ? -7.663  3.880   11.431  1.00 17.20 ? 92  GLN A NE2  1 
ATOM   749  N  N    . PHE A 1 93  ? -12.687 2.616   10.369  1.00 9.14  ? 93  PHE A N    1 
ATOM   750  C  CA   . PHE A 1 93  ? -12.551 1.311   10.971  1.00 8.67  ? 93  PHE A CA   1 
ATOM   751  C  C    . PHE A 1 93  ? -11.581 0.476   10.169  1.00 7.72  ? 93  PHE A C    1 
ATOM   752  O  O    . PHE A 1 93  ? -11.360 0.679   8.991   1.00 9.62  ? 93  PHE A O    1 
ATOM   753  C  CB   . PHE A 1 93  ? -13.911 0.616   11.216  1.00 8.51  ? 93  PHE A CB   1 
ATOM   754  C  CG   . PHE A 1 93  ? -14.626 0.161   9.991   1.00 9.81  ? 93  PHE A CG   1 
ATOM   755  C  CD1  . PHE A 1 93  ? -14.242 -0.985  9.292   1.00 9.75  ? 93  PHE A CD1  1 
ATOM   756  C  CD2  . PHE A 1 93  ? -15.743 0.885   9.567   1.00 10.31 ? 93  PHE A CD2  1 
ATOM   757  C  CE1  . PHE A 1 93  ? -14.898 -1.455  8.192   1.00 11.32 ? 93  PHE A CE1  1 
ATOM   758  C  CE2  . PHE A 1 93  ? -16.435 0.386   8.470   1.00 11.79 ? 93  PHE A CE2  1 
ATOM   759  C  CZ   . PHE A 1 93  ? -16.009 -0.766  7.769   1.00 11.30 ? 93  PHE A CZ   1 
ATOM   760  N  N    . HIS A 1 94  ? -11.057 -0.546  10.849  1.00 8.15  ? 94  HIS A N    1 
ATOM   761  C  CA   . HIS A 1 94  ? -10.186 -1.531  10.218  1.00 7.80  ? 94  HIS A CA   1 
ATOM   762  C  C    . HIS A 1 94  ? -10.236 -2.780  11.043  1.00 7.78  ? 94  HIS A C    1 
ATOM   763  O  O    . HIS A 1 94  ? -10.877 -2.810  12.083  1.00 7.78  ? 94  HIS A O    1 
ATOM   764  C  CB   . HIS A 1 94  ? -8.737  -0.993  10.196  1.00 9.54  ? 94  HIS A CB   1 
ATOM   765  C  CG   . HIS A 1 94  ? -8.203  -0.719  11.560  1.00 7.97  ? 94  HIS A CG   1 
ATOM   766  N  ND1  . HIS A 1 94  ? -8.384  0.477   12.214  1.00 7.98  ? 94  HIS A ND1  1 
ATOM   767  C  CD2  . HIS A 1 94  ? -7.588  -1.538  12.441  1.00 7.82  ? 94  HIS A CD2  1 
ATOM   768  C  CE1  . HIS A 1 94  ? -7.902  0.367   13.444  1.00 7.40  ? 94  HIS A CE1  1 
ATOM   769  N  NE2  . HIS A 1 94  ? -7.322  -0.844  13.602  1.00 8.70  ? 94  HIS A NE2  1 
ATOM   770  N  N    . PHE A 1 95  ? -9.521  -3.826  10.561  1.00 8.20  ? 95  PHE A N    1 
ATOM   771  C  CA   . PHE A 1 95  ? -9.515  -5.082  11.246  1.00 7.96  ? 95  PHE A CA   1 
ATOM   772  C  C    . PHE A 1 95  ? -8.086  -5.537  11.433  1.00 8.59  ? 95  PHE A C    1 
ATOM   773  O  O    . PHE A 1 95  ? -7.149  -5.062  10.760  1.00 8.65  ? 95  PHE A O    1 
ATOM   774  C  CB   . PHE A 1 95  ? -10.223 -6.164  10.410  1.00 8.72  ? 95  PHE A CB   1 
ATOM   775  C  CG   . PHE A 1 95  ? -11.651 -5.844  10.117  1.00 7.45  ? 95  PHE A CG   1 
ATOM   776  C  CD1  . PHE A 1 95  ? -12.010 -5.023  9.031   1.00 9.17  ? 95  PHE A CD1  1 
ATOM   777  C  CD2  . PHE A 1 95  ? -12.696 -6.529  10.743  1.00 9.79  ? 95  PHE A CD2  1 
ATOM   778  C  CE1  . PHE A 1 95  ? -13.352 -4.781  8.682   1.00 9.28  ? 95  PHE A CE1  1 
ATOM   779  C  CE2  . PHE A 1 95  ? -14.023 -6.290  10.428  1.00 9.89  ? 95  PHE A CE2  1 
ATOM   780  C  CZ   . PHE A 1 95  ? -14.352 -5.454  9.389   1.00 10.11 ? 95  PHE A CZ   1 
ATOM   781  N  N    . HIS A 1 96  ? -7.935  -6.477  12.361  1.00 8.35  ? 96  HIS A N    1 
ATOM   782  C  CA   . HIS A 1 96  ? -6.726  -7.294  12.478  1.00 8.03  ? 96  HIS A CA   1 
ATOM   783  C  C    . HIS A 1 96  ? -7.158  -8.743  12.386  1.00 7.32  ? 96  HIS A C    1 
ATOM   784  O  O    . HIS A 1 96  ? -8.219  -9.090  12.866  1.00 8.37  ? 96  HIS A O    1 
ATOM   785  C  CB   . HIS A 1 96  ? -6.041  -7.052  13.859  1.00 7.78  ? 96  HIS A CB   1 
ATOM   786  C  CG   . HIS A 1 96  ? -5.766  -5.619  14.166  1.00 7.84  ? 96  HIS A CG   1 
ATOM   787  N  ND1  . HIS A 1 96  ? -4.551  -5.039  13.936  1.00 8.14  ? 96  HIS A ND1  1 
ATOM   788  C  CD2  . HIS A 1 96  ? -6.625  -4.611  14.511  1.00 8.27  ? 96  HIS A CD2  1 
ATOM   789  C  CE1  . HIS A 1 96  ? -4.630  -3.752  14.293  1.00 8.15  ? 96  HIS A CE1  1 
ATOM   790  N  NE2  . HIS A 1 96  ? -5.867  -3.450  14.577  1.00 7.40  ? 96  HIS A NE2  1 
ATOM   791  N  N    . TRP A 1 97  ? -6.341  -9.600  11.727  1.00 8.46  ? 97  TRP A N    1 
ATOM   792  C  CA   . TRP A 1 97  ? -6.779  -10.971 11.502  1.00 8.46  ? 97  TRP A CA   1 
ATOM   793  C  C    . TRP A 1 97  ? -5.573  -11.863 11.367  1.00 7.92  ? 97  TRP A C    1 
ATOM   794  O  O    . TRP A 1 97  ? -4.415  -11.414 11.263  1.00 9.46  ? 97  TRP A O    1 
ATOM   795  C  CB   . TRP A 1 97  ? -7.656  -11.072 10.251  1.00 9.54  ? 97  TRP A CB   1 
ATOM   796  C  CG   . TRP A 1 97  ? -7.000  -10.637 8.968   1.00 8.79  ? 97  TRP A CG   1 
ATOM   797  C  CD1  . TRP A 1 97  ? -6.296  -11.446 8.129   1.00 10.04 ? 97  TRP A CD1  1 
ATOM   798  C  CD2  . TRP A 1 97  ? -6.944  -9.321  8.406   1.00 8.98  ? 97  TRP A CD2  1 
ATOM   799  N  NE1  . TRP A 1 97  ? -5.856  -10.751 7.023   1.00 11.48 ? 97  TRP A NE1  1 
ATOM   800  C  CE2  . TRP A 1 97  ? -6.198  -9.420  7.198   1.00 11.47 ? 97  TRP A CE2  1 
ATOM   801  C  CE3  . TRP A 1 97  ? -7.435  -8.042  8.804   1.00 9.06  ? 97  TRP A CE3  1 
ATOM   802  C  CZ2  . TRP A 1 97  ? -5.995  -8.313  6.369   1.00 11.29 ? 97  TRP A CZ2  1 
ATOM   803  C  CZ3  . TRP A 1 97  ? -7.200  -6.968  7.998   1.00 10.92 ? 97  TRP A CZ3  1 
ATOM   804  C  CH2  . TRP A 1 97  ? -6.510  -7.092  6.810   1.00 12.01 ? 97  TRP A CH2  1 
ATOM   805  N  N    . GLY A 1 98  ? -5.851  -13.166 11.370  1.00 9.10  ? 98  GLY A N    1 
ATOM   806  C  CA   . GLY A 1 98  ? -4.796  -14.114 11.388  1.00 8.88  ? 98  GLY A CA   1 
ATOM   807  C  C    . GLY A 1 98  ? -4.574  -14.837 10.081  1.00 9.58  ? 98  GLY A C    1 
ATOM   808  O  O    . GLY A 1 98  ? -5.308  -14.695 9.122   1.00 11.28 ? 98  GLY A O    1 
ATOM   809  N  N    . SER A 1 99  ? -3.554  -15.682 10.088  1.00 10.91 ? 99  SER A N    1 
ATOM   810  C  CA   . SER A 1 99  ? -3.330  -16.584 8.959   1.00 11.79 ? 99  SER A CA   1 
ATOM   811  C  C    . SER A 1 99  ? -4.156  -17.845 9.080   1.00 12.10 ? 99  SER A C    1 
ATOM   812  O  O    . SER A 1 99  ? -4.266  -18.583 8.094   1.00 15.25 ? 99  SER A O    1 
ATOM   813  C  CB   . SER A 1 99  ? -1.844  -16.927 8.896   1.00 12.90 ? 99  SER A CB   1 
ATOM   814  O  OG   . SER A 1 99  ? -1.438  -17.481 10.152  1.00 13.35 ? 99  SER A OG   1 
ATOM   815  N  N    . LEU A 1 100 ? -4.757  -18.060 10.248  1.00 12.31 ? 100 LEU A N    1 
ATOM   816  C  CA   . LEU A 1 100 ? -5.582  -19.231 10.609  1.00 13.69 ? 100 LEU A CA   1 
ATOM   817  C  C    . LEU A 1 100 ? -6.736  -18.788 11.449  1.00 12.95 ? 100 LEU A C    1 
ATOM   818  O  O    . LEU A 1 100 ? -6.560  -17.783 12.161  1.00 12.39 ? 100 LEU A O    1 
ATOM   819  C  CB   . LEU A 1 100 ? -4.781  -20.208 11.562  1.00 18.76 ? 100 LEU A CB   1 
ATOM   820  C  CG   . LEU A 1 100 ? -3.496  -20.626 10.947  1.00 20.81 ? 100 LEU A CG   1 
ATOM   821  C  CD1  . LEU A 1 100 ? -2.438  -20.996 11.978  1.00 27.99 ? 100 LEU A CD1  1 
ATOM   822  C  CD2  . LEU A 1 100 ? -3.808  -21.842 10.060  1.00 27.61 ? 100 LEU A CD2  1 
ATOM   823  N  N    . ASP A 1 101 ? -7.835  -19.558 11.482  1.00 13.10 ? 101 ASP A N    1 
ATOM   824  C  CA   . ASP A 1 101 ? -8.997  -19.085 12.245  1.00 13.21 ? 101 ASP A CA   1 
ATOM   825  C  C    . ASP A 1 101 ? -8.707  -18.998 13.739  1.00 13.32 ? 101 ASP A C    1 
ATOM   826  O  O    . ASP A 1 101 ? -9.385  -18.293 14.444  1.00 14.84 ? 101 ASP A O    1 
ATOM   827  C  CB   . ASP A 1 101 ? -10.179 -20.012 11.992  1.00 13.38 ? 101 ASP A CB   1 
ATOM   828  C  CG   . ASP A 1 101 ? -10.699 -19.973 10.590  1.00 15.86 ? 101 ASP A CG   1 
ATOM   829  O  OD1  . ASP A 1 101 ? -10.319 -19.134 9.751   1.00 15.80 ? 101 ASP A OD1  1 
ATOM   830  O  OD2  . ASP A 1 101 ? -11.535 -20.829 10.316  1.00 20.23 ? 101 ASP A OD2  1 
ATOM   831  N  N    . GLY A 1 102 ? -7.708  -19.777 14.210  1.00 13.37 ? 102 GLY A N    1 
ATOM   832  C  CA   . GLY A 1 102 ? -7.422  -19.779 15.633  1.00 13.74 ? 102 GLY A CA   1 
ATOM   833  C  C    . GLY A 1 102 ? -6.661  -18.594 16.201  1.00 11.40 ? 102 GLY A C    1 
ATOM   834  O  O    . GLY A 1 102 ? -6.310  -18.609 17.357  1.00 12.73 ? 102 GLY A O    1 
ATOM   835  N  N    . GLN A 1 103 ? -6.390  -17.565 15.407  1.00 11.13 ? 103 GLN A N    1 
ATOM   836  C  CA   . GLN A 1 103 ? -5.654  -16.408 15.875  1.00 9.57  ? 103 GLN A CA   1 
ATOM   837  C  C    . GLN A 1 103 ? -6.045  -15.244 15.014  1.00 8.87  ? 103 GLN A C    1 
ATOM   838  O  O    . GLN A 1 103 ? -6.574  -15.430 13.923  1.00 10.07 ? 103 GLN A O    1 
ATOM   839  C  CB   . GLN A 1 103 ? -4.138  -16.618 15.874  1.00 11.44 ? 103 GLN A CB   1 
ATOM   840  C  CG   . GLN A 1 103 ? -3.547  -16.837 14.466  1.00 12.40 ? 103 GLN A CG   1 
ATOM   841  C  CD   . GLN A 1 103 ? -2.163  -17.368 14.527  1.00 14.16 ? 103 GLN A CD   1 
ATOM   842  O  OE1  . GLN A 1 103 ? -1.935  -18.290 15.334  1.00 22.72 ? 103 GLN A OE1  1 
ATOM   843  N  NE2  . GLN A 1 103 ? -1.253  -16.908 13.740  1.00 15.34 ? 103 GLN A NE2  1 
ATOM   844  N  N    . GLY A 1 104 ? -5.711  -14.015 15.489  1.00 9.24  ? 104 GLY A N    1 
ATOM   845  C  CA   . GLY A 1 104 ? -6.016  -12.820 14.656  1.00 8.48  ? 104 GLY A CA   1 
ATOM   846  C  C    . GLY A 1 104 ? -6.482  -11.693 15.507  1.00 8.43  ? 104 GLY A C    1 
ATOM   847  O  O    . GLY A 1 104 ? -6.176  -10.549 15.160  1.00 9.20  ? 104 GLY A O    1 
ATOM   848  N  N    . SER A 1 105 ? -7.155  -11.922 16.640  1.00 8.00  ? 105 SER A N    1 
ATOM   849  C  CA   . SER A 1 105 ? -7.566  -10.810 17.479  1.00 8.04  ? 105 SER A CA   1 
ATOM   850  C  C    . SER A 1 105 ? -6.369  -10.258 18.229  1.00 7.77  ? 105 SER A C    1 
ATOM   851  O  O    . SER A 1 105 ? -5.341  -10.941 18.421  1.00 8.82  ? 105 SER A O    1 
ATOM   852  C  CB   . SER A 1 105 ? -8.689  -11.171 18.396  1.00 7.57  ? 105 SER A CB   1 
ATOM   853  O  OG   . SER A 1 105 ? -8.316  -12.131 19.363  1.00 8.38  ? 105 SER A OG   1 
ATOM   854  N  N    . GLU A 1 106 ? -6.493  -9.006  18.622  1.00 7.43  ? 106 GLU A N    1 
ATOM   855  C  CA   . GLU A 1 106 ? -5.463  -8.317  19.444  1.00 7.71  ? 106 GLU A CA   1 
ATOM   856  C  C    . GLU A 1 106 ? -5.808  -8.487  20.905  1.00 7.23  ? 106 GLU A C    1 
ATOM   857  O  O    . GLU A 1 106 ? -5.053  -9.078  21.702  1.00 8.33  ? 106 GLU A O    1 
ATOM   858  C  CB   . GLU A 1 106 ? -5.396  -6.851  18.995  1.00 8.04  ? 106 GLU A CB   1 
ATOM   859  C  CG   . GLU A 1 106 ? -4.960  -6.746  17.583  1.00 8.93  ? 106 GLU A CG   1 
ATOM   860  C  CD   . GLU A 1 106 ? -4.301  -5.441  17.302  1.00 8.45  ? 106 GLU A CD   1 
ATOM   861  O  OE1  . GLU A 1 106 ? -4.949  -4.376  17.538  1.00 7.90  ? 106 GLU A OE1  1 
ATOM   862  O  OE2  . GLU A 1 106 ? -3.155  -5.465  16.810  1.00 9.03  ? 106 GLU A OE2  1 
ATOM   863  N  N    . HIS A 1 107 ? -7.015  -8.040  21.307  1.00 7.45  ? 107 HIS A N    1 
ATOM   864  C  CA   . HIS A 1 107 ? -7.501  -8.435  22.628  1.00 7.19  ? 107 HIS A CA   1 
ATOM   865  C  C    . HIS A 1 107 ? -7.809  -9.927  22.658  1.00 7.09  ? 107 HIS A C    1 
ATOM   866  O  O    . HIS A 1 107 ? -8.114  -10.531 21.614  1.00 7.85  ? 107 HIS A O    1 
ATOM   867  C  CB   . HIS A 1 107 ? -8.731  -7.642  23.034  1.00 7.84  ? 107 HIS A CB   1 
ATOM   868  C  CG   . HIS A 1 107 ? -8.386  -6.196  23.186  1.00 6.96  ? 107 HIS A CG   1 
ATOM   869  N  ND1  . HIS A 1 107 ? -8.456  -5.292  22.137  1.00 7.31  ? 107 HIS A ND1  1 
ATOM   870  C  CD2  . HIS A 1 107 ? -7.958  -5.486  24.260  1.00 7.80  ? 107 HIS A CD2  1 
ATOM   871  C  CE1  . HIS A 1 107 ? -8.016  -4.101  22.555  1.00 7.44  ? 107 HIS A CE1  1 
ATOM   872  N  NE2  . HIS A 1 107 ? -7.721  -4.180  23.841  1.00 8.49  ? 107 HIS A NE2  1 
ATOM   873  N  N    . THR A 1 108 ? -7.648  -10.497 23.847  1.00 7.99  ? 108 THR A N    1 
ATOM   874  C  CA   . THR A 1 108 ? -8.035  -11.897 24.086  1.00 8.12  ? 108 THR A CA   1 
ATOM   875  C  C    . THR A 1 108 ? -9.016  -11.899 25.258  1.00 8.58  ? 108 THR A C    1 
ATOM   876  O  O    . THR A 1 108 ? -9.032  -10.936 26.059  1.00 9.05  ? 108 THR A O    1 
ATOM   877  C  CB   . THR A 1 108 ? -6.818  -12.794 24.274  1.00 8.71  ? 108 THR A CB   1 
ATOM   878  O  OG1  . THR A 1 108 ? -6.010  -12.284 25.323  1.00 9.23  ? 108 THR A OG1  1 
ATOM   879  C  CG2  . THR A 1 108 ? -5.992  -12.879 22.977  1.00 10.05 ? 108 THR A CG2  1 
ATOM   880  N  N    . VAL A 1 109 ? -9.778  -12.987 25.408  1.00 8.57  ? 109 VAL A N    1 
ATOM   881  C  CA   . VAL A 1 109 ? -10.734 -13.038 26.507  1.00 9.67  ? 109 VAL A CA   1 
ATOM   882  C  C    . VAL A 1 109 ? -10.388 -14.341 27.238  1.00 10.95 ? 109 VAL A C    1 
ATOM   883  O  O    . VAL A 1 109 ? -10.543 -15.435 26.667  1.00 11.14 ? 109 VAL A O    1 
ATOM   884  C  CB   . VAL A 1 109 ? -12.157 -13.070 25.925  1.00 11.11 ? 109 VAL A CB   1 
ATOM   885  C  CG1  . VAL A 1 109 ? -13.238 -13.200 27.047  1.00 12.56 ? 109 VAL A CG1  1 
ATOM   886  C  CG2  . VAL A 1 109 ? -12.479 -11.798 25.132  1.00 11.54 ? 109 VAL A CG2  1 
ATOM   887  N  N    . ASP A 1 110 ? -9.934  -14.233 28.463  1.00 10.43 ? 110 ASP A N    1 
ATOM   888  C  CA   . ASP A 1 110 ? -9.451  -15.432 29.169  1.00 11.04 ? 110 ASP A CA   1 
ATOM   889  C  C    . ASP A 1 110 ? -8.514  -16.238 28.284  1.00 11.63 ? 110 ASP A C    1 
ATOM   890  O  O    . ASP A 1 110 ? -8.584  -17.484 28.232  1.00 13.07 ? 110 ASP A O    1 
ATOM   891  C  CB   . ASP A 1 110 ? -10.631 -16.286 29.667  1.00 13.62 ? 110 ASP A CB   1 
ATOM   892  C  CG   . ASP A 1 110 ? -11.502 -15.491 30.650  1.00 12.96 ? 110 ASP A CG   1 
ATOM   893  O  OD1  . ASP A 1 110 ? -10.969 -14.638 31.331  1.00 15.55 ? 110 ASP A OD1  1 
ATOM   894  O  OD2  . ASP A 1 110 ? -12.694 -15.792 30.749  1.00 17.44 ? 110 ASP A OD2  1 
ATOM   895  N  N    . LYS A 1 111 ? -7.617  -15.500 27.588  1.00 10.78 ? 111 LYS A N    1 
ATOM   896  C  CA   . LYS A 1 111 ? -6.585  -16.050 26.712  1.00 11.36 ? 111 LYS A CA   1 
ATOM   897  C  C    . LYS A 1 111 ? -7.103  -16.565 25.384  1.00 11.67 ? 111 LYS A C    1 
ATOM   898  O  O    . LYS A 1 111 ? -6.300  -16.897 24.519  1.00 13.45 ? 111 LYS A O    1 
ATOM   899  C  CB   . LYS A 1 111 ? -5.702  -17.124 27.404  1.00 13.64 ? 111 LYS A CB   1 
ATOM   900  C  CG   . LYS A 1 111 ? -5.096  -16.564 28.703  1.00 17.37 ? 111 LYS A CG   1 
ATOM   901  C  CD   . LYS A 1 111 ? -4.044  -15.563 28.432  1.00 20.46 ? 111 LYS A CD   1 
ATOM   902  C  CE   . LYS A 1 111 ? -3.353  -15.006 29.665  1.00 27.92 ? 111 LYS A CE   1 
ATOM   903  N  NZ   . LYS A 1 111 ? -2.003  -15.445 29.639  1.00 29.32 ? 111 LYS A NZ   1 
ATOM   904  N  N    . LYS A 1 112 ? -8.421  -16.538 25.163  1.00 10.72 ? 112 LYS A N    1 
ATOM   905  C  CA   . LYS A 1 112 ? -8.948  -16.939 23.905  1.00 10.56 ? 112 LYS A CA   1 
ATOM   906  C  C    . LYS A 1 112 ? -8.622  -15.870 22.842  1.00 10.20 ? 112 LYS A C    1 
ATOM   907  O  O    . LYS A 1 112 ? -8.970  -14.688 23.059  1.00 10.53 ? 112 LYS A O    1 
ATOM   908  C  CB   . LYS A 1 112 ? -10.527 -17.077 24.015  1.00 13.74 ? 112 LYS A CB   1 
ATOM   909  C  CG   . LYS A 1 112 ? -11.183 -17.386 22.699  1.00 14.38 ? 112 LYS A CG   1 
ATOM   910  C  CD   . LYS A 1 112 ? -12.728 -17.340 22.802  1.00 19.42 ? 112 LYS A CD   1 
ATOM   911  C  CE   . LYS A 1 112 ? -13.303 -17.586 21.446  1.00 20.39 ? 112 LYS A CE   1 
ATOM   912  N  NZ   . LYS A 1 112 ? -13.115 -18.880 20.930  1.00 22.77 ? 112 LYS A NZ   1 
ATOM   913  N  N    . LYS A 1 113 ? -8.104  -16.352 21.711  1.00 10.41 ? 113 LYS A N    1 
ATOM   914  C  CA   . LYS A 1 113 ? -7.965  -15.568 20.477  1.00 10.30 ? 113 LYS A CA   1 
ATOM   915  C  C    . LYS A 1 113 ? -9.081  -15.795 19.521  1.00 9.74  ? 113 LYS A C    1 
ATOM   916  O  O    . LYS A 1 113 ? -9.477  -16.934 19.261  1.00 12.43 ? 113 LYS A O    1 
ATOM   917  C  CB   . LYS A 1 113 ? -6.669  -15.916 19.796  1.00 10.42 ? 113 LYS A CB   1 
ATOM   918  C  CG   . LYS A 1 113 ? -5.406  -15.572 20.647  1.00 11.35 ? 113 LYS A CG   1 
ATOM   919  C  CD   . LYS A 1 113 ? -4.196  -16.192 19.954  1.00 12.74 ? 113 LYS A CD   1 
ATOM   920  C  CE   . LYS A 1 113 ? -2.944  -15.621 20.513  1.00 16.00 ? 113 LYS A CE   1 
ATOM   921  N  NZ   . LYS A 1 113 ? -2.379  -16.376 21.589  1.00 25.53 ? 113 LYS A NZ   1 
ATOM   922  N  N    . TYR A 1 114 ? -9.674  -14.698 19.024  1.00 8.99  ? 114 TYR A N    1 
ATOM   923  C  CA   . TYR A 1 114 ? -10.644 -14.748 17.974  1.00 8.49  ? 114 TYR A CA   1 
ATOM   924  C  C    . TYR A 1 114 ? -9.979  -14.713 16.604  1.00 8.61  ? 114 TYR A C    1 
ATOM   925  O  O    . TYR A 1 114 ? -8.775  -14.414 16.491  1.00 9.10  ? 114 TYR A O    1 
ATOM   926  C  CB   . TYR A 1 114 ? -11.710 -13.678 18.091  1.00 8.99  ? 114 TYR A CB   1 
ATOM   927  C  CG   . TYR A 1 114 ? -12.626 -13.906 19.244  1.00 9.03  ? 114 TYR A CG   1 
ATOM   928  C  CD1  . TYR A 1 114 ? -12.341 -13.470 20.530  1.00 10.07 ? 114 TYR A CD1  1 
ATOM   929  C  CD2  . TYR A 1 114 ? -13.832 -14.528 19.048  1.00 10.69 ? 114 TYR A CD2  1 
ATOM   930  C  CE1  . TYR A 1 114 ? -13.180 -13.678 21.587  1.00 12.60 ? 114 TYR A CE1  1 
ATOM   931  C  CE2  . TYR A 1 114 ? -14.752 -14.695 20.090  1.00 11.30 ? 114 TYR A CE2  1 
ATOM   932  C  CZ   . TYR A 1 114 ? -14.416 -14.250 21.353  1.00 13.69 ? 114 TYR A CZ   1 
ATOM   933  O  OH   . TYR A 1 114 ? -15.294 -14.393 22.439  1.00 18.85 ? 114 TYR A OH   1 
ATOM   934  N  N    . ALA A 1 115 ? -10.722 -15.022 15.557  1.00 8.19  ? 115 ALA A N    1 
ATOM   935  C  CA   . ALA A 1 115 ? -10.189 -14.995 14.223  1.00 8.13  ? 115 ALA A CA   1 
ATOM   936  C  C    . ALA A 1 115 ? -9.795  -13.632 13.752  1.00 8.15  ? 115 ALA A C    1 
ATOM   937  O  O    . ALA A 1 115 ? -8.934  -13.456 12.876  1.00 9.56  ? 115 ALA A O    1 
ATOM   938  C  CB   . ALA A 1 115 ? -11.207 -15.634 13.265  1.00 11.42 ? 115 ALA A CB   1 
ATOM   939  N  N    . ALA A 1 116 ? -10.447 -12.613 14.290  1.00 8.34  ? 116 ALA A N    1 
ATOM   940  C  CA   . ALA A 1 116 ? -10.153 -11.233 13.838  1.00 8.50  ? 116 ALA A CA   1 
ATOM   941  C  C    . ALA A 1 116 ? -10.763 -10.280 14.851  1.00 7.93  ? 116 ALA A C    1 
ATOM   942  O  O    . ALA A 1 116 ? -11.491 -10.715 15.734  1.00 8.37  ? 116 ALA A O    1 
ATOM   943  C  CB   . ALA A 1 116 ? -10.705 -10.975 12.444  1.00 8.44  ? 116 ALA A CB   1 
ATOM   944  N  N    . GLU A 1 117 ? -10.423 -9.003  14.728  1.00 7.56  ? 117 GLU A N    1 
ATOM   945  C  CA   . GLU A 1 117 ? -11.000 -8.008  15.615  1.00 7.57  ? 117 GLU A CA   1 
ATOM   946  C  C    . GLU A 1 117 ? -11.177 -6.766  14.737  1.00 7.54  ? 117 GLU A C    1 
ATOM   947  O  O    . GLU A 1 117 ? -10.250 -6.336  14.040  1.00 8.75  ? 117 GLU A O    1 
ATOM   948  C  CB   . GLU A 1 117 ? -10.037 -7.750  16.735  1.00 7.12  ? 117 GLU A CB   1 
ATOM   949  C  CG   . GLU A 1 117 ? -10.522 -6.860  17.800  1.00 7.96  ? 117 GLU A CG   1 
ATOM   950  C  CD   . GLU A 1 117 ? -9.612  -6.774  18.994  1.00 7.14  ? 117 GLU A CD   1 
ATOM   951  O  OE1  . GLU A 1 117 ? -8.918  -7.761  19.298  1.00 8.79  ? 117 GLU A OE1  1 
ATOM   952  O  OE2  . GLU A 1 117 ? -9.572  -5.715  19.687  1.00 7.90  ? 117 GLU A OE2  1 
ATOM   953  N  N    . LEU A 1 118 ? -12.333 -6.171  14.877  1.00 7.43  ? 118 LEU A N    1 
ATOM   954  C  CA   . LEU A 1 118 ? -12.723 -4.921  14.226  1.00 6.93  ? 118 LEU A CA   1 
ATOM   955  C  C    . LEU A 1 118 ? -12.504 -3.790  15.234  1.00 6.85  ? 118 LEU A C    1 
ATOM   956  O  O    . LEU A 1 118 ? -12.891 -3.857  16.367  1.00 7.21  ? 118 LEU A O    1 
ATOM   957  C  CB   . LEU A 1 118 ? -14.214 -5.013  13.891  1.00 7.68  ? 118 LEU A CB   1 
ATOM   958  C  CG   . LEU A 1 118 ? -14.954 -3.730  13.567  1.00 8.57  ? 118 LEU A CG   1 
ATOM   959  C  CD1  . LEU A 1 118 ? -14.386 -3.068  12.353  1.00 10.22 ? 118 LEU A CD1  1 
ATOM   960  C  CD2  . LEU A 1 118 ? -16.416 -4.088  13.312  1.00 10.99 ? 118 LEU A CD2  1 
ATOM   961  N  N    . HIS A 1 119 ? -11.872 -2.717  14.725  1.00 7.27  ? 119 HIS A N    1 
ATOM   962  C  CA   . HIS A 1 119 ? -11.661 -1.481  15.522  1.00 6.79  ? 119 HIS A CA   1 
ATOM   963  C  C    . HIS A 1 119 ? -12.321 -0.340  14.830  1.00 6.74  ? 119 HIS A C    1 
ATOM   964  O  O    . HIS A 1 119 ? -11.962 0.037   13.694  1.00 8.01  ? 119 HIS A O    1 
ATOM   965  C  CB   . HIS A 1 119 ? -10.177 -1.219  15.586  1.00 7.91  ? 119 HIS A CB   1 
ATOM   966  C  CG   . HIS A 1 119 ? -9.490  -2.199  16.476  1.00 7.54  ? 119 HIS A CG   1 
ATOM   967  N  ND1  . HIS A 1 119 ? -8.112  -2.451  16.440  1.00 6.89  ? 119 HIS A ND1  1 
ATOM   968  C  CD2  . HIS A 1 119 ? -10.001 -3.019  17.418  1.00 7.53  ? 119 HIS A CD2  1 
ATOM   969  C  CE1  . HIS A 1 119 ? -7.811  -3.341  17.383  1.00 7.10  ? 119 HIS A CE1  1 
ATOM   970  N  NE2  . HIS A 1 119 ? -8.951  -3.748  17.950  1.00 8.81  ? 119 HIS A NE2  1 
ATOM   971  N  N    . LEU A 1 120 ? -13.328 0.237   15.500  1.00 7.34  ? 120 LEU A N    1 
ATOM   972  C  CA   . LEU A 1 120 ? -13.971 1.479   15.064  1.00 7.75  ? 120 LEU A CA   1 
ATOM   973  C  C    . LEU A 1 120 ? -13.352 2.610   15.834  1.00 7.42  ? 120 LEU A C    1 
ATOM   974  O  O    . LEU A 1 120 ? -13.512 2.684   17.048  1.00 7.04  ? 120 LEU A O    1 
ATOM   975  C  CB   . LEU A 1 120 ? -15.486 1.360   15.280  1.00 8.00  ? 120 LEU A CB   1 
ATOM   976  C  CG   . LEU A 1 120 ? -16.189 0.282   14.397  1.00 8.99  ? 120 LEU A CG   1 
ATOM   977  C  CD1  . LEU A 1 120 ? -17.025 -0.621  15.229  1.00 13.08 ? 120 LEU A CD1  1 
ATOM   978  C  CD2  . LEU A 1 120 ? -17.057 1.012   13.367  1.00 11.89 ? 120 LEU A CD2  1 
ATOM   979  N  N    . VAL A 1 121 ? -12.584 3.444   15.105  1.00 8.08  ? 121 VAL A N    1 
ATOM   980  C  CA   . VAL A 1 121 ? -11.757 4.455   15.784  1.00 8.15  ? 121 VAL A CA   1 
ATOM   981  C  C    . VAL A 1 121 ? -12.480 5.791   15.809  1.00 7.89  ? 121 VAL A C    1 
ATOM   982  O  O    . VAL A 1 121 ? -12.924 6.274   14.735  1.00 8.82  ? 121 VAL A O    1 
ATOM   983  C  CB   . VAL A 1 121 ? -10.422 4.591   14.996  1.00 8.41  ? 121 VAL A CB   1 
ATOM   984  C  CG1  . VAL A 1 121 ? -9.551  5.678   15.621  1.00 9.71  ? 121 VAL A CG1  1 
ATOM   985  C  CG2  . VAL A 1 121 ? -9.708  3.252   14.876  1.00 9.02  ? 121 VAL A CG2  1 
ATOM   986  N  N    . HIS A 1 122 ? -12.539 6.411   17.016  1.00 7.05  ? 122 HIS A N    1 
ATOM   987  C  CA   . HIS A 1 122 ? -13.270 7.675   17.160  1.00 7.76  ? 122 HIS A CA   1 
ATOM   988  C  C    . HIS A 1 122 ? -12.393 8.667   17.893  1.00 7.89  ? 122 HIS A C    1 
ATOM   989  O  O    . HIS A 1 122 ? -11.654 8.240   18.799  1.00 9.41  ? 122 HIS A O    1 
ATOM   990  C  CB   . HIS A 1 122 ? -14.550 7.504   18.009  1.00 8.66  ? 122 HIS A CB   1 
ATOM   991  C  CG   . HIS A 1 122 ? -15.414 6.388   17.563  1.00 8.43  ? 122 HIS A CG   1 
ATOM   992  N  ND1  . HIS A 1 122 ? -15.089 5.071   17.835  1.00 8.59  ? 122 HIS A ND1  1 
ATOM   993  C  CD2  . HIS A 1 122 ? -16.636 6.362   16.970  1.00 9.27  ? 122 HIS A CD2  1 
ATOM   994  C  CE1  . HIS A 1 122 ? -16.096 4.313   17.379  1.00 8.48  ? 122 HIS A CE1  1 
ATOM   995  N  NE2  . HIS A 1 122 ? -17.055 5.055   16.876  1.00 9.11  ? 122 HIS A NE2  1 
ATOM   996  N  N    . TRP A 1 123 ? -12.489 9.948   17.540  1.00 8.66  ? 123 TRP A N    1 
ATOM   997  C  CA   . TRP A 1 123 ? -11.692 10.920  18.259  1.00 8.45  ? 123 TRP A CA   1 
ATOM   998  C  C    . TRP A 1 123 ? -12.579 11.896  18.996  1.00 8.43  ? 123 TRP A C    1 
ATOM   999  O  O    . TRP A 1 123 ? -13.685 12.260  18.575  1.00 10.06 ? 123 TRP A O    1 
ATOM   1000 C  CB   . TRP A 1 123 ? -10.718 11.669  17.368  1.00 10.28 ? 123 TRP A CB   1 
ATOM   1001 C  CG   . TRP A 1 123 ? -11.339 12.287  16.154  1.00 10.33 ? 123 TRP A CG   1 
ATOM   1002 C  CD1  . TRP A 1 123 ? -11.540 11.684  14.924  1.00 11.09 ? 123 TRP A CD1  1 
ATOM   1003 C  CD2  . TRP A 1 123 ? -11.829 13.639  16.005  1.00 10.82 ? 123 TRP A CD2  1 
ATOM   1004 N  NE1  . TRP A 1 123 ? -12.143 12.551  14.044  1.00 12.38 ? 123 TRP A NE1  1 
ATOM   1005 C  CE2  . TRP A 1 123 ? -12.326 13.766  14.678  1.00 11.53 ? 123 TRP A CE2  1 
ATOM   1006 C  CE3  . TRP A 1 123 ? -11.899 14.739  16.867  1.00 11.51 ? 123 TRP A CE3  1 
ATOM   1007 C  CZ2  . TRP A 1 123 ? -12.850 14.931  14.192  1.00 13.44 ? 123 TRP A CZ2  1 
ATOM   1008 C  CZ3  . TRP A 1 123 ? -12.428 15.910  16.354  1.00 13.29 ? 123 TRP A CZ3  1 
ATOM   1009 C  CH2  . TRP A 1 123 ? -12.861 15.996  15.045  1.00 13.84 ? 123 TRP A CH2  1 
ATOM   1010 N  N    . ASN A 1 124 ? -12.035 12.389  20.105  1.00 8.09  ? 124 ASN A N    1 
ATOM   1011 C  CA   . ASN A 1 124 ? -12.785 13.225  21.011  1.00 10.28 ? 124 ASN A CA   1 
ATOM   1012 C  C    . ASN A 1 124 ? -12.954 14.597  20.384  1.00 10.66 ? 124 ASN A C    1 
ATOM   1013 O  O    . ASN A 1 124 ? -11.968 15.339  20.147  1.00 10.62 ? 124 ASN A O    1 
ATOM   1014 C  CB   . ASN A 1 124 ? -11.999 13.342  22.296  1.00 9.90  ? 124 ASN A CB   1 
ATOM   1015 C  CG   . ASN A 1 124 ? -12.795 13.974  23.423  1.00 10.65 ? 124 ASN A CG   1 
ATOM   1016 O  OD1  . ASN A 1 124 ? -13.597 14.880  23.185  1.00 12.78 ? 124 ASN A OD1  1 
ATOM   1017 N  ND2  . ASN A 1 124 ? -12.566 13.487  24.662  1.00 12.58 ? 124 ASN A ND2  1 
ATOM   1018 N  N    . THR A 1 125 ? -14.203 15.071  20.220  1.00 11.91 ? 125 THR A N    1 
ATOM   1019 C  CA   . THR A 1 125 ? -14.406 16.322  19.463  1.00 12.05 ? 125 THR A CA   1 
ATOM   1020 C  C    . THR A 1 125 ? -13.815 17.545  20.195  1.00 13.16 ? 125 THR A C    1 
ATOM   1021 O  O    . THR A 1 125 ? -13.620 18.587  19.588  1.00 15.14 ? 125 THR A O    1 
ATOM   1022 C  CB   . THR A 1 125 ? -15.891 16.545  19.143  1.00 14.73 ? 125 THR A CB   1 
ATOM   1023 O  OG1  . THR A 1 125 ? -16.596 16.593  20.386  1.00 17.43 ? 125 THR A OG1  1 
ATOM   1024 C  CG2  . THR A 1 125 ? -16.462 15.436  18.229  1.00 16.47 ? 125 THR A CG2  1 
ATOM   1025 N  N    . LYS A 1 126 ? -13.527 17.410  21.557  1.00 12.26 ? 127 LYS A N    1 
ATOM   1026 C  CA   . LYS A 1 126 ? -13.005 18.545  22.246  1.00 14.82 ? 127 LYS A CA   1 
ATOM   1027 C  C    . LYS A 1 126 ? -11.624 18.887  21.718  1.00 13.30 ? 127 LYS A C    1 
ATOM   1028 O  O    . LYS A 1 126 ? -11.100 20.002  21.973  1.00 16.55 ? 127 LYS A O    1 
ATOM   1029 C  CB   . LYS A 1 126 ? -13.068 18.310  23.744  1.00 16.40 ? 127 LYS A CB   1 
ATOM   1030 C  CG   . LYS A 1 126 ? -12.035 17.574  24.346  1.00 16.96 ? 127 LYS A CG   1 
ATOM   1031 C  CD   . LYS A 1 126 ? -12.515 17.244  25.793  1.00 22.62 ? 127 LYS A CD   1 
ATOM   1032 C  CE   . LYS A 1 126 ? -11.511 16.431  26.457  1.00 25.74 ? 127 LYS A CE   1 
ATOM   1033 N  NZ   . LYS A 1 126 ? -11.008 16.764  27.866  1.00 30.87 ? 127 LYS A NZ   1 
ATOM   1034 N  N    . TYR A 1 127 ? -10.977 17.964  21.024  1.00 12.09 ? 128 TYR A N    1 
ATOM   1035 C  CA   . TYR A 1 127 ? -9.618  18.252  20.493  1.00 12.38 ? 128 TYR A CA   1 
ATOM   1036 C  C    . TYR A 1 127 ? -9.588  18.632  19.028  1.00 12.53 ? 128 TYR A C    1 
ATOM   1037 O  O    . TYR A 1 127 ? -8.475  18.868  18.458  1.00 13.35 ? 128 TYR A O    1 
ATOM   1038 C  CB   . TYR A 1 127 ? -8.653  17.087  20.752  1.00 12.49 ? 128 TYR A CB   1 
ATOM   1039 C  CG   . TYR A 1 127 ? -8.575  16.791  22.195  1.00 11.06 ? 128 TYR A CG   1 
ATOM   1040 C  CD1  . TYR A 1 127 ? -8.166  17.766  23.096  1.00 12.81 ? 128 TYR A CD1  1 
ATOM   1041 C  CD2  . TYR A 1 127 ? -8.911  15.544  22.699  1.00 11.36 ? 128 TYR A CD2  1 
ATOM   1042 C  CE1  . TYR A 1 127 ? -8.126  17.522  24.428  1.00 13.63 ? 128 TYR A CE1  1 
ATOM   1043 C  CE2  . TYR A 1 127 ? -8.804  15.242  24.056  1.00 11.30 ? 128 TYR A CE2  1 
ATOM   1044 C  CZ   . TYR A 1 127 ? -8.374  16.267  24.930  1.00 12.15 ? 128 TYR A CZ   1 
ATOM   1045 O  OH   . TYR A 1 127 ? -8.346  16.063  26.236  1.00 15.21 ? 128 TYR A OH   1 
ATOM   1046 N  N    . GLY A 1 128 ? -10.761 18.759  18.396  1.00 11.92 ? 129 GLY A N    1 
ATOM   1047 C  CA   . GLY A 1 128 ? -10.784 19.428  17.095  1.00 12.66 ? 129 GLY A CA   1 
ATOM   1048 C  C    . GLY A 1 128 ? -10.464 18.551  15.891  1.00 11.78 ? 129 GLY A C    1 
ATOM   1049 O  O    . GLY A 1 128 ? -11.062 18.688  14.808  1.00 14.89 ? 129 GLY A O    1 
ATOM   1050 N  N    . ASP A 1 129 ? -9.436  17.705  16.008  1.00 12.51 ? 130 ASP A N    1 
ATOM   1051 C  CA   . ASP A 1 129 ? -9.178  16.747  14.949  1.00 14.07 ? 130 ASP A CA   1 
ATOM   1052 C  C    . ASP A 1 129 ? -8.426  15.531  15.494  1.00 13.46 ? 130 ASP A C    1 
ATOM   1053 O  O    . ASP A 1 129 ? -7.959  15.532  16.662  1.00 13.91 ? 130 ASP A O    1 
ATOM   1054 C  CB   . ASP A 1 129 ? -8.536  17.373  13.696  1.00 15.35 ? 130 ASP A CB   1 
ATOM   1055 C  CG   . ASP A 1 129 ? -7.100  17.834  13.936  1.00 14.75 ? 130 ASP A CG   1 
ATOM   1056 O  OD1  . ASP A 1 129 ? -6.410  17.418  14.859  1.00 22.12 ? 130 ASP A OD1  1 
ATOM   1057 O  OD2  . ASP A 1 129 ? -6.580  18.593  13.155  1.00 21.48 ? 130 ASP A OD2  1 
ATOM   1058 N  N    . PHE A 1 130 ? -8.301  14.516  14.650  1.00 13.22 ? 131 PHE A N    1 
ATOM   1059 C  CA   . PHE A 1 130 ? -7.643  13.266  15.056  1.00 12.69 ? 131 PHE A CA   1 
ATOM   1060 C  C    . PHE A 1 130 ? -6.187  13.504  15.446  1.00 11.38 ? 131 PHE A C    1 
ATOM   1061 O  O    . PHE A 1 130 ? -5.746  12.952  16.426  1.00 11.11 ? 131 PHE A O    1 
ATOM   1062 C  CB   . PHE A 1 130 ? -7.746  12.270  13.894  1.00 12.47 ? 131 PHE A CB   1 
ATOM   1063 C  CG   . PHE A 1 130 ? -7.050  10.989  14.136  1.00 11.94 ? 131 PHE A CG   1 
ATOM   1064 C  CD1  . PHE A 1 130 ? -7.646  9.954   14.846  1.00 11.74 ? 131 PHE A CD1  1 
ATOM   1065 C  CD2  . PHE A 1 130 ? -5.706  10.850  13.746  1.00 13.89 ? 131 PHE A CD2  1 
ATOM   1066 C  CE1  . PHE A 1 130 ? -6.973  8.789   15.014  1.00 12.64 ? 131 PHE A CE1  1 
ATOM   1067 C  CE2  . PHE A 1 130 ? -5.049  9.656   13.888  1.00 15.64 ? 131 PHE A CE2  1 
ATOM   1068 C  CZ   . PHE A 1 130 ? -5.722  8.617   14.553  1.00 15.59 ? 131 PHE A CZ   1 
ATOM   1069 N  N    . GLY A 1 131 ? -5.465  14.284  14.635  1.00 12.58 ? 132 GLY A N    1 
ATOM   1070 C  CA   . GLY A 1 131 ? -4.060  14.465  14.932  1.00 13.35 ? 132 GLY A CA   1 
ATOM   1071 C  C    . GLY A 1 131 ? -3.787  15.101  16.272  1.00 12.21 ? 132 GLY A C    1 
ATOM   1072 O  O    . GLY A 1 131 ? -2.770  14.789  16.942  1.00 15.26 ? 132 GLY A O    1 
ATOM   1073 N  N    A LYS A 1 132 ? -4.605  16.073  16.699  0.50 12.02 ? 133 LYS A N    1 
ATOM   1074 N  N    B LYS A 1 132 ? -4.665  16.033  16.652  0.50 12.65 ? 133 LYS A N    1 
ATOM   1075 C  CA   A LYS A 1 132 ? -4.410  16.593  18.061  0.50 11.12 ? 133 LYS A CA   1 
ATOM   1076 C  CA   B LYS A 1 132 ? -4.576  16.681  17.942  0.50 12.37 ? 133 LYS A CA   1 
ATOM   1077 C  C    A LYS A 1 132 ? -4.921  15.601  19.087  0.50 10.69 ? 133 LYS A C    1 
ATOM   1078 C  C    B LYS A 1 132 ? -5.028  15.754  19.081  0.50 12.07 ? 133 LYS A C    1 
ATOM   1079 O  O    A LYS A 1 132 ? -4.332  15.438  20.168  0.50 10.86 ? 133 LYS A O    1 
ATOM   1080 O  O    B LYS A 1 132 ? -4.470  15.753  20.200  0.50 12.32 ? 133 LYS A O    1 
ATOM   1081 C  CB   A LYS A 1 132 ? -5.079  17.955  18.273  0.50 10.39 ? 133 LYS A CB   1 
ATOM   1082 C  CB   B LYS A 1 132 ? -5.384  17.969  17.902  0.50 12.83 ? 133 LYS A CB   1 
ATOM   1083 C  CG   A LYS A 1 132 ? -4.531  19.036  17.333  0.50 10.46 ? 133 LYS A CG   1 
ATOM   1084 C  CG   B LYS A 1 132 ? -4.650  19.140  18.514  0.01 11.48 ? 133 LYS A CG   1 
ATOM   1085 C  CD   A LYS A 1 132 ? -3.176  19.528  17.812  0.01 9.12  ? 133 LYS A CD   1 
ATOM   1086 C  CD   B LYS A 1 132 ? -3.258  19.291  17.930  0.01 10.21 ? 133 LYS A CD   1 
ATOM   1087 C  CE   A LYS A 1 132 ? -3.318  20.403  19.048  0.01 8.79  ? 133 LYS A CE   1 
ATOM   1088 C  CE   B LYS A 1 132 ? -2.470  20.352  18.673  0.01 9.99  ? 133 LYS A CE   1 
ATOM   1089 N  NZ   A LYS A 1 132 ? -2.008  20.928  19.522  0.01 8.53  ? 133 LYS A NZ   1 
ATOM   1090 N  NZ   B LYS A 1 132 ? -1.127  20.559  18.070  0.01 9.09  ? 133 LYS A NZ   1 
ATOM   1091 N  N    . ALA A 1 133 ? -6.067  14.951  18.801  1.00 10.88 ? 134 ALA A N    1 
ATOM   1092 C  CA   . ALA A 1 133 ? -6.589  13.999  19.771  1.00 10.95 ? 134 ALA A CA   1 
ATOM   1093 C  C    . ALA A 1 133 ? -5.586  12.934  20.179  1.00 10.31 ? 134 ALA A C    1 
ATOM   1094 O  O    . ALA A 1 133 ? -5.585  12.585  21.368  1.00 10.09 ? 134 ALA A O    1 
ATOM   1095 C  CB   . ALA A 1 133 ? -7.859  13.315  19.186  1.00 10.74 ? 134 ALA A CB   1 
ATOM   1096 N  N    . VAL A 1 134 ? -4.767  12.421  19.258  1.00 10.62 ? 135 VAL A N    1 
ATOM   1097 C  CA   . VAL A 1 134 ? -3.917  11.317  19.644  1.00 11.38 ? 135 VAL A CA   1 
ATOM   1098 C  C    . VAL A 1 134 ? -2.804  11.754  20.602  1.00 10.44 ? 135 VAL A C    1 
ATOM   1099 O  O    . VAL A 1 134 ? -2.112  10.891  21.167  1.00 12.00 ? 135 VAL A O    1 
ATOM   1100 C  CB   . VAL A 1 134 ? -3.267  10.611  18.426  1.00 12.29 ? 135 VAL A CB   1 
ATOM   1101 C  CG1  . VAL A 1 134 ? -4.351  9.965   17.600  1.00 12.92 ? 135 VAL A CG1  1 
ATOM   1102 C  CG2  . VAL A 1 134 ? -2.383  11.500  17.613  1.00 12.49 ? 135 VAL A CG2  1 
ATOM   1103 N  N    A GLN A 1 135 ? -2.626  13.074  20.779  0.50 11.26 ? 136 GLN A N    1 
ATOM   1104 N  N    B GLN A 1 135 ? -2.676  13.080  20.769  0.50 11.16 ? 136 GLN A N    1 
ATOM   1105 C  CA   A GLN A 1 135 ? -1.661  13.537  21.786  0.50 12.27 ? 136 GLN A CA   1 
ATOM   1106 C  CA   B GLN A 1 135 ? -1.727  13.639  21.728  0.50 12.33 ? 136 GLN A CA   1 
ATOM   1107 C  C    A GLN A 1 135 ? -2.282  13.782  23.147  0.50 12.17 ? 136 GLN A C    1 
ATOM   1108 C  C    B GLN A 1 135 ? -2.239  13.682  23.168  0.50 12.10 ? 136 GLN A C    1 
ATOM   1109 O  O    A GLN A 1 135 ? -1.706  14.498  23.979  0.50 12.67 ? 136 GLN A O    1 
ATOM   1110 O  O    B GLN A 1 135 ? -1.516  14.111  24.092  0.50 13.59 ? 136 GLN A O    1 
ATOM   1111 C  CB   A GLN A 1 135 ? -0.981  14.833  21.300  0.50 12.83 ? 136 GLN A CB   1 
ATOM   1112 C  CB   B GLN A 1 135 ? -1.304  15.046  21.220  0.50 12.66 ? 136 GLN A CB   1 
ATOM   1113 C  CG   A GLN A 1 135 ? -0.294  14.703  19.948  0.50 14.47 ? 136 GLN A CG   1 
ATOM   1114 C  CG   B GLN A 1 135 ? -0.712  14.953  19.822  0.50 14.97 ? 136 GLN A CG   1 
ATOM   1115 C  CD   A GLN A 1 135 ? 0.921   13.834  19.993  0.50 20.47 ? 136 GLN A CD   1 
ATOM   1116 C  CD   B GLN A 1 135 ? -0.115  16.262  19.331  0.50 17.77 ? 136 GLN A CD   1 
ATOM   1117 O  OE1  A GLN A 1 135 ? 1.623   13.781  21.002  0.50 24.18 ? 136 GLN A OE1  1 
ATOM   1118 O  OE1  B GLN A 1 135 ? 0.744   16.871  19.986  0.50 21.19 ? 136 GLN A OE1  1 
ATOM   1119 N  NE2  A GLN A 1 135 ? 1.193   13.149  18.888  0.50 20.56 ? 136 GLN A NE2  1 
ATOM   1120 N  NE2  B GLN A 1 135 ? -0.547  16.669  18.164  0.50 17.75 ? 136 GLN A NE2  1 
ATOM   1121 N  N    . GLN A 1 136 ? -3.501  13.288  23.365  1.00 11.66 ? 137 GLN A N    1 
ATOM   1122 C  CA   . GLN A 1 136 ? -4.180  13.504  24.623  1.00 11.43 ? 137 GLN A CA   1 
ATOM   1123 C  C    . GLN A 1 136 ? -4.524  12.154  25.254  1.00 10.48 ? 137 GLN A C    1 
ATOM   1124 O  O    . GLN A 1 136 ? -4.910  11.231  24.509  1.00 10.80 ? 137 GLN A O    1 
ATOM   1125 C  CB   . GLN A 1 136 ? -5.406  14.332  24.451  1.00 11.82 ? 137 GLN A CB   1 
ATOM   1126 C  CG   . GLN A 1 136 ? -5.219  15.634  23.606  1.00 16.20 ? 137 GLN A CG   1 
ATOM   1127 C  CD   . GLN A 1 136 ? -4.250  16.539  24.261  1.00 19.81 ? 137 GLN A CD   1 
ATOM   1128 O  OE1  . GLN A 1 136 ? -4.077  16.472  25.467  1.00 19.27 ? 137 GLN A OE1  1 
ATOM   1129 N  NE2  . GLN A 1 136 ? -3.469  17.278  23.452  1.00 27.41 ? 137 GLN A NE2  1 
ATOM   1130 N  N    . PRO A 1 137 ? -4.558  12.109  26.584  1.00 11.45 ? 138 PRO A N    1 
ATOM   1131 C  CA   . PRO A 1 137 ? -4.792  10.812  27.223  1.00 13.32 ? 138 PRO A CA   1 
ATOM   1132 C  C    . PRO A 1 137 ? -6.257  10.289  27.047  1.00 12.91 ? 138 PRO A C    1 
ATOM   1133 O  O    . PRO A 1 137 ? -6.509  9.062   27.160  1.00 14.57 ? 138 PRO A O    1 
ATOM   1134 C  CB   . PRO A 1 137 ? -4.376  11.025  28.685  1.00 15.43 ? 138 PRO A CB   1 
ATOM   1135 C  CG   . PRO A 1 137 ? -4.347  12.434  28.860  1.00 17.67 ? 138 PRO A CG   1 
ATOM   1136 C  CD   . PRO A 1 137 ? -4.122  13.129  27.543  1.00 12.77 ? 138 PRO A CD   1 
ATOM   1137 N  N    . ASP A 1 138 ? -7.165  11.202  26.703  1.00 11.34 ? 139 ASP A N    1 
ATOM   1138 C  CA   . ASP A 1 138 ? -8.555  10.803  26.455  1.00 10.91 ? 139 ASP A CA   1 
ATOM   1139 C  C    . ASP A 1 138 ? -8.917  11.179  25.018  1.00 9.81  ? 139 ASP A C    1 
ATOM   1140 O  O    . ASP A 1 138 ? -10.020 11.660  24.745  1.00 11.05 ? 139 ASP A O    1 
ATOM   1141 C  CB   . ASP A 1 138 ? -9.538  11.451  27.441  1.00 12.60 ? 139 ASP A CB   1 
ATOM   1142 C  CG   . ASP A 1 138 ? -9.414  12.927  27.463  1.00 14.61 ? 139 ASP A CG   1 
ATOM   1143 O  OD1  . ASP A 1 138 ? -8.485  13.534  26.833  1.00 15.42 ? 139 ASP A OD1  1 
ATOM   1144 O  OD2  . ASP A 1 138 ? -10.249 13.578  28.145  1.00 18.39 ? 139 ASP A OD2  1 
ATOM   1145 N  N    . GLY A 1 139 ? -7.953  11.119  24.078  1.00 8.80  ? 140 GLY A N    1 
ATOM   1146 C  CA   . GLY A 1 139 ? -8.172  11.581  22.738  1.00 8.45  ? 140 GLY A CA   1 
ATOM   1147 C  C    . GLY A 1 139 ? -9.034  10.668  21.866  1.00 9.01  ? 140 GLY A C    1 
ATOM   1148 O  O    . GLY A 1 139 ? -9.743  11.200  21.020  1.00 9.37  ? 140 GLY A O    1 
ATOM   1149 N  N    . LEU A 1 140 ? -8.897  9.335   22.044  1.00 7.69  ? 141 LEU A N    1 
ATOM   1150 C  CA   . LEU A 1 140 ? -9.606  8.433   21.153  1.00 7.89  ? 141 LEU A CA   1 
ATOM   1151 C  C    . LEU A 1 140 ? -10.474 7.494   21.980  1.00 8.10  ? 141 LEU A C    1 
ATOM   1152 O  O    . LEU A 1 140 ? -10.183 7.237   23.142  1.00 8.44  ? 141 LEU A O    1 
ATOM   1153 C  CB   . LEU A 1 140 ? -8.606  7.544   20.406  1.00 8.76  ? 141 LEU A CB   1 
ATOM   1154 C  CG   . LEU A 1 140 ? -7.694  8.292   19.433  1.00 8.46  ? 141 LEU A CG   1 
ATOM   1155 C  CD1  . LEU A 1 140 ? -6.909  7.238   18.621  1.00 9.68  ? 141 LEU A CD1  1 
ATOM   1156 C  CD2  . LEU A 1 140 ? -8.321  9.316   18.509  1.00 10.83 ? 141 LEU A CD2  1 
ATOM   1157 N  N    . ALA A 1 141 ? -11.490 6.990   21.304  1.00 8.11  ? 142 ALA A N    1 
ATOM   1158 C  CA   . ALA A 1 141 ? -12.259 5.840   21.883  1.00 7.73  ? 142 ALA A CA   1 
ATOM   1159 C  C    . ALA A 1 141 ? -12.374 4.832   20.758  1.00 7.53  ? 142 ALA A C    1 
ATOM   1160 O  O    . ALA A 1 141 ? -12.716 5.217   19.643  1.00 8.85  ? 142 ALA A O    1 
ATOM   1161 C  CB   . ALA A 1 141 ? -13.627 6.298   22.328  1.00 8.96  ? 142 ALA A CB   1 
ATOM   1162 N  N    . VAL A 1 142 ? -11.870 3.605   21.030  1.00 8.05  ? 143 VAL A N    1 
ATOM   1163 C  CA   . VAL A 1 142 ? -11.920 2.606   20.014  1.00 8.03  ? 143 VAL A CA   1 
ATOM   1164 C  C    . VAL A 1 142 ? -12.926 1.555   20.472  1.00 7.37  ? 143 VAL A C    1 
ATOM   1165 O  O    . VAL A 1 142 ? -12.811 1.036   21.575  1.00 7.56  ? 143 VAL A O    1 
ATOM   1166 C  CB   . VAL A 1 142 ? -10.552 1.975   19.658  1.00 7.89  ? 143 VAL A CB   1 
ATOM   1167 C  CG1  . VAL A 1 142 ? -10.745 0.945   18.520  1.00 10.11 ? 143 VAL A CG1  1 
ATOM   1168 C  CG2  . VAL A 1 142 ? -9.598  3.082   19.225  1.00 10.50 ? 143 VAL A CG2  1 
ATOM   1169 N  N    . LEU A 1 143 ? -13.907 1.297   19.624  1.00 7.37  ? 144 LEU A N    1 
ATOM   1170 C  CA   . LEU A 1 143 ? -14.844 0.195   19.879  1.00 8.12  ? 144 LEU A CA   1 
ATOM   1171 C  C    . LEU A 1 143 ? -14.288 -1.025  19.196  1.00 7.77  ? 144 LEU A C    1 
ATOM   1172 O  O    . LEU A 1 143 ? -14.143 -1.054  17.974  1.00 8.62  ? 144 LEU A O    1 
ATOM   1173 C  CB   . LEU A 1 143 ? -16.241 0.629   19.285  1.00 9.61  ? 144 LEU A CB   1 
ATOM   1174 C  CG   . LEU A 1 143 ? -17.357 -0.340  19.429  1.00 10.19 ? 144 LEU A CG   1 
ATOM   1175 C  CD1  . LEU A 1 143 ? -17.608 -0.627  20.912  1.00 12.07 ? 144 LEU A CD1  1 
ATOM   1176 C  CD2  . LEU A 1 143 ? -18.631 0.271   18.788  1.00 13.03 ? 144 LEU A CD2  1 
ATOM   1177 N  N    . GLY A 1 144 ? -13.991 -2.042  20.019  1.00 7.35  ? 145 GLY A N    1 
ATOM   1178 C  CA   . GLY A 1 144 ? -13.409 -3.283  19.506  1.00 7.39  ? 145 GLY A CA   1 
ATOM   1179 C  C    . GLY A 1 144 ? -14.437 -4.362  19.505  1.00 7.07  ? 145 GLY A C    1 
ATOM   1180 O  O    . GLY A 1 144 ? -15.204 -4.524  20.462  1.00 8.33  ? 145 GLY A O    1 
ATOM   1181 N  N    . ILE A 1 145 ? -14.494 -5.103  18.374  1.00 7.53  ? 146 ILE A N    1 
ATOM   1182 C  CA   . ILE A 1 145 ? -15.549 -6.164  18.231  1.00 7.63  ? 146 ILE A CA   1 
ATOM   1183 C  C    . ILE A 1 145 ? -14.802 -7.366  17.721  1.00 7.55  ? 146 ILE A C    1 
ATOM   1184 O  O    . ILE A 1 145 ? -14.134 -7.341  16.705  1.00 8.30  ? 146 ILE A O    1 
ATOM   1185 C  CB   . ILE A 1 145 ? -16.639 -5.674  17.236  1.00 8.19  ? 146 ILE A CB   1 
ATOM   1186 C  CG1  . ILE A 1 145 ? -17.249 -4.380  17.763  1.00 10.29 ? 146 ILE A CG1  1 
ATOM   1187 C  CG2  . ILE A 1 145 ? -17.668 -6.771  17.049  1.00 10.15 ? 146 ILE A CG2  1 
ATOM   1188 C  CD1  . ILE A 1 145 ? -18.345 -3.786  16.859  1.00 10.41 ? 146 ILE A CD1  1 
ATOM   1189 N  N    . PHE A 1 146 ? -15.012 -8.491  18.387  1.00 7.35  ? 147 PHE A N    1 
ATOM   1190 C  CA   . PHE A 1 146 ? -14.380 -9.769  17.963  1.00 7.82  ? 147 PHE A CA   1 
ATOM   1191 C  C    . PHE A 1 146 ? -15.148 -10.385 16.802  1.00 7.56  ? 147 PHE A C    1 
ATOM   1192 O  O    . PHE A 1 146 ? -16.358 -10.251 16.736  1.00 8.79  ? 147 PHE A O    1 
ATOM   1193 C  CB   . PHE A 1 146 ? -14.341 -10.727 19.145  1.00 8.10  ? 147 PHE A CB   1 
ATOM   1194 C  CG   . PHE A 1 146 ? -13.504 -10.245 20.278  1.00 6.92  ? 147 PHE A CG   1 
ATOM   1195 C  CD1  . PHE A 1 146 ? -12.125 -10.108 20.102  1.00 8.29  ? 147 PHE A CD1  1 
ATOM   1196 C  CD2  . PHE A 1 146 ? -14.034 -10.011 21.516  1.00 8.21  ? 147 PHE A CD2  1 
ATOM   1197 C  CE1  . PHE A 1 146 ? -11.326 -9.685  21.150  1.00 8.52  ? 147 PHE A CE1  1 
ATOM   1198 C  CE2  . PHE A 1 146 ? -13.270 -9.602  22.567  1.00 8.54  ? 147 PHE A CE2  1 
ATOM   1199 C  CZ   . PHE A 1 146 ? -11.876 -9.468  22.384  1.00 7.32  ? 147 PHE A CZ   1 
ATOM   1200 N  N    . LEU A 1 147 ? -14.398 -11.057 15.948  1.00 8.03  ? 148 LEU A N    1 
ATOM   1201 C  CA   . LEU A 1 147 ? -14.963 -11.821 14.853  1.00 8.00  ? 148 LEU A CA   1 
ATOM   1202 C  C    . LEU A 1 147 ? -14.612 -13.299 15.074  1.00 7.47  ? 148 LEU A C    1 
ATOM   1203 O  O    . LEU A 1 147 ? -13.456 -13.660 15.259  1.00 8.79  ? 148 LEU A O    1 
ATOM   1204 C  CB   . LEU A 1 147 ? -14.379 -11.445 13.491  1.00 7.92  ? 148 LEU A CB   1 
ATOM   1205 C  CG   . LEU A 1 147 ? -14.963 -10.178 12.864  1.00 9.00  ? 148 LEU A CG   1 
ATOM   1206 C  CD1  . LEU A 1 147 ? -14.701 -8.924  13.729  1.00 11.41 ? 148 LEU A CD1  1 
ATOM   1207 C  CD2  . LEU A 1 147 ? -14.360 -9.972  11.461  1.00 10.90 ? 148 LEU A CD2  1 
ATOM   1208 N  N    . LYS A 1 148 ? -15.644 -14.137 15.064  1.00 9.66  ? 149 LYS A N    1 
ATOM   1209 C  CA   . LYS A 1 148 ? -15.460 -15.567 14.992  1.00 10.69 ? 149 LYS A CA   1 
ATOM   1210 C  C    . LYS A 1 148 ? -15.951 -16.074 13.634  1.00 10.62 ? 149 LYS A C    1 
ATOM   1211 O  O    . LYS A 1 148 ? -16.788 -15.484 13.003  1.00 11.47 ? 149 LYS A O    1 
ATOM   1212 C  CB   . LYS A 1 148 ? -16.206 -16.296 16.127  1.00 11.82 ? 149 LYS A CB   1 
ATOM   1213 C  CG   . LYS A 1 148 ? -17.720 -16.180 16.084  1.00 13.75 ? 149 LYS A CG   1 
ATOM   1214 C  CD   . LYS A 1 148 ? -18.353 -16.955 17.256  1.00 20.70 ? 149 LYS A CD   1 
ATOM   1215 C  CE   . LYS A 1 148 ? -19.842 -16.796 17.266  1.00 26.53 ? 149 LYS A CE   1 
ATOM   1216 N  NZ   . LYS A 1 148 ? -20.424 -17.723 18.280  1.00 32.69 ? 149 LYS A NZ   1 
ATOM   1217 N  N    . VAL A 1 149 ? -15.417 -17.192 13.231  1.00 11.40 ? 150 VAL A N    1 
ATOM   1218 C  CA   . VAL A 1 149 ? -15.823 -17.821 11.968  1.00 12.27 ? 150 VAL A CA   1 
ATOM   1219 C  C    . VAL A 1 149 ? -17.050 -18.725 12.168  1.00 13.74 ? 150 VAL A C    1 
ATOM   1220 O  O    . VAL A 1 149 ? -17.042 -19.626 13.005  1.00 14.82 ? 150 VAL A O    1 
ATOM   1221 C  CB   . VAL A 1 149 ? -14.656 -18.536 11.318  1.00 12.02 ? 150 VAL A CB   1 
ATOM   1222 C  CG1  . VAL A 1 149 ? -15.049 -19.289 10.058  1.00 14.14 ? 150 VAL A CG1  1 
ATOM   1223 C  CG2  . VAL A 1 149 ? -13.518 -17.556 11.022  1.00 14.82 ? 150 VAL A CG2  1 
ATOM   1224 N  N    . GLY A 1 150 ? -18.082 -18.480 11.398  1.00 11.91 ? 151 GLY A N    1 
ATOM   1225 C  CA   . GLY A 1 150 ? -19.321 -19.302 11.436  1.00 13.14 ? 151 GLY A CA   1 
ATOM   1226 C  C    . GLY A 1 150 ? -20.169 -18.843 10.300  1.00 11.46 ? 151 GLY A C    1 
ATOM   1227 O  O    . GLY A 1 150 ? -19.764 -18.911 9.159   1.00 13.30 ? 151 GLY A O    1 
ATOM   1228 N  N    A SER A 1 151 ? -21.389 -18.381 10.626  0.50 13.42 ? 152 SER A N    1 
ATOM   1229 N  N    B SER A 1 151 ? -21.356 -18.334 10.633  0.50 13.72 ? 152 SER A N    1 
ATOM   1230 C  CA   A SER A 1 151 ? -22.314 -17.859 9.605   0.50 13.01 ? 152 SER A CA   1 
ATOM   1231 C  CA   B SER A 1 151 ? -22.192 -17.767 9.591   0.50 13.76 ? 152 SER A CA   1 
ATOM   1232 C  C    A SER A 1 151 ? -21.771 -16.500 9.091   0.50 12.85 ? 152 SER A C    1 
ATOM   1233 C  C    B SER A 1 151 ? -21.547 -16.500 8.996   0.50 13.54 ? 152 SER A C    1 
ATOM   1234 O  O    A SER A 1 151 ? -21.151 -15.776 9.894   0.50 9.68  ? 152 SER A O    1 
ATOM   1235 O  O    B SER A 1 151 ? -20.661 -15.843 9.599   0.50 13.89 ? 152 SER A O    1 
ATOM   1236 C  CB   A SER A 1 151 ? -23.692 -17.642 10.233  0.50 16.09 ? 152 SER A CB   1 
ATOM   1237 C  CB   B SER A 1 151 ? -23.583 -17.462 10.137  0.50 15.80 ? 152 SER A CB   1 
ATOM   1238 O  OG   A SER A 1 151 ? -23.682 -16.517 11.083  0.50 18.35 ? 152 SER A OG   1 
ATOM   1239 O  OG   B SER A 1 151 ? -24.105 -18.654 10.675  0.50 16.81 ? 152 SER A OG   1 
ATOM   1240 N  N    . ALA A 1 152 ? -21.989 -16.185 7.795   1.00 13.46 ? 153 ALA A N    1 
ATOM   1241 C  CA   . ALA A 1 152 ? -21.550 -14.937 7.183   1.00 13.44 ? 153 ALA A CA   1 
ATOM   1242 C  C    . ALA A 1 152 ? -22.183 -13.722 7.908   1.00 13.33 ? 153 ALA A C    1 
ATOM   1243 O  O    . ALA A 1 152 ? -23.283 -13.815 8.487   1.00 15.17 ? 153 ALA A O    1 
ATOM   1244 C  CB   . ALA A 1 152 ? -21.931 -14.876 5.720   1.00 15.46 ? 153 ALA A CB   1 
ATOM   1245 N  N    . LYS A 1 153 ? -21.469 -12.592 7.895   1.00 13.18 ? 154 LYS A N    1 
ATOM   1246 C  CA   . LYS A 1 153 ? -22.016 -11.329 8.295   1.00 14.04 ? 154 LYS A CA   1 
ATOM   1247 C  C    . LYS A 1 153 ? -22.441 -10.552 7.046   1.00 13.43 ? 154 LYS A C    1 
ATOM   1248 O  O    . LYS A 1 153 ? -21.604 -10.100 6.296   1.00 13.06 ? 154 LYS A O    1 
ATOM   1249 C  CB   . LYS A 1 153 ? -20.977 -10.511 9.064   1.00 13.45 ? 154 LYS A CB   1 
ATOM   1250 C  CG   . LYS A 1 153 ? -21.539 -9.288  9.790   1.00 16.27 ? 154 LYS A CG   1 
ATOM   1251 C  CD   . LYS A 1 153 ? -22.405 -9.722  11.004  1.00 17.78 ? 154 LYS A CD   1 
ATOM   1252 C  CE   . LYS A 1 153 ? -22.767 -8.568  11.923  1.00 21.06 ? 154 LYS A CE   1 
ATOM   1253 N  NZ   . LYS A 1 153 ? -23.672 -8.988  12.999  1.00 25.36 ? 154 LYS A NZ   1 
ATOM   1254 N  N    . PRO A 1 154 ? -23.760 -10.475 6.797   1.00 14.77 ? 155 PRO A N    1 
ATOM   1255 C  CA   . PRO A 1 154 ? -24.149 -9.892  5.496   1.00 15.23 ? 155 PRO A CA   1 
ATOM   1256 C  C    . PRO A 1 154 ? -23.679 -8.441  5.371   1.00 15.01 ? 155 PRO A C    1 
ATOM   1257 O  O    . PRO A 1 154 ? -23.242 -8.065  4.288   1.00 16.60 ? 155 PRO A O    1 
ATOM   1258 C  CB   . PRO A 1 154 ? -25.699 -9.952  5.527   1.00 17.12 ? 155 PRO A CB   1 
ATOM   1259 C  CG   . PRO A 1 154 ? -25.987 -11.037 6.591   1.00 20.42 ? 155 PRO A CG   1 
ATOM   1260 C  CD   . PRO A 1 154 ? -24.899 -11.033 7.581   1.00 16.05 ? 155 PRO A CD   1 
ATOM   1261 N  N    . GLY A 1 155 ? -23.647 -7.692  6.479   1.00 13.93 ? 156 GLY A N    1 
ATOM   1262 C  CA   . GLY A 1 155 ? -23.203 -6.327  6.476   1.00 15.21 ? 156 GLY A CA   1 
ATOM   1263 C  C    . GLY A 1 155 ? -21.730 -6.130  6.221   1.00 14.35 ? 156 GLY A C    1 
ATOM   1264 O  O    . GLY A 1 155 ? -21.300 -5.006  6.058   1.00 17.98 ? 156 GLY A O    1 
ATOM   1265 N  N    . LEU A 1 156 ? -20.932 -7.176  6.313   1.00 13.85 ? 157 LEU A N    1 
ATOM   1266 C  CA   . LEU A 1 156 ? -19.550 -7.175  5.916   1.00 11.80 ? 157 LEU A CA   1 
ATOM   1267 C  C    . LEU A 1 156 ? -19.276 -7.379  4.451   1.00 12.67 ? 157 LEU A C    1 
ATOM   1268 O  O    . LEU A 1 156 ? -18.145 -7.088  3.949   1.00 13.14 ? 157 LEU A O    1 
ATOM   1269 C  CB   . LEU A 1 156 ? -18.772 -8.184  6.737   1.00 13.01 ? 157 LEU A CB   1 
ATOM   1270 C  CG   . LEU A 1 156 ? -17.280 -8.287  6.584   1.00 11.64 ? 157 LEU A CG   1 
ATOM   1271 C  CD1  . LEU A 1 156 ? -16.581 -6.982  7.021   1.00 15.08 ? 157 LEU A CD1  1 
ATOM   1272 C  CD2  . LEU A 1 156 ? -16.658 -9.430  7.395   1.00 13.39 ? 157 LEU A CD2  1 
ATOM   1273 N  N    . GLN A 1 157 ? -20.252 -7.926  3.716   1.00 12.68 ? 158 GLN A N    1 
ATOM   1274 C  CA   . GLN A 1 157 ? -19.924 -8.388  2.382   1.00 14.93 ? 158 GLN A CA   1 
ATOM   1275 C  C    . GLN A 1 157 ? -19.513 -7.251  1.467   1.00 14.03 ? 158 GLN A C    1 
ATOM   1276 O  O    . GLN A 1 157 ? -18.611 -7.471  0.641   1.00 14.92 ? 158 GLN A O    1 
ATOM   1277 C  CB   . GLN A 1 157 ? -21.056 -9.224  1.796   1.00 15.46 ? 158 GLN A CB   1 
ATOM   1278 C  CG   . GLN A 1 157 ? -20.633 -9.935  0.488   1.00 16.31 ? 158 GLN A CG   1 
ATOM   1279 C  CD   . GLN A 1 157 ? -19.480 -10.939 0.723   1.00 14.19 ? 158 GLN A CD   1 
ATOM   1280 O  OE1  . GLN A 1 157 ? -19.338 -11.546 1.821   1.00 16.79 ? 158 GLN A OE1  1 
ATOM   1281 N  NE2  . GLN A 1 157 ? -18.677 -11.160 -0.306  1.00 18.96 ? 158 GLN A NE2  1 
ATOM   1282 N  N    . LYS A 1 158 ? -20.104 -6.053  1.614   1.00 15.38 ? 159 LYS A N    1 
ATOM   1283 C  CA   . LYS A 1 158 ? -19.637 -4.953  0.764   1.00 14.36 ? 159 LYS A CA   1 
ATOM   1284 C  C    . LYS A 1 158 ? -18.119 -4.635  0.901   1.00 13.27 ? 159 LYS A C    1 
ATOM   1285 O  O    . LYS A 1 158 ? -17.448 -4.280  -0.052  1.00 15.06 ? 159 LYS A O    1 
ATOM   1286 C  CB   . LYS A 1 158 ? -20.567 -3.746  0.911   1.00 17.32 ? 159 LYS A CB   1 
ATOM   1287 C  CG   . LYS A 1 158 ? -21.974 -3.996  0.182   1.00 22.96 ? 159 LYS A CG   1 
ATOM   1288 C  CD   . LYS A 1 158 ? -22.417 -5.490  0.243   1.00 32.17 ? 159 LYS A CD   1 
ATOM   1289 C  CE   . LYS A 1 158 ? -23.906 -5.750  0.384   1.00 34.18 ? 159 LYS A CE   1 
ATOM   1290 N  NZ   . LYS A 1 158 ? -24.088 -7.198  0.294   1.00 28.67 ? 159 LYS A NZ   1 
ATOM   1291 N  N    . VAL A 1 159 ? -17.629 -4.795  2.115   1.00 12.92 ? 160 VAL A N    1 
ATOM   1292 C  CA   . VAL A 1 159 ? -16.226 -4.547  2.378   1.00 12.07 ? 160 VAL A CA   1 
ATOM   1293 C  C    . VAL A 1 159 ? -15.400 -5.676  1.709   1.00 13.60 ? 160 VAL A C    1 
ATOM   1294 O  O    . VAL A 1 159 ? -14.459 -5.451  0.962   1.00 14.54 ? 160 VAL A O    1 
ATOM   1295 C  CB   . VAL A 1 159 ? -15.967 -4.566  3.855   1.00 13.12 ? 160 VAL A CB   1 
ATOM   1296 C  CG1  . VAL A 1 159 ? -14.423 -4.576  4.154   1.00 13.50 ? 160 VAL A CG1  1 
ATOM   1297 C  CG2  . VAL A 1 159 ? -16.685 -3.432  4.554   1.00 14.60 ? 160 VAL A CG2  1 
ATOM   1298 N  N    . VAL A 1 160 ? -15.807 -6.917  1.941   1.00 13.64 ? 161 VAL A N    1 
ATOM   1299 C  CA   . VAL A 1 160 ? -15.077 -8.044  1.371   1.00 16.59 ? 161 VAL A CA   1 
ATOM   1300 C  C    . VAL A 1 160 ? -14.995 -7.939  -0.138  1.00 16.03 ? 161 VAL A C    1 
ATOM   1301 O  O    . VAL A 1 160 ? -13.951 -8.238  -0.753  1.00 15.79 ? 161 VAL A O    1 
ATOM   1302 C  CB   . VAL A 1 160 ? -15.823 -9.453  1.806   1.00 16.66 ? 161 VAL A CB   1 
ATOM   1303 C  CG1  . VAL A 1 160 ? -15.390 -10.603 0.890   1.00 19.43 ? 161 VAL A CG1  1 
ATOM   1304 C  CG2  . VAL A 1 160 ? -15.531 -9.622  3.268   1.00 18.59 ? 161 VAL A CG2  1 
ATOM   1305 N  N    . ASP A 1 161 ? -16.102 -7.540  -0.755  1.00 16.70 ? 162 ASP A N    1 
ATOM   1306 C  CA   . ASP A 1 161 ? -16.098 -7.568  -2.202  1.00 20.11 ? 162 ASP A CA   1 
ATOM   1307 C  C    . ASP A 1 161 ? -15.254 -6.508  -2.880  1.00 19.11 ? 162 ASP A C    1 
ATOM   1308 O  O    . ASP A 1 161 ? -14.950 -6.666  -4.082  1.00 23.70 ? 162 ASP A O    1 
ATOM   1309 C  CB   . ASP A 1 161 ? -17.482 -7.519  -2.683  1.00 20.96 ? 162 ASP A CB   1 
ATOM   1310 C  CG   . ASP A 1 161 ? -18.105 -8.851  -2.657  1.00 21.63 ? 162 ASP A CG   1 
ATOM   1311 O  OD1  . ASP A 1 161 ? -17.325 -9.859  -2.747  1.00 25.00 ? 162 ASP A OD1  1 
ATOM   1312 O  OD2  . ASP A 1 161 ? -19.325 -8.914  -2.464  1.00 24.64 ? 162 ASP A OD2  1 
ATOM   1313 N  N    . VAL A 1 162 ? -14.850 -5.438  -2.165  1.00 16.21 ? 163 VAL A N    1 
ATOM   1314 C  CA   . VAL A 1 162 ? -14.061 -4.401  -2.815  1.00 18.11 ? 163 VAL A CA   1 
ATOM   1315 C  C    . VAL A 1 162 ? -12.549 -4.698  -2.592  1.00 15.65 ? 163 VAL A C    1 
ATOM   1316 O  O    . VAL A 1 162 ? -11.686 -3.994  -3.118  1.00 17.48 ? 163 VAL A O    1 
ATOM   1317 C  CB   . VAL A 1 162 ? -14.465 -3.015  -2.205  1.00 19.39 ? 163 VAL A CB   1 
ATOM   1318 C  CG1  . VAL A 1 162 ? -13.810 -2.773  -0.920  1.00 19.26 ? 163 VAL A CG1  1 
ATOM   1319 C  CG2  . VAL A 1 162 ? -14.179 -1.810  -3.110  1.00 22.53 ? 163 VAL A CG2  1 
ATOM   1320 N  N    . LEU A 1 163 ? -12.197 -5.690  -1.742  1.00 15.95 ? 164 LEU A N    1 
ATOM   1321 C  CA   . LEU A 1 163 ? -10.763 -5.921  -1.403  1.00 15.22 ? 164 LEU A CA   1 
ATOM   1322 C  C    . LEU A 1 163 ? -9.856  -6.232  -2.562  1.00 16.81 ? 164 LEU A C    1 
ATOM   1323 O  O    . LEU A 1 163 ? -8.665  -5.845  -2.569  1.00 17.79 ? 164 LEU A O    1 
ATOM   1324 C  CB   . LEU A 1 163 ? -10.572 -6.949  -0.286  1.00 13.55 ? 164 LEU A CB   1 
ATOM   1325 C  CG   . LEU A 1 163 ? -11.306 -6.628  1.026   1.00 14.39 ? 164 LEU A CG   1 
ATOM   1326 C  CD1  . LEU A 1 163 ? -11.081 -7.769  2.044   1.00 16.68 ? 164 LEU A CD1  1 
ATOM   1327 C  CD2  . LEU A 1 163 ? -10.798 -5.352  1.627   1.00 15.07 ? 164 LEU A CD2  1 
ATOM   1328 N  N    . ASP A 1 164 ? -10.418 -6.894  -3.568  1.00 19.63 ? 165 ASP A N    1 
ATOM   1329 C  CA   . ASP A 1 164 ? -9.577  -7.188  -4.737  1.00 22.11 ? 165 ASP A CA   1 
ATOM   1330 C  C    . ASP A 1 164 ? -9.130  -5.904  -5.474  1.00 22.45 ? 165 ASP A C    1 
ATOM   1331 O  O    . ASP A 1 164 ? -8.085  -5.918  -6.209  1.00 24.73 ? 165 ASP A O    1 
ATOM   1332 C  CB   . ASP A 1 164 ? -10.355 -8.110  -5.714  1.00 24.23 ? 165 ASP A CB   1 
ATOM   1333 C  CG   . ASP A 1 164 ? -11.351 -7.331  -6.532  1.00 26.76 ? 165 ASP A CG   1 
ATOM   1334 O  OD1  . ASP A 1 164 ? -12.404 -6.899  -5.985  1.00 30.88 ? 165 ASP A OD1  1 
ATOM   1335 O  OD2  . ASP A 1 164 ? -11.079 -7.064  -7.729  1.00 35.53 ? 165 ASP A OD2  1 
ATOM   1336 N  N    . SER A 1 165 ? -9.869  -4.800  -5.258  1.00 19.99 ? 166 SER A N    1 
ATOM   1337 C  CA   . SER A 1 165 ? -9.491  -3.516  -5.882  1.00 19.70 ? 166 SER A CA   1 
ATOM   1338 C  C    . SER A 1 165 ? -8.417  -2.758  -5.086  1.00 17.22 ? 166 SER A C    1 
ATOM   1339 O  O    . SER A 1 165 ? -7.874  -1.781  -5.584  1.00 18.89 ? 166 SER A O    1 
ATOM   1340 C  CB   . SER A 1 165 ? -10.708 -2.664  -6.097  1.00 23.09 ? 166 SER A CB   1 
ATOM   1341 O  OG   . SER A 1 165 ? -11.099 -2.101  -4.912  1.00 23.45 ? 166 SER A OG   1 
ATOM   1342 N  N    . ILE A 1 166 ? -8.127  -3.237  -3.873  1.00 16.10 ? 167 ILE A N    1 
ATOM   1343 C  CA   . ILE A 1 166 ? -7.109  -2.629  -3.009  1.00 14.68 ? 167 ILE A CA   1 
ATOM   1344 C  C    . ILE A 1 166 ? -6.094  -3.642  -2.499  1.00 14.10 ? 167 ILE A C    1 
ATOM   1345 O  O    . ILE A 1 166 ? -5.719  -3.622  -1.347  1.00 14.52 ? 167 ILE A O    1 
ATOM   1346 C  CB   . ILE A 1 166 ? -7.770  -1.775  -1.867  1.00 14.80 ? 167 ILE A CB   1 
ATOM   1347 C  CG1  . ILE A 1 166 ? -8.655  -2.621  -0.972  1.00 13.01 ? 167 ILE A CG1  1 
ATOM   1348 C  CG2  . ILE A 1 166 ? -8.467  -0.591  -2.466  1.00 16.82 ? 167 ILE A CG2  1 
ATOM   1349 C  CD1  . ILE A 1 166 ? -8.604  -2.128  0.405   1.00 14.58 ? 167 ILE A CD1  1 
ATOM   1350 N  N    . LYS A 1 167 ? -5.677  -4.531  -3.403  1.00 15.58 ? 168 LYS A N    1 
ATOM   1351 C  CA   . LYS A 1 167 ? -4.922  -5.671  -2.986  1.00 15.13 ? 168 LYS A CA   1 
ATOM   1352 C  C    . LYS A 1 167 ? -3.619  -5.268  -2.328  1.00 14.90 ? 168 LYS A C    1 
ATOM   1353 O  O    . LYS A 1 167 ? -3.197  -5.893  -1.380  1.00 15.55 ? 168 LYS A O    1 
ATOM   1354 C  CB   . LYS A 1 167 ? -4.710  -6.619  -4.180  1.00 16.95 ? 168 LYS A CB   1 
ATOM   1355 C  CG   . LYS A 1 167 ? -3.990  -7.905  -3.749  1.00 18.68 ? 168 LYS A CG   1 
ATOM   1356 C  CD   . LYS A 1 167 ? -3.714  -8.777  -4.977  1.00 23.70 ? 168 LYS A CD   1 
ATOM   1357 C  CE   . LYS A 1 167 ? -3.028  -10.016 -4.578  1.00 27.62 ? 168 LYS A CE   1 
ATOM   1358 N  NZ   . LYS A 1 167 ? -2.743  -10.842 -5.825  1.00 32.57 ? 168 LYS A NZ   1 
ATOM   1359 N  N    . THR A 1 168 ? -2.973  -4.212  -2.836  1.00 14.87 ? 169 THR A N    1 
ATOM   1360 C  CA   . THR A 1 168 ? -1.588  -3.910  -2.451  1.00 15.32 ? 169 THR A CA   1 
ATOM   1361 C  C    . THR A 1 168 ? -1.517  -2.514  -1.795  1.00 13.51 ? 169 THR A C    1 
ATOM   1362 O  O    . THR A 1 168 ? -2.457  -1.667  -1.865  1.00 15.24 ? 169 THR A O    1 
ATOM   1363 C  CB   . THR A 1 168 ? -0.650  -3.903  -3.673  1.00 16.50 ? 169 THR A CB   1 
ATOM   1364 O  OG1  . THR A 1 168 ? -1.283  -3.143  -4.705  1.00 18.49 ? 169 THR A OG1  1 
ATOM   1365 C  CG2  . THR A 1 168 ? -0.487  -5.365  -4.125  1.00 18.16 ? 169 THR A CG2  1 
ATOM   1366 N  N    . LYS A 1 169 ? -0.433  -2.376  -1.069  1.00 17.02 ? 170 LYS A N    1 
ATOM   1367 C  CA   . LYS A 1 169 ? -0.164  -1.172  -0.285  1.00 16.39 ? 170 LYS A CA   1 
ATOM   1368 C  C    . LYS A 1 169 ? -0.297  0.104   -1.054  1.00 15.88 ? 170 LYS A C    1 
ATOM   1369 O  O    . LYS A 1 169 ? 0.250   0.226   -2.176  1.00 19.62 ? 170 LYS A O    1 
ATOM   1370 C  CB   . LYS A 1 169 ? 1.245   -1.306  0.326   1.00 17.68 ? 170 LYS A CB   1 
ATOM   1371 C  CG   . LYS A 1 169 ? 1.724   -0.042  1.152   1.00 18.54 ? 170 LYS A CG   1 
ATOM   1372 C  CD   . LYS A 1 169 ? 3.062   -0.266  1.799   1.00 22.67 ? 170 LYS A CD   1 
ATOM   1373 C  CE   . LYS A 1 169 ? 3.522   1.005   2.540   1.00 29.82 ? 170 LYS A CE   1 
ATOM   1374 N  NZ   . LYS A 1 169 ? 4.976   0.897   2.956   1.00 36.06 ? 170 LYS A NZ   1 
ATOM   1375 N  N    . GLY A 1 170 ? -1.043  1.054   -0.509  1.00 17.18 ? 171 GLY A N    1 
ATOM   1376 C  CA   . GLY A 1 170 ? -1.214  2.352   -1.155  1.00 17.81 ? 171 GLY A CA   1 
ATOM   1377 C  C    . GLY A 1 170 ? -2.421  2.429   -2.080  1.00 19.22 ? 171 GLY A C    1 
ATOM   1378 O  O    . GLY A 1 170 ? -2.819  3.537   -2.512  1.00 21.73 ? 171 GLY A O    1 
ATOM   1379 N  N    . LYS A 1 171 ? -3.047  1.298   -2.428  1.00 17.64 ? 172 LYS A N    1 
ATOM   1380 C  CA   . LYS A 1 171 ? -4.266  1.364   -3.233  1.00 16.72 ? 172 LYS A CA   1 
ATOM   1381 C  C    . LYS A 1 171 ? -5.490  1.803   -2.421  1.00 15.76 ? 172 LYS A C    1 
ATOM   1382 O  O    . LYS A 1 171 ? -5.676  1.389   -1.272  1.00 16.29 ? 172 LYS A O    1 
ATOM   1383 C  CB   . LYS A 1 171 ? -4.538  0.032   -3.922  1.00 18.54 ? 172 LYS A CB   1 
ATOM   1384 C  CG   . LYS A 1 171 ? -3.550  -0.286  -5.012  1.00 20.75 ? 172 LYS A CG   1 
ATOM   1385 C  CD   . LYS A 1 171 ? -3.956  -1.431  -5.912  1.00 26.03 ? 172 LYS A CD   1 
ATOM   1386 C  CE   . LYS A 1 171 ? -5.102  -1.039  -6.897  1.00 31.46 ? 172 LYS A CE   1 
ATOM   1387 N  NZ   . LYS A 1 171 ? -5.559  -2.211  -7.800  1.00 31.84 ? 172 LYS A NZ   1 
ATOM   1388 N  N    . SER A 1 172 ? -6.336  2.609   -3.020  1.00 17.09 ? 173 SER A N    1 
ATOM   1389 C  CA   . SER A 1 172 ? -7.602  3.036   -2.446  1.00 17.44 ? 173 SER A CA   1 
ATOM   1390 C  C    . SER A 1 172 ? -8.731  2.907   -3.445  1.00 16.70 ? 173 SER A C    1 
ATOM   1391 O  O    . SER A 1 172 ? -8.508  2.874   -4.691  1.00 19.86 ? 173 SER A O    1 
ATOM   1392 C  CB   . SER A 1 172 ? -7.511  4.472   -1.895  1.00 17.75 ? 173 SER A CB   1 
ATOM   1393 O  OG   . SER A 1 172 ? -7.279  5.363   -2.939  1.00 21.25 ? 173 SER A OG   1 
ATOM   1394 N  N    . ALA A 1 173 ? -9.941  2.913   -2.929  1.00 18.16 ? 174 ALA A N    1 
ATOM   1395 C  CA   . ALA A 1 173 ? -11.131 2.856   -3.787  1.00 18.24 ? 174 ALA A CA   1 
ATOM   1396 C  C    . ALA A 1 173 ? -12.244 3.653   -3.126  1.00 18.88 ? 174 ALA A C    1 
ATOM   1397 O  O    . ALA A 1 173 ? -12.360 3.708   -1.897  1.00 17.11 ? 174 ALA A O    1 
ATOM   1398 C  CB   . ALA A 1 173 ? -11.541 1.427   -4.072  1.00 19.45 ? 174 ALA A CB   1 
ATOM   1399 N  N    . ASP A 1 174 ? -13.059 4.315   -3.930  1.00 20.07 ? 175 ASP A N    1 
ATOM   1400 C  CA   . ASP A 1 174 ? -14.223 4.981   -3.380  1.00 20.99 ? 175 ASP A CA   1 
ATOM   1401 C  C    . ASP A 1 174 ? -15.023 3.947   -2.624  1.00 20.05 ? 175 ASP A C    1 
ATOM   1402 O  O    . ASP A 1 174 ? -15.121 2.761   -3.052  1.00 21.36 ? 175 ASP A O    1 
ATOM   1403 C  CB   . ASP A 1 174 ? -15.093 5.582   -4.514  1.00 22.90 ? 175 ASP A CB   1 
ATOM   1404 C  CG   . ASP A 1 174 ? -14.315 6.576   -5.395  1.00 31.28 ? 175 ASP A CG   1 
ATOM   1405 O  OD1  . ASP A 1 174 ? -13.532 7.419   -4.873  1.00 34.77 ? 175 ASP A OD1  1 
ATOM   1406 O  OD2  . ASP A 1 174 ? -14.510 6.520   -6.651  1.00 33.61 ? 175 ASP A OD2  1 
ATOM   1407 N  N    . PHE A 1 175 ? -15.640 4.380   -1.520  1.00 17.38 ? 176 PHE A N    1 
ATOM   1408 C  CA   . PHE A 1 175 ? -16.373 3.425   -0.699  1.00 15.88 ? 176 PHE A CA   1 
ATOM   1409 C  C    . PHE A 1 175 ? -17.424 4.197   0.032   1.00 16.24 ? 176 PHE A C    1 
ATOM   1410 O  O    . PHE A 1 175 ? -17.338 4.414   1.240   1.00 18.66 ? 176 PHE A O    1 
ATOM   1411 C  CB   . PHE A 1 175 ? -15.434 2.647   0.207   1.00 14.38 ? 176 PHE A CB   1 
ATOM   1412 C  CG   . PHE A 1 175 ? -16.021 1.365   0.737   1.00 14.31 ? 176 PHE A CG   1 
ATOM   1413 C  CD1  . PHE A 1 175 ? -16.273 0.298   -0.110  1.00 15.80 ? 176 PHE A CD1  1 
ATOM   1414 C  CD2  . PHE A 1 175 ? -16.392 1.257   2.053   1.00 14.79 ? 176 PHE A CD2  1 
ATOM   1415 C  CE1  . PHE A 1 175 ? -16.818 -0.889  0.401   1.00 16.78 ? 176 PHE A CE1  1 
ATOM   1416 C  CE2  . PHE A 1 175 ? -16.931 0.060   2.560   1.00 16.70 ? 176 PHE A CE2  1 
ATOM   1417 C  CZ   . PHE A 1 175 ? -17.187 -0.994  1.676   1.00 15.10 ? 176 PHE A CZ   1 
ATOM   1418 N  N    . THR A 1 176 ? -18.405 4.630   -0.713  1.00 15.92 ? 177 THR A N    1 
ATOM   1419 C  CA   . THR A 1 176 ? -19.538 5.420   -0.154  1.00 15.15 ? 177 THR A CA   1 
ATOM   1420 C  C    . THR A 1 176 ? -20.689 4.584   0.280   1.00 14.01 ? 177 THR A C    1 
ATOM   1421 O  O    . THR A 1 176 ? -20.847 3.436   -0.188  1.00 14.56 ? 177 THR A O    1 
ATOM   1422 C  CB   . THR A 1 176 ? -20.034 6.483   -1.137  1.00 16.47 ? 177 THR A CB   1 
ATOM   1423 O  OG1  . THR A 1 176 ? -20.386 5.803   -2.356  1.00 19.60 ? 177 THR A OG1  1 
ATOM   1424 C  CG2  . THR A 1 176 ? -18.927 7.525   -1.369  1.00 20.32 ? 177 THR A CG2  1 
ATOM   1425 N  N    . ASN A 1 177 ? -21.484 5.156   1.165   1.00 13.76 ? 178 ASN A N    1 
ATOM   1426 C  CA   . ASN A 1 177 ? -22.750 4.591   1.562   1.00 15.32 ? 178 ASN A CA   1 
ATOM   1427 C  C    . ASN A 1 177 ? -22.613 3.287   2.308   1.00 15.52 ? 178 ASN A C    1 
ATOM   1428 O  O    . ASN A 1 177 ? -23.565 2.466   2.278   1.00 18.60 ? 178 ASN A O    1 
ATOM   1429 C  CB   . ASN A 1 177 ? -23.705 4.468   0.400   1.00 15.55 ? 178 ASN A CB   1 
ATOM   1430 C  CG   . ASN A 1 177 ? -23.973 5.844   -0.217  1.00 16.61 ? 178 ASN A CG   1 
ATOM   1431 O  OD1  . ASN A 1 177 ? -24.666 6.692   0.373   1.00 19.94 ? 178 ASN A OD1  1 
ATOM   1432 N  ND2  . ASN A 1 177 ? -23.365 6.093   -1.345  1.00 16.32 ? 178 ASN A ND2  1 
ATOM   1433 N  N    . PHE A 1 178 ? -21.464 3.064   2.940   1.00 14.33 ? 179 PHE A N    1 
ATOM   1434 C  CA   . PHE A 1 178 ? -21.295 1.870   3.761   1.00 13.97 ? 179 PHE A CA   1 
ATOM   1435 C  C    . PHE A 1 178 ? -21.852 2.132   5.138   1.00 14.34 ? 179 PHE A C    1 
ATOM   1436 O  O    . PHE A 1 178 ? -21.417 3.098   5.775   1.00 14.95 ? 179 PHE A O    1 
ATOM   1437 C  CB   . PHE A 1 178 ? -19.872 1.415   3.858   1.00 13.05 ? 179 PHE A CB   1 
ATOM   1438 C  CG   . PHE A 1 178 ? -19.755 0.186   4.685   1.00 13.03 ? 179 PHE A CG   1 
ATOM   1439 C  CD1  . PHE A 1 178 ? -20.138 -1.076  4.152   1.00 14.16 ? 179 PHE A CD1  1 
ATOM   1440 C  CD2  . PHE A 1 178 ? -19.458 0.273   6.021   1.00 13.71 ? 179 PHE A CD2  1 
ATOM   1441 C  CE1  . PHE A 1 178 ? -20.119 -2.201  4.922   1.00 13.40 ? 179 PHE A CE1  1 
ATOM   1442 C  CE2  . PHE A 1 178 ? -19.382 -0.945  6.805   1.00 13.11 ? 179 PHE A CE2  1 
ATOM   1443 C  CZ   . PHE A 1 178 ? -19.786 -2.162  6.237   1.00 14.02 ? 179 PHE A CZ   1 
ATOM   1444 N  N    . ASP A 1 179 ? -22.739 1.271   5.664   1.00 14.05 ? 180 ASP A N    1 
ATOM   1445 C  CA   . ASP A 1 179 ? -23.343 1.454   6.974   1.00 13.83 ? 180 ASP A CA   1 
ATOM   1446 C  C    . ASP A 1 179 ? -22.658 0.604   8.004   1.00 12.50 ? 180 ASP A C    1 
ATOM   1447 O  O    . ASP A 1 179 ? -22.840 -0.605  8.068   1.00 13.60 ? 180 ASP A O    1 
ATOM   1448 C  CB   . ASP A 1 179 ? -24.829 1.094   6.854   1.00 14.83 ? 180 ASP A CB   1 
ATOM   1449 C  CG   . ASP A 1 179 ? -25.619 1.437   8.052   1.00 17.29 ? 180 ASP A CG   1 
ATOM   1450 O  OD1  . ASP A 1 179 ? -25.069 1.746   9.113   1.00 15.02 ? 180 ASP A OD1  1 
ATOM   1451 O  OD2  . ASP A 1 179 ? -26.848 1.433   7.888   1.00 24.61 ? 180 ASP A OD2  1 
ATOM   1452 N  N    . PRO A 1 180 ? -21.879 1.232   8.904   1.00 11.79 ? 181 PRO A N    1 
ATOM   1453 C  CA   . PRO A 1 180 ? -21.184 0.407   9.894   1.00 12.30 ? 181 PRO A CA   1 
ATOM   1454 C  C    . PRO A 1 180 ? -22.080 -0.196  10.953  1.00 10.72 ? 181 PRO A C    1 
ATOM   1455 O  O    . PRO A 1 180 ? -21.650 -1.106  11.675  1.00 11.97 ? 181 PRO A O    1 
ATOM   1456 C  CB   . PRO A 1 180 ? -20.179 1.400   10.491  1.00 12.31 ? 181 PRO A CB   1 
ATOM   1457 C  CG   . PRO A 1 180 ? -20.873 2.783   10.414  1.00 13.52 ? 181 PRO A CG   1 
ATOM   1458 C  CD   . PRO A 1 180 ? -21.634 2.702   9.064   1.00 13.74 ? 181 PRO A CD   1 
ATOM   1459 N  N    . ARG A 1 181 ? -23.367 0.195   10.975  1.00 11.39 ? 182 ARG A N    1 
ATOM   1460 C  CA   . ARG A 1 181 ? -24.309 -0.511  11.924  1.00 12.54 ? 182 ARG A CA   1 
ATOM   1461 C  C    . ARG A 1 181 ? -24.399 -1.994  11.542  1.00 13.38 ? 182 ARG A C    1 
ATOM   1462 O  O    . ARG A 1 181 ? -24.721 -2.805  12.412  1.00 13.89 ? 182 ARG A O    1 
ATOM   1463 C  CB   . ARG A 1 181 ? -25.699 0.089   11.817  1.00 13.34 ? 182 ARG A CB   1 
ATOM   1464 C  CG   . ARG A 1 181 ? -25.658 1.502   12.464  1.00 15.47 ? 182 ARG A CG   1 
ATOM   1465 C  CD   . ARG A 1 181 ? -27.017 2.219   12.374  1.00 16.85 ? 182 ARG A CD   1 
ATOM   1466 N  NE   . ARG A 1 181 ? -27.348 2.488   10.973  1.00 15.76 ? 182 ARG A NE   1 
ATOM   1467 C  CZ   . ARG A 1 181 ? -28.414 3.192   10.593  1.00 17.44 ? 182 ARG A CZ   1 
ATOM   1468 N  NH1  . ARG A 1 181 ? -29.225 3.684   11.511  1.00 21.95 ? 182 ARG A NH1  1 
ATOM   1469 N  NH2  . ARG A 1 181 ? -28.658 3.342   9.286   1.00 21.34 ? 182 ARG A NH2  1 
ATOM   1470 N  N    . GLY A 1 182 ? -24.134 -2.365  10.282  1.00 12.87 ? 183 GLY A N    1 
ATOM   1471 C  CA   . GLY A 1 182 ? -24.224 -3.771  9.912   1.00 13.37 ? 183 GLY A CA   1 
ATOM   1472 C  C    . GLY A 1 182 ? -23.058 -4.650  10.434  1.00 14.57 ? 183 GLY A C    1 
ATOM   1473 O  O    . GLY A 1 182 ? -23.010 -5.828  10.167  1.00 15.60 ? 183 GLY A O    1 
ATOM   1474 N  N    . LEU A 1 183 ? -22.115 -4.033  11.149  1.00 12.81 ? 184 LEU A N    1 
ATOM   1475 C  CA   . LEU A 1 183 ? -20.977 -4.739  11.711  1.00 11.56 ? 184 LEU A CA   1 
ATOM   1476 C  C    . LEU A 1 183 ? -21.156 -4.938  13.222  1.00 10.20 ? 184 LEU A C    1 
ATOM   1477 O  O    . LEU A 1 183 ? -20.261 -5.532  13.816  1.00 13.65 ? 184 LEU A O    1 
ATOM   1478 C  CB   . LEU A 1 183 ? -19.690 -3.971  11.457  1.00 10.45 ? 184 LEU A CB   1 
ATOM   1479 C  CG   . LEU A 1 183 ? -19.361 -3.853  9.953   1.00 13.26 ? 184 LEU A CG   1 
ATOM   1480 C  CD1  . LEU A 1 183 ? -18.130 -3.077  9.787   1.00 16.49 ? 184 LEU A CD1  1 
ATOM   1481 C  CD2  . LEU A 1 183 ? -19.283 -5.195  9.243   1.00 16.31 ? 184 LEU A CD2  1 
ATOM   1482 N  N    . LEU A 1 184 ? -22.303 -4.515  13.820  1.00 12.55 ? 185 LEU A N    1 
ATOM   1483 C  CA   . LEU A 1 184 ? -22.434 -4.533  15.287  1.00 12.46 ? 185 LEU A CA   1 
ATOM   1484 C  C    . LEU A 1 184 ? -23.221 -5.759  15.764  1.00 13.72 ? 185 LEU A C    1 
ATOM   1485 O  O    . LEU A 1 184 ? -24.188 -6.183  15.124  1.00 17.98 ? 185 LEU A O    1 
ATOM   1486 C  CB   . LEU A 1 184 ? -23.265 -3.277  15.775  1.00 12.45 ? 185 LEU A CB   1 
ATOM   1487 C  CG   . LEU A 1 184 ? -22.611 -1.950  15.346  1.00 12.29 ? 185 LEU A CG   1 
ATOM   1488 C  CD1  . LEU A 1 184 ? -23.484 -0.828  15.846  1.00 14.27 ? 185 LEU A CD1  1 
ATOM   1489 C  CD2  . LEU A 1 184 ? -21.198 -1.837  15.901  1.00 14.10 ? 185 LEU A CD2  1 
ATOM   1490 N  N    . PRO A 1 185 ? -22.763 -6.367  16.846  1.00 11.68 ? 186 PRO A N    1 
ATOM   1491 C  CA   . PRO A 1 185 ? -23.552 -7.505  17.382  1.00 11.81 ? 186 PRO A CA   1 
ATOM   1492 C  C    . PRO A 1 185 ? -24.810 -6.969  18.057  1.00 11.77 ? 186 PRO A C    1 
ATOM   1493 O  O    . PRO A 1 185 ? -25.015 -5.772  18.098  1.00 13.45 ? 186 PRO A O    1 
ATOM   1494 C  CB   . PRO A 1 185 ? -22.612 -8.083  18.414  1.00 12.07 ? 186 PRO A CB   1 
ATOM   1495 C  CG   . PRO A 1 185 ? -21.799 -6.890  18.926  1.00 11.06 ? 186 PRO A CG   1 
ATOM   1496 C  CD   . PRO A 1 185 ? -21.604 -5.983  17.669  1.00 11.04 ? 186 PRO A CD   1 
ATOM   1497 N  N    A GLU A 1 186 ? -25.732 -7.824  18.566  0.50 13.42 ? 187 GLU A N    1 
ATOM   1498 N  N    B GLU A 1 186 ? -25.623 -7.899  18.527  0.50 13.06 ? 187 GLU A N    1 
ATOM   1499 C  CA   A GLU A 1 186 ? -26.991 -7.325  19.184  0.50 13.96 ? 187 GLU A CA   1 
ATOM   1500 C  CA   B GLU A 1 186 ? -26.857 -7.551  19.072  0.50 13.08 ? 187 GLU A CA   1 
ATOM   1501 C  C    A GLU A 1 186 ? -26.733 -6.676  20.492  0.50 13.45 ? 187 GLU A C    1 
ATOM   1502 C  C    B GLU A 1 186 ? -26.622 -6.711  20.308  0.50 11.71 ? 187 GLU A C    1 
ATOM   1503 O  O    A GLU A 1 186 ? -27.444 -5.744  20.890  0.50 14.53 ? 187 GLU A O    1 
ATOM   1504 O  O    B GLU A 1 186 ? -27.149 -5.559  20.363  0.50 11.92 ? 187 GLU A O    1 
ATOM   1505 C  CB   A GLU A 1 186 ? -27.926 -8.482  19.560  0.50 15.90 ? 187 GLU A CB   1 
ATOM   1506 C  CB   B GLU A 1 186 ? -27.544 -8.872  19.377  0.50 14.03 ? 187 GLU A CB   1 
ATOM   1507 C  CG   A GLU A 1 186 ? -28.417 -9.283  18.418  0.50 18.03 ? 187 GLU A CG   1 
ATOM   1508 C  CG   B GLU A 1 186 ? -28.721 -8.712  20.257  0.50 15.44 ? 187 GLU A CG   1 
ATOM   1509 C  CD   A GLU A 1 186 ? -29.272 -10.530 18.848  0.50 17.60 ? 187 GLU A CD   1 
ATOM   1510 C  CD   B GLU A 1 186 ? -29.315 -10.047 20.593  0.50 19.02 ? 187 GLU A CD   1 
ATOM   1511 O  OE1  A GLU A 1 186 ? -29.575 -10.727 20.039  0.50 16.47 ? 187 GLU A OE1  1 
ATOM   1512 O  OE1  B GLU A 1 186 ? -28.989 -10.999 19.829  0.50 19.29 ? 187 GLU A OE1  1 
ATOM   1513 O  OE2  A GLU A 1 186 ? -29.663 -11.275 17.955  0.50 21.10 ? 187 GLU A OE2  1 
ATOM   1514 O  OE2  B GLU A 1 186 ? -30.071 -10.109 21.583  0.50 22.13 ? 187 GLU A OE2  1 
ATOM   1515 N  N    . SER A 1 187 ? -25.814 -7.236  21.262  1.00 12.15 ? 188 SER A N    1 
ATOM   1516 C  CA   . SER A 1 187 ? -25.588 -6.621  22.556  1.00 12.37 ? 188 SER A CA   1 
ATOM   1517 C  C    . SER A 1 187 ? -24.480 -5.591  22.504  1.00 11.90 ? 188 SER A C    1 
ATOM   1518 O  O    . SER A 1 187 ? -23.427 -5.841  21.895  1.00 13.68 ? 188 SER A O    1 
ATOM   1519 C  CB   . SER A 1 187 ? -25.169 -7.704  23.574  1.00 13.88 ? 188 SER A CB   1 
ATOM   1520 O  OG   . SER A 1 187 ? -24.958 -7.131  24.870  1.00 15.49 ? 188 SER A OG   1 
ATOM   1521 N  N    . LEU A 1 188 ? -24.663 -4.528  23.269  1.00 12.14 ? 189 LEU A N    1 
ATOM   1522 C  CA   . LEU A 1 188 ? -23.596 -3.539  23.496  1.00 12.34 ? 189 LEU A CA   1 
ATOM   1523 C  C    . LEU A 1 188 ? -22.949 -3.670  24.865  1.00 11.40 ? 189 LEU A C    1 
ATOM   1524 O  O    . LEU A 1 188 ? -22.230 -2.780  25.312  1.00 13.64 ? 189 LEU A O    1 
ATOM   1525 C  CB   . LEU A 1 188 ? -24.066 -2.092  23.235  1.00 14.27 ? 189 LEU A CB   1 
ATOM   1526 C  CG   . LEU A 1 188 ? -24.522 -1.753  21.828  1.00 14.40 ? 189 LEU A CG   1 
ATOM   1527 C  CD1  . LEU A 1 188 ? -25.026 -0.309  21.687  1.00 16.99 ? 189 LEU A CD1  1 
ATOM   1528 C  CD2  . LEU A 1 188 ? -23.399 -1.973  20.874  1.00 17.34 ? 189 LEU A CD2  1 
ATOM   1529 N  N    . ASP A 1 189 ? -23.071 -4.841  25.529  1.00 12.26 ? 190 ASP A N    1 
ATOM   1530 C  CA   . ASP A 1 189 ? -22.312 -5.087  26.789  1.00 12.44 ? 190 ASP A CA   1 
ATOM   1531 C  C    . ASP A 1 189 ? -20.794 -5.021  26.479  1.00 9.69  ? 190 ASP A C    1 
ATOM   1532 O  O    . ASP A 1 189 ? -20.361 -5.480  25.416  1.00 10.40 ? 190 ASP A O    1 
ATOM   1533 C  CB   . ASP A 1 189 ? -22.631 -6.462  27.382  1.00 13.62 ? 190 ASP A CB   1 
ATOM   1534 C  CG   . ASP A 1 189 ? -24.062 -6.555  27.985  1.00 17.75 ? 190 ASP A CG   1 
ATOM   1535 O  OD1  . ASP A 1 189 ? -24.669 -5.502  28.214  1.00 24.46 ? 190 ASP A OD1  1 
ATOM   1536 O  OD2  . ASP A 1 189 ? -24.518 -7.702  28.194  1.00 25.17 ? 190 ASP A OD2  1 
ATOM   1537 N  N    . TYR A 1 190 ? -20.028 -4.405  27.374  1.00 9.68  ? 191 TYR A N    1 
ATOM   1538 C  CA   . TYR A 1 190 ? -18.618 -4.175  27.038  1.00 9.61  ? 191 TYR A CA   1 
ATOM   1539 C  C    . TYR A 1 190 ? -17.704 -4.239  28.268  1.00 9.14  ? 191 TYR A C    1 
ATOM   1540 O  O    . TYR A 1 190 ? -18.157 -4.101  29.432  1.00 10.87 ? 191 TYR A O    1 
ATOM   1541 C  CB   . TYR A 1 190 ? -18.514 -2.774  26.335  1.00 10.79 ? 191 TYR A CB   1 
ATOM   1542 C  CG   . TYR A 1 190 ? -18.904 -1.621  27.252  1.00 9.54  ? 191 TYR A CG   1 
ATOM   1543 C  CD1  . TYR A 1 190 ? -17.981 -1.006  28.119  1.00 10.53 ? 191 TYR A CD1  1 
ATOM   1544 C  CD2  . TYR A 1 190 ? -20.181 -1.124  27.221  1.00 10.88 ? 191 TYR A CD2  1 
ATOM   1545 C  CE1  . TYR A 1 190 ? -18.362 0.002   28.988  1.00 11.44 ? 191 TYR A CE1  1 
ATOM   1546 C  CE2  . TYR A 1 190 ? -20.560 -0.062  28.038  1.00 12.15 ? 191 TYR A CE2  1 
ATOM   1547 C  CZ   . TYR A 1 190 ? -19.677 0.491   28.927  1.00 11.52 ? 191 TYR A CZ   1 
ATOM   1548 O  OH   . TYR A 1 190 ? -20.051 1.534   29.757  1.00 12.99 ? 191 TYR A OH   1 
ATOM   1549 N  N    . TRP A 1 191 ? -16.421 -4.399  27.954  1.00 8.86  ? 192 TRP A N    1 
ATOM   1550 C  CA   . TRP A 1 191 ? -15.332 -4.134  28.894  1.00 8.83  ? 192 TRP A CA   1 
ATOM   1551 C  C    . TRP A 1 191 ? -14.667 -2.822  28.494  1.00 8.26  ? 192 TRP A C    1 
ATOM   1552 O  O    . TRP A 1 191 ? -14.660 -2.473  27.308  1.00 9.23  ? 192 TRP A O    1 
ATOM   1553 C  CB   . TRP A 1 191 ? -14.315 -5.240  28.797  1.00 9.22  ? 192 TRP A CB   1 
ATOM   1554 C  CG   . TRP A 1 191 ? -14.855 -6.567  29.208  1.00 9.26  ? 192 TRP A CG   1 
ATOM   1555 C  CD1  . TRP A 1 191 ? -15.094 -7.013  30.506  1.00 10.30 ? 192 TRP A CD1  1 
ATOM   1556 C  CD2  . TRP A 1 191 ? -15.100 -7.704  28.358  1.00 9.75  ? 192 TRP A CD2  1 
ATOM   1557 N  NE1  . TRP A 1 191 ? -15.471 -8.341  30.487  1.00 11.39 ? 192 TRP A NE1  1 
ATOM   1558 C  CE2  . TRP A 1 191 ? -15.552 -8.775  29.187  1.00 10.06 ? 192 TRP A CE2  1 
ATOM   1559 C  CE3  . TRP A 1 191 ? -15.039 -7.917  26.983  1.00 10.72 ? 192 TRP A CE3  1 
ATOM   1560 C  CZ2  . TRP A 1 191 ? -15.864 -10.050 28.653  1.00 11.27 ? 192 TRP A CZ2  1 
ATOM   1561 C  CZ3  . TRP A 1 191 ? -15.350 -9.186  26.473  1.00 10.99 ? 192 TRP A CZ3  1 
ATOM   1562 C  CH2  . TRP A 1 191 ? -15.738 -10.213 27.326  1.00 11.49 ? 192 TRP A CH2  1 
ATOM   1563 N  N    . THR A 1 192 ? -14.125 -2.125  29.461  1.00 7.96  ? 193 THR A N    1 
ATOM   1564 C  CA   . THR A 1 192 ? -13.406 -0.897  29.079  1.00 8.26  ? 193 THR A CA   1 
ATOM   1565 C  C    . THR A 1 192 ? -12.139 -0.726  29.960  1.00 8.19  ? 193 THR A C    1 
ATOM   1566 O  O    . THR A 1 192 ? -12.113 -1.168  31.120  1.00 9.14  ? 193 THR A O    1 
ATOM   1567 C  CB   . THR A 1 192 ? -14.330 0.315   29.192  1.00 7.92  ? 193 THR A CB   1 
ATOM   1568 O  OG1  . THR A 1 192 ? -13.625 1.489   28.798  1.00 9.27  ? 193 THR A OG1  1 
ATOM   1569 C  CG2  . THR A 1 192 ? -14.847 0.552   30.613  1.00 10.67 ? 193 THR A CG2  1 
ATOM   1570 N  N    . TYR A 1 193 ? -11.109 -0.168  29.358  1.00 8.05  ? 194 TYR A N    1 
ATOM   1571 C  CA   . TYR A 1 193 ? -9.885  0.108   30.102  1.00 7.86  ? 194 TYR A CA   1 
ATOM   1572 C  C    . TYR A 1 193 ? -9.112  1.154   29.322  1.00 8.97  ? 194 TYR A C    1 
ATOM   1573 O  O    . TYR A 1 193 ? -9.351  1.341   28.124  1.00 8.48  ? 194 TYR A O    1 
ATOM   1574 C  CB   . TYR A 1 193 ? -9.050  -1.156  30.240  1.00 9.17  ? 194 TYR A CB   1 
ATOM   1575 C  CG   . TYR A 1 193 ? -8.361  -1.640  28.994  1.00 7.68  ? 194 TYR A CG   1 
ATOM   1576 C  CD1  . TYR A 1 193 ? -9.022  -2.363  28.014  1.00 8.12  ? 194 TYR A CD1  1 
ATOM   1577 C  CD2  . TYR A 1 193 ? -7.040  -1.264  28.769  1.00 8.15  ? 194 TYR A CD2  1 
ATOM   1578 C  CE1  . TYR A 1 193 ? -8.412  -2.698  26.842  1.00 7.06  ? 194 TYR A CE1  1 
ATOM   1579 C  CE2  . TYR A 1 193 ? -6.388  -1.632  27.583  1.00 8.81  ? 194 TYR A CE2  1 
ATOM   1580 C  CZ   . TYR A 1 193 ? -7.064  -2.313  26.632  1.00 7.01  ? 194 TYR A CZ   1 
ATOM   1581 O  OH   . TYR A 1 193 ? -6.452  -2.592  25.462  1.00 8.64  ? 194 TYR A OH   1 
ATOM   1582 N  N    . PRO A 1 194 ? -8.194  1.888   29.995  1.00 8.44  ? 195 PRO A N    1 
ATOM   1583 C  CA   . PRO A 1 194 ? -7.359  2.893   29.310  1.00 8.83  ? 195 PRO A CA   1 
ATOM   1584 C  C    . PRO A 1 194 ? -6.183  2.205   28.630  1.00 7.21  ? 195 PRO A C    1 
ATOM   1585 O  O    . PRO A 1 194 ? -5.403  1.475   29.292  1.00 9.52  ? 195 PRO A O    1 
ATOM   1586 C  CB   . PRO A 1 194 ? -6.876  3.774   30.428  1.00 9.50  ? 195 PRO A CB   1 
ATOM   1587 C  CG   . PRO A 1 194 ? -6.855  2.838   31.693  1.00 10.28 ? 195 PRO A CG   1 
ATOM   1588 C  CD   . PRO A 1 194 ? -8.031  1.859   31.448  1.00 10.75 ? 195 PRO A CD   1 
ATOM   1589 N  N    . GLY A 1 195 ? -5.945  2.541   27.380  1.00 7.90  ? 196 GLY A N    1 
ATOM   1590 C  CA   . GLY A 1 195 ? -4.791  1.924   26.675  1.00 8.34  ? 196 GLY A CA   1 
ATOM   1591 C  C    . GLY A 1 195 ? -4.278  2.815   25.553  1.00 8.02  ? 196 GLY A C    1 
ATOM   1592 O  O    . GLY A 1 195 ? -4.161  4.048   25.714  1.00 8.37  ? 196 GLY A O    1 
ATOM   1593 N  N    . SER A 1 196 ? -3.870  2.142   24.485  1.00 7.86  ? 197 SER A N    1 
ATOM   1594 C  CA   . SER A 1 196 ? -3.041  2.807   23.471  1.00 7.77  ? 197 SER A CA   1 
ATOM   1595 C  C    . SER A 1 196 ? -3.476  2.406   22.063  1.00 5.84  ? 197 SER A C    1 
ATOM   1596 O  O    . SER A 1 196 ? -4.237  1.459   21.869  1.00 7.75  ? 197 SER A O    1 
ATOM   1597 C  CB   . SER A 1 196 ? -1.564  2.438   23.655  1.00 9.14  ? 197 SER A CB   1 
ATOM   1598 O  OG   . SER A 1 196 ? -1.332  1.056   23.224  1.00 8.67  ? 197 SER A OG   1 
ATOM   1599 N  N    . LEU A 1 197 ? -2.925  3.091   21.050  1.00 7.17  ? 198 LEU A N    1 
ATOM   1600 C  CA   . LEU A 1 197 ? -2.933  2.502   19.727  1.00 7.17  ? 198 LEU A CA   1 
ATOM   1601 C  C    . LEU A 1 197 ? -2.223  1.161   19.818  1.00 6.77  ? 198 LEU A C    1 
ATOM   1602 O  O    . LEU A 1 197 ? -1.202  1.015   20.495  1.00 8.72  ? 198 LEU A O    1 
ATOM   1603 C  CB   . LEU A 1 197 ? -2.154  3.344   18.745  1.00 9.69  ? 198 LEU A CB   1 
ATOM   1604 C  CG   . LEU A 1 197 ? -2.514  4.809   18.628  1.00 15.66 ? 198 LEU A CG   1 
ATOM   1605 C  CD1  . LEU A 1 197 ? -1.706  5.390   17.452  1.00 16.14 ? 198 LEU A CD1  1 
ATOM   1606 C  CD2  . LEU A 1 197 ? -3.799  5.369   18.702  1.00 14.12 ? 198 LEU A CD2  1 
ATOM   1607 N  N    . THR A 1 198 ? -2.707  0.207   19.000  1.00 7.14  ? 199 THR A N    1 
ATOM   1608 C  CA   . THR A 1 198 ? -1.982  -1.104  18.920  1.00 7.80  ? 199 THR A CA   1 
ATOM   1609 C  C    . THR A 1 198 ? -1.002  -1.129  17.804  1.00 7.96  ? 199 THR A C    1 
ATOM   1610 O  O    . THR A 1 198 ? -0.324  -2.140  17.636  1.00 8.24  ? 199 THR A O    1 
ATOM   1611 C  CB   . THR A 1 198 ? -3.036  -2.179  18.723  1.00 7.53  ? 199 THR A CB   1 
ATOM   1612 O  OG1  . THR A 1 198 ? -3.570  -2.111  17.489  1.00 3.34  ? 199 THR A OG1  1 
ATOM   1613 C  CG2  . THR A 1 198 ? -4.000  -2.262  19.865  1.00 12.76 ? 199 THR A CG2  1 
ATOM   1614 N  N    . THR A 1 199 ? -0.902  -0.051  17.034  1.00 10.01 ? 200 THR A N    1 
ATOM   1615 C  CA   . THR A 1 199 ? 0.089   0.048   15.960  1.00 10.36 ? 200 THR A CA   1 
ATOM   1616 C  C    . THR A 1 199 ? 0.952   1.249   16.276  1.00 10.99 ? 200 THR A C    1 
ATOM   1617 O  O    . THR A 1 199 ? 0.513   2.212   16.887  1.00 10.31 ? 200 THR A O    1 
ATOM   1618 C  CB   . THR A 1 199 ? -0.590  0.317   14.648  1.00 11.59 ? 200 THR A CB   1 
ATOM   1619 O  OG1  . THR A 1 199 ? -1.511  1.404   14.789  1.00 15.13 ? 200 THR A OG1  1 
ATOM   1620 C  CG2  . THR A 1 199 ? -1.358  -0.923  14.183  1.00 12.10 ? 200 THR A CG2  1 
ATOM   1621 N  N    . PRO A 1 200 ? 2.217   1.222   15.859  1.00 10.35 ? 201 PRO A N    1 
ATOM   1622 C  CA   . PRO A 1 200 ? 3.067   2.449   15.957  1.00 11.46 ? 201 PRO A CA   1 
ATOM   1623 C  C    . PRO A 1 200 ? 2.240   3.649   15.418  1.00 11.17 ? 201 PRO A C    1 
ATOM   1624 O  O    . PRO A 1 200 ? 1.622   3.559   14.348  1.00 12.15 ? 201 PRO A O    1 
ATOM   1625 C  CB   . PRO A 1 200 ? 4.247   2.089   15.017  1.00 10.98 ? 201 PRO A CB   1 
ATOM   1626 C  CG   . PRO A 1 200 ? 4.415   0.599   15.281  1.00 12.58 ? 201 PRO A CG   1 
ATOM   1627 C  CD   . PRO A 1 200 ? 2.967   0.102   15.236  1.00 11.59 ? 201 PRO A CD   1 
ATOM   1628 N  N    . PRO A 1 201 ? 2.323   4.792   16.088  1.00 11.66 ? 202 PRO A N    1 
ATOM   1629 C  CA   . PRO A 1 201 ? 3.257   5.143   17.184  1.00 12.62 ? 202 PRO A CA   1 
ATOM   1630 C  C    . PRO A 1 201 ? 2.865   4.709   18.583  1.00 10.64 ? 202 PRO A C    1 
ATOM   1631 O  O    . PRO A 1 201 ? 3.478   5.153   19.512  1.00 11.61 ? 202 PRO A O    1 
ATOM   1632 C  CB   . PRO A 1 201 ? 3.342   6.676   17.049  1.00 13.34 ? 202 PRO A CB   1 
ATOM   1633 C  CG   . PRO A 1 201 ? 1.977   7.101   16.489  1.00 15.34 ? 202 PRO A CG   1 
ATOM   1634 C  CD   . PRO A 1 201 ? 1.553   5.967   15.562  1.00 13.39 ? 202 PRO A CD   1 
ATOM   1635 N  N    . LEU A 1 202 ? 1.809   3.879   18.741  1.00 9.46  ? 203 LEU A N    1 
ATOM   1636 C  CA   . LEU A 1 202 ? 1.524   3.272   20.054  1.00 8.96  ? 203 LEU A CA   1 
ATOM   1637 C  C    . LEU A 1 202 ? 1.183   4.317   21.117  1.00 8.62  ? 203 LEU A C    1 
ATOM   1638 O  O    . LEU A 1 202 ? 1.324   4.055   22.294  1.00 9.54  ? 203 LEU A O    1 
ATOM   1639 C  CB   . LEU A 1 202 ? 2.682   2.405   20.529  1.00 10.09 ? 203 LEU A CB   1 
ATOM   1640 C  CG   . LEU A 1 202 ? 3.017   1.240   19.545  1.00 9.50  ? 203 LEU A CG   1 
ATOM   1641 C  CD1  . LEU A 1 202 ? 4.285   0.595   19.984  1.00 12.51 ? 203 LEU A CD1  1 
ATOM   1642 C  CD2  . LEU A 1 202 ? 1.905   0.210   19.399  1.00 11.15 ? 203 LEU A CD2  1 
ATOM   1643 N  N    . LEU A 1 203 ? 0.619   5.444   20.672  1.00 9.81  ? 204 LEU A N    1 
ATOM   1644 C  CA   . LEU A 1 203 ? 0.312   6.528   21.592  1.00 10.44 ? 204 LEU A CA   1 
ATOM   1645 C  C    . LEU A 1 203 ? -0.710  6.117   22.631  1.00 8.42  ? 204 LEU A C    1 
ATOM   1646 O  O    . LEU A 1 203 ? -1.689  5.410   22.313  1.00 9.74  ? 204 LEU A O    1 
ATOM   1647 C  CB   . LEU A 1 203 ? -0.191  7.755   20.815  1.00 10.59 ? 204 LEU A CB   1 
ATOM   1648 C  CG   . LEU A 1 203 ? 0.902   8.311   19.882  1.00 12.59 ? 204 LEU A CG   1 
ATOM   1649 C  CD1  . LEU A 1 203 ? 0.314   9.361   18.984  1.00 13.21 ? 204 LEU A CD1  1 
ATOM   1650 C  CD2  . LEU A 1 203 ? 2.052   8.964   20.706  1.00 16.18 ? 204 LEU A CD2  1 
ATOM   1651 N  N    . GLU A 1 204 ? -0.533  6.578   23.838  1.00 10.20 ? 205 GLU A N    1 
ATOM   1652 C  CA   . GLU A 1 204 ? -1.350  6.158   24.984  1.00 9.09  ? 205 GLU A CA   1 
ATOM   1653 C  C    . GLU A 1 204 ? -2.560  7.139   25.114  1.00 9.08  ? 205 GLU A C    1 
ATOM   1654 O  O    . GLU A 1 204 ? -2.661  7.922   26.074  1.00 11.88 ? 205 GLU A O    1 
ATOM   1655 C  CB   . GLU A 1 204 ? -0.538  6.017   26.271  1.00 10.59 ? 205 GLU A CB   1 
ATOM   1656 C  CG   . GLU A 1 204 ? 0.368   4.824   26.105  1.00 11.38 ? 205 GLU A CG   1 
ATOM   1657 C  CD   . GLU A 1 204 ? 1.272   4.541   27.254  1.00 11.68 ? 205 GLU A CD   1 
ATOM   1658 O  OE1  . GLU A 1 204 ? 1.634   5.468   28.002  1.00 14.92 ? 205 GLU A OE1  1 
ATOM   1659 O  OE2  . GLU A 1 204 ? 1.724   3.379   27.428  1.00 12.01 ? 205 GLU A OE2  1 
ATOM   1660 N  N    . CYS A 1 205 ? -3.442  7.078   24.156  1.00 8.52  ? 206 CYS A N    1 
ATOM   1661 C  CA   . CYS A 1 205 ? -4.503  8.031   23.985  1.00 7.64  ? 206 CYS A CA   1 
ATOM   1662 C  C    . CYS A 1 205 ? -5.855  7.414   23.864  1.00 8.61  ? 206 CYS A C    1 
ATOM   1663 O  O    . CYS A 1 205 ? -6.803  8.130   23.533  1.00 9.92  ? 206 CYS A O    1 
ATOM   1664 C  CB   . CYS A 1 205 ? -4.250  8.908   22.749  1.00 9.85  ? 206 CYS A CB   1 
ATOM   1665 S  SG   . CYS A 1 205 ? -4.158  7.930   21.222  1.00 10.77 ? 206 CYS A SG   1 
ATOM   1666 N  N    . VAL A 1 206 ? -6.010  6.118   24.098  1.00 8.24  ? 207 VAL A N    1 
ATOM   1667 C  CA   . VAL A 1 206 ? -7.251  5.404   23.791  1.00 7.83  ? 207 VAL A CA   1 
ATOM   1668 C  C    . VAL A 1 206 ? -8.014  4.966   25.004  1.00 8.11  ? 207 VAL A C    1 
ATOM   1669 O  O    . VAL A 1 206 ? -7.472  4.313   25.888  1.00 9.23  ? 207 VAL A O    1 
ATOM   1670 C  CB   . VAL A 1 206 ? -6.937  4.146   22.920  1.00 8.44  ? 207 VAL A CB   1 
ATOM   1671 C  CG1  . VAL A 1 206 ? -8.277  3.428   22.570  1.00 7.87  ? 207 VAL A CG1  1 
ATOM   1672 C  CG2  . VAL A 1 206 ? -6.161  4.537   21.652  1.00 10.41 ? 207 VAL A CG2  1 
ATOM   1673 N  N    . THR A 1 207 ? -9.296  5.263   25.058  1.00 7.65  ? 208 THR A N    1 
ATOM   1674 C  CA   . THR A 1 207 ? -10.247 4.502   25.917  1.00 7.43  ? 208 THR A CA   1 
ATOM   1675 C  C    . THR A 1 207 ? -10.789 3.365   25.087  1.00 7.08  ? 208 THR A C    1 
ATOM   1676 O  O    . THR A 1 207 ? -11.443 3.567   24.091  1.00 8.51  ? 208 THR A O    1 
ATOM   1677 C  CB   . THR A 1 207 ? -11.446 5.381   26.394  1.00 8.06  ? 208 THR A CB   1 
ATOM   1678 O  OG1  . THR A 1 207 ? -10.881 6.529   27.097  1.00 10.06 ? 208 THR A OG1  1 
ATOM   1679 C  CG2  . THR A 1 207 ? -12.328 4.544   27.255  1.00 9.69  ? 208 THR A CG2  1 
ATOM   1680 N  N    . TRP A 1 208 ? -10.396 2.153   25.489  1.00 7.43  ? 209 TRP A N    1 
ATOM   1681 C  CA   . TRP A 1 208 ? -10.822 0.959   24.795  1.00 7.51  ? 209 TRP A CA   1 
ATOM   1682 C  C    . TRP A 1 208 ? -12.196 0.515   25.281  1.00 7.48  ? 209 TRP A C    1 
ATOM   1683 O  O    . TRP A 1 208 ? -12.429 0.464   26.516  1.00 8.04  ? 209 TRP A O    1 
ATOM   1684 C  CB   . TRP A 1 208 ? -9.816  -0.183  25.012  1.00 7.14  ? 209 TRP A CB   1 
ATOM   1685 C  CG   . TRP A 1 208 ? -8.701  -0.088  24.028  1.00 6.63  ? 209 TRP A CG   1 
ATOM   1686 C  CD1  . TRP A 1 208 ? -7.466  0.556   24.187  1.00 7.78  ? 209 TRP A CD1  1 
ATOM   1687 C  CD2  . TRP A 1 208 ? -8.791  -0.472  22.658  1.00 7.45  ? 209 TRP A CD2  1 
ATOM   1688 N  NE1  . TRP A 1 208 ? -6.780  0.528   23.014  1.00 8.81  ? 209 TRP A NE1  1 
ATOM   1689 C  CE2  . TRP A 1 208 ? -7.546  -0.075  22.038  1.00 7.28  ? 209 TRP A CE2  1 
ATOM   1690 C  CE3  . TRP A 1 208 ? -9.772  -1.109  21.884  1.00 7.71  ? 209 TRP A CE3  1 
ATOM   1691 C  CZ2  . TRP A 1 208 ? -7.289  -0.307  20.697  1.00 7.19  ? 209 TRP A CZ2  1 
ATOM   1692 C  CZ3  . TRP A 1 208 ? -9.474  -1.410  20.600  1.00 7.98  ? 209 TRP A CZ3  1 
ATOM   1693 C  CH2  . TRP A 1 208 ? -8.269  -0.973  19.986  1.00 7.83  ? 209 TRP A CH2  1 
ATOM   1694 N  N    . ILE A 1 209 ? -13.078 0.190   24.352  1.00 7.17  ? 210 ILE A N    1 
ATOM   1695 C  CA   . ILE A 1 209 ? -14.393 -0.322  24.724  1.00 6.69  ? 210 ILE A CA   1 
ATOM   1696 C  C    . ILE A 1 209 ? -14.557 -1.576  23.845  1.00 6.97  ? 210 ILE A C    1 
ATOM   1697 O  O    . ILE A 1 209 ? -14.634 -1.485  22.639  1.00 7.80  ? 210 ILE A O    1 
ATOM   1698 C  CB   . ILE A 1 209 ? -15.466 0.718   24.371  1.00 8.04  ? 210 ILE A CB   1 
ATOM   1699 C  CG1  . ILE A 1 209 ? -15.245 2.003   25.172  1.00 10.03 ? 210 ILE A CG1  1 
ATOM   1700 C  CG2  . ILE A 1 209 ? -16.893 0.096   24.607  1.00 9.18  ? 210 ILE A CG2  1 
ATOM   1701 C  CD1  . ILE A 1 209 ? -16.109 3.158   24.681  1.00 11.24 ? 210 ILE A CD1  1 
ATOM   1702 N  N    . VAL A 1 210 ? -14.452 -2.740  24.511  1.00 7.34  ? 211 VAL A N    1 
ATOM   1703 C  CA   . VAL A 1 210 ? -14.429 -4.030  23.795  1.00 7.33  ? 211 VAL A CA   1 
ATOM   1704 C  C    . VAL A 1 210 ? -15.766 -4.713  24.014  1.00 7.58  ? 211 VAL A C    1 
ATOM   1705 O  O    . VAL A 1 210 ? -16.094 -5.019  25.178  1.00 8.84  ? 211 VAL A O    1 
ATOM   1706 C  CB   . VAL A 1 210 ? -13.229 -4.887  24.226  1.00 7.49  ? 211 VAL A CB   1 
ATOM   1707 C  CG1  . VAL A 1 210 ? -13.247 -6.247  23.450  1.00 8.26  ? 211 VAL A CG1  1 
ATOM   1708 C  CG2  . VAL A 1 210 ? -11.924 -4.123  23.922  1.00 8.88  ? 211 VAL A CG2  1 
ATOM   1709 N  N    . LEU A 1 211 ? -16.531 -5.007  22.956  1.00 8.42  ? 212 LEU A N    1 
ATOM   1710 C  CA   . LEU A 1 211 ? -17.839 -5.636  23.157  1.00 8.36  ? 212 LEU A CA   1 
ATOM   1711 C  C    . LEU A 1 211 ? -17.613 -7.093  23.557  1.00 8.46  ? 212 LEU A C    1 
ATOM   1712 O  O    . LEU A 1 211 ? -16.773 -7.819  22.998  1.00 9.17  ? 212 LEU A O    1 
ATOM   1713 C  CB   . LEU A 1 211 ? -18.578 -5.532  21.835  1.00 10.01 ? 212 LEU A CB   1 
ATOM   1714 C  CG   . LEU A 1 211 ? -18.957 -4.104  21.463  1.00 10.42 ? 212 LEU A CG   1 
ATOM   1715 C  CD1  . LEU A 1 211 ? -20.044 -4.223  20.301  1.00 13.60 ? 212 LEU A CD1  1 
ATOM   1716 C  CD2  . LEU A 1 211 ? -19.501 -3.294  22.634  1.00 11.40 ? 212 LEU A CD2  1 
ATOM   1717 N  N    . LYS A 1 212 ? -18.494 -7.539  24.457  1.00 10.09 ? 213 LYS A N    1 
ATOM   1718 C  CA   . LYS A 1 212 ? -18.449 -8.977  24.820  1.00 10.48 ? 213 LYS A CA   1 
ATOM   1719 C  C    . LYS A 1 212 ? -18.919 -9.914  23.770  1.00 9.69  ? 213 LYS A C    1 
ATOM   1720 O  O    . LYS A 1 212 ? -18.397 -10.993 23.630  1.00 11.66 ? 213 LYS A O    1 
ATOM   1721 C  CB   . LYS A 1 212 ? -19.301 -9.154  26.063  1.00 13.86 ? 213 LYS A CB   1 
ATOM   1722 C  CG   . LYS A 1 212 ? -19.616 -10.619 26.549  1.00 19.75 ? 213 LYS A CG   1 
ATOM   1723 C  CD   . LYS A 1 212 ? -20.917 -10.418 27.483  1.00 26.87 ? 213 LYS A CD   1 
ATOM   1724 C  CE   . LYS A 1 212 ? -22.358 -10.279 26.795  1.00 29.74 ? 213 LYS A CE   1 
ATOM   1725 N  NZ   . LYS A 1 212 ? -22.600 -9.627  25.405  1.00 25.50 ? 213 LYS A NZ   1 
ATOM   1726 N  N    . GLU A 1 213 ? -19.895 -9.515  22.965  1.00 9.07  ? 214 GLU A N    1 
ATOM   1727 C  CA   . GLU A 1 213 ? -20.452 -10.435 22.007  1.00 9.41  ? 214 GLU A CA   1 
ATOM   1728 C  C    . GLU A 1 213 ? -19.721 -10.317 20.662  1.00 9.56  ? 214 GLU A C    1 
ATOM   1729 O  O    . GLU A 1 213 ? -19.658 -9.212  20.108  1.00 9.32  ? 214 GLU A O    1 
ATOM   1730 C  CB   . GLU A 1 213 ? -21.888 -10.054 21.744  1.00 10.79 ? 214 GLU A CB   1 
ATOM   1731 C  CG   . GLU A 1 213 ? -22.601 -11.005 20.801  1.00 13.39 ? 214 GLU A CG   1 
ATOM   1732 C  CD   . GLU A 1 213 ? -24.063 -10.753 20.566  1.00 16.43 ? 214 GLU A CD   1 
ATOM   1733 O  OE1  . GLU A 1 213 ? -24.673 -9.947  21.204  1.00 15.06 ? 214 GLU A OE1  1 
ATOM   1734 O  OE2  . GLU A 1 213 ? -24.666 -11.627 19.865  1.00 25.51 ? 214 GLU A OE2  1 
ATOM   1735 N  N    . PRO A 1 214 ? -19.132 -11.409 20.178  1.00 9.38  ? 215 PRO A N    1 
ATOM   1736 C  CA   . PRO A 1 214 ? -18.536 -11.353 18.875  1.00 9.65  ? 215 PRO A CA   1 
ATOM   1737 C  C    . PRO A 1 214 ? -19.537 -11.314 17.760  1.00 10.03 ? 215 PRO A C    1 
ATOM   1738 O  O    . PRO A 1 214 ? -20.703 -11.710 17.981  1.00 12.20 ? 215 PRO A O    1 
ATOM   1739 C  CB   . PRO A 1 214 ? -17.749 -12.684 18.782  1.00 9.82  ? 215 PRO A CB   1 
ATOM   1740 C  CG   . PRO A 1 214 ? -18.560 -13.587 19.605  1.00 16.02 ? 215 PRO A CG   1 
ATOM   1741 C  CD   . PRO A 1 214 ? -19.078 -12.740 20.788  1.00 11.28 ? 215 PRO A CD   1 
ATOM   1742 N  N    . ILE A 1 215 ? -19.107 -10.888 16.578  1.00 9.85  ? 216 ILE A N    1 
ATOM   1743 C  CA   . ILE A 1 215 ? -19.914 -11.096 15.413  1.00 10.55 ? 216 ILE A CA   1 
ATOM   1744 C  C    . ILE A 1 215 ? -19.336 -12.331 14.731  1.00 10.08 ? 216 ILE A C    1 
ATOM   1745 O  O    . ILE A 1 215 ? -18.187 -12.708 14.907  1.00 11.43 ? 216 ILE A O    1 
ATOM   1746 C  CB   . ILE A 1 215 ? -19.942 -9.916  14.444  1.00 10.03 ? 216 ILE A CB   1 
ATOM   1747 C  CG1  . ILE A 1 215 ? -18.509 -9.529  14.008  1.00 12.06 ? 216 ILE A CG1  1 
ATOM   1748 C  CG2  . ILE A 1 215 ? -20.660 -8.734  15.148  1.00 12.67 ? 216 ILE A CG2  1 
ATOM   1749 C  CD1  . ILE A 1 215 ? -18.546 -8.579  12.740  1.00 13.08 ? 216 ILE A CD1  1 
ATOM   1750 N  N    A SER A 1 216 ? -20.216 -13.083 14.079  0.50 10.66 ? 217 SER A N    1 
ATOM   1751 N  N    B SER A 1 216 ? -20.212 -12.931 13.929  0.50 10.24 ? 217 SER A N    1 
ATOM   1752 C  CA   A SER A 1 216 ? -19.675 -14.148 13.215  0.50 11.93 ? 217 SER A CA   1 
ATOM   1753 C  CA   B SER A 1 216 ? -19.881 -14.108 13.131  0.50 10.30 ? 217 SER A CA   1 
ATOM   1754 C  C    A SER A 1 216 ? -19.552 -13.670 11.804  0.50 11.66 ? 217 SER A C    1 
ATOM   1755 C  C    B SER A 1 216 ? -19.652 -13.752 11.685  0.50 10.68 ? 217 SER A C    1 
ATOM   1756 O  O    A SER A 1 216 ? -20.376 -12.866 11.342  0.50 11.91 ? 217 SER A O    1 
ATOM   1757 O  O    B SER A 1 216 ? -20.509 -13.110 11.058  0.50 11.48 ? 217 SER A O    1 
ATOM   1758 C  CB   A SER A 1 216 ? -20.452 -15.440 13.229  0.50 13.36 ? 217 SER A CB   1 
ATOM   1759 C  CB   B SER A 1 216 ? -21.008 -15.116 13.201  0.50 9.80  ? 217 SER A CB   1 
ATOM   1760 O  OG   A SER A 1 216 ? -21.781 -15.197 12.858  0.50 17.09 ? 217 SER A OG   1 
ATOM   1761 O  OG   B SER A 1 216 ? -20.950 -15.844 14.440  0.50 14.61 ? 217 SER A OG   1 
ATOM   1762 N  N    . VAL A 1 217 ? -18.510 -14.167 11.144  1.00 10.49 ? 218 VAL A N    1 
ATOM   1763 C  CA   . VAL A 1 217 ? -18.239 -13.932 9.716   1.00 10.55 ? 218 VAL A CA   1 
ATOM   1764 C  C    . VAL A 1 217 ? -17.977 -15.311 9.086   1.00 11.19 ? 218 VAL A C    1 
ATOM   1765 O  O    . VAL A 1 217 ? -17.582 -16.267 9.787   1.00 12.51 ? 218 VAL A O    1 
ATOM   1766 C  CB   . VAL A 1 217 ? -17.059 -12.986 9.506   1.00 11.97 ? 218 VAL A CB   1 
ATOM   1767 C  CG1  . VAL A 1 217 ? -17.302 -11.701 10.240  1.00 12.31 ? 218 VAL A CG1  1 
ATOM   1768 C  CG2  . VAL A 1 217 ? -15.749 -13.646 9.968   1.00 13.75 ? 218 VAL A CG2  1 
ATOM   1769 N  N    . SER A 1 218 ? -18.145 -15.446 7.783   1.00 11.97 ? 219 SER A N    1 
ATOM   1770 C  CA   . SER A 1 218 ? -17.941 -16.794 7.230   1.00 12.20 ? 219 SER A CA   1 
ATOM   1771 C  C    . SER A 1 218 ? -16.477 -17.050 6.930   1.00 11.30 ? 219 SER A C    1 
ATOM   1772 O  O    . SER A 1 218 ? -15.650 -16.128 6.825   1.00 11.71 ? 219 SER A O    1 
ATOM   1773 C  CB   . SER A 1 218 ? -18.726 -16.965 5.944   1.00 12.34 ? 219 SER A CB   1 
ATOM   1774 O  OG   . SER A 1 218 ? -18.272 -16.087 4.960   1.00 13.72 ? 219 SER A OG   1 
ATOM   1775 N  N    . SER A 1 219 ? -16.128 -18.292 6.753   1.00 12.10 ? 220 SER A N    1 
ATOM   1776 C  CA   . SER A 1 219 ? -14.764 -18.668 6.390   1.00 13.79 ? 220 SER A CA   1 
ATOM   1777 C  C    . SER A 1 219 ? -14.422 -18.010 5.035   1.00 13.41 ? 220 SER A C    1 
ATOM   1778 O  O    . SER A 1 219 ? -13.307 -17.512 4.890   1.00 14.43 ? 220 SER A O    1 
ATOM   1779 C  CB   . SER A 1 219 ? -14.655 -20.212 6.343   1.00 16.76 ? 220 SER A CB   1 
ATOM   1780 O  OG   . SER A 1 219 ? -15.601 -20.788 5.470   1.00 20.74 ? 220 SER A OG   1 
ATOM   1781 N  N    . GLU A 1 220 ? -15.394 -17.866 4.113   1.00 13.54 ? 221 GLU A N    1 
ATOM   1782 C  CA   . GLU A 1 220 ? -15.069 -17.217 2.867   1.00 14.54 ? 221 GLU A CA   1 
ATOM   1783 C  C    . GLU A 1 220 ? -14.780 -15.724 3.056   1.00 14.06 ? 221 GLU A C    1 
ATOM   1784 O  O    . GLU A 1 220 ? -13.909 -15.182 2.377   1.00 14.64 ? 221 GLU A O    1 
ATOM   1785 C  CB   . GLU A 1 220 ? -16.167 -17.332 1.826   1.00 16.50 ? 221 GLU A CB   1 
ATOM   1786 C  CG   . GLU A 1 220 ? -16.366 -18.777 1.338   1.00 19.49 ? 221 GLU A CG   1 
ATOM   1787 C  CD   . GLU A 1 220 ? -17.341 -19.536 2.244   1.00 20.01 ? 221 GLU A CD   1 
ATOM   1788 O  OE1  . GLU A 1 220 ? -17.859 -19.080 3.275   1.00 18.97 ? 221 GLU A OE1  1 
ATOM   1789 O  OE2  . GLU A 1 220 ? -17.628 -20.714 1.946   1.00 29.42 ? 221 GLU A OE2  1 
ATOM   1790 N  N    . GLN A 1 221 ? -15.494 -15.076 3.960   1.00 12.52 ? 222 GLN A N    1 
ATOM   1791 C  CA   . GLN A 1 221 ? -15.216 -13.632 4.172   1.00 11.92 ? 222 GLN A CA   1 
ATOM   1792 C  C    . GLN A 1 221 ? -13.793 -13.441 4.724   1.00 12.42 ? 222 GLN A C    1 
ATOM   1793 O  O    . GLN A 1 221 ? -13.052 -12.575 4.240   1.00 12.77 ? 222 GLN A O    1 
ATOM   1794 C  CB   . GLN A 1 221 ? -16.210 -13.112 5.117   1.00 12.50 ? 222 GLN A CB   1 
ATOM   1795 C  CG   . GLN A 1 221 ? -17.593 -12.985 4.400   1.00 12.61 ? 222 GLN A CG   1 
ATOM   1796 C  CD   . GLN A 1 221 ? -18.696 -12.456 5.300   1.00 11.54 ? 222 GLN A CD   1 
ATOM   1797 O  OE1  . GLN A 1 221 ? -18.835 -12.835 6.472   1.00 11.93 ? 222 GLN A OE1  1 
ATOM   1798 N  NE2  . GLN A 1 221 ? -19.532 -11.583 4.732   1.00 12.28 ? 222 GLN A NE2  1 
ATOM   1799 N  N    . VAL A 1 222 ? -13.420 -14.238 5.731   1.00 12.14 ? 223 VAL A N    1 
ATOM   1800 C  CA   . VAL A 1 222 ? -12.066 -14.007 6.312   1.00 12.76 ? 223 VAL A CA   1 
ATOM   1801 C  C    . VAL A 1 222 ? -10.967 -14.470 5.319   1.00 13.09 ? 223 VAL A C    1 
ATOM   1802 O  O    . VAL A 1 222 ? -9.865  -13.866 5.245   1.00 13.75 ? 223 VAL A O    1 
ATOM   1803 C  CB   . VAL A 1 222 ? -11.938 -14.566 7.755   1.00 14.97 ? 223 VAL A CB   1 
ATOM   1804 C  CG1  . VAL A 1 222 ? -11.953 -16.040 7.746   1.00 18.46 ? 223 VAL A CG1  1 
ATOM   1805 C  CG2  . VAL A 1 222 ? -10.665 -14.080 8.425   1.00 16.08 ? 223 VAL A CG2  1 
ATOM   1806 N  N    . LEU A 1 223 ? -11.264 -15.468 4.502   1.00 13.59 ? 224 LEU A N    1 
ATOM   1807 C  CA   . LEU A 1 223 ? -10.305 -15.856 3.472   1.00 15.81 ? 224 LEU A CA   1 
ATOM   1808 C  C    . LEU A 1 223 ? -9.954  -14.696 2.560   1.00 15.32 ? 224 LEU A C    1 
ATOM   1809 O  O    . LEU A 1 223 ? -8.769  -14.516 2.164   1.00 16.65 ? 224 LEU A O    1 
ATOM   1810 C  CB   . LEU A 1 223 ? -10.810 -17.075 2.656   1.00 17.87 ? 224 LEU A CB   1 
ATOM   1811 C  CG   . LEU A 1 223 ? -10.639 -18.377 3.452   0.50 18.32 ? 224 LEU A CG   1 
ATOM   1812 C  CD1  . LEU A 1 223 ? -11.542 -19.579 2.941   0.50 20.95 ? 224 LEU A CD1  1 
ATOM   1813 C  CD2  . LEU A 1 223 ? -9.107  -18.734 3.605   0.50 19.64 ? 224 LEU A CD2  1 
ATOM   1814 N  N    . LYS A 1 224 ? -10.955 -13.868 2.245   1.00 14.59 ? 225 LYS A N    1 
ATOM   1815 C  CA   . LYS A 1 224 ? -10.701 -12.715 1.360   1.00 14.80 ? 225 LYS A CA   1 
ATOM   1816 C  C    . LYS A 1 224 ? -9.837  -11.700 2.042   1.00 13.41 ? 225 LYS A C    1 
ATOM   1817 O  O    . LYS A 1 224 ? -9.015  -11.105 1.401   1.00 14.58 ? 225 LYS A O    1 
ATOM   1818 C  CB   . LYS A 1 224 ? -12.022 -12.197 0.820   1.00 16.57 ? 225 LYS A CB   1 
ATOM   1819 C  CG   . LYS A 1 224 ? -12.607 -13.246 -0.248  1.00 21.71 ? 225 LYS A CG   1 
ATOM   1820 C  CD   . LYS A 1 224 ? -13.995 -12.977 -0.824  1.00 28.49 ? 225 LYS A CD   1 
ATOM   1821 C  CE   . LYS A 1 224 ? -14.514 -14.133 -1.845  1.00 31.91 ? 225 LYS A CE   1 
ATOM   1822 N  NZ   . LYS A 1 224 ? -15.837 -13.855 -2.602  1.00 30.90 ? 225 LYS A NZ   1 
ATOM   1823 N  N    . PHE A 1 225 ? -9.956  -11.528 3.352   1.00 12.09 ? 226 PHE A N    1 
ATOM   1824 C  CA   . PHE A 1 225 ? -9.018  -10.660 4.070   1.00 11.47 ? 226 PHE A CA   1 
ATOM   1825 C  C    . PHE A 1 225 ? -7.601  -11.145 3.820   1.00 11.76 ? 226 PHE A C    1 
ATOM   1826 O  O    . PHE A 1 225 ? -6.653  -10.378 3.660   1.00 12.74 ? 226 PHE A O    1 
ATOM   1827 C  CB   . PHE A 1 225 ? -9.218  -10.693 5.590   1.00 11.23 ? 226 PHE A CB   1 
ATOM   1828 C  CG   . PHE A 1 225 ? -10.439 -9.918  6.120   1.00 11.48 ? 226 PHE A CG   1 
ATOM   1829 C  CD1  . PHE A 1 225 ? -11.481 -9.488  5.338   1.00 15.55 ? 226 PHE A CD1  1 
ATOM   1830 C  CD2  . PHE A 1 225 ? -10.553 -9.734  7.541   1.00 14.55 ? 226 PHE A CD2  1 
ATOM   1831 C  CE1  . PHE A 1 225 ? -12.595 -8.777  5.945   1.00 15.05 ? 226 PHE A CE1  1 
ATOM   1832 C  CE2  . PHE A 1 225 ? -11.642 -9.057  8.140   1.00 16.29 ? 226 PHE A CE2  1 
ATOM   1833 C  CZ   . PHE A 1 225 ? -12.633 -8.537  7.324   1.00 15.45 ? 226 PHE A CZ   1 
ATOM   1834 N  N    . ARG A 1 226 ? -7.446  -12.452 3.886   1.00 11.52 ? 227 ARG A N    1 
ATOM   1835 C  CA   . ARG A 1 226 ? -6.101  -13.077 3.796   1.00 12.27 ? 227 ARG A CA   1 
ATOM   1836 C  C    . ARG A 1 226 ? -5.503  -13.055 2.396   1.00 12.83 ? 227 ARG A C    1 
ATOM   1837 O  O    . ARG A 1 226 ? -4.338  -13.404 2.262   1.00 14.79 ? 227 ARG A O    1 
ATOM   1838 C  CB   . ARG A 1 226 ? -6.133  -14.515 4.332   1.00 12.94 ? 227 ARG A CB   1 
ATOM   1839 C  CG   . ARG A 1 226 ? -6.549  -14.648 5.779   1.00 12.25 ? 227 ARG A CG   1 
ATOM   1840 C  CD   . ARG A 1 226 ? -6.508  -16.103 6.212   1.00 15.11 ? 227 ARG A CD   1 
ATOM   1841 N  NE   . ARG A 1 226 ? -7.048  -16.234 7.555   1.00 13.13 ? 227 ARG A NE   1 
ATOM   1842 C  CZ   . ARG A 1 226 ? -7.960  -17.119 7.944   1.00 12.42 ? 227 ARG A CZ   1 
ATOM   1843 N  NH1  . ARG A 1 226 ? -8.410  -18.037 7.079   1.00 17.17 ? 227 ARG A NH1  1 
ATOM   1844 N  NH2  . ARG A 1 226 ? -8.437  -17.086 9.168   1.00 14.86 ? 227 ARG A NH2  1 
ATOM   1845 N  N    . LYS A 1 227 ? -6.233  -12.577 1.400   1.00 13.75 ? 228 LYS A N    1 
ATOM   1846 C  CA   . LYS A 1 227 ? -5.658  -12.409 0.085   1.00 14.62 ? 228 LYS A CA   1 
ATOM   1847 C  C    . LYS A 1 227 ? -5.073  -11.056 -0.176  1.00 13.24 ? 228 LYS A C    1 
ATOM   1848 O  O    . LYS A 1 227 ? -4.428  -10.846 -1.189  1.00 16.05 ? 228 LYS A O    1 
ATOM   1849 C  CB   . LYS A 1 227 ? -6.742  -12.677 -0.961  1.00 17.66 ? 228 LYS A CB   1 
ATOM   1850 C  CG   . LYS A 1 227 ? -7.124  -14.150 -1.018  1.00 20.97 ? 228 LYS A CG   1 
ATOM   1851 C  CD   . LYS A 1 227 ? -8.181  -14.431 -2.084  1.00 28.57 ? 228 LYS A CD   1 
ATOM   1852 C  CE   . LYS A 1 227 ? -8.857  -15.829 -1.790  1.00 33.21 ? 228 LYS A CE   1 
ATOM   1853 N  NZ   . LYS A 1 227 ? -9.137  -16.699 -2.985  1.00 36.74 ? 228 LYS A NZ   1 
ATOM   1854 N  N    . LEU A 1 228 ? -5.302  -10.114 0.747   1.00 12.51 ? 229 LEU A N    1 
ATOM   1855 C  CA   . LEU A 1 228 ? -4.678  -8.836  0.653   1.00 12.94 ? 229 LEU A CA   1 
ATOM   1856 C  C    . LEU A 1 228 ? -3.180  -8.993  0.799   1.00 13.98 ? 229 LEU A C    1 
ATOM   1857 O  O    . LEU A 1 228 ? -2.678  -10.034 1.226   1.00 13.94 ? 229 LEU A O    1 
ATOM   1858 C  CB   . LEU A 1 228 ? -5.193  -7.933  1.771   1.00 12.58 ? 229 LEU A CB   1 
ATOM   1859 C  CG   . LEU A 1 228 ? -6.629  -7.485  1.600   1.00 13.07 ? 229 LEU A CG   1 
ATOM   1860 C  CD1  . LEU A 1 228 ? -7.142  -6.869  2.873   1.00 14.17 ? 229 LEU A CD1  1 
ATOM   1861 C  CD2  . LEU A 1 228 ? -6.675  -6.468  0.443   1.00 15.78 ? 229 LEU A CD2  1 
ATOM   1862 N  N    . ASN A 1 229 ? -2.463  -7.943  0.422   1.00 14.93 ? 230 ASN A N    1 
ATOM   1863 C  CA   . ASN A 1 229 ? -1.010  -7.895  0.453   1.00 14.81 ? 230 ASN A CA   1 
ATOM   1864 C  C    . ASN A 1 229 ? -0.480  -6.761  1.317   1.00 14.80 ? 230 ASN A C    1 
ATOM   1865 O  O    . ASN A 1 229 ? -0.998  -5.641  1.247   1.00 16.22 ? 230 ASN A O    1 
ATOM   1866 C  CB   . ASN A 1 229 ? -0.460  -7.665  -0.980  1.00 15.09 ? 230 ASN A CB   1 
ATOM   1867 C  CG   . ASN A 1 229 ? -0.483  -8.894  -1.909  1.00 16.00 ? 230 ASN A CG   1 
ATOM   1868 O  OD1  . ASN A 1 229 ? 0.057   -8.760  -3.010  1.00 21.03 ? 230 ASN A OD1  1 
ATOM   1869 N  ND2  . ASN A 1 229 ? -1.086  -10.029 -1.514  1.00 16.53 ? 230 ASN A ND2  1 
ATOM   1870 N  N    . PHE A 1 230 ? 0.594   -7.066  2.065   1.00 14.34 ? 231 PHE A N    1 
ATOM   1871 C  CA   . PHE A 1 230 ? 1.255   -5.993  2.753   1.00 14.81 ? 231 PHE A CA   1 
ATOM   1872 C  C    . PHE A 1 230 ? 2.142   -5.184  1.766   1.00 17.17 ? 231 PHE A C    1 
ATOM   1873 O  O    . PHE A 1 230 ? 2.408   -3.989  2.002   1.00 17.74 ? 231 PHE A O    1 
ATOM   1874 C  CB   . PHE A 1 230 ? 2.250   -6.555  3.716   1.00 15.03 ? 231 PHE A CB   1 
ATOM   1875 C  CG   . PHE A 1 230 ? 1.672   -7.177  4.994   1.00 15.40 ? 231 PHE A CG   1 
ATOM   1876 C  CD1  . PHE A 1 230 ? 0.900   -6.424  5.881   1.00 14.36 ? 231 PHE A CD1  1 
ATOM   1877 C  CD2  . PHE A 1 230 ? 2.040   -8.469  5.361   1.00 15.37 ? 231 PHE A CD2  1 
ATOM   1878 C  CE1  . PHE A 1 230 ? 0.475   -6.982  7.093   1.00 14.01 ? 231 PHE A CE1  1 
ATOM   1879 C  CE2  . PHE A 1 230 ? 1.600   -9.047  6.597   1.00 16.21 ? 231 PHE A CE2  1 
ATOM   1880 C  CZ   . PHE A 1 230 ? 0.849   -8.297  7.493   1.00 14.88 ? 231 PHE A CZ   1 
ATOM   1881 N  N    . ASN A 1 231 ? 2.696   -5.849  0.764   1.00 15.04 ? 232 ASN A N    1 
ATOM   1882 C  CA   . ASN A 1 231 ? 3.520   -5.205  -0.271  1.00 16.24 ? 232 ASN A CA   1 
ATOM   1883 C  C    . ASN A 1 231 ? 2.773   -4.278  -1.212  1.00 17.29 ? 232 ASN A C    1 
ATOM   1884 O  O    . ASN A 1 231 ? 1.547   -4.418  -1.396  1.00 17.82 ? 232 ASN A O    1 
ATOM   1885 C  CB   . ASN A 1 231 ? 4.179   -6.267  -1.075  1.00 16.91 ? 232 ASN A CB   1 
ATOM   1886 C  CG   . ASN A 1 231 ? 3.194   -7.165  -1.665  1.00 15.25 ? 232 ASN A CG   1 
ATOM   1887 O  OD1  . ASN A 1 231 ? 2.700   -8.082  -0.989  1.00 17.70 ? 232 ASN A OD1  1 
ATOM   1888 N  ND2  . ASN A 1 231 ? 2.900   -6.958  -2.960  1.00 19.71 ? 232 ASN A ND2  1 
ATOM   1889 N  N    . GLY A 1 232 ? 3.547   -3.380  -1.870  1.00 17.77 ? 233 GLY A N    1 
ATOM   1890 C  CA   . GLY A 1 232 ? 2.975   -2.625  -2.967  1.00 18.28 ? 233 GLY A CA   1 
ATOM   1891 C  C    . GLY A 1 232 ? 2.962   -3.418  -4.247  1.00 18.09 ? 233 GLY A C    1 
ATOM   1892 O  O    . GLY A 1 232 ? 3.615   -4.474  -4.350  1.00 18.58 ? 233 GLY A O    1 
ATOM   1893 N  N    . GLU A 1 233 ? 2.207   -2.931  -5.237  1.00 17.96 ? 234 GLU A N    1 
ATOM   1894 C  CA   . GLU A 1 233 ? 2.153   -3.523  -6.557  1.00 19.36 ? 234 GLU A CA   1 
ATOM   1895 C  C    . GLU A 1 233 ? 3.538   -3.591  -7.171  1.00 18.84 ? 234 GLU A C    1 
ATOM   1896 O  O    . GLU A 1 233 ? 4.341   -2.683  -7.035  1.00 20.42 ? 234 GLU A O    1 
ATOM   1897 C  CB   . GLU A 1 233 ? 1.200   -2.687  -7.431  1.00 18.54 ? 234 GLU A CB   1 
ATOM   1898 C  CG   . GLU A 1 233 ? 0.874   -3.341  -8.774  1.00 19.11 ? 234 GLU A CG   1 
ATOM   1899 C  CD   . GLU A 1 233 ? 0.020   -2.452  -9.630  1.00 27.42 ? 234 GLU A CD   1 
ATOM   1900 O  OE1  . GLU A 1 233 ? -0.277  -1.270  -9.229  1.00 26.88 ? 234 GLU A OE1  1 
ATOM   1901 O  OE2  . GLU A 1 233 ? -0.328  -2.943  -10.734 1.00 27.63 ? 234 GLU A OE2  1 
ATOM   1902 N  N    . GLY A 1 234 ? 3.822   -4.723  -7.800  1.00 20.34 ? 235 GLY A N    1 
ATOM   1903 C  CA   . GLY A 1 234 ? 5.123   -4.833  -8.449  1.00 23.10 ? 235 GLY A CA   1 
ATOM   1904 C  C    . GLY A 1 234 ? 6.228   -5.241  -7.485  1.00 22.60 ? 235 GLY A C    1 
ATOM   1905 O  O    . GLY A 1 234 ? 7.474   -5.278  -7.829  1.00 24.95 ? 235 GLY A O    1 
ATOM   1906 N  N    . GLU A 1 235 ? 5.824   -5.620  -6.261  1.00 22.66 ? 236 GLU A N    1 
ATOM   1907 C  CA   . GLU A 1 235 ? 6.794   -6.162  -5.255  1.00 22.38 ? 236 GLU A CA   1 
ATOM   1908 C  C    . GLU A 1 235 ? 6.458   -7.613  -4.937  1.00 24.51 ? 236 GLU A C    1 
ATOM   1909 O  O    . GLU A 1 235 ? 5.331   -8.034  -5.250  1.00 25.58 ? 236 GLU A O    1 
ATOM   1910 C  CB   . GLU A 1 235 ? 6.755   -5.379  -3.938  1.00 22.54 ? 236 GLU A CB   1 
ATOM   1911 C  CG   . GLU A 1 235 ? 7.147   -3.933  -4.084  1.00 22.50 ? 236 GLU A CG   1 
ATOM   1912 C  CD   . GLU A 1 235 ? 6.884   -3.074  -2.835  1.00 31.11 ? 236 GLU A CD   1 
ATOM   1913 O  OE1  . GLU A 1 235 ? 6.346   -3.551  -1.796  1.00 32.50 ? 236 GLU A OE1  1 
ATOM   1914 O  OE2  . GLU A 1 235 ? 7.247   -1.877  -2.892  1.00 39.06 ? 236 GLU A OE2  1 
ATOM   1915 N  N    . PRO A 1 236 ? 7.422   -8.383  -4.355  1.00 23.34 ? 237 PRO A N    1 
ATOM   1916 C  CA   . PRO A 1 236 ? 7.186   -9.775  -4.010  1.00 23.85 ? 237 PRO A CA   1 
ATOM   1917 C  C    . PRO A 1 236 ? 5.899   -9.861  -3.132  1.00 22.29 ? 237 PRO A C    1 
ATOM   1918 O  O    . PRO A 1 236 ? 5.699   -9.058  -2.214  1.00 20.98 ? 237 PRO A O    1 
ATOM   1919 C  CB   . PRO A 1 236 ? 8.445   -10.132 -3.222  1.00 24.53 ? 237 PRO A CB   1 
ATOM   1920 C  CG   . PRO A 1 236 ? 9.524   -9.316  -3.820  1.00 24.65 ? 237 PRO A CG   1 
ATOM   1921 C  CD   . PRO A 1 236 ? 8.830   -7.981  -4.076  1.00 25.32 ? 237 PRO A CD   1 
ATOM   1922 N  N    . GLU A 1 237 ? 5.057   -10.835 -3.400  1.00 21.45 ? 238 GLU A N    1 
ATOM   1923 C  CA   . GLU A 1 237 ? 3.820   -10.925 -2.657  1.00 19.33 ? 238 GLU A CA   1 
ATOM   1924 C  C    . GLU A 1 237 ? 4.061   -11.426 -1.208  1.00 18.25 ? 238 GLU A C    1 
ATOM   1925 O  O    . GLU A 1 237 ? 4.608   -12.501 -0.989  1.00 18.51 ? 238 GLU A O    1 
ATOM   1926 C  CB   . GLU A 1 237 ? 2.832   -11.875 -3.341  1.00 20.69 ? 238 GLU A CB   1 
ATOM   1927 C  CG   . GLU A 1 237 ? 1.542   -11.998 -2.567  1.00 22.85 ? 238 GLU A CG   1 
ATOM   1928 C  CD   . GLU A 1 237 ? 0.412   -12.682 -3.325  1.00 24.03 ? 238 GLU A CD   1 
ATOM   1929 O  OE1  . GLU A 1 237 ? 0.734   -13.648 -4.077  1.00 30.25 ? 238 GLU A OE1  1 
ATOM   1930 O  OE2  . GLU A 1 237 ? -0.766  -12.245 -3.238  1.00 22.39 ? 238 GLU A OE2  1 
ATOM   1931 N  N    A GLU A 1 238 ? 3.634   -10.665 -0.207  0.50 17.68 ? 239 GLU A N    1 
ATOM   1932 N  N    B GLU A 1 238 ? 3.487   -10.662 -0.267  0.50 16.42 ? 239 GLU A N    1 
ATOM   1933 C  CA   A GLU A 1 238 ? 3.591   -11.143 1.170   0.50 17.58 ? 239 GLU A CA   1 
ATOM   1934 C  CA   B GLU A 1 238 ? 3.531   -10.889 1.175   0.50 16.59 ? 239 GLU A CA   1 
ATOM   1935 C  C    A GLU A 1 238 ? 2.128   -10.892 1.555   0.50 15.58 ? 239 GLU A C    1 
ATOM   1936 C  C    B GLU A 1 238 ? 2.094   -10.826 1.686   0.50 14.17 ? 239 GLU A C    1 
ATOM   1937 O  O    A GLU A 1 238 ? 1.588   -9.791  1.380   0.50 16.64 ? 239 GLU A O    1 
ATOM   1938 O  O    B GLU A 1 238 ? 1.545   -9.727  1.841   0.50 14.71 ? 239 GLU A O    1 
ATOM   1939 C  CB   A GLU A 1 238 ? 4.592   -10.416 2.088   0.50 17.91 ? 239 GLU A CB   1 
ATOM   1940 C  CB   B GLU A 1 238 ? 4.281   -9.771  1.882   0.50 16.51 ? 239 GLU A CB   1 
ATOM   1941 C  CG   A GLU A 1 238 ? 4.561   -8.902  1.929   0.01 16.97 ? 239 GLU A CG   1 
ATOM   1942 C  CG   B GLU A 1 238 ? 5.699   -9.529  1.399   0.01 15.51 ? 239 GLU A CG   1 
ATOM   1943 C  CD   A GLU A 1 238 ? 5.659   -8.199  2.704   0.01 16.41 ? 239 GLU A CD   1 
ATOM   1944 C  CD   B GLU A 1 238 ? 6.397   -8.439  2.191   0.01 14.56 ? 239 GLU A CD   1 
ATOM   1945 O  OE1  A GLU A 1 238 ? 6.406   -7.411  2.087   0.01 15.94 ? 239 GLU A OE1  1 
ATOM   1946 O  OE1  B GLU A 1 238 ? 6.464   -7.294  1.698   0.01 13.99 ? 239 GLU A OE1  1 
ATOM   1947 O  OE2  A GLU A 1 238 ? 5.775   -8.432  3.926   0.01 16.23 ? 239 GLU A OE2  1 
ATOM   1948 O  OE2  B GLU A 1 238 ? 6.863   -8.721  3.315   0.01 14.11 ? 239 GLU A OE2  1 
ATOM   1949 N  N    . LEU A 1 239 ? 1.462   -11.986 1.932   1.00 15.16 ? 240 LEU A N    1 
ATOM   1950 C  CA   . LEU A 1 239 ? 0.032   -11.942 2.254   1.00 14.32 ? 240 LEU A CA   1 
ATOM   1951 C  C    . LEU A 1 239 ? -0.129  -11.135 3.546   1.00 12.62 ? 240 LEU A C    1 
ATOM   1952 O  O    . LEU A 1 239 ? 0.637   -11.303 4.535   1.00 14.64 ? 240 LEU A O    1 
ATOM   1953 C  CB   . LEU A 1 239 ? -0.498  -13.348 2.489   1.00 14.77 ? 240 LEU A CB   1 
ATOM   1954 C  CG   . LEU A 1 239 ? -0.595  -14.215 1.217   1.00 14.99 ? 240 LEU A CG   1 
ATOM   1955 C  CD1  . LEU A 1 239 ? -1.263  -15.552 1.656   1.00 18.18 ? 240 LEU A CD1  1 
ATOM   1956 C  CD2  . LEU A 1 239 ? -1.307  -13.509 0.086   1.00 17.64 ? 240 LEU A CD2  1 
ATOM   1957 N  N    . MET A 1 240 ? -1.172  -10.314 3.544   1.00 11.78 ? 241 MET A N    1 
ATOM   1958 C  CA   . MET A 1 240 ? -1.523  -9.522  4.718   1.00 12.41 ? 241 MET A CA   1 
ATOM   1959 C  C    . MET A 1 240 ? -2.324  -10.437 5.643   1.00 12.10 ? 241 MET A C    1 
ATOM   1960 O  O    . MET A 1 240 ? -3.510  -10.617 5.521   1.00 12.64 ? 241 MET A O    1 
ATOM   1961 C  CB   . MET A 1 240 ? -2.341  -8.326  4.284   1.00 13.08 ? 241 MET A CB   1 
ATOM   1962 C  CG   . MET A 1 240 ? -2.729  -7.376  5.480   1.00 12.33 ? 241 MET A CG   1 
ATOM   1963 S  SD   . MET A 1 240 ? -3.669  -5.966  4.968   1.00 14.12 ? 241 MET A SD   1 
ATOM   1964 C  CE   . MET A 1 240 ? -2.360  -4.908  4.315   1.00 14.97 ? 241 MET A CE   1 
ATOM   1965 N  N    . VAL A 1 241 ? -1.548  -11.044 6.528   1.00 10.86 ? 242 VAL A N    1 
ATOM   1966 C  CA   . VAL A 1 241 ? -2.093  -11.914 7.584   1.00 10.54 ? 242 VAL A CA   1 
ATOM   1967 C  C    . VAL A 1 241 ? -1.305  -11.747 8.854   1.00 10.97 ? 242 VAL A C    1 
ATOM   1968 O  O    . VAL A 1 241 ? -0.131  -11.348 8.809   1.00 11.00 ? 242 VAL A O    1 
ATOM   1969 C  CB   . VAL A 1 241 ? -2.031  -13.442 7.214   1.00 11.40 ? 242 VAL A CB   1 
ATOM   1970 C  CG1  . VAL A 1 241 ? -2.952  -13.736 6.010   1.00 12.79 ? 242 VAL A CG1  1 
ATOM   1971 C  CG2  . VAL A 1 241 ? -0.555  -13.917 6.944   1.00 12.66 ? 242 VAL A CG2  1 
ATOM   1972 N  N    . ASP A 1 242 ? -1.915  -12.064 9.991   1.00 9.60  ? 243 ASP A N    1 
ATOM   1973 C  CA   . ASP A 1 242 ? -1.230  -11.926 11.281  1.00 9.55  ? 243 ASP A CA   1 
ATOM   1974 C  C    . ASP A 1 242 ? -0.725  -10.520 11.534  1.00 8.86  ? 243 ASP A C    1 
ATOM   1975 O  O    . ASP A 1 242 ? 0.337   -10.274 12.032  1.00 10.81 ? 243 ASP A O    1 
ATOM   1976 C  CB   . ASP A 1 242 ? -0.146  -12.976 11.450  1.00 9.98  ? 243 ASP A CB   1 
ATOM   1977 C  CG   . ASP A 1 242 ? -0.717  -14.369 11.562  1.00 10.52 ? 243 ASP A CG   1 
ATOM   1978 O  OD1  . ASP A 1 242 ? -1.785  -14.565 12.208  1.00 10.83 ? 243 ASP A OD1  1 
ATOM   1979 O  OD2  . ASP A 1 242 ? -0.061  -15.271 10.997  1.00 12.60 ? 243 ASP A OD2  1 
ATOM   1980 N  N    . ASN A 1 243 ? -1.645  -9.595  11.242  1.00 8.44  ? 244 ASN A N    1 
ATOM   1981 C  CA   . ASN A 1 243 ? -1.382  -8.179  11.452  1.00 9.29  ? 244 ASN A CA   1 
ATOM   1982 C  C    . ASN A 1 243 ? -1.932  -7.753  12.816  1.00 8.38  ? 244 ASN A C    1 
ATOM   1983 O  O    . ASN A 1 243 ? -2.584  -6.695  12.925  1.00 9.56  ? 244 ASN A O    1 
ATOM   1984 C  CB   . ASN A 1 243 ? -1.920  -7.311  10.307  1.00 9.62  ? 244 ASN A CB   1 
ATOM   1985 C  CG   . ASN A 1 243 ? -3.397  -7.442  10.103  1.00 9.92  ? 244 ASN A CG   1 
ATOM   1986 O  OD1  . ASN A 1 243 ? -4.041  -8.321  10.677  1.00 10.58 ? 244 ASN A OD1  1 
ATOM   1987 N  ND2  . ASN A 1 243 ? -3.971  -6.549  9.297   1.00 13.62 ? 244 ASN A ND2  1 
ATOM   1988 N  N    . TRP A 1 244 ? -1.657  -8.542  13.866  1.00 8.47  ? 245 TRP A N    1 
ATOM   1989 C  CA   . TRP A 1 244 ? -2.138  -8.269  15.215  1.00 7.80  ? 245 TRP A CA   1 
ATOM   1990 C  C    . TRP A 1 244 ? -0.910  -8.119  16.111  1.00 7.85  ? 245 TRP A C    1 
ATOM   1991 O  O    . TRP A 1 244 ? 0.073   -8.871  15.998  1.00 9.57  ? 245 TRP A O    1 
ATOM   1992 C  CB   . TRP A 1 244 ? -3.099  -9.344  15.731  1.00 8.27  ? 245 TRP A CB   1 
ATOM   1993 C  CG   . TRP A 1 244 ? -2.581  -10.776 15.509  1.00 7.99  ? 245 TRP A CG   1 
ATOM   1994 C  CD1  . TRP A 1 244 ? -2.736  -11.540 14.340  1.00 9.33  ? 245 TRP A CD1  1 
ATOM   1995 C  CD2  . TRP A 1 244 ? -2.020  -11.649 16.475  1.00 7.58  ? 245 TRP A CD2  1 
ATOM   1996 N  NE1  . TRP A 1 244 ? -2.169  -12.787 14.529  1.00 8.64  ? 245 TRP A NE1  1 
ATOM   1997 C  CE2  . TRP A 1 244 ? -1.760  -12.885 15.833  1.00 8.79  ? 245 TRP A CE2  1 
ATOM   1998 C  CE3  . TRP A 1 244 ? -1.719  -11.517 17.842  1.00 9.20  ? 245 TRP A CE3  1 
ATOM   1999 C  CZ2  . TRP A 1 244 ? -1.152  -13.956 16.517  1.00 9.99  ? 245 TRP A CZ2  1 
ATOM   2000 C  CZ3  . TRP A 1 244 ? -1.155  -12.620 18.526  1.00 11.06 ? 245 TRP A CZ3  1 
ATOM   2001 C  CH2  . TRP A 1 244 ? -0.903  -13.820 17.827  1.00 10.67 ? 245 TRP A CH2  1 
ATOM   2002 N  N    . ARG A 1 245 ? -1.035  -7.263  17.077  1.00 7.87  ? 246 ARG A N    1 
ATOM   2003 C  CA   . ARG A 1 245 ? -0.120  -7.176  18.186  1.00 8.72  ? 246 ARG A CA   1 
ATOM   2004 C  C    . ARG A 1 245 ? -0.573  -8.071  19.332  1.00 7.97  ? 246 ARG A C    1 
ATOM   2005 O  O    . ARG A 1 245 ? -1.758  -8.080  19.606  1.00 8.95  ? 246 ARG A O    1 
ATOM   2006 C  CB   . ARG A 1 245 ? -0.032  -5.713  18.691  1.00 9.23  ? 246 ARG A CB   1 
ATOM   2007 C  CG   . ARG A 1 245 ? 1.078   -5.504  19.728  1.00 8.58  ? 246 ARG A CG   1 
ATOM   2008 C  CD   . ARG A 1 245 ? 0.954   -4.114  20.383  1.00 9.83  ? 246 ARG A CD   1 
ATOM   2009 N  NE   . ARG A 1 245 ? 2.214   -3.812  21.066  1.00 10.00 ? 246 ARG A NE   1 
ATOM   2010 C  CZ   . ARG A 1 245 ? 2.422   -2.818  21.900  1.00 8.55  ? 246 ARG A CZ   1 
ATOM   2011 N  NH1  . ARG A 1 245 ? 1.385   -2.005  22.218  1.00 9.45  ? 246 ARG A NH1  1 
ATOM   2012 N  NH2  . ARG A 1 245 ? 3.677   -2.579  22.391  1.00 11.13 ? 246 ARG A NH2  1 
ATOM   2013 N  N    . PRO A 1 246 ? 0.323   -8.865  19.939  1.00 9.33  ? 247 PRO A N    1 
ATOM   2014 C  CA   . PRO A 1 246 ? -0.121  -9.740  21.063  1.00 8.90  ? 247 PRO A CA   1 
ATOM   2015 C  C    . PRO A 1 246 ? -0.486  -8.898  22.297  1.00 8.30  ? 247 PRO A C    1 
ATOM   2016 O  O    . PRO A 1 246 ? -0.117  -7.701  22.426  1.00 9.87  ? 247 PRO A O    1 
ATOM   2017 C  CB   . PRO A 1 246 ? 1.105   -10.563 21.363  1.00 13.62 ? 247 PRO A CB   1 
ATOM   2018 C  CG   . PRO A 1 246 ? 2.052   -10.367 20.262  1.00 16.56 ? 247 PRO A CG   1 
ATOM   2019 C  CD   . PRO A 1 246 ? 1.762   -9.058  19.616  1.00 10.20 ? 247 PRO A CD   1 
ATOM   2020 N  N    . ALA A 1 247 ? -1.108  -9.554  23.268  1.00 9.95  ? 248 ALA A N    1 
ATOM   2021 C  CA   . ALA A 1 247 ? -1.464  -8.954  24.528  1.00 9.74  ? 248 ALA A CA   1 
ATOM   2022 C  C    . ALA A 1 247 ? -0.234  -8.404  25.233  1.00 11.17 ? 248 ALA A C    1 
ATOM   2023 O  O    . ALA A 1 247 ? 0.813   -9.081  25.252  1.00 11.58 ? 248 ALA A O    1 
ATOM   2024 C  CB   . ALA A 1 247 ? -2.239  -9.924  25.389  1.00 12.03 ? 248 ALA A CB   1 
ATOM   2025 N  N    . GLN A 1 248 ? -0.381  -7.224  25.830  1.00 9.97  ? 249 GLN A N    1 
ATOM   2026 C  CA   . GLN A 1 248 ? 0.664   -6.511  26.536  1.00 10.32 ? 249 GLN A CA   1 
ATOM   2027 C  C    . GLN A 1 248 ? 0.371   -6.540  28.022  1.00 10.69 ? 249 GLN A C    1 
ATOM   2028 O  O    . GLN A 1 248 ? -0.793  -6.740  28.453  1.00 10.65 ? 249 GLN A O    1 
ATOM   2029 C  CB   . GLN A 1 248 ? 0.724   -5.082  26.002  1.00 11.97 ? 249 GLN A CB   1 
ATOM   2030 C  CG   . GLN A 1 248 ? 1.068   -5.013  24.506  1.00 11.14 ? 249 GLN A CG   1 
ATOM   2031 C  CD   . GLN A 1 248 ? 2.388   -5.699  24.189  1.00 10.90 ? 249 GLN A CD   1 
ATOM   2032 O  OE1  . GLN A 1 248 ? 3.398   -5.371  24.813  1.00 14.24 ? 249 GLN A OE1  1 
ATOM   2033 N  NE2  . GLN A 1 248 ? 2.382   -6.606  23.229  1.00 12.03 ? 249 GLN A NE2  1 
ATOM   2034 N  N    . PRO A 1 249 ? 1.367   -6.314  28.868  1.00 13.27 ? 250 PRO A N    1 
ATOM   2035 C  CA   . PRO A 1 249 ? 1.131   -6.357  30.298  1.00 13.69 ? 250 PRO A CA   1 
ATOM   2036 C  C    . PRO A 1 249 ? 0.072   -5.326  30.783  1.00 12.70 ? 250 PRO A C    1 
ATOM   2037 O  O    . PRO A 1 249 ? 0.072   -4.163  30.364  1.00 13.38 ? 250 PRO A O    1 
ATOM   2038 C  CB   . PRO A 1 249 ? 2.527   -5.975  30.857  1.00 16.74 ? 250 PRO A CB   1 
ATOM   2039 C  CG   . PRO A 1 249 ? 3.495   -6.392  29.820  1.00 18.51 ? 250 PRO A CG   1 
ATOM   2040 C  CD   . PRO A 1 249 ? 2.787   -6.124  28.511  1.00 16.11 ? 250 PRO A CD   1 
ATOM   2041 N  N    . LEU A 1 250 ? -0.855  -5.758  31.623  1.00 12.90 ? 251 LEU A N    1 
ATOM   2042 C  CA   . LEU A 1 250 ? -1.886  -4.893  32.096  1.00 11.71 ? 251 LEU A CA   1 
ATOM   2043 C  C    . LEU A 1 250 ? -1.345  -3.820  33.058  1.00 13.32 ? 251 LEU A C    1 
ATOM   2044 O  O    . LEU A 1 250 ? -1.833  -2.692  33.118  1.00 13.59 ? 251 LEU A O    1 
ATOM   2045 C  CB   . LEU A 1 250 ? -2.932  -5.770  32.818  1.00 13.96 ? 251 LEU A CB   1 
ATOM   2046 C  CG   . LEU A 1 250 ? -4.176  -5.054  33.284  1.00 14.47 ? 251 LEU A CG   1 
ATOM   2047 C  CD1  . LEU A 1 250 ? -4.941  -4.472  32.079  1.00 14.76 ? 251 LEU A CD1  1 
ATOM   2048 C  CD2  . LEU A 1 250 ? -5.130  -5.999  34.024  1.00 17.33 ? 251 LEU A CD2  1 
ATOM   2049 N  N    . LYS A 1 251 ? -0.268  -4.147  33.753  1.00 13.75 ? 252 LYS A N    1 
ATOM   2050 C  CA   . LYS A 1 251 ? 0.360   -3.135  34.634  1.00 14.30 ? 252 LYS A CA   1 
ATOM   2051 C  C    . LYS A 1 251 ? -0.661  -2.578  35.633  1.00 15.54 ? 252 LYS A C    1 
ATOM   2052 O  O    . LYS A 1 251 ? -1.435  -3.403  36.171  1.00 18.76 ? 252 LYS A O    1 
ATOM   2053 C  CB   . LYS A 1 251 ? 1.120   -2.073  33.872  1.00 15.05 ? 252 LYS A CB   1 
ATOM   2054 C  CG   . LYS A 1 251 ? 2.267   -2.766  33.095  1.00 17.63 ? 252 LYS A CG   1 
ATOM   2055 C  CD   . LYS A 1 251 ? 3.255   -1.750  32.503  1.00 19.41 ? 252 LYS A CD   1 
ATOM   2056 C  CE   . LYS A 1 251 ? 4.252   -2.536  31.758  1.00 20.11 ? 252 LYS A CE   1 
ATOM   2057 N  NZ   . LYS A 1 251 ? 5.235   -1.620  31.230  1.00 25.16 ? 252 LYS A NZ   1 
ATOM   2058 N  N    . ASN A 1 252 ? -0.639  -1.273  35.879  1.00 15.61 ? 253 ASN A N    1 
ATOM   2059 C  CA   . ASN A 1 252 ? -1.477  -0.737  36.893  1.00 20.78 ? 253 ASN A CA   1 
ATOM   2060 C  C    . ASN A 1 252 ? -2.799  -0.262  36.325  1.00 20.13 ? 253 ASN A C    1 
ATOM   2061 O  O    . ASN A 1 252 ? -2.998  1.034   36.267  1.00 22.73 ? 253 ASN A O    1 
ATOM   2062 C  CB   . ASN A 1 252 ? -0.764  0.426   37.584  1.00 22.13 ? 253 ASN A CB   1 
ATOM   2063 C  CG   . ASN A 1 252 ? -1.586  0.976   38.758  1.00 27.93 ? 253 ASN A CG   1 
ATOM   2064 O  OD1  . ASN A 1 252 ? -2.172  0.206   39.542  1.00 36.21 ? 253 ASN A OD1  1 
ATOM   2065 N  ND2  . ASN A 1 252 ? -1.664  2.299   38.866  1.00 32.02 ? 253 ASN A ND2  1 
ATOM   2066 N  N    . ARG A 1 253 ? -3.560  -1.261  35.775  1.00 15.56 ? 254 ARG A N    1 
ATOM   2067 C  CA   . ARG A 1 253 ? -4.878  -0.985  35.201  1.00 12.59 ? 254 ARG A CA   1 
ATOM   2068 C  C    . ARG A 1 253 ? -5.951  -1.943  35.628  1.00 14.01 ? 254 ARG A C    1 
ATOM   2069 O  O    . ARG A 1 253 ? -5.687  -3.123  35.817  1.00 17.08 ? 254 ARG A O    1 
ATOM   2070 C  CB   . ARG A 1 253 ? -4.810  -0.974  33.666  1.00 11.40 ? 254 ARG A CB   1 
ATOM   2071 C  CG   . ARG A 1 253 ? -3.924  0.130   33.138  1.00 11.21 ? 254 ARG A CG   1 
ATOM   2072 C  CD   . ARG A 1 253 ? -3.875  0.149   31.616  1.00 11.28 ? 254 ARG A CD   1 
ATOM   2073 N  NE   . ARG A 1 253 ? -3.004  -0.967  31.171  1.00 10.49 ? 254 ARG A NE   1 
ATOM   2074 C  CZ   . ARG A 1 253 ? -2.781  -1.263  29.896  1.00 8.61  ? 254 ARG A CZ   1 
ATOM   2075 N  NH1  . ARG A 1 253 ? -3.370  -0.544  28.948  1.00 9.33  ? 254 ARG A NH1  1 
ATOM   2076 N  NH2  . ARG A 1 253 ? -1.937  -2.248  29.591  1.00 9.74  ? 254 ARG A NH2  1 
ATOM   2077 N  N    . GLN A 1 254 ? -7.176  -1.416  35.640  1.00 14.63 ? 255 GLN A N    1 
ATOM   2078 C  CA   . GLN A 1 254 ? -8.326  -2.228  35.962  1.00 16.60 ? 255 GLN A CA   1 
ATOM   2079 C  C    . GLN A 1 254 ? -9.222  -2.246  34.745  1.00 14.98 ? 255 GLN A C    1 
ATOM   2080 O  O    . GLN A 1 254 ? -9.474  -1.201  34.102  1.00 17.89 ? 255 GLN A O    1 
ATOM   2081 C  CB   . GLN A 1 254 ? -9.114  -1.557  37.103  1.00 19.60 ? 255 GLN A CB   1 
ATOM   2082 C  CG   . GLN A 1 254 ? -10.015 -2.544  37.717  1.00 26.87 ? 255 GLN A CG   1 
ATOM   2083 C  CD   . GLN A 1 254 ? -10.784 -1.969  38.861  1.00 33.29 ? 255 GLN A CD   1 
ATOM   2084 O  OE1  . GLN A 1 254 ? -10.745 -0.729  39.154  1.00 38.91 ? 255 GLN A OE1  1 
ATOM   2085 N  NE2  . GLN A 1 254 ? -11.502 -2.835  39.534  1.00 34.18 ? 255 GLN A NE2  1 
ATOM   2086 N  N    . ILE A 1 255 ? -9.618  -3.434  34.319  1.00 12.54 ? 256 ILE A N    1 
ATOM   2087 C  CA   . ILE A 1 255 ? -10.679 -3.565  33.286  1.00 11.35 ? 256 ILE A CA   1 
ATOM   2088 C  C    . ILE A 1 255 ? -12.045 -3.574  33.949  1.00 10.52 ? 256 ILE A C    1 
ATOM   2089 O  O    . ILE A 1 255 ? -12.286 -4.292  34.938  1.00 11.99 ? 256 ILE A O    1 
ATOM   2090 C  CB   . ILE A 1 255 ? -10.466 -4.806  32.438  1.00 12.03 ? 256 ILE A CB   1 
ATOM   2091 C  CG1  . ILE A 1 255 ? -9.016  -4.793  31.844  1.00 11.81 ? 256 ILE A CG1  1 
ATOM   2092 C  CG2  . ILE A 1 255 ? -11.567 -4.910  31.342  1.00 12.87 ? 256 ILE A CG2  1 
ATOM   2093 C  CD1  . ILE A 1 255 ? -8.721  -6.017  31.058  1.00 14.64 ? 256 ILE A CD1  1 
ATOM   2094 N  N    . LYS A 1 256 ? -12.942 -2.720  33.457  1.00 10.61 ? 257 LYS A N    1 
ATOM   2095 C  CA   . LYS A 1 256 ? -14.297 -2.620  34.005  1.00 11.74 ? 257 LYS A CA   1 
ATOM   2096 C  C    . LYS A 1 256 ? -15.260 -3.275  33.046  1.00 10.37 ? 257 LYS A C    1 
ATOM   2097 O  O    . LYS A 1 256 ? -15.054 -3.199  31.831  1.00 12.16 ? 257 LYS A O    1 
ATOM   2098 C  CB   . LYS A 1 256 ? -14.737 -1.159  34.252  1.00 13.06 ? 257 LYS A CB   1 
ATOM   2099 C  CG   . LYS A 1 256 ? -13.752 -0.418  35.079  1.00 17.85 ? 257 LYS A CG   1 
ATOM   2100 C  CD   . LYS A 1 256 ? -13.319 -0.931  36.303  1.00 27.14 ? 257 LYS A CD   1 
ATOM   2101 C  CE   . LYS A 1 256 ? -12.527 0.289   36.978  1.00 33.03 ? 257 LYS A CE   1 
ATOM   2102 N  NZ   . LYS A 1 256 ? -13.553 1.398   37.308  1.00 40.21 ? 257 LYS A NZ   1 
ATOM   2103 N  N    . ALA A 1 257 ? -16.313 -3.882  33.573  1.00 11.26 ? 258 ALA A N    1 
ATOM   2104 C  CA   . ALA A 1 257 ? -17.370 -4.523  32.831  1.00 12.00 ? 258 ALA A CA   1 
ATOM   2105 C  C    . ALA A 1 257 ? -18.668 -3.718  32.976  1.00 10.55 ? 258 ALA A C    1 
ATOM   2106 O  O    . ALA A 1 257 ? -19.005 -3.287  34.105  1.00 13.32 ? 258 ALA A O    1 
ATOM   2107 C  CB   . ALA A 1 257 ? -17.558 -5.980  33.260  1.00 13.59 ? 258 ALA A CB   1 
ATOM   2108 N  N    . SER A 1 258 ? -19.406 -3.546  31.882  1.00 11.46 ? 259 SER A N    1 
ATOM   2109 C  CA   . SER A 1 258 ? -20.684 -2.869  31.967  1.00 12.82 ? 259 SER A CA   1 
ATOM   2110 C  C    . SER A 1 258 ? -21.839 -3.812  32.349  1.00 14.30 ? 259 SER A C    1 
ATOM   2111 O  O    . SER A 1 258 ? -22.992 -3.403  32.463  1.00 18.32 ? 259 SER A O    1 
ATOM   2112 C  CB   . SER A 1 258 ? -20.941 -2.282  30.598  1.00 13.65 ? 259 SER A CB   1 
ATOM   2113 O  OG   . SER A 1 258 ? -21.384 -3.289  29.698  1.00 12.47 ? 259 SER A OG   1 
ATOM   2114 N  N    . PHE A 1 259 ? -21.505 -5.073  32.586  1.00 13.97 ? 260 PHE A N    1 
ATOM   2115 C  CA   . PHE A 1 259 ? -22.515 -6.130  32.756  1.00 15.10 ? 260 PHE A CA   1 
ATOM   2116 C  C    . PHE A 1 259 ? -21.993 -7.104  33.779  1.00 19.35 ? 260 PHE A C    1 
ATOM   2117 O  O    . PHE A 1 259 ? -20.780 -7.202  34.060  1.00 20.05 ? 260 PHE A O    1 
ATOM   2118 C  CB   . PHE A 1 259 ? -22.740 -6.861  31.445  1.00 17.53 ? 260 PHE A CB   1 
ATOM   2119 C  CG   . PHE A 1 259 ? -21.475 -7.566  30.941  1.00 16.75 ? 260 PHE A CG   1 
ATOM   2120 C  CD1  . PHE A 1 259 ? -20.469 -6.852  30.262  1.00 13.93 ? 260 PHE A CD1  1 
ATOM   2121 C  CD2  . PHE A 1 259 ? -21.221 -8.914  31.264  1.00 19.39 ? 260 PHE A CD2  1 
ATOM   2122 C  CE1  . PHE A 1 259 ? -19.284 -7.494  29.877  1.00 16.27 ? 260 PHE A CE1  1 
ATOM   2123 C  CE2  . PHE A 1 259 ? -20.039 -9.540  30.882  1.00 20.12 ? 260 PHE A CE2  1 
ATOM   2124 C  CZ   . PHE A 1 259 ? -19.063 -8.844  30.154  1.00 19.65 ? 260 PHE A CZ   1 
ATOM   2125 N  N    . LYS A 1 260 ? -23.018 -7.786  34.304  1.00 24.11 ? 261 LYS A N    1 
ATOM   2126 C  CA   . LYS A 1 260 ? -23.100 -9.010  35.155  1.00 32.16 ? 261 LYS A CA   1 
ATOM   2127 C  C    . LYS A 1 260 ? -23.042 -8.940  36.667  1.00 35.72 ? 261 LYS A C    1 
ATOM   2128 O  O    . LYS A 1 260 ? -23.668 -7.997  37.208  1.00 39.01 ? 261 LYS A O    1 
ATOM   2129 C  CB   . LYS A 1 260 ? -22.567 -10.300 34.505  1.00 31.83 ? 261 LYS A CB   1 
ATOM   2130 C  CG   . LYS A 1 260 ? -23.468 -10.677 33.314  1.00 33.43 ? 261 LYS A CG   1 
ATOM   2131 C  CD   . LYS A 1 260 ? -22.994 -11.934 32.519  1.00 40.12 ? 261 LYS A CD   1 
ATOM   2132 C  CE   . LYS A 1 260 ? -21.460 -12.209 32.655  1.00 43.38 ? 261 LYS A CE   1 
ATOM   2133 N  NZ   . LYS A 1 260 ? -21.007 -13.442 31.933  1.00 45.47 ? 261 LYS A NZ   1 
ATOM   2134 O  OXT  . LYS A 1 260 ? -22.497 -9.791  37.363  1.00 39.34 ? 261 LYS A OXT  1 
HETATM 2135 ZN ZN   . ZN  B 2 .   ? -6.644  -1.683  15.241  1.00 8.29  ? 262 ZN  A ZN   1 
HETATM 2136 O  O1   . MES C 3 .   ? -7.654  -8.998  -2.600  0.30 18.23 ? 263 MES A O1   1 
HETATM 2137 C  C2   . MES C 3 .   ? -7.654  -9.898  -3.732  0.30 16.60 ? 263 MES A C2   1 
HETATM 2138 C  C3   . MES C 3 .   ? -8.797  -10.953 -3.699  0.30 18.59 ? 263 MES A C3   1 
HETATM 2139 N  N4   . MES C 3 .   ? -9.818  -10.687 -2.664  0.30 17.31 ? 263 MES A N4   1 
HETATM 2140 C  C5   . MES C 3 .   ? -9.513  -10.049 -1.362  0.30 9.49  ? 263 MES A C5   1 
HETATM 2141 C  C6   . MES C 3 .   ? -8.054  -9.652  -1.399  0.30 14.32 ? 263 MES A C6   1 
HETATM 2142 C  C7   . MES C 3 .   ? -11.206 -11.101 -2.863  0.30 17.43 ? 263 MES A C7   1 
HETATM 2143 C  C8   . MES C 3 .   ? -11.734 -10.156 -3.940  0.30 22.72 ? 263 MES A C8   1 
HETATM 2144 S  S    . MES C 3 .   ? -12.590 -8.976  -3.151  0.30 21.30 ? 263 MES A S    1 
HETATM 2145 O  O1S  . MES C 3 .   ? -12.057 -9.080  -1.785  0.30 25.59 ? 263 MES A O1S  1 
HETATM 2146 O  O2S  . MES C 3 .   ? -12.498 -7.611  -3.694  0.30 25.94 ? 263 MES A O2S  1 
HETATM 2147 O  O3S  . MES C 3 .   ? -14.013 -9.403  -3.131  0.30 26.08 ? 263 MES A O3S  1 
HETATM 2148 S  S    . DMS D 4 .   ? 1.352   -11.693 14.905  1.00 23.55 ? 264 DMS A S    1 
HETATM 2149 O  O    . DMS D 4 .   ? 2.203   -13.090 14.512  1.00 26.60 ? 264 DMS A O    1 
HETATM 2150 C  C1   . DMS D 4 .   ? 2.528   -10.445 14.409  1.00 24.57 ? 264 DMS A C1   1 
HETATM 2151 C  C2   . DMS D 4 .   ? 1.682   -11.505 16.645  1.00 21.07 ? 264 DMS A C2   1 
HETATM 2152 S  S    . DMS E 4 .   ? -5.643  7.186   11.022  1.00 31.37 ? 265 DMS A S    1 
HETATM 2153 O  O    . DMS E 4 .   ? -7.027  6.550   10.364  1.00 33.10 ? 265 DMS A O    1 
HETATM 2154 C  C1   . DMS E 4 .   ? -5.963  8.932   10.592  1.00 31.81 ? 265 DMS A C1   1 
HETATM 2155 C  C2   . DMS E 4 .   ? -4.559  7.020   9.585   1.00 33.86 ? 265 DMS A C2   1 
HETATM 2156 N  N1   . E27 F 5 .   ? -2.232  5.546   11.540  0.01 33.43 ? 266 E27 A N1   1 
HETATM 2157 C  C2   . E27 F 5 .   ? -1.932  4.912   10.397  0.01 32.55 ? 266 E27 A C2   1 
HETATM 2158 N  N3   . E27 F 5 .   ? -0.773  5.355   9.894   0.01 33.42 ? 266 E27 A N3   1 
HETATM 2159 C  C4   . E27 F 5 .   ? -0.341  6.278   10.735  0.01 34.10 ? 266 E27 A C4   1 
HETATM 2160 C  C5   . E27 F 5 .   ? 0.805   7.057   10.704  0.01 34.51 ? 266 E27 A C5   1 
HETATM 2161 N  N6   . E27 F 5 .   ? 0.993   7.925   11.702  0.01 34.83 ? 266 E27 A N6   1 
HETATM 2162 C  C7   . E27 F 5 .   ? 0.124   8.063   12.713  0.01 34.98 ? 266 E27 A C7   1 
HETATM 2163 C  C8   . E27 F 5 .   ? -1.037  7.295   12.775  0.01 34.74 ? 266 E27 A C8   1 
HETATM 2164 C  C9   . E27 F 5 .   ? -1.244  6.394   11.749  0.01 34.19 ? 266 E27 A C9   1 
HETATM 2165 C  C10  . E27 F 5 .   ? 0.377   8.984   13.723  0.01 35.15 ? 266 E27 A C10  1 
HETATM 2166 C  C11  . E27 F 5 .   ? -0.522  9.132   14.774  0.01 35.21 ? 266 E27 A C11  1 
HETATM 2167 C  C12  . E27 F 5 .   ? -1.678  8.359   14.825  0.01 35.14 ? 266 E27 A C12  1 
HETATM 2168 C  C13  . E27 F 5 .   ? -1.940  7.434   13.820  0.01 34.95 ? 266 E27 A C13  1 
HETATM 2169 S  S14  . E27 F 5 .   ? -2.973  3.667   9.688   0.01 30.95 ? 266 E27 A S14  1 
HETATM 2170 C  C15  . E27 F 5 .   ? -4.334  3.455   10.862  1.00 28.73 ? 266 E27 A C15  1 
HETATM 2171 C  C16  . E27 F 5 .   ? -3.984  2.670   12.188  1.00 23.21 ? 266 E27 A C16  1 
HETATM 2172 O  O17  . E27 F 5 .   ? -3.128  1.723   12.240  1.00 23.62 ? 266 E27 A O17  1 
HETATM 2173 C  C18  . E27 F 5 .   ? -4.646  2.928   13.566  1.00 16.69 ? 266 E27 A C18  1 
HETATM 2174 C  C19  . E27 F 5 .   ? -4.921  1.898   14.442  1.00 12.48 ? 266 E27 A C19  1 
HETATM 2175 C  C20  . E27 F 5 .   ? -5.523  2.127   15.630  1.00 10.57 ? 266 E27 A C20  1 
HETATM 2176 C  C21  . E27 F 5 .   ? -5.937  3.403   15.937  1.00 12.80 ? 266 E27 A C21  1 
HETATM 2177 C  C22  . E27 F 5 .   ? -5.719  4.471   15.075  1.00 15.75 ? 266 E27 A C22  1 
HETATM 2178 C  C23  . E27 F 5 .   ? -5.100  4.195   13.903  1.00 16.21 ? 266 E27 A C23  1 
HETATM 2179 S  S24  . E27 F 5 .   ? -5.946  0.802   16.741  1.00 9.52  ? 266 E27 A S24  1 
HETATM 2180 O  O25  . E27 F 5 .   ? -7.433  0.774   16.738  1.00 10.05 ? 266 E27 A O25  1 
HETATM 2181 CL CL26 . E27 F 5 .   ? -6.776  3.831   17.405  1.00 13.37 ? 266 E27 A CL26 1 
HETATM 2182 O  O27  . E27 F 5 .   ? -5.310  1.107   18.023  1.00 8.99  ? 266 E27 A O27  1 
HETATM 2183 N  N28  . E27 F 5 .   ? -5.374  -0.555  16.047  1.00 9.60  ? 266 E27 A N28  1 
HETATM 2184 O  O    . HOH G 6 .   ? -15.239 19.299  13.118  1.00 22.30 ? 126 HOH A O    1 
HETATM 2185 O  O    . HOH G 6 .   ? -4.517  -13.486 17.964  1.00 10.18 ? 267 HOH A O    1 
HETATM 2186 O  O    . HOH G 6 .   ? -10.643 8.625   25.508  1.00 11.18 ? 268 HOH A O    1 
HETATM 2187 O  O    . HOH G 6 .   ? -21.553 -7.132  23.482  1.00 12.83 ? 269 HOH A O    1 
HETATM 2188 O  O    . HOH G 6 .   ? -16.976 -8.429  20.363  1.00 9.16  ? 270 HOH A O    1 
HETATM 2189 O  O    . HOH G 6 .   ? -17.803 -20.462 7.958   1.00 14.72 ? 271 HOH A O    1 
HETATM 2190 O  O    . HOH G 6 .   ? 4.848   -4.934  20.940  1.00 14.69 ? 272 HOH A O    1 
HETATM 2191 O  O    . HOH G 6 .   ? -1.186  -4.019  15.720  1.00 9.32  ? 273 HOH A O    1 
HETATM 2192 O  O    . HOH G 6 .   ? -3.421  -13.266 25.081  1.00 12.67 ? 274 HOH A O    1 
HETATM 2193 O  O    . HOH G 6 .   ? 3.566   5.031   29.648  1.00 19.49 ? 275 HOH A O    1 
HETATM 2194 O  O    . HOH G 6 .   ? -21.857 5.678   4.800   1.00 16.95 ? 276 HOH A O    1 
HETATM 2195 O  O    . HOH G 6 .   ? -2.501  -8.741  29.050  1.00 12.89 ? 277 HOH A O    1 
HETATM 2196 O  O    . HOH G 6 .   ? -3.506  -11.133 20.793  1.00 10.49 ? 278 HOH A O    1 
HETATM 2197 O  O    . HOH G 6 .   ? -9.540  -7.986  33.921  1.00 21.88 ? 279 HOH A O    1 
HETATM 2198 O  O    . HOH G 6 .   ? -3.799  -15.865 24.274  1.00 13.94 ? 280 HOH A O    1 
HETATM 2199 O  O    . HOH G 6 .   ? -17.879 10.482  11.347  1.00 17.61 ? 281 HOH A O    1 
HETATM 2200 O  O    . HOH G 6 .   ? -19.350 9.966   8.980   1.00 14.90 ? 282 HOH A O    1 
HETATM 2201 O  O    . HOH G 6 .   ? 1.182   -1.548  29.341  1.00 16.07 ? 283 HOH A O    1 
HETATM 2202 O  O    . HOH G 6 .   ? -13.934 10.372  27.802  1.00 19.32 ? 284 HOH A O    1 
HETATM 2203 O  O    . HOH G 6 .   ? -2.058  -12.289 22.780  1.00 10.62 ? 285 HOH A O    1 
HETATM 2204 O  O    . HOH G 6 .   ? -28.641 0.226   24.475  1.00 20.82 ? 286 HOH A O    1 
HETATM 2205 O  O    . HOH G 6 .   ? -7.893  -15.396 11.291  1.00 10.87 ? 287 HOH A O    1 
HETATM 2206 O  O    . HOH G 6 .   ? 5.409   7.026   20.190  1.00 17.70 ? 288 HOH A O    1 
HETATM 2207 O  O    . HOH G 6 .   ? -23.802 -0.882  3.959   1.00 21.15 ? 289 HOH A O    1 
HETATM 2208 O  O    . HOH G 6 .   ? 8.501   -3.831  21.069  1.00 14.98 ? 290 HOH A O    1 
HETATM 2209 O  O    . HOH G 6 .   ? -16.087 -12.327 24.314  1.00 15.90 ? 291 HOH A O    1 
HETATM 2210 O  O    . HOH G 6 .   ? -10.353 -18.211 16.977  1.00 15.10 ? 292 HOH A O    1 
HETATM 2211 O  O    . HOH G 6 .   ? -30.795 1.369   26.095  1.00 25.62 ? 293 HOH A O    1 
HETATM 2212 O  O    . HOH G 6 .   ? 7.559   6.068   21.705  1.00 17.19 ? 294 HOH A O    1 
HETATM 2213 O  O    . HOH G 6 .   ? -16.310 -9.892  32.821  1.00 18.52 ? 295 HOH A O    1 
HETATM 2214 O  O    . HOH G 6 .   ? -13.332 -18.473 14.585  1.00 19.83 ? 296 HOH A O    1 
HETATM 2215 O  O    . HOH G 6 .   ? -13.240 -22.403 11.517  1.00 29.88 ? 297 HOH A O    1 
HETATM 2216 O  O    . HOH G 6 .   ? -9.989  14.587  12.168  1.00 18.38 ? 298 HOH A O    1 
HETATM 2217 O  O    . HOH G 6 .   ? -11.958 2.675   30.794  1.00 20.19 ? 299 HOH A O    1 
HETATM 2218 O  O    . HOH G 6 .   ? -17.615 -21.147 17.529  1.00 25.81 ? 300 HOH A O    1 
HETATM 2219 O  O    . HOH G 6 .   ? 2.758   -4.169  7.670   1.00 26.71 ? 301 HOH A O    1 
HETATM 2220 O  O    . HOH G 6 .   ? -12.793 -17.198 16.744  1.00 15.36 ? 302 HOH A O    1 
HETATM 2221 O  O    . HOH G 6 .   ? -5.084  0.634   9.863   1.00 25.22 ? 303 HOH A O    1 
HETATM 2222 O  O    . HOH G 6 .   ? -21.064 7.823   1.909   1.00 16.48 ? 304 HOH A O    1 
HETATM 2223 O  O    . HOH G 6 .   ? -16.491 -11.181 41.457  1.00 21.80 ? 305 HOH A O    1 
HETATM 2224 O  O    . HOH G 6 .   ? -6.863  -14.894 31.518  1.00 20.48 ? 306 HOH A O    1 
HETATM 2225 O  O    . HOH G 6 .   ? -24.098 8.624   20.118  1.00 23.60 ? 307 HOH A O    1 
HETATM 2226 O  O    . HOH G 6 .   ? -29.001 -5.784  24.412  1.00 26.77 ? 308 HOH A O    1 
HETATM 2227 O  O    . HOH G 6 .   ? -4.703  0.934   43.244  1.00 25.17 ? 309 HOH A O    1 
HETATM 2228 O  O    . HOH G 6 .   ? -4.646  -11.900 31.942  1.00 23.23 ? 310 HOH A O    1 
HETATM 2229 O  O    . HOH G 6 .   ? -26.309 -11.393 1.948   1.00 23.81 ? 311 HOH A O    1 
HETATM 2230 O  O    . HOH G 6 .   ? -8.083  -19.318 21.521  1.00 18.18 ? 312 HOH A O    1 
HETATM 2231 O  O    . HOH G 6 .   ? 1.308   -11.785 24.914  1.00 23.42 ? 313 HOH A O    1 
HETATM 2232 O  O    . HOH G 6 .   ? -5.960  -4.471  -6.370  1.00 25.57 ? 314 HOH A O    1 
HETATM 2233 O  O    . HOH G 6 .   ? -0.500  10.810  23.387  1.00 17.71 ? 315 HOH A O    1 
HETATM 2234 O  O    . HOH G 6 .   ? -25.476 9.576   13.339  1.00 29.97 ? 316 HOH A O    1 
HETATM 2235 O  O    . HOH G 6 .   ? -8.511  -15.261 36.683  1.00 25.87 ? 317 HOH A O    1 
HETATM 2236 O  O    . HOH G 6 .   ? -16.167 15.785  23.570  1.00 20.34 ? 318 HOH A O    1 
HETATM 2237 O  O    . HOH G 6 .   ? 4.159   -3.448  26.489  1.00 20.13 ? 319 HOH A O    1 
HETATM 2238 O  O    . HOH G 6 .   ? -25.519 -15.284 7.764   1.00 26.94 ? 320 HOH A O    1 
HETATM 2239 O  O    . HOH G 6 .   ? -7.324  -8.677  32.504  1.00 17.30 ? 321 HOH A O    1 
HETATM 2240 O  O    . HOH G 6 .   ? -14.527 -18.518 18.665  1.00 19.25 ? 322 HOH A O    1 
HETATM 2241 O  O    . HOH G 6 .   ? -26.345 3.573   15.486  1.00 27.46 ? 323 HOH A O    1 
HETATM 2242 O  O    . HOH G 6 .   ? -20.337 10.726  26.577  1.00 20.04 ? 324 HOH A O    1 
HETATM 2243 O  O    . HOH G 6 .   ? -2.568  -3.332  11.484  1.00 18.39 ? 325 HOH A O    1 
HETATM 2244 O  O    . HOH G 6 .   ? -17.663 -21.965 6.015   1.00 13.91 ? 326 HOH A O    1 
HETATM 2245 O  O    . HOH G 6 .   ? -7.978  -22.100 10.317  1.00 24.36 ? 327 HOH A O    1 
HETATM 2246 O  O    . HOH G 6 .   ? -1.523  11.372  25.823  1.00 23.36 ? 328 HOH A O    1 
HETATM 2247 O  O    . HOH G 6 .   ? -24.790 -7.707  9.046   1.00 19.25 ? 329 HOH A O    1 
HETATM 2248 O  O    . HOH G 6 .   ? -23.211 -0.776  34.200  1.00 26.36 ? 330 HOH A O    1 
HETATM 2249 O  O    . HOH G 6 .   ? -22.918 -11.750 13.994  1.00 21.42 ? 331 HOH A O    1 
HETATM 2250 O  O    . HOH G 6 .   ? -22.265 3.664   -2.941  1.00 24.02 ? 332 HOH A O    1 
HETATM 2251 O  O    . HOH G 6 .   ? -22.656 -5.853  2.802   1.00 22.03 ? 333 HOH A O    1 
HETATM 2252 O  O    . HOH G 6 .   ? -8.644  -3.825  7.856   1.00 11.43 ? 334 HOH A O    1 
HETATM 2253 O  O    . HOH G 6 .   ? -23.080 -13.651 11.069  1.00 29.83 ? 335 HOH A O    1 
HETATM 2254 O  O    . HOH G 6 .   ? -14.803 19.842  17.567  1.00 25.61 ? 336 HOH A O    1 
HETATM 2255 O  O    . HOH G 6 .   ? -25.884 -6.047  13.049  1.00 35.13 ? 337 HOH A O    1 
HETATM 2256 O  O    . HOH G 6 .   ? -9.030  -5.885  35.758  1.00 19.44 ? 338 HOH A O    1 
HETATM 2257 O  O    . HOH G 6 .   ? -23.960 -0.693  26.418  1.00 17.64 ? 339 HOH A O    1 
HETATM 2258 O  O    . HOH G 6 .   ? 1.184   8.746   24.368  1.00 18.71 ? 340 HOH A O    1 
HETATM 2259 O  O    . HOH G 6 .   ? -2.544  -17.592 5.238   1.00 32.12 ? 341 HOH A O    1 
HETATM 2260 O  O    . HOH G 6 .   ? -18.521 3.694   -3.584  1.00 31.93 ? 342 HOH A O    1 
HETATM 2261 O  O    . HOH G 6 .   ? 11.242  -7.017  22.395  1.00 30.81 ? 343 HOH A O    1 
HETATM 2262 O  O    . HOH G 6 .   ? 2.632   -11.318 9.456   1.00 22.98 ? 344 HOH A O    1 
HETATM 2263 O  O    . HOH G 6 .   ? -12.452 12.448  29.131  1.00 25.51 ? 345 HOH A O    1 
HETATM 2264 O  O    . HOH G 6 .   ? -7.054  1.509   35.167  1.00 24.88 ? 346 HOH A O    1 
HETATM 2265 O  O    . HOH G 6 .   ? -26.670 -2.574  14.386  1.00 21.10 ? 347 HOH A O    1 
HETATM 2266 O  O    . HOH G 6 .   ? 8.132   -5.893  -10.367 1.00 24.14 ? 348 HOH A O    1 
HETATM 2267 O  O    . HOH G 6 .   ? -23.163 -3.010  6.663   1.00 21.21 ? 349 HOH A O    1 
HETATM 2268 O  O    . HOH G 6 .   ? -8.546  0.732   -6.445  1.00 30.55 ? 350 HOH A O    1 
HETATM 2269 O  O    . HOH G 6 .   ? -6.406  -19.803 23.887  1.00 26.06 ? 351 HOH A O    1 
HETATM 2270 O  O    . HOH G 6 .   ? -14.285 -16.506 28.950  1.00 25.51 ? 352 HOH A O    1 
HETATM 2271 O  O    . HOH G 6 .   ? -9.170  5.883   29.013  1.00 22.92 ? 353 HOH A O    1 
HETATM 2272 O  O    . HOH G 6 .   ? -0.068  1.054   34.411  1.00 24.05 ? 354 HOH A O    1 
HETATM 2273 O  O    . HOH G 6 .   ? -22.060 -18.326 13.540  1.00 24.47 ? 355 HOH A O    1 
HETATM 2274 O  O    . HOH G 6 .   ? -3.391  -12.896 -2.787  1.00 25.52 ? 356 HOH A O    1 
HETATM 2275 O  O    . HOH G 6 .   ? -8.008  -18.929 30.609  1.00 29.45 ? 357 HOH A O    1 
HETATM 2276 O  O    . HOH G 6 .   ? -23.376 8.302   3.592   1.00 23.62 ? 358 HOH A O    1 
HETATM 2277 O  O    . HOH G 6 .   ? -6.045  15.126  11.839  1.00 27.95 ? 359 HOH A O    1 
HETATM 2278 O  O    . HOH G 6 .   ? -26.479 2.866   20.919  1.00 28.85 ? 360 HOH A O    1 
HETATM 2279 O  O    . HOH G 6 .   ? -24.554 -9.491  1.978   1.00 26.27 ? 361 HOH A O    1 
HETATM 2280 O  O    . HOH G 6 .   ? -6.650  20.702  19.442  1.00 16.05 ? 362 HOH A O    1 
HETATM 2281 O  O    . HOH G 6 .   ? -4.264  -8.597  31.127  1.00 21.86 ? 363 HOH A O    1 
HETATM 2282 O  O    . HOH G 6 .   ? 4.308   -6.460  7.790   1.00 24.26 ? 364 HOH A O    1 
HETATM 2283 O  O    . HOH G 6 .   ? -13.057 -16.807 26.534  1.00 20.23 ? 365 HOH A O    1 
HETATM 2284 O  O    . HOH G 6 .   ? -18.705 -9.080  34.316  1.00 24.82 ? 366 HOH A O    1 
HETATM 2285 O  O    . HOH G 6 .   ? 1.626   12.502  22.640  1.00 27.97 ? 367 HOH A O    1 
HETATM 2286 O  O    . HOH G 6 .   ? -0.602  -8.572  32.328  1.00 24.23 ? 368 HOH A O    1 
HETATM 2287 O  O    . HOH G 6 .   ? -5.284  3.741   -5.649  1.00 28.46 ? 369 HOH A O    1 
HETATM 2288 O  O    . HOH G 6 .   ? -18.850 12.124  13.018  1.00 23.13 ? 370 HOH A O    1 
HETATM 2289 O  O    . HOH G 6 .   ? -14.053 14.174  27.101  1.00 27.92 ? 371 HOH A O    1 
HETATM 2290 O  O    . HOH G 6 .   ? 8.583   -4.729  23.629  1.00 25.20 ? 372 HOH A O    1 
HETATM 2291 O  O    . HOH G 6 .   ? -11.092 -15.203 33.930  1.00 26.90 ? 373 HOH A O    1 
HETATM 2292 O  O    . HOH G 6 .   ? 0.191   -0.907  -4.642  1.00 19.25 ? 374 HOH A O    1 
HETATM 2293 O  O    . HOH G 6 .   ? 9.826   -4.569  -7.961  1.00 23.69 ? 375 HOH A O    1 
HETATM 2294 O  O    . HOH G 6 .   ? 7.661   -7.601  -0.665  1.00 28.69 ? 376 HOH A O    1 
HETATM 2295 O  O    . HOH G 6 .   ? 1.271   -6.479  34.314  1.00 26.81 ? 377 HOH A O    1 
HETATM 2296 O  O    . HOH G 6 .   ? 4.299   -2.499  28.818  1.00 26.57 ? 378 HOH A O    1 
HETATM 2297 O  O    . HOH G 6 .   ? -1.139  -17.552 17.975  1.00 31.13 ? 379 HOH A O    1 
HETATM 2298 O  O    . HOH G 6 .   ? -12.759 -22.129 8.452   1.00 29.46 ? 380 HOH A O    1 
HETATM 2299 O  O    . HOH G 6 .   ? 9.881   6.088   13.109  1.00 36.71 ? 381 HOH A O    1 
HETATM 2300 O  O    . HOH G 6 .   ? -19.465 17.298  6.059   1.00 22.96 ? 382 HOH A O    1 
HETATM 2301 O  O    . HOH G 6 .   ? 2.549   -13.126 5.133   1.00 24.79 ? 383 HOH A O    1 
HETATM 2302 O  O    . HOH G 6 .   ? -26.989 -6.402  7.705   1.00 33.81 ? 384 HOH A O    1 
HETATM 2303 O  O    . HOH G 6 .   ? -12.098 10.667  5.933   1.00 27.07 ? 385 HOH A O    1 
HETATM 2304 O  O    . HOH G 6 .   ? -25.835 6.163   27.049  1.00 24.17 ? 386 HOH A O    1 
HETATM 2305 O  O    . HOH G 6 .   ? -24.721 12.010  6.341   1.00 28.05 ? 387 HOH A O    1 
HETATM 2306 O  O    . HOH G 6 .   ? 10.198  -2.649  13.769  1.00 27.67 ? 388 HOH A O    1 
HETATM 2307 O  O    . HOH G 6 .   ? -5.978  17.126  27.331  1.00 25.94 ? 389 HOH A O    1 
HETATM 2308 O  O    . HOH G 6 .   ? -15.392 -16.330 25.494  1.00 30.32 ? 390 HOH A O    1 
HETATM 2309 O  O    . HOH G 6 .   ? -18.483 -3.658  -2.541  1.00 27.09 ? 391 HOH A O    1 
HETATM 2310 O  O    . HOH G 6 .   ? -24.768 4.539   8.404   1.00 32.02 ? 392 HOH A O    1 
HETATM 2311 O  O    . HOH G 6 .   ? 11.591  -0.385  16.008  1.00 24.43 ? 393 HOH A O    1 
HETATM 2312 O  O    . HOH G 6 .   ? -17.371 -16.188 21.956  1.00 23.79 ? 394 HOH A O    1 
HETATM 2313 O  O    . HOH G 6 .   ? -3.385  17.983  21.274  1.00 26.69 ? 395 HOH A O    1 
HETATM 2314 O  O    . HOH G 6 .   ? 12.930  -3.739  13.483  1.00 28.27 ? 396 HOH A O    1 
HETATM 2315 O  O    . HOH G 6 .   ? -9.240  3.122   34.711  1.00 25.14 ? 397 HOH A O    1 
HETATM 2316 O  O    . HOH G 6 .   ? 1.970   -15.512 9.240   1.00 24.56 ? 398 HOH A O    1 
HETATM 2317 O  O    . HOH G 6 .   ? -5.170  2.115   37.244  1.00 28.02 ? 399 HOH A O    1 
HETATM 2318 O  O    . HOH G 6 .   ? -11.140 1.129   33.436  1.00 26.73 ? 400 HOH A O    1 
HETATM 2319 O  O    . HOH G 6 .   ? -15.476 -10.250 37.168  1.00 27.36 ? 401 HOH A O    1 
HETATM 2320 O  O    . HOH G 6 .   ? -10.502 4.876   30.689  1.00 26.76 ? 402 HOH A O    1 
HETATM 2321 O  O    . HOH G 6 .   ? -16.942 -7.268  39.726  1.00 26.26 ? 403 HOH A O    1 
HETATM 2322 O  O    . HOH G 6 .   ? -26.678 -1.230  25.902  1.00 22.46 ? 404 HOH A O    1 
HETATM 2323 O  O    . HOH G 6 .   ? -6.657  -5.300  37.243  1.00 20.84 ? 405 HOH A O    1 
HETATM 2324 O  O    . HOH G 6 .   ? 3.757   9.774   23.819  1.00 25.86 ? 406 HOH A O    1 
HETATM 2325 O  O    . HOH G 6 .   ? -7.039  -16.727 1.447   1.00 24.70 ? 407 HOH A O    1 
HETATM 2326 O  O    . HOH G 6 .   ? -1.639  3.039   -6.953  1.00 31.60 ? 408 HOH A O    1 
HETATM 2327 O  O    . HOH G 6 .   ? -0.235  -14.291 22.161  1.00 23.66 ? 409 HOH A O    1 
HETATM 2328 O  O    . HOH G 6 .   ? -27.890 4.996   25.240  1.00 32.33 ? 410 HOH A O    1 
HETATM 2329 O  O    . HOH G 6 .   ? -16.815 -13.938 26.358  1.00 22.80 ? 411 HOH A O    1 
HETATM 2330 O  O    . HOH G 6 .   ? 15.180  -3.985  25.100  1.00 20.82 ? 412 HOH A O    1 
HETATM 2331 O  O    . HOH G 6 .   ? -0.614  6.471   32.089  1.00 27.73 ? 413 HOH A O    1 
HETATM 2332 O  O    . HOH G 6 .   ? -25.307 10.923  19.543  1.00 32.15 ? 414 HOH A O    1 
HETATM 2333 O  O    . HOH G 6 .   ? -17.135 0.114   -3.896  1.00 41.09 ? 415 HOH A O    1 
HETATM 2334 O  O    . HOH G 6 .   ? -22.586 -0.184  -4.957  1.00 20.46 ? 416 HOH A O    1 
HETATM 2335 O  O    . HOH G 6 .   ? -12.822 7.933   29.131  1.00 28.32 ? 417 HOH A O    1 
HETATM 2336 O  O    . HOH G 6 .   ? -9.943  15.559  29.650  1.00 30.26 ? 418 HOH A O    1 
HETATM 2337 O  O    . HOH G 6 .   ? -4.354  -1.070  11.925  1.00 21.79 ? 419 HOH A O    1 
HETATM 2338 O  O    . HOH G 6 .   ? -13.705 -21.163 14.983  1.00 22.14 ? 420 HOH A O    1 
HETATM 2339 O  O    . HOH G 6 .   ? -11.065 -23.582 12.245  1.00 23.22 ? 421 HOH A O    1 
HETATM 2340 O  O    . HOH G 6 .   ? -1.555  -13.164 27.087  1.00 26.01 ? 422 HOH A O    1 
HETATM 2341 O  O    . HOH G 6 .   ? -1.127  -11.141 28.847  1.00 19.32 ? 423 HOH A O    1 
HETATM 2342 O  O    . HOH G 6 .   ? -2.091  -12.184 31.332  1.00 29.67 ? 424 HOH A O    1 
HETATM 2343 O  O    . HOH G 6 .   ? -10.585 21.512  19.858  1.00 23.76 ? 425 HOH A O    1 
HETATM 2344 O  O    . HOH G 6 .   ? -20.835 0.315   -1.061  1.00 34.74 ? 426 HOH A O    1 
HETATM 2345 O  O    . HOH G 6 .   ? -25.552 -10.616 17.619  1.00 24.93 ? 427 HOH A O    1 
HETATM 2346 O  O    . HOH G 6 .   ? -1.043  4.048   14.225  1.00 23.58 ? 428 HOH A O    1 
HETATM 2347 O  O    . HOH G 6 .   ? 5.165   -7.222  22.342  1.00 26.14 ? 429 HOH A O    1 
HETATM 2348 O  O    . HOH G 6 .   ? -14.116 -8.449  -5.347  1.00 30.77 ? 430 HOH A O    1 
HETATM 2349 O  O    . HOH G 6 .   ? -12.789 12.969  31.958  1.00 29.11 ? 431 HOH A O    1 
HETATM 2350 O  O    . HOH G 6 .   ? -2.907  6.068   -1.114  1.00 29.46 ? 432 HOH A O    1 
HETATM 2351 O  O    . HOH G 6 .   ? -2.311  -4.391  -6.843  1.00 30.05 ? 433 HOH A O    1 
HETATM 2352 O  O    . HOH G 6 .   ? 10.248  -6.816  -8.850  1.00 27.98 ? 434 HOH A O    1 
HETATM 2353 O  O    . HOH G 6 .   ? 6.233   -10.921 15.366  1.00 34.87 ? 435 HOH A O    1 
HETATM 2354 O  O    . HOH G 6 .   ? -19.482 -4.372  41.267  1.00 35.54 ? 436 HOH A O    1 
HETATM 2355 O  O    . HOH G 6 .   ? -25.153 -9.729  15.034  1.00 34.62 ? 437 HOH A O    1 
HETATM 2356 O  O    . HOH G 6 .   ? -28.095 5.720   19.184  1.00 27.12 ? 438 HOH A O    1 
HETATM 2357 O  O    . HOH G 6 .   ? -17.130 17.858  4.061   1.00 32.04 ? 439 HOH A O    1 
HETATM 2358 O  O    . HOH G 6 .   ? -10.974 -19.240 6.913   1.00 30.41 ? 440 HOH A O    1 
HETATM 2359 O  O    . HOH G 6 .   ? -4.562  -15.887 0.727   1.00 29.75 ? 441 HOH A O    1 
HETATM 2360 O  O    . HOH G 6 .   ? -12.121 9.414   3.359   1.00 24.17 ? 442 HOH A O    1 
HETATM 2361 O  O    . HOH G 6 .   ? -17.296 -6.720  42.165  1.00 29.75 ? 443 HOH A O    1 
HETATM 2362 O  O    . HOH G 6 .   ? -4.071  -1.802  37.652  1.00 32.55 ? 444 HOH A O    1 
HETATM 2363 O  O    . HOH G 6 .   ? -12.254 16.318  9.054   1.00 28.17 ? 445 HOH A O    1 
HETATM 2364 O  O    . HOH G 6 .   ? -2.004  4.595   -4.891  1.00 32.88 ? 446 HOH A O    1 
HETATM 2365 O  O    . HOH G 6 .   ? -26.270 -7.459  30.353  1.00 30.88 ? 447 HOH A O    1 
HETATM 2366 O  O    . HOH G 6 .   ? -25.553 -3.284  31.564  1.00 35.80 ? 448 HOH A O    1 
HETATM 2367 O  O    . HOH G 6 .   ? 2.168   7.975   27.774  1.00 31.59 ? 449 HOH A O    1 
HETATM 2368 O  O    . HOH G 6 .   ? -11.750 10.797  0.791   1.00 28.87 ? 450 HOH A O    1 
HETATM 2369 O  O    . HOH G 6 .   ? 4.275   -11.496 23.397  1.00 34.95 ? 451 HOH A O    1 
HETATM 2370 O  O    . HOH G 6 .   ? -3.421  -15.635 -2.054  1.00 33.67 ? 452 HOH A O    1 
HETATM 2371 O  O    . HOH G 6 .   ? -11.507 0.856   -7.632  1.00 35.65 ? 453 HOH A O    1 
HETATM 2372 O  O    . HOH G 6 .   ? 0.162   8.315   37.677  1.00 30.88 ? 454 HOH A O    1 
HETATM 2373 O  O    . HOH G 6 .   ? -1.915  -17.432 25.371  1.00 28.78 ? 455 HOH A O    1 
HETATM 2374 O  O    . HOH G 6 .   ? -23.972 -2.564  28.926  1.00 29.86 ? 456 HOH A O    1 
HETATM 2375 O  O    . HOH G 6 .   ? 9.516   2.046   12.069  1.00 33.02 ? 457 HOH A O    1 
HETATM 2376 O  O    . HOH G 6 .   ? -10.436 -5.581  38.114  1.00 28.31 ? 458 HOH A O    1 
HETATM 2377 O  O    . HOH G 6 .   ? 6.229   -5.168  3.557   1.00 41.70 ? 459 HOH A O    1 
HETATM 2378 O  O    . HOH G 6 .   ? -0.475  13.816  16.015  1.00 26.23 ? 460 HOH A O    1 
HETATM 2379 O  O    . HOH G 6 .   ? -22.515 -12.624 24.487  1.00 39.00 ? 461 HOH A O    1 
HETATM 2380 O  O    . HOH G 6 .   ? -25.698 -6.756  33.616  1.00 36.03 ? 462 HOH A O    1 
HETATM 2381 O  O    . HOH G 6 .   ? -17.987 -20.656 -1.291  1.00 32.30 ? 463 HOH A O    1 
HETATM 2382 O  O    . HOH G 6 .   ? -19.985 -13.754 24.289  1.00 35.52 ? 464 HOH A O    1 
HETATM 2383 O  O    . HOH G 6 .   ? -14.066 3.679   33.190  1.00 34.88 ? 465 HOH A O    1 
HETATM 2384 O  O    . HOH G 6 .   ? 3.856   -2.952  4.196   1.00 33.55 ? 466 HOH A O    1 
HETATM 2385 O  O    . HOH G 6 .   ? -8.501  -19.938 26.595  1.00 29.86 ? 467 HOH A O    1 
HETATM 2386 O  O    . HOH G 6 .   ? -0.301  -20.560 14.635  1.00 34.07 ? 468 HOH A O    1 
HETATM 2387 O  O    . HOH G 6 .   ? -20.009 -15.532 22.320  1.00 31.20 ? 469 HOH A O    1 
HETATM 2388 O  O    . HOH G 6 .   ? -10.299 -20.316 24.904  1.00 28.61 ? 470 HOH A O    1 
HETATM 2389 O  O    . HOH G 6 .   ? -27.937 -1.522  28.347  1.00 31.64 ? 471 HOH A O    1 
HETATM 2390 O  O    . HOH G 6 .   ? -2.997  7.071   -8.062  1.00 28.30 ? 472 HOH A O    1 
HETATM 2391 O  O    . HOH G 6 .   ? -27.479 -0.102  15.004  1.00 25.93 ? 473 HOH A O    1 
HETATM 2392 O  O    . HOH G 6 .   ? -6.604  12.572  10.137  1.00 32.88 ? 474 HOH A O    1 
HETATM 2393 O  O    . HOH G 6 .   ? -20.950 0.908   -6.527  1.00 26.23 ? 475 HOH A O    1 
HETATM 2394 O  O    . HOH G 6 .   ? 5.463   9.001   21.862  1.00 31.78 ? 476 HOH A O    1 
HETATM 2395 O  O    . HOH G 6 .   ? -6.040  -20.672 26.415  1.00 32.01 ? 477 HOH A O    1 
HETATM 2396 O  O    . HOH G 6 .   ? -0.888  -17.206 -2.112  1.00 34.62 ? 478 HOH A O    1 
HETATM 2397 O  O    . HOH G 6 .   ? 1.837   -9.824  30.511  1.00 33.95 ? 479 HOH A O    1 
HETATM 2398 O  O    . HOH G 6 .   ? 3.069   1.690   -2.190  1.00 37.45 ? 480 HOH A O    1 
HETATM 2399 O  O    . HOH G 6 .   ? -12.954 10.726  35.769  1.00 36.04 ? 481 HOH A O    1 
HETATM 2400 O  O    . HOH G 6 .   ? -0.433  1.022   -10.836 1.00 29.51 ? 482 HOH A O    1 
HETATM 2401 O  O    . HOH G 6 .   ? -15.976 3.472   35.088  1.00 38.93 ? 483 HOH A O    1 
HETATM 2402 O  O    . HOH G 6 .   ? 1.988   -4.392  -12.226 1.00 34.11 ? 484 HOH A O    1 
HETATM 2403 O  O    . HOH G 6 .   ? -16.718 -17.908 20.124  1.00 30.40 ? 485 HOH A O    1 
HETATM 2404 O  O    . HOH G 6 .   ? -27.777 6.238   21.544  1.00 34.60 ? 486 HOH A O    1 
HETATM 2405 O  O    . HOH G 6 .   ? 0.386   0.802   -6.675  1.00 29.83 ? 487 HOH A O    1 
HETATM 2406 O  O    . HOH G 6 .   ? 0.345   17.755  24.478  1.00 37.64 ? 488 HOH A O    1 
HETATM 2407 O  O    . HOH G 6 .   ? -29.708 4.078   27.282  1.00 35.02 ? 489 HOH A O    1 
HETATM 2408 O  O    . HOH G 6 .   ? -27.740 2.434   23.347  1.00 31.03 ? 490 HOH A O    1 
HETATM 2409 O  O    . HOH G 6 .   ? -19.493 -15.133 25.937  1.00 36.34 ? 491 HOH A O    1 
HETATM 2410 O  O    . HOH G 6 .   ? -26.035 2.171   39.035  1.00 40.19 ? 492 HOH A O    1 
HETATM 2411 O  O    . HOH G 6 .   ? -13.920 0.148   42.575  1.00 39.58 ? 493 HOH A O    1 
HETATM 2412 O  O    . HOH G 6 .   ? 6.407   5.289   28.716  1.00 30.98 ? 494 HOH A O    1 
HETATM 2413 O  O    . HOH G 6 .   ? -16.441 -15.449 32.591  1.00 33.89 ? 495 HOH A O    1 
HETATM 2414 O  O    . HOH G 6 .   ? -25.131 8.542   26.150  1.00 40.00 ? 496 HOH A O    1 
HETATM 2415 O  O    . HOH G 6 .   ? 8.185   3.161   27.617  1.00 32.29 ? 497 HOH A O    1 
HETATM 2416 O  O    . HOH G 6 .   ? -12.841 3.698   -6.796  1.00 29.42 ? 498 HOH A O    1 
HETATM 2417 O  O    . HOH G 6 .   ? -23.522 -17.982 6.157   1.00 32.38 ? 499 HOH A O    1 
HETATM 2418 O  O    . HOH G 6 .   ? -20.890 -6.831  -1.983  1.00 30.64 ? 500 HOH A O    1 
HETATM 2419 O  O    . HOH G 6 .   ? -16.146 -12.410 -6.359  1.00 30.79 ? 501 HOH A O    1 
HETATM 2420 O  O    . HOH G 6 .   ? -23.333 -11.160 17.106  1.00 27.49 ? 502 HOH A O    1 
HETATM 2421 O  O    . HOH G 6 .   ? -26.862 -12.866 20.294  1.00 34.85 ? 503 HOH A O    1 
HETATM 2422 O  O    . HOH G 6 .   ? -10.700 8.609   7.655   1.00 27.63 ? 504 HOH A O    1 
HETATM 2423 O  O    . HOH G 6 .   ? -7.090  6.055   6.423   1.00 20.69 ? 505 HOH A O    1 
HETATM 2424 O  O    . HOH G 6 .   ? -8.211  7.579   8.406   1.00 28.33 ? 506 HOH A O    1 
HETATM 2425 O  O    . HOH G 6 .   ? -2.978  -20.217 29.409  1.00 29.02 ? 507 HOH A O    1 
HETATM 2426 O  O    . HOH G 6 .   ? -11.560 8.946   33.059  1.00 39.34 ? 508 HOH A O    1 
HETATM 2427 O  O    . HOH G 6 .   ? 6.493   8.478   18.038  1.00 29.76 ? 509 HOH A O    1 
HETATM 2428 O  O    . HOH G 6 .   ? -2.499  -14.794 32.835  1.00 31.36 ? 510 HOH A O    1 
HETATM 2429 O  O    . HOH G 6 .   ? -21.917 -14.077 18.515  1.00 28.13 ? 511 HOH A O    1 
HETATM 2430 O  O    . HOH G 6 .   ? -10.273 15.019  5.872   1.00 40.46 ? 512 HOH A O    1 
HETATM 2431 O  O    . HOH G 6 .   ? -13.532 -0.798  -5.999  1.00 33.90 ? 513 HOH A O    1 
HETATM 2432 O  O    . HOH G 6 .   ? 5.010   -12.721 -5.803  1.00 28.46 ? 514 HOH A O    1 
HETATM 2433 O  O    . HOH G 6 .   ? -18.160 -23.957 -3.990  1.00 33.02 ? 515 HOH A O    1 
HETATM 2434 O  O    . HOH G 6 .   ? 6.948   -3.598  29.937  1.00 35.91 ? 516 HOH A O    1 
HETATM 2435 O  O    . HOH G 6 .   ? 6.433   -5.059  27.437  1.00 38.42 ? 517 HOH A O    1 
HETATM 2436 O  O    . HOH G 6 .   ? 1.401   -16.118 -1.902  1.00 43.77 ? 518 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   ? 0.3402 0.3307 0.4070 -0.0293 0.0619  0.0459  4   HIS A N    
2    C  CA   . HIS A 4   ? 0.3331 0.3101 0.4182 -0.0411 0.0422  0.0216  4   HIS A CA   
3    C  C    . HIS A 4   ? 0.2679 0.2681 0.3790 -0.0335 0.0679  -0.0044 4   HIS A C    
4    O  O    . HIS A 4   ? 0.2920 0.2553 0.4003 -0.0508 0.0533  -0.0150 4   HIS A O    
5    C  CB   . HIS A 4   ? 0.3557 0.3391 0.4326 -0.0244 0.0343  0.0176  4   HIS A CB   
6    C  CG   . HIS A 4   ? 0.4172 0.4290 0.4885 -0.0096 -0.0083 0.0224  4   HIS A CG   
7    N  ND1  . HIS A 4   ? 0.4467 0.5335 0.5028 -0.0147 0.0051  0.0223  4   HIS A ND1  
8    C  CD2  . HIS A 4   ? 0.4845 0.4906 0.5105 0.0014  -0.0024 -0.0066 4   HIS A CD2  
9    C  CE1  . HIS A 4   ? 0.5008 0.5241 0.5366 -0.0097 -0.0148 0.0081  4   HIS A CE1  
10   N  NE2  . HIS A 4   ? 0.5167 0.5361 0.5456 -0.0105 -0.0082 -0.0134 4   HIS A NE2  
11   N  N    . TRP A 5   ? 0.2349 0.2488 0.3591 -0.0381 0.0709  -0.0210 5   TRP A N    
12   C  CA   . TRP A 5   ? 0.1763 0.1729 0.3057 -0.0470 0.0596  -0.0197 5   TRP A CA   
13   C  C    . TRP A 5   ? 0.1954 0.1833 0.3059 -0.0278 0.0612  -0.0216 5   TRP A C    
14   O  O    . TRP A 5   ? 0.2161 0.2057 0.3094 -0.0360 0.0538  -0.0113 5   TRP A O    
15   C  CB   . TRP A 5   ? 0.1516 0.1542 0.3125 -0.0460 0.0589  -0.0277 5   TRP A CB   
16   C  CG   . TRP A 5   ? 0.2071 0.1390 0.2939 -0.0518 0.0644  0.0053  5   TRP A CG   
17   C  CD1  . TRP A 5   ? 0.2691 0.1885 0.2824 0.0027  0.0502  0.0310  5   TRP A CD1  
18   C  CD2  . TRP A 5   ? 0.1846 0.1474 0.2528 -0.0313 0.0034  -0.0313 5   TRP A CD2  
19   N  NE1  . TRP A 5   ? 0.2411 0.1905 0.2722 -0.0437 0.0519  0.0181  5   TRP A NE1  
20   C  CE2  . TRP A 5   ? 0.1842 0.1730 0.2309 -0.0290 0.0286  -0.0057 5   TRP A CE2  
21   C  CE3  . TRP A 5   ? 0.1704 0.1669 0.2141 -0.0431 0.0557  -0.0609 5   TRP A CE3  
22   C  CZ2  . TRP A 5   ? 0.2468 0.2143 0.2430 -0.0248 0.0020  -0.0231 5   TRP A CZ2  
23   C  CZ3  . TRP A 5   ? 0.1861 0.1611 0.2272 -0.0073 0.0185  -0.0173 5   TRP A CZ3  
24   C  CH2  . TRP A 5   ? 0.1949 0.1717 0.2147 0.0076  0.0029  -0.0317 5   TRP A CH2  
25   N  N    . GLY A 6   ? 0.1781 0.1359 0.2986 -0.0418 0.0663  -0.0413 6   GLY A N    
26   C  CA   . GLY A 6   ? 0.1773 0.1426 0.2936 -0.0313 0.0491  -0.0306 6   GLY A CA   
27   C  C    . GLY A 6   ? 0.1479 0.1465 0.2861 -0.0219 0.0635  -0.0289 6   GLY A C    
28   O  O    . GLY A 6   ? 0.1424 0.1338 0.2886 -0.0126 0.0672  -0.0395 6   GLY A O    
29   N  N    . TYR A 7   ? 0.1700 0.1366 0.3231 -0.0299 0.0820  -0.0371 7   TYR A N    
30   C  CA   . TYR A 7   ? 0.1859 0.1313 0.3657 -0.0228 0.0811  -0.0312 7   TYR A CA   
31   C  C    . TYR A 7   ? 0.2038 0.1355 0.4182 -0.0100 0.0784  -0.0437 7   TYR A C    
32   O  O    . TYR A 7   ? 0.2449 0.1757 0.5240 -0.0083 0.1109  -0.0131 7   TYR A O    
33   C  CB   . TYR A 7   ? 0.1447 0.1375 0.3262 -0.0108 0.0818  -0.0544 7   TYR A CB   
34   C  CG   . TYR A 7   ? 0.1389 0.0726 0.2578 -0.0385 0.0403  -0.0352 7   TYR A CG   
35   C  CD1  . TYR A 7   ? 0.1039 0.1324 0.2123 -0.0532 0.0356  -0.0347 7   TYR A CD1  
36   C  CD2  . TYR A 7   ? 0.1122 0.0986 0.2482 -0.0231 0.0459  -0.0371 7   TYR A CD2  
37   C  CE1  . TYR A 7   ? 0.1150 0.0523 0.2405 0.0033  0.0259  -0.0094 7   TYR A CE1  
38   C  CE2  . TYR A 7   ? 0.1404 0.1363 0.2111 -0.0185 0.0466  -0.0278 7   TYR A CE2  
39   C  CZ   . TYR A 7   ? 0.1322 0.0855 0.1991 -0.0321 0.0313  -0.0278 7   TYR A CZ   
40   O  OH   . TYR A 7   ? 0.1205 0.0833 0.2235 -0.0202 0.0384  -0.0216 7   TYR A OH   
41   N  N    . GLY A 8   ? 0.2204 0.1525 0.4421 0.0013  0.0894  -0.0606 8   GLY A N    
42   C  CA   . GLY A 8   ? 0.1933 0.1551 0.4521 0.0131  0.1029  -0.0589 8   GLY A CA   
43   C  C    . GLY A 8   ? 0.2700 0.2235 0.4387 0.0005  0.0825  -0.0425 8   GLY A C    
44   O  O    . GLY A 8   ? 0.2408 0.3074 0.4798 -0.0025 0.1080  -0.0538 8   GLY A O    
45   N  N    . LYS A 9   ? 0.2630 0.2681 0.4770 0.0204  0.0595  -0.0258 9   LYS A N    
46   C  CA   . LYS A 9   ? 0.3021 0.2940 0.4556 0.0012  0.0330  -0.0332 9   LYS A CA   
47   C  C    . LYS A 9   ? 0.2647 0.3115 0.4377 0.0065  0.0501  -0.0158 9   LYS A C    
48   O  O    . LYS A 9   ? 0.2185 0.3314 0.4641 -0.0252 0.0475  -0.0347 9   LYS A O    
49   C  CB   . LYS A 9   ? 0.2955 0.3269 0.4605 0.0135  0.0300  -0.0174 9   LYS A CB   
50   C  CG   . LYS A 9   ? 0.3256 0.3269 0.4098 0.0000  0.0176  -0.0139 9   LYS A CG   
51   C  CD   . LYS A 9   ? 0.3374 0.3416 0.3749 0.0022  0.0046  -0.0044 9   LYS A CD   
52   C  CE   . LYS A 9   ? 0.3438 0.3436 0.3626 -0.0002 0.0036  -0.0024 9   LYS A CE   
53   N  NZ   . LYS A 9   ? 0.3440 0.3445 0.3554 0.0002  0.0008  -0.0017 9   LYS A NZ   
54   N  N    . HIS A 10  ? 0.2031 0.2207 0.4273 0.0442  0.0982  -0.0355 10  HIS A N    
55   C  CA   . HIS A 10  ? 0.2310 0.2451 0.4103 0.0344  0.0957  -0.0253 10  HIS A CA   
56   C  C    . HIS A 10  ? 0.1910 0.2160 0.3749 0.0506  0.0867  -0.0208 10  HIS A C    
57   O  O    . HIS A 10  ? 0.1945 0.2563 0.3972 0.0438  0.0946  -0.0255 10  HIS A O    
58   C  CB   . HIS A 10  ? 0.2521 0.2301 0.3852 0.0399  0.1157  -0.0385 10  HIS A CB   
59   C  CG   . HIS A 10  ? 0.2825 0.3043 0.4108 0.0330  0.0741  0.0111  10  HIS A CG   
60   N  ND1  . HIS A 10  ? 0.3145 0.2874 0.4436 0.0423  0.0863  -0.0169 10  HIS A ND1  
61   C  CD2  . HIS A 10  ? 0.2526 0.3084 0.4676 -0.0273 0.1040  0.0237  10  HIS A CD2  
62   C  CE1  . HIS A 10  ? 0.3269 0.2945 0.4155 0.0611  0.0631  -0.0097 10  HIS A CE1  
63   N  NE2  . HIS A 10  ? 0.2432 0.3176 0.4229 0.0216  0.0742  -0.0170 10  HIS A NE2  
64   N  N    . ASN A 11  ? 0.1479 0.1988 0.3593 0.0442  0.0944  -0.0141 11  ASN A N    
65   C  CA   . ASN A 11  ? 0.1620 0.1785 0.3047 0.0080  0.0810  -0.0271 11  ASN A CA   
66   C  C    . ASN A 11  ? 0.1661 0.1840 0.2955 0.0166  0.0753  -0.0284 11  ASN A C    
67   O  O    . ASN A 11  ? 0.1515 0.1531 0.3130 0.0135  0.0695  -0.0296 11  ASN A O    
68   C  CB   . ASN A 11  ? 0.1804 0.1925 0.2894 0.0266  0.0737  -0.0253 11  ASN A CB   
69   C  CG   . ASN A 11  ? 0.1741 0.2073 0.3085 0.0144  0.0989  -0.0422 11  ASN A CG   
70   O  OD1  . ASN A 11  ? 0.2000 0.2490 0.3301 -0.0352 0.0890  -0.0174 11  ASN A OD1  
71   N  ND2  . ASN A 11  ? 0.2320 0.1989 0.3353 -0.0077 0.0460  -0.0030 11  ASN A ND2  
72   N  N    . GLY A 12  ? 0.1584 0.2047 0.2850 0.0043  0.0849  -0.0300 12  GLY A N    
73   C  CA   . GLY A 12  ? 0.1503 0.1981 0.2684 0.0002  0.0694  -0.0178 12  GLY A CA   
74   C  C    . GLY A 12  ? 0.1295 0.1561 0.2746 0.0108  0.0605  -0.0249 12  GLY A C    
75   O  O    . GLY A 12  ? 0.0920 0.1418 0.3168 0.0251  0.0388  -0.0037 12  GLY A O    
76   N  N    . PRO A 13  ? 0.1069 0.1308 0.2488 -0.0126 0.0486  -0.0227 13  PRO A N    
77   C  CA   . PRO A 13  ? 0.1225 0.1265 0.2578 -0.0053 0.0407  -0.0148 13  PRO A CA   
78   C  C    . PRO A 13  ? 0.1183 0.1023 0.2397 0.0117  0.0353  -0.0151 13  PRO A C    
79   O  O    . PRO A 13  ? 0.1181 0.1201 0.2775 0.0016  0.0392  -0.0324 13  PRO A O    
80   C  CB   . PRO A 13  ? 0.1057 0.1367 0.2455 -0.0306 0.0567  -0.0086 13  PRO A CB   
81   C  CG   . PRO A 13  ? 0.1457 0.1552 0.2376 -0.0063 0.0464  -0.0305 13  PRO A CG   
82   C  CD   . PRO A 13  ? 0.1169 0.1338 0.2726 -0.0044 0.0434  -0.0230 13  PRO A CD   
83   N  N    . GLU A 14  ? 0.1327 0.1043 0.2869 0.0177  0.0285  0.0080  14  GLU A N    
84   C  CA   . GLU A 14  ? 0.1594 0.1252 0.2998 0.0290  0.0131  0.0192  14  GLU A CA   
85   C  C    . GLU A 14  ? 0.1257 0.1467 0.2828 0.0325  0.0217  -0.0006 14  GLU A C    
86   O  O    . GLU A 14  ? 0.1575 0.1512 0.3213 0.0405  0.0054  0.0116  14  GLU A O    
87   C  CB   . GLU A 14  ? 0.2156 0.1796 0.3529 0.0317  0.0179  0.0126  14  GLU A CB   
88   C  CG   . GLU A 14  ? 0.2483 0.2929 0.3726 0.0273  0.0041  -0.0236 14  GLU A CG   
89   C  CD   . GLU A 14  ? 0.3653 0.3170 0.4202 0.0411  -0.0011 -0.0347 14  GLU A CD   
90   O  OE1  . GLU A 14  ? 0.3328 0.1874 0.4012 0.1027  -0.0197 -0.0757 14  GLU A OE1  
91   O  OE2  . GLU A 14  ? 0.4594 0.2466 0.4025 0.0301  0.0388  -0.0444 14  GLU A OE2  
92   N  N    . HIS A 15  ? 0.1118 0.1114 0.2822 0.0234  0.0166  -0.0009 15  HIS A N    
93   C  CA   . HIS A 15  ? 0.1073 0.1181 0.2873 0.0143  0.0313  -0.0155 15  HIS A CA   
94   C  C    . HIS A 15  ? 0.0863 0.1072 0.2781 0.0245  0.0077  -0.0200 15  HIS A C    
95   O  O    . HIS A 15  ? 0.0686 0.1148 0.3308 0.0067  -0.0028 -0.0220 15  HIS A O    
96   C  CB   . HIS A 15  ? 0.1189 0.1254 0.3039 0.0266  0.0321  -0.0044 15  HIS A CB   
97   C  CG   . HIS A 15  ? 0.1164 0.1638 0.2996 0.0122  0.0670  0.0206  15  HIS A CG   
98   N  ND1  . HIS A 15  ? 0.1436 0.1982 0.3307 0.0486  0.0378  -0.0396 15  HIS A ND1  
99   C  CD2  . HIS A 15  ? 0.1781 0.1578 0.3331 0.0724  0.0424  -0.0089 15  HIS A CD2  
100  C  CE1  . HIS A 15  ? 0.2141 0.1890 0.3484 0.0709  0.0229  -0.0090 15  HIS A CE1  
101  N  NE2  . HIS A 15  ? 0.1955 0.1736 0.3682 0.0873  0.0557  -0.0346 15  HIS A NE2  
102  N  N    . TRP A 16  ? 0.0710 0.1126 0.2820 0.0295  0.0238  -0.0029 16  TRP A N    
103  C  CA   . TRP A 16  ? 0.0826 0.0809 0.2712 0.0217  -0.0077 -0.0266 16  TRP A CA   
104  C  C    . TRP A 16  ? 0.0850 0.0919 0.2709 -0.0011 0.0148  -0.0138 16  TRP A C    
105  O  O    . TRP A 16  ? 0.0876 0.0848 0.3096 -0.0060 0.0036  -0.0015 16  TRP A O    
106  C  CB   . TRP A 16  ? 0.0501 0.0956 0.2673 -0.0315 0.0125  -0.0276 16  TRP A CB   
107  C  CG   . TRP A 16  ? 0.0893 0.0797 0.2569 -0.0129 0.0115  -0.0036 16  TRP A CG   
108  C  CD1  . TRP A 16  ? 0.0817 0.1328 0.2465 -0.0038 0.0269  -0.0086 16  TRP A CD1  
109  C  CD2  . TRP A 16  ? 0.0684 0.0835 0.2393 -0.0087 0.0024  -0.0314 16  TRP A CD2  
110  N  NE1  . TRP A 16  ? 0.0569 0.1076 0.2598 0.0049  0.0086  -0.0404 16  TRP A NE1  
111  C  CE2  . TRP A 16  ? 0.0820 0.0825 0.2224 0.0047  0.0144  0.0046  16  TRP A CE2  
112  C  CE3  . TRP A 16  ? 0.0690 0.0661 0.2588 -0.0057 0.0493  -0.0002 16  TRP A CE3  
113  C  CZ2  . TRP A 16  ? 0.0901 0.0836 0.2241 -0.0115 0.0059  -0.0176 16  TRP A CZ2  
114  C  CZ3  . TRP A 16  ? 0.0656 0.1302 0.2228 -0.0138 0.0117  -0.0217 16  TRP A CZ3  
115  C  CH2  . TRP A 16  ? 0.1177 0.1296 0.2006 0.0080  0.0257  -0.0231 16  TRP A CH2  
116  N  N    . HIS A 17  ? 0.0716 0.1407 0.2656 0.0062  0.0105  -0.0181 17  HIS A N    
117  C  CA   . HIS A 17  ? 0.0885 0.1526 0.2818 0.0010  0.0054  -0.0017 17  HIS A CA   
118  C  C    . HIS A 17  ? 0.0841 0.1566 0.3014 -0.0078 0.0128  -0.0033 17  HIS A C    
119  O  O    . HIS A 17  ? 0.0891 0.1628 0.3160 -0.0022 0.0261  -0.0137 17  HIS A O    
120  C  CB   . HIS A 17  ? 0.0712 0.1536 0.2778 0.0187  0.0001  0.0112  17  HIS A CB   
121  C  CG   . HIS A 17  ? 0.0751 0.1428 0.3044 -0.0105 0.0191  0.0069  17  HIS A CG   
122  N  ND1  . HIS A 17  ? 0.1226 0.1794 0.3389 0.0071  0.0047  0.0493  17  HIS A ND1  
123  C  CD2  . HIS A 17  ? 0.1087 0.1480 0.3079 0.0252  0.0355  0.0236  17  HIS A CD2  
124  C  CE1  . HIS A 17  ? 0.1368 0.1653 0.3236 0.0843  -0.0151 0.0350  17  HIS A CE1  
125  N  NE2  . HIS A 17  ? 0.1024 0.1919 0.3364 0.0148  0.0171  0.0416  17  HIS A NE2  
126  N  N    . LYS A 18  ? 0.0743 0.1541 0.3206 -0.0119 0.0163  0.0024  18  LYS A N    
127  C  CA   . LYS A 18  ? 0.0726 0.1567 0.3354 -0.0163 0.0273  -0.0043 18  LYS A CA   
128  C  C    . LYS A 18  ? 0.0806 0.1720 0.3528 -0.0463 0.0146  0.0117  18  LYS A C    
129  O  O    . LYS A 18  ? 0.1005 0.1908 0.4187 -0.0574 -0.0199 0.0461  18  LYS A O    
130  C  CB   . LYS A 18  ? 0.0730 0.1757 0.3508 0.0128  0.0224  0.0049  18  LYS A CB   
131  C  CG   . LYS A 18  ? 0.0841 0.1632 0.3601 0.0395  0.0096  0.0051  18  LYS A CG   
132  C  CD   . LYS A 18  ? 0.0558 0.1920 0.3305 0.0038  0.0495  0.0343  18  LYS A CD   
133  C  CE   . LYS A 18  ? 0.0595 0.1468 0.3579 0.0043  0.0495  0.0025  18  LYS A CE   
134  N  NZ   . LYS A 18  ? 0.0807 0.1999 0.3189 0.0562  0.0190  0.0420  18  LYS A NZ   
135  N  N    . ASP A 19  ? 0.0856 0.1567 0.3244 -0.0244 0.0160  0.0217  19  ASP A N    
136  C  CA   . ASP A 19  ? 0.0983 0.1907 0.3327 -0.0422 0.0276  0.0109  19  ASP A CA   
137  C  C    . ASP A 19  ? 0.0936 0.1400 0.3536 -0.0380 0.0230  -0.0017 19  ASP A C    
138  O  O    . ASP A 19  ? 0.1388 0.1319 0.3920 -0.0346 0.0377  0.0137  19  ASP A O    
139  C  CB   . ASP A 19  ? 0.1158 0.2696 0.3183 -0.0113 0.0250  0.0188  19  ASP A CB   
140  C  CG   . ASP A 19  ? 0.1583 0.3109 0.3266 -0.0307 0.0143  -0.0020 19  ASP A CG   
141  O  OD1  . ASP A 19  ? 0.1517 0.3370 0.4380 -0.0490 0.0671  0.0217  19  ASP A OD1  
142  O  OD2  . ASP A 19  ? 0.3629 0.4334 0.4569 -0.0228 0.0202  -0.0144 19  ASP A OD2  
143  N  N    . PHE A 20  ? 0.0735 0.1361 0.3397 -0.0389 0.0206  0.0000  20  PHE A N    
144  C  CA   . PHE A 20  ? 0.0956 0.1462 0.2844 -0.0254 0.0023  -0.0239 20  PHE A CA   
145  C  C    . PHE A 20  ? 0.0914 0.1372 0.2711 -0.0227 -0.0018 -0.0052 20  PHE A C    
146  O  O    . PHE A 20  ? 0.0895 0.1252 0.2881 0.0019  0.0082  -0.0142 20  PHE A O    
147  C  CB   . PHE A 20  ? 0.0815 0.1637 0.2871 -0.0282 0.0074  0.0001  20  PHE A CB   
148  C  CG   . PHE A 20  ? 0.0789 0.1434 0.2658 -0.0190 0.0207  0.0044  20  PHE A CG   
149  C  CD1  . PHE A 20  ? 0.0837 0.2205 0.3069 0.0100  0.0129  0.0371  20  PHE A CD1  
150  C  CD2  . PHE A 20  ? 0.1362 0.1705 0.2650 -0.0443 0.0432  0.0093  20  PHE A CD2  
151  C  CE1  . PHE A 20  ? 0.1410 0.2305 0.2742 -0.0079 0.0074  0.0262  20  PHE A CE1  
152  C  CE2  . PHE A 20  ? 0.1502 0.2200 0.2993 -0.0122 0.0024  0.0073  20  PHE A CE2  
153  C  CZ   . PHE A 20  ? 0.1219 0.2236 0.2865 -0.0416 0.0463  0.0516  20  PHE A CZ   
154  N  N    A PRO A 21  ? 0.0959 0.1424 0.2687 -0.0210 -0.0041 -0.0057 21  PRO A N    
155  N  N    B PRO A 21  ? 0.0965 0.1300 0.2705 -0.0233 0.0004  -0.0063 21  PRO A N    
156  C  CA   A PRO A 21  ? 0.0864 0.1641 0.2555 -0.0320 -0.0220 -0.0088 21  PRO A CA   
157  C  CA   B PRO A 21  ? 0.0728 0.1356 0.2506 -0.0375 -0.0169 -0.0127 21  PRO A CA   
158  C  C    A PRO A 21  ? 0.0863 0.1329 0.2382 -0.0171 -0.0150 -0.0078 21  PRO A C    
159  C  C    B PRO A 21  ? 0.0654 0.1071 0.2361 -0.0173 -0.0172 -0.0101 21  PRO A C    
160  O  O    A PRO A 21  ? 0.0825 0.1527 0.2683 -0.0409 -0.0781 -0.0173 21  PRO A O    
161  O  O    B PRO A 21  ? 0.0734 0.1111 0.2512 -0.0107 -0.0324 0.0031  21  PRO A O    
162  C  CB   A PRO A 21  ? 0.0834 0.1575 0.2692 -0.0334 -0.0177 -0.0167 21  PRO A CB   
163  C  CB   B PRO A 21  ? 0.0735 0.1251 0.2862 -0.0536 -0.0218 -0.0074 21  PRO A CB   
164  C  CG   A PRO A 21  ? 0.1095 0.1679 0.2626 -0.0388 -0.0400 -0.0053 21  PRO A CG   
165  C  CG   B PRO A 21  ? 0.1635 0.1583 0.2693 -0.0194 -0.0078 -0.0062 21  PRO A CG   
166  C  CD   A PRO A 21  ? 0.1187 0.1449 0.2769 -0.0412 -0.0077 0.0018  21  PRO A CD   
167  C  CD   B PRO A 21  ? 0.1245 0.1376 0.2825 -0.0447 0.0007  0.0013  21  PRO A CD   
168  N  N    A ILE A 22  ? 0.0623 0.1311 0.2291 -0.0117 -0.0096 -0.0138 22  ILE A N    
169  N  N    B ILE A 22  ? 0.0423 0.0819 0.2205 -0.0098 -0.0074 -0.0215 22  ILE A N    
170  C  CA   A ILE A 22  ? 0.0931 0.1020 0.2221 -0.0130 -0.0059 -0.0100 22  ILE A CA   
171  C  CA   B ILE A 22  ? 0.0524 0.0920 0.1984 -0.0083 -0.0233 -0.0118 22  ILE A CA   
172  C  C    A ILE A 22  ? 0.1150 0.0918 0.2162 0.0020  -0.0067 -0.0086 22  ILE A C    
173  C  C    B ILE A 22  ? 0.1072 0.0882 0.2177 0.0136  -0.0023 -0.0086 22  ILE A C    
174  O  O    A ILE A 22  ? 0.0898 0.0759 0.2407 -0.0067 -0.0175 -0.0079 22  ILE A O    
175  O  O    B ILE A 22  ? 0.0721 0.1075 0.2493 0.0247  -0.0066 0.0012  22  ILE A O    
176  C  CB   A ILE A 22  ? 0.1169 0.1046 0.2062 0.0074  0.0004  -0.0129 22  ILE A CB   
177  C  CB   B ILE A 22  ? 0.1053 0.0613 0.1950 0.0050  -0.0196 -0.0215 22  ILE A CB   
178  C  CG1  A ILE A 22  ? 0.1489 0.1578 0.2165 0.0095  0.0012  -0.0104 22  ILE A CG1  
179  C  CG1  B ILE A 22  ? 0.0611 0.0714 0.1864 -0.0378 -0.0351 0.0096  22  ILE A CG1  
180  C  CG2  A ILE A 22  ? 0.0824 0.1568 0.2130 -0.0079 -0.0225 0.0051  22  ILE A CG2  
181  C  CG2  B ILE A 22  ? 0.1039 0.1357 0.1695 -0.0473 -0.0210 -0.0037 22  ILE A CG2  
182  C  CD1  A ILE A 22  ? 0.1534 0.1639 0.2461 0.0121  -0.0178 -0.0084 22  ILE A CD1  
183  C  CD1  B ILE A 22  ? 0.0485 0.1010 0.2389 0.0166  -0.0330 0.0134  22  ILE A CD1  
184  N  N    . ALA A 23  ? 0.1101 0.0762 0.2469 -0.0032 -0.0124 -0.0200 23  ALA A N    
185  C  CA   . ALA A 23  ? 0.1300 0.0611 0.2366 -0.0107 0.0057  -0.0112 23  ALA A CA   
186  C  C    . ALA A 23  ? 0.0694 0.1088 0.2404 0.0104  -0.0052 -0.0126 23  ALA A C    
187  O  O    . ALA A 23  ? 0.1263 0.1030 0.2545 -0.0220 0.0119  -0.0006 23  ALA A O    
188  C  CB   . ALA A 23  ? 0.1097 0.0954 0.2662 -0.0049 -0.0069 -0.0198 23  ALA A CB   
189  N  N    . LYS A 24  ? 0.1192 0.1131 0.2430 -0.0008 -0.0252 -0.0104 24  LYS A N    
190  C  CA   . LYS A 24  ? 0.1133 0.1668 0.2456 0.0071  -0.0171 -0.0054 24  LYS A CA   
191  C  C    . LYS A 24  ? 0.1224 0.1869 0.2454 -0.0064 -0.0160 -0.0174 24  LYS A C    
192  O  O    . LYS A 24  ? 0.1235 0.2265 0.2958 0.0024  -0.0251 0.0008  24  LYS A O    
193  C  CB   . LYS A 24  ? 0.1337 0.1773 0.2683 0.0119  -0.0082 0.0073  24  LYS A CB   
194  C  CG   . LYS A 24  ? 0.1417 0.2214 0.2748 0.0211  0.0059  0.0051  24  LYS A CG   
195  C  CD   . LYS A 24  ? 0.2188 0.2760 0.3969 0.0562  0.0109  0.0107  24  LYS A CD   
196  C  CE   . LYS A 24  ? 0.2593 0.3187 0.3883 0.0331  0.0238  0.0000  24  LYS A CE   
197  N  NZ   . LYS A 24  ? 0.3635 0.3244 0.4643 0.0245  0.0226  -0.0060 24  LYS A NZ   
198  N  N    . GLY A 25  ? 0.1404 0.1320 0.2597 0.0008  -0.0026 -0.0216 25  GLY A N    
199  C  CA   . GLY A 25  ? 0.1243 0.1636 0.2626 -0.0117 0.0051  -0.0282 25  GLY A CA   
200  C  C    . GLY A 25  ? 0.1236 0.1564 0.2320 -0.0082 -0.0078 -0.0398 25  GLY A C    
201  O  O    . GLY A 25  ? 0.1321 0.1729 0.2488 -0.0043 -0.0183 -0.0220 25  GLY A O    
202  N  N    . GLU A 26  ? 0.1357 0.1776 0.2374 -0.0013 -0.0159 -0.0443 26  GLU A N    
203  C  CA   . GLU A 26  ? 0.1474 0.1898 0.2250 -0.0048 -0.0076 -0.0328 26  GLU A CA   
204  C  C    . GLU A 26  ? 0.1356 0.1573 0.2027 0.0127  0.0000  -0.0286 26  GLU A C    
205  O  O    . GLU A 26  ? 0.1698 0.2198 0.1929 -0.0154 -0.0192 -0.0085 26  GLU A O    
206  C  CB   . GLU A 26  ? 0.1613 0.2239 0.2252 -0.0094 -0.0321 -0.0486 26  GLU A CB   
207  C  CG   . GLU A 26  ? 0.2066 0.2608 0.2553 0.0019  -0.0207 -0.0239 26  GLU A CG   
208  C  CD   . GLU A 26  ? 0.3050 0.3291 0.3596 0.0127  -0.0212 0.0105  26  GLU A CD   
209  O  OE1  . GLU A 26  ? 0.3743 0.3862 0.3553 0.0118  -0.0217 -0.0102 26  GLU A OE1  
210  O  OE2  . GLU A 26  ? 0.3956 0.4721 0.4360 0.0391  -0.0082 -0.0078 26  GLU A OE2  
211  N  N    . ARG A 27  ? 0.1182 0.1111 0.2098 0.0114  -0.0080 -0.0264 27  ARG A N    
212  C  CA   . ARG A 27  ? 0.1141 0.1215 0.1944 0.0344  -0.0162 -0.0271 27  ARG A CA   
213  C  C    . ARG A 27  ? 0.0957 0.0844 0.1805 -0.0002 -0.0002 -0.0078 27  ARG A C    
214  O  O    . ARG A 27  ? 0.1154 0.0919 0.1931 0.0125  -0.0112 -0.0165 27  ARG A O    
215  C  CB   . ARG A 27  ? 0.1720 0.1191 0.2122 0.0288  0.0064  -0.0219 27  ARG A CB   
216  C  CG   . ARG A 27  ? 0.1541 0.1662 0.2553 0.0180  -0.0012 -0.0254 27  ARG A CG   
217  C  CD   . ARG A 27  ? 0.1184 0.2333 0.3210 0.0227  0.0019  -0.0070 27  ARG A CD   
218  N  NE   . ARG A 27  ? 0.1396 0.1643 0.2875 -0.0031 0.0214  -0.0320 27  ARG A NE   
219  C  CZ   . ARG A 27  ? 0.1524 0.1405 0.2109 0.0328  0.0437  0.0078  27  ARG A CZ   
220  N  NH1  . ARG A 27  ? 0.1930 0.1358 0.2646 0.0307  0.0054  -0.0904 27  ARG A NH1  
221  N  NH2  . ARG A 27  ? 0.1476 0.1570 0.2807 -0.0333 0.0288  -0.0376 27  ARG A NH2  
222  N  N    . GLN A 28  ? 0.0919 0.0803 0.1829 0.0108  -0.0080 -0.0237 28  GLN A N    
223  C  CA   . GLN A 28  ? 0.0877 0.0782 0.1737 -0.0036 0.0064  -0.0216 28  GLN A CA   
224  C  C    . GLN A 28  ? 0.0839 0.0389 0.1667 0.0046  -0.0033 -0.0057 28  GLN A C    
225  O  O    . GLN A 28  ? 0.1212 0.0676 0.1564 -0.0186 0.0020  0.0004  28  GLN A O    
226  C  CB   . GLN A 28  ? 0.0702 0.0916 0.1949 0.0105  0.0027  -0.0194 28  GLN A CB   
227  C  CG   . GLN A 28  ? 0.0766 0.0675 0.2168 -0.0282 -0.0173 0.0175  28  GLN A CG   
228  C  CD   . GLN A 28  ? 0.0808 0.1197 0.1627 0.0071  -0.0199 -0.0234 28  GLN A CD   
229  O  OE1  . GLN A 28  ? 0.0925 0.0801 0.2065 -0.0095 0.0003  -0.0275 28  GLN A OE1  
230  N  NE2  . GLN A 28  ? 0.0820 0.0628 0.2290 0.0267  0.0063  -0.0166 28  GLN A NE2  
231  N  N    . SER A 29  ? 0.0720 0.0638 0.1686 -0.0130 0.0016  -0.0144 29  SER A N    
232  C  CA   . SER A 29  ? 0.0712 0.0315 0.1800 -0.0121 -0.0066 -0.0196 29  SER A CA   
233  C  C    . SER A 29  ? 0.0516 0.0458 0.1812 0.0089  -0.0057 -0.0182 29  SER A C    
234  O  O    . SER A 29  ? 0.0688 0.0685 0.2020 0.0102  0.0233  -0.0211 29  SER A O    
235  C  CB   . SER A 29  ? 0.0893 0.0502 0.1758 0.0135  0.0118  -0.0156 29  SER A CB   
236  O  OG   . SER A 29  ? 0.0722 0.0413 0.2046 0.0083  0.0178  -0.0241 29  SER A OG   
237  N  N    . PRO A 30  ? 0.0597 0.0562 0.1929 0.0134  -0.0079 -0.0142 30  PRO A N    
238  C  CA   . PRO A 30  ? 0.0495 0.0545 0.1733 -0.0102 -0.0147 0.0110  30  PRO A CA   
239  C  C    . PRO A 30  ? 0.0890 0.0511 0.1681 0.0030  -0.0176 -0.0152 30  PRO A C    
240  O  O    . PRO A 30  ? 0.0913 0.0640 0.1642 0.0045  -0.0105 -0.0036 30  PRO A O    
241  C  CB   . PRO A 30  ? 0.0572 0.0514 0.1926 0.0137  0.0000  -0.0284 30  PRO A CB   
242  C  CG   . PRO A 30  ? 0.0567 0.0608 0.1795 -0.0068 0.0272  -0.0036 30  PRO A CG   
243  C  CD   . PRO A 30  ? 0.1071 0.0402 0.1744 0.0012  0.0296  -0.0237 30  PRO A CD   
244  N  N    . VAL A 31  ? 0.0967 0.0281 0.1693 0.0139  0.0211  0.0003  31  VAL A N    
245  C  CA   . VAL A 31  ? 0.0994 0.0306 0.1673 -0.0138 0.0101  0.0100  31  VAL A CA   
246  C  C    . VAL A 31  ? 0.0850 0.0570 0.1606 -0.0071 0.0041  0.0049  31  VAL A C    
247  O  O    . VAL A 31  ? 0.0986 0.0664 0.1692 0.0006  -0.0129 0.0206  31  VAL A O    
248  C  CB   . VAL A 31  ? 0.0972 0.0713 0.1651 -0.0129 0.0014  -0.0016 31  VAL A CB   
249  C  CG1  . VAL A 31  ? 0.0682 0.0829 0.2095 -0.0188 0.0136  -0.0014 31  VAL A CG1  
250  C  CG2  . VAL A 31  ? 0.0690 0.0970 0.2101 0.0165  0.0170  -0.0166 31  VAL A CG2  
251  N  N    . ASP A 32  ? 0.1064 0.0473 0.1743 -0.0034 -0.0005 0.0262  32  ASP A N    
252  C  CA   . ASP A 32  ? 0.0877 0.0383 0.1879 0.0124  0.0109  0.0120  32  ASP A CA   
253  C  C    . ASP A 32  ? 0.1002 0.0615 0.1626 -0.0040 0.0096  0.0027  32  ASP A C    
254  O  O    . ASP A 32  ? 0.1312 0.1025 0.1721 0.0049  0.0075  -0.0237 32  ASP A O    
255  C  CB   . ASP A 32  ? 0.1332 0.0609 0.2023 0.0163  0.0039  0.0290  32  ASP A CB   
256  C  CG   . ASP A 32  ? 0.1506 0.0609 0.2087 0.0013  -0.0118 -0.0174 32  ASP A CG   
257  O  OD1  . ASP A 32  ? 0.1308 0.0617 0.1718 -0.0042 -0.0024 0.0166  32  ASP A OD1  
258  O  OD2  . ASP A 32  ? 0.2426 0.1111 0.1916 -0.0167 0.0012  0.0397  32  ASP A OD2  
259  N  N    . ILE A 33  ? 0.0746 0.0538 0.2099 0.0028  0.0150  0.0131  33  ILE A N    
260  C  CA   . ILE A 33  ? 0.0974 0.0759 0.1897 0.0470  0.0243  0.0447  33  ILE A CA   
261  C  C    . ILE A 33  ? 0.1377 0.0773 0.1847 0.0291  0.0214  0.0168  33  ILE A C    
262  O  O    . ILE A 33  ? 0.1585 0.0685 0.2050 0.0024  0.0234  0.0182  33  ILE A O    
263  C  CB   . ILE A 33  ? 0.0969 0.0697 0.2084 0.0409  0.0251  0.0197  33  ILE A CB   
264  C  CG1  . ILE A 33  ? 0.1192 0.0526 0.2098 0.0097  0.0125  0.0656  33  ILE A CG1  
265  C  CG2  . ILE A 33  ? 0.0922 0.1245 0.2030 0.0342  0.0489  0.0120  33  ILE A CG2  
266  C  CD1  . ILE A 33  ? 0.1093 0.1138 0.2339 0.0272  0.0094  0.0405  33  ILE A CD1  
267  N  N    A ASP A 34  ? 0.1574 0.1072 0.1704 0.0369  0.0197  0.0321  34  ASP A N    
268  N  N    B ASP A 34  ? 0.1630 0.0993 0.1661 0.0379  0.0203  0.0286  34  ASP A N    
269  C  CA   A ASP A 34  ? 0.1778 0.1221 0.1878 0.0412  0.0227  0.0372  34  ASP A CA   
270  C  CA   B ASP A 34  ? 0.1898 0.1154 0.1830 0.0446  0.0234  0.0352  34  ASP A CA   
271  C  C    A ASP A 34  ? 0.1834 0.1150 0.1825 0.0354  0.0261  0.0361  34  ASP A C    
272  C  C    B ASP A 34  ? 0.1946 0.1133 0.1796 0.0340  0.0253  0.0369  34  ASP A C    
273  O  O    A ASP A 34  ? 0.1953 0.1131 0.1950 0.0646  0.0340  0.0380  34  ASP A O    
274  O  O    B ASP A 34  ? 0.2423 0.1342 0.1883 0.0404  0.0245  0.0455  34  ASP A O    
275  C  CB   A ASP A 34  ? 0.2033 0.1312 0.1928 0.0410  0.0116  0.0407  34  ASP A CB   
276  C  CB   B ASP A 34  ? 0.2133 0.1089 0.1727 0.0568  0.0192  0.0226  34  ASP A CB   
277  C  CG   A ASP A 34  ? 0.2047 0.1786 0.1915 0.0178  0.0082  0.0227  34  ASP A CG   
278  C  CG   B ASP A 34  ? 0.2494 0.1832 0.2114 0.0285  0.0064  0.0262  34  ASP A CG   
279  O  OD1  A ASP A 34  ? 0.1725 0.1662 0.1707 0.0441  -0.0090 0.0630  34  ASP A OD1  
280  O  OD1  B ASP A 34  ? 0.2894 0.1729 0.2628 0.0806  0.0255  0.0490  34  ASP A OD1  
281  O  OD2  A ASP A 34  ? 0.2462 0.2755 0.2486 -0.0009 -0.0155 0.0760  34  ASP A OD2  
282  O  OD2  B ASP A 34  ? 0.2844 0.1770 0.2234 0.0342  0.0222  0.0748  34  ASP A OD2  
283  N  N    . THR A 35  ? 0.1869 0.1352 0.2047 0.0434  0.0247  0.0454  35  THR A N    
284  C  CA   . THR A 35  ? 0.1906 0.1481 0.2143 0.0619  0.0387  0.0445  35  THR A CA   
285  C  C    . THR A 35  ? 0.2372 0.1268 0.2249 0.0528  0.0515  0.0473  35  THR A C    
286  O  O    . THR A 35  ? 0.2438 0.2051 0.2487 0.0748  0.0756  0.0600  35  THR A O    
287  C  CB   . THR A 35  ? 0.2250 0.1358 0.2211 0.0327  0.0369  0.0392  35  THR A CB   
288  O  OG1  . THR A 35  ? 0.2586 0.1699 0.2550 0.0602  0.0563  0.0554  35  THR A OG1  
289  C  CG2  . THR A 35  ? 0.2315 0.1897 0.2234 0.0614  0.0392  0.0536  35  THR A CG2  
290  N  N    . HIS A 36  ? 0.2433 0.1815 0.1994 0.0603  0.0600  0.0533  36  HIS A N    
291  C  CA   . HIS A 36  ? 0.2772 0.1710 0.2133 0.0452  0.0233  0.0584  36  HIS A CA   
292  C  C    . HIS A 36  ? 0.2566 0.2135 0.2172 0.0448  0.0420  0.0116  36  HIS A C    
293  O  O    . HIS A 36  ? 0.3056 0.2695 0.2287 0.0610  0.0541  0.0031  36  HIS A O    
294  C  CB   . HIS A 36  ? 0.2822 0.1997 0.2158 0.0552  0.0101  0.0651  36  HIS A CB   
295  C  CG   . HIS A 36  ? 0.3666 0.2132 0.2265 0.0401  -0.0272 0.0532  36  HIS A CG   
296  N  ND1  . HIS A 36  ? 0.4307 0.2162 0.2813 0.0601  -0.0763 0.0768  36  HIS A ND1  
297  C  CD2  . HIS A 36  ? 0.3908 0.1965 0.2529 0.0023  -0.0419 0.0698  36  HIS A CD2  
298  C  CE1  . HIS A 36  ? 0.4303 0.1495 0.3076 0.0694  -0.0252 0.0283  36  HIS A CE1  
299  N  NE2  . HIS A 36  ? 0.4756 0.3119 0.3567 -0.0032 -0.0479 0.0354  36  HIS A NE2  
300  N  N    A THR A 37  ? 0.2677 0.1957 0.2259 0.0523  0.0430  0.0222  37  THR A N    
301  N  N    B THR A 37  ? 0.2547 0.1777 0.2195 0.0577  0.0435  0.0230  37  THR A N    
302  C  CA   A THR A 37  ? 0.2696 0.2111 0.2171 0.0437  0.0366  0.0262  37  THR A CA   
303  C  CA   B THR A 37  ? 0.2414 0.1817 0.2124 0.0489  0.0353  0.0263  37  THR A CA   
304  C  C    A THR A 37  ? 0.2496 0.1887 0.2027 0.0435  0.0356  0.0248  37  THR A C    
305  C  C    B THR A 37  ? 0.2303 0.1701 0.1935 0.0481  0.0372  0.0235  37  THR A C    
306  O  O    A THR A 37  ? 0.2401 0.2094 0.2038 0.0487  0.0350  0.0217  37  THR A O    
307  O  O    B THR A 37  ? 0.2402 0.1786 0.1868 0.0408  0.0490  0.0208  37  THR A O    
308  C  CB   A THR A 37  ? 0.2803 0.2334 0.2252 0.0385  0.0293  0.0255  37  THR A CB   
309  C  CB   B THR A 37  ? 0.2525 0.1881 0.1999 0.0479  0.0239  0.0261  37  THR A CB   
310  O  OG1  A THR A 37  ? 0.2854 0.2647 0.2258 0.0680  0.0371  0.0252  37  THR A OG1  
311  O  OG1  B THR A 37  ? 0.3150 0.1515 0.2874 0.0419  0.0538  0.0148  37  THR A OG1  
312  C  CG2  A THR A 37  ? 0.2877 0.2373 0.2064 0.0303  0.0436  0.0247  37  THR A CG2  
313  C  CG2  B THR A 37  ? 0.1903 0.1925 0.1969 0.0396  0.0037  0.0314  37  THR A CG2  
314  N  N    . ALA A 38  ? 0.2494 0.1604 0.2030 0.0460  0.0437  0.0210  38  ALA A N    
315  C  CA   . ALA A 38  ? 0.2200 0.1425 0.1916 0.0511  0.0542  0.0273  38  ALA A CA   
316  C  C    . ALA A 38  ? 0.2410 0.1561 0.2465 0.0216  0.0524  0.0045  38  ALA A C    
317  O  O    . ALA A 38  ? 0.2698 0.1713 0.2954 0.0389  0.0830  0.0103  38  ALA A O    
318  C  CB   . ALA A 38  ? 0.2475 0.1324 0.2030 0.0191  0.0424  0.0072  38  ALA A CB   
319  N  N    . LYS A 39  ? 0.2039 0.1515 0.2244 0.0561  0.0395  0.0141  39  LYS A N    
320  C  CA   . LYS A 39  ? 0.2014 0.1812 0.2342 0.0679  0.0227  0.0060  39  LYS A CA   
321  C  C    . LYS A 39  ? 0.1882 0.1795 0.1967 0.0378  0.0278  0.0137  39  LYS A C    
322  O  O    . LYS A 39  ? 0.1738 0.1780 0.1875 0.0397  0.0371  0.0097  39  LYS A O    
323  C  CB   . LYS A 39  ? 0.2619 0.2060 0.2524 0.0361  0.0144  -0.0041 39  LYS A CB   
324  C  CG   . LYS A 39  ? 0.2635 0.2814 0.2627 0.0471  0.0202  0.0277  39  LYS A CG   
325  C  CD   . LYS A 39  ? 0.2396 0.2390 0.2825 0.0604  0.0482  0.0364  39  LYS A CD   
326  C  CE   . LYS A 39  ? 0.2600 0.3189 0.2944 0.0344  0.0293  0.0109  39  LYS A CE   
327  N  NZ   . LYS A 39  ? 0.2136 0.3632 0.3490 0.0323  0.0130  0.0616  39  LYS A NZ   
328  N  N    . TYR A 40  ? 0.2097 0.2113 0.2201 0.0222  0.0226  0.0186  40  TYR A N    
329  C  CA   . TYR A 40  ? 0.1995 0.2276 0.2320 0.0104  0.0423  0.0132  40  TYR A CA   
330  C  C    . TYR A 40  ? 0.1800 0.2440 0.2207 0.0297  0.0276  0.0077  40  TYR A C    
331  O  O    . TYR A 40  ? 0.2016 0.2931 0.2156 0.0467  0.0375  -0.0077 40  TYR A O    
332  C  CB   . TYR A 40  ? 0.2046 0.2812 0.2475 -0.0139 0.0331  0.0423  40  TYR A CB   
333  C  CG   . TYR A 40  ? 0.2535 0.2988 0.2723 0.0002  0.0464  0.0058  40  TYR A CG   
334  C  CD1  . TYR A 40  ? 0.2711 0.3250 0.3138 0.0062  0.0139  0.0230  40  TYR A CD1  
335  C  CD2  . TYR A 40  ? 0.2917 0.3647 0.3182 -0.0023 0.0507  0.0167  40  TYR A CD2  
336  C  CE1  . TYR A 40  ? 0.2334 0.3563 0.3003 0.0174  0.0349  0.0109  40  TYR A CE1  
337  C  CE2  . TYR A 40  ? 0.3309 0.4231 0.3659 0.0278  0.0332  0.0179  40  TYR A CE2  
338  C  CZ   . TYR A 40  ? 0.2303 0.4190 0.3518 0.0228  0.0255  0.0099  40  TYR A CZ   
339  O  OH   . TYR A 40  ? 0.2829 0.4843 0.4367 0.0725  0.0372  -0.0079 40  TYR A OH   
340  N  N    . ASP A 41  ? 0.1898 0.2056 0.2198 0.0424  0.0363  0.0028  41  ASP A N    
341  C  CA   . ASP A 41  ? 0.2335 0.2429 0.2365 0.0467  0.0343  -0.0091 41  ASP A CA   
342  C  C    . ASP A 41  ? 0.2707 0.2842 0.2606 0.0587  0.0399  -0.0055 41  ASP A C    
343  O  O    . ASP A 41  ? 0.2626 0.2766 0.2620 0.0720  0.0513  0.0071  41  ASP A O    
344  C  CB   . ASP A 41  ? 0.2462 0.2239 0.2880 0.0469  0.0299  -0.0149 41  ASP A CB   
345  C  CG   . ASP A 41  ? 0.3476 0.3061 0.3583 0.0149  0.0159  -0.0252 41  ASP A CG   
346  O  OD1  . ASP A 41  ? 0.4114 0.3111 0.3378 0.0571  -0.0019 -0.0368 41  ASP A OD1  
347  O  OD2  . ASP A 41  ? 0.4147 0.3394 0.4305 -0.0406 -0.0064 -0.0186 41  ASP A OD2  
348  N  N    . PRO A 42  ? 0.2996 0.3423 0.2639 0.0692  0.0429  -0.0092 42  PRO A N    
349  C  CA   . PRO A 42  ? 0.3203 0.3491 0.2889 0.0537  0.0478  -0.0023 42  PRO A CA   
350  C  C    . PRO A 42  ? 0.3472 0.3569 0.3091 0.0543  0.0428  -0.0145 42  PRO A C    
351  O  O    . PRO A 42  ? 0.3790 0.4128 0.3598 0.0609  0.0350  -0.0084 42  PRO A O    
352  C  CB   . PRO A 42  ? 0.3339 0.3843 0.2959 0.0540  0.0588  -0.0099 42  PRO A CB   
353  C  CG   . PRO A 42  ? 0.2994 0.3909 0.2955 0.0593  0.0631  -0.0156 42  PRO A CG   
354  C  CD   . PRO A 42  ? 0.3097 0.3249 0.2544 0.0754  0.0676  0.0022  42  PRO A CD   
355  N  N    . SER A 43  ? 0.3597 0.3233 0.2887 0.0489  0.0246  -0.0334 43  SER A N    
356  C  CA   . SER A 43  ? 0.4033 0.3255 0.3394 0.0418  0.0035  -0.0221 43  SER A CA   
357  C  C    . SER A 43  ? 0.3834 0.3010 0.3297 0.0550  0.0172  -0.0171 43  SER A C    
358  O  O    . SER A 43  ? 0.4088 0.3216 0.3788 0.0688  0.0148  -0.0068 43  SER A O    
359  C  CB   . SER A 43  ? 0.4200 0.3564 0.3689 0.0359  0.0032  -0.0333 43  SER A CB   
360  O  OG   . SER A 43  ? 0.4439 0.3153 0.3977 -0.0020 0.0061  -0.0621 43  SER A OG   
361  N  N    . LEU A 44  ? 0.3338 0.3009 0.3207 0.0516  0.0032  -0.0205 44  LEU A N    
362  C  CA   . LEU A 44  ? 0.2798 0.2601 0.2994 0.0379  0.0048  0.0183  44  LEU A CA   
363  C  C    . LEU A 44  ? 0.2748 0.2662 0.3219 0.0281  0.0079  0.0207  44  LEU A C    
364  O  O    . LEU A 44  ? 0.2932 0.3238 0.3650 0.0293  0.0080  0.0611  44  LEU A O    
365  C  CB   . LEU A 44  ? 0.2664 0.2789 0.2868 0.0320  0.0175  0.0078  44  LEU A CB   
366  C  CG   . LEU A 44  ? 0.2349 0.1963 0.2706 0.0120  0.0097  0.0206  44  LEU A CG   
367  C  CD1  . LEU A 44  ? 0.2139 0.2427 0.2709 -0.0108 0.0114  -0.0185 44  LEU A CD1  
368  C  CD2  . LEU A 44  ? 0.2823 0.2055 0.2765 0.0006  0.0094  0.0458  44  LEU A CD2  
369  N  N    . LYS A 45  ? 0.2480 0.2296 0.3040 0.0314  0.0006  0.0194  45  LYS A N    
370  C  CA   . LYS A 45  ? 0.2699 0.2594 0.3279 0.0251  0.0060  -0.0112 45  LYS A CA   
371  C  C    . LYS A 45  ? 0.2186 0.2519 0.3118 0.0283  0.0023  -0.0081 45  LYS A C    
372  O  O    . LYS A 45  ? 0.1905 0.2269 0.3310 0.0116  0.0182  -0.0338 45  LYS A O    
373  C  CB   . LYS A 45  ? 0.2741 0.2215 0.3130 0.0545  0.0219  -0.0166 45  LYS A CB   
374  C  CG   . LYS A 45  ? 0.2993 0.3360 0.3516 -0.0086 0.0036  -0.0285 45  LYS A CG   
375  C  CD   . LYS A 45  ? 0.3892 0.3875 0.4536 -0.0148 0.0061  -0.0165 45  LYS A CD   
376  C  CE   . LYS A 45  ? 0.4940 0.4527 0.5032 -0.0113 -0.0015 -0.0427 45  LYS A CE   
377  N  NZ   . LYS A 45  ? 0.5644 0.4736 0.5136 0.0020  0.0076  -0.0169 45  LYS A NZ   
378  N  N    . PRO A 46  ? 0.1970 0.2335 0.2992 0.0022  0.0198  -0.0017 46  PRO A N    
379  C  CA   . PRO A 46  ? 0.1784 0.2290 0.2932 0.0062  0.0074  0.0103  46  PRO A CA   
380  C  C    . PRO A 46  ? 0.1642 0.2106 0.2893 0.0077  0.0295  0.0212  46  PRO A C    
381  O  O    . PRO A 46  ? 0.1403 0.2258 0.3113 -0.0198 0.0257  0.0167  46  PRO A O    
382  C  CB   . PRO A 46  ? 0.1503 0.2382 0.3028 0.0050  0.0111  -0.0019 46  PRO A CB   
383  C  CG   . PRO A 46  ? 0.2085 0.3166 0.3391 0.0139  0.0100  -0.0307 46  PRO A CG   
384  C  CD   . PRO A 46  ? 0.2246 0.2585 0.3132 0.0458  0.0174  -0.0330 46  PRO A CD   
385  N  N    . LEU A 47  ? 0.1807 0.1914 0.3165 0.0117  0.0073  0.0332  47  LEU A N    
386  C  CA   . LEU A 47  ? 0.1376 0.2066 0.2916 -0.0138 0.0159  0.0212  47  LEU A CA   
387  C  C    . LEU A 47  ? 0.1445 0.1751 0.3143 -0.0348 -0.0094 0.0281  47  LEU A C    
388  O  O    . LEU A 47  ? 0.1437 0.2325 0.3847 -0.0807 -0.0485 0.0432  47  LEU A O    
389  C  CB   . LEU A 47  ? 0.2118 0.2272 0.3332 -0.0231 0.0156  0.0084  47  LEU A CB   
390  C  CG   . LEU A 47  ? 0.2240 0.2387 0.3494 -0.0281 0.0019  -0.0622 47  LEU A CG   
391  C  CD1  . LEU A 47  ? 0.1747 0.2876 0.3594 -0.0552 -0.0284 -0.0542 47  LEU A CD1  
392  C  CD2  . LEU A 47  ? 0.1985 0.2333 0.3959 0.0277  0.0002  -0.0722 47  LEU A CD2  
393  N  N    . SER A 48  ? 0.1124 0.1341 0.2882 -0.0070 0.0064  0.0246  48  SER A N    
394  C  CA   . SER A 48  ? 0.1358 0.1492 0.2695 -0.0408 0.0099  0.0100  48  SER A CA   
395  C  C    . SER A 48  ? 0.1233 0.1444 0.2533 -0.0294 0.0168  -0.0147 48  SER A C    
396  O  O    . SER A 48  ? 0.1417 0.1610 0.2726 -0.0669 0.0227  -0.0158 48  SER A O    
397  C  CB   . SER A 48  ? 0.1973 0.1544 0.2814 -0.0019 0.0038  0.0010  48  SER A CB   
398  O  OG   . SER A 48  ? 0.1867 0.2497 0.3196 0.0303  -0.0023 0.0096  48  SER A OG   
399  N  N    . VAL A 49  ? 0.1715 0.1734 0.2541 -0.0662 0.0058  -0.0111 49  VAL A N    
400  C  CA   . VAL A 49  ? 0.1941 0.1738 0.2789 -0.0642 0.0159  -0.0176 49  VAL A CA   
401  C  C    . VAL A 49  ? 0.1746 0.2029 0.2881 -0.0791 0.0066  -0.0140 49  VAL A C    
402  O  O    . VAL A 49  ? 0.1919 0.2542 0.3246 -0.1180 -0.0121 -0.0079 49  VAL A O    
403  C  CB   . VAL A 49  ? 0.2415 0.1946 0.2751 -0.0406 0.0178  -0.0296 49  VAL A CB   
404  C  CG1  . VAL A 49  ? 0.3149 0.2437 0.2902 -0.0509 0.0200  -0.0224 49  VAL A CG1  
405  C  CG2  . VAL A 49  ? 0.1741 0.1707 0.3477 -0.0353 0.0173  -0.0120 49  VAL A CG2  
406  N  N    . SER A 50  ? 0.1803 0.1946 0.2998 -0.0570 0.0041  -0.0189 50  SER A N    
407  C  CA   . SER A 50  ? 0.1680 0.2085 0.3213 -0.0282 -0.0090 -0.0155 50  SER A CA   
408  C  C    . SER A 50  ? 0.1048 0.1863 0.3056 -0.0059 -0.0229 -0.0253 50  SER A C    
409  O  O    . SER A 50  ? 0.1518 0.1537 0.3387 -0.0248 -0.0018 -0.0177 50  SER A O    
410  C  CB   . SER A 50  ? 0.1901 0.2140 0.3134 -0.0390 0.0313  -0.0191 50  SER A CB   
411  O  OG   . SER A 50  ? 0.2946 0.3029 0.3810 -0.0182 0.0200  -0.0244 50  SER A OG   
412  N  N    . TYR A 51  ? 0.1661 0.1784 0.2936 -0.0113 -0.0214 -0.0259 51  TYR A N    
413  C  CA   . TYR A 51  ? 0.1456 0.1702 0.2840 -0.0093 -0.0118 -0.0042 51  TYR A CA   
414  C  C    . TYR A 51  ? 0.1763 0.1909 0.2909 0.0005  -0.0058 0.0087  51  TYR A C    
415  O  O    . TYR A 51  ? 0.2039 0.1685 0.2936 0.0045  -0.0417 0.0025  51  TYR A O    
416  C  CB   . TYR A 51  ? 0.1559 0.1565 0.2787 -0.0160 -0.0161 -0.0001 51  TYR A CB   
417  C  CG   . TYR A 51  ? 0.1450 0.1218 0.2562 -0.0073 -0.0188 0.0029  51  TYR A CG   
418  C  CD1  . TYR A 51  ? 0.1492 0.1445 0.2779 -0.0172 -0.0103 -0.0173 51  TYR A CD1  
419  C  CD2  . TYR A 51  ? 0.1200 0.1311 0.2445 -0.0119 0.0030  0.0207  51  TYR A CD2  
420  C  CE1  . TYR A 51  ? 0.1449 0.0840 0.2674 -0.0219 0.0083  0.0096  51  TYR A CE1  
421  C  CE2  . TYR A 51  ? 0.1197 0.0916 0.2208 -0.0421 -0.0058 0.0059  51  TYR A CE2  
422  C  CZ   . TYR A 51  ? 0.1079 0.0797 0.2359 -0.0347 -0.0095 0.0099  51  TYR A CZ   
423  O  OH   . TYR A 51  ? 0.1467 0.0973 0.2296 -0.0323 -0.0146 -0.0054 51  TYR A OH   
424  N  N    . ASP A 52  ? 0.1682 0.2224 0.3341 0.0044  -0.0157 0.0119  52  ASP A N    
425  C  CA   . ASP A 52  ? 0.2211 0.2509 0.3285 -0.0054 -0.0067 0.0252  52  ASP A CA   
426  C  C    . ASP A 52  ? 0.2362 0.2393 0.3469 0.0188  -0.0119 0.0238  52  ASP A C    
427  O  O    . ASP A 52  ? 0.2765 0.2374 0.3456 0.0110  -0.0284 0.0506  52  ASP A O    
428  C  CB   . ASP A 52  ? 0.2272 0.2658 0.3452 0.0221  -0.0071 0.0129  52  ASP A CB   
429  C  CG   . ASP A 52  ? 0.3275 0.3705 0.4001 0.0249  0.0055  0.0026  52  ASP A CG   
430  O  OD1  . ASP A 52  ? 0.4128 0.4662 0.4460 0.0512  0.0221  -0.0080 52  ASP A OD1  
431  O  OD2  . ASP A 52  ? 0.4944 0.4272 0.5349 0.0243  -0.0014 0.0210  52  ASP A OD2  
432  N  N    . GLN A 53  ? 0.2231 0.2363 0.3608 0.0092  -0.0165 0.0297  53  GLN A N    
433  C  CA   . GLN A 53  ? 0.2518 0.2281 0.3647 0.0104  -0.0127 0.0242  53  GLN A CA   
434  C  C    . GLN A 53  ? 0.2373 0.1837 0.3183 0.0235  -0.0151 0.0072  53  GLN A C    
435  O  O    . GLN A 53  ? 0.2308 0.1918 0.3391 0.0208  -0.0278 0.0194  53  GLN A O    
436  C  CB   . GLN A 53  ? 0.2719 0.2464 0.3767 0.0217  -0.0091 0.0057  53  GLN A CB   
437  C  CG   . GLN A 53  ? 0.3152 0.3686 0.4205 0.0091  -0.0033 0.0105  53  GLN A CG   
438  C  CD   . GLN A 53  ? 0.3837 0.4697 0.4540 0.0148  -0.0218 0.0301  53  GLN A CD   
439  O  OE1  . GLN A 53  ? 0.3703 0.4766 0.5142 0.0327  -0.0184 0.0639  53  GLN A OE1  
440  N  NE2  . GLN A 53  ? 0.4171 0.4400 0.4707 0.0241  -0.0111 0.0358  53  GLN A NE2  
441  N  N    . ALA A 54  ? 0.2329 0.1346 0.3099 0.0043  -0.0317 0.0105  54  ALA A N    
442  C  CA   . ALA A 54  ? 0.2129 0.1002 0.2733 0.0136  -0.0249 -0.0092 54  ALA A CA   
443  C  C    . ALA A 54  ? 0.2389 0.1209 0.2772 0.0071  -0.0310 -0.0211 54  ALA A C    
444  O  O    . ALA A 54  ? 0.2217 0.1933 0.3108 -0.0119 -0.0625 -0.0361 54  ALA A O    
445  C  CB   . ALA A 54  ? 0.2044 0.1162 0.2919 0.0338  -0.0251 0.0053  54  ALA A CB   
446  N  N    . THR A 55  ? 0.2158 0.0876 0.2556 0.0107  -0.0320 0.0264  55  THR A N    
447  C  CA   . THR A 55  ? 0.2209 0.1094 0.2667 0.0440  -0.0618 0.0202  55  THR A CA   
448  C  C    . THR A 55  ? 0.2019 0.0940 0.2318 0.0371  -0.0717 0.0239  55  THR A C    
449  O  O    . THR A 55  ? 0.2331 0.0635 0.2384 0.0226  -0.0712 0.0168  55  THR A O    
450  C  CB   . THR A 55  ? 0.2457 0.1212 0.2604 0.0338  -0.0284 0.0278  55  THR A CB   
451  O  OG1  . THR A 55  ? 0.3164 0.1035 0.3893 0.0196  -0.0882 0.0157  55  THR A OG1  
452  C  CG2  . THR A 55  ? 0.3350 0.1434 0.2989 0.0799  -0.0386 0.0593  55  THR A CG2  
453  N  N    . SER A 56  ? 0.2561 0.0677 0.2328 0.0288  -0.0522 0.0195  56  SER A N    
454  C  CA   . SER A 56  ? 0.2563 0.0539 0.2260 0.0133  -0.0365 0.0041  56  SER A CA   
455  C  C    . SER A 56  ? 0.2857 0.1010 0.2363 0.0221  -0.0312 0.0130  56  SER A C    
456  O  O    . SER A 56  ? 0.2777 0.0963 0.2410 0.0314  -0.0624 0.0115  56  SER A O    
457  C  CB   . SER A 56  ? 0.2809 0.0683 0.2147 -0.0214 -0.0494 -0.0064 56  SER A CB   
458  O  OG   . SER A 56  ? 0.3028 0.0868 0.2378 -0.0247 -0.0597 0.0177  56  SER A OG   
459  N  N    . LEU A 57  ? 0.2714 0.0815 0.2010 0.0132  -0.0219 0.0182  57  LEU A N    
460  C  CA   . LEU A 57  ? 0.2951 0.0967 0.2248 0.0308  -0.0046 0.0237  57  LEU A CA   
461  C  C    . LEU A 57  ? 0.2998 0.0846 0.2145 0.0340  -0.0166 0.0028  57  LEU A C    
462  O  O    . LEU A 57  ? 0.3280 0.1107 0.1957 0.0496  -0.0279 0.0144  57  LEU A O    
463  C  CB   . LEU A 57  ? 0.3111 0.0996 0.2682 0.0200  0.0233  0.0262  57  LEU A CB   
464  C  CG   . LEU A 57  ? 0.3516 0.1050 0.2740 0.0314  0.0008  0.0184  57  LEU A CG   
465  C  CD1  . LEU A 57  ? 0.3732 0.1714 0.3624 -0.0113 0.0208  0.0133  57  LEU A CD1  
466  C  CD2  . LEU A 57  ? 0.3986 0.1243 0.3278 0.0873  0.0013  0.0229  57  LEU A CD2  
467  N  N    . ARG A 58  ? 0.2690 0.0660 0.2151 0.0376  -0.0120 0.0208  58  ARG A N    
468  C  CA   . ARG A 58  ? 0.2383 0.0927 0.2181 0.0270  -0.0108 0.0379  58  ARG A CA   
469  C  C    . ARG A 58  ? 0.2436 0.1018 0.2008 0.0028  -0.0019 0.0129  58  ARG A C    
470  O  O    . ARG A 58  ? 0.2323 0.1139 0.1784 0.0183  0.0011  0.0152  58  ARG A O    
471  C  CB   . ARG A 58  ? 0.2833 0.1197 0.2544 0.0281  0.0020  0.0251  58  ARG A CB   
472  C  CG   . ARG A 58  ? 0.2398 0.1804 0.3190 -0.0290 0.0322  0.0593  58  ARG A CG   
473  C  CD   . ARG A 58  ? 0.2922 0.2648 0.3170 -0.0491 -0.0004 0.0482  58  ARG A CD   
474  N  NE   . ARG A 58  ? 0.2127 0.1720 0.3411 -0.0348 0.0116  0.0392  58  ARG A NE   
475  C  CZ   . ARG A 58  ? 0.1653 0.2068 0.2878 -0.0549 0.0302  0.0639  58  ARG A CZ   
476  N  NH1  . ARG A 58  ? 0.2962 0.1613 0.2921 -0.0762 0.0458  0.0155  58  ARG A NH1  
477  N  NH2  . ARG A 58  ? 0.2494 0.1923 0.3097 -0.0479 0.0146  0.0372  58  ARG A NH2  
478  N  N    . ILE A 59  ? 0.2317 0.0680 0.1948 0.0124  -0.0079 0.0071  59  ILE A N    
479  C  CA   . ILE A 59  ? 0.2146 0.0734 0.1887 0.0032  -0.0109 0.0098  59  ILE A CA   
480  C  C    . ILE A 59  ? 0.2051 0.0859 0.1648 -0.0204 -0.0043 0.0184  59  ILE A C    
481  O  O    . ILE A 59  ? 0.2839 0.1383 0.1581 0.0031  0.0006  0.0177  59  ILE A O    
482  C  CB   . ILE A 59  ? 0.2225 0.0683 0.1796 -0.0126 -0.0371 0.0112  59  ILE A CB   
483  C  CG1  . ILE A 59  ? 0.2461 0.0757 0.1883 0.0096  -0.0134 0.0357  59  ILE A CG1  
484  C  CG2  . ILE A 59  ? 0.2602 0.1244 0.1948 0.0331  -0.0509 -0.0059 59  ILE A CG2  
485  C  CD1  . ILE A 59  ? 0.2681 0.0605 0.2137 -0.0067 0.0006  0.0166  59  ILE A CD1  
486  N  N    . LEU A 60  ? 0.2297 0.1062 0.1770 -0.0257 -0.0188 0.0137  60  LEU A N    
487  C  CA   . LEU A 60  ? 0.2174 0.1084 0.1918 -0.0176 -0.0056 0.0344  60  LEU A CA   
488  C  C    . LEU A 60  ? 0.1937 0.1132 0.1603 -0.0283 0.0012  0.0169  60  LEU A C    
489  O  O    . LEU A 60  ? 0.1809 0.1248 0.1653 -0.0064 0.0176  0.0333  60  LEU A O    
490  C  CB   . LEU A 60  ? 0.2285 0.1083 0.2441 -0.0298 -0.0081 0.0155  60  LEU A CB   
491  C  CG   . LEU A 60  ? 0.2549 0.1283 0.2228 -0.0199 -0.0041 0.0209  60  LEU A CG   
492  C  CD1  . LEU A 60  ? 0.2983 0.1224 0.2956 -0.0736 0.0465  0.0163  60  LEU A CD1  
493  C  CD2  . LEU A 60  ? 0.2502 0.1089 0.2932 -0.0683 -0.0104 -0.0253 60  LEU A CD2  
494  N  N    . ASN A 61  ? 0.2323 0.0805 0.1737 -0.0444 0.0296  0.0053  61  ASN A N    
495  C  CA   . ASN A 61  ? 0.2231 0.0956 0.1896 -0.0519 0.0249  -0.0012 61  ASN A CA   
496  C  C    . ASN A 61  ? 0.2087 0.1296 0.1848 -0.0492 0.0297  0.0100  61  ASN A C    
497  O  O    . ASN A 61  ? 0.2523 0.1279 0.2157 -0.0515 0.0233  0.0407  61  ASN A O    
498  C  CB   . ASN A 61  ? 0.2429 0.1049 0.1796 -0.0390 0.0347  -0.0146 61  ASN A CB   
499  C  CG   . ASN A 61  ? 0.2192 0.0894 0.1927 -0.0558 0.0190  0.0077  61  ASN A CG   
500  O  OD1  . ASN A 61  ? 0.2265 0.1556 0.2064 -0.0575 0.0459  0.0025  61  ASN A OD1  
501  N  ND2  . ASN A 61  ? 0.2645 0.1115 0.2009 -0.0630 0.0536  -0.0182 61  ASN A ND2  
502  N  N    . ASN A 62  ? 0.1814 0.1136 0.1960 -0.0592 0.0030  0.0062  62  ASN A N    
503  C  CA   . ASN A 62  ? 0.1877 0.1366 0.2016 -0.0568 0.0087  -0.0056 62  ASN A CA   
504  C  C    . ASN A 62  ? 0.1903 0.1538 0.2411 -0.0478 0.0168  0.0022  62  ASN A C    
505  O  O    . ASN A 62  ? 0.2245 0.1933 0.2861 -0.0672 -0.0067 0.0131  62  ASN A O    
506  C  CB   . ASN A 62  ? 0.2173 0.1173 0.2337 -0.0403 0.0031  -0.0115 62  ASN A CB   
507  C  CG   . ASN A 62  ? 0.2096 0.1591 0.1793 -0.0359 0.0118  -0.0068 62  ASN A CG   
508  O  OD1  . ASN A 62  ? 0.1943 0.1310 0.2336 -0.0543 0.0233  0.0000  62  ASN A OD1  
509  N  ND2  . ASN A 62  ? 0.3596 0.1766 0.2474 0.0272  0.0334  -0.0014 62  ASN A ND2  
510  N  N    . GLY A 63  ? 0.2127 0.1472 0.2211 -0.0511 0.0189  0.0065  63  GLY A N    
511  C  CA   . GLY A 63  ? 0.1823 0.1406 0.2485 -0.0467 0.0170  0.0372  63  GLY A CA   
512  C  C    . GLY A 63  ? 0.2010 0.1438 0.2355 -0.0442 0.0225  0.0130  63  GLY A C    
513  O  O    . GLY A 63  ? 0.1769 0.1591 0.2752 -0.0436 0.0211  0.0064  63  GLY A O    
514  N  N    . HIS A 64  ? 0.1550 0.1141 0.2303 -0.0293 0.0310  0.0197  64  HIS A N    
515  C  CA   A HIS A 64  ? 0.1641 0.1378 0.2325 -0.0220 0.0083  0.0146  64  HIS A CA   
516  C  CA   B HIS A 64  ? 0.1594 0.1302 0.2301 -0.0173 0.0064  0.0186  64  HIS A CA   
517  C  C    . HIS A 64  ? 0.1675 0.1161 0.2412 -0.0393 0.0091  0.0324  64  HIS A C    
518  O  O    . HIS A 64  ? 0.1904 0.1616 0.3013 -0.0413 -0.0123 0.0761  64  HIS A O    
519  C  CB   A HIS A 64  ? 0.1614 0.1527 0.2439 -0.0296 0.0067  0.0035  64  HIS A CB   
520  C  CB   B HIS A 64  ? 0.1619 0.1332 0.2480 -0.0278 -0.0026 0.0218  64  HIS A CB   
521  C  CG   A HIS A 64  ? 0.2075 0.1701 0.2490 -0.0498 -0.0109 -0.0054 64  HIS A CG   
522  C  CG   B HIS A 64  ? 0.1944 0.1436 0.2167 0.0068  -0.0221 0.0056  64  HIS A CG   
523  N  ND1  A HIS A 64  ? 0.1831 0.2074 0.2865 -0.0502 -0.0092 0.0073  64  HIS A ND1  
524  N  ND1  B HIS A 64  ? 0.2039 0.1150 0.2663 0.0009  0.0070  -0.0189 64  HIS A ND1  
525  C  CD2  A HIS A 64  ? 0.2565 0.2269 0.2670 -0.0318 -0.0109 -0.0285 64  HIS A CD2  
526  C  CD2  B HIS A 64  ? 0.1840 0.1843 0.2333 -0.0067 -0.0201 0.0088  64  HIS A CD2  
527  C  CE1  A HIS A 64  ? 0.1594 0.2027 0.3077 -0.0762 0.0319  0.0259  64  HIS A CE1  
528  C  CE1  B HIS A 64  ? 0.1867 0.1829 0.1923 0.0169  -0.0076 -0.0269 64  HIS A CE1  
529  N  NE2  A HIS A 64  ? 0.1470 0.2707 0.3121 -0.0706 0.0300  -0.0191 64  HIS A NE2  
530  N  NE2  B HIS A 64  ? 0.2225 0.1755 0.2161 0.0216  -0.0076 -0.0082 64  HIS A NE2  
531  N  N    . ALA A 65  ? 0.1728 0.0929 0.2102 -0.0351 0.0337  0.0103  65  ALA A N    
532  C  CA   . ALA A 65  ? 0.1479 0.0972 0.2070 -0.0286 0.0152  0.0112  65  ALA A CA   
533  C  C    . ALA A 65  ? 0.1597 0.0917 0.1743 -0.0113 0.0293  0.0094  65  ALA A C    
534  O  O    . ALA A 65  ? 0.1643 0.1131 0.2146 -0.0343 0.0371  0.0173  65  ALA A O    
535  C  CB   . ALA A 65  ? 0.1456 0.1335 0.1962 -0.0090 0.0167  0.0074  65  ALA A CB   
536  N  N    . PHE A 66  ? 0.1396 0.0948 0.1883 -0.0047 0.0134  0.0090  66  PHE A N    
537  C  CA   . PHE A 66  ? 0.1727 0.1040 0.1755 -0.0199 0.0059  0.0081  66  PHE A CA   
538  C  C    . PHE A 66  ? 0.1886 0.1052 0.1558 -0.0217 0.0151  0.0036  66  PHE A C    
539  O  O    . PHE A 66  ? 0.2218 0.0899 0.1812 -0.0271 0.0175  0.0067  66  PHE A O    
540  C  CB   . PHE A 66  ? 0.1800 0.1294 0.1972 -0.0303 0.0026  0.0066  66  PHE A CB   
541  C  CG   . PHE A 66  ? 0.2054 0.1022 0.1803 -0.0201 -0.0060 -0.0030 66  PHE A CG   
542  C  CD1  . PHE A 66  ? 0.1618 0.1389 0.1895 -0.0268 -0.0237 0.0035  66  PHE A CD1  
543  C  CD2  . PHE A 66  ? 0.2415 0.1030 0.1642 -0.0193 0.0181  0.0052  66  PHE A CD2  
544  C  CE1  . PHE A 66  ? 0.1550 0.1231 0.1895 -0.0094 -0.0143 -0.0019 66  PHE A CE1  
545  C  CE2  . PHE A 66  ? 0.2172 0.1017 0.1820 -0.0034 0.0109  -0.0100 66  PHE A CE2  
546  C  CZ   . PHE A 66  ? 0.1805 0.1185 0.2070 -0.0258 -0.0245 0.0057  66  PHE A CZ   
547  N  N    . ASN A 67  ? 0.1823 0.0846 0.1700 -0.0094 -0.0006 0.0193  67  ASN A N    
548  C  CA   . ASN A 67  ? 0.1881 0.0868 0.1887 -0.0082 0.0069  0.0028  67  ASN A CA   
549  C  C    . ASN A 67  ? 0.1938 0.0768 0.1600 -0.0129 0.0020  0.0174  67  ASN A C    
550  O  O    . ASN A 67  ? 0.2119 0.1117 0.1743 -0.0047 0.0122  0.0119  67  ASN A O    
551  C  CB   . ASN A 67  ? 0.1587 0.1144 0.2132 -0.0148 0.0048  0.0023  67  ASN A CB   
552  C  CG   . ASN A 67  ? 0.2011 0.1346 0.2506 0.0047  0.0164  0.0094  67  ASN A CG   
553  O  OD1  . ASN A 67  ? 0.2121 0.1684 0.2729 -0.0532 -0.0282 0.0629  67  ASN A OD1  
554  N  ND2  . ASN A 67  ? 0.2544 0.2045 0.3338 -0.0367 0.0161  -0.0085 67  ASN A ND2  
555  N  N    . VAL A 68  ? 0.1869 0.0468 0.1672 0.0116  -0.0093 0.0197  68  VAL A N    
556  C  CA   . VAL A 68  ? 0.2016 0.0648 0.1625 0.0446  -0.0265 0.0164  68  VAL A CA   
557  C  C    . VAL A 68  ? 0.2453 0.0927 0.1862 0.0332  -0.0151 0.0162  68  VAL A C    
558  O  O    . VAL A 68  ? 0.2098 0.0832 0.1789 0.0266  -0.0218 0.0202  68  VAL A O    
559  C  CB   . VAL A 68  ? 0.2128 0.0747 0.2129 0.0418  -0.0344 0.0057  68  VAL A CB   
560  C  CG1  . VAL A 68  ? 0.2019 0.1265 0.2210 0.0466  -0.0512 -0.0334 68  VAL A CG1  
561  C  CG2  . VAL A 68  ? 0.1923 0.1174 0.2100 0.0116  -0.0131 -0.0503 68  VAL A CG2  
562  N  N    . GLU A 69  ? 0.2728 0.0844 0.1772 0.0398  0.0056  0.0031  69  GLU A N    
563  C  CA   . GLU A 69  ? 0.2546 0.0687 0.2046 0.0171  0.0062  0.0261  69  GLU A CA   
564  C  C    . GLU A 69  ? 0.2826 0.0927 0.2121 0.0357  -0.0115 0.0248  69  GLU A C    
565  O  O    . GLU A 69  ? 0.3618 0.0614 0.2320 0.0427  -0.0281 0.0130  69  GLU A O    
566  C  CB   . GLU A 69  ? 0.2664 0.0951 0.2547 0.0334  0.0182  0.0429  69  GLU A CB   
567  C  CG   . GLU A 69  ? 0.2207 0.1216 0.2922 -0.0105 0.0289  0.0171  69  GLU A CG   
568  C  CD   . GLU A 69  ? 0.2622 0.1212 0.3145 0.0139  0.0252  0.0364  69  GLU A CD   
569  O  OE1  . GLU A 69  ? 0.2615 0.1918 0.2867 0.0086  0.0503  0.0690  69  GLU A OE1  
570  O  OE2  . GLU A 69  ? 0.2419 0.1598 0.3954 0.0259  0.0537  0.0580  69  GLU A OE2  
571  N  N    . PHE A 70  ? 0.2271 0.0573 0.2005 0.0157  0.0005  0.0327  70  PHE A N    
572  C  CA   . PHE A 70  ? 0.1973 0.0666 0.2063 0.0041  -0.0172 0.0405  70  PHE A CA   
573  C  C    . PHE A 70  ? 0.2051 0.0740 0.1927 -0.0011 -0.0136 0.0041  70  PHE A C    
574  O  O    . PHE A 70  ? 0.1836 0.0845 0.2275 -0.0012 -0.0208 0.0096  70  PHE A O    
575  C  CB   . PHE A 70  ? 0.1707 0.0559 0.1989 -0.0181 -0.0047 0.0156  70  PHE A CB   
576  C  CG   . PHE A 70  ? 0.1662 0.0730 0.2150 -0.0078 -0.0203 0.0137  70  PHE A CG   
577  C  CD1  . PHE A 70  ? 0.2072 0.0479 0.1903 0.0341  -0.0332 0.0277  70  PHE A CD1  
578  C  CD2  . PHE A 70  ? 0.2159 0.0883 0.1830 -0.0360 -0.0209 0.0108  70  PHE A CD2  
579  C  CE1  . PHE A 70  ? 0.2114 0.1183 0.2185 -0.0011 -0.0073 -0.0084 70  PHE A CE1  
580  C  CE2  . PHE A 70  ? 0.1701 0.0544 0.1996 0.0073  -0.0131 0.0232  70  PHE A CE2  
581  C  CZ   . PHE A 70  ? 0.2507 0.0471 0.1866 -0.0071 -0.0080 0.0124  70  PHE A CZ   
582  N  N    . ASP A 71  ? 0.2242 0.0754 0.2237 0.0010  -0.0280 0.0059  71  ASP A N    
583  C  CA   . ASP A 71  ? 0.2270 0.0512 0.2568 -0.0052 -0.0220 0.0309  71  ASP A CA   
584  C  C    . ASP A 71  ? 0.2021 0.0465 0.2685 0.0062  -0.0209 0.0034  71  ASP A C    
585  O  O    . ASP A 71  ? 0.2563 0.1254 0.3321 -0.0471 -0.0132 0.0116  71  ASP A O    
586  C  CB   . ASP A 71  ? 0.2468 0.0822 0.2775 0.0221  -0.0456 0.0077  71  ASP A CB   
587  C  CG   . ASP A 71  ? 0.2529 0.0869 0.3174 0.0020  -0.0657 0.0235  71  ASP A CG   
588  O  OD1  . ASP A 71  ? 0.2756 0.0739 0.3698 -0.0030 -0.0750 0.0289  71  ASP A OD1  
589  O  OD2  . ASP A 71  ? 0.2757 0.1429 0.4708 0.0052  -0.1228 0.0274  71  ASP A OD2  
590  N  N    . ASP A 72  ? 0.1918 0.0305 0.2613 -0.0098 -0.0333 0.0235  72  ASP A N    
591  C  CA   . ASP A 72  ? 0.1951 0.0351 0.2599 -0.0177 -0.0323 0.0106  72  ASP A CA   
592  C  C    . ASP A 72  ? 0.2149 0.0623 0.2812 -0.0113 -0.0414 -0.0101 72  ASP A C    
593  O  O    . ASP A 72  ? 0.2698 0.0679 0.2886 -0.0112 -0.0567 0.0036  72  ASP A O    
594  C  CB   . ASP A 72  ? 0.1665 0.0603 0.2666 -0.0093 -0.0335 0.0180  72  ASP A CB   
595  C  CG   . ASP A 72  ? 0.2245 0.0707 0.2364 -0.0110 -0.0063 0.0099  72  ASP A CG   
596  O  OD1  . ASP A 72  ? 0.2423 0.1432 0.2713 -0.0119 -0.0266 0.0470  72  ASP A OD1  
597  O  OD2  . ASP A 72  ? 0.2507 0.1095 0.2492 0.0000  -0.0323 0.0131  72  ASP A OD2  
598  N  N    . SER A 73  ? 0.2326 0.0500 0.3074 -0.0332 -0.0350 0.0208  73  SER A N    
599  C  CA   . SER A 73  ? 0.2343 0.0837 0.3097 -0.0297 -0.0383 -0.0054 73  SER A CA   
600  C  C    . SER A 73  ? 0.2453 0.1090 0.3348 0.0037  -0.0299 -0.0110 73  SER A C    
601  O  O    . SER A 73  ? 0.2794 0.0689 0.3542 0.0056  -0.0351 -0.0106 73  SER A O    
602  C  CB   . SER A 73  ? 0.2612 0.1039 0.3271 -0.0253 -0.0389 0.0184  73  SER A CB   
603  O  OG   . SER A 73  ? 0.3059 0.0854 0.3222 0.0211  -0.0369 0.0451  73  SER A OG   
604  N  N    . GLN A 74  ? 0.2579 0.1027 0.3337 0.0119  -0.0277 -0.0085 74  GLN A N    
605  C  CA   . GLN A 74  ? 0.2395 0.1870 0.3429 -0.0068 -0.0206 -0.0044 74  GLN A CA   
606  C  C    . GLN A 74  ? 0.2371 0.2027 0.3336 -0.0030 -0.0300 -0.0194 74  GLN A C    
607  O  O    . GLN A 74  ? 0.2104 0.1891 0.3281 -0.0329 -0.0242 -0.0162 74  GLN A O    
608  C  CB   . GLN A 74  ? 0.2499 0.2109 0.3760 0.0158  -0.0187 0.0038  74  GLN A CB   
609  C  CG   . GLN A 74  ? 0.3007 0.2602 0.3972 0.0095  -0.0188 0.0054  74  GLN A CG   
610  C  CD   . GLN A 74  ? 0.3287 0.2951 0.4083 -0.0009 -0.0286 0.0135  74  GLN A CD   
611  O  OE1  . GLN A 74  ? 0.3605 0.3808 0.4947 -0.0177 -0.0056 0.0237  74  GLN A OE1  
612  N  NE2  . GLN A 74  ? 0.3818 0.2831 0.3850 0.0064  -0.0360 0.0188  74  GLN A NE2  
613  N  N    . ASP A 75  ? 0.2761 0.2715 0.3270 -0.0003 -0.0355 -0.0271 75  ASP A N    
614  C  CA   . ASP A 75  ? 0.2986 0.3006 0.3593 0.0082  -0.0251 -0.0216 75  ASP A CA   
615  C  C    . ASP A 75  ? 0.2922 0.2908 0.3488 0.0163  -0.0401 -0.0221 75  ASP A C    
616  O  O    . ASP A 75  ? 0.3201 0.3506 0.4126 0.0174  -0.0330 -0.0047 75  ASP A O    
617  C  CB   . ASP A 75  ? 0.3475 0.3367 0.3674 0.0272  -0.0418 -0.0258 75  ASP A CB   
618  C  CG   . ASP A 75  ? 0.3922 0.3758 0.3915 -0.0023 -0.0254 -0.0328 75  ASP A CG   
619  O  OD1  . ASP A 75  ? 0.4255 0.4729 0.4273 0.0216  -0.0209 -0.0558 75  ASP A OD1  
620  O  OD2  . ASP A 75  ? 0.5403 0.5014 0.4743 0.0108  0.0175  -0.0437 75  ASP A OD2  
621  N  N    . LYS A 76  ? 0.2735 0.2145 0.3174 0.0145  -0.0414 0.0199  76  LYS A N    
622  C  CA   . LYS A 76  ? 0.2501 0.1828 0.3306 -0.0113 -0.0384 0.0153  76  LYS A CA   
623  C  C    . LYS A 76  ? 0.2703 0.2172 0.3348 0.0001  -0.0384 0.0373  76  LYS A C    
624  O  O    . LYS A 76  ? 0.3038 0.2583 0.3897 -0.0071 -0.0522 0.0355  76  LYS A O    
625  C  CB   . LYS A 76  ? 0.3043 0.1519 0.3034 -0.0085 -0.0456 0.0249  76  LYS A CB   
626  C  CG   . LYS A 76  ? 0.3464 0.1888 0.3357 -0.0031 -0.0356 0.0364  76  LYS A CG   
627  C  CD   . LYS A 76  ? 0.3303 0.1490 0.3522 -0.0495 -0.0169 0.0152  76  LYS A CD   
628  C  CE   . LYS A 76  ? 0.3270 0.2197 0.3326 -0.0200 -0.0140 0.0224  76  LYS A CE   
629  N  NZ   . LYS A 76  ? 0.3827 0.2164 0.3465 0.0318  -0.0068 0.0001  76  LYS A NZ   
630  N  N    . ALA A 77  ? 0.2341 0.1900 0.3164 0.0212  -0.0477 0.0296  77  ALA A N    
631  C  CA   . ALA A 77  ? 0.2082 0.1830 0.2807 0.0093  -0.0280 0.0147  77  ALA A CA   
632  C  C    . ALA A 77  ? 0.2016 0.1718 0.2833 -0.0071 -0.0266 0.0000  77  ALA A C    
633  O  O    . ALA A 77  ? 0.1791 0.2276 0.3162 -0.0413 -0.0004 -0.0225 77  ALA A O    
634  C  CB   . ALA A 77  ? 0.2405 0.2155 0.2680 0.0108  -0.0402 -0.0140 77  ALA A CB   
635  N  N    . VAL A 78  ? 0.1709 0.1089 0.2543 -0.0058 -0.0240 0.0008  78  VAL A N    
636  C  CA   . VAL A 78  ? 0.2147 0.1130 0.2676 -0.0018 -0.0087 0.0235  78  VAL A CA   
637  C  C    . VAL A 78  ? 0.1578 0.0879 0.2640 -0.0253 -0.0091 0.0243  78  VAL A C    
638  O  O    . VAL A 78  ? 0.1511 0.1218 0.3077 -0.0423 -0.0473 0.0342  78  VAL A O    
639  C  CB   . VAL A 78  ? 0.2435 0.1323 0.3190 0.0095  0.0107  0.0223  78  VAL A CB   
640  C  CG1  . VAL A 78  ? 0.3098 0.1161 0.3644 0.0022  0.0035  0.0320  78  VAL A CG1  
641  C  CG2  . VAL A 78  ? 0.2015 0.1721 0.3481 0.0266  0.0314  0.0169  78  VAL A CG2  
642  N  N    . LEU A 79  ? 0.1488 0.0970 0.2359 0.0097  -0.0027 0.0054  79  LEU A N    
643  C  CA   . LEU A 79  ? 0.1425 0.1049 0.2512 -0.0028 0.0084  -0.0063 79  LEU A CA   
644  C  C    . LEU A 79  ? 0.1402 0.0837 0.2253 -0.0014 0.0098  -0.0007 79  LEU A C    
645  O  O    . LEU A 79  ? 0.1557 0.1101 0.2757 -0.0301 0.0002  -0.0330 79  LEU A O    
646  C  CB   . LEU A 79  ? 0.1034 0.1283 0.2798 -0.0145 -0.0193 0.0077  79  LEU A CB   
647  C  CG   . LEU A 79  ? 0.1186 0.1222 0.2854 0.0084  0.0109  0.0072  79  LEU A CG   
648  C  CD1  . LEU A 79  ? 0.1534 0.1312 0.4125 -0.0018 0.0105  0.0666  79  LEU A CD1  
649  C  CD2  . LEU A 79  ? 0.1255 0.1144 0.2630 0.0259  0.0181  0.0086  79  LEU A CD2  
650  N  N    . LYS A 80  ? 0.1583 0.1039 0.2198 -0.0073 0.0228  -0.0056 80  LYS A N    
651  C  CA   . LYS A 80  ? 0.1848 0.1269 0.2501 0.0152  0.0356  -0.0060 80  LYS A CA   
652  C  C    . LYS A 80  ? 0.1426 0.1315 0.2566 0.0165  0.0487  -0.0025 80  LYS A C    
653  O  O    . LYS A 80  ? 0.1471 0.1097 0.2950 -0.0206 0.0207  -0.0177 80  LYS A O    
654  C  CB   . LYS A 80  ? 0.3105 0.1630 0.2945 0.0387  0.0278  0.0248  80  LYS A CB   
655  C  CG   . LYS A 80  ? 0.3538 0.3163 0.3498 -0.0018 0.0443  0.0042  80  LYS A CG   
656  C  CD   . LYS A 80  ? 0.3214 0.3672 0.4008 0.0508  -0.0035 0.0020  80  LYS A CD   
657  C  CE   . LYS A 80  ? 0.3027 0.3774 0.4280 0.0636  0.0192  0.0064  80  LYS A CE   
658  N  NZ   . LYS A 80  ? 0.4414 0.4144 0.4301 0.0386  -0.0187 0.0137  80  LYS A NZ   
659  N  N    . GLY A 81  ? 0.1650 0.1500 0.2645 0.0016  0.0374  0.0074  81  GLY A N    
660  C  CA   . GLY A 81  ? 0.1294 0.1413 0.2870 0.0227  0.0549  0.0186  81  GLY A CA   
661  C  C    . GLY A 81  ? 0.1645 0.1136 0.2694 0.0031  0.0410  0.0077  81  GLY A C    
662  O  O    . GLY A 81  ? 0.1635 0.1407 0.2769 -0.0156 0.0366  -0.0015 81  GLY A O    
663  N  N    . GLY A 82  ? 0.1871 0.1213 0.3207 -0.0140 0.0398  0.0253  82  GLY A N    
664  C  CA   . GLY A 82  ? 0.1902 0.1218 0.3318 -0.0029 0.0329  0.0208  82  GLY A CA   
665  C  C    . GLY A 82  ? 0.1910 0.1392 0.2886 0.0249  0.0439  0.0114  82  GLY A C    
666  O  O    . GLY A 82  ? 0.1900 0.2300 0.3410 0.0726  0.0685  0.0180  82  GLY A O    
667  N  N    . PRO A 83  ? 0.1763 0.1220 0.2968 0.0019  0.0433  0.0146  83  PRO A N    
668  C  CA   . PRO A 83  ? 0.1601 0.1199 0.2605 0.0435  0.0280  0.0118  83  PRO A CA   
669  C  C    . PRO A 83  ? 0.1911 0.1501 0.2720 0.0303  0.0304  -0.0133 83  PRO A C    
670  O  O    . PRO A 83  ? 0.2103 0.2204 0.2941 0.0284  0.0028  -0.0164 83  PRO A O    
671  C  CB   . PRO A 83  ? 0.1877 0.1485 0.2898 0.0569  0.0438  0.0090  83  PRO A CB   
672  C  CG   . PRO A 83  ? 0.1444 0.1282 0.2462 0.0281  0.0346  -0.0042 83  PRO A CG   
673  C  CD   . PRO A 83  ? 0.1497 0.1068 0.2777 0.0162  0.0510  -0.0021 83  PRO A CD   
674  N  N    . LEU A 84  ? 0.1856 0.1216 0.2315 0.0229  0.0321  -0.0208 84  LEU A N    
675  C  CA   . LEU A 84  ? 0.2014 0.0924 0.2526 0.0164  0.0369  -0.0391 84  LEU A CA   
676  C  C    . LEU A 84  ? 0.2316 0.1605 0.2993 0.0272  0.0361  -0.0447 84  LEU A C    
677  O  O    . LEU A 84  ? 0.2369 0.1710 0.3106 0.0296  0.0829  -0.0521 84  LEU A O    
678  C  CB   . LEU A 84  ? 0.1431 0.0888 0.2390 0.0128  0.0488  -0.0132 84  LEU A CB   
679  C  CG   . LEU A 84  ? 0.1037 0.0871 0.2538 0.0256  0.0396  -0.0330 84  LEU A CG   
680  C  CD1  . LEU A 84  ? 0.1322 0.1602 0.2587 0.0192  0.0159  -0.0169 84  LEU A CD1  
681  C  CD2  . LEU A 84  ? 0.1147 0.1016 0.2640 0.0216  0.0201  -0.0412 84  LEU A CD2  
682  N  N    . ASP A 85  ? 0.2744 0.1152 0.3253 0.0213  0.0339  -0.0537 85  ASP A N    
683  C  CA   . ASP A 85  ? 0.3305 0.1706 0.3471 -0.0034 0.0155  -0.0692 85  ASP A CA   
684  C  C    . ASP A 85  ? 0.3096 0.1538 0.3755 -0.0138 0.0175  -0.0561 85  ASP A C    
685  O  O    . ASP A 85  ? 0.3900 0.2199 0.4101 0.0040  0.0268  -0.0795 85  ASP A O    
686  C  CB   . ASP A 85  ? 0.3768 0.1969 0.3620 -0.0062 -0.0072 -0.0514 85  ASP A CB   
687  C  CG   . ASP A 85  ? 0.4208 0.3501 0.4267 0.0057  0.0163  -0.0430 85  ASP A CG   
688  O  OD1  . ASP A 85  ? 0.4637 0.4178 0.4835 -0.0296 0.0290  -0.0444 85  ASP A OD1  
689  O  OD2  . ASP A 85  ? 0.4474 0.4154 0.4770 0.0175  0.0045  -0.0573 85  ASP A OD2  
690  N  N    . GLY A 86  ? 0.3426 0.2277 0.3889 -0.0308 -0.0003 -0.0287 86  GLY A N    
691  C  CA   . GLY A 86  ? 0.3324 0.2348 0.3375 -0.0237 0.0214  -0.0448 86  GLY A CA   
692  C  C    . GLY A 86  ? 0.3235 0.1427 0.3278 -0.0255 0.0185  -0.0500 86  GLY A C    
693  O  O    . GLY A 86  ? 0.3270 0.2164 0.3471 -0.0921 0.0122  -0.0500 86  GLY A O    
694  N  N    . THR A 87  ? 0.2283 0.1380 0.3035 -0.0070 0.0447  -0.0461 87  THR A N    
695  C  CA   . THR A 87  ? 0.1894 0.1592 0.3005 0.0091  0.0387  -0.0258 87  THR A CA   
696  C  C    . THR A 87  ? 0.1081 0.1094 0.2975 -0.0073 0.0088  -0.0250 87  THR A C    
697  O  O    . THR A 87  ? 0.1335 0.0777 0.3085 -0.0145 0.0363  -0.0420 87  THR A O    
698  C  CB   . THR A 87  ? 0.1674 0.2612 0.3143 0.0678  0.0303  -0.0399 87  THR A CB   
699  O  OG1  . THR A 87  ? 0.2281 0.2999 0.4166 0.0340  0.0608  -0.0778 87  THR A OG1  
700  C  CG2  . THR A 87  ? 0.2462 0.2326 0.3512 0.0434  0.0062  -0.0210 87  THR A CG2  
701  N  N    . TYR A 88  ? 0.1030 0.0739 0.2655 0.0100  0.0150  -0.0298 88  TYR A N    
702  C  CA   . TYR A 88  ? 0.1063 0.0869 0.2549 -0.0081 0.0162  -0.0126 88  TYR A CA   
703  C  C    . TYR A 88  ? 0.1340 0.0737 0.2407 0.0008  -0.0005 0.0092  88  TYR A C    
704  O  O    . TYR A 88  ? 0.1703 0.1266 0.2857 -0.0622 -0.0129 0.0380  88  TYR A O    
705  C  CB   . TYR A 88  ? 0.1036 0.0792 0.2486 0.0206  0.0176  -0.0188 88  TYR A CB   
706  C  CG   . TYR A 88  ? 0.1248 0.0551 0.2040 0.0302  0.0140  -0.0287 88  TYR A CG   
707  C  CD1  . TYR A 88  ? 0.1216 0.0484 0.1907 0.0199  0.0097  -0.0199 88  TYR A CD1  
708  C  CD2  . TYR A 88  ? 0.1237 0.0587 0.2277 0.0439  0.0251  -0.0065 88  TYR A CD2  
709  C  CE1  . TYR A 88  ? 0.1157 0.1044 0.2080 0.0174  0.0000  -0.0374 88  TYR A CE1  
710  C  CE2  . TYR A 88  ? 0.1601 0.0558 0.1876 -0.0031 0.0232  -0.0199 88  TYR A CE2  
711  C  CZ   . TYR A 88  ? 0.1363 0.0417 0.2115 -0.0120 0.0022  -0.0427 88  TYR A CZ   
712  O  OH   . TYR A 88  ? 0.1265 0.0837 0.2107 -0.0088 0.0197  -0.0256 88  TYR A OH   
713  N  N    . ARG A 89  ? 0.1222 0.0677 0.2316 0.0261  0.0121  -0.0101 89  ARG A N    
714  C  CA   . ARG A 89  ? 0.1574 0.0559 0.2404 0.0168  0.0057  0.0136  89  ARG A CA   
715  C  C    . ARG A 89  ? 0.0915 0.0476 0.1991 -0.0033 0.0014  0.0060  89  ARG A C    
716  O  O    . ARG A 89  ? 0.0973 0.0475 0.2299 -0.0086 -0.0017 0.0136  89  ARG A O    
717  C  CB   . ARG A 89  ? 0.1893 0.0640 0.2963 0.0108  0.0038  0.0054  89  ARG A CB   
718  C  CG   . ARG A 89  ? 0.2279 0.2325 0.3413 0.0335  -0.0106 0.0348  89  ARG A CG   
719  C  CD   . ARG A 89  ? 0.2378 0.0890 0.4076 0.0185  -0.0182 0.0496  89  ARG A CD   
720  N  NE   . ARG A 89  ? 0.2333 0.1934 0.3147 0.0474  -0.0275 0.0235  89  ARG A NE   
721  C  CZ   . ARG A 89  ? 0.3115 0.0930 0.3547 0.0599  -0.0598 0.0429  89  ARG A CZ   
722  N  NH1  . ARG A 89  ? 0.4032 0.1890 0.2953 0.0585  -0.0180 0.0234  89  ARG A NH1  
723  N  NH2  . ARG A 89  ? 0.2917 0.2969 0.4178 0.0585  -0.0018 -0.0460 89  ARG A NH2  
724  N  N    . LEU A 90  ? 0.1538 0.0494 0.1887 -0.0069 -0.0169 -0.0060 90  LEU A N    
725  C  CA   . LEU A 90  ? 0.1516 0.0390 0.1931 -0.0289 0.0016  -0.0034 90  LEU A CA   
726  C  C    . LEU A 90  ? 0.1441 0.0467 0.1864 -0.0226 -0.0126 0.0246  90  LEU A C    
727  O  O    . LEU A 90  ? 0.1770 0.0747 0.2246 -0.0174 -0.0186 0.0290  90  LEU A O    
728  C  CB   . LEU A 90  ? 0.1642 0.0615 0.1814 -0.0160 -0.0197 0.0016  90  LEU A CB   
729  C  CG   . LEU A 90  ? 0.1475 0.0451 0.1836 -0.0043 0.0028  -0.0056 90  LEU A CG   
730  C  CD1  . LEU A 90  ? 0.1863 0.0643 0.2182 -0.0310 -0.0233 0.0094  90  LEU A CD1  
731  C  CD2  . LEU A 90  ? 0.1742 0.1105 0.2193 -0.0287 -0.0397 -0.0287 90  LEU A CD2  
732  N  N    . ILE A 91  ? 0.1271 0.0493 0.1833 -0.0109 0.0115  0.0059  91  ILE A N    
733  C  CA   . ILE A 91  ? 0.1366 0.0608 0.1897 -0.0208 -0.0053 0.0009  91  ILE A CA   
734  C  C    . ILE A 91  ? 0.1456 0.0444 0.1790 -0.0059 -0.0004 0.0178  91  ILE A C    
735  O  O    . ILE A 91  ? 0.1450 0.0529 0.1749 -0.0186 -0.0206 0.0255  91  ILE A O    
736  C  CB   . ILE A 91  ? 0.1451 0.0406 0.1966 -0.0216 -0.0055 -0.0009 91  ILE A CB   
737  C  CG1  . ILE A 91  ? 0.1685 0.0872 0.1904 -0.0638 0.0216  -0.0188 91  ILE A CG1  
738  C  CG2  . ILE A 91  ? 0.1308 0.0749 0.2023 -0.0105 -0.0244 -0.0101 91  ILE A CG2  
739  C  CD1  . ILE A 91  ? 0.1793 0.1127 0.2569 -0.0690 0.0242  -0.0214 91  ILE A CD1  
740  N  N    . GLN A 92  ? 0.1462 0.0283 0.1845 -0.0083 0.0001  0.0198  92  GLN A N    
741  C  CA   . GLN A 92  ? 0.1372 0.0377 0.1684 0.0039  0.0234  0.0221  92  GLN A CA   
742  C  C    . GLN A 92  ? 0.1357 0.0463 0.1445 -0.0122 0.0211  0.0072  92  GLN A C    
743  O  O    . GLN A 92  ? 0.1373 0.0277 0.1480 -0.0051 0.0067  0.0053  92  GLN A O    
744  C  CB   . GLN A 92  ? 0.1388 0.0613 0.1973 0.0090  0.0116  0.0170  92  GLN A CB   
745  C  CG   . GLN A 92  ? 0.1177 0.0760 0.2273 0.0015  -0.0141 0.0260  92  GLN A CG   
746  C  CD   . GLN A 92  ? 0.2115 0.0293 0.1658 -0.0035 -0.0085 0.0235  92  GLN A CD   
747  O  OE1  . GLN A 92  ? 0.1945 0.0378 0.2132 0.0000  -0.0184 0.0159  92  GLN A OE1  
748  N  NE2  . GLN A 92  ? 0.2071 0.1532 0.2929 0.0050  0.0088  0.0192  92  GLN A NE2  
749  N  N    . PHE A 93  ? 0.1492 0.0254 0.1724 -0.0039 -0.0108 -0.0002 93  PHE A N    
750  C  CA   . PHE A 93  ? 0.1303 0.0259 0.1729 -0.0021 0.0078  0.0091  93  PHE A CA   
751  C  C    . PHE A 93  ? 0.1114 0.0401 0.1417 -0.0247 -0.0047 0.0023  93  PHE A C    
752  O  O    . PHE A 93  ? 0.1660 0.0463 0.1529 0.0030  0.0010  0.0037  93  PHE A O    
753  C  CB   . PHE A 93  ? 0.1245 0.0347 0.1640 -0.0279 -0.0263 0.0121  93  PHE A CB   
754  C  CG   . PHE A 93  ? 0.1534 0.0335 0.1857 -0.0182 -0.0387 0.0038  93  PHE A CG   
755  C  CD1  . PHE A 93  ? 0.1351 0.0359 0.1991 -0.0305 -0.0162 -0.0053 93  PHE A CD1  
756  C  CD2  . PHE A 93  ? 0.1324 0.0820 0.1771 -0.0148 -0.0647 0.0373  93  PHE A CD2  
757  C  CE1  . PHE A 93  ? 0.1447 0.0685 0.2167 -0.0043 -0.0610 0.0068  93  PHE A CE1  
758  C  CE2  . PHE A 93  ? 0.1975 0.0565 0.1939 0.0013  -0.0498 0.0176  93  PHE A CE2  
759  C  CZ   . PHE A 93  ? 0.1896 0.0347 0.2051 -0.0040 -0.0540 -0.0074 93  PHE A CZ   
760  N  N    . HIS A 94  ? 0.1009 0.0304 0.1783 -0.0028 -0.0104 0.0053  94  HIS A N    
761  C  CA   . HIS A 94  ? 0.1107 0.0272 0.1582 -0.0053 0.0084  0.0140  94  HIS A CA   
762  C  C    . HIS A 94  ? 0.0955 0.0612 0.1388 -0.0126 0.0033  -0.0010 94  HIS A C    
763  O  O    . HIS A 94  ? 0.1166 0.0308 0.1479 0.0046  0.0093  0.0064  94  HIS A O    
764  C  CB   . HIS A 94  ? 0.1472 0.0691 0.1461 -0.0043 0.0022  -0.0001 94  HIS A CB   
765  C  CG   . HIS A 94  ? 0.1308 0.0286 0.1432 -0.0096 0.0105  -0.0050 94  HIS A CG   
766  N  ND1  . HIS A 94  ? 0.1103 0.0336 0.1590 -0.0232 0.0121  0.0106  94  HIS A ND1  
767  C  CD2  . HIS A 94  ? 0.0866 0.0407 0.1696 -0.0100 -0.0008 0.0127  94  HIS A CD2  
768  C  CE1  . HIS A 94  ? 0.1047 0.0407 0.1358 0.0183  0.0131  0.0379  94  HIS A CE1  
769  N  NE2  . HIS A 94  ? 0.1481 0.0256 0.1566 -0.0009 0.0040  -0.0068 94  HIS A NE2  
770  N  N    . PHE A 95  ? 0.0979 0.0358 0.1776 0.0137  0.0023  0.0076  95  PHE A N    
771  C  CA   . PHE A 95  ? 0.1196 0.0273 0.1555 0.0124  -0.0096 0.0060  95  PHE A CA   
772  C  C    . PHE A 95  ? 0.1273 0.0300 0.1692 0.0213  0.0243  0.0000  95  PHE A C    
773  O  O    . PHE A 95  ? 0.0873 0.0619 0.1792 -0.0047 0.0132  0.0163  95  PHE A O    
774  C  CB   . PHE A 95  ? 0.1119 0.0502 0.1690 0.0042  -0.0047 -0.0139 95  PHE A CB   
775  C  CG   . PHE A 95  ? 0.0919 0.0254 0.1655 0.0016  -0.0151 0.0025  95  PHE A CG   
776  C  CD1  . PHE A 95  ? 0.1309 0.0352 0.1822 0.0000  -0.0025 -0.0183 95  PHE A CD1  
777  C  CD2  . PHE A 95  ? 0.1202 0.0471 0.2045 -0.0224 -0.0243 -0.0402 95  PHE A CD2  
778  C  CE1  . PHE A 95  ? 0.1055 0.0790 0.1678 0.0209  -0.0131 -0.0009 95  PHE A CE1  
779  C  CE2  . PHE A 95  ? 0.1225 0.0599 0.1933 0.0114  -0.0080 -0.0063 95  PHE A CE2  
780  C  CZ   . PHE A 95  ? 0.1381 0.0469 0.1989 -0.0067 -0.0066 -0.0221 95  PHE A CZ   
781  N  N    . HIS A 96  ? 0.1336 0.0298 0.1539 0.0092  0.0081  0.0022  96  HIS A N    
782  C  CA   . HIS A 96  ? 0.1104 0.0261 0.1684 0.0081  0.0110  0.0004  96  HIS A CA   
783  C  C    . HIS A 96  ? 0.0649 0.0370 0.1762 -0.0137 0.0091  -0.0072 96  HIS A C    
784  O  O    . HIS A 96  ? 0.0796 0.0466 0.1917 -0.0083 0.0251  0.0021  96  HIS A O    
785  C  CB   . HIS A 96  ? 0.1036 0.0268 0.1651 -0.0079 -0.0014 -0.0097 96  HIS A CB   
786  C  CG   . HIS A 96  ? 0.1104 0.0340 0.1532 -0.0219 0.0332  -0.0041 96  HIS A CG   
787  N  ND1  . HIS A 96  ? 0.0814 0.0424 0.1852 -0.0057 0.0237  -0.0013 96  HIS A ND1  
788  C  CD2  . HIS A 96  ? 0.0993 0.0299 0.1848 -0.0043 -0.0111 -0.0256 96  HIS A CD2  
789  C  CE1  . HIS A 96  ? 0.0723 0.0473 0.1898 0.0132  0.0009  -0.0258 96  HIS A CE1  
790  N  NE2  . HIS A 96  ? 0.0425 0.0564 0.1821 0.0182  -0.0219 -0.0151 96  HIS A NE2  
791  N  N    . TRP A 97  ? 0.1117 0.0400 0.1696 -0.0061 0.0125  -0.0111 97  TRP A N    
792  C  CA   . TRP A 97  ? 0.1133 0.0332 0.1748 -0.0105 0.0030  -0.0320 97  TRP A CA   
793  C  C    . TRP A 97  ? 0.0984 0.0422 0.1601 -0.0079 0.0099  -0.0224 97  TRP A C    
794  O  O    . TRP A 97  ? 0.1225 0.0463 0.1906 -0.0137 0.0393  -0.0080 97  TRP A O    
795  C  CB   . TRP A 97  ? 0.1202 0.0737 0.1686 -0.0136 0.0119  -0.0197 97  TRP A CB   
796  C  CG   . TRP A 97  ? 0.1426 0.0390 0.1523 -0.0209 0.0138  -0.0197 97  TRP A CG   
797  C  CD1  . TRP A 97  ? 0.1544 0.0604 0.1666 -0.0078 0.0010  -0.0230 97  TRP A CD1  
798  C  CD2  . TRP A 97  ? 0.1448 0.0501 0.1460 -0.0281 0.0009  -0.0108 97  TRP A CD2  
799  N  NE1  . TRP A 97  ? 0.2107 0.0600 0.1655 0.0108  0.0217  -0.0045 97  TRP A NE1  
800  C  CE2  . TRP A 97  ? 0.1990 0.0711 0.1656 -0.0139 0.0215  -0.0174 97  TRP A CE2  
801  C  CE3  . TRP A 97  ? 0.1434 0.0544 0.1463 0.0026  -0.0068 -0.0214 97  TRP A CE3  
802  C  CZ2  . TRP A 97  ? 0.1830 0.0528 0.1929 -0.0200 0.0221  0.0077  97  TRP A CZ2  
803  C  CZ3  . TRP A 97  ? 0.1661 0.0668 0.1818 -0.0106 0.0011  0.0437  97  TRP A CZ3  
804  C  CH2  . TRP A 97  ? 0.1999 0.0670 0.1893 -0.0187 0.0384  -0.0073 97  TRP A CH2  
805  N  N    . GLY A 98  ? 0.1427 0.0316 0.1712 0.0003  0.0066  -0.0050 98  GLY A N    
806  C  CA   . GLY A 98  ? 0.1133 0.0416 0.1825 0.0119  0.0154  -0.0188 98  GLY A CA   
807  C  C    . GLY A 98  ? 0.1080 0.0525 0.2034 -0.0069 0.0079  -0.0120 98  GLY A C    
808  O  O    . GLY A 98  ? 0.1584 0.0657 0.2045 0.0066  0.0081  -0.0210 98  GLY A O    
809  N  N    . SER A 99  ? 0.1442 0.0568 0.2135 0.0089  0.0234  -0.0247 99  SER A N    
810  C  CA   . SER A 99  ? 0.1699 0.0688 0.2093 0.0142  0.0266  -0.0444 99  SER A CA   
811  C  C    . SER A 99  ? 0.1915 0.0625 0.2057 0.0164  0.0176  -0.0415 99  SER A C    
812  O  O    . SER A 99  ? 0.2468 0.0908 0.2416 -0.0005 0.0200  -0.0391 99  SER A O    
813  C  CB   . SER A 99  ? 0.1728 0.0906 0.2266 0.0464  0.0184  -0.0571 99  SER A CB   
814  O  OG   . SER A 99  ? 0.1427 0.0804 0.2838 0.0079  0.0265  -0.0374 99  SER A OG   
815  N  N    . LEU A 100 ? 0.1580 0.0707 0.2390 -0.0076 0.0225  -0.0133 100 LEU A N    
816  C  CA   . LEU A 100 ? 0.1702 0.0602 0.2898 0.0074  0.0413  -0.0122 100 LEU A CA   
817  C  C    . LEU A 100 ? 0.1639 0.0729 0.2551 -0.0195 0.0168  -0.0251 100 LEU A C    
818  O  O    . LEU A 100 ? 0.1860 0.0361 0.2486 -0.0047 0.0152  -0.0231 100 LEU A O    
819  C  CB   . LEU A 100 ? 0.2489 0.1472 0.3167 0.0123  0.0299  0.0147  100 LEU A CB   
820  C  CG   . LEU A 100 ? 0.2952 0.1693 0.3261 0.0117  0.0254  0.0122  100 LEU A CG   
821  C  CD1  . LEU A 100 ? 0.3424 0.3707 0.3501 0.0529  0.0128  0.0065  100 LEU A CD1  
822  C  CD2  . LEU A 100 ? 0.4251 0.2703 0.3534 0.0394  0.0607  -0.0906 100 LEU A CD2  
823  N  N    . ASP A 101 ? 0.1378 0.0748 0.2850 -0.0212 0.0075  -0.0121 101 ASP A N    
824  C  CA   . ASP A 101 ? 0.1671 0.0766 0.2582 -0.0196 0.0023  0.0015  101 ASP A CA   
825  C  C    . ASP A 101 ? 0.1900 0.0627 0.2532 -0.0075 0.0265  0.0044  101 ASP A C    
826  O  O    . ASP A 101 ? 0.2191 0.0843 0.2602 0.0112  0.0314  0.0293  101 ASP A O    
827  C  CB   . ASP A 101 ? 0.1916 0.0728 0.2440 -0.0585 -0.0011 0.0195  101 ASP A CB   
828  C  CG   . ASP A 101 ? 0.2281 0.0694 0.3050 -0.0050 -0.0175 -0.0118 101 ASP A CG   
829  O  OD1  . ASP A 101 ? 0.2224 0.0974 0.2803 -0.0289 -0.0020 -0.0004 101 ASP A OD1  
830  O  OD2  . ASP A 101 ? 0.2716 0.1192 0.3776 -0.0883 -0.0440 -0.0132 101 ASP A OD2  
831  N  N    . GLY A 102 ? 0.2113 0.0606 0.2358 -0.0176 -0.0023 0.0234  102 GLY A N    
832  C  CA   . GLY A 102 ? 0.1967 0.0715 0.2536 -0.0208 -0.0177 0.0155  102 GLY A CA   
833  C  C    . GLY A 102 ? 0.1617 0.0479 0.2235 -0.0013 0.0083  0.0113  102 GLY A C    
834  O  O    . GLY A 102 ? 0.1786 0.0876 0.2172 -0.0162 0.0153  0.0205  102 GLY A O    
835  N  N    . GLN A 103 ? 0.1467 0.0553 0.2209 0.0054  0.0086  0.0128  103 GLN A N    
836  C  CA   . GLN A 103 ? 0.1207 0.0400 0.2029 0.0054  -0.0077 -0.0062 103 GLN A CA   
837  C  C    . GLN A 103 ? 0.1124 0.0590 0.1654 -0.0214 0.0234  -0.0052 103 GLN A C    
838  O  O    . GLN A 103 ? 0.1584 0.0433 0.1807 0.0029  0.0141  -0.0045 103 GLN A O    
839  C  CB   . GLN A 103 ? 0.1485 0.0688 0.2172 0.0036  0.0302  -0.0070 103 GLN A CB   
840  C  CG   . GLN A 103 ? 0.1716 0.0802 0.2191 0.0619  0.0719  0.0048  103 GLN A CG   
841  C  CD   . GLN A 103 ? 0.1929 0.0734 0.2714 0.0590  0.0483  0.0174  103 GLN A CD   
842  O  OE1  . GLN A 103 ? 0.2974 0.2247 0.3411 0.1242  0.0993  0.1052  103 GLN A OE1  
843  N  NE2  . GLN A 103 ? 0.1455 0.1578 0.2794 0.0264  0.0517  0.0274  103 GLN A NE2  
844  N  N    . GLY A 104 ? 0.0976 0.0527 0.2006 0.0055  0.0082  -0.0127 104 GLY A N    
845  C  CA   . GLY A 104 ? 0.1087 0.0495 0.1637 0.0048  0.0338  0.0050  104 GLY A CA   
846  C  C    . GLY A 104 ? 0.1062 0.0545 0.1593 -0.0021 0.0214  -0.0143 104 GLY A C    
847  O  O    . GLY A 104 ? 0.1087 0.0598 0.1810 -0.0225 0.0186  0.0076  104 GLY A O    
848  N  N    . SER A 105 ? 0.1017 0.0494 0.1529 0.0050  0.0330  -0.0109 105 SER A N    
849  C  CA   . SER A 105 ? 0.1060 0.0329 0.1663 -0.0074 0.0280  -0.0222 105 SER A CA   
850  C  C    . SER A 105 ? 0.0963 0.0344 0.1644 0.0071  0.0183  -0.0086 105 SER A C    
851  O  O    . SER A 105 ? 0.1243 0.0269 0.1839 0.0014  0.0003  -0.0159 105 SER A O    
852  C  CB   . SER A 105 ? 0.0758 0.0426 0.1692 0.0219  0.0141  0.0050  105 SER A CB   
853  O  OG   . SER A 105 ? 0.0954 0.0293 0.1937 0.0013  0.0156  0.0032  105 SER A OG   
854  N  N    . GLU A 106 ? 0.1125 0.0284 0.1412 -0.0160 0.0147  -0.0065 106 GLU A N    
855  C  CA   . GLU A 106 ? 0.1184 0.0279 0.1466 -0.0147 0.0072  0.0051  106 GLU A CA   
856  C  C    . GLU A 106 ? 0.1098 0.0254 0.1396 0.0021  0.0116  -0.0014 106 GLU A C    
857  O  O    . GLU A 106 ? 0.0952 0.0437 0.1776 -0.0022 0.0005  -0.0057 106 GLU A O    
858  C  CB   . GLU A 106 ? 0.1245 0.0330 0.1478 -0.0180 0.0107  0.0212  106 GLU A CB   
859  C  CG   . GLU A 106 ? 0.1415 0.0500 0.1478 -0.0339 0.0389  0.0101  106 GLU A CG   
860  C  CD   . GLU A 106 ? 0.1076 0.0591 0.1541 -0.0162 0.0592  -0.0002 106 GLU A CD   
861  O  OE1  . GLU A 106 ? 0.0570 0.0354 0.2075 0.0023  0.0174  -0.0129 106 GLU A OE1  
862  O  OE2  . GLU A 106 ? 0.0962 0.0489 0.1977 -0.0080 0.0294  -0.0122 106 GLU A OE2  
863  N  N    . HIS A 107 ? 0.0827 0.0323 0.1680 0.0051  0.0226  -0.0145 107 HIS A N    
864  C  CA   . HIS A 107 ? 0.0915 0.0292 0.1523 0.0127  0.0230  -0.0088 107 HIS A CA   
865  C  C    . HIS A 107 ? 0.0739 0.0440 0.1514 0.0016  0.0069  0.0011  107 HIS A C    
866  O  O    . HIS A 107 ? 0.0849 0.0518 0.1615 0.0015  0.0078  0.0029  107 HIS A O    
867  C  CB   . HIS A 107 ? 0.1035 0.0302 0.1640 0.0150  0.0322  -0.0098 107 HIS A CB   
868  C  CG   . HIS A 107 ? 0.0856 0.0262 0.1526 0.0065  0.0150  0.0043  107 HIS A CG   
869  N  ND1  . HIS A 107 ? 0.0766 0.0286 0.1723 -0.0046 -0.0185 0.0040  107 HIS A ND1  
870  C  CD2  . HIS A 107 ? 0.0925 0.0499 0.1537 0.0013  0.0238  -0.0149 107 HIS A CD2  
871  C  CE1  . HIS A 107 ? 0.0776 0.0257 0.1794 0.0036  -0.0056 0.0040  107 HIS A CE1  
872  N  NE2  . HIS A 107 ? 0.0862 0.0531 0.1830 0.0024  0.0242  0.0212  107 HIS A NE2  
873  N  N    . THR A 108 ? 0.0949 0.0522 0.1563 -0.0048 0.0222  0.0213  108 THR A N    
874  C  CA   . THR A 108 ? 0.1039 0.0375 0.1672 0.0127  0.0196  0.0304  108 THR A CA   
875  C  C    . THR A 108 ? 0.1013 0.0584 0.1661 0.0048  0.0109  0.0057  108 THR A C    
876  O  O    . THR A 108 ? 0.1227 0.0483 0.1727 0.0007  0.0208  0.0159  108 THR A O    
877  C  CB   . THR A 108 ? 0.1068 0.0435 0.1804 0.0235  -0.0092 0.0027  108 THR A CB   
878  O  OG1  . THR A 108 ? 0.1237 0.0551 0.1719 0.0037  0.0046  0.0110  108 THR A OG1  
879  C  CG2  . THR A 108 ? 0.1374 0.0797 0.1645 0.0313  0.0284  -0.0045 108 THR A CG2  
880  N  N    . VAL A 109 ? 0.0872 0.0640 0.1744 -0.0154 0.0087  0.0249  109 VAL A N    
881  C  CA   . VAL A 109 ? 0.1502 0.0546 0.1627 -0.0052 0.0138  0.0363  109 VAL A CA   
882  C  C    . VAL A 109 ? 0.1494 0.0743 0.1922 -0.0179 0.0139  0.0290  109 VAL A C    
883  O  O    . VAL A 109 ? 0.1490 0.0424 0.2319 -0.0159 0.0278  0.0266  109 VAL A O    
884  C  CB   . VAL A 109 ? 0.1185 0.0837 0.2196 0.0053  0.0184  0.0423  109 VAL A CB   
885  C  CG1  . VAL A 109 ? 0.1356 0.0997 0.2419 -0.0112 0.0264  0.0253  109 VAL A CG1  
886  C  CG2  . VAL A 109 ? 0.1349 0.0831 0.2203 -0.0007 -0.0115 0.0361  109 VAL A CG2  
887  N  N    . ASP A 110 ? 0.1729 0.0537 0.1695 0.0187  0.0180  0.0342  110 ASP A N    
888  C  CA   . ASP A 110 ? 0.1684 0.0618 0.1890 0.0269  0.0282  0.0408  110 ASP A CA   
889  C  C    . ASP A 110 ? 0.1838 0.0599 0.1979 0.0213  0.0319  0.0138  110 ASP A C    
890  O  O    . ASP A 110 ? 0.2016 0.0643 0.2306 0.0111  0.0023  0.0298  110 ASP A O    
891  C  CB   . ASP A 110 ? 0.2030 0.0949 0.2195 0.0183  0.0616  0.0483  110 ASP A CB   
892  C  CG   . ASP A 110 ? 0.2227 0.0675 0.2021 0.0032  0.0561  0.0397  110 ASP A CG   
893  O  OD1  . ASP A 110 ? 0.2391 0.1105 0.2409 0.0423  0.0681  0.0230  110 ASP A OD1  
894  O  OD2  . ASP A 110 ? 0.2048 0.1763 0.2815 0.0139  0.0754  0.0412  110 ASP A OD2  
895  N  N    . LYS A 111 ? 0.1660 0.0620 0.1816 0.0188  0.0405  0.0207  111 LYS A N    
896  C  CA   . LYS A 111 ? 0.1589 0.0620 0.2104 0.0407  0.0079  0.0023  111 LYS A CA   
897  C  C    . LYS A 111 ? 0.1737 0.0690 0.2005 0.0227  0.0084  0.0093  111 LYS A C    
898  O  O    . LYS A 111 ? 0.1868 0.0842 0.2397 0.0328  0.0146  0.0013  111 LYS A O    
899  C  CB   . LYS A 111 ? 0.2088 0.0810 0.2282 0.0576  -0.0066 0.0231  111 LYS A CB   
900  C  CG   . LYS A 111 ? 0.2411 0.1631 0.2555 0.0550  -0.0294 0.0100  111 LYS A CG   
901  C  CD   . LYS A 111 ? 0.2097 0.2586 0.3089 0.0390  -0.0322 -0.0375 111 LYS A CD   
902  C  CE   . LYS A 111 ? 0.3264 0.3742 0.3603 0.0309  -0.0383 -0.0604 111 LYS A CE   
903  N  NZ   . LYS A 111 ? 0.3009 0.4038 0.4093 0.0128  -0.0206 0.0082  111 LYS A NZ   
904  N  N    . LYS A 112 ? 0.1736 0.0436 0.1898 0.0011  0.0005  0.0461  112 LYS A N    
905  C  CA   . LYS A 112 ? 0.1462 0.0686 0.1863 -0.0075 0.0095  0.0114  112 LYS A CA   
906  C  C    . LYS A 112 ? 0.1308 0.0752 0.1815 0.0128  0.0171  0.0218  112 LYS A C    
907  O  O    . LYS A 112 ? 0.1467 0.0579 0.1955 0.0160  0.0125  -0.0003 112 LYS A O    
908  C  CB   . LYS A 112 ? 0.1701 0.1235 0.2282 -0.0629 0.0082  0.0273  112 LYS A CB   
909  C  CG   . LYS A 112 ? 0.1464 0.1686 0.2311 -0.0304 0.0209  -0.0382 112 LYS A CG   
910  C  CD   . LYS A 112 ? 0.1743 0.2367 0.3266 -0.0209 -0.0333 0.0067  112 LYS A CD   
911  C  CE   . LYS A 112 ? 0.2853 0.1939 0.2956 0.0432  -0.0060 0.0075  112 LYS A CE   
912  N  NZ   . LYS A 112 ? 0.3335 0.2099 0.3215 0.0172  -0.0319 0.0154  112 LYS A NZ   
913  N  N    . LYS A 113 ? 0.1453 0.0644 0.1855 0.0103  0.0255  0.0172  113 LYS A N    
914  C  CA   . LYS A 113 ? 0.1337 0.0647 0.1930 0.0093  0.0180  0.0191  113 LYS A CA   
915  C  C    . LYS A 113 ? 0.1422 0.0388 0.1887 0.0184  -0.0042 0.0156  113 LYS A C    
916  O  O    . LYS A 113 ? 0.1906 0.0308 0.2508 -0.0016 -0.0102 0.0049  113 LYS A O    
917  C  CB   . LYS A 113 ? 0.1246 0.0656 0.2054 0.0092  0.0168  0.0048  113 LYS A CB   
918  C  CG   . LYS A 113 ? 0.1299 0.0909 0.2103 0.0439  0.0268  0.0093  113 LYS A CG   
919  C  CD   . LYS A 113 ? 0.1075 0.1064 0.2701 0.0144  0.0086  -0.0061 113 LYS A CD   
920  C  CE   . LYS A 113 ? 0.1254 0.1465 0.3358 -0.0032 -0.0088 -0.0440 113 LYS A CE   
921  N  NZ   . LYS A 113 ? 0.2990 0.2407 0.4302 0.0048  -0.1083 -0.0406 113 LYS A NZ   
922  N  N    . TYR A 114 ? 0.1111 0.0507 0.1797 0.0277  -0.0036 0.0081  114 TYR A N    
923  C  CA   . TYR A 114 ? 0.1154 0.0450 0.1623 0.0103  -0.0077 0.0263  114 TYR A CA   
924  C  C    . TYR A 114 ? 0.0980 0.0552 0.1738 -0.0071 0.0067  -0.0014 114 TYR A C    
925  O  O    . TYR A 114 ? 0.0879 0.0467 0.2110 -0.0066 0.0136  -0.0031 114 TYR A O    
926  C  CB   . TYR A 114 ? 0.0759 0.0628 0.2026 0.0007  0.0188  -0.0021 114 TYR A CB   
927  C  CG   . TYR A 114 ? 0.1176 0.0336 0.1918 0.0127  -0.0057 0.0321  114 TYR A CG   
928  C  CD1  . TYR A 114 ? 0.1365 0.0576 0.1882 -0.0014 0.0121  0.0432  114 TYR A CD1  
929  C  CD2  . TYR A 114 ? 0.1118 0.0642 0.2302 -0.0216 0.0230  0.0275  114 TYR A CD2  
930  C  CE1  . TYR A 114 ? 0.2027 0.0764 0.1997 0.0069  0.0052  0.0236  114 TYR A CE1  
931  C  CE2  . TYR A 114 ? 0.1116 0.0996 0.2181 -0.0127 0.0220  0.0292  114 TYR A CE2  
932  C  CZ   . TYR A 114 ? 0.2131 0.0983 0.2086 -0.0113 0.0388  0.0323  114 TYR A CZ   
933  O  OH   . TYR A 114 ? 0.2396 0.1896 0.2868 0.0067  0.0997  0.0260  114 TYR A OH   
934  N  N    . ALA A 115 ? 0.1185 0.0268 0.1659 -0.0101 -0.0044 -0.0068 115 ALA A N    
935  C  CA   . ALA A 115 ? 0.1139 0.0263 0.1687 -0.0091 0.0115  -0.0046 115 ALA A CA   
936  C  C    . ALA A 115 ? 0.1009 0.0290 0.1798 0.0066  0.0097  0.0009  115 ALA A C    
937  O  O    . ALA A 115 ? 0.1257 0.0348 0.2025 -0.0055 0.0209  -0.0153 115 ALA A O    
938  C  CB   . ALA A 115 ? 0.1577 0.0436 0.2325 -0.0205 0.0011  -0.0173 115 ALA A CB   
939  N  N    . ALA A 116 ? 0.1110 0.0266 0.1792 0.0104  -0.0022 -0.0011 116 ALA A N    
940  C  CA   . ALA A 116 ? 0.1329 0.0295 0.1605 0.0013  0.0220  0.0076  116 ALA A CA   
941  C  C    . ALA A 116 ? 0.1053 0.0260 0.1697 -0.0076 0.0235  0.0001  116 ALA A C    
942  O  O    . ALA A 116 ? 0.1055 0.0366 0.1759 -0.0058 0.0061  0.0002  116 ALA A O    
943  C  CB   . ALA A 116 ? 0.0982 0.0634 0.1589 -0.0047 0.0151  0.0100  116 ALA A CB   
944  N  N    . GLU A 117 ? 0.0980 0.0266 0.1624 -0.0096 0.0094  -0.0019 117 GLU A N    
945  C  CA   . GLU A 117 ? 0.1163 0.0301 0.1410 0.0104  0.0109  -0.0189 117 GLU A CA   
946  C  C    . GLU A 117 ? 0.0782 0.0544 0.1538 -0.0146 0.0098  0.0047  117 GLU A C    
947  O  O    . GLU A 117 ? 0.0886 0.0546 0.1891 -0.0037 0.0193  0.0064  117 GLU A O    
948  C  CB   . GLU A 117 ? 0.0873 0.0349 0.1483 -0.0105 0.0061  -0.0199 117 GLU A CB   
949  C  CG   . GLU A 117 ? 0.1015 0.0559 0.1447 -0.0166 -0.0073 -0.0313 117 GLU A CG   
950  C  CD   . GLU A 117 ? 0.0740 0.0332 0.1637 -0.0143 0.0134  -0.0262 117 GLU A CD   
951  O  OE1  . GLU A 117 ? 0.0793 0.0564 0.1983 0.0046  0.0102  -0.0043 117 GLU A OE1  
952  O  OE2  . GLU A 117 ? 0.1118 0.0339 0.1544 -0.0155 -0.0132 -0.0060 117 GLU A OE2  
953  N  N    . LEU A 118 ? 0.0878 0.0325 0.1620 0.0197  -0.0094 0.0087  118 LEU A N    
954  C  CA   . LEU A 118 ? 0.0793 0.0300 0.1537 0.0136  -0.0167 -0.0169 118 LEU A CA   
955  C  C    . LEU A 118 ? 0.0775 0.0446 0.1379 0.0056  0.0161  -0.0006 118 LEU A C    
956  O  O    . LEU A 118 ? 0.1044 0.0257 0.1436 -0.0005 0.0119  -0.0073 118 LEU A O    
957  C  CB   . LEU A 118 ? 0.0772 0.0325 0.1818 0.0051  -0.0202 0.0045  118 LEU A CB   
958  C  CG   . LEU A 118 ? 0.1142 0.0312 0.1802 0.0005  0.0030  0.0303  118 LEU A CG   
959  C  CD1  . LEU A 118 ? 0.1632 0.0539 0.1712 -0.0131 0.0000  0.0032  118 LEU A CD1  
960  C  CD2  . LEU A 118 ? 0.0906 0.1051 0.2217 -0.0283 -0.0272 0.0072  118 LEU A CD2  
961  N  N    . HIS A 119 ? 0.0961 0.0268 0.1530 -0.0102 0.0180  -0.0045 119 HIS A N    
962  C  CA   . HIS A 119 ? 0.0623 0.0402 0.1552 -0.0085 -0.0069 -0.0003 119 HIS A CA   
963  C  C    . HIS A 119 ? 0.0681 0.0394 0.1485 -0.0193 -0.0028 -0.0007 119 HIS A C    
964  O  O    . HIS A 119 ? 0.0986 0.0363 0.1694 -0.0044 0.0128  0.0002  119 HIS A O    
965  C  CB   . HIS A 119 ? 0.0835 0.0528 0.1642 0.0341  0.0150  0.0085  119 HIS A CB   
966  C  CG   . HIS A 119 ? 0.1012 0.0335 0.1515 -0.0034 -0.0019 -0.0056 119 HIS A CG   
967  N  ND1  . HIS A 119 ? 0.0663 0.0271 0.1684 -0.0065 -0.0154 0.0083  119 HIS A ND1  
968  C  CD2  . HIS A 119 ? 0.1080 0.0254 0.1526 -0.0025 0.0213  0.0017  119 HIS A CD2  
969  C  CE1  . HIS A 119 ? 0.0807 0.0385 0.1505 0.0060  -0.0152 -0.0153 119 HIS A CE1  
970  N  NE2  . HIS A 119 ? 0.1030 0.0442 0.1874 0.0352  0.0077  0.0169  119 HIS A NE2  
971  N  N    . LEU A 120 ? 0.0892 0.0272 0.1622 0.0104  -0.0019 0.0056  120 LEU A N    
972  C  CA   . LEU A 120 ? 0.0973 0.0308 0.1662 0.0062  -0.0213 -0.0088 120 LEU A CA   
973  C  C    . LEU A 120 ? 0.1119 0.0276 0.1421 0.0111  -0.0007 0.0101  120 LEU A C    
974  O  O    . LEU A 120 ? 0.0781 0.0264 0.1629 -0.0009 -0.0014 0.0121  120 LEU A O    
975  C  CB   . LEU A 120 ? 0.0818 0.0403 0.1815 -0.0057 -0.0295 0.0006  120 LEU A CB   
976  C  CG   . LEU A 120 ? 0.1040 0.0564 0.1809 -0.0045 -0.0074 -0.0013 120 LEU A CG   
977  C  CD1  . LEU A 120 ? 0.1802 0.1049 0.2119 -0.0714 0.0142  0.0359  120 LEU A CD1  
978  C  CD2  . LEU A 120 ? 0.1151 0.1059 0.2307 -0.0073 -0.0792 -0.0045 120 LEU A CD2  
979  N  N    . VAL A 121 ? 0.1099 0.0282 0.1687 -0.0143 -0.0051 0.0094  121 VAL A N    
980  C  CA   . VAL A 121 ? 0.1036 0.0288 0.1770 -0.0092 0.0002  0.0043  121 VAL A CA   
981  C  C    . VAL A 121 ? 0.1125 0.0268 0.1603 -0.0105 -0.0056 0.0063  121 VAL A C    
982  O  O    . VAL A 121 ? 0.1360 0.0438 0.1553 -0.0056 -0.0080 0.0009  121 VAL A O    
983  C  CB   . VAL A 121 ? 0.0880 0.0263 0.2049 -0.0078 0.0100  -0.0045 121 VAL A CB   
984  C  CG1  . VAL A 121 ? 0.1140 0.0487 0.2061 -0.0303 0.0139  -0.0244 121 VAL A CG1  
985  C  CG2  . VAL A 121 ? 0.1323 0.0345 0.1758 -0.0011 -0.0157 0.0043  121 VAL A CG2  
986  N  N    . HIS A 122 ? 0.0913 0.0281 0.1485 -0.0045 0.0066  -0.0178 122 HIS A N    
987  C  CA   . HIS A 122 ? 0.0910 0.0260 0.1777 -0.0034 0.0109  -0.0095 122 HIS A CA   
988  C  C    . HIS A 122 ? 0.0854 0.0438 0.1703 -0.0094 0.0064  0.0035  122 HIS A C    
989  O  O    . HIS A 122 ? 0.1307 0.0266 0.2002 -0.0095 -0.0148 -0.0074 122 HIS A O    
990  C  CB   . HIS A 122 ? 0.0800 0.0444 0.2046 0.0036  0.0144  -0.0103 122 HIS A CB   
991  C  CG   . HIS A 122 ? 0.1261 0.0275 0.1667 -0.0061 0.0181  0.0033  122 HIS A CG   
992  N  ND1  . HIS A 122 ? 0.0695 0.0265 0.2303 -0.0069 0.0059  -0.0066 122 HIS A ND1  
993  C  CD2  . HIS A 122 ? 0.1236 0.0311 0.1974 -0.0190 0.0005  -0.0113 122 HIS A CD2  
994  C  CE1  . HIS A 122 ? 0.0483 0.0595 0.2144 0.0227  0.0081  -0.0057 122 HIS A CE1  
995  N  NE2  . HIS A 122 ? 0.0718 0.0597 0.2145 -0.0003 -0.0122 -0.0078 122 HIS A NE2  
996  N  N    . TRP A 123 ? 0.1151 0.0256 0.1881 -0.0014 0.0056  -0.0069 123 TRP A N    
997  C  CA   . TRP A 123 ? 0.0995 0.0289 0.1926 -0.0154 0.0213  -0.0124 123 TRP A CA   
998  C  C    . TRP A 123 ? 0.0958 0.0337 0.1904 -0.0090 0.0002  0.0004  123 TRP A C    
999  O  O    . TRP A 123 ? 0.1158 0.0385 0.2280 0.0108  -0.0178 -0.0167 123 TRP A O    
1000 C  CB   . TRP A 123 ? 0.1272 0.0691 0.1942 -0.0130 0.0090  -0.0054 123 TRP A CB   
1001 C  CG   . TRP A 123 ? 0.1552 0.0303 0.2068 -0.0120 -0.0038 0.0270  123 TRP A CG   
1002 C  CD1  . TRP A 123 ? 0.1514 0.0916 0.1783 -0.0308 -0.0223 0.0245  123 TRP A CD1  
1003 C  CD2  . TRP A 123 ? 0.1965 0.0437 0.1707 -0.0091 0.0114  -0.0173 123 TRP A CD2  
1004 N  NE1  . TRP A 123 ? 0.2331 0.0478 0.1893 -0.0387 -0.0271 -0.0034 123 TRP A NE1  
1005 C  CE2  . TRP A 123 ? 0.2074 0.0397 0.1907 -0.0099 -0.0192 0.0045  123 TRP A CE2  
1006 C  CE3  . TRP A 123 ? 0.2103 0.0265 0.2003 -0.0152 -0.0051 -0.0004 123 TRP A CE3  
1007 C  CZ2  . TRP A 123 ? 0.2515 0.0295 0.2295 0.0042  0.0029  0.0113  123 TRP A CZ2  
1008 C  CZ3  . TRP A 123 ? 0.1935 0.0635 0.2479 -0.0062 -0.0113 0.0223  123 TRP A CZ3  
1009 C  CH2  . TRP A 123 ? 0.2334 0.0607 0.2317 -0.0469 -0.0288 0.0161  123 TRP A CH2  
1010 N  N    . ASN A 124 ? 0.0628 0.0423 0.2021 -0.0097 -0.0042 -0.0388 124 ASN A N    
1011 C  CA   . ASN A 124 ? 0.1610 0.0331 0.1965 -0.0086 0.0151  -0.0273 124 ASN A CA   
1012 C  C    . ASN A 124 ? 0.1419 0.0438 0.2192 0.0015  0.0034  -0.0218 124 ASN A C    
1013 O  O    . ASN A 124 ? 0.1254 0.0420 0.2359 -0.0082 -0.0007 -0.0248 124 ASN A O    
1014 C  CB   . ASN A 124 ? 0.1363 0.0636 0.1760 0.0007  0.0347  -0.0372 124 ASN A CB   
1015 C  CG   . ASN A 124 ? 0.1746 0.0262 0.2037 -0.0081 0.0197  -0.0101 124 ASN A CG   
1016 O  OD1  . ASN A 124 ? 0.2055 0.0401 0.2398 0.0173  0.0084  -0.0128 124 ASN A OD1  
1017 N  ND2  . ASN A 124 ? 0.2170 0.0560 0.2048 -0.0068 0.0202  -0.0183 124 ASN A ND2  
1018 N  N    . THR A 125 ? 0.1638 0.0464 0.2421 0.0309  -0.0109 -0.0032 125 THR A N    
1019 C  CA   . THR A 125 ? 0.1459 0.0588 0.2530 0.0373  -0.0358 -0.0071 125 THR A CA   
1020 C  C    . THR A 125 ? 0.1548 0.0746 0.2705 0.0621  -0.0113 -0.0122 125 THR A C    
1021 O  O    . THR A 125 ? 0.1797 0.0643 0.3312 0.0292  -0.0091 -0.0070 125 THR A O    
1022 C  CB   . THR A 125 ? 0.1512 0.1152 0.2934 0.0421  -0.0245 0.0051  125 THR A CB   
1023 O  OG1  . THR A 125 ? 0.2114 0.1151 0.3356 0.0591  0.0254  -0.0081 125 THR A OG1  
1024 C  CG2  . THR A 125 ? 0.2016 0.1183 0.3058 0.0200  -0.0331 0.0121  125 THR A CG2  
1025 N  N    . LYS A 126 ? 0.1864 0.0363 0.2430 0.0042  0.0201  -0.0374 127 LYS A N    
1026 C  CA   . LYS A 126 ? 0.2094 0.0882 0.2651 -0.0072 0.0217  -0.0561 127 LYS A CA   
1027 C  C    . LYS A 126 ? 0.2007 0.0407 0.2636 -0.0096 0.0146  -0.0282 127 LYS A C    
1028 O  O    . LYS A 126 ? 0.2447 0.0744 0.3095 -0.0156 0.0270  -0.0782 127 LYS A O    
1029 C  CB   . LYS A 126 ? 0.2175 0.1127 0.2929 -0.0040 0.0035  -0.0541 127 LYS A CB   
1030 C  CG   . LYS A 126 ? 0.2456 0.1433 0.2555 0.0076  0.0070  -0.0467 127 LYS A CG   
1031 C  CD   . LYS A 126 ? 0.3160 0.2556 0.2879 -0.0321 0.0328  -0.0289 127 LYS A CD   
1032 C  CE   . LYS A 126 ? 0.3085 0.3049 0.3645 0.0141  0.0047  -0.0356 127 LYS A CE   
1033 N  NZ   . LYS A 126 ? 0.4791 0.3229 0.3707 0.0265  0.0089  -0.0533 127 LYS A NZ   
1034 N  N    . TYR A 127 ? 0.1982 0.0304 0.2305 -0.0034 0.0155  -0.0188 128 TYR A N    
1035 C  CA   . TYR A 127 ? 0.1869 0.0629 0.2206 -0.0030 -0.0050 0.0111  128 TYR A CA   
1036 C  C    . TYR A 127 ? 0.1967 0.0446 0.2346 -0.0019 0.0108  -0.0040 128 TYR A C    
1037 O  O    . TYR A 127 ? 0.1795 0.0661 0.2614 -0.0142 0.0213  0.0192  128 TYR A O    
1038 C  CB   . TYR A 127 ? 0.1878 0.0662 0.2205 -0.0028 0.0094  -0.0210 128 TYR A CB   
1039 C  CG   . TYR A 127 ? 0.1599 0.0702 0.1898 -0.0198 -0.0031 -0.0248 128 TYR A CG   
1040 C  CD1  . TYR A 127 ? 0.2101 0.0578 0.2187 -0.0091 -0.0080 -0.0471 128 TYR A CD1  
1041 C  CD2  . TYR A 127 ? 0.1575 0.0724 0.2013 0.0101  0.0200  -0.0014 128 TYR A CD2  
1042 C  CE1  . TYR A 127 ? 0.2312 0.0695 0.2168 0.0014  -0.0220 -0.0415 128 TYR A CE1  
1043 C  CE2  . TYR A 127 ? 0.1471 0.0752 0.2068 0.0237  0.0047  -0.0504 128 TYR A CE2  
1044 C  CZ   . TYR A 127 ? 0.1695 0.1047 0.1873 0.0027  0.0013  -0.0362 128 TYR A CZ   
1045 O  OH   . TYR A 127 ? 0.2934 0.0840 0.2002 0.0253  0.0078  -0.0435 128 TYR A OH   
1046 N  N    . GLY A 128 ? 0.1766 0.0422 0.2340 -0.0034 0.0062  0.0068  129 GLY A N    
1047 C  CA   . GLY A 128 ? 0.1943 0.0545 0.2321 -0.0090 0.0202  0.0191  129 GLY A CA   
1048 C  C    . GLY A 128 ? 0.1866 0.0339 0.2270 -0.0049 0.0071  0.0240  129 GLY A C    
1049 O  O    . GLY A 128 ? 0.2590 0.0727 0.2339 -0.0016 -0.0103 0.0430  129 GLY A O    
1050 N  N    . ASP A 129 ? 0.1953 0.0482 0.2318 0.0173  -0.0085 0.0047  130 ASP A N    
1051 C  CA   . ASP A 129 ? 0.2521 0.0574 0.2248 0.0032  0.0056  0.0060  130 ASP A CA   
1052 C  C    . ASP A 129 ? 0.2186 0.0779 0.2149 0.0001  -0.0095 -0.0113 130 ASP A C    
1053 O  O    . ASP A 129 ? 0.2427 0.0738 0.2119 0.0069  -0.0177 -0.0117 130 ASP A O    
1054 C  CB   . ASP A 129 ? 0.2354 0.1025 0.2451 0.0184  0.0221  -0.0046 130 ASP A CB   
1055 C  CG   . ASP A 129 ? 0.2313 0.0316 0.2972 0.0347  0.0285  0.0157  130 ASP A CG   
1056 O  OD1  . ASP A 129 ? 0.3450 0.1548 0.3405 -0.0585 -0.0821 0.0472  130 ASP A OD1  
1057 O  OD2  . ASP A 129 ? 0.2826 0.1375 0.3958 0.0025  0.0992  0.0708  130 ASP A OD2  
1058 N  N    . PHE A 130 ? 0.2301 0.0616 0.2105 0.0116  -0.0026 -0.0072 131 PHE A N    
1059 C  CA   . PHE A 130 ? 0.1951 0.0783 0.2084 -0.0006 -0.0088 -0.0013 131 PHE A CA   
1060 C  C    . PHE A 130 ? 0.1811 0.0523 0.1989 -0.0107 0.0075  0.0100  131 PHE A C    
1061 O  O    . PHE A 130 ? 0.1739 0.0673 0.1807 -0.0235 0.0086  0.0048  131 PHE A O    
1062 C  CB   . PHE A 130 ? 0.2236 0.0382 0.2120 -0.0070 -0.0065 0.0099  131 PHE A CB   
1063 C  CG   . PHE A 130 ? 0.1856 0.0570 0.2108 -0.0220 0.0163  -0.0076 131 PHE A CG   
1064 C  CD1  . PHE A 130 ? 0.2097 0.0284 0.2080 -0.0134 0.0271  0.0146  131 PHE A CD1  
1065 C  CD2  . PHE A 130 ? 0.2185 0.0532 0.2561 -0.0090 0.0367  -0.0009 131 PHE A CD2  
1066 C  CE1  . PHE A 130 ? 0.1906 0.0761 0.2134 -0.0417 -0.0003 -0.0144 131 PHE A CE1  
1067 C  CE2  . PHE A 130 ? 0.2477 0.0800 0.2664 -0.0115 0.0373  0.0201  131 PHE A CE2  
1068 C  CZ   . PHE A 130 ? 0.2381 0.1113 0.2427 -0.0274 0.0109  0.0116  131 PHE A CZ   
1069 N  N    . GLY A 131 ? 0.1860 0.0727 0.2191 -0.0302 0.0226  -0.0048 132 GLY A N    
1070 C  CA   . GLY A 131 ? 0.1766 0.1057 0.2248 -0.0393 0.0221  0.0182  132 GLY A CA   
1071 C  C    . GLY A 131 ? 0.1652 0.0726 0.2259 -0.0396 0.0307  0.0228  132 GLY A C    
1072 O  O    . GLY A 131 ? 0.2007 0.1081 0.2710 -0.0194 0.0206  -0.0059 132 GLY A O    
1073 N  N    A LYS A 132 ? 0.1684 0.0630 0.2253 -0.0392 0.0284  0.0116  133 LYS A N    
1074 N  N    B LYS A 132 ? 0.1750 0.0784 0.2272 -0.0471 0.0287  0.0063  133 LYS A N    
1075 C  CA   A LYS A 132 ? 0.1626 0.0347 0.2253 -0.0271 0.0091  0.0148  133 LYS A CA   
1076 C  CA   B LYS A 132 ? 0.1746 0.0687 0.2268 -0.0414 0.0159  0.0008  133 LYS A CA   
1077 C  C    A LYS A 132 ? 0.1371 0.0510 0.2178 -0.0315 0.0070  0.0157  133 LYS A C    
1078 C  C    B LYS A 132 ? 0.1596 0.0721 0.2268 -0.0422 0.0138  0.0025  133 LYS A C    
1079 O  O    A LYS A 132 ? 0.1373 0.0463 0.2288 -0.0108 -0.0086 0.0107  133 LYS A O    
1080 O  O    B LYS A 132 ? 0.1647 0.0637 0.2397 -0.0140 0.0184  -0.0055 133 LYS A O    
1081 C  CB   A LYS A 132 ? 0.1277 0.0321 0.2346 0.0069  0.0055  0.0175  133 LYS A CB   
1082 C  CB   B LYS A 132 ? 0.1552 0.0960 0.2362 -0.0300 0.0124  -0.0032 133 LYS A CB   
1083 C  CG   A LYS A 132 ? 0.1475 0.0313 0.2185 -0.0023 0.0091  0.0338  133 LYS A CG   
1084 C  CG   B LYS A 132 ? 0.1492 0.1021 0.1848 -0.0180 0.0080  -0.0007 133 LYS A CG   
1085 C  CD   A LYS A 132 ? 0.1257 0.0736 0.1468 0.0034  0.0061  0.0094  133 LYS A CD   
1086 C  CD   B LYS A 132 ? 0.1343 0.1050 0.1486 -0.0046 0.0017  0.0021  133 LYS A CD   
1087 C  CE   A LYS A 132 ? 0.1136 0.0937 0.1267 -0.0014 -0.0010 0.0083  133 LYS A CE   
1088 C  CE   B LYS A 132 ? 0.1273 0.1166 0.1354 -0.0008 0.0010  0.0008  133 LYS A CE   
1089 N  NZ   A LYS A 132 ? 0.1121 0.0967 0.1150 0.0002  -0.0019 0.0021  133 LYS A NZ   
1090 N  NZ   B LYS A 132 ? 0.1194 0.1040 0.1218 0.0003  -0.0002 0.0001  133 LYS A NZ   
1091 N  N    . ALA A 133 ? 0.1336 0.0601 0.2196 -0.0468 0.0223  -0.0100 134 ALA A N    
1092 C  CA   . ALA A 133 ? 0.1316 0.0850 0.1993 -0.0223 0.0255  0.0050  134 ALA A CA   
1093 C  C    . ALA A 133 ? 0.1405 0.0644 0.1868 -0.0239 0.0062  -0.0108 134 ALA A C    
1094 O  O    . ALA A 133 ? 0.1056 0.0877 0.1899 -0.0169 0.0153  -0.0213 134 ALA A O    
1095 C  CB   . ALA A 133 ? 0.1290 0.0766 0.2024 -0.0723 0.0152  -0.0017 134 ALA A CB   
1096 N  N    . VAL A 134 ? 0.1505 0.0574 0.1955 -0.0353 0.0127  -0.0020 135 VAL A N    
1097 C  CA   . VAL A 134 ? 0.1497 0.0899 0.1928 -0.0189 0.0062  -0.0034 135 VAL A CA   
1098 C  C    . VAL A 134 ? 0.1196 0.0649 0.2118 -0.0209 0.0244  0.0023  135 VAL A C    
1099 O  O    . VAL A 134 ? 0.1387 0.0748 0.2424 -0.0130 0.0196  0.0043  135 VAL A O    
1100 C  CB   . VAL A 134 ? 0.1713 0.1042 0.1914 -0.0319 0.0260  -0.0073 135 VAL A CB   
1101 C  CG1  . VAL A 134 ? 0.1827 0.1207 0.1872 -0.0284 0.0032  -0.0353 135 VAL A CG1  
1102 C  CG2  . VAL A 134 ? 0.1516 0.1127 0.2099 -0.0566 0.0519  -0.0105 135 VAL A CG2  
1103 N  N    A GLN A 135 ? 0.1348 0.0837 0.2093 -0.0233 0.0176  -0.0124 136 GLN A N    
1104 N  N    B GLN A 135 ? 0.1290 0.0834 0.2116 -0.0214 0.0158  -0.0102 136 GLN A N    
1105 C  CA   A GLN A 135 ? 0.1514 0.0918 0.2228 -0.0285 0.0063  -0.0043 136 GLN A CA   
1106 C  CA   B GLN A 135 ? 0.1438 0.0955 0.2291 -0.0212 0.0009  0.0004  136 GLN A CA   
1107 C  C    A GLN A 135 ? 0.1439 0.1021 0.2162 -0.0091 -0.0059 -0.0102 136 GLN A C    
1108 C  C    B GLN A 135 ? 0.1353 0.1043 0.2201 -0.0034 -0.0103 -0.0105 136 GLN A C    
1109 O  O    A GLN A 135 ? 0.1653 0.0844 0.2315 -0.0277 -0.0125 -0.0171 136 GLN A O    
1110 O  O    B GLN A 135 ? 0.1560 0.1243 0.2357 -0.0132 -0.0238 -0.0176 136 GLN A O    
1111 C  CB   A GLN A 135 ? 0.1340 0.1270 0.2262 -0.0329 0.0223  0.0050  136 GLN A CB   
1112 C  CB   B GLN A 135 ? 0.1372 0.1163 0.2275 -0.0334 0.0143  0.0154  136 GLN A CB   
1113 C  CG   A GLN A 135 ? 0.1911 0.1166 0.2418 -0.0287 0.0349  0.0076  136 GLN A CG   
1114 C  CG   B GLN A 135 ? 0.1752 0.1486 0.2448 -0.0246 0.0028  0.0420  136 GLN A CG   
1115 C  CD   A GLN A 135 ? 0.2534 0.2329 0.2914 0.0000  0.0176  0.0106  136 GLN A CD   
1116 C  CD   B GLN A 135 ? 0.1999 0.1923 0.2827 -0.0482 -0.0036 0.0264  136 GLN A CD   
1117 O  OE1  A GLN A 135 ? 0.2282 0.3445 0.3457 -0.0147 0.0291  0.0026  136 GLN A OE1  
1118 O  OE1  B GLN A 135 ? 0.2209 0.2461 0.3378 -0.0465 0.0020  0.0247  136 GLN A OE1  
1119 N  NE2  A GLN A 135 ? 0.2853 0.1847 0.3109 -0.0422 0.0273  -0.0090 136 GLN A NE2  
1120 N  NE2  B GLN A 135 ? 0.1397 0.2105 0.3240 -0.0328 0.0064  0.0396  136 GLN A NE2  
1121 N  N    . GLN A 136 ? 0.1425 0.0937 0.2067 -0.0086 0.0213  -0.0111 137 GLN A N    
1122 C  CA   . GLN A 136 ? 0.1735 0.0902 0.1704 0.0114  0.0134  -0.0072 137 GLN A CA   
1123 C  C    . GLN A 136 ? 0.1433 0.0854 0.1696 0.0121  -0.0033 -0.0264 137 GLN A C    
1124 O  O    . GLN A 136 ? 0.1534 0.0921 0.1648 0.0012  -0.0034 -0.0349 137 GLN A O    
1125 C  CB   . GLN A 136 ? 0.1747 0.0698 0.2046 0.0175  -0.0103 -0.0014 137 GLN A CB   
1126 C  CG   . GLN A 136 ? 0.2408 0.1324 0.2422 0.0278  0.0206  0.0380  137 GLN A CG   
1127 C  CD   . GLN A 136 ? 0.2206 0.2129 0.3189 0.0059  0.0191  0.0638  137 GLN A CD   
1128 O  OE1  . GLN A 136 ? 0.2874 0.1064 0.3383 -0.0329 -0.0189 -0.0718 137 GLN A OE1  
1129 N  NE2  . GLN A 136 ? 0.3147 0.2680 0.4586 -0.0248 0.0494  0.0591  137 GLN A NE2  
1130 N  N    . PRO A 137 ? 0.1463 0.1205 0.1681 0.0013  0.0062  -0.0269 138 PRO A N    
1131 C  CA   . PRO A 137 ? 0.1896 0.1366 0.1795 -0.0043 0.0014  -0.0140 138 PRO A CA   
1132 C  C    . PRO A 137 ? 0.1793 0.1286 0.1824 -0.0142 -0.0023 -0.0081 138 PRO A C    
1133 O  O    . PRO A 137 ? 0.2027 0.1003 0.2504 0.0102  0.0245  0.0194  138 PRO A O    
1134 C  CB   . PRO A 137 ? 0.2385 0.1630 0.1846 0.0159  0.0090  -0.0326 138 PRO A CB   
1135 C  CG   . PRO A 137 ? 0.2751 0.1738 0.2224 -0.0299 -0.0114 -0.0352 138 PRO A CG   
1136 C  CD   . PRO A 137 ? 0.1509 0.1621 0.1719 -0.0410 -0.0133 -0.0547 138 PRO A CD   
1137 N  N    . ASP A 138 ? 0.1357 0.1304 0.1647 -0.0074 -0.0138 -0.0183 139 ASP A N    
1138 C  CA   . ASP A 138 ? 0.1354 0.1098 0.1691 -0.0041 0.0154  -0.0222 139 ASP A CA   
1139 C  C    . ASP A 138 ? 0.1365 0.0586 0.1774 -0.0130 0.0143  -0.0011 139 ASP A C    
1140 O  O    . ASP A 138 ? 0.1272 0.0934 0.1991 0.0120  0.0185  -0.0116 139 ASP A O    
1141 C  CB   . ASP A 138 ? 0.1715 0.1113 0.1959 -0.0008 0.0339  -0.0168 139 ASP A CB   
1142 C  CG   . ASP A 138 ? 0.1992 0.1523 0.2034 0.0142  0.0172  -0.0287 139 ASP A CG   
1143 O  OD1  . ASP A 138 ? 0.2291 0.1173 0.2391 0.0169  0.0069  -0.0464 139 ASP A OD1  
1144 O  OD2  . ASP A 138 ? 0.2255 0.1779 0.2951 0.0382  0.0563  -0.0753 139 ASP A OD2  
1145 N  N    . GLY A 139 ? 0.1245 0.0507 0.1589 -0.0308 0.0198  -0.0100 140 GLY A N    
1146 C  CA   . GLY A 139 ? 0.1170 0.0498 0.1542 -0.0148 0.0183  -0.0064 140 GLY A CA   
1147 C  C    . GLY A 139 ? 0.1202 0.0350 0.1869 -0.0301 0.0043  -0.0062 140 GLY A C    
1148 O  O    . GLY A 139 ? 0.1370 0.0303 0.1888 0.0200  0.0019  -0.0148 140 GLY A O    
1149 N  N    . LEU A 140 ? 0.0861 0.0270 0.1791 -0.0100 0.0152  -0.0019 141 LEU A N    
1150 C  CA   . LEU A 140 ? 0.0925 0.0342 0.1728 -0.0226 0.0329  -0.0239 141 LEU A CA   
1151 C  C    . LEU A 140 ? 0.1167 0.0474 0.1437 -0.0022 0.0173  -0.0182 141 LEU A C    
1152 O  O    . LEU A 140 ? 0.1329 0.0306 0.1570 -0.0148 0.0225  -0.0119 141 LEU A O    
1153 C  CB   . LEU A 140 ? 0.0913 0.0493 0.1922 -0.0009 0.0421  -0.0163 141 LEU A CB   
1154 C  CG   . LEU A 140 ? 0.0661 0.0619 0.1932 -0.0006 0.0175  0.0023  141 LEU A CG   
1155 C  CD1  . LEU A 140 ? 0.0867 0.0610 0.2200 0.0023  0.0352  -0.0304 141 LEU A CD1  
1156 C  CD2  . LEU A 140 ? 0.1366 0.0547 0.2199 0.0195  -0.0183 0.0074  141 LEU A CD2  
1157 N  N    . ALA A 141 ? 0.0960 0.0338 0.1784 -0.0167 0.0145  -0.0294 142 ALA A N    
1158 C  CA   . ALA A 141 ? 0.0713 0.0304 0.1916 -0.0149 0.0170  -0.0124 142 ALA A CA   
1159 C  C    . ALA A 141 ? 0.0948 0.0357 0.1555 -0.0096 -0.0087 -0.0046 142 ALA A C    
1160 O  O    . ALA A 141 ? 0.1214 0.0309 0.1839 -0.0116 -0.0070 0.0086  142 ALA A O    
1161 C  CB   . ALA A 141 ? 0.0904 0.0492 0.2006 -0.0200 0.0292  -0.0087 142 ALA A CB   
1162 N  N    . VAL A 142 ? 0.1079 0.0255 0.1724 0.0029  0.0062  -0.0005 143 VAL A N    
1163 C  CA   . VAL A 142 ? 0.1035 0.0262 0.1750 0.0068  0.0155  -0.0059 143 VAL A CA   
1164 C  C    . VAL A 142 ? 0.0855 0.0330 0.1614 -0.0024 0.0228  0.0095  143 VAL A C    
1165 O  O    . VAL A 142 ? 0.0810 0.0396 0.1662 -0.0037 -0.0043 0.0076  143 VAL A O    
1166 C  CB   . VAL A 142 ? 0.0786 0.0550 0.1661 0.0044  0.0004  -0.0168 143 VAL A CB   
1167 C  CG1  . VAL A 142 ? 0.1521 0.0664 0.1655 0.0189  -0.0163 -0.0376 143 VAL A CG1  
1168 C  CG2  . VAL A 142 ? 0.1053 0.1125 0.1809 -0.0306 0.0202  0.0105  143 VAL A CG2  
1169 N  N    . LEU A 143 ? 0.0737 0.0275 0.1788 -0.0037 0.0004  0.0091  144 LEU A N    
1170 C  CA   . LEU A 143 ? 0.0854 0.0362 0.1869 -0.0068 -0.0008 -0.0130 144 LEU A CA   
1171 C  C    . LEU A 143 ? 0.0966 0.0477 0.1507 -0.0318 0.0010  -0.0134 144 LEU A C    
1172 O  O    . LEU A 143 ? 0.1281 0.0303 0.1688 -0.0145 0.0089  -0.0004 144 LEU A O    
1173 C  CB   . LEU A 143 ? 0.1030 0.0620 0.2002 -0.0159 -0.0060 0.0091  144 LEU A CB   
1174 C  CG   . LEU A 143 ? 0.1075 0.0648 0.2148 -0.0155 0.0083  -0.0135 144 LEU A CG   
1175 C  CD1  . LEU A 143 ? 0.1087 0.1389 0.2110 -0.0278 -0.0044 0.0190  144 LEU A CD1  
1176 C  CD2  . LEU A 143 ? 0.1137 0.1301 0.2513 0.0181  -0.0404 0.0224  144 LEU A CD2  
1177 N  N    . GLY A 144 ? 0.0817 0.0254 0.1718 0.0023  0.0077  0.0033  145 GLY A N    
1178 C  CA   . GLY A 144 ? 0.0854 0.0306 0.1646 -0.0162 0.0194  0.0055  145 GLY A CA   
1179 C  C    . GLY A 144 ? 0.0579 0.0546 0.1560 -0.0009 0.0066  0.0106  145 GLY A C    
1180 O  O    . GLY A 144 ? 0.1014 0.0358 0.1793 -0.0047 0.0288  -0.0049 145 GLY A O    
1181 N  N    . ILE A 145 ? 0.0949 0.0254 0.1657 0.0027  0.0050  -0.0006 146 ILE A N    
1182 C  CA   . ILE A 145 ? 0.0679 0.0423 0.1798 0.0117  -0.0034 0.0117  146 ILE A CA   
1183 C  C    . ILE A 145 ? 0.0813 0.0408 0.1644 0.0028  0.0119  0.0071  146 ILE A C    
1184 O  O    . ILE A 145 ? 0.1025 0.0359 0.1769 -0.0043 0.0066  -0.0048 146 ILE A O    
1185 C  CB   . ILE A 145 ? 0.0991 0.0267 0.1853 0.0092  0.0027  0.0061  146 ILE A CB   
1186 C  CG1  . ILE A 145 ? 0.1260 0.0357 0.2290 0.0277  0.0127  0.0023  146 ILE A CG1  
1187 C  CG2  . ILE A 145 ? 0.1096 0.0384 0.2377 -0.0222 -0.0141 -0.0127 146 ILE A CG2  
1188 C  CD1  . ILE A 145 ? 0.1298 0.0451 0.2206 0.0337  0.0021  -0.0009 146 ILE A CD1  
1189 N  N    . PHE A 146 ? 0.0813 0.0255 0.1722 -0.0035 -0.0055 -0.0019 147 PHE A N    
1190 C  CA   . PHE A 146 ? 0.1092 0.0259 0.1620 0.0048  0.0000  -0.0073 147 PHE A CA   
1191 C  C    . PHE A 146 ? 0.0829 0.0331 0.1708 -0.0064 0.0049  -0.0025 147 PHE A C    
1192 O  O    . PHE A 146 ? 0.0701 0.0609 0.2030 0.0024  0.0035  -0.0133 147 PHE A O    
1193 C  CB   . PHE A 146 ? 0.0984 0.0394 0.1697 -0.0217 -0.0069 0.0045  147 PHE A CB   
1194 C  CG   . PHE A 146 ? 0.0861 0.0303 0.1463 0.0076  0.0041  0.0008  147 PHE A CG   
1195 C  CD1  . PHE A 146 ? 0.0773 0.0297 0.2077 0.0053  0.0241  -0.0188 147 PHE A CD1  
1196 C  CD2  . PHE A 146 ? 0.1134 0.0296 0.1688 -0.0035 -0.0031 0.0190  147 PHE A CD2  
1197 C  CE1  . PHE A 146 ? 0.1057 0.0512 0.1666 -0.0034 0.0017  -0.0166 147 PHE A CE1  
1198 C  CE2  . PHE A 146 ? 0.0933 0.0410 0.1902 -0.0323 -0.0054 0.0092  147 PHE A CE2  
1199 C  CZ   . PHE A 146 ? 0.0740 0.0377 0.1661 -0.0154 -0.0100 0.0164  147 PHE A CZ   
1200 N  N    . LEU A 147 ? 0.1140 0.0342 0.1569 0.0011  0.0134  -0.0155 148 LEU A N    
1201 C  CA   . LEU A 147 ? 0.1035 0.0260 0.1743 0.0017  -0.0074 -0.0099 148 LEU A CA   
1202 C  C    . LEU A 147 ? 0.0745 0.0415 0.1676 0.0071  0.0043  0.0019  148 LEU A C    
1203 O  O    . LEU A 147 ? 0.0729 0.0445 0.2165 0.0032  0.0098  -0.0042 148 LEU A O    
1204 C  CB   . LEU A 147 ? 0.0999 0.0381 0.1629 0.0024  -0.0033 -0.0079 148 LEU A CB   
1205 C  CG   . LEU A 147 ? 0.1291 0.0343 0.1783 -0.0076 -0.0040 0.0003  148 LEU A CG   
1206 C  CD1  . LEU A 147 ? 0.2051 0.0330 0.1951 -0.0269 -0.0110 -0.0198 148 LEU A CD1  
1207 C  CD2  . LEU A 147 ? 0.1305 0.0879 0.1956 -0.0142 -0.0057 -0.0045 148 LEU A CD2  
1208 N  N    . LYS A 148 ? 0.1347 0.0297 0.2023 -0.0100 0.0008  -0.0102 149 LYS A N    
1209 C  CA   . LYS A 148 ? 0.1552 0.0481 0.2028 -0.0006 -0.0172 -0.0185 149 LYS A CA   
1210 C  C    . LYS A 148 ? 0.1314 0.0611 0.2108 0.0006  -0.0229 -0.0223 149 LYS A C    
1211 O  O    . LYS A 148 ? 0.1333 0.0798 0.2225 0.0272  -0.0405 -0.0194 149 LYS A O    
1212 C  CB   . LYS A 148 ? 0.1592 0.0638 0.2261 0.0027  -0.0047 0.0133  149 LYS A CB   
1213 C  CG   . LYS A 148 ? 0.1892 0.0814 0.2515 0.0095  0.0240  0.0111  149 LYS A CG   
1214 C  CD   . LYS A 148 ? 0.2884 0.1983 0.2997 -0.0006 0.0244  0.0659  149 LYS A CD   
1215 C  CE   . LYS A 148 ? 0.3475 0.3067 0.3535 -0.0061 0.0578  0.0515  149 LYS A CE   
1216 N  NZ   . LYS A 148 ? 0.4329 0.4119 0.3971 -0.0801 0.0525  0.0544  149 LYS A NZ   
1217 N  N    . VAL A 149 ? 0.1650 0.0342 0.2337 -0.0254 -0.0229 -0.0254 150 VAL A N    
1218 C  CA   . VAL A 149 ? 0.1736 0.0514 0.2411 -0.0218 -0.0301 -0.0267 150 VAL A CA   
1219 C  C    . VAL A 149 ? 0.1793 0.0827 0.2598 -0.0106 -0.0237 -0.0156 150 VAL A C    
1220 O  O    . VAL A 149 ? 0.2198 0.0848 0.2584 -0.0203 -0.0415 -0.0031 150 VAL A O    
1221 C  CB   . VAL A 149 ? 0.1690 0.0425 0.2450 -0.0086 -0.0163 -0.0116 150 VAL A CB   
1222 C  CG1  . VAL A 149 ? 0.1751 0.1012 0.2608 -0.0135 -0.0136 -0.0384 150 VAL A CG1  
1223 C  CG2  . VAL A 149 ? 0.1737 0.1117 0.2773 -0.0430 0.0014  -0.0154 150 VAL A CG2  
1224 N  N    . GLY A 150 ? 0.1549 0.0489 0.2484 -0.0068 -0.0275 -0.0341 151 GLY A N    
1225 C  CA   . GLY A 150 ? 0.1563 0.0969 0.2460 -0.0417 -0.0284 0.0059  151 GLY A CA   
1226 C  C    . GLY A 150 ? 0.1268 0.0789 0.2297 -0.0441 -0.0078 -0.0128 151 GLY A C    
1227 O  O    . GLY A 150 ? 0.1717 0.0797 0.2537 -0.0357 0.0006  -0.0136 151 GLY A O    
1228 N  N    A SER A 151 ? 0.1580 0.0859 0.2659 -0.0275 -0.0248 -0.0083 152 SER A N    
1229 N  N    B SER A 151 ? 0.1641 0.0910 0.2660 -0.0268 -0.0223 -0.0049 152 SER A N    
1230 C  CA   A SER A 151 ? 0.1556 0.0799 0.2586 -0.0193 -0.0282 -0.0118 152 SER A CA   
1231 C  CA   B SER A 151 ? 0.1691 0.0956 0.2579 -0.0236 -0.0195 0.0026  152 SER A CA   
1232 C  C    A SER A 151 ? 0.1740 0.0689 0.2450 -0.0182 -0.0292 -0.0267 152 SER A C    
1233 C  C    B SER A 151 ? 0.1816 0.0909 0.2419 -0.0188 -0.0216 -0.0144 152 SER A C    
1234 O  O    A SER A 151 ? 0.0965 0.0326 0.2385 0.0084  -0.0265 -0.0389 152 SER A O    
1235 O  O    B SER A 151 ? 0.2006 0.1175 0.2094 -0.0192 -0.0159 -0.0206 152 SER A O    
1236 C  CB   A SER A 151 ? 0.1919 0.1268 0.2923 -0.0378 -0.0105 -0.0116 152 SER A CB   
1237 C  CB   B SER A 151 ? 0.1949 0.1228 0.2826 -0.0410 -0.0036 -0.0048 152 SER A CB   
1238 O  OG   A SER A 151 ? 0.2065 0.2041 0.2865 -0.0014 -0.0196 -0.0311 152 SER A OG   
1239 O  OG   B SER A 151 ? 0.1448 0.1267 0.3669 -0.0327 0.0070  0.0343  152 SER A OG   
1240 N  N    . ALA A 152 ? 0.1947 0.0806 0.2359 -0.0200 -0.0264 -0.0123 153 ALA A N    
1241 C  CA   . ALA A 152 ? 0.1989 0.0755 0.2362 -0.0317 -0.0263 -0.0195 153 ALA A CA   
1242 C  C    . ALA A 152 ? 0.1604 0.0990 0.2470 -0.0249 -0.0328 -0.0196 153 ALA A C    
1243 O  O    . ALA A 152 ? 0.1830 0.0710 0.3224 -0.0077 -0.0233 -0.0099 153 ALA A O    
1244 C  CB   . ALA A 152 ? 0.2301 0.1196 0.2375 -0.0028 -0.0375 -0.0145 153 ALA A CB   
1245 N  N    . LYS A 153 ? 0.1903 0.0591 0.2511 -0.0089 -0.0299 -0.0150 154 LYS A N    
1246 C  CA   . LYS A 153 ? 0.2018 0.0924 0.2392 -0.0036 -0.0428 -0.0091 154 LYS A CA   
1247 C  C    . LYS A 153 ? 0.1548 0.1049 0.2505 0.0045  -0.0433 -0.0095 154 LYS A C    
1248 O  O    . LYS A 153 ? 0.1637 0.0923 0.2401 -0.0144 -0.0457 -0.0234 154 LYS A O    
1249 C  CB   . LYS A 153 ? 0.1605 0.1077 0.2429 0.0121  -0.0545 -0.0256 154 LYS A CB   
1250 C  CG   . LYS A 153 ? 0.2591 0.0932 0.2659 -0.0087 -0.0373 -0.0437 154 LYS A CG   
1251 C  CD   . LYS A 153 ? 0.3222 0.1029 0.2503 0.0003  -0.0185 -0.0347 154 LYS A CD   
1252 C  CE   . LYS A 153 ? 0.3396 0.1691 0.2915 0.0304  -0.0130 -0.0271 154 LYS A CE   
1253 N  NZ   . LYS A 153 ? 0.3896 0.2366 0.3372 -0.0377 -0.0021 -0.0063 154 LYS A NZ   
1254 N  N    . PRO A 154 ? 0.1506 0.1440 0.2664 -0.0033 -0.0367 -0.0038 155 PRO A N    
1255 C  CA   . PRO A 154 ? 0.1458 0.1523 0.2805 -0.0130 -0.0393 0.0171  155 PRO A CA   
1256 C  C    . PRO A 154 ? 0.1550 0.1460 0.2692 0.0095  -0.0545 0.0016  155 PRO A C    
1257 O  O    . PRO A 154 ? 0.1901 0.1524 0.2879 0.0058  -0.0472 0.0158  155 PRO A O    
1258 C  CB   . PRO A 154 ? 0.1455 0.1738 0.3310 -0.0050 -0.0340 0.0151  155 PRO A CB   
1259 C  CG   . PRO A 154 ? 0.2003 0.2525 0.3229 -0.0028 -0.0288 0.0485  155 PRO A CG   
1260 C  CD   . PRO A 154 ? 0.1490 0.1810 0.2796 0.0074  -0.0146 0.0130  155 PRO A CD   
1261 N  N    . GLY A 155 ? 0.1628 0.0851 0.2810 0.0124  -0.0514 -0.0184 156 GLY A N    
1262 C  CA   . GLY A 155 ? 0.1833 0.1116 0.2828 -0.0121 -0.0298 0.0089  156 GLY A CA   
1263 C  C    . GLY A 155 ? 0.1851 0.0815 0.2787 -0.0280 -0.0342 0.0132  156 GLY A C    
1264 O  O    . GLY A 155 ? 0.2414 0.0905 0.3510 -0.0086 -0.0314 0.0248  156 GLY A O    
1265 N  N    . LEU A 156 ? 0.1673 0.0924 0.2665 -0.0121 -0.0416 -0.0045 157 LEU A N    
1266 C  CA   . LEU A 156 ? 0.1608 0.0658 0.2216 -0.0162 -0.0531 -0.0078 157 LEU A CA   
1267 C  C    . LEU A 156 ? 0.1748 0.0779 0.2284 -0.0170 -0.0577 0.0024  157 LEU A C    
1268 O  O    . LEU A 156 ? 0.1912 0.0753 0.2328 -0.0299 -0.0528 0.0041  157 LEU A O    
1269 C  CB   . LEU A 156 ? 0.1683 0.0982 0.2274 -0.0169 -0.0509 -0.0041 157 LEU A CB   
1270 C  CG   . LEU A 156 ? 0.1268 0.0918 0.2234 -0.0346 -0.0301 0.0019  157 LEU A CG   
1271 C  CD1  . LEU A 156 ? 0.1827 0.1311 0.2590 -0.0433 -0.0278 -0.0047 157 LEU A CD1  
1272 C  CD2  . LEU A 156 ? 0.1567 0.0955 0.2562 -0.0027 -0.0484 -0.0036 157 LEU A CD2  
1273 N  N    . GLN A 157 ? 0.1779 0.0795 0.2243 -0.0352 -0.0644 -0.0147 158 GLN A N    
1274 C  CA   . GLN A 157 ? 0.2079 0.1194 0.2396 -0.0321 -0.0384 -0.0242 158 GLN A CA   
1275 C  C    . GLN A 157 ? 0.2041 0.1138 0.2149 -0.0084 -0.0531 -0.0232 158 GLN A C    
1276 O  O    . GLN A 157 ? 0.2532 0.0824 0.2313 -0.0195 -0.0436 -0.0163 158 GLN A O    
1277 C  CB   . GLN A 157 ? 0.2481 0.0987 0.2403 -0.0400 -0.0363 -0.0302 158 GLN A CB   
1278 C  CG   . GLN A 157 ? 0.2704 0.1021 0.2472 -0.0234 -0.0244 -0.0469 158 GLN A CG   
1279 C  CD   . GLN A 157 ? 0.2433 0.0865 0.2094 -0.0366 -0.0063 -0.0278 158 GLN A CD   
1280 O  OE1  . GLN A 157 ? 0.3086 0.1038 0.2254 -0.0437 -0.0382 -0.0195 158 GLN A OE1  
1281 N  NE2  . GLN A 157 ? 0.3119 0.1625 0.2457 -0.0871 -0.0112 -0.0426 158 GLN A NE2  
1282 N  N    . LYS A 158 ? 0.2061 0.1232 0.2550 -0.0222 -0.0572 -0.0217 159 LYS A N    
1283 C  CA   . LYS A 158 ? 0.1778 0.1221 0.2456 -0.0090 -0.0357 -0.0160 159 LYS A CA   
1284 C  C    . LYS A 158 ? 0.1956 0.0886 0.2199 0.0064  -0.0318 -0.0066 159 LYS A C    
1285 O  O    . LYS A 158 ? 0.2068 0.1367 0.2284 -0.0489 -0.0413 0.0039  159 LYS A O    
1286 C  CB   . LYS A 158 ? 0.2447 0.1459 0.2676 0.0042  -0.0399 -0.0178 159 LYS A CB   
1287 C  CG   . LYS A 158 ? 0.3253 0.2141 0.3329 -0.0178 -0.0388 -0.0034 159 LYS A CG   
1288 C  CD   . LYS A 158 ? 0.4163 0.3512 0.4549 -0.0341 -0.0245 0.0165  159 LYS A CD   
1289 C  CE   . LYS A 158 ? 0.4330 0.3989 0.4667 0.0021  -0.0286 0.0086  159 LYS A CE   
1290 N  NZ   . LYS A 158 ? 0.3737 0.3173 0.3979 -0.0017 -0.0680 0.0236  159 LYS A NZ   
1291 N  N    . VAL A 159 ? 0.2016 0.0733 0.2158 -0.0043 -0.0489 -0.0148 160 VAL A N    
1292 C  CA   . VAL A 159 ? 0.1838 0.0671 0.2074 -0.0244 -0.0366 -0.0139 160 VAL A CA   
1293 C  C    . VAL A 159 ? 0.1967 0.1025 0.2176 -0.0196 -0.0239 -0.0173 160 VAL A C    
1294 O  O    . VAL A 159 ? 0.2203 0.0943 0.2377 -0.0295 -0.0119 -0.0101 160 VAL A O    
1295 C  CB   . VAL A 159 ? 0.2071 0.0882 0.2030 -0.0119 -0.0333 -0.0102 160 VAL A CB   
1296 C  CG1  . VAL A 159 ? 0.1711 0.1288 0.2127 -0.0366 -0.0179 -0.0050 160 VAL A CG1  
1297 C  CG2  . VAL A 159 ? 0.2446 0.0961 0.2137 0.0340  -0.0199 -0.0342 160 VAL A CG2  
1298 N  N    . VAL A 160 ? 0.2174 0.0815 0.2192 -0.0192 -0.0256 -0.0146 161 VAL A N    
1299 C  CA   . VAL A 160 ? 0.2504 0.1315 0.2483 -0.0183 -0.0050 -0.0131 161 VAL A CA   
1300 C  C    . VAL A 160 ? 0.2530 0.1096 0.2464 -0.0284 -0.0077 -0.0317 161 VAL A C    
1301 O  O    . VAL A 160 ? 0.2645 0.0906 0.2445 -0.0338 0.0031  -0.0365 161 VAL A O    
1302 C  CB   . VAL A 160 ? 0.2931 0.1037 0.2362 -0.0013 0.0168  -0.0300 161 VAL A CB   
1303 C  CG1  . VAL A 160 ? 0.3044 0.1503 0.2836 -0.0385 -0.0104 -0.0393 161 VAL A CG1  
1304 C  CG2  . VAL A 160 ? 0.3069 0.1304 0.2690 -0.0033 0.0053  0.0027  161 VAL A CG2  
1305 N  N    . ASP A 161 ? 0.2997 0.1169 0.2176 -0.0549 -0.0278 -0.0338 162 ASP A N    
1306 C  CA   . ASP A 161 ? 0.3210 0.1909 0.2519 -0.0492 -0.0201 -0.0110 162 ASP A CA   
1307 C  C    . ASP A 161 ? 0.3193 0.1956 0.2110 -0.0615 -0.0213 -0.0049 162 ASP A C    
1308 O  O    . ASP A 161 ? 0.3895 0.2495 0.2615 -0.0788 -0.0245 -0.0166 162 ASP A O    
1309 C  CB   . ASP A 161 ? 0.3290 0.2169 0.2502 -0.0353 -0.0247 -0.0096 162 ASP A CB   
1310 C  CG   . ASP A 161 ? 0.3070 0.2119 0.3027 -0.0216 0.0061  -0.0216 162 ASP A CG   
1311 O  OD1  . ASP A 161 ? 0.3576 0.2149 0.3773 -0.0600 -0.0313 -0.0298 162 ASP A OD1  
1312 O  OD2  . ASP A 161 ? 0.3508 0.2538 0.3316 -0.0374 -0.0456 -0.0171 162 ASP A OD2  
1313 N  N    . VAL A 162 ? 0.2777 0.1213 0.2168 -0.0392 -0.0389 -0.0017 163 VAL A N    
1314 C  CA   . VAL A 162 ? 0.2870 0.1699 0.2312 -0.0438 -0.0218 0.0062  163 VAL A CA   
1315 C  C    . VAL A 162 ? 0.2621 0.1280 0.2044 -0.0353 -0.0096 0.0008  163 VAL A C    
1316 O  O    . VAL A 162 ? 0.2906 0.1713 0.2021 -0.0383 0.0083  0.0021  163 VAL A O    
1317 C  CB   . VAL A 162 ? 0.3161 0.1479 0.2725 -0.0357 -0.0162 0.0213  163 VAL A CB   
1318 C  CG1  . VAL A 162 ? 0.3560 0.1164 0.2591 -0.0220 -0.0029 -0.0166 163 VAL A CG1  
1319 C  CG2  . VAL A 162 ? 0.3496 0.2175 0.2887 -0.0137 0.0059  0.0334  163 VAL A CG2  
1320 N  N    . LEU A 163 ? 0.2568 0.1374 0.2116 -0.0390 -0.0296 -0.0089 164 LEU A N    
1321 C  CA   . LEU A 163 ? 0.2626 0.1294 0.1863 -0.0275 0.0052  -0.0008 164 LEU A CA   
1322 C  C    . LEU A 163 ? 0.2978 0.1368 0.2040 -0.0239 0.0009  -0.0091 164 LEU A C    
1323 O  O    . LEU A 163 ? 0.3082 0.1373 0.2303 -0.0378 0.0325  0.0086  164 LEU A O    
1324 C  CB   . LEU A 163 ? 0.2353 0.0958 0.1837 -0.0042 0.0047  -0.0131 164 LEU A CB   
1325 C  CG   . LEU A 163 ? 0.2911 0.0991 0.1565 -0.0380 0.0107  -0.0063 164 LEU A CG   
1326 C  CD1  . LEU A 163 ? 0.2662 0.1266 0.2408 -0.0158 0.0002  0.0743  164 LEU A CD1  
1327 C  CD2  . LEU A 163 ? 0.2356 0.1388 0.1979 -0.0481 -0.0186 -0.0309 164 LEU A CD2  
1328 N  N    . ASP A 164 ? 0.3536 0.1686 0.2235 -0.0514 0.0191  -0.0268 165 ASP A N    
1329 C  CA   . ASP A 164 ? 0.3683 0.2202 0.2513 -0.0401 0.0213  -0.0346 165 ASP A CA   
1330 C  C    . ASP A 164 ? 0.3648 0.2456 0.2426 -0.0250 0.0277  -0.0049 165 ASP A C    
1331 O  O    . ASP A 164 ? 0.4034 0.2611 0.2750 -0.0113 0.0473  -0.0040 165 ASP A O    
1332 C  CB   . ASP A 164 ? 0.4030 0.2565 0.2611 -0.0502 0.0137  -0.0391 165 ASP A CB   
1333 C  CG   . ASP A 164 ? 0.3989 0.2883 0.3292 -0.0524 -0.0027 -0.0378 165 ASP A CG   
1334 O  OD1  . ASP A 164 ? 0.4735 0.3087 0.3909 -0.0557 0.0169  -0.0191 165 ASP A OD1  
1335 O  OD2  . ASP A 164 ? 0.5455 0.4489 0.3555 -0.0301 0.0294  -0.0408 165 ASP A OD2  
1336 N  N    . SER A 165 ? 0.3275 0.2162 0.2156 -0.0205 -0.0008 0.0204  166 SER A N    
1337 C  CA   . SER A 165 ? 0.3117 0.2118 0.2248 -0.0257 -0.0011 0.0113  166 SER A CA   
1338 C  C    . SER A 165 ? 0.2911 0.1716 0.1915 -0.0384 0.0118  0.0156  166 SER A C    
1339 O  O    . SER A 165 ? 0.3313 0.1561 0.2300 -0.0405 0.0110  0.0321  166 SER A O    
1340 C  CB   . SER A 165 ? 0.3689 0.2420 0.2661 -0.0126 0.0197  0.0259  166 SER A CB   
1341 O  OG   . SER A 165 ? 0.3729 0.2314 0.2867 0.0163  0.0036  0.0165  166 SER A OG   
1342 N  N    . ILE A 166 ? 0.2610 0.1655 0.1850 -0.0216 -0.0170 0.0064  167 ILE A N    
1343 C  CA   . ILE A 166 ? 0.2447 0.1117 0.2013 -0.0180 0.0086  -0.0012 167 ILE A CA   
1344 C  C    . ILE A 166 ? 0.2246 0.1261 0.1850 -0.0130 0.0132  -0.0130 167 ILE A C    
1345 O  O    . ILE A 166 ? 0.2260 0.1307 0.1948 -0.0255 0.0255  0.0007  167 ILE A O    
1346 C  CB   . ILE A 166 ? 0.2471 0.1279 0.1870 -0.0276 0.0123  -0.0003 167 ILE A CB   
1347 C  CG1  . ILE A 166 ? 0.1873 0.1295 0.1771 -0.0370 0.0250  -0.0118 167 ILE A CG1  
1348 C  CG2  . ILE A 166 ? 0.2669 0.1403 0.2318 -0.0089 -0.0010 0.0084  167 ILE A CG2  
1349 C  CD1  . ILE A 166 ? 0.2197 0.1372 0.1968 -0.0131 0.0418  0.0033  167 ILE A CD1  
1350 N  N    . LYS A 167 ? 0.2474 0.1352 0.2094 -0.0052 0.0186  -0.0080 168 LYS A N    
1351 C  CA   . LYS A 167 ? 0.2455 0.1332 0.1958 0.0003  -0.0057 -0.0219 168 LYS A CA   
1352 C  C    . LYS A 167 ? 0.2323 0.1492 0.1844 -0.0066 0.0305  -0.0168 168 LYS A C    
1353 O  O    . LYS A 167 ? 0.2535 0.1379 0.1992 -0.0209 0.0016  0.0046  168 LYS A O    
1354 C  CB   . LYS A 167 ? 0.3022 0.1396 0.2019 0.0078  0.0000  -0.0237 168 LYS A CB   
1355 C  CG   . LYS A 167 ? 0.2878 0.1903 0.2316 0.0361  0.0028  -0.0137 168 LYS A CG   
1356 C  CD   . LYS A 167 ? 0.3699 0.2514 0.2789 0.0161  -0.0289 -0.0549 168 LYS A CD   
1357 C  CE   . LYS A 167 ? 0.3922 0.2904 0.3667 0.0157  -0.0151 -0.0232 168 LYS A CE   
1358 N  NZ   . LYS A 167 ? 0.4091 0.4352 0.3931 0.0136  -0.0019 -0.0345 168 LYS A NZ   
1359 N  N    . THR A 168 ? 0.2277 0.1407 0.1962 -0.0180 0.0326  0.0097  169 THR A N    
1360 C  CA   . THR A 168 ? 0.2248 0.1578 0.1994 -0.0038 0.0427  0.0037  169 THR A CA   
1361 C  C    . THR A 168 ? 0.1882 0.1342 0.1908 -0.0041 0.0485  0.0103  169 THR A C    
1362 O  O    . THR A 168 ? 0.2092 0.1498 0.2199 -0.0223 0.0364  0.0214  169 THR A O    
1363 C  CB   . THR A 168 ? 0.2587 0.1456 0.2227 -0.0134 0.0349  0.0131  169 THR A CB   
1364 O  OG1  . THR A 168 ? 0.3264 0.1721 0.2038 -0.0055 0.0355  0.0161  169 THR A OG1  
1365 C  CG2  . THR A 168 ? 0.2994 0.1597 0.2307 0.0261  0.0489  -0.0274 169 THR A CG2  
1366 N  N    . LYS A 169 ? 0.2601 0.1843 0.2022 -0.0449 0.0484  -0.0076 170 LYS A N    
1367 C  CA   . LYS A 169 ? 0.2608 0.1482 0.2135 -0.0322 0.0303  0.0161  170 LYS A CA   
1368 C  C    . LYS A 169 ? 0.2217 0.1583 0.2230 -0.0301 0.0349  0.0261  170 LYS A C    
1369 O  O    . LYS A 169 ? 0.2729 0.2246 0.2479 -0.0531 0.0518  0.0305  170 LYS A O    
1370 C  CB   . LYS A 169 ? 0.2591 0.1953 0.2172 -0.0254 0.0423  0.0015  170 LYS A CB   
1371 C  CG   . LYS A 169 ? 0.2757 0.1852 0.2433 -0.0227 0.0107  -0.0013 170 LYS A CG   
1372 C  CD   . LYS A 169 ? 0.3038 0.2467 0.3106 -0.0143 0.0029  -0.0042 170 LYS A CD   
1373 C  CE   . LYS A 169 ? 0.3409 0.3747 0.4172 -0.0383 -0.0434 -0.0217 170 LYS A CE   
1374 N  NZ   . LYS A 169 ? 0.3804 0.4931 0.4963 0.0154  -0.0437 -0.0136 170 LYS A NZ   
1375 N  N    . GLY A 170 ? 0.2691 0.1458 0.2378 -0.0360 0.0302  0.0236  171 GLY A N    
1376 C  CA   . GLY A 170 ? 0.2565 0.1343 0.2857 -0.0410 0.0094  0.0530  171 GLY A CA   
1377 C  C    . GLY A 170 ? 0.2766 0.1616 0.2921 -0.0276 0.0117  0.0377  171 GLY A C    
1378 O  O    . GLY A 170 ? 0.3199 0.1508 0.3547 -0.0513 0.0035  0.0559  171 GLY A O    
1379 N  N    . LYS A 171 ? 0.2856 0.1476 0.2367 -0.0581 0.0313  0.0447  172 LYS A N    
1380 C  CA   . LYS A 171 ? 0.2700 0.1403 0.2247 -0.0254 0.0338  0.0085  172 LYS A CA   
1381 C  C    . LYS A 171 ? 0.2746 0.1214 0.2026 -0.0101 0.0277  0.0234  172 LYS A C    
1382 O  O    . LYS A 171 ? 0.2891 0.1218 0.2080 -0.0165 0.0327  0.0274  172 LYS A O    
1383 C  CB   . LYS A 171 ? 0.2920 0.1766 0.2357 -0.0443 0.0083  0.0016  172 LYS A CB   
1384 C  CG   . LYS A 171 ? 0.2673 0.2192 0.3017 -0.0183 0.0211  -0.0553 172 LYS A CG   
1385 C  CD   . LYS A 171 ? 0.3589 0.2889 0.3411 -0.0655 -0.0046 -0.0104 172 LYS A CD   
1386 C  CE   . LYS A 171 ? 0.4453 0.3913 0.3587 -0.0194 -0.0282 -0.0047 172 LYS A CE   
1387 N  NZ   . LYS A 171 ? 0.4774 0.3668 0.3652 -0.0472 0.0463  -0.0039 172 LYS A NZ   
1388 N  N    . SER A 172 ? 0.2902 0.1649 0.1939 0.0067  0.0289  0.0275  173 SER A N    
1389 C  CA   . SER A 172 ? 0.3040 0.1647 0.1939 0.0093  0.0289  0.0098  173 SER A CA   
1390 C  C    . SER A 172 ? 0.3010 0.1446 0.1887 0.0391  0.0264  0.0209  173 SER A C    
1391 O  O    . SER A 172 ? 0.3532 0.2260 0.1754 0.0569  0.0098  0.0146  173 SER A O    
1392 C  CB   . SER A 172 ? 0.3121 0.1625 0.1998 -0.0106 0.0360  0.0279  173 SER A CB   
1393 O  OG   . SER A 172 ? 0.4065 0.1547 0.2461 -0.0101 0.0417  0.0561  173 SER A OG   
1394 N  N    . ALA A 173 ? 0.3058 0.1917 0.1922 0.0419  0.0082  0.0080  174 ALA A N    
1395 C  CA   . ALA A 173 ? 0.3048 0.1910 0.1972 0.0654  -0.0060 0.0142  174 ALA A CA   
1396 C  C    . ALA A 173 ? 0.3036 0.2143 0.1994 0.0665  -0.0123 0.0241  174 ALA A C    
1397 O  O    . ALA A 173 ? 0.3076 0.1715 0.1708 0.0855  -0.0170 0.0310  174 ALA A O    
1398 C  CB   . ALA A 173 ? 0.3258 0.1972 0.2158 0.0562  -0.0084 0.0011  174 ALA A CB   
1399 N  N    . ASP A 174 ? 0.3097 0.2316 0.2209 0.0763  -0.0178 0.0422  175 ASP A N    
1400 C  CA   . ASP A 174 ? 0.3135 0.2429 0.2411 0.0575  -0.0078 0.0380  175 ASP A CA   
1401 C  C    . ASP A 174 ? 0.3101 0.2124 0.2390 0.0553  -0.0177 0.0293  175 ASP A C    
1402 O  O    . ASP A 174 ? 0.3546 0.2201 0.2368 0.0591  -0.0229 -0.0106 175 ASP A O    
1403 C  CB   . ASP A 174 ? 0.2926 0.2965 0.2808 0.0595  -0.0067 0.0414  175 ASP A CB   
1404 C  CG   . ASP A 174 ? 0.4217 0.3798 0.3867 0.0138  -0.0132 0.0242  175 ASP A CG   
1405 O  OD1  . ASP A 174 ? 0.4343 0.4426 0.4440 -0.0058 -0.0557 0.0107  175 ASP A OD1  
1406 O  OD2  . ASP A 174 ? 0.4248 0.4789 0.3732 0.0114  0.0029  0.0296  175 ASP A OD2  
1407 N  N    . PHE A 175 ? 0.2813 0.1716 0.2074 0.0371  0.0011  0.0193  176 PHE A N    
1408 C  CA   . PHE A 175 ? 0.2646 0.1407 0.1977 0.0342  -0.0219 0.0130  176 PHE A CA   
1409 C  C    . PHE A 175 ? 0.2836 0.1243 0.2092 0.0085  -0.0278 0.0008  176 PHE A C    
1410 O  O    . PHE A 175 ? 0.3085 0.1785 0.2218 0.0782  -0.0455 -0.0140 176 PHE A O    
1411 C  CB   . PHE A 175 ? 0.2652 0.1049 0.1760 -0.0044 -0.0298 0.0268  176 PHE A CB   
1412 C  CG   . PHE A 175 ? 0.2464 0.0918 0.2051 0.0130  -0.0333 -0.0057 176 PHE A CG   
1413 C  CD1  . PHE A 175 ? 0.2486 0.1214 0.2302 -0.0052 -0.0135 -0.0157 176 PHE A CD1  
1414 C  CD2  . PHE A 175 ? 0.2277 0.1269 0.2072 -0.0013 -0.0333 0.0213  176 PHE A CD2  
1415 C  CE1  . PHE A 175 ? 0.3152 0.1149 0.2072 0.0067  -0.0139 -0.0045 176 PHE A CE1  
1416 C  CE2  . PHE A 175 ? 0.2876 0.1105 0.2364 0.0131  -0.0403 0.0075  176 PHE A CE2  
1417 C  CZ   . PHE A 175 ? 0.2450 0.1298 0.1988 0.0168  -0.0411 -0.0007 176 PHE A CZ   
1418 N  N    . THR A 176 ? 0.2765 0.1064 0.2220 0.0247  -0.0399 0.0147  177 THR A N    
1419 C  CA   . THR A 176 ? 0.2481 0.1065 0.2210 0.0133  -0.0533 0.0326  177 THR A CA   
1420 C  C    . THR A 176 ? 0.2448 0.0982 0.1890 0.0117  -0.0383 0.0180  177 THR A C    
1421 O  O    . THR A 176 ? 0.2509 0.0793 0.2227 -0.0083 -0.0332 0.0225  177 THR A O    
1422 C  CB   . THR A 176 ? 0.2705 0.1307 0.2244 -0.0033 -0.0736 0.0389  177 THR A CB   
1423 O  OG1  . THR A 176 ? 0.3442 0.1607 0.2397 0.0345  -0.0646 0.0169  177 THR A OG1  
1424 C  CG2  . THR A 176 ? 0.2477 0.2238 0.3003 -0.0040 -0.0362 0.0502  177 THR A CG2  
1425 N  N    . ASN A 177 ? 0.2477 0.0794 0.1956 0.0114  -0.0401 0.0306  178 ASN A N    
1426 C  CA   . ASN A 177 ? 0.2527 0.1177 0.2117 0.0057  -0.0445 0.0329  178 ASN A CA   
1427 C  C    . ASN A 177 ? 0.2585 0.1096 0.2212 0.0079  -0.0515 0.0305  178 ASN A C    
1428 O  O    . ASN A 177 ? 0.2736 0.1617 0.2713 -0.0014 -0.0697 0.0729  178 ASN A O    
1429 C  CB   . ASN A 177 ? 0.2399 0.1033 0.2474 0.0241  -0.0660 0.0426  178 ASN A CB   
1430 C  CG   . ASN A 177 ? 0.2537 0.1478 0.2293 0.0360  -0.0412 0.0414  178 ASN A CG   
1431 O  OD1  . ASN A 177 ? 0.3115 0.1286 0.3175 0.0500  -0.0143 0.0486  178 ASN A OD1  
1432 N  ND2  . ASN A 177 ? 0.2799 0.1211 0.2191 0.0125  -0.0340 0.0645  178 ASN A ND2  
1433 N  N    . PHE A 178 ? 0.2725 0.0778 0.1941 0.0157  -0.0627 0.0465  179 PHE A N    
1434 C  CA   . PHE A 178 ? 0.2460 0.0889 0.1956 0.0017  -0.0513 0.0361  179 PHE A CA   
1435 C  C    . PHE A 178 ? 0.2584 0.0892 0.1972 -0.0030 -0.0456 0.0295  179 PHE A C    
1436 O  O    . PHE A 178 ? 0.2815 0.0851 0.2013 -0.0237 -0.0594 0.0236  179 PHE A O    
1437 C  CB   . PHE A 178 ? 0.2369 0.0628 0.1961 0.0157  -0.0372 0.0422  179 PHE A CB   
1438 C  CG   . PHE A 178 ? 0.2098 0.0762 0.2090 -0.0312 -0.0332 0.0406  179 PHE A CG   
1439 C  CD1  . PHE A 178 ? 0.2520 0.0485 0.2374 0.0055  -0.0314 0.0131  179 PHE A CD1  
1440 C  CD2  . PHE A 178 ? 0.2249 0.1113 0.1844 -0.0044 -0.0175 0.0173  179 PHE A CD2  
1441 C  CE1  . PHE A 178 ? 0.2036 0.0789 0.2263 -0.0107 -0.0461 0.0278  179 PHE A CE1  
1442 C  CE2  . PHE A 178 ? 0.1976 0.1056 0.1946 -0.0484 -0.0193 0.0155  179 PHE A CE2  
1443 C  CZ   . PHE A 178 ? 0.2315 0.1019 0.1994 -0.0133 -0.0165 -0.0070 179 PHE A CZ   
1444 N  N    . ASP A 179 ? 0.2182 0.1100 0.2056 0.0245  -0.0497 0.0287  180 ASP A N    
1445 C  CA   . ASP A 179 ? 0.1897 0.1109 0.2248 0.0329  -0.0459 0.0277  180 ASP A CA   
1446 C  C    . ASP A 179 ? 0.1740 0.0883 0.2126 0.0200  -0.0374 0.0140  180 ASP A C    
1447 O  O    . ASP A 179 ? 0.1982 0.0766 0.2418 -0.0024 -0.0275 0.0046  180 ASP A O    
1448 C  CB   . ASP A 179 ? 0.1837 0.1466 0.2331 0.0291  -0.0459 0.0152  180 ASP A CB   
1449 C  CG   . ASP A 179 ? 0.1885 0.2188 0.2493 -0.0006 -0.0466 0.0131  180 ASP A CG   
1450 O  OD1  . ASP A 179 ? 0.1879 0.1179 0.2649 0.0492  -0.0340 0.0179  180 ASP A OD1  
1451 O  OD2  . ASP A 179 ? 0.2024 0.3643 0.3683 -0.0273 -0.0279 -0.0135 180 ASP A OD2  
1452 N  N    . PRO A 180 ? 0.1527 0.0696 0.2257 0.0097  -0.0358 0.0078  181 PRO A N    
1453 C  CA   . PRO A 180 ? 0.1296 0.1253 0.2122 0.0056  -0.0278 0.0050  181 PRO A CA   
1454 C  C    . PRO A 180 ? 0.1184 0.0979 0.1908 0.0070  -0.0243 0.0158  181 PRO A C    
1455 O  O    . PRO A 180 ? 0.1508 0.0891 0.2147 -0.0002 -0.0380 0.0222  181 PRO A O    
1456 C  CB   . PRO A 180 ? 0.1234 0.1160 0.2281 -0.0074 -0.0310 0.0031  181 PRO A CB   
1457 C  CG   . PRO A 180 ? 0.1878 0.1203 0.2052 -0.0132 -0.0261 -0.0021 181 PRO A CG   
1458 C  CD   . PRO A 180 ? 0.1921 0.0913 0.2384 -0.0023 -0.0411 0.0043  181 PRO A CD   
1459 N  N    . ARG A 181 ? 0.1264 0.0997 0.2064 0.0083  -0.0145 0.0126  182 ARG A N    
1460 C  CA   . ARG A 181 ? 0.1373 0.1041 0.2348 0.0058  -0.0100 0.0119  182 ARG A CA   
1461 C  C    . ARG A 181 ? 0.1486 0.1279 0.2318 0.0181  -0.0225 0.0104  182 ARG A C    
1462 O  O    . ARG A 181 ? 0.1555 0.1237 0.2482 0.0059  -0.0216 0.0306  182 ARG A O    
1463 C  CB   . ARG A 181 ? 0.1407 0.1088 0.2570 0.0172  -0.0110 -0.0124 182 ARG A CB   
1464 C  CG   . ARG A 181 ? 0.1972 0.1078 0.2825 -0.0006 0.0074  0.0162  182 ARG A CG   
1465 C  CD   . ARG A 181 ? 0.1796 0.1331 0.3274 0.0289  0.0020  0.0361  182 ARG A CD   
1466 N  NE   . ARG A 181 ? 0.1394 0.0983 0.3609 0.0097  -0.0258 0.0592  182 ARG A NE   
1467 C  CZ   . ARG A 181 ? 0.1774 0.1806 0.3044 0.0312  -0.0003 0.0478  182 ARG A CZ   
1468 N  NH1  . ARG A 181 ? 0.2266 0.2080 0.3991 -0.0063 0.0416  0.0284  182 ARG A NH1  
1469 N  NH2  . ARG A 181 ? 0.1558 0.2968 0.3582 0.0142  -0.0087 0.0548  182 ARG A NH2  
1470 N  N    . GLY A 182 ? 0.1576 0.0997 0.2317 0.0204  -0.0367 0.0034  183 GLY A N    
1471 C  CA   . GLY A 182 ? 0.1802 0.0743 0.2534 -0.0008 -0.0472 -0.0051 183 GLY A CA   
1472 C  C    . GLY A 182 ? 0.2134 0.0899 0.2501 0.0135  -0.0312 0.0094  183 GLY A C    
1473 O  O    . GLY A 182 ? 0.2194 0.0770 0.2961 -0.0014 -0.0731 0.0039  183 GLY A O    
1474 N  N    . LEU A 183 ? 0.1672 0.0860 0.2334 0.0361  -0.0498 0.0112  184 LEU A N    
1475 C  CA   . LEU A 183 ? 0.1268 0.0908 0.2215 0.0150  -0.0244 0.0086  184 LEU A CA   
1476 C  C    . LEU A 183 ? 0.1284 0.0513 0.2077 0.0055  -0.0225 -0.0048 184 LEU A C    
1477 O  O    . LEU A 183 ? 0.1721 0.1033 0.2430 0.0452  -0.0200 0.0364  184 LEU A O    
1478 C  CB   . LEU A 183 ? 0.0912 0.0785 0.2274 0.0050  -0.0289 0.0146  184 LEU A CB   
1479 C  CG   . LEU A 183 ? 0.1883 0.0902 0.2252 0.0183  -0.0173 0.0129  184 LEU A CG   
1480 C  CD1  . LEU A 183 ? 0.1809 0.2027 0.2428 -0.0060 -0.0134 0.0395  184 LEU A CD1  
1481 C  CD2  . LEU A 183 ? 0.2360 0.1209 0.2628 0.0394  0.0051  -0.0290 184 LEU A CD2  
1482 N  N    . LEU A 184 ? 0.1509 0.0977 0.2282 0.0068  -0.0038 0.0074  185 LEU A N    
1483 C  CA   . LEU A 184 ? 0.1206 0.1251 0.2277 -0.0229 0.0015  0.0198  185 LEU A CA   
1484 C  C    . LEU A 184 ? 0.1705 0.1204 0.2302 -0.0516 -0.0350 0.0236  185 LEU A C    
1485 O  O    . LEU A 184 ? 0.2180 0.1816 0.2834 -0.0976 -0.0903 0.0713  185 LEU A O    
1486 C  CB   . LEU A 184 ? 0.0941 0.1348 0.2440 -0.0025 -0.0062 -0.0036 185 LEU A CB   
1487 C  CG   . LEU A 184 ? 0.0881 0.1362 0.2425 0.0012  0.0069  0.0064  185 LEU A CG   
1488 C  CD1  . LEU A 184 ? 0.1190 0.1815 0.2415 0.0116  0.0045  0.0090  185 LEU A CD1  
1489 C  CD2  . LEU A 184 ? 0.1307 0.1446 0.2603 0.0061  -0.0033 -0.0040 185 LEU A CD2  
1490 N  N    . PRO A 185 ? 0.1307 0.0895 0.2236 -0.0139 -0.0203 0.0305  186 PRO A N    
1491 C  CA   . PRO A 185 ? 0.1120 0.0960 0.2406 -0.0248 0.0002  0.0430  186 PRO A CA   
1492 C  C    . PRO A 185 ? 0.1142 0.0824 0.2505 -0.0122 -0.0186 0.0449  186 PRO A C    
1493 O  O    . PRO A 185 ? 0.0932 0.0787 0.3389 -0.0095 -0.0277 0.0496  186 PRO A O    
1494 C  CB   . PRO A 185 ? 0.1020 0.0965 0.2600 -0.0118 0.0037  0.0320  186 PRO A CB   
1495 C  CG   . PRO A 185 ? 0.1250 0.0885 0.2067 0.0270  -0.0132 0.0209  186 PRO A CG   
1496 C  CD   . PRO A 185 ? 0.1235 0.0832 0.2126 0.0000  -0.0098 -0.0036 186 PRO A CD   
1497 N  N    A GLU A 186 ? 0.1347 0.1226 0.2524 -0.0326 0.0027  0.0352  187 GLU A N    
1498 N  N    B GLU A 186 ? 0.1260 0.1134 0.2566 -0.0368 -0.0009 0.0328  187 GLU A N    
1499 C  CA   A GLU A 186 ? 0.1418 0.1371 0.2516 -0.0290 0.0088  0.0249  187 GLU A CA   
1500 C  CA   B GLU A 186 ? 0.1209 0.1194 0.2564 -0.0285 0.0004  0.0274  187 GLU A CA   
1501 C  C    A GLU A 186 ? 0.1233 0.1327 0.2550 -0.0186 0.0026  0.0329  187 GLU A C    
1502 C  C    B GLU A 186 ? 0.0919 0.1008 0.2521 -0.0169 0.0057  0.0330  187 GLU A C    
1503 O  O    A GLU A 186 ? 0.1379 0.1692 0.2447 -0.0033 0.0266  0.0196  187 GLU A O    
1504 O  O    B GLU A 186 ? 0.0661 0.1110 0.2756 0.0193  0.0150  0.0244  187 GLU A O    
1505 C  CB   A GLU A 186 ? 0.1649 0.1689 0.2702 -0.0228 0.0054  0.0312  187 GLU A CB   
1506 C  CB   B GLU A 186 ? 0.1333 0.1167 0.2830 -0.0222 -0.0102 0.0169  187 GLU A CB   
1507 C  CG   A GLU A 186 ? 0.2074 0.1806 0.2969 -0.0330 -0.0029 0.0239  187 GLU A CG   
1508 C  CG   B GLU A 186 ? 0.1446 0.1608 0.2812 -0.0366 0.0031  0.0233  187 GLU A CG   
1509 C  CD   A GLU A 186 ? 0.1777 0.1927 0.2980 -0.0369 0.0130  0.0164  187 GLU A CD   
1510 C  CD   B GLU A 186 ? 0.2253 0.1959 0.3014 -0.0158 0.0083  0.0181  187 GLU A CD   
1511 O  OE1  A GLU A 186 ? 0.0488 0.2167 0.3600 -0.0257 0.0112  0.0039  187 GLU A OE1  
1512 O  OE1  B GLU A 186 ? 0.2168 0.1454 0.3706 -0.0083 0.0174  0.0000  187 GLU A OE1  
1513 O  OE2  A GLU A 186 ? 0.1315 0.2347 0.4355 -0.0228 -0.0003 -0.0051 187 GLU A OE2  
1514 O  OE2  B GLU A 186 ? 0.2520 0.2518 0.3369 0.0084  0.0450  0.0370  187 GLU A OE2  
1515 N  N    . SER A 187 ? 0.0661 0.1334 0.2621 -0.0232 -0.0100 0.0228  188 SER A N    
1516 C  CA   . SER A 187 ? 0.1002 0.1107 0.2591 -0.0197 0.0008  0.0208  188 SER A CA   
1517 C  C    . SER A 187 ? 0.0740 0.1110 0.2669 -0.0029 0.0150  0.0003  188 SER A C    
1518 O  O    . SER A 187 ? 0.0965 0.1405 0.2826 -0.0090 0.0156  -0.0219 188 SER A O    
1519 C  CB   . SER A 187 ? 0.1171 0.1465 0.2635 -0.0062 0.0136  0.0374  188 SER A CB   
1520 O  OG   . SER A 187 ? 0.1238 0.1606 0.3041 -0.0377 0.0109  0.0318  188 SER A OG   
1521 N  N    . LEU A 188 ? 0.0945 0.0910 0.2757 -0.0144 0.0045  -0.0148 189 LEU A N    
1522 C  CA   . LEU A 188 ? 0.0951 0.0960 0.2775 -0.0030 -0.0027 -0.0057 189 LEU A CA   
1523 C  C    . LEU A 188 ? 0.0587 0.1136 0.2607 -0.0107 -0.0043 -0.0149 189 LEU A C    
1524 O  O    . LEU A 188 ? 0.0924 0.1457 0.2801 -0.0374 -0.0194 -0.0339 189 LEU A O    
1525 C  CB   . LEU A 188 ? 0.1495 0.0896 0.3029 -0.0244 -0.0180 0.0011  189 LEU A CB   
1526 C  CG   . LEU A 188 ? 0.1119 0.1268 0.3085 0.0031  0.0066  -0.0074 189 LEU A CG   
1527 C  CD1  . LEU A 188 ? 0.1824 0.1094 0.3536 0.0268  -0.0141 0.0078  189 LEU A CD1  
1528 C  CD2  . LEU A 188 ? 0.0808 0.2406 0.3373 -0.0003 0.0109  -0.0142 189 LEU A CD2  
1529 N  N    . ASP A 189 ? 0.0892 0.1213 0.2552 -0.0002 0.0066  -0.0096 190 ASP A N    
1530 C  CA   . ASP A 189 ? 0.0819 0.1477 0.2430 -0.0147 0.0149  -0.0045 190 ASP A CA   
1531 C  C    . ASP A 189 ? 0.0663 0.1004 0.2013 -0.0236 0.0311  -0.0132 190 ASP A C    
1532 O  O    . ASP A 189 ? 0.1004 0.0894 0.2053 -0.0010 0.0244  -0.0059 190 ASP A O    
1533 C  CB   . ASP A 189 ? 0.0993 0.1715 0.2463 -0.0470 0.0265  0.0176  190 ASP A CB   
1534 C  CG   . ASP A 189 ? 0.1315 0.2713 0.2714 -0.0487 -0.0053 0.0099  190 ASP A CG   
1535 O  OD1  . ASP A 189 ? 0.1887 0.3930 0.3474 -0.0611 0.1003  -0.0120 190 ASP A OD1  
1536 O  OD2  . ASP A 189 ? 0.2378 0.3706 0.3480 -0.1111 0.0250  0.0403  190 ASP A OD2  
1537 N  N    . TYR A 190 ? 0.0609 0.1148 0.1918 -0.0182 0.0100  -0.0012 191 TYR A N    
1538 C  CA   . TYR A 190 ? 0.0662 0.0976 0.2014 -0.0139 0.0038  0.0168  191 TYR A CA   
1539 C  C    . TYR A 190 ? 0.0897 0.0842 0.1731 -0.0117 0.0176  0.0051  191 TYR A C    
1540 O  O    . TYR A 190 ? 0.1044 0.1241 0.1844 0.0137  0.0391  0.0092  191 TYR A O    
1541 C  CB   . TYR A 190 ? 0.1173 0.0887 0.2037 -0.0089 0.0151  0.0020  191 TYR A CB   
1542 C  CG   . TYR A 190 ? 0.1023 0.0738 0.1861 -0.0184 0.0354  0.0262  191 TYR A CG   
1543 C  CD1  . TYR A 190 ? 0.1300 0.0863 0.1837 -0.0155 0.0099  0.0002  191 TYR A CD1  
1544 C  CD2  . TYR A 190 ? 0.0872 0.1348 0.1913 0.0085  0.0356  0.0066  191 TYR A CD2  
1545 C  CE1  . TYR A 190 ? 0.1314 0.1025 0.2006 -0.0033 0.0212  0.0211  191 TYR A CE1  
1546 C  CE2  . TYR A 190 ? 0.1440 0.1283 0.1892 -0.0249 0.0084  -0.0248 191 TYR A CE2  
1547 C  CZ   . TYR A 190 ? 0.1701 0.0681 0.1992 -0.0184 0.0008  0.0015  191 TYR A CZ   
1548 O  OH   . TYR A 190 ? 0.1648 0.1080 0.2206 -0.0024 0.0034  -0.0337 191 TYR A OH   
1549 N  N    . TRP A 191 ? 0.0869 0.0636 0.1859 -0.0098 0.0192  0.0025  192 TRP A N    
1550 C  CA   . TRP A 191 ? 0.0925 0.0595 0.1833 -0.0232 0.0166  0.0051  192 TRP A CA   
1551 C  C    . TRP A 191 ? 0.0935 0.0725 0.1475 0.0035  0.0292  -0.0052 192 TRP A C    
1552 O  O    . TRP A 191 ? 0.1207 0.0718 0.1578 -0.0131 0.0158  -0.0098 192 TRP A O    
1553 C  CB   . TRP A 191 ? 0.1118 0.0439 0.1944 -0.0145 0.0378  0.0082  192 TRP A CB   
1554 C  CG   . TRP A 191 ? 0.0945 0.0781 0.1792 0.0070  0.0150  0.0136  192 TRP A CG   
1555 C  CD1  . TRP A 191 ? 0.1228 0.0612 0.2074 -0.0024 0.0190  -0.0017 192 TRP A CD1  
1556 C  CD2  . TRP A 191 ? 0.1045 0.0776 0.1880 0.0081  0.0294  0.0110  192 TRP A CD2  
1557 N  NE1  . TRP A 191 ? 0.1639 0.0853 0.1834 -0.0160 0.0301  0.0278  192 TRP A NE1  
1558 C  CE2  . TRP A 191 ? 0.0997 0.1030 0.1795 0.0072  0.0316  0.0007  192 TRP A CE2  
1559 C  CE3  . TRP A 191 ? 0.1082 0.0993 0.1996 0.0004  0.0173  0.0007  192 TRP A CE3  
1560 C  CZ2  . TRP A 191 ? 0.1209 0.0929 0.2143 0.0035  -0.0033 -0.0007 192 TRP A CZ2  
1561 C  CZ3  . TRP A 191 ? 0.1014 0.0849 0.2312 -0.0243 0.0208  -0.0132 192 TRP A CZ3  
1562 C  CH2  . TRP A 191 ? 0.1072 0.1032 0.2259 -0.0061 0.0126  0.0164  192 TRP A CH2  
1563 N  N    . THR A 192 ? 0.0776 0.0722 0.1523 -0.0116 0.0033  0.0046  193 THR A N    
1564 C  CA   . THR A 192 ? 0.0615 0.0955 0.1566 0.0001  0.0171  -0.0005 193 THR A CA   
1565 C  C    . THR A 192 ? 0.0794 0.0788 0.1528 -0.0011 0.0241  0.0047  193 THR A C    
1566 O  O    . THR A 192 ? 0.1102 0.0973 0.1397 0.0072  0.0175  0.0123  193 THR A O    
1567 C  CB   . THR A 192 ? 0.0947 0.0516 0.1546 0.0124  0.0341  0.0022  193 THR A CB   
1568 O  OG1  . THR A 192 ? 0.1001 0.0561 0.1959 -0.0057 0.0264  -0.0009 193 THR A OG1  
1569 C  CG2  . THR A 192 ? 0.1207 0.1103 0.1741 0.0256  0.0266  -0.0012 193 THR A CG2  
1570 N  N    . TYR A 193 ? 0.0532 0.0690 0.1835 -0.0233 0.0242  -0.0046 194 TYR A N    
1571 C  CA   . TYR A 193 ? 0.0641 0.0542 0.1801 -0.0074 0.0254  -0.0021 194 TYR A CA   
1572 C  C    . TYR A 193 ? 0.0878 0.0743 0.1785 0.0040  0.0182  -0.0205 194 TYR A C    
1573 O  O    . TYR A 193 ? 0.0929 0.0659 0.1632 -0.0165 0.0128  0.0050  194 TYR A O    
1574 C  CB   . TYR A 193 ? 0.0977 0.0789 0.1718 0.0204  0.0297  -0.0165 194 TYR A CB   
1575 C  CG   . TYR A 193 ? 0.0979 0.0429 0.1510 0.0045  0.0259  -0.0024 194 TYR A CG   
1576 C  CD1  . TYR A 193 ? 0.1262 0.0422 0.1400 0.0100  -0.0045 0.0059  194 TYR A CD1  
1577 C  CD2  . TYR A 193 ? 0.0985 0.0468 0.1641 0.0129  -0.0038 -0.0046 194 TYR A CD2  
1578 C  CE1  . TYR A 193 ? 0.0719 0.0473 0.1488 -0.0018 0.0370  0.0026  194 TYR A CE1  
1579 C  CE2  . TYR A 193 ? 0.1444 0.0366 0.1536 0.0097  -0.0006 -0.0225 194 TYR A CE2  
1580 C  CZ   . TYR A 193 ? 0.0876 0.0302 0.1485 0.0117  0.0098  -0.0139 194 TYR A CZ   
1581 O  OH   . TYR A 193 ? 0.1202 0.0492 0.1588 0.0225  0.0213  -0.0078 194 TYR A OH   
1582 N  N    . PRO A 194 ? 0.0814 0.0800 0.1591 -0.0063 0.0039  -0.0154 195 PRO A N    
1583 C  CA   . PRO A 194 ? 0.0928 0.0772 0.1655 -0.0061 0.0292  -0.0347 195 PRO A CA   
1584 C  C    . PRO A 194 ? 0.0611 0.0519 0.1607 -0.0096 0.0167  -0.0204 195 PRO A C    
1585 O  O    . PRO A 194 ? 0.1083 0.0812 0.1723 0.0100  -0.0040 -0.0054 195 PRO A O    
1586 C  CB   . PRO A 194 ? 0.1191 0.0757 0.1661 -0.0017 0.0076  -0.0239 195 PRO A CB   
1587 C  CG   . PRO A 194 ? 0.1117 0.1118 0.1671 -0.0202 0.0014  -0.0192 195 PRO A CG   
1588 C  CD   . PRO A 194 ? 0.1328 0.1230 0.1525 -0.0416 -0.0029 -0.0355 195 PRO A CD   
1589 N  N    . GLY A 195 ? 0.0701 0.0743 0.1555 -0.0013 0.0410  -0.0253 196 GLY A N    
1590 C  CA   . GLY A 195 ? 0.1013 0.0516 0.1639 0.0075  0.0344  -0.0016 196 GLY A CA   
1591 C  C    . GLY A 195 ? 0.0854 0.0735 0.1458 -0.0308 0.0395  -0.0107 196 GLY A C    
1592 O  O    . GLY A 195 ? 0.0920 0.0450 0.1810 -0.0158 0.0059  -0.0177 196 GLY A O    
1593 N  N    . SER A 196 ? 0.1056 0.0680 0.1251 -0.0154 0.0316  -0.0225 197 SER A N    
1594 C  CA   . SER A 196 ? 0.0878 0.0652 0.1419 0.0165  0.0329  -0.0060 197 SER A CA   
1595 C  C    . SER A 196 ? 0.0363 0.0490 0.1365 0.0086  0.0075  0.0015  197 SER A C    
1596 O  O    . SER A 196 ? 0.0731 0.0445 0.1768 -0.0115 0.0192  -0.0036 197 SER A O    
1597 C  CB   . SER A 196 ? 0.0797 0.0515 0.2158 0.0063  0.0082  -0.0259 197 SER A CB   
1598 O  OG   . SER A 196 ? 0.0595 0.0661 0.2037 0.0121  0.0091  -0.0229 197 SER A OG   
1599 N  N    . LEU A 197 ? 0.0861 0.0623 0.1238 0.0211  0.0197  0.0045  198 LEU A N    
1600 C  CA   . LEU A 197 ? 0.0825 0.0459 0.1439 0.0046  0.0415  -0.0089 198 LEU A CA   
1601 C  C    . LEU A 197 ? 0.0599 0.0515 0.1456 -0.0073 0.0040  -0.0182 198 LEU A C    
1602 O  O    . LEU A 197 ? 0.0792 0.0613 0.1905 -0.0082 -0.0036 -0.0151 198 LEU A O    
1603 C  CB   . LEU A 197 ? 0.1087 0.0739 0.1855 0.0030  0.0499  0.0044  198 LEU A CB   
1604 C  CG   . LEU A 197 ? 0.1653 0.1567 0.2729 0.0157  0.0620  0.0564  198 LEU A CG   
1605 C  CD1  . LEU A 197 ? 0.1394 0.1323 0.3413 0.0112  0.1179  0.0900  198 LEU A CD1  
1606 C  CD2  . LEU A 197 ? 0.1489 0.1219 0.2653 -0.0038 0.0738  0.0249  198 LEU A CD2  
1607 N  N    . THR A 198 ? 0.0735 0.0398 0.1578 -0.0039 0.0039  -0.0176 199 THR A N    
1608 C  CA   . THR A 198 ? 0.0726 0.0372 0.1863 0.0030  0.0406  -0.0181 199 THR A CA   
1609 C  C    . THR A 198 ? 0.0608 0.0532 0.1885 0.0128  0.0105  -0.0157 199 THR A C    
1610 O  O    . THR A 198 ? 0.0579 0.0581 0.1969 0.0043  0.0178  -0.0235 199 THR A O    
1611 C  CB   . THR A 198 ? 0.0636 0.0361 0.1861 0.0041  0.0319  -0.0338 199 THR A CB   
1612 O  OG1  . THR A 198 ? 0.0286 0.0282 0.0701 0.0031  -0.0122 -0.0114 199 THR A OG1  
1613 C  CG2  . THR A 198 ? 0.1321 0.1370 0.2157 -0.0040 0.0217  -0.0011 199 THR A CG2  
1614 N  N    . THR A 199 ? 0.1053 0.0681 0.2068 -0.0135 0.0357  -0.0012 200 THR A N    
1615 C  CA   . THR A 199 ? 0.1081 0.0937 0.1916 -0.0298 0.0089  -0.0215 200 THR A CA   
1616 C  C    . THR A 199 ? 0.1009 0.1062 0.2105 -0.0191 0.0426  -0.0114 200 THR A C    
1617 O  O    . THR A 199 ? 0.1060 0.0701 0.2154 -0.0239 0.0309  -0.0159 200 THR A O    
1618 C  CB   . THR A 199 ? 0.1302 0.0909 0.2190 -0.0151 0.0000  -0.0115 200 THR A CB   
1619 O  OG1  . THR A 199 ? 0.2095 0.0764 0.2889 0.0167  0.0000  -0.0089 200 THR A OG1  
1620 C  CG2  . THR A 199 ? 0.1630 0.0674 0.2293 -0.0567 0.0000  -0.0277 200 THR A CG2  
1621 N  N    . PRO A 200 ? 0.0850 0.0862 0.2219 -0.0290 0.0489  -0.0190 201 PRO A N    
1622 C  CA   . PRO A 200 ? 0.0943 0.1010 0.2398 -0.0371 0.0400  0.0015  201 PRO A CA   
1623 C  C    . PRO A 200 ? 0.1070 0.1086 0.2088 -0.0270 0.0550  -0.0024 201 PRO A C    
1624 O  O    . PRO A 200 ? 0.1591 0.0914 0.2110 -0.0037 0.0307  -0.0121 201 PRO A O    
1625 C  CB   . PRO A 200 ? 0.0740 0.0931 0.2499 -0.0321 0.0390  -0.0100 201 PRO A CB   
1626 C  CG   . PRO A 200 ? 0.1258 0.0844 0.2676 -0.0377 0.0492  -0.0277 201 PRO A CG   
1627 C  CD   . PRO A 200 ? 0.1014 0.1061 0.2326 -0.0107 0.0542  -0.0366 201 PRO A CD   
1628 N  N    . PRO A 201 ? 0.1276 0.1071 0.2082 -0.0180 0.0357  -0.0059 202 PRO A N    
1629 C  CA   . PRO A 201 ? 0.1652 0.0984 0.2158 -0.0278 0.0306  0.0019  202 PRO A CA   
1630 C  C    . PRO A 201 ? 0.0974 0.1024 0.2041 0.0039  0.0288  -0.0121 202 PRO A C    
1631 O  O    . PRO A 201 ? 0.1226 0.0729 0.2454 -0.0356 0.0369  -0.0276 202 PRO A O    
1632 C  CB   . PRO A 201 ? 0.1872 0.0722 0.2474 -0.0304 0.0295  0.0230  202 PRO A CB   
1633 C  CG   . PRO A 201 ? 0.2188 0.1114 0.2527 -0.0210 0.0036  -0.0005 202 PRO A CG   
1634 C  CD   . PRO A 201 ? 0.1897 0.0910 0.2280 -0.0122 0.0077  -0.0069 202 PRO A CD   
1635 N  N    . LEU A 202 ? 0.0814 0.0726 0.2053 -0.0142 0.0335  -0.0082 203 LEU A N    
1636 C  CA   . LEU A 202 ? 0.1028 0.0492 0.1881 0.0139  0.0203  -0.0119 203 LEU A CA   
1637 C  C    . LEU A 202 ? 0.0653 0.0625 0.1998 -0.0241 0.0029  -0.0116 203 LEU A C    
1638 O  O    . LEU A 202 ? 0.0798 0.0720 0.2106 -0.0047 0.0083  -0.0161 203 LEU A O    
1639 C  CB   . LEU A 202 ? 0.0916 0.0515 0.2400 0.0109  0.0073  -0.0204 203 LEU A CB   
1640 C  CG   . LEU A 202 ? 0.0745 0.0499 0.2362 0.0139  0.0287  -0.0193 203 LEU A CG   
1641 C  CD1  . LEU A 202 ? 0.0993 0.1013 0.2745 0.0458  0.0246  -0.0375 203 LEU A CD1  
1642 C  CD2  . LEU A 202 ? 0.1133 0.0824 0.2278 -0.0329 -0.0001 -0.0414 203 LEU A CD2  
1643 N  N    . LEU A 203 ? 0.1041 0.0505 0.2179 -0.0116 0.0221  -0.0202 204 LEU A N    
1644 C  CA   . LEU A 203 ? 0.1150 0.0814 0.2000 -0.0115 0.0194  -0.0173 204 LEU A CA   
1645 C  C    . LEU A 203 ? 0.0858 0.0428 0.1910 -0.0025 0.0070  -0.0037 204 LEU A C    
1646 O  O    . LEU A 203 ? 0.1092 0.0555 0.2051 -0.0282 0.0040  -0.0285 204 LEU A O    
1647 C  CB   . LEU A 203 ? 0.1035 0.0724 0.2263 -0.0199 0.0130  0.0147  204 LEU A CB   
1648 C  CG   . LEU A 203 ? 0.1317 0.0798 0.2667 -0.0303 0.0246  0.0192  204 LEU A CG   
1649 C  CD1  . LEU A 203 ? 0.1484 0.0866 0.2668 0.0122  0.0282  0.0486  204 LEU A CD1  
1650 C  CD2  . LEU A 203 ? 0.1191 0.1210 0.3743 -0.0682 0.0137  0.0042  204 LEU A CD2  
1651 N  N    . GLU A 204 ? 0.1174 0.0879 0.1823 -0.0050 0.0054  -0.0247 205 GLU A N    
1652 C  CA   . GLU A 204 ? 0.0842 0.0743 0.1868 0.0020  -0.0106 -0.0341 205 GLU A CA   
1653 C  C    . GLU A 204 ? 0.0862 0.0660 0.1927 0.0012  -0.0162 -0.0194 205 GLU A C    
1654 O  O    . GLU A 204 ? 0.1442 0.1050 0.2019 0.0110  -0.0016 -0.0428 205 GLU A O    
1655 C  CB   . GLU A 204 ? 0.1287 0.0671 0.2066 0.0145  -0.0134 -0.0248 205 GLU A CB   
1656 C  CG   . GLU A 204 ? 0.0834 0.1116 0.2372 0.0112  -0.0081 -0.0248 205 GLU A CG   
1657 C  CD   . GLU A 204 ? 0.1137 0.0967 0.2333 -0.0144 -0.0149 -0.0097 205 GLU A CD   
1658 O  OE1  . GLU A 204 ? 0.1542 0.1239 0.2887 -0.0101 -0.0579 -0.0544 205 GLU A OE1  
1659 O  OE2  . GLU A 204 ? 0.1194 0.0979 0.2390 -0.0081 -0.0175 -0.0253 205 GLU A OE2  
1660 N  N    . CYS A 205 ? 0.0644 0.0565 0.2027 -0.0063 -0.0133 -0.0098 206 CYS A N    
1661 C  CA   . CYS A 205 ? 0.0672 0.0484 0.1747 0.0018  -0.0132 -0.0002 206 CYS A CA   
1662 C  C    . CYS A 205 ? 0.0899 0.0437 0.1934 -0.0006 -0.0004 -0.0204 206 CYS A C    
1663 O  O    . CYS A 205 ? 0.1027 0.0583 0.2159 -0.0041 -0.0269 0.0037  206 CYS A O    
1664 C  CB   . CYS A 205 ? 0.1185 0.0708 0.1849 -0.0344 0.0132  -0.0133 206 CYS A CB   
1665 S  SG   . CYS A 205 ? 0.1432 0.0641 0.2018 -0.0019 0.0032  -0.0082 206 CYS A SG   
1666 N  N    . VAL A 206 ? 0.0971 0.0430 0.1729 -0.0147 0.0061  -0.0124 207 VAL A N    
1667 C  CA   . VAL A 206 ? 0.0834 0.0348 0.1794 -0.0230 0.0173  -0.0142 207 VAL A CA   
1668 C  C    . VAL A 206 ? 0.0739 0.0568 0.1773 0.0114  0.0065  -0.0122 207 VAL A C    
1669 O  O    . VAL A 206 ? 0.0830 0.0662 0.2015 -0.0111 0.0107  -0.0089 207 VAL A O    
1670 C  CB   . VAL A 206 ? 0.1036 0.0370 0.1801 0.0057  0.0236  -0.0361 207 VAL A CB   
1671 C  CG1  . VAL A 206 ? 0.0544 0.0620 0.1825 -0.0195 -0.0151 -0.0370 207 VAL A CG1  
1672 C  CG2  . VAL A 206 ? 0.1225 0.0893 0.1836 -0.0118 0.0443  -0.0049 207 VAL A CG2  
1673 N  N    . THR A 207 ? 0.0778 0.0371 0.1755 -0.0105 0.0252  -0.0114 208 THR A N    
1674 C  CA   . THR A 207 ? 0.0753 0.0396 0.1673 -0.0061 0.0170  -0.0104 208 THR A CA   
1675 C  C    . THR A 207 ? 0.0568 0.0526 0.1594 -0.0052 0.0069  0.0110  208 THR A C    
1676 O  O    . THR A 207 ? 0.1097 0.0553 0.1584 -0.0088 0.0077  0.0041  208 THR A O    
1677 C  CB   . THR A 207 ? 0.0749 0.0628 0.1684 0.0156  0.0287  -0.0046 208 THR A CB   
1678 O  OG1  . THR A 207 ? 0.1452 0.0525 0.1845 -0.0108 0.0172  -0.0306 208 THR A OG1  
1679 C  CG2  . THR A 207 ? 0.0823 0.0930 0.1927 -0.0205 0.0432  0.0030  208 THR A CG2  
1680 N  N    . TRP A 208 ? 0.0839 0.0256 0.1727 -0.0008 0.0049  0.0061  209 TRP A N    
1681 C  CA   . TRP A 208 ? 0.0722 0.0358 0.1771 -0.0221 -0.0003 0.0002  209 TRP A CA   
1682 C  C    . TRP A 208 ? 0.0804 0.0459 0.1577 -0.0016 0.0106  -0.0032 209 TRP A C    
1683 O  O    . TRP A 208 ? 0.0728 0.0664 0.1660 -0.0009 0.0078  -0.0107 209 TRP A O    
1684 C  CB   . TRP A 208 ? 0.0815 0.0364 0.1530 0.0061  0.0345  0.0154  209 TRP A CB   
1685 C  CG   . TRP A 208 ? 0.0665 0.0315 0.1539 -0.0104 0.0237  0.0142  209 TRP A CG   
1686 C  CD1  . TRP A 208 ? 0.0944 0.0270 0.1742 0.0094  0.0267  0.0110  209 TRP A CD1  
1687 C  CD2  . TRP A 208 ? 0.1071 0.0254 0.1505 -0.0031 0.0296  -0.0015 209 TRP A CD2  
1688 N  NE1  . TRP A 208 ? 0.1102 0.0682 0.1563 0.0216  0.0034  -0.0205 209 TRP A NE1  
1689 C  CE2  . TRP A 208 ? 0.0819 0.0410 0.1534 0.0180  0.0042  -0.0096 209 TRP A CE2  
1690 C  CE3  . TRP A 208 ? 0.0974 0.0288 0.1664 -0.0059 0.0089  -0.0214 209 TRP A CE3  
1691 C  CZ2  . TRP A 208 ? 0.0856 0.0334 0.1539 0.0106  0.0153  -0.0217 209 TRP A CZ2  
1692 C  CZ3  . TRP A 208 ? 0.0909 0.0444 0.1678 0.0352  0.0246  0.0080  209 TRP A CZ3  
1693 C  CH2  . TRP A 208 ? 0.0999 0.0312 0.1663 0.0070  0.0092  -0.0261 209 TRP A CH2  
1694 N  N    . ILE A 209 ? 0.0711 0.0408 0.1603 -0.0210 0.0037  -0.0033 210 ILE A N    
1695 C  CA   . ILE A 209 ? 0.0539 0.0293 0.1708 -0.0044 -0.0041 -0.0108 210 ILE A CA   
1696 C  C    . ILE A 209 ? 0.0747 0.0573 0.1327 0.0037  0.0203  0.0068  210 ILE A C    
1697 O  O    . ILE A 209 ? 0.1102 0.0461 0.1399 0.0070  0.0121  0.0027  210 ILE A O    
1698 C  CB   . ILE A 209 ? 0.0651 0.0609 0.1793 -0.0154 0.0020  0.0005  210 ILE A CB   
1699 C  CG1  . ILE A 209 ? 0.0968 0.0466 0.2376 0.0359  -0.0039 -0.0283 210 ILE A CG1  
1700 C  CG2  . ILE A 209 ? 0.0635 0.0824 0.2028 -0.0021 0.0064  0.0331  210 ILE A CG2  
1701 C  CD1  . ILE A 209 ? 0.1093 0.0553 0.2621 0.0378  0.0059  0.0007  210 ILE A CD1  
1702 N  N    . VAL A 210 ? 0.0779 0.0327 0.1680 0.0003  0.0161  0.0022  211 VAL A N    
1703 C  CA   . VAL A 210 ? 0.0706 0.0412 0.1665 -0.0144 0.0032  -0.0167 211 VAL A CA   
1704 C  C    . VAL A 210 ? 0.0831 0.0344 0.1704 0.0082  0.0105  -0.0132 211 VAL A C    
1705 O  O    . VAL A 210 ? 0.1076 0.0709 0.1573 -0.0048 0.0285  -0.0018 211 VAL A O    
1706 C  CB   . VAL A 210 ? 0.0510 0.0484 0.1850 -0.0012 0.0069  0.0006  211 VAL A CB   
1707 C  CG1  . VAL A 210 ? 0.0991 0.0306 0.1842 0.0082  -0.0131 -0.0276 211 VAL A CG1  
1708 C  CG2  . VAL A 210 ? 0.0697 0.0601 0.2074 -0.0024 0.0195  -0.0076 211 VAL A CG2  
1709 N  N    . LEU A 211 ? 0.0900 0.0483 0.1812 -0.0094 0.0038  -0.0097 212 LEU A N    
1710 C  CA   . LEU A 211 ? 0.0758 0.0625 0.1790 -0.0329 0.0119  0.0221  212 LEU A CA   
1711 C  C    . LEU A 211 ? 0.0828 0.0629 0.1757 -0.0324 0.0141  0.0052  212 LEU A C    
1712 O  O    . LEU A 211 ? 0.0808 0.0742 0.1932 -0.0098 0.0184  -0.0074 212 LEU A O    
1713 C  CB   . LEU A 211 ? 0.1143 0.0741 0.1916 -0.0150 -0.0028 0.0293  212 LEU A CB   
1714 C  CG   . LEU A 211 ? 0.1252 0.0477 0.2229 -0.0132 -0.0104 0.0089  212 LEU A CG   
1715 C  CD1  . LEU A 211 ? 0.1289 0.1365 0.2513 -0.0176 -0.0114 0.0207  212 LEU A CD1  
1716 C  CD2  . LEU A 211 ? 0.1137 0.0760 0.2432 0.0003  0.0390  0.0017  212 LEU A CD2  
1717 N  N    . LYS A 212 ? 0.1079 0.0833 0.1920 -0.0402 0.0274  0.0071  213 LYS A N    
1718 C  CA   . LYS A 212 ? 0.1293 0.0646 0.2040 -0.0263 0.0224  -0.0004 213 LYS A CA   
1719 C  C    . LYS A 212 ? 0.1004 0.0483 0.2191 -0.0216 -0.0008 0.0125  213 LYS A C    
1720 O  O    . LYS A 212 ? 0.1044 0.0682 0.2702 -0.0117 -0.0130 -0.0050 213 LYS A O    
1721 C  CB   . LYS A 212 ? 0.1907 0.1203 0.2153 -0.0434 0.0245  0.0021  213 LYS A CB   
1722 C  CG   . LYS A 212 ? 0.2574 0.1878 0.3050 -0.0565 -0.0005 -0.0023 213 LYS A CG   
1723 C  CD   . LYS A 212 ? 0.3362 0.3318 0.3528 -0.0841 0.0150  -0.0127 213 LYS A CD   
1724 C  CE   . LYS A 212 ? 0.4089 0.3466 0.3745 -0.0313 -0.0137 0.0419  213 LYS A CE   
1725 N  NZ   . LYS A 212 ? 0.2952 0.2720 0.4014 -0.0140 -0.0249 0.0270  213 LYS A NZ   
1726 N  N    . GLU A 213 ? 0.0782 0.0608 0.2057 -0.0193 0.0059  0.0069  214 GLU A N    
1727 C  CA   . GLU A 213 ? 0.0789 0.0739 0.2046 -0.0162 -0.0199 -0.0157 214 GLU A CA   
1728 C  C    . GLU A 213 ? 0.0928 0.0613 0.2090 -0.0159 0.0118  0.0025  214 GLU A C    
1729 O  O    . GLU A 213 ? 0.0872 0.0537 0.2129 -0.0110 0.0093  0.0080  214 GLU A O    
1730 C  CB   . GLU A 213 ? 0.1059 0.0925 0.2115 -0.0193 0.0002  0.0034  214 GLU A CB   
1731 C  CG   . GLU A 213 ? 0.0692 0.1403 0.2990 -0.0316 -0.0273 -0.0304 214 GLU A CG   
1732 C  CD   . GLU A 213 ? 0.1356 0.1151 0.3733 -0.0682 0.0089  -0.0616 214 GLU A CD   
1733 O  OE1  . GLU A 213 ? 0.1335 0.0889 0.3498 -0.0134 -0.0185 -0.0046 214 GLU A OE1  
1734 O  OE2  . GLU A 213 ? 0.1855 0.3576 0.4261 -0.0667 -0.0288 -0.0788 214 GLU A OE2  
1735 N  N    . PRO A 214 ? 0.1091 0.0459 0.2012 -0.0009 0.0152  0.0192  215 PRO A N    
1736 C  CA   . PRO A 214 ? 0.1036 0.0721 0.1910 -0.0028 0.0143  -0.0023 215 PRO A CA   
1737 C  C    . PRO A 214 ? 0.1026 0.0839 0.1942 -0.0054 0.0006  0.0020  215 PRO A C    
1738 O  O    . PRO A 214 ? 0.1259 0.1140 0.2236 -0.0349 0.0071  0.0047  215 PRO A O    
1739 C  CB   . PRO A 214 ? 0.0916 0.0579 0.2234 -0.0120 0.0032  0.0107  215 PRO A CB   
1740 C  CG   . PRO A 214 ? 0.1947 0.1304 0.2834 0.0057  0.0271  0.0114  215 PRO A CG   
1741 C  CD   . PRO A 214 ? 0.1456 0.0648 0.2182 0.0131  0.0478  0.0216  215 PRO A CD   
1742 N  N    . ILE A 215 ? 0.1306 0.0622 0.1813 0.0101  -0.0088 -0.0041 216 ILE A N    
1743 C  CA   . ILE A 215 ? 0.1330 0.0721 0.1956 -0.0027 -0.0107 -0.0153 216 ILE A CA   
1744 C  C    . ILE A 215 ? 0.1059 0.0684 0.2087 -0.0039 -0.0228 -0.0016 216 ILE A C    
1745 O  O    . ILE A 215 ? 0.1427 0.0675 0.2239 0.0005  -0.0192 -0.0359 216 ILE A O    
1746 C  CB   . ILE A 215 ? 0.1169 0.0677 0.1962 0.0162  0.0066  -0.0073 216 ILE A CB   
1747 C  CG1  . ILE A 215 ? 0.1562 0.0916 0.2102 -0.0088 0.0133  -0.0011 216 ILE A CG1  
1748 C  CG2  . ILE A 215 ? 0.1381 0.0978 0.2453 0.0161  -0.0014 -0.0195 216 ILE A CG2  
1749 C  CD1  . ILE A 215 ? 0.1852 0.0830 0.2288 -0.0123 -0.0125 0.0139  216 ILE A CD1  
1750 N  N    A SER A 216 ? 0.1132 0.0643 0.2275 -0.0030 -0.0277 -0.0153 217 SER A N    
1751 N  N    B SER A 216 ? 0.1227 0.0466 0.2198 -0.0067 -0.0294 -0.0275 217 SER A N    
1752 C  CA   A SER A 216 ? 0.1299 0.1053 0.2178 -0.0131 -0.0235 -0.0192 217 SER A CA   
1753 C  CA   B SER A 216 ? 0.1208 0.0586 0.2117 -0.0129 -0.0280 -0.0286 217 SER A CA   
1754 C  C    A SER A 216 ? 0.1494 0.0765 0.2171 -0.0051 -0.0282 -0.0174 217 SER A C    
1755 C  C    B SER A 216 ? 0.1522 0.0401 0.2134 -0.0044 -0.0318 -0.0270 217 SER A C    
1756 O  O    A SER A 216 ? 0.1362 0.1073 0.2088 -0.0115 -0.0378 -0.0159 217 SER A O    
1757 O  O    B SER A 216 ? 0.1854 0.0295 0.2212 -0.0121 -0.0395 -0.0219 217 SER A O    
1758 C  CB   A SER A 216 ? 0.1508 0.1147 0.2419 -0.0041 0.0023  0.0121  217 SER A CB   
1759 C  CB   B SER A 216 ? 0.1272 0.0279 0.2173 -0.0065 -0.0328 -0.0179 217 SER A CB   
1760 O  OG   A SER A 216 ? 0.1804 0.2091 0.2596 -0.0434 -0.0509 -0.0046 217 SER A OG   
1761 O  OG   B SER A 216 ? 0.2353 0.1046 0.2151 -0.0178 -0.0176 -0.0160 217 SER A OG   
1762 N  N    . VAL A 217 ? 0.1435 0.0402 0.2147 -0.0290 -0.0228 -0.0165 218 VAL A N    
1763 C  CA   . VAL A 217 ? 0.1445 0.0450 0.2112 -0.0045 -0.0284 -0.0137 218 VAL A CA   
1764 C  C    . VAL A 217 ? 0.1566 0.0572 0.2113 -0.0097 -0.0303 -0.0202 218 VAL A C    
1765 O  O    . VAL A 217 ? 0.1875 0.0571 0.2306 -0.0240 -0.0600 -0.0183 218 VAL A O    
1766 C  CB   . VAL A 217 ? 0.1682 0.0501 0.2365 -0.0362 -0.0473 -0.0191 218 VAL A CB   
1767 C  CG1  . VAL A 217 ? 0.1634 0.0606 0.2433 -0.0164 -0.0339 -0.0430 218 VAL A CG1  
1768 C  CG2  . VAL A 217 ? 0.1555 0.0738 0.2931 -0.0369 -0.0532 -0.0182 218 VAL A CG2  
1769 N  N    . SER A 218 ? 0.1866 0.0577 0.2104 -0.0132 -0.0125 -0.0300 219 SER A N    
1770 C  CA   . SER A 218 ? 0.1877 0.0477 0.2281 -0.0232 -0.0038 -0.0217 219 SER A CA   
1771 C  C    . SER A 218 ? 0.1629 0.0358 0.2306 -0.0139 0.0032  -0.0125 219 SER A C    
1772 O  O    . SER A 218 ? 0.1872 0.0349 0.2226 -0.0175 -0.0265 0.0111  219 SER A O    
1773 C  CB   . SER A 218 ? 0.1910 0.0550 0.2229 -0.0206 0.0017  -0.0126 219 SER A CB   
1774 O  OG   . SER A 218 ? 0.1980 0.0700 0.2532 -0.0479 0.0070  -0.0196 219 SER A OG   
1775 N  N    . SER A 219 ? 0.1808 0.0484 0.2305 -0.0108 -0.0033 -0.0083 220 SER A N    
1776 C  CA   . SER A 219 ? 0.2120 0.0464 0.2655 -0.0009 0.0051  -0.0254 220 SER A CA   
1777 C  C    . SER A 219 ? 0.1756 0.0532 0.2805 -0.0093 -0.0013 -0.0203 220 SER A C    
1778 O  O    . SER A 219 ? 0.1694 0.0669 0.3117 -0.0189 -0.0002 0.0077  220 SER A O    
1779 C  CB   . SER A 219 ? 0.2634 0.0727 0.3006 -0.0319 -0.0071 -0.0458 220 SER A CB   
1780 O  OG   . SER A 219 ? 0.3561 0.0901 0.3418 -0.0144 -0.0030 -0.0322 220 SER A OG   
1781 N  N    . GLU A 220 ? 0.1865 0.0793 0.2486 0.0082  0.0005  -0.0070 221 GLU A N    
1782 C  CA   . GLU A 220 ? 0.2040 0.0972 0.2513 0.0030  -0.0018 -0.0245 221 GLU A CA   
1783 C  C    . GLU A 220 ? 0.2141 0.0801 0.2398 -0.0079 0.0051  -0.0133 221 GLU A C    
1784 O  O    . GLU A 220 ? 0.1951 0.1048 0.2560 -0.0006 0.0136  -0.0358 221 GLU A O    
1785 C  CB   . GLU A 220 ? 0.2528 0.1282 0.2456 -0.0123 -0.0149 -0.0531 221 GLU A CB   
1786 C  CG   . GLU A 220 ? 0.3066 0.1246 0.3092 -0.0059 -0.0084 -0.0337 221 GLU A CG   
1787 C  CD   . GLU A 220 ? 0.3299 0.1141 0.3161 -0.0340 -0.0266 -0.0423 221 GLU A CD   
1788 O  OE1  . GLU A 220 ? 0.2693 0.1528 0.2985 -0.0692 -0.0032 -0.0182 221 GLU A OE1  
1789 O  OE2  . GLU A 220 ? 0.5104 0.1740 0.4331 -0.1032 0.0182  -0.1036 221 GLU A OE2  
1790 N  N    . GLN A 221 ? 0.1831 0.0703 0.2223 -0.0131 -0.0099 -0.0113 222 GLN A N    
1791 C  CA   . GLN A 221 ? 0.1660 0.0583 0.2286 -0.0289 0.0021  -0.0059 222 GLN A CA   
1792 C  C    . GLN A 221 ? 0.1659 0.0737 0.2321 -0.0276 0.0000  0.0122  222 GLN A C    
1793 O  O    . GLN A 221 ? 0.1936 0.0810 0.2103 -0.0385 0.0030  0.0156  222 GLN A O    
1794 C  CB   . GLN A 221 ? 0.1636 0.0918 0.2194 -0.0248 -0.0126 -0.0320 222 GLN A CB   
1795 C  CG   . GLN A 221 ? 0.1690 0.1101 0.1998 -0.0241 -0.0170 -0.0215 222 GLN A CG   
1796 C  CD   . GLN A 221 ? 0.1774 0.0534 0.2075 -0.0222 -0.0192 0.0056  222 GLN A CD   
1797 O  OE1  . GLN A 221 ? 0.1946 0.0649 0.1937 -0.0130 -0.0083 -0.0053 222 GLN A OE1  
1798 N  NE2  . GLN A 221 ? 0.1625 0.0520 0.2519 -0.0091 -0.0297 0.0031  222 GLN A NE2  
1799 N  N    . VAL A 222 ? 0.1654 0.0892 0.2067 -0.0069 -0.0211 0.0187  223 VAL A N    
1800 C  CA   . VAL A 222 ? 0.1605 0.1121 0.2120 0.0050  -0.0167 0.0123  223 VAL A CA   
1801 C  C    . VAL A 222 ? 0.1504 0.1038 0.2428 0.0000  -0.0147 0.0085  223 VAL A C    
1802 O  O    . VAL A 222 ? 0.1660 0.1139 0.2423 -0.0224 0.0046  0.0189  223 VAL A O    
1803 C  CB   . VAL A 222 ? 0.1705 0.1424 0.2556 0.0121  -0.0622 0.0493  223 VAL A CB   
1804 C  CG1  . VAL A 222 ? 0.2254 0.1724 0.3035 -0.0094 -0.0096 0.0411  223 VAL A CG1  
1805 C  CG2  . VAL A 222 ? 0.1575 0.1989 0.2545 -0.0075 -0.0392 0.0084  223 VAL A CG2  
1806 N  N    . LEU A 223 ? 0.1641 0.0873 0.2646 0.0092  0.0164  -0.0110 224 LEU A N    
1807 C  CA   . LEU A 223 ? 0.2084 0.1041 0.2880 0.0005  0.0302  -0.0147 224 LEU A CA   
1808 C  C    . LEU A 223 ? 0.2021 0.1039 0.2758 -0.0064 0.0101  -0.0062 224 LEU A C    
1809 O  O    . LEU A 223 ? 0.1751 0.1513 0.3060 -0.0147 0.0310  -0.0197 224 LEU A O    
1810 C  CB   . LEU A 223 ? 0.2348 0.1324 0.3116 0.0013  0.0075  -0.0281 224 LEU A CB   
1811 C  CG   . LEU A 223 ? 0.2509 0.1501 0.2951 -0.0106 0.0204  -0.0252 224 LEU A CG   
1812 C  CD1  . LEU A 223 ? 0.2709 0.2053 0.3197 -0.0300 -0.0040 -0.0060 224 LEU A CD1  
1813 C  CD2  . LEU A 223 ? 0.2609 0.1532 0.3318 -0.0033 0.0426  -0.0382 224 LEU A CD2  
1814 N  N    . LYS A 224 ? 0.2029 0.1092 0.2421 -0.0069 0.0094  0.0035  225 LYS A N    
1815 C  CA   . LYS A 224 ? 0.2074 0.1345 0.2204 -0.0131 0.0070  0.0183  225 LYS A CA   
1816 C  C    . LYS A 224 ? 0.1920 0.1237 0.1937 -0.0066 0.0195  0.0119  225 LYS A C    
1817 O  O    . LYS A 224 ? 0.2305 0.1322 0.1910 -0.0256 0.0230  0.0093  225 LYS A O    
1818 C  CB   . LYS A 224 ? 0.2349 0.1674 0.2271 -0.0014 0.0045  0.0498  225 LYS A CB   
1819 C  CG   . LYS A 224 ? 0.2297 0.2741 0.3209 -0.0227 -0.0153 0.0089  225 LYS A CG   
1820 C  CD   . LYS A 224 ? 0.3297 0.3483 0.4044 0.0008  -0.0256 0.0003  225 LYS A CD   
1821 C  CE   . LYS A 224 ? 0.4178 0.4020 0.3925 -0.0103 -0.0354 -0.0164 225 LYS A CE   
1822 N  NZ   . LYS A 224 ? 0.3983 0.3312 0.4443 0.0015  0.0044  -0.0322 225 LYS A NZ   
1823 N  N    . PHE A 225 ? 0.1825 0.0948 0.1821 -0.0014 0.0064  -0.0023 226 PHE A N    
1824 C  CA   . PHE A 225 ? 0.1764 0.0781 0.1809 -0.0014 0.0151  -0.0203 226 PHE A CA   
1825 C  C    . PHE A 225 ? 0.1656 0.0951 0.1859 -0.0130 0.0090  -0.0175 226 PHE A C    
1826 O  O    . PHE A 225 ? 0.1805 0.0995 0.2038 -0.0181 0.0262  -0.0143 226 PHE A O    
1827 C  CB   . PHE A 225 ? 0.1466 0.1023 0.1775 -0.0013 0.0217  -0.0207 226 PHE A CB   
1828 C  CG   . PHE A 225 ? 0.1603 0.0780 0.1976 -0.0099 0.0167  -0.0061 226 PHE A CG   
1829 C  CD1  . PHE A 225 ? 0.2420 0.1344 0.2144 0.0574  0.0190  0.0017  226 PHE A CD1  
1830 C  CD2  . PHE A 225 ? 0.1582 0.1690 0.2256 -0.0370 0.0298  -0.0462 226 PHE A CD2  
1831 C  CE1  . PHE A 225 ? 0.1833 0.1408 0.2477 0.0179  0.0269  0.0228  226 PHE A CE1  
1832 C  CE2  . PHE A 225 ? 0.1652 0.1966 0.2571 0.0078  0.0170  -0.0742 226 PHE A CE2  
1833 C  CZ   . PHE A 225 ? 0.1892 0.1168 0.2807 -0.0091 -0.0093 -0.0469 226 PHE A CZ   
1834 N  N    . ARG A 226 ? 0.1639 0.0843 0.1895 -0.0073 0.0214  -0.0184 227 ARG A N    
1835 C  CA   . ARG A 226 ? 0.1650 0.1117 0.1892 -0.0061 0.0235  -0.0022 227 ARG A CA   
1836 C  C    . ARG A 226 ? 0.1697 0.1087 0.2089 -0.0225 0.0211  -0.0051 227 ARG A C    
1837 O  O    . ARG A 226 ? 0.1620 0.1680 0.2319 0.0040  0.0202  -0.0007 227 ARG A O    
1838 C  CB   . ARG A 226 ? 0.1780 0.1053 0.2083 -0.0036 0.0303  0.0052  227 ARG A CB   
1839 C  CG   . ARG A 226 ? 0.1679 0.0934 0.2039 0.0080  0.0117  0.0149  227 ARG A CG   
1840 C  CD   . ARG A 226 ? 0.2413 0.0970 0.2355 -0.0161 0.0238  0.0101  227 ARG A CD   
1841 N  NE   . ARG A 226 ? 0.1706 0.0960 0.2323 -0.0222 -0.0054 0.0198  227 ARG A NE   
1842 C  CZ   . ARG A 226 ? 0.1792 0.0862 0.2064 -0.0103 0.0098  -0.0289 227 ARG A CZ   
1843 N  NH1  . ARG A 226 ? 0.2626 0.1075 0.2821 -0.0478 -0.0231 -0.0487 227 ARG A NH1  
1844 N  NH2  . ARG A 226 ? 0.2582 0.0724 0.2340 -0.0525 0.0319  -0.0145 227 ARG A NH2  
1845 N  N    . LYS A 227 ? 0.2208 0.1198 0.1817 -0.0219 0.0311  -0.0246 228 LYS A N    
1846 C  CA   . LYS A 227 ? 0.2457 0.1275 0.1822 -0.0308 0.0329  -0.0215 228 LYS A CA   
1847 C  C    . LYS A 227 ? 0.2154 0.1198 0.1679 -0.0192 0.0411  -0.0271 228 LYS A C    
1848 O  O    . LYS A 227 ? 0.2634 0.1658 0.1806 -0.0267 0.0446  -0.0347 228 LYS A O    
1849 C  CB   . LYS A 227 ? 0.2883 0.1801 0.2025 -0.0358 -0.0038 -0.0205 228 LYS A CB   
1850 C  CG   . LYS A 227 ? 0.3190 0.2193 0.2583 -0.0450 0.0053  -0.0313 228 LYS A CG   
1851 C  CD   . LYS A 227 ? 0.3521 0.3460 0.3874 -0.0295 -0.0159 -0.0226 228 LYS A CD   
1852 C  CE   . LYS A 227 ? 0.4229 0.3820 0.4565 -0.0252 0.0013  -0.0204 228 LYS A CE   
1853 N  NZ   . LYS A 227 ? 0.4476 0.4845 0.4636 -0.0221 -0.0095 -0.0294 228 LYS A NZ   
1854 N  N    . LEU A 228 ? 0.2054 0.0932 0.1765 -0.0300 0.0271  -0.0349 229 LEU A N    
1855 C  CA   . LEU A 228 ? 0.1947 0.0974 0.1992 -0.0231 0.0261  -0.0249 229 LEU A CA   
1856 C  C    . LEU A 228 ? 0.2168 0.1140 0.2004 -0.0207 0.0324  -0.0231 229 LEU A C    
1857 O  O    . LEU A 228 ? 0.2125 0.1098 0.2071 -0.0031 0.0193  -0.0224 229 LEU A O    
1858 C  CB   . LEU A 228 ? 0.1907 0.1013 0.1857 0.0020  0.0288  -0.0252 229 LEU A CB   
1859 C  CG   . LEU A 228 ? 0.1934 0.1203 0.1827 -0.0025 0.0244  -0.0043 229 LEU A CG   
1860 C  CD1  . LEU A 228 ? 0.2115 0.1360 0.1908 -0.0062 0.0187  -0.0434 229 LEU A CD1  
1861 C  CD2  . LEU A 228 ? 0.2764 0.1198 0.2032 0.0006  0.0335  0.0342  229 LEU A CD2  
1862 N  N    . ASN A 229 ? 0.2267 0.1344 0.2060 -0.0348 0.0381  -0.0159 230 ASN A N    
1863 C  CA   . ASN A 229 ? 0.2101 0.1699 0.1825 -0.0271 0.0245  -0.0309 230 ASN A CA   
1864 C  C    . ASN A 229 ? 0.2230 0.1434 0.1959 -0.0051 0.0268  -0.0090 230 ASN A C    
1865 O  O    . ASN A 229 ? 0.2536 0.1386 0.2239 -0.0209 0.0336  0.0060  230 ASN A O    
1866 C  CB   . ASN A 229 ? 0.2315 0.1485 0.1931 -0.0216 0.0293  -0.0076 230 ASN A CB   
1867 C  CG   . ASN A 229 ? 0.1917 0.1833 0.2328 -0.0370 0.0332  -0.0316 230 ASN A CG   
1868 O  OD1  . ASN A 229 ? 0.3517 0.2240 0.2233 -0.0219 0.0756  -0.0567 230 ASN A OD1  
1869 N  ND2  . ASN A 229 ? 0.2483 0.1460 0.2334 -0.0249 0.0426  -0.0468 230 ASN A ND2  
1870 N  N    . PHE A 230 ? 0.1895 0.1694 0.1858 -0.0596 0.0290  -0.0152 231 PHE A N    
1871 C  CA   . PHE A 230 ? 0.2300 0.1439 0.1887 -0.0667 0.0273  -0.0017 231 PHE A CA   
1872 C  C    . PHE A 230 ? 0.2441 0.2044 0.2036 -0.0593 0.0362  -0.0168 231 PHE A C    
1873 O  O    . PHE A 230 ? 0.2472 0.1973 0.2293 -0.0848 0.0308  -0.0021 231 PHE A O    
1874 C  CB   . PHE A 230 ? 0.2343 0.1458 0.1907 -0.0380 0.0219  0.0060  231 PHE A CB   
1875 C  CG   . PHE A 230 ? 0.2305 0.1470 0.2075 -0.0598 0.0434  -0.0046 231 PHE A CG   
1876 C  CD1  . PHE A 230 ? 0.1736 0.1732 0.1987 -0.0291 0.0141  -0.0066 231 PHE A CD1  
1877 C  CD2  . PHE A 230 ? 0.2336 0.1421 0.2079 -0.0352 0.0222  -0.0231 231 PHE A CD2  
1878 C  CE1  . PHE A 230 ? 0.1783 0.1395 0.2144 -0.0647 0.0121  -0.0039 231 PHE A CE1  
1879 C  CE2  . PHE A 230 ? 0.2498 0.1551 0.2108 -0.0189 0.0201  -0.0153 231 PHE A CE2  
1880 C  CZ   . PHE A 230 ? 0.1925 0.1548 0.2179 -0.0372 -0.0038 -0.0271 231 PHE A CZ   
1881 N  N    . ASN A 231 ? 0.2082 0.1935 0.1697 -0.0619 0.0504  -0.0133 232 ASN A N    
1882 C  CA   . ASN A 231 ? 0.2425 0.1731 0.2013 -0.0462 0.0560  -0.0100 232 ASN A CA   
1883 C  C    . ASN A 231 ? 0.2336 0.2128 0.2105 -0.0314 0.0530  -0.0029 232 ASN A C    
1884 O  O    . ASN A 231 ? 0.2598 0.1877 0.2294 -0.0165 0.0426  -0.0154 232 ASN A O    
1885 C  CB   . ASN A 231 ? 0.2036 0.2017 0.2373 -0.0389 0.0838  -0.0211 232 ASN A CB   
1886 C  CG   . ASN A 231 ? 0.1907 0.1759 0.2127 -0.0219 0.0343  0.0024  232 ASN A CG   
1887 O  OD1  . ASN A 231 ? 0.2679 0.1629 0.2417 -0.0222 0.0795  -0.0291 232 ASN A OD1  
1888 N  ND2  . ASN A 231 ? 0.2412 0.2919 0.2156 0.0473  0.0516  -0.0022 232 ASN A ND2  
1889 N  N    . GLY A 232 ? 0.2661 0.1907 0.2181 -0.0331 0.0491  0.0180  233 GLY A N    
1890 C  CA   . GLY A 232 ? 0.2482 0.2027 0.2435 -0.0138 0.0394  0.0244  233 GLY A CA   
1891 C  C    . GLY A 232 ? 0.2575 0.1904 0.2392 0.0013  0.0252  0.0317  233 GLY A C    
1892 O  O    . GLY A 232 ? 0.2392 0.2011 0.2655 0.0085  0.0744  0.0297  233 GLY A O    
1893 N  N    . GLU A 233 ? 0.2511 0.2019 0.2292 -0.0008 0.0298  0.0218  234 GLU A N    
1894 C  CA   . GLU A 233 ? 0.2625 0.2318 0.2410 0.0124  0.0251  0.0169  234 GLU A CA   
1895 C  C    . GLU A 233 ? 0.2572 0.2159 0.2424 0.0056  0.0274  0.0080  234 GLU A C    
1896 O  O    . GLU A 233 ? 0.2684 0.2519 0.2554 -0.0116 0.0283  0.0201  234 GLU A O    
1897 C  CB   . GLU A 233 ? 0.2561 0.2204 0.2279 0.0195  0.0179  0.0309  234 GLU A CB   
1898 C  CG   . GLU A 233 ? 0.2510 0.2284 0.2464 -0.0366 0.0334  0.0301  234 GLU A CG   
1899 C  CD   . GLU A 233 ? 0.3624 0.3100 0.3694 0.0137  -0.0121 -0.0055 234 GLU A CD   
1900 O  OE1  . GLU A 233 ? 0.3131 0.2743 0.4336 -0.0210 0.0232  -0.0087 234 GLU A OE1  
1901 O  OE2  . GLU A 233 ? 0.3614 0.3262 0.3621 -0.0390 -0.0194 -0.0150 234 GLU A OE2  
1902 N  N    . GLY A 234 ? 0.2737 0.2510 0.2478 0.0409  0.0513  -0.0008 235 GLY A N    
1903 C  CA   . GLY A 234 ? 0.2775 0.3041 0.2959 0.0428  0.0354  0.0080  235 GLY A CA   
1904 C  C    . GLY A 234 ? 0.2489 0.3271 0.2827 0.0311  0.0340  0.0252  235 GLY A C    
1905 O  O    . GLY A 234 ? 0.2728 0.3601 0.3149 0.0561  0.0678  -0.0043 235 GLY A O    
1906 N  N    . GLU A 235 ? 0.2627 0.3199 0.2783 0.0324  0.0491  -0.0054 236 GLU A N    
1907 C  CA   . GLU A 235 ? 0.2641 0.2995 0.2865 0.0208  0.0337  0.0109  236 GLU A CA   
1908 C  C    . GLU A 235 ? 0.2938 0.3385 0.2986 0.0097  0.0440  0.0198  236 GLU A C    
1909 O  O    . GLU A 235 ? 0.3117 0.3643 0.2959 0.0149  0.0500  0.0405  236 GLU A O    
1910 C  CB   . GLU A 235 ? 0.2475 0.2941 0.3149 0.0340  0.0356  -0.0038 236 GLU A CB   
1911 C  CG   . GLU A 235 ? 0.3001 0.2584 0.2962 0.0018  0.0462  0.0292  236 GLU A CG   
1912 C  CD   . GLU A 235 ? 0.4293 0.3814 0.3713 -0.0035 0.0201  0.0050  236 GLU A CD   
1913 O  OE1  . GLU A 235 ? 0.3477 0.4324 0.4545 -0.0555 0.0604  0.0203  236 GLU A OE1  
1914 O  OE2  . GLU A 235 ? 0.5086 0.4730 0.5023 -0.0364 0.0346  0.0117  236 GLU A OE2  
1915 N  N    . PRO A 236 ? 0.2762 0.3177 0.2928 -0.0010 0.0566  0.0340  237 PRO A N    
1916 C  CA   . PRO A 236 ? 0.2745 0.3373 0.2941 0.0010  0.0698  0.0311  237 PRO A CA   
1917 C  C    . PRO A 236 ? 0.2658 0.3153 0.2658 -0.0028 0.0660  0.0163  237 PRO A C    
1918 O  O    . PRO A 236 ? 0.2326 0.2944 0.2699 0.0199  0.0574  0.0104  237 PRO A O    
1919 C  CB   . PRO A 236 ? 0.2730 0.3634 0.2956 -0.0030 0.0717  0.0293  237 PRO A CB   
1920 C  CG   . PRO A 236 ? 0.3008 0.3078 0.3277 0.0014  0.0456  0.0726  237 PRO A CG   
1921 C  CD   . PRO A 236 ? 0.3010 0.3531 0.3078 0.0116  0.0388  0.0357  237 PRO A CD   
1922 N  N    . GLU A 237 ? 0.2473 0.2985 0.2691 0.0120  0.0526  -0.0120 238 GLU A N    
1923 C  CA   . GLU A 237 ? 0.2340 0.2484 0.2519 -0.0052 0.0614  -0.0269 238 GLU A CA   
1924 C  C    . GLU A 237 ? 0.2302 0.2091 0.2541 -0.0105 0.0459  -0.0283 238 GLU A C    
1925 O  O    . GLU A 237 ? 0.2139 0.2255 0.2636 -0.0014 0.0342  -0.0226 238 GLU A O    
1926 C  CB   . GLU A 237 ? 0.2365 0.2663 0.2831 0.0087  0.0376  -0.0296 238 GLU A CB   
1927 C  CG   . GLU A 237 ? 0.2592 0.2963 0.3126 -0.0157 0.0304  -0.0394 238 GLU A CG   
1928 C  CD   . GLU A 237 ? 0.2929 0.2848 0.3351 -0.0016 0.0227  -0.0885 238 GLU A CD   
1929 O  OE1  . GLU A 237 ? 0.3810 0.3273 0.4410 -0.0196 0.0302  -0.1158 238 GLU A OE1  
1930 O  OE2  . GLU A 237 ? 0.3339 0.1803 0.3362 0.0173  0.0325  -0.0785 238 GLU A OE2  
1931 N  N    A GLU A 238 ? 0.2263 0.1994 0.2460 -0.0251 0.0408  -0.0311 239 GLU A N    
1932 N  N    B GLU A 238 ? 0.2182 0.1806 0.2247 -0.0331 0.0422  -0.0290 239 GLU A N    
1933 C  CA   A GLU A 238 ? 0.2132 0.2062 0.2483 -0.0122 0.0389  -0.0281 239 GLU A CA   
1934 C  CA   B GLU A 238 ? 0.2235 0.1900 0.2167 -0.0197 0.0419  -0.0211 239 GLU A CA   
1935 C  C    A GLU A 238 ? 0.1916 0.1703 0.2300 -0.0158 0.0510  -0.0222 239 GLU A C    
1936 C  C    B GLU A 238 ? 0.1923 0.1460 0.1999 -0.0151 0.0552  -0.0233 239 GLU A C    
1937 O  O    A GLU A 238 ? 0.1968 0.1958 0.2396 -0.0301 0.0477  -0.0208 239 GLU A O    
1938 O  O    B GLU A 238 ? 0.2110 0.1612 0.1866 -0.0258 0.0646  -0.0379 239 GLU A O    
1939 C  CB   A GLU A 238 ? 0.1965 0.1996 0.2841 -0.0140 0.0304  -0.0206 239 GLU A CB   
1940 C  CB   B GLU A 238 ? 0.2336 0.1691 0.2244 -0.0209 0.0326  -0.0033 239 GLU A CB   
1941 C  CG   A GLU A 238 ? 0.2066 0.2047 0.2331 -0.0070 0.0145  -0.0117 239 GLU A CG   
1942 C  CG   B GLU A 238 ? 0.2075 0.1813 0.2002 -0.0076 0.0151  -0.0074 239 GLU A CG   
1943 C  CD   A GLU A 238 ? 0.2023 0.2035 0.2175 -0.0024 0.0055  -0.0022 239 GLU A CD   
1944 C  CD   B GLU A 238 ? 0.1904 0.1776 0.1851 -0.0014 0.0058  -0.0003 239 GLU A CD   
1945 O  OE1  A GLU A 238 ? 0.1982 0.2009 0.2065 -0.0015 0.0017  -0.0026 239 GLU A OE1  
1946 O  OE1  B GLU A 238 ? 0.1801 0.1737 0.1775 -0.0017 0.0029  -0.0014 239 GLU A OE1  
1947 O  OE2  A GLU A 238 ? 0.1985 0.2051 0.2129 -0.0023 0.0024  -0.0054 239 GLU A OE2  
1948 O  OE2  B GLU A 238 ? 0.1818 0.1721 0.1821 0.0016  0.0045  -0.0028 239 GLU A OE2  
1949 N  N    . LEU A 239 ? 0.1994 0.1689 0.2075 -0.0221 0.0618  -0.0296 240 LEU A N    
1950 C  CA   . LEU A 239 ? 0.1845 0.1460 0.2134 -0.0202 0.0555  -0.0139 240 LEU A CA   
1951 C  C    . LEU A 239 ? 0.1669 0.1152 0.1975 -0.0002 0.0424  -0.0070 240 LEU A C    
1952 O  O    . LEU A 239 ? 0.1938 0.1441 0.2182 -0.0043 0.0563  -0.0317 240 LEU A O    
1953 C  CB   . LEU A 239 ? 0.2331 0.0976 0.2303 0.0144  0.0241  -0.0146 240 LEU A CB   
1954 C  CG   . LEU A 239 ? 0.1876 0.1396 0.2423 0.0000  0.0317  -0.0226 240 LEU A CG   
1955 C  CD1  . LEU A 239 ? 0.2082 0.1276 0.3547 -0.0196 -0.0181 -0.0403 240 LEU A CD1  
1956 C  CD2  . LEU A 239 ? 0.2717 0.1635 0.2346 0.0421  -0.0128 -0.0387 240 LEU A CD2  
1957 N  N    . MET A 240 ? 0.1629 0.0972 0.1875 -0.0024 0.0637  -0.0054 241 MET A N    
1958 C  CA   . MET A 240 ? 0.1935 0.0972 0.1805 0.0062  0.0485  -0.0057 241 MET A CA   
1959 C  C    . MET A 240 ? 0.1725 0.1176 0.1693 -0.0170 0.0337  -0.0187 241 MET A C    
1960 O  O    . MET A 240 ? 0.1810 0.1122 0.1869 -0.0086 0.0393  -0.0045 241 MET A O    
1961 C  CB   . MET A 240 ? 0.1828 0.1198 0.1941 0.0145  0.0388  -0.0145 241 MET A CB   
1962 C  CG   . MET A 240 ? 0.1784 0.0951 0.1948 -0.0015 0.0507  -0.0179 241 MET A CG   
1963 S  SD   . MET A 240 ? 0.2245 0.0931 0.2187 -0.0173 0.0571  -0.0097 241 MET A SD   
1964 C  CE   . MET A 240 ? 0.2622 0.1074 0.1990 -0.0668 0.0537  0.0089  241 MET A CE   
1965 N  N    . VAL A 241 ? 0.1771 0.0811 0.1543 -0.0207 0.0347  -0.0050 242 VAL A N    
1966 C  CA   . VAL A 241 ? 0.1920 0.0514 0.1568 -0.0201 0.0258  -0.0231 242 VAL A CA   
1967 C  C    . VAL A 241 ? 0.1513 0.0835 0.1817 0.0049  0.0074  -0.0091 242 VAL A C    
1968 O  O    . VAL A 241 ? 0.1344 0.0932 0.1904 -0.0056 0.0271  -0.0201 242 VAL A O    
1969 C  CB   . VAL A 241 ? 0.1349 0.1039 0.1941 -0.0199 0.0391  -0.0355 242 VAL A CB   
1970 C  CG1  . VAL A 241 ? 0.1774 0.0984 0.2100 -0.0402 0.0171  -0.0439 242 VAL A CG1  
1971 C  CG2  . VAL A 241 ? 0.1751 0.0931 0.2125 0.0160  0.0429  -0.0102 242 VAL A CG2  
1972 N  N    . ASP A 242 ? 0.1481 0.0718 0.1446 0.0012  0.0223  -0.0148 243 ASP A N    
1973 C  CA   . ASP A 242 ? 0.1307 0.0482 0.1839 0.0172  0.0260  -0.0181 243 ASP A CA   
1974 C  C    . ASP A 242 ? 0.1020 0.0550 0.1795 -0.0273 0.0156  -0.0124 243 ASP A C    
1975 O  O    . ASP A 242 ? 0.1192 0.0758 0.2155 -0.0090 0.0146  -0.0212 243 ASP A O    
1976 C  CB   . ASP A 242 ? 0.0968 0.0558 0.2265 0.0013  0.0045  -0.0140 243 ASP A CB   
1977 C  CG   . ASP A 242 ? 0.1284 0.0550 0.2163 0.0119  0.0282  -0.0145 243 ASP A CG   
1978 O  OD1  . ASP A 242 ? 0.1607 0.0588 0.1919 0.0124  0.0176  -0.0266 243 ASP A OD1  
1979 O  OD2  . ASP A 242 ? 0.1557 0.0604 0.2624 0.0167  0.0489  -0.0422 243 ASP A OD2  
1980 N  N    . ASN A 243 ? 0.0996 0.0422 0.1786 -0.0003 0.0223  -0.0206 244 ASN A N    
1981 C  CA   . ASN A 243 ? 0.1272 0.0672 0.1586 -0.0116 0.0093  -0.0157 244 ASN A CA   
1982 C  C    . ASN A 243 ? 0.1045 0.0406 0.1734 -0.0193 0.0200  -0.0123 244 ASN A C    
1983 O  O    . ASN A 243 ? 0.1002 0.0673 0.1956 0.0113  0.0258  0.0044  244 ASN A O    
1984 C  CB   . ASN A 243 ? 0.1179 0.0738 0.1736 -0.0089 0.0087  -0.0048 244 ASN A CB   
1985 C  CG   . ASN A 243 ? 0.1142 0.0703 0.1923 -0.0528 0.0329  0.0004  244 ASN A CG   
1986 O  OD1  . ASN A 243 ? 0.1109 0.0788 0.2121 -0.0169 0.0248  0.0148  244 ASN A OD1  
1987 N  ND2  . ASN A 243 ? 0.1806 0.1213 0.2154 -0.0330 -0.0171 0.0524  244 ASN A ND2  
1988 N  N    . TRP A 244 ? 0.1066 0.0555 0.1595 -0.0220 0.0150  0.0032  245 TRP A N    
1989 C  CA   . TRP A 244 ? 0.0788 0.0533 0.1641 -0.0194 0.0078  -0.0183 245 TRP A CA   
1990 C  C    . TRP A 244 ? 0.0844 0.0326 0.1811 -0.0063 0.0105  -0.0032 245 TRP A C    
1991 O  O    . TRP A 244 ? 0.0970 0.0657 0.2008 0.0113  0.0092  -0.0224 245 TRP A O    
1992 C  CB   . TRP A 244 ? 0.0941 0.0281 0.1920 0.0074  0.0319  -0.0138 245 TRP A CB   
1993 C  CG   . TRP A 244 ? 0.0833 0.0479 0.1724 0.0011  0.0119  0.0057  245 TRP A CG   
1994 C  CD1  . TRP A 244 ? 0.1185 0.0438 0.1919 0.0014  0.0181  -0.0259 245 TRP A CD1  
1995 C  CD2  . TRP A 244 ? 0.0964 0.0311 0.1602 -0.0112 0.0234  0.0056  245 TRP A CD2  
1996 N  NE1  . TRP A 244 ? 0.0938 0.0477 0.1864 0.0112  0.0337  -0.0030 245 TRP A NE1  
1997 C  CE2  . TRP A 244 ? 0.1162 0.0673 0.1504 -0.0071 0.0288  -0.0186 245 TRP A CE2  
1998 C  CE3  . TRP A 244 ? 0.1040 0.0783 0.1670 0.0018  0.0093  -0.0004 245 TRP A CE3  
1999 C  CZ2  . TRP A 244 ? 0.1215 0.0717 0.1862 -0.0012 -0.0194 0.0260  245 TRP A CZ2  
2000 C  CZ3  . TRP A 244 ? 0.1533 0.0881 0.1786 0.0499  0.0144  0.0299  245 TRP A CZ3  
2001 C  CH2  . TRP A 244 ? 0.1443 0.0544 0.2065 0.0448  0.0072  0.0023  245 TRP A CH2  
2002 N  N    . ARG A 245 ? 0.1116 0.0483 0.1389 -0.0130 0.0040  -0.0174 246 ARG A N    
2003 C  CA   . ARG A 245 ? 0.1061 0.0671 0.1579 -0.0343 0.0104  -0.0151 246 ARG A CA   
2004 C  C    . ARG A 245 ? 0.0712 0.0701 0.1612 -0.0032 0.0123  -0.0228 246 ARG A C    
2005 O  O    . ARG A 245 ? 0.0749 0.0699 0.1949 -0.0149 0.0186  -0.0133 246 ARG A O    
2006 C  CB   . ARG A 245 ? 0.0968 0.0755 0.1782 -0.0128 0.0167  -0.0436 246 ARG A CB   
2007 C  CG   . ARG A 245 ? 0.0767 0.0678 0.1812 -0.0250 -0.0053 -0.0420 246 ARG A CG   
2008 C  CD   . ARG A 245 ? 0.0992 0.0701 0.2041 -0.0394 0.0044  -0.0414 246 ARG A CD   
2009 N  NE   . ARG A 245 ? 0.0718 0.0809 0.2270 -0.0358 0.0060  -0.0605 246 ARG A NE   
2010 C  CZ   . ARG A 245 ? 0.0820 0.0458 0.1967 -0.0334 0.0148  -0.0200 246 ARG A CZ   
2011 N  NH1  . ARG A 245 ? 0.0656 0.0794 0.2139 -0.0032 0.0256  -0.0171 246 ARG A NH1  
2012 N  NH2  . ARG A 245 ? 0.0453 0.1230 0.2546 -0.0313 0.0015  -0.0231 246 ARG A NH2  
2013 N  N    . PRO A 246 ? 0.1052 0.0685 0.1808 0.0066  0.0199  -0.0041 247 PRO A N    
2014 C  CA   . PRO A 246 ? 0.1030 0.0606 0.1745 0.0167  0.0349  0.0020  247 PRO A CA   
2015 C  C    . PRO A 246 ? 0.1116 0.0475 0.1563 0.0152  0.0192  0.0018  247 PRO A C    
2016 O  O    . PRO A 246 ? 0.1185 0.0488 0.2074 0.0044  0.0087  -0.0003 247 PRO A O    
2017 C  CB   . PRO A 246 ? 0.1575 0.1383 0.2216 0.0663  0.0301  -0.0013 247 PRO A CB   
2018 C  CG   . PRO A 246 ? 0.1626 0.1849 0.2813 0.0410  0.0160  0.0582  247 PRO A CG   
2019 C  CD   . PRO A 246 ? 0.0696 0.0736 0.2441 0.0373  0.0248  0.0013  247 PRO A CD   
2020 N  N    . ALA A 247 ? 0.1315 0.0765 0.1697 0.0207  0.0227  0.0156  248 ALA A N    
2021 C  CA   . ALA A 247 ? 0.1437 0.0620 0.1643 0.0095  0.0284  -0.0046 248 ALA A CA   
2022 C  C    . ALA A 247 ? 0.1666 0.0589 0.1988 0.0250  0.0079  -0.0046 248 ALA A C    
2023 O  O    . ALA A 247 ? 0.1649 0.0637 0.2111 0.0396  0.0021  -0.0006 248 ALA A O    
2024 C  CB   . ALA A 247 ? 0.1799 0.0987 0.1783 0.0315  0.0386  0.0238  248 ALA A CB   
2025 N  N    . GLN A 248 ? 0.1414 0.0574 0.1799 0.0200  -0.0054 -0.0058 249 GLN A N    
2026 C  CA   . GLN A 248 ? 0.1143 0.0918 0.1859 0.0316  -0.0106 -0.0074 249 GLN A CA   
2027 C  C    . GLN A 248 ? 0.1137 0.1082 0.1842 0.0365  -0.0128 -0.0033 249 GLN A C    
2028 O  O    . GLN A 248 ? 0.1050 0.1035 0.1959 0.0285  0.0055  -0.0013 249 GLN A O    
2029 C  CB   . GLN A 248 ? 0.1737 0.0615 0.2193 0.0458  -0.0011 -0.0067 249 GLN A CB   
2030 C  CG   . GLN A 248 ? 0.1215 0.1045 0.1970 0.0026  0.0243  0.0047  249 GLN A CG   
2031 C  CD   . GLN A 248 ? 0.0959 0.1362 0.1817 -0.0088 0.0286  -0.0006 249 GLN A CD   
2032 O  OE1  . GLN A 248 ? 0.1139 0.1701 0.2569 -0.0391 0.0081  -0.0340 249 GLN A OE1  
2033 N  NE2  . GLN A 248 ? 0.1420 0.1404 0.1747 0.0300  0.0102  -0.0146 249 GLN A NE2  
2034 N  N    . PRO A 249 ? 0.1340 0.1741 0.1960 0.0446  -0.0056 -0.0060 250 PRO A N    
2035 C  CA   . PRO A 249 ? 0.1278 0.1975 0.1946 0.0573  -0.0014 -0.0138 250 PRO A CA   
2036 C  C    . PRO A 249 ? 0.1306 0.1519 0.2000 0.0400  -0.0078 0.0110  250 PRO A C    
2037 O  O    . PRO A 249 ? 0.1416 0.1618 0.2046 0.0492  -0.0121 0.0116  250 PRO A O    
2038 C  CB   . PRO A 249 ? 0.1586 0.2582 0.2191 0.0469  -0.0225 -0.0134 250 PRO A CB   
2039 C  CG   . PRO A 249 ? 0.1817 0.2944 0.2270 0.0429  -0.0487 -0.0300 250 PRO A CG   
2040 C  CD   . PRO A 249 ? 0.1411 0.2230 0.2480 0.0392  -0.0362 -0.0076 250 PRO A CD   
2041 N  N    . LEU A 250 ? 0.1494 0.1381 0.2025 0.0507  0.0104  -0.0031 251 LEU A N    
2042 C  CA   . LEU A 250 ? 0.1344 0.1093 0.2011 0.0301  0.0120  -0.0126 251 LEU A CA   
2043 C  C    . LEU A 250 ? 0.1745 0.1286 0.2027 0.0278  -0.0084 -0.0059 251 LEU A C    
2044 O  O    . LEU A 250 ? 0.1554 0.1121 0.2488 0.0202  -0.0152 0.0190  251 LEU A O    
2045 C  CB   . LEU A 250 ? 0.1935 0.1250 0.2118 0.0320  0.0154  0.0040  251 LEU A CB   
2046 C  CG   . LEU A 250 ? 0.2047 0.1305 0.2146 0.0150  0.0348  0.0072  251 LEU A CG   
2047 C  CD1  . LEU A 250 ? 0.1361 0.1748 0.2498 0.0139  -0.0196 -0.0346 251 LEU A CD1  
2048 C  CD2  . LEU A 250 ? 0.2189 0.1715 0.2680 -0.0534 0.0466  0.0043  251 LEU A CD2  
2049 N  N    . LYS A 251 ? 0.1671 0.1505 0.2046 0.0439  -0.0274 -0.0134 252 LYS A N    
2050 C  CA   . LYS A 251 ? 0.1705 0.1699 0.2029 0.0302  -0.0169 -0.0191 252 LYS A CA   
2051 C  C    . LYS A 251 ? 0.1668 0.1658 0.2577 0.0349  -0.0161 -0.0171 252 LYS A C    
2052 O  O    . LYS A 251 ? 0.2260 0.2366 0.2501 0.0099  0.0104  -0.0152 252 LYS A O    
2053 C  CB   . LYS A 251 ? 0.1812 0.1581 0.2323 0.0295  -0.0038 -0.0324 252 LYS A CB   
2054 C  CG   . LYS A 251 ? 0.1583 0.2208 0.2906 -0.0146 -0.0057 -0.0448 252 LYS A CG   
2055 C  CD   . LYS A 251 ? 0.1766 0.2304 0.3305 0.0005  0.0126  -0.0142 252 LYS A CD   
2056 C  CE   . LYS A 251 ? 0.1283 0.2756 0.3601 0.0415  0.0147  0.0255  252 LYS A CE   
2057 N  NZ   . LYS A 251 ? 0.2090 0.3335 0.4133 -0.0221 0.0354  0.0032  252 LYS A NZ   
2058 N  N    . ASN A 252 ? 0.1753 0.1967 0.2212 0.0453  -0.0256 -0.0483 253 ASN A N    
2059 C  CA   . ASN A 252 ? 0.2246 0.2782 0.2866 0.0283  -0.0156 -0.0318 253 ASN A CA   
2060 C  C    . ASN A 252 ? 0.2317 0.2352 0.2977 0.0358  -0.0229 -0.0230 253 ASN A C    
2061 O  O    . ASN A 252 ? 0.2939 0.2422 0.3273 0.0387  -0.0214 -0.0024 253 ASN A O    
2062 C  CB   . ASN A 252 ? 0.2548 0.2872 0.2985 0.0135  -0.0326 -0.0375 253 ASN A CB   
2063 C  CG   . ASN A 252 ? 0.3235 0.3695 0.3679 0.0177  0.0006  -0.0284 253 ASN A CG   
2064 O  OD1  . ASN A 252 ? 0.4870 0.4839 0.4047 -0.0125 0.0201  0.0069  253 ASN A OD1  
2065 N  ND2  . ASN A 252 ? 0.3816 0.3888 0.4462 0.0023  -0.0121 -0.0218 253 ASN A ND2  
2066 N  N    . ARG A 253 ? 0.1317 0.2314 0.2279 0.0313  -0.0034 -0.0192 254 ARG A N    
2067 C  CA   . ARG A 253 ? 0.1293 0.1446 0.2043 0.0334  0.0053  -0.0149 254 ARG A CA   
2068 C  C    . ARG A 253 ? 0.1729 0.1442 0.2150 0.0311  0.0165  -0.0272 254 ARG A C    
2069 O  O    . ARG A 253 ? 0.2071 0.1619 0.2797 0.0364  0.0610  0.0148  254 ARG A O    
2070 C  CB   . ARG A 253 ? 0.1388 0.1006 0.1936 0.0248  -0.0008 -0.0035 254 ARG A CB   
2071 C  CG   . ARG A 253 ? 0.1685 0.0853 0.1722 0.0066  0.0015  -0.0210 254 ARG A CG   
2072 C  CD   . ARG A 253 ? 0.1656 0.0953 0.1677 0.0363  0.0367  -0.0182 254 ARG A CD   
2073 N  NE   . ARG A 253 ? 0.1383 0.0861 0.1738 0.0353  0.0122  -0.0146 254 ARG A NE   
2074 C  CZ   . ARG A 253 ? 0.0908 0.0755 0.1605 -0.0026 0.0205  -0.0107 254 ARG A CZ   
2075 N  NH1  . ARG A 253 ? 0.1015 0.0644 0.1883 0.0000  0.0017  0.0135  254 ARG A NH1  
2076 N  NH2  . ARG A 253 ? 0.1120 0.0821 0.1757 0.0201  0.0100  -0.0126 254 ARG A NH2  
2077 N  N    . GLN A 254 ? 0.1476 0.1770 0.2313 0.0119  0.0170  -0.0508 255 GLN A N    
2078 C  CA   . GLN A 254 ? 0.2027 0.2109 0.2171 0.0065  -0.0103 -0.0521 255 GLN A CA   
2079 C  C    . GLN A 254 ? 0.1893 0.1510 0.2287 0.0083  -0.0334 -0.0179 255 GLN A C    
2080 O  O    . GLN A 254 ? 0.2545 0.1558 0.2694 -0.0042 -0.0433 -0.0094 255 GLN A O    
2081 C  CB   . GLN A 254 ? 0.2481 0.2621 0.2343 0.0080  0.0155  -0.0457 255 GLN A CB   
2082 C  CG   . GLN A 254 ? 0.3468 0.3310 0.3428 -0.0288 0.0171  -0.0388 255 GLN A CG   
2083 C  CD   . GLN A 254 ? 0.4714 0.4007 0.3927 -0.0307 0.0376  -0.0396 255 GLN A CD   
2084 O  OE1  . GLN A 254 ? 0.5611 0.4180 0.4993 -0.0264 0.0473  -0.0210 255 GLN A OE1  
2085 N  NE2  . GLN A 254 ? 0.5265 0.4000 0.3721 -0.0443 0.0223  -0.0204 255 GLN A NE2  
2086 N  N    . ILE A 255 ? 0.1514 0.1276 0.1973 -0.0221 0.0049  -0.0333 256 ILE A N    
2087 C  CA   . ILE A 255 ? 0.1300 0.1229 0.1782 0.0142  0.0282  -0.0145 256 ILE A CA   
2088 C  C    . ILE A 255 ? 0.1162 0.1177 0.1657 0.0166  0.0291  0.0177  256 ILE A C    
2089 O  O    . ILE A 255 ? 0.1406 0.1170 0.1978 0.0230  0.0263  0.0302  256 ILE A O    
2090 C  CB   . ILE A 255 ? 0.1506 0.1231 0.1831 -0.0070 0.0299  -0.0340 256 ILE A CB   
2091 C  CG1  . ILE A 255 ? 0.1244 0.0902 0.2342 0.0393  0.0283  -0.0223 256 ILE A CG1  
2092 C  CG2  . ILE A 255 ? 0.1555 0.1436 0.1896 0.0057  0.0092  0.0078  256 ILE A CG2  
2093 C  CD1  . ILE A 255 ? 0.2114 0.1266 0.2179 -0.0057 -0.0045 -0.0306 256 ILE A CD1  
2094 N  N    . LYS A 256 ? 0.1138 0.1109 0.1781 0.0306  0.0038  0.0004  257 LYS A N    
2095 C  CA   . LYS A 256 ? 0.1423 0.1199 0.1836 0.0040  0.0262  -0.0093 257 LYS A CA   
2096 C  C    . LYS A 256 ? 0.1039 0.1278 0.1622 0.0031  0.0300  -0.0021 257 LYS A C    
2097 O  O    . LYS A 256 ? 0.1539 0.1425 0.1656 -0.0489 0.0247  0.0125  257 LYS A O    
2098 C  CB   . LYS A 256 ? 0.1448 0.1334 0.2181 0.0185  0.0248  -0.0300 257 LYS A CB   
2099 C  CG   . LYS A 256 ? 0.2496 0.1367 0.2916 0.0199  0.0307  -0.0457 257 LYS A CG   
2100 C  CD   . LYS A 256 ? 0.3470 0.3236 0.3606 0.0209  0.0044  -0.0302 257 LYS A CD   
2101 C  CE   . LYS A 256 ? 0.4161 0.3669 0.4721 0.0001  0.0031  -0.0507 257 LYS A CE   
2102 N  NZ   . LYS A 256 ? 0.5087 0.4882 0.5308 0.0735  0.0138  -0.0216 257 LYS A NZ   
2103 N  N    . ALA A 257 ? 0.1038 0.1421 0.1818 -0.0127 0.0346  0.0179  258 ALA A N    
2104 C  CA   . ALA A 257 ? 0.1258 0.1355 0.1945 -0.0070 0.0173  0.0092  258 ALA A CA   
2105 C  C    . ALA A 257 ? 0.1165 0.1150 0.1691 -0.0019 0.0325  0.0090  258 ALA A C    
2106 O  O    . ALA A 257 ? 0.1405 0.1854 0.1801 0.0072  0.0338  -0.0095 258 ALA A O    
2107 C  CB   . ALA A 257 ? 0.1461 0.1317 0.2385 -0.0319 0.0282  0.0387  258 ALA A CB   
2108 N  N    . SER A 258 ? 0.1086 0.1360 0.1906 -0.0026 0.0392  0.0027  259 SER A N    
2109 C  CA   . SER A 258 ? 0.1137 0.1640 0.2091 0.0008  0.0373  0.0020  259 SER A CA   
2110 C  C    . SER A 258 ? 0.1220 0.1847 0.2363 0.0025  0.0282  0.0132  259 SER A C    
2111 O  O    . SER A 258 ? 0.1555 0.2590 0.2813 0.0397  0.0478  0.0249  259 SER A O    
2112 C  CB   . SER A 258 ? 0.1637 0.1356 0.2194 0.0175  0.0027  0.0117  259 SER A CB   
2113 O  OG   . SER A 258 ? 0.1138 0.1525 0.2072 -0.0245 0.0266  -0.0095 259 SER A OG   
2114 N  N    . PHE A 259 ? 0.1123 0.1637 0.2546 -0.0206 0.0407  0.0055  260 PHE A N    
2115 C  CA   . PHE A 259 ? 0.1260 0.1782 0.2692 -0.0167 0.0303  0.0218  260 PHE A CA   
2116 C  C    . PHE A 259 ? 0.2109 0.2238 0.3004 -0.0311 0.0411  0.0368  260 PHE A C    
2117 O  O    . PHE A 259 ? 0.2605 0.1929 0.3081 -0.0155 0.0229  0.0593  260 PHE A O    
2118 C  CB   . PHE A 259 ? 0.1797 0.2161 0.2700 -0.0113 0.0422  0.0040  260 PHE A CB   
2119 C  CG   . PHE A 259 ? 0.1747 0.1800 0.2816 -0.0035 0.0300  0.0063  260 PHE A CG   
2120 C  CD1  . PHE A 259 ? 0.1341 0.1425 0.2523 -0.0212 0.0355  -0.0213 260 PHE A CD1  
2121 C  CD2  . PHE A 259 ? 0.2274 0.2112 0.2981 -0.0182 0.0411  0.0443  260 PHE A CD2  
2122 C  CE1  . PHE A 259 ? 0.1725 0.1715 0.2739 -0.0133 0.0187  -0.0187 260 PHE A CE1  
2123 C  CE2  . PHE A 259 ? 0.2512 0.1807 0.3324 -0.0280 0.0337  0.0183  260 PHE A CE2  
2124 C  CZ   . PHE A 259 ? 0.2187 0.1725 0.3553 -0.0158 0.0155  0.0175  260 PHE A CZ   
2125 N  N    . LYS A 260 ? 0.2998 0.2791 0.3370 -0.0494 0.0509  0.0606  261 LYS A N    
2126 C  CA   . LYS A 260 ? 0.4350 0.3715 0.4154 -0.0109 0.0342  0.0471  261 LYS A CA   
2127 C  C    . LYS A 260 ? 0.4764 0.4197 0.4610 -0.0026 0.0256  0.0355  261 LYS A C    
2128 O  O    . LYS A 260 ? 0.5213 0.4504 0.5102 0.0081  0.0407  0.0292  261 LYS A O    
2129 C  CB   . LYS A 260 ? 0.4239 0.3662 0.4190 -0.0148 0.0421  0.0468  261 LYS A CB   
2130 C  CG   . LYS A 260 ? 0.4573 0.3732 0.4396 -0.0355 0.0327  0.0403  261 LYS A CG   
2131 C  CD   . LYS A 260 ? 0.5239 0.4880 0.5124 -0.0081 0.0318  0.0126  261 LYS A CD   
2132 C  CE   . LYS A 260 ? 0.5551 0.5374 0.5557 0.0020  0.0289  0.0164  261 LYS A CE   
2133 N  NZ   . LYS A 260 ? 0.5793 0.5518 0.5964 0.0147  0.0212  -0.0046 261 LYS A NZ   
2134 O  OXT  . LYS A 260 ? 0.5177 0.4571 0.5197 0.0078  0.0207  0.0410  261 LYS A OXT  
2135 ZN ZN   . ZN  B .   ? 0.0984 0.0395 0.1770 -0.0084 0.0117  -0.0054 262 ZN  A ZN   
2136 O  O1   . MES C .   ? 0.2506 0.2286 0.2132 -0.0069 0.0222  0.0195  263 MES A O1   
2137 C  C2   . MES C .   ? 0.2021 0.2095 0.2190 -0.0128 -0.0010 0.0189  263 MES A C2   
2138 C  C3   . MES C .   ? 0.2653 0.1971 0.2438 -0.0137 -0.0124 -0.0104 263 MES A C3   
2139 N  N4   . MES C .   ? 0.2273 0.2036 0.2267 0.0050  -0.0123 0.0217  263 MES A N4   
2140 C  C5   . MES C .   ? 0.1614 0.0686 0.1304 0.0465  0.0259  0.0184  263 MES A C5   
2141 C  C6   . MES C .   ? 0.2164 0.1489 0.1785 -0.0152 -0.0046 -0.0123 263 MES A C6   
2142 C  C7   . MES C .   ? 0.2444 0.1877 0.2298 -0.0066 0.0058  0.0031  263 MES A C7   
2143 C  C8   . MES C .   ? 0.2939 0.2763 0.2929 0.0225  -0.0066 -0.0120 263 MES A C8   
2144 S  S    . MES C .   ? 0.3486 0.2177 0.2427 -0.0410 0.0174  -0.0729 263 MES A S    
2145 O  O1S  . MES C .   ? 0.3118 0.3404 0.3200 0.0156  -0.0031 -0.0191 263 MES A O1S  
2146 O  O2S  . MES C .   ? 0.3338 0.3311 0.3204 0.0000  0.0102  -0.0144 263 MES A O2S  
2147 O  O3S  . MES C .   ? 0.3391 0.3480 0.3037 0.0108  -0.0005 -0.0393 263 MES A O3S  
2148 S  S    . DMS D .   ? 0.2304 0.2717 0.3927 -0.0255 0.0223  -0.0275 264 DMS A S    
2149 O  O    . DMS D .   ? 0.3314 0.2658 0.4134 0.0282  0.0616  -0.0253 264 DMS A O    
2150 C  C1   . DMS D .   ? 0.3002 0.2281 0.4053 -0.0179 0.0367  -0.0115 264 DMS A C1   
2151 C  C2   . DMS D .   ? 0.2461 0.2329 0.3214 0.0366  0.0478  -0.0455 264 DMS A C2   
2152 S  S    . DMS E .   ? 0.4397 0.2943 0.4577 -0.0263 0.0102  -0.0163 265 DMS A S    
2153 O  O    . DMS E .   ? 0.4134 0.3612 0.4829 -0.0262 0.0085  -0.0140 265 DMS A O    
2154 C  C1   . DMS E .   ? 0.4462 0.2914 0.4708 -0.0002 0.0164  -0.0113 265 DMS A C1   
2155 C  C2   . DMS E .   ? 0.4067 0.4206 0.4592 -0.0215 0.0362  -0.0107 265 DMS A C2   
2156 N  N1   . E27 F .   ? 0.4272 0.4208 0.4223 0.0014  0.0001  -0.0013 266 E27 A N1   
2157 C  C2   . E27 F .   ? 0.4173 0.4038 0.4155 -0.0019 -0.0045 -0.0017 266 E27 A C2   
2158 N  N3   . E27 F .   ? 0.4241 0.4211 0.4243 -0.0003 0.0005  0.0010  266 E27 A N3   
2159 C  C4   . E27 F .   ? 0.4338 0.4295 0.4321 0.0000  -0.0007 -0.0010 266 E27 A C4   
2160 C  C5   . E27 F .   ? 0.4367 0.4359 0.4385 -0.0007 -0.0001 0.0004  266 E27 A C5   
2161 N  N6   . E27 F .   ? 0.4417 0.4403 0.4414 -0.0001 -0.0004 -0.0005 266 E27 A N6   
2162 C  C7   . E27 F .   ? 0.4430 0.4424 0.4434 -0.0002 0.0000  0.0001  266 E27 A C7   
2163 C  C8   . E27 F .   ? 0.4412 0.4388 0.4398 0.0001  -0.0006 -0.0010 266 E27 A C8   
2164 C  C9   . E27 F .   ? 0.4330 0.4314 0.4346 -0.0008 -0.0002 0.0002  266 E27 A C9   
2165 C  C10  . E27 F .   ? 0.4458 0.4443 0.4454 -0.0001 -0.0004 -0.0002 266 E27 A C10  
2166 C  C11  . E27 F .   ? 0.4463 0.4453 0.4460 0.0001  0.0000  -0.0001 266 E27 A C11  
2167 C  C12  . E27 F .   ? 0.4454 0.4448 0.4447 0.0003  0.0000  -0.0002 266 E27 A C12  
2168 C  C13  . E27 F .   ? 0.4424 0.4425 0.4429 0.0002  0.0003  0.0000  266 E27 A C13  
2169 S  S14  . E27 F .   ? 0.4050 0.3761 0.3947 0.0021  -0.0020 0.0001  266 E27 A S14  
2170 C  C15  . E27 F .   ? 0.3955 0.3213 0.3746 0.0003  -0.0228 -0.0087 266 E27 A C15  
2171 C  C16  . E27 F .   ? 0.3379 0.2099 0.3338 -0.0013 0.0238  0.0006  266 E27 A C16  
2172 O  O17  . E27 F .   ? 0.3106 0.3024 0.2842 0.0253  0.0432  0.0075  266 E27 A O17  
2173 C  C18  . E27 F .   ? 0.2664 0.1051 0.2626 -0.0292 0.0029  -0.0039 266 E27 A C18  
2174 C  C19  . E27 F .   ? 0.1416 0.1257 0.2066 -0.0126 0.0184  0.0252  266 E27 A C19  
2175 C  C20  . E27 F .   ? 0.1115 0.0820 0.2078 -0.0064 0.0240  -0.0083 266 E27 A C20  
2176 C  C21  . E27 F .   ? 0.1383 0.0768 0.2710 -0.0146 0.0333  -0.0157 266 E27 A C21  
2177 C  C22  . E27 F .   ? 0.2063 0.1075 0.2847 -0.0283 0.0133  0.0108  266 E27 A C22  
2178 C  C23  . E27 F .   ? 0.2149 0.1195 0.2814 -0.0391 0.0279  0.0322  266 E27 A C23  
2179 S  S24  . E27 F .   ? 0.1317 0.0438 0.1861 -0.0122 0.0202  -0.0070 266 E27 A S24  
2180 O  O25  . E27 F .   ? 0.1104 0.0568 0.2143 -0.0067 0.0150  -0.0138 266 E27 A O25  
2181 CL CL26 . E27 F .   ? 0.1291 0.0598 0.3189 -0.0004 0.0099  -0.0393 266 E27 A CL26 
2182 O  O27  . E27 F .   ? 0.0934 0.0662 0.1819 0.0088  0.0115  -0.0118 266 E27 A O27  
2183 N  N28  . E27 F .   ? 0.1160 0.0384 0.2104 -0.0185 0.0506  -0.0093 266 E27 A N28  
2184 O  O    . HOH G .   ? 0.2555 0.1884 0.4032 0.0052  -0.0613 0.0396  126 HOH A O    
2185 O  O    . HOH G .   ? 0.1382 0.0549 0.1937 0.0065  0.0015  -0.0144 267 HOH A O    
2186 O  O    . HOH G .   ? 0.1547 0.0536 0.2163 -0.0272 0.0350  -0.0152 268 HOH A O    
2187 O  O    . HOH G .   ? 0.0971 0.0961 0.2943 -0.0104 0.0225  -0.0373 269 HOH A O    
2188 O  O    . HOH G .   ? 0.0811 0.0684 0.1983 -0.0266 0.0265  -0.0034 270 HOH A O    
2189 O  O    . HOH G .   ? 0.2163 0.0761 0.2670 -0.0167 0.0062  -0.0214 271 HOH A O    
2190 O  O    . HOH G .   ? 0.1106 0.1577 0.2898 0.0103  0.0218  -0.0294 272 HOH A O    
2191 O  O    . HOH G .   ? 0.0927 0.0732 0.1880 -0.0088 0.0098  -0.0042 273 HOH A O    
2192 O  O    . HOH G .   ? 0.1501 0.0736 0.2575 0.0019  -0.0042 0.0262  274 HOH A O    
2193 O  O    . HOH G .   ? 0.2146 0.1693 0.3564 0.0018  -0.0910 -0.0386 275 HOH A O    
2194 O  O    . HOH G .   ? 0.2923 0.1080 0.2435 0.0019  -0.0792 0.0147  276 HOH A O    
2195 O  O    . HOH G .   ? 0.1288 0.1273 0.2334 0.0178  -0.0278 0.0230  277 HOH A O    
2196 O  O    . HOH G .   ? 0.1139 0.0832 0.2014 0.0110  0.0160  -0.0085 278 HOH A O    
2197 O  O    . HOH G .   ? 0.2933 0.1907 0.3473 0.0568  0.0856  0.0459  279 HOH A O    
2198 O  O    . HOH G .   ? 0.1796 0.0927 0.2574 0.0110  -0.0031 -0.0135 280 HOH A O    
2199 O  O    . HOH G .   ? 0.2305 0.1588 0.2796 0.0104  -0.0310 -0.0048 281 HOH A O    
2200 O  O    . HOH G .   ? 0.1702 0.1385 0.2572 0.0011  -0.0271 0.0152  282 HOH A O    
2201 O  O    . HOH G .   ? 0.1745 0.2008 0.2351 -0.0013 -0.0432 0.0356  283 HOH A O    
2202 O  O    . HOH G .   ? 0.2723 0.1953 0.2665 -0.0322 0.0938  -0.0578 284 HOH A O    
2203 O  O    . HOH G .   ? 0.1052 0.0759 0.2223 0.0148  0.0100  0.0025  285 HOH A O    
2204 O  O    . HOH G .   ? 0.1540 0.2623 0.3748 -0.0266 -0.0067 0.0063  286 HOH A O    
2205 O  O    . HOH G .   ? 0.1424 0.0731 0.1973 -0.0036 0.0041  -0.0206 287 HOH A O    
2206 O  O    . HOH G .   ? 0.1583 0.1300 0.3842 -0.0246 -0.0312 0.0026  288 HOH A O    
2207 O  O    . HOH G .   ? 0.3269 0.1809 0.2955 -0.0582 -0.0458 -0.0210 289 HOH A O    
2208 O  O    . HOH G .   ? 0.1044 0.1402 0.3244 -0.0320 0.0124  -0.0026 290 HOH A O    
2209 O  O    . HOH G .   ? 0.1704 0.1538 0.2800 0.0342  -0.0012 0.0002  291 HOH A O    
2210 O  O    . HOH G .   ? 0.2111 0.0778 0.2846 -0.0262 0.0097  -0.0036 292 HOH A O    
2211 O  O    . HOH G .   ? 0.1874 0.3635 0.4225 -0.0120 0.0116  0.0244  293 HOH A O    
2212 O  O    . HOH G .   ? 0.1195 0.1551 0.3786 -0.0171 0.0070  -0.0062 294 HOH A O    
2213 O  O    . HOH G .   ? 0.2675 0.1570 0.2791 0.0344  0.0776  0.1025  295 HOH A O    
2214 O  O    . HOH G .   ? 0.2480 0.1832 0.3219 0.0757  -0.0287 0.0023  296 HOH A O    
2215 O  O    . HOH G .   ? 0.3768 0.1892 0.5692 -0.0379 0.0264  0.0328  297 HOH A O    
2216 O  O    . HOH G .   ? 0.2742 0.1533 0.2706 0.0136  -0.0346 -0.0100 298 HOH A O    
2217 O  O    . HOH G .   ? 0.3025 0.1717 0.2927 -0.0204 -0.0162 -0.0537 299 HOH A O    
2218 O  O    . HOH G .   ? 0.3148 0.2913 0.3746 0.0365  -0.0198 0.0431  300 HOH A O    
2219 O  O    . HOH G .   ? 0.4329 0.2116 0.3702 -0.0187 0.0090  -0.0233 301 HOH A O    
2220 O  O    . HOH G .   ? 0.2024 0.0840 0.2970 -0.0100 0.0015  0.0099  302 HOH A O    
2221 O  O    . HOH G .   ? 0.3343 0.2760 0.3477 -0.1089 -0.0615 0.1166  303 HOH A O    
2222 O  O    . HOH G .   ? 0.2794 0.0858 0.2608 0.0287  -0.0672 0.0132  304 HOH A O    
2223 O  O    . HOH G .   ? 0.2298 0.2373 0.3611 -0.0246 -0.0693 0.1425  305 HOH A O    
2224 O  O    . HOH G .   ? 0.3758 0.1520 0.2504 -0.0358 0.0200  0.0397  306 HOH A O    
2225 O  O    . HOH G .   ? 0.3099 0.2140 0.3727 0.0085  -0.0051 -0.0277 307 HOH A O    
2226 O  O    . HOH G .   ? 0.2722 0.2807 0.4644 -0.0103 0.0723  0.0402  308 HOH A O    
2227 O  O    . HOH G .   ? 0.3183 0.2060 0.4319 0.0263  0.0784  0.0074  309 HOH A O    
2228 O  O    . HOH G .   ? 0.3780 0.2297 0.2748 -0.0178 -0.0651 0.0239  310 HOH A O    
2229 O  O    . HOH G .   ? 0.3674 0.2186 0.3185 -0.0008 -0.0149 -0.1229 311 HOH A O    
2230 O  O    . HOH G .   ? 0.3210 0.0649 0.3048 0.0601  0.0230  -0.0155 312 HOH A O    
2231 O  O    . HOH G .   ? 0.3221 0.1546 0.4130 0.1324  -0.0569 -0.0123 313 HOH A O    
2232 O  O    . HOH G .   ? 0.4732 0.2882 0.2099 0.0810  0.0311  0.0062  314 HOH A O    
2233 O  O    . HOH G .   ? 0.2224 0.1381 0.3123 0.0143  -0.0416 -0.0448 315 HOH A O    
2234 O  O    . HOH G .   ? 0.3381 0.2987 0.5019 -0.0027 -0.0626 0.0101  316 HOH A O    
2235 O  O    . HOH G .   ? 0.3634 0.1807 0.4386 -0.0079 -0.0021 0.1190  317 HOH A O    
2236 O  O    . HOH G .   ? 0.2466 0.1191 0.4071 0.0182  0.0732  -0.0412 318 HOH A O    
2237 O  O    . HOH G .   ? 0.2940 0.1706 0.3001 -0.0766 -0.0246 -0.0046 319 HOH A O    
2238 O  O    . HOH G .   ? 0.2823 0.3065 0.4345 -0.0654 -0.0820 0.0052  320 HOH A O    
2239 O  O    . HOH G .   ? 0.2498 0.1658 0.2415 0.0015  0.0455  -0.0238 321 HOH A O    
2240 O  O    . HOH G .   ? 0.2356 0.2142 0.2815 -0.0201 -0.0025 0.0327  322 HOH A O    
2241 O  O    . HOH G .   ? 0.2771 0.4491 0.3172 -0.1241 -0.0166 -0.0271 323 HOH A O    
2242 O  O    . HOH G .   ? 0.2202 0.1889 0.3522 0.0236  0.0282  -0.0487 324 HOH A O    
2243 O  O    . HOH G .   ? 0.1724 0.2701 0.2560 0.0026  0.0297  0.0043  325 HOH A O    
2244 O  O    . HOH G .   ? 0.2232 0.0300 0.2752 0.0000  -0.0279 -0.0043 326 HOH A O    
2245 O  O    . HOH G .   ? 0.4433 0.1536 0.3286 -0.0363 -0.0402 -0.0748 327 HOH A O    
2246 O  O    . HOH G .   ? 0.2258 0.3199 0.3417 0.0566  -0.0075 -0.0104 328 HOH A O    
2247 O  O    . HOH G .   ? 0.2593 0.1569 0.3152 0.0254  -0.0620 0.0035  329 HOH A O    
2248 O  O    . HOH G .   ? 0.2917 0.3202 0.3895 0.0271  -0.0282 0.0249  330 HOH A O    
2249 O  O    . HOH G .   ? 0.1848 0.2437 0.3853 0.0790  -0.0478 -0.0250 331 HOH A O    
2250 O  O    . HOH G .   ? 0.2820 0.3763 0.2541 0.1070  -0.0486 -0.0453 332 HOH A O    
2251 O  O    . HOH G .   ? 0.2401 0.2046 0.3921 0.0048  -0.0147 0.0891  333 HOH A O    
2252 O  O    . HOH G .   ? 0.2005 0.0848 0.1490 -0.0332 0.0073  0.0104  334 HOH A O    
2253 O  O    . HOH G .   ? 0.3279 0.4685 0.3369 -0.2302 -0.0960 0.0807  335 HOH A O    
2254 O  O    . HOH G .   ? 0.3507 0.3034 0.3190 -0.0430 -0.0458 0.0077  336 HOH A O    
2255 O  O    . HOH G .   ? 0.4342 0.5393 0.3613 0.0806  -0.0023 0.0579  337 HOH A O    
2256 O  O    . HOH G .   ? 0.2699 0.2114 0.2571 0.0269  -0.0170 0.0389  338 HOH A O    
2257 O  O    . HOH G .   ? 0.1875 0.1471 0.3356 -0.0104 0.0320  -0.0321 339 HOH A O    
2258 O  O    . HOH G .   ? 0.1716 0.1613 0.3777 -0.0877 -0.0319 -0.0373 340 HOH A O    
2259 O  O    . HOH G .   ? 0.5010 0.2556 0.4639 0.0426  -0.0009 -0.0158 341 HOH A O    
2260 O  O    . HOH G .   ? 0.4796 0.4184 0.3152 0.0963  -0.0998 -0.0201 342 HOH A O    
2261 O  O    . HOH G .   ? 0.4438 0.3750 0.3517 -0.0419 0.0153  0.0412  343 HOH A O    
2262 O  O    . HOH G .   ? 0.2264 0.2680 0.3788 0.0085  0.0311  0.0065  344 HOH A O    
2263 O  O    . HOH G .   ? 0.2959 0.3261 0.3471 -0.0749 0.0797  -0.1026 345 HOH A O    
2264 O  O    . HOH G .   ? 0.3094 0.2315 0.4043 0.0186  0.0296  0.0149  346 HOH A O    
2265 O  O    . HOH G .   ? 0.1479 0.3353 0.3183 0.0391  0.0268  0.0667  347 HOH A O    
2266 O  O    . HOH G .   ? 0.3579 0.2617 0.2974 0.0385  0.0723  -0.0141 348 HOH A O    
2267 O  O    . HOH G .   ? 0.2813 0.1499 0.3746 -0.0193 -0.0246 -0.0583 349 HOH A O    
2268 O  O    . HOH G .   ? 0.5778 0.3138 0.2690 0.0328  0.0140  0.0318  350 HOH A O    
2269 O  O    . HOH G .   ? 0.3866 0.1739 0.4294 0.0688  -0.0492 -0.0644 351 HOH A O    
2270 O  O    . HOH G .   ? 0.2990 0.3400 0.3301 -0.0370 0.0369  0.0462  352 HOH A O    
2271 O  O    . HOH G .   ? 0.2434 0.2619 0.3653 0.0441  -0.0384 -0.0466 353 HOH A O    
2272 O  O    . HOH G .   ? 0.4653 0.2135 0.2348 0.0139  -0.0075 -0.0106 354 HOH A O    
2273 O  O    . HOH G .   ? 0.3750 0.2288 0.3259 -0.0502 0.0214  -0.0137 355 HOH A O    
2274 O  O    . HOH G .   ? 0.3567 0.2989 0.3137 0.0007  0.0549  -0.0859 356 HOH A O    
2275 O  O    . HOH G .   ? 0.4795 0.3187 0.3207 0.0138  0.0137  0.0960  357 HOH A O    
2276 O  O    . HOH G .   ? 0.4096 0.1786 0.3092 0.0453  -0.0413 0.0138  358 HOH A O    
2277 O  O    . HOH G .   ? 0.4613 0.3378 0.2628 0.0093  0.0484  0.0384  359 HOH A O    
2278 O  O    . HOH G .   ? 0.2904 0.3552 0.4504 -0.1886 -0.0108 0.0224  360 HOH A O    
2279 O  O    . HOH G .   ? 0.3756 0.2794 0.3431 -0.0355 -0.0030 -0.0358 361 HOH A O    
2280 O  O    . HOH G .   ? 0.2130 0.1329 0.2639 -0.0019 0.0118  -0.0010 362 HOH A O    
2281 O  O    . HOH G .   ? 0.2488 0.3181 0.2636 -0.0434 -0.0048 -0.0420 363 HOH A O    
2282 O  O    . HOH G .   ? 0.3062 0.2845 0.3308 -0.0151 0.0528  -0.0410 364 HOH A O    
2283 O  O    . HOH G .   ? 0.2195 0.1645 0.3847 -0.0312 0.0581  -0.0023 365 HOH A O    
2284 O  O    . HOH G .   ? 0.3415 0.1991 0.4024 0.0270  0.0747  0.0454  366 HOH A O    
2285 O  O    . HOH G .   ? 0.2395 0.3320 0.4912 -0.0564 -0.0093 -0.0180 367 HOH A O    
2286 O  O    . HOH G .   ? 0.4192 0.1481 0.3532 0.0650  0.0090  0.0567  368 HOH A O    
2287 O  O    . HOH G .   ? 0.4272 0.3620 0.2919 -0.0626 0.0470  0.1021  369 HOH A O    
2288 O  O    . HOH G .   ? 0.3009 0.1811 0.3967 -0.0061 -0.0627 -0.0565 370 HOH A O    
2289 O  O    . HOH G .   ? 0.4521 0.3330 0.2757 -0.0539 0.1310  -0.0826 371 HOH A O    
2290 O  O    . HOH G .   ? 0.2848 0.2636 0.4090 0.0211  -0.0165 -0.0274 372 HOH A O    
2291 O  O    . HOH G .   ? 0.3655 0.2673 0.3893 -0.0034 0.0186  0.0270  373 HOH A O    
2292 O  O    . HOH G .   ? 0.2781 0.2071 0.2460 -0.0284 0.0782  0.0436  374 HOH A O    
2293 O  O    . HOH G .   ? 0.2960 0.2360 0.3681 0.0680  0.0365  0.0477  375 HOH A O    
2294 O  O    . HOH G .   ? 0.3308 0.3522 0.4071 -0.0186 0.0318  0.0238  376 HOH A O    
2295 O  O    . HOH G .   ? 0.4045 0.3221 0.2920 0.1852  -0.0745 0.0095  377 HOH A O    
2296 O  O    . HOH G .   ? 0.3456 0.2421 0.4215 -0.0445 0.0554  -0.0860 378 HOH A O    
2297 O  O    . HOH G .   ? 0.4419 0.2908 0.4500 0.0980  -0.0046 -0.0192 379 HOH A O    
2298 O  O    . HOH G .   ? 0.3590 0.3074 0.4526 -0.0192 -0.0385 0.0007  380 HOH A O    
2299 O  O    . HOH G .   ? 0.4704 0.4380 0.4861 -0.0952 0.0419  0.0757  381 HOH A O    
2300 O  O    . HOH G .   ? 0.3014 0.1639 0.4070 -0.0074 -0.0882 0.0632  382 HOH A O    
2301 O  O    . HOH G .   ? 0.2709 0.3367 0.3342 0.0512  0.0158  0.0060  383 HOH A O    
2302 O  O    . HOH G .   ? 0.3600 0.4353 0.4893 0.0665  -0.0296 0.0157  384 HOH A O    
2303 O  O    . HOH G .   ? 0.2661 0.3266 0.4358 0.0036  0.0873  -0.0081 385 HOH A O    
2304 O  O    . HOH G .   ? 0.1770 0.2873 0.4537 0.0500  -0.0074 -0.0012 386 HOH A O    
2305 O  O    . HOH G .   ? 0.3953 0.2846 0.3858 -0.0264 -0.0217 0.0799  387 HOH A O    
2306 O  O    . HOH G .   ? 0.3108 0.2970 0.4433 -0.0451 0.0336  -0.0211 388 HOH A O    
2307 O  O    . HOH G .   ? 0.2581 0.3216 0.4056 -0.0356 0.0103  -0.0004 389 HOH A O    
2308 O  O    . HOH G .   ? 0.3855 0.3031 0.4634 0.0910  -0.0200 -0.0618 390 HOH A O    
2309 O  O    . HOH G .   ? 0.3636 0.3895 0.2761 -0.0397 -0.1050 0.0777  391 HOH A O    
2310 O  O    . HOH G .   ? 0.4756 0.2393 0.5016 -0.0322 -0.0313 -0.0454 392 HOH A O    
2311 O  O    . HOH G .   ? 0.2690 0.2630 0.3960 0.0655  0.0272  0.0412  393 HOH A O    
2312 O  O    . HOH G .   ? 0.3114 0.2119 0.3803 -0.0397 0.0449  0.0932  394 HOH A O    
2313 O  O    . HOH G .   ? 0.3855 0.2011 0.4271 -0.0897 -0.0207 -0.0248 395 HOH A O    
2314 O  O    . HOH G .   ? 0.2429 0.3984 0.4325 -0.0100 0.0084  -0.0050 396 HOH A O    
2315 O  O    . HOH G .   ? 0.2570 0.3573 0.3409 0.0359  0.0417  -0.0570 397 HOH A O    
2316 O  O    . HOH G .   ? 0.2473 0.3578 0.3278 0.0375  0.0667  -0.0400 398 HOH A O    
2317 O  O    . HOH G .   ? 0.3298 0.2618 0.4728 0.0186  -0.0138 -0.0957 399 HOH A O    
2318 O  O    . HOH G .   ? 0.3738 0.2197 0.4221 0.0120  0.1192  0.0106  400 HOH A O    
2319 O  O    . HOH G .   ? 0.3576 0.2227 0.4593 0.0225  0.0426  0.0187  401 HOH A O    
2320 O  O    . HOH G .   ? 0.2914 0.2973 0.4280 -0.0581 -0.0328 -0.0365 402 HOH A O    
2321 O  O    . HOH G .   ? 0.3193 0.3298 0.3484 0.0109  0.0356  0.1037  403 HOH A O    
2322 O  O    . HOH G .   ? 0.2437 0.2318 0.3778 0.0346  -0.0055 0.0179  404 HOH A O    
2323 O  O    . HOH G .   ? 0.2405 0.2318 0.3196 0.0199  0.0231  -0.0025 405 HOH A O    
2324 O  O    . HOH G .   ? 0.1944 0.2989 0.4890 -0.0597 -0.0311 -0.0724 406 HOH A O    
2325 O  O    . HOH G .   ? 0.2787 0.2444 0.4152 0.0188  -0.0058 -0.0256 407 HOH A O    
2326 O  O    . HOH G .   ? 0.4701 0.2658 0.4648 -0.0164 0.0148  0.0891  408 HOH A O    
2327 O  O    . HOH G .   ? 0.2168 0.2346 0.4474 0.1042  -0.0220 -0.0124 409 HOH A O    
2328 O  O    . HOH G .   ? 0.2083 0.4156 0.6042 -0.0576 -0.0693 0.0825  410 HOH A O    
2329 O  O    . HOH G .   ? 0.3085 0.1933 0.3643 -0.0058 0.0200  0.0611  411 HOH A O    
2330 O  O    . HOH G .   ? 0.1545 0.2013 0.4350 0.0468  0.0620  0.0098  412 HOH A O    
2331 O  O    . HOH G .   ? 0.3328 0.3768 0.3437 -0.0509 -0.0017 -0.0824 413 HOH A O    
2332 O  O    . HOH G .   ? 0.4148 0.3474 0.4593 0.0508  -0.0213 0.0012  414 HOH A O    
2333 O  O    . HOH G .   ? 0.5195 0.5227 0.5190 0.0167  -0.0247 0.0003  415 HOH A O    
2334 O  O    . HOH G .   ? 0.2844 0.1651 0.3278 0.0232  0.0066  -0.0117 416 HOH A O    
2335 O  O    . HOH G .   ? 0.2972 0.2393 0.5393 0.0406  -0.0642 0.0707  417 HOH A O    
2336 O  O    . HOH G .   ? 0.4550 0.3490 0.3455 -0.0157 0.0758  -0.0642 418 HOH A O    
2337 O  O    . HOH G .   ? 0.2557 0.2229 0.3490 -0.0248 0.0081  0.0225  419 HOH A O    
2338 O  O    . HOH G .   ? 0.3466 0.1022 0.3924 0.0172  -0.0742 0.0115  420 HOH A O    
2339 O  O    . HOH G .   ? 0.3491 0.1811 0.3520 -0.0196 -0.0327 0.0074  421 HOH A O    
2340 O  O    . HOH G .   ? 0.3538 0.2257 0.4087 0.0957  -0.1096 0.0066  422 HOH A O    
2341 O  O    . HOH G .   ? 0.2887 0.1502 0.2950 0.0439  -0.0132 0.0397  423 HOH A O    
2342 O  O    . HOH G .   ? 0.3215 0.4506 0.3552 0.0112  -0.0311 0.0757  424 HOH A O    
2343 O  O    . HOH G .   ? 0.3968 0.1269 0.3790 0.0043  0.0535  0.0081  425 HOH A O    
2344 O  O    . HOH G .   ? 0.4677 0.2223 0.6300 -0.0345 0.0433  0.0495  426 HOH A O    
2345 O  O    . HOH G .   ? 0.3107 0.2045 0.4319 -0.0044 -0.0132 0.0301  427 HOH A O    
2346 O  O    . HOH G .   ? 0.2563 0.1781 0.4616 -0.0552 -0.0257 0.0157  428 HOH A O    
2347 O  O    . HOH G .   ? 0.2810 0.3379 0.3742 0.1179  0.0411  0.0092  429 HOH A O    
2348 O  O    . HOH G .   ? 0.5478 0.2516 0.3694 -0.1589 0.0291  -0.0614 430 HOH A O    
2349 O  O    . HOH G .   ? 0.3248 0.3672 0.4139 -0.0680 0.0736  -0.1103 431 HOH A O    
2350 O  O    . HOH G .   ? 0.2922 0.2235 0.6035 -0.0791 0.0945  0.0443  432 HOH A O    
2351 O  O    . HOH G .   ? 0.4667 0.3483 0.3266 -0.1456 -0.0237 -0.0189 433 HOH A O    
2352 O  O    . HOH G .   ? 0.3474 0.2603 0.4554 0.0009  0.0758  0.0206  434 HOH A O    
2353 O  O    . HOH G .   ? 0.3802 0.3814 0.5630 0.0249  -0.0666 -0.0514 435 HOH A O    
2354 O  O    . HOH G .   ? 0.5184 0.4798 0.3519 -0.0307 0.0147  0.0675  436 HOH A O    
2355 O  O    . HOH G .   ? 0.4177 0.4049 0.4926 -0.0969 0.0000  -0.0363 437 HOH A O    
2356 O  O    . HOH G .   ? 0.2752 0.2210 0.5340 -0.0526 0.0346  0.0405  438 HOH A O    
2357 O  O    . HOH G .   ? 0.4729 0.2623 0.4820 -0.0376 -0.0342 0.0052  439 HOH A O    
2358 O  O    . HOH G .   ? 0.3556 0.3143 0.4854 -0.0351 -0.0351 -0.0794 440 HOH A O    
2359 O  O    . HOH G .   ? 0.3619 0.3178 0.4504 -0.0116 -0.0047 -0.0795 441 HOH A O    
2360 O  O    . HOH G .   ? 0.2614 0.2363 0.4205 -0.0209 -0.0096 0.0369  442 HOH A O    
2361 O  O    . HOH G .   ? 0.3185 0.3508 0.4610 0.0182  -0.0346 0.0413  443 HOH A O    
2362 O  O    . HOH G .   ? 0.4037 0.3927 0.4402 0.0177  -0.1099 0.0272  444 HOH A O    
2363 O  O    . HOH G .   ? 0.3536 0.2476 0.4690 -0.0533 0.0364  0.0784  445 HOH A O    
2364 O  O    . HOH G .   ? 0.5088 0.3830 0.3573 -0.0897 0.0464  0.0428  446 HOH A O    
2365 O  O    . HOH G .   ? 0.2000 0.5509 0.4222 -0.0416 0.0558  0.0379  447 HOH A O    
2366 O  O    . HOH G .   ? 0.3647 0.5246 0.4708 0.0249  0.0098  -0.0531 448 HOH A O    
2367 O  O    . HOH G .   ? 0.5351 0.2217 0.4436 -0.0438 -0.0318 -0.0055 449 HOH A O    
2368 O  O    . HOH G .   ? 0.3766 0.2587 0.4615 -0.0660 -0.0064 0.0430  450 HOH A O    
2369 O  O    . HOH G .   ? 0.3862 0.4553 0.4862 0.0684  -0.0254 -0.0141 451 HOH A O    
2370 O  O    . HOH G .   ? 0.4890 0.2745 0.5156 -0.0171 0.0180  -0.0275 452 HOH A O    
2371 O  O    . HOH G .   ? 0.5115 0.4669 0.3759 -0.0124 -0.0110 0.0121  453 HOH A O    
2372 O  O    . HOH G .   ? 0.3614 0.2426 0.5692 0.0174  -0.0153 -0.0373 454 HOH A O    
2373 O  O    . HOH G .   ? 0.3446 0.3171 0.4317 0.1154  -0.0482 0.0306  455 HOH A O    
2374 O  O    . HOH G .   ? 0.1844 0.5144 0.4355 0.0482  -0.0143 -0.1189 456 HOH A O    
2375 O  O    . HOH G .   ? 0.4014 0.3387 0.5144 -0.0649 0.0795  -0.0618 457 HOH A O    
2376 O  O    . HOH G .   ? 0.3467 0.3372 0.3915 0.0215  0.0469  0.0104  458 HOH A O    
2377 O  O    . HOH G .   ? 0.5964 0.4485 0.5394 -0.0363 0.0032  0.0326  459 HOH A O    
2378 O  O    . HOH G .   ? 0.2482 0.3130 0.4354 -0.0046 0.1114  0.0720  460 HOH A O    
2379 O  O    . HOH G .   ? 0.4973 0.4530 0.5313 -0.0275 -0.0010 0.0650  461 HOH A O    
2380 O  O    . HOH G .   ? 0.2161 0.5940 0.5587 -0.0962 -0.0001 0.0256  462 HOH A O    
2381 O  O    . HOH G .   ? 0.4541 0.3336 0.4395 -0.0717 -0.0169 -0.0594 463 HOH A O    
2382 O  O    . HOH G .   ? 0.4306 0.4714 0.4474 -0.0313 0.0276  0.0552  464 HOH A O    
2383 O  O    . HOH G .   ? 0.5171 0.3923 0.4158 0.0258  -0.0143 -0.0289 465 HOH A O    
2384 O  O    . HOH G .   ? 0.3955 0.4114 0.4677 -0.0469 -0.0114 -0.0224 466 HOH A O    
2385 O  O    . HOH G .   ? 0.4310 0.2986 0.4049 -0.0445 -0.0064 -0.0738 467 HOH A O    
2386 O  O    . HOH G .   ? 0.3965 0.3541 0.5438 0.0915  0.0124  -0.0264 468 HOH A O    
2387 O  O    . HOH G .   ? 0.3636 0.3523 0.4694 -0.0842 0.0279  0.0783  469 HOH A O    
2388 O  O    . HOH G .   ? 0.5193 0.1352 0.4322 0.0036  -0.0450 -0.0329 470 HOH A O    
2389 O  O    . HOH G .   ? 0.3067 0.4514 0.4442 0.0264  0.0265  0.0092  471 HOH A O    
2390 O  O    . HOH G .   ? 0.3610 0.3136 0.4005 0.0969  0.0002  0.0018  472 HOH A O    
2391 O  O    . HOH G .   ? 0.3189 0.2929 0.3733 0.0512  0.0420  0.0409  473 HOH A O    
2392 O  O    . HOH G .   ? 0.4920 0.3498 0.4074 -0.0413 0.0409  0.0477  474 HOH A O    
2393 O  O    . HOH G .   ? 0.2702 0.3180 0.4081 0.0518  -0.0560 -0.0036 475 HOH A O    
2394 O  O    . HOH G .   ? 0.3437 0.3981 0.4656 -0.1030 -0.0279 -0.0525 476 HOH A O    
2395 O  O    . HOH G .   ? 0.4474 0.2486 0.5202 0.0320  -0.0357 0.0059  477 HOH A O    
2396 O  O    . HOH G .   ? 0.5346 0.3179 0.4628 -0.0206 -0.0007 -0.0610 478 HOH A O    
2397 O  O    . HOH G .   ? 0.4636 0.2551 0.5710 0.0770  -0.0253 0.0232  479 HOH A O    
2398 O  O    . HOH G .   ? 0.4363 0.4748 0.5117 -0.0041 0.0764  -0.0344 480 HOH A O    
2399 O  O    . HOH G .   ? 0.5502 0.2903 0.5289 0.0422  -0.0107 -0.0011 481 HOH A O    
2400 O  O    . HOH G .   ? 0.3763 0.2506 0.4942 -0.1178 -0.0998 0.0259  482 HOH A O    
2401 O  O    . HOH G .   ? 0.5172 0.4283 0.5334 -0.0210 -0.0315 0.0178  483 HOH A O    
2402 O  O    . HOH G .   ? 0.5147 0.4133 0.3679 -0.0081 0.0289  -0.0612 484 HOH A O    
2403 O  O    . HOH G .   ? 0.3571 0.3581 0.4399 -0.0528 0.0159  0.0024  485 HOH A O    
2404 O  O    . HOH G .   ? 0.2938 0.4723 0.5484 -0.0119 -0.0048 -0.0101 486 HOH A O    
2405 O  O    . HOH G .   ? 0.4181 0.3426 0.3724 -0.0575 0.0466  0.0900  487 HOH A O    
2406 O  O    . HOH G .   ? 0.4104 0.5294 0.4902 -0.0138 -0.0269 0.0221  488 HOH A O    
2407 O  O    . HOH G .   ? 0.4237 0.4276 0.4791 -0.0618 -0.0083 0.0209  489 HOH A O    
2408 O  O    . HOH G .   ? 0.3090 0.3765 0.4935 0.1487  0.0665  0.0885  490 HOH A O    
2409 O  O    . HOH G .   ? 0.4829 0.3966 0.5013 0.0124  0.0447  0.0003  491 HOH A O    
2410 O  O    . HOH G .   ? 0.5275 0.4797 0.5196 -0.0104 0.0077  -0.0008 492 HOH A O    
2411 O  O    . HOH G .   ? 0.5423 0.3640 0.5973 -0.0259 0.0096  -0.0466 493 HOH A O    
2412 O  O    . HOH G .   ? 0.3383 0.3325 0.5060 -0.0940 -0.0678 -0.0427 494 HOH A O    
2413 O  O    . HOH G .   ? 0.3648 0.5263 0.3966 -0.0112 -0.0069 0.0868  495 HOH A O    
2414 O  O    . HOH G .   ? 0.4690 0.5318 0.5189 0.0197  0.0245  0.0025  496 HOH A O    
2415 O  O    . HOH G .   ? 0.3929 0.4249 0.4091 -0.0003 -0.0121 0.0106  497 HOH A O    
2416 O  O    . HOH G .   ? 0.3845 0.4167 0.3167 0.0483  0.0194  0.0134  498 HOH A O    
2417 O  O    . HOH G .   ? 0.4740 0.3228 0.4332 -0.1332 -0.1057 -0.0522 499 HOH A O    
2418 O  O    . HOH G .   ? 0.3876 0.3188 0.4574 -0.0089 -0.1168 -0.1178 500 HOH A O    
2419 O  O    . HOH G .   ? 0.3488 0.4008 0.4200 0.0010  -0.0596 -0.0134 501 HOH A O    
2420 O  O    . HOH G .   ? 0.3521 0.3390 0.3534 -0.0484 -0.0521 0.0114  502 HOH A O    
2421 O  O    . HOH G .   ? 0.4242 0.4321 0.4676 -0.0618 -0.0339 0.0079  503 HOH A O    
2422 O  O    . HOH G .   ? 0.3481 0.3078 0.3939 -0.0251 0.0272  -0.0176 504 HOH A O    
2423 O  O    . HOH G .   ? 0.2430 0.1747 0.3684 -0.0428 0.0048  0.0031  505 HOH A O    
2424 O  O    . HOH G .   ? 0.3543 0.3480 0.3739 0.0344  0.0630  0.0285  506 HOH A O    
2425 O  O    . HOH G .   ? 0.3084 0.2870 0.5069 0.0289  -0.0030 0.0448  507 HOH A O    
2426 O  O    . HOH G .   ? 0.5464 0.4833 0.4649 -0.0125 0.0187  -0.0066 508 HOH A O    
2427 O  O    . HOH G .   ? 0.4059 0.3001 0.4245 -0.1275 -0.0090 0.0428  509 HOH A O    
2428 O  O    . HOH G .   ? 0.3980 0.3067 0.4866 0.0290  0.0186  0.0119  510 HOH A O    
2429 O  O    . HOH G .   ? 0.3649 0.1920 0.5120 -0.1026 -0.0081 0.0267  511 HOH A O    
2430 O  O    . HOH G .   ? 0.5209 0.4708 0.5455 -0.0112 0.0082  -0.0036 512 HOH A O    
2431 O  O    . HOH G .   ? 0.5514 0.2418 0.4948 0.0590  -0.0105 -0.0254 513 HOH A O    
2432 O  O    . HOH G .   ? 0.3608 0.3245 0.3958 0.1335  0.0487  -0.0389 514 HOH A O    
2433 O  O    . HOH G .   ? 0.4595 0.2050 0.5899 -0.0356 -0.0257 -0.0203 515 HOH A O    
2434 O  O    . HOH G .   ? 0.4142 0.4305 0.5195 0.0952  -0.0213 0.0132  516 HOH A O    
2435 O  O    . HOH G .   ? 0.4332 0.5097 0.5167 0.0094  0.0066  0.0447  517 HOH A O    
2436 O  O    . HOH G .   ? 0.5732 0.5509 0.5390 0.0033  0.0450  0.0116  518 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 MES 1   263 1   MES MES A . 
D 4 DMS 1   264 1   DMS DMS A . 
E 4 DMS 1   265 2   DMS DMS A . 
F 5 E27 1   266 1   E27 E27 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 149 414 150 HOH HOH A . 
G 6 HOH 150 415 151 HOH HOH A . 
G 6 HOH 151 416 152 HOH HOH A . 
G 6 HOH 152 417 153 HOH HOH A . 
G 6 HOH 153 418 154 HOH HOH A . 
G 6 HOH 154 419 155 HOH HOH A . 
G 6 HOH 155 420 156 HOH HOH A . 
G 6 HOH 156 421 157 HOH HOH A . 
G 6 HOH 157 422 158 HOH HOH A . 
G 6 HOH 158 423 159 HOH HOH A . 
G 6 HOH 159 424 160 HOH HOH A . 
G 6 HOH 160 425 161 HOH HOH A . 
G 6 HOH 161 426 162 HOH HOH A . 
G 6 HOH 162 427 163 HOH HOH A . 
G 6 HOH 163 428 164 HOH HOH A . 
G 6 HOH 164 429 165 HOH HOH A . 
G 6 HOH 165 430 166 HOH HOH A . 
G 6 HOH 166 431 167 HOH HOH A . 
G 6 HOH 167 432 168 HOH HOH A . 
G 6 HOH 168 433 169 HOH HOH A . 
G 6 HOH 169 434 170 HOH HOH A . 
G 6 HOH 170 435 171 HOH HOH A . 
G 6 HOH 171 436 172 HOH HOH A . 
G 6 HOH 172 437 173 HOH HOH A . 
G 6 HOH 173 438 174 HOH HOH A . 
G 6 HOH 174 439 175 HOH HOH A . 
G 6 HOH 175 440 176 HOH HOH A . 
G 6 HOH 176 441 177 HOH HOH A . 
G 6 HOH 177 442 178 HOH HOH A . 
G 6 HOH 178 443 179 HOH HOH A . 
G 6 HOH 179 444 180 HOH HOH A . 
G 6 HOH 180 445 181 HOH HOH A . 
G 6 HOH 181 446 182 HOH HOH A . 
G 6 HOH 182 447 183 HOH HOH A . 
G 6 HOH 183 448 184 HOH HOH A . 
G 6 HOH 184 449 185 HOH HOH A . 
G 6 HOH 185 450 186 HOH HOH A . 
G 6 HOH 186 451 187 HOH HOH A . 
G 6 HOH 187 452 188 HOH HOH A . 
G 6 HOH 188 453 189 HOH HOH A . 
G 6 HOH 189 454 190 HOH HOH A . 
G 6 HOH 190 455 191 HOH HOH A . 
G 6 HOH 191 456 192 HOH HOH A . 
G 6 HOH 192 457 193 HOH HOH A . 
G 6 HOH 193 458 194 HOH HOH A . 
G 6 HOH 194 459 195 HOH HOH A . 
G 6 HOH 195 460 197 HOH HOH A . 
G 6 HOH 196 461 198 HOH HOH A . 
G 6 HOH 197 462 199 HOH HOH A . 
G 6 HOH 198 463 201 HOH HOH A . 
G 6 HOH 199 464 202 HOH HOH A . 
G 6 HOH 200 465 203 HOH HOH A . 
G 6 HOH 201 466 204 HOH HOH A . 
G 6 HOH 202 467 205 HOH HOH A . 
G 6 HOH 203 468 206 HOH HOH A . 
G 6 HOH 204 469 207 HOH HOH A . 
G 6 HOH 205 470 208 HOH HOH A . 
G 6 HOH 206 471 209 HOH HOH A . 
G 6 HOH 207 472 211 HOH HOH A . 
G 6 HOH 208 473 212 HOH HOH A . 
G 6 HOH 209 474 213 HOH HOH A . 
G 6 HOH 210 475 214 HOH HOH A . 
G 6 HOH 211 476 215 HOH HOH A . 
G 6 HOH 212 477 216 HOH HOH A . 
G 6 HOH 213 478 217 HOH HOH A . 
G 6 HOH 214 479 218 HOH HOH A . 
G 6 HOH 215 480 219 HOH HOH A . 
G 6 HOH 216 481 220 HOH HOH A . 
G 6 HOH 217 482 221 HOH HOH A . 
G 6 HOH 218 483 222 HOH HOH A . 
G 6 HOH 219 484 224 HOH HOH A . 
G 6 HOH 220 485 225 HOH HOH A . 
G 6 HOH 221 486 226 HOH HOH A . 
G 6 HOH 222 487 227 HOH HOH A . 
G 6 HOH 223 488 228 HOH HOH A . 
G 6 HOH 224 489 229 HOH HOH A . 
G 6 HOH 225 490 230 HOH HOH A . 
G 6 HOH 226 491 231 HOH HOH A . 
G 6 HOH 227 492 232 HOH HOH A . 
G 6 HOH 228 493 233 HOH HOH A . 
G 6 HOH 229 494 235 HOH HOH A . 
G 6 HOH 230 495 236 HOH HOH A . 
G 6 HOH 231 496 237 HOH HOH A . 
G 6 HOH 232 497 238 HOH HOH A . 
G 6 HOH 233 498 239 HOH HOH A . 
G 6 HOH 234 499 240 HOH HOH A . 
G 6 HOH 235 500 241 HOH HOH A . 
G 6 HOH 236 501 243 HOH HOH A . 
G 6 HOH 237 502 244 HOH HOH A . 
G 6 HOH 238 503 245 HOH HOH A . 
G 6 HOH 239 504 246 HOH HOH A . 
G 6 HOH 240 505 248 HOH HOH A . 
G 6 HOH 241 506 249 HOH HOH A . 
G 6 HOH 242 507 251 HOH HOH A . 
G 6 HOH 243 508 252 HOH HOH A . 
G 6 HOH 244 509 253 HOH HOH A . 
G 6 HOH 245 510 254 HOH HOH A . 
G 6 HOH 246 511 255 HOH HOH A . 
G 6 HOH 247 512 256 HOH HOH A . 
G 6 HOH 248 513 257 HOH HOH A . 
G 6 HOH 249 514 259 HOH HOH A . 
G 6 HOH 250 515 261 HOH HOH A . 
G 6 HOH 251 516 262 HOH HOH A . 
G 6 HOH 252 517 263 HOH HOH A . 
G 6 HOH 253 518 264 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_555 103.3 ? 
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_555 113.7 ? 
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 98.0  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N28 ? F E27 .   ? A E27 266 ? 1_555 109.6 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N28 ? F E27 .   ? A E27 266 ? 1_555 113.7 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N28 ? F E27 .   ? A E27 266 ? 1_555 117.3 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 S24 ? F E27 .   ? A E27 266 ? 1_555 98.3  ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 S24 ? F E27 .   ? A E27 266 ? 1_555 142.7 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 S24 ? F E27 .   ? A E27 266 ? 1_555 100.7 ? 
10 N28 ? F E27 .   ? A E27 266 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 S24 ? F E27 .   ? A E27 266 ? 1_555 29.2  ? 
# 
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 2011-02-02 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2023-09-06 
# 
_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' 'Version format compliance' 
2 3 'Structure model' 'Data collection'           
3 3 'Structure model' 'Database references'       
4 3 'Structure model' 'Derived calculations'      
5 3 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' chem_comp_atom                
2 3 'Structure model' chem_comp_bond                
3 3 'Structure model' database_2                    
4 3 'Structure model' diffrn_source                 
5 3 'Structure model' pdbx_initial_refinement_model 
6 3 'Structure model' pdbx_struct_conn_angle        
7 3 'Structure model' struct_conn                   
8 3 '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' '_database_2.pdbx_DOI'                        
2  3 'Structure model' '_database_2.pdbx_database_accession'         
3  3 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
4  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.value'               
17 3 'Structure model' '_struct_conn.pdbx_dist_value'                
18 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
19 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
20 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
21 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
22 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
23 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
24 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
25 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
26 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
27 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
28 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
29 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
30 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
31 3 '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 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 N   A ARG 254 ? ? O A HOH 444 ? ? 2.02 
2 1 OE1 A GLN 136 ? A O A HOH 367 ? ? 2.08 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH1 A ARG 27  ? ? 123.96 120.30 3.66   0.50 N 
2 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH2 A ARG 27  ? ? 116.96 120.30 -3.34  0.50 N 
3 1 CB A ASP 52  ? ? CG A ASP 52  ? ? OD1 A ASP 52  ? ? 124.59 118.30 6.29   0.90 N 
4 1 CG A ARG 89  ? ? CD A ARG 89  ? ? NE  A ARG 89  ? ? 97.58  111.80 -14.22 2.10 N 
5 1 NE A ARG 89  ? ? CZ A ARG 89  ? ? NH2 A ARG 89  ? ? 116.83 120.30 -3.47  0.50 N 
6 1 CB A LEU 198 ? ? CG A LEU 198 ? ? CD2 A LEU 198 ? ? 126.87 111.00 15.87  1.70 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 ILE A 22  ? B -57.01  -8.31   
2 1 ARG A 27  ? ? -143.41 53.53   
3 1 LYS A 111 ? ? 74.79   -3.34   
4 1 PHE A 176 ? ? -154.40 70.97   
5 1 ASN A 244 ? ? -95.13  46.52   
6 1 LYS A 252 ? ? 55.49   -138.90 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
E27 N1   N  Y N 98  
E27 C2   C  Y N 99  
E27 N3   N  Y N 100 
E27 C4   C  Y N 101 
E27 C5   C  Y N 102 
E27 N6   N  Y N 103 
E27 C7   C  Y N 104 
E27 C8   C  Y N 105 
E27 C9   C  Y N 106 
E27 C10  C  Y N 107 
E27 C11  C  Y N 108 
E27 C12  C  Y N 109 
E27 C13  C  Y N 110 
E27 S14  S  N N 111 
E27 C15  C  N N 112 
E27 C16  C  N N 113 
E27 O17  O  N N 114 
E27 C18  C  Y N 115 
E27 C19  C  Y N 116 
E27 C20  C  Y N 117 
E27 C21  C  Y N 118 
E27 C22  C  Y N 119 
E27 C23  C  Y N 120 
E27 S24  S  N N 121 
E27 O25  O  N N 122 
E27 CL26 CL N N 123 
E27 O27  O  N N 124 
E27 N28  N  N N 125 
E27 H5   H  N N 126 
E27 H10  H  N N 127 
E27 H11  H  N N 128 
E27 H12  H  N N 129 
E27 H13  H  N N 130 
E27 H15  H  N N 131 
E27 H15A H  N N 132 
E27 H19  H  N N 133 
E27 H22  H  N N 134 
E27 H23  H  N N 135 
E27 HN28 H  N N 136 
E27 HN2A H  N N 137 
E27 HN1  H  N N 138 
GLN N    N  N N 139 
GLN CA   C  N S 140 
GLN C    C  N N 141 
GLN O    O  N N 142 
GLN CB   C  N N 143 
GLN CG   C  N N 144 
GLN CD   C  N N 145 
GLN OE1  O  N N 146 
GLN NE2  N  N N 147 
GLN OXT  O  N N 148 
GLN H    H  N N 149 
GLN H2   H  N N 150 
GLN HA   H  N N 151 
GLN HB2  H  N N 152 
GLN HB3  H  N N 153 
GLN HG2  H  N N 154 
GLN HG3  H  N N 155 
GLN HE21 H  N N 156 
GLN HE22 H  N N 157 
GLN HXT  H  N N 158 
GLU N    N  N N 159 
GLU CA   C  N S 160 
GLU C    C  N N 161 
GLU O    O  N N 162 
GLU CB   C  N N 163 
GLU CG   C  N N 164 
GLU CD   C  N N 165 
GLU OE1  O  N N 166 
GLU OE2  O  N N 167 
GLU OXT  O  N N 168 
GLU H    H  N N 169 
GLU H2   H  N N 170 
GLU HA   H  N N 171 
GLU HB2  H  N N 172 
GLU HB3  H  N N 173 
GLU HG2  H  N N 174 
GLU HG3  H  N N 175 
GLU HE2  H  N N 176 
GLU HXT  H  N N 177 
GLY N    N  N N 178 
GLY CA   C  N N 179 
GLY C    C  N N 180 
GLY O    O  N N 181 
GLY OXT  O  N N 182 
GLY H    H  N N 183 
GLY H2   H  N N 184 
GLY HA2  H  N N 185 
GLY HA3  H  N N 186 
GLY HXT  H  N N 187 
HIS N    N  N N 188 
HIS CA   C  N S 189 
HIS C    C  N N 190 
HIS O    O  N N 191 
HIS CB   C  N N 192 
HIS CG   C  Y N 193 
HIS ND1  N  Y N 194 
HIS CD2  C  Y N 195 
HIS CE1  C  Y N 196 
HIS NE2  N  Y N 197 
HIS OXT  O  N N 198 
HIS H    H  N N 199 
HIS H2   H  N N 200 
HIS HA   H  N N 201 
HIS HB2  H  N N 202 
HIS HB3  H  N N 203 
HIS HD1  H  N N 204 
HIS HD2  H  N N 205 
HIS HE1  H  N N 206 
HIS HE2  H  N N 207 
HIS HXT  H  N N 208 
HOH O    O  N N 209 
HOH H1   H  N N 210 
HOH H2   H  N N 211 
ILE N    N  N N 212 
ILE CA   C  N S 213 
ILE C    C  N N 214 
ILE O    O  N N 215 
ILE CB   C  N S 216 
ILE CG1  C  N N 217 
ILE CG2  C  N N 218 
ILE CD1  C  N N 219 
ILE OXT  O  N N 220 
ILE H    H  N N 221 
ILE H2   H  N N 222 
ILE HA   H  N N 223 
ILE HB   H  N N 224 
ILE HG12 H  N N 225 
ILE HG13 H  N N 226 
ILE HG21 H  N N 227 
ILE HG22 H  N N 228 
ILE HG23 H  N N 229 
ILE HD11 H  N N 230 
ILE HD12 H  N N 231 
ILE HD13 H  N N 232 
ILE HXT  H  N N 233 
LEU N    N  N N 234 
LEU CA   C  N S 235 
LEU C    C  N N 236 
LEU O    O  N N 237 
LEU CB   C  N N 238 
LEU CG   C  N N 239 
LEU CD1  C  N N 240 
LEU CD2  C  N N 241 
LEU OXT  O  N N 242 
LEU H    H  N N 243 
LEU H2   H  N N 244 
LEU HA   H  N N 245 
LEU HB2  H  N N 246 
LEU HB3  H  N N 247 
LEU HG   H  N N 248 
LEU HD11 H  N N 249 
LEU HD12 H  N N 250 
LEU HD13 H  N N 251 
LEU HD21 H  N N 252 
LEU HD22 H  N N 253 
LEU HD23 H  N N 254 
LEU HXT  H  N N 255 
LYS N    N  N N 256 
LYS CA   C  N S 257 
LYS C    C  N N 258 
LYS O    O  N N 259 
LYS CB   C  N N 260 
LYS CG   C  N N 261 
LYS CD   C  N N 262 
LYS CE   C  N N 263 
LYS NZ   N  N N 264 
LYS OXT  O  N N 265 
LYS H    H  N N 266 
LYS H2   H  N N 267 
LYS HA   H  N N 268 
LYS HB2  H  N N 269 
LYS HB3  H  N N 270 
LYS HG2  H  N N 271 
LYS HG3  H  N N 272 
LYS HD2  H  N N 273 
LYS HD3  H  N N 274 
LYS HE2  H  N N 275 
LYS HE3  H  N N 276 
LYS HZ1  H  N N 277 
LYS HZ2  H  N N 278 
LYS HZ3  H  N N 279 
LYS HXT  H  N N 280 
MES O1   O  N N 281 
MES C2   C  N N 282 
MES C3   C  N N 283 
MES N4   N  N N 284 
MES C5   C  N N 285 
MES C6   C  N N 286 
MES C7   C  N N 287 
MES C8   C  N N 288 
MES S    S  N N 289 
MES O1S  O  N N 290 
MES O2S  O  N N 291 
MES O3S  O  N N 292 
MES H21  H  N N 293 
MES H22  H  N N 294 
MES H31  H  N N 295 
MES H32  H  N N 296 
MES HN4  H  N N 297 
MES H51  H  N N 298 
MES H52  H  N N 299 
MES H61  H  N N 300 
MES H62  H  N N 301 
MES H71  H  N N 302 
MES H72  H  N N 303 
MES H81  H  N N 304 
MES H82  H  N N 305 
MET N    N  N N 306 
MET CA   C  N S 307 
MET C    C  N N 308 
MET O    O  N N 309 
MET CB   C  N N 310 
MET CG   C  N N 311 
MET SD   S  N N 312 
MET CE   C  N N 313 
MET OXT  O  N N 314 
MET H    H  N N 315 
MET H2   H  N N 316 
MET HA   H  N N 317 
MET HB2  H  N N 318 
MET HB3  H  N N 319 
MET HG2  H  N N 320 
MET HG3  H  N N 321 
MET HE1  H  N N 322 
MET HE2  H  N N 323 
MET HE3  H  N N 324 
MET HXT  H  N N 325 
PHE N    N  N N 326 
PHE CA   C  N S 327 
PHE C    C  N N 328 
PHE O    O  N N 329 
PHE CB   C  N N 330 
PHE CG   C  Y N 331 
PHE CD1  C  Y N 332 
PHE CD2  C  Y N 333 
PHE CE1  C  Y N 334 
PHE CE2  C  Y N 335 
PHE CZ   C  Y N 336 
PHE OXT  O  N N 337 
PHE H    H  N N 338 
PHE H2   H  N N 339 
PHE HA   H  N N 340 
PHE HB2  H  N N 341 
PHE HB3  H  N N 342 
PHE HD1  H  N N 343 
PHE HD2  H  N N 344 
PHE HE1  H  N N 345 
PHE HE2  H  N N 346 
PHE HZ   H  N N 347 
PHE HXT  H  N N 348 
PRO N    N  N N 349 
PRO CA   C  N S 350 
PRO C    C  N N 351 
PRO O    O  N N 352 
PRO CB   C  N N 353 
PRO CG   C  N N 354 
PRO CD   C  N N 355 
PRO OXT  O  N N 356 
PRO H    H  N N 357 
PRO HA   H  N N 358 
PRO HB2  H  N N 359 
PRO HB3  H  N N 360 
PRO HG2  H  N N 361 
PRO HG3  H  N N 362 
PRO HD2  H  N N 363 
PRO HD3  H  N N 364 
PRO HXT  H  N N 365 
SER N    N  N N 366 
SER CA   C  N S 367 
SER C    C  N N 368 
SER O    O  N N 369 
SER CB   C  N N 370 
SER OG   O  N N 371 
SER OXT  O  N N 372 
SER H    H  N N 373 
SER H2   H  N N 374 
SER HA   H  N N 375 
SER HB2  H  N N 376 
SER HB3  H  N N 377 
SER HG   H  N N 378 
SER HXT  H  N N 379 
THR N    N  N N 380 
THR CA   C  N S 381 
THR C    C  N N 382 
THR O    O  N N 383 
THR CB   C  N R 384 
THR OG1  O  N N 385 
THR CG2  C  N N 386 
THR OXT  O  N N 387 
THR H    H  N N 388 
THR H2   H  N N 389 
THR HA   H  N N 390 
THR HB   H  N N 391 
THR HG1  H  N N 392 
THR HG21 H  N N 393 
THR HG22 H  N N 394 
THR HG23 H  N N 395 
THR HXT  H  N N 396 
TRP N    N  N N 397 
TRP CA   C  N S 398 
TRP C    C  N N 399 
TRP O    O  N N 400 
TRP CB   C  N N 401 
TRP CG   C  Y N 402 
TRP CD1  C  Y N 403 
TRP CD2  C  Y N 404 
TRP NE1  N  Y N 405 
TRP CE2  C  Y N 406 
TRP CE3  C  Y N 407 
TRP CZ2  C  Y N 408 
TRP CZ3  C  Y N 409 
TRP CH2  C  Y N 410 
TRP OXT  O  N N 411 
TRP H    H  N N 412 
TRP H2   H  N N 413 
TRP HA   H  N N 414 
TRP HB2  H  N N 415 
TRP HB3  H  N N 416 
TRP HD1  H  N N 417 
TRP HE1  H  N N 418 
TRP HE3  H  N N 419 
TRP HZ2  H  N N 420 
TRP HZ3  H  N N 421 
TRP HH2  H  N N 422 
TRP HXT  H  N N 423 
TYR N    N  N N 424 
TYR CA   C  N S 425 
TYR C    C  N N 426 
TYR O    O  N N 427 
TYR CB   C  N N 428 
TYR CG   C  Y N 429 
TYR CD1  C  Y N 430 
TYR CD2  C  Y N 431 
TYR CE1  C  Y N 432 
TYR CE2  C  Y N 433 
TYR CZ   C  Y N 434 
TYR OH   O  N N 435 
TYR OXT  O  N N 436 
TYR H    H  N N 437 
TYR H2   H  N N 438 
TYR HA   H  N N 439 
TYR HB2  H  N N 440 
TYR HB3  H  N N 441 
TYR HD1  H  N N 442 
TYR HD2  H  N N 443 
TYR HE1  H  N N 444 
TYR HE2  H  N N 445 
TYR HH   H  N N 446 
TYR HXT  H  N N 447 
VAL N    N  N N 448 
VAL CA   C  N S 449 
VAL C    C  N N 450 
VAL O    O  N N 451 
VAL CB   C  N N 452 
VAL CG1  C  N N 453 
VAL CG2  C  N N 454 
VAL OXT  O  N N 455 
VAL H    H  N N 456 
VAL H2   H  N N 457 
VAL HA   H  N N 458 
VAL HB   H  N N 459 
VAL HG11 H  N N 460 
VAL HG12 H  N N 461 
VAL HG13 H  N N 462 
VAL HG21 H  N N 463 
VAL HG22 H  N N 464 
VAL HG23 H  N N 465 
VAL HXT  H  N N 466 
ZN  ZN   ZN N N 467 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
E27 C2  N1   sing Y N 92  
E27 N1  C9   sing Y N 93  
E27 S14 C2   sing N N 94  
E27 N3  C2   doub Y N 95  
E27 N3  C4   sing Y N 96  
E27 C5  C4   doub Y N 97  
E27 C4  C9   sing Y N 98  
E27 C5  N6   sing Y N 99  
E27 C5  H5   sing N N 100 
E27 N6  C7   doub Y N 101 
E27 C7  C8   sing Y N 102 
E27 C7  C10  sing Y N 103 
E27 C9  C8   doub Y N 104 
E27 C8  C13  sing Y N 105 
E27 C10 C11  doub Y N 106 
E27 C10 H10  sing N N 107 
E27 C11 C12  sing Y N 108 
E27 C11 H11  sing N N 109 
E27 C13 C12  doub Y N 110 
E27 C12 H12  sing N N 111 
E27 C13 H13  sing N N 112 
E27 S14 C15  sing N N 113 
E27 C15 C16  sing N N 114 
E27 C15 H15  sing N N 115 
E27 C15 H15A sing N N 116 
E27 C16 O17  doub N N 117 
E27 C16 C18  sing N N 118 
E27 C18 C23  doub Y N 119 
E27 C18 C19  sing Y N 120 
E27 C19 C20  doub Y N 121 
E27 C19 H19  sing N N 122 
E27 C20 C21  sing Y N 123 
E27 C20 S24  sing N N 124 
E27 C22 C21  doub Y N 125 
E27 C21 CL26 sing N N 126 
E27 C23 C22  sing Y N 127 
E27 C22 H22  sing N N 128 
E27 C23 H23  sing N N 129 
E27 N28 S24  sing N N 130 
E27 O25 S24  doub N N 131 
E27 S24 O27  doub N N 132 
E27 N28 HN28 sing N N 133 
E27 N28 HN2A sing N N 134 
E27 N1  HN1  sing N N 135 
GLN N   CA   sing N N 136 
GLN N   H    sing N N 137 
GLN N   H2   sing N N 138 
GLN CA  C    sing N N 139 
GLN CA  CB   sing N N 140 
GLN CA  HA   sing N N 141 
GLN C   O    doub N N 142 
GLN C   OXT  sing N N 143 
GLN CB  CG   sing N N 144 
GLN CB  HB2  sing N N 145 
GLN CB  HB3  sing N N 146 
GLN CG  CD   sing N N 147 
GLN CG  HG2  sing N N 148 
GLN CG  HG3  sing N N 149 
GLN CD  OE1  doub N N 150 
GLN CD  NE2  sing N N 151 
GLN NE2 HE21 sing N N 152 
GLN NE2 HE22 sing N N 153 
GLN OXT HXT  sing N N 154 
GLU N   CA   sing N N 155 
GLU N   H    sing N N 156 
GLU N   H2   sing N N 157 
GLU CA  C    sing N N 158 
GLU CA  CB   sing N N 159 
GLU CA  HA   sing N N 160 
GLU C   O    doub N N 161 
GLU C   OXT  sing N N 162 
GLU CB  CG   sing N N 163 
GLU CB  HB2  sing N N 164 
GLU CB  HB3  sing N N 165 
GLU CG  CD   sing N N 166 
GLU CG  HG2  sing N N 167 
GLU CG  HG3  sing N N 168 
GLU CD  OE1  doub N N 169 
GLU CD  OE2  sing N N 170 
GLU OE2 HE2  sing N N 171 
GLU OXT HXT  sing N N 172 
GLY N   CA   sing N N 173 
GLY N   H    sing N N 174 
GLY N   H2   sing N N 175 
GLY CA  C    sing N N 176 
GLY CA  HA2  sing N N 177 
GLY CA  HA3  sing N N 178 
GLY C   O    doub N N 179 
GLY C   OXT  sing N N 180 
GLY OXT HXT  sing N N 181 
HIS N   CA   sing N N 182 
HIS N   H    sing N N 183 
HIS N   H2   sing N N 184 
HIS CA  C    sing N N 185 
HIS CA  CB   sing N N 186 
HIS CA  HA   sing N N 187 
HIS C   O    doub N N 188 
HIS C   OXT  sing N N 189 
HIS CB  CG   sing N N 190 
HIS CB  HB2  sing N N 191 
HIS CB  HB3  sing N N 192 
HIS CG  ND1  sing Y N 193 
HIS CG  CD2  doub Y N 194 
HIS ND1 CE1  doub Y N 195 
HIS ND1 HD1  sing N N 196 
HIS CD2 NE2  sing Y N 197 
HIS CD2 HD2  sing N N 198 
HIS CE1 NE2  sing Y N 199 
HIS CE1 HE1  sing N N 200 
HIS NE2 HE2  sing N N 201 
HIS OXT HXT  sing N N 202 
HOH O   H1   sing N N 203 
HOH O   H2   sing N N 204 
ILE N   CA   sing N N 205 
ILE N   H    sing N N 206 
ILE N   H2   sing N N 207 
ILE CA  C    sing N N 208 
ILE CA  CB   sing N N 209 
ILE CA  HA   sing N N 210 
ILE C   O    doub N N 211 
ILE C   OXT  sing N N 212 
ILE CB  CG1  sing N N 213 
ILE CB  CG2  sing N N 214 
ILE CB  HB   sing N N 215 
ILE CG1 CD1  sing N N 216 
ILE CG1 HG12 sing N N 217 
ILE CG1 HG13 sing N N 218 
ILE CG2 HG21 sing N N 219 
ILE CG2 HG22 sing N N 220 
ILE CG2 HG23 sing N N 221 
ILE CD1 HD11 sing N N 222 
ILE CD1 HD12 sing N N 223 
ILE CD1 HD13 sing N N 224 
ILE OXT HXT  sing N N 225 
LEU N   CA   sing N N 226 
LEU N   H    sing N N 227 
LEU N   H2   sing N N 228 
LEU CA  C    sing N N 229 
LEU CA  CB   sing N N 230 
LEU CA  HA   sing N N 231 
LEU C   O    doub N N 232 
LEU C   OXT  sing N N 233 
LEU CB  CG   sing N N 234 
LEU CB  HB2  sing N N 235 
LEU CB  HB3  sing N N 236 
LEU CG  CD1  sing N N 237 
LEU CG  CD2  sing N N 238 
LEU CG  HG   sing N N 239 
LEU CD1 HD11 sing N N 240 
LEU CD1 HD12 sing N N 241 
LEU CD1 HD13 sing N N 242 
LEU CD2 HD21 sing N N 243 
LEU CD2 HD22 sing N N 244 
LEU CD2 HD23 sing N N 245 
LEU OXT HXT  sing N N 246 
LYS N   CA   sing N N 247 
LYS N   H    sing N N 248 
LYS N   H2   sing N N 249 
LYS CA  C    sing N N 250 
LYS CA  CB   sing N N 251 
LYS CA  HA   sing N N 252 
LYS C   O    doub N N 253 
LYS C   OXT  sing N N 254 
LYS CB  CG   sing N N 255 
LYS CB  HB2  sing N N 256 
LYS CB  HB3  sing N N 257 
LYS CG  CD   sing N N 258 
LYS CG  HG2  sing N N 259 
LYS CG  HG3  sing N N 260 
LYS CD  CE   sing N N 261 
LYS CD  HD2  sing N N 262 
LYS CD  HD3  sing N N 263 
LYS CE  NZ   sing N N 264 
LYS CE  HE2  sing N N 265 
LYS CE  HE3  sing N N 266 
LYS NZ  HZ1  sing N N 267 
LYS NZ  HZ2  sing N N 268 
LYS NZ  HZ3  sing N N 269 
LYS OXT HXT  sing N N 270 
MES O1  C2   sing N N 271 
MES O1  C6   sing N N 272 
MES C2  C3   sing N N 273 
MES C2  H21  sing N N 274 
MES C2  H22  sing N N 275 
MES C3  N4   sing N N 276 
MES C3  H31  sing N N 277 
MES C3  H32  sing N N 278 
MES N4  C5   sing N N 279 
MES N4  C7   sing N N 280 
MES N4  HN4  sing N N 281 
MES C5  C6   sing N N 282 
MES C5  H51  sing N N 283 
MES C5  H52  sing N N 284 
MES C6  H61  sing N N 285 
MES C6  H62  sing N N 286 
MES C7  C8   sing N N 287 
MES C7  H71  sing N N 288 
MES C7  H72  sing N N 289 
MES C8  S    sing N N 290 
MES C8  H81  sing N N 291 
MES C8  H82  sing N N 292 
MES S   O1S  doub N N 293 
MES S   O2S  doub N N 294 
MES S   O3S  sing N N 295 
MET N   CA   sing N N 296 
MET N   H    sing N N 297 
MET N   H2   sing N N 298 
MET CA  C    sing N N 299 
MET CA  CB   sing N N 300 
MET CA  HA   sing N N 301 
MET C   O    doub N N 302 
MET C   OXT  sing N N 303 
MET CB  CG   sing N N 304 
MET CB  HB2  sing N N 305 
MET CB  HB3  sing N N 306 
MET CG  SD   sing N N 307 
MET CG  HG2  sing N N 308 
MET CG  HG3  sing N N 309 
MET SD  CE   sing N N 310 
MET CE  HE1  sing N N 311 
MET CE  HE2  sing N N 312 
MET CE  HE3  sing N N 313 
MET OXT HXT  sing N N 314 
PHE N   CA   sing N N 315 
PHE N   H    sing N N 316 
PHE N   H2   sing N N 317 
PHE CA  C    sing N N 318 
PHE CA  CB   sing N N 319 
PHE CA  HA   sing N N 320 
PHE C   O    doub N N 321 
PHE C   OXT  sing N N 322 
PHE CB  CG   sing N N 323 
PHE CB  HB2  sing N N 324 
PHE CB  HB3  sing N N 325 
PHE CG  CD1  doub Y N 326 
PHE CG  CD2  sing Y N 327 
PHE CD1 CE1  sing Y N 328 
PHE CD1 HD1  sing N N 329 
PHE CD2 CE2  doub Y N 330 
PHE CD2 HD2  sing N N 331 
PHE CE1 CZ   doub Y N 332 
PHE CE1 HE1  sing N N 333 
PHE CE2 CZ   sing Y N 334 
PHE CE2 HE2  sing N N 335 
PHE CZ  HZ   sing N N 336 
PHE OXT HXT  sing N N 337 
PRO N   CA   sing N N 338 
PRO N   CD   sing N N 339 
PRO N   H    sing N N 340 
PRO CA  C    sing N N 341 
PRO CA  CB   sing N N 342 
PRO CA  HA   sing N N 343 
PRO C   O    doub N N 344 
PRO C   OXT  sing N N 345 
PRO CB  CG   sing N N 346 
PRO CB  HB2  sing N N 347 
PRO CB  HB3  sing N N 348 
PRO CG  CD   sing N N 349 
PRO CG  HG2  sing N N 350 
PRO CG  HG3  sing N N 351 
PRO CD  HD2  sing N N 352 
PRO CD  HD3  sing N N 353 
PRO OXT HXT  sing N N 354 
SER N   CA   sing N N 355 
SER N   H    sing N N 356 
SER N   H2   sing N N 357 
SER CA  C    sing N N 358 
SER CA  CB   sing N N 359 
SER CA  HA   sing N N 360 
SER C   O    doub N N 361 
SER C   OXT  sing N N 362 
SER CB  OG   sing N N 363 
SER CB  HB2  sing N N 364 
SER CB  HB3  sing N N 365 
SER OG  HG   sing N N 366 
SER OXT HXT  sing N N 367 
THR N   CA   sing N N 368 
THR N   H    sing N N 369 
THR N   H2   sing N N 370 
THR CA  C    sing N N 371 
THR CA  CB   sing N N 372 
THR CA  HA   sing N N 373 
THR C   O    doub N N 374 
THR C   OXT  sing N N 375 
THR CB  OG1  sing N N 376 
THR CB  CG2  sing N N 377 
THR CB  HB   sing N N 378 
THR OG1 HG1  sing N N 379 
THR CG2 HG21 sing N N 380 
THR CG2 HG22 sing N N 381 
THR CG2 HG23 sing N N 382 
THR OXT HXT  sing N N 383 
TRP N   CA   sing N N 384 
TRP N   H    sing N N 385 
TRP N   H2   sing N N 386 
TRP CA  C    sing N N 387 
TRP CA  CB   sing N N 388 
TRP CA  HA   sing N N 389 
TRP C   O    doub N N 390 
TRP C   OXT  sing N N 391 
TRP CB  CG   sing N N 392 
TRP CB  HB2  sing N N 393 
TRP CB  HB3  sing N N 394 
TRP CG  CD1  doub Y N 395 
TRP CG  CD2  sing Y N 396 
TRP CD1 NE1  sing Y N 397 
TRP CD1 HD1  sing N N 398 
TRP CD2 CE2  doub Y N 399 
TRP CD2 CE3  sing Y N 400 
TRP NE1 CE2  sing Y N 401 
TRP NE1 HE1  sing N N 402 
TRP CE2 CZ2  sing Y N 403 
TRP CE3 CZ3  doub Y N 404 
TRP CE3 HE3  sing N N 405 
TRP CZ2 CH2  doub Y N 406 
TRP CZ2 HZ2  sing N N 407 
TRP CZ3 CH2  sing Y N 408 
TRP CZ3 HZ3  sing N N 409 
TRP CH2 HH2  sing N N 410 
TRP OXT HXT  sing N N 411 
TYR N   CA   sing N N 412 
TYR N   H    sing N N 413 
TYR N   H2   sing N N 414 
TYR CA  C    sing N N 415 
TYR CA  CB   sing N N 416 
TYR CA  HA   sing N N 417 
TYR C   O    doub N N 418 
TYR C   OXT  sing N N 419 
TYR CB  CG   sing N N 420 
TYR CB  HB2  sing N N 421 
TYR CB  HB3  sing N N 422 
TYR CG  CD1  doub Y N 423 
TYR CG  CD2  sing Y N 424 
TYR CD1 CE1  sing Y N 425 
TYR CD1 HD1  sing N N 426 
TYR CD2 CE2  doub Y N 427 
TYR CD2 HD2  sing N N 428 
TYR CE1 CZ   doub Y N 429 
TYR CE1 HE1  sing N N 430 
TYR CE2 CZ   sing Y N 431 
TYR CE2 HE2  sing N N 432 
TYR CZ  OH   sing N N 433 
TYR OH  HH   sing N N 434 
TYR OXT HXT  sing N N 435 
VAL N   CA   sing N N 436 
VAL N   H    sing N N 437 
VAL N   H2   sing N N 438 
VAL CA  C    sing N N 439 
VAL CA  CB   sing N N 440 
VAL CA  HA   sing N N 441 
VAL C   O    doub N N 442 
VAL C   OXT  sing N N 443 
VAL CB  CG1  sing N N 444 
VAL CB  CG2  sing N N 445 
VAL CB  HB   sing N N 446 
VAL CG1 HG11 sing N N 447 
VAL CG1 HG12 sing N N 448 
VAL CG1 HG13 sing N N 449 
VAL CG2 HG21 sing N N 450 
VAL CG2 HG22 sing N N 451 
VAL CG2 HG23 sing N N 452 
VAL OXT HXT  sing N N 453 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                      ZN  
3 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                          MES 
4 'DIMETHYL SULFOXIDE'                                                            DMS 
5 '2-chloro-5-[(1H-imidazo[4,5-c]quinolin-2-ylsulfanyl)acetyl]benzenesulfonamide' E27 
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          'PDB entry 3HLJ' 
# 
