data_3S9T
# 
_entry.id   3S9T 
# 
_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   3S9T         pdb_00003s9t 10.2210/pdb3s9t/pdb 
RCSB  RCSB065941   ?            ?                   
WWPDB D_1000065941 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3SBI .                                                                                                                   
unspecified 
PDB 3S8X 'human carbonic anhydrase II with 4-{[(4-methyl-6-oxo-1,6-dihydro-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide' 
unspecified 
PDB 3SAX 'human carbonic anhydrase II with 2-chloro-5-{[(5-ethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'           
unspecified 
PDB 3SAP 'human carbonic anhydrase II with 4-{[(5-butyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'                    
unspecified 
PDB 3SBH 'human carbonic anhydrase II with 4-{[(4,6-dimethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'               
unspecified 
# 
_pdbx_database_status.entry_id                        3S9T 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2011-06-02 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Grazulis, S.'     1 ? 
'Manakova, E.'     2 ? 
'Tamulaitiene, G.' 3 ? 
# 
_citation.id                        primary 
_citation.title                     
'Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            51 
_citation.page_first                259 
_citation.page_last                 270 
_citation.year                      2012 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22440859 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2012.02.050 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1 ? 
primary 'Zubriene, A.'      2 ? 
primary 'Baranauskiene, L.' 3 ? 
primary 'Tamulaitiene, G.'  4 ? 
primary 'Manakova, E.'      5 ? 
primary 'Kairys, V.'        6 ? 
primary 'Grazulis, S.'      7 ? 
primary 'Tumkevicius, S.'   8 ? 
primary 'Matulis, D.'       9 ? 
# 
_cell.entry_id           3S9T 
_cell.length_a           42.012 
_cell.length_b           41.058 
_cell.length_c           71.839 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.150 
_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                         3S9T 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                        29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                    65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                          78.133    2   ?       ? ? ? 
4 non-polymer syn BICINE                                                                        163.172   1   ?       ? ? ? 
5 non-polymer syn '2-chloro-5-{[(4,6-dimethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' 371.862   1   ?       ? ? ? 
6 water       nat water                                                                         18.015    304 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3S9T 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                       ? 'C3 H7 N O2'          
89.093  
ARG 'L-peptide linking' y ARGININE                                                                      ? 'C6 H15 N4 O2 1'      
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                    ? 'C4 H8 N2 O3'         
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                               ? 'C4 H7 N O4'          
133.103 
BCN non-polymer         . BICINE                                                                        ? 'C6 H13 N O4'         
163.172 
CYS 'L-peptide linking' y CYSTEINE                                                                      ? 'C3 H7 N O2 S'        
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                          ? 'C2 H6 O S'           
78.133  
E49 non-polymer         . '2-chloro-5-{[(4,6-dimethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' ? 'C14 H14 Cl N3 O3 S2' 
371.862 
GLN 'L-peptide linking' y GLUTAMINE                                                                     ? 'C5 H10 N2 O3'        
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                               ? 'C5 H9 N O4'          
147.129 
GLY 'peptide linking'   y GLYCINE                                                                       ? 'C2 H5 N O2'          
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                     ? 'C6 H10 N3 O2 1'      
156.162 
HOH non-polymer         . WATER                                                                         ? 'H2 O'                
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                    ? 'C6 H13 N O2'         
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                       ? 'C6 H13 N O2'         
131.173 
LYS 'L-peptide linking' y LYSINE                                                                        ? 'C6 H15 N2 O2 1'      
147.195 
MET 'L-peptide linking' y METHIONINE                                                                    ? 'C5 H11 N O2 S'       
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                 ? 'C9 H11 N O2'         
165.189 
PRO 'L-peptide linking' y PROLINE                                                                       ? 'C5 H9 N O2'          
115.130 
SER 'L-peptide linking' y SERINE                                                                        ? 'C3 H7 N O3'          
105.093 
THR 'L-peptide linking' y THREONINE                                                                     ? 'C4 H9 N O3'          
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                    ? 'C11 H12 N2 O2'       
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                      ? 'C9 H11 N O3'         
181.189 
VAL 'L-peptide linking' y VALINE                                                                        ? 'C5 H11 N O2'         
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                    ? 'Zn 2'                
65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3S9T 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.6 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '2.4M Na-Malonate, pH 7, VAPOR DIFFUSION, temperature 298K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMosaic, 225 mm' 
_diffrn_detector.pdbx_collection_date   2010-11-13 
_diffrn_detector.details                'Detector swing-out angle up to 30 degrees' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Double crystal Si(111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9748 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X12' 
_diffrn_source.pdbx_wavelength_list        0.9748 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X12 
# 
_reflns.entry_id                     3S9T 
_reflns.d_resolution_high            1.300 
_reflns.d_resolution_low             69.673 
_reflns.number_all                   ? 
_reflns.number_obs                   58642 
_reflns.pdbx_Rmerge_I_obs            0.129 
_reflns.pdbx_netI_over_sigmaI        14.000 
_reflns.pdbx_Rsym_value              0.129 
_reflns.pdbx_redundancy              7.000 
_reflns.percent_possible_obs         100.000 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        10.8 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.30 1.37  ? 49079 ? 0.368 1.6 0.368 ? 5.80  ? 8514 100.00 1  1 
1.37 1.45  ? 46633 ? 0.313 1.9 0.313 ? 5.80  ? 8040 100.00 2  1 
1.45 1.55  ? 44120 ? 0.249 2.4 0.249 ? 5.80  ? 7581 100.00 3  1 
1.55 1.68  ? 41328 ? 0.206 3.0 0.206 ? 5.80  ? 7089 100.00 4  1 
1.68 1.84  ? 37889 ? 0.176 3.4 0.176 ? 5.80  ? 6510 100.00 5  1 
1.84 2.06  ? 34000 ? 0.151 3.9 0.151 ? 5.80  ? 5869 100.00 6  1 
2.06 2.37  ? 35918 ? 0.143 4.0 0.143 ? 6.90  ? 5206 100.00 7  1 
2.37 2.91  ? 55357 ? 0.136 4.1 0.136 ? 12.50 ? 4428 100.00 8  1 
2.91 4.11  ? 42709 ? 0.113 4.8 0.113 ? 12.40 ? 3452 100.00 9  1 
4.11 69.67 ? 22693 ? 0.106 5.1 0.106 ? 11.60 ? 1953 100.00 10 1 
# 
_refine.entry_id                                 3S9T 
_refine.ls_d_res_high                            1.300 
_refine.ls_d_res_low                             69.670 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    100.000 
_refine.ls_number_reflns_obs                     58625 
_refine.ls_number_reflns_all                     58625 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          0.148 
_refine.ls_R_factor_obs                          0.148 
_refine.ls_R_factor_R_work                       0.143 
_refine.ls_wR_factor_R_work                      0.144 
_refine.ls_R_factor_R_free                       0.192 
_refine.ls_wR_factor_R_free                      0.191 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  5908 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               14.204 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.580 
_refine.aniso_B[2][2]                            0.340 
_refine.aniso_B[3][3]                            -1.210 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.600 
_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                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          MR 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.864 
_refine.B_iso_max                                51.10 
_refine.B_iso_min                                5.11 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_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_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2059 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             304 
_refine_hist.number_atoms_total               2406 
_refine_hist.d_res_high                       1.300 
_refine_hist.d_res_low                        69.670 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d         2546 0.034  0.022  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      3469 2.641  1.968  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   316  6.990  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   116  34.353 25.086 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   426  13.316 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   8    21.041 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           363  0.203  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     1985 0.018  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            1182 0.240  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          1529 0.321  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    245  0.186  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      3    0.061  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   106  0.233  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 76   0.232  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              1537 3.185  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             2500 4.035  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              1009 5.479  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             969  6.921  4.500  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr       2546 3.716  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free        310  16.406 3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded      2471 10.158 3.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.300 
_refine_ls_shell.d_res_low                        1.334 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               100.000 
_refine_ls_shell.number_reflns_R_work             3869 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.202 
_refine_ls_shell.R_factor_R_free                  0.313 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             433 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                4302 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3S9T 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 2-chloro-5-{[(4,6-dimethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3S9T 
_struct_keywords.text            'drug design, sulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'lyase/lyase inhibitor' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  262 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  262 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  262 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E49 . N23 ? ? A ZN  262 A E49 266 1_555 ? ? ? ? ? ? ? 1.976 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E49 . S19 ? ? A ZN  262 A E49 266 1_555 ? ? ? ? ? ? ? 2.994 ? ? 
# 
_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 -1.45 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 13.40 
# 
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 ARG A 58  ? N ARG A 58  
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 DMS 263 ? 3  'BINDING SITE FOR RESIDUE DMS A 263' 
AC3 Software A DMS 264 ? 4  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A BCN 265 ? 9  'BINDING SITE FOR RESIDUE BCN A 265' 
AC5 Software A E49 266 ? 14 'BINDING SITE FOR RESIDUE E49 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  E49 F .   ? E49 A 266 . ? 1_555 ? 
5  AC2 3  GLN A 92  ? GLN A 92  . ? 1_555 ? 
6  AC2 3  PHE A 130 ? PHE A 131 . ? 1_555 ? 
7  AC2 3  E49 F .   ? E49 A 266 . ? 1_555 ? 
8  AC3 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
9  AC3 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
10 AC3 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
11 AC3 4  HOH G .   ? HOH A 534 . ? 1_555 ? 
12 AC4 9  LYS A 148 ? LYS A 149 . ? 1_555 ? 
13 AC4 9  LYS A 212 ? LYS A 213 . ? 1_555 ? 
14 AC4 9  GLU A 213 ? GLU A 214 . ? 1_555 ? 
15 AC4 9  PRO A 214 ? PRO A 215 . ? 1_555 ? 
16 AC4 9  HOH G .   ? HOH A 281 . ? 1_555 ? 
17 AC4 9  HOH G .   ? HOH A 370 . ? 1_555 ? 
18 AC4 9  HOH G .   ? HOH A 374 . ? 1_555 ? 
19 AC4 9  HOH G .   ? HOH A 463 . ? 1_555 ? 
20 AC4 9  HOH G .   ? HOH A 476 . ? 1_555 ? 
21 AC5 14 ASN A 62  ? ASN A 62  . ? 1_555 ? 
22 AC5 14 ASN A 67  ? ASN A 67  . ? 1_555 ? 
23 AC5 14 GLN A 92  ? GLN A 92  . ? 1_555 ? 
24 AC5 14 HIS A 94  ? HIS A 94  . ? 1_555 ? 
25 AC5 14 HIS A 96  ? HIS A 96  . ? 1_555 ? 
26 AC5 14 HIS A 119 ? HIS A 119 . ? 1_555 ? 
27 AC5 14 LEU A 140 ? LEU A 141 . ? 1_555 ? 
28 AC5 14 VAL A 142 ? VAL A 143 . ? 1_555 ? 
29 AC5 14 LEU A 197 ? LEU A 198 . ? 1_555 ? 
30 AC5 14 THR A 198 ? THR A 199 . ? 1_555 ? 
31 AC5 14 THR A 199 ? THR A 200 . ? 1_555 ? 
32 AC5 14 TRP A 208 ? TRP A 209 . ? 1_555 ? 
33 AC5 14 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
34 AC5 14 DMS C .   ? DMS A 263 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3S9T 
_atom_sites.fract_transf_matrix[1][1]   0.023803 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006003 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024356 
_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]   0.014356 
_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 3   ? 13.641  0.083   6.462   1.00 24.73 ? 3   HIS A N    1 
ATOM   2    C  CA   . HIS A 1 3   ? 13.287  -0.948  7.567   1.00 28.67 ? 3   HIS A CA   1 
ATOM   3    C  C    . HIS A 1 3   ? 12.179  -0.464  8.600   1.00 29.25 ? 3   HIS A C    1 
ATOM   4    O  O    . HIS A 1 3   ? 12.394  -0.427  9.908   1.00 33.58 ? 3   HIS A O    1 
ATOM   5    C  CB   . HIS A 1 3   ? 14.524  -1.364  8.376   1.00 27.32 ? 3   HIS A CB   1 
ATOM   6    C  CG   . HIS A 1 3   ? 14.306  -2.594  9.187   1.00 31.67 ? 3   HIS A CG   1 
ATOM   7    N  ND1  . HIS A 1 3   ? 13.909  -2.551  10.529  1.00 30.73 ? 3   HIS A ND1  1 
ATOM   8    C  CD2  . HIS A 1 3   ? 14.455  -3.927  8.850   1.00 29.78 ? 3   HIS A CD2  1 
ATOM   9    C  CE1  . HIS A 1 3   ? 13.869  -3.819  10.982  1.00 34.99 ? 3   HIS A CE1  1 
ATOM   10   N  NE2  . HIS A 1 3   ? 14.207  -4.661  10.002  1.00 30.80 ? 3   HIS A NE2  1 
ATOM   11   N  N    . HIS A 1 4   ? 10.966  -0.143  8.057   1.00 24.75 ? 4   HIS A N    1 
ATOM   12   C  CA   . HIS A 1 4   ? 9.935   0.403   8.889   1.00 22.70 ? 4   HIS A CA   1 
ATOM   13   C  C    . HIS A 1 4   ? 9.150   -0.724  9.525   1.00 17.79 ? 4   HIS A C    1 
ATOM   14   O  O    . HIS A 1 4   ? 9.383   -1.935  9.303   1.00 19.21 ? 4   HIS A O    1 
ATOM   15   C  CB   . HIS A 1 4   ? 9.057   1.322   8.088   1.00 27.77 ? 4   HIS A CB   1 
ATOM   16   C  CG   . HIS A 1 4   ? 8.616   0.798   6.747   1.00 36.54 ? 4   HIS A CG   1 
ATOM   17   N  ND1  . HIS A 1 4   ? 9.031   1.379   5.552   1.00 47.48 ? 4   HIS A ND1  1 
ATOM   18   C  CD2  . HIS A 1 4   ? 7.672   -0.126  6.403   1.00 45.62 ? 4   HIS A CD2  1 
ATOM   19   C  CE1  . HIS A 1 4   ? 8.403   0.803   4.533   1.00 51.06 ? 4   HIS A CE1  1 
ATOM   20   N  NE2  . HIS A 1 4   ? 7.569   -0.119  5.019   1.00 51.10 ? 4   HIS A NE2  1 
ATOM   21   N  N    . TRP A 1 5   ? 8.244   -0.327  10.315  1.00 15.61 ? 5   TRP A N    1 
ATOM   22   C  CA   . TRP A 1 5   ? 7.611   -1.400  11.161  1.00 13.86 ? 5   TRP A CA   1 
ATOM   23   C  C    . TRP A 1 5   ? 6.576   -2.139  10.395  1.00 14.19 ? 5   TRP A C    1 
ATOM   24   O  O    . TRP A 1 5   ? 6.027   -1.675  9.348   1.00 14.17 ? 5   TRP A O    1 
ATOM   25   C  CB   . TRP A 1 5   ? 6.925   -0.642  12.374  1.00 12.73 ? 5   TRP A CB   1 
ATOM   26   C  CG   . TRP A 1 5   ? 5.721   0.193   12.014  1.00 12.36 ? 5   TRP A CG   1 
ATOM   27   C  CD1  . TRP A 1 5   ? 5.699   1.518   11.752  1.00 14.96 ? 5   TRP A CD1  1 
ATOM   28   C  CD2  . TRP A 1 5   ? 4.388   -0.323  11.975  1.00 11.57 ? 5   TRP A CD2  1 
ATOM   29   N  NE1  . TRP A 1 5   ? 4.434   1.851   11.519  1.00 13.63 ? 5   TRP A NE1  1 
ATOM   30   C  CE2  . TRP A 1 5   ? 3.569   0.759   11.654  1.00 13.40 ? 5   TRP A CE2  1 
ATOM   31   C  CE3  . TRP A 1 5   ? 3.774   -1.580  12.297  1.00 11.85 ? 5   TRP A CE3  1 
ATOM   32   C  CZ2  . TRP A 1 5   ? 2.161   0.676   11.554  1.00 13.64 ? 5   TRP A CZ2  1 
ATOM   33   C  CZ3  . TRP A 1 5   ? 2.367   -1.704  12.107  1.00 11.20 ? 5   TRP A CZ3  1 
ATOM   34   C  CH2  . TRP A 1 5   ? 1.549   -0.538  11.794  1.00 13.19 ? 5   TRP A CH2  1 
ATOM   35   N  N    . GLY A 1 6   ? 6.346   -3.374  10.907  1.00 11.80 ? 6   GLY A N    1 
ATOM   36   C  CA   . GLY A 1 6   ? 5.319   -4.187  10.298  1.00 12.61 ? 6   GLY A CA   1 
ATOM   37   C  C    . GLY A 1 6   ? 4.982   -5.330  11.216  1.00 12.33 ? 6   GLY A C    1 
ATOM   38   O  O    . GLY A 1 6   ? 4.995   -5.182  12.429  1.00 11.85 ? 6   GLY A O    1 
ATOM   39   N  N    . TYR A 1 7   ? 4.751   -6.519  10.606  1.00 13.66 ? 7   TYR A N    1 
ATOM   40   C  CA   . TYR A 1 7   ? 4.216   -7.646  11.394  1.00 13.11 ? 7   TYR A CA   1 
ATOM   41   C  C    . TYR A 1 7   ? 5.192   -8.869  11.153  1.00 18.23 ? 7   TYR A C    1 
ATOM   42   O  O    . TYR A 1 7   ? 4.882   -9.956  11.746  1.00 22.27 ? 7   TYR A O    1 
ATOM   43   C  CB   . TYR A 1 7   ? 2.733   -7.981  11.084  1.00 12.02 ? 7   TYR A CB   1 
ATOM   44   C  CG   . TYR A 1 7   ? 1.864   -6.867  11.664  1.00 9.54  ? 7   TYR A CG   1 
ATOM   45   C  CD1  . TYR A 1 7   ? 1.575   -6.878  13.025  1.00 10.12 ? 7   TYR A CD1  1 
ATOM   46   C  CD2  . TYR A 1 7   ? 1.374   -5.845  10.861  1.00 9.32  ? 7   TYR A CD2  1 
ATOM   47   C  CE1  . TYR A 1 7   ? 0.686   -5.851  13.553  1.00 8.80  ? 7   TYR A CE1  1 
ATOM   48   C  CE2  . TYR A 1 7   ? 0.533   -4.860  11.388  1.00 8.75  ? 7   TYR A CE2  1 
ATOM   49   C  CZ   . TYR A 1 7   ? 0.188   -4.884  12.725  1.00 7.87  ? 7   TYR A CZ   1 
ATOM   50   O  OH   . TYR A 1 7   ? -0.659  -3.908  13.179  1.00 8.80  ? 7   TYR A OH   1 
ATOM   51   N  N    . GLY A 1 8   ? 6.328   -8.721  10.474  1.00 19.69 ? 8   GLY A N    1 
ATOM   52   C  CA   . GLY A 1 8   ? 7.250   -9.847  10.292  1.00 22.57 ? 8   GLY A CA   1 
ATOM   53   C  C    . GLY A 1 8   ? 8.245   -10.225 11.402  1.00 21.52 ? 8   GLY A C    1 
ATOM   54   O  O    . GLY A 1 8   ? 8.256   -9.667  12.543  1.00 25.81 ? 8   GLY A O    1 
ATOM   55   N  N    . LYS A 1 9   ? 9.160   -11.199 11.141  1.00 24.87 ? 9   LYS A N    1 
ATOM   56   C  CA   . LYS A 1 9   ? 10.141  -11.584 12.197  1.00 26.36 ? 9   LYS A CA   1 
ATOM   57   C  C    . LYS A 1 9   ? 11.093  -10.464 12.438  1.00 24.62 ? 9   LYS A C    1 
ATOM   58   O  O    . LYS A 1 9   ? 11.577  -10.319 13.670  1.00 24.60 ? 9   LYS A O    1 
ATOM   59   C  CB   . LYS A 1 9   ? 10.989  -12.742 11.766  1.00 29.63 ? 9   LYS A CB   1 
ATOM   60   C  CG   . LYS A 1 9   ? 12.064  -13.134 12.794  1.00 26.84 ? 9   LYS A CG   1 
ATOM   61   C  CD   . LYS A 1 9   ? 12.561  -14.624 12.425  1.00 34.93 ? 9   LYS A CD   1 
ATOM   62   C  CE   . LYS A 1 9   ? 13.799  -14.932 13.283  1.00 43.47 ? 9   LYS A CE   1 
ATOM   63   N  NZ   . LYS A 1 9   ? 15.185  -14.911 12.572  1.00 49.73 ? 9   LYS A NZ   1 
ATOM   64   N  N    . HIS A 1 10  ? 11.356  -9.679  11.362  1.00 19.26 ? 10  HIS A N    1 
ATOM   65   C  CA   . HIS A 1 10  ? 12.388  -8.720  11.619  1.00 20.44 ? 10  HIS A CA   1 
ATOM   66   C  C    . HIS A 1 10  ? 11.867  -7.357  11.900  1.00 17.04 ? 10  HIS A C    1 
ATOM   67   O  O    . HIS A 1 10  ? 12.699  -6.518  12.301  1.00 19.28 ? 10  HIS A O    1 
ATOM   68   C  CB   . HIS A 1 10  ? 13.360  -8.681  10.455  1.00 18.99 ? 10  HIS A CB   1 
ATOM   69   C  CG   . HIS A 1 10  ? 14.069  -10.049 10.333  1.00 23.94 ? 10  HIS A CG   1 
ATOM   70   N  ND1  . HIS A 1 10  ? 15.108  -10.461 11.163  1.00 24.08 ? 10  HIS A ND1  1 
ATOM   71   C  CD2  . HIS A 1 10  ? 13.808  -11.069 9.507   1.00 24.90 ? 10  HIS A CD2  1 
ATOM   72   C  CE1  . HIS A 1 10  ? 15.538  -11.670 10.782  1.00 25.62 ? 10  HIS A CE1  1 
ATOM   73   N  NE2  . HIS A 1 10  ? 14.699  -12.093 9.806   1.00 22.99 ? 10  HIS A NE2  1 
ATOM   74   N  N    . ASN A 1 11  ? 10.505  -7.088  11.687  1.00 16.18 ? 11  ASN A N    1 
ATOM   75   C  CA   . ASN A 1 11  ? 10.035  -5.753  12.011  1.00 14.19 ? 11  ASN A CA   1 
ATOM   76   C  C    . ASN A 1 11  ? 8.711   -5.787  12.746  1.00 13.13 ? 11  ASN A C    1 
ATOM   77   O  O    . ASN A 1 11  ? 8.064   -4.750  12.822  1.00 14.31 ? 11  ASN A O    1 
ATOM   78   C  CB   . ASN A 1 11  ? 9.872   -4.961  10.702  1.00 14.39 ? 11  ASN A CB   1 
ATOM   79   C  CG   . ASN A 1 11  ? 8.812   -5.577  9.765   1.00 15.48 ? 11  ASN A CG   1 
ATOM   80   O  OD1  . ASN A 1 11  ? 8.228   -6.651  10.102  1.00 17.56 ? 11  ASN A OD1  1 
ATOM   81   N  ND2  . ASN A 1 11  ? 8.485   -4.908  8.632   1.00 18.85 ? 11  ASN A ND2  1 
ATOM   82   N  N    . GLY A 1 12  ? 8.354   -6.892  13.353  1.00 13.62 ? 12  GLY A N    1 
ATOM   83   C  CA   . GLY A 1 12  ? 7.049   -7.065  13.996  1.00 12.23 ? 12  GLY A CA   1 
ATOM   84   C  C    . GLY A 1 12  ? 7.053   -6.537  15.428  1.00 11.24 ? 12  GLY A C    1 
ATOM   85   O  O    . GLY A 1 12  ? 7.996   -5.832  15.888  1.00 11.79 ? 12  GLY A O    1 
ATOM   86   N  N    . PRO A 1 13  ? 5.956   -6.801  16.146  1.00 11.11 ? 13  PRO A N    1 
ATOM   87   C  CA   . PRO A 1 13  ? 5.762   -6.320  17.475  1.00 12.11 ? 13  PRO A CA   1 
ATOM   88   C  C    . PRO A 1 13  ? 6.913   -6.298  18.477  1.00 11.18 ? 13  PRO A C    1 
ATOM   89   O  O    . PRO A 1 13  ? 7.072   -5.290  19.251  1.00 12.73 ? 13  PRO A O    1 
ATOM   90   C  CB   . PRO A 1 13  ? 4.537   -7.204  17.975  1.00 13.43 ? 13  PRO A CB   1 
ATOM   91   C  CG   . PRO A 1 13  ? 3.738   -7.327  16.706  1.00 14.01 ? 13  PRO A CG   1 
ATOM   92   C  CD   . PRO A 1 13  ? 4.805   -7.571  15.676  1.00 11.90 ? 13  PRO A CD   1 
ATOM   93   N  N    A GLU A 1 14  ? 7.716   -7.328  18.417  0.50 11.84 ? 14  GLU A N    1 
ATOM   94   N  N    B GLU A 1 14  ? 7.736   -7.358  18.516  0.50 12.00 ? 14  GLU A N    1 
ATOM   95   C  CA   A GLU A 1 14  ? 8.794   -7.469  19.328  0.50 14.04 ? 14  GLU A CA   1 
ATOM   96   C  CA   B GLU A 1 14  ? 8.835   -7.340  19.468  0.50 14.03 ? 14  GLU A CA   1 
ATOM   97   C  C    A GLU A 1 14  ? 9.957   -6.478  19.051  0.50 12.68 ? 14  GLU A C    1 
ATOM   98   C  C    B GLU A 1 14  ? 9.976   -6.363  19.111  0.50 12.49 ? 14  GLU A C    1 
ATOM   99   O  O    A GLU A 1 14  ? 10.825  -6.323  19.899  0.50 14.72 ? 14  GLU A O    1 
ATOM   100  O  O    B GLU A 1 14  ? 10.856  -6.106  19.964  0.50 15.00 ? 14  GLU A O    1 
ATOM   101  C  CB   A GLU A 1 14  ? 9.297   -8.910  19.211  0.50 16.73 ? 14  GLU A CB   1 
ATOM   102  C  CB   B GLU A 1 14  ? 9.481   -8.717  19.529  0.50 16.77 ? 14  GLU A CB   1 
ATOM   103  C  CG   A GLU A 1 14  ? 10.065  -9.188  17.928  0.50 16.29 ? 14  GLU A CG   1 
ATOM   104  C  CG   B GLU A 1 14  ? 8.508   -9.841  19.840  0.50 17.27 ? 14  GLU A CG   1 
ATOM   105  C  CD   A GLU A 1 14  ? 9.212   -9.848  16.862  0.50 18.39 ? 14  GLU A CD   1 
ATOM   106  C  CD   B GLU A 1 14  ? 7.802   -9.634  21.163  0.50 28.05 ? 14  GLU A CD   1 
ATOM   107  O  OE1  A GLU A 1 14  ? 8.030   -9.460  16.721  0.50 13.49 ? 14  GLU A OE1  1 
ATOM   108  O  OE1  B GLU A 1 14  ? 8.493   -9.511  22.192  0.50 33.94 ? 14  GLU A OE1  1 
ATOM   109  O  OE2  A GLU A 1 14  ? 9.716   -10.751 16.168  0.50 16.30 ? 14  GLU A OE2  1 
ATOM   110  O  OE2  B GLU A 1 14  ? 6.554   -9.578  21.175  0.50 31.80 ? 14  GLU A OE2  1 
ATOM   111  N  N    . HIS A 1 15  ? 9.949   -5.827  17.871  1.00 11.03 ? 15  HIS A N    1 
ATOM   112  C  CA   . HIS A 1 15  ? 10.993  -4.834  17.541  1.00 11.30 ? 15  HIS A CA   1 
ATOM   113  C  C    . HIS A 1 15  ? 10.466  -3.396  17.728  1.00 10.77 ? 15  HIS A C    1 
ATOM   114  O  O    . HIS A 1 15  ? 11.304  -2.467  17.674  1.00 12.98 ? 15  HIS A O    1 
ATOM   115  C  CB   . HIS A 1 15  ? 11.271  -5.006  16.044  1.00 11.22 ? 15  HIS A CB   1 
ATOM   116  C  CG   . HIS A 1 15  ? 12.031  -6.248  15.808  1.00 13.19 ? 15  HIS A CG   1 
ATOM   117  N  ND1  . HIS A 1 15  ? 13.410  -6.288  15.874  1.00 15.92 ? 15  HIS A ND1  1 
ATOM   118  C  CD2  . HIS A 1 15  ? 11.552  -7.467  15.434  1.00 15.82 ? 15  HIS A CD2  1 
ATOM   119  C  CE1  . HIS A 1 15  ? 13.779  -7.516  15.590  1.00 22.43 ? 15  HIS A CE1  1 
ATOM   120  N  NE2  . HIS A 1 15  ? 12.701  -8.264  15.387  1.00 18.14 ? 15  HIS A NE2  1 
ATOM   121  N  N    . TRP A 1 16  ? 9.159   -3.112  17.851  1.00 10.28 ? 16  TRP A N    1 
ATOM   122  C  CA   . TRP A 1 16  ? 8.646   -1.819  17.757  1.00 9.67  ? 16  TRP A CA   1 
ATOM   123  C  C    . TRP A 1 16  ? 9.228   -0.847  18.783  1.00 11.29 ? 16  TRP A C    1 
ATOM   124  O  O    . TRP A 1 16  ? 9.284   0.391   18.530  1.00 11.54 ? 16  TRP A O    1 
ATOM   125  C  CB   . TRP A 1 16  ? 7.099   -1.899  17.908  1.00 11.06 ? 16  TRP A CB   1 
ATOM   126  C  CG   . TRP A 1 16  ? 6.441   -2.534  16.776  1.00 9.71  ? 16  TRP A CG   1 
ATOM   127  C  CD1  . TRP A 1 16  ? 6.956   -2.931  15.556  1.00 9.89  ? 16  TRP A CD1  1 
ATOM   128  C  CD2  . TRP A 1 16  ? 5.002   -2.871  16.723  1.00 9.28  ? 16  TRP A CD2  1 
ATOM   129  N  NE1  . TRP A 1 16  ? 5.980   -3.560  14.778  1.00 9.22  ? 16  TRP A NE1  1 
ATOM   130  C  CE2  . TRP A 1 16  ? 4.772   -3.412  15.438  1.00 8.72  ? 16  TRP A CE2  1 
ATOM   131  C  CE3  . TRP A 1 16  ? 3.926   -2.661  17.616  1.00 9.23  ? 16  TRP A CE3  1 
ATOM   132  C  CZ2  . TRP A 1 16  ? 3.498   -3.914  15.099  1.00 8.70  ? 16  TRP A CZ2  1 
ATOM   133  C  CZ3  . TRP A 1 16  ? 2.692   -3.206  17.234  1.00 9.33  ? 16  TRP A CZ3  1 
ATOM   134  C  CH2  . TRP A 1 16  ? 2.476   -3.658  15.971  1.00 7.99  ? 16  TRP A CH2  1 
ATOM   135  N  N    . HIS A 1 17  ? 9.639   -1.349  19.945  1.00 11.51 ? 17  HIS A N    1 
ATOM   136  C  CA   . HIS A 1 17  ? 10.112  -0.584  21.019  1.00 12.38 ? 17  HIS A CA   1 
ATOM   137  C  C    . HIS A 1 17  ? 11.382  0.218   20.648  1.00 13.97 ? 17  HIS A C    1 
ATOM   138  O  O    . HIS A 1 17  ? 11.595  1.299   21.274  1.00 13.58 ? 17  HIS A O    1 
ATOM   139  C  CB   . HIS A 1 17  ? 10.392  -1.330  22.281  1.00 10.95 ? 17  HIS A CB   1 
ATOM   140  C  CG   . HIS A 1 17  ? 11.586  -2.208  22.206  1.00 11.92 ? 17  HIS A CG   1 
ATOM   141  N  ND1  . HIS A 1 17  ? 12.810  -1.795  22.689  1.00 16.36 ? 17  HIS A ND1  1 
ATOM   142  C  CD2  . HIS A 1 17  ? 11.812  -3.408  21.619  1.00 14.32 ? 17  HIS A CD2  1 
ATOM   143  C  CE1  . HIS A 1 17  ? 13.718  -2.709  22.494  1.00 18.18 ? 17  HIS A CE1  1 
ATOM   144  N  NE2  . HIS A 1 17  ? 13.182  -3.681  21.815  1.00 14.85 ? 17  HIS A NE2  1 
ATOM   145  N  N    . LYS A 1 18  ? 12.134  -0.218  19.647  1.00 14.03 ? 18  LYS A N    1 
ATOM   146  C  CA   . LYS A 1 18  ? 13.350  0.515   19.325  1.00 14.15 ? 18  LYS A CA   1 
ATOM   147  C  C    . LYS A 1 18  ? 12.981  1.869   18.674  1.00 14.80 ? 18  LYS A C    1 
ATOM   148  O  O    . LYS A 1 18  ? 13.593  2.874   18.999  1.00 20.78 ? 18  LYS A O    1 
ATOM   149  C  CB   . LYS A 1 18  ? 14.181  -0.367  18.409  1.00 13.45 ? 18  LYS A CB   1 
ATOM   150  C  CG   . LYS A 1 18  ? 14.821  -1.491  19.142  1.00 13.76 ? 18  LYS A CG   1 
ATOM   151  C  CD   . LYS A 1 18  ? 15.565  -2.492  18.172  1.00 15.56 ? 18  LYS A CD   1 
ATOM   152  C  CE   . LYS A 1 18  ? 14.539  -3.525  17.571  1.00 14.32 ? 18  LYS A CE   1 
ATOM   153  N  NZ   . LYS A 1 18  ? 15.197  -4.358  16.472  1.00 14.87 ? 18  LYS A NZ   1 
ATOM   154  N  N    . ASP A 1 19  ? 12.012  1.901   17.710  1.00 13.27 ? 19  ASP A N    1 
ATOM   155  C  CA   . ASP A 1 19  ? 11.572  3.160   17.182  1.00 15.06 ? 19  ASP A CA   1 
ATOM   156  C  C    . ASP A 1 19  ? 10.523  3.874   18.066  1.00 14.13 ? 19  ASP A C    1 
ATOM   157  O  O    . ASP A 1 19  ? 10.434  5.083   17.948  1.00 15.41 ? 19  ASP A O    1 
ATOM   158  C  CB   . ASP A 1 19  ? 11.060  3.063   15.780  1.00 18.18 ? 19  ASP A CB   1 
ATOM   159  C  CG   . ASP A 1 19  ? 12.131  2.975   14.692  1.00 20.43 ? 19  ASP A CG   1 
ATOM   160  O  OD1  . ASP A 1 19  ? 13.173  3.508   14.893  1.00 23.61 ? 19  ASP A OD1  1 
ATOM   161  O  OD2  . ASP A 1 19  ? 11.843  2.461   13.545  1.00 31.79 ? 19  ASP A OD2  1 
ATOM   162  N  N    . PHE A 1 20  ? 9.776   3.128   18.900  1.00 13.05 ? 20  PHE A N    1 
ATOM   163  C  CA   . PHE A 1 20  ? 8.725   3.700   19.640  1.00 12.77 ? 20  PHE A CA   1 
ATOM   164  C  C    . PHE A 1 20  ? 8.815   3.194   21.095  1.00 13.01 ? 20  PHE A C    1 
ATOM   165  O  O    . PHE A 1 20  ? 8.173   2.199   21.456  1.00 12.25 ? 20  PHE A O    1 
ATOM   166  C  CB   . PHE A 1 20  ? 7.366   3.264   19.040  1.00 13.53 ? 20  PHE A CB   1 
ATOM   167  C  CG   . PHE A 1 20  ? 7.277   3.569   17.554  1.00 12.89 ? 20  PHE A CG   1 
ATOM   168  C  CD1  . PHE A 1 20  ? 6.898   4.924   17.188  1.00 14.34 ? 20  PHE A CD1  1 
ATOM   169  C  CD2  . PHE A 1 20  ? 7.650   2.695   16.553  1.00 13.98 ? 20  PHE A CD2  1 
ATOM   170  C  CE1  . PHE A 1 20  ? 6.854   5.228   15.819  1.00 15.65 ? 20  PHE A CE1  1 
ATOM   171  C  CE2  . PHE A 1 20  ? 7.612   3.009   15.174  1.00 15.96 ? 20  PHE A CE2  1 
ATOM   172  C  CZ   . PHE A 1 20  ? 7.202   4.311   14.841  1.00 15.00 ? 20  PHE A CZ   1 
ATOM   173  N  N    . PRO A 1 21  ? 9.686   3.793   21.869  1.00 13.42 ? 21  PRO A N    1 
ATOM   174  C  CA   . PRO A 1 21  ? 9.919   3.277   23.222  1.00 12.97 ? 21  PRO A CA   1 
ATOM   175  C  C    . PRO A 1 21  ? 8.693   3.171   24.092  1.00 12.14 ? 21  PRO A C    1 
ATOM   176  O  O    . PRO A 1 21  ? 8.708   2.407   25.070  1.00 12.61 ? 21  PRO A O    1 
ATOM   177  C  CB   . PRO A 1 21  ? 11.057  4.166   23.833  1.00 15.01 ? 21  PRO A CB   1 
ATOM   178  C  CG   . PRO A 1 21  ? 11.097  5.261   22.809  1.00 18.74 ? 21  PRO A CG   1 
ATOM   179  C  CD   . PRO A 1 21  ? 10.648  4.876   21.468  1.00 12.51 ? 21  PRO A CD   1 
ATOM   180  N  N    A ILE A 1 22  ? 7.625   3.957   23.839  0.50 10.82 ? 22  ILE A N    1 
ATOM   181  N  N    B ILE A 1 22  ? 7.645   3.959   23.716  0.50 10.96 ? 22  ILE A N    1 
ATOM   182  C  CA   A ILE A 1 22  ? 6.416   3.784   24.678  0.50 9.84  ? 22  ILE A CA   1 
ATOM   183  C  CA   B ILE A 1 22  ? 6.348   3.889   24.406  0.50 10.50 ? 22  ILE A CA   1 
ATOM   184  C  C    A ILE A 1 22  ? 5.811   2.372   24.502  0.50 9.81  ? 22  ILE A C    1 
ATOM   185  C  C    B ILE A 1 22  ? 5.709   2.475   24.295  0.50 9.77  ? 22  ILE A C    1 
ATOM   186  O  O    A ILE A 1 22  ? 4.983   2.002   25.332  0.50 8.76  ? 22  ILE A O    1 
ATOM   187  O  O    B ILE A 1 22  ? 4.765   2.180   24.959  0.50 10.91 ? 22  ILE A O    1 
ATOM   188  C  CB   A ILE A 1 22  ? 5.330   4.848   24.302  0.50 9.22  ? 22  ILE A CB   1 
ATOM   189  C  CB   B ILE A 1 22  ? 5.403   5.058   23.910  0.50 11.77 ? 22  ILE A CB   1 
ATOM   190  C  CG1  A ILE A 1 22  ? 4.322   5.121   25.400  0.50 12.69 ? 22  ILE A CG1  1 
ATOM   191  C  CG1  B ILE A 1 22  ? 4.328   5.427   24.950  0.50 10.36 ? 22  ILE A CG1  1 
ATOM   192  C  CG2  A ILE A 1 22  ? 4.700   4.445   22.948  0.50 10.27 ? 22  ILE A CG2  1 
ATOM   193  C  CG2  B ILE A 1 22  ? 4.805   4.709   22.507  0.50 12.56 ? 22  ILE A CG2  1 
ATOM   194  C  CD1  A ILE A 1 22  ? 4.896   5.801   26.490  0.50 15.76 ? 22  ILE A CD1  1 
ATOM   195  C  CD1  B ILE A 1 22  ? 3.413   6.462   24.631  0.50 9.63  ? 22  ILE A CD1  1 
ATOM   196  N  N    . ALA A 1 23  ? 6.283   1.554   23.508  1.00 10.34 ? 23  ALA A N    1 
ATOM   197  C  CA   . ALA A 1 23  ? 5.803   0.235   23.408  1.00 10.26 ? 23  ALA A CA   1 
ATOM   198  C  C    . ALA A 1 23  ? 5.927   -0.522  24.762  1.00 10.21 ? 23  ALA A C    1 
ATOM   199  O  O    . ALA A 1 23  ? 5.191   -1.536  24.941  1.00 10.79 ? 23  ALA A O    1 
ATOM   200  C  CB   . ALA A 1 23  ? 6.709   -0.532  22.374  1.00 10.95 ? 23  ALA A CB   1 
ATOM   201  N  N    . LYS A 1 24  ? 6.858   -0.083  25.645  1.00 10.86 ? 24  LYS A N    1 
ATOM   202  C  CA   . LYS A 1 24  ? 7.047   -0.686  26.950  1.00 12.23 ? 24  LYS A CA   1 
ATOM   203  C  C    . LYS A 1 24  ? 6.473   0.216   28.038  1.00 12.38 ? 24  LYS A C    1 
ATOM   204  O  O    . LYS A 1 24  ? 6.798   0.068   29.231  1.00 15.75 ? 24  LYS A O    1 
ATOM   205  C  CB   . LYS A 1 24  ? 8.490   -1.048  27.236  1.00 12.22 ? 24  LYS A CB   1 
ATOM   206  C  CG   . LYS A 1 24  ? 9.102   -2.022  26.242  1.00 14.39 ? 24  LYS A CG   1 
ATOM   207  C  CD   . LYS A 1 24  ? 10.634  -2.262  26.717  1.00 18.25 ? 24  LYS A CD   1 
ATOM   208  C  CE   . LYS A 1 24  ? 11.313  -3.059  25.647  1.00 22.34 ? 24  LYS A CE   1 
ATOM   209  N  NZ   . LYS A 1 24  ? 10.858  -4.426  25.523  1.00 29.87 ? 24  LYS A NZ   1 
ATOM   210  N  N    . GLY A 1 25  ? 5.437   0.975   27.675  1.00 12.14 ? 25  GLY A N    1 
ATOM   211  C  CA   . GLY A 1 25  ? 4.866   1.950   28.602  1.00 12.16 ? 25  GLY A CA   1 
ATOM   212  C  C    . GLY A 1 25  ? 3.859   1.351   29.541  1.00 11.43 ? 25  GLY A C    1 
ATOM   213  O  O    . GLY A 1 25  ? 3.705   0.157   29.647  1.00 14.01 ? 25  GLY A O    1 
ATOM   214  N  N    . GLU A 1 26  ? 3.239   2.261   30.270  1.00 12.93 ? 26  GLU A N    1 
ATOM   215  C  CA   . GLU A 1 26  ? 2.317   1.870   31.340  1.00 12.60 ? 26  GLU A CA   1 
ATOM   216  C  C    . GLU A 1 26  ? 0.887   1.642   31.005  1.00 11.32 ? 26  GLU A C    1 
ATOM   217  O  O    . GLU A 1 26  ? 0.150   1.145   31.846  1.00 13.84 ? 26  GLU A O    1 
ATOM   218  C  CB   . GLU A 1 26  ? 2.386   2.948   32.444  1.00 16.12 ? 26  GLU A CB   1 
ATOM   219  C  CG   . GLU A 1 26  ? 3.765   3.149   33.092  1.00 17.48 ? 26  GLU A CG   1 
ATOM   220  C  CD   . GLU A 1 26  ? 4.328   1.860   33.679  1.00 23.71 ? 26  GLU A CD   1 
ATOM   221  O  OE1  . GLU A 1 26  ? 3.670   1.285   34.565  1.00 29.70 ? 26  GLU A OE1  1 
ATOM   222  O  OE2  . GLU A 1 26  ? 5.412   1.406   33.249  1.00 29.76 ? 26  GLU A OE2  1 
ATOM   223  N  N    . ARG A 1 27  ? 0.500   1.995   29.756  1.00 10.28 ? 27  ARG A N    1 
ATOM   224  C  CA   . ARG A 1 27  ? -0.921  1.737   29.410  1.00 8.36  ? 27  ARG A CA   1 
ATOM   225  C  C    . ARG A 1 27  ? -0.949  1.272   27.924  1.00 7.71  ? 27  ARG A C    1 
ATOM   226  O  O    . ARG A 1 27  ? -1.604  1.903   27.081  1.00 8.65  ? 27  ARG A O    1 
ATOM   227  C  CB   . ARG A 1 27  ? -1.878  2.904   29.698  1.00 11.51 ? 27  ARG A CB   1 
ATOM   228  C  CG   . ARG A 1 27  ? -1.393  4.229   29.095  1.00 14.11 ? 27  ARG A CG   1 
ATOM   229  C  CD   . ARG A 1 27  ? -2.368  5.384   29.299  1.00 16.45 ? 27  ARG A CD   1 
ATOM   230  N  NE   . ARG A 1 27  ? -3.538  5.297   28.427  1.00 15.15 ? 27  ARG A NE   1 
ATOM   231  C  CZ   . ARG A 1 27  ? -4.475  6.231   28.337  1.00 12.24 ? 27  ARG A CZ   1 
ATOM   232  N  NH1  . ARG A 1 27  ? -4.385  7.341   29.064  1.00 14.04 ? 27  ARG A NH1  1 
ATOM   233  N  NH2  . ARG A 1 27  ? -5.506  6.069   27.517  1.00 12.90 ? 27  ARG A NH2  1 
ATOM   234  N  N    . GLN A 1 28  ? -0.202  0.154   27.642  1.00 7.46  ? 28  GLN A N    1 
ATOM   235  C  CA   . GLN A 1 28  ? -0.199  -0.339  26.266  1.00 6.84  ? 28  GLN A CA   1 
ATOM   236  C  C    . GLN A 1 28  ? -1.358  -1.311  25.977  1.00 6.49  ? 28  GLN A C    1 
ATOM   237  O  O    . GLN A 1 28  ? -1.865  -1.994  26.872  1.00 8.21  ? 28  GLN A O    1 
ATOM   238  C  CB   . GLN A 1 28  ? 1.153   -1.072  25.974  1.00 8.56  ? 28  GLN A CB   1 
ATOM   239  C  CG   . GLN A 1 28  ? 2.246   0.077   25.947  1.00 7.99  ? 28  GLN A CG   1 
ATOM   240  C  CD   . GLN A 1 28  ? 2.127   0.822   24.638  1.00 9.11  ? 28  GLN A CD   1 
ATOM   241  O  OE1  . GLN A 1 28  ? 2.275   0.311   23.549  1.00 8.35  ? 28  GLN A OE1  1 
ATOM   242  N  NE2  . GLN A 1 28  ? 1.812   2.157   24.755  1.00 8.23  ? 28  GLN A NE2  1 
ATOM   243  N  N    . SER A 1 29  ? -1.713  -1.396  24.691  1.00 5.91  ? 29  SER A N    1 
ATOM   244  C  CA   . SER A 1 29  ? -2.804  -2.247  24.234  1.00 6.30  ? 29  SER A CA   1 
ATOM   245  C  C    . SER A 1 29  ? -2.291  -3.138  23.100  1.00 6.13  ? 29  SER A C    1 
ATOM   246  O  O    . SER A 1 29  ? -1.334  -2.785  22.433  1.00 7.14  ? 29  SER A O    1 
ATOM   247  C  CB   . SER A 1 29  ? -3.947  -1.401  23.699  1.00 6.67  ? 29  SER A CB   1 
ATOM   248  O  OG   . SER A 1 29  ? -4.580  -0.675  24.784  1.00 6.91  ? 29  SER A OG   1 
ATOM   249  N  N    . PRO A 1 30  ? -2.918  -4.281  22.868  1.00 6.83  ? 30  PRO A N    1 
ATOM   250  C  CA   . PRO A 1 30  ? -4.047  -4.864  23.564  1.00 6.48  ? 30  PRO A CA   1 
ATOM   251  C  C    . PRO A 1 30  ? -3.693  -5.487  24.887  1.00 6.38  ? 30  PRO A C    1 
ATOM   252  O  O    . PRO A 1 30  ? -2.459  -5.535  25.216  1.00 7.47  ? 30  PRO A O    1 
ATOM   253  C  CB   . PRO A 1 30  ? -4.625  -5.838  22.559  1.00 6.84  ? 30  PRO A CB   1 
ATOM   254  C  CG   . PRO A 1 30  ? -3.319  -6.458  21.981  1.00 7.16  ? 30  PRO A CG   1 
ATOM   255  C  CD   . PRO A 1 30  ? -2.393  -5.219  21.814  1.00 7.70  ? 30  PRO A CD   1 
ATOM   256  N  N    . VAL A 1 31  ? -4.669  -6.072  25.561  1.00 6.18  ? 31  VAL A N    1 
ATOM   257  C  CA   . VAL A 1 31  ? -4.461  -6.798  26.794  1.00 7.58  ? 31  VAL A CA   1 
ATOM   258  C  C    . VAL A 1 31  ? -5.328  -8.043  26.736  1.00 7.24  ? 31  VAL A C    1 
ATOM   259  O  O    . VAL A 1 31  ? -6.327  -8.078  26.012  1.00 6.88  ? 31  VAL A O    1 
ATOM   260  C  CB   . VAL A 1 31  ? -4.785  -6.029  28.078  1.00 7.79  ? 31  VAL A CB   1 
ATOM   261  C  CG1  . VAL A 1 31  ? -3.851  -4.786  28.185  1.00 10.69 ? 31  VAL A CG1  1 
ATOM   262  C  CG2  . VAL A 1 31  ? -6.271  -5.523  28.103  1.00 8.37  ? 31  VAL A CG2  1 
ATOM   263  N  N    . ASP A 1 32  ? -4.984  -9.017  27.597  1.00 7.32  ? 32  ASP A N    1 
ATOM   264  C  CA   . ASP A 1 32  ? -5.894  -10.097 27.925  1.00 7.01  ? 32  ASP A CA   1 
ATOM   265  C  C    . ASP A 1 32  ? -6.972  -9.566  28.883  1.00 8.15  ? 32  ASP A C    1 
ATOM   266  O  O    . ASP A 1 32  ? -6.707  -8.921  29.873  1.00 9.21  ? 32  ASP A O    1 
ATOM   267  C  CB   . ASP A 1 32  ? -5.112  -11.297 28.498  1.00 8.65  ? 32  ASP A CB   1 
ATOM   268  C  CG   . ASP A 1 32  ? -6.102  -12.506 28.809  1.00 8.53  ? 32  ASP A CG   1 
ATOM   269  O  OD1  . ASP A 1 32  ? -6.778  -12.905 27.860  1.00 8.71  ? 32  ASP A OD1  1 
ATOM   270  O  OD2  . ASP A 1 32  ? -6.158  -12.856 30.033  1.00 11.60 ? 32  ASP A OD2  1 
ATOM   271  N  N    . ILE A 1 33  ? -8.222  -9.892  28.604  1.00 7.11  ? 33  ILE A N    1 
ATOM   272  C  CA   . ILE A 1 33  ? -9.301  -9.472  29.477  1.00 9.32  ? 33  ILE A CA   1 
ATOM   273  C  C    . ILE A 1 33  ? -9.627  -10.766 30.326  1.00 8.67  ? 33  ILE A C    1 
ATOM   274  O  O    . ILE A 1 33  ? -10.121 -11.761 29.829  1.00 9.42  ? 33  ILE A O    1 
ATOM   275  C  CB   . ILE A 1 33  ? -10.583 -9.145  28.641  1.00 9.23  ? 33  ILE A CB   1 
ATOM   276  C  CG1  . ILE A 1 33  ? -10.153 -7.865  27.808  1.00 8.53  ? 33  ILE A CG1  1 
ATOM   277  C  CG2  . ILE A 1 33  ? -11.751 -8.866  29.640  1.00 11.43 ? 33  ILE A CG2  1 
ATOM   278  C  CD1  . ILE A 1 33  ? -11.274 -7.572  26.678  1.00 10.09 ? 33  ILE A CD1  1 
ATOM   279  N  N    A ASP A 1 34  ? -9.225  -10.706 31.590  0.50 9.56  ? 34  ASP A N    1 
ATOM   280  N  N    B ASP A 1 34  ? -9.186  -10.716 31.582  0.50 10.14 ? 34  ASP A N    1 
ATOM   281  C  CA   A ASP A 1 34  ? -9.520  -11.809 32.495  0.50 11.30 ? 34  ASP A CA   1 
ATOM   282  C  CA   B ASP A 1 34  ? -9.482  -11.778 32.564  0.50 11.86 ? 34  ASP A CA   1 
ATOM   283  C  C    A ASP A 1 34  ? -10.916 -11.526 33.030  0.50 11.30 ? 34  ASP A C    1 
ATOM   284  C  C    B ASP A 1 34  ? -10.902 -11.547 33.073  0.50 11.50 ? 34  ASP A C    1 
ATOM   285  O  O    A ASP A 1 34  ? -11.179 -10.504 33.778  0.50 13.49 ? 34  ASP A O    1 
ATOM   286  O  O    B ASP A 1 34  ? -11.153 -10.586 33.898  0.50 14.38 ? 34  ASP A O    1 
ATOM   287  C  CB   A ASP A 1 34  ? -8.428  -11.872 33.578  0.50 11.62 ? 34  ASP A CB   1 
ATOM   288  C  CB   B ASP A 1 34  ? -8.454  -11.627 33.709  0.50 11.98 ? 34  ASP A CB   1 
ATOM   289  C  CG   A ASP A 1 34  ? -8.631  -13.097 34.462  0.50 17.32 ? 34  ASP A CG   1 
ATOM   290  C  CG   B ASP A 1 34  ? -8.660  -12.675 34.780  0.50 16.86 ? 34  ASP A CG   1 
ATOM   291  O  OD1  A ASP A 1 34  ? -9.500  -12.971 35.316  0.50 14.81 ? 34  ASP A OD1  1 
ATOM   292  O  OD1  B ASP A 1 34  ? -9.807  -13.220 34.809  0.50 20.56 ? 34  ASP A OD1  1 
ATOM   293  O  OD2  A ASP A 1 34  ? -8.054  -14.150 34.106  0.50 20.03 ? 34  ASP A OD2  1 
ATOM   294  O  OD2  B ASP A 1 34  ? -7.677  -12.983 35.489  0.50 20.68 ? 34  ASP A OD2  1 
ATOM   295  N  N    . THR A 1 35  ? -11.870 -12.300 32.562  1.00 12.48 ? 35  THR A N    1 
ATOM   296  C  CA   . THR A 1 35  ? -13.286 -11.926 32.789  1.00 13.48 ? 35  THR A CA   1 
ATOM   297  C  C    . THR A 1 35  ? -13.699 -12.057 34.229  1.00 13.42 ? 35  THR A C    1 
ATOM   298  O  O    . THR A 1 35  ? -14.565 -11.382 34.731  1.00 15.73 ? 35  THR A O    1 
ATOM   299  C  CB   . THR A 1 35  ? -14.217 -12.859 32.006  1.00 14.68 ? 35  THR A CB   1 
ATOM   300  O  OG1  . THR A 1 35  ? -14.042 -14.239 32.473  1.00 14.76 ? 35  THR A OG1  1 
ATOM   301  C  CG2  . THR A 1 35  ? -13.869 -12.768 30.492  1.00 14.22 ? 35  THR A CG2  1 
ATOM   302  N  N    . HIS A 1 36  ? -12.965 -12.872 34.958  1.00 15.34 ? 36  HIS A N    1 
ATOM   303  C  CA   . HIS A 1 36  ? -13.225 -13.109 36.419  1.00 16.88 ? 36  HIS A CA   1 
ATOM   304  C  C    . HIS A 1 36  ? -12.726 -11.970 37.247  1.00 17.90 ? 36  HIS A C    1 
ATOM   305  O  O    . HIS A 1 36  ? -13.468 -11.656 38.199  1.00 21.70 ? 36  HIS A O    1 
ATOM   306  C  CB   . HIS A 1 36  ? -12.664 -14.517 36.804  1.00 17.93 ? 36  HIS A CB   1 
ATOM   307  C  CG   . HIS A 1 36  ? -13.531 -15.626 36.263  1.00 21.13 ? 36  HIS A CG   1 
ATOM   308  N  ND1  . HIS A 1 36  ? -14.906 -15.683 36.586  1.00 23.94 ? 36  HIS A ND1  1 
ATOM   309  C  CD2  . HIS A 1 36  ? -13.317 -16.564 35.281  1.00 20.63 ? 36  HIS A CD2  1 
ATOM   310  C  CE1  . HIS A 1 36  ? -15.453 -16.677 35.906  1.00 27.50 ? 36  HIS A CE1  1 
ATOM   311  N  NE2  . HIS A 1 36  ? -14.526 -17.177 35.089  1.00 23.69 ? 36  HIS A NE2  1 
ATOM   312  N  N    . THR A 1 37  ? -11.667 -11.253 36.787  1.00 15.84 ? 37  THR A N    1 
ATOM   313  C  CA   . THR A 1 37  ? -10.989 -10.148 37.478  1.00 15.52 ? 37  THR A CA   1 
ATOM   314  C  C    . THR A 1 37  ? -11.535 -8.741  37.089  1.00 13.65 ? 37  THR A C    1 
ATOM   315  O  O    . THR A 1 37  ? -11.258 -7.715  37.787  1.00 16.87 ? 37  THR A O    1 
ATOM   316  C  CB   . THR A 1 37  ? -9.519  -10.154 37.250  1.00 17.34 ? 37  THR A CB   1 
ATOM   317  O  OG1  . THR A 1 37  ? -9.021  -11.376 37.764  1.00 18.54 ? 37  THR A OG1  1 
ATOM   318  C  CG2  . THR A 1 37  ? -8.794  -8.958  38.019  1.00 14.30 ? 37  THR A CG2  1 
ATOM   319  N  N    . ALA A 1 38  ? -12.209 -8.726  35.967  1.00 14.59 ? 38  ALA A N    1 
ATOM   320  C  CA   . ALA A 1 38  ? -12.897 -7.417  35.533  1.00 12.68 ? 38  ALA A CA   1 
ATOM   321  C  C    . ALA A 1 38  ? -13.961 -7.118  36.507  1.00 13.71 ? 38  ALA A C    1 
ATOM   322  O  O    . ALA A 1 38  ? -14.682 -7.982  36.988  1.00 18.82 ? 38  ALA A O    1 
ATOM   323  C  CB   . ALA A 1 38  ? -13.457 -7.558  34.133  1.00 14.70 ? 38  ALA A CB   1 
ATOM   324  N  N    . LYS A 1 39  ? -13.989 -5.870  36.892  1.00 14.79 ? 39  LYS A N    1 
ATOM   325  C  CA   . LYS A 1 39  ? -14.970 -5.431  37.934  1.00 17.79 ? 39  LYS A CA   1 
ATOM   326  C  C    . LYS A 1 39  ? -16.240 -4.911  37.232  1.00 15.71 ? 39  LYS A C    1 
ATOM   327  O  O    . LYS A 1 39  ? -16.180 -3.904  36.524  1.00 13.71 ? 39  LYS A O    1 
ATOM   328  C  CB   . LYS A 1 39  ? -14.176 -4.328  38.655  1.00 20.31 ? 39  LYS A CB   1 
ATOM   329  C  CG   . LYS A 1 39  ? -14.939 -3.477  39.554  1.00 20.58 ? 39  LYS A CG   1 
ATOM   330  C  CD   . LYS A 1 39  ? -15.137 -4.087  41.018  1.00 21.90 ? 39  LYS A CD   1 
ATOM   331  C  CE   . LYS A 1 39  ? -16.023 -3.220  41.890  1.00 23.50 ? 39  LYS A CE   1 
ATOM   332  N  NZ   . LYS A 1 39  ? -16.274 -3.959  43.087  1.00 21.96 ? 39  LYS A NZ   1 
ATOM   333  N  N    . TYR A 1 40  ? -17.342 -5.357  37.702  1.00 16.59 ? 40  TYR A N    1 
ATOM   334  C  CA   . TYR A 1 40  ? -18.624 -4.836  37.260  1.00 15.89 ? 40  TYR A CA   1 
ATOM   335  C  C    . TYR A 1 40  ? -18.768 -3.424  37.869  1.00 15.59 ? 40  TYR A C    1 
ATOM   336  O  O    . TYR A 1 40  ? -18.562 -3.201  39.121  1.00 16.27 ? 40  TYR A O    1 
ATOM   337  C  CB   . TYR A 1 40  ? -19.805 -5.797  37.669  1.00 17.34 ? 40  TYR A CB   1 
ATOM   338  C  CG   . TYR A 1 40  ? -21.093 -5.084  37.488  1.00 19.33 ? 40  TYR A CG   1 
ATOM   339  C  CD1  . TYR A 1 40  ? -21.526 -4.650  36.218  1.00 22.08 ? 40  TYR A CD1  1 
ATOM   340  C  CD2  . TYR A 1 40  ? -21.983 -4.883  38.592  1.00 24.87 ? 40  TYR A CD2  1 
ATOM   341  C  CE1  . TYR A 1 40  ? -22.723 -3.955  36.066  1.00 23.31 ? 40  TYR A CE1  1 
ATOM   342  C  CE2  . TYR A 1 40  ? -23.218 -4.237  38.415  1.00 26.46 ? 40  TYR A CE2  1 
ATOM   343  C  CZ   . TYR A 1 40  ? -23.573 -3.756  37.169  1.00 24.09 ? 40  TYR A CZ   1 
ATOM   344  O  OH   . TYR A 1 40  ? -24.817 -3.113  37.035  1.00 29.05 ? 40  TYR A OH   1 
ATOM   345  N  N    . ASP A 1 41  ? -19.068 -2.476  36.979  1.00 14.15 ? 41  ASP A N    1 
ATOM   346  C  CA   . ASP A 1 41  ? -19.182 -1.025  37.491  1.00 14.26 ? 41  ASP A CA   1 
ATOM   347  C  C    . ASP A 1 41  ? -20.550 -0.575  37.228  1.00 19.28 ? 41  ASP A C    1 
ATOM   348  O  O    . ASP A 1 41  ? -20.903 -0.198  36.076  1.00 15.98 ? 41  ASP A O    1 
ATOM   349  C  CB   . ASP A 1 41  ? -18.181 -0.157  36.793  1.00 17.13 ? 41  ASP A CB   1 
ATOM   350  C  CG   . ASP A 1 41  ? -18.123 1.241   37.368  1.00 22.32 ? 41  ASP A CG   1 
ATOM   351  O  OD1  . ASP A 1 41  ? -19.069 1.612   38.089  1.00 23.91 ? 41  ASP A OD1  1 
ATOM   352  O  OD2  . ASP A 1 41  ? -17.091 1.998   37.050  1.00 24.67 ? 41  ASP A OD2  1 
ATOM   353  N  N    . PRO A 1 42  ? -21.365 -0.586  38.308  1.00 20.99 ? 42  PRO A N    1 
ATOM   354  C  CA   . PRO A 1 42  ? -22.755 -0.198  38.057  1.00 22.88 ? 42  PRO A CA   1 
ATOM   355  C  C    . PRO A 1 42  ? -22.889 1.246   37.653  1.00 23.54 ? 42  PRO A C    1 
ATOM   356  O  O    . PRO A 1 42  ? -23.962 1.677   37.178  1.00 27.14 ? 42  PRO A O    1 
ATOM   357  C  CB   . PRO A 1 42  ? -23.457 -0.509  39.434  1.00 24.67 ? 42  PRO A CB   1 
ATOM   358  C  CG   . PRO A 1 42  ? -22.321 -0.282  40.462  1.00 26.42 ? 42  PRO A CG   1 
ATOM   359  C  CD   . PRO A 1 42  ? -21.099 -0.893  39.764  1.00 21.08 ? 42  PRO A CD   1 
ATOM   360  N  N    . SER A 1 43  ? -21.836 2.045   37.816  1.00 22.25 ? 43  SER A N    1 
ATOM   361  C  CA   . SER A 1 43  ? -21.876 3.458   37.424  1.00 24.30 ? 43  SER A CA   1 
ATOM   362  C  C    . SER A 1 43  ? -21.610 3.637   35.887  1.00 23.48 ? 43  SER A C    1 
ATOM   363  O  O    . SER A 1 43  ? -21.885 4.776   35.302  1.00 26.24 ? 43  SER A O    1 
ATOM   364  C  CB   . SER A 1 43  ? -20.827 4.356   38.190  1.00 24.54 ? 43  SER A CB   1 
ATOM   365  O  OG   . SER A 1 43  ? -19.555 4.395   37.609  1.00 30.16 ? 43  SER A OG   1 
ATOM   366  N  N    . LEU A 1 44  ? -21.169 2.603   35.197  1.00 21.98 ? 44  LEU A N    1 
ATOM   367  C  CA   . LEU A 1 44  ? -20.987 2.684   33.730  1.00 20.09 ? 44  LEU A CA   1 
ATOM   368  C  C    . LEU A 1 44  ? -22.324 2.823   33.041  1.00 21.18 ? 44  LEU A C    1 
ATOM   369  O  O    . LEU A 1 44  ? -23.324 2.248   33.443  1.00 25.16 ? 44  LEU A O    1 
ATOM   370  C  CB   . LEU A 1 44  ? -20.254 1.395   33.208  1.00 17.08 ? 44  LEU A CB   1 
ATOM   371  C  CG   . LEU A 1 44  ? -18.746 1.497   33.435  1.00 15.21 ? 44  LEU A CG   1 
ATOM   372  C  CD1  . LEU A 1 44  ? -18.230 0.100   33.031  1.00 15.95 ? 44  LEU A CD1  1 
ATOM   373  C  CD2  . LEU A 1 44  ? -17.959 2.591   32.725  1.00 18.37 ? 44  LEU A CD2  1 
ATOM   374  N  N    . LYS A 1 45  ? -22.363 3.631   31.989  1.00 19.12 ? 45  LYS A N    1 
ATOM   375  C  CA   . LYS A 1 45  ? -23.643 3.922   31.256  1.00 19.84 ? 45  LYS A CA   1 
ATOM   376  C  C    . LYS A 1 45  ? -23.751 3.010   30.031  1.00 17.84 ? 45  LYS A C    1 
ATOM   377  O  O    . LYS A 1 45  ? -22.722 2.424   29.589  1.00 18.38 ? 45  LYS A O    1 
ATOM   378  C  CB   . LYS A 1 45  ? -23.638 5.327   30.818  1.00 21.86 ? 45  LYS A CB   1 
ATOM   379  C  CG   . LYS A 1 45  ? -23.567 6.354   31.925  1.00 25.20 ? 45  LYS A CG   1 
ATOM   380  C  CD   . LYS A 1 45  ? -23.447 7.705   31.326  1.00 35.02 ? 45  LYS A CD   1 
ATOM   381  C  CE   . LYS A 1 45  ? -22.643 8.663   32.270  1.00 42.51 ? 45  LYS A CE   1 
ATOM   382  N  NZ   . LYS A 1 45  ? -23.453 9.049   33.471  1.00 46.62 ? 45  LYS A NZ   1 
ATOM   383  N  N    . PRO A 1 46  ? -24.955 2.800   29.504  1.00 16.58 ? 46  PRO A N    1 
ATOM   384  C  CA   . PRO A 1 46  ? -25.033 2.125   28.187  1.00 17.21 ? 46  PRO A CA   1 
ATOM   385  C  C    . PRO A 1 46  ? -24.209 2.883   27.208  1.00 15.18 ? 46  PRO A C    1 
ATOM   386  O  O    . PRO A 1 46  ? -24.099 4.079   27.280  1.00 15.99 ? 46  PRO A O    1 
ATOM   387  C  CB   . PRO A 1 46  ? -26.588 2.139   27.835  1.00 18.86 ? 46  PRO A CB   1 
ATOM   388  C  CG   . PRO A 1 46  ? -27.205 2.469   29.139  1.00 18.79 ? 46  PRO A CG   1 
ATOM   389  C  CD   . PRO A 1 46  ? -26.260 3.201   30.072  1.00 19.81 ? 46  PRO A CD   1 
ATOM   390  N  N    . LEU A 1 47  ? -23.592 2.152   26.285  1.00 17.74 ? 47  LEU A N    1 
ATOM   391  C  CA   . LEU A 1 47  ? -22.881 2.858   25.245  1.00 13.80 ? 47  LEU A CA   1 
ATOM   392  C  C    . LEU A 1 47  ? -23.892 3.522   24.307  1.00 16.30 ? 47  LEU A C    1 
ATOM   393  O  O    . LEU A 1 47  ? -24.972 2.904   24.144  1.00 19.23 ? 47  LEU A O    1 
ATOM   394  C  CB   . LEU A 1 47  ? -22.059 1.778   24.520  1.00 17.89 ? 47  LEU A CB   1 
ATOM   395  C  CG   . LEU A 1 47  ? -21.067 2.088   23.601  1.00 19.11 ? 47  LEU A CG   1 
ATOM   396  C  CD1  . LEU A 1 47  ? -19.923 2.909   24.395  1.00 18.50 ? 47  LEU A CD1  1 
ATOM   397  C  CD2  . LEU A 1 47  ? -20.425 0.734   23.124  1.00 17.30 ? 47  LEU A CD2  1 
ATOM   398  N  N    . SER A 1 48  ? -23.592 4.678   23.769  1.00 13.99 ? 48  SER A N    1 
ATOM   399  C  CA   . SER A 1 48  ? -24.421 5.274   22.730  1.00 13.90 ? 48  SER A CA   1 
ATOM   400  C  C    . SER A 1 48  ? -23.669 5.297   21.423  1.00 12.71 ? 48  SER A C    1 
ATOM   401  O  O    . SER A 1 48  ? -22.687 6.027   21.272  1.00 13.06 ? 48  SER A O    1 
ATOM   402  C  CB   . SER A 1 48  ? -24.862 6.675   23.165  1.00 14.67 ? 48  SER A CB   1 
ATOM   403  O  OG   . SER A 1 48  ? -25.432 7.481   22.146  1.00 17.87 ? 48  SER A OG   1 
ATOM   404  N  N    . VAL A 1 49  ? -24.109 4.506   20.503  1.00 13.80 ? 49  VAL A N    1 
ATOM   405  C  CA   . VAL A 1 49  ? -23.571 4.406   19.188  1.00 13.23 ? 49  VAL A CA   1 
ATOM   406  C  C    . VAL A 1 49  ? -24.550 4.995   18.185  1.00 14.27 ? 49  VAL A C    1 
ATOM   407  O  O    . VAL A 1 49  ? -25.584 4.452   17.966  1.00 17.43 ? 49  VAL A O    1 
ATOM   408  C  CB   . VAL A 1 49  ? -23.194 2.956   18.827  1.00 15.70 ? 49  VAL A CB   1 
ATOM   409  C  CG1  . VAL A 1 49  ? -22.572 2.889   17.452  1.00 19.76 ? 49  VAL A CG1  1 
ATOM   410  C  CG2  . VAL A 1 49  ? -22.416 2.293   19.963  1.00 17.72 ? 49  VAL A CG2  1 
ATOM   411  N  N    . SER A 1 50  ? -24.206 6.106   17.606  1.00 16.47 ? 50  SER A N    1 
ATOM   412  C  CA   . SER A 1 50  ? -25.161 6.792   16.720  1.00 15.86 ? 50  SER A CA   1 
ATOM   413  C  C    . SER A 1 50  ? -24.580 6.895   15.364  1.00 15.70 ? 50  SER A C    1 
ATOM   414  O  O    . SER A 1 50  ? -23.849 7.873   15.055  1.00 16.66 ? 50  SER A O    1 
ATOM   415  C  CB   . SER A 1 50  ? -25.595 8.145   17.277  1.00 17.07 ? 50  SER A CB   1 
ATOM   416  O  OG   . SER A 1 50  ? -26.172 8.019   18.578  1.00 23.73 ? 50  SER A OG   1 
ATOM   417  N  N    . TYR A 1 51  ? -24.785 5.834   14.556  1.00 15.82 ? 51  TYR A N    1 
ATOM   418  C  CA   . TYR A 1 51  ? -24.211 5.775   13.243  1.00 14.90 ? 51  TYR A CA   1 
ATOM   419  C  C    . TYR A 1 51  ? -25.198 6.051   12.060  1.00 16.42 ? 51  TYR A C    1 
ATOM   420  O  O    . TYR A 1 51  ? -24.774 5.892   10.908  1.00 16.87 ? 51  TYR A O    1 
ATOM   421  C  CB   . TYR A 1 51  ? -23.525 4.388   13.059  1.00 14.78 ? 51  TYR A CB   1 
ATOM   422  C  CG   . TYR A 1 51  ? -22.271 4.128   13.853  1.00 11.39 ? 51  TYR A CG   1 
ATOM   423  C  CD1  . TYR A 1 51  ? -21.491 5.153   14.411  1.00 12.86 ? 51  TYR A CD1  1 
ATOM   424  C  CD2  . TYR A 1 51  ? -21.787 2.855   13.930  1.00 12.10 ? 51  TYR A CD2  1 
ATOM   425  C  CE1  . TYR A 1 51  ? -20.340 4.851   15.160  1.00 12.57 ? 51  TYR A CE1  1 
ATOM   426  C  CE2  . TYR A 1 51  ? -20.587 2.522   14.564  1.00 9.57  ? 51  TYR A CE2  1 
ATOM   427  C  CZ   . TYR A 1 51  ? -19.887 3.550   15.197  1.00 11.26 ? 51  TYR A CZ   1 
ATOM   428  O  OH   . TYR A 1 51  ? -18.755 3.186   15.901  1.00 10.65 ? 51  TYR A OH   1 
ATOM   429  N  N    A ASP A 1 52  ? -26.438 6.462   12.416  0.50 18.15 ? 52  ASP A N    1 
ATOM   430  N  N    B ASP A 1 52  ? -26.474 6.417   12.326  0.50 18.46 ? 52  ASP A N    1 
ATOM   431  C  CA   A ASP A 1 52  ? -27.519 6.833   11.433  0.50 18.75 ? 52  ASP A CA   1 
ATOM   432  C  CA   B ASP A 1 52  ? -27.479 6.736   11.218  0.50 19.43 ? 52  ASP A CA   1 
ATOM   433  C  C    A ASP A 1 52  ? -27.122 7.728   10.253  0.50 20.19 ? 52  ASP A C    1 
ATOM   434  C  C    B ASP A 1 52  ? -26.877 7.581   10.087  0.50 21.31 ? 52  ASP A C    1 
ATOM   435  O  O    A ASP A 1 52  ? -27.602 7.538   9.094   0.50 20.93 ? 52  ASP A O    1 
ATOM   436  O  O    B ASP A 1 52  ? -27.011 7.289   8.848   0.50 21.61 ? 52  ASP A O    1 
ATOM   437  C  CB   A ASP A 1 52  ? -28.792 7.333   12.121  0.50 21.73 ? 52  ASP A CB   1 
ATOM   438  C  CB   B ASP A 1 52  ? -28.728 7.474   11.731  0.50 21.95 ? 52  ASP A CB   1 
ATOM   439  C  CG   A ASP A 1 52  ? -28.515 8.363   13.224  0.50 23.67 ? 52  ASP A CG   1 
ATOM   440  C  CG   B ASP A 1 52  ? -29.909 7.362   10.793  0.50 25.26 ? 52  ASP A CG   1 
ATOM   441  O  OD1  A ASP A 1 52  ? -27.743 8.120   14.225  0.50 26.53 ? 52  ASP A OD1  1 
ATOM   442  O  OD1  B ASP A 1 52  ? -30.248 6.243   10.342  0.50 31.52 ? 52  ASP A OD1  1 
ATOM   443  O  OD2  A ASP A 1 52  ? -29.115 9.411   13.066  0.50 33.92 ? 52  ASP A OD2  1 
ATOM   444  O  OD2  B ASP A 1 52  ? -30.520 8.405   10.478  0.50 33.32 ? 52  ASP A OD2  1 
ATOM   445  N  N    . GLN A 1 53  ? -26.184 8.619   10.492  1.00 19.35 ? 53  GLN A N    1 
ATOM   446  C  CA   . GLN A 1 53  ? -25.705 9.568   9.396   1.00 21.83 ? 53  GLN A CA   1 
ATOM   447  C  C    . GLN A 1 53  ? -24.307 9.389   8.940   1.00 19.28 ? 53  GLN A C    1 
ATOM   448  O  O    . GLN A 1 53  ? -23.702 10.289  8.377   1.00 19.47 ? 53  GLN A O    1 
ATOM   449  C  CB   . GLN A 1 53  ? -26.056 11.003  9.792   1.00 25.21 ? 53  GLN A CB   1 
ATOM   450  C  CG   . GLN A 1 53  ? -27.665 11.280  9.831   1.00 28.81 ? 53  GLN A CG   1 
ATOM   451  C  CD   . GLN A 1 53  ? -28.497 10.640  8.614   1.00 38.85 ? 53  GLN A CD   1 
ATOM   452  O  OE1  . GLN A 1 53  ? -28.133 10.751  7.350   1.00 42.01 ? 53  GLN A OE1  1 
ATOM   453  N  NE2  . GLN A 1 53  ? -29.622 9.950   8.978   1.00 39.87 ? 53  GLN A NE2  1 
ATOM   454  N  N    . ALA A 1 54  ? -23.700 8.275   9.310   1.00 17.29 ? 54  ALA A N    1 
ATOM   455  C  CA   . ALA A 1 54  ? -22.333 8.036   8.922   1.00 14.94 ? 54  ALA A CA   1 
ATOM   456  C  C    . ALA A 1 54  ? -22.085 8.096   7.423   1.00 16.02 ? 54  ALA A C    1 
ATOM   457  O  O    . ALA A 1 54  ? -22.955 7.644   6.637   1.00 22.55 ? 54  ALA A O    1 
ATOM   458  C  CB   . ALA A 1 54  ? -21.793 6.598   9.443   1.00 16.81 ? 54  ALA A CB   1 
ATOM   459  N  N    A THR A 1 55  ? -21.109 8.885   7.034   0.50 14.42 ? 55  THR A N    1 
ATOM   460  N  N    B THR A 1 55  ? -20.988 8.673   6.959   0.50 14.79 ? 55  THR A N    1 
ATOM   461  C  CA   A THR A 1 55  ? -20.755 9.002   5.648   0.50 13.89 ? 55  THR A CA   1 
ATOM   462  C  CA   B THR A 1 55  ? -20.665 8.785   5.523   0.50 15.55 ? 55  THR A CA   1 
ATOM   463  C  C    A THR A 1 55  ? -19.506 8.296   5.440   0.50 11.42 ? 55  THR A C    1 
ATOM   464  C  C    B THR A 1 55  ? -19.180 8.379   5.185   0.50 13.30 ? 55  THR A C    1 
ATOM   465  O  O    A THR A 1 55  ? -18.475 8.921   5.679   0.50 11.41 ? 55  THR A O    1 
ATOM   466  O  O    B THR A 1 55  ? -18.208 9.160   5.422   0.50 15.08 ? 55  THR A O    1 
ATOM   467  C  CB   A THR A 1 55  ? -20.529 10.469  5.160   0.50 16.09 ? 55  THR A CB   1 
ATOM   468  C  CB   B THR A 1 55  ? -21.076 10.220  5.036   0.50 16.97 ? 55  THR A CB   1 
ATOM   469  O  OG1  A THR A 1 55  ? -21.720 11.210  5.382   0.50 16.55 ? 55  THR A OG1  1 
ATOM   470  O  OG1  B THR A 1 55  ? -20.232 11.094  5.742   0.50 18.35 ? 55  THR A OG1  1 
ATOM   471  C  CG2  A THR A 1 55  ? -20.158 10.397  3.617   0.50 14.63 ? 55  THR A CG2  1 
ATOM   472  C  CG2  B THR A 1 55  ? -22.453 10.576  5.454   0.50 18.32 ? 55  THR A CG2  1 
ATOM   473  N  N    A SER A 1 56  ? -19.558 7.078   4.944   0.50 10.44 ? 56  SER A N    1 
ATOM   474  N  N    B SER A 1 56  ? -19.032 7.190   4.609   0.50 13.44 ? 56  SER A N    1 
ATOM   475  C  CA   A SER A 1 56  ? -18.306 6.536   4.527   0.50 10.39 ? 56  SER A CA   1 
ATOM   476  C  CA   B SER A 1 56  ? -17.746 6.650   4.266   0.50 13.08 ? 56  SER A CA   1 
ATOM   477  C  C    A SER A 1 56  ? -17.930 7.169   3.246   0.50 11.74 ? 56  SER A C    1 
ATOM   478  C  C    B SER A 1 56  ? -17.203 7.313   2.999   0.50 11.36 ? 56  SER A C    1 
ATOM   479  O  O    A SER A 1 56  ? -18.785 7.581   2.461   0.50 10.11 ? 56  SER A O    1 
ATOM   480  O  O    B SER A 1 56  ? -17.979 7.772   2.156   0.50 13.37 ? 56  SER A O    1 
ATOM   481  C  CB   A SER A 1 56  ? -18.440 5.002   4.349   0.50 11.57 ? 56  SER A CB   1 
ATOM   482  C  CB   B SER A 1 56  ? -17.778 5.102   4.077   0.50 12.42 ? 56  SER A CB   1 
ATOM   483  O  OG   A SER A 1 56  ? -19.323 4.673   3.261   0.50 14.20 ? 56  SER A OG   1 
ATOM   484  O  OG   B SER A 1 56  ? -18.707 4.708   3.050   0.50 12.03 ? 56  SER A OG   1 
ATOM   485  N  N    A LEU A 1 57  ? -16.647 7.171   2.974   0.50 9.86  ? 57  LEU A N    1 
ATOM   486  N  N    B LEU A 1 57  ? -15.893 7.390   2.867   0.50 11.68 ? 57  LEU A N    1 
ATOM   487  C  CA   A LEU A 1 57  ? -16.120 7.858   1.773   0.50 9.87  ? 57  LEU A CA   1 
ATOM   488  C  CA   B LEU A 1 57  ? -15.295 7.986   1.700   0.50 11.84 ? 57  LEU A CA   1 
ATOM   489  C  C    A LEU A 1 57  ? -15.270 6.877   0.937   0.50 9.29  ? 57  LEU A C    1 
ATOM   490  C  C    B LEU A 1 57  ? -14.420 7.002   0.810   0.50 12.30 ? 57  LEU A C    1 
ATOM   491  O  O    A LEU A 1 57  ? -15.271 6.969   -0.314  0.50 9.72  ? 57  LEU A O    1 
ATOM   492  O  O    B LEU A 1 57  ? -14.430 7.060   -0.436  0.50 11.87 ? 57  LEU A O    1 
ATOM   493  C  CB   A LEU A 1 57  ? -15.367 9.088   2.109   0.50 12.21 ? 57  LEU A CB   1 
ATOM   494  C  CB   B LEU A 1 57  ? -14.374 9.068   2.167   0.50 13.87 ? 57  LEU A CB   1 
ATOM   495  C  CG   A LEU A 1 57  ? -16.173 10.248  2.795   0.50 12.46 ? 57  LEU A CG   1 
ATOM   496  C  CG   B LEU A 1 57  ? -15.156 10.352  2.742   0.50 15.99 ? 57  LEU A CG   1 
ATOM   497  C  CD1  A LEU A 1 57  ? -15.248 11.371  3.133   0.50 19.00 ? 57  LEU A CD1  1 
ATOM   498  C  CD1  B LEU A 1 57  ? -14.096 11.323  3.217   0.50 16.70 ? 57  LEU A CD1  1 
ATOM   499  C  CD2  A LEU A 1 57  ? -17.464 10.668  1.870   0.50 15.08 ? 57  LEU A CD2  1 
ATOM   500  C  CD2  B LEU A 1 57  ? -16.266 11.012  1.784   0.50 23.36 ? 57  LEU A CD2  1 
ATOM   501  N  N    A ARG A 1 58  ? -14.395 6.089   1.602   0.50 8.04  ? 58  ARG A N    1 
ATOM   502  N  N    B ARG A 1 58  ? -13.632 6.169   1.448   0.50 11.66 ? 58  ARG A N    1 
ATOM   503  C  CA   A ARG A 1 58  ? -13.339 5.453   0.808   0.50 8.54  ? 58  ARG A CA   1 
ATOM   504  C  CA   B ARG A 1 58  ? -12.587 5.484   0.737   0.50 12.60 ? 58  ARG A CA   1 
ATOM   505  C  C    A ARG A 1 58  ? -12.769 4.357   1.641   0.50 7.70  ? 58  ARG A C    1 
ATOM   506  C  C    B ARG A 1 58  ? -11.941 4.415   1.555   0.50 11.75 ? 58  ARG A C    1 
ATOM   507  O  O    A ARG A 1 58  ? -12.908 4.376   2.883   0.50 7.74  ? 58  ARG A O    1 
ATOM   508  O  O    B ARG A 1 58  ? -12.153 4.397   2.759   0.50 12.34 ? 58  ARG A O    1 
ATOM   509  C  CB   A ARG A 1 58  ? -12.204 6.503   0.655   0.50 11.11 ? 58  ARG A CB   1 
ATOM   510  C  CB   B ARG A 1 58  ? -11.513 6.506   0.400   0.50 12.23 ? 58  ARG A CB   1 
ATOM   511  C  CG   A ARG A 1 58  ? -10.932 6.102   -0.118  0.50 10.31 ? 58  ARG A CG   1 
ATOM   512  C  CG   B ARG A 1 58  ? -10.709 6.156   -0.797  0.50 14.35 ? 58  ARG A CG   1 
ATOM   513  C  CD   A ARG A 1 58  ? -10.071 7.319   -0.275  0.50 14.62 ? 58  ARG A CD   1 
ATOM   514  C  CD   B ARG A 1 58  ? -9.486  7.100   -0.926  0.50 14.14 ? 58  ARG A CD   1 
ATOM   515  N  NE   A ARG A 1 58  ? -9.070  7.349   0.798   0.50 11.89 ? 58  ARG A NE   1 
ATOM   516  N  NE   B ARG A 1 58  ? -8.869  7.045   0.403   0.50 16.07 ? 58  ARG A NE   1 
ATOM   517  C  CZ   A ARG A 1 58  ? -7.748  7.263   0.595   0.50 13.21 ? 58  ARG A CZ   1 
ATOM   518  C  CZ   B ARG A 1 58  ? -7.581  7.273   0.592   0.50 11.94 ? 58  ARG A CZ   1 
ATOM   519  N  NH1  A ARG A 1 58  ? -7.306  7.387   -0.624  0.50 18.63 ? 58  ARG A NH1  1 
ATOM   520  N  NH1  B ARG A 1 58  ? -6.871  7.670   -0.442  0.50 14.11 ? 58  ARG A NH1  1 
ATOM   521  N  NH2  A ARG A 1 58  ? -6.917  7.280   1.635   0.50 17.55 ? 58  ARG A NH2  1 
ATOM   522  N  NH2  B ARG A 1 58  ? -7.093  7.302   1.840   0.50 11.06 ? 58  ARG A NH2  1 
ATOM   523  N  N    A ILE A 1 59  ? -12.165 3.369   0.943   0.50 6.80  ? 59  ILE A N    1 
ATOM   524  N  N    B ILE A 1 59  ? -11.237 3.522   0.887   0.50 9.11  ? 59  ILE A N    1 
ATOM   525  C  CA   A ILE A 1 59  ? -11.469 2.255   1.590   0.50 6.88  ? 59  ILE A CA   1 
ATOM   526  C  CA   B ILE A 1 59  ? -10.599 2.325   1.492   0.50 10.36 ? 59  ILE A CA   1 
ATOM   527  C  C    A ILE A 1 59  ? -10.057 2.269   1.103   0.50 5.11  ? 59  ILE A C    1 
ATOM   528  C  C    B ILE A 1 59  ? -9.146  2.239   0.975   0.50 9.38  ? 59  ILE A C    1 
ATOM   529  O  O    A ILE A 1 59  ? -9.815  2.392   -0.104  0.50 7.98  ? 59  ILE A O    1 
ATOM   530  O  O    B ILE A 1 59  ? -8.870  2.393   -0.204  0.50 10.82 ? 59  ILE A O    1 
ATOM   531  C  CB   A ILE A 1 59  ? -12.243 0.944   1.379   0.50 7.21  ? 59  ILE A CB   1 
ATOM   532  C  CB   B ILE A 1 59  ? -11.367 1.008   1.235   0.50 10.22 ? 59  ILE A CB   1 
ATOM   533  C  CG1  A ILE A 1 59  ? -11.672 -0.205  2.228   0.50 8.73  ? 59  ILE A CG1  1 
ATOM   534  C  CG1  B ILE A 1 59  ? -10.820 -0.122  2.130   0.50 9.44  ? 59  ILE A CG1  1 
ATOM   535  C  CG2  A ILE A 1 59  ? -12.306 0.537   -0.112  0.50 7.97  ? 59  ILE A CG2  1 
ATOM   536  C  CG2  B ILE A 1 59  ? -11.306 0.554   -0.375  0.50 10.36 ? 59  ILE A CG2  1 
ATOM   537  C  CD1  A ILE A 1 59  ? -12.562 -1.403  2.157   0.50 9.52  ? 59  ILE A CD1  1 
ATOM   538  C  CD1  B ILE A 1 59  ? -11.663 -1.451  2.032   0.50 12.16 ? 59  ILE A CD1  1 
ATOM   539  N  N    A LEU A 1 60  ? -9.121  2.148   2.074   0.50 5.86  ? 60  LEU A N    1 
ATOM   540  N  N    B LEU A 1 60  ? -8.231  2.065   1.921   0.50 10.36 ? 60  LEU A N    1 
ATOM   541  C  CA   A LEU A 1 60  ? -7.689  2.242   1.813   0.50 6.22  ? 60  LEU A CA   1 
ATOM   542  C  CA   B LEU A 1 60  ? -6.810  2.104   1.615   0.50 10.44 ? 60  LEU A CA   1 
ATOM   543  C  C    A LEU A 1 60  ? -6.897  1.039   2.323   0.50 6.41  ? 60  LEU A C    1 
ATOM   544  C  C    B LEU A 1 60  ? -6.131  0.839   2.206   0.50 9.64  ? 60  LEU A C    1 
ATOM   545  O  O    A LEU A 1 60  ? -6.994  0.693   3.489   0.50 6.37  ? 60  LEU A O    1 
ATOM   546  O  O    B LEU A 1 60  ? -6.175  0.617   3.385   0.50 9.42  ? 60  LEU A O    1 
ATOM   547  C  CB   A LEU A 1 60  ? -7.114  3.496   2.530   0.50 6.70  ? 60  LEU A CB   1 
ATOM   548  C  CB   B LEU A 1 60  ? -6.191  3.393   2.224   0.50 11.21 ? 60  LEU A CB   1 
ATOM   549  C  CG   A LEU A 1 60  ? -5.577  3.582   2.447   0.50 8.44  ? 60  LEU A CG   1 
ATOM   550  C  CG   B LEU A 1 60  ? -4.647  3.478   2.246   0.50 12.37 ? 60  LEU A CG   1 
ATOM   551  C  CD1  A LEU A 1 60  ? -5.039  3.927   0.921   0.50 7.38  ? 60  LEU A CD1  1 
ATOM   552  C  CD1  B LEU A 1 60  ? -3.994  3.557   0.848   0.50 11.35 ? 60  LEU A CD1  1 
ATOM   553  C  CD2  A LEU A 1 60  ? -5.030  4.685   3.400   0.50 6.95  ? 60  LEU A CD2  1 
ATOM   554  C  CD2  B LEU A 1 60  ? -4.200  4.647   3.234   0.50 12.28 ? 60  LEU A CD2  1 
ATOM   555  N  N    A ASN A 1 61  ? -6.090  0.460   1.437   0.50 6.72  ? 61  ASN A N    1 
ATOM   556  N  N    B ASN A 1 61  ? -5.431  0.102   1.342   0.50 9.81  ? 61  ASN A N    1 
ATOM   557  C  CA   A ASN A 1 61  ? -5.085  -0.509  1.934   0.50 7.64  ? 61  ASN A CA   1 
ATOM   558  C  CA   B ASN A 1 61  ? -4.472  -0.881  1.839   0.50 10.13 ? 61  ASN A CA   1 
ATOM   559  C  C    A ASN A 1 61  ? -3.767  0.316   2.256   0.50 7.57  ? 61  ASN A C    1 
ATOM   560  C  C    B ASN A 1 61  ? -3.249  0.008   2.232   0.50 11.55 ? 61  ASN A C    1 
ATOM   561  O  O    A ASN A 1 61  ? -3.211  0.824   1.290   0.50 7.34  ? 61  ASN A O    1 
ATOM   562  O  O    B ASN A 1 61  ? -2.440  0.527   1.411   0.50 10.71 ? 61  ASN A O    1 
ATOM   563  C  CB   A ASN A 1 61  ? -4.777  -1.473  0.793   0.50 7.53  ? 61  ASN A CB   1 
ATOM   564  C  CB   B ASN A 1 61  ? -4.065  -1.867  0.754   0.50 9.19  ? 61  ASN A CB   1 
ATOM   565  C  CG   A ASN A 1 61  ? -3.808  -2.564  1.222   0.50 6.52  ? 61  ASN A CG   1 
ATOM   566  C  CG   B ASN A 1 61  ? -2.921  -2.868  1.200   0.50 10.15 ? 61  ASN A CG   1 
ATOM   567  O  OD1  A ASN A 1 61  ? -2.907  -2.327  2.014   0.50 8.17  ? 61  ASN A OD1  1 
ATOM   568  O  OD1  B ASN A 1 61  ? -2.124  -2.592  2.129   0.50 11.26 ? 61  ASN A OD1  1 
ATOM   569  N  ND2  A ASN A 1 61  ? -3.847  -3.719  0.573   0.50 5.21  ? 61  ASN A ND2  1 
ATOM   570  N  ND2  B ASN A 1 61  ? -2.922  -4.067  0.623   0.50 10.16 ? 61  ASN A ND2  1 
ATOM   571  N  N    . ASN A 1 62  ? -3.233  0.298   3.528   1.00 12.05 ? 62  ASN A N    1 
ATOM   572  C  CA   . ASN A 1 62  ? -2.150  1.121   3.962   1.00 12.03 ? 62  ASN A CA   1 
ATOM   573  C  C    . ASN A 1 62  ? -0.907  0.291   4.138   1.00 13.59 ? 62  ASN A C    1 
ATOM   574  O  O    . ASN A 1 62  ? 0.170   0.719   4.741   1.00 17.28 ? 62  ASN A O    1 
ATOM   575  C  CB   . ASN A 1 62  ? -2.444  1.934   5.227   1.00 14.24 ? 62  ASN A CB   1 
ATOM   576  C  CG   . ASN A 1 62  ? -2.674  1.000   6.432   1.00 15.12 ? 62  ASN A CG   1 
ATOM   577  O  OD1  . ASN A 1 62  ? -2.493  -0.222  6.377   1.00 13.85 ? 62  ASN A OD1  1 
ATOM   578  N  ND2  . ASN A 1 62  ? -2.952  1.624   7.539   1.00 20.54 ? 62  ASN A ND2  1 
ATOM   579  N  N    . GLY A 1 63  ? -0.935  -1.057  3.752   1.00 13.78 ? 63  GLY A N    1 
ATOM   580  C  CA   . GLY A 1 63  ? 0.223   -1.878  3.944   1.00 12.60 ? 63  GLY A CA   1 
ATOM   581  C  C    . GLY A 1 63  ? 0.264   -2.602  5.309   1.00 13.53 ? 63  GLY A C    1 
ATOM   582  O  O    . GLY A 1 63  ? 1.169   -3.426  5.563   1.00 12.94 ? 63  GLY A O    1 
ATOM   583  N  N    . HIS A 1 64  ? -0.676  -2.298  6.184   1.00 11.17 ? 64  HIS A N    1 
ATOM   584  C  CA   . HIS A 1 64  ? -0.835  -2.917  7.525   1.00 13.65 ? 64  HIS A CA   1 
ATOM   585  C  C    . HIS A 1 64  ? -2.159  -3.563  7.713   1.00 10.56 ? 64  HIS A C    1 
ATOM   586  O  O    . HIS A 1 64  ? -2.190  -4.642  8.261   1.00 15.29 ? 64  HIS A O    1 
ATOM   587  C  CB   . HIS A 1 64  ? -0.621  -1.829  8.654   1.00 12.66 ? 64  HIS A CB   1 
ATOM   588  C  CG   . HIS A 1 64  ? 0.668   -1.061  8.497   1.00 14.37 ? 64  HIS A CG   1 
ATOM   589  N  ND1  . HIS A 1 64  ? 1.920   -1.659  8.578   1.00 15.53 ? 64  HIS A ND1  1 
ATOM   590  C  CD2  . HIS A 1 64  ? 0.893   0.256   8.282   1.00 14.33 ? 64  HIS A CD2  1 
ATOM   591  C  CE1  . HIS A 1 64  ? 2.866   -0.714  8.462   1.00 16.40 ? 64  HIS A CE1  1 
ATOM   592  N  NE2  . HIS A 1 64  ? 2.283   0.444   8.187   1.00 18.36 ? 64  HIS A NE2  1 
ATOM   593  N  N    . ALA A 1 65  ? -3.169  -2.943  7.216   1.00 9.96  ? 65  ALA A N    1 
ATOM   594  C  CA   . ALA A 1 65  ? -4.535  -3.433  7.222   1.00 10.99 ? 65  ALA A CA   1 
ATOM   595  C  C    . ALA A 1 65  ? -5.261  -2.698  6.093   1.00 10.84 ? 65  ALA A C    1 
ATOM   596  O  O    . ALA A 1 65  ? -4.559  -2.034  5.214   1.00 12.62 ? 65  ALA A O    1 
ATOM   597  C  CB   . ALA A 1 65  ? -5.199  -3.210  8.597   1.00 11.68 ? 65  ALA A CB   1 
ATOM   598  N  N    . PHE A 1 66  ? -6.565  -2.643  6.121   1.00 10.09 ? 66  PHE A N    1 
ATOM   599  C  CA   . PHE A 1 66  ? -7.300  -1.684  5.292   1.00 11.58 ? 66  PHE A CA   1 
ATOM   600  C  C    . PHE A 1 66  ? -8.164  -0.775  6.180   1.00 10.32 ? 66  PHE A C    1 
ATOM   601  O  O    . PHE A 1 66  ? -8.854  -1.254  7.107   1.00 10.83 ? 66  PHE A O    1 
ATOM   602  C  CB   . PHE A 1 66  ? -8.141  -2.346  4.159   1.00 12.30 ? 66  PHE A CB   1 
ATOM   603  C  CG   . PHE A 1 66  ? -9.179  -3.306  4.654   1.00 12.42 ? 66  PHE A CG   1 
ATOM   604  C  CD1  . PHE A 1 66  ? -10.500 -2.884  5.006   1.00 10.63 ? 66  PHE A CD1  1 
ATOM   605  C  CD2  . PHE A 1 66  ? -8.893  -4.690  4.748   1.00 10.56 ? 66  PHE A CD2  1 
ATOM   606  C  CE1  . PHE A 1 66  ? -11.432 -3.714  5.525   1.00 11.72 ? 66  PHE A CE1  1 
ATOM   607  C  CE2  . PHE A 1 66  ? -9.859  -5.586  5.321   1.00 11.68 ? 66  PHE A CE2  1 
ATOM   608  C  CZ   . PHE A 1 66  ? -11.155 -5.076  5.590   1.00 11.74 ? 66  PHE A CZ   1 
ATOM   609  N  N    A ASN A 1 67  ? -8.344  0.530   5.814   0.50 8.47  ? 67  ASN A N    1 
ATOM   610  N  N    B ASN A 1 67  ? -7.905  0.509   5.928   0.50 10.69 ? 67  ASN A N    1 
ATOM   611  C  CA   A ASN A 1 67  ? -9.271  1.433   6.604   0.50 7.94  ? 67  ASN A CA   1 
ATOM   612  C  CA   B ASN A 1 67  ? -8.675  1.476   6.635   0.50 9.55  ? 67  ASN A CA   1 
ATOM   613  C  C    A ASN A 1 67  ? -10.513 1.812   5.771   0.50 6.32  ? 67  ASN A C    1 
ATOM   614  C  C    B ASN A 1 67  ? -9.758  1.892   5.752   0.50 10.70 ? 67  ASN A C    1 
ATOM   615  O  O    A ASN A 1 67  ? -10.316 2.227   4.595   0.50 5.90  ? 67  ASN A O    1 
ATOM   616  O  O    B ASN A 1 67  ? -9.531  2.389   4.655   0.50 11.04 ? 67  ASN A O    1 
ATOM   617  C  CB   A ASN A 1 67  ? -8.525  2.737   6.911   0.50 7.24  ? 67  ASN A CB   1 
ATOM   618  C  CB   B ASN A 1 67  ? -7.824  2.713   7.031   0.50 9.81  ? 67  ASN A CB   1 
ATOM   619  C  CG   A ASN A 1 67  ? -7.413  2.562   7.863   0.50 8.18  ? 67  ASN A CG   1 
ATOM   620  C  CG   B ASN A 1 67  ? -6.644  2.363   8.008   0.50 13.90 ? 67  ASN A CG   1 
ATOM   621  O  OD1  A ASN A 1 67  ? -7.381  1.607   8.615   0.50 8.99  ? 67  ASN A OD1  1 
ATOM   622  O  OD1  B ASN A 1 67  ? -6.767  1.458   8.777   0.50 13.12 ? 67  ASN A OD1  1 
ATOM   623  N  ND2  A ASN A 1 67  ? -6.458  3.551   7.880   0.50 9.21  ? 67  ASN A ND2  1 
ATOM   624  N  ND2  B ASN A 1 67  ? -5.463  3.062   7.911   0.50 15.71 ? 67  ASN A ND2  1 
ATOM   625  N  N    A VAL A 1 68  ? -11.697 1.639   6.366   0.50 6.45  ? 68  VAL A N    1 
ATOM   626  N  N    B VAL A 1 68  ? -10.964 1.769   6.287   0.50 9.61  ? 68  VAL A N    1 
ATOM   627  C  CA   A VAL A 1 68  ? -12.883 2.199   5.787   0.50 6.68  ? 68  VAL A CA   1 
ATOM   628  C  CA   B VAL A 1 68  ? -12.093 2.460   5.669   0.50 8.22  ? 68  VAL A CA   1 
ATOM   629  C  C    A VAL A 1 68  ? -13.086 3.587   6.430   0.50 6.01  ? 68  VAL A C    1 
ATOM   630  C  C    B VAL A 1 68  ? -12.227 3.827   6.369   0.50 12.15 ? 68  VAL A C    1 
ATOM   631  O  O    A VAL A 1 68  ? -13.280 3.658   7.656   0.50 6.01  ? 68  VAL A O    1 
ATOM   632  O  O    B VAL A 1 68  ? -12.527 3.840   7.590   0.50 9.54  ? 68  VAL A O    1 
ATOM   633  C  CB   A VAL A 1 68  ? -14.131 1.337   6.070   0.50 7.37  ? 68  VAL A CB   1 
ATOM   634  C  CB   B VAL A 1 68  ? -13.383 1.616   5.775   0.50 10.12 ? 68  VAL A CB   1 
ATOM   635  C  CG1  A VAL A 1 68  ? -15.444 2.070   5.573   0.50 6.84  ? 68  VAL A CG1  1 
ATOM   636  C  CG1  B VAL A 1 68  ? -14.651 2.487   5.260   0.50 11.46 ? 68  VAL A CG1  1 
ATOM   637  C  CG2  A VAL A 1 68  ? -13.926 0.006   5.259   0.50 8.36  ? 68  VAL A CG2  1 
ATOM   638  C  CG2  B VAL A 1 68  ? -13.210 0.290   4.982   0.50 10.92 ? 68  VAL A CG2  1 
ATOM   639  N  N    A GLU A 1 69  ? -12.984 4.619   5.593   0.50 5.87  ? 69  GLU A N    1 
ATOM   640  N  N    B GLU A 1 69  ? -11.975 4.912   5.629   0.50 10.40 ? 69  GLU A N    1 
ATOM   641  C  CA   A GLU A 1 69  ? -12.871 5.990   6.130   0.50 6.02  ? 69  GLU A CA   1 
ATOM   642  C  CA   B GLU A 1 69  ? -11.925 6.203   6.254   0.50 12.00 ? 69  GLU A CA   1 
ATOM   643  C  C    A GLU A 1 69  ? -14.201 6.697   6.039   0.50 7.12  ? 69  GLU A C    1 
ATOM   644  C  C    B GLU A 1 69  ? -13.233 6.963   5.990   0.50 11.96 ? 69  GLU A C    1 
ATOM   645  O  O    A GLU A 1 69  ? -14.950 6.498   5.096   0.50 6.27  ? 69  GLU A O    1 
ATOM   646  O  O    B GLU A 1 69  ? -13.878 6.821   4.926   0.50 15.72 ? 69  GLU A O    1 
ATOM   647  C  CB   A GLU A 1 69  ? -11.818 6.739   5.244   0.50 6.81  ? 69  GLU A CB   1 
ATOM   648  C  CB   B GLU A 1 69  ? -10.912 7.057   5.526   0.50 18.00 ? 69  GLU A CB   1 
ATOM   649  C  CG   A GLU A 1 69  ? -10.468 6.118   5.226   0.50 6.57  ? 69  GLU A CG   1 
ATOM   650  C  CG   B GLU A 1 69  ? -9.736  6.284   5.206   0.50 20.84 ? 69  GLU A CG   1 
ATOM   651  C  CD   A GLU A 1 69  ? -9.638  6.733   4.146   0.50 6.65  ? 69  GLU A CD   1 
ATOM   652  C  CD   B GLU A 1 69  ? -9.042  6.676   3.926   0.50 26.13 ? 69  GLU A CD   1 
ATOM   653  O  OE1  A GLU A 1 69  ? -10.137 7.471   3.265   0.50 9.21  ? 69  GLU A OE1  1 
ATOM   654  O  OE1  B GLU A 1 69  ? -9.744  7.217   3.013   0.50 27.28 ? 69  GLU A OE1  1 
ATOM   655  O  OE2  A GLU A 1 69  ? -8.442  6.369   4.116   0.50 7.70  ? 69  GLU A OE2  1 
ATOM   656  O  OE2  B GLU A 1 69  ? -7.795  6.393   3.852   0.50 29.67 ? 69  GLU A OE2  1 
ATOM   657  N  N    A PHE A 1 70  ? -14.404 7.574   7.000   0.50 7.88  ? 70  PHE A N    1 
ATOM   658  N  N    B PHE A 1 70  ? -13.666 7.770   6.982   0.50 12.00 ? 70  PHE A N    1 
ATOM   659  C  CA   A PHE A 1 70  ? -15.625 8.348   7.136   0.50 8.47  ? 70  PHE A CA   1 
ATOM   660  C  CA   B PHE A 1 70  ? -15.036 8.422   6.900   0.50 11.46 ? 70  PHE A CA   1 
ATOM   661  C  C    A PHE A 1 70  ? -15.283 9.814   7.091   0.50 9.91  ? 70  PHE A C    1 
ATOM   662  C  C    B PHE A 1 70  ? -15.021 9.906   6.796   0.50 11.56 ? 70  PHE A C    1 
ATOM   663  O  O    A PHE A 1 70  ? -14.258 10.256  7.615   0.50 9.25  ? 70  PHE A O    1 
ATOM   664  O  O    B PHE A 1 70  ? -13.949 10.449  7.083   0.50 11.38 ? 70  PHE A O    1 
ATOM   665  C  CB   A PHE A 1 70  ? -16.363 7.982   8.442   0.50 8.82  ? 70  PHE A CB   1 
ATOM   666  C  CB   B PHE A 1 70  ? -15.826 8.150   8.170   0.50 11.08 ? 70  PHE A CB   1 
ATOM   667  C  CG   A PHE A 1 70  ? -16.988 6.574   8.387   0.50 7.21  ? 70  PHE A CG   1 
ATOM   668  C  CG   B PHE A 1 70  ? -16.398 6.779   8.158   0.50 10.63 ? 70  PHE A CG   1 
ATOM   669  C  CD1  A PHE A 1 70  ? -16.178 5.451   8.541   0.50 10.64 ? 70  PHE A CD1  1 
ATOM   670  C  CD1  B PHE A 1 70  ? -17.724 6.544   7.766   0.50 11.76 ? 70  PHE A CD1  1 
ATOM   671  C  CD2  A PHE A 1 70  ? -18.344 6.383   8.084   0.50 6.14  ? 70  PHE A CD2  1 
ATOM   672  C  CD2  B PHE A 1 70  ? -15.569 5.692   8.481   0.50 9.44  ? 70  PHE A CD2  1 
ATOM   673  C  CE1  A PHE A 1 70  ? -16.713 4.128   8.430   0.50 11.32 ? 70  PHE A CE1  1 
ATOM   674  C  CE1  B PHE A 1 70  ? -18.283 5.292   7.669   0.50 8.22  ? 70  PHE A CE1  1 
ATOM   675  C  CE2  A PHE A 1 70  ? -18.909 5.067   7.965   0.50 7.99  ? 70  PHE A CE2  1 
ATOM   676  C  CE2  B PHE A 1 70  ? -16.132 4.345   8.374   0.50 8.73  ? 70  PHE A CE2  1 
ATOM   677  C  CZ   A PHE A 1 70  ? -18.086 3.947   8.127   0.50 10.42 ? 70  PHE A CZ   1 
ATOM   678  C  CZ   B PHE A 1 70  ? -17.456 4.192   7.972   0.50 8.13  ? 70  PHE A CZ   1 
ATOM   679  N  N    . ASP A 1 71  ? -16.176 10.591  6.497   1.00 13.33 ? 71  ASP A N    1 
ATOM   680  C  CA   . ASP A 1 71  ? -16.068 12.067  6.506   1.00 14.79 ? 71  ASP A CA   1 
ATOM   681  C  C    . ASP A 1 71  ? -16.407 12.472  7.930   1.00 13.04 ? 71  ASP A C    1 
ATOM   682  O  O    . ASP A 1 71  ? -17.579 12.302  8.365   1.00 17.94 ? 71  ASP A O    1 
ATOM   683  C  CB   . ASP A 1 71  ? -17.149 12.566  5.559   1.00 17.90 ? 71  ASP A CB   1 
ATOM   684  C  CG   . ASP A 1 71  ? -17.341 14.110  5.747   1.00 21.76 ? 71  ASP A CG   1 
ATOM   685  O  OD1  . ASP A 1 71  ? -16.528 14.766  6.342   1.00 19.09 ? 71  ASP A OD1  1 
ATOM   686  O  OD2  . ASP A 1 71  ? -18.392 14.636  5.299   1.00 30.07 ? 71  ASP A OD2  1 
ATOM   687  N  N    . ASP A 1 72  ? -15.435 12.945  8.673   1.00 12.63 ? 72  ASP A N    1 
ATOM   688  C  CA   . ASP A 1 72  ? -15.607 13.317  10.075  1.00 12.50 ? 72  ASP A CA   1 
ATOM   689  C  C    . ASP A 1 72  ? -15.570 14.887  10.198  1.00 14.46 ? 72  ASP A C    1 
ATOM   690  O  O    . ASP A 1 72  ? -15.169 15.347  11.252  1.00 15.51 ? 72  ASP A O    1 
ATOM   691  C  CB   . ASP A 1 72  ? -14.501 12.736  10.962  1.00 12.85 ? 72  ASP A CB   1 
ATOM   692  C  CG   . ASP A 1 72  ? -13.098 13.218  10.591  1.00 12.01 ? 72  ASP A CG   1 
ATOM   693  O  OD1  . ASP A 1 72  ? -12.976 13.925  9.521   1.00 15.20 ? 72  ASP A OD1  1 
ATOM   694  O  OD2  . ASP A 1 72  ? -12.131 12.839  11.291  1.00 13.52 ? 72  ASP A OD2  1 
ATOM   695  N  N    . SER A 1 73  ? -15.981 15.564  9.149   1.00 15.00 ? 73  SER A N    1 
ATOM   696  C  CA   . SER A 1 73  ? -15.962 17.107  9.187   1.00 16.20 ? 73  SER A CA   1 
ATOM   697  C  C    . SER A 1 73  ? -17.309 17.590  9.748   1.00 15.93 ? 73  SER A C    1 
ATOM   698  O  O    . SER A 1 73  ? -17.439 18.805  9.928   1.00 16.81 ? 73  SER A O    1 
ATOM   699  C  CB   . SER A 1 73  ? -15.725 17.557  7.763   1.00 19.30 ? 73  SER A CB   1 
ATOM   700  O  OG   . SER A 1 73  ? -16.856 17.414  6.962   1.00 21.99 ? 73  SER A OG   1 
ATOM   701  N  N    . GLN A 1 74  ? -18.244 16.704  10.123  1.00 17.98 ? 74  GLN A N    1 
ATOM   702  C  CA   . GLN A 1 74  ? -19.417 17.200  10.759  1.00 20.14 ? 74  GLN A CA   1 
ATOM   703  C  C    . GLN A 1 74  ? -19.791 16.226  11.812  1.00 19.96 ? 74  GLN A C    1 
ATOM   704  O  O    . GLN A 1 74  ? -19.253 15.162  11.857  1.00 16.04 ? 74  GLN A O    1 
ATOM   705  C  CB   . GLN A 1 74  ? -20.600 17.210  9.702   1.00 21.14 ? 74  GLN A CB   1 
ATOM   706  C  CG   . GLN A 1 74  ? -20.558 18.393  8.854   1.00 27.58 ? 74  GLN A CG   1 
ATOM   707  C  CD   . GLN A 1 74  ? -20.961 18.008  7.478   1.00 31.82 ? 74  GLN A CD   1 
ATOM   708  O  OE1  . GLN A 1 74  ? -22.169 17.991  7.226   1.00 34.73 ? 74  GLN A OE1  1 
ATOM   709  N  NE2  . GLN A 1 74  ? -19.908 17.731  6.501   1.00 34.07 ? 74  GLN A NE2  1 
ATOM   710  N  N    . ASP A 1 75  ? -20.760 16.618  12.653  1.00 19.67 ? 75  ASP A N    1 
ATOM   711  C  CA   . ASP A 1 75  ? -21.170 15.907  13.772  1.00 18.75 ? 75  ASP A CA   1 
ATOM   712  C  C    . ASP A 1 75  ? -22.079 14.761  13.254  1.00 18.87 ? 75  ASP A C    1 
ATOM   713  O  O    . ASP A 1 75  ? -23.331 14.968  13.287  1.00 24.51 ? 75  ASP A O    1 
ATOM   714  C  CB   . ASP A 1 75  ? -21.912 17.019  14.684  1.00 18.09 ? 75  ASP A CB   1 
ATOM   715  C  CG   . ASP A 1 75  ? -22.678 16.382  15.820  1.00 28.69 ? 75  ASP A CG   1 
ATOM   716  O  OD1  . ASP A 1 75  ? -22.333 15.184  16.088  1.00 22.78 ? 75  ASP A OD1  1 
ATOM   717  O  OD2  . ASP A 1 75  ? -23.681 17.017  16.369  1.00 35.52 ? 75  ASP A OD2  1 
ATOM   718  N  N    . LYS A 1 76  ? -21.530 13.659  12.788  1.00 17.17 ? 76  LYS A N    1 
ATOM   719  C  CA   . LYS A 1 76  ? -22.280 12.504  12.332  1.00 20.28 ? 76  LYS A CA   1 
ATOM   720  C  C    . LYS A 1 76  ? -21.375 11.343  12.939  1.00 20.49 ? 76  LYS A C    1 
ATOM   721  O  O    . LYS A 1 76  ? -20.153 11.497  13.204  1.00 22.91 ? 76  LYS A O    1 
ATOM   722  C  CB   . LYS A 1 76  ? -22.165 12.376  10.784  1.00 19.15 ? 76  LYS A CB   1 
ATOM   723  C  CG   . LYS A 1 76  ? -22.717 13.571  9.867   1.00 25.75 ? 76  LYS A CG   1 
ATOM   724  C  CD   . LYS A 1 76  ? -21.893 13.391  8.546   1.00 29.62 ? 76  LYS A CD   1 
ATOM   725  C  CE   . LYS A 1 76  ? -22.314 14.223  7.312   1.00 32.09 ? 76  LYS A CE   1 
ATOM   726  N  NZ   . LYS A 1 76  ? -21.435 14.021  6.148   1.00 30.37 ? 76  LYS A NZ   1 
ATOM   727  N  N    . ALA A 1 77  ? -21.986 10.292  13.134  1.00 20.41 ? 77  ALA A N    1 
ATOM   728  C  CA   . ALA A 1 77  ? -21.422 9.008   13.507  1.00 16.45 ? 77  ALA A CA   1 
ATOM   729  C  C    . ALA A 1 77  ? -20.662 9.235   14.825  1.00 14.59 ? 77  ALA A C    1 
ATOM   730  O  O    . ALA A 1 77  ? -19.419 9.416   14.843  1.00 18.72 ? 77  ALA A O    1 
ATOM   731  C  CB   . ALA A 1 77  ? -20.502 8.469   12.451  1.00 16.92 ? 77  ALA A CB   1 
ATOM   732  N  N    . VAL A 1 78  ? -21.356 9.256   15.911  1.00 13.27 ? 78  VAL A N    1 
ATOM   733  C  CA   . VAL A 1 78  ? -20.734 9.503   17.246  1.00 14.39 ? 78  VAL A CA   1 
ATOM   734  C  C    . VAL A 1 78  ? -20.916 8.443   18.232  1.00 12.12 ? 78  VAL A C    1 
ATOM   735  O  O    . VAL A 1 78  ? -21.962 7.776   18.312  1.00 12.71 ? 78  VAL A O    1 
ATOM   736  C  CB   . VAL A 1 78  ? -21.142 10.867  17.856  1.00 22.08 ? 78  VAL A CB   1 
ATOM   737  C  CG1  . VAL A 1 78  ? -20.866 11.996  16.872  1.00 20.32 ? 78  VAL A CG1  1 
ATOM   738  C  CG2  . VAL A 1 78  ? -22.589 10.838  18.298  1.00 20.52 ? 78  VAL A CG2  1 
ATOM   739  N  N    . LEU A 1 79  ? -19.867 8.258   19.017  1.00 10.96 ? 79  LEU A N    1 
ATOM   740  C  CA   . LEU A 1 79  ? -19.863 7.432   20.152  1.00 11.19 ? 79  LEU A CA   1 
ATOM   741  C  C    . LEU A 1 79  ? -19.845 8.219   21.376  1.00 10.47 ? 79  LEU A C    1 
ATOM   742  O  O    . LEU A 1 79  ? -19.023 9.188   21.511  1.00 11.83 ? 79  LEU A O    1 
ATOM   743  C  CB   . LEU A 1 79  ? -18.601 6.546   20.072  1.00 11.94 ? 79  LEU A CB   1 
ATOM   744  C  CG   . LEU A 1 79  ? -18.428 5.400   21.073  1.00 11.27 ? 79  LEU A CG   1 
ATOM   745  C  CD1  . LEU A 1 79  ? -19.471 4.330   20.854  1.00 14.76 ? 79  LEU A CD1  1 
ATOM   746  C  CD2  . LEU A 1 79  ? -17.037 4.838   21.020  1.00 11.59 ? 79  LEU A CD2  1 
ATOM   747  N  N    . LYS A 1 80  ? -20.679 7.928   22.321  1.00 11.24 ? 80  LYS A N    1 
ATOM   748  C  CA   . LYS A 1 80  ? -20.693 8.584   23.602  1.00 11.69 ? 80  LYS A CA   1 
ATOM   749  C  C    . LYS A 1 80  ? -21.289 7.723   24.656  1.00 12.16 ? 80  LYS A C    1 
ATOM   750  O  O    . LYS A 1 80  ? -21.568 6.539   24.394  1.00 12.69 ? 80  LYS A O    1 
ATOM   751  C  CB   . LYS A 1 80  ? -21.386 9.932   23.511  1.00 14.94 ? 80  LYS A CB   1 
ATOM   752  C  CG   . LYS A 1 80  ? -22.920 9.741   23.316  1.00 16.60 ? 80  LYS A CG   1 
ATOM   753  C  CD   . LYS A 1 80  ? -23.649 11.164  23.164  1.00 18.69 ? 80  LYS A CD   1 
ATOM   754  C  CE   . LYS A 1 80  ? -25.192 11.016  23.248  1.00 23.31 ? 80  LYS A CE   1 
ATOM   755  N  NZ   . LYS A 1 80  ? -25.828 10.191  22.148  1.00 34.70 ? 80  LYS A NZ   1 
ATOM   756  N  N    . GLY A 1 81  ? -21.396 8.200   25.918  1.00 12.57 ? 81  GLY A N    1 
ATOM   757  C  CA   . GLY A 1 81  ? -21.894 7.320   26.985  1.00 13.56 ? 81  GLY A CA   1 
ATOM   758  C  C    . GLY A 1 81  ? -20.885 6.258   27.305  1.00 13.27 ? 81  GLY A C    1 
ATOM   759  O  O    . GLY A 1 81  ? -19.713 6.507   27.114  1.00 12.88 ? 81  GLY A O    1 
ATOM   760  N  N    . GLY A 1 82  ? -21.326 5.193   27.916  1.00 14.45 ? 82  GLY A N    1 
ATOM   761  C  CA   . GLY A 1 82  ? -20.367 4.235   28.250  1.00 14.24 ? 82  GLY A CA   1 
ATOM   762  C  C    . GLY A 1 82  ? -19.503 4.789   29.347  1.00 14.91 ? 82  GLY A C    1 
ATOM   763  O  O    . GLY A 1 82  ? -19.988 5.502   30.261  1.00 20.02 ? 82  GLY A O    1 
ATOM   764  N  N    . PRO A 1 83  ? -18.195 4.533   29.276  1.00 13.70 ? 83  PRO A N    1 
ATOM   765  C  CA   . PRO A 1 83  ? -17.309 5.187   30.233  1.00 12.68 ? 83  PRO A CA   1 
ATOM   766  C  C    . PRO A 1 83  ? -16.818 6.615   29.803  1.00 14.51 ? 83  PRO A C    1 
ATOM   767  O  O    . PRO A 1 83  ? -16.005 7.220   30.499  1.00 15.56 ? 83  PRO A O    1 
ATOM   768  C  CB   . PRO A 1 83  ? -15.989 4.266   29.999  1.00 13.75 ? 83  PRO A CB   1 
ATOM   769  C  CG   . PRO A 1 83  ? -16.033 3.970   28.581  1.00 11.67 ? 83  PRO A CG   1 
ATOM   770  C  CD   . PRO A 1 83  ? -17.470 3.674   28.286  1.00 12.15 ? 83  PRO A CD   1 
ATOM   771  N  N    . LEU A 1 84  ? -17.376 7.122   28.712  1.00 12.12 ? 84  LEU A N    1 
ATOM   772  C  CA   . LEU A 1 84  ? -16.836 8.323   28.078  1.00 12.34 ? 84  LEU A CA   1 
ATOM   773  C  C    . LEU A 1 84  ? -17.451 9.569   28.690  1.00 14.45 ? 84  LEU A C    1 
ATOM   774  O  O    . LEU A 1 84  ? -18.668 9.601   28.904  1.00 14.66 ? 84  LEU A O    1 
ATOM   775  C  CB   . LEU A 1 84  ? -17.049 8.319   26.573  1.00 11.12 ? 84  LEU A CB   1 
ATOM   776  C  CG   . LEU A 1 84  ? -16.512 7.039   25.922  1.00 9.96  ? 84  LEU A CG   1 
ATOM   777  C  CD1  . LEU A 1 84  ? -16.896 6.983   24.427  1.00 11.55 ? 84  LEU A CD1  1 
ATOM   778  C  CD2  . LEU A 1 84  ? -14.923 7.067   25.966  1.00 9.82  ? 84  LEU A CD2  1 
ATOM   779  N  N    . ASP A 1 85  ? -16.672 10.618  28.689  1.00 14.38 ? 85  ASP A N    1 
ATOM   780  C  CA   . ASP A 1 85  ? -17.203 11.976  28.976  1.00 17.83 ? 85  ASP A CA   1 
ATOM   781  C  C    . ASP A 1 85  ? -17.247 12.584  27.533  1.00 15.71 ? 85  ASP A C    1 
ATOM   782  O  O    . ASP A 1 85  ? -16.231 12.571  26.819  1.00 21.19 ? 85  ASP A O    1 
ATOM   783  C  CB   . ASP A 1 85  ? -16.198 12.700  29.935  1.00 18.80 ? 85  ASP A CB   1 
ATOM   784  C  CG   . ASP A 1 85  ? -16.299 12.219  31.319  1.00 24.27 ? 85  ASP A CG   1 
ATOM   785  O  OD1  . ASP A 1 85  ? -17.374 11.639  31.726  1.00 26.83 ? 85  ASP A OD1  1 
ATOM   786  O  OD2  . ASP A 1 85  ? -15.208 12.363  32.033  1.00 32.87 ? 85  ASP A OD2  1 
ATOM   787  N  N    . GLY A 1 86  ? -18.221 13.398  27.210  1.00 20.04 ? 86  GLY A N    1 
ATOM   788  C  CA   . GLY A 1 86  ? -18.187 14.019  25.952  1.00 19.24 ? 86  GLY A CA   1 
ATOM   789  C  C    . GLY A 1 86  ? -18.425 13.101  24.728  1.00 18.35 ? 86  GLY A C    1 
ATOM   790  O  O    . GLY A 1 86  ? -19.076 12.094  24.821  1.00 22.13 ? 86  GLY A O    1 
ATOM   791  N  N    . THR A 1 87  ? -18.015 13.517  23.535  1.00 14.61 ? 87  THR A N    1 
ATOM   792  C  CA   . THR A 1 87  ? -18.482 12.902  22.320  1.00 13.22 ? 87  THR A CA   1 
ATOM   793  C  C    . THR A 1 87  ? -17.311 12.635  21.457  1.00 11.06 ? 87  THR A C    1 
ATOM   794  O  O    . THR A 1 87  ? -16.364 13.457  21.315  1.00 11.21 ? 87  THR A O    1 
ATOM   795  C  CB   . THR A 1 87  ? -19.571 13.810  21.575  1.00 16.12 ? 87  THR A CB   1 
ATOM   796  O  OG1  . THR A 1 87  ? -18.948 15.057  21.405  1.00 17.51 ? 87  THR A OG1  1 
ATOM   797  C  CG2  . THR A 1 87  ? -20.759 14.142  22.354  1.00 16.60 ? 87  THR A CG2  1 
ATOM   798  N  N    . TYR A 1 88  ? -17.344 11.473  20.848  1.00 9.98  ? 88  TYR A N    1 
ATOM   799  C  CA   . TYR A 1 88  ? -16.264 11.013  20.016  1.00 8.48  ? 88  TYR A CA   1 
ATOM   800  C  C    . TYR A 1 88  ? -16.743 10.764  18.624  1.00 8.51  ? 88  TYR A C    1 
ATOM   801  O  O    . TYR A 1 88  ? -17.748 10.056  18.462  1.00 12.69 ? 88  TYR A O    1 
ATOM   802  C  CB   . TYR A 1 88  ? -15.555 9.805   20.579  1.00 8.87  ? 88  TYR A CB   1 
ATOM   803  C  CG   . TYR A 1 88  ? -14.851 10.005  21.851  1.00 9.07  ? 88  TYR A CG   1 
ATOM   804  C  CD1  . TYR A 1 88  ? -15.505 10.282  23.037  1.00 9.02  ? 88  TYR A CD1  1 
ATOM   805  C  CD2  . TYR A 1 88  ? -13.409 9.858   21.934  1.00 7.74  ? 88  TYR A CD2  1 
ATOM   806  C  CE1  . TYR A 1 88  ? -14.867 10.477  24.199  1.00 9.09  ? 88  TYR A CE1  1 
ATOM   807  C  CE2  . TYR A 1 88  ? -12.771 10.072  23.122  1.00 7.07  ? 88  TYR A CE2  1 
ATOM   808  C  CZ   . TYR A 1 88  ? -13.425 10.265  24.233  1.00 8.35  ? 88  TYR A CZ   1 
ATOM   809  O  OH   . TYR A 1 88  ? -12.760 10.384  25.425  1.00 8.32  ? 88  TYR A OH   1 
ATOM   810  N  N    . ARG A 1 89  ? -16.086 11.213  17.592  1.00 9.67  ? 89  ARG A N    1 
ATOM   811  C  CA   . ARG A 1 89  ? -16.564 11.073  16.212  1.00 9.53  ? 89  ARG A CA   1 
ATOM   812  C  C    . ARG A 1 89  ? -15.780 10.022  15.431  1.00 7.93  ? 89  ARG A C    1 
ATOM   813  O  O    . ARG A 1 89  ? -14.545 9.889   15.531  1.00 8.38  ? 89  ARG A O    1 
ATOM   814  C  CB   . ARG A 1 89  ? -16.339 12.415  15.565  1.00 12.76 ? 89  ARG A CB   1 
ATOM   815  C  CG   . ARG A 1 89  ? -17.091 12.537  14.269  1.00 13.96 ? 89  ARG A CG   1 
ATOM   816  C  CD   . ARG A 1 89  ? -16.927 13.995  13.746  1.00 15.25 ? 89  ARG A CD   1 
ATOM   817  N  NE   . ARG A 1 89  ? -17.619 15.011  14.562  1.00 14.86 ? 89  ARG A NE   1 
ATOM   818  C  CZ   . ARG A 1 89  ? -17.430 16.316  14.388  1.00 13.89 ? 89  ARG A CZ   1 
ATOM   819  N  NH1  . ARG A 1 89  ? -16.639 16.755  13.399  1.00 15.83 ? 89  ARG A NH1  1 
ATOM   820  N  NH2  . ARG A 1 89  ? -18.093 17.161  15.177  1.00 14.89 ? 89  ARG A NH2  1 
ATOM   821  N  N    . LEU A 1 90  ? -16.609 9.221   14.696  1.00 8.30  ? 90  LEU A N    1 
ATOM   822  C  CA   . LEU A 1 90  ? -16.008 8.076   13.957  1.00 9.41  ? 90  LEU A CA   1 
ATOM   823  C  C    . LEU A 1 90  ? -15.127 8.656   12.802  1.00 8.51  ? 90  LEU A C    1 
ATOM   824  O  O    . LEU A 1 90  ? -15.563 9.493   12.005  1.00 10.39 ? 90  LEU A O    1 
ATOM   825  C  CB   . LEU A 1 90  ? -17.133 7.252   13.326  1.00 9.20  ? 90  LEU A CB   1 
ATOM   826  C  CG   . LEU A 1 90  ? -16.661 6.105   12.444  1.00 9.57  ? 90  LEU A CG   1 
ATOM   827  C  CD1  . LEU A 1 90  ? -15.954 4.977   13.248  1.00 10.85 ? 90  LEU A CD1  1 
ATOM   828  C  CD2  . LEU A 1 90  ? -17.915 5.452   11.819  1.00 11.60 ? 90  LEU A CD2  1 
ATOM   829  N  N    . ILE A 1 91  ? -13.899 8.173   12.742  1.00 8.49  ? 91  ILE A N    1 
ATOM   830  C  CA   . ILE A 1 91  ? -13.001 8.572   11.648  1.00 10.63 ? 91  ILE A CA   1 
ATOM   831  C  C    . ILE A 1 91  ? -12.714 7.400   10.697  1.00 9.42  ? 91  ILE A C    1 
ATOM   832  O  O    . ILE A 1 91  ? -12.620 7.579   9.468   1.00 9.43  ? 91  ILE A O    1 
ATOM   833  C  CB   . ILE A 1 91  ? -11.669 9.183   12.133  1.00 11.16 ? 91  ILE A CB   1 
ATOM   834  C  CG1  . ILE A 1 91  ? -10.740 9.563   10.949  1.00 11.82 ? 91  ILE A CG1  1 
ATOM   835  C  CG2  . ILE A 1 91  ? -10.944 8.352   13.157  1.00 10.54 ? 91  ILE A CG2  1 
ATOM   836  C  CD1  . ILE A 1 91  ? -9.514  10.451  11.297  1.00 13.69 ? 91  ILE A CD1  1 
ATOM   837  N  N    . GLN A 1 92  ? -12.618 6.138   11.225  1.00 8.97  ? 92  GLN A N    1 
ATOM   838  C  CA   . GLN A 1 92  ? -12.303 5.048   10.309  1.00 9.62  ? 92  GLN A CA   1 
ATOM   839  C  C    . GLN A 1 92  ? -12.593 3.750   11.102  1.00 9.43  ? 92  GLN A C    1 
ATOM   840  O  O    . GLN A 1 92  ? -12.656 3.782   12.333  1.00 9.03  ? 92  GLN A O    1 
ATOM   841  C  CB   . GLN A 1 92  ? -10.877 5.013   9.827   1.00 10.75 ? 92  GLN A CB   1 
ATOM   842  C  CG   . GLN A 1 92  ? -9.838  5.060   10.973  1.00 9.54  ? 92  GLN A CG   1 
ATOM   843  C  CD   . GLN A 1 92  ? -9.098  3.771   11.099  1.00 9.74  ? 92  GLN A CD   1 
ATOM   844  O  OE1  . GLN A 1 92  ? -9.677  2.674   11.241  1.00 10.67 ? 92  GLN A OE1  1 
ATOM   845  N  NE2  . GLN A 1 92  ? -7.793  3.854   11.101  1.00 11.48 ? 92  GLN A NE2  1 
ATOM   846  N  N    . PHE A 1 93  ? -12.772 2.649   10.350  1.00 9.66  ? 93  PHE A N    1 
ATOM   847  C  CA   . PHE A 1 93  ? -12.614 1.377   10.992  1.00 8.69  ? 93  PHE A CA   1 
ATOM   848  C  C    . PHE A 1 93  ? -11.610 0.499   10.194  1.00 8.06  ? 93  PHE A C    1 
ATOM   849  O  O    . PHE A 1 93  ? -11.386 0.695   9.004   1.00 9.96  ? 93  PHE A O    1 
ATOM   850  C  CB   . PHE A 1 93  ? -13.936 0.629   11.244  1.00 9.28  ? 93  PHE A CB   1 
ATOM   851  C  CG   . PHE A 1 93  ? -14.685 0.197   9.982   1.00 10.82 ? 93  PHE A CG   1 
ATOM   852  C  CD1  . PHE A 1 93  ? -14.321 -1.012  9.338   1.00 10.79 ? 93  PHE A CD1  1 
ATOM   853  C  CD2  . PHE A 1 93  ? -15.757 0.946   9.529   1.00 11.18 ? 93  PHE A CD2  1 
ATOM   854  C  CE1  . PHE A 1 93  ? -15.013 -1.428  8.239   1.00 11.83 ? 93  PHE A CE1  1 
ATOM   855  C  CE2  . PHE A 1 93  ? -16.521 0.443   8.411   1.00 12.43 ? 93  PHE A CE2  1 
ATOM   856  C  CZ   . PHE A 1 93  ? -16.121 -0.678  7.781   1.00 12.26 ? 93  PHE A CZ   1 
ATOM   857  N  N    . HIS A 1 94  ? -11.067 -0.541  10.874  1.00 9.27  ? 94  HIS A N    1 
ATOM   858  C  CA   . HIS A 1 94  ? -10.220 -1.505  10.190  1.00 7.87  ? 94  HIS A CA   1 
ATOM   859  C  C    . HIS A 1 94  ? -10.326 -2.754  11.080  1.00 7.31  ? 94  HIS A C    1 
ATOM   860  O  O    . HIS A 1 94  ? -10.890 -2.795  12.139  1.00 7.30  ? 94  HIS A O    1 
ATOM   861  C  CB   . HIS A 1 94  ? -8.774  -1.036  10.155  1.00 8.39  ? 94  HIS A CB   1 
ATOM   862  C  CG   . HIS A 1 94  ? -8.267  -0.738  11.524  1.00 8.39  ? 94  HIS A CG   1 
ATOM   863  N  ND1  . HIS A 1 94  ? -8.390  0.470   12.156  1.00 7.56  ? 94  HIS A ND1  1 
ATOM   864  C  CD2  . HIS A 1 94  ? -7.617  -1.526  12.430  1.00 8.39  ? 94  HIS A CD2  1 
ATOM   865  C  CE1  . HIS A 1 94  ? -7.957  0.404   13.369  1.00 7.35  ? 94  HIS A CE1  1 
ATOM   866  N  NE2  . HIS A 1 94  ? -7.514  -0.825  13.592  1.00 6.98  ? 94  HIS A NE2  1 
ATOM   867  N  N    . PHE A 1 95  ? -9.614  -3.789  10.575  1.00 8.28  ? 95  PHE A N    1 
ATOM   868  C  CA   . PHE A 1 95  ? -9.565  -5.144  11.242  1.00 8.58  ? 95  PHE A CA   1 
ATOM   869  C  C    . PHE A 1 95  ? -8.108  -5.567  11.476  1.00 7.94  ? 95  PHE A C    1 
ATOM   870  O  O    . PHE A 1 95  ? -7.231  -5.069  10.790  1.00 7.89  ? 95  PHE A O    1 
ATOM   871  C  CB   . PHE A 1 95  ? -10.312 -6.219  10.430  1.00 8.36  ? 95  PHE A CB   1 
ATOM   872  C  CG   . PHE A 1 95  ? -11.715 -5.878  10.136  1.00 7.94  ? 95  PHE A CG   1 
ATOM   873  C  CD1  . PHE A 1 95  ? -12.047 -5.057  9.051   1.00 8.29  ? 95  PHE A CD1  1 
ATOM   874  C  CD2  . PHE A 1 95  ? -12.755 -6.491  10.804  1.00 9.06  ? 95  PHE A CD2  1 
ATOM   875  C  CE1  . PHE A 1 95  ? -13.354 -4.829  8.719   1.00 8.32  ? 95  PHE A CE1  1 
ATOM   876  C  CE2  . PHE A 1 95  ? -14.077 -6.307  10.445  1.00 8.72  ? 95  PHE A CE2  1 
ATOM   877  C  CZ   . PHE A 1 95  ? -14.346 -5.478  9.381   1.00 8.99  ? 95  PHE A CZ   1 
ATOM   878  N  N    . HIS A 1 96  ? -7.954  -6.494  12.385  1.00 6.75  ? 96  HIS A N    1 
ATOM   879  C  CA   . HIS A 1 96  ? -6.758  -7.317  12.520  1.00 6.93  ? 96  HIS A CA   1 
ATOM   880  C  C    . HIS A 1 96  ? -7.221  -8.743  12.437  1.00 6.38  ? 96  HIS A C    1 
ATOM   881  O  O    . HIS A 1 96  ? -8.264  -9.105  12.915  1.00 7.16  ? 96  HIS A O    1 
ATOM   882  C  CB   . HIS A 1 96  ? -6.125  -7.077  13.917  1.00 7.18  ? 96  HIS A CB   1 
ATOM   883  C  CG   . HIS A 1 96  ? -5.805  -5.616  14.179  1.00 6.13  ? 96  HIS A CG   1 
ATOM   884  N  ND1  . HIS A 1 96  ? -4.547  -5.041  13.963  1.00 8.15  ? 96  HIS A ND1  1 
ATOM   885  C  CD2  . HIS A 1 96  ? -6.681  -4.611  14.532  1.00 7.21  ? 96  HIS A CD2  1 
ATOM   886  C  CE1  . HIS A 1 96  ? -4.637  -3.738  14.267  1.00 7.61  ? 96  HIS A CE1  1 
ATOM   887  N  NE2  . HIS A 1 96  ? -5.866  -3.399  14.564  1.00 7.96  ? 96  HIS A NE2  1 
ATOM   888  N  N    . TRP A 1 97  ? -6.400  -9.619  11.732  1.00 6.86  ? 97  TRP A N    1 
ATOM   889  C  CA   . TRP A 1 97  ? -6.887  -11.005 11.527  1.00 6.69  ? 97  TRP A CA   1 
ATOM   890  C  C    . TRP A 1 97  ? -5.669  -11.910 11.380  1.00 6.54  ? 97  TRP A C    1 
ATOM   891  O  O    . TRP A 1 97  ? -4.479  -11.454 11.306  1.00 8.29  ? 97  TRP A O    1 
ATOM   892  C  CB   . TRP A 1 97  ? -7.719  -11.063 10.269  1.00 8.30  ? 97  TRP A CB   1 
ATOM   893  C  CG   . TRP A 1 97  ? -7.113  -10.676 8.997   1.00 7.64  ? 97  TRP A CG   1 
ATOM   894  C  CD1  . TRP A 1 97  ? -6.396  -11.493 8.165   1.00 9.61  ? 97  TRP A CD1  1 
ATOM   895  C  CD2  . TRP A 1 97  ? -7.045  -9.374  8.422   1.00 8.34  ? 97  TRP A CD2  1 
ATOM   896  N  NE1  . TRP A 1 97  ? -5.934  -10.796 7.061   1.00 10.21 ? 97  TRP A NE1  1 
ATOM   897  C  CE2  . TRP A 1 97  ? -6.316  -9.450  7.207   1.00 8.51  ? 97  TRP A CE2  1 
ATOM   898  C  CE3  . TRP A 1 97  ? -7.568  -8.090  8.840   1.00 7.16  ? 97  TRP A CE3  1 
ATOM   899  C  CZ2  . TRP A 1 97  ? -6.063  -8.373  6.409   1.00 9.99  ? 97  TRP A CZ2  1 
ATOM   900  C  CZ3  . TRP A 1 97  ? -7.261  -7.004  8.011   1.00 9.14  ? 97  TRP A CZ3  1 
ATOM   901  C  CH2  . TRP A 1 97  ? -6.644  -7.174  6.826   1.00 10.39 ? 97  TRP A CH2  1 
ATOM   902  N  N    . GLY A 1 98  ? -5.946  -13.229 11.422  1.00 7.75  ? 98  GLY A N    1 
ATOM   903  C  CA   . GLY A 1 98  ? -4.919  -14.245 11.416  1.00 8.41  ? 98  GLY A CA   1 
ATOM   904  C  C    . GLY A 1 98  ? -4.654  -14.870 10.131  1.00 8.19  ? 98  GLY A C    1 
ATOM   905  O  O    . GLY A 1 98  ? -5.372  -14.736 9.181   1.00 8.91  ? 98  GLY A O    1 
ATOM   906  N  N    . SER A 1 99  ? -3.644  -15.760 10.141  1.00 9.12  ? 99  SER A N    1 
ATOM   907  C  CA   . SER A 1 99  ? -3.394  -16.635 8.967   1.00 9.26  ? 99  SER A CA   1 
ATOM   908  C  C    . SER A 1 99  ? -4.276  -17.891 9.103   1.00 10.21 ? 99  SER A C    1 
ATOM   909  O  O    . SER A 1 99  ? -4.380  -18.605 8.112   1.00 11.86 ? 99  SER A O    1 
ATOM   910  C  CB   . SER A 1 99  ? -1.924  -16.988 8.928   1.00 10.71 ? 99  SER A CB   1 
ATOM   911  O  OG   . SER A 1 99  ? -1.514  -17.534 10.193  1.00 10.98 ? 99  SER A OG   1 
ATOM   912  N  N    . LEU A 1 100 ? -4.835  -18.145 10.261  1.00 9.22  ? 100 LEU A N    1 
ATOM   913  C  CA   . LEU A 1 100 ? -5.626  -19.238 10.618  1.00 10.10 ? 100 LEU A CA   1 
ATOM   914  C  C    . LEU A 1 100 ? -6.762  -18.832 11.487  1.00 9.19  ? 100 LEU A C    1 
ATOM   915  O  O    . LEU A 1 100 ? -6.649  -17.790 12.131  1.00 10.66 ? 100 LEU A O    1 
ATOM   916  C  CB   . LEU A 1 100 ? -4.766  -20.205 11.445  1.00 13.56 ? 100 LEU A CB   1 
ATOM   917  C  CG   . LEU A 1 100 ? -3.374  -20.567 10.928  1.00 16.47 ? 100 LEU A CG   1 
ATOM   918  C  CD1  . LEU A 1 100 ? -2.388  -20.807 12.072  1.00 21.30 ? 100 LEU A CD1  1 
ATOM   919  C  CD2  . LEU A 1 100 ? -3.498  -21.802 10.062  1.00 22.54 ? 100 LEU A CD2  1 
ATOM   920  N  N    . ASP A 1 101 ? -7.848  -19.589 11.514  1.00 9.02  ? 101 ASP A N    1 
ATOM   921  C  CA   . ASP A 1 101 ? -9.036  -19.106 12.246  1.00 9.81  ? 101 ASP A CA   1 
ATOM   922  C  C    . ASP A 1 101 ? -8.778  -19.054 13.799  1.00 9.62  ? 101 ASP A C    1 
ATOM   923  O  O    . ASP A 1 101 ? -9.450  -18.319 14.495  1.00 12.04 ? 101 ASP A O    1 
ATOM   924  C  CB   . ASP A 1 101 ? -10.253 -20.006 12.059  1.00 10.61 ? 101 ASP A CB   1 
ATOM   925  C  CG   . ASP A 1 101 ? -10.701 -20.116 10.609  1.00 12.57 ? 101 ASP A CG   1 
ATOM   926  O  OD1  . ASP A 1 101 ? -10.413 -19.213 9.793   1.00 13.66 ? 101 ASP A OD1  1 
ATOM   927  O  OD2  . ASP A 1 101 ? -11.535 -20.988 10.370  1.00 18.69 ? 101 ASP A OD2  1 
ATOM   928  N  N    . GLY A 1 102 ? -7.776  -19.854 14.245  1.00 10.06 ? 102 GLY A N    1 
ATOM   929  C  CA   . GLY A 1 102 ? -7.476  -19.863 15.689  1.00 8.90  ? 102 GLY A CA   1 
ATOM   930  C  C    . GLY A 1 102 ? -6.660  -18.669 16.246  1.00 9.85  ? 102 GLY A C    1 
ATOM   931  O  O    . GLY A 1 102 ? -6.294  -18.642 17.424  1.00 9.53  ? 102 GLY A O    1 
ATOM   932  N  N    A GLN A 1 103 ? -6.503  -17.627 15.401  0.50 9.08  ? 103 GLN A N    1 
ATOM   933  N  N    B GLN A 1 103 ? -6.300  -17.652 15.432  0.50 8.65  ? 103 GLN A N    1 
ATOM   934  C  CA   A GLN A 1 103 ? -5.760  -16.441 15.830  0.50 7.67  ? 103 GLN A CA   1 
ATOM   935  C  CA   B GLN A 1 103 ? -5.584  -16.493 16.036  0.50 7.67  ? 103 GLN A CA   1 
ATOM   936  C  C    A GLN A 1 103 ? -6.244  -15.290 14.969  0.50 6.18  ? 103 GLN A C    1 
ATOM   937  C  C    B GLN A 1 103 ? -5.949  -15.322 15.191  0.50 8.27  ? 103 GLN A C    1 
ATOM   938  O  O    A GLN A 1 103 ? -6.843  -15.472 13.943  0.50 7.57  ? 103 GLN A O    1 
ATOM   939  O  O    B GLN A 1 103 ? -6.429  -15.491 14.019  0.50 6.87  ? 103 GLN A O    1 
ATOM   940  C  CB   A GLN A 1 103 ? -4.270  -16.625 15.764  0.50 8.15  ? 103 GLN A CB   1 
ATOM   941  C  CB   B GLN A 1 103 ? -4.086  -16.715 16.139  0.50 9.24  ? 103 GLN A CB   1 
ATOM   942  C  CG   A GLN A 1 103 ? -3.751  -16.918 14.316  0.50 8.10  ? 103 GLN A CG   1 
ATOM   943  C  CG   B GLN A 1 103 ? -3.431  -16.959 14.763  0.50 8.69  ? 103 GLN A CG   1 
ATOM   944  C  CD   A GLN A 1 103 ? -2.380  -17.530 14.358  0.50 8.54  ? 103 GLN A CD   1 
ATOM   945  C  CD   B GLN A 1 103 ? -1.966  -17.315 14.904  0.50 9.87  ? 103 GLN A CD   1 
ATOM   946  O  OE1  A GLN A 1 103 ? -2.181  -18.545 15.105  0.50 9.53  ? 103 GLN A OE1  1 
ATOM   947  O  OE1  B GLN A 1 103 ? -1.614  -17.899 15.881  0.50 14.15 ? 103 GLN A OE1  1 
ATOM   948  N  NE2  A GLN A 1 103 ? -1.451  -17.028 13.535  0.50 10.57 ? 103 GLN A NE2  1 
ATOM   949  N  NE2  B GLN A 1 103 ? -1.143  -16.948 13.963  0.50 9.67  ? 103 GLN A NE2  1 
ATOM   950  N  N    A GLY A 1 104 ? -5.828  -14.086 15.409  0.50 7.05  ? 104 GLY A N    1 
ATOM   951  N  N    B GLY A 1 104 ? -5.617  -14.121 15.738  0.50 6.51  ? 104 GLY A N    1 
ATOM   952  C  CA   A GLY A 1 104 ? -6.187  -12.851 14.664  0.50 5.68  ? 104 GLY A CA   1 
ATOM   953  C  CA   B GLY A 1 104 ? -5.874  -12.899 14.938  0.50 6.41  ? 104 GLY A CA   1 
ATOM   954  C  C    A GLY A 1 104 ? -6.649  -11.702 15.478  0.50 5.98  ? 104 GLY A C    1 
ATOM   955  C  C    B GLY A 1 104 ? -6.391  -11.736 15.677  0.50 8.20  ? 104 GLY A C    1 
ATOM   956  O  O    A GLY A 1 104 ? -6.379  -10.505 15.109  0.50 5.28  ? 104 GLY A O    1 
ATOM   957  O  O    B GLY A 1 104 ? -6.078  -10.605 15.384  0.50 7.36  ? 104 GLY A O    1 
ATOM   958  N  N    . SER A 1 105 ? -7.199  -11.953 16.688  1.00 5.90  ? 105 SER A N    1 
ATOM   959  C  CA   . SER A 1 105 ? -7.609  -10.802 17.551  1.00 5.96  ? 105 SER A CA   1 
ATOM   960  C  C    . SER A 1 105 ? -6.391  -10.288 18.305  1.00 7.39  ? 105 SER A C    1 
ATOM   961  O  O    . SER A 1 105 ? -5.366  -10.960 18.506  1.00 7.09  ? 105 SER A O    1 
ATOM   962  C  CB   . SER A 1 105 ? -8.709  -11.210 18.440  1.00 6.76  ? 105 SER A CB   1 
ATOM   963  O  OG   . SER A 1 105 ? -8.357  -12.155 19.448  1.00 7.32  ? 105 SER A OG   1 
ATOM   964  N  N    . GLU A 1 106 ? -6.528  -9.040  18.680  1.00 5.73  ? 106 GLU A N    1 
ATOM   965  C  CA   . GLU A 1 106 ? -5.513  -8.397  19.495  1.00 6.30  ? 106 GLU A CA   1 
ATOM   966  C  C    . GLU A 1 106 ? -5.814  -8.510  20.992  1.00 6.87  ? 106 GLU A C    1 
ATOM   967  O  O    . GLU A 1 106 ? -5.058  -9.091  21.763  1.00 7.03  ? 106 GLU A O    1 
ATOM   968  C  CB   . GLU A 1 106 ? -5.441  -6.864  19.070  1.00 6.28  ? 106 GLU A CB   1 
ATOM   969  C  CG   . GLU A 1 106 ? -4.913  -6.781  17.695  1.00 7.97  ? 106 GLU A CG   1 
ATOM   970  C  CD   . GLU A 1 106 ? -4.310  -5.473  17.351  1.00 6.30  ? 106 GLU A CD   1 
ATOM   971  O  OE1  . GLU A 1 106 ? -4.955  -4.421  17.574  1.00 7.28  ? 106 GLU A OE1  1 
ATOM   972  O  OE2  . GLU A 1 106 ? -3.142  -5.469  16.819  1.00 9.40  ? 106 GLU A OE2  1 
ATOM   973  N  N    . HIS A 1 107 ? -7.039  -8.069  21.367  1.00 6.33  ? 107 HIS A N    1 
ATOM   974  C  CA   . HIS A 1 107 ? -7.524  -8.440  22.681  1.00 5.74  ? 107 HIS A CA   1 
ATOM   975  C  C    . HIS A 1 107 ? -7.818  -9.983  22.717  1.00 6.76  ? 107 HIS A C    1 
ATOM   976  O  O    . HIS A 1 107 ? -8.109  -10.520 21.685  1.00 6.71  ? 107 HIS A O    1 
ATOM   977  C  CB   . HIS A 1 107 ? -8.765  -7.622  23.078  1.00 6.23  ? 107 HIS A CB   1 
ATOM   978  C  CG   . HIS A 1 107 ? -8.441  -6.177  23.261  1.00 6.81  ? 107 HIS A CG   1 
ATOM   979  N  ND1  . HIS A 1 107 ? -8.484  -5.296  22.191  1.00 7.28  ? 107 HIS A ND1  1 
ATOM   980  C  CD2  . HIS A 1 107 ? -7.985  -5.478  24.352  1.00 6.09  ? 107 HIS A CD2  1 
ATOM   981  C  CE1  . HIS A 1 107 ? -8.037  -4.103  22.620  1.00 6.23  ? 107 HIS A CE1  1 
ATOM   982  N  NE2  . HIS A 1 107 ? -7.717  -4.170  23.926  1.00 6.50  ? 107 HIS A NE2  1 
ATOM   983  N  N    . THR A 1 108 ? -7.677  -10.500 23.925  1.00 6.54  ? 108 THR A N    1 
ATOM   984  C  CA   . THR A 1 108 ? -8.050  -11.950 24.180  1.00 7.58  ? 108 THR A CA   1 
ATOM   985  C  C    . THR A 1 108 ? -8.954  -11.923 25.380  1.00 7.46  ? 108 THR A C    1 
ATOM   986  O  O    . THR A 1 108 ? -9.042  -10.934 26.140  1.00 7.84  ? 108 THR A O    1 
ATOM   987  C  CB   . THR A 1 108 ? -6.795  -12.837 24.345  1.00 8.32  ? 108 THR A CB   1 
ATOM   988  O  OG1  . THR A 1 108 ? -5.986  -12.321 25.427  1.00 8.01  ? 108 THR A OG1  1 
ATOM   989  C  CG2  . THR A 1 108 ? -5.995  -12.898 23.040  1.00 8.35  ? 108 THR A CG2  1 
ATOM   990  N  N    . VAL A 1 109 ? -9.725  -12.984 25.519  1.00 6.75  ? 109 VAL A N    1 
ATOM   991  C  CA   . VAL A 1 109 ? -10.719 -13.076 26.618  1.00 8.96  ? 109 VAL A CA   1 
ATOM   992  C  C    . VAL A 1 109 ? -10.418 -14.384 27.336  1.00 8.53  ? 109 VAL A C    1 
ATOM   993  O  O    . VAL A 1 109 ? -10.575 -15.479 26.771  1.00 8.35  ? 109 VAL A O    1 
ATOM   994  C  CB   . VAL A 1 109 ? -12.173 -13.080 26.063  1.00 9.29  ? 109 VAL A CB   1 
ATOM   995  C  CG1  . VAL A 1 109 ? -13.215 -13.232 27.174  1.00 11.09 ? 109 VAL A CG1  1 
ATOM   996  C  CG2  . VAL A 1 109 ? -12.460 -11.818 25.270  1.00 8.55  ? 109 VAL A CG2  1 
ATOM   997  N  N    . ASP A 1 110 ? -9.920  -14.244 28.582  1.00 8.66  ? 110 ASP A N    1 
ATOM   998  C  CA   . ASP A 1 110 ? -9.359  -15.494 29.318  1.00 10.08 ? 110 ASP A CA   1 
ATOM   999  C  C    . ASP A 1 110 ? -8.514  -16.270 28.368  1.00 9.71  ? 110 ASP A C    1 
ATOM   1000 O  O    . ASP A 1 110 ? -8.549  -17.511 28.314  1.00 10.26 ? 110 ASP A O    1 
ATOM   1001 C  CB   . ASP A 1 110 ? -10.503 -16.328 29.833  1.00 12.38 ? 110 ASP A CB   1 
ATOM   1002 C  CG   . ASP A 1 110 ? -11.421 -15.510 30.794  1.00 11.15 ? 110 ASP A CG   1 
ATOM   1003 O  OD1  . ASP A 1 110 ? -10.869 -14.666 31.497  1.00 12.55 ? 110 ASP A OD1  1 
ATOM   1004 O  OD2  . ASP A 1 110 ? -12.579 -15.864 30.938  1.00 14.51 ? 110 ASP A OD2  1 
ATOM   1005 N  N    . LYS A 1 111 ? -7.612  -15.530 27.640  1.00 8.43  ? 111 LYS A N    1 
ATOM   1006 C  CA   . LYS A 1 111 ? -6.592  -16.100 26.760  1.00 9.41  ? 111 LYS A CA   1 
ATOM   1007 C  C    . LYS A 1 111 ? -7.136  -16.608 25.450  1.00 8.62  ? 111 LYS A C    1 
ATOM   1008 O  O    . LYS A 1 111 ? -6.337  -17.000 24.587  1.00 10.85 ? 111 LYS A O    1 
ATOM   1009 C  CB   . LYS A 1 111 ? -5.664  -17.188 27.442  1.00 11.19 ? 111 LYS A CB   1 
ATOM   1010 C  CG   . LYS A 1 111 ? -4.926  -16.648 28.687  1.00 14.80 ? 111 LYS A CG   1 
ATOM   1011 C  CD   . LYS A 1 111 ? -4.051  -15.453 28.324  1.00 17.67 ? 111 LYS A CD   1 
ATOM   1012 C  CE   . LYS A 1 111 ? -3.308  -14.883 29.525  1.00 18.97 ? 111 LYS A CE   1 
ATOM   1013 N  NZ   . LYS A 1 111 ? -2.033  -15.604 29.804  1.00 22.97 ? 111 LYS A NZ   1 
ATOM   1014 N  N    . LYS A 1 112 ? -8.486  -16.586 25.267  1.00 7.77  ? 112 LYS A N    1 
ATOM   1015 C  CA   . LYS A 1 112 ? -9.035  -17.002 24.001  1.00 8.32  ? 112 LYS A CA   1 
ATOM   1016 C  C    . LYS A 1 112 ? -8.650  -15.927 22.914  1.00 9.18  ? 112 LYS A C    1 
ATOM   1017 O  O    . LYS A 1 112 ? -8.948  -14.741 23.125  1.00 8.08  ? 112 LYS A O    1 
ATOM   1018 C  CB   . LYS A 1 112 ? -10.575 -17.063 24.106  1.00 9.58  ? 112 LYS A CB   1 
ATOM   1019 C  CG   . LYS A 1 112 ? -11.224 -17.376 22.742  1.00 11.38 ? 112 LYS A CG   1 
ATOM   1020 C  CD   . LYS A 1 112 ? -12.776 -17.302 22.853  1.00 12.74 ? 112 LYS A CD   1 
ATOM   1021 C  CE   . LYS A 1 112 ? -13.351 -17.593 21.477  1.00 15.20 ? 112 LYS A CE   1 
ATOM   1022 N  NZ   . LYS A 1 112 ? -13.227 -18.916 21.051  1.00 14.53 ? 112 LYS A NZ   1 
ATOM   1023 N  N    . LYS A 1 113 ? -8.170  -16.375 21.805  1.00 8.14  ? 113 LYS A N    1 
ATOM   1024 C  CA   . LYS A 1 113 ? -7.940  -15.584 20.621  1.00 7.50  ? 113 LYS A CA   1 
ATOM   1025 C  C    . LYS A 1 113 ? -9.072  -15.816 19.576  1.00 8.20  ? 113 LYS A C    1 
ATOM   1026 O  O    . LYS A 1 113 ? -9.388  -16.942 19.207  1.00 10.01 ? 113 LYS A O    1 
ATOM   1027 C  CB   . LYS A 1 113 ? -6.651  -15.997 19.943  1.00 8.10  ? 113 LYS A CB   1 
ATOM   1028 C  CG   . LYS A 1 113 ? -5.439  -15.746 20.760  1.00 10.88 ? 113 LYS A CG   1 
ATOM   1029 C  CD   . LYS A 1 113 ? -4.209  -16.323 20.123  1.00 12.36 ? 113 LYS A CD   1 
ATOM   1030 C  CE   . LYS A 1 113 ? -2.983  -15.560 20.601  1.00 13.35 ? 113 LYS A CE   1 
ATOM   1031 N  NZ   . LYS A 1 113 ? -1.890  -16.442 21.091  1.00 23.31 ? 113 LYS A NZ   1 
ATOM   1032 N  N    . TYR A 1 114 ? -9.714  -14.741 19.143  1.00 7.21  ? 114 TYR A N    1 
ATOM   1033 C  CA   . TYR A 1 114 ? -10.698 -14.815 18.090  1.00 7.25  ? 114 TYR A CA   1 
ATOM   1034 C  C    . TYR A 1 114 ? -10.088 -14.778 16.719  1.00 6.79  ? 114 TYR A C    1 
ATOM   1035 O  O    . TYR A 1 114 ? -8.829  -14.468 16.615  1.00 7.69  ? 114 TYR A O    1 
ATOM   1036 C  CB   . TYR A 1 114 ? -11.771 -13.682 18.190  1.00 7.90  ? 114 TYR A CB   1 
ATOM   1037 C  CG   . TYR A 1 114 ? -12.688 -13.931 19.341  1.00 8.08  ? 114 TYR A CG   1 
ATOM   1038 C  CD1  . TYR A 1 114 ? -12.417 -13.519 20.666  1.00 9.26  ? 114 TYR A CD1  1 
ATOM   1039 C  CD2  . TYR A 1 114 ? -13.917 -14.542 19.099  1.00 8.99  ? 114 TYR A CD2  1 
ATOM   1040 C  CE1  . TYR A 1 114 ? -13.293 -13.679 21.698  1.00 10.94 ? 114 TYR A CE1  1 
ATOM   1041 C  CE2  . TYR A 1 114 ? -14.847 -14.695 20.129  1.00 9.69  ? 114 TYR A CE2  1 
ATOM   1042 C  CZ   . TYR A 1 114 ? -14.491 -14.319 21.421  1.00 10.81 ? 114 TYR A CZ   1 
ATOM   1043 O  OH   . TYR A 1 114 ? -15.398 -14.408 22.484  1.00 16.51 ? 114 TYR A OH   1 
ATOM   1044 N  N    . ALA A 1 115 ? -10.764 -15.036 15.664  1.00 7.16  ? 115 ALA A N    1 
ATOM   1045 C  CA   . ALA A 1 115 ? -10.282 -15.044 14.315  1.00 6.74  ? 115 ALA A CA   1 
ATOM   1046 C  C    . ALA A 1 115 ? -9.823  -13.679 13.798  1.00 7.40  ? 115 ALA A C    1 
ATOM   1047 O  O    . ALA A 1 115 ? -9.011  -13.536 12.940  1.00 7.88  ? 115 ALA A O    1 
ATOM   1048 C  CB   . ALA A 1 115 ? -11.287 -15.668 13.340  1.00 8.72  ? 115 ALA A CB   1 
ATOM   1049 N  N    . ALA A 1 116 ? -10.523 -12.640 14.358  1.00 7.38  ? 116 ALA A N    1 
ATOM   1050 C  CA   . ALA A 1 116 ? -10.213 -11.316 13.909  1.00 7.34  ? 116 ALA A CA   1 
ATOM   1051 C  C    . ALA A 1 116 ? -10.826 -10.375 14.924  1.00 6.32  ? 116 ALA A C    1 
ATOM   1052 O  O    . ALA A 1 116 ? -11.557 -10.749 15.823  1.00 6.64  ? 116 ALA A O    1 
ATOM   1053 C  CB   . ALA A 1 116 ? -10.716 -10.987 12.526  1.00 8.76  ? 116 ALA A CB   1 
ATOM   1054 N  N    . GLU A 1 117 ? -10.437 -9.091  14.736  1.00 6.26  ? 117 GLU A N    1 
ATOM   1055 C  CA   . GLU A 1 117 ? -11.041 -8.006  15.637  1.00 6.86  ? 117 GLU A CA   1 
ATOM   1056 C  C    . GLU A 1 117 ? -11.234 -6.745  14.833  1.00 6.48  ? 117 GLU A C    1 
ATOM   1057 O  O    . GLU A 1 117 ? -10.317 -6.363  14.069  1.00 7.95  ? 117 GLU A O    1 
ATOM   1058 C  CB   . GLU A 1 117 ? -9.965  -7.747  16.759  1.00 8.10  ? 117 GLU A CB   1 
ATOM   1059 C  CG   . GLU A 1 117 ? -10.542 -6.801  17.828  1.00 7.46  ? 117 GLU A CG   1 
ATOM   1060 C  CD   . GLU A 1 117 ? -9.622  -6.736  19.067  1.00 7.12  ? 117 GLU A CD   1 
ATOM   1061 O  OE1  . GLU A 1 117 ? -8.960  -7.787  19.382  1.00 7.61  ? 117 GLU A OE1  1 
ATOM   1062 O  OE2  . GLU A 1 117 ? -9.618  -5.717  19.745  1.00 7.36  ? 117 GLU A OE2  1 
ATOM   1063 N  N    . LEU A 1 118 ? -12.432 -6.192  14.951  1.00 7.13  ? 118 LEU A N    1 
ATOM   1064 C  CA   . LEU A 1 118 ? -12.717 -4.916  14.273  1.00 7.77  ? 118 LEU A CA   1 
ATOM   1065 C  C    . LEU A 1 118 ? -12.533 -3.761  15.278  1.00 6.92  ? 118 LEU A C    1 
ATOM   1066 O  O    . LEU A 1 118 ? -12.915 -3.842  16.437  1.00 7.01  ? 118 LEU A O    1 
ATOM   1067 C  CB   . LEU A 1 118 ? -14.222 -4.990  13.914  1.00 7.60  ? 118 LEU A CB   1 
ATOM   1068 C  CG   . LEU A 1 118 ? -15.033 -3.671  13.575  1.00 7.37  ? 118 LEU A CG   1 
ATOM   1069 C  CD1  . LEU A 1 118 ? -14.473 -3.064  12.315  1.00 9.90  ? 118 LEU A CD1  1 
ATOM   1070 C  CD2  . LEU A 1 118 ? -16.468 -4.097  13.274  1.00 8.99  ? 118 LEU A CD2  1 
ATOM   1071 N  N    . HIS A 1 119 ? -11.830 -2.688  14.756  1.00 6.73  ? 119 HIS A N    1 
ATOM   1072 C  CA   . HIS A 1 119 ? -11.627 -1.472  15.553  1.00 6.41  ? 119 HIS A CA   1 
ATOM   1073 C  C    . HIS A 1 119 ? -12.334 -0.291  14.891  1.00 6.41  ? 119 HIS A C    1 
ATOM   1074 O  O    . HIS A 1 119 ? -11.985 0.024   13.746  1.00 8.45  ? 119 HIS A O    1 
ATOM   1075 C  CB   . HIS A 1 119 ? -10.172 -1.131  15.623  1.00 6.16  ? 119 HIS A CB   1 
ATOM   1076 C  CG   . HIS A 1 119 ? -9.488  -2.173  16.507  1.00 7.09  ? 119 HIS A CG   1 
ATOM   1077 N  ND1  . HIS A 1 119 ? -8.124  -2.463  16.477  1.00 6.88  ? 119 HIS A ND1  1 
ATOM   1078 C  CD2  . HIS A 1 119 ? -10.018 -3.060  17.402  1.00 5.91  ? 119 HIS A CD2  1 
ATOM   1079 C  CE1  . HIS A 1 119 ? -7.782  -3.259  17.386  1.00 7.20  ? 119 HIS A CE1  1 
ATOM   1080 N  NE2  . HIS A 1 119 ? -8.931  -3.758  17.914  1.00 6.65  ? 119 HIS A NE2  1 
ATOM   1081 N  N    . LEU A 1 120 ? -13.341 0.266   15.554  1.00 6.84  ? 120 LEU A N    1 
ATOM   1082 C  CA   . LEU A 1 120 ? -14.044 1.514   15.075  1.00 6.95  ? 120 LEU A CA   1 
ATOM   1083 C  C    . LEU A 1 120 ? -13.432 2.635   15.869  1.00 6.49  ? 120 LEU A C    1 
ATOM   1084 O  O    . LEU A 1 120 ? -13.541 2.677   17.083  1.00 6.11  ? 120 LEU A O    1 
ATOM   1085 C  CB   . LEU A 1 120 ? -15.520 1.376   15.297  1.00 7.41  ? 120 LEU A CB   1 
ATOM   1086 C  CG   . LEU A 1 120 ? -16.214 0.278   14.460  1.00 8.66  ? 120 LEU A CG   1 
ATOM   1087 C  CD1  . LEU A 1 120 ? -17.215 -0.585  15.258  1.00 11.28 ? 120 LEU A CD1  1 
ATOM   1088 C  CD2  . LEU A 1 120 ? -16.997 0.991   13.339  1.00 11.00 ? 120 LEU A CD2  1 
ATOM   1089 N  N    . VAL A 1 121 ? -12.683 3.490   15.168  1.00 6.72  ? 121 VAL A N    1 
ATOM   1090 C  CA   . VAL A 1 121 ? -11.856 4.542   15.833  1.00 7.01  ? 121 VAL A CA   1 
ATOM   1091 C  C    . VAL A 1 121 ? -12.554 5.891   15.819  1.00 7.29  ? 121 VAL A C    1 
ATOM   1092 O  O    . VAL A 1 121 ? -12.996 6.313   14.755  1.00 7.50  ? 121 VAL A O    1 
ATOM   1093 C  CB   . VAL A 1 121 ? -10.554 4.627   15.006  1.00 7.92  ? 121 VAL A CB   1 
ATOM   1094 C  CG1  . VAL A 1 121 ? -9.591  5.709   15.602  1.00 9.35  ? 121 VAL A CG1  1 
ATOM   1095 C  CG2  . VAL A 1 121 ? -9.861  3.248   14.911  1.00 8.94  ? 121 VAL A CG2  1 
ATOM   1096 N  N    . HIS A 1 122 ? -12.613 6.466   17.017  1.00 6.41  ? 122 HIS A N    1 
ATOM   1097 C  CA   . HIS A 1 122 ? -13.343 7.717   17.179  1.00 7.24  ? 122 HIS A CA   1 
ATOM   1098 C  C    . HIS A 1 122 ? -12.380 8.692   17.938  1.00 8.19  ? 122 HIS A C    1 
ATOM   1099 O  O    . HIS A 1 122 ? -11.659 8.305   18.841  1.00 7.57  ? 122 HIS A O    1 
ATOM   1100 C  CB   . HIS A 1 122 ? -14.599 7.579   18.066  1.00 8.50  ? 122 HIS A CB   1 
ATOM   1101 C  CG   . HIS A 1 122 ? -15.494 6.434   17.632  1.00 7.95  ? 122 HIS A CG   1 
ATOM   1102 N  ND1  . HIS A 1 122 ? -15.130 5.131   17.875  1.00 7.39  ? 122 HIS A ND1  1 
ATOM   1103 C  CD2  . HIS A 1 122 ? -16.651 6.379   17.002  1.00 8.74  ? 122 HIS A CD2  1 
ATOM   1104 C  CE1  . HIS A 1 122 ? -16.088 4.326   17.404  1.00 8.61  ? 122 HIS A CE1  1 
ATOM   1105 N  NE2  . HIS A 1 122 ? -17.068 5.056   16.927  1.00 8.19  ? 122 HIS A NE2  1 
ATOM   1106 N  N    . TRP A 1 123 ? -12.476 9.957   17.576  1.00 6.92  ? 123 TRP A N    1 
ATOM   1107 C  CA   . TRP A 1 123 ? -11.693 10.962  18.267  1.00 7.56  ? 123 TRP A CA   1 
ATOM   1108 C  C    . TRP A 1 123 ? -12.616 11.971  19.017  1.00 6.91  ? 123 TRP A C    1 
ATOM   1109 O  O    . TRP A 1 123 ? -13.741 12.333  18.639  1.00 8.13  ? 123 TRP A O    1 
ATOM   1110 C  CB   . TRP A 1 123 ? -10.760 11.769  17.335  1.00 7.66  ? 123 TRP A CB   1 
ATOM   1111 C  CG   . TRP A 1 123 ? -11.395 12.368  16.104  1.00 9.32  ? 123 TRP A CG   1 
ATOM   1112 C  CD1  . TRP A 1 123 ? -11.595 11.761  14.904  1.00 10.90 ? 123 TRP A CD1  1 
ATOM   1113 C  CD2  . TRP A 1 123 ? -11.985 13.679  16.006  1.00 10.04 ? 123 TRP A CD2  1 
ATOM   1114 N  NE1  . TRP A 1 123 ? -12.287 12.574  14.057  1.00 11.33 ? 123 TRP A NE1  1 
ATOM   1115 C  CE2  . TRP A 1 123 ? -12.496 13.809  14.674  1.00 11.95 ? 123 TRP A CE2  1 
ATOM   1116 C  CE3  . TRP A 1 123 ? -11.995 14.816  16.847  1.00 10.12 ? 123 TRP A CE3  1 
ATOM   1117 C  CZ2  . TRP A 1 123 ? -13.179 14.964  14.196  1.00 11.66 ? 123 TRP A CZ2  1 
ATOM   1118 C  CZ3  . TRP A 1 123 ? -12.650 15.980  16.353  1.00 12.64 ? 123 TRP A CZ3  1 
ATOM   1119 C  CH2  . TRP A 1 123 ? -13.175 16.048  15.013  1.00 11.69 ? 123 TRP A CH2  1 
ATOM   1120 N  N    . ASN A 1 124 ? -12.026 12.429  20.135  1.00 8.22  ? 124 ASN A N    1 
ATOM   1121 C  CA   . ASN A 1 124 ? -12.784 13.306  21.047  1.00 8.75  ? 124 ASN A CA   1 
ATOM   1122 C  C    . ASN A 1 124 ? -12.960 14.663  20.483  1.00 8.98  ? 124 ASN A C    1 
ATOM   1123 O  O    . ASN A 1 124 ? -11.948 15.372  20.193  1.00 8.70  ? 124 ASN A O    1 
ATOM   1124 C  CB   . ASN A 1 124 ? -12.006 13.383  22.365  1.00 8.63  ? 124 ASN A CB   1 
ATOM   1125 C  CG   . ASN A 1 124 ? -12.758 13.967  23.488  1.00 8.48  ? 124 ASN A CG   1 
ATOM   1126 O  OD1  . ASN A 1 124 ? -13.599 14.874  23.269  1.00 10.05 ? 124 ASN A OD1  1 
ATOM   1127 N  ND2  . ASN A 1 124 ? -12.481 13.536  24.748  1.00 9.62  ? 124 ASN A ND2  1 
ATOM   1128 N  N    . THR A 1 125 ? -14.212 15.103  20.268  1.00 9.10  ? 125 THR A N    1 
ATOM   1129 C  CA   . THR A 1 125 ? -14.454 16.412  19.606  1.00 9.88  ? 125 THR A CA   1 
ATOM   1130 C  C    . THR A 1 125 ? -13.839 17.601  20.319  1.00 11.39 ? 125 THR A C    1 
ATOM   1131 O  O    . THR A 1 125 ? -13.715 18.662  19.728  1.00 12.29 ? 125 THR A O    1 
ATOM   1132 C  CB   . THR A 1 125 ? -15.951 16.616  19.280  1.00 13.19 ? 125 THR A CB   1 
ATOM   1133 O  OG1  . THR A 1 125 ? -16.708 16.525  20.471  1.00 15.30 ? 125 THR A OG1  1 
ATOM   1134 C  CG2  . THR A 1 125 ? -16.349 15.458  18.217  1.00 14.86 ? 125 THR A CG2  1 
ATOM   1135 N  N    . LYS A 1 126 ? -13.593 17.427  21.693  1.00 10.69 ? 127 LYS A N    1 
ATOM   1136 C  CA   . LYS A 1 126 ? -12.969 18.541  22.381  1.00 11.15 ? 127 LYS A CA   1 
ATOM   1137 C  C    . LYS A 1 126 ? -11.613 18.932  21.861  1.00 10.29 ? 127 LYS A C    1 
ATOM   1138 O  O    . LYS A 1 126 ? -11.100 19.984  22.173  1.00 12.83 ? 127 LYS A O    1 
ATOM   1139 C  CB   . LYS A 1 126 ? -13.037 18.330  23.908  1.00 13.06 ? 127 LYS A CB   1 
ATOM   1140 C  CG   . LYS A 1 126 ? -12.013 17.472  24.478  1.00 12.40 ? 127 LYS A CG   1 
ATOM   1141 C  CD   . LYS A 1 126 ? -12.401 17.194  25.918  1.00 20.85 ? 127 LYS A CD   1 
ATOM   1142 C  CE   . LYS A 1 126 ? -11.408 16.443  26.558  1.00 28.77 ? 127 LYS A CE   1 
ATOM   1143 N  NZ   . LYS A 1 126 ? -11.925 16.116  27.949  1.00 33.94 ? 127 LYS A NZ   1 
ATOM   1144 N  N    . TYR A 1 127 ? -10.975 18.034  21.080  1.00 10.06 ? 128 TYR A N    1 
ATOM   1145 C  CA   . TYR A 1 127 ? -9.619  18.342  20.572  1.00 9.64  ? 128 TYR A CA   1 
ATOM   1146 C  C    . TYR A 1 127 ? -9.595  18.666  19.080  1.00 10.15 ? 128 TYR A C    1 
ATOM   1147 O  O    . TYR A 1 127 ? -8.549  18.961  18.486  1.00 11.25 ? 128 TYR A O    1 
ATOM   1148 C  CB   . TYR A 1 127 ? -8.630  17.212  20.838  1.00 9.76  ? 128 TYR A CB   1 
ATOM   1149 C  CG   . TYR A 1 127 ? -8.550  16.915  22.270  1.00 8.51  ? 128 TYR A CG   1 
ATOM   1150 C  CD1  . TYR A 1 127 ? -8.175  17.902  23.211  1.00 11.04 ? 128 TYR A CD1  1 
ATOM   1151 C  CD2  . TYR A 1 127 ? -8.862  15.626  22.783  1.00 8.14  ? 128 TYR A CD2  1 
ATOM   1152 C  CE1  . TYR A 1 127 ? -8.124  17.614  24.611  1.00 10.81 ? 128 TYR A CE1  1 
ATOM   1153 C  CE2  . TYR A 1 127 ? -8.786  15.369  24.128  1.00 9.19  ? 128 TYR A CE2  1 
ATOM   1154 C  CZ   . TYR A 1 127 ? -8.380  16.349  25.010  1.00 9.88  ? 128 TYR A CZ   1 
ATOM   1155 O  OH   . TYR A 1 127 ? -8.364  16.121  26.345  1.00 12.65 ? 128 TYR A OH   1 
ATOM   1156 N  N    . GLY A 1 128 ? -10.804 18.833  18.493  1.00 9.33  ? 129 GLY A N    1 
ATOM   1157 C  CA   . GLY A 1 128 ? -10.913 19.392  17.169  1.00 9.67  ? 129 GLY A CA   1 
ATOM   1158 C  C    . GLY A 1 128 ? -10.562 18.560  15.989  1.00 9.52  ? 129 GLY A C    1 
ATOM   1159 O  O    . GLY A 1 128 ? -11.202 18.698  14.888  1.00 11.99 ? 129 GLY A O    1 
ATOM   1160 N  N    . ASP A 1 129 ? -9.519  17.706  16.081  1.00 11.26 ? 130 ASP A N    1 
ATOM   1161 C  CA   . ASP A 1 129 ? -9.284  16.759  15.002  1.00 12.04 ? 130 ASP A CA   1 
ATOM   1162 C  C    . ASP A 1 129 ? -8.536  15.585  15.550  1.00 12.26 ? 130 ASP A C    1 
ATOM   1163 O  O    . ASP A 1 129 ? -8.060  15.603  16.710  1.00 12.16 ? 130 ASP A O    1 
ATOM   1164 C  CB   . ASP A 1 129 ? -8.611  17.350  13.750  1.00 12.51 ? 130 ASP A CB   1 
ATOM   1165 C  CG   . ASP A 1 129 ? -7.271  17.861  13.971  1.00 11.91 ? 130 ASP A CG   1 
ATOM   1166 O  OD1  . ASP A 1 129 ? -6.592  17.579  15.016  1.00 18.86 ? 130 ASP A OD1  1 
ATOM   1167 O  OD2  . ASP A 1 129 ? -6.733  18.604  13.140  1.00 17.24 ? 130 ASP A OD2  1 
ATOM   1168 N  N    . PHE A 1 130 ? -8.411  14.564  14.707  1.00 12.15 ? 131 PHE A N    1 
ATOM   1169 C  CA   . PHE A 1 130 ? -7.744  13.293  15.138  1.00 12.79 ? 131 PHE A CA   1 
ATOM   1170 C  C    . PHE A 1 130 ? -6.243  13.555  15.476  1.00 11.21 ? 131 PHE A C    1 
ATOM   1171 O  O    . PHE A 1 130 ? -5.704  13.055  16.467  1.00 10.70 ? 131 PHE A O    1 
ATOM   1172 C  CB   . PHE A 1 130 ? -7.789  12.297  13.963  1.00 11.35 ? 131 PHE A CB   1 
ATOM   1173 C  CG   . PHE A 1 130 ? -7.097  11.046  14.200  1.00 9.55  ? 131 PHE A CG   1 
ATOM   1174 C  CD1  . PHE A 1 130 ? -7.717  9.961   14.883  1.00 9.05  ? 131 PHE A CD1  1 
ATOM   1175 C  CD2  . PHE A 1 130 ? -5.732  10.849  13.890  1.00 11.04 ? 131 PHE A CD2  1 
ATOM   1176 C  CE1  . PHE A 1 130 ? -7.005  8.747   15.097  1.00 10.29 ? 131 PHE A CE1  1 
ATOM   1177 C  CE2  . PHE A 1 130 ? -5.030  9.658   14.067  1.00 12.75 ? 131 PHE A CE2  1 
ATOM   1178 C  CZ   . PHE A 1 130 ? -5.719  8.573   14.686  1.00 10.30 ? 131 PHE A CZ   1 
ATOM   1179 N  N    . GLY A 1 131 ? -5.535  14.407  14.658  1.00 11.78 ? 132 GLY A N    1 
ATOM   1180 C  CA   . GLY A 1 131 ? -4.106  14.527  14.954  1.00 12.14 ? 132 GLY A CA   1 
ATOM   1181 C  C    . GLY A 1 131 ? -3.843  15.178  16.279  1.00 12.40 ? 132 GLY A C    1 
ATOM   1182 O  O    . GLY A 1 131 ? -2.824  14.880  16.936  1.00 12.98 ? 132 GLY A O    1 
ATOM   1183 N  N    . LYS A 1 132 ? -4.668  16.145  16.652  1.00 11.10 ? 133 LYS A N    1 
ATOM   1184 C  CA   . LYS A 1 132 ? -4.499  16.711  18.014  1.00 10.65 ? 133 LYS A CA   1 
ATOM   1185 C  C    . LYS A 1 132 ? -4.998  15.754  19.099  1.00 10.30 ? 133 LYS A C    1 
ATOM   1186 O  O    . LYS A 1 132 ? -4.439  15.684  20.228  1.00 10.14 ? 133 LYS A O    1 
ATOM   1187 C  CB   . LYS A 1 132 ? -5.280  18.024  18.149  1.00 10.95 ? 133 LYS A CB   1 
ATOM   1188 C  CG   . LYS A 1 132 ? -4.586  19.100  17.327  1.00 15.96 ? 133 LYS A CG   1 
ATOM   1189 C  CD   . LYS A 1 132 ? -3.187  19.508  17.876  1.00 20.47 ? 133 LYS A CD   1 
ATOM   1190 C  CE   . LYS A 1 132 ? -2.712  20.857  17.511  1.00 22.19 ? 133 LYS A CE   1 
ATOM   1191 N  NZ   . LYS A 1 132 ? -1.792  21.323  18.716  1.00 36.26 ? 133 LYS A NZ   1 
ATOM   1192 N  N    . ALA A 1 133 ? -6.083  15.001  18.813  1.00 8.85  ? 134 ALA A N    1 
ATOM   1193 C  CA   . ALA A 1 133 ? -6.648  14.098  19.832  1.00 8.90  ? 134 ALA A CA   1 
ATOM   1194 C  C    . ALA A 1 133 ? -5.607  13.027  20.245  1.00 8.91  ? 134 ALA A C    1 
ATOM   1195 O  O    . ALA A 1 133 ? -5.568  12.678  21.440  1.00 8.44  ? 134 ALA A O    1 
ATOM   1196 C  CB   . ALA A 1 133 ? -7.887  13.421  19.249  1.00 9.15  ? 134 ALA A CB   1 
ATOM   1197 N  N    . VAL A 1 134 ? -4.859  12.494  19.286  1.00 8.85  ? 135 VAL A N    1 
ATOM   1198 C  CA   . VAL A 1 134 ? -3.926  11.412  19.698  1.00 10.42 ? 135 VAL A CA   1 
ATOM   1199 C  C    . VAL A 1 134 ? -2.793  11.845  20.632  1.00 9.57  ? 135 VAL A C    1 
ATOM   1200 O  O    . VAL A 1 134 ? -2.075  11.026  21.184  1.00 10.03 ? 135 VAL A O    1 
ATOM   1201 C  CB   . VAL A 1 134 ? -3.304  10.664  18.487  1.00 10.96 ? 135 VAL A CB   1 
ATOM   1202 C  CG1  . VAL A 1 134 ? -4.398  9.982   17.694  1.00 12.45 ? 135 VAL A CG1  1 
ATOM   1203 C  CG2  . VAL A 1 134 ? -2.456  11.613  17.625  1.00 10.08 ? 135 VAL A CG2  1 
ATOM   1204 N  N    A GLN A 1 135 ? -2.671  13.177  20.811  0.50 9.84  ? 136 GLN A N    1 
ATOM   1205 N  N    B GLN A 1 135 ? -2.724  13.186  20.818  0.50 9.60  ? 136 GLN A N    1 
ATOM   1206 C  CA   A GLN A 1 135 ? -1.625  13.637  21.762  0.50 10.91 ? 136 GLN A CA   1 
ATOM   1207 C  CA   B GLN A 1 135 ? -1.706  13.782  21.744  0.50 10.56 ? 136 GLN A CA   1 
ATOM   1208 C  C    A GLN A 1 135 ? -2.238  13.878  23.166  0.50 10.59 ? 136 GLN A C    1 
ATOM   1209 C  C    B GLN A 1 135 ? -2.222  13.752  23.215  0.50 10.34 ? 136 GLN A C    1 
ATOM   1210 O  O    A GLN A 1 135 ? -1.612  14.583  24.011  0.50 12.50 ? 136 GLN A O    1 
ATOM   1211 O  O    B GLN A 1 135 ? -1.543  14.089  24.173  0.50 12.23 ? 136 GLN A O    1 
ATOM   1212 C  CB   A GLN A 1 135 ? -0.949  14.909  21.249  0.50 10.47 ? 136 GLN A CB   1 
ATOM   1213 C  CB   B GLN A 1 135 ? -1.323  15.199  21.235  0.50 11.43 ? 136 GLN A CB   1 
ATOM   1214 C  CG   A GLN A 1 135 ? -0.215  14.691  19.981  0.50 12.25 ? 136 GLN A CG   1 
ATOM   1215 C  CG   B GLN A 1 135 ? -0.824  15.013  19.783  0.50 11.65 ? 136 GLN A CG   1 
ATOM   1216 C  CD   A GLN A 1 135 ? 1.131   13.977  20.252  0.50 18.32 ? 136 GLN A CD   1 
ATOM   1217 C  CD   B GLN A 1 135 ? -0.064  16.188  19.288  0.50 15.58 ? 136 GLN A CD   1 
ATOM   1218 O  OE1  A GLN A 1 135 ? 1.685   14.046  21.352  0.50 24.23 ? 136 GLN A OE1  1 
ATOM   1219 O  OE1  B GLN A 1 135 ? 0.802   16.774  19.975  0.50 16.64 ? 136 GLN A OE1  1 
ATOM   1220 N  NE2  A GLN A 1 135 ? 1.625   13.182  19.235  0.50 23.31 ? 136 GLN A NE2  1 
ATOM   1221 N  NE2  B GLN A 1 135 ? -0.419  16.575  18.058  0.50 16.19 ? 136 GLN A NE2  1 
ATOM   1222 N  N    . GLN A 1 136 ? -3.471  13.374  23.434  1.00 9.64  ? 137 GLN A N    1 
ATOM   1223 C  CA   . GLN A 1 136 ? -4.135  13.544  24.700  1.00 10.08 ? 137 GLN A CA   1 
ATOM   1224 C  C    . GLN A 1 136 ? -4.496  12.200  25.294  1.00 9.59  ? 137 GLN A C    1 
ATOM   1225 O  O    . GLN A 1 136 ? -4.864  11.280  24.569  1.00 9.65  ? 137 GLN A O    1 
ATOM   1226 C  CB   . GLN A 1 136 ? -5.439  14.360  24.529  1.00 10.05 ? 137 GLN A CB   1 
ATOM   1227 C  CG   . GLN A 1 136 ? -5.161  15.690  23.767  1.00 12.58 ? 137 GLN A CG   1 
ATOM   1228 C  CD   . GLN A 1 136 ? -4.266  16.623  24.541  1.00 12.71 ? 137 GLN A CD   1 
ATOM   1229 O  OE1  . GLN A 1 136 ? -4.111  16.486  25.743  1.00 17.93 ? 137 GLN A OE1  1 
ATOM   1230 N  NE2  . GLN A 1 136 ? -3.564  17.530  23.816  1.00 23.60 ? 137 GLN A NE2  1 
ATOM   1231 N  N    . PRO A 1 137 ? -4.494  12.076  26.647  1.00 9.32  ? 138 PRO A N    1 
ATOM   1232 C  CA   . PRO A 1 137 ? -4.786  10.785  27.266  1.00 9.02  ? 138 PRO A CA   1 
ATOM   1233 C  C    . PRO A 1 137 ? -6.200  10.348  27.055  1.00 8.92  ? 138 PRO A C    1 
ATOM   1234 O  O    . PRO A 1 137 ? -6.478  9.131   27.210  1.00 11.39 ? 138 PRO A O    1 
ATOM   1235 C  CB   . PRO A 1 137 ? -4.503  10.964  28.754  1.00 11.44 ? 138 PRO A CB   1 
ATOM   1236 C  CG   . PRO A 1 137 ? -4.356  12.370  28.924  1.00 17.16 ? 138 PRO A CG   1 
ATOM   1237 C  CD   . PRO A 1 137 ? -4.019  13.107  27.596  1.00 11.69 ? 138 PRO A CD   1 
ATOM   1238 N  N    . ASP A 1 138 ? -7.166  11.244  26.743  1.00 8.57  ? 139 ASP A N    1 
ATOM   1239 C  CA   . ASP A 1 138 ? -8.547  10.896  26.523  1.00 8.95  ? 139 ASP A CA   1 
ATOM   1240 C  C    . ASP A 1 138 ? -8.893  11.279  25.069  1.00 8.41  ? 139 ASP A C    1 
ATOM   1241 O  O    . ASP A 1 138 ? -10.013 11.687  24.815  1.00 8.95  ? 139 ASP A O    1 
ATOM   1242 C  CB   . ASP A 1 138 ? -9.512  11.536  27.517  1.00 9.95  ? 139 ASP A CB   1 
ATOM   1243 C  CG   . ASP A 1 138 ? -9.403  13.036  27.543  1.00 10.76 ? 139 ASP A CG   1 
ATOM   1244 O  OD1  . ASP A 1 138 ? -8.451  13.589  26.954  1.00 11.75 ? 139 ASP A OD1  1 
ATOM   1245 O  OD2  . ASP A 1 138 ? -10.278 13.652  28.175  1.00 15.36 ? 139 ASP A OD2  1 
ATOM   1246 N  N    . GLY A 1 139 ? -7.952  11.180  24.181  1.00 7.84  ? 140 GLY A N    1 
ATOM   1247 C  CA   . GLY A 1 139 ? -8.085  11.618  22.810  1.00 8.00  ? 140 GLY A CA   1 
ATOM   1248 C  C    . GLY A 1 139 ? -8.998  10.721  21.933  1.00 6.91  ? 140 GLY A C    1 
ATOM   1249 O  O    . GLY A 1 139 ? -9.720  11.232  21.082  1.00 7.94  ? 140 GLY A O    1 
ATOM   1250 N  N    . LEU A 1 140 ? -8.868  9.413   22.136  1.00 6.07  ? 141 LEU A N    1 
ATOM   1251 C  CA   . LEU A 1 140 ? -9.561  8.509   21.235  1.00 6.36  ? 141 LEU A CA   1 
ATOM   1252 C  C    . LEU A 1 140 ? -10.467 7.532   22.033  1.00 6.14  ? 141 LEU A C    1 
ATOM   1253 O  O    . LEU A 1 140 ? -10.162 7.250   23.223  1.00 7.19  ? 141 LEU A O    1 
ATOM   1254 C  CB   . LEU A 1 140 ? -8.571  7.608   20.467  1.00 7.36  ? 141 LEU A CB   1 
ATOM   1255 C  CG   . LEU A 1 140 ? -7.701  8.362   19.486  1.00 7.45  ? 141 LEU A CG   1 
ATOM   1256 C  CD1  . LEU A 1 140 ? -6.915  7.268   18.668  1.00 8.69  ? 141 LEU A CD1  1 
ATOM   1257 C  CD2  . LEU A 1 140 ? -8.371  9.335   18.563  1.00 7.94  ? 141 LEU A CD2  1 
ATOM   1258 N  N    . ALA A 1 141 ? -11.488 6.951   21.387  1.00 6.70  ? 142 ALA A N    1 
ATOM   1259 C  CA   . ALA A 1 141 ? -12.302 5.844   21.969  1.00 6.22  ? 142 ALA A CA   1 
ATOM   1260 C  C    . ALA A 1 141 ? -12.379 4.885   20.842  1.00 7.42  ? 142 ALA A C    1 
ATOM   1261 O  O    . ALA A 1 141 ? -12.729 5.241   19.696  1.00 7.79  ? 142 ALA A O    1 
ATOM   1262 C  CB   . ALA A 1 141 ? -13.680 6.373   22.393  1.00 7.86  ? 142 ALA A CB   1 
ATOM   1263 N  N    . VAL A 1 142 ? -11.878 3.665   21.093  1.00 7.36  ? 143 VAL A N    1 
ATOM   1264 C  CA   . VAL A 1 142 ? -12.025 2.640   20.097  1.00 7.53  ? 143 VAL A CA   1 
ATOM   1265 C  C    . VAL A 1 142 ? -13.000 1.538   20.557  1.00 6.59  ? 143 VAL A C    1 
ATOM   1266 O  O    . VAL A 1 142 ? -12.898 1.074   21.672  1.00 6.54  ? 143 VAL A O    1 
ATOM   1267 C  CB   . VAL A 1 142 ? -10.653 1.991   19.754  1.00 7.55  ? 143 VAL A CB   1 
ATOM   1268 C  CG1  . VAL A 1 142 ? -10.826 1.011   18.590  1.00 8.81  ? 143 VAL A CG1  1 
ATOM   1269 C  CG2  . VAL A 1 142 ? -9.720  3.090   19.288  1.00 9.28  ? 143 VAL A CG2  1 
ATOM   1270 N  N    . LEU A 1 143 ? -13.944 1.294   19.647  1.00 7.22  ? 144 LEU A N    1 
ATOM   1271 C  CA   . LEU A 1 143 ? -14.921 0.215   19.922  1.00 7.36  ? 144 LEU A CA   1 
ATOM   1272 C  C    . LEU A 1 143 ? -14.303 -1.028  19.196  1.00 7.21  ? 144 LEU A C    1 
ATOM   1273 O  O    . LEU A 1 143 ? -14.191 -1.055  17.986  1.00 7.64  ? 144 LEU A O    1 
ATOM   1274 C  CB   . LEU A 1 143 ? -16.292 0.627   19.316  1.00 8.27  ? 144 LEU A CB   1 
ATOM   1275 C  CG   . LEU A 1 143 ? -17.360 -0.378  19.479  1.00 9.26  ? 144 LEU A CG   1 
ATOM   1276 C  CD1  . LEU A 1 143 ? -17.635 -0.649  21.007  1.00 9.80  ? 144 LEU A CD1  1 
ATOM   1277 C  CD2  . LEU A 1 143 ? -18.708 0.254   18.863  1.00 10.70 ? 144 LEU A CD2  1 
ATOM   1278 N  N    . GLY A 1 144 ? -14.035 -2.028  20.044  1.00 6.79  ? 145 GLY A N    1 
ATOM   1279 C  CA   . GLY A 1 144 ? -13.470 -3.263  19.510  1.00 6.55  ? 145 GLY A CA   1 
ATOM   1280 C  C    . GLY A 1 144 ? -14.487 -4.388  19.562  1.00 6.62  ? 145 GLY A C    1 
ATOM   1281 O  O    . GLY A 1 144 ? -15.164 -4.512  20.524  1.00 7.68  ? 145 GLY A O    1 
ATOM   1282 N  N    . ILE A 1 145 ? -14.559 -5.080  18.407  1.00 6.43  ? 146 ILE A N    1 
ATOM   1283 C  CA   . ILE A 1 145 ? -15.591 -6.145  18.277  1.00 6.48  ? 146 ILE A CA   1 
ATOM   1284 C  C    . ILE A 1 145 ? -14.824 -7.368  17.782  1.00 7.02  ? 146 ILE A C    1 
ATOM   1285 O  O    . ILE A 1 145 ? -14.175 -7.344  16.756  1.00 7.28  ? 146 ILE A O    1 
ATOM   1286 C  CB   . ILE A 1 145 ? -16.659 -5.666  17.272  1.00 7.53  ? 146 ILE A CB   1 
ATOM   1287 C  CG1  . ILE A 1 145 ? -17.330 -4.335  17.822  1.00 8.92  ? 146 ILE A CG1  1 
ATOM   1288 C  CG2  . ILE A 1 145 ? -17.686 -6.791  17.037  1.00 8.99  ? 146 ILE A CG2  1 
ATOM   1289 C  CD1  . ILE A 1 145 ? -18.358 -3.771  16.868  1.00 8.51  ? 146 ILE A CD1  1 
ATOM   1290 N  N    . PHE A 1 146 ? -15.084 -8.516  18.429  1.00 6.23  ? 147 PHE A N    1 
ATOM   1291 C  CA   . PHE A 1 146 ? -14.385 -9.760  18.014  1.00 6.81  ? 147 PHE A CA   1 
ATOM   1292 C  C    . PHE A 1 146 ? -15.195 -10.360 16.810  1.00 7.57  ? 147 PHE A C    1 
ATOM   1293 O  O    . PHE A 1 146 ? -16.396 -10.252 16.753  1.00 7.47  ? 147 PHE A O    1 
ATOM   1294 C  CB   . PHE A 1 146 ? -14.423 -10.708 19.175  1.00 7.93  ? 147 PHE A CB   1 
ATOM   1295 C  CG   . PHE A 1 146 ? -13.576 -10.261 20.329  1.00 6.33  ? 147 PHE A CG   1 
ATOM   1296 C  CD1  . PHE A 1 146 ? -12.167 -10.088 20.152  1.00 7.44  ? 147 PHE A CD1  1 
ATOM   1297 C  CD2  . PHE A 1 146 ? -14.044 -10.112 21.548  1.00 7.24  ? 147 PHE A CD2  1 
ATOM   1298 C  CE1  . PHE A 1 146 ? -11.385 -9.737  21.209  1.00 7.31  ? 147 PHE A CE1  1 
ATOM   1299 C  CE2  . PHE A 1 146 ? -13.299 -9.648  22.629  1.00 7.03  ? 147 PHE A CE2  1 
ATOM   1300 C  CZ   . PHE A 1 146 ? -11.922 -9.503  22.462  1.00 6.18  ? 147 PHE A CZ   1 
ATOM   1301 N  N    . LEU A 1 147 ? -14.415 -11.110 15.970  1.00 7.80  ? 148 LEU A N    1 
ATOM   1302 C  CA   . LEU A 1 147 ? -15.068 -11.836 14.910  1.00 7.92  ? 148 LEU A CA   1 
ATOM   1303 C  C    . LEU A 1 147 ? -14.709 -13.320 15.108  1.00 7.52  ? 148 LEU A C    1 
ATOM   1304 O  O    . LEU A 1 147 ? -13.537 -13.697 15.297  1.00 8.12  ? 148 LEU A O    1 
ATOM   1305 C  CB   . LEU A 1 147 ? -14.404 -11.508 13.527  1.00 8.40  ? 148 LEU A CB   1 
ATOM   1306 C  CG   . LEU A 1 147 ? -14.978 -10.193 12.850  1.00 10.03 ? 148 LEU A CG   1 
ATOM   1307 C  CD1  . LEU A 1 147 ? -14.788 -8.936  13.745  1.00 10.49 ? 148 LEU A CD1  1 
ATOM   1308 C  CD2  . LEU A 1 147 ? -14.335 -10.028 11.512  1.00 10.27 ? 148 LEU A CD2  1 
ATOM   1309 N  N    . LYS A 1 148 ? -15.746 -14.179 15.044  1.00 7.69  ? 149 LYS A N    1 
ATOM   1310 C  CA   . LYS A 1 148 ? -15.523 -15.631 14.991  1.00 8.80  ? 149 LYS A CA   1 
ATOM   1311 C  C    . LYS A 1 148 ? -16.054 -16.130 13.635  1.00 8.59  ? 149 LYS A C    1 
ATOM   1312 O  O    . LYS A 1 148 ? -16.856 -15.488 13.030  1.00 9.23  ? 149 LYS A O    1 
ATOM   1313 C  CB   . LYS A 1 148 ? -16.286 -16.348 16.129  1.00 8.99  ? 149 LYS A CB   1 
ATOM   1314 C  CG   . LYS A 1 148 ? -17.772 -16.156 16.093  1.00 13.03 ? 149 LYS A CG   1 
ATOM   1315 C  CD   . LYS A 1 148 ? -18.473 -17.007 17.318  1.00 16.10 ? 149 LYS A CD   1 
ATOM   1316 C  CE   . LYS A 1 148 ? -19.935 -16.789 17.240  1.00 22.78 ? 149 LYS A CE   1 
ATOM   1317 N  NZ   . LYS A 1 148 ? -20.694 -17.878 18.037  1.00 30.98 ? 149 LYS A NZ   1 
ATOM   1318 N  N    . VAL A 1 149 ? -15.545 -17.277 13.197  1.00 9.24  ? 150 VAL A N    1 
ATOM   1319 C  CA   . VAL A 1 149 ? -15.915 -17.824 11.923  1.00 8.34  ? 150 VAL A CA   1 
ATOM   1320 C  C    . VAL A 1 149 ? -17.157 -18.768 12.129  1.00 10.13 ? 150 VAL A C    1 
ATOM   1321 O  O    . VAL A 1 149 ? -17.077 -19.749 12.890  1.00 10.94 ? 150 VAL A O    1 
ATOM   1322 C  CB   . VAL A 1 149 ? -14.727 -18.593 11.344  1.00 9.39  ? 150 VAL A CB   1 
ATOM   1323 C  CG1  . VAL A 1 149 ? -15.101 -19.344 10.055  1.00 10.87 ? 150 VAL A CG1  1 
ATOM   1324 C  CG2  . VAL A 1 149 ? -13.609 -17.620 11.027  1.00 11.59 ? 150 VAL A CG2  1 
ATOM   1325 N  N    . GLY A 1 150 ? -18.176 -18.520 11.363  1.00 8.97  ? 151 GLY A N    1 
ATOM   1326 C  CA   . GLY A 1 150 ? -19.437 -19.295 11.449  1.00 10.93 ? 151 GLY A CA   1 
ATOM   1327 C  C    . GLY A 1 150 ? -20.295 -18.841 10.281  1.00 10.32 ? 151 GLY A C    1 
ATOM   1328 O  O    . GLY A 1 150 ? -19.922 -18.931 9.126   1.00 11.56 ? 151 GLY A O    1 
ATOM   1329 N  N    A SER A 1 151 ? -21.510 -18.381 10.580  0.50 13.08 ? 152 SER A N    1 
ATOM   1330 N  N    B SER A 1 151 ? -21.432 -18.246 10.672  0.50 12.53 ? 152 SER A N    1 
ATOM   1331 C  CA   A SER A 1 151 ? -22.412 -17.859 9.517   0.50 12.67 ? 152 SER A CA   1 
ATOM   1332 C  CA   B SER A 1 151 ? -22.387 -17.639 9.702   0.50 11.14 ? 152 SER A CA   1 
ATOM   1333 C  C    A SER A 1 151 ? -21.839 -16.514 9.045   0.50 11.91 ? 152 SER A C    1 
ATOM   1334 C  C    B SER A 1 151 ? -21.717 -16.437 9.014   0.50 11.10 ? 152 SER A C    1 
ATOM   1335 O  O    A SER A 1 151 ? -21.225 -15.799 9.871   0.50 10.28 ? 152 SER A O    1 
ATOM   1336 O  O    B SER A 1 151 ? -20.871 -15.766 9.606   0.50 12.53 ? 152 SER A O    1 
ATOM   1337 C  CB   A SER A 1 151 ? -23.802 -17.637 10.063  0.50 16.04 ? 152 SER A CB   1 
ATOM   1338 C  CB   B SER A 1 151 ? -23.750 -17.304 10.315  0.50 12.85 ? 152 SER A CB   1 
ATOM   1339 O  OG   A SER A 1 151 ? -23.733 -16.669 11.095  0.50 17.15 ? 152 SER A OG   1 
ATOM   1340 O  OG   B SER A 1 151 ? -24.345 -18.485 10.805  0.50 14.69 ? 152 SER A OG   1 
ATOM   1341 N  N    . ALA A 1 152 ? -22.104 -16.185 7.763   1.00 10.52 ? 153 ALA A N    1 
ATOM   1342 C  CA   . ALA A 1 152 ? -21.681 -14.901 7.203   1.00 11.13 ? 153 ALA A CA   1 
ATOM   1343 C  C    . ALA A 1 152 ? -22.341 -13.677 7.905   1.00 10.66 ? 153 ALA A C    1 
ATOM   1344 O  O    . ALA A 1 152 ? -23.430 -13.739 8.430   1.00 14.07 ? 153 ALA A O    1 
ATOM   1345 C  CB   . ALA A 1 152 ? -21.978 -14.822 5.709   1.00 14.55 ? 153 ALA A CB   1 
ATOM   1346 N  N    A LYS A 1 153 ? -21.655 -12.516 7.982   0.50 10.78 ? 154 LYS A N    1 
ATOM   1347 N  N    B LYS A 1 153 ? -21.561 -12.555 7.732   0.50 11.18 ? 154 LYS A N    1 
ATOM   1348 C  CA   A LYS A 1 153 ? -22.321 -11.298 8.483   0.50 10.12 ? 154 LYS A CA   1 
ATOM   1349 C  CA   B LYS A 1 153 ? -22.021 -11.226 8.058   0.50 11.38 ? 154 LYS A CA   1 
ATOM   1350 C  C    A LYS A 1 153 ? -22.732 -10.553 7.218   0.50 8.60  ? 154 LYS A C    1 
ATOM   1351 C  C    B LYS A 1 153 ? -22.380 -10.499 6.747   0.50 10.61 ? 154 LYS A C    1 
ATOM   1352 O  O    A LYS A 1 153 ? -21.893 -10.044 6.457   0.50 9.56  ? 154 LYS A O    1 
ATOM   1353 O  O    B LYS A 1 153 ? -21.474 -10.025 6.019   0.50 10.73 ? 154 LYS A O    1 
ATOM   1354 C  CB   A LYS A 1 153 ? -21.261 -10.560 9.354   0.50 8.83  ? 154 LYS A CB   1 
ATOM   1355 C  CB   B LYS A 1 153 ? -20.885 -10.473 8.820   0.50 10.30 ? 154 LYS A CB   1 
ATOM   1356 C  CG   A LYS A 1 153 ? -21.887 -9.296  10.085  0.50 11.36 ? 154 LYS A CG   1 
ATOM   1357 C  CG   B LYS A 1 153 ? -21.377 -9.245  9.581   0.50 11.63 ? 154 LYS A CG   1 
ATOM   1358 C  CD   A LYS A 1 153 ? -22.929 -9.733  11.196  0.50 12.74 ? 154 LYS A CD   1 
ATOM   1359 C  CD   B LYS A 1 153 ? -22.112 -9.644  10.919  0.50 11.28 ? 154 LYS A CD   1 
ATOM   1360 C  CE   A LYS A 1 153 ? -23.306 -8.512  12.019  0.50 10.71 ? 154 LYS A CE   1 
ATOM   1361 C  CE   B LYS A 1 153 ? -22.215 -8.469  11.824  0.50 12.20 ? 154 LYS A CE   1 
ATOM   1362 N  NZ   A LYS A 1 153 ? -24.348 -8.799  12.981  0.50 15.63 ? 154 LYS A NZ   1 
ATOM   1363 N  NZ   B LYS A 1 153 ? -23.192 -8.789  12.867  0.50 12.89 ? 154 LYS A NZ   1 
ATOM   1364 N  N    A PRO A 1 154 ? -24.019 -10.453 6.958   0.50 8.56  ? 155 PRO A N    1 
ATOM   1365 N  N    B PRO A 1 154 ? -23.679 -10.449 6.420   0.50 10.47 ? 155 PRO A N    1 
ATOM   1366 C  CA   A PRO A 1 154 ? -24.468 -9.860  5.698   0.50 10.26 ? 155 PRO A CA   1 
ATOM   1367 C  CA   B PRO A 1 154 ? -24.000 -9.847  5.138   0.50 10.57 ? 155 PRO A CA   1 
ATOM   1368 C  C    A PRO A 1 154 ? -24.034 -8.391  5.526   0.50 7.86  ? 155 PRO A C    1 
ATOM   1369 C  C    B PRO A 1 154 ? -23.407 -8.403  5.019   0.50 11.36 ? 155 PRO A C    1 
ATOM   1370 O  O    A PRO A 1 154 ? -23.671 -7.983  4.407   0.50 9.27  ? 155 PRO A O    1 
ATOM   1371 O  O    B PRO A 1 154 ? -22.896 -8.043  3.982   0.50 11.10 ? 155 PRO A O    1 
ATOM   1372 C  CB   A PRO A 1 154 ? -25.997 -9.911  5.855   0.50 10.58 ? 155 PRO A CB   1 
ATOM   1373 C  CB   B PRO A 1 154 ? -25.548 -9.768  5.146   0.50 10.70 ? 155 PRO A CB   1 
ATOM   1374 C  CG   A PRO A 1 154 ? -26.249 -11.036 6.897   0.50 13.47 ? 155 PRO A CG   1 
ATOM   1375 C  CG   B PRO A 1 154 ? -25.925 -11.071 5.995   0.50 11.94 ? 155 PRO A CG   1 
ATOM   1376 C  CD   A PRO A 1 154 ? -25.144 -10.869 7.804   0.50 11.14 ? 155 PRO A CD   1 
ATOM   1377 C  CD   B PRO A 1 154 ? -24.888 -11.005 7.110   0.50 9.69  ? 155 PRO A CD   1 
ATOM   1378 N  N    A GLY A 1 155 ? -23.983 -7.703  6.659   0.50 8.17  ? 156 GLY A N    1 
ATOM   1379 N  N    B GLY A 1 155 ? -23.415 -7.652  6.130   0.50 9.65  ? 156 GLY A N    1 
ATOM   1380 C  CA   A GLY A 1 155 ? -23.530 -6.319  6.640   0.50 8.42  ? 156 GLY A CA   1 
ATOM   1381 C  CA   B GLY A 1 155 ? -22.996 -6.257  6.093   0.50 10.26 ? 156 GLY A CA   1 
ATOM   1382 C  C    A GLY A 1 155 ? -22.067 -6.111  6.455   0.50 8.10  ? 156 GLY A C    1 
ATOM   1383 C  C    B GLY A 1 155 ? -21.522 -6.075  5.881   0.50 11.01 ? 156 GLY A C    1 
ATOM   1384 O  O    A GLY A 1 155 ? -21.562 -4.986  6.285   0.50 9.20  ? 156 GLY A O    1 
ATOM   1385 O  O    B GLY A 1 155 ? -21.077 -4.928  5.581   0.50 11.91 ? 156 GLY A O    1 
ATOM   1386 N  N    A LEU A 1 156 ? -21.326 -7.186  6.449   0.50 7.35  ? 157 LEU A N    1 
ATOM   1387 N  N    B LEU A 1 156 ? -20.723 -7.123  5.980   0.50 9.05  ? 157 LEU A N    1 
ATOM   1388 C  CA   A LEU A 1 156 ? -19.918 -7.121  6.084   0.50 7.17  ? 157 LEU A CA   1 
ATOM   1389 C  CA   B LEU A 1 156 ? -19.248 -7.110  5.654   0.50 10.41 ? 157 LEU A CA   1 
ATOM   1390 C  C    A LEU A 1 156 ? -19.625 -7.375  4.589   0.50 6.68  ? 157 LEU A C    1 
ATOM   1391 C  C    B LEU A 1 156 ? -18.993 -7.334  4.157   0.50 10.52 ? 157 LEU A C    1 
ATOM   1392 O  O    A LEU A 1 156 ? -18.548 -7.000  4.095   0.50 7.57  ? 157 LEU A O    1 
ATOM   1393 O  O    B LEU A 1 156 ? -17.909 -7.044  3.687   0.50 10.22 ? 157 LEU A O    1 
ATOM   1394 C  CB   A LEU A 1 156 ? -19.106 -8.101  6.956   0.50 8.12  ? 157 LEU A CB   1 
ATOM   1395 C  CB   B LEU A 1 156 ? -18.485 -8.182  6.493   0.50 10.40 ? 157 LEU A CB   1 
ATOM   1396 C  CG   A LEU A 1 156 ? -17.580 -8.156  6.736   0.50 8.38  ? 157 LEU A CG   1 
ATOM   1397 C  CG   B LEU A 1 156 ? -16.982 -8.416  6.276   0.50 9.31  ? 157 LEU A CG   1 
ATOM   1398 C  CD1  A LEU A 1 156 ? -16.911 -6.798  7.083   0.50 7.78  ? 157 LEU A CD1  1 
ATOM   1399 C  CD1  B LEU A 1 156 ? -16.225 -7.200  6.820   0.50 11.00 ? 157 LEU A CD1  1 
ATOM   1400 C  CD2  A LEU A 1 156 ? -16.886 -9.318  7.542   0.50 9.30  ? 157 LEU A CD2  1 
ATOM   1401 C  CD2  B LEU A 1 156 ? -16.431 -9.579  7.005   0.50 10.98 ? 157 LEU A CD2  1 
ATOM   1402 N  N    A GLN A 1 157 ? -20.592 -7.849  3.809   0.50 7.18  ? 158 GLN A N    1 
ATOM   1403 N  N    B GLN A 1 157 ? -19.970 -7.867  3.414   0.50 10.86 ? 158 GLN A N    1 
ATOM   1404 C  CA   A GLN A 1 157 ? -20.254 -8.328  2.486   0.50 9.04  ? 158 GLN A CA   1 
ATOM   1405 C  CA   B GLN A 1 157 ? -19.608 -8.422  2.093   0.50 10.52 ? 158 GLN A CA   1 
ATOM   1406 C  C    A GLN A 1 157 ? -19.806 -7.207  1.587   0.50 8.51  ? 158 GLN A C    1 
ATOM   1407 C  C    B GLN A 1 157 ? -19.134 -7.240  1.186   0.50 12.21 ? 158 GLN A C    1 
ATOM   1408 O  O    A GLN A 1 157 ? -18.922 -7.410  0.739   0.50 7.88  ? 158 GLN A O    1 
ATOM   1409 O  O    B GLN A 1 157 ? -18.271 -7.454  0.340   0.50 12.14 ? 158 GLN A O    1 
ATOM   1410 C  CB   A GLN A 1 157 ? -21.453 -9.134  1.911   0.50 8.49  ? 158 GLN A CB   1 
ATOM   1411 C  CB   B GLN A 1 157 ? -20.731 -9.309  1.497   0.50 12.34 ? 158 GLN A CB   1 
ATOM   1412 C  CG   A GLN A 1 157 ? -21.066 -9.982  0.603   0.50 10.02 ? 158 GLN A CG   1 
ATOM   1413 C  CG   B GLN A 1 157 ? -20.318 -9.988  0.194   0.50 9.69  ? 158 GLN A CG   1 
ATOM   1414 C  CD   A GLN A 1 157 ? -19.880 -10.868 0.830   0.50 9.68  ? 158 GLN A CD   1 
ATOM   1415 C  CD   B GLN A 1 157 ? -19.197 -11.028 0.466   0.50 12.95 ? 158 GLN A CD   1 
ATOM   1416 O  OE1  A GLN A 1 157 ? -19.657 -11.444 1.945   0.50 9.79  ? 158 GLN A OE1  1 
ATOM   1417 O  OE1  B GLN A 1 157 ? -19.032 -11.566 1.573   0.50 13.97 ? 158 GLN A OE1  1 
ATOM   1418 N  NE2  A GLN A 1 157 ? -19.116 -11.053 -0.237  0.50 10.97 ? 158 GLN A NE2  1 
ATOM   1419 N  NE2  B GLN A 1 157 ? -18.432 -11.288 -0.533  0.50 12.03 ? 158 GLN A NE2  1 
ATOM   1420 N  N    A LYS A 1 158 ? -20.406 -5.995  1.707   0.50 7.91  ? 159 LYS A N    1 
ATOM   1421 N  N    B LYS A 1 158 ? -19.705 -6.025  1.300   0.50 12.88 ? 159 LYS A N    1 
ATOM   1422 C  CA   A LYS A 1 158 ? -19.928 -4.912  0.854   0.50 10.43 ? 159 LYS A CA   1 
ATOM   1423 C  CA   B LYS A 1 158 ? -19.288 -4.880  0.438   0.50 13.29 ? 159 LYS A CA   1 
ATOM   1424 C  C    A LYS A 1 158 ? -18.469 -4.609  1.018   0.50 8.65  ? 159 LYS A C    1 
ATOM   1425 C  C    B LYS A 1 158 ? -17.777 -4.558  0.631   0.50 13.85 ? 159 LYS A C    1 
ATOM   1426 O  O    A LYS A 1 158 ? -17.813 -4.215  0.017   0.50 9.22  ? 159 LYS A O    1 
ATOM   1427 O  O    B LYS A 1 158 ? -17.073 -4.209  -0.330  0.50 15.09 ? 159 LYS A O    1 
ATOM   1428 C  CB   A LYS A 1 158 ? -20.854 -3.663  1.070   0.50 8.61  ? 159 LYS A CB   1 
ATOM   1429 C  CB   B LYS A 1 158 ? -20.228 -3.666  0.656   0.50 16.24 ? 159 LYS A CB   1 
ATOM   1430 C  CG   A LYS A 1 158 ? -22.310 -3.907  0.360   0.50 16.99 ? 159 LYS A CG   1 
ATOM   1431 C  CG   B LYS A 1 158 ? -21.603 -3.861  0.008   0.50 21.41 ? 159 LYS A CG   1 
ATOM   1432 C  CD   A LYS A 1 158 ? -22.992 -2.560  -0.034  0.50 19.24 ? 159 LYS A CD   1 
ATOM   1433 C  CD   B LYS A 1 158 ? -22.720 -2.815  0.605   0.50 19.84 ? 159 LYS A CD   1 
ATOM   1434 C  CE   A LYS A 1 158 ? -24.226 -2.899  -0.924  0.50 21.42 ? 159 LYS A CE   1 
ATOM   1435 C  CE   B LYS A 1 158 ? -24.254 -3.100  0.126   0.50 22.33 ? 159 LYS A CE   1 
ATOM   1436 N  NZ   A LYS A 1 158 ? -25.215 -1.789  -1.037  0.50 25.38 ? 159 LYS A NZ   1 
ATOM   1437 N  NZ   B LYS A 1 158 ? -25.226 -1.842  0.101   0.50 23.69 ? 159 LYS A NZ   1 
ATOM   1438 N  N    A VAL A 1 159 ? -17.953 -4.705  2.265   0.50 8.27  ? 160 VAL A N    1 
ATOM   1439 N  N    B VAL A 1 159 ? -17.288 -4.657  1.880   0.50 12.06 ? 160 VAL A N    1 
ATOM   1440 C  CA   A VAL A 1 159 ? -16.514 -4.533  2.509   0.50 7.71  ? 160 VAL A CA   1 
ATOM   1441 C  CA   B VAL A 1 159 ? -15.859 -4.476  2.156   0.50 11.58 ? 160 VAL A CA   1 
ATOM   1442 C  C    A VAL A 1 159 ? -15.749 -5.639  1.796   0.50 7.68  ? 160 VAL A C    1 
ATOM   1443 C  C    B VAL A 1 159 ? -15.095 -5.656  1.502   0.50 11.04 ? 160 VAL A C    1 
ATOM   1444 O  O    A VAL A 1 159 ? -14.828 -5.424  1.042   0.50 8.50  ? 160 VAL A O    1 
ATOM   1445 O  O    B VAL A 1 159 ? -14.166 -5.435  0.739   0.50 11.95 ? 160 VAL A O    1 
ATOM   1446 C  CB   A VAL A 1 159 ? -16.276 -4.565  4.009   0.50 8.66  ? 160 VAL A CB   1 
ATOM   1447 C  CB   B VAL A 1 159 ? -15.585 -4.430  3.664   0.50 11.80 ? 160 VAL A CB   1 
ATOM   1448 C  CG1  A VAL A 1 159 ? -14.751 -4.525  4.324   0.50 10.98 ? 160 VAL A CG1  1 
ATOM   1449 C  CG1  B VAL A 1 159 ? -14.166 -4.786  3.968   0.50 12.55 ? 160 VAL A CG1  1 
ATOM   1450 C  CG2  A VAL A 1 159 ? -16.919 -3.404  4.636   0.50 7.52  ? 160 VAL A CG2  1 
ATOM   1451 C  CG2  B VAL A 1 159 ? -16.001 -3.084  4.319   0.50 13.13 ? 160 VAL A CG2  1 
ATOM   1452 N  N    A VAL A 1 160 ? -16.165 -6.876  2.036   0.50 7.57  ? 161 VAL A N    1 
ATOM   1453 N  N    B VAL A 1 160 ? -15.556 -6.898  1.713   0.50 10.43 ? 161 VAL A N    1 
ATOM   1454 C  CA   A VAL A 1 160 ? -15.494 -7.989  1.373   0.50 10.31 ? 161 VAL A CA   1 
ATOM   1455 C  CA   B VAL A 1 160 ? -14.812 -8.048  1.199   0.50 10.66 ? 161 VAL A CA   1 
ATOM   1456 C  C    A VAL A 1 160 ? -15.449 -7.830  -0.109  0.50 8.71  ? 161 VAL A C    1 
ATOM   1457 C  C    B VAL A 1 160 ? -14.672 -8.017  -0.303  0.50 11.47 ? 161 VAL A C    1 
ATOM   1458 O  O    A VAL A 1 160 ? -14.432 -8.126  -0.752  0.50 10.25 ? 161 VAL A O    1 
ATOM   1459 O  O    B VAL A 1 160 ? -13.603 -8.281  -0.881  0.50 10.67 ? 161 VAL A O    1 
ATOM   1460 C  CB   A VAL A 1 160 ? -16.309 -9.369  1.769   0.50 7.57  ? 161 VAL A CB   1 
ATOM   1461 C  CB   B VAL A 1 160 ? -15.518 -9.393  1.708   0.50 14.24 ? 161 VAL A CB   1 
ATOM   1462 C  CG1  A VAL A 1 160 ? -15.891 -10.455 0.864   0.50 13.38 ? 161 VAL A CG1  1 
ATOM   1463 C  CG1  B VAL A 1 160 ? -14.993 -10.570 0.782   0.50 12.83 ? 161 VAL A CG1  1 
ATOM   1464 C  CG2  A VAL A 1 160 ? -15.990 -9.617  3.236   0.50 12.19 ? 161 VAL A CG2  1 
ATOM   1465 C  CG2  B VAL A 1 160 ? -15.269 -9.504  3.198   0.50 14.63 ? 161 VAL A CG2  1 
ATOM   1466 N  N    A ASP A 1 161 ? -16.545 -7.361  -0.706  0.50 10.21 ? 162 ASP A N    1 
ATOM   1467 N  N    B ASP A 1 161 ? -15.754 -7.662  -0.987  0.50 11.55 ? 162 ASP A N    1 
ATOM   1468 C  CA   A ASP A 1 161 ? -16.568 -7.359  -2.153  0.50 10.36 ? 162 ASP A CA   1 
ATOM   1469 C  CA   B ASP A 1 161 ? -15.722 -7.660  -2.469  0.50 12.52 ? 162 ASP A CA   1 
ATOM   1470 C  C    A ASP A 1 161 ? -15.724 -6.286  -2.809  0.50 10.55 ? 162 ASP A C    1 
ATOM   1471 C  C    B ASP A 1 161 ? -14.803 -6.569  -3.066  0.50 13.31 ? 162 ASP A C    1 
ATOM   1472 O  O    A ASP A 1 161 ? -15.439 -6.421  -4.077  0.50 13.64 ? 162 ASP A O    1 
ATOM   1473 O  O    B ASP A 1 161 ? -14.436 -6.693  -4.245  0.50 16.04 ? 162 ASP A O    1 
ATOM   1474 C  CB   A ASP A 1 161 ? -18.034 -7.386  -2.654  0.50 12.26 ? 162 ASP A CB   1 
ATOM   1475 C  CB   B ASP A 1 161 ? -17.089 -7.492  -3.012  0.50 15.72 ? 162 ASP A CB   1 
ATOM   1476 C  CG   A ASP A 1 161 ? -18.557 -8.858  -2.739  0.50 13.10 ? 162 ASP A CG   1 
ATOM   1477 C  CG   B ASP A 1 161 ? -18.043 -8.631  -2.586  0.50 19.73 ? 162 ASP A CG   1 
ATOM   1478 O  OD1  A ASP A 1 161 ? -17.641 -9.722  -3.034  0.50 16.70 ? 162 ASP A OD1  1 
ATOM   1479 O  OD1  B ASP A 1 161 ? -17.588 -9.738  -2.280  0.50 22.24 ? 162 ASP A OD1  1 
ATOM   1480 O  OD2  A ASP A 1 161 ? -19.768 -9.006  -2.488  0.50 19.79 ? 162 ASP A OD2  1 
ATOM   1481 O  OD2  B ASP A 1 161 ? -19.289 -8.416  -2.589  0.50 19.35 ? 162 ASP A OD2  1 
ATOM   1482 N  N    A VAL A 1 162 ? -15.308 -5.275  -2.037  0.50 9.38  ? 163 VAL A N    1 
ATOM   1483 N  N    B VAL A 1 162 ? -14.482 -5.462  -2.347  0.50 11.99 ? 163 VAL A N    1 
ATOM   1484 C  CA   A VAL A 1 162 ? -14.465 -4.236  -2.661  0.50 9.87  ? 163 VAL A CA   1 
ATOM   1485 C  CA   B VAL A 1 162 ? -13.635 -4.406  -2.911  0.50 13.31 ? 163 VAL A CA   1 
ATOM   1486 C  C    A VAL A 1 162 ? -12.962 -4.579  -2.538  0.50 9.59  ? 163 VAL A C    1 
ATOM   1487 C  C    B VAL A 1 162 ? -12.133 -4.732  -2.665  0.50 12.47 ? 163 VAL A C    1 
ATOM   1488 O  O    A VAL A 1 162 ? -12.126 -3.896  -3.123  0.50 9.48  ? 163 VAL A O    1 
ATOM   1489 O  O    B VAL A 1 162 ? -11.244 -4.079  -3.173  0.50 10.54 ? 163 VAL A O    1 
ATOM   1490 C  CB   A VAL A 1 162 ? -14.892 -2.846  -2.080  0.50 11.78 ? 163 VAL A CB   1 
ATOM   1491 C  CB   B VAL A 1 162 ? -13.962 -2.968  -2.235  0.50 14.49 ? 163 VAL A CB   1 
ATOM   1492 C  CG1  A VAL A 1 162 ? -14.098 -2.660  -0.740  0.50 10.91 ? 163 VAL A CG1  1 
ATOM   1493 C  CG1  B VAL A 1 162 ? -13.209 -2.752  -0.978  0.50 13.62 ? 163 VAL A CG1  1 
ATOM   1494 C  CG2  A VAL A 1 162 ? -14.528 -1.743  -3.031  0.50 13.02 ? 163 VAL A CG2  1 
ATOM   1495 C  CG2  B VAL A 1 162 ? -13.783 -1.802  -3.144  0.50 16.53 ? 163 VAL A CG2  1 
ATOM   1496 N  N    A LEU A 1 163 ? -12.638 -5.563  -1.690  0.50 10.09 ? 164 LEU A N    1 
ATOM   1497 N  N    B LEU A 1 163 ? -11.820 -5.767  -1.876  0.50 11.51 ? 164 LEU A N    1 
ATOM   1498 C  CA   A LEU A 1 163 ? -11.259 -5.867  -1.443  0.50 9.15  ? 164 LEU A CA   1 
ATOM   1499 C  CA   B LEU A 1 163 ? -10.406 -5.951  -1.453  0.50 11.20 ? 164 LEU A CA   1 
ATOM   1500 C  C    A LEU A 1 163 ? -10.412 -6.206  -2.664  0.50 8.26  ? 164 LEU A C    1 
ATOM   1501 C  C    B LEU A 1 163 ? -9.507  -6.384  -2.587  0.50 12.70 ? 164 LEU A C    1 
ATOM   1502 O  O    A LEU A 1 163 ? -9.181  -5.916  -2.684  0.50 9.33  ? 164 LEU A O    1 
ATOM   1503 O  O    B LEU A 1 163 ? -8.305  -6.062  -2.603  0.50 12.93 ? 164 LEU A O    1 
ATOM   1504 C  CB   A LEU A 1 163 ? -11.094 -6.923  -0.362  0.50 8.48  ? 164 LEU A CB   1 
ATOM   1505 C  CB   B LEU A 1 163 ? -10.295 -7.009  -0.372  0.50 9.83  ? 164 LEU A CB   1 
ATOM   1506 C  CG   A LEU A 1 163 ? -11.711 -6.532  1.018   0.50 7.77  ? 164 LEU A CG   1 
ATOM   1507 C  CG   B LEU A 1 163 ? -10.979 -6.685  0.960   0.50 9.76  ? 164 LEU A CG   1 
ATOM   1508 C  CD1  A LEU A 1 163 ? -11.494 -7.600  2.100   0.50 10.43 ? 164 LEU A CD1  1 
ATOM   1509 C  CD1  B LEU A 1 163 ? -10.744 -7.895  1.912   0.50 11.14 ? 164 LEU A CD1  1 
ATOM   1510 C  CD2  A LEU A 1 163 ? -11.203 -5.163  1.575   0.50 11.94 ? 164 LEU A CD2  1 
ATOM   1511 C  CD2  B LEU A 1 163 ? -10.486 -5.360  1.586   0.50 10.40 ? 164 LEU A CD2  1 
ATOM   1512 N  N    A ASP A 1 164 ? -11.021 -6.788  -3.686  0.50 9.60  ? 165 ASP A N    1 
ATOM   1513 N  N    B ASP A 1 164 ? -10.078 -7.060  -3.579  0.50 14.22 ? 165 ASP A N    1 
ATOM   1514 C  CA   A ASP A 1 164 ? -10.231 -7.160  -4.855  0.50 11.43 ? 165 ASP A CA   1 
ATOM   1515 C  CA   B ASP A 1 164 ? -9.193  -7.442  -4.668  0.50 12.25 ? 165 ASP A CA   1 
ATOM   1516 C  C    A ASP A 1 164 ? -9.737  -5.912  -5.602  0.50 11.60 ? 165 ASP A C    1 
ATOM   1517 C  C    B ASP A 1 164 ? -8.669  -6.154  -5.437  0.50 11.73 ? 165 ASP A C    1 
ATOM   1518 O  O    A ASP A 1 164 ? -8.712  -6.036  -6.378  0.50 12.56 ? 165 ASP A O    1 
ATOM   1519 O  O    B ASP A 1 164 ? -7.597  -6.154  -6.090  0.50 14.74 ? 165 ASP A O    1 
ATOM   1520 C  CB   A ASP A 1 164 ? -11.109 -8.066  -5.740  0.50 10.99 ? 165 ASP A CB   1 
ATOM   1521 C  CB   B ASP A 1 164 ? -9.840  -8.420  -5.636  0.50 16.56 ? 165 ASP A CB   1 
ATOM   1522 C  CG   A ASP A 1 164 ? -12.058 -7.206  -6.628  0.50 16.53 ? 165 ASP A CG   1 
ATOM   1523 C  CG   B ASP A 1 164 ? -10.981 -7.798  -6.424  0.50 17.86 ? 165 ASP A CG   1 
ATOM   1524 O  OD1  A ASP A 1 164 ? -13.024 -6.666  -6.021  0.50 19.78 ? 165 ASP A OD1  1 
ATOM   1525 O  OD1  B ASP A 1 164 ? -11.946 -7.145  -5.858  0.50 16.50 ? 165 ASP A OD1  1 
ATOM   1526 O  OD2  A ASP A 1 164 ? -11.833 -7.088  -7.896  0.50 23.78 ? 165 ASP A OD2  1 
ATOM   1527 O  OD2  B ASP A 1 164 ? -10.873 -7.966  -7.639  0.50 25.95 ? 165 ASP A OD2  1 
ATOM   1528 N  N    A SER A 1 165 ? -10.318 -4.743  -5.258  0.50 10.47 ? 166 SER A N    1 
ATOM   1529 N  N    B SER A 1 165 ? -9.381  -5.014  -5.333  0.50 13.12 ? 166 SER A N    1 
ATOM   1530 C  CA   A SER A 1 165 ? -9.941  -3.515  -5.928  0.50 10.01 ? 166 SER A CA   1 
ATOM   1531 C  CA   B SER A 1 165 ? -8.859  -3.801  -5.999  0.50 12.90 ? 166 SER A CA   1 
ATOM   1532 C  C    A SER A 1 165 ? -8.831  -2.807  -5.176  0.50 9.45  ? 166 SER A C    1 
ATOM   1533 C  C    B SER A 1 165 ? -7.794  -3.050  -5.198  0.50 13.35 ? 166 SER A C    1 
ATOM   1534 O  O    A SER A 1 165 ? -8.253  -1.766  -5.645  0.50 9.55  ? 166 SER A O    1 
ATOM   1535 O  O    B SER A 1 165 ? -7.215  -2.001  -5.659  0.50 13.12 ? 166 SER A O    1 
ATOM   1536 C  CB   A SER A 1 165 ? -11.099 -2.541  -6.190  0.50 10.63 ? 166 SER A CB   1 
ATOM   1537 C  CB   B SER A 1 165 ? -10.015 -2.846  -6.253  0.50 14.18 ? 166 SER A CB   1 
ATOM   1538 O  OG   A SER A 1 165 ? -11.530 -2.042  -4.966  0.50 12.94 ? 166 SER A OG   1 
ATOM   1539 O  OG   B SER A 1 165 ? -10.504 -2.199  -5.088  0.50 15.49 ? 166 SER A OG   1 
ATOM   1540 N  N    A ILE A 1 166 ? -8.550  -3.283  -3.945  0.50 7.00  ? 167 ILE A N    1 
ATOM   1541 N  N    B ILE A 1 166 ? -7.613  -3.475  -3.959  0.50 12.64 ? 167 ILE A N    1 
ATOM   1542 C  CA   A ILE A 1 166 ? -7.483  -2.619  -3.141  0.50 7.30  ? 167 ILE A CA   1 
ATOM   1543 C  CA   B ILE A 1 166 ? -6.645  -2.796  -3.056  0.50 12.05 ? 167 ILE A CA   1 
ATOM   1544 C  C    A ILE A 1 166 ? -6.490  -3.716  -2.652  0.50 6.92  ? 167 ILE A C    1 
ATOM   1545 C  C    B ILE A 1 166 ? -5.656  -3.853  -2.527  0.50 10.43 ? 167 ILE A C    1 
ATOM   1546 O  O    A ILE A 1 166 ? -6.088  -3.727  -1.506  0.50 6.62  ? 167 ILE A O    1 
ATOM   1547 O  O    B ILE A 1 166 ? -5.234  -3.855  -1.414  0.50 11.29 ? 167 ILE A O    1 
ATOM   1548 C  CB   A ILE A 1 166 ? -8.106  -1.777  -1.947  0.50 6.42  ? 167 ILE A CB   1 
ATOM   1549 C  CB   B ILE A 1 166 ? -7.270  -1.956  -1.913  0.50 12.16 ? 167 ILE A CB   1 
ATOM   1550 C  CG1  A ILE A 1 166 ? -8.938  -2.642  -1.018  0.50 8.58  ? 167 ILE A CG1  1 
ATOM   1551 C  CG1  B ILE A 1 166 ? -8.306  -2.762  -1.088  0.50 12.88 ? 167 ILE A CG1  1 
ATOM   1552 C  CG2  A ILE A 1 166 ? -8.948  -0.591  -2.458  0.50 7.11  ? 167 ILE A CG2  1 
ATOM   1553 C  CG2  B ILE A 1 166 ? -7.988  -0.681  -2.537  0.50 14.47 ? 167 ILE A CG2  1 
ATOM   1554 C  CD1  A ILE A 1 166 ? -8.329  -2.367  0.490   0.50 12.62 ? 167 ILE A CD1  1 
ATOM   1555 C  CD1  B ILE A 1 166 ? -8.860  -2.078  0.185   0.50 10.21 ? 167 ILE A CD1  1 
ATOM   1556 N  N    A LYS A 1 167 ? -6.030  -4.581  -3.562  0.50 7.92  ? 168 LYS A N    1 
ATOM   1557 N  N    B LYS A 1 167 ? -5.212  -4.708  -3.440  0.50 11.69 ? 168 LYS A N    1 
ATOM   1558 C  CA   A LYS A 1 167 ? -5.257  -5.743  -3.094  0.50 8.83  ? 168 LYS A CA   1 
ATOM   1559 C  CA   B LYS A 1 167 ? -4.541  -5.872  -2.982  0.50 12.33 ? 168 LYS A CA   1 
ATOM   1560 C  C    A LYS A 1 167 ? -3.972  -5.351  -2.378  0.50 7.85  ? 168 LYS A C    1 
ATOM   1561 C  C    B LYS A 1 167 ? -3.157  -5.553  -2.361  0.50 11.20 ? 168 LYS A C    1 
ATOM   1562 O  O    A LYS A 1 167 ? -3.595  -5.963  -1.396  0.50 7.39  ? 168 LYS A O    1 
ATOM   1563 O  O    B LYS A 1 167 ? -2.759  -6.215  -1.430  0.50 9.56  ? 168 LYS A O    1 
ATOM   1564 C  CB   A LYS A 1 167 ? -4.992  -6.642  -4.304  0.50 10.15 ? 168 LYS A CB   1 
ATOM   1565 C  CB   B LYS A 1 167 ? -4.325  -6.822  -4.163  0.50 12.77 ? 168 LYS A CB   1 
ATOM   1566 C  CG   A LYS A 1 167 ? -3.983  -7.796  -4.004  0.50 13.69 ? 168 LYS A CG   1 
ATOM   1567 C  CG   B LYS A 1 167 ? -3.996  -8.192  -3.786  0.50 15.01 ? 168 LYS A CG   1 
ATOM   1568 C  CD   A LYS A 1 167 ? -3.301  -8.611  -5.289  0.50 14.31 ? 168 LYS A CD   1 
ATOM   1569 C  CD   B LYS A 1 167 ? -4.108  -9.029  -5.127  0.50 16.85 ? 168 LYS A CD   1 
ATOM   1570 C  CE   A LYS A 1 167 ? -2.558  -9.749  -4.736  0.50 18.62 ? 168 LYS A CE   1 
ATOM   1571 C  CE   B LYS A 1 167 ? -3.478  -10.364 -5.039  0.50 21.31 ? 168 LYS A CE   1 
ATOM   1572 N  NZ   A LYS A 1 167 ? -1.902  -10.639 -5.631  0.50 23.38 ? 168 LYS A NZ   1 
ATOM   1573 N  NZ   B LYS A 1 167 ? -3.145  -10.718 -6.528  0.50 21.29 ? 168 LYS A NZ   1 
ATOM   1574 N  N    A THR A 1 168 ? -3.334  -4.293  -2.907  0.50 6.33  ? 169 THR A N    1 
ATOM   1575 N  N    B THR A 1 168 ? -2.415  -4.552  -2.898  0.50 10.17 ? 169 THR A N    1 
ATOM   1576 C  CA   A THR A 1 168 ? -1.975  -3.996  -2.540  0.50 6.75  ? 169 THR A CA   1 
ATOM   1577 C  CA   B THR A 1 168 ? -1.090  -4.281  -2.444  0.50 12.21 ? 169 THR A CA   1 
ATOM   1578 C  C    A THR A 1 168 ? -1.832  -2.633  -1.825  0.50 6.52  ? 169 THR A C    1 
ATOM   1579 C  C    B THR A 1 168 ? -0.973  -2.974  -1.738  0.50 12.29 ? 169 THR A C    1 
ATOM   1580 O  O    A THR A 1 168 ? -2.699  -1.738  -1.961  0.50 7.15  ? 169 THR A O    1 
ATOM   1581 O  O    B THR A 1 168 ? -1.798  -2.103  -1.935  0.50 12.05 ? 169 THR A O    1 
ATOM   1582 C  CB   A THR A 1 168 ? -0.996  -4.026  -3.774  0.50 8.43  ? 169 THR A CB   1 
ATOM   1583 C  CB   B THR A 1 168 ? -0.085  -4.378  -3.627  0.50 12.41 ? 169 THR A CB   1 
ATOM   1584 O  OG1  A THR A 1 168 ? -1.585  -3.251  -4.832  0.50 7.94  ? 169 THR A OG1  1 
ATOM   1585 O  OG1  B THR A 1 168 ? -0.570  -3.597  -4.685  0.50 13.79 ? 169 THR A OG1  1 
ATOM   1586 C  CG2  A THR A 1 168 ? -0.759  -5.489  -4.243  0.50 8.30  ? 169 THR A CG2  1 
ATOM   1587 C  CG2  B THR A 1 168 ? 0.069   -5.771  -4.112  0.50 14.38 ? 169 THR A CG2  1 
ATOM   1588 N  N    A LYS A 1 169 ? -0.740  -2.441  -1.134  0.50 7.38  ? 170 LYS A N    1 
ATOM   1589 N  N    B LYS A 1 169 ? 0.032   -2.865  -0.890  0.50 11.03 ? 170 LYS A N    1 
ATOM   1590 C  CA   A LYS A 1 169 ? -0.463  -1.223  -0.384  0.50 6.27  ? 170 LYS A CA   1 
ATOM   1591 C  CA   B LYS A 1 169 ? 0.351   -1.576  -0.260  0.50 11.96 ? 170 LYS A CA   1 
ATOM   1592 C  C    A LYS A 1 169 ? -0.525  0.040   -1.189  0.50 7.30  ? 170 LYS A C    1 
ATOM   1593 C  C    B LYS A 1 169 ? 0.274   -0.351  -1.113  0.50 12.00 ? 170 LYS A C    1 
ATOM   1594 O  O    A LYS A 1 169 ? -0.056  0.109   -2.315  0.50 8.33  ? 170 LYS A O    1 
ATOM   1595 O  O    B LYS A 1 169 ? 0.893   -0.315  -2.200  0.50 13.13 ? 170 LYS A O    1 
ATOM   1596 C  CB   A LYS A 1 169 ? 0.943   -1.411  0.202   0.50 5.83  ? 170 LYS A CB   1 
ATOM   1597 C  CB   B LYS A 1 169 ? 1.684   -1.652  0.439   0.50 12.56 ? 170 LYS A CB   1 
ATOM   1598 C  CG   A LYS A 1 169 ? 1.482   -0.228  0.978   0.50 10.11 ? 170 LYS A CG   1 
ATOM   1599 C  CG   B LYS A 1 169 ? 2.082   -0.397  1.292   0.50 12.02 ? 170 LYS A CG   1 
ATOM   1600 C  CD   A LYS A 1 169 ? 2.712   -0.556  1.717   0.50 10.59 ? 170 LYS A CD   1 
ATOM   1601 C  CD   B LYS A 1 169 ? 3.543   -0.455  1.743   0.50 15.02 ? 170 LYS A CD   1 
ATOM   1602 C  CE   A LYS A 1 169 ? 3.879   -1.026  0.755   0.50 15.62 ? 170 LYS A CE   1 
ATOM   1603 C  CE   B LYS A 1 169 ? 4.240   0.292   0.559   0.50 19.59 ? 170 LYS A CE   1 
ATOM   1604 N  NZ   A LYS A 1 169 ? 5.298   -1.222  1.354   0.50 19.71 ? 170 LYS A NZ   1 
ATOM   1605 N  NZ   B LYS A 1 169 ? 5.455   1.136   0.897   0.50 26.37 ? 170 LYS A NZ   1 
ATOM   1606 N  N    A GLY A 1 170 ? -1.307  0.974   -0.662  0.50 7.85  ? 171 GLY A N    1 
ATOM   1607 N  N    B GLY A 1 170 ? -0.420  0.672   -0.616  0.50 10.94 ? 171 GLY A N    1 
ATOM   1608 C  CA   A GLY A 1 170 ? -1.501  2.252   -1.285  0.50 8.64  ? 171 GLY A CA   1 
ATOM   1609 C  CA   B GLY A 1 170 ? -0.462  1.968   -1.414  0.50 12.58 ? 171 GLY A CA   1 
ATOM   1610 C  C    A GLY A 1 170 ? -2.676  2.353   -2.237  0.50 10.32 ? 171 GLY A C    1 
ATOM   1611 C  C    B GLY A 1 170 ? -1.702  2.055   -2.291  0.50 12.65 ? 171 GLY A C    1 
ATOM   1612 O  O    A GLY A 1 170 ? -2.963  3.476   -2.740  0.50 10.15 ? 171 GLY A O    1 
ATOM   1613 O  O    B GLY A 1 170 ? -2.024  3.134   -2.824  0.50 14.13 ? 171 GLY A O    1 
ATOM   1614 N  N    A LYS A 1 171 ? -3.365  1.258   -2.519  0.50 7.46  ? 172 LYS A N    1 
ATOM   1615 N  N    B LYS A 1 171 ? -2.398  0.943   -2.571  0.50 10.89 ? 172 LYS A N    1 
ATOM   1616 C  CA   A LYS A 1 171 ? -4.589  1.258   -3.368  0.50 8.00  ? 172 LYS A CA   1 
ATOM   1617 C  CA   B LYS A 1 171 ? -3.636  1.036   -3.290  0.50 12.26 ? 172 LYS A CA   1 
ATOM   1618 C  C    A LYS A 1 171 ? -5.769  1.715   -2.539  0.50 7.87  ? 172 LYS A C    1 
ATOM   1619 C  C    B LYS A 1 171 ? -4.816  1.526   -2.474  0.50 12.38 ? 172 LYS A C    1 
ATOM   1620 O  O    A LYS A 1 171 ? -5.921  1.327   -1.381  0.50 7.87  ? 172 LYS A O    1 
ATOM   1621 O  O    B LYS A 1 171 ? -5.008  1.137   -1.303  0.50 12.55 ? 172 LYS A O    1 
ATOM   1622 C  CB   A LYS A 1 171 ? -4.904  -0.035  -4.036  0.50 8.96  ? 172 LYS A CB   1 
ATOM   1623 C  CB   B LYS A 1 171 ? -3.959  -0.371  -3.938  0.50 12.49 ? 172 LYS A CB   1 
ATOM   1624 C  CG   A LYS A 1 171 ? -3.803  -0.441  -5.063  0.50 9.81  ? 172 LYS A CG   1 
ATOM   1625 C  CG   B LYS A 1 171 ? -2.883  -0.723  -4.903  0.50 15.24 ? 172 LYS A CG   1 
ATOM   1626 C  CD   A LYS A 1 171 ? -4.218  -1.534  -6.139  0.50 13.22 ? 172 LYS A CD   1 
ATOM   1627 C  CD   B LYS A 1 171 ? -3.250  -1.935  -5.838  0.50 17.73 ? 172 LYS A CD   1 
ATOM   1628 C  CE   A LYS A 1 171 ? -5.412  -1.088  -6.947  0.50 14.72 ? 172 LYS A CE   1 
ATOM   1629 C  CE   B LYS A 1 171 ? -3.645  -1.466  -7.240  0.50 21.03 ? 172 LYS A CE   1 
ATOM   1630 N  NZ   A LYS A 1 171 ? -5.899  -2.133  -7.917  0.50 14.63 ? 172 LYS A NZ   1 
ATOM   1631 N  NZ   B LYS A 1 171 ? -4.567  -2.541  -7.811  0.50 25.65 ? 172 LYS A NZ   1 
ATOM   1632 N  N    A SER A 1 172 ? -6.625  2.597   -3.099  0.50 7.93  ? 173 SER A N    1 
ATOM   1633 N  N    B SER A 1 172 ? -5.618  2.348   -3.112  0.50 12.52 ? 173 SER A N    1 
ATOM   1634 C  CA   A SER A 1 172 ? -7.858  3.034   -2.477  0.50 8.47  ? 173 SER A CA   1 
ATOM   1635 C  CA   B SER A 1 172 ? -6.851  2.781   -2.471  0.50 10.45 ? 173 SER A CA   1 
ATOM   1636 C  C    A SER A 1 172 ? -8.999  2.845   -3.494  0.50 7.70  ? 173 SER A C    1 
ATOM   1637 C  C    B SER A 1 172 ? -7.943  2.813   -3.484  0.50 11.43 ? 173 SER A C    1 
ATOM   1638 O  O    A SER A 1 172 ? -8.798  2.794   -4.741  0.50 10.56 ? 173 SER A O    1 
ATOM   1639 O  O    B SER A 1 172 ? -7.674  2.779   -4.718  0.50 13.10 ? 173 SER A O    1 
ATOM   1640 C  CB   A SER A 1 172 ? -7.798  4.467   -1.963  0.50 8.51  ? 173 SER A CB   1 
ATOM   1641 C  CB   B SER A 1 172 ? -6.693  4.195   -1.857  0.50 12.73 ? 173 SER A CB   1 
ATOM   1642 O  OG   A SER A 1 172 ? -7.520  5.279   -3.089  0.50 13.45 ? 173 SER A OG   1 
ATOM   1643 O  OG   B SER A 1 172 ? -6.338  5.234   -2.836  0.50 13.01 ? 173 SER A OG   1 
ATOM   1644 N  N    A ALA A 1 173 ? -10.204 2.753   -2.945  0.50 8.64  ? 174 ALA A N    1 
ATOM   1645 N  N    B ALA A 1 173 ? -9.159  2.977   -2.969  0.50 11.99 ? 174 ALA A N    1 
ATOM   1646 C  CA   A ALA A 1 173 ? -11.399 2.646   -3.790  0.50 8.14  ? 174 ALA A CA   1 
ATOM   1647 C  CA   B ALA A 1 173 ? -10.367 3.101   -3.799  0.50 12.88 ? 174 ALA A CA   1 
ATOM   1648 C  C    A ALA A 1 173 ? -12.488 3.513   -3.159  0.50 8.54  ? 174 ALA A C    1 
ATOM   1649 C  C    B ALA A 1 173 ? -11.423 4.005   -3.138  0.50 13.59 ? 174 ALA A C    1 
ATOM   1650 O  O    A ALA A 1 173 ? -12.608 3.668   -1.925  0.50 7.42  ? 174 ALA A O    1 
ATOM   1651 O  O    B ALA A 1 173 ? -11.474 3.990   -1.900  0.50 12.88 ? 174 ALA A O    1 
ATOM   1652 C  CB   A ALA A 1 173 ? -11.864 1.254   -3.940  0.50 10.60 ? 174 ALA A CB   1 
ATOM   1653 C  CB   B ALA A 1 173 ? -10.935 1.661   -4.137  0.50 12.39 ? 174 ALA A CB   1 
ATOM   1654 N  N    A ASP A 1 174 ? -13.284 4.144   -4.030  0.50 9.49  ? 175 ASP A N    1 
ATOM   1655 N  N    B ASP A 1 174 ? -12.235 4.698   -3.960  0.50 14.25 ? 175 ASP A N    1 
ATOM   1656 C  CA   A ASP A 1 174 ? -14.480 4.805   -3.579  0.50 9.18  ? 175 ASP A CA   1 
ATOM   1657 C  CA   B ASP A 1 174 ? -13.528 5.251   -3.454  0.50 13.16 ? 175 ASP A CA   1 
ATOM   1658 C  C    A ASP A 1 174 ? -15.344 3.840   -2.766  0.50 9.82  ? 175 ASP A C    1 
ATOM   1659 C  C    B ASP A 1 174 ? -14.375 4.188   -2.803  0.50 15.09 ? 175 ASP A C    1 
ATOM   1660 O  O    A ASP A 1 174 ? -15.520 2.697   -3.150  0.50 10.75 ? 175 ASP A O    1 
ATOM   1661 O  O    B ASP A 1 174 ? -14.455 2.999   -3.251  0.50 14.75 ? 175 ASP A O    1 
ATOM   1662 C  CB   A ASP A 1 174 ? -15.278 5.382   -4.798  0.50 13.38 ? 175 ASP A CB   1 
ATOM   1663 C  CB   B ASP A 1 174 ? -14.437 6.028   -4.516  0.50 17.67 ? 175 ASP A CB   1 
ATOM   1664 C  CG   A ASP A 1 174 ? -14.403 6.356   -5.569  0.50 12.84 ? 175 ASP A CG   1 
ATOM   1665 C  CG   B ASP A 1 174 ? -13.757 7.229   -5.246  0.50 21.05 ? 175 ASP A CG   1 
ATOM   1666 O  OD1  A ASP A 1 174 ? -13.318 6.769   -4.990  0.50 20.99 ? 175 ASP A OD1  1 
ATOM   1667 O  OD1  B ASP A 1 174 ? -13.306 8.161   -4.604  0.50 27.05 ? 175 ASP A OD1  1 
ATOM   1668 O  OD2  A ASP A 1 174 ? -14.663 6.659   -6.740  0.50 14.47 ? 175 ASP A OD2  1 
ATOM   1669 O  OD2  B ASP A 1 174 ? -13.762 7.251   -6.533  0.50 27.03 ? 175 ASP A OD2  1 
ATOM   1670 N  N    A PHE A 1 175 ? -15.899 4.335   -1.661  0.50 8.40  ? 176 PHE A N    1 
ATOM   1671 N  N    B PHE A 1 175 ? -14.909 4.559   -1.629  0.50 12.34 ? 176 PHE A N    1 
ATOM   1672 C  CA   A PHE A 1 175 ? -16.648 3.424   -0.735  0.50 8.07  ? 176 PHE A CA   1 
ATOM   1673 C  CA   B PHE A 1 175 ? -15.722 3.596   -0.932  0.50 13.03 ? 176 PHE A CA   1 
ATOM   1674 C  C    A PHE A 1 175 ? -17.674 4.249   0.030   0.50 7.55  ? 176 PHE A C    1 
ATOM   1675 C  C    B PHE A 1 175 ? -16.806 4.352   -0.208  0.50 12.66 ? 176 PHE A C    1 
ATOM   1676 O  O    A PHE A 1 175 ? -17.533 4.419   1.222   0.50 10.18 ? 176 PHE A O    1 
ATOM   1677 O  O    B PHE A 1 175 ? -16.656 4.718   0.954   0.50 12.55 ? 176 PHE A O    1 
ATOM   1678 C  CB   A PHE A 1 175 ? -15.740 2.618   0.191   0.50 8.04  ? 176 PHE A CB   1 
ATOM   1679 C  CB   B PHE A 1 175 ? -14.803 2.779   -0.005  0.50 11.24 ? 176 PHE A CB   1 
ATOM   1680 C  CG   A PHE A 1 175 ? -16.387 1.367   0.728   0.50 9.09  ? 176 PHE A CG   1 
ATOM   1681 C  CG   B PHE A 1 175 ? -15.454 1.513   0.488   0.50 9.80  ? 176 PHE A CG   1 
ATOM   1682 C  CD1  A PHE A 1 175 ? -16.791 0.405   -0.113  0.50 9.19  ? 176 PHE A CD1  1 
ATOM   1683 C  CD1  B PHE A 1 175 ? -15.740 0.448   -0.356  0.50 11.82 ? 176 PHE A CD1  1 
ATOM   1684 C  CD2  A PHE A 1 175 ? -16.646 1.228   2.103   0.50 7.61  ? 176 PHE A CD2  1 
ATOM   1685 C  CD2  B PHE A 1 175 ? -15.735 1.324   1.829   0.50 12.34 ? 176 PHE A CD2  1 
ATOM   1686 C  CE1  A PHE A 1 175 ? -17.400 -0.747  0.383   0.50 10.76 ? 176 PHE A CE1  1 
ATOM   1687 C  CE1  B PHE A 1 175 ? -16.323 -0.730  0.131   0.50 10.94 ? 176 PHE A CE1  1 
ATOM   1688 C  CE2  A PHE A 1 175 ? -17.219 0.016   2.647   0.50 9.29  ? 176 PHE A CE2  1 
ATOM   1689 C  CE2  B PHE A 1 175 ? -16.369 0.089   2.330   0.50 10.24 ? 176 PHE A CE2  1 
ATOM   1690 C  CZ   A PHE A 1 175 ? -17.579 -0.950  1.758   0.50 8.73  ? 176 PHE A CZ   1 
ATOM   1691 C  CZ   B PHE A 1 175 ? -16.629 -0.884  1.457   0.50 10.97 ? 176 PHE A CZ   1 
ATOM   1692 N  N    A THR A 1 176 ? -18.730 4.619   -0.671  0.50 9.90  ? 177 THR A N    1 
ATOM   1693 N  N    B THR A 1 176 ? -17.904 4.665   -0.918  0.50 10.01 ? 177 THR A N    1 
ATOM   1694 C  CA   A THR A 1 176 ? -19.800 5.471   -0.066  0.50 10.20 ? 177 THR A CA   1 
ATOM   1695 C  CA   B THR A 1 176 ? -19.018 5.421   -0.335  0.50 12.78 ? 177 THR A CA   1 
ATOM   1696 C  C    A THR A 1 176 ? -20.988 4.696   0.412   0.50 9.16  ? 177 THR A C    1 
ATOM   1697 C  C    B THR A 1 176 ? -20.253 4.618   0.087   0.50 11.77 ? 177 THR A C    1 
ATOM   1698 O  O    A THR A 1 176 ? -21.251 3.582   -0.052  0.50 9.20  ? 177 THR A O    1 
ATOM   1699 O  O    B THR A 1 176 ? -20.380 3.392   -0.314  0.50 11.52 ? 177 THR A O    1 
ATOM   1700 C  CB   A THR A 1 176 ? -20.277 6.567   -1.073  0.50 11.49 ? 177 THR A CB   1 
ATOM   1701 C  CB   B THR A 1 176 ? -19.444 6.521   -1.341  0.50 10.24 ? 177 THR A CB   1 
ATOM   1702 O  OG1  A THR A 1 176 ? -20.762 5.923   -2.244  0.50 11.68 ? 177 THR A OG1  1 
ATOM   1703 O  OG1  B THR A 1 176 ? -19.820 5.953   -2.563  0.50 13.68 ? 177 THR A OG1  1 
ATOM   1704 C  CG2  A THR A 1 176 ? -19.216 7.715   -1.378  0.50 13.91 ? 177 THR A CG2  1 
ATOM   1705 C  CG2  B THR A 1 176 ? -18.313 7.489   -1.598  0.50 13.54 ? 177 THR A CG2  1 
ATOM   1706 N  N    A ASN A 1 177 ? -21.744 5.295   1.322   0.50 9.56  ? 178 ASN A N    1 
ATOM   1707 N  N    B ASN A 1 177 ? -21.067 5.209   0.948   0.50 11.97 ? 178 ASN A N    1 
ATOM   1708 C  CA   A ASN A 1 177 ? -22.980 4.745   1.761   0.50 10.20 ? 178 ASN A CA   1 
ATOM   1709 C  CA   B ASN A 1 177 ? -22.397 4.641   1.341   0.50 11.84 ? 178 ASN A CA   1 
ATOM   1710 C  C    A ASN A 1 177 ? -22.725 3.453   2.523   0.50 12.44 ? 178 ASN A C    1 
ATOM   1711 C  C    B ASN A 1 177 ? -22.401 3.283   2.085   0.50 13.28 ? 178 ASN A C    1 
ATOM   1712 O  O    A ASN A 1 177 ? -23.736 2.804   2.730   0.50 12.46 ? 178 ASN A O    1 
ATOM   1713 O  O    B ASN A 1 177 ? -23.289 2.459   1.976   0.50 14.64 ? 178 ASN A O    1 
ATOM   1714 C  CB   A ASN A 1 177 ? -23.965 4.576   0.607   0.50 11.91 ? 178 ASN A CB   1 
ATOM   1715 C  CB   B ASN A 1 177 ? -23.355 4.624   0.169   0.50 12.83 ? 178 ASN A CB   1 
ATOM   1716 C  CG   A ASN A 1 177 ? -24.120 5.872   -0.181  0.50 13.95 ? 178 ASN A CG   1 
ATOM   1717 C  CG   B ASN A 1 177 ? -23.710 6.112   -0.245  0.50 14.55 ? 178 ASN A CG   1 
ATOM   1718 O  OD1  A ASN A 1 177 ? -24.916 6.709   0.211   0.50 15.95 ? 178 ASN A OD1  1 
ATOM   1719 O  OD1  B ASN A 1 177 ? -24.300 6.865   0.555   0.50 14.25 ? 178 ASN A OD1  1 
ATOM   1720 N  ND2  A ASN A 1 177 ? -23.344 6.030   -1.300  0.50 13.14 ? 178 ASN A ND2  1 
ATOM   1721 N  ND2  B ASN A 1 177 ? -23.231 6.520   -1.409  0.50 16.94 ? 178 ASN A ND2  1 
ATOM   1722 N  N    . PHE A 1 178 ? -21.423 3.153   2.944   1.00 13.23 ? 179 PHE A N    1 
ATOM   1723 C  CA   . PHE A 1 178 ? -21.277 1.929   3.744   1.00 14.42 ? 179 PHE A CA   1 
ATOM   1724 C  C    . PHE A 1 178 ? -21.832 2.160   5.109   1.00 13.53 ? 179 PHE A C    1 
ATOM   1725 O  O    . PHE A 1 178 ? -21.360 3.145   5.744   1.00 16.00 ? 179 PHE A O    1 
ATOM   1726 C  CB   . PHE A 1 178 ? -19.928 1.450   3.831   1.00 14.81 ? 179 PHE A CB   1 
ATOM   1727 C  CG   . PHE A 1 178 ? -19.765 0.202   4.637   1.00 13.55 ? 179 PHE A CG   1 
ATOM   1728 C  CD1  . PHE A 1 178 ? -20.209 -1.049  4.123   1.00 15.13 ? 179 PHE A CD1  1 
ATOM   1729 C  CD2  . PHE A 1 178 ? -19.410 0.331   6.008   1.00 12.34 ? 179 PHE A CD2  1 
ATOM   1730 C  CE1  . PHE A 1 178 ? -20.123 -2.178  4.861   1.00 14.05 ? 179 PHE A CE1  1 
ATOM   1731 C  CE2  . PHE A 1 178 ? -19.404 -0.907  6.808   1.00 11.82 ? 179 PHE A CE2  1 
ATOM   1732 C  CZ   . PHE A 1 178 ? -19.769 -2.105  6.233   1.00 13.83 ? 179 PHE A CZ   1 
ATOM   1733 N  N    . ASP A 1 179 ? -22.751 1.332   5.646   1.00 14.03 ? 180 ASP A N    1 
ATOM   1734 C  CA   . ASP A 1 179 ? -23.344 1.561   6.934   1.00 13.27 ? 180 ASP A CA   1 
ATOM   1735 C  C    . ASP A 1 179 ? -22.684 0.662   8.001   1.00 12.32 ? 180 ASP A C    1 
ATOM   1736 O  O    . ASP A 1 179 ? -22.960 -0.545  8.043   1.00 13.19 ? 180 ASP A O    1 
ATOM   1737 C  CB   . ASP A 1 179 ? -24.869 1.284   6.826   1.00 15.34 ? 180 ASP A CB   1 
ATOM   1738 C  CG   . ASP A 1 179 ? -25.599 1.658   8.027   1.00 16.17 ? 180 ASP A CG   1 
ATOM   1739 O  OD1  . ASP A 1 179 ? -25.055 1.830   9.149   1.00 15.39 ? 180 ASP A OD1  1 
ATOM   1740 O  OD2  . ASP A 1 179 ? -26.874 1.913   7.917   1.00 23.29 ? 180 ASP A OD2  1 
ATOM   1741 N  N    . PRO A 1 180 ? -21.863 1.258   8.885   1.00 11.66 ? 181 PRO A N    1 
ATOM   1742 C  CA   . PRO A 1 180 ? -21.158 0.402   9.900   1.00 11.88 ? 181 PRO A CA   1 
ATOM   1743 C  C    . PRO A 1 180 ? -22.156 -0.205  10.955  1.00 11.55 ? 181 PRO A C    1 
ATOM   1744 O  O    . PRO A 1 180 ? -21.723 -1.072  11.701  1.00 11.48 ? 181 PRO A O    1 
ATOM   1745 C  CB   . PRO A 1 180 ? -20.181 1.357   10.494  1.00 12.69 ? 181 PRO A CB   1 
ATOM   1746 C  CG   . PRO A 1 180 ? -20.815 2.693   10.427  1.00 12.86 ? 181 PRO A CG   1 
ATOM   1747 C  CD   . PRO A 1 180 ? -21.531 2.687   8.999   1.00 11.94 ? 181 PRO A CD   1 
ATOM   1748 N  N    . ARG A 1 181 ? -23.423 0.231   10.927  1.00 10.34 ? 182 ARG A N    1 
ATOM   1749 C  CA   . ARG A 1 181 ? -24.341 -0.467  11.888  1.00 11.98 ? 182 ARG A CA   1 
ATOM   1750 C  C    . ARG A 1 181 ? -24.442 -1.906  11.516  1.00 13.63 ? 182 ARG A C    1 
ATOM   1751 O  O    . ARG A 1 181 ? -24.823 -2.711  12.389  1.00 13.76 ? 182 ARG A O    1 
ATOM   1752 C  CB   . ARG A 1 181 ? -25.733 0.159   11.835  1.00 13.46 ? 182 ARG A CB   1 
ATOM   1753 C  CG   . ARG A 1 181 ? -25.699 1.630   12.335  1.00 13.53 ? 182 ARG A CG   1 
ATOM   1754 C  CD   . ARG A 1 181 ? -27.045 2.340   12.271  1.00 15.46 ? 182 ARG A CD   1 
ATOM   1755 N  NE   . ARG A 1 181 ? -27.313 2.532   10.822  1.00 15.47 ? 182 ARG A NE   1 
ATOM   1756 C  CZ   . ARG A 1 181 ? -28.403 3.288   10.515  1.00 19.34 ? 182 ARG A CZ   1 
ATOM   1757 N  NH1  . ARG A 1 181 ? -29.164 3.735   11.514  1.00 23.05 ? 182 ARG A NH1  1 
ATOM   1758 N  NH2  . ARG A 1 181 ? -28.706 3.525   9.233   1.00 21.44 ? 182 ARG A NH2  1 
ATOM   1759 N  N    . GLY A 1 182 ? -24.176 -2.272  10.250  1.00 13.42 ? 183 GLY A N    1 
ATOM   1760 C  CA   . GLY A 1 182 ? -24.292 -3.685  9.894   1.00 14.30 ? 183 GLY A CA   1 
ATOM   1761 C  C    . GLY A 1 182 ? -23.157 -4.561  10.385  1.00 14.43 ? 183 GLY A C    1 
ATOM   1762 O  O    . GLY A 1 182 ? -23.121 -5.770  10.121  1.00 16.37 ? 183 GLY A O    1 
ATOM   1763 N  N    . LEU A 1 183 ? -22.190 -3.988  11.153  1.00 13.08 ? 184 LEU A N    1 
ATOM   1764 C  CA   . LEU A 1 183 ? -21.043 -4.735  11.677  1.00 12.08 ? 184 LEU A CA   1 
ATOM   1765 C  C    . LEU A 1 183 ? -21.205 -4.937  13.210  1.00 11.11 ? 184 LEU A C    1 
ATOM   1766 O  O    . LEU A 1 183 ? -20.288 -5.531  13.817  1.00 13.02 ? 184 LEU A O    1 
ATOM   1767 C  CB   . LEU A 1 183 ? -19.723 -4.010  11.422  1.00 10.99 ? 184 LEU A CB   1 
ATOM   1768 C  CG   . LEU A 1 183 ? -19.432 -3.830  9.920   1.00 11.24 ? 184 LEU A CG   1 
ATOM   1769 C  CD1  . LEU A 1 183 ? -18.231 -2.969  9.790   1.00 13.61 ? 184 LEU A CD1  1 
ATOM   1770 C  CD2  . LEU A 1 183 ? -19.275 -5.192  9.193   1.00 17.38 ? 184 LEU A CD2  1 
ATOM   1771 N  N    A LEU A 1 184 ? -22.367 -4.558  13.824  0.50 11.59 ? 185 LEU A N    1 
ATOM   1772 N  N    B LEU A 1 184 ? -22.198 -4.340  13.831  0.50 11.53 ? 185 LEU A N    1 
ATOM   1773 C  CA   A LEU A 1 184 ? -22.572 -4.481  15.306  0.50 9.70  ? 185 LEU A CA   1 
ATOM   1774 C  CA   B LEU A 1 184 ? -22.313 -4.515  15.250  0.50 10.27 ? 185 LEU A CA   1 
ATOM   1775 C  C    A LEU A 1 184 ? -23.465 -5.626  15.918  0.50 7.82  ? 185 LEU A C    1 
ATOM   1776 C  C    B LEU A 1 184 ? -22.869 -5.921  15.467  0.50 9.92  ? 185 LEU A C    1 
ATOM   1777 O  O    A LEU A 1 184 ? -24.502 -5.974  15.380  0.50 7.98  ? 185 LEU A O    1 
ATOM   1778 O  O    B LEU A 1 184 ? -23.580 -6.522  14.597  0.50 12.11 ? 185 LEU A O    1 
ATOM   1779 C  CB   A LEU A 1 184 ? -23.268 -3.161  15.682  0.50 8.54  ? 185 LEU A CB   1 
ATOM   1780 C  CB   B LEU A 1 184 ? -23.250 -3.402  15.877  0.50 9.89  ? 185 LEU A CB   1 
ATOM   1781 C  CG   A LEU A 1 184 ? -22.601 -1.893  15.194  0.50 6.83  ? 185 LEU A CG   1 
ATOM   1782 C  CG   B LEU A 1 184 ? -22.683 -2.009  15.587  0.50 8.99  ? 185 LEU A CG   1 
ATOM   1783 C  CD1  A LEU A 1 184 ? -23.310 -0.679  15.859  0.50 9.41  ? 185 LEU A CD1  1 
ATOM   1784 C  CD1  B LEU A 1 184 ? -23.681 -0.889  15.918  0.50 15.20 ? 185 LEU A CD1  1 
ATOM   1785 C  CD2  A LEU A 1 184 ? -21.132 -1.832  15.615  0.50 7.94  ? 185 LEU A CD2  1 
ATOM   1786 C  CD2  B LEU A 1 184 ? -21.377 -1.738  16.328  0.50 11.64 ? 185 LEU A CD2  1 
ATOM   1787 N  N    A PRO A 1 185 ? -23.001 -6.245  17.016  0.50 7.93  ? 186 PRO A N    1 
ATOM   1788 N  N    B PRO A 1 185 ? -22.650 -6.439  16.670  0.50 9.35  ? 186 PRO A N    1 
ATOM   1789 C  CA   A PRO A 1 185 ? -23.692 -7.367  17.651  0.50 7.39  ? 186 PRO A CA   1 
ATOM   1790 C  CA   B PRO A 1 185 ? -23.503 -7.582  17.067  0.50 9.14  ? 186 PRO A CA   1 
ATOM   1791 C  C    A PRO A 1 185 ? -24.940 -6.866  18.317  0.50 7.92  ? 186 PRO A C    1 
ATOM   1792 C  C    B PRO A 1 185 ? -24.733 -7.051  17.702  0.50 7.57  ? 186 PRO A C    1 
ATOM   1793 O  O    A PRO A 1 185 ? -25.081 -5.656  18.540  0.50 7.81  ? 186 PRO A O    1 
ATOM   1794 O  O    B PRO A 1 185 ? -24.975 -5.876  17.657  0.50 8.51  ? 186 PRO A O    1 
ATOM   1795 C  CB   A PRO A 1 185 ? -22.649 -7.894  18.693  0.50 8.57  ? 186 PRO A CB   1 
ATOM   1796 C  CB   B PRO A 1 185 ? -22.606 -8.281  18.148  0.50 8.79  ? 186 PRO A CB   1 
ATOM   1797 C  CG   A PRO A 1 185 ? -21.768 -6.651  18.993  0.50 8.58  ? 186 PRO A CG   1 
ATOM   1798 C  CG   B PRO A 1 185 ? -22.012 -7.035  18.847  0.50 7.52  ? 186 PRO A CG   1 
ATOM   1799 C  CD   A PRO A 1 185 ? -21.705 -5.843  17.670  0.50 9.29  ? 186 PRO A CD   1 
ATOM   1800 C  CD   B PRO A 1 185 ? -21.611 -6.099  17.690  0.50 9.28  ? 186 PRO A CD   1 
ATOM   1801 N  N    A GLU A 1 186 ? -25.873 -7.759  18.656  0.50 10.01 ? 187 GLU A N    1 
ATOM   1802 N  N    B GLU A 1 186 ? -25.513 -7.949  18.318  0.50 11.30 ? 187 GLU A N    1 
ATOM   1803 C  CA   A GLU A 1 186 ? -27.043 -7.317  19.267  0.50 10.66 ? 187 GLU A CA   1 
ATOM   1804 C  CA   B GLU A 1 186 ? -26.753 -7.545  18.994  0.50 11.61 ? 187 GLU A CA   1 
ATOM   1805 C  C    A GLU A 1 186 ? -26.803 -6.674  20.579  0.50 10.47 ? 187 GLU A C    1 
ATOM   1806 C  C    B GLU A 1 186 ? -26.557 -6.688  20.274  0.50 11.23 ? 187 GLU A C    1 
ATOM   1807 O  O    A GLU A 1 186 ? -27.476 -5.677  20.988  0.50 11.08 ? 187 GLU A O    1 
ATOM   1808 O  O    B GLU A 1 186 ? -27.084 -5.526  20.304  0.50 11.79 ? 187 GLU A O    1 
ATOM   1809 C  CB   A GLU A 1 186 ? -28.029 -8.487  19.367  0.50 12.35 ? 187 GLU A CB   1 
ATOM   1810 C  CB   B GLU A 1 186 ? -27.533 -8.801  19.395  0.50 12.68 ? 187 GLU A CB   1 
ATOM   1811 C  CG   A GLU A 1 186 ? -28.906 -8.503  20.590  0.50 13.86 ? 187 GLU A CG   1 
ATOM   1812 C  CG   B GLU A 1 186 ? -28.618 -9.229  18.430  0.50 15.92 ? 187 GLU A CG   1 
ATOM   1813 C  CD   A GLU A 1 186 ? -29.556 -9.858  20.808  0.50 16.35 ? 187 GLU A CD   1 
ATOM   1814 C  CD   B GLU A 1 186 ? -29.212 -10.582 18.790  0.50 12.67 ? 187 GLU A CD   1 
ATOM   1815 O  OE1  A GLU A 1 186 ? -29.430 -10.737 19.926  0.50 14.35 ? 187 GLU A OE1  1 
ATOM   1816 O  OE1  B GLU A 1 186 ? -28.977 -11.062 19.922  0.50 19.78 ? 187 GLU A OE1  1 
ATOM   1817 O  OE2  A GLU A 1 186 ? -30.189 -10.048 21.866  0.50 19.53 ? 187 GLU A OE2  1 
ATOM   1818 O  OE2  B GLU A 1 186 ? -29.916 -11.167 17.940  0.50 19.15 ? 187 GLU A OE2  1 
ATOM   1819 N  N    . SER A 1 187 ? -25.837 -7.228  21.295  1.00 11.56 ? 188 SER A N    1 
ATOM   1820 C  CA   . SER A 1 187 ? -25.648 -6.645  22.586  1.00 12.65 ? 188 SER A CA   1 
ATOM   1821 C  C    . SER A 1 187 ? -24.473 -5.604  22.593  1.00 12.21 ? 188 SER A C    1 
ATOM   1822 O  O    . SER A 1 187 ? -23.451 -5.884  21.989  1.00 12.86 ? 188 SER A O    1 
ATOM   1823 C  CB   . SER A 1 187 ? -25.276 -7.664  23.591  1.00 14.30 ? 188 SER A CB   1 
ATOM   1824 O  OG   . SER A 1 187 ? -24.978 -7.135  24.888  1.00 12.74 ? 188 SER A OG   1 
ATOM   1825 N  N    . LEU A 1 188 ? -24.648 -4.561  23.356  1.00 10.61 ? 189 LEU A N    1 
ATOM   1826 C  CA   . LEU A 1 188 ? -23.562 -3.568  23.530  1.00 11.01 ? 189 LEU A CA   1 
ATOM   1827 C  C    . LEU A 1 188 ? -22.966 -3.683  24.942  1.00 10.63 ? 189 LEU A C    1 
ATOM   1828 O  O    . LEU A 1 188 ? -22.238 -2.787  25.360  1.00 12.96 ? 189 LEU A O    1 
ATOM   1829 C  CB   . LEU A 1 188 ? -24.013 -2.077  23.254  1.00 12.46 ? 189 LEU A CB   1 
ATOM   1830 C  CG   . LEU A 1 188 ? -24.451 -1.755  21.806  1.00 14.06 ? 189 LEU A CG   1 
ATOM   1831 C  CD1  . LEU A 1 188 ? -25.015 -0.308  21.791  1.00 16.79 ? 189 LEU A CD1  1 
ATOM   1832 C  CD2  . LEU A 1 188 ? -23.366 -1.995  20.771  1.00 18.17 ? 189 LEU A CD2  1 
ATOM   1833 N  N    . ASP A 1 189 ? -23.052 -4.852  25.595  1.00 11.66 ? 190 ASP A N    1 
ATOM   1834 C  CA   . ASP A 1 189 ? -22.306 -5.111  26.849  1.00 10.37 ? 190 ASP A CA   1 
ATOM   1835 C  C    . ASP A 1 189 ? -20.781 -5.072  26.517  1.00 9.43  ? 190 ASP A C    1 
ATOM   1836 O  O    . ASP A 1 189 ? -20.364 -5.534  25.466  1.00 8.94  ? 190 ASP A O    1 
ATOM   1837 C  CB   . ASP A 1 189 ? -22.639 -6.516  27.365  1.00 13.53 ? 190 ASP A CB   1 
ATOM   1838 C  CG   . ASP A 1 189 ? -24.043 -6.568  28.018  1.00 18.76 ? 190 ASP A CG   1 
ATOM   1839 O  OD1  . ASP A 1 189 ? -24.610 -5.539  28.275  1.00 20.25 ? 190 ASP A OD1  1 
ATOM   1840 O  OD2  . ASP A 1 189 ? -24.469 -7.688  28.253  1.00 24.06 ? 190 ASP A OD2  1 
ATOM   1841 N  N    . TYR A 1 190 ? -20.013 -4.500  27.439  1.00 8.77  ? 191 TYR A N    1 
ATOM   1842 C  CA   . TYR A 1 190 ? -18.627 -4.212  27.089  1.00 8.17  ? 191 TYR A CA   1 
ATOM   1843 C  C    . TYR A 1 190 ? -17.731 -4.313  28.271  1.00 6.90  ? 191 TYR A C    1 
ATOM   1844 O  O    . TYR A 1 190 ? -18.145 -4.146  29.445  1.00 9.05  ? 191 TYR A O    1 
ATOM   1845 C  CB   . TYR A 1 190 ? -18.521 -2.852  26.410  1.00 8.81  ? 191 TYR A CB   1 
ATOM   1846 C  CG   . TYR A 1 190 ? -18.902 -1.658  27.309  1.00 8.82  ? 191 TYR A CG   1 
ATOM   1847 C  CD1  . TYR A 1 190 ? -17.970 -1.046  28.191  1.00 9.59  ? 191 TYR A CD1  1 
ATOM   1848 C  CD2  . TYR A 1 190 ? -20.200 -1.184  27.307  1.00 9.67  ? 191 TYR A CD2  1 
ATOM   1849 C  CE1  . TYR A 1 190 ? -18.383 -0.068  29.015  1.00 9.64  ? 191 TYR A CE1  1 
ATOM   1850 C  CE2  . TYR A 1 190 ? -20.588 -0.078  28.081  1.00 10.16 ? 191 TYR A CE2  1 
ATOM   1851 C  CZ   . TYR A 1 190 ? -19.663 0.442   28.971  1.00 10.43 ? 191 TYR A CZ   1 
ATOM   1852 O  OH   . TYR A 1 190 ? -20.018 1.469   29.826  1.00 11.85 ? 191 TYR A OH   1 
ATOM   1853 N  N    . TRP A 1 191 ? -16.411 -4.429  28.015  1.00 7.42  ? 192 TRP A N    1 
ATOM   1854 C  CA   . TRP A 1 191 ? -15.382 -4.156  28.985  1.00 7.41  ? 192 TRP A CA   1 
ATOM   1855 C  C    . TRP A 1 191 ? -14.698 -2.865  28.567  1.00 7.01  ? 192 TRP A C    1 
ATOM   1856 O  O    . TRP A 1 191 ? -14.658 -2.533  27.370  1.00 7.97  ? 192 TRP A O    1 
ATOM   1857 C  CB   . TRP A 1 191 ? -14.303 -5.254  28.918  1.00 7.78  ? 192 TRP A CB   1 
ATOM   1858 C  CG   . TRP A 1 191 ? -14.849 -6.618  29.354  1.00 9.24  ? 192 TRP A CG   1 
ATOM   1859 C  CD1  . TRP A 1 191 ? -15.047 -7.057  30.668  1.00 9.78  ? 192 TRP A CD1  1 
ATOM   1860 C  CD2  . TRP A 1 191 ? -15.128 -7.750  28.479  1.00 7.70  ? 192 TRP A CD2  1 
ATOM   1861 N  NE1  . TRP A 1 191 ? -15.500 -8.387  30.633  1.00 9.53  ? 192 TRP A NE1  1 
ATOM   1862 C  CE2  . TRP A 1 191 ? -15.543 -8.803  29.310  1.00 9.44  ? 192 TRP A CE2  1 
ATOM   1863 C  CE3  . TRP A 1 191 ? -15.078 -7.946  27.095  1.00 8.73  ? 192 TRP A CE3  1 
ATOM   1864 C  CZ2  . TRP A 1 191 ? -15.849 -10.077 28.808  1.00 9.13  ? 192 TRP A CZ2  1 
ATOM   1865 C  CZ3  . TRP A 1 191 ? -15.348 -9.248  26.574  1.00 10.01 ? 192 TRP A CZ3  1 
ATOM   1866 C  CH2  . TRP A 1 191 ? -15.747 -10.244 27.464  1.00 9.82  ? 192 TRP A CH2  1 
ATOM   1867 N  N    . THR A 1 192 ? -14.082 -2.202  29.530  1.00 6.32  ? 193 THR A N    1 
ATOM   1868 C  CA   . THR A 1 192 ? -13.372 -0.947  29.120  1.00 6.81  ? 193 THR A CA   1 
ATOM   1869 C  C    . THR A 1 192 ? -12.123 -0.767  30.025  1.00 7.08  ? 193 THR A C    1 
ATOM   1870 O  O    . THR A 1 192 ? -12.098 -1.149  31.196  1.00 7.40  ? 193 THR A O    1 
ATOM   1871 C  CB   . THR A 1 192 ? -14.359 0.290   29.267  1.00 7.30  ? 193 THR A CB   1 
ATOM   1872 O  OG1  . THR A 1 192 ? -13.627 1.476   28.879  1.00 7.53  ? 193 THR A OG1  1 
ATOM   1873 C  CG2  . THR A 1 192 ? -14.832 0.475   30.672  1.00 8.72  ? 193 THR A CG2  1 
ATOM   1874 N  N    . TYR A 1 193 ? -11.069 -0.155  29.455  1.00 6.86  ? 194 TYR A N    1 
ATOM   1875 C  CA   . TYR A 1 193 ? -9.893  0.124   30.201  1.00 6.25  ? 194 TYR A CA   1 
ATOM   1876 C  C    . TYR A 1 193 ? -9.118  1.164   29.440  1.00 6.32  ? 194 TYR A C    1 
ATOM   1877 O  O    . TYR A 1 193 ? -9.356  1.346   28.208  1.00 6.46  ? 194 TYR A O    1 
ATOM   1878 C  CB   . TYR A 1 193 ? -9.014  -1.154  30.402  1.00 7.37  ? 194 TYR A CB   1 
ATOM   1879 C  CG   . TYR A 1 193 ? -8.359  -1.618  29.130  1.00 6.38  ? 194 TYR A CG   1 
ATOM   1880 C  CD1  . TYR A 1 193 ? -9.024  -2.377  28.122  1.00 6.81  ? 194 TYR A CD1  1 
ATOM   1881 C  CD2  . TYR A 1 193 ? -7.043  -1.296  28.934  1.00 7.11  ? 194 TYR A CD2  1 
ATOM   1882 C  CE1  . TYR A 1 193 ? -8.402  -2.692  26.918  1.00 7.12  ? 194 TYR A CE1  1 
ATOM   1883 C  CE2  . TYR A 1 193 ? -6.364  -1.634  27.716  1.00 6.88  ? 194 TYR A CE2  1 
ATOM   1884 C  CZ   . TYR A 1 193 ? -7.058  -2.313  26.750  1.00 6.58  ? 194 TYR A CZ   1 
ATOM   1885 O  OH   . TYR A 1 193 ? -6.461  -2.579  25.539  1.00 6.71  ? 194 TYR A OH   1 
ATOM   1886 N  N    . PRO A 1 194 ? -8.150  1.895   30.086  1.00 6.27  ? 195 PRO A N    1 
ATOM   1887 C  CA   . PRO A 1 194 ? -7.366  2.938   29.397  1.00 6.68  ? 195 PRO A CA   1 
ATOM   1888 C  C    . PRO A 1 194 ? -6.177  2.280   28.727  1.00 6.56  ? 195 PRO A C    1 
ATOM   1889 O  O    . PRO A 1 194 ? -5.396  1.476   29.360  1.00 8.32  ? 195 PRO A O    1 
ATOM   1890 C  CB   . PRO A 1 194 ? -6.854  3.773   30.547  1.00 9.25  ? 195 PRO A CB   1 
ATOM   1891 C  CG   . PRO A 1 194 ? -6.851  2.885   31.818  1.00 9.39  ? 195 PRO A CG   1 
ATOM   1892 C  CD   . PRO A 1 194 ? -7.988  1.880   31.551  1.00 8.55  ? 195 PRO A CD   1 
ATOM   1893 N  N    . GLY A 1 195 ? -5.977  2.566   27.428  1.00 6.52  ? 196 GLY A N    1 
ATOM   1894 C  CA   . GLY A 1 195 ? -4.792  1.862   26.742  1.00 7.72  ? 196 GLY A CA   1 
ATOM   1895 C  C    . GLY A 1 195 ? -4.261  2.806   25.621  1.00 6.97  ? 196 GLY A C    1 
ATOM   1896 O  O    . GLY A 1 195 ? -4.168  4.062   25.800  1.00 7.69  ? 196 GLY A O    1 
ATOM   1897 N  N    . SER A 1 196 ? -3.865  2.174   24.538  1.00 6.47  ? 197 SER A N    1 
ATOM   1898 C  CA   . SER A 1 196 ? -3.046  2.875   23.530  1.00 5.80  ? 197 SER A CA   1 
ATOM   1899 C  C    . SER A 1 196 ? -3.485  2.456   22.175  1.00 7.16  ? 197 SER A C    1 
ATOM   1900 O  O    . SER A 1 196 ? -4.260  1.485   21.957  1.00 6.86  ? 197 SER A O    1 
ATOM   1901 C  CB   . SER A 1 196 ? -1.565  2.395   23.704  1.00 7.41  ? 197 SER A CB   1 
ATOM   1902 O  OG   . SER A 1 196 ? -1.331  1.041   23.279  1.00 6.98  ? 197 SER A OG   1 
ATOM   1903 N  N    . LEU A 1 197 ? -2.901  3.062   21.165  1.00 6.96  ? 198 LEU A N    1 
ATOM   1904 C  CA   . LEU A 1 197 ? -2.955  2.554   19.797  1.00 6.66  ? 198 LEU A CA   1 
ATOM   1905 C  C    . LEU A 1 197 ? -2.249  1.192   19.864  1.00 6.52  ? 198 LEU A C    1 
ATOM   1906 O  O    . LEU A 1 197 ? -1.251  1.007   20.603  1.00 7.31  ? 198 LEU A O    1 
ATOM   1907 C  CB   . LEU A 1 197 ? -2.154  3.427   18.833  1.00 8.28  ? 198 LEU A CB   1 
ATOM   1908 C  CG   . LEU A 1 197 ? -2.439  4.922   18.810  1.00 10.87 ? 198 LEU A CG   1 
ATOM   1909 C  CD1  . LEU A 1 197 ? -1.564  5.625   17.799  1.00 12.57 ? 198 LEU A CD1  1 
ATOM   1910 C  CD2  . LEU A 1 197 ? -3.916  5.311   18.640  1.00 12.34 ? 198 LEU A CD2  1 
ATOM   1911 N  N    . THR A 1 198 ? -2.745  0.215   19.076  1.00 6.73  ? 199 THR A N    1 
ATOM   1912 C  CA   . THR A 1 198 ? -2.036  -1.109  18.997  1.00 6.54  ? 199 THR A CA   1 
ATOM   1913 C  C    . THR A 1 198 ? -1.048  -1.121  17.871  1.00 7.57  ? 199 THR A C    1 
ATOM   1914 O  O    . THR A 1 198 ? -0.395  -2.179  17.692  1.00 7.46  ? 199 THR A O    1 
ATOM   1915 C  CB   . THR A 1 198 ? -3.052  -2.210  18.830  1.00 7.37  ? 199 THR A CB   1 
ATOM   1916 O  OG1  . THR A 1 198 ? -3.623  -2.099  17.547  1.00 6.07  ? 199 THR A OG1  1 
ATOM   1917 C  CG2  . THR A 1 198 ? -4.067  -2.245  19.951  1.00 7.32  ? 199 THR A CG2  1 
ATOM   1918 N  N    . THR A 1 199 ? -0.861  -0.056  17.125  1.00 8.06  ? 200 THR A N    1 
ATOM   1919 C  CA   . THR A 1 199 ? 0.089   0.051   16.097  1.00 8.23  ? 200 THR A CA   1 
ATOM   1920 C  C    . THR A 1 199 ? 0.949   1.258   16.376  1.00 8.87  ? 200 THR A C    1 
ATOM   1921 O  O    . THR A 1 199 ? 0.515   2.238   17.013  1.00 8.86  ? 200 THR A O    1 
ATOM   1922 C  CB   . THR A 1 199 ? -0.515  0.358   14.717  1.00 9.32  ? 200 THR A CB   1 
ATOM   1923 O  OG1  . THR A 1 199 ? -1.340  1.529   14.801  1.00 13.10 ? 200 THR A OG1  1 
ATOM   1924 C  CG2  . THR A 1 199 ? -1.433  -0.821  14.185  1.00 10.61 ? 200 THR A CG2  1 
ATOM   1925 N  N    . PRO A 1 200 ? 2.217   1.254   15.975  1.00 9.21  ? 201 PRO A N    1 
ATOM   1926 C  CA   . PRO A 1 200 ? 2.997   2.532   16.048  1.00 9.25  ? 201 PRO A CA   1 
ATOM   1927 C  C    . PRO A 1 200 ? 2.139   3.654   15.526  1.00 10.16 ? 201 PRO A C    1 
ATOM   1928 O  O    . PRO A 1 200 ? 1.506   3.531   14.479  1.00 10.39 ? 201 PRO A O    1 
ATOM   1929 C  CB   . PRO A 1 200 ? 4.212   2.168   15.151  1.00 9.49  ? 201 PRO A CB   1 
ATOM   1930 C  CG   . PRO A 1 200 ? 4.430   0.675   15.378  1.00 10.11 ? 201 PRO A CG   1 
ATOM   1931 C  CD   . PRO A 1 200 ? 2.970   0.102   15.300  1.00 8.96  ? 201 PRO A CD   1 
ATOM   1932 N  N    . PRO A 1 201 ? 2.168   4.804   16.194  1.00 9.63  ? 202 PRO A N    1 
ATOM   1933 C  CA   . PRO A 1 201 ? 3.171   5.135   17.211  1.00 9.09  ? 202 PRO A CA   1 
ATOM   1934 C  C    . PRO A 1 201 ? 2.829   4.715   18.641  1.00 9.96  ? 202 PRO A C    1 
ATOM   1935 O  O    . PRO A 1 201 ? 3.490   5.167   19.568  1.00 10.59 ? 202 PRO A O    1 
ATOM   1936 C  CB   . PRO A 1 201 ? 3.263   6.665   17.115  1.00 12.46 ? 202 PRO A CB   1 
ATOM   1937 C  CG   . PRO A 1 201 ? 1.934   7.082   16.605  1.00 13.63 ? 202 PRO A CG   1 
ATOM   1938 C  CD   . PRO A 1 201 ? 1.514   6.005   15.650  1.00 11.16 ? 202 PRO A CD   1 
ATOM   1939 N  N    . LEU A 1 202 ? 1.826   3.861   18.814  1.00 8.31  ? 203 LEU A N    1 
ATOM   1940 C  CA   . LEU A 1 202 ? 1.527   3.286   20.126  1.00 8.17  ? 203 LEU A CA   1 
ATOM   1941 C  C    . LEU A 1 202 ? 1.202   4.326   21.196  1.00 8.30  ? 203 LEU A C    1 
ATOM   1942 O  O    . LEU A 1 202 ? 1.441   4.110   22.379  1.00 7.43  ? 203 LEU A O    1 
ATOM   1943 C  CB   . LEU A 1 202 ? 2.687   2.400   20.590  1.00 8.90  ? 203 LEU A CB   1 
ATOM   1944 C  CG   . LEU A 1 202 ? 3.054   1.261   19.632  1.00 8.90  ? 203 LEU A CG   1 
ATOM   1945 C  CD1  . LEU A 1 202 ? 4.321   0.561   20.088  1.00 11.18 ? 203 LEU A CD1  1 
ATOM   1946 C  CD2  . LEU A 1 202 ? 1.906   0.264   19.515  1.00 9.83  ? 203 LEU A CD2  1 
ATOM   1947 N  N    . LEU A 1 203 ? 0.634   5.444   20.759  1.00 8.86  ? 204 LEU A N    1 
ATOM   1948 C  CA   . LEU A 1 203 ? 0.307   6.602   21.661  1.00 9.29  ? 204 LEU A CA   1 
ATOM   1949 C  C    . LEU A 1 203 ? -0.783  6.170   22.690  1.00 7.71  ? 204 LEU A C    1 
ATOM   1950 O  O    . LEU A 1 203 ? -1.721  5.422   22.403  1.00 8.18  ? 204 LEU A O    1 
ATOM   1951 C  CB   . LEU A 1 203 ? -0.204  7.822   20.935  1.00 9.27  ? 204 LEU A CB   1 
ATOM   1952 C  CG   . LEU A 1 203 ? 0.901   8.328   19.941  1.00 11.45 ? 204 LEU A CG   1 
ATOM   1953 C  CD1  . LEU A 1 203 ? 0.302   9.466   19.045  1.00 12.29 ? 204 LEU A CD1  1 
ATOM   1954 C  CD2  . LEU A 1 203 ? 2.152   8.975   20.794  1.00 15.97 ? 204 LEU A CD2  1 
ATOM   1955 N  N    . GLU A 1 204 ? -0.529  6.559   23.970  1.00 7.86  ? 205 GLU A N    1 
ATOM   1956 C  CA   . GLU A 1 204 ? -1.367  6.191   25.076  1.00 9.07  ? 205 GLU A CA   1 
ATOM   1957 C  C    . GLU A 1 204 ? -2.564  7.184   25.190  1.00 9.87  ? 205 GLU A C    1 
ATOM   1958 O  O    . GLU A 1 204 ? -2.667  7.905   26.179  1.00 9.82  ? 205 GLU A O    1 
ATOM   1959 C  CB   . GLU A 1 204 ? -0.529  6.072   26.348  1.00 9.15  ? 205 GLU A CB   1 
ATOM   1960 C  CG   . GLU A 1 204 ? 0.385   4.820   26.181  1.00 10.03 ? 205 GLU A CG   1 
ATOM   1961 C  CD   . GLU A 1 204 ? 1.281   4.576   27.389  1.00 11.49 ? 205 GLU A CD   1 
ATOM   1962 O  OE1  . GLU A 1 204 ? 1.645   5.477   28.123  1.00 12.49 ? 205 GLU A OE1  1 
ATOM   1963 O  OE2  . GLU A 1 204 ? 1.715   3.373   27.563  1.00 10.62 ? 205 GLU A OE2  1 
ATOM   1964 N  N    . CYS A 1 205 ? -3.426  7.087   24.207  1.00 7.89  ? 206 CYS A N    1 
ATOM   1965 C  CA   . CYS A 1 205 ? -4.500  8.095   24.043  1.00 7.43  ? 206 CYS A CA   1 
ATOM   1966 C  C    . CYS A 1 205 ? -5.842  7.449   23.897  1.00 7.04  ? 206 CYS A C    1 
ATOM   1967 O  O    . CYS A 1 205 ? -6.796  8.155   23.568  1.00 8.47  ? 206 CYS A O    1 
ATOM   1968 C  CB   . CYS A 1 205 ? -4.300  8.904   22.780  1.00 10.62 ? 206 CYS A CB   1 
ATOM   1969 S  SG   . CYS A 1 205 ? -4.142  7.960   21.283  1.00 9.50  ? 206 CYS A SG   1 
ATOM   1970 N  N    . VAL A 1 206 ? -5.999  6.148   24.218  1.00 6.92  ? 207 VAL A N    1 
ATOM   1971 C  CA   . VAL A 1 206 ? -7.274  5.483   23.862  1.00 6.81  ? 207 VAL A CA   1 
ATOM   1972 C  C    . VAL A 1 206 ? -8.020  5.019   25.075  1.00 6.31  ? 207 VAL A C    1 
ATOM   1973 O  O    . VAL A 1 206 ? -7.448  4.339   25.942  1.00 8.09  ? 207 VAL A O    1 
ATOM   1974 C  CB   . VAL A 1 206 ? -6.975  4.197   22.997  1.00 7.40  ? 207 VAL A CB   1 
ATOM   1975 C  CG1  . VAL A 1 206 ? -8.283  3.473   22.656  1.00 6.81  ? 207 VAL A CG1  1 
ATOM   1976 C  CG2  . VAL A 1 206 ? -6.201  4.541   21.732  1.00 8.12  ? 207 VAL A CG2  1 
ATOM   1977 N  N    . THR A 1 207 ? -9.333  5.321   25.131  1.00 6.35  ? 208 THR A N    1 
ATOM   1978 C  CA   . THR A 1 207 ? -10.217 4.528   25.967  1.00 6.26  ? 208 THR A CA   1 
ATOM   1979 C  C    . THR A 1 207 ? -10.829 3.414   25.180  1.00 6.11  ? 208 THR A C    1 
ATOM   1980 O  O    . THR A 1 207 ? -11.444 3.567   24.158  1.00 6.40  ? 208 THR A O    1 
ATOM   1981 C  CB   . THR A 1 207 ? -11.423 5.417   26.451  1.00 6.81  ? 208 THR A CB   1 
ATOM   1982 O  OG1  . THR A 1 207 ? -10.886 6.525   27.199  1.00 8.03  ? 208 THR A OG1  1 
ATOM   1983 C  CG2  . THR A 1 207 ? -12.354 4.623   27.323  1.00 8.64  ? 208 THR A CG2  1 
ATOM   1984 N  N    . TRP A 1 208 ? -10.378 2.205   25.564  1.00 6.17  ? 209 TRP A N    1 
ATOM   1985 C  CA   . TRP A 1 208 ? -10.884 0.997   24.861  1.00 6.87  ? 209 TRP A CA   1 
ATOM   1986 C  C    . TRP A 1 208 ? -12.211 0.529   25.391  1.00 5.87  ? 209 TRP A C    1 
ATOM   1987 O  O    . TRP A 1 208 ? -12.436 0.471   26.607  1.00 6.70  ? 209 TRP A O    1 
ATOM   1988 C  CB   . TRP A 1 208 ? -9.823  -0.156  25.076  1.00 7.56  ? 209 TRP A CB   1 
ATOM   1989 C  CG   . TRP A 1 208 ? -8.706  -0.072  24.081  1.00 5.58  ? 209 TRP A CG   1 
ATOM   1990 C  CD1  . TRP A 1 208 ? -7.449  0.554   24.295  1.00 6.07  ? 209 TRP A CD1  1 
ATOM   1991 C  CD2  . TRP A 1 208 ? -8.786  -0.428  22.708  1.00 6.14  ? 209 TRP A CD2  1 
ATOM   1992 N  NE1  . TRP A 1 208 ? -6.792  0.552   23.098  1.00 7.06  ? 209 TRP A NE1  1 
ATOM   1993 C  CE2  . TRP A 1 208 ? -7.493  -0.099  22.113  1.00 6.21  ? 209 TRP A CE2  1 
ATOM   1994 C  CE3  . TRP A 1 208 ? -9.773  -1.116  21.934  1.00 6.26  ? 209 TRP A CE3  1 
ATOM   1995 C  CZ2  . TRP A 1 208 ? -7.283  -0.247  20.765  1.00 6.91  ? 209 TRP A CZ2  1 
ATOM   1996 C  CZ3  . TRP A 1 208 ? -9.509  -1.335  20.623  1.00 6.81  ? 209 TRP A CZ3  1 
ATOM   1997 C  CH2  . TRP A 1 208 ? -8.237  -0.926  20.035  1.00 7.24  ? 209 TRP A CH2  1 
ATOM   1998 N  N    . ILE A 1 209 ? -13.072 0.222   24.440  1.00 6.28  ? 210 ILE A N    1 
ATOM   1999 C  CA   . ILE A 1 209 ? -14.411 -0.303  24.791  1.00 7.37  ? 210 ILE A CA   1 
ATOM   2000 C  C    . ILE A 1 209 ? -14.602 -1.588  23.931  1.00 6.00  ? 210 ILE A C    1 
ATOM   2001 O  O    . ILE A 1 209 ? -14.686 -1.494  22.703  1.00 7.67  ? 210 ILE A O    1 
ATOM   2002 C  CB   . ILE A 1 209 ? -15.514 0.710   24.403  1.00 7.57  ? 210 ILE A CB   1 
ATOM   2003 C  CG1  . ILE A 1 209 ? -15.245 1.965   25.214  1.00 9.54  ? 210 ILE A CG1  1 
ATOM   2004 C  CG2  . ILE A 1 209 ? -16.894 0.086   24.701  1.00 9.34  ? 210 ILE A CG2  1 
ATOM   2005 C  CD1  . ILE A 1 209 ? -16.080 3.164   24.752  1.00 11.21 ? 210 ILE A CD1  1 
ATOM   2006 N  N    . VAL A 1 210 ? -14.441 -2.730  24.568  1.00 7.53  ? 211 VAL A N    1 
ATOM   2007 C  CA   . VAL A 1 210 ? -14.458 -4.067  23.837  1.00 6.27  ? 211 VAL A CA   1 
ATOM   2008 C  C    . VAL A 1 210 ? -15.779 -4.743  24.111  1.00 6.11  ? 211 VAL A C    1 
ATOM   2009 O  O    . VAL A 1 210 ? -16.080 -4.983  25.262  1.00 7.09  ? 211 VAL A O    1 
ATOM   2010 C  CB   . VAL A 1 210 ? -13.212 -4.891  24.313  1.00 6.54  ? 211 VAL A CB   1 
ATOM   2011 C  CG1  . VAL A 1 210 ? -13.256 -6.248  23.578  1.00 7.65  ? 211 VAL A CG1  1 
ATOM   2012 C  CG2  . VAL A 1 210 ? -11.907 -4.138  24.037  1.00 8.99  ? 211 VAL A CG2  1 
ATOM   2013 N  N    . LEU A 1 211 ? -16.487 -5.033  23.035  1.00 7.29  ? 212 LEU A N    1 
ATOM   2014 C  CA   . LEU A 1 211 ? -17.814 -5.689  23.258  1.00 7.79  ? 212 LEU A CA   1 
ATOM   2015 C  C    . LEU A 1 211 ? -17.573 -7.141  23.607  1.00 7.07  ? 212 LEU A C    1 
ATOM   2016 O  O    . LEU A 1 211 ? -16.756 -7.886  23.052  1.00 8.32  ? 212 LEU A O    1 
ATOM   2017 C  CB   . LEU A 1 211 ? -18.610 -5.585  21.905  1.00 7.78  ? 212 LEU A CB   1 
ATOM   2018 C  CG   . LEU A 1 211 ? -18.943 -4.139  21.513  1.00 10.30 ? 212 LEU A CG   1 
ATOM   2019 C  CD1  . LEU A 1 211 ? -20.025 -4.275  20.346  1.00 12.10 ? 212 LEU A CD1  1 
ATOM   2020 C  CD2  . LEU A 1 211 ? -19.537 -3.387  22.666  1.00 9.87  ? 212 LEU A CD2  1 
ATOM   2021 N  N    . LYS A 1 212 ? -18.484 -7.611  24.478  1.00 8.46  ? 213 LYS A N    1 
ATOM   2022 C  CA   . LYS A 1 212 ? -18.378 -8.996  24.843  1.00 10.26 ? 213 LYS A CA   1 
ATOM   2023 C  C    . LYS A 1 212 ? -18.903 -9.934  23.779  1.00 7.61  ? 213 LYS A C    1 
ATOM   2024 O  O    . LYS A 1 212 ? -18.389 -11.027 23.625  1.00 10.01 ? 213 LYS A O    1 
ATOM   2025 C  CB   . LYS A 1 212 ? -19.190 -9.226  26.107  1.00 11.50 ? 213 LYS A CB   1 
ATOM   2026 C  CG   . LYS A 1 212 ? -19.319 -10.738 26.474  1.00 14.23 ? 213 LYS A CG   1 
ATOM   2027 C  CD   . LYS A 1 212 ? -20.031 -10.851 27.685  1.00 21.68 ? 213 LYS A CD   1 
ATOM   2028 C  CE   . LYS A 1 212 ? -20.180 -12.269 28.128  1.00 26.10 ? 213 LYS A CE   1 
ATOM   2029 N  NZ   . LYS A 1 212 ? -20.978 -12.410 29.458  1.00 34.09 ? 213 LYS A NZ   1 
ATOM   2030 N  N    . GLU A 1 213 ? -19.933 -9.513  23.006  1.00 8.18  ? 214 GLU A N    1 
ATOM   2031 C  CA   . GLU A 1 213 ? -20.557 -10.429 21.974  1.00 8.47  ? 214 GLU A CA   1 
ATOM   2032 C  C    . GLU A 1 213 ? -19.802 -10.289 20.665  1.00 7.72  ? 214 GLU A C    1 
ATOM   2033 O  O    . GLU A 1 213 ? -19.708 -9.215  20.130  1.00 8.42  ? 214 GLU A O    1 
ATOM   2034 C  CB   . GLU A 1 213 ? -22.015 -10.011 21.810  1.00 9.65  ? 214 GLU A CB   1 
ATOM   2035 C  CG   . GLU A 1 213 ? -22.700 -11.016 20.868  1.00 11.35 ? 214 GLU A CG   1 
ATOM   2036 C  CD   . GLU A 1 213 ? -24.152 -10.722 20.616  1.00 17.59 ? 214 GLU A CD   1 
ATOM   2037 O  OE1  . GLU A 1 213 ? -24.777 -9.915  21.274  1.00 14.10 ? 214 GLU A OE1  1 
ATOM   2038 O  OE2  . GLU A 1 213 ? -24.690 -11.599 19.912  1.00 26.38 ? 214 GLU A OE2  1 
ATOM   2039 N  N    . PRO A 1 214 ? -19.195 -11.397 20.212  1.00 7.28  ? 215 PRO A N    1 
ATOM   2040 C  CA   . PRO A 1 214 ? -18.606 -11.352 18.909  1.00 6.86  ? 215 PRO A CA   1 
ATOM   2041 C  C    . PRO A 1 214 ? -19.579 -11.298 17.783  1.00 9.27  ? 215 PRO A C    1 
ATOM   2042 O  O    . PRO A 1 214 ? -20.749 -11.724 18.005  1.00 10.58 ? 215 PRO A O    1 
ATOM   2043 C  CB   . PRO A 1 214 ? -17.818 -12.674 18.847  1.00 7.89  ? 215 PRO A CB   1 
ATOM   2044 C  CG   . PRO A 1 214 ? -18.616 -13.646 19.663  1.00 14.52 ? 215 PRO A CG   1 
ATOM   2045 C  CD   . PRO A 1 214 ? -19.218 -12.770 20.818  1.00 9.23  ? 215 PRO A CD   1 
ATOM   2046 N  N    . ILE A 1 215 ? -19.161 -10.892 16.603  1.00 8.49  ? 216 ILE A N    1 
ATOM   2047 C  CA   . ILE A 1 215 ? -19.948 -11.074 15.400  1.00 9.58  ? 216 ILE A CA   1 
ATOM   2048 C  C    . ILE A 1 215 ? -19.433 -12.327 14.700  1.00 8.47  ? 216 ILE A C    1 
ATOM   2049 O  O    . ILE A 1 215 ? -18.302 -12.711 14.875  1.00 9.14  ? 216 ILE A O    1 
ATOM   2050 C  CB   . ILE A 1 215 ? -20.014 -9.877  14.475  1.00 9.53  ? 216 ILE A CB   1 
ATOM   2051 C  CG1  . ILE A 1 215 ? -18.579 -9.516  14.031  1.00 10.92 ? 216 ILE A CG1  1 
ATOM   2052 C  CG2  . ILE A 1 215 ? -20.762 -8.702  15.147  1.00 10.94 ? 216 ILE A CG2  1 
ATOM   2053 C  CD1  . ILE A 1 215 ? -18.577 -8.500  12.746  1.00 13.97 ? 216 ILE A CD1  1 
ATOM   2054 N  N    . SER A 1 216 ? -20.347 -12.996 13.940  1.00 9.56  ? 217 SER A N    1 
ATOM   2055 C  CA   . SER A 1 216 ? -19.847 -14.110 13.128  1.00 10.80 ? 217 SER A CA   1 
ATOM   2056 C  C    . SER A 1 216 ? -19.693 -13.675 11.697  1.00 10.43 ? 217 SER A C    1 
ATOM   2057 O  O    . SER A 1 216 ? -20.573 -12.909 11.197  1.00 10.81 ? 217 SER A O    1 
ATOM   2058 C  CB   . SER A 1 216 ? -20.966 -15.221 13.106  1.00 14.66 ? 217 SER A CB   1 
ATOM   2059 O  OG   . SER A 1 216 ? -21.088 -15.780 14.414  1.00 17.20 ? 217 SER A OG   1 
ATOM   2060 N  N    . VAL A 1 217 ? -18.586 -14.135 11.106  1.00 10.00 ? 218 VAL A N    1 
ATOM   2061 C  CA   . VAL A 1 217 ? -18.347 -13.993 9.706   1.00 9.78  ? 218 VAL A CA   1 
ATOM   2062 C  C    . VAL A 1 217 ? -18.059 -15.334 9.102   1.00 10.56 ? 218 VAL A C    1 
ATOM   2063 O  O    . VAL A 1 217 ? -17.713 -16.283 9.822   1.00 10.47 ? 218 VAL A O    1 
ATOM   2064 C  CB   . VAL A 1 217 ? -17.184 -13.023 9.435   1.00 10.14 ? 218 VAL A CB   1 
ATOM   2065 C  CG1  . VAL A 1 217 ? -17.406 -11.635 10.183  1.00 11.23 ? 218 VAL A CG1  1 
ATOM   2066 C  CG2  . VAL A 1 217 ? -15.849 -13.671 9.988   1.00 11.95 ? 218 VAL A CG2  1 
ATOM   2067 N  N    . SER A 1 218 ? -18.261 -15.494 7.775   1.00 9.73  ? 219 SER A N    1 
ATOM   2068 C  CA   . SER A 1 218 ? -18.023 -16.771 7.201   1.00 9.98  ? 219 SER A CA   1 
ATOM   2069 C  C    . SER A 1 218 ? -16.576 -17.020 6.919   1.00 10.15 ? 219 SER A C    1 
ATOM   2070 O  O    . SER A 1 218 ? -15.753 -16.097 6.802   1.00 10.53 ? 219 SER A O    1 
ATOM   2071 C  CB   . SER A 1 218 ? -18.881 -16.975 5.944   1.00 11.49 ? 219 SER A CB   1 
ATOM   2072 O  OG   . SER A 1 218 ? -18.413 -16.096 4.927   1.00 12.03 ? 219 SER A OG   1 
ATOM   2073 N  N    A SER A 1 219 ? -16.205 -18.284 6.734   0.50 10.77 ? 220 SER A N    1 
ATOM   2074 N  N    B SER A 1 219 ? -16.238 -18.285 6.785   0.50 11.14 ? 220 SER A N    1 
ATOM   2075 C  CA   A SER A 1 219 ? -14.824 -18.668 6.314   0.50 13.14 ? 220 SER A CA   1 
ATOM   2076 C  CA   B SER A 1 219 ? -14.883 -18.642 6.413   0.50 14.11 ? 220 SER A CA   1 
ATOM   2077 C  C    A SER A 1 219 ? -14.461 -18.013 4.992   0.50 11.57 ? 220 SER A C    1 
ATOM   2078 C  C    B SER A 1 219 ? -14.510 -17.937 5.087   0.50 12.16 ? 220 SER A C    1 
ATOM   2079 O  O    A SER A 1 219 ? -13.304 -17.656 4.747   0.50 11.86 ? 220 SER A O    1 
ATOM   2080 O  O    B SER A 1 219 ? -13.389 -17.368 4.995   0.50 14.19 ? 220 SER A O    1 
ATOM   2081 C  CB   A SER A 1 219 ? -14.778 -20.234 6.221   0.50 14.57 ? 220 SER A CB   1 
ATOM   2082 C  CB   B SER A 1 219 ? -14.838 -20.183 6.364   0.50 15.12 ? 220 SER A CB   1 
ATOM   2083 O  OG   A SER A 1 219 ? -15.757 -20.769 5.336   0.50 12.64 ? 220 SER A OG   1 
ATOM   2084 O  OG   B SER A 1 219 ? -13.536 -20.622 6.047   0.50 15.11 ? 220 SER A OG   1 
ATOM   2085 N  N    . GLU A 1 220 ? -15.458 -17.892 4.097   1.00 11.76 ? 221 GLU A N    1 
ATOM   2086 C  CA   . GLU A 1 220 ? -15.177 -17.278 2.791   1.00 14.57 ? 221 GLU A CA   1 
ATOM   2087 C  C    . GLU A 1 220 ? -14.954 -15.776 2.978   1.00 13.44 ? 221 GLU A C    1 
ATOM   2088 O  O    . GLU A 1 220 ? -14.111 -15.218 2.241   1.00 14.60 ? 221 GLU A O    1 
ATOM   2089 C  CB   . GLU A 1 220 ? -16.333 -17.510 1.817   1.00 16.20 ? 221 GLU A CB   1 
ATOM   2090 C  CG   . GLU A 1 220 ? -16.554 -18.962 1.441   1.00 20.01 ? 221 GLU A CG   1 
ATOM   2091 C  CD   . GLU A 1 220 ? -17.655 -19.611 2.256   1.00 22.95 ? 221 GLU A CD   1 
ATOM   2092 O  OE1  . GLU A 1 220 ? -17.895 -19.166 3.398   1.00 18.58 ? 221 GLU A OE1  1 
ATOM   2093 O  OE2  . GLU A 1 220 ? -18.282 -20.568 1.754   1.00 32.54 ? 221 GLU A OE2  1 
ATOM   2094 N  N    . GLN A 1 221 ? -15.640 -15.097 3.910   1.00 11.49 ? 222 GLN A N    1 
ATOM   2095 C  CA   . GLN A 1 221 ? -15.346 -13.689 4.131   1.00 11.61 ? 222 GLN A CA   1 
ATOM   2096 C  C    . GLN A 1 221 ? -13.925 -13.475 4.697   1.00 11.91 ? 222 GLN A C    1 
ATOM   2097 O  O    . GLN A 1 221 ? -13.136 -12.613 4.177   1.00 12.34 ? 222 GLN A O    1 
ATOM   2098 C  CB   . GLN A 1 221 ? -16.328 -13.111 5.114   1.00 11.84 ? 222 GLN A CB   1 
ATOM   2099 C  CG   . GLN A 1 221 ? -17.746 -12.952 4.394   1.00 11.67 ? 222 GLN A CG   1 
ATOM   2100 C  CD   . GLN A 1 221 ? -18.829 -12.458 5.278   1.00 11.33 ? 222 GLN A CD   1 
ATOM   2101 O  OE1  . GLN A 1 221 ? -18.944 -12.800 6.469   1.00 10.30 ? 222 GLN A OE1  1 
ATOM   2102 N  NE2  . GLN A 1 221 ? -19.668 -11.544 4.702   1.00 11.02 ? 222 GLN A NE2  1 
ATOM   2103 N  N    . VAL A 1 222 ? -13.550 -14.278 5.689   1.00 12.08 ? 223 VAL A N    1 
ATOM   2104 C  CA   . VAL A 1 222 ? -12.191 -14.056 6.230   1.00 12.26 ? 223 VAL A CA   1 
ATOM   2105 C  C    . VAL A 1 222 ? -11.108 -14.507 5.246   1.00 12.87 ? 223 VAL A C    1 
ATOM   2106 O  O    . VAL A 1 222 ? -9.997  -13.953 5.191   1.00 12.86 ? 223 VAL A O    1 
ATOM   2107 C  CB   . VAL A 1 222 ? -12.103 -14.628 7.691   1.00 15.52 ? 223 VAL A CB   1 
ATOM   2108 C  CG1  . VAL A 1 222 ? -12.072 -16.100 7.671   1.00 16.20 ? 223 VAL A CG1  1 
ATOM   2109 C  CG2  . VAL A 1 222 ? -10.743 -14.090 8.422   1.00 15.39 ? 223 VAL A CG2  1 
ATOM   2110 N  N    . LEU A 1 223 ? -11.383 -15.542 4.499   1.00 14.10 ? 224 LEU A N    1 
ATOM   2111 C  CA   . LEU A 1 223 ? -10.408 -15.912 3.464   1.00 14.01 ? 224 LEU A CA   1 
ATOM   2112 C  C    . LEU A 1 223 ? -10.091 -14.790 2.500   1.00 15.69 ? 224 LEU A C    1 
ATOM   2113 O  O    . LEU A 1 223 ? -8.928  -14.690 2.067   1.00 15.33 ? 224 LEU A O    1 
ATOM   2114 C  CB   . LEU A 1 223 ? -10.801 -17.188 2.675   1.00 18.74 ? 224 LEU A CB   1 
ATOM   2115 C  CG   . LEU A 1 223 ? -10.679 -18.404 3.579   1.00 20.54 ? 224 LEU A CG   1 
ATOM   2116 C  CD1  . LEU A 1 223 ? -11.616 -19.594 3.097   1.00 24.56 ? 224 LEU A CD1  1 
ATOM   2117 C  CD2  . LEU A 1 223 ? -9.135  -18.799 3.516   1.00 22.83 ? 224 LEU A CD2  1 
ATOM   2118 N  N    . LYS A 1 224 ? -11.084 -13.972 2.164   1.00 13.94 ? 225 LYS A N    1 
ATOM   2119 C  CA   . LYS A 1 224 ? -10.846 -12.849 1.301   1.00 13.72 ? 225 LYS A CA   1 
ATOM   2120 C  C    . LYS A 1 224 ? -9.990  -11.780 1.989   1.00 11.88 ? 225 LYS A C    1 
ATOM   2121 O  O    . LYS A 1 224 ? -9.134  -11.157 1.336   1.00 13.00 ? 225 LYS A O    1 
ATOM   2122 C  CB   . LYS A 1 224 ? -12.177 -12.242 0.768   1.00 15.54 ? 225 LYS A CB   1 
ATOM   2123 C  CG   . LYS A 1 224 ? -12.668 -13.364 -0.370  1.00 19.03 ? 225 LYS A CG   1 
ATOM   2124 C  CD   . LYS A 1 224 ? -14.008 -13.038 -0.967  1.00 21.79 ? 225 LYS A CD   1 
ATOM   2125 C  CE   . LYS A 1 224 ? -14.541 -14.204 -1.943  1.00 24.67 ? 225 LYS A CE   1 
ATOM   2126 N  NZ   . LYS A 1 224 ? -15.934 -13.828 -2.566  1.00 26.92 ? 225 LYS A NZ   1 
ATOM   2127 N  N    . PHE A 1 225 ? -10.075 -11.577 3.327   1.00 10.81 ? 226 PHE A N    1 
ATOM   2128 C  CA   . PHE A 1 225 ? -9.118  -10.692 4.035   1.00 9.51  ? 226 PHE A CA   1 
ATOM   2129 C  C    . PHE A 1 225 ? -7.687  -11.231 3.797   1.00 9.93  ? 226 PHE A C    1 
ATOM   2130 O  O    . PHE A 1 225 ? -6.769  -10.439 3.578   1.00 11.36 ? 226 PHE A O    1 
ATOM   2131 C  CB   . PHE A 1 225 ? -9.346  -10.748 5.560   1.00 10.60 ? 226 PHE A CB   1 
ATOM   2132 C  CG   . PHE A 1 225 ? -10.545 -9.953  6.077   1.00 10.61 ? 226 PHE A CG   1 
ATOM   2133 C  CD1  . PHE A 1 225 ? -11.553 -9.496  5.243   1.00 14.15 ? 226 PHE A CD1  1 
ATOM   2134 C  CD2  . PHE A 1 225 ? -10.649 -9.687  7.441   1.00 14.98 ? 226 PHE A CD2  1 
ATOM   2135 C  CE1  . PHE A 1 225 ? -12.639 -8.782  5.768   1.00 15.05 ? 226 PHE A CE1  1 
ATOM   2136 C  CE2  . PHE A 1 225 ? -11.722 -8.982  7.964   1.00 15.80 ? 226 PHE A CE2  1 
ATOM   2137 C  CZ   . PHE A 1 225 ? -12.720 -8.530  7.130   1.00 11.90 ? 226 PHE A CZ   1 
ATOM   2138 N  N    . ARG A 1 226 ? -7.517  -12.529 3.850   1.00 10.54 ? 227 ARG A N    1 
ATOM   2139 C  CA   . ARG A 1 226 ? -6.153  -13.118 3.788   1.00 11.13 ? 227 ARG A CA   1 
ATOM   2140 C  C    . ARG A 1 226 ? -5.592  -13.118 2.367   1.00 10.85 ? 227 ARG A C    1 
ATOM   2141 O  O    . ARG A 1 226 ? -4.488  -13.575 2.221   1.00 13.08 ? 227 ARG A O    1 
ATOM   2142 C  CB   . ARG A 1 226 ? -6.278  -14.616 4.271   1.00 12.22 ? 227 ARG A CB   1 
ATOM   2143 C  CG   . ARG A 1 226 ? -6.726  -14.620 5.743   1.00 11.95 ? 227 ARG A CG   1 
ATOM   2144 C  CD   . ARG A 1 226 ? -6.770  -16.202 6.172   1.00 12.94 ? 227 ARG A CD   1 
ATOM   2145 N  NE   . ARG A 1 226 ? -7.203  -16.260 7.549   1.00 12.30 ? 227 ARG A NE   1 
ATOM   2146 C  CZ   . ARG A 1 226 ? -8.187  -17.117 7.968   1.00 12.41 ? 227 ARG A CZ   1 
ATOM   2147 N  NH1  . ARG A 1 226 ? -8.647  -18.082 7.092   1.00 15.89 ? 227 ARG A NH1  1 
ATOM   2148 N  NH2  . ARG A 1 226 ? -8.635  -17.123 9.203   1.00 12.87 ? 227 ARG A NH2  1 
ATOM   2149 N  N    . LYS A 1 227 ? -6.357  -12.647 1.378   1.00 11.29 ? 228 LYS A N    1 
ATOM   2150 C  CA   . LYS A 1 227 ? -5.854  -12.543 0.034   1.00 12.28 ? 228 LYS A CA   1 
ATOM   2151 C  C    . LYS A 1 227 ? -5.192  -11.161 -0.209  1.00 11.87 ? 228 LYS A C    1 
ATOM   2152 O  O    . LYS A 1 227 ? -4.532  -11.007 -1.197  1.00 14.12 ? 228 LYS A O    1 
ATOM   2153 C  CB   . LYS A 1 227 ? -6.969  -12.769 -0.954  1.00 14.08 ? 228 LYS A CB   1 
ATOM   2154 C  CG   . LYS A 1 227 ? -7.380  -14.164 -1.044  1.00 17.88 ? 228 LYS A CG   1 
ATOM   2155 C  CD   . LYS A 1 227 ? -8.523  -14.317 -2.133  1.00 24.62 ? 228 LYS A CD   1 
ATOM   2156 C  CE   . LYS A 1 227 ? -7.832  -14.440 -3.520  1.00 31.31 ? 228 LYS A CE   1 
ATOM   2157 N  NZ   . LYS A 1 227 ? -8.823  -14.606 -4.637  1.00 33.29 ? 228 LYS A NZ   1 
ATOM   2158 N  N    . LEU A 1 228 ? -5.457  -10.199 0.698   1.00 11.75 ? 229 LEU A N    1 
ATOM   2159 C  CA   . LEU A 1 228 ? -4.799  -8.909  0.603   1.00 11.97 ? 229 LEU A CA   1 
ATOM   2160 C  C    . LEU A 1 228 ? -3.322  -9.136  0.780   1.00 11.51 ? 229 LEU A C    1 
ATOM   2161 O  O    . LEU A 1 228 ? -2.802  -10.185 1.193   1.00 12.13 ? 229 LEU A O    1 
ATOM   2162 C  CB   . LEU A 1 228 ? -5.319  -7.998  1.690   1.00 11.31 ? 229 LEU A CB   1 
ATOM   2163 C  CG   . LEU A 1 228 ? -6.763  -7.555  1.541   1.00 13.06 ? 229 LEU A CG   1 
ATOM   2164 C  CD1  . LEU A 1 228 ? -7.233  -6.907  2.826   1.00 13.89 ? 229 LEU A CD1  1 
ATOM   2165 C  CD2  . LEU A 1 228 ? -6.843  -6.554  0.327   1.00 14.51 ? 229 LEU A CD2  1 
ATOM   2166 N  N    . ASN A 1 229 ? -2.580  -8.108  0.380   1.00 12.92 ? 230 ASN A N    1 
ATOM   2167 C  CA   . ASN A 1 229 ? -1.150  -8.091  0.448   1.00 12.76 ? 230 ASN A CA   1 
ATOM   2168 C  C    . ASN A 1 229 ? -0.601  -6.901  1.260   1.00 13.16 ? 230 ASN A C    1 
ATOM   2169 O  O    . ASN A 1 229 ? -1.054  -5.792  1.212   1.00 13.78 ? 230 ASN A O    1 
ATOM   2170 C  CB   . ASN A 1 229 ? -0.612  -7.857  -1.036  1.00 14.55 ? 230 ASN A CB   1 
ATOM   2171 C  CG   . ASN A 1 229 ? -0.647  -9.033  -1.943  1.00 14.50 ? 230 ASN A CG   1 
ATOM   2172 O  OD1  . ASN A 1 229 ? -0.059  -8.898  -3.027  1.00 17.78 ? 230 ASN A OD1  1 
ATOM   2173 N  ND2  . ASN A 1 229 ? -1.294  -10.195 -1.570  1.00 15.32 ? 230 ASN A ND2  1 
ATOM   2174 N  N    . PHE A 1 230 ? 0.428   -7.261  2.054   1.00 12.16 ? 231 PHE A N    1 
ATOM   2175 C  CA   . PHE A 1 230 ? 1.201   -6.176  2.723   1.00 12.46 ? 231 PHE A CA   1 
ATOM   2176 C  C    . PHE A 1 230 ? 2.110   -5.400  1.757   1.00 14.68 ? 231 PHE A C    1 
ATOM   2177 O  O    . PHE A 1 230 ? 2.427   -4.207  2.000   1.00 15.86 ? 231 PHE A O    1 
ATOM   2178 C  CB   . PHE A 1 230 ? 2.209   -6.749  3.713   1.00 13.78 ? 231 PHE A CB   1 
ATOM   2179 C  CG   . PHE A 1 230 ? 1.581   -7.384  5.027   1.00 13.75 ? 231 PHE A CG   1 
ATOM   2180 C  CD1  . PHE A 1 230 ? 0.809   -6.584  5.882   1.00 13.67 ? 231 PHE A CD1  1 
ATOM   2181 C  CD2  . PHE A 1 230 ? 1.899   -8.645  5.416   1.00 13.64 ? 231 PHE A CD2  1 
ATOM   2182 C  CE1  . PHE A 1 230 ? 0.338   -7.056  7.087   1.00 14.72 ? 231 PHE A CE1  1 
ATOM   2183 C  CE2  . PHE A 1 230 ? 1.456   -9.153  6.639   1.00 13.06 ? 231 PHE A CE2  1 
ATOM   2184 C  CZ   . PHE A 1 230 ? 0.653   -8.375  7.446   1.00 13.38 ? 231 PHE A CZ   1 
ATOM   2185 N  N    . ASN A 1 231 ? 2.582   -6.054  0.725   1.00 14.40 ? 232 ASN A N    1 
ATOM   2186 C  CA   . ASN A 1 231 ? 3.464   -5.430  -0.278  1.00 15.44 ? 232 ASN A CA   1 
ATOM   2187 C  C    . ASN A 1 231 ? 2.679   -4.526  -1.234  1.00 13.67 ? 232 ASN A C    1 
ATOM   2188 O  O    . ASN A 1 231 ? 1.482   -4.665  -1.435  1.00 15.61 ? 232 ASN A O    1 
ATOM   2189 C  CB   . ASN A 1 231 ? 4.129   -6.578  -1.093  1.00 14.65 ? 232 ASN A CB   1 
ATOM   2190 C  CG   . ASN A 1 231 ? 3.083   -7.475  -1.695  1.00 16.13 ? 232 ASN A CG   1 
ATOM   2191 O  OD1  . ASN A 1 231 ? 2.513   -8.304  -1.005  1.00 17.61 ? 232 ASN A OD1  1 
ATOM   2192 N  ND2  . ASN A 1 231 ? 2.839   -7.335  -3.005  1.00 17.07 ? 232 ASN A ND2  1 
ATOM   2193 N  N    . GLY A 1 232 ? 3.532   -3.631  -1.901  1.00 15.98 ? 233 GLY A N    1 
ATOM   2194 C  CA   . GLY A 1 232 ? 2.871   -2.826  -3.005  1.00 16.46 ? 233 GLY A CA   1 
ATOM   2195 C  C    . GLY A 1 232 ? 2.903   -3.583  -4.330  1.00 15.40 ? 233 GLY A C    1 
ATOM   2196 O  O    . GLY A 1 232 ? 3.554   -4.635  -4.396  1.00 18.05 ? 233 GLY A O    1 
ATOM   2197 N  N    . GLU A 1 233 ? 2.173   -3.044  -5.362  1.00 15.80 ? 234 GLU A N    1 
ATOM   2198 C  CA   . GLU A 1 233 ? 2.041   -3.652  -6.707  1.00 13.86 ? 234 GLU A CA   1 
ATOM   2199 C  C    . GLU A 1 233 ? 3.423   -3.769  -7.265  1.00 17.13 ? 234 GLU A C    1 
ATOM   2200 O  O    . GLU A 1 233 ? 4.250   -2.894  -7.102  1.00 17.24 ? 234 GLU A O    1 
ATOM   2201 C  CB   . GLU A 1 233 ? 1.160   -2.783  -7.600  1.00 14.40 ? 234 GLU A CB   1 
ATOM   2202 C  CG   . GLU A 1 233 ? 0.894   -3.358  -8.978  1.00 15.97 ? 234 GLU A CG   1 
ATOM   2203 C  CD   . GLU A 1 233 ? 0.009   -2.453  -9.810  1.00 26.19 ? 234 GLU A CD   1 
ATOM   2204 O  OE1  . GLU A 1 233 ? -0.379  -1.379  -9.304  1.00 26.99 ? 234 GLU A OE1  1 
ATOM   2205 O  OE2  . GLU A 1 233 ? -0.301  -2.812  -10.965 1.00 23.88 ? 234 GLU A OE2  1 
ATOM   2206 N  N    . GLY A 1 234 ? 3.675   -4.883  -7.941  1.00 16.72 ? 235 GLY A N    1 
ATOM   2207 C  CA   . GLY A 1 234 ? 4.990   -5.082  -8.502  1.00 18.53 ? 235 GLY A CA   1 
ATOM   2208 C  C    . GLY A 1 234 ? 6.008   -5.497  -7.564  1.00 17.32 ? 235 GLY A C    1 
ATOM   2209 O  O    . GLY A 1 234 ? 7.211   -5.637  -7.920  1.00 22.04 ? 235 GLY A O    1 
ATOM   2210 N  N    . GLU A 1 235 ? 5.603   -5.846  -6.318  1.00 17.02 ? 236 GLU A N    1 
ATOM   2211 C  CA   . GLU A 1 235 ? 6.664   -6.383  -5.414  1.00 15.59 ? 236 GLU A CA   1 
ATOM   2212 C  C    . GLU A 1 235 ? 6.235   -7.819  -5.044  1.00 18.30 ? 236 GLU A C    1 
ATOM   2213 O  O    . GLU A 1 235 ? 5.068   -8.172  -5.302  1.00 20.83 ? 236 GLU A O    1 
ATOM   2214 C  CB   . GLU A 1 235 ? 6.531   -5.580  -3.994  1.00 15.74 ? 236 GLU A CB   1 
ATOM   2215 C  CG   . GLU A 1 235 ? 6.974   -4.134  -4.231  1.00 17.58 ? 236 GLU A CG   1 
ATOM   2216 C  CD   . GLU A 1 235 ? 6.716   -3.244  -3.043  1.00 21.57 ? 236 GLU A CD   1 
ATOM   2217 O  OE1  . GLU A 1 235 ? 6.095   -3.666  -2.017  1.00 21.85 ? 236 GLU A OE1  1 
ATOM   2218 O  OE2  . GLU A 1 235 ? 7.166   -2.058  -3.031  1.00 29.09 ? 236 GLU A OE2  1 
ATOM   2219 N  N    . PRO A 1 236 ? 7.110   -8.610  -4.484  1.00 15.51 ? 237 PRO A N    1 
ATOM   2220 C  CA   . PRO A 1 236 ? 6.823   -10.050 -4.196  1.00 17.59 ? 237 PRO A CA   1 
ATOM   2221 C  C    . PRO A 1 236 ? 5.723   -10.137 -3.164  1.00 17.09 ? 237 PRO A C    1 
ATOM   2222 O  O    . PRO A 1 236 ? 5.649   -9.315  -2.255  1.00 17.02 ? 237 PRO A O    1 
ATOM   2223 C  CB   . PRO A 1 236 ? 8.113   -10.542 -3.559  1.00 18.23 ? 237 PRO A CB   1 
ATOM   2224 C  CG   . PRO A 1 236 ? 9.260   -9.463  -3.925  1.00 21.97 ? 237 PRO A CG   1 
ATOM   2225 C  CD   . PRO A 1 236 ? 8.530   -8.213  -4.128  1.00 20.10 ? 237 PRO A CD   1 
ATOM   2226 N  N    . GLU A 1 237 ? 4.885   -11.119 -3.300  1.00 16.70 ? 238 GLU A N    1 
ATOM   2227 C  CA   . GLU A 1 237 ? 3.665   -11.160 -2.624  1.00 17.25 ? 238 GLU A CA   1 
ATOM   2228 C  C    . GLU A 1 237 ? 3.948   -11.653 -1.174  1.00 17.00 ? 238 GLU A C    1 
ATOM   2229 O  O    . GLU A 1 237 ? 4.491   -12.707 -0.942  1.00 15.90 ? 238 GLU A O    1 
ATOM   2230 C  CB   . GLU A 1 237 ? 2.707   -12.206 -3.349  1.00 17.46 ? 238 GLU A CB   1 
ATOM   2231 C  CG   . GLU A 1 237 ? 1.429   -12.179 -2.630  1.00 18.37 ? 238 GLU A CG   1 
ATOM   2232 C  CD   . GLU A 1 237 ? 0.346   -12.876 -3.310  1.00 18.80 ? 238 GLU A CD   1 
ATOM   2233 O  OE1  . GLU A 1 237 ? 0.806   -13.885 -3.990  1.00 23.02 ? 238 GLU A OE1  1 
ATOM   2234 O  OE2  . GLU A 1 237 ? -0.844  -12.462 -3.322  1.00 16.27 ? 238 GLU A OE2  1 
ATOM   2235 N  N    . GLU A 1 238 ? 3.450   -10.866 -0.233  1.00 13.84 ? 239 GLU A N    1 
ATOM   2236 C  CA   . GLU A 1 238 ? 3.450   -11.196 1.223   1.00 16.55 ? 239 GLU A CA   1 
ATOM   2237 C  C    . GLU A 1 238 ? 1.996   -11.051 1.642   1.00 12.06 ? 239 GLU A C    1 
ATOM   2238 O  O    . GLU A 1 238 ? 1.522   -9.897  1.695   1.00 16.17 ? 239 GLU A O    1 
ATOM   2239 C  CB   . GLU A 1 238 ? 4.312   -10.243 2.056   1.00 17.95 ? 239 GLU A CB   1 
ATOM   2240 C  CG   . GLU A 1 238 ? 5.753   -10.070 1.594   1.00 22.98 ? 239 GLU A CG   1 
ATOM   2241 C  CD   . GLU A 1 238 ? 6.763   -10.872 2.416   1.00 23.45 ? 239 GLU A CD   1 
ATOM   2242 O  OE1  . GLU A 1 238 ? 6.370   -11.876 3.044   1.00 36.50 ? 239 GLU A OE1  1 
ATOM   2243 O  OE2  . GLU A 1 238 ? 7.958   -10.501 2.424   1.00 33.66 ? 239 GLU A OE2  1 
ATOM   2244 N  N    . LEU A 1 239 ? 1.269   -12.178 1.952   1.00 12.11 ? 240 LEU A N    1 
ATOM   2245 C  CA   . LEU A 1 239 ? -0.098  -12.066 2.208   1.00 11.32 ? 240 LEU A CA   1 
ATOM   2246 C  C    . LEU A 1 239 ? -0.255  -11.253 3.505   1.00 10.43 ? 240 LEU A C    1 
ATOM   2247 O  O    . LEU A 1 239 ? 0.442   -11.483 4.482   1.00 11.99 ? 240 LEU A O    1 
ATOM   2248 C  CB   . LEU A 1 239 ? -0.712  -13.477 2.432   1.00 12.88 ? 240 LEU A CB   1 
ATOM   2249 C  CG   . LEU A 1 239 ? -0.647  -14.365 1.195   1.00 11.75 ? 240 LEU A CG   1 
ATOM   2250 C  CD1  . LEU A 1 239 ? -1.253  -15.728 1.687   1.00 17.54 ? 240 LEU A CD1  1 
ATOM   2251 C  CD2  . LEU A 1 239 ? -1.514  -13.714 0.066   1.00 12.41 ? 240 LEU A CD2  1 
ATOM   2252 N  N    . MET A 1 240 ? -1.263  -10.420 3.505   1.00 11.19 ? 241 MET A N    1 
ATOM   2253 C  CA   . MET A 1 240 ? -1.642  -9.598  4.717   1.00 11.53 ? 241 MET A CA   1 
ATOM   2254 C  C    . MET A 1 240 ? -2.455  -10.542 5.653   1.00 9.59  ? 241 MET A C    1 
ATOM   2255 O  O    . MET A 1 240 ? -3.629  -10.753 5.543   1.00 11.25 ? 241 MET A O    1 
ATOM   2256 C  CB   . MET A 1 240 ? -2.494  -8.497  4.243   1.00 13.62 ? 241 MET A CB   1 
ATOM   2257 C  CG   . MET A 1 240 ? -2.844  -7.456  5.438   1.00 12.38 ? 241 MET A CG   1 
ATOM   2258 S  SD   . MET A 1 240 ? -3.803  -6.082  4.894   1.00 13.75 ? 241 MET A SD   1 
ATOM   2259 C  CE   . MET A 1 240 ? -2.501  -4.913  4.236   1.00 13.12 ? 241 MET A CE   1 
ATOM   2260 N  N    . VAL A 1 241 ? -1.643  -11.172 6.532   1.00 10.10 ? 242 VAL A N    1 
ATOM   2261 C  CA   . VAL A 1 241 ? -2.239  -12.034 7.617   1.00 8.81  ? 242 VAL A CA   1 
ATOM   2262 C  C    . VAL A 1 241 ? -1.403  -11.862 8.845   1.00 8.86  ? 242 VAL A C    1 
ATOM   2263 O  O    . VAL A 1 241 ? -0.218  -11.395 8.805   1.00 11.05 ? 242 VAL A O    1 
ATOM   2264 C  CB   . VAL A 1 241 ? -2.112  -13.542 7.179   1.00 10.19 ? 242 VAL A CB   1 
ATOM   2265 C  CG1  . VAL A 1 241 ? -3.083  -13.860 5.946   1.00 11.79 ? 242 VAL A CG1  1 
ATOM   2266 C  CG2  . VAL A 1 241 ? -0.658  -14.021 6.956   1.00 11.01 ? 242 VAL A CG2  1 
ATOM   2267 N  N    . ASP A 1 242 ? -1.962  -12.132 10.004  1.00 8.09  ? 243 ASP A N    1 
ATOM   2268 C  CA   . ASP A 1 242 ? -1.351  -12.061 11.253  1.00 8.17  ? 243 ASP A CA   1 
ATOM   2269 C  C    . ASP A 1 242 ? -0.817  -10.589 11.509  1.00 8.46  ? 243 ASP A C    1 
ATOM   2270 O  O    . ASP A 1 242 ? 0.277   -10.321 12.002  1.00 9.57  ? 243 ASP A O    1 
ATOM   2271 C  CB   . ASP A 1 242 ? -0.213  -13.092 11.465  1.00 7.82  ? 243 ASP A CB   1 
ATOM   2272 C  CG   . ASP A 1 242 ? -0.770  -14.472 11.597  1.00 8.82  ? 243 ASP A CG   1 
ATOM   2273 O  OD1  . ASP A 1 242 ? -1.828  -14.623 12.247  1.00 9.12  ? 243 ASP A OD1  1 
ATOM   2274 O  OD2  . ASP A 1 242 ? -0.171  -15.375 11.001  1.00 11.11 ? 243 ASP A OD2  1 
ATOM   2275 N  N    . ASN A 1 243 ? -1.743  -9.663  11.252  1.00 8.22  ? 244 ASN A N    1 
ATOM   2276 C  CA   . ASN A 1 243 ? -1.458  -8.213  11.463  1.00 7.45  ? 244 ASN A CA   1 
ATOM   2277 C  C    . ASN A 1 243 ? -2.002  -7.776  12.808  1.00 8.45  ? 244 ASN A C    1 
ATOM   2278 O  O    . ASN A 1 243 ? -2.673  -6.725  12.904  1.00 9.07  ? 244 ASN A O    1 
ATOM   2279 C  CB   . ASN A 1 243 ? -2.004  -7.378  10.309  1.00 9.43  ? 244 ASN A CB   1 
ATOM   2280 C  CG   . ASN A 1 243 ? -3.484  -7.543  10.094  1.00 8.42  ? 244 ASN A CG   1 
ATOM   2281 O  OD1  . ASN A 1 243 ? -4.161  -8.367  10.712  1.00 10.07 ? 244 ASN A OD1  1 
ATOM   2282 N  ND2  . ASN A 1 243 ? -4.032  -6.718  9.183   1.00 13.63 ? 244 ASN A ND2  1 
ATOM   2283 N  N    . TRP A 1 244 ? -1.710  -8.499  13.880  1.00 6.71  ? 245 TRP A N    1 
ATOM   2284 C  CA   . TRP A 1 244 ? -2.146  -8.285  15.238  1.00 6.92  ? 245 TRP A CA   1 
ATOM   2285 C  C    . TRP A 1 244 ? -0.965  -8.162  16.149  1.00 7.36  ? 245 TRP A C    1 
ATOM   2286 O  O    . TRP A 1 244 ? 0.022   -8.898  15.986  1.00 7.93  ? 245 TRP A O    1 
ATOM   2287 C  CB   . TRP A 1 244 ? -3.140  -9.414  15.739  1.00 7.14  ? 245 TRP A CB   1 
ATOM   2288 C  CG   . TRP A 1 244 ? -2.637  -10.809 15.538  1.00 7.87  ? 245 TRP A CG   1 
ATOM   2289 C  CD1  . TRP A 1 244 ? -2.780  -11.550 14.373  1.00 7.80  ? 245 TRP A CD1  1 
ATOM   2290 C  CD2  . TRP A 1 244 ? -2.022  -11.623 16.512  1.00 7.10  ? 245 TRP A CD2  1 
ATOM   2291 N  NE1  . TRP A 1 244 ? -2.254  -12.804 14.590  1.00 7.16  ? 245 TRP A NE1  1 
ATOM   2292 C  CE2  . TRP A 1 244 ? -1.819  -12.892 15.897  1.00 8.13  ? 245 TRP A CE2  1 
ATOM   2293 C  CE3  . TRP A 1 244 ? -1.784  -11.519 17.869  1.00 8.60  ? 245 TRP A CE3  1 
ATOM   2294 C  CZ2  . TRP A 1 244 ? -1.172  -13.946 16.577  1.00 8.56  ? 245 TRP A CZ2  1 
ATOM   2295 C  CZ3  . TRP A 1 244 ? -1.227  -12.607 18.573  1.00 9.10  ? 245 TRP A CZ3  1 
ATOM   2296 C  CH2  . TRP A 1 244 ? -0.942  -13.825 17.905  1.00 9.55  ? 245 TRP A CH2  1 
ATOM   2297 N  N    . ARG A 1 245 ? -1.067  -7.274  17.123  1.00 6.33  ? 246 ARG A N    1 
ATOM   2298 C  CA   . ARG A 1 245 ? -0.146  -7.142  18.218  1.00 8.08  ? 246 ARG A CA   1 
ATOM   2299 C  C    . ARG A 1 245 ? -0.640  -8.077  19.367  1.00 7.45  ? 246 ARG A C    1 
ATOM   2300 O  O    . ARG A 1 245 ? -1.817  -8.102  19.669  1.00 7.96  ? 246 ARG A O    1 
ATOM   2301 C  CB   . ARG A 1 245 ? -0.065  -5.711  18.727  1.00 6.94  ? 246 ARG A CB   1 
ATOM   2302 C  CG   . ARG A 1 245 ? 1.023   -5.513  19.776  1.00 7.27  ? 246 ARG A CG   1 
ATOM   2303 C  CD   . ARG A 1 245 ? 0.935   -4.151  20.446  1.00 8.43  ? 246 ARG A CD   1 
ATOM   2304 N  NE   . ARG A 1 245 ? 2.205   -3.796  21.081  1.00 8.82  ? 246 ARG A NE   1 
ATOM   2305 C  CZ   . ARG A 1 245 ? 2.375   -2.801  21.948  1.00 7.15  ? 246 ARG A CZ   1 
ATOM   2306 N  NH1  . ARG A 1 245 ? 1.343   -2.050  22.327  1.00 9.00  ? 246 ARG A NH1  1 
ATOM   2307 N  NH2  . ARG A 1 245 ? 3.591   -2.572  22.429  1.00 9.91  ? 246 ARG A NH2  1 
ATOM   2308 N  N    . PRO A 1 246 ? 0.284   -8.872  19.974  1.00 9.28  ? 247 PRO A N    1 
ATOM   2309 C  CA   . PRO A 1 246 ? -0.147  -9.715  21.083  1.00 7.85  ? 247 PRO A CA   1 
ATOM   2310 C  C    . PRO A 1 246 ? -0.512  -8.881  22.336  1.00 8.92  ? 247 PRO A C    1 
ATOM   2311 O  O    . PRO A 1 246 ? -0.145  -7.689  22.492  1.00 8.31  ? 247 PRO A O    1 
ATOM   2312 C  CB   . PRO A 1 246 ? 1.013   -10.612 21.351  1.00 10.20 ? 247 PRO A CB   1 
ATOM   2313 C  CG   . PRO A 1 246 ? 1.998   -10.205 20.495  1.00 15.32 ? 247 PRO A CG   1 
ATOM   2314 C  CD   . PRO A 1 246 ? 1.712   -9.057  19.699  1.00 10.10 ? 247 PRO A CD   1 
ATOM   2315 N  N    . ALA A 1 247 ? -1.144  -9.535  23.281  1.00 7.99  ? 248 ALA A N    1 
ATOM   2316 C  CA   . ALA A 1 247 ? -1.436  -8.921  24.581  1.00 7.81  ? 248 ALA A CA   1 
ATOM   2317 C  C    . ALA A 1 247 ? -0.206  -8.431  25.268  1.00 7.69  ? 248 ALA A C    1 
ATOM   2318 O  O    . ALA A 1 247 ? 0.853   -9.079  25.317  1.00 9.96  ? 248 ALA A O    1 
ATOM   2319 C  CB   . ALA A 1 247 ? -2.277  -9.947  25.460  1.00 9.84  ? 248 ALA A CB   1 
ATOM   2320 N  N    . GLN A 1 248 ? -0.406  -7.257  25.893  1.00 7.30  ? 249 GLN A N    1 
ATOM   2321 C  CA   . GLN A 1 248 ? 0.689   -6.545  26.619  1.00 8.85  ? 249 GLN A CA   1 
ATOM   2322 C  C    . GLN A 1 248 ? 0.397   -6.575  28.109  1.00 9.29  ? 249 GLN A C    1 
ATOM   2323 O  O    . GLN A 1 248 ? -0.774  -6.720  28.513  1.00 10.32 ? 249 GLN A O    1 
ATOM   2324 C  CB   . GLN A 1 248 ? 0.744   -5.055  26.073  1.00 8.78  ? 249 GLN A CB   1 
ATOM   2325 C  CG   . GLN A 1 248 ? 1.035   -5.008  24.568  1.00 8.74  ? 249 GLN A CG   1 
ATOM   2326 C  CD   . GLN A 1 248 ? 2.358   -5.717  24.234  1.00 9.90  ? 249 GLN A CD   1 
ATOM   2327 O  OE1  . GLN A 1 248 ? 3.393   -5.327  24.818  1.00 11.65 ? 249 GLN A OE1  1 
ATOM   2328 N  NE2  . GLN A 1 248 ? 2.326   -6.618  23.275  1.00 10.24 ? 249 GLN A NE2  1 
ATOM   2329 N  N    . PRO A 1 249 ? 1.394   -6.291  28.931  1.00 11.74 ? 250 PRO A N    1 
ATOM   2330 C  CA   . PRO A 1 249 ? 1.164   -6.358  30.351  1.00 13.59 ? 250 PRO A CA   1 
ATOM   2331 C  C    . PRO A 1 249 ? 0.096   -5.333  30.784  1.00 10.17 ? 250 PRO A C    1 
ATOM   2332 O  O    . PRO A 1 249 ? 0.143   -4.155  30.398  1.00 11.02 ? 250 PRO A O    1 
ATOM   2333 C  CB   . PRO A 1 249 ? 2.654   -5.931  30.909  1.00 14.99 ? 250 PRO A CB   1 
ATOM   2334 C  CG   . PRO A 1 249 ? 3.515   -6.409  29.890  1.00 16.65 ? 250 PRO A CG   1 
ATOM   2335 C  CD   . PRO A 1 249 ? 2.815   -6.025  28.603  1.00 12.78 ? 250 PRO A CD   1 
ATOM   2336 N  N    . LEU A 1 250 ? -0.759  -5.807  31.689  1.00 10.80 ? 251 LEU A N    1 
ATOM   2337 C  CA   . LEU A 1 250 ? -1.804  -4.950  32.203  1.00 9.68  ? 251 LEU A CA   1 
ATOM   2338 C  C    . LEU A 1 250 ? -1.285  -3.832  33.120  1.00 11.27 ? 251 LEU A C    1 
ATOM   2339 O  O    . LEU A 1 250 ? -1.868  -2.734  33.200  1.00 10.87 ? 251 LEU A O    1 
ATOM   2340 C  CB   . LEU A 1 250 ? -2.897  -5.790  32.901  1.00 11.96 ? 251 LEU A CB   1 
ATOM   2341 C  CG   . LEU A 1 250 ? -4.123  -5.035  33.325  1.00 11.68 ? 251 LEU A CG   1 
ATOM   2342 C  CD1  . LEU A 1 250 ? -4.923  -4.448  32.148  1.00 12.07 ? 251 LEU A CD1  1 
ATOM   2343 C  CD2  . LEU A 1 250 ? -4.990  -6.080  34.076  1.00 17.00 ? 251 LEU A CD2  1 
ATOM   2344 N  N    . LYS A 1 251 ? -0.204  -4.189  33.837  1.00 12.54 ? 252 LYS A N    1 
ATOM   2345 C  CA   . LYS A 1 251 ? 0.492   -3.175  34.743  1.00 12.39 ? 252 LYS A CA   1 
ATOM   2346 C  C    . LYS A 1 251 ? -0.608  -2.536  35.683  1.00 13.30 ? 252 LYS A C    1 
ATOM   2347 O  O    . LYS A 1 251 ? -1.430  -3.360  36.209  1.00 17.37 ? 252 LYS A O    1 
ATOM   2348 C  CB   . LYS A 1 251 ? 1.225   -2.079  33.941  1.00 14.94 ? 252 LYS A CB   1 
ATOM   2349 C  CG   . LYS A 1 251 ? 2.366   -2.756  33.133  1.00 17.39 ? 252 LYS A CG   1 
ATOM   2350 C  CD   . LYS A 1 251 ? 3.255   -1.805  32.569  1.00 20.83 ? 252 LYS A CD   1 
ATOM   2351 C  CE   . LYS A 1 251 ? 4.383   -2.473  31.981  1.00 19.18 ? 252 LYS A CE   1 
ATOM   2352 N  NZ   . LYS A 1 251 ? 5.270   -1.611  31.195  1.00 24.46 ? 252 LYS A NZ   1 
ATOM   2353 N  N    . ASN A 1 252 ? -0.545  -1.306  35.996  1.00 12.84 ? 253 ASN A N    1 
ATOM   2354 C  CA   . ASN A 1 252 ? -1.454  -0.797  36.978  1.00 19.44 ? 253 ASN A CA   1 
ATOM   2355 C  C    . ASN A 1 252 ? -2.806  -0.308  36.432  1.00 18.47 ? 253 ASN A C    1 
ATOM   2356 O  O    . ASN A 1 252 ? -3.014  1.002   36.418  1.00 22.10 ? 253 ASN A O    1 
ATOM   2357 C  CB   . ASN A 1 252 ? -0.779  0.419   37.637  1.00 22.70 ? 253 ASN A CB   1 
ATOM   2358 C  CG   . ASN A 1 252 ? -1.560  0.933   38.911  1.00 24.56 ? 253 ASN A CG   1 
ATOM   2359 O  OD1  . ASN A 1 252 ? -2.233  0.144   39.629  1.00 32.98 ? 253 ASN A OD1  1 
ATOM   2360 N  ND2  . ASN A 1 252 ? -1.513  2.268   39.135  1.00 27.08 ? 253 ASN A ND2  1 
ATOM   2361 N  N    . ARG A 1 253 ? -3.616  -1.344  35.907  1.00 14.44 ? 254 ARG A N    1 
ATOM   2362 C  CA   . ARG A 1 253 ? -4.849  -0.965  35.295  1.00 9.46  ? 254 ARG A CA   1 
ATOM   2363 C  C    . ARG A 1 253 ? -5.911  -1.899  35.750  1.00 12.17 ? 254 ARG A C    1 
ATOM   2364 O  O    . ARG A 1 253 ? -5.670  -3.079  36.033  1.00 14.95 ? 254 ARG A O    1 
ATOM   2365 C  CB   . ARG A 1 253 ? -4.784  -0.948  33.755  1.00 8.62  ? 254 ARG A CB   1 
ATOM   2366 C  CG   . ARG A 1 253 ? -3.863  0.198   33.208  1.00 8.66  ? 254 ARG A CG   1 
ATOM   2367 C  CD   . ARG A 1 253 ? -3.814  0.137   31.701  1.00 8.40  ? 254 ARG A CD   1 
ATOM   2368 N  NE   . ARG A 1 253 ? -2.940  -0.938  31.262  1.00 7.32  ? 254 ARG A NE   1 
ATOM   2369 C  CZ   . ARG A 1 253 ? -2.753  -1.258  29.987  1.00 6.47  ? 254 ARG A CZ   1 
ATOM   2370 N  NH1  . ARG A 1 253 ? -3.373  -0.572  29.032  1.00 7.09  ? 254 ARG A NH1  1 
ATOM   2371 N  NH2  . ARG A 1 253 ? -1.943  -2.261  29.667  1.00 6.13  ? 254 ARG A NH2  1 
ATOM   2372 N  N    . GLN A 1 254 ? -7.147  -1.410  35.746  1.00 11.88 ? 255 GLN A N    1 
ATOM   2373 C  CA   . GLN A 1 254 ? -8.337  -2.216  36.080  1.00 12.22 ? 255 GLN A CA   1 
ATOM   2374 C  C    . GLN A 1 254 ? -9.231  -2.215  34.846  1.00 12.51 ? 255 GLN A C    1 
ATOM   2375 O  O    . GLN A 1 254 ? -9.499  -1.141  34.244  1.00 14.75 ? 255 GLN A O    1 
ATOM   2376 C  CB   . GLN A 1 254 ? -9.133  -1.514  37.200  1.00 15.49 ? 255 GLN A CB   1 
ATOM   2377 C  CG   . GLN A 1 254 ? -10.480 -1.966  37.385  1.00 30.25 ? 255 GLN A CG   1 
ATOM   2378 C  CD   . GLN A 1 254 ? -10.492 -3.329  38.077  1.00 40.72 ? 255 GLN A CD   1 
ATOM   2379 O  OE1  . GLN A 1 254 ? -9.607  -3.585  38.948  1.00 48.38 ? 255 GLN A OE1  1 
ATOM   2380 N  NE2  . GLN A 1 254 ? -11.531 -4.241  37.709  1.00 38.03 ? 255 GLN A NE2  1 
ATOM   2381 N  N    . ILE A 1 255 ? -9.633  -3.399  34.419  1.00 10.10 ? 256 ILE A N    1 
ATOM   2382 C  CA   . ILE A 1 255 ? -10.631 -3.549  33.406  1.00 9.79  ? 256 ILE A CA   1 
ATOM   2383 C  C    . ILE A 1 255 ? -11.997 -3.599  34.059  1.00 9.50  ? 256 ILE A C    1 
ATOM   2384 O  O    . ILE A 1 255 ? -12.221 -4.296  35.030  1.00 11.02 ? 256 ILE A O    1 
ATOM   2385 C  CB   . ILE A 1 255 ? -10.438 -4.799  32.583  1.00 10.63 ? 256 ILE A CB   1 
ATOM   2386 C  CG1  . ILE A 1 255 ? -8.978  -4.744  32.007  1.00 11.13 ? 256 ILE A CG1  1 
ATOM   2387 C  CG2  . ILE A 1 255 ? -11.476 -4.882  31.477  1.00 10.67 ? 256 ILE A CG2  1 
ATOM   2388 C  CD1  . ILE A 1 255 ? -8.663  -5.997  31.258  1.00 12.26 ? 256 ILE A CD1  1 
ATOM   2389 N  N    . LYS A 1 256 ? -12.917 -2.728  33.566  1.00 9.21  ? 257 LYS A N    1 
ATOM   2390 C  CA   . LYS A 1 256 ? -14.266 -2.629  34.077  1.00 9.99  ? 257 LYS A CA   1 
ATOM   2391 C  C    . LYS A 1 256 ? -15.283 -3.235  33.169  1.00 9.33  ? 257 LYS A C    1 
ATOM   2392 O  O    . LYS A 1 256 ? -15.084 -3.159  31.934  1.00 10.71 ? 257 LYS A O    1 
ATOM   2393 C  CB   . LYS A 1 256 ? -14.654 -1.120  34.361  1.00 10.51 ? 257 LYS A CB   1 
ATOM   2394 C  CG   . LYS A 1 256 ? -13.688 -0.556  35.476  1.00 16.95 ? 257 LYS A CG   1 
ATOM   2395 C  CD   . LYS A 1 256 ? -14.193 0.783   35.978  1.00 21.53 ? 257 LYS A CD   1 
ATOM   2396 C  CE   . LYS A 1 256 ? -13.666 1.033   37.396  1.00 33.75 ? 257 LYS A CE   1 
ATOM   2397 N  NZ   . LYS A 1 256 ? -12.143 0.785   37.284  1.00 35.92 ? 257 LYS A NZ   1 
ATOM   2398 N  N    . ALA A 1 257 ? -16.296 -3.899  33.708  1.00 8.93  ? 258 ALA A N    1 
ATOM   2399 C  CA   . ALA A 1 257 ? -17.407 -4.515  32.938  1.00 9.82  ? 258 ALA A CA   1 
ATOM   2400 C  C    . ALA A 1 257 ? -18.683 -3.728  33.080  1.00 8.64  ? 258 ALA A C    1 
ATOM   2401 O  O    . ALA A 1 257 ? -19.006 -3.343  34.206  1.00 11.34 ? 258 ALA A O    1 
ATOM   2402 C  CB   . ALA A 1 257 ? -17.576 -6.029  33.327  1.00 11.85 ? 258 ALA A CB   1 
ATOM   2403 N  N    . SER A 1 258 ? -19.361 -3.586  31.957  1.00 9.80  ? 259 SER A N    1 
ATOM   2404 C  CA   . SER A 1 258 ? -20.635 -2.870  32.012  1.00 12.67 ? 259 SER A CA   1 
ATOM   2405 C  C    . SER A 1 258 ? -21.781 -3.758  32.439  1.00 12.42 ? 259 SER A C    1 
ATOM   2406 O  O    . SER A 1 258 ? -22.926 -3.261  32.618  1.00 15.48 ? 259 SER A O    1 
ATOM   2407 C  CB   . SER A 1 258 ? -20.963 -2.313  30.614  1.00 11.85 ? 259 SER A CB   1 
ATOM   2408 O  OG   . SER A 1 258 ? -21.424 -3.348  29.722  1.00 12.10 ? 259 SER A OG   1 
ATOM   2409 N  N    . PHE A 1 259 ? -21.523 -5.008  32.711  1.00 13.51 ? 260 PHE A N    1 
ATOM   2410 C  CA   . PHE A 1 259 ? -22.520 -6.118  32.917  1.00 15.01 ? 260 PHE A CA   1 
ATOM   2411 C  C    . PHE A 1 259 ? -22.075 -7.025  33.956  1.00 19.46 ? 260 PHE A C    1 
ATOM   2412 O  O    . PHE A 1 259 ? -20.889 -7.194  34.241  1.00 18.43 ? 260 PHE A O    1 
ATOM   2413 C  CB   . PHE A 1 259 ? -22.750 -6.866  31.577  1.00 16.60 ? 260 PHE A CB   1 
ATOM   2414 C  CG   . PHE A 1 259 ? -21.462 -7.601  31.083  1.00 14.95 ? 260 PHE A CG   1 
ATOM   2415 C  CD1  . PHE A 1 259 ? -20.454 -6.890  30.405  1.00 12.58 ? 260 PHE A CD1  1 
ATOM   2416 C  CD2  . PHE A 1 259 ? -21.189 -8.941  31.515  1.00 16.03 ? 260 PHE A CD2  1 
ATOM   2417 C  CE1  . PHE A 1 259 ? -19.258 -7.576  30.040  1.00 14.17 ? 260 PHE A CE1  1 
ATOM   2418 C  CE2  . PHE A 1 259 ? -20.070 -9.590  31.163  1.00 17.30 ? 260 PHE A CE2  1 
ATOM   2419 C  CZ   . PHE A 1 259 ? -19.039 -8.847  30.443  1.00 17.37 ? 260 PHE A CZ   1 
ATOM   2420 N  N    . LYS A 1 260 ? -23.120 -7.698  34.538  1.00 24.69 ? 261 LYS A N    1 
ATOM   2421 C  CA   . LYS A 1 260 ? -23.039 -8.947  35.384  1.00 35.86 ? 261 LYS A CA   1 
ATOM   2422 C  C    . LYS A 1 260 ? -21.912 -8.818  36.382  1.00 40.44 ? 261 LYS A C    1 
ATOM   2423 O  O    . LYS A 1 260 ? -21.374 -9.819  36.929  1.00 46.05 ? 261 LYS A O    1 
ATOM   2424 C  CB   . LYS A 1 260 ? -22.901 -10.268 34.568  1.00 34.94 ? 261 LYS A CB   1 
ATOM   2425 C  CG   . LYS A 1 260 ? -24.011 -10.476 33.530  1.00 38.18 ? 261 LYS A CG   1 
ATOM   2426 C  CD   . LYS A 1 260 ? -23.829 -11.827 32.728  1.00 38.14 ? 261 LYS A CD   1 
ATOM   2427 C  CE   . LYS A 1 260 ? -22.290 -12.029 32.487  1.00 40.44 ? 261 LYS A CE   1 
ATOM   2428 N  NZ   . LYS A 1 260 ? -21.678 -13.273 31.899  1.00 41.25 ? 261 LYS A NZ   1 
ATOM   2429 O  OXT  . LYS A 1 260 ? -21.499 -7.664  36.703  1.00 45.61 ? 261 LYS A OXT  1 
HETATM 2430 ZN ZN   . ZN  B 2 .   ? -6.654  -1.702  15.262  1.00 7.22  ? 262 ZN  A ZN   1 
HETATM 2431 S  S    . DMS C 3 .   ? -5.433  7.160   11.040  1.00 17.20 ? 263 DMS A S    1 
HETATM 2432 O  O    . DMS C 3 .   ? -6.844  6.524   10.622  1.00 16.39 ? 263 DMS A O    1 
HETATM 2433 C  C1   . DMS C 3 .   ? -5.618  8.903   10.733  1.00 17.61 ? 263 DMS A C1   1 
HETATM 2434 C  C2   . DMS C 3 .   ? -4.319  6.627   9.700   1.00 17.92 ? 263 DMS A C2   1 
HETATM 2435 S  S    . DMS D 3 .   ? 1.354   -11.700 14.897  1.00 18.19 ? 264 DMS A S    1 
HETATM 2436 O  O    . DMS D 3 .   ? 2.091   -13.108 14.345  1.00 23.11 ? 264 DMS A O    1 
HETATM 2437 C  C1   . DMS D 3 .   ? 2.411   -10.460 14.275  1.00 18.34 ? 264 DMS A C1   1 
HETATM 2438 C  C2   . DMS D 3 .   ? 1.651   -11.542 16.595  1.00 16.04 ? 264 DMS A C2   1 
HETATM 2439 N  N1   . BCN E 4 .   ? -20.349 -14.718 23.201  1.00 26.15 ? 265 BCN A N1   1 
HETATM 2440 C  C1   . BCN E 4 .   ? -19.576 -14.264 24.379  1.00 26.41 ? 265 BCN A C1   1 
HETATM 2441 C  C2   . BCN E 4 .   ? -19.811 -15.214 25.513  1.00 25.84 ? 265 BCN A C2   1 
HETATM 2442 O  O21  . BCN E 4 .   ? -20.807 -15.997 25.427  1.00 30.29 ? 265 BCN A O21  1 
HETATM 2443 O  O22  . BCN E 4 .   ? -19.341 -14.945 26.662  1.00 27.56 ? 265 BCN A O22  1 
HETATM 2444 C  C3   . BCN E 4 .   ? -20.035 -15.509 22.090  1.00 20.29 ? 265 BCN A C3   1 
HETATM 2445 C  C4   . BCN E 4 .   ? -20.196 -16.690 21.262  1.00 32.95 ? 265 BCN A C4   1 
HETATM 2446 O  O4   . BCN E 4 .   ? -21.067 -16.252 20.136  1.00 30.81 ? 265 BCN A O4   1 
HETATM 2447 C  C5   . BCN E 4 .   ? -21.587 -14.011 23.022  1.00 16.33 ? 265 BCN A C5   1 
HETATM 2448 C  C6   . BCN E 4 .   ? -21.532 -12.876 24.025  1.00 37.04 ? 265 BCN A C6   1 
HETATM 2449 O  O6   . BCN E 4 .   ? -22.644 -12.433 24.721  1.00 29.75 ? 265 BCN A O6   1 
HETATM 2450 N  N1   . E49 F 5 .   ? -0.774  4.767   10.215  1.00 20.09 ? 266 E49 A N1   1 
HETATM 2451 C  C2   . E49 F 5 .   ? -1.517  4.150   11.113  1.00 19.31 ? 266 E49 A C2   1 
HETATM 2452 N  N3   . E49 F 5 .   ? -1.889  4.728   12.258  1.00 18.89 ? 266 E49 A N3   1 
HETATM 2453 C  C4   . E49 F 5 .   ? -1.629  6.019   12.524  1.00 22.02 ? 266 E49 A C4   1 
HETATM 2454 C  C5   . E49 F 5 .   ? -0.895  6.704   11.570  1.00 24.41 ? 266 E49 A C5   1 
HETATM 2455 C  C6   . E49 F 5 .   ? -0.437  6.063   10.412  1.00 22.92 ? 266 E49 A C6   1 
HETATM 2456 S  S7   . E49 F 5 .   ? -1.931  2.501   10.707  1.00 18.94 ? 266 E49 A S7   1 
HETATM 2457 C  C8   . E49 F 5 .   ? -3.080  1.964   12.054  1.00 12.79 ? 266 E49 A C8   1 
HETATM 2458 C  C9   . E49 F 5 .   ? -4.228  2.963   12.223  1.00 11.63 ? 266 E49 A C9   1 
HETATM 2459 O  O10  . E49 F 5 .   ? -4.678  3.607   11.212  1.00 15.73 ? 266 E49 A O10  1 
HETATM 2460 C  C11  . E49 F 5 .   ? -2.170  6.731   13.796  1.00 18.31 ? 266 E49 A C11  1 
HETATM 2461 C  C12  . E49 F 5 .   ? 0.406   6.742   9.444   1.00 22.79 ? 266 E49 A C12  1 
HETATM 2462 C  C13  . E49 F 5 .   ? -4.844  3.121   13.586  1.00 9.17  ? 266 E49 A C13  1 
HETATM 2463 C  C14  . E49 F 5 .   ? -5.059  2.085   14.456  1.00 9.02  ? 266 E49 A C14  1 
HETATM 2464 C  C15  . E49 F 5 .   ? -5.636  2.276   15.637  1.00 7.78  ? 266 E49 A C15  1 
HETATM 2465 C  C16  . E49 F 5 .   ? -6.197  3.492   15.925  1.00 10.80 ? 266 E49 A C16  1 
HETATM 2466 C  C17  . E49 F 5 .   ? -5.933  4.636   15.135  1.00 10.46 ? 266 E49 A C17  1 
HETATM 2467 C  C18  . E49 F 5 .   ? -5.428  4.359   13.957  1.00 10.11 ? 266 E49 A C18  1 
HETATM 2468 S  S19  . E49 F 5 .   ? -5.954  0.835   16.689  1.00 7.88  ? 266 E49 A S19  1 
HETATM 2469 O  O20  . E49 F 5 .   ? -7.458  0.784   16.722  1.00 7.94  ? 266 E49 A O20  1 
HETATM 2470 O  O22  . E49 F 5 .   ? -5.356  1.046   17.954  1.00 9.49  ? 266 E49 A O22  1 
HETATM 2471 N  N23  . E49 F 5 .   ? -5.297  -0.506  16.058  1.00 7.86  ? 266 E49 A N23  1 
HETATM 2472 CL CL21 . E49 F 5 .   ? -6.849  3.818   17.458  1.00 10.34 ? 266 E49 A CL21 1 
HETATM 2473 O  O    . HOH G 6 .   ? -5.054  2.245   37.198  1.00 28.61 ? 126 HOH A O    1 
HETATM 2474 O  O    . HOH G 6 .   ? 1.472   -16.218 18.056  1.00 39.27 ? 267 HOH A O    1 
HETATM 2475 O  O    . HOH G 6 .   ? -1.161  5.851   40.786  1.00 35.06 ? 268 HOH A O    1 
HETATM 2476 O  O    . HOH G 6 .   ? 6.875   -8.216  -9.870  1.00 37.56 ? 269 HOH A O    1 
HETATM 2477 O  O    . HOH G 6 .   ? -25.928 8.080   6.179   1.00 35.99 ? 270 HOH A O    1 
HETATM 2478 O  O    . HOH G 6 .   ? -20.309 13.693  29.235  1.00 37.34 ? 271 HOH A O    1 
HETATM 2479 O  O    . HOH G 6 .   ? -0.469  1.070   -10.724 1.00 30.41 ? 272 HOH A O    1 
HETATM 2480 O  O    . HOH G 6 .   ? 5.774   -12.384 11.697  1.00 36.08 ? 273 HOH A O    1 
HETATM 2481 O  O    . HOH G 6 .   ? -23.885 11.019  14.859  1.00 37.66 ? 274 HOH A O    1 
HETATM 2482 O  O    . HOH G 6 .   ? -3.595  5.820   -2.819  1.00 29.72 ? 275 HOH A O    1 
HETATM 2483 O  O    . HOH G 6 .   ? -23.555 -17.865 6.117   1.00 43.11 ? 276 HOH A O    1 
HETATM 2484 O  O    . HOH G 6 .   ? -19.668 16.964  23.361  1.00 35.50 ? 277 HOH A O    1 
HETATM 2485 O  O    . HOH G 6 .   ? -17.836 -12.069 31.639  1.00 27.71 ? 278 HOH A O    1 
HETATM 2486 O  O    . HOH G 6 .   ? -16.027 3.596   35.440  1.00 31.77 ? 279 HOH A O    1 
HETATM 2487 O  O    . HOH G 6 .   ? -7.004  -8.399  -7.182  1.00 35.00 ? 280 HOH A O    1 
HETATM 2488 O  O    . HOH G 6 .   ? -24.976 -11.149 23.851  1.00 29.93 ? 281 HOH A O    1 
HETATM 2489 O  O    . HOH G 6 .   ? 4.312   -10.882 -7.255  1.00 32.11 ? 282 HOH A O    1 
HETATM 2490 O  O    . HOH G 6 .   ? -17.108 0.404   -3.782  1.00 40.82 ? 283 HOH A O    1 
HETATM 2491 O  O    . HOH G 6 .   ? -24.216 -14.150 19.520  1.00 31.89 ? 284 HOH A O    1 
HETATM 2492 O  O    . HOH G 6 .   ? -3.352  21.034  27.009  1.00 31.72 ? 285 HOH A O    1 
HETATM 2493 O  O    . HOH G 6 .   ? -25.472 4.403   4.133   1.00 30.30 ? 286 HOH A O    1 
HETATM 2494 O  O    . HOH G 6 .   ? -4.428  -21.250 5.461   1.00 30.99 ? 287 HOH A O    1 
HETATM 2495 O  O    . HOH G 6 .   ? -24.119 -3.460  4.177   1.00 34.81 ? 288 HOH A O    1 
HETATM 2496 O  O    . HOH G 6 .   ? 2.041   -7.082  -8.232  1.00 30.44 ? 289 HOH A O    1 
HETATM 2497 O  O    . HOH G 6 .   ? -5.045  -7.876  -8.545  1.00 40.65 ? 290 HOH A O    1 
HETATM 2498 O  O    . HOH G 6 .   ? 6.267   5.388   28.846  1.00 31.68 ? 291 HOH A O    1 
HETATM 2499 O  O    . HOH G 6 .   ? -4.552  -5.709  -8.059  1.00 37.35 ? 292 HOH A O    1 
HETATM 2500 O  O    . HOH G 6 .   ? -24.354 -7.815  37.337  1.00 42.65 ? 293 HOH A O    1 
HETATM 2501 O  O    . HOH G 6 .   ? -1.720  17.913  15.162  1.00 32.38 ? 294 HOH A O    1 
HETATM 2502 O  O    . HOH G 6 .   ? 9.939   6.575   13.734  1.00 41.56 ? 295 HOH A O    1 
HETATM 2503 O  O    . HOH G 6 .   ? 7.145   3.119   31.778  1.00 45.79 ? 296 HOH A O    1 
HETATM 2504 O  O    . HOH G 6 .   ? -12.771 -22.411 12.225  1.00 30.68 ? 297 HOH A O    1 
HETATM 2505 O  O    . HOH G 6 .   ? -14.058 3.468   33.242  1.00 28.50 ? 298 HOH A O    1 
HETATM 2506 O  O    . HOH G 6 .   ? -15.298 8.461   34.889  1.00 36.26 ? 299 HOH A O    1 
HETATM 2507 O  O    . HOH G 6 .   ? -1.904  16.357  12.450  1.00 30.58 ? 300 HOH A O    1 
HETATM 2508 O  O    . HOH G 6 .   ? -19.733 14.966  16.510  1.00 23.99 ? 301 HOH A O    1 
HETATM 2509 O  O    . HOH G 6 .   ? -12.248 13.353  4.817   1.00 27.04 ? 302 HOH A O    1 
HETATM 2510 O  O    . HOH G 6 .   ? -16.458 7.339   36.416  1.00 28.85 ? 303 HOH A O    1 
HETATM 2511 O  O    . HOH G 6 .   ? 1.957   8.036   12.546  1.00 30.00 ? 304 HOH A O    1 
HETATM 2512 O  O    . HOH G 6 .   ? -1.255  -3.944  15.727  1.00 8.08  ? 305 HOH A O    1 
HETATM 2513 O  O    . HOH G 6 .   ? -17.006 -8.436  20.417  1.00 8.56  ? 306 HOH A O    1 
HETATM 2514 O  O    . HOH G 6 .   ? -4.528  -13.549 18.047  1.00 8.36  ? 307 HOH A O    1 
HETATM 2515 O  O    . HOH G 6 .   ? -3.531  -11.168 20.882  1.00 8.11  ? 308 HOH A O    1 
HETATM 2516 O  O    . HOH G 6 .   ? -10.610 8.641   25.599  1.00 8.65  ? 309 HOH A O    1 
HETATM 2517 O  O    A HOH G 6 .   ? -21.540 -7.133  23.193  0.50 9.70  ? 310 HOH A O    1 
HETATM 2518 O  O    B HOH G 6 .   ? -21.629 -7.177  23.950  0.50 8.77  ? 310 HOH A O    1 
HETATM 2519 O  O    . HOH G 6 .   ? -7.972  -15.403 11.334  1.00 9.60  ? 311 HOH A O    1 
HETATM 2520 O  O    . HOH G 6 .   ? -8.766  -3.825  7.876   1.00 10.12 ? 312 HOH A O    1 
HETATM 2521 O  O    . HOH G 6 .   ? -3.419  -13.291 25.126  1.00 9.78  ? 313 HOH A O    1 
HETATM 2522 O  O    . HOH G 6 .   ? -3.784  -15.928 24.348  1.00 11.04 ? 314 HOH A O    1 
HETATM 2523 O  O    . HOH G 6 .   ? -17.962 -20.376 7.954   1.00 12.36 ? 315 HOH A O    1 
HETATM 2524 O  O    . HOH G 6 .   ? 1.213   -1.540  29.437  1.00 13.67 ? 316 HOH A O    1 
HETATM 2525 O  O    . HOH G 6 .   ? 4.844   -4.885  20.907  1.00 12.48 ? 317 HOH A O    1 
HETATM 2526 O  O    . HOH G 6 .   ? -10.386 -18.290 17.026  1.00 10.71 ? 318 HOH A O    1 
HETATM 2527 O  O    . HOH G 6 .   ? -2.498  -8.771  29.113  1.00 11.33 ? 319 HOH A O    1 
HETATM 2528 O  O    . HOH G 6 .   ? -12.856 -17.203 16.816  1.00 11.76 ? 320 HOH A O    1 
HETATM 2529 O  O    . HOH G 6 .   ? -2.082  -12.329 22.796  1.00 8.54  ? 321 HOH A O    1 
HETATM 2530 O  O    . HOH G 6 .   ? -8.202  -19.390 21.585  1.00 11.83 ? 322 HOH A O    1 
HETATM 2531 O  O    . HOH G 6 .   ? 8.480   -3.859  21.072  1.00 13.30 ? 323 HOH A O    1 
HETATM 2532 O  O    . HOH G 6 .   ? -13.432 -18.549 14.584  1.00 12.73 ? 324 HOH A O    1 
HETATM 2533 O  O    A HOH G 6 .   ? 3.416   4.993   30.056  0.50 14.75 ? 325 HOH A O    1 
HETATM 2534 O  O    B HOH G 6 .   ? 3.930   5.139   29.412  0.50 15.57 ? 325 HOH A O    1 
HETATM 2535 O  O    . HOH G 6 .   ? -9.432  -8.008  34.104  1.00 17.85 ? 326 HOH A O    1 
HETATM 2536 O  O    . HOH G 6 .   ? -13.951 10.324  27.944  1.00 15.56 ? 327 HOH A O    1 
HETATM 2537 O  O    . HOH G 6 .   ? -16.089 -12.348 24.420  1.00 12.95 ? 328 HOH A O    1 
HETATM 2538 O  O    . HOH G 6 .   ? -24.129 8.585   20.213  1.00 16.92 ? 329 HOH A O    1 
HETATM 2539 O  O    A HOH G 6 .   ? -22.111 5.669   4.895   0.50 9.90  ? 330 HOH A O    1 
HETATM 2540 O  O    B HOH G 6 .   ? -21.213 5.811   4.610   0.50 13.11 ? 330 HOH A O    1 
HETATM 2541 O  O    . HOH G 6 .   ? 2.648   -4.257  7.871   1.00 18.09 ? 331 HOH A O    1 
HETATM 2542 O  O    . HOH G 6 .   ? -17.971 10.697  11.354  1.00 15.85 ? 332 HOH A O    1 
HETATM 2543 O  O    . HOH G 6 .   ? -16.093 15.860  23.810  1.00 15.15 ? 333 HOH A O    1 
HETATM 2544 O  O    . HOH G 6 .   ? -16.301 -9.982  32.961  1.00 15.95 ? 334 HOH A O    1 
HETATM 2545 O  O    . HOH G 6 .   ? 1.190   8.808   24.377  1.00 15.84 ? 335 HOH A O    1 
HETATM 2546 O  O    A HOH G 6 .   ? -0.074  -1.067  -4.818  0.50 7.54  ? 336 HOH A O    1 
HETATM 2547 O  O    B HOH G 6 .   ? 0.802   -1.250  -4.553  0.50 14.30 ? 336 HOH A O    1 
HETATM 2548 O  O    . HOH G 6 .   ? -7.891  -22.170 10.427  1.00 16.95 ? 337 HOH A O    1 
HETATM 2549 O  O    . HOH G 6 .   ? -19.276 10.075  8.886   1.00 13.88 ? 338 HOH A O    1 
HETATM 2550 O  O    . HOH G 6 .   ? -24.795 -7.668  8.959   1.00 17.85 ? 339 HOH A O    1 
HETATM 2551 O  O    . HOH G 6 .   ? -10.608 -19.413 20.012  1.00 14.66 ? 340 HOH A O    1 
HETATM 2552 O  O    . HOH G 6 .   ? -20.310 10.681  26.828  1.00 14.71 ? 341 HOH A O    1 
HETATM 2553 O  O    . HOH G 6 .   ? -6.759  -20.277 19.495  1.00 11.11 ? 342 HOH A O    1 
HETATM 2554 O  O    A HOH G 6 .   ? -21.096 -12.636 -1.619  0.50 13.75 ? 343 HOH A O    1 
HETATM 2555 O  O    B HOH G 6 .   ? -20.600 -12.570 -2.096  0.50 14.92 ? 343 HOH A O    1 
HETATM 2556 O  O    . HOH G 6 .   ? -13.051 -16.839 26.673  1.00 14.26 ? 344 HOH A O    1 
HETATM 2557 O  O    . HOH G 6 .   ? -12.008 2.721   30.891  1.00 16.76 ? 345 HOH A O    1 
HETATM 2558 O  O    . HOH G 6 .   ? 5.352   7.065   20.236  1.00 15.53 ? 346 HOH A O    1 
HETATM 2559 O  O    . HOH G 6 .   ? -13.831 -21.240 15.116  1.00 14.55 ? 347 HOH A O    1 
HETATM 2560 O  O    . HOH G 6 .   ? -2.614  -3.185  11.366  1.00 14.89 ? 348 HOH A O    1 
HETATM 2561 O  O    . HOH G 6 .   ? -22.155 -18.233 13.456  1.00 20.00 ? 349 HOH A O    1 
HETATM 2562 O  O    . HOH G 6 .   ? -4.738  0.981   43.428  1.00 20.17 ? 350 HOH A O    1 
HETATM 2563 O  O    . HOH G 6 .   ? -6.893  5.957   6.386   1.00 16.77 ? 351 HOH A O    1 
HETATM 2564 O  O    . HOH G 6 .   ? -14.968 -21.187 17.650  1.00 15.74 ? 352 HOH A O    1 
HETATM 2565 O  O    . HOH G 6 .   ? -8.428  -19.831 26.609  1.00 17.61 ? 353 HOH A O    1 
HETATM 2566 O  O    . HOH G 6 .   ? -23.167 -2.970  6.614   1.00 20.79 ? 354 HOH A O    1 
HETATM 2567 O  O    . HOH G 6 .   ? 1.371   -11.763 25.075  1.00 21.10 ? 355 HOH A O    1 
HETATM 2568 O  O    . HOH G 6 .   ? -14.692 -18.546 18.712  1.00 14.10 ? 356 HOH A O    1 
HETATM 2569 O  O    . HOH G 6 .   ? 7.564   6.099   21.718  1.00 15.40 ? 357 HOH A O    1 
HETATM 2570 O  O    . HOH G 6 .   ? -2.013  -17.476 25.609  1.00 23.74 ? 358 HOH A O    1 
HETATM 2571 O  O    . HOH G 6 .   ? -0.479  10.854  23.479  1.00 14.55 ? 359 HOH A O    1 
HETATM 2572 O  O    . HOH G 6 .   ? 4.190   -3.466  26.518  1.00 16.93 ? 360 HOH A O    1 
HETATM 2573 O  O    . HOH G 6 .   ? -1.220  9.322   27.885  1.00 20.14 ? 361 HOH A O    1 
HETATM 2574 O  O    . HOH G 6 .   ? -1.457  -13.142 27.045  1.00 22.94 ? 362 HOH A O    1 
HETATM 2575 O  O    . HOH G 6 .   ? -22.935 -11.660 13.928  1.00 20.01 ? 363 HOH A O    1 
HETATM 2576 O  O    . HOH G 6 .   ? -9.019  -5.850  35.879  1.00 18.27 ? 364 HOH A O    1 
HETATM 2577 O  O    . HOH G 6 .   ? -22.870 -5.867  2.662   1.00 19.28 ? 365 HOH A O    1 
HETATM 2578 O  O    . HOH G 6 .   ? -10.227 14.644  12.284  1.00 15.95 ? 366 HOH A O    1 
HETATM 2579 O  O    . HOH G 6 .   ? -23.963 -0.748  26.526  1.00 16.90 ? 367 HOH A O    1 
HETATM 2580 O  O    . HOH G 6 .   ? -15.358 -21.829 13.064  1.00 15.56 ? 368 HOH A O    1 
HETATM 2581 O  O    . HOH G 6 .   ? -26.723 -2.428  14.471  1.00 19.40 ? 369 HOH A O    1 
HETATM 2582 O  O    . HOH G 6 .   ? -16.776 -13.952 26.387  1.00 14.92 ? 370 HOH A O    1 
HETATM 2583 O  O    . HOH G 6 .   ? -4.656  -11.944 32.043  1.00 19.44 ? 371 HOH A O    1 
HETATM 2584 O  O    . HOH G 6 .   ? -30.823 1.382   25.937  1.00 23.36 ? 372 HOH A O    1 
HETATM 2585 O  O    . HOH G 6 .   ? -17.614 -21.078 17.519  1.00 20.14 ? 373 HOH A O    1 
HETATM 2586 O  O    . HOH G 6 .   ? -17.412 -16.187 22.007  1.00 18.42 ? 374 HOH A O    1 
HETATM 2587 O  O    . HOH G 6 .   ? -2.366  7.256   -5.158  1.00 17.69 ? 375 HOH A O    1 
HETATM 2588 O  O    . HOH G 6 .   ? 8.358   -5.817  -10.399 1.00 23.58 ? 376 HOH A O    1 
HETATM 2589 O  O    . HOH G 6 .   ? -7.292  -8.684  32.574  1.00 16.07 ? 377 HOH A O    1 
HETATM 2590 O  O    . HOH G 6 .   ? -14.230 -16.722 29.038  1.00 20.82 ? 378 HOH A O    1 
HETATM 2591 O  O    . HOH G 6 .   ? -28.677 0.254   24.528  1.00 19.83 ? 379 HOH A O    1 
HETATM 2592 O  O    . HOH G 6 .   ? -26.225 3.462   15.466  1.00 21.98 ? 380 HOH A O    1 
HETATM 2593 O  O    . HOH G 6 .   ? 4.816   -12.893 -5.873  1.00 18.54 ? 381 HOH A O    1 
HETATM 2594 O  O    . HOH G 6 .   ? -3.618  -12.919 -2.924  1.00 20.81 ? 382 HOH A O    1 
HETATM 2595 O  O    . HOH G 6 .   ? -16.944 -18.006 20.055  1.00 20.66 ? 383 HOH A O    1 
HETATM 2596 O  O    . HOH G 6 .   ? -6.936  -14.900 31.602  1.00 20.40 ? 384 HOH A O    1 
HETATM 2597 O  O    . HOH G 6 .   ? -1.127  -11.186 28.974  1.00 16.61 ? 385 HOH A O    1 
HETATM 2598 O  O    . HOH G 6 .   ? -6.030  -4.655  -6.504  1.00 22.24 ? 386 HOH A O    1 
HETATM 2599 O  O    . HOH G 6 .   ? -14.027 14.255  27.186  1.00 20.08 ? 387 HOH A O    1 
HETATM 2600 O  O    . HOH G 6 .   ? -23.395 -13.141 11.278  1.00 20.38 ? 388 HOH A O    1 
HETATM 2601 O  O    . HOH G 6 .   ? -4.276  -1.113  11.822  1.00 17.05 ? 389 HOH A O    1 
HETATM 2602 O  O    . HOH G 6 .   ? -23.888 -0.778  4.023   1.00 23.04 ? 390 HOH A O    1 
HETATM 2603 O  O    . HOH G 6 .   ? -6.299  -19.730 23.804  1.00 19.43 ? 391 HOH A O    1 
HETATM 2604 O  O    . HOH G 6 .   ? -11.086 -19.539 7.232   1.00 27.25 ? 392 HOH A O    1 
HETATM 2605 O  O    . HOH G 6 .   ? -10.574 8.438   7.757   1.00 19.68 ? 393 HOH A O    1 
HETATM 2606 O  O    . HOH G 6 .   ? -0.692  -8.613  32.479  1.00 21.80 ? 394 HOH A O    1 
HETATM 2607 O  O    . HOH G 6 .   ? -20.806 1.008   -6.613  1.00 23.40 ? 395 HOH A O    1 
HETATM 2608 O  O    . HOH G 6 .   ? -6.996  0.183   44.721  1.00 17.25 ? 396 HOH A O    1 
HETATM 2609 O  O    . HOH G 6 .   ? -26.832 -3.975  25.006  1.00 21.46 ? 397 HOH A O    1 
HETATM 2610 O  O    . HOH G 6 .   ? -29.054 -5.847  24.310  1.00 22.20 ? 398 HOH A O    1 
HETATM 2611 O  O    . HOH G 6 .   ? 2.452   -11.393 9.518   1.00 19.91 ? 399 HOH A O    1 
HETATM 2612 O  O    . HOH G 6 .   ? -19.887 -16.818 2.829   1.00 25.71 ? 400 HOH A O    1 
HETATM 2613 O  O    . HOH G 6 .   ? 4.377   -6.452  7.857   1.00 20.60 ? 401 HOH A O    1 
HETATM 2614 O  O    . HOH G 6 .   ? -10.965 -15.117 34.130  1.00 24.85 ? 402 HOH A O    1 
HETATM 2615 O  O    . HOH G 6 .   ? -25.844 6.237   27.090  1.00 23.05 ? 403 HOH A O    1 
HETATM 2616 O  O    . HOH G 6 .   ? -17.838 -21.993 5.880   1.00 17.35 ? 404 HOH A O    1 
HETATM 2617 O  O    . HOH G 6 .   ? 6.211   -5.390  -11.857 1.00 21.97 ? 405 HOH A O    1 
HETATM 2618 O  O    . HOH G 6 .   ? -30.634 -7.054  22.295  1.00 27.64 ? 406 HOH A O    1 
HETATM 2619 O  O    . HOH G 6 .   ? 4.333   -2.625  28.949  1.00 23.69 ? 407 HOH A O    1 
HETATM 2620 O  O    . HOH G 6 .   ? -9.627  -25.517 7.927   1.00 19.36 ? 408 HOH A O    1 
HETATM 2621 O  O    . HOH G 6 .   ? -26.442 -11.489 2.106   1.00 21.15 ? 409 HOH A O    1 
HETATM 2622 O  O    . HOH G 6 .   ? -4.802  0.210   9.430   1.00 23.76 ? 410 HOH A O    1 
HETATM 2623 O  O    . HOH G 6 .   ? 8.054   -13.005 -8.372  1.00 18.17 ? 411 HOH A O    1 
HETATM 2624 O  O    . HOH G 6 .   ? -33.524 -4.683  23.723  1.00 24.07 ? 412 HOH A O    1 
HETATM 2625 O  O    . HOH G 6 .   ? -18.530 -21.143 14.708  1.00 18.89 ? 413 HOH A O    1 
HETATM 2626 O  O    . HOH G 6 .   ? 1.742   12.454  22.792  1.00 25.04 ? 414 HOH A O    1 
HETATM 2627 O  O    . HOH G 6 .   ? -4.854  -20.636 21.349  1.00 17.64 ? 415 HOH A O    1 
HETATM 2628 O  O    . HOH G 6 .   ? -1.112  5.299   36.809  1.00 30.46 ? 416 HOH A O    1 
HETATM 2629 O  O    . HOH G 6 .   ? -0.237  -14.295 22.182  1.00 22.14 ? 417 HOH A O    1 
HETATM 2630 O  O    . HOH G 6 .   ? -13.012 -22.185 8.570   1.00 19.82 ? 418 HOH A O    1 
HETATM 2631 O  O    . HOH G 6 .   ? -25.547 -10.559 17.660  1.00 23.28 ? 419 HOH A O    1 
HETATM 2632 O  O    . HOH G 6 .   ? -9.161  5.795   29.096  1.00 17.68 ? 420 HOH A O    1 
HETATM 2633 O  O    . HOH G 6 .   ? -25.038 9.602   12.994  1.00 27.36 ? 421 HOH A O    1 
HETATM 2634 O  O    . HOH G 6 .   ? 1.380   -6.487  34.386  1.00 23.74 ? 422 HOH A O    1 
HETATM 2635 O  O    . HOH G 6 .   ? -26.380 2.775   20.985  1.00 24.40 ? 423 HOH A O    1 
HETATM 2636 O  O    . HOH G 6 .   ? -0.319  -19.853 6.723   1.00 24.23 ? 424 HOH A O    1 
HETATM 2637 O  O    . HOH G 6 .   ? 4.970   -7.476  22.319  1.00 24.03 ? 425 HOH A O    1 
HETATM 2638 O  O    . HOH G 6 .   ? -18.370 -3.693  -2.641  1.00 27.30 ? 426 HOH A O    1 
HETATM 2639 O  O    . HOH G 6 .   ? -3.373  -23.052 21.407  1.00 20.99 ? 427 HOH A O    1 
HETATM 2640 O  O    . HOH G 6 .   ? -8.452  0.708   -6.485  1.00 27.37 ? 428 HOH A O    1 
HETATM 2641 O  O    . HOH G 6 .   ? -0.979  -17.515 17.898  1.00 28.08 ? 429 HOH A O    1 
HETATM 2642 O  O    . HOH G 6 .   ? -23.299 -11.256 17.064  1.00 28.54 ? 430 HOH A O    1 
HETATM 2643 O  O    . HOH G 6 .   ? -26.089 -6.027  13.139  1.00 30.26 ? 431 HOH A O    1 
HETATM 2644 O  O    . HOH G 6 .   ? -12.380 12.560  29.198  1.00 23.98 ? 432 HOH A O    1 
HETATM 2645 O  O    . HOH G 6 .   ? -19.376 -20.662 4.944   1.00 23.59 ? 433 HOH A O    1 
HETATM 2646 O  O    . HOH G 6 .   ? -10.982 15.317  32.234  1.00 18.73 ? 434 HOH A O    1 
HETATM 2647 O  O    . HOH G 6 .   ? -30.434 -0.363  16.103  1.00 22.39 ? 435 HOH A O    1 
HETATM 2648 O  O    . HOH G 6 .   ? -2.034  -11.880 31.562  1.00 26.19 ? 436 HOH A O    1 
HETATM 2649 O  O    . HOH G 6 .   ? -33.740 2.946   27.723  1.00 26.51 ? 437 HOH A O    1 
HETATM 2650 O  O    . HOH G 6 .   ? -18.464 -12.284 -3.643  1.00 23.70 ? 438 HOH A O    1 
HETATM 2651 O  O    . HOH G 6 .   ? -2.918  7.121   -8.124  1.00 25.37 ? 439 HOH A O    1 
HETATM 2652 O  O    . HOH G 6 .   ? -4.723  -15.818 0.712   1.00 24.02 ? 440 HOH A O    1 
HETATM 2653 O  O    . HOH G 6 .   ? -10.369 -27.522 8.779   1.00 22.67 ? 441 HOH A O    1 
HETATM 2654 O  O    . HOH G 6 .   ? 0.249   0.068   -14.924 1.00 28.97 ? 442 HOH A O    1 
HETATM 2655 O  O    . HOH G 6 .   ? -17.583 -19.528 35.160  1.00 22.86 ? 443 HOH A O    1 
HETATM 2656 O  O    . HOH G 6 .   ? 11.121  -3.263  -12.161 1.00 19.84 ? 444 HOH A O    1 
HETATM 2657 O  O    . HOH G 6 .   ? -17.873 13.503  -0.337  1.00 27.89 ? 445 HOH A O    1 
HETATM 2658 O  O    . HOH G 6 .   ? 0.200   -14.338 31.035  1.00 27.64 ? 446 HOH A O    1 
HETATM 2659 O  O    . HOH G 6 .   ? -24.593 4.796   8.109   1.00 33.35 ? 447 HOH A O    1 
HETATM 2660 O  O    . HOH G 6 .   ? -21.197 -20.520 14.709  1.00 26.96 ? 448 HOH A O    1 
HETATM 2661 O  O    . HOH G 6 .   ? 3.763   9.760   23.818  1.00 29.50 ? 449 HOH A O    1 
HETATM 2662 O  O    . HOH G 6 .   ? -8.473  -1.346  41.099  1.00 26.68 ? 450 HOH A O    1 
HETATM 2663 O  O    . HOH G 6 .   ? -7.225  -16.708 1.390   1.00 19.59 ? 451 HOH A O    1 
HETATM 2664 O  O    . HOH G 6 .   ? -0.500  13.822  16.053  1.00 24.58 ? 452 HOH A O    1 
HETATM 2665 O  O    . HOH G 6 .   ? -23.280 -0.648  34.387  1.00 28.91 ? 453 HOH A O    1 
HETATM 2666 O  O    . HOH G 6 .   ? -25.219 11.058  19.544  1.00 22.86 ? 454 HOH A O    1 
HETATM 2667 O  O    . HOH G 6 .   ? 1.965   -15.567 9.246   1.00 20.50 ? 455 HOH A O    1 
HETATM 2668 O  O    . HOH G 6 .   ? -16.527 5.381   -7.838  1.00 27.18 ? 456 HOH A O    1 
HETATM 2669 O  O    . HOH G 6 .   ? -4.862  -7.454  37.729  1.00 25.96 ? 457 HOH A O    1 
HETATM 2670 O  O    . HOH G 6 .   ? -10.595 -19.031 34.266  1.00 23.79 ? 458 HOH A O    1 
HETATM 2671 O  O    . HOH G 6 .   ? -8.444  -17.466 34.850  1.00 23.87 ? 459 HOH A O    1 
HETATM 2672 O  O    . HOH G 6 .   ? -9.141  5.175   32.980  1.00 24.29 ? 460 HOH A O    1 
HETATM 2673 O  O    . HOH G 6 .   ? -1.358  11.423  25.975  1.00 25.31 ? 461 HOH A O    1 
HETATM 2674 O  O    . HOH G 6 .   ? -5.867  -23.525 27.487  1.00 29.29 ? 462 HOH A O    1 
HETATM 2675 O  O    . HOH G 6 .   ? -22.671 -9.679  25.304  1.00 22.58 ? 463 HOH A O    1 
HETATM 2676 O  O    . HOH G 6 .   ? -2.523  6.276   5.849   1.00 28.15 ? 464 HOH A O    1 
HETATM 2677 O  O    . HOH G 6 .   ? 1.569   3.040   -5.024  1.00 33.01 ? 465 HOH A O    1 
HETATM 2678 O  O    . HOH G 6 .   ? 3.921   -11.892 23.398  1.00 37.53 ? 466 HOH A O    1 
HETATM 2679 O  O    . HOH G 6 .   ? 1.056   3.019   1.811   1.00 25.42 ? 467 HOH A O    1 
HETATM 2680 O  O    . HOH G 6 .   ? 6.441   -5.488  3.747   1.00 33.19 ? 468 HOH A O    1 
HETATM 2681 O  O    . HOH G 6 .   ? -7.365  -8.791  -2.383  1.00 28.55 ? 469 HOH A O    1 
HETATM 2682 O  O    . HOH G 6 .   ? -29.092 11.587  3.238   1.00 27.59 ? 470 HOH A O    1 
HETATM 2683 O  O    . HOH G 6 .   ? -5.199  3.678   -5.648  1.00 26.21 ? 471 HOH A O    1 
HETATM 2684 O  O    . HOH G 6 .   ? -27.482 0.032   15.047  1.00 28.08 ? 472 HOH A O    1 
HETATM 2685 O  O    . HOH G 6 .   ? -15.270 -16.324 25.494  1.00 30.56 ? 473 HOH A O    1 
HETATM 2686 O  O    . HOH G 6 .   ? -9.309  -10.005 -1.308  1.00 24.01 ? 474 HOH A O    1 
HETATM 2687 O  O    . HOH G 6 .   ? -28.173 5.743   19.126  1.00 26.90 ? 475 HOH A O    1 
HETATM 2688 O  O    . HOH G 6 .   ? -21.980 -14.102 18.498  1.00 24.99 ? 476 HOH A O    1 
HETATM 2689 O  O    . HOH G 6 .   ? -12.813 7.730   29.111  1.00 23.85 ? 477 HOH A O    1 
HETATM 2690 O  O    . HOH G 6 .   ? -14.569 -8.335  -5.464  1.00 27.74 ? 478 HOH A O    1 
HETATM 2691 O  O    . HOH G 6 .   ? -2.245  -4.499  -7.092  1.00 25.67 ? 479 HOH A O    1 
HETATM 2692 O  O    . HOH G 6 .   ? -31.971 -2.433  13.767  1.00 22.08 ? 480 HOH A O    1 
HETATM 2693 O  O    . HOH G 6 .   ? -4.299  -8.535  31.170  1.00 21.09 ? 481 HOH A O    1 
HETATM 2694 O  O    . HOH G 6 .   ? -11.496 1.301   -7.755  1.00 31.57 ? 482 HOH A O    1 
HETATM 2695 O  O    . HOH G 6 .   ? 7.435   -7.895  -0.794  1.00 23.91 ? 483 HOH A O    1 
HETATM 2696 O  O    . HOH G 6 .   ? -25.036 8.805   26.191  1.00 29.70 ? 484 HOH A O    1 
HETATM 2697 O  O    . HOH G 6 .   ? -20.662 8.320   30.151  1.00 28.07 ? 485 HOH A O    1 
HETATM 2698 O  O    . HOH G 6 .   ? -29.190 -3.708  13.535  1.00 25.38 ? 486 HOH A O    1 
HETATM 2699 O  O    . HOH G 6 .   ? -11.037 1.106   33.595  1.00 24.81 ? 487 HOH A O    1 
HETATM 2700 O  O    . HOH G 6 .   ? 2.382   4.638   12.077  1.00 31.25 ? 488 HOH A O    1 
HETATM 2701 O  O    . HOH G 6 .   ? 9.978   -5.602  -5.811  1.00 26.13 ? 489 HOH A O    1 
HETATM 2702 O  O    . HOH G 6 .   ? -23.081 -17.072 3.356   1.00 30.49 ? 490 HOH A O    1 
HETATM 2703 O  O    . HOH G 6 .   ? -6.707  -22.222 7.945   1.00 25.31 ? 491 HOH A O    1 
HETATM 2704 O  O    . HOH G 6 .   ? -19.999 -25.231 19.021  1.00 26.18 ? 492 HOH A O    1 
HETATM 2705 O  O    . HOH G 6 .   ? 2.034   8.161   27.980  1.00 28.26 ? 493 HOH A O    1 
HETATM 2706 O  O    . HOH G 6 .   ? 9.893   -3.013  -10.065 1.00 24.17 ? 494 HOH A O    1 
HETATM 2707 O  O    . HOH G 6 .   ? -12.817 3.598   -6.866  1.00 24.79 ? 495 HOH A O    1 
HETATM 2708 O  O    . HOH G 6 .   ? -26.831 -1.288  26.017  1.00 22.62 ? 496 HOH A O    1 
HETATM 2709 O  O    . HOH G 6 .   ? -15.232 -10.266 37.497  1.00 29.09 ? 497 HOH A O    1 
HETATM 2710 O  O    . HOH G 6 .   ? -2.631  -19.194 21.571  1.00 25.67 ? 498 HOH A O    1 
HETATM 2711 O  O    . HOH G 6 .   ? 1.714   -16.255 -7.558  1.00 28.14 ? 499 HOH A O    1 
HETATM 2712 O  O    . HOH G 6 .   ? -24.677 12.017  6.307   1.00 25.02 ? 500 HOH A O    1 
HETATM 2713 O  O    . HOH G 6 .   ? -11.691 -24.809 8.890   1.00 26.68 ? 501 HOH A O    1 
HETATM 2714 O  O    . HOH G 6 .   ? -6.020  -20.939 26.270  1.00 27.13 ? 502 HOH A O    1 
HETATM 2715 O  O    . HOH G 6 .   ? -17.882 -20.627 -1.412  1.00 27.33 ? 503 HOH A O    1 
HETATM 2716 O  O    . HOH G 6 .   ? -24.818 -9.367  1.912   1.00 23.61 ? 504 HOH A O    1 
HETATM 2717 O  O    . HOH G 6 .   ? -10.428 4.898   30.864  1.00 23.04 ? 505 HOH A O    1 
HETATM 2718 O  O    . HOH G 6 .   ? 11.959  -9.779  -5.698  1.00 26.71 ? 506 HOH A O    1 
HETATM 2719 O  O    . HOH G 6 .   ? -27.993 -1.340  28.387  1.00 29.47 ? 507 HOH A O    1 
HETATM 2720 O  O    . HOH G 6 .   ? -21.139 13.888  2.099   1.00 29.26 ? 508 HOH A O    1 
HETATM 2721 O  O    . HOH G 6 .   ? 0.799   -9.632  -5.392  1.00 30.69 ? 509 HOH A O    1 
HETATM 2722 O  O    . HOH G 6 .   ? -27.742 6.390   21.587  1.00 28.26 ? 510 HOH A O    1 
HETATM 2723 O  O    . HOH G 6 .   ? -5.427  -12.520 -5.221  1.00 33.03 ? 511 HOH A O    1 
HETATM 2724 O  O    . HOH G 6 .   ? -7.228  -10.053 -4.424  1.00 28.05 ? 512 HOH A O    1 
HETATM 2725 O  O    . HOH G 6 .   ? 6.578   8.439   18.193  1.00 27.18 ? 513 HOH A O    1 
HETATM 2726 O  O    . HOH G 6 .   ? 2.905   0.951   -6.363  1.00 32.04 ? 514 HOH A O    1 
HETATM 2727 O  O    . HOH G 6 .   ? -9.819  1.466   39.091  1.00 25.11 ? 515 HOH A O    1 
HETATM 2728 O  O    . HOH G 6 .   ? -0.615  13.119  29.888  1.00 28.87 ? 516 HOH A O    1 
HETATM 2729 O  O    . HOH G 6 .   ? -16.927 -13.941 37.472  1.00 29.90 ? 517 HOH A O    1 
HETATM 2730 O  O    . HOH G 6 .   ? -2.343  0.438   46.721  1.00 24.49 ? 518 HOH A O    1 
HETATM 2731 O  O    . HOH G 6 .   ? -27.243 -6.767  7.677   1.00 32.41 ? 519 HOH A O    1 
HETATM 2732 O  O    . HOH G 6 .   ? -21.642 -21.560 12.147  1.00 24.33 ? 520 HOH A O    1 
HETATM 2733 O  O    . HOH G 6 .   ? -0.706  9.202   33.112  1.00 28.63 ? 521 HOH A O    1 
HETATM 2734 O  O    . HOH G 6 .   ? 2.680   -14.460 0.696   1.00 23.12 ? 522 HOH A O    1 
HETATM 2735 O  O    . HOH G 6 .   ? 4.786   -3.450  2.961   1.00 28.88 ? 523 HOH A O    1 
HETATM 2736 O  O    . HOH G 6 .   ? -24.042 -2.924  29.143  1.00 30.47 ? 524 HOH A O    1 
HETATM 2737 O  O    . HOH G 6 .   ? 2.059   -14.142 20.590  1.00 28.01 ? 525 HOH A O    1 
HETATM 2738 O  O    . HOH G 6 .   ? 5.709   -2.831  6.856   1.00 29.74 ? 526 HOH A O    1 
HETATM 2739 O  O    . HOH G 6 .   ? -10.021 15.802  29.635  1.00 28.58 ? 527 HOH A O    1 
HETATM 2740 O  O    . HOH G 6 .   ? -17.124 17.897  4.157   1.00 33.19 ? 528 HOH A O    1 
HETATM 2741 O  O    . HOH G 6 .   ? 5.494   9.124   21.883  1.00 26.88 ? 529 HOH A O    1 
HETATM 2742 O  O    . HOH G 6 .   ? 10.231  -8.616  8.570   1.00 32.55 ? 530 HOH A O    1 
HETATM 2743 O  O    . HOH G 6 .   ? -13.473 -16.539 -0.138  1.00 34.74 ? 531 HOH A O    1 
HETATM 2744 O  O    . HOH G 6 .   ? 9.497   -14.308 4.011   1.00 36.08 ? 532 HOH A O    1 
HETATM 2745 O  O    . HOH G 6 .   ? 4.756   -7.752  -11.016 1.00 33.84 ? 533 HOH A O    1 
HETATM 2746 O  O    . HOH G 6 .   ? 3.422   -13.740 12.311  1.00 32.02 ? 534 HOH A O    1 
HETATM 2747 O  O    . HOH G 6 .   ? -19.641 -4.305  41.429  1.00 32.21 ? 535 HOH A O    1 
HETATM 2748 O  O    . HOH G 6 .   ? 11.093  -3.423  7.804   1.00 35.14 ? 536 HOH A O    1 
HETATM 2749 O  O    . HOH G 6 .   ? -14.766 11.099  35.139  1.00 32.66 ? 537 HOH A O    1 
HETATM 2750 O  O    . HOH G 6 .   ? -26.250 -7.755  30.377  1.00 29.38 ? 538 HOH A O    1 
HETATM 2751 O  O    . HOH G 6 .   ? -21.610 19.680  17.277  1.00 33.17 ? 539 HOH A O    1 
HETATM 2752 O  O    . HOH G 6 .   ? -22.927 -14.710 16.111  1.00 31.88 ? 540 HOH A O    1 
HETATM 2753 O  O    . HOH G 6 .   ? -18.456 -9.013  34.560  1.00 30.31 ? 541 HOH A O    1 
HETATM 2754 O  O    . HOH G 6 .   ? -25.555 -3.429  31.701  1.00 32.83 ? 542 HOH A O    1 
HETATM 2755 O  O    . HOH G 6 .   ? 6.476   -5.790  6.670   1.00 29.20 ? 543 HOH A O    1 
HETATM 2756 O  O    . HOH G 6 .   ? -16.343 14.349  33.262  1.00 28.27 ? 544 HOH A O    1 
HETATM 2757 O  O    . HOH G 6 .   ? -21.072 -20.585 1.959   1.00 31.60 ? 545 HOH A O    1 
HETATM 2758 O  O    . HOH G 6 .   ? -27.894 4.951   25.304  1.00 29.68 ? 546 HOH A O    1 
HETATM 2759 O  O    . HOH G 6 .   ? 1.346   -15.938 -1.770  1.00 29.79 ? 547 HOH A O    1 
HETATM 2760 O  O    . HOH G 6 .   ? -0.477  13.934  27.177  1.00 29.07 ? 548 HOH A O    1 
HETATM 2761 O  O    . HOH G 6 .   ? 3.738   -2.390  4.877   1.00 39.61 ? 549 HOH A O    1 
HETATM 2762 O  O    . HOH G 6 .   ? -19.108 13.936  9.252   1.00 27.30 ? 550 HOH A O    1 
HETATM 2763 O  O    . HOH G 6 .   ? -26.788 -12.576 20.264  1.00 36.97 ? 551 HOH A O    1 
HETATM 2764 O  O    . HOH G 6 .   ? -27.090 -7.812  26.411  1.00 30.79 ? 552 HOH A O    1 
HETATM 2765 O  O    . HOH G 6 .   ? 5.870   0.963   8.397   1.00 28.66 ? 553 HOH A O    1 
HETATM 2766 O  O    . HOH G 6 .   ? -6.109  -11.522 36.427  1.00 37.70 ? 554 HOH A O    1 
HETATM 2767 O  O    . HOH G 6 .   ? -7.447  8.063   29.563  1.00 26.73 ? 555 HOH A O    1 
HETATM 2768 O  O    . HOH G 6 .   ? -10.615 -16.348 -7.700  1.00 38.27 ? 556 HOH A O    1 
HETATM 2769 O  O    . HOH G 6 .   ? 9.554   0.018   14.477  1.00 25.73 ? 557 HOH A O    1 
HETATM 2770 O  O    . HOH G 6 .   ? 7.043   -10.472 -7.828  1.00 25.51 ? 558 HOH A O    1 
HETATM 2771 O  O    . HOH G 6 .   ? -25.924 -9.884  14.873  1.00 35.18 ? 559 HOH A O    1 
HETATM 2772 O  O    . HOH G 6 .   ? -2.686  -14.874 32.795  1.00 29.14 ? 560 HOH A O    1 
HETATM 2773 O  O    . HOH G 6 .   ? 9.720   1.893   12.423  1.00 31.32 ? 561 HOH A O    1 
HETATM 2774 O  O    . HOH G 6 .   ? -11.620 10.681  0.696   1.00 29.69 ? 562 HOH A O    1 
HETATM 2775 O  O    . HOH G 6 .   ? 6.499   -0.513  -1.144  1.00 33.65 ? 563 HOH A O    1 
HETATM 2776 O  O    . HOH G 6 .   ? -1.785  -1.146  -12.813 1.00 43.32 ? 564 HOH A O    1 
HETATM 2777 O  O    . HOH G 6 .   ? -27.757 2.421   23.492  1.00 45.87 ? 565 HOH A O    1 
HETATM 2778 O  O    . HOH G 6 .   ? -13.798 14.833  6.043   1.00 41.85 ? 566 HOH A O    1 
HETATM 2779 O  O    . HOH G 6 .   ? 6.100   -10.872 15.346  1.00 34.34 ? 567 HOH A O    1 
HETATM 2780 O  O    . HOH G 6 .   ? -20.636 -19.917 -0.249  1.00 34.71 ? 568 HOH A O    1 
HETATM 2781 O  O    . HOH G 6 .   ? -1.411  4.403   -4.871  1.00 31.68 ? 569 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 3   ? 0.2024 0.3280 0.4092 0.0702  -0.0313 0.0258  3   HIS A N    
2    C  CA   . HIS A 3   ? 0.2723 0.4081 0.4089 0.0346  -0.0035 0.0410  3   HIS A CA   
3    C  C    . HIS A 3   ? 0.2998 0.4132 0.3984 0.0142  -0.0081 0.0304  3   HIS A C    
4    O  O    . HIS A 3   ? 0.3600 0.4828 0.4329 -0.0211 -0.0483 -0.0038 3   HIS A O    
5    C  CB   . HIS A 3   ? 0.3032 0.3648 0.3702 0.0030  -0.0535 0.0522  3   HIS A CB   
6    C  CG   . HIS A 3   ? 0.3801 0.3819 0.4409 -0.0142 -0.0062 0.0328  3   HIS A CG   
7    N  ND1  . HIS A 3   ? 0.3556 0.3882 0.4236 -0.0412 0.0148  0.0612  3   HIS A ND1  
8    C  CD2  . HIS A 3   ? 0.3691 0.3291 0.4332 0.0614  -0.0046 0.0277  3   HIS A CD2  
9    C  CE1  . HIS A 3   ? 0.4315 0.4354 0.4623 -0.0390 -0.0005 0.0176  3   HIS A CE1  
10   N  NE2  . HIS A 3   ? 0.3431 0.2973 0.5299 -0.1107 0.0186  0.0366  3   HIS A NE2  
11   N  N    . HIS A 4   ? 0.1798 0.3819 0.3783 0.0010  0.0218  0.0423  4   HIS A N    
12   C  CA   . HIS A 4   ? 0.2064 0.2976 0.3585 -0.0406 0.0744  0.0493  4   HIS A CA   
13   C  C    . HIS A 4   ? 0.1872 0.1800 0.3086 -0.0474 0.0639  0.0208  4   HIS A C    
14   O  O    . HIS A 4   ? 0.1859 0.1879 0.3558 -0.0243 0.0900  0.0434  4   HIS A O    
15   C  CB   . HIS A 4   ? 0.2951 0.3763 0.3837 -0.0247 0.0593  0.0531  4   HIS A CB   
16   C  CG   . HIS A 4   ? 0.4300 0.4792 0.4789 -0.0529 0.0137  0.0086  4   HIS A CG   
17   N  ND1  . HIS A 4   ? 0.6276 0.5938 0.5824 -0.0568 0.0285  0.0049  4   HIS A ND1  
18   C  CD2  . HIS A 4   ? 0.5935 0.5575 0.5824 -0.0829 0.0131  0.0131  4   HIS A CD2  
19   C  CE1  . HIS A 4   ? 0.6578 0.6481 0.6341 -0.0264 -0.0076 0.0013  4   HIS A CE1  
20   N  NE2  . HIS A 4   ? 0.6631 0.6427 0.6355 -0.0443 0.0060  0.0222  4   HIS A NE2  
21   N  N    . TRP A 5   ? 0.1360 0.1494 0.3077 -0.0496 0.0644  0.0146  5   TRP A N    
22   C  CA   . TRP A 5   ? 0.1103 0.1462 0.2698 -0.0355 0.0619  0.0093  5   TRP A CA   
23   C  C    . TRP A 5   ? 0.1428 0.1410 0.2554 -0.0136 0.0621  0.0065  5   TRP A C    
24   O  O    . TRP A 5   ? 0.1582 0.0815 0.2987 -0.0142 0.0527  0.0156  5   TRP A O    
25   C  CB   . TRP A 5   ? 0.0909 0.1171 0.2755 -0.0366 0.0671  0.0154  5   TRP A CB   
26   C  CG   . TRP A 5   ? 0.1297 0.0595 0.2802 -0.0410 0.0700  -0.0118 5   TRP A CG   
27   C  CD1  . TRP A 5   ? 0.1473 0.1437 0.2772 0.0013  0.0877  0.0263  5   TRP A CD1  
28   C  CD2  . TRP A 5   ? 0.1103 0.0889 0.2400 -0.0516 0.0406  -0.0015 5   TRP A CD2  
29   N  NE1  . TRP A 5   ? 0.1554 0.0934 0.2687 0.0065  0.0483  0.0441  5   TRP A NE1  
30   C  CE2  . TRP A 5   ? 0.1088 0.1376 0.2626 -0.0041 0.0249  -0.0010 5   TRP A CE2  
31   C  CE3  . TRP A 5   ? 0.1289 0.1071 0.2143 -0.0511 0.0533  -0.0337 5   TRP A CE3  
32   C  CZ2  . TRP A 5   ? 0.1482 0.1755 0.1941 -0.0188 0.0395  0.0038  5   TRP A CZ2  
33   C  CZ3  . TRP A 5   ? 0.0833 0.1306 0.2116 0.0188  0.0606  -0.0163 5   TRP A CZ3  
34   C  CH2  . TRP A 5   ? 0.1033 0.1568 0.2407 -0.0030 0.0286  -0.0230 5   TRP A CH2  
35   N  N    . GLY A 6   ? 0.1203 0.0776 0.2504 0.0170  0.0608  -0.0291 6   GLY A N    
36   C  CA   . GLY A 6   ? 0.1185 0.0803 0.2804 -0.0017 0.0684  -0.0098 6   GLY A CA   
37   C  C    . GLY A 6   ? 0.0939 0.0913 0.2831 0.0430  0.0899  -0.0172 6   GLY A C    
38   O  O    . GLY A 6   ? 0.0939 0.1004 0.2560 0.0304  0.0584  -0.0251 6   GLY A O    
39   N  N    . TYR A 7   ? 0.1458 0.0736 0.2994 0.0232  0.0876  -0.0281 7   TYR A N    
40   C  CA   . TYR A 7   ? 0.1169 0.0357 0.3454 0.0143  0.0948  -0.0104 7   TYR A CA   
41   C  C    . TYR A 7   ? 0.1766 0.1013 0.4143 -0.0091 0.1289  -0.0226 7   TYR A C    
42   O  O    . TYR A 7   ? 0.1649 0.1288 0.5521 -0.0031 0.1483  -0.0013 7   TYR A O    
43   C  CB   . TYR A 7   ? 0.1083 0.0478 0.3003 -0.0198 0.0581  -0.0082 7   TYR A CB   
44   C  CG   . TYR A 7   ? 0.0697 0.0302 0.2626 -0.0148 0.0344  -0.0116 7   TYR A CG   
45   C  CD1  . TYR A 7   ? 0.0650 0.0639 0.2556 -0.0146 0.0230  -0.0087 7   TYR A CD1  
46   C  CD2  . TYR A 7   ? 0.0891 0.0458 0.2189 0.0175  0.0287  -0.0244 7   TYR A CD2  
47   C  CE1  . TYR A 7   ? 0.0948 0.0313 0.2081 -0.0203 -0.0053 -0.0020 7   TYR A CE1  
48   C  CE2  . TYR A 7   ? 0.0866 0.0596 0.1861 0.0125  0.0461  -0.0237 7   TYR A CE2  
49   C  CZ   . TYR A 7   ? 0.0670 0.0417 0.1900 -0.0241 0.0272  0.0027  7   TYR A CZ   
50   O  OH   . TYR A 7   ? 0.0706 0.0483 0.2153 0.0282  0.0318  -0.0104 7   TYR A OH   
51   N  N    . GLY A 8   ? 0.1712 0.1297 0.4472 -0.0370 0.1032  -0.0401 8   GLY A N    
52   C  CA   . GLY A 8   ? 0.2125 0.1865 0.4584 -0.0153 0.1040  -0.0339 8   GLY A CA   
53   C  C    . GLY A 8   ? 0.2782 0.1171 0.4222 0.0275  0.1085  -0.0263 8   GLY A C    
54   O  O    . GLY A 8   ? 0.2452 0.2222 0.5133 -0.0010 0.1262  -0.0099 8   GLY A O    
55   N  N    . LYS A 9   ? 0.2260 0.1941 0.5246 -0.0049 0.0846  0.0298  9   LYS A N    
56   C  CA   . LYS A 9   ? 0.3023 0.2035 0.4954 0.0041  0.0542  -0.0103 9   LYS A CA   
57   C  C    . LYS A 9   ? 0.1970 0.2637 0.4743 0.0031  0.0873  0.0207  9   LYS A C    
58   O  O    . LYS A 9   ? 0.1708 0.2718 0.4918 -0.0619 0.1155  -0.0098 9   LYS A O    
59   C  CB   . LYS A 9   ? 0.3124 0.2966 0.5167 0.0447  0.0324  0.0296  9   LYS A CB   
60   C  CG   . LYS A 9   ? 0.3210 0.2168 0.4818 0.1067  0.0304  -0.0152 9   LYS A CG   
61   C  CD   . LYS A 9   ? 0.4355 0.3359 0.5554 0.0610  0.0263  -0.0264 9   LYS A CD   
62   C  CE   . LYS A 9   ? 0.5328 0.5073 0.6115 0.0270  -0.0305 0.0104  9   LYS A CE   
63   N  NZ   . LYS A 9   ? 0.6284 0.6118 0.6492 -0.0368 0.0178  0.0225  9   LYS A NZ   
64   N  N    . HIS A 10  ? 0.1950 0.0864 0.4501 0.0826  0.1444  -0.0085 10  HIS A N    
65   C  CA   . HIS A 10  ? 0.1985 0.1534 0.4246 0.0313  0.1322  0.0020  10  HIS A CA   
66   C  C    . HIS A 10  ? 0.1412 0.1322 0.3740 0.0392  0.1092  0.0184  10  HIS A C    
67   O  O    . HIS A 10  ? 0.1642 0.1768 0.3914 0.0540  0.1105  -0.0060 10  HIS A O    
68   C  CB   . HIS A 10  ? 0.1999 0.1336 0.3878 0.0209  0.1581  0.0035  10  HIS A CB   
69   C  CG   . HIS A 10  ? 0.2028 0.2797 0.4271 0.0142  0.1140  0.0551  10  HIS A CG   
70   N  ND1  . HIS A 10  ? 0.2306 0.2064 0.4778 0.0700  0.1620  0.0153  10  HIS A ND1  
71   C  CD2  . HIS A 10  ? 0.2071 0.2540 0.4847 -0.0281 0.1898  0.0806  10  HIS A CD2  
72   C  CE1  . HIS A 10  ? 0.3461 0.1721 0.4549 0.0807  0.0944  -0.0141 10  HIS A CE1  
73   N  NE2  . HIS A 10  ? 0.2015 0.2064 0.4656 0.0645  0.1031  -0.0208 10  HIS A NE2  
74   N  N    . ASN A 11  ? 0.1507 0.1252 0.3388 0.0487  0.1168  0.0148  11  ASN A N    
75   C  CA   . ASN A 11  ? 0.1394 0.0991 0.3005 0.0098  0.0869  -0.0007 11  ASN A CA   
76   C  C    . ASN A 11  ? 0.0986 0.1228 0.2773 0.0326  0.0869  0.0126  11  ASN A C    
77   O  O    . ASN A 11  ? 0.1089 0.1070 0.3278 0.0478  0.0780  -0.0035 11  ASN A O    
78   C  CB   . ASN A 11  ? 0.1552 0.1018 0.2894 0.0178  0.0843  0.0041  11  ASN A CB   
79   C  CG   . ASN A 11  ? 0.1895 0.0986 0.2998 0.0452  0.0837  -0.0333 11  ASN A CG   
80   O  OD1  . ASN A 11  ? 0.1717 0.1360 0.3592 0.0040  0.0700  -0.0030 11  ASN A OD1  
81   N  ND2  . ASN A 11  ? 0.2371 0.1884 0.2908 -0.0333 0.0331  0.0177  11  ASN A ND2  
82   N  N    . GLY A 12  ? 0.1115 0.1324 0.2736 -0.0054 0.0860  -0.0087 12  GLY A N    
83   C  CA   . GLY A 12  ? 0.0675 0.1563 0.2405 -0.0043 0.0522  0.0043  12  GLY A CA   
84   C  C    . GLY A 12  ? 0.0600 0.0995 0.2675 -0.0233 0.0443  -0.0136 12  GLY A C    
85   O  O    . GLY A 12  ? 0.0340 0.1027 0.3113 0.0063  0.0417  0.0362  12  GLY A O    
86   N  N    . PRO A 13  ? 0.0643 0.1146 0.2432 -0.0258 0.0564  -0.0097 13  PRO A N    
87   C  CA   . PRO A 13  ? 0.1103 0.0982 0.2517 -0.0263 0.0538  -0.0274 13  PRO A CA   
88   C  C    . PRO A 13  ? 0.1191 0.0675 0.2380 -0.0049 0.0504  0.0010  13  PRO A C    
89   O  O    . PRO A 13  ? 0.0821 0.1164 0.2851 0.0017  0.0509  -0.0208 13  PRO A O    
90   C  CB   . PRO A 13  ? 0.0914 0.1626 0.2561 -0.0751 0.0815  -0.0108 13  PRO A CB   
91   C  CG   . PRO A 13  ? 0.1056 0.1721 0.2545 0.0222  0.0762  -0.0219 13  PRO A CG   
92   C  CD   . PRO A 13  ? 0.0407 0.1455 0.2660 -0.0221 0.0564  -0.0262 13  PRO A CD   
93   N  N    A GLU A 14  ? 0.1079 0.0711 0.2709 0.0010  0.0438  0.0054  14  GLU A N    
94   N  N    B GLU A 14  ? 0.1088 0.0684 0.2788 0.0006  0.0445  0.0076  14  GLU A N    
95   C  CA   A GLU A 14  ? 0.1347 0.1083 0.2901 -0.0054 0.0176  -0.0007 14  GLU A CA   
96   C  CA   B GLU A 14  ? 0.1331 0.1045 0.2955 -0.0026 0.0244  -0.0031 14  GLU A CA   
97   C  C    A GLU A 14  ? 0.1038 0.1002 0.2777 0.0109  0.0297  0.0006  14  GLU A C    
98   C  C    B GLU A 14  ? 0.1045 0.0930 0.2768 0.0132  0.0291  -0.0026 14  GLU A C    
99   O  O    A GLU A 14  ? 0.1475 0.1205 0.2910 0.0417  0.0302  0.0040  14  GLU A O    
100  O  O    B GLU A 14  ? 0.1370 0.1234 0.3093 0.0392  0.0315  0.0160  14  GLU A O    
101  C  CB   A GLU A 14  ? 0.1927 0.1221 0.3208 0.0131  0.0043  0.0153  14  GLU A CB   
102  C  CB   B GLU A 14  ? 0.1834 0.1099 0.3440 0.0065  0.0153  0.0285  14  GLU A CB   
103  C  CG   A GLU A 14  ? 0.1631 0.1791 0.2768 -0.0439 -0.0291 -0.0103 14  GLU A CG   
104  C  CG   B GLU A 14  ? 0.1491 0.1825 0.3242 -0.0073 0.0417  0.0043  14  GLU A CG   
105  C  CD   A GLU A 14  ? 0.3048 0.1660 0.2279 0.0082  -0.0230 0.0160  14  GLU A CD   
106  C  CD   B GLU A 14  ? 0.3540 0.3673 0.3445 -0.0125 -0.0012 0.0076  14  GLU A CD   
107  O  OE1  A GLU A 14  ? 0.1694 0.1185 0.2245 0.0995  -0.0265 -0.0873 14  GLU A OE1  
108  O  OE1  B GLU A 14  ? 0.4761 0.3993 0.4139 -0.0207 -0.0284 -0.0013 14  GLU A OE1  
109  O  OE2  A GLU A 14  ? 0.3382 0.0463 0.2347 0.0132  0.0406  -0.0131 14  GLU A OE2  
110  O  OE2  B GLU A 14  ? 0.4429 0.4200 0.3454 0.0088  0.0593  0.0126  14  GLU A OE2  
111  N  N    . HIS A 15  ? 0.0643 0.0756 0.2791 0.0153  0.0099  0.0024  15  HIS A N    
112  C  CA   . HIS A 15  ? 0.0480 0.0781 0.3032 0.0060  0.0310  -0.0241 15  HIS A CA   
113  C  C    . HIS A 15  ? 0.0464 0.0799 0.2827 0.0308  0.0182  -0.0197 15  HIS A C    
114  O  O    . HIS A 15  ? 0.0463 0.0939 0.3528 0.0197  0.0174  0.0073  15  HIS A O    
115  C  CB   . HIS A 15  ? 0.0289 0.0949 0.3026 0.0128  0.0188  0.0015  15  HIS A CB   
116  C  CG   . HIS A 15  ? 0.0785 0.1194 0.3032 0.0217  0.0526  0.0197  15  HIS A CG   
117  N  ND1  . HIS A 15  ? 0.1049 0.1501 0.3495 0.0295  0.0262  -0.0003 15  HIS A ND1  
118  C  CD2  . HIS A 15  ? 0.1121 0.1424 0.3465 0.0614  0.0491  -0.0121 15  HIS A CD2  
119  C  CE1  . HIS A 15  ? 0.2824 0.2048 0.3650 0.0944  -0.0073 -0.0524 15  HIS A CE1  
120  N  NE2  . HIS A 15  ? 0.1753 0.1428 0.3711 0.0768  0.0361  0.0093  15  HIS A NE2  
121  N  N    . TRP A 16  ? 0.0441 0.0747 0.2718 0.0253  0.0282  -0.0121 16  TRP A N    
122  C  CA   . TRP A 16  ? 0.0384 0.0521 0.2768 0.0186  -0.0140 -0.0120 16  TRP A CA   
123  C  C    . TRP A 16  ? 0.0505 0.1054 0.2727 0.0062  0.0087  0.0031  16  TRP A C    
124  O  O    . TRP A 16  ? 0.0551 0.0573 0.3258 -0.0017 0.0015  -0.0068 16  TRP A O    
125  C  CB   . TRP A 16  ? 0.0390 0.1198 0.2612 0.0103  -0.0142 -0.0274 16  TRP A CB   
126  C  CG   . TRP A 16  ? 0.0661 0.0767 0.2260 -0.0220 0.0175  0.0137  16  TRP A CG   
127  C  CD1  . TRP A 16  ? 0.0715 0.0973 0.2069 -0.0153 0.0285  0.0026  16  TRP A CD1  
128  C  CD2  . TRP A 16  ? 0.0343 0.0826 0.2354 -0.0126 0.0162  -0.0285 16  TRP A CD2  
129  N  NE1  . TRP A 16  ? 0.0361 0.0661 0.2479 -0.0060 0.0307  -0.0210 16  TRP A NE1  
130  C  CE2  . TRP A 16  ? 0.0460 0.0595 0.2256 -0.0197 0.0208  0.0051  16  TRP A CE2  
131  C  CE3  . TRP A 16  ? 0.0693 0.0386 0.2426 0.0233  0.0176  -0.0037 16  TRP A CE3  
132  C  CZ2  . TRP A 16  ? 0.0353 0.0641 0.2310 0.0070  0.0125  0.0026  16  TRP A CZ2  
133  C  CZ3  . TRP A 16  ? 0.0515 0.0675 0.2353 -0.0129 0.0274  -0.0395 16  TRP A CZ3  
134  C  CH2  . TRP A 16  ? 0.0370 0.0531 0.2132 0.0065  0.0361  -0.0221 16  TRP A CH2  
135  N  N    . HIS A 17  ? 0.0609 0.0997 0.2766 0.0126  0.0126  -0.0031 17  HIS A N    
136  C  CA   . HIS A 17  ? 0.0575 0.1176 0.2951 -0.0063 0.0010  0.0031  17  HIS A CA   
137  C  C    . HIS A 17  ? 0.0584 0.1498 0.3224 -0.0227 0.0229  0.0043  17  HIS A C    
138  O  O    . HIS A 17  ? 0.0437 0.1286 0.3436 0.0135  -0.0003 0.0043  17  HIS A O    
139  C  CB   . HIS A 17  ? 0.0367 0.1106 0.2687 -0.0120 0.0178  0.0140  17  HIS A CB   
140  C  CG   . HIS A 17  ? 0.0319 0.1101 0.3106 -0.0038 -0.0098 0.0013  17  HIS A CG   
141  N  ND1  . HIS A 17  ? 0.0891 0.1796 0.3526 0.0013  -0.0423 0.0623  17  HIS A ND1  
142  C  CD2  . HIS A 17  ? 0.1189 0.1209 0.3043 0.0252  0.0346  0.0151  17  HIS A CD2  
143  C  CE1  . HIS A 17  ? 0.1665 0.1730 0.3510 0.0904  0.0043  0.0115  17  HIS A CE1  
144  N  NE2  . HIS A 17  ? 0.0436 0.1920 0.3285 0.0189  0.0096  0.0564  17  HIS A NE2  
145  N  N    . LYS A 18  ? 0.0447 0.1313 0.3571 -0.0214 0.0102  0.0243  18  LYS A N    
146  C  CA   . LYS A 18  ? 0.0379 0.1371 0.3625 -0.0241 0.0412  0.0137  18  LYS A CA   
147  C  C    . LYS A 18  ? 0.0851 0.1322 0.3449 -0.0577 -0.0152 0.0273  18  LYS A C    
148  O  O    . LYS A 18  ? 0.1358 0.2364 0.4171 -0.0463 -0.0340 0.0320  18  LYS A O    
149  C  CB   . LYS A 18  ? 0.0291 0.1083 0.3736 -0.0148 0.0163  0.0209  18  LYS A CB   
150  C  CG   . LYS A 18  ? 0.0515 0.1081 0.3632 0.0331  0.0285  0.0285  18  LYS A CG   
151  C  CD   . LYS A 18  ? 0.0742 0.1306 0.3862 -0.0046 0.0329  0.0476  18  LYS A CD   
152  C  CE   . LYS A 18  ? 0.0973 0.1121 0.3345 -0.0031 0.0310  0.0608  18  LYS A CE   
153  N  NZ   . LYS A 18  ? 0.0684 0.1841 0.3124 0.0342  0.0218  0.0252  18  LYS A NZ   
154  N  N    . ASP A 19  ? 0.0446 0.1142 0.3452 0.0000  0.0000  0.0472  19  ASP A N    
155  C  CA   . ASP A 19  ? 0.0778 0.1550 0.3393 0.0054  0.0197  0.0151  19  ASP A CA   
156  C  C    . ASP A 19  ? 0.0599 0.1230 0.3537 0.0110  0.0114  0.0155  19  ASP A C    
157  O  O    . ASP A 19  ? 0.0697 0.1194 0.3962 -0.0307 0.0291  0.0344  19  ASP A O    
158  C  CB   . ASP A 19  ? 0.1228 0.2337 0.3341 0.0052  0.0146  0.0480  19  ASP A CB   
159  C  CG   . ASP A 19  ? 0.1805 0.2867 0.3086 -0.0098 0.0041  -0.0131 19  ASP A CG   
160  O  OD1  . ASP A 19  ? 0.2227 0.2838 0.3905 -0.0728 0.0126  0.0153  19  ASP A OD1  
161  O  OD2  . ASP A 19  ? 0.3842 0.3517 0.4717 -0.0077 0.0238  -0.0342 19  ASP A OD2  
162  N  N    . PHE A 20  ? 0.0316 0.1150 0.3490 -0.0173 0.0240  0.0313  20  PHE A N    
163  C  CA   . PHE A 20  ? 0.0344 0.1361 0.3143 -0.0027 0.0271  0.0038  20  PHE A CA   
164  C  C    . PHE A 20  ? 0.0657 0.1103 0.3181 0.0088  0.0137  -0.0140 20  PHE A C    
165  O  O    . PHE A 20  ? 0.0592 0.0706 0.3357 -0.0024 -0.0176 -0.0165 20  PHE A O    
166  C  CB   . PHE A 20  ? 0.0579 0.1371 0.3190 -0.0432 -0.0230 0.0379  20  PHE A CB   
167  C  CG   . PHE A 20  ? 0.0343 0.1498 0.3054 -0.0329 0.0076  0.0087  20  PHE A CG   
168  C  CD1  . PHE A 20  ? 0.0571 0.1608 0.3267 -0.0220 0.0231  0.0627  20  PHE A CD1  
169  C  CD2  . PHE A 20  ? 0.0731 0.1909 0.2669 -0.0666 0.0027  0.0062  20  PHE A CD2  
170  C  CE1  . PHE A 20  ? 0.1599 0.1597 0.2750 -0.0280 -0.0015 0.0375  20  PHE A CE1  
171  C  CE2  . PHE A 20  ? 0.0643 0.2197 0.3222 -0.0109 -0.0020 0.0252  20  PHE A CE2  
172  C  CZ   . PHE A 20  ? 0.0477 0.2100 0.3120 -0.0516 0.0113  0.0183  20  PHE A CZ   
173  N  N    . PRO A 21  ? 0.0481 0.1453 0.3165 -0.0082 -0.0088 -0.0038 21  PRO A N    
174  C  CA   . PRO A 21  ? 0.0652 0.1464 0.2809 -0.0533 -0.0200 0.0274  21  PRO A CA   
175  C  C    . PRO A 21  ? 0.0758 0.1061 0.2791 -0.0153 -0.0231 0.0060  21  PRO A C    
176  O  O    . PRO A 21  ? 0.0485 0.1320 0.2984 -0.0272 -0.0162 0.0161  21  PRO A O    
177  C  CB   . PRO A 21  ? 0.0672 0.1897 0.3134 -0.0471 -0.0355 0.0156  21  PRO A CB   
178  C  CG   . PRO A 21  ? 0.1865 0.1816 0.3438 -0.0588 -0.0593 -0.0020 21  PRO A CG   
179  C  CD   . PRO A 21  ? 0.0361 0.1076 0.3314 -0.0297 0.0020  -0.0054 21  PRO A CD   
180  N  N    A ILE A 22  ? 0.0296 0.1020 0.2793 -0.0120 -0.0198 -0.0262 22  ILE A N    
181  N  N    B ILE A 22  ? 0.0282 0.1054 0.2825 -0.0080 -0.0198 -0.0311 22  ILE A N    
182  C  CA   A ILE A 22  ? 0.0672 0.0578 0.2487 0.0131  0.0000  -0.0082 22  ILE A CA   
183  C  CA   B ILE A 22  ? 0.0618 0.0806 0.2565 -0.0006 -0.0054 -0.0208 22  ILE A CA   
184  C  C    A ILE A 22  ? 0.0511 0.0927 0.2286 -0.0041 -0.0272 -0.0098 22  ILE A C    
185  C  C    B ILE A 22  ? 0.0485 0.0794 0.2432 0.0135  -0.0208 -0.0031 22  ILE A C    
186  O  O    A ILE A 22  ? 0.0516 0.0424 0.2385 0.0207  -0.0164 0.0000  22  ILE A O    
187  O  O    B ILE A 22  ? 0.0643 0.1067 0.2432 0.0209  0.0065  -0.0024 22  ILE A O    
188  C  CB   A ILE A 22  ? 0.0604 0.0580 0.2319 0.0103  0.0037  0.0140  22  ILE A CB   
189  C  CB   B ILE A 22  ? 0.0839 0.0988 0.2644 0.0405  -0.0209 -0.0141 22  ILE A CB   
190  C  CG1  A ILE A 22  ? 0.1018 0.1464 0.2340 0.0080  0.0126  -0.0131 22  ILE A CG1  
191  C  CG1  B ILE A 22  ? 0.0724 0.0785 0.2425 -0.0500 0.0006  0.0038  22  ILE A CG1  
192  C  CG2  A ILE A 22  ? 0.0257 0.1334 0.2309 0.0066  -0.0002 0.0197  22  ILE A CG2  
193  C  CG2  B ILE A 22  ? 0.0995 0.1412 0.2364 -0.0562 -0.0126 0.0074  22  ILE A CG2  
194  C  CD1  A ILE A 22  ? 0.1550 0.2168 0.2267 -0.0068 0.0181  0.0386  22  ILE A CD1  
195  C  CD1  B ILE A 22  ? 0.0398 0.0593 0.2666 -0.0024 0.0031  -0.0241 22  ILE A CD1  
196  N  N    . ALA A 23  ? 0.0463 0.0760 0.2703 0.0030  -0.0250 -0.0031 23  ALA A N    
197  C  CA   . ALA A 23  ? 0.0785 0.0468 0.2644 -0.0282 -0.0031 0.0034  23  ALA A CA   
198  C  C    . ALA A 23  ? 0.0371 0.0798 0.2711 0.0077  -0.0155 -0.0261 23  ALA A C    
199  O  O    . ALA A 23  ? 0.0512 0.0864 0.2723 -0.0152 -0.0177 -0.0240 23  ALA A O    
200  C  CB   . ALA A 23  ? 0.0590 0.0392 0.3179 0.0142  -0.0096 -0.0344 23  ALA A CB   
201  N  N    . LYS A 24  ? 0.0472 0.0878 0.2777 0.0189  -0.0208 -0.0030 24  LYS A N    
202  C  CA   . LYS A 24  ? 0.0568 0.1444 0.2635 -0.0285 -0.0238 -0.0172 24  LYS A CA   
203  C  C    . LYS A 24  ? 0.0736 0.1334 0.2632 -0.0333 -0.0333 -0.0219 24  LYS A C    
204  O  O    . LYS A 24  ? 0.0948 0.1904 0.3129 0.0108  -0.0653 0.0006  24  LYS A O    
205  C  CB   . LYS A 24  ? 0.0715 0.1225 0.2702 -0.0003 -0.0131 0.0126  24  LYS A CB   
206  C  CG   . LYS A 24  ? 0.0573 0.1999 0.2894 0.0445  0.0006  0.0000  24  LYS A CG   
207  C  CD   . LYS A 24  ? 0.1313 0.2154 0.3465 0.0658  0.0148  -0.0303 24  LYS A CD   
208  C  CE   . LYS A 24  ? 0.2135 0.2723 0.3628 0.0046  0.0304  -0.0390 24  LYS A CE   
209  N  NZ   . LYS A 24  ? 0.3231 0.3560 0.4559 0.0189  -0.0204 -0.0098 24  LYS A NZ   
210  N  N    . GLY A 25  ? 0.0754 0.1205 0.2651 0.0140  -0.0203 -0.0272 25  GLY A N    
211  C  CA   . GLY A 25  ? 0.0465 0.1489 0.2664 -0.0103 -0.0074 -0.0324 25  GLY A CA   
212  C  C    . GLY A 25  ? 0.0537 0.1674 0.2128 0.0164  -0.0361 -0.0331 25  GLY A C    
213  O  O    . GLY A 25  ? 0.0828 0.2048 0.2444 0.0024  -0.0388 -0.0355 25  GLY A O    
214  N  N    . GLU A 26  ? 0.0679 0.1909 0.2322 0.0178  -0.0205 -0.0397 26  GLU A N    
215  C  CA   . GLU A 26  ? 0.0961 0.1895 0.1931 0.0052  -0.0206 -0.0225 26  GLU A CA   
216  C  C    . GLU A 26  ? 0.0891 0.1606 0.1801 0.0071  -0.0262 -0.0381 26  GLU A C    
217  O  O    . GLU A 26  ? 0.1712 0.1877 0.1667 -0.0006 -0.0161 0.0027  26  GLU A O    
218  C  CB   . GLU A 26  ? 0.1403 0.2522 0.2197 -0.0430 -0.0130 -0.0671 26  GLU A CB   
219  C  CG   . GLU A 26  ? 0.1457 0.2351 0.2833 0.0348  -0.0355 -0.0040 26  GLU A CG   
220  C  CD   . GLU A 26  ? 0.2565 0.3265 0.3176 -0.0417 -0.0579 -0.0031 26  GLU A CD   
221  O  OE1  . GLU A 26  ? 0.3003 0.4480 0.3801 -0.0544 -0.0570 -0.0119 26  GLU A OE1  
222  O  OE2  . GLU A 26  ? 0.3179 0.4314 0.3815 0.0059  -0.0557 -0.0834 26  GLU A OE2  
223  N  N    . ARG A 27  ? 0.0974 0.0925 0.2005 -0.0052 -0.0307 -0.0266 27  ARG A N    
224  C  CA   . ARG A 27  ? 0.0621 0.0672 0.1884 -0.0164 -0.0077 -0.0125 27  ARG A CA   
225  C  C    . ARG A 27  ? 0.0322 0.0763 0.1845 -0.0104 -0.0043 0.0013  27  ARG A C    
226  O  O    . ARG A 27  ? 0.0603 0.0851 0.1832 0.0020  -0.0308 -0.0035 27  ARG A O    
227  C  CB   . ARG A 27  ? 0.1365 0.0891 0.2114 0.0087  -0.0017 -0.0381 27  ARG A CB   
228  C  CG   . ARG A 27  ? 0.0860 0.1581 0.2919 -0.0329 0.0012  -0.0588 27  ARG A CG   
229  C  CD   . ARG A 27  ? 0.1848 0.1579 0.2822 0.0370  -0.0197 -0.0272 27  ARG A CD   
230  N  NE   . ARG A 27  ? 0.1870 0.1546 0.2339 -0.0135 0.0062  -0.0110 27  ARG A NE   
231  C  CZ   . ARG A 27  ? 0.1689 0.1054 0.1904 0.0142  -0.0164 -0.0003 27  ARG A CZ   
232  N  NH1  . ARG A 27  ? 0.1243 0.1550 0.2538 0.0082  0.0107  -0.0772 27  ARG A NH1  
233  N  NH2  . ARG A 27  ? 0.1194 0.1455 0.2249 0.0020  0.0229  -0.0322 27  ARG A NH2  
234  N  N    . GLN A 28  ? 0.0355 0.0503 0.1976 0.0158  -0.0055 -0.0136 28  GLN A N    
235  C  CA   . GLN A 28  ? 0.0254 0.0414 0.1929 0.0004  -0.0039 -0.0199 28  GLN A CA   
236  C  C    . GLN A 28  ? 0.0337 0.0364 0.1763 0.0090  0.0034  -0.0103 28  GLN A C    
237  O  O    . GLN A 28  ? 0.0579 0.0760 0.1780 -0.0043 -0.0074 -0.0017 28  GLN A O    
238  C  CB   . GLN A 28  ? 0.0258 0.0698 0.2296 0.0044  -0.0042 -0.0138 28  GLN A CB   
239  C  CG   . GLN A 28  ? 0.0335 0.0573 0.2125 -0.0120 -0.0307 0.0152  28  GLN A CG   
240  C  CD   . GLN A 28  ? 0.0803 0.1013 0.1643 -0.0093 -0.0359 -0.0159 28  GLN A CD   
241  O  OE1  . GLN A 28  ? 0.0458 0.0446 0.2265 -0.0096 0.0063  -0.0251 28  GLN A OE1  
242  N  NE2  . GLN A 28  ? 0.0427 0.0345 0.2355 0.0125  -0.0222 -0.0126 28  GLN A NE2  
243  N  N    . SER A 29  ? 0.0285 0.0300 0.1659 -0.0001 0.0124  -0.0212 29  SER A N    
244  C  CA   . SER A 29  ? 0.0301 0.0269 0.1825 -0.0027 0.0271  -0.0158 29  SER A CA   
245  C  C    . SER A 29  ? 0.0333 0.0348 0.1647 0.0024  0.0136  -0.0274 29  SER A C    
246  O  O    . SER A 29  ? 0.0333 0.0494 0.1884 0.0093  0.0210  -0.0119 29  SER A O    
247  C  CB   . SER A 29  ? 0.0332 0.0275 0.1926 -0.0031 -0.0010 -0.0081 29  SER A CB   
248  O  OG   . SER A 29  ? 0.0307 0.0353 0.1967 -0.0069 0.0199  -0.0163 29  SER A OG   
249  N  N    . PRO A 30  ? 0.0428 0.0494 0.1671 0.0204  -0.0061 -0.0034 30  PRO A N    
250  C  CA   . PRO A 30  ? 0.0381 0.0439 0.1642 0.0141  0.0197  0.0041  30  PRO A CA   
251  C  C    . PRO A 30  ? 0.0501 0.0386 0.1537 0.0049  0.0245  -0.0305 30  PRO A C    
252  O  O    . PRO A 30  ? 0.0583 0.0521 0.1732 0.0037  -0.0040 -0.0052 30  PRO A O    
253  C  CB   . PRO A 30  ? 0.0377 0.0534 0.1685 0.0142  0.0146  -0.0216 30  PRO A CB   
254  C  CG   . PRO A 30  ? 0.0393 0.0494 0.1834 0.0148  0.0109  0.0203  30  PRO A CG   
255  C  CD   . PRO A 30  ? 0.0490 0.0436 0.1999 0.0027  0.0093  -0.0317 30  PRO A CD   
256  N  N    . VAL A 31  ? 0.0316 0.0315 0.1714 -0.0015 0.0109  -0.0031 31  VAL A N    
257  C  CA   . VAL A 31  ? 0.0930 0.0388 0.1561 -0.0285 -0.0024 0.0137  31  VAL A CA   
258  C  C    . VAL A 31  ? 0.0542 0.0630 0.1579 -0.0137 0.0043  0.0198  31  VAL A C    
259  O  O    . VAL A 31  ? 0.0433 0.0515 0.1665 0.0017  -0.0040 0.0130  31  VAL A O    
260  C  CB   . VAL A 31  ? 0.0614 0.0436 0.1908 -0.0132 -0.0115 -0.0162 31  VAL A CB   
261  C  CG1  . VAL A 31  ? 0.1112 0.0878 0.2071 -0.0421 0.0038  -0.0051 31  VAL A CG1  
262  C  CG2  . VAL A 31  ? 0.0640 0.0397 0.2143 0.0148  0.0167  0.0043  31  VAL A CG2  
263  N  N    . ASP A 32  ? 0.0625 0.0512 0.1644 -0.0034 0.0054  0.0186  32  ASP A N    
264  C  CA   . ASP A 32  ? 0.0384 0.0379 0.1897 0.0127  0.0210  0.0190  32  ASP A CA   
265  C  C    . ASP A 32  ? 0.0848 0.0605 0.1640 0.0359  0.0087  -0.0137 32  ASP A C    
266  O  O    . ASP A 32  ? 0.0636 0.0925 0.1936 0.0184  0.0074  -0.0194 32  ASP A O    
267  C  CB   . ASP A 32  ? 0.0754 0.0440 0.2091 0.0305  -0.0196 -0.0070 32  ASP A CB   
268  C  CG   . ASP A 32  ? 0.0765 0.0366 0.2109 0.0172  -0.0035 0.0093  32  ASP A CG   
269  O  OD1  . ASP A 32  ? 0.1209 0.0450 0.1649 0.0291  -0.0051 0.0006  32  ASP A OD1  
270  O  OD2  . ASP A 32  ? 0.1622 0.1020 0.1764 -0.0266 -0.0242 0.0148  32  ASP A OD2  
271  N  N    . ILE A 33  ? 0.0432 0.0512 0.1755 0.0023  0.0097  0.0104  33  ILE A N    
272  C  CA   . ILE A 33  ? 0.0916 0.0769 0.1854 0.0379  0.0043  0.0250  33  ILE A CA   
273  C  C    . ILE A 33  ? 0.0927 0.0416 0.1947 0.0208  0.0051  0.0059  33  ILE A C    
274  O  O    . ILE A 33  ? 0.1137 0.0454 0.1987 -0.0010 0.0243  0.0131  33  ILE A O    
275  C  CB   . ILE A 33  ? 0.0799 0.0625 0.2081 -0.0059 0.0131  0.0096  33  ILE A CB   
276  C  CG1  . ILE A 33  ? 0.0803 0.0512 0.1924 -0.0007 0.0182  0.0027  33  ILE A CG1  
277  C  CG2  . ILE A 33  ? 0.0605 0.1593 0.2143 0.0120  0.0425  -0.0115 33  ILE A CG2  
278  C  CD1  . ILE A 33  ? 0.0970 0.0736 0.2125 0.0408  -0.0040 0.0080  33  ILE A CD1  
279  N  N    A ASP A 34  ? 0.1347 0.0654 0.1629 0.0207  0.0243  0.0141  34  ASP A N    
280  N  N    B ASP A 34  ? 0.1473 0.0697 0.1681 0.0182  0.0164  0.0160  34  ASP A N    
281  C  CA   A ASP A 34  ? 0.1689 0.0930 0.1672 0.0271  0.0252  0.0233  34  ASP A CA   
282  C  CA   B ASP A 34  ? 0.1793 0.0986 0.1726 0.0238  0.0197  0.0211  34  ASP A CA   
283  C  C    A ASP A 34  ? 0.1653 0.0745 0.1895 0.0208  0.0296  0.0288  34  ASP A C    
284  C  C    B ASP A 34  ? 0.1712 0.0715 0.1938 0.0225  0.0259  0.0294  34  ASP A C    
285  O  O    A ASP A 34  ? 0.2288 0.0925 0.1908 0.0425  0.0436  0.0153  34  ASP A O    
286  O  O    B ASP A 34  ? 0.2398 0.1151 0.1913 0.0303  0.0375  0.0065  34  ASP A O    
287  C  CB   A ASP A 34  ? 0.1877 0.0738 0.1798 0.0142  0.0082  0.0392  34  ASP A CB   
288  C  CB   B ASP A 34  ? 0.1791 0.0930 0.1827 -0.0175 -0.0051 0.0423  34  ASP A CB   
289  C  CG   A ASP A 34  ? 0.2486 0.2046 0.2048 0.0255  0.0217  0.0531  34  ASP A CG   
290  C  CG   B ASP A 34  ? 0.2759 0.1855 0.1791 -0.0019 -0.0188 0.0059  34  ASP A CG   
291  O  OD1  A ASP A 34  ? 0.2879 0.0846 0.1902 0.0461  0.1102  0.0335  34  ASP A OD1  
292  O  OD1  B ASP A 34  ? 0.3185 0.2263 0.2362 -0.0297 -0.0060 0.0599  34  ASP A OD1  
293  O  OD2  A ASP A 34  ? 0.3767 0.1344 0.2498 0.0320  0.0636  0.0252  34  ASP A OD2  
294  O  OD2  B ASP A 34  ? 0.3691 0.2367 0.1798 0.0041  -0.0571 0.0810  34  ASP A OD2  
295  N  N    . THR A 35  ? 0.1958 0.0866 0.1916 0.0498  0.0368  0.0373  35  THR A N    
296  C  CA   . THR A 35  ? 0.1977 0.1189 0.1954 0.0568  0.0368  0.0125  35  THR A CA   
297  C  C    . THR A 35  ? 0.2161 0.1133 0.1805 0.0731  0.0516  0.0320  35  THR A C    
298  O  O    . THR A 35  ? 0.2179 0.1395 0.2398 0.0753  0.0859  0.0162  35  THR A O    
299  C  CB   . THR A 35  ? 0.1949 0.1343 0.2283 0.0728  0.0449  0.0184  35  THR A CB   
300  O  OG1  . THR A 35  ? 0.1888 0.1458 0.2260 0.0487  0.0579  0.0331  35  THR A OG1  
301  C  CG2  . THR A 35  ? 0.1791 0.1712 0.1898 0.0597  0.0252  0.0469  35  THR A CG2  
302  N  N    . HIS A 36  ? 0.2669 0.1431 0.1726 0.0527  0.0463  0.0436  36  HIS A N    
303  C  CA   . HIS A 36  ? 0.2696 0.1653 0.2064 0.0544  0.0456  0.0421  36  HIS A CA   
304  C  C    . HIS A 36  ? 0.2930 0.2138 0.1732 0.0414  0.0615  0.0147  36  HIS A C    
305  O  O    . HIS A 36  ? 0.3111 0.2933 0.2200 0.0737  0.0381  0.0184  36  HIS A O    
306  C  CB   . HIS A 36  ? 0.2984 0.1615 0.2214 0.0355  0.0263  0.0566  36  HIS A CB   
307  C  CG   . HIS A 36  ? 0.3860 0.2039 0.2128 0.0759  -0.0379 0.0500  36  HIS A CG   
308  N  ND1  . HIS A 36  ? 0.4070 0.2215 0.2808 0.0068  -0.0386 0.0003  36  HIS A ND1  
309  C  CD2  . HIS A 36  ? 0.4059 0.1624 0.2154 0.0648  -0.0803 0.0781  36  HIS A CD2  
310  C  CE1  . HIS A 36  ? 0.4577 0.2482 0.3386 -0.0164 -0.0423 0.0076  36  HIS A CE1  
311  N  NE2  . HIS A 36  ? 0.4211 0.1798 0.2992 0.0644  0.0162  0.0124  36  HIS A NE2  
312  N  N    . THR A 37  ? 0.2666 0.1246 0.2103 0.0483  0.0496  0.0274  37  THR A N    
313  C  CA   . THR A 37  ? 0.2369 0.1473 0.2051 0.0509  0.0478  0.0205  37  THR A CA   
314  C  C    . THR A 37  ? 0.1904 0.1365 0.1916 0.0750  0.0377  0.0193  37  THR A C    
315  O  O    . THR A 37  ? 0.2642 0.1773 0.1994 0.0689  0.0241  -0.0147 37  THR A O    
316  C  CB   . THR A 37  ? 0.2527 0.1952 0.2107 0.0612  0.0130  0.0239  37  THR A CB   
317  O  OG1  . THR A 37  ? 0.3309 0.0772 0.2964 0.0671  0.0483  -0.0057 37  THR A OG1  
318  C  CG2  . THR A 37  ? 0.2275 0.1383 0.1773 0.0361  0.0110  0.0625  37  THR A CG2  
319  N  N    . ALA A 38  ? 0.2102 0.1532 0.1908 0.0379  0.0516  0.0007  38  ALA A N    
320  C  CA   . ALA A 38  ? 0.1579 0.1439 0.1796 0.0750  0.0568  0.0252  38  ALA A CA   
321  C  C    . ALA A 38  ? 0.1679 0.1230 0.2299 0.0275  0.0553  0.0104  38  ALA A C    
322  O  O    . ALA A 38  ? 0.2387 0.1780 0.2982 0.0474  0.1102  0.0031  38  ALA A O    
323  C  CB   . ALA A 38  ? 0.2281 0.1268 0.2035 0.0432  0.0340  0.0146  38  ALA A CB   
324  N  N    . LYS A 39  ? 0.1981 0.1498 0.2138 0.0724  0.0379  0.0019  39  LYS A N    
325  C  CA   . LYS A 39  ? 0.1778 0.2153 0.2824 0.0860  0.0197  -0.0076 39  LYS A CA   
326  C  C    . LYS A 39  ? 0.1647 0.2105 0.2213 0.0399  0.0087  0.0013  39  LYS A C    
327  O  O    . LYS A 39  ? 0.1669 0.1577 0.1962 0.0434  0.0305  -0.0017 39  LYS A O    
328  C  CB   . LYS A 39  ? 0.2827 0.2242 0.2646 0.0494  0.0147  -0.0560 39  LYS A CB   
329  C  CG   . LYS A 39  ? 0.2502 0.2466 0.2849 0.0750  -0.0020 -0.0015 39  LYS A CG   
330  C  CD   . LYS A 39  ? 0.2319 0.2996 0.3005 0.1074  0.0048  0.0443  39  LYS A CD   
331  C  CE   . LYS A 39  ? 0.2919 0.3147 0.2863 0.0120  0.0439  0.0000  39  LYS A CE   
332  N  NZ   . LYS A 39  ? 0.2057 0.2766 0.3517 0.0189  0.0263  0.0449  39  LYS A NZ   
333  N  N    . TYR A 40  ? 0.1908 0.2066 0.2326 0.0200  0.0483  0.0070  40  TYR A N    
334  C  CA   . TYR A 40  ? 0.1994 0.1689 0.2351 -0.0251 0.0559  -0.0218 40  TYR A CA   
335  C  C    . TYR A 40  ? 0.1956 0.1844 0.2121 -0.0135 0.0458  -0.0077 40  TYR A C    
336  O  O    . TYR A 40  ? 0.1884 0.2383 0.1913 0.0438  0.0443  0.0015  40  TYR A O    
337  C  CB   . TYR A 40  ? 0.1839 0.2017 0.2732 -0.0535 0.0631  0.0296  40  TYR A CB   
338  C  CG   . TYR A 40  ? 0.2159 0.2561 0.2624 0.0038  0.0828  -0.0027 40  TYR A CG   
339  C  CD1  . TYR A 40  ? 0.2319 0.3183 0.2887 -0.0379 0.0333  0.0020  40  TYR A CD1  
340  C  CD2  . TYR A 40  ? 0.2189 0.4092 0.3167 -0.0065 0.0524  -0.0185 40  TYR A CD2  
341  C  CE1  . TYR A 40  ? 0.2761 0.3091 0.3003 0.0219  0.0821  0.0136  40  TYR A CE1  
342  C  CE2  . TYR A 40  ? 0.1866 0.4983 0.3201 0.0071  0.0318  0.0340  40  TYR A CE2  
343  C  CZ   . TYR A 40  ? 0.1920 0.4049 0.3185 0.0103  0.0175  0.0082  40  TYR A CZ   
344  O  OH   . TYR A 40  ? 0.2508 0.4707 0.3819 0.0652  0.0527  0.0197  40  TYR A OH   
345  N  N    . ASP A 41  ? 0.1665 0.1476 0.2233 0.0046  0.0399  -0.0142 41  ASP A N    
346  C  CA   . ASP A 41  ? 0.1455 0.1841 0.2120 -0.0063 0.0192  -0.0097 41  ASP A CA   
347  C  C    . ASP A 41  ? 0.2426 0.2409 0.2487 0.0340  0.0297  -0.0351 41  ASP A C    
348  O  O    . ASP A 41  ? 0.1694 0.2085 0.2290 0.0195  0.0373  -0.0082 41  ASP A O    
349  C  CB   . ASP A 41  ? 0.2035 0.1802 0.2671 -0.0178 0.0164  0.0109  41  ASP A CB   
350  C  CG   . ASP A 41  ? 0.2479 0.2741 0.3260 -0.0241 -0.0210 -0.0199 41  ASP A CG   
351  O  OD1  . ASP A 41  ? 0.3267 0.2790 0.3028 0.0417  0.0052  -0.0595 41  ASP A OD1  
352  O  OD2  . ASP A 41  ? 0.3012 0.2495 0.3865 -0.0696 -0.0305 0.0087  41  ASP A OD2  
353  N  N    . PRO A 42  ? 0.2283 0.3222 0.2469 0.0285  0.0317  -0.0074 42  PRO A N    
354  C  CA   . PRO A 42  ? 0.2292 0.3641 0.2759 0.0333  0.0507  0.0038  42  PRO A CA   
355  C  C    . PRO A 42  ? 0.2556 0.3560 0.2829 0.0441  0.0388  0.0006  42  PRO A C    
356  O  O    . PRO A 42  ? 0.2662 0.4186 0.3461 0.0913  0.0232  -0.0019 42  PRO A O    
357  C  CB   . PRO A 42  ? 0.2394 0.4222 0.2754 0.0478  0.0680  0.0035  42  PRO A CB   
358  C  CG   . PRO A 42  ? 0.3206 0.4092 0.2739 0.0285  0.0491  -0.0074 42  PRO A CG   
359  C  CD   . PRO A 42  ? 0.2725 0.2960 0.2324 0.0542  0.0604  0.0065  42  PRO A CD   
360  N  N    . SER A 43  ? 0.2958 0.3027 0.2468 0.0230  0.0195  -0.0285 43  SER A N    
361  C  CA   . SER A 43  ? 0.3373 0.2754 0.3106 0.0370  -0.0071 -0.0038 43  SER A CA   
362  C  C    . SER A 43  ? 0.3325 0.2556 0.3039 0.0463  -0.0020 -0.0006 43  SER A C    
363  O  O    . SER A 43  ? 0.4016 0.2344 0.3610 0.1124  0.0035  0.0114  43  SER A O    
364  C  CB   . SER A 43  ? 0.2876 0.3188 0.3260 0.0207  -0.0115 -0.0196 43  SER A CB   
365  O  OG   . SER A 43  ? 0.4357 0.2840 0.4260 -0.0443 0.0110  -0.0582 43  SER A OG   
366  N  N    . LEU A 44  ? 0.2949 0.2569 0.2833 0.0265  -0.0031 -0.0292 44  LEU A N    
367  C  CA   . LEU A 44  ? 0.2357 0.2538 0.2739 0.0193  -0.0141 0.0333  44  LEU A CA   
368  C  C    . LEU A 44  ? 0.2351 0.2709 0.2987 -0.0263 -0.0046 0.0302  44  LEU A C    
369  O  O    . LEU A 44  ? 0.2181 0.3749 0.3630 -0.0200 0.0017  0.0926  44  LEU A O    
370  C  CB   . LEU A 44  ? 0.1938 0.1755 0.2795 -0.0006 0.0135  0.0017  44  LEU A CB   
371  C  CG   . LEU A 44  ? 0.1789 0.1823 0.2163 -0.0035 -0.0107 0.0346  44  LEU A CG   
372  C  CD1  . LEU A 44  ? 0.1863 0.1825 0.2371 0.0366  0.0184  -0.0087 44  LEU A CD1  
373  C  CD2  . LEU A 44  ? 0.2401 0.1994 0.2581 -0.0715 -0.0115 0.0390  44  LEU A CD2  
374  N  N    . LYS A 45  ? 0.2196 0.2172 0.2894 -0.0049 -0.0388 0.0337  45  LYS A N    
375  C  CA   . LYS A 45  ? 0.2078 0.2161 0.3298 0.0249  -0.0318 -0.0197 45  LYS A CA   
376  C  C    . LYS A 45  ? 0.1599 0.2091 0.3088 0.0615  -0.0098 -0.0007 45  LYS A C    
377  O  O    . LYS A 45  ? 0.1306 0.2326 0.3348 0.0205  -0.0013 -0.0270 45  LYS A O    
378  C  CB   . LYS A 45  ? 0.2878 0.2319 0.3109 0.0689  -0.0237 -0.0109 45  LYS A CB   
379  C  CG   . LYS A 45  ? 0.2475 0.3368 0.3731 0.0362  -0.0847 -0.0570 45  LYS A CG   
380  C  CD   . LYS A 45  ? 0.4476 0.4189 0.4641 -0.0244 -0.0155 -0.0406 45  LYS A CD   
381  C  CE   . LYS A 45  ? 0.5296 0.5357 0.5497 0.0203  -0.0020 -0.0443 45  LYS A CE   
382  N  NZ   . LYS A 45  ? 0.6273 0.6115 0.5325 0.0140  0.0281  -0.0414 45  LYS A NZ   
383  N  N    . PRO A 46  ? 0.1371 0.1951 0.2976 -0.0322 0.0052  -0.0215 46  PRO A N    
384  C  CA   . PRO A 46  ? 0.1455 0.2067 0.3014 -0.0048 0.0153  0.0060  46  PRO A CA   
385  C  C    . PRO A 46  ? 0.1191 0.1884 0.2689 0.0181  0.0361  0.0140  46  PRO A C    
386  O  O    . PRO A 46  ? 0.0790 0.2110 0.3174 -0.0160 -0.0038 -0.0120 46  PRO A O    
387  C  CB   . PRO A 46  ? 0.1575 0.2394 0.3194 0.0208  0.0185  -0.0052 46  PRO A CB   
388  C  CG   . PRO A 46  ? 0.1360 0.2608 0.3172 -0.0054 0.0298  -0.0518 46  PRO A CG   
389  C  CD   . PRO A 46  ? 0.1818 0.2272 0.3433 0.0649  -0.0019 -0.0592 46  PRO A CD   
390  N  N    . LEU A 47  ? 0.1261 0.2276 0.3203 0.0487  0.0093  0.0242  47  LEU A N    
391  C  CA   . LEU A 47  ? 0.0722 0.1561 0.2957 0.0230  0.0175  0.0458  47  LEU A CA   
392  C  C    . LEU A 47  ? 0.1036 0.1870 0.3285 -0.0148 -0.0241 0.0296  47  LEU A C    
393  O  O    . LEU A 47  ? 0.0970 0.2265 0.4070 -0.0688 -0.0087 0.0671  47  LEU A O    
394  C  CB   . LEU A 47  ? 0.1588 0.1762 0.3447 0.0203  0.0226  0.0355  47  LEU A CB   
395  C  CG   . LEU A 47  ? 0.1173 0.2172 0.3914 0.0317  -0.0121 -0.0623 47  LEU A CG   
396  C  CD1  . LEU A 47  ? 0.1110 0.1808 0.4110 -0.0073 -0.0218 -0.0557 47  LEU A CD1  
397  C  CD2  . LEU A 47  ? 0.0927 0.1816 0.3829 0.0394  -0.0196 -0.0410 47  LEU A CD2  
398  N  N    . SER A 48  ? 0.0828 0.1543 0.2944 -0.0046 -0.0035 0.0131  48  SER A N    
399  C  CA   . SER A 48  ? 0.1121 0.1322 0.2838 -0.0324 0.0148  0.0031  48  SER A CA   
400  C  C    . SER A 48  ? 0.0658 0.1424 0.2745 -0.0068 0.0054  -0.0271 48  SER A C    
401  O  O    . SER A 48  ? 0.0499 0.1177 0.3287 -0.0450 0.0080  -0.0308 48  SER A O    
402  C  CB   . SER A 48  ? 0.0986 0.1482 0.3104 -0.0186 0.0115  0.0121  48  SER A CB   
403  O  OG   . SER A 48  ? 0.1611 0.1556 0.3621 0.0571  -0.0272 0.0027  48  SER A OG   
404  N  N    . VAL A 49  ? 0.1133 0.1216 0.2892 -0.0364 0.0065  -0.0199 49  VAL A N    
405  C  CA   . VAL A 49  ? 0.0974 0.1239 0.2815 -0.0377 -0.0114 -0.0092 49  VAL A CA   
406  C  C    . VAL A 49  ? 0.0905 0.1525 0.2991 -0.0335 -0.0450 -0.0177 49  VAL A C    
407  O  O    . VAL A 49  ? 0.1004 0.2380 0.3237 -0.0942 -0.0285 -0.0265 49  VAL A O    
408  C  CB   . VAL A 49  ? 0.1956 0.1180 0.2827 -0.0076 0.0034  -0.0361 49  VAL A CB   
409  C  CG1  . VAL A 49  ? 0.2436 0.1917 0.3154 -0.0513 0.0494  -0.0264 49  VAL A CG1  
410  C  CG2  . VAL A 49  ? 0.1180 0.2109 0.3440 -0.0348 0.0071  -0.0076 49  VAL A CG2  
411  N  N    . SER A 50  ? 0.1674 0.1868 0.2714 -0.0132 -0.0421 0.0003  50  SER A N    
412  C  CA   . SER A 50  ? 0.1324 0.1566 0.3136 -0.0308 -0.0399 0.0023  50  SER A CA   
413  C  C    . SER A 50  ? 0.1298 0.1692 0.2975 -0.0038 -0.0807 -0.0043 50  SER A C    
414  O  O    . SER A 50  ? 0.1570 0.1525 0.3233 -0.0584 -0.0579 0.0052  50  SER A O    
415  C  CB   . SER A 50  ? 0.1604 0.2020 0.2858 0.0175  -0.0315 0.0320  50  SER A CB   
416  O  OG   . SER A 50  ? 0.2189 0.3066 0.3759 -0.0098 -0.0181 0.0142  50  SER A OG   
417  N  N    . TYR A 51  ? 0.1410 0.1511 0.3086 -0.0087 -0.0489 -0.0141 51  TYR A N    
418  C  CA   . TYR A 51  ? 0.1574 0.1494 0.2592 -0.0335 -0.0610 0.0165  51  TYR A CA   
419  C  C    . TYR A 51  ? 0.1629 0.1658 0.2951 0.0198  -0.0410 0.0408  51  TYR A C    
420  O  O    . TYR A 51  ? 0.1685 0.1870 0.2854 -0.0051 -0.0636 0.0318  51  TYR A O    
421  C  CB   . TYR A 51  ? 0.1298 0.1519 0.2795 -0.0306 -0.0581 -0.0030 51  TYR A CB   
422  C  CG   . TYR A 51  ? 0.1094 0.0993 0.2240 -0.0308 -0.0329 0.0559  51  TYR A CG   
423  C  CD1  . TYR A 51  ? 0.0997 0.1090 0.2799 0.0013  -0.0142 0.0228  51  TYR A CD1  
424  C  CD2  . TYR A 51  ? 0.1234 0.1300 0.2060 -0.0271 -0.0092 0.0653  51  TYR A CD2  
425  C  CE1  . TYR A 51  ? 0.1070 0.1101 0.2606 -0.0174 -0.0423 0.0274  51  TYR A CE1  
426  C  CE2  . TYR A 51  ? 0.0706 0.0819 0.2107 -0.0318 -0.0186 0.0197  51  TYR A CE2  
427  C  CZ   . TYR A 51  ? 0.0916 0.0862 0.2498 -0.0465 -0.0093 0.0203  51  TYR A CZ   
428  O  OH   . TYR A 51  ? 0.0830 0.0900 0.2315 -0.0192 -0.0241 -0.0046 51  TYR A OH   
429  N  N    A ASP A 52  ? 0.1672 0.2012 0.3212 -0.0043 -0.0505 0.0355  52  ASP A N    
430  N  N    B ASP A 52  ? 0.1676 0.2202 0.3134 -0.0077 -0.0509 0.0408  52  ASP A N    
431  C  CA   A ASP A 52  ? 0.1888 0.2189 0.3046 0.0153  -0.0333 0.0509  52  ASP A CA   
432  C  CA   B ASP A 52  ? 0.1902 0.2473 0.3005 0.0120  -0.0408 0.0515  52  ASP A CA   
433  C  C    A ASP A 52  ? 0.2078 0.2227 0.3366 0.0186  -0.0348 0.0483  52  ASP A C    
434  C  C    B ASP A 52  ? 0.2092 0.2671 0.3330 0.0231  -0.0401 0.0441  52  ASP A C    
435  O  O    A ASP A 52  ? 0.2592 0.2056 0.3301 0.0153  -0.0337 0.0803  52  ASP A O    
436  O  O    B ASP A 52  ? 0.1847 0.2992 0.3368 0.0610  -0.0250 0.0441  52  ASP A O    
437  C  CB   A ASP A 52  ? 0.2204 0.2693 0.3361 0.0087  -0.0318 0.0340  52  ASP A CB   
438  C  CB   B ASP A 52  ? 0.2232 0.3106 0.3000 -0.0026 -0.0275 0.0366  52  ASP A CB   
439  C  CG   A ASP A 52  ? 0.2430 0.2964 0.3600 0.0074  -0.0026 0.0080  52  ASP A CG   
440  C  CG   B ASP A 52  ? 0.2694 0.3206 0.3695 0.0206  -0.0315 0.0353  52  ASP A CG   
441  O  OD1  A ASP A 52  ? 0.2583 0.3260 0.4235 -0.0243 -0.0126 -0.0006 52  ASP A OD1  
442  O  OD1  B ASP A 52  ? 0.4110 0.3781 0.4085 0.0593  -0.0137 0.0113  52  ASP A OD1  
443  O  OD2  A ASP A 52  ? 0.4592 0.3537 0.4757 0.0161  0.0006  0.0397  52  ASP A OD2  
444  O  OD2  B ASP A 52  ? 0.4271 0.3727 0.4660 0.0342  0.0248  0.0315  52  ASP A OD2  
445  N  N    . GLN A 53  ? 0.1658 0.2218 0.3476 0.0219  -0.0443 0.0723  53  GLN A N    
446  C  CA   . GLN A 53  ? 0.2279 0.2279 0.3732 0.0148  -0.0230 0.0538  53  GLN A CA   
447  C  C    . GLN A 53  ? 0.2348 0.1870 0.3106 0.0219  -0.0140 0.0175  53  GLN A C    
448  O  O    . GLN A 53  ? 0.2109 0.1755 0.3531 0.0154  -0.0317 0.0247  53  GLN A O    
449  C  CB   . GLN A 53  ? 0.2815 0.2678 0.4084 0.0167  -0.0096 0.0280  53  GLN A CB   
450  C  CG   . GLN A 53  ? 0.2799 0.3704 0.4444 0.0185  0.0098  0.0430  53  GLN A CG   
451  C  CD   . GLN A 53  ? 0.4531 0.5242 0.4986 -0.0027 0.0120  0.0383  53  GLN A CD   
452  O  OE1  . GLN A 53  ? 0.4921 0.5619 0.5422 0.0586  0.0693  0.0432  53  GLN A OE1  
453  N  NE2  . GLN A 53  ? 0.4131 0.5766 0.5249 0.0006  0.0238  0.0230  53  GLN A NE2  
454  N  N    . ALA A 54  ? 0.2096 0.1370 0.3104 -0.0227 -0.0366 0.0115  54  ALA A N    
455  C  CA   . ALA A 54  ? 0.1760 0.1239 0.2675 0.0364  -0.0445 0.0210  54  ALA A CA   
456  C  C    . ALA A 54  ? 0.2089 0.1448 0.2549 0.0131  -0.0608 -0.0087 54  ALA A C    
457  O  O    . ALA A 54  ? 0.2335 0.3027 0.3206 -0.0423 -0.0687 -0.0366 54  ALA A O    
458  C  CB   . ALA A 54  ? 0.1983 0.1286 0.3115 0.0384  -0.0403 0.0013  54  ALA A CB   
459  N  N    A THR A 55  ? 0.1656 0.1396 0.2423 0.0386  -0.0270 0.0274  55  THR A N    
460  N  N    B THR A 55  ? 0.1996 0.1189 0.2430 0.0355  -0.0284 0.0331  55  THR A N    
461  C  CA   A THR A 55  ? 0.1881 0.1124 0.2269 0.0417  -0.0465 0.0102  55  THR A CA   
462  C  CA   B THR A 55  ? 0.2168 0.1369 0.2371 0.0291  -0.0355 0.0087  55  THR A CA   
463  C  C    A THR A 55  ? 0.1635 0.0785 0.1916 0.0241  -0.0255 0.0062  55  THR A C    
464  C  C    B THR A 55  ? 0.2152 0.1088 0.1812 0.0175  -0.0368 0.0225  55  THR A C    
465  O  O    A THR A 55  ? 0.1872 0.0465 0.1996 0.0187  -0.0228 0.0258  55  THR A O    
466  O  O    B THR A 55  ? 0.2632 0.1124 0.1974 -0.0031 -0.0292 0.0031  55  THR A O    
467  C  CB   A THR A 55  ? 0.2256 0.1412 0.2443 0.0080  -0.0320 -0.0086 55  THR A CB   
468  C  CB   B THR A 55  ? 0.2191 0.1543 0.2711 0.0307  -0.0062 0.0109  55  THR A CB   
469  O  OG1  A THR A 55  ? 0.2712 0.0397 0.3181 0.0230  -0.0666 -0.0070 55  THR A OG1  
470  O  OG1  B THR A 55  ? 0.2655 0.1708 0.2608 0.0132  0.0203  -0.0183 55  THR A OG1  
471  C  CG2  A THR A 55  ? 0.2797 0.0709 0.2051 0.1032  0.0274  0.0074  55  THR A CG2  
472  C  CG2  B THR A 55  ? 0.2242 0.1798 0.2917 0.0060  -0.0351 0.0390  55  THR A CG2  
473  N  N    A SER A 56  ? 0.1353 0.0643 0.1970 0.0142  -0.0177 0.0198  56  SER A N    
474  N  N    B SER A 56  ? 0.2245 0.1071 0.1787 0.0197  -0.0132 -0.0007 56  SER A N    
475  C  CA   A SER A 56  ? 0.1151 0.0803 0.1992 -0.0027 -0.0003 0.0153  56  SER A CA   
476  C  CA   B SER A 56  ? 0.2015 0.0925 0.2026 -0.0051 -0.0037 -0.0136 56  SER A CA   
477  C  C    A SER A 56  ? 0.1430 0.0970 0.2057 0.0031  -0.0283 -0.0023 56  SER A C    
478  C  C    B SER A 56  ? 0.1444 0.0702 0.2168 -0.0013 0.0132  -0.0230 56  SER A C    
479  O  O    A SER A 56  ? 0.0907 0.0895 0.2037 0.0283  -0.0210 0.0160  56  SER A O    
480  O  O    B SER A 56  ? 0.2308 0.0828 0.1941 -0.0093 -0.0148 -0.0322 56  SER A O    
481  C  CB   A SER A 56  ? 0.1708 0.0659 0.2028 -0.0043 -0.0244 -0.0231 56  SER A CB   
482  C  CB   B SER A 56  ? 0.1972 0.0889 0.1854 -0.0118 -0.0054 -0.0017 56  SER A CB   
483  O  OG   A SER A 56  ? 0.2013 0.1128 0.2250 0.0121  -0.0291 0.0120  56  SER A OG   
484  O  OG   B SER A 56  ? 0.2177 0.0371 0.2019 0.0012  -0.0537 -0.0136 56  SER A OG   
485  N  N    A LEU A 57  ? 0.1027 0.0894 0.1826 0.0124  -0.0200 0.0226  57  LEU A N    
486  N  N    B LEU A 57  ? 0.1859 0.1088 0.1487 0.0160  0.0137  -0.0010 57  LEU A N    
487  C  CA   A LEU A 57  ? 0.1223 0.0575 0.1949 0.0236  -0.0093 0.0091  57  LEU A CA   
488  C  CA   B LEU A 57  ? 0.2028 0.0769 0.1701 0.0160  0.0322  -0.0012 57  LEU A CA   
489  C  C    A LEU A 57  ? 0.0909 0.0855 0.1762 0.0087  -0.0034 -0.0217 57  LEU A C    
490  C  C    B LEU A 57  ? 0.2145 0.0693 0.1834 0.0370  0.0146  -0.0003 57  LEU A C    
491  O  O    A LEU A 57  ? 0.0988 0.0925 0.1780 0.0046  0.0026  0.0192  57  LEU A O    
492  O  O    B LEU A 57  ? 0.2118 0.0948 0.1441 0.0104  0.0038  0.0159  57  LEU A O    
493  C  CB   A LEU A 57  ? 0.1419 0.0916 0.2304 -0.0104 -0.0178 -0.0282 57  LEU A CB   
494  C  CB   B LEU A 57  ? 0.2328 0.1097 0.1844 0.0340  0.0384  -0.0052 57  LEU A CB   
495  C  CG   A LEU A 57  ? 0.1581 0.0824 0.2329 0.0104  -0.0238 0.0125  57  LEU A CG   
496  C  CG   B LEU A 57  ? 0.2461 0.1097 0.2517 0.0452  0.0130  -0.0405 57  LEU A CG   
497  C  CD1  A LEU A 57  ? 0.1956 0.1913 0.3348 -0.0608 -0.0450 0.0221  57  LEU A CD1  
498  C  CD1  B LEU A 57  ? 0.2660 0.1658 0.2028 0.0302  0.0518  -0.0260 57  LEU A CD1  
499  C  CD2  A LEU A 57  ? 0.2001 0.0693 0.3034 0.0570  -0.0417 0.0315  57  LEU A CD2  
500  C  CD2  B LEU A 57  ? 0.3122 0.2682 0.3070 0.0454  0.0006  -0.0015 57  LEU A CD2  
501  N  N    A ARG A 58  ? 0.0477 0.0589 0.1987 -0.0037 0.0046  0.0143  58  ARG A N    
502  N  N    B ARG A 58  ? 0.1776 0.1200 0.1453 0.0199  0.0017  0.0238  58  ARG A N    
503  C  CA   A ARG A 58  ? 0.0636 0.0763 0.1843 -0.0003 0.0228  0.0370  58  ARG A CA   
504  C  CA   B ARG A 58  ? 0.1940 0.0993 0.1852 0.0153  0.0296  0.0340  58  ARG A CA   
505  C  C    A ARG A 58  ? 0.0540 0.0646 0.1740 -0.0280 0.0187  0.0215  58  ARG A C    
506  C  C    B ARG A 58  ? 0.1710 0.0988 0.1764 0.0063  0.0252  0.0189  58  ARG A C    
507  O  O    A ARG A 58  ? 0.0577 0.0528 0.1834 -0.0010 0.0046  -0.0088 58  ARG A O    
508  O  O    B ARG A 58  ? 0.1915 0.1194 0.1579 0.0487  0.0259  0.0463  58  ARG A O    
509  C  CB   A ARG A 58  ? 0.0970 0.1318 0.1933 -0.0118 0.0023  0.0081  58  ARG A CB   
510  C  CB   B ARG A 58  ? 0.1805 0.0921 0.1917 0.0211  0.0357  0.0093  58  ARG A CB   
511  C  CG   A ARG A 58  ? 0.0912 0.1401 0.1602 -0.0608 0.0412  0.0414  58  ARG A CG   
512  C  CG   B ARG A 58  ? 0.1435 0.1951 0.2064 0.0054  0.0206  0.0081  58  ARG A CG   
513  C  CD   A ARG A 58  ? 0.1632 0.1891 0.2030 -0.0244 0.0153  -0.0086 58  ARG A CD   
514  C  CD   B ARG A 58  ? 0.1394 0.1338 0.2640 0.0623  -0.0577 -0.0384 58  ARG A CD   
515  N  NE   A ARG A 58  ? 0.1013 0.1593 0.1908 0.0335  0.0221  0.0283  58  ARG A NE   
516  N  NE   B ARG A 58  ? 0.1737 0.2243 0.2121 -0.0438 -0.0119 -0.0162 58  ARG A NE   
517  C  CZ   A ARG A 58  ? 0.0627 0.2211 0.2177 -0.0007 -0.0197 0.0408  58  ARG A CZ   
518  C  CZ   B ARG A 58  ? 0.0905 0.1783 0.1845 0.0048  -0.0031 0.0221  58  ARG A CZ   
519  N  NH1  A ARG A 58  ? 0.1708 0.2662 0.2705 0.0093  0.0003  -0.0272 58  ARG A NH1  
520  N  NH1  B ARG A 58  ? 0.1805 0.1342 0.2211 -0.1206 0.0286  0.0143  58  ARG A NH1  
521  N  NH2  A ARG A 58  ? 0.1861 0.1780 0.3027 0.0390  -0.0126 0.0059  58  ARG A NH2  
522  N  NH2  B ARG A 58  ? 0.1203 0.0557 0.2441 0.0155  0.0052  -0.0052 58  ARG A NH2  
523  N  N    A ILE A 59  ? 0.0445 0.0433 0.1703 -0.0104 0.0013  -0.0057 59  ILE A N    
524  N  N    B ILE A 59  ? 0.1259 0.0483 0.1719 0.0023  0.0259  0.0182  59  ILE A N    
525  C  CA   A ILE A 59  ? 0.0316 0.0707 0.1589 -0.0098 0.0207  0.0104  59  ILE A CA   
526  C  CA   B ILE A 59  ? 0.1399 0.0864 0.1672 0.0015  0.0118  0.0087  59  ILE A CA   
527  C  C    A ILE A 59  ? 0.0254 0.0309 0.1377 0.0006  0.0017  -0.0074 59  ILE A C    
528  C  C    B ILE A 59  ? 0.1421 0.0592 0.1550 -0.0208 0.0188  0.0031  59  ILE A C    
529  O  O    A ILE A 59  ? 0.0458 0.1128 0.1444 -0.0098 0.0027  0.0017  59  ILE A O    
530  O  O    B ILE A 59  ? 0.1361 0.1575 0.1173 -0.0026 0.0092  0.0174  59  ILE A O    
531  C  CB   A ILE A 59  ? 0.0625 0.0639 0.1473 -0.0351 0.0126  0.0131  59  ILE A CB   
532  C  CB   B ILE A 59  ? 0.1428 0.1033 0.1421 -0.0113 0.0153  0.0073  59  ILE A CB   
533  C  CG1  A ILE A 59  ? 0.1130 0.0783 0.1401 -0.0086 0.0315  0.0198  59  ILE A CG1  
534  C  CG1  B ILE A 59  ? 0.1153 0.0769 0.1663 0.0126  0.0013  0.0302  59  ILE A CG1  
535  C  CG2  A ILE A 59  ? 0.0763 0.0636 0.1626 0.0181  0.0000  0.0401  59  ILE A CG2  
536  C  CG2  B ILE A 59  ? 0.1207 0.1047 0.1678 -0.0326 0.0114  -0.0293 59  ILE A CG2  
537  C  CD1  A ILE A 59  ? 0.1243 0.0489 0.1884 -0.0483 0.0313  -0.0141 59  ILE A CD1  
538  C  CD1  B ILE A 59  ? 0.1455 0.1092 0.2071 0.0119  0.0200  0.0019  59  ILE A CD1  
539  N  N    A LEU A 60  ? 0.0417 0.0588 0.1221 0.0006  0.0007  0.0019  60  LEU A N    
540  N  N    B LEU A 60  ? 0.1491 0.0837 0.1607 -0.0108 0.0023  0.0151  60  LEU A N    
541  C  CA   A LEU A 60  ? 0.0445 0.0329 0.1586 -0.0020 -0.0096 0.0151  60  LEU A CA   
542  C  CA   B LEU A 60  ? 0.1742 0.0521 0.1701 -0.0137 0.0248  0.0017  60  LEU A CA   
543  C  C    A LEU A 60  ? 0.0525 0.0376 0.1533 -0.0173 0.0113  0.0048  60  LEU A C    
544  C  C    B LEU A 60  ? 0.1563 0.0542 0.1557 -0.0205 0.0254  0.0049  60  LEU A C    
545  O  O    A LEU A 60  ? 0.0654 0.0367 0.1397 -0.0109 0.0131  0.0054  60  LEU A O    
546  O  O    B LEU A 60  ? 0.1568 0.0675 0.1334 -0.0192 0.0208  0.0104  60  LEU A O    
547  C  CB   A LEU A 60  ? 0.0455 0.0274 0.1816 -0.0063 0.0221  -0.0035 60  LEU A CB   
548  C  CB   B LEU A 60  ? 0.1773 0.0463 0.2023 -0.0370 0.0031  0.0193  60  LEU A CB   
549  C  CG   A LEU A 60  ? 0.0711 0.0582 0.1913 -0.0353 -0.0176 0.0020  60  LEU A CG   
550  C  CG   B LEU A 60  ? 0.1689 0.1176 0.1832 -0.0126 -0.0121 -0.0118 60  LEU A CG   
551  C  CD1  A LEU A 60  ? 0.0297 0.0556 0.1951 -0.0114 0.0109  -0.0306 60  LEU A CD1  
552  C  CD1  B LEU A 60  ? 0.1572 0.0834 0.1906 0.0129  0.0329  0.0247  60  LEU A CD1  
553  C  CD2  A LEU A 60  ? 0.0465 0.0481 0.1694 -0.0214 0.0192  -0.0087 60  LEU A CD2  
554  C  CD2  B LEU A 60  ? 0.1888 0.0975 0.1802 -0.0258 0.0239  -0.0207 60  LEU A CD2  
555  N  N    A ASN A 61  ? 0.0675 0.0297 0.1581 -0.0121 0.0063  -0.0122 61  ASN A N    
556  N  N    B ASN A 61  ? 0.1661 0.0803 0.1263 -0.0216 0.0206  -0.0250 61  ASN A N    
557  C  CA   A ASN A 61  ? 0.0837 0.0511 0.1550 -0.0015 -0.0068 -0.0188 61  ASN A CA   
558  C  CA   B ASN A 61  ? 0.1559 0.0778 0.1509 -0.0287 0.0335  0.0006  61  ASN A CA   
559  C  C    A ASN A 61  ? 0.0432 0.0785 0.1658 0.0185  -0.0135 0.0115  61  ASN A C    
560  C  C    B ASN A 61  ? 0.1906 0.0898 0.1582 -0.0359 0.0478  -0.0137 61  ASN A C    
561  O  O    A ASN A 61  ? 0.0625 0.0632 0.1532 0.0250  -0.0043 0.0487  61  ASN A O    
562  O  O    B ASN A 61  ? 0.1861 0.0658 0.1550 -0.0272 0.0412  -0.0035 61  ASN A O    
563  C  CB   A ASN A 61  ? 0.0446 0.0733 0.1681 0.0126  -0.0109 -0.0500 61  ASN A CB   
564  C  CB   B ASN A 61  ? 0.1272 0.0645 0.1572 -0.0296 0.0214  -0.0390 61  ASN A CB   
565  C  CG   A ASN A 61  ? 0.0429 0.0724 0.1324 -0.0027 0.0000  0.0031  61  ASN A CG   
566  C  CG   B ASN A 61  ? 0.1295 0.0923 0.1636 -0.0248 0.0159  0.0003  61  ASN A CG   
567  O  OD1  A ASN A 61  ? 0.1263 0.0436 0.1403 0.0000  0.0309  -0.0096 61  ASN A OD1  
568  O  OD1  B ASN A 61  ? 0.1518 0.0810 0.1947 -0.0281 0.0020  -0.0160 61  ASN A OD1  
569  N  ND2  A ASN A 61  ? 0.0269 0.0503 0.1205 -0.0052 0.0070  -0.0021 61  ASN A ND2  
570  N  ND2  B ASN A 61  ? 0.1475 0.0634 0.1748 -0.0299 0.0120  -0.0052 61  ASN A ND2  
571  N  N    . ASN A 62  ? 0.1987 0.0889 0.1701 -0.0562 0.0102  0.0104  62  ASN A N    
572  C  CA   . ASN A 62  ? 0.1963 0.0977 0.1629 -0.0522 0.0184  -0.0118 62  ASN A CA   
573  C  C    . ASN A 62  ? 0.2344 0.1108 0.1708 -0.0348 0.0406  -0.0153 62  ASN A C    
574  O  O    . ASN A 62  ? 0.2899 0.1525 0.2139 -0.0759 0.0286  -0.0270 62  ASN A O    
575  C  CB   . ASN A 62  ? 0.2829 0.0927 0.1654 -0.0636 0.0110  0.0074  62  ASN A CB   
576  C  CG   . ASN A 62  ? 0.2971 0.1306 0.1467 -0.0592 -0.0060 -0.0054 62  ASN A CG   
577  O  OD1  . ASN A 62  ? 0.2725 0.0483 0.2053 -0.0538 0.0553  0.0015  62  ASN A OD1  
578  N  ND2  . ASN A 62  ? 0.4222 0.1306 0.2275 -0.0568 0.0469  -0.0185 62  ASN A ND2  
579  N  N    . GLY A 63  ? 0.2576 0.0900 0.1757 -0.0342 0.0410  -0.0098 63  GLY A N    
580  C  CA   . GLY A 63  ? 0.1938 0.1180 0.1668 -0.0375 0.0489  0.0071  63  GLY A CA   
581  C  C    . GLY A 63  ? 0.2046 0.1047 0.2046 -0.0584 0.0230  -0.0093 63  GLY A C    
582  O  O    . GLY A 63  ? 0.1697 0.1198 0.2017 -0.0324 0.0225  -0.0156 63  GLY A O    
583  N  N    . HIS A 64  ? 0.1895 0.0715 0.1632 -0.0351 0.0384  0.0043  64  HIS A N    
584  C  CA   . HIS A 64  ? 0.1613 0.1629 0.1941 -0.0291 0.0270  0.0024  64  HIS A CA   
585  C  C    . HIS A 64  ? 0.1067 0.0939 0.2005 -0.0399 0.0265  0.0209  64  HIS A C    
586  O  O    . HIS A 64  ? 0.1491 0.1358 0.2960 -0.0364 0.0129  0.0843  64  HIS A O    
587  C  CB   . HIS A 64  ? 0.1751 0.1155 0.1902 -0.0544 0.0140  -0.0118 64  HIS A CB   
588  C  CG   . HIS A 64  ? 0.1819 0.1437 0.2200 -0.0529 0.0071  -0.0038 64  HIS A CG   
589  N  ND1  . HIS A 64  ? 0.1819 0.2078 0.2001 -0.0666 0.0274  -0.0445 64  HIS A ND1  
590  C  CD2  . HIS A 64  ? 0.1816 0.1232 0.2394 -0.0390 0.0461  -0.0035 64  HIS A CD2  
591  C  CE1  . HIS A 64  ? 0.1361 0.2269 0.2597 -0.0619 0.0403  -0.0324 64  HIS A CE1  
592  N  NE2  . HIS A 64  ? 0.1771 0.2551 0.2651 -0.0502 0.0759  0.0030  64  HIS A NE2  
593  N  N    . ALA A 65  ? 0.1288 0.0706 0.1787 -0.0348 0.0143  0.0031  65  ALA A N    
594  C  CA   . ALA A 65  ? 0.1642 0.0727 0.1805 -0.0573 0.0099  -0.0043 65  ALA A CA   
595  C  C    . ALA A 65  ? 0.1550 0.0959 0.1608 -0.0286 0.0057  -0.0096 65  ALA A C    
596  O  O    . ALA A 65  ? 0.2033 0.0855 0.1905 -0.0434 0.0252  0.0186  65  ALA A O    
597  C  CB   . ALA A 65  ? 0.1333 0.1342 0.1762 -0.0313 0.0142  -0.0046 65  ALA A CB   
598  N  N    . PHE A 66  ? 0.1390 0.0657 0.1784 -0.0098 0.0091  0.0085  66  PHE A N    
599  C  CA   . PHE A 66  ? 0.1622 0.1038 0.1737 0.0012  0.0114  0.0226  66  PHE A CA   
600  C  C    . PHE A 66  ? 0.1620 0.0590 0.1708 -0.0126 -0.0142 -0.0126 66  PHE A C    
601  O  O    . PHE A 66  ? 0.1787 0.0607 0.1717 -0.0023 0.0000  0.0164  66  PHE A O    
602  C  CB   . PHE A 66  ? 0.1676 0.1277 0.1719 -0.0159 -0.0107 0.0307  66  PHE A CB   
603  C  CG   . PHE A 66  ? 0.2064 0.0993 0.1660 -0.0340 -0.0081 -0.0013 66  PHE A CG   
604  C  CD1  . PHE A 66  ? 0.1546 0.0835 0.1658 -0.0196 -0.0183 0.0019  66  PHE A CD1  
605  C  CD2  . PHE A 66  ? 0.1703 0.0808 0.1500 -0.0346 -0.0207 -0.0041 66  PHE A CD2  
606  C  CE1  . PHE A 66  ? 0.1685 0.0758 0.2008 -0.0443 0.0076  -0.0299 66  PHE A CE1  
607  C  CE2  . PHE A 66  ? 0.1879 0.0612 0.1944 -0.0166 -0.0153 0.0107  66  PHE A CE2  
608  C  CZ   . PHE A 66  ? 0.1622 0.0995 0.1841 -0.0077 -0.0546 -0.0131 66  PHE A CZ   
609  N  N    A ASN A 67  ? 0.1142 0.0627 0.1448 -0.0015 -0.0232 0.0242  67  ASN A N    
610  N  N    B ASN A 67  ? 0.1704 0.0469 0.1884 -0.0339 -0.0364 -0.0109 67  ASN A N    
611  C  CA   A ASN A 67  ? 0.0934 0.0564 0.1519 0.0099  -0.0291 0.0027  67  ASN A CA   
612  C  CA   B ASN A 67  ? 0.1396 0.0690 0.1538 -0.0264 -0.0456 -0.0031 67  ASN A CA   
613  C  C    A ASN A 67  ? 0.0428 0.0465 0.1507 0.0104  0.0093  0.0052  67  ASN A C    
614  C  C    B ASN A 67  ? 0.1464 0.0623 0.1978 -0.0178 -0.0248 0.0043  67  ASN A C    
615  O  O    A ASN A 67  ? 0.0384 0.0505 0.1351 -0.0178 -0.0076 0.0026  67  ASN A O    
616  O  O    B ASN A 67  ? 0.1543 0.1052 0.1597 0.0046  -0.0219 0.0299  67  ASN A O    
617  C  CB   A ASN A 67  ? 0.0663 0.0463 0.1624 0.0277  -0.0173 0.0043  67  ASN A CB   
618  C  CB   B ASN A 67  ? 0.1022 0.0740 0.1967 -0.0577 -0.0251 -0.0104 67  ASN A CB   
619  C  CG   A ASN A 67  ? 0.0948 0.0887 0.1272 -0.0183 -0.0010 0.0136  67  ASN A CG   
620  C  CG   B ASN A 67  ? 0.1647 0.1369 0.2265 -0.0076 -0.0186 0.0184  67  ASN A CG   
621  O  OD1  A ASN A 67  ? 0.1164 0.0675 0.1575 -0.0610 -0.0432 0.0164  67  ASN A OD1  
622  O  OD1  B ASN A 67  ? 0.1762 0.1106 0.2116 -0.0326 -0.0232 0.0489  67  ASN A OD1  
623  N  ND2  A ASN A 67  ? 0.0551 0.0894 0.2053 0.0074  0.0383  -0.0276 67  ASN A ND2  
624  N  ND2  B ASN A 67  ? 0.1509 0.1760 0.2700 -0.0263 0.0020  0.0315  67  ASN A ND2  
625  N  N    A VAL A 68  ? 0.0454 0.0570 0.1425 -0.0251 -0.0112 0.0091  68  VAL A N    
626  N  N    B VAL A 68  ? 0.1376 0.0445 0.1830 0.0210  0.0035  0.0165  68  VAL A N    
627  C  CA   A VAL A 68  ? 0.0690 0.0464 0.1383 -0.0041 -0.0071 0.0027  68  VAL A CA   
628  C  CA   B VAL A 68  ? 0.0891 0.0449 0.1780 0.0335  -0.0030 -0.0060 68  VAL A CA   
629  C  C    A VAL A 68  ? 0.0331 0.0422 0.1529 0.0087  -0.0153 0.0093  68  VAL A C    
630  C  C    B VAL A 68  ? 0.1778 0.0828 0.2008 0.0076  -0.0031 0.0048  68  VAL A C    
631  O  O    A VAL A 68  ? 0.0445 0.0328 0.1509 -0.0076 -0.0093 0.0125  68  VAL A O    
632  O  O    B VAL A 68  ? 0.1331 0.0478 0.1812 0.0048  -0.0030 0.0065  68  VAL A O    
633  C  CB   A VAL A 68  ? 0.0334 0.0367 0.2098 0.0027  0.0109  0.0115  68  VAL A CB   
634  C  CB   B VAL A 68  ? 0.1238 0.0794 0.1811 0.0000  -0.0093 -0.0024 68  VAL A CB   
635  C  CG1  A VAL A 68  ? 0.0409 0.0659 0.1532 -0.0251 -0.0002 -0.0016 68  VAL A CG1  
636  C  CG1  B VAL A 68  ? 0.1146 0.1307 0.1899 0.0461  0.0161  0.0007  68  VAL A CG1  
637  C  CG2  A VAL A 68  ? 0.0825 0.0681 0.1667 -0.0359 0.0174  0.0049  68  VAL A CG2  
638  C  CG2  B VAL A 68  ? 0.1110 0.1140 0.1897 0.0054  0.0054  -0.0040 68  VAL A CG2  
639  N  N    A GLU A 69  ? 0.0433 0.0449 0.1347 -0.0186 -0.0125 0.0091  69  GLU A N    
640  N  N    B GLU A 69  ? 0.1575 0.0487 0.1886 0.0107  -0.0230 -0.0007 69  GLU A N    
641  C  CA   A GLU A 69  ? 0.0301 0.0392 0.1595 -0.0043 -0.0173 -0.0109 69  GLU A CA   
642  C  CA   B GLU A 69  ? 0.1801 0.0709 0.2048 0.0007  -0.0071 0.0087  69  GLU A CA   
643  C  C    A GLU A 69  ? 0.0895 0.0495 0.1315 0.0051  -0.0231 0.0322  69  GLU A C    
644  C  C    B GLU A 69  ? 0.1607 0.0794 0.2139 0.0189  -0.0362 0.0040  69  GLU A C    
645  O  O    A GLU A 69  ? 0.0526 0.0271 0.1586 -0.0063 -0.0142 0.0093  69  GLU A O    
646  O  O    B GLU A 69  ? 0.2608 0.1254 0.2107 0.0443  -0.0219 -0.0253 69  GLU A O    
647  C  CB   A GLU A 69  ? 0.0454 0.0570 0.1561 0.0126  -0.0210 -0.0065 69  GLU A CB   
648  C  CB   B GLU A 69  ? 0.2545 0.1771 0.2522 -0.0074 0.0131  0.0342  69  GLU A CB   
649  C  CG   A GLU A 69  ? 0.0376 0.0491 0.1631 0.0125  0.0344  0.0142  69  GLU A CG   
650  C  CG   B GLU A 69  ? 0.2486 0.2369 0.3063 -0.0035 -0.0227 0.0076  69  GLU A CG   
651  C  CD   A GLU A 69  ? 0.0525 0.0353 0.1647 0.0097  0.0259  0.0366  69  GLU A CD   
652  C  CD   B GLU A 69  ? 0.3258 0.3233 0.3436 0.0236  0.0038  0.0252  69  GLU A CD   
653  O  OE1  A GLU A 69  ? 0.1108 0.0742 0.1647 -0.0452 0.0115  0.0500  69  GLU A OE1  
654  O  OE1  B GLU A 69  ? 0.3427 0.3030 0.3908 0.1032  0.0027  -0.0125 69  GLU A OE1  
655  O  OE2  A GLU A 69  ? 0.0469 0.0535 0.1920 -0.0211 0.0230  0.0098  69  GLU A OE2  
656  O  OE2  B GLU A 69  ? 0.3693 0.3499 0.4082 0.0832  0.1120  0.1027  69  GLU A OE2  
657  N  N    A PHE A 70  ? 0.0612 0.0767 0.1613 0.0057  -0.0005 0.0362  70  PHE A N    
658  N  N    B PHE A 70  ? 0.2060 0.0445 0.2051 0.0017  -0.0043 0.0137  70  PHE A N    
659  C  CA   A PHE A 70  ? 0.0904 0.0537 0.1775 0.0060  -0.0087 0.0366  70  PHE A CA   
660  C  CA   B PHE A 70  ? 0.1834 0.0560 0.1959 -0.0035 -0.0218 0.0132  70  PHE A CA   
661  C  C    A PHE A 70  ? 0.1482 0.0684 0.1597 0.0051  -0.0142 0.0242  70  PHE A C    
662  C  C    B PHE A 70  ? 0.1949 0.0722 0.1721 -0.0031 -0.0126 0.0197  70  PHE A C    
663  O  O    A PHE A 70  ? 0.1230 0.0616 0.1665 0.0010  -0.0019 0.0425  70  PHE A O    
664  O  O    B PHE A 70  ? 0.2292 0.0498 0.1532 -0.0318 -0.0137 0.0518  70  PHE A O    
665  C  CB   A PHE A 70  ? 0.0977 0.0864 0.1507 0.0080  0.0303  -0.0023 70  PHE A CB   
666  C  CB   B PHE A 70  ? 0.1747 0.0654 0.1807 -0.0093 -0.0153 0.0052  70  PHE A CB   
667  C  CG   A PHE A 70  ? 0.0480 0.0415 0.1844 -0.0059 0.0131  0.0438  70  PHE A CG   
668  C  CG   B PHE A 70  ? 0.1465 0.0561 0.2010 0.0046  -0.0564 -0.0126 70  PHE A CG   
669  C  CD1  A PHE A 70  ? 0.0842 0.1142 0.2056 0.0357  -0.0344 0.0449  70  PHE A CD1  
670  C  CD1  B PHE A 70  ? 0.1789 0.0668 0.2008 -0.0240 -0.0412 0.0035  70  PHE A CD1  
671  C  CD2  A PHE A 70  ? 0.0330 0.0588 0.1413 0.0019  0.0298  0.0060  70  PHE A CD2  
672  C  CD2  B PHE A 70  ? 0.1503 0.0478 0.1604 -0.0148 -0.0441 0.0076  70  PHE A CD2  
673  C  CE1  A PHE A 70  ? 0.1031 0.1212 0.2055 -0.0294 -0.0353 0.0295  70  PHE A CE1  
674  C  CE1  B PHE A 70  ? 0.0758 0.0342 0.2023 0.0115  0.0065  -0.0010 70  PHE A CE1  
675  C  CE2  A PHE A 70  ? 0.0907 0.0467 0.1660 0.0167  0.0104  0.0000  70  PHE A CE2  
676  C  CE2  B PHE A 70  ? 0.1228 0.0560 0.1529 -0.0335 -0.0392 0.0219  70  PHE A CE2  
677  C  CZ   A PHE A 70  ? 0.1171 0.1058 0.1729 0.0233  0.0156  0.0020  70  PHE A CZ   
678  C  CZ   B PHE A 70  ? 0.1044 0.0289 0.1756 0.0162  -0.0074 0.0044  70  PHE A CZ   
679  N  N    . ASP A 71  ? 0.2211 0.0570 0.2283 0.0013  -0.0482 0.0031  71  ASP A N    
680  C  CA   . ASP A 71  ? 0.2240 0.0828 0.2549 0.0043  -0.0427 0.0164  71  ASP A CA   
681  C  C    . ASP A 71  ? 0.1848 0.0556 0.2549 0.0230  -0.0040 -0.0126 71  ASP A C    
682  O  O    . ASP A 71  ? 0.2150 0.1579 0.3086 -0.0285 -0.0241 0.0137  71  ASP A O    
683  C  CB   . ASP A 71  ? 0.2752 0.1171 0.2879 0.0665  -0.0684 -0.0020 71  ASP A CB   
684  C  CG   . ASP A 71  ? 0.2799 0.1570 0.3896 0.0137  -0.0838 0.0147  71  ASP A CG   
685  O  OD1  . ASP A 71  ? 0.2957 0.0738 0.3558 0.0544  -0.0331 0.0355  71  ASP A OD1  
686  O  OD2  . ASP A 71  ? 0.3603 0.2017 0.5802 0.0286  -0.1032 0.0307  71  ASP A OD2  
687  N  N    . ASP A 72  ? 0.2030 0.0348 0.2418 0.0020  -0.0035 0.0196  72  ASP A N    
688  C  CA   . ASP A 72  ? 0.1914 0.0334 0.2498 -0.0355 -0.0171 -0.0059 72  ASP A CA   
689  C  C    . ASP A 72  ? 0.2371 0.0433 0.2687 -0.0015 0.0182  -0.0147 72  ASP A C    
690  O  O    . ASP A 72  ? 0.2285 0.0684 0.2921 -0.0164 0.0252  -0.0362 72  ASP A O    
691  C  CB   . ASP A 72  ? 0.1581 0.0704 0.2596 -0.0482 -0.0031 -0.0135 72  ASP A CB   
692  C  CG   . ASP A 72  ? 0.1805 0.0538 0.2218 -0.0297 -0.0205 -0.0164 72  ASP A CG   
693  O  OD1  . ASP A 72  ? 0.1954 0.1394 0.2426 -0.0322 -0.0329 0.0261  72  ASP A OD1  
694  O  OD2  . ASP A 72  ? 0.1739 0.1225 0.2172 -0.0132 -0.0388 0.0087  72  ASP A OD2  
695  N  N    . SER A 73  ? 0.2299 0.0421 0.2978 -0.0192 0.0269  -0.0005 73  SER A N    
696  C  CA   . SER A 73  ? 0.2531 0.0736 0.2890 0.0173  0.0273  -0.0071 73  SER A CA   
697  C  C    . SER A 73  ? 0.2301 0.0781 0.2969 0.0146  0.0428  -0.0057 73  SER A C    
698  O  O    . SER A 73  ? 0.2544 0.0556 0.3285 -0.0035 0.0052  -0.0070 73  SER A O    
699  C  CB   . SER A 73  ? 0.3039 0.1088 0.3204 -0.0255 0.0417  0.0297  73  SER A CB   
700  O  OG   . SER A 73  ? 0.3984 0.0905 0.3465 0.0465  0.0331  0.0276  73  SER A OG   
701  N  N    . GLN A 74  ? 0.2218 0.1042 0.3571 0.0115  0.0375  -0.0142 74  GLN A N    
702  C  CA   . GLN A 74  ? 0.2569 0.1737 0.3346 -0.0065 0.0285  0.0137  74  GLN A CA   
703  C  C    . GLN A 74  ? 0.2628 0.1981 0.2976 -0.0060 0.0148  -0.0326 74  GLN A C    
704  O  O    . GLN A 74  ? 0.1924 0.1164 0.3003 -0.0504 -0.0270 0.0242  74  GLN A O    
705  C  CB   . GLN A 74  ? 0.2621 0.1862 0.3546 0.0232  0.0115  0.0331  74  GLN A CB   
706  C  CG   . GLN A 74  ? 0.3855 0.2394 0.4228 -0.0428 0.0238  0.0617  74  GLN A CG   
707  C  CD   . GLN A 74  ? 0.4350 0.3070 0.4670 -0.0399 -0.0077 -0.0052 74  GLN A CD   
708  O  OE1  . GLN A 74  ? 0.3630 0.3716 0.5849 0.0450  -0.0412 0.0560  74  GLN A OE1  
709  N  NE2  . GLN A 74  ? 0.3837 0.4045 0.5062 -0.0942 -0.0142 0.0652  74  GLN A NE2  
710  N  N    . ASP A 75  ? 0.2308 0.2195 0.2967 -0.0115 0.0152  -0.0351 75  ASP A N    
711  C  CA   . ASP A 75  ? 0.2242 0.1649 0.3231 0.0030  -0.0031 -0.0178 75  ASP A CA   
712  C  C    . ASP A 75  ? 0.1880 0.1999 0.3289 0.0416  -0.0049 -0.0436 75  ASP A C    
713  O  O    . ASP A 75  ? 0.2362 0.2915 0.4034 -0.0171 0.0093  -0.0099 75  ASP A O    
714  C  CB   . ASP A 75  ? 0.1969 0.1893 0.3007 0.0049  0.0197  -0.0155 75  ASP A CB   
715  C  CG   . ASP A 75  ? 0.4265 0.2827 0.3806 0.0276  0.0318  0.0571  75  ASP A CG   
716  O  OD1  . ASP A 75  ? 0.2073 0.2204 0.4379 0.0049  -0.0432 0.0688  75  ASP A OD1  
717  O  OD2  . ASP A 75  ? 0.4081 0.4551 0.4864 0.0262  0.0373  -0.0006 75  ASP A OD2  
718  N  N    . LYS A 76  ? 0.2138 0.1604 0.2779 0.0070  -0.0156 0.0076  76  LYS A N    
719  C  CA   . LYS A 76  ? 0.2698 0.1563 0.3445 0.0447  -0.0247 -0.0005 76  LYS A CA   
720  C  C    . LYS A 76  ? 0.2306 0.2152 0.3325 0.0264  -0.0483 0.0153  76  LYS A C    
721  O  O    . LYS A 76  ? 0.2265 0.2461 0.3977 0.0948  -0.0141 -0.0110 76  LYS A O    
722  C  CB   . LYS A 76  ? 0.2628 0.1543 0.3106 -0.0109 -0.0513 0.0041  76  LYS A CB   
723  C  CG   . LYS A 76  ? 0.4089 0.1890 0.3801 0.0120  0.0000  0.0231  76  LYS A CG   
724  C  CD   . LYS A 76  ? 0.5228 0.2409 0.3616 -0.0443 -0.0148 -0.0027 76  LYS A CD   
725  C  CE   . LYS A 76  ? 0.5070 0.2890 0.4233 -0.0184 0.0131  0.0281  76  LYS A CE   
726  N  NZ   . LYS A 76  ? 0.4685 0.2921 0.3934 -0.0077 -0.0241 0.0247  76  LYS A NZ   
727  N  N    . ALA A 77  ? 0.2348 0.1970 0.3434 0.0142  -0.0392 -0.0243 77  ALA A N    
728  C  CA   . ALA A 77  ? 0.1719 0.1875 0.2657 0.0146  -0.0745 -0.0035 77  ALA A CA   
729  C  C    . ALA A 77  ? 0.1273 0.1879 0.2387 0.0006  -0.0571 -0.0333 77  ALA A C    
730  O  O    . ALA A 77  ? 0.1465 0.2632 0.3014 -0.0023 -0.0362 -0.0627 77  ALA A O    
731  C  CB   . ALA A 77  ? 0.2497 0.1290 0.2639 0.0159  -0.0274 -0.0307 77  ALA A CB   
732  N  N    . VAL A 78  ? 0.1475 0.1171 0.2394 0.0003  -0.0447 0.0148  78  VAL A N    
733  C  CA   . VAL A 78  ? 0.1717 0.1171 0.2576 0.0232  -0.0274 0.0126  78  VAL A CA   
734  C  C    . VAL A 78  ? 0.1186 0.1065 0.2353 0.0087  -0.0298 0.0171  78  VAL A C    
735  O  O    . VAL A 78  ? 0.0772 0.1119 0.2937 -0.0140 -0.0252 0.0126  78  VAL A O    
736  C  CB   . VAL A 78  ? 0.3143 0.1854 0.3388 0.0452  -0.0207 0.0103  78  VAL A CB   
737  C  CG1  . VAL A 78  ? 0.3208 0.0816 0.3695 -0.0174 -0.0194 0.0183  78  VAL A CG1  
738  C  CG2  . VAL A 78  ? 0.2612 0.1694 0.3488 -0.0159 0.0294  0.0375  78  VAL A CG2  
739  N  N    . LEU A 79  ? 0.1070 0.0515 0.2579 0.0006  -0.0176 0.0189  79  LEU A N    
740  C  CA   . LEU A 79  ? 0.0871 0.1263 0.2116 -0.0035 0.0068  0.0046  79  LEU A CA   
741  C  C    . LEU A 79  ? 0.0709 0.1061 0.2206 -0.0052 0.0142  -0.0096 79  LEU A C    
742  O  O    . LEU A 79  ? 0.0778 0.1083 0.2632 -0.0161 -0.0013 -0.0147 79  LEU A O    
743  C  CB   . LEU A 79  ? 0.0625 0.1270 0.2640 -0.0012 -0.0017 0.0401  79  LEU A CB   
744  C  CG   . LEU A 79  ? 0.1076 0.0916 0.2286 0.0295  0.0052  0.0003  79  LEU A CG   
745  C  CD1  . LEU A 79  ? 0.0930 0.1097 0.3583 -0.0240 -0.0077 0.0531  79  LEU A CD1  
746  C  CD2  . LEU A 79  ? 0.0625 0.1604 0.2171 0.0215  0.0143  0.0115  79  LEU A CD2  
747  N  N    . LYS A 80  ? 0.1040 0.1128 0.2100 0.0006  0.0137  -0.0096 80  LYS A N    
748  C  CA   . LYS A 80  ? 0.1011 0.1031 0.2398 0.0043  0.0034  -0.0077 80  LYS A CA   
749  C  C    . LYS A 80  ? 0.0882 0.1225 0.2511 0.0271  0.0238  -0.0210 80  LYS A C    
750  O  O    . LYS A 80  ? 0.0851 0.1243 0.2727 -0.0505 0.0057  -0.0023 80  LYS A O    
751  C  CB   . LYS A 80  ? 0.1467 0.1437 0.2770 0.0071  0.0214  -0.0012 80  LYS A CB   
752  C  CG   . LYS A 80  ? 0.1338 0.1514 0.3454 0.0403  0.0318  0.0015  80  LYS A CG   
753  C  CD   . LYS A 80  ? 0.1604 0.1945 0.3553 0.0675  -0.0143 0.0281  80  LYS A CD   
754  C  CE   . LYS A 80  ? 0.2130 0.2702 0.4024 0.0225  -0.0276 -0.0333 80  LYS A CE   
755  N  NZ   . LYS A 80  ? 0.4235 0.4533 0.4415 -0.0005 -0.0493 -0.0507 80  LYS A NZ   
756  N  N    . GLY A 81  ? 0.1009 0.1306 0.2459 0.0294  0.0322  -0.0010 81  GLY A N    
757  C  CA   . GLY A 81  ? 0.1225 0.1198 0.2727 0.0483  0.0670  0.0199  81  GLY A CA   
758  C  C    . GLY A 81  ? 0.1367 0.0973 0.2700 0.0295  0.0697  0.0175  81  GLY A C    
759  O  O    . GLY A 81  ? 0.1058 0.1159 0.2675 -0.0252 0.0195  -0.0026 81  GLY A O    
760  N  N    . GLY A 82  ? 0.1133 0.1232 0.3125 -0.0031 0.0114  0.0240  82  GLY A N    
761  C  CA   . GLY A 82  ? 0.1168 0.1079 0.3163 -0.0038 0.0263  0.0333  82  GLY A CA   
762  C  C    . GLY A 82  ? 0.1279 0.1439 0.2946 0.0564  0.0087  -0.0007 82  GLY A C    
763  O  O    . GLY A 82  ? 0.2242 0.2267 0.3095 0.0789  0.0843  -0.0104 82  GLY A O    
764  N  N    . PRO A 83  ? 0.1140 0.1164 0.2899 0.0326  0.0195  0.0288  83  PRO A N    
765  C  CA   . PRO A 83  ? 0.1247 0.0900 0.2671 0.0251  0.0096  0.0107  83  PRO A CA   
766  C  C    . PRO A 83  ? 0.1110 0.1532 0.2870 0.0141  0.0353  -0.0013 83  PRO A C    
767  O  O    . PRO A 83  ? 0.1274 0.1507 0.3129 0.0307  -0.0121 0.0109  83  PRO A O    
768  C  CB   . PRO A 83  ? 0.1272 0.1274 0.2678 0.0417  0.0266  0.0104  83  PRO A CB   
769  C  CG   . PRO A 83  ? 0.0997 0.1126 0.2308 0.0286  0.0141  -0.0027 83  PRO A CG   
770  C  CD   . PRO A 83  ? 0.1013 0.1027 0.2576 -0.0221 0.0710  -0.0030 83  PRO A CD   
771  N  N    . LEU A 84  ? 0.1119 0.0997 0.2486 0.0070  0.0295  0.0049  84  LEU A N    
772  C  CA   . LEU A 84  ? 0.1592 0.0618 0.2477 0.0342  0.0241  -0.0218 84  LEU A CA   
773  C  C    . LEU A 84  ? 0.1484 0.1171 0.2831 0.0291  -0.0006 -0.0219 84  LEU A C    
774  O  O    . LEU A 84  ? 0.1288 0.1358 0.2926 0.0266  0.0465  -0.0434 84  LEU A O    
775  C  CB   . LEU A 84  ? 0.1029 0.0812 0.2382 0.0399  0.0270  -0.0051 84  LEU A CB   
776  C  CG   . LEU A 84  ? 0.0824 0.0527 0.2434 0.0174  0.0137  -0.0238 84  LEU A CG   
777  C  CD1  . LEU A 84  ? 0.0449 0.1151 0.2788 0.0229  0.0020  -0.0043 84  LEU A CD1  
778  C  CD2  . LEU A 84  ? 0.0772 0.0609 0.2346 0.0244  0.0020  -0.0178 84  LEU A CD2  
779  N  N    . ASP A 85  ? 0.2041 0.0745 0.2675 0.0006  0.0060  -0.0500 85  ASP A N    
780  C  CA   . ASP A 85  ? 0.2605 0.1306 0.2863 0.0043  0.0108  -0.0342 85  ASP A CA   
781  C  C    . ASP A 85  ? 0.1683 0.0957 0.3328 -0.0148 0.0182  0.0097  85  ASP A C    
782  O  O    . ASP A 85  ? 0.2890 0.1615 0.3546 0.0178  0.0636  -0.0274 85  ASP A O    
783  C  CB   . ASP A 85  ? 0.3352 0.0889 0.2899 0.0333  0.0048  -0.0320 85  ASP A CB   
784  C  CG   . ASP A 85  ? 0.2824 0.2633 0.3761 -0.0252 0.0571  -0.0006 85  ASP A CG   
785  O  OD1  . ASP A 85  ? 0.2294 0.4185 0.3711 -0.0702 0.0952  0.0082  85  ASP A OD1  
786  O  OD2  . ASP A 85  ? 0.4002 0.3828 0.4659 0.0366  -0.0307 -0.0656 85  ASP A OD2  
787  N  N    . GLY A 86  ? 0.2134 0.1676 0.3801 -0.0305 0.0182  0.0231  86  GLY A N    
788  C  CA   . GLY A 86  ? 0.2445 0.2188 0.2676 -0.0430 0.0114  -0.0043 86  GLY A CA   
789  C  C    . GLY A 86  ? 0.2526 0.1546 0.2899 -0.0478 -0.0062 0.0046  86  GLY A C    
790  O  O    . GLY A 86  ? 0.2885 0.2416 0.3106 -0.1349 -0.0204 0.0207  86  GLY A O    
791  N  N    . THR A 87  ? 0.1376 0.1608 0.2565 0.0074  0.0303  -0.0198 87  THR A N    
792  C  CA   . THR A 87  ? 0.0952 0.1300 0.2770 0.0381  0.0342  -0.0163 87  THR A CA   
793  C  C    . THR A 87  ? 0.0645 0.1067 0.2486 0.0060  0.0228  -0.0339 87  THR A C    
794  O  O    . THR A 87  ? 0.0817 0.0557 0.2885 0.0087  0.0118  -0.0148 87  THR A O    
795  C  CB   . THR A 87  ? 0.1151 0.1920 0.3050 -0.0038 0.0178  -0.0074 87  THR A CB   
796  O  OG1  . THR A 87  ? 0.1992 0.1730 0.2928 0.0041  0.0329  0.0104  87  THR A OG1  
797  C  CG2  . THR A 87  ? 0.1423 0.1852 0.3030 0.0351  0.0485  -0.0746 87  THR A CG2  
798  N  N    . TYR A 88  ? 0.0582 0.0760 0.2448 0.0340  0.0071  -0.0423 88  TYR A N    
799  C  CA   . TYR A 88  ? 0.0376 0.0636 0.2208 0.0187  0.0126  -0.0212 88  TYR A CA   
800  C  C    . TYR A 88  ? 0.0571 0.0449 0.2213 0.0244  -0.0076 -0.0088 88  TYR A C    
801  O  O    . TYR A 88  ? 0.0945 0.1033 0.2840 -0.0362 -0.0182 0.0390  88  TYR A O    
802  C  CB   . TYR A 88  ? 0.0736 0.0372 0.2260 0.0225  -0.0088 -0.0184 88  TYR A CB   
803  C  CG   . TYR A 88  ? 0.1085 0.0450 0.1908 0.0261  -0.0137 0.0073  88  TYR A CG   
804  C  CD1  . TYR A 88  ? 0.0846 0.0679 0.1899 0.0142  -0.0151 0.0153  88  TYR A CD1  
805  C  CD2  . TYR A 88  ? 0.0709 0.0371 0.1859 0.0196  -0.0209 0.0133  88  TYR A CD2  
806  C  CE1  . TYR A 88  ? 0.0776 0.0709 0.1965 0.0410  -0.0164 0.0087  88  TYR A CE1  
807  C  CE2  . TYR A 88  ? 0.0654 0.0273 0.1757 0.0074  0.0208  -0.0049 88  TYR A CE2  
808  C  CZ   . TYR A 88  ? 0.0942 0.0313 0.1918 0.0195  -0.0046 -0.0098 88  TYR A CZ   
809  O  OH   . TYR A 88  ? 0.0566 0.0390 0.2204 0.0164  0.0049  -0.0054 88  TYR A OH   
810  N  N    . ARG A 89  ? 0.1004 0.0670 0.1999 0.0527  -0.0063 -0.0186 89  ARG A N    
811  C  CA   . ARG A 89  ? 0.1369 0.0276 0.1974 0.0141  -0.0209 0.0071  89  ARG A CA   
812  C  C    . ARG A 89  ? 0.0889 0.0502 0.1618 0.0324  -0.0098 0.0096  89  ARG A C    
813  O  O    . ARG A 89  ? 0.0663 0.0521 0.1996 0.0052  -0.0219 0.0216  89  ARG A O    
814  C  CB   . ARG A 89  ? 0.1747 0.0873 0.2227 -0.0178 -0.0383 0.0093  89  ARG A CB   
815  C  CG   . ARG A 89  ? 0.1924 0.1040 0.2337 -0.0353 -0.0423 0.0421  89  ARG A CG   
816  C  CD   . ARG A 89  ? 0.2084 0.1031 0.2676 0.0568  0.0229  0.0082  89  ARG A CD   
817  N  NE   . ARG A 89  ? 0.2256 0.1216 0.2171 0.0671  -0.0024 0.0364  89  ARG A NE   
818  C  CZ   . ARG A 89  ? 0.1740 0.0794 0.2743 -0.0048 0.0306  0.0240  89  ARG A CZ   
819  N  NH1  . ARG A 89  ? 0.1737 0.1483 0.2793 0.0588  0.0373  0.0229  89  ARG A NH1  
820  N  NH2  . ARG A 89  ? 0.1550 0.1234 0.2870 0.0281  0.0272  0.0109  89  ARG A NH2  
821  N  N    . LEU A 90  ? 0.0864 0.0492 0.1793 -0.0017 -0.0187 -0.0087 90  LEU A N    
822  C  CA   . LEU A 90  ? 0.1067 0.0455 0.2053 -0.0153 -0.0003 0.0165  90  LEU A CA   
823  C  C    . LEU A 90  ? 0.0948 0.0270 0.2014 0.0054  -0.0055 0.0142  90  LEU A C    
824  O  O    . LEU A 90  ? 0.1234 0.0622 0.2091 0.0020  -0.0160 0.0395  90  LEU A O    
825  C  CB   . LEU A 90  ? 0.0913 0.0615 0.1965 -0.0329 0.0052  -0.0142 90  LEU A CB   
826  C  CG   . LEU A 90  ? 0.1153 0.0711 0.1769 -0.0164 -0.0006 -0.0077 90  LEU A CG   
827  C  CD1  . LEU A 90  ? 0.1221 0.0772 0.2127 -0.0109 -0.0491 -0.0052 90  LEU A CD1  
828  C  CD2  . LEU A 90  ? 0.1216 0.0992 0.2200 -0.0151 -0.0551 -0.0253 90  LEU A CD2  
829  N  N    . ILE A 91  ? 0.0887 0.0314 0.2024 -0.0013 0.0174  -0.0164 91  ILE A N    
830  C  CA   . ILE A 91  ? 0.1377 0.0794 0.1866 -0.0120 0.0208  -0.0005 91  ILE A CA   
831  C  C    . ILE A 91  ? 0.1164 0.0571 0.1841 -0.0060 0.0043  0.0098  91  ILE A C    
832  O  O    . ILE A 91  ? 0.1331 0.0480 0.1771 -0.0342 -0.0170 0.0164  91  ILE A O    
833  C  CB   . ILE A 91  ? 0.1374 0.0825 0.2039 -0.0390 0.0031  -0.0046 91  ILE A CB   
834  C  CG1  . ILE A 91  ? 0.1546 0.0799 0.2145 -0.0627 0.0568  0.0065  91  ILE A CG1  
835  C  CG2  . ILE A 91  ? 0.1500 0.0521 0.1981 0.0035  0.0120  -0.0030 91  ILE A CG2  
836  C  CD1  . ILE A 91  ? 0.1798 0.1058 0.2344 -0.0785 0.0241  -0.0046 91  ILE A CD1  
837  N  N    . GLN A 92  ? 0.1383 0.0349 0.1676 -0.0031 -0.0189 0.0114  92  GLN A N    
838  C  CA   . GLN A 92  ? 0.1438 0.0295 0.1922 -0.0060 0.0064  0.0250  92  GLN A CA   
839  C  C    . GLN A 92  ? 0.1482 0.0293 0.1805 0.0087  -0.0024 0.0068  92  GLN A C    
840  O  O    . GLN A 92  ? 0.1678 0.0253 0.1497 -0.0006 -0.0111 0.0000  92  GLN A O    
841  C  CB   . GLN A 92  ? 0.1613 0.0574 0.1893 -0.0068 -0.0207 0.0221  92  GLN A CB   
842  C  CG   . GLN A 92  ? 0.1080 0.0256 0.2286 0.0044  -0.0195 0.0024  92  GLN A CG   
843  C  CD   . GLN A 92  ? 0.1316 0.0661 0.1721 0.0177  0.0244  0.0074  92  GLN A CD   
844  O  OE1  . GLN A 92  ? 0.1739 0.0334 0.1978 -0.0015 -0.0166 0.0153  92  GLN A OE1  
845  N  NE2  . GLN A 92  ? 0.1351 0.0577 0.2433 0.0059  0.0230  -0.0074 92  GLN A NE2  
846  N  N    . PHE A 93  ? 0.1854 0.0267 0.1548 0.0116  -0.0335 0.0055  93  PHE A N    
847  C  CA   . PHE A 93  ? 0.1381 0.0256 0.1662 0.0000  -0.0075 -0.0067 93  PHE A CA   
848  C  C    . PHE A 93  ? 0.1088 0.0460 0.1511 -0.0174 0.0000  0.0060  93  PHE A C    
849  O  O    . PHE A 93  ? 0.1974 0.0261 0.1546 -0.0098 -0.0162 -0.0010 93  PHE A O    
850  C  CB   . PHE A 93  ? 0.1410 0.0308 0.1807 -0.0173 -0.0577 -0.0063 93  PHE A CB   
851  C  CG   . PHE A 93  ? 0.1884 0.0293 0.1931 -0.0003 -0.0511 0.0020  93  PHE A CG   
852  C  CD1  . PHE A 93  ? 0.1836 0.0272 0.1990 -0.0171 -0.0390 0.0007  93  PHE A CD1  
853  C  CD2  . PHE A 93  ? 0.1471 0.0763 0.2010 0.0164  -0.0608 0.0417  93  PHE A CD2  
854  C  CE1  . PHE A 93  ? 0.1857 0.0749 0.1888 0.0331  -0.0494 -0.0340 93  PHE A CE1  
855  C  CE2  . PHE A 93  ? 0.2056 0.0575 0.2089 0.0577  -0.0621 -0.0203 93  PHE A CE2  
856  C  CZ   . PHE A 93  ? 0.1992 0.0702 0.1963 -0.0027 -0.0599 -0.0097 93  PHE A CZ   
857  N  N    . HIS A 94  ? 0.1419 0.0379 0.1721 -0.0140 -0.0329 -0.0068 94  HIS A N    
858  C  CA   . HIS A 94  ? 0.1178 0.0307 0.1503 -0.0120 -0.0115 0.0156  94  HIS A CA   
859  C  C    . HIS A 94  ? 0.1022 0.0274 0.1478 -0.0063 -0.0054 -0.0136 94  HIS A C    
860  O  O    . HIS A 94  ? 0.0995 0.0291 0.1487 -0.0165 -0.0140 -0.0010 94  HIS A O    
861  C  CB   . HIS A 94  ? 0.1272 0.0349 0.1566 -0.0171 0.0000  0.0141  94  HIS A CB   
862  C  CG   . HIS A 94  ? 0.1500 0.0377 0.1309 -0.0377 -0.0159 0.0152  94  HIS A CG   
863  N  ND1  . HIS A 94  ? 0.1056 0.0368 0.1446 -0.0303 -0.0099 0.0007  94  HIS A ND1  
864  C  CD2  . HIS A 94  ? 0.1250 0.0500 0.1435 -0.0170 0.0454  0.0174  94  HIS A CD2  
865  C  CE1  . HIS A 94  ? 0.0835 0.0306 0.1651 -0.0136 -0.0032 0.0175  94  HIS A CE1  
866  N  NE2  . HIS A 94  ? 0.0790 0.0767 0.1094 -0.0524 -0.0215 0.0230  94  HIS A NE2  
867  N  N    . PHE A 95  ? 0.1102 0.0262 0.1780 -0.0066 -0.0071 0.0076  95  PHE A N    
868  C  CA   . PHE A 95  ? 0.1232 0.0326 0.1699 -0.0209 0.0046  0.0192  95  PHE A CA   
869  C  C    . PHE A 95  ? 0.1076 0.0474 0.1464 -0.0131 0.0041  0.0015  95  PHE A C    
870  O  O    . PHE A 95  ? 0.0873 0.0298 0.1823 -0.0043 0.0196  0.0156  95  PHE A O    
871  C  CB   . PHE A 95  ? 0.1272 0.0357 0.1544 -0.0271 -0.0098 -0.0174 95  PHE A CB   
872  C  CG   . PHE A 95  ? 0.1189 0.0370 0.1456 -0.0322 -0.0181 -0.0023 95  PHE A CG   
873  C  CD1  . PHE A 95  ? 0.0982 0.0598 0.1568 -0.0384 -0.0006 -0.0296 95  PHE A CD1  
874  C  CD2  . PHE A 95  ? 0.1076 0.0672 0.1694 -0.0463 -0.0447 -0.0099 95  PHE A CD2  
875  C  CE1  . PHE A 95  ? 0.0939 0.0582 0.1640 -0.0010 -0.0062 -0.0057 95  PHE A CE1  
876  C  CE2  . PHE A 95  ? 0.1140 0.0505 0.1665 -0.0282 -0.0262 -0.0307 95  PHE A CE2  
877  C  CZ   . PHE A 95  ? 0.1052 0.0630 0.1733 -0.0287 -0.0120 -0.0162 95  PHE A CZ   
878  N  N    . HIS A 96  ? 0.0716 0.0276 0.1568 -0.0063 0.0057  0.0130  96  HIS A N    
879  C  CA   . HIS A 96  ? 0.0650 0.0253 0.1730 -0.0007 0.0088  -0.0005 96  HIS A CA   
880  C  C    . HIS A 96  ? 0.0505 0.0345 0.1571 -0.0142 0.0165  0.0031  96  HIS A C    
881  O  O    . HIS A 96  ? 0.0661 0.0253 0.1805 0.0000  0.0213  0.0000  96  HIS A O    
882  C  CB   . HIS A 96  ? 0.0846 0.0255 0.1626 -0.0009 -0.0034 -0.0045 96  HIS A CB   
883  C  CG   . HIS A 96  ? 0.0555 0.0334 0.1437 -0.0153 0.0087  0.0006  96  HIS A CG   
884  N  ND1  . HIS A 96  ? 0.0605 0.0498 0.1992 -0.0275 0.0236  0.0017  96  HIS A ND1  
885  C  CD2  . HIS A 96  ? 0.0599 0.0392 0.1747 0.0208  -0.0059 0.0100  96  HIS A CD2  
886  C  CE1  . HIS A 96  ? 0.0870 0.0298 0.1722 -0.0038 -0.0476 0.0245  96  HIS A CE1  
887  N  NE2  . HIS A 96  ? 0.0682 0.0377 0.1966 0.0226  -0.0133 -0.0152 96  HIS A NE2  
888  N  N    . TRP A 97  ? 0.0621 0.0282 0.1703 -0.0012 0.0082  0.0041  97  TRP A N    
889  C  CA   . TRP A 97  ? 0.0693 0.0270 0.1579 0.0052  0.0115  -0.0103 97  TRP A CA   
890  C  C    . TRP A 97  ? 0.0641 0.0388 0.1456 -0.0183 0.0109  -0.0164 97  TRP A C    
891  O  O    . TRP A 97  ? 0.0846 0.0437 0.1866 -0.0285 0.0274  -0.0176 97  TRP A O    
892  C  CB   . TRP A 97  ? 0.1254 0.0343 0.1553 -0.0215 0.0200  -0.0010 97  TRP A CB   
893  C  CG   . TRP A 97  ? 0.1270 0.0361 0.1268 -0.0236 0.0109  -0.0005 97  TRP A CG   
894  C  CD1  . TRP A 97  ? 0.1412 0.0763 0.1473 -0.0038 0.0093  0.0012  97  TRP A CD1  
895  C  CD2  . TRP A 97  ? 0.1439 0.0350 0.1379 -0.0255 0.0006  -0.0109 97  TRP A CD2  
896  N  NE1  . TRP A 97  ? 0.1800 0.0566 0.1509 0.0254  0.0221  -0.0120 97  TRP A NE1  
897  C  CE2  . TRP A 97  ? 0.1394 0.0358 0.1480 -0.0342 0.0379  -0.0080 97  TRP A CE2  
898  C  CE3  . TRP A 97  ? 0.0837 0.0366 0.1514 -0.0164 -0.0219 -0.0214 97  TRP A CE3  
899  C  CZ2  . TRP A 97  ? 0.1494 0.0542 0.1761 -0.0567 0.0371  0.0031  97  TRP A CZ2  
900  C  CZ3  . TRP A 97  ? 0.1097 0.0605 0.1771 -0.0287 0.0156  0.0167  97  TRP A CZ3  
901  C  CH2  . TRP A 97  ? 0.1581 0.0528 0.1836 -0.0214 0.0162  0.0037  97  TRP A CH2  
902  N  N    . GLY A 98  ? 0.1062 0.0266 0.1615 -0.0086 0.0054  0.0067  98  GLY A N    
903  C  CA   . GLY A 98  ? 0.1256 0.0350 0.1586 0.0164  0.0048  -0.0043 98  GLY A CA   
904  C  C    . GLY A 98  ? 0.0941 0.0333 0.1836 -0.0188 0.0013  0.0023  98  GLY A C    
905  O  O    . GLY A 98  ? 0.1092 0.0370 0.1920 0.0086  -0.0063 -0.0115 98  GLY A O    
906  N  N    . SER A 99  ? 0.0988 0.0456 0.2019 0.0143  0.0285  -0.0317 99  SER A N    
907  C  CA   . SER A 99  ? 0.0983 0.0478 0.2055 -0.0244 0.0513  -0.0082 99  SER A CA   
908  C  C    . SER A 99  ? 0.1169 0.0803 0.1905 0.0031  0.0467  -0.0207 99  SER A C    
909  O  O    . SER A 99  ? 0.1507 0.0871 0.2128 -0.0207 0.0291  -0.0148 99  SER A O    
910  C  CB   . SER A 99  ? 0.1368 0.0643 0.2056 0.0348  0.0299  -0.0225 99  SER A CB   
911  O  OG   . SER A 99  ? 0.1119 0.0557 0.2495 0.0063  0.0348  -0.0375 99  SER A OG   
912  N  N    . LEU A 100 ? 0.0948 0.0437 0.2116 -0.0132 0.0340  -0.0068 100 LEU A N    
913  C  CA   . LEU A 100 ? 0.0904 0.0259 0.2673 -0.0053 0.0513  -0.0093 100 LEU A CA   
914  C  C    . LEU A 100 ? 0.0654 0.0486 0.2348 -0.0098 0.0177  -0.0087 100 LEU A C    
915  O  O    . LEU A 100 ? 0.1254 0.0394 0.2403 -0.0178 0.0230  -0.0104 100 LEU A O    
916  C  CB   . LEU A 100 ? 0.1024 0.1151 0.2976 -0.0093 0.0445  0.0353  100 LEU A CB   
917  C  CG   . LEU A 100 ? 0.1597 0.1633 0.3027 0.0397  0.0198  0.0070  100 LEU A CG   
918  C  CD1  . LEU A 100 ? 0.1606 0.2795 0.3689 0.0522  0.0313  -0.0049 100 LEU A CD1  
919  C  CD2  . LEU A 100 ? 0.2861 0.2813 0.2890 -0.0114 0.0575  -0.0741 100 LEU A CD2  
920  N  N    . ASP A 101 ? 0.0456 0.0499 0.2473 -0.0098 0.0108  -0.0131 101 ASP A N    
921  C  CA   . ASP A 101 ? 0.0821 0.0652 0.2254 -0.0441 0.0161  0.0198  101 ASP A CA   
922  C  C    . ASP A 101 ? 0.1059 0.0324 0.2272 -0.0236 0.0051  0.0038  101 ASP A C    
923  O  O    . ASP A 101 ? 0.1644 0.0573 0.2357 0.0092  0.0395  0.0198  101 ASP A O    
924  C  CB   . ASP A 101 ? 0.1032 0.0614 0.2386 -0.0466 0.0124  0.0338  101 ASP A CB   
925  C  CG   . ASP A 101 ? 0.1739 0.0561 0.2475 0.0109  0.0103  -0.0170 101 ASP A CG   
926  O  OD1  . ASP A 101 ? 0.2170 0.0851 0.2166 -0.0129 0.0296  0.0175  101 ASP A OD1  
927  O  OD2  . ASP A 101 ? 0.2563 0.1509 0.3030 -0.1412 -0.0544 0.0136  101 ASP A OD2  
928  N  N    . GLY A 102 ? 0.0945 0.0468 0.2408 -0.0307 0.0046  0.0176  102 GLY A N    
929  C  CA   . GLY A 102 ? 0.0837 0.0411 0.2132 -0.0252 0.0054  0.0186  102 GLY A CA   
930  C  C    . GLY A 102 ? 0.1010 0.0529 0.2204 0.0097  0.0131  0.0153  102 GLY A C    
931  O  O    . GLY A 102 ? 0.1155 0.0485 0.1978 -0.0175 0.0130  0.0229  102 GLY A O    
932  N  N    A GLN A 103 ? 0.1014 0.0334 0.2101 0.0193  -0.0055 0.0227  103 GLN A N    
933  N  N    B GLN A 103 ? 0.0923 0.0282 0.2082 -0.0114 0.0167  0.0098  103 GLN A N    
934  C  CA   A GLN A 103 ? 0.0882 0.0375 0.1654 0.0181  -0.0193 0.0142  103 GLN A CA   
935  C  CA   B GLN A 103 ? 0.0670 0.0336 0.1905 -0.0186 -0.0076 0.0044  103 GLN A CA   
936  C  C    A GLN A 103 ? 0.0625 0.0289 0.1432 0.0092  0.0100  0.0146  103 GLN A C    
937  C  C    B GLN A 103 ? 0.0871 0.0480 0.1791 -0.0204 0.0165  0.0000  103 GLN A C    
938  O  O    A GLN A 103 ? 0.0943 0.0258 0.1674 -0.0019 -0.0207 -0.0070 103 GLN A O    
939  O  O    B GLN A 103 ? 0.0368 0.0348 0.1895 -0.0104 0.0116  -0.0098 103 GLN A O    
940  C  CB   A GLN A 103 ? 0.1239 0.0271 0.1586 -0.0046 -0.0013 0.0038  103 GLN A CB   
941  C  CB   B GLN A 103 ? 0.1130 0.0718 0.1660 -0.0024 0.0034  0.0120  103 GLN A CB   
942  C  CG   A GLN A 103 ? 0.0801 0.0886 0.1388 0.0588  0.0081  0.0120  103 GLN A CG   
943  C  CG   B GLN A 103 ? 0.0769 0.0658 0.1873 -0.0006 0.0159  -0.0292 103 GLN A CG   
944  C  CD   A GLN A 103 ? 0.1281 0.0281 0.1681 0.0141  -0.0100 -0.0121 103 GLN A CD   
945  C  CD   B GLN A 103 ? 0.1369 0.0670 0.1710 0.0173  0.0074  -0.0342 103 GLN A CD   
946  O  OE1  A GLN A 103 ? 0.1178 0.0697 0.1746 0.0635  0.0121  0.0179  103 GLN A OE1  
947  O  OE1  B GLN A 103 ? 0.1191 0.1862 0.2319 0.0535  0.0159  0.0254  103 GLN A OE1  
948  N  NE2  A GLN A 103 ? 0.0639 0.1074 0.2303 0.0549  0.0000  -0.0265 103 GLN A NE2  
949  N  NE2  B GLN A 103 ? 0.0988 0.0706 0.1981 -0.0283 0.0057  -0.0109 103 GLN A NE2  
950  N  N    A GLY A 104 ? 0.0885 0.0309 0.1483 0.0183  0.0082  0.0087  104 GLY A N    
951  N  N    B GLY A 104 ? 0.0414 0.0271 0.1789 -0.0005 0.0054  -0.0165 104 GLY A N    
952  C  CA   A GLY A 104 ? 0.0507 0.0320 0.1329 0.0115  0.0131  0.0175  104 GLY A CA   
953  C  CA   B GLY A 104 ? 0.0516 0.0397 0.1523 -0.0141 -0.0182 -0.0181 104 GLY A CA   
954  C  C    A GLY A 104 ? 0.0695 0.0289 0.1286 0.0121  -0.0065 -0.0068 104 GLY A C    
955  C  C    B GLY A 104 ? 0.0688 0.0666 0.1762 0.0208  0.0119  -0.0093 104 GLY A C    
956  O  O    A GLY A 104 ? 0.0434 0.0299 0.1270 -0.0086 0.0087  0.0031  104 GLY A O    
957  O  O    B GLY A 104 ? 0.0406 0.0512 0.1875 -0.0185 -0.0197 0.0017  104 GLY A O    
958  N  N    . SER A 105 ? 0.0422 0.0407 0.1410 -0.0019 0.0153  -0.0006 105 SER A N    
959  C  CA   . SER A 105 ? 0.0455 0.0333 0.1475 -0.0116 0.0285  -0.0074 105 SER A CA   
960  C  C    . SER A 105 ? 0.0574 0.0561 0.1672 -0.0153 -0.0006 -0.0121 105 SER A C    
961  O  O    . SER A 105 ? 0.0582 0.0319 0.1791 -0.0115 0.0100  -0.0230 105 SER A O    
962  C  CB   . SER A 105 ? 0.0483 0.0460 0.1622 -0.0010 0.0162  0.0146  105 SER A CB   
963  O  OG   . SER A 105 ? 0.0722 0.0282 0.1775 -0.0108 0.0162  0.0035  105 SER A OG   
964  N  N    . GLU A 106 ? 0.0499 0.0273 0.1406 -0.0033 0.0149  -0.0148 106 GLU A N    
965  C  CA   . GLU A 106 ? 0.0516 0.0344 0.1532 -0.0153 0.0041  0.0000  106 GLU A CA   
966  C  C    . GLU A 106 ? 0.0684 0.0512 0.1414 0.0027  0.0120  0.0024  106 GLU A C    
967  O  O    . GLU A 106 ? 0.0348 0.0625 0.1696 -0.0109 0.0074  -0.0052 106 GLU A O    
968  C  CB   . GLU A 106 ? 0.0700 0.0282 0.1403 -0.0110 0.0153  0.0000  106 GLU A CB   
969  C  CG   . GLU A 106 ? 0.0961 0.0318 0.1748 -0.0183 0.0030  -0.0172 106 GLU A CG   
970  C  CD   . GLU A 106 ? 0.0329 0.0300 0.1760 -0.0060 -0.0074 0.0043  106 GLU A CD   
971  O  OE1  . GLU A 106 ? 0.0379 0.0320 0.2064 0.0030  -0.0052 0.0093  106 GLU A OE1  
972  O  OE2  . GLU A 106 ? 0.1072 0.0530 0.1967 -0.0043 0.0390  -0.0085 106 GLU A OE2  
973  N  N    . HIS A 107 ? 0.0368 0.0357 0.1677 0.0107  0.0142  0.0065  107 HIS A N    
974  C  CA   . HIS A 107 ? 0.0348 0.0282 0.1550 0.0051  0.0153  0.0043  107 HIS A CA   
975  C  C    . HIS A 107 ? 0.0645 0.0460 0.1459 0.0159  0.0329  0.0049  107 HIS A C    
976  O  O    . HIS A 107 ? 0.0608 0.0340 0.1599 0.0160  0.0226  -0.0010 107 HIS A O    
977  C  CB   . HIS A 107 ? 0.0404 0.0385 0.1575 0.0136  0.0126  0.0005  107 HIS A CB   
978  C  CG   . HIS A 107 ? 0.0579 0.0603 0.1403 -0.0165 0.0038  0.0155  107 HIS A CG   
979  N  ND1  . HIS A 107 ? 0.0670 0.0643 0.1453 -0.0046 -0.0104 -0.0115 107 HIS A ND1  
980  C  CD2  . HIS A 107 ? 0.0432 0.0366 0.1516 -0.0027 0.0043  -0.0082 107 HIS A CD2  
981  C  CE1  . HIS A 107 ? 0.0324 0.0269 0.1773 0.0026  -0.0093 -0.0122 107 HIS A CE1  
982  N  NE2  . HIS A 107 ? 0.0265 0.0258 0.1944 0.0000  0.0060  -0.0087 107 HIS A NE2  
983  N  N    . THR A 108 ? 0.0562 0.0421 0.1502 -0.0142 0.0271  0.0194  108 THR A N    
984  C  CA   . THR A 108 ? 0.1054 0.0297 0.1528 0.0073  0.0286  0.0233  108 THR A CA   
985  C  C    . THR A 108 ? 0.1035 0.0260 0.1537 -0.0006 0.0093  0.0089  108 THR A C    
986  O  O    . THR A 108 ? 0.0749 0.0508 0.1719 0.0087  0.0057  0.0104  108 THR A O    
987  C  CB   . THR A 108 ? 0.0815 0.0467 0.1877 0.0342  0.0104  0.0157  108 THR A CB   
988  O  OG1  . THR A 108 ? 0.0718 0.0449 0.1875 0.0296  -0.0032 0.0076  108 THR A OG1  
989  C  CG2  . THR A 108 ? 0.0927 0.0618 0.1624 0.0108  0.0439  0.0104  108 THR A CG2  
990  N  N    . VAL A 109 ? 0.0578 0.0305 0.1679 0.0102  0.0082  0.0193  109 VAL A N    
991  C  CA   . VAL A 109 ? 0.1133 0.0666 0.1604 0.0166  0.0204  0.0248  109 VAL A CA   
992  C  C    . VAL A 109 ? 0.1000 0.0450 0.1791 -0.0038 0.0307  0.0010  109 VAL A C    
993  O  O    . VAL A 109 ? 0.0979 0.0291 0.1902 -0.0027 0.0208  0.0020  109 VAL A O    
994  C  CB   . VAL A 109 ? 0.0930 0.0569 0.2028 -0.0131 0.0162  0.0137  109 VAL A CB   
995  C  CG1  . VAL A 109 ? 0.0991 0.0939 0.2283 0.0012  0.0390  0.0372  109 VAL A CG1  
996  C  CG2  . VAL A 109 ? 0.0975 0.0328 0.1945 0.0220  0.0082  0.0125  109 VAL A CG2  
997  N  N    . ASP A 110 ? 0.1272 0.0320 0.1696 0.0227  0.0074  0.0054  110 ASP A N    
998  C  CA   . ASP A 110 ? 0.1121 0.0740 0.1967 0.0549  0.0281  0.0236  110 ASP A CA   
999  C  C    . ASP A 110 ? 0.1178 0.0499 0.2010 0.0176  0.0185  -0.0164 110 ASP A C    
1000 O  O    . ASP A 110 ? 0.1377 0.0580 0.1940 0.0232  -0.0147 0.0142  110 ASP A O    
1001 C  CB   . ASP A 110 ? 0.1687 0.0957 0.2060 0.0093  0.0445  0.0159  110 ASP A CB   
1002 C  CG   . ASP A 110 ? 0.1507 0.0578 0.2150 0.0153  0.0175  0.0230  110 ASP A CG   
1003 O  OD1  . ASP A 110 ? 0.1658 0.0711 0.2396 0.0204  0.0516  0.0241  110 ASP A OD1  
1004 O  OD2  . ASP A 110 ? 0.1553 0.1459 0.2500 0.0326  0.0604  0.0167  110 ASP A OD2  
1005 N  N    . LYS A 111 ? 0.0986 0.0586 0.1629 0.0366  0.0220  -0.0019 111 LYS A N    
1006 C  CA   . LYS A 111 ? 0.0961 0.0733 0.1877 0.0258  -0.0035 0.0119  111 LYS A CA   
1007 C  C    . LYS A 111 ? 0.1298 0.0410 0.1567 0.0363  -0.0002 0.0197  111 LYS A C    
1008 O  O    . LYS A 111 ? 0.1390 0.0724 0.2005 0.0107  0.0184  -0.0046 111 LYS A O    
1009 C  CB   . LYS A 111 ? 0.1268 0.0801 0.2180 0.0697  -0.0313 0.0136  111 LYS A CB   
1010 C  CG   . LYS A 111 ? 0.1660 0.1377 0.2583 0.0320  -0.0379 0.0184  111 LYS A CG   
1011 C  CD   . LYS A 111 ? 0.1292 0.2484 0.2935 0.0531  -0.0465 -0.0432 111 LYS A CD   
1012 C  CE   . LYS A 111 ? 0.1776 0.2299 0.3131 0.0326  -0.0581 -0.0408 111 LYS A CE   
1013 N  NZ   . LYS A 111 ? 0.2321 0.3181 0.3224 -0.0230 -0.0408 0.0087  111 LYS A NZ   
1014 N  N    . LYS A 112 ? 0.0925 0.0518 0.1507 0.0104  -0.0120 0.0274  112 LYS A N    
1015 C  CA   . LYS A 112 ? 0.0803 0.0599 0.1755 0.0339  0.0098  0.0143  112 LYS A CA   
1016 C  C    . LYS A 112 ? 0.1243 0.0715 0.1527 -0.0031 -0.0043 0.0049  112 LYS A C    
1017 O  O    . LYS A 112 ? 0.0813 0.0354 0.1899 0.0236  -0.0043 0.0031  112 LYS A O    
1018 C  CB   . LYS A 112 ? 0.0927 0.0833 0.1879 -0.0192 -0.0017 0.0198  112 LYS A CB   
1019 C  CG   . LYS A 112 ? 0.0812 0.1347 0.2163 0.0119  0.0272  -0.0326 112 LYS A CG   
1020 C  CD   . LYS A 112 ? 0.1176 0.1225 0.2439 0.0108  -0.0335 0.0104  112 LYS A CD   
1021 C  CE   . LYS A 112 ? 0.2005 0.1238 0.2533 -0.0091 -0.0054 -0.0013 112 LYS A CE   
1022 N  NZ   . LYS A 112 ? 0.2168 0.1063 0.2290 0.0003  -0.0283 0.0012  112 LYS A NZ   
1023 N  N    . LYS A 113 ? 0.0900 0.0657 0.1534 0.0239  0.0087  0.0082  113 LYS A N    
1024 C  CA   . LYS A 113 ? 0.0900 0.0379 0.1570 0.0263  -0.0031 0.0140  113 LYS A CA   
1025 C  C    . LYS A 113 ? 0.0830 0.0379 0.1904 -0.0093 0.0125  0.0175  113 LYS A C    
1026 O  O    . LYS A 113 ? 0.1394 0.0262 0.2146 -0.0062 -0.0195 0.0114  113 LYS A O    
1027 C  CB   . LYS A 113 ? 0.0810 0.0333 0.1934 0.0186  0.0068  0.0191  113 LYS A CB   
1028 C  CG   . LYS A 113 ? 0.1221 0.0900 0.2010 0.0227  -0.0178 0.0152  113 LYS A CG   
1029 C  CD   . LYS A 113 ? 0.0603 0.1115 0.2978 0.0093  0.0156  0.0070  113 LYS A CD   
1030 C  CE   . LYS A 113 ? 0.1228 0.1121 0.2721 0.0379  0.0280  0.0063  113 LYS A CE   
1031 N  NZ   . LYS A 113 ? 0.2535 0.1737 0.4581 -0.0232 -0.1027 -0.0241 113 LYS A NZ   
1032 N  N    . TYR A 114 ? 0.0645 0.0424 0.1667 0.0113  0.0156  0.0038  114 TYR A N    
1033 C  CA   . TYR A 114 ? 0.0690 0.0406 0.1658 -0.0012 0.0030  0.0183  114 TYR A CA   
1034 C  C    . TYR A 114 ? 0.0735 0.0254 0.1588 -0.0020 0.0113  -0.0004 114 TYR A C    
1035 O  O    . TYR A 114 ? 0.0768 0.0463 0.1687 -0.0308 0.0487  -0.0142 114 TYR A O    
1036 C  CB   . TYR A 114 ? 0.0458 0.0679 0.1862 0.0118  0.0298  -0.0027 114 TYR A CB   
1037 C  CG   . TYR A 114 ? 0.0925 0.0468 0.1674 0.0065  0.0070  0.0027  114 TYR A CG   
1038 C  CD1  . TYR A 114 ? 0.0882 0.0566 0.2069 0.0035  0.0154  0.0331  114 TYR A CD1  
1039 C  CD2  . TYR A 114 ? 0.0806 0.0467 0.2142 -0.0339 0.0145  0.0002  114 TYR A CD2  
1040 C  CE1  . TYR A 114 ? 0.1782 0.0731 0.1642 -0.0263 0.0132  0.0164  114 TYR A CE1  
1041 C  CE2  . TYR A 114 ? 0.1115 0.0812 0.1751 0.0000  0.0344  0.0027  114 TYR A CE2  
1042 C  CZ   . TYR A 114 ? 0.1205 0.0855 0.2044 -0.0303 0.0436  0.0217  114 TYR A CZ   
1043 O  OH   . TYR A 114 ? 0.1931 0.2001 0.2340 -0.0086 0.0860  0.0088  114 TYR A OH   
1044 N  N    . ALA A 115 ? 0.0880 0.0266 0.1574 0.0073  0.0027  0.0083  115 ALA A N    
1045 C  CA   . ALA A 115 ? 0.0737 0.0256 0.1565 0.0023  0.0192  -0.0036 115 ALA A CA   
1046 C  C    . ALA A 115 ? 0.0853 0.0368 0.1588 -0.0098 0.0233  0.0070  115 ALA A C    
1047 O  O    . ALA A 115 ? 0.1076 0.0275 0.1640 -0.0136 0.0362  -0.0048 115 ALA A O    
1048 C  CB   . ALA A 115 ? 0.1088 0.0427 0.1796 0.0052  -0.0176 0.0023  115 ALA A CB   
1049 N  N    . ALA A 116 ? 0.0832 0.0254 0.1718 0.0000  0.0048  -0.0046 116 ALA A N    
1050 C  CA   . ALA A 116 ? 0.0821 0.0477 0.1487 -0.0351 0.0215  -0.0215 116 ALA A CA   
1051 C  C    . ALA A 116 ? 0.0389 0.0376 0.1635 -0.0109 0.0099  -0.0006 116 ALA A C    
1052 O  O    . ALA A 116 ? 0.0542 0.0375 0.1605 0.0169  0.0218  -0.0034 116 ALA A O    
1053 C  CB   . ALA A 116 ? 0.1079 0.0512 0.1737 -0.0461 0.0187  -0.0049 116 ALA A CB   
1054 N  N    . GLU A 117 ? 0.0517 0.0284 0.1577 -0.0082 -0.0062 -0.0065 117 GLU A N    
1055 C  CA   . GLU A 117 ? 0.0725 0.0284 0.1593 0.0121  -0.0065 -0.0030 117 GLU A CA   
1056 C  C    . GLU A 117 ? 0.0416 0.0408 0.1635 0.0020  -0.0017 -0.0077 117 GLU A C    
1057 O  O    . GLU A 117 ? 0.0661 0.0282 0.2074 -0.0085 0.0203  0.0093  117 GLU A O    
1058 C  CB   . GLU A 117 ? 0.1171 0.0358 0.1545 -0.0107 -0.0052 -0.0172 117 GLU A CB   
1059 C  CG   . GLU A 117 ? 0.0767 0.0463 0.1606 -0.0265 -0.0153 -0.0223 117 GLU A CG   
1060 C  CD   . GLU A 117 ? 0.0571 0.0643 0.1491 0.0015  0.0252  -0.0164 117 GLU A CD   
1061 O  OE1  . GLU A 117 ? 0.0524 0.0504 0.1861 0.0070  0.0086  -0.0037 117 GLU A OE1  
1062 O  OE2  . GLU A 117 ? 0.0939 0.0436 0.1422 0.0137  -0.0093 -0.0255 117 GLU A OE2  
1063 N  N    . LEU A 118 ? 0.0681 0.0327 0.1699 0.0129  -0.0143 0.0178  118 LEU A N    
1064 C  CA   . LEU A 118 ? 0.1242 0.0263 0.1446 0.0099  0.0063  0.0017  118 LEU A CA   
1065 C  C    . LEU A 118 ? 0.0825 0.0278 0.1527 0.0118  0.0113  0.0021  118 LEU A C    
1066 O  O    . LEU A 118 ? 0.0785 0.0325 0.1550 0.0071  0.0104  0.0115  118 LEU A O    
1067 C  CB   . LEU A 118 ? 0.0859 0.0288 0.1741 0.0054  -0.0076 0.0203  118 LEU A CB   
1068 C  CG   . LEU A 118 ? 0.0727 0.0306 0.1767 0.0146  -0.0064 0.0088  118 LEU A CG   
1069 C  CD1  . LEU A 118 ? 0.1500 0.0578 0.1681 0.0384  -0.0035 0.0465  118 LEU A CD1  
1070 C  CD2  . LEU A 118 ? 0.0749 0.0864 0.1801 -0.0176 -0.0275 0.0136  118 LEU A CD2  
1071 N  N    . HIS A 119 ? 0.0813 0.0271 0.1474 -0.0097 -0.0048 -0.0027 119 HIS A N    
1072 C  CA   . HIS A 119 ? 0.0608 0.0327 0.1500 0.0147  0.0017  -0.0119 119 HIS A CA   
1073 C  C    . HIS A 119 ? 0.0595 0.0266 0.1575 -0.0053 -0.0014 0.0078  119 HIS A C    
1074 O  O    . HIS A 119 ? 0.1089 0.0404 0.1714 0.0035  0.0130  0.0010  119 HIS A O    
1075 C  CB   . HIS A 119 ? 0.0473 0.0269 0.1599 0.0054  0.0000  -0.0040 119 HIS A CB   
1076 C  CG   . HIS A 119 ? 0.0740 0.0458 0.1492 0.0313  -0.0024 0.0031  119 HIS A CG   
1077 N  ND1  . HIS A 119 ? 0.0774 0.0695 0.1142 -0.0478 -0.0131 0.0065  119 HIS A ND1  
1078 C  CD2  . HIS A 119 ? 0.0352 0.0265 0.1629 0.0007  0.0057  -0.0115 119 HIS A CD2  
1079 C  CE1  . HIS A 119 ? 0.0429 0.0846 0.1458 -0.0243 -0.0007 -0.0538 119 HIS A CE1  
1080 N  NE2  . HIS A 119 ? 0.0288 0.0254 0.1983 0.0006  -0.0243 -0.0045 119 HIS A NE2  
1081 N  N    . LEU A 120 ? 0.0528 0.0343 0.1723 0.0049  -0.0037 0.0015  120 LEU A N    
1082 C  CA   . LEU A 120 ? 0.0564 0.0340 0.1737 -0.0051 -0.0186 -0.0091 120 LEU A CA   
1083 C  C    . LEU A 120 ? 0.0494 0.0417 0.1554 0.0197  0.0082  0.0052  120 LEU A C    
1084 O  O    . LEU A 120 ? 0.0435 0.0264 0.1623 0.0025  -0.0022 0.0095  120 LEU A O    
1085 C  CB   . LEU A 120 ? 0.0553 0.0291 0.1969 0.0104  -0.0146 -0.0006 120 LEU A CB   
1086 C  CG   . LEU A 120 ? 0.0733 0.0873 0.1683 -0.0313 -0.0233 -0.0148 120 LEU A CG   
1087 C  CD1  . LEU A 120 ? 0.1142 0.0916 0.2227 -0.0621 0.0074  0.0107  120 LEU A CD1  
1088 C  CD2  . LEU A 120 ? 0.1080 0.0939 0.2161 -0.0236 -0.0571 -0.0119 120 LEU A CD2  
1089 N  N    . VAL A 121 ? 0.0463 0.0353 0.1737 -0.0040 -0.0015 0.0046  121 VAL A N    
1090 C  CA   . VAL A 121 ? 0.0599 0.0408 0.1654 0.0142  0.0140  -0.0200 121 VAL A CA   
1091 C  C    . VAL A 121 ? 0.0767 0.0307 0.1694 -0.0164 0.0015  -0.0031 121 VAL A C    
1092 O  O    . VAL A 121 ? 0.0758 0.0436 0.1654 0.0057  -0.0196 -0.0020 121 VAL A O    
1093 C  CB   . VAL A 121 ? 0.0728 0.0398 0.1884 -0.0250 0.0284  -0.0288 121 VAL A CB   
1094 C  CG1  . VAL A 121 ? 0.1376 0.0420 0.1755 -0.0187 0.0124  -0.0136 121 VAL A CG1  
1095 C  CG2  . VAL A 121 ? 0.0975 0.0582 0.1836 0.0447  0.0287  -0.0094 121 VAL A CG2  
1096 N  N    . HIS A 122 ? 0.0558 0.0259 0.1619 0.0011  0.0101  -0.0079 122 HIS A N    
1097 C  CA   . HIS A 122 ? 0.0740 0.0259 0.1752 -0.0027 0.0197  -0.0089 122 HIS A CA   
1098 C  C    . HIS A 122 ? 0.0874 0.0397 0.1838 -0.0286 0.0104  0.0085  122 HIS A C    
1099 O  O    . HIS A 122 ? 0.0510 0.0403 0.1963 -0.0195 -0.0173 0.0141  122 HIS A O    
1100 C  CB   . HIS A 122 ? 0.0652 0.0395 0.2179 0.0215  0.0167  -0.0129 122 HIS A CB   
1101 C  CG   . HIS A 122 ? 0.0988 0.0408 0.1622 0.0130  0.0013  0.0074  122 HIS A CG   
1102 N  ND1  . HIS A 122 ? 0.0464 0.0258 0.2085 -0.0033 0.0027  -0.0016 122 HIS A ND1  
1103 C  CD2  . HIS A 122 ? 0.1395 0.0327 0.1597 -0.0230 -0.0132 0.0013  122 HIS A CD2  
1104 C  CE1  . HIS A 122 ? 0.0603 0.0632 0.2037 0.0362  -0.0035 -0.0052 122 HIS A CE1  
1105 N  NE2  . HIS A 122 ? 0.0465 0.0410 0.2236 0.0175  -0.0146 -0.0269 122 HIS A NE2  
1106 N  N    . TRP A 123 ? 0.0425 0.0261 0.1943 0.0035  -0.0015 -0.0003 123 TRP A N    
1107 C  CA   . TRP A 123 ? 0.0697 0.0274 0.1899 0.0052  0.0082  -0.0148 123 TRP A CA   
1108 C  C    . TRP A 123 ? 0.0580 0.0327 0.1717 0.0154  0.0099  0.0076  123 TRP A C    
1109 O  O    . TRP A 123 ? 0.0577 0.0526 0.1985 0.0037  -0.0030 -0.0065 123 TRP A O    
1110 C  CB   . TRP A 123 ? 0.0767 0.0362 0.1780 -0.0160 -0.0081 0.0000  123 TRP A CB   
1111 C  CG   . TRP A 123 ? 0.0992 0.0407 0.2143 -0.0063 0.0046  0.0188  123 TRP A CG   
1112 C  CD1  . TRP A 123 ? 0.1606 0.1015 0.1519 -0.0120 -0.0181 0.0142  123 TRP A CD1  
1113 C  CD2  . TRP A 123 ? 0.1767 0.0311 0.1735 0.0024  -0.0146 -0.0294 123 TRP A CD2  
1114 N  NE1  . TRP A 123 ? 0.2112 0.0449 0.1739 -0.0505 -0.0247 0.0017  123 TRP A NE1  
1115 C  CE2  . TRP A 123 ? 0.1897 0.0573 0.2069 -0.0027 -0.0261 -0.0065 123 TRP A CE2  
1116 C  CE3  . TRP A 123 ? 0.1703 0.0335 0.1805 -0.0302 0.0225  0.0126  123 TRP A CE3  
1117 C  CZ2  . TRP A 123 ? 0.2089 0.0482 0.1859 -0.0241 0.0147  -0.0024 123 TRP A CZ2  
1118 C  CZ3  . TRP A 123 ? 0.1913 0.0675 0.2213 -0.0043 -0.0131 -0.0027 123 TRP A CZ3  
1119 C  CH2  . TRP A 123 ? 0.1888 0.0485 0.2067 -0.0340 -0.0093 -0.0006 123 TRP A CH2  
1120 N  N    . ASN A 124 ? 0.0826 0.0518 0.1780 -0.0023 -0.0019 -0.0239 124 ASN A N    
1121 C  CA   . ASN A 124 ? 0.1045 0.0334 0.1945 -0.0003 0.0082  -0.0195 124 ASN A CA   
1122 C  C    . ASN A 124 ? 0.0934 0.0472 0.2003 0.0051  0.0031  -0.0390 124 ASN A C    
1123 O  O    . ASN A 124 ? 0.0806 0.0416 0.2082 0.0035  0.0020  -0.0085 124 ASN A O    
1124 C  CB   . ASN A 124 ? 0.0973 0.0794 0.1511 0.0164  0.0152  -0.0253 124 ASN A CB   
1125 C  CG   . ASN A 124 ? 0.1171 0.0384 0.1665 -0.0342 0.0229  -0.0028 124 ASN A CG   
1126 O  OD1  . ASN A 124 ? 0.1138 0.0494 0.2182 0.0456  0.0147  -0.0028 124 ASN A OD1  
1127 N  ND2  . ASN A 124 ? 0.1480 0.0357 0.1818 0.0108  0.0007  -0.0208 124 ASN A ND2  
1128 N  N    . THR A 125 ? 0.1018 0.0451 0.1985 0.0364  0.0214  -0.0102 125 THR A N    
1129 C  CA   . THR A 125 ? 0.0968 0.0577 0.2206 0.0261  -0.0003 -0.0074 125 THR A CA   
1130 C  C    . THR A 125 ? 0.1254 0.0704 0.2366 0.0671  0.0071  0.0041  125 THR A C    
1131 O  O    . THR A 125 ? 0.1512 0.0564 0.2590 0.0299  0.0020  0.0012  125 THR A O    
1132 C  CB   . THR A 125 ? 0.1243 0.1272 0.2495 0.0368  0.0000  0.0010  125 THR A CB   
1133 O  OG1  . THR A 125 ? 0.1626 0.1186 0.3000 0.0471  0.0291  0.0172  125 THR A OG1  
1134 C  CG2  . THR A 125 ? 0.1890 0.0961 0.2793 0.0148  -0.0087 -0.0174 125 THR A CG2  
1135 N  N    . LYS A 126 ? 0.1543 0.0395 0.2120 0.0205  0.0188  -0.0155 127 LYS A N    
1136 C  CA   . LYS A 126 ? 0.1383 0.0702 0.2150 -0.0052 0.0342  -0.0419 127 LYS A CA   
1137 C  C    . LYS A 126 ? 0.1343 0.0293 0.2272 -0.0186 0.0144  0.0098  127 LYS A C    
1138 O  O    . LYS A 126 ? 0.1737 0.0445 0.2693 -0.0184 0.0126  -0.0439 127 LYS A O    
1139 C  CB   . LYS A 126 ? 0.1556 0.0957 0.2448 0.0049  0.0043  -0.0353 127 LYS A CB   
1140 C  CG   . LYS A 126 ? 0.1403 0.1045 0.2260 0.0074  0.0026  -0.0269 127 LYS A CG   
1141 C  CD   . LYS A 126 ? 0.2852 0.2441 0.2626 -0.0744 0.0241  0.0113  127 LYS A CD   
1142 C  CE   . LYS A 126 ? 0.3361 0.4150 0.3418 0.0043  0.0303  0.0259  127 LYS A CE   
1143 N  NZ   . LYS A 126 ? 0.4602 0.5098 0.3194 0.0401  0.0249  0.0287  127 LYS A NZ   
1144 N  N    . TYR A 127 ? 0.1396 0.0524 0.1899 0.0048  0.0250  -0.0076 128 TYR A N    
1145 C  CA   . TYR A 127 ? 0.1270 0.0363 0.2028 0.0124  0.0102  0.0040  128 TYR A CA   
1146 C  C    . TYR A 127 ? 0.1423 0.0309 0.2121 0.0242  -0.0021 0.0098  128 TYR A C    
1147 O  O    . TYR A 127 ? 0.1516 0.0411 0.2344 0.0041  0.0080  -0.0031 128 TYR A O    
1148 C  CB   . TYR A 127 ? 0.1496 0.0361 0.1848 0.0237  0.0043  -0.0017 128 TYR A CB   
1149 C  CG   . TYR A 127 ? 0.1052 0.0390 0.1791 -0.0164 -0.0054 -0.0193 128 TYR A CG   
1150 C  CD1  . TYR A 127 ? 0.1401 0.0788 0.2003 0.0013  0.0068  -0.0065 128 TYR A CD1  
1151 C  CD2  . TYR A 127 ? 0.0799 0.0451 0.1841 0.0076  0.0097  0.0003  128 TYR A CD2  
1152 C  CE1  . TYR A 127 ? 0.1480 0.0465 0.2161 0.0175  -0.0211 -0.0125 128 TYR A CE1  
1153 C  CE2  . TYR A 127 ? 0.0982 0.0604 0.1905 0.0305  -0.0020 -0.0333 128 TYR A CE2  
1154 C  CZ   . TYR A 127 ? 0.1599 0.0553 0.1599 0.0331  0.0129  -0.0258 128 TYR A CZ   
1155 O  OH   . TYR A 127 ? 0.2193 0.0571 0.2042 0.0421  0.0037  -0.0230 128 TYR A OH   
1156 N  N    . GLY A 128 ? 0.1252 0.0282 0.2010 0.0098  -0.0087 0.0082  129 GLY A N    
1157 C  CA   . GLY A 128 ? 0.1203 0.0547 0.1923 -0.0154 0.0244  0.0119  129 GLY A CA   
1158 C  C    . GLY A 128 ? 0.0970 0.0675 0.1969 -0.0252 0.0015  0.0126  129 GLY A C    
1159 O  O    . GLY A 128 ? 0.1746 0.0634 0.2171 0.0020  -0.0208 0.0379  129 GLY A O    
1160 N  N    . ASP A 129 ? 0.1419 0.0825 0.2035 0.0082  0.0113  -0.0184 130 ASP A N    
1161 C  CA   . ASP A 129 ? 0.1862 0.0837 0.1872 0.0328  0.0218  0.0076  130 ASP A CA   
1162 C  C    . ASP A 129 ? 0.1798 0.0921 0.1938 0.0219  -0.0091 -0.0010 130 ASP A C    
1163 O  O    . ASP A 129 ? 0.1965 0.0740 0.1913 0.0126  -0.0241 0.0030  130 ASP A O    
1164 C  CB   . ASP A 129 ? 0.1694 0.0693 0.2365 0.0494  0.0222  -0.0098 130 ASP A CB   
1165 C  CG   . ASP A 129 ? 0.1653 0.0401 0.2468 0.0216  0.0155  0.0148  130 ASP A CG   
1166 O  OD1  . ASP A 129 ? 0.2980 0.1004 0.3181 -0.0390 -0.0653 0.0255  130 ASP A OD1  
1167 O  OD2  . ASP A 129 ? 0.2651 0.0925 0.2973 0.0154  0.0675  0.0449  130 ASP A OD2  
1168 N  N    . PHE A 130 ? 0.2204 0.0587 0.1825 -0.0007 0.0086  -0.0027 131 PHE A N    
1169 C  CA   . PHE A 130 ? 0.2049 0.0790 0.2019 0.0012  -0.0077 0.0119  131 PHE A CA   
1170 C  C    . PHE A 130 ? 0.1773 0.0615 0.1868 -0.0186 0.0392  0.0076  131 PHE A C    
1171 O  O    . PHE A 130 ? 0.1552 0.0702 0.1811 -0.0093 0.0217  0.0065  131 PHE A O    
1172 C  CB   . PHE A 130 ? 0.1999 0.0300 0.2012 0.0219  0.0172  -0.0043 131 PHE A CB   
1173 C  CG   . PHE A 130 ? 0.1307 0.0427 0.1893 0.0015  0.0087  -0.0230 131 PHE A CG   
1174 C  CD1  . PHE A 130 ? 0.1349 0.0354 0.1732 -0.0230 0.0091  -0.0043 131 PHE A CD1  
1175 C  CD2  . PHE A 130 ? 0.1780 0.0318 0.2093 -0.0093 0.0546  0.0052  131 PHE A CD2  
1176 C  CE1  . PHE A 130 ? 0.1212 0.0584 0.2112 -0.0137 0.0161  -0.0027 131 PHE A CE1  
1177 C  CE2  . PHE A 130 ? 0.1992 0.0516 0.2335 -0.0205 0.0076  -0.0167 131 PHE A CE2  
1178 C  CZ   . PHE A 130 ? 0.1286 0.0509 0.2118 -0.0464 -0.0248 -0.0176 131 PHE A CZ   
1179 N  N    . GLY A 131 ? 0.1755 0.0661 0.2057 -0.0526 0.0304  -0.0010 132 GLY A N    
1180 C  CA   . GLY A 131 ? 0.1586 0.1203 0.1820 -0.0057 0.0175  0.0130  132 GLY A CA   
1181 C  C    . GLY A 131 ? 0.1660 0.0882 0.2168 -0.0395 0.0322  0.0273  132 GLY A C    
1182 O  O    . GLY A 131 ? 0.1500 0.0769 0.2660 -0.0318 0.0386  0.0024  132 GLY A O    
1183 N  N    . LYS A 132 ? 0.1388 0.0561 0.2268 -0.0472 0.0260  0.0052  133 LYS A N    
1184 C  CA   . LYS A 132 ? 0.1516 0.0401 0.2128 -0.0285 0.0226  0.0125  133 LYS A CA   
1185 C  C    . LYS A 132 ? 0.1207 0.0450 0.2256 -0.0137 0.0296  0.0006  133 LYS A C    
1186 O  O    . LYS A 132 ? 0.1070 0.0569 0.2213 -0.0507 -0.0031 0.0005  133 LYS A O    
1187 C  CB   . LYS A 132 ? 0.1315 0.0553 0.2292 -0.0252 0.0410  0.0137  133 LYS A CB   
1188 C  CG   . LYS A 132 ? 0.2157 0.0788 0.3120 -0.0098 -0.0046 0.0392  133 LYS A CG   
1189 C  CD   . LYS A 132 ? 0.2423 0.0903 0.4448 -0.0421 0.0339  0.0794  133 LYS A CD   
1190 C  CE   . LYS A 132 ? 0.3163 0.1056 0.4211 -0.0996 -0.0121 0.0467  133 LYS A CE   
1191 N  NZ   . LYS A 132 ? 0.4976 0.4236 0.4562 -0.0891 -0.0447 -0.0017 133 LYS A NZ   
1192 N  N    . ALA A 133 ? 0.0858 0.0364 0.2139 -0.0247 0.0277  0.0014  134 ALA A N    
1193 C  CA   . ALA A 133 ? 0.0907 0.0482 0.1992 -0.0020 0.0441  -0.0031 134 ALA A CA   
1194 C  C    . ALA A 133 ? 0.0819 0.0663 0.1900 -0.0469 0.0252  -0.0032 134 ALA A C    
1195 O  O    . ALA A 133 ? 0.0855 0.0588 0.1762 -0.0142 0.0148  -0.0098 134 ALA A O    
1196 C  CB   . ALA A 133 ? 0.0920 0.0607 0.1949 -0.0478 0.0258  -0.0071 134 ALA A CB   
1197 N  N    . VAL A 134 ? 0.0984 0.0445 0.1931 -0.0221 0.0326  -0.0020 135 VAL A N    
1198 C  CA   . VAL A 134 ? 0.1203 0.0973 0.1783 0.0070  0.0194  -0.0071 135 VAL A CA   
1199 C  C    . VAL A 134 ? 0.0803 0.0866 0.1967 -0.0076 0.0265  0.0049  135 VAL A C    
1200 O  O    . VAL A 134 ? 0.0909 0.0702 0.2199 -0.0076 0.0305  -0.0038 135 VAL A O    
1201 C  CB   . VAL A 134 ? 0.1365 0.1049 0.1748 -0.0054 0.0283  0.0000  135 VAL A CB   
1202 C  CG1  . VAL A 134 ? 0.1543 0.1302 0.1881 -0.0461 0.0259  -0.0054 135 VAL A CG1  
1203 C  CG2  . VAL A 134 ? 0.1140 0.0627 0.2062 -0.0120 0.0399  -0.0219 135 VAL A CG2  
1204 N  N    A GLN A 135 ? 0.1049 0.0769 0.1920 -0.0120 0.0274  0.0054  136 GLN A N    
1205 N  N    B GLN A 135 ? 0.0997 0.0727 0.1920 -0.0143 0.0320  0.0087  136 GLN A N    
1206 C  CA   A GLN A 135 ? 0.1239 0.0934 0.1969 -0.0474 0.0091  0.0086  136 GLN A CA   
1207 C  CA   B GLN A 135 ? 0.1218 0.0812 0.1981 -0.0412 0.0164  0.0197  136 GLN A CA   
1208 C  C    A GLN A 135 ? 0.1182 0.0903 0.1938 -0.0263 0.0155  0.0031  136 GLN A C    
1209 C  C    B GLN A 135 ? 0.1040 0.0864 0.2021 -0.0141 0.0229  0.0006  136 GLN A C    
1210 O  O    A GLN A 135 ? 0.1665 0.1013 0.2071 -0.0065 -0.0252 -0.0043 136 GLN A O    
1211 O  O    B GLN A 135 ? 0.0975 0.1282 0.2389 0.0054  -0.0159 0.0163  136 GLN A O    
1212 C  CB   A GLN A 135 ? 0.1058 0.0763 0.2153 -0.0452 -0.0086 0.0119  136 GLN A CB   
1213 C  CB   B GLN A 135 ? 0.1144 0.1110 0.2089 -0.0812 0.0373  0.0098  136 GLN A CB   
1214 C  CG   A GLN A 135 ? 0.1142 0.1119 0.2394 -0.0657 0.0368  0.0285  136 GLN A CG   
1215 C  CG   B GLN A 135 ? 0.1446 0.0792 0.2186 -0.0284 0.0370  0.0333  136 GLN A CG   
1216 C  CD   A GLN A 135 ? 0.1523 0.2459 0.2976 -0.0333 0.0878  0.0035  136 GLN A CD   
1217 C  CD   B GLN A 135 ? 0.1949 0.1658 0.2310 -0.0974 0.0250  -0.0164 136 GLN A CD   
1218 O  OE1  A GLN A 135 ? 0.2678 0.2917 0.3610 0.0109  0.0395  0.0031  136 GLN A OE1  
1219 O  OE1  B GLN A 135 ? 0.1848 0.1740 0.2730 -0.0215 -0.0060 0.0377  136 GLN A OE1  
1220 N  NE2  A GLN A 135 ? 0.3711 0.2161 0.2985 -0.0872 0.1146  -0.0216 136 GLN A NE2  
1221 N  NE2  B GLN A 135 ? 0.1640 0.1683 0.2827 -0.1208 0.0099  0.0636  136 GLN A NE2  
1222 N  N    . GLN A 136 ? 0.0912 0.0835 0.1913 -0.0350 0.0406  -0.0038 137 GLN A N    
1223 C  CA   . GLN A 136 ? 0.1263 0.0860 0.1705 -0.0164 0.0147  -0.0175 137 GLN A CA   
1224 C  C    . GLN A 136 ? 0.1133 0.0968 0.1539 -0.0027 0.0143  0.0017  137 GLN A C    
1225 O  O    . GLN A 136 ? 0.1089 0.0939 0.1640 0.0185  -0.0043 -0.0153 137 GLN A O    
1226 C  CB   . GLN A 136 ? 0.0986 0.0652 0.2177 0.0214  0.0076  -0.0153 137 GLN A CB   
1227 C  CG   . GLN A 136 ? 0.1406 0.0984 0.2389 -0.0020 0.0131  0.0003  137 GLN A CG   
1228 C  CD   . GLN A 136 ? 0.1097 0.0918 0.2813 0.0260  0.0331  0.0489  137 GLN A CD   
1229 O  OE1  . GLN A 136 ? 0.2705 0.1214 0.2890 -0.0088 -0.0126 -0.0509 137 GLN A OE1  
1230 N  NE2  . GLN A 136 ? 0.2763 0.1500 0.4702 0.0531  0.0526  0.0755  137 GLN A NE2  
1231 N  N    . PRO A 137 ? 0.0873 0.0970 0.1697 0.0164  0.0073  -0.0199 138 PRO A N    
1232 C  CA   . PRO A 137 ? 0.0862 0.0776 0.1789 0.0070  0.0065  -0.0043 138 PRO A CA   
1233 C  C    . PRO A 137 ? 0.0943 0.0672 0.1773 -0.0006 -0.0027 -0.0173 138 PRO A C    
1234 O  O    . PRO A 137 ? 0.1327 0.0654 0.2344 0.0406  0.0135  0.0131  138 PRO A O    
1235 C  CB   . PRO A 137 ? 0.1523 0.0968 0.1852 0.0294  -0.0068 -0.0082 138 PRO A CB   
1236 C  CG   . PRO A 137 ? 0.2576 0.2056 0.1888 0.0248  -0.0269 0.0071  138 PRO A CG   
1237 C  CD   . PRO A 137 ? 0.1144 0.1430 0.1866 -0.0103 -0.0115 -0.0241 138 PRO A CD   
1238 N  N    . ASP A 138 ? 0.0846 0.0722 0.1685 0.0175  0.0049  -0.0210 139 ASP A N    
1239 C  CA   . ASP A 138 ? 0.0758 0.0803 0.1836 0.0052  0.0217  0.0038  139 ASP A CA   
1240 C  C    . ASP A 138 ? 0.0891 0.0469 0.1834 -0.0280 0.0186  0.0051  139 ASP A C    
1241 O  O    . ASP A 138 ? 0.0769 0.0557 0.2073 0.0051  0.0193  -0.0141 139 ASP A O    
1242 C  CB   . ASP A 138 ? 0.1094 0.0846 0.1837 -0.0285 0.0306  -0.0037 139 ASP A CB   
1243 C  CG   . ASP A 138 ? 0.0984 0.1149 0.1954 0.0148  0.0120  -0.0244 139 ASP A CG   
1244 O  OD1  . ASP A 138 ? 0.1399 0.0790 0.2274 0.0516  0.0103  -0.0295 139 ASP A OD1  
1245 O  OD2  . ASP A 138 ? 0.1636 0.1615 0.2583 0.0483  0.0306  -0.0700 139 ASP A OD2  
1246 N  N    . GLY A 139 ? 0.0842 0.0450 0.1685 0.0070  0.0110  0.0052  140 GLY A N    
1247 C  CA   . GLY A 139 ? 0.0758 0.0571 0.1710 0.0093  0.0015  -0.0003 140 GLY A CA   
1248 C  C    . GLY A 139 ? 0.0518 0.0274 0.1830 -0.0070 0.0063  -0.0082 140 GLY A C    
1249 O  O    . GLY A 139 ? 0.0747 0.0397 0.1870 0.0137  -0.0151 -0.0205 140 GLY A O    
1250 N  N    . LEU A 140 ? 0.0253 0.0267 0.1786 0.0001  -0.0010 -0.0144 141 LEU A N    
1251 C  CA   . LEU A 140 ? 0.0295 0.0340 0.1780 0.0059  0.0022  0.0005  141 LEU A CA   
1252 C  C    . LEU A 140 ? 0.0295 0.0260 0.1778 0.0013  -0.0071 -0.0076 141 LEU A C    
1253 O  O    . LEU A 140 ? 0.0677 0.0403 0.1650 -0.0020 -0.0015 -0.0035 141 LEU A O    
1254 C  CB   . LEU A 140 ? 0.0382 0.0438 0.1978 0.0145  0.0132  -0.0025 141 LEU A CB   
1255 C  CG   . LEU A 140 ? 0.0384 0.0499 0.1945 0.0003  -0.0037 0.0063  141 LEU A CG   
1256 C  CD1  . LEU A 140 ? 0.0463 0.0869 0.1967 0.0274  0.0248  -0.0098 141 LEU A CD1  
1257 C  CD2  . LEU A 140 ? 0.0825 0.0333 0.1859 -0.0211 0.0052  -0.0055 141 LEU A CD2  
1258 N  N    . ALA A 141 ? 0.0326 0.0429 0.1787 0.0113  -0.0092 -0.0168 142 ALA A N    
1259 C  CA   . ALA A 141 ? 0.0497 0.0253 0.1611 0.0002  0.0069  -0.0015 142 ALA A CA   
1260 C  C    . ALA A 141 ? 0.0480 0.0715 0.1622 0.0175  0.0162  0.0020  142 ALA A C    
1261 O  O    . ALA A 141 ? 0.0897 0.0255 0.1807 0.0033  0.0037  0.0013  142 ALA A O    
1262 C  CB   . ALA A 141 ? 0.0510 0.0398 0.2076 -0.0151 0.0127  0.0237  142 ALA A CB   
1263 N  N    . VAL A 142 ? 0.0657 0.0423 0.1715 0.0109  0.0126  -0.0003 143 VAL A N    
1264 C  CA   . VAL A 142 ? 0.0681 0.0492 0.1685 -0.0080 0.0065  0.0041  143 VAL A CA   
1265 C  C    . VAL A 142 ? 0.0731 0.0284 0.1485 -0.0071 0.0207  -0.0024 143 VAL A C    
1266 O  O    . VAL A 142 ? 0.0684 0.0364 0.1438 -0.0215 -0.0030 -0.0045 143 VAL A O    
1267 C  CB   . VAL A 142 ? 0.0505 0.0634 0.1728 0.0129  -0.0038 0.0030  143 VAL A CB   
1268 C  CG1  . VAL A 142 ? 0.0864 0.0760 0.1719 0.0197  -0.0035 -0.0504 143 VAL A CG1  
1269 C  CG2  . VAL A 142 ? 0.0361 0.1401 0.1762 0.0198  0.0153  0.0219  143 VAL A CG2  
1270 N  N    . LEU A 143 ? 0.0675 0.0371 0.1696 -0.0156 -0.0003 0.0060  144 LEU A N    
1271 C  CA   . LEU A 143 ? 0.0778 0.0262 0.1755 0.0063  -0.0274 -0.0054 144 LEU A CA   
1272 C  C    . LEU A 143 ? 0.0690 0.0494 0.1553 -0.0313 -0.0074 -0.0087 144 LEU A C    
1273 O  O    . LEU A 143 ? 0.0812 0.0403 0.1685 -0.0283 -0.0020 -0.0078 144 LEU A O    
1274 C  CB   . LEU A 143 ? 0.0695 0.0539 0.1906 -0.0076 -0.0093 0.0057  144 LEU A CB   
1275 C  CG   . LEU A 143 ? 0.0715 0.0593 0.2206 0.0024  0.0307  -0.0082 144 LEU A CG   
1276 C  CD1  . LEU A 143 ? 0.0715 0.0876 0.2132 -0.0288 -0.0132 0.0329  144 LEU A CD1  
1277 C  CD2  . LEU A 143 ? 0.0589 0.1264 0.2211 0.0164  0.0164  0.0059  144 LEU A CD2  
1278 N  N    . GLY A 144 ? 0.0715 0.0282 0.1581 -0.0006 -0.0230 -0.0063 145 GLY A N    
1279 C  CA   . GLY A 144 ? 0.0454 0.0256 0.1776 -0.0003 -0.0020 -0.0062 145 GLY A CA   
1280 C  C    . GLY A 144 ? 0.0454 0.0495 0.1566 0.0219  0.0070  0.0102  145 GLY A C    
1281 O  O    . GLY A 144 ? 0.0758 0.0515 0.1642 -0.0283 0.0070  -0.0065 145 GLY A O    
1282 N  N    . ILE A 145 ? 0.0502 0.0334 0.1604 0.0137  -0.0048 0.0043  146 ILE A N    
1283 C  CA   . ILE A 145 ? 0.0275 0.0254 0.1932 -0.0005 -0.0098 0.0030  146 ILE A CA   
1284 C  C    . ILE A 145 ? 0.0565 0.0334 0.1765 -0.0154 0.0089  0.0019  146 ILE A C    
1285 O  O    . ILE A 145 ? 0.0720 0.0270 0.1775 0.0027  -0.0041 0.0109  146 ILE A O    
1286 C  CB   . ILE A 145 ? 0.0515 0.0269 0.2075 -0.0049 -0.0057 0.0119  146 ILE A CB   
1287 C  CG1  . ILE A 145 ? 0.0927 0.0424 0.2035 0.0326  -0.0251 -0.0040 146 ILE A CG1  
1288 C  CG2  . ILE A 145 ? 0.0706 0.0459 0.2249 -0.0271 -0.0271 -0.0120 146 ILE A CG2  
1289 C  CD1  . ILE A 145 ? 0.0878 0.0370 0.1983 0.0263  -0.0082 0.0073  146 ILE A CD1  
1290 N  N    . PHE A 146 ? 0.0334 0.0260 0.1771 -0.0010 -0.0205 -0.0043 147 PHE A N    
1291 C  CA   . PHE A 146 ? 0.0623 0.0380 0.1583 0.0209  -0.0113 -0.0164 147 PHE A CA   
1292 C  C    . PHE A 146 ? 0.0763 0.0309 0.1800 0.0140  -0.0087 0.0141  147 PHE A C    
1293 O  O    . PHE A 146 ? 0.0574 0.0257 0.2006 0.0026  0.0043  -0.0062 147 PHE A O    
1294 C  CB   . PHE A 146 ? 0.0778 0.0509 0.1726 0.0026  -0.0164 0.0183  147 PHE A CB   
1295 C  CG   . PHE A 146 ? 0.0681 0.0487 0.1237 -0.0114 -0.0070 0.0135  147 PHE A CG   
1296 C  CD1  . PHE A 146 ? 0.0476 0.0412 0.1938 0.0183  -0.0087 -0.0185 147 PHE A CD1  
1297 C  CD2  . PHE A 146 ? 0.0636 0.0401 0.1712 0.0136  -0.0104 0.0337  147 PHE A CD2  
1298 C  CE1  . PHE A 146 ? 0.0445 0.0386 0.1945 -0.0159 0.0088  -0.0070 147 PHE A CE1  
1299 C  CE2  . PHE A 146 ? 0.0441 0.0524 0.1703 0.0216  0.0076  0.0005  147 PHE A CE2  
1300 C  CZ   . PHE A 146 ? 0.0407 0.0319 0.1622 -0.0063 0.0114  0.0181  147 PHE A CZ   
1301 N  N    . LEU A 147 ? 0.1090 0.0307 0.1565 0.0131  0.0138  -0.0182 148 LEU A N    
1302 C  CA   . LEU A 147 ? 0.1146 0.0291 0.1572 0.0173  -0.0057 0.0062  148 LEU A CA   
1303 C  C    . LEU A 147 ? 0.0825 0.0361 0.1672 0.0041  0.0020  -0.0006 148 LEU A C    
1304 O  O    . LEU A 147 ? 0.0765 0.0322 0.1995 -0.0005 0.0142  0.0104  148 LEU A O    
1305 C  CB   . LEU A 147 ? 0.1058 0.0340 0.1793 -0.0007 0.0093  -0.0031 148 LEU A CB   
1306 C  CG   . LEU A 147 ? 0.1629 0.0320 0.1859 -0.0038 0.0049  -0.0063 148 LEU A CG   
1307 C  CD1  . LEU A 147 ? 0.1841 0.0419 0.1723 -0.0368 0.0183  -0.0211 148 LEU A CD1  
1308 C  CD2  . LEU A 147 ? 0.1676 0.0546 0.1678 -0.0109 0.0006  0.0109  148 LEU A CD2  
1309 N  N    . LYS A 148 ? 0.0683 0.0255 0.1982 0.0001  -0.0056 -0.0065 149 LYS A N    
1310 C  CA   . LYS A 148 ? 0.1067 0.0335 0.1942 0.0254  -0.0256 -0.0024 149 LYS A CA   
1311 C  C    . LYS A 148 ? 0.0632 0.0677 0.1951 0.0057  -0.0192 -0.0087 149 LYS A C    
1312 O  O    . LYS A 148 ? 0.0842 0.0494 0.2170 -0.0081 -0.0182 -0.0162 149 LYS A O    
1313 C  CB   . LYS A 148 ? 0.0815 0.0538 0.2060 -0.0054 -0.0209 0.0309  149 LYS A CB   
1314 C  CG   . LYS A 148 ? 0.1635 0.0995 0.2319 0.0082  0.0043  0.0328  149 LYS A CG   
1315 C  CD   . LYS A 148 ? 0.1388 0.1974 0.2752 -0.0034 0.0309  0.0461  149 LYS A CD   
1316 C  CE   . LYS A 148 ? 0.2436 0.2773 0.3443 0.0340  0.0527  0.0608  149 LYS A CE   
1317 N  NZ   . LYS A 148 ? 0.3745 0.4128 0.3898 -0.0776 0.0516  0.0546  149 LYS A NZ   
1318 N  N    . VAL A 149 ? 0.1074 0.0480 0.1954 0.0137  -0.0186 -0.0249 150 VAL A N    
1319 C  CA   . VAL A 149 ? 0.0509 0.0587 0.2073 0.0160  -0.0272 -0.0218 150 VAL A CA   
1320 C  C    . VAL A 149 ? 0.1065 0.0815 0.1967 0.0059  -0.0176 -0.0189 150 VAL A C    
1321 O  O    . VAL A 149 ? 0.1140 0.0846 0.2168 0.0241  -0.0283 0.0115  150 VAL A O    
1322 C  CB   . VAL A 149 ? 0.1061 0.0515 0.1992 0.0164  -0.0071 -0.0087 150 VAL A CB   
1323 C  CG1  . VAL A 149 ? 0.0903 0.1162 0.2064 0.0231  -0.0313 -0.0287 150 VAL A CG1  
1324 C  CG2  . VAL A 149 ? 0.0914 0.1018 0.2468 -0.0533 0.0057  -0.0188 150 VAL A CG2  
1325 N  N    . GLY A 150 ? 0.0927 0.0487 0.1992 -0.0230 -0.0357 -0.0038 151 GLY A N    
1326 C  CA   . GLY A 150 ? 0.1045 0.0799 0.2306 -0.0581 -0.0555 -0.0035 151 GLY A CA   
1327 C  C    . GLY A 150 ? 0.1142 0.0608 0.2170 -0.0441 -0.0200 0.0104  151 GLY A C    
1328 O  O    . GLY A 150 ? 0.1405 0.0731 0.2254 -0.0434 -0.0219 -0.0041 151 GLY A O    
1329 N  N    A SER A 151 ? 0.1606 0.0948 0.2416 -0.0130 -0.0153 0.0098  152 SER A N    
1330 N  N    B SER A 151 ? 0.1574 0.0785 0.2398 -0.0206 -0.0146 0.0010  152 SER A N    
1331 C  CA   A SER A 151 ? 0.1500 0.0983 0.2328 -0.0085 -0.0238 0.0222  152 SER A CA   
1332 C  CA   B SER A 151 ? 0.1322 0.0772 0.2136 -0.0320 -0.0205 0.0154  152 SER A CA   
1333 C  C    A SER A 151 ? 0.1622 0.0715 0.2186 -0.0082 -0.0177 -0.0120 152 SER A C    
1334 C  C    B SER A 151 ? 0.1550 0.0615 0.2053 -0.0293 -0.0148 -0.0059 152 SER A C    
1335 O  O    A SER A 151 ? 0.0853 0.0790 0.2260 0.0086  -0.0326 -0.0226 152 SER A O    
1336 O  O    B SER A 151 ? 0.1676 0.1209 0.1872 -0.0196 -0.0377 -0.0121 152 SER A O    
1337 C  CB   A SER A 151 ? 0.2121 0.1647 0.2326 -0.0242 0.0049  -0.0142 152 SER A CB   
1338 C  CB   B SER A 151 ? 0.1536 0.1038 0.2308 -0.0755 -0.0162 -0.0438 152 SER A CB   
1339 O  OG   A SER A 151 ? 0.1938 0.2172 0.2405 0.0274  0.0186  -0.0489 152 SER A OG   
1340 O  OG   B SER A 151 ? 0.0772 0.1775 0.3034 -0.0705 0.0098  0.0344  152 SER A OG   
1341 N  N    . ALA A 152 ? 0.1539 0.0535 0.1920 -0.0110 -0.0313 -0.0087 153 ALA A N    
1342 C  CA   . ALA A 152 ? 0.1690 0.0427 0.2109 -0.0010 -0.0353 -0.0129 153 ALA A CA   
1343 C  C    . ALA A 152 ? 0.1228 0.0896 0.1926 0.0085  -0.0329 -0.0023 153 ALA A C    
1344 O  O    . ALA A 152 ? 0.1744 0.0878 0.2723 0.0013  -0.0156 -0.0184 153 ALA A O    
1345 C  CB   . ALA A 152 ? 0.2186 0.1252 0.2089 -0.0062 -0.0428 -0.0244 153 ALA A CB   
1346 N  N    A LYS A 153 ? 0.1624 0.0265 0.2207 0.0053  -0.0339 -0.0150 154 LYS A N    
1347 N  N    B LYS A 153 ? 0.1834 0.0334 0.2078 0.0026  -0.0493 0.0006  154 LYS A N    
1348 C  CA   A LYS A 153 ? 0.1509 0.0379 0.1958 0.0121  0.0003  0.0059  154 LYS A CA   
1349 C  CA   B LYS A 153 ? 0.1773 0.0801 0.1746 0.0065  -0.0136 0.0131  154 LYS A CA   
1350 C  C    A LYS A 153 ? 0.0977 0.0697 0.1589 0.0203  0.0000  -0.0254 154 LYS A C    
1351 C  C    B LYS A 153 ? 0.1446 0.0970 0.1611 0.0092  -0.0017 -0.0098 154 LYS A C    
1352 O  O    A LYS A 153 ? 0.1110 0.0627 0.1895 0.0126  0.0162  -0.0007 154 LYS A O    
1353 O  O    B LYS A 153 ? 0.1615 0.1101 0.1360 -0.0230 -0.0087 -0.0241 154 LYS A O    
1354 C  CB   A LYS A 153 ? 0.0952 0.0557 0.1843 -0.0248 0.0248  -0.0302 154 LYS A CB   
1355 C  CB   B LYS A 153 ? 0.1441 0.0860 0.1611 0.0104  -0.0211 -0.0176 154 LYS A CB   
1356 C  CG   A LYS A 153 ? 0.1419 0.0880 0.2017 0.0176  0.0148  -0.0318 154 LYS A CG   
1357 C  CG   B LYS A 153 ? 0.1629 0.1140 0.1647 -0.0115 -0.0041 0.0088  154 LYS A CG   
1358 C  CD   A LYS A 153 ? 0.1877 0.0402 0.2563 -0.0216 0.0251  -0.0554 154 LYS A CD   
1359 C  CD   B LYS A 153 ? 0.1198 0.1333 0.1751 0.0182  0.0119  -0.0204 154 LYS A CD   
1360 C  CE   A LYS A 153 ? 0.0891 0.1036 0.2141 0.0375  0.0225  -0.0218 154 LYS A CE   
1361 C  CE   B LYS A 153 ? 0.1263 0.1798 0.1570 0.0359  0.0104  -0.0065 154 LYS A CE   
1362 N  NZ   A LYS A 153 ? 0.1588 0.1473 0.2874 -0.0489 0.0579  -0.0274 154 LYS A NZ   
1363 N  NZ   B LYS A 153 ? 0.0710 0.2143 0.2046 0.0274  0.0284  -0.0027 154 LYS A NZ   
1364 N  N    A PRO A 154 ? 0.1076 0.0636 0.1539 0.0000  -0.0057 -0.0151 155 PRO A N    
1365 N  N    B PRO A 154 ? 0.1351 0.1074 0.1550 0.0030  0.0161  -0.0183 155 PRO A N    
1366 C  CA   A PRO A 154 ? 0.1092 0.1250 0.1552 -0.0164 0.0049  0.0142  155 PRO A CA   
1367 C  CA   B PRO A 154 ? 0.1151 0.1435 0.1430 0.0049  0.0194  0.0104  155 PRO A CA   
1368 C  C    A PRO A 154 ? 0.0502 0.0970 0.1512 0.0060  0.0102  0.0087  155 PRO A C    
1369 C  C    B PRO A 154 ? 0.1426 0.1428 0.1458 0.0038  -0.0125 0.0098  155 PRO A C    
1370 O  O    A PRO A 154 ? 0.0733 0.1013 0.1775 0.0195  0.0236  0.0337  155 PRO A O    
1371 O  O    B PRO A 154 ? 0.1189 0.1370 0.1658 0.0165  0.0093  -0.0274 155 PRO A O    
1372 C  CB   A PRO A 154 ? 0.0693 0.1259 0.2066 0.0229  0.0207  -0.0007 155 PRO A CB   
1373 C  CB   B PRO A 154 ? 0.1333 0.1295 0.1437 0.0108  -0.0024 0.0109  155 PRO A CB   
1374 C  CG   A PRO A 154 ? 0.1566 0.2026 0.1523 0.0099  0.0057  0.0254  155 PRO A CG   
1375 C  CG   B PRO A 154 ? 0.1597 0.1550 0.1386 0.0174  0.0390  -0.0275 155 PRO A CG   
1376 C  CD   A PRO A 154 ? 0.1635 0.1263 0.1333 -0.0408 -0.0003 0.0035  155 PRO A CD   
1377 C  CD   B PRO A 154 ? 0.1142 0.1040 0.1500 0.0283  0.0430  -0.0119 155 PRO A CD   
1378 N  N    A GLY A 155 ? 0.0797 0.0615 0.1692 -0.0141 0.0115  -0.0093 156 GLY A N    
1379 N  N    B GLY A 155 ? 0.1358 0.0803 0.1505 0.0287  0.0220  0.0076  156 GLY A N    
1380 C  CA   A GLY A 155 ? 0.0797 0.0627 0.1775 -0.0361 0.0285  -0.0003 156 GLY A CA   
1381 C  CA   B GLY A 155 ? 0.1424 0.0927 0.1546 0.0184  0.0288  -0.0098 156 GLY A CA   
1382 C  C    A GLY A 155 ? 0.0894 0.0492 0.1690 -0.0361 0.0174  0.0119  156 GLY A C    
1383 C  C    B GLY A 155 ? 0.1568 0.1164 0.1450 0.0091  0.0293  0.0020  156 GLY A C    
1384 O  O    A GLY A 155 ? 0.1288 0.0361 0.1843 -0.0137 0.0408  0.0074  156 GLY A O    
1385 O  O    B GLY A 155 ? 0.1708 0.1176 0.1640 0.0060  0.0265  0.0147  156 GLY A O    
1386 N  N    A LEU A 156 ? 0.0593 0.0679 0.1518 -0.0062 0.0372  -0.0017 157 LEU A N    
1387 N  N    B LEU A 156 ? 0.1376 0.0668 0.1392 0.0020  0.0085  -0.0043 157 LEU A N    
1388 C  CA   A LEU A 156 ? 0.0828 0.0517 0.1378 -0.0186 0.0263  0.0063  157 LEU A CA   
1389 C  CA   B LEU A 156 ? 0.1360 0.1164 0.1430 0.0049  0.0131  -0.0035 157 LEU A CA   
1390 C  C    A LEU A 156 ? 0.0690 0.0390 0.1455 0.0093  0.0153  -0.0119 157 LEU A C    
1391 C  C    B LEU A 156 ? 0.1232 0.1171 0.1590 -0.0109 0.0175  -0.0097 157 LEU A C    
1392 O  O    A LEU A 156 ? 0.0815 0.0333 0.1728 -0.0163 0.0275  -0.0167 157 LEU A O    
1393 O  O    B LEU A 156 ? 0.1349 0.1225 0.1307 -0.0441 0.0309  0.0007  157 LEU A O    
1394 C  CB   A LEU A 156 ? 0.0781 0.0525 0.1780 -0.0068 0.0238  0.0038  157 LEU A CB   
1395 C  CB   B LEU A 156 ? 0.1553 0.1054 0.1343 -0.0052 0.0171  -0.0175 157 LEU A CB   
1396 C  CG   A LEU A 156 ? 0.0742 0.0925 0.1514 -0.0076 -0.0013 -0.0043 157 LEU A CG   
1397 C  CG   B LEU A 156 ? 0.1137 0.0749 0.1649 -0.0249 0.0511  0.0167  157 LEU A CG   
1398 C  CD1  A LEU A 156 ? 0.0327 0.0695 0.1931 0.0171  0.0048  -0.0175 157 LEU A CD1  
1399 C  CD1  B LEU A 156 ? 0.1115 0.1106 0.1956 0.0035  0.0060  -0.0237 157 LEU A CD1  
1400 C  CD2  A LEU A 156 ? 0.1121 0.0977 0.1431 0.0293  0.0291  -0.0285 157 LEU A CD2  
1401 C  CD2  B LEU A 156 ? 0.1371 0.1081 0.1719 0.0052  0.0115  -0.0098 157 LEU A CD2  
1402 N  N    A GLN A 157 ? 0.0754 0.0621 0.1352 -0.0092 0.0108  -0.0142 158 GLN A N    
1403 N  N    B GLN A 157 ? 0.1502 0.1351 0.1272 -0.0120 0.0146  -0.0054 158 GLN A N    
1404 C  CA   A GLN A 157 ? 0.1036 0.0834 0.1563 -0.0384 0.0017  -0.0035 158 GLN A CA   
1405 C  CA   B GLN A 157 ? 0.1112 0.1458 0.1424 -0.0306 0.0209  -0.0296 158 GLN A CA   
1406 C  C    A GLN A 157 ? 0.1010 0.0700 0.1523 -0.0065 0.0153  -0.0040 158 GLN A C    
1407 C  C    B GLN A 157 ? 0.1536 0.1527 0.1572 -0.0017 0.0178  -0.0081 158 GLN A C    
1408 O  O    A GLN A 157 ? 0.0889 0.0412 0.1690 -0.0065 0.0238  0.0012  158 GLN A O    
1409 O  O    B GLN A 157 ? 0.1671 0.1473 0.1466 -0.0324 0.0219  -0.0307 158 GLN A O    
1410 C  CB   A GLN A 157 ? 0.0939 0.0539 0.1744 -0.0307 0.0167  -0.0227 158 GLN A CB   
1411 C  CB   B GLN A 157 ? 0.1428 0.1505 0.1755 -0.0240 0.0293  -0.0263 158 GLN A CB   
1412 C  CG   A GLN A 157 ? 0.0885 0.1237 0.1685 0.0276  0.0331  -0.0266 158 GLN A CG   
1413 C  CG   B GLN A 157 ? 0.1009 0.1040 0.1629 -0.0722 0.0306  -0.0381 158 GLN A CG   
1414 C  CD   A GLN A 157 ? 0.1225 0.0815 0.1635 0.0183  0.0113  -0.0068 158 GLN A CD   
1415 C  CD   B GLN A 157 ? 0.1771 0.1424 0.1721 -0.0478 0.0302  -0.0086 158 GLN A CD   
1416 O  OE1  A GLN A 157 ? 0.1519 0.0351 0.1847 0.0333  -0.0043 -0.0132 158 GLN A OE1  
1417 O  OE1  B GLN A 157 ? 0.2042 0.1385 0.1879 -0.0414 0.0003  -0.0176 158 GLN A OE1  
1418 N  NE2  A GLN A 157 ? 0.1929 0.0690 0.1545 0.0152  0.0273  -0.0438 158 GLN A NE2  
1419 N  NE2  B GLN A 157 ? 0.1108 0.1586 0.1877 -0.0428 0.0392  -0.0207 158 GLN A NE2  
1420 N  N    A LYS A 158 ? 0.0627 0.0627 0.1751 -0.0167 0.0082  -0.0031 159 LYS A N    
1421 N  N    B LYS A 158 ? 0.1755 0.1690 0.1444 -0.0231 0.0142  -0.0020 159 LYS A N    
1422 C  CA   A LYS A 158 ? 0.1191 0.0828 0.1940 0.0093  -0.0035 -0.0103 159 LYS A CA   
1423 C  CA   B LYS A 158 ? 0.1830 0.1640 0.1577 -0.0104 0.0081  -0.0038 159 LYS A CA   
1424 C  C    A LYS A 158 ? 0.1155 0.0575 0.1552 -0.0034 0.0205  0.0076  159 LYS A C    
1425 C  C    B LYS A 158 ? 0.1938 0.1651 0.1671 -0.0088 0.0043  -0.0006 159 LYS A C    
1426 O  O    A LYS A 158 ? 0.1150 0.0864 0.1489 -0.0582 0.0204  -0.0020 159 LYS A O    
1427 O  O    B LYS A 158 ? 0.2013 0.1884 0.1834 0.0052  -0.0015 -0.0119 159 LYS A O    
1428 C  CB   A LYS A 158 ? 0.0988 0.0440 0.1841 0.0097  -0.0104 0.0126  159 LYS A CB   
1429 C  CB   B LYS A 158 ? 0.2213 0.1956 0.1999 -0.0153 0.0088  0.0208  159 LYS A CB   
1430 C  CG   A LYS A 158 ? 0.1830 0.1927 0.2696 0.0305  0.0093  -0.0006 159 LYS A CG   
1431 C  CG   B LYS A 158 ? 0.2847 0.2741 0.2544 0.0096  0.0153  0.0188  159 LYS A CG   
1432 C  CD   A LYS A 158 ? 0.2342 0.2193 0.2775 0.0531  -0.0151 -0.0006 159 LYS A CD   
1433 C  CD   B LYS A 158 ? 0.2714 0.2685 0.2138 0.0263  -0.0152 0.0166  159 LYS A CD   
1434 C  CE   A LYS A 158 ? 0.2592 0.2680 0.2865 0.0595  -0.0472 0.0041  159 LYS A CE   
1435 C  CE   B LYS A 158 ? 0.2910 0.2469 0.3104 -0.0024 0.0074  0.0220  159 LYS A CE   
1436 N  NZ   A LYS A 158 ? 0.3370 0.2531 0.3740 0.0630  -0.0242 0.0450  159 LYS A NZ   
1437 N  NZ   B LYS A 158 ? 0.3479 0.3115 0.2405 0.0308  -0.0148 0.0230  159 LYS A NZ   
1438 N  N    A VAL A 159 ? 0.0916 0.0519 0.1703 -0.0208 -0.0034 0.0006  160 VAL A N    
1439 N  N    B VAL A 159 ? 0.1694 0.1160 0.1728 0.0140  0.0124  -0.0038 160 VAL A N    
1440 C  CA   A VAL A 159 ? 0.0873 0.0600 0.1453 -0.0182 0.0063  -0.0197 160 VAL A CA   
1441 C  CA   B VAL A 159 ? 0.1672 0.0988 0.1737 0.0164  0.0199  -0.0088 160 VAL A CA   
1442 C  C    A VAL A 159 ? 0.0900 0.0666 0.1351 -0.0199 0.0068  -0.0051 160 VAL A C    
1443 C  C    B VAL A 159 ? 0.1633 0.0825 0.1735 -0.0015 0.0293  -0.0034 160 VAL A C    
1444 O  O    A VAL A 159 ? 0.0945 0.0706 0.1577 -0.0200 0.0110  0.0096  160 VAL A O    
1445 O  O    B VAL A 159 ? 0.1665 0.0799 0.2073 0.0082  0.0379  -0.0159 160 VAL A O    
1446 C  CB   A VAL A 159 ? 0.0997 0.0833 0.1458 0.0052  -0.0041 0.0035  160 VAL A CB   
1447 C  CB   B VAL A 159 ? 0.1787 0.0807 0.1890 0.0136  0.0118  0.0119  160 VAL A CB   
1448 C  CG1  A VAL A 159 ? 0.1101 0.1216 0.1854 0.0206  0.0203  0.0086  160 VAL A CG1  
1449 C  CG1  B VAL A 159 ? 0.1453 0.1492 0.1819 -0.0068 0.0450  -0.0140 160 VAL A CG1  
1450 C  CG2  A VAL A 159 ? 0.0473 0.0580 0.1802 -0.0266 0.0026  -0.0077 160 VAL A CG2  
1451 C  CG2  B VAL A 159 ? 0.2089 0.1076 0.1823 0.0749  0.0274  -0.0093 160 VAL A CG2  
1452 N  N    A VAL A 160 ? 0.0707 0.0385 0.1782 -0.0243 0.0152  -0.0070 161 VAL A N    
1453 N  N    B VAL A 160 ? 0.1683 0.0695 0.1581 -0.0074 0.0271  -0.0113 161 VAL A N    
1454 C  CA   A VAL A 160 ? 0.1133 0.0846 0.1936 -0.0237 0.0120  -0.0131 161 VAL A CA   
1455 C  CA   B VAL A 160 ? 0.1455 0.0598 0.1995 -0.0065 0.0220  0.0063  161 VAL A CA   
1456 C  C    A VAL A 160 ? 0.0979 0.0557 0.1773 -0.0222 0.0156  -0.0222 161 VAL A C    
1457 C  C    B VAL A 160 ? 0.1491 0.0857 0.2008 -0.0052 0.0197  -0.0098 161 VAL A C    
1458 O  O    A VAL A 160 ? 0.0632 0.1185 0.2078 -0.0038 0.0000  -0.0251 161 VAL A O    
1459 O  O    B VAL A 160 ? 0.1694 0.0529 0.1830 0.0143  0.0263  0.0000  161 VAL A O    
1460 C  CB   A VAL A 160 ? 0.0688 0.0299 0.1886 0.0020  0.0120  -0.0263 161 VAL A CB   
1461 C  CB   B VAL A 160 ? 0.2039 0.1101 0.2267 0.0143  0.0322  -0.0120 161 VAL A CB   
1462 C  CG1  A VAL A 160 ? 0.1088 0.1492 0.2502 0.0366  -0.0119 -0.0322 161 VAL A CG1  
1463 C  CG1  B VAL A 160 ? 0.1718 0.0754 0.2402 -0.0855 0.0068  -0.0086 161 VAL A CG1  
1464 C  CG2  A VAL A 160 ? 0.1297 0.1058 0.2272 0.0068  0.0232  -0.0230 161 VAL A CG2  
1465 C  CG2  B VAL A 160 ? 0.2109 0.1011 0.2437 0.0093  0.0237  0.0379  161 VAL A CG2  
1466 N  N    A ASP A 161 ? 0.1223 0.0979 0.1676 -0.0148 0.0080  -0.0262 162 ASP A N    
1467 N  N    B ASP A 161 ? 0.1554 0.1158 0.1676 -0.0261 0.0142  0.0040  162 ASP A N    
1468 C  CA   A ASP A 161 ? 0.1052 0.1004 0.1880 -0.0299 -0.0015 -0.0040 162 ASP A CA   
1469 C  CA   B ASP A 161 ? 0.1620 0.1408 0.1726 -0.0093 0.0093  -0.0204 162 ASP A CA   
1470 C  C    A ASP A 161 ? 0.1097 0.1297 0.1613 -0.0206 0.0153  -0.0027 162 ASP A C    
1471 C  C    B ASP A 161 ? 0.1647 0.1643 0.1765 -0.0120 -0.0070 -0.0041 162 ASP A C    
1472 O  O    A ASP A 161 ? 0.1807 0.1453 0.1920 0.0054  0.0243  -0.0252 162 ASP A O    
1473 O  O    B ASP A 161 ? 0.1721 0.2193 0.2177 -0.0114 0.0065  0.0035  162 ASP A O    
1474 C  CB   A ASP A 161 ? 0.1367 0.1632 0.1658 -0.0232 0.0153  -0.0091 162 ASP A CB   
1475 C  CB   B ASP A 161 ? 0.1999 0.2171 0.1800 -0.0310 0.0003  -0.0194 162 ASP A CB   
1476 C  CG   A ASP A 161 ? 0.1509 0.1450 0.2015 -0.0310 -0.0238 -0.0454 162 ASP A CG   
1477 C  CG   B ASP A 161 ? 0.2840 0.2184 0.2470 -0.0124 -0.0006 -0.0115 162 ASP A CG   
1478 O  OD1  A ASP A 161 ? 0.2567 0.1685 0.2093 -0.0460 -0.0604 -0.0445 162 ASP A OD1  
1479 O  OD1  B ASP A 161 ? 0.3321 0.2179 0.2951 -0.0697 -0.0930 0.0483  162 ASP A OD1  
1480 O  OD2  A ASP A 161 ? 0.2804 0.1898 0.2815 -0.0313 0.0062  0.0310  162 ASP A OD2  
1481 O  OD2  B ASP A 161 ? 0.2321 0.2416 0.2612 -0.1282 -0.0165 -0.0657 162 ASP A OD2  
1482 N  N    A VAL A 162 ? 0.0979 0.0684 0.1899 0.0220  0.0222  -0.0147 163 VAL A N    
1483 N  N    B VAL A 162 ? 0.1582 0.1288 0.1683 -0.0196 -0.0140 -0.0142 163 VAL A N    
1484 C  CA   A VAL A 162 ? 0.0885 0.1045 0.1819 -0.0046 -0.0048 -0.0035 163 VAL A CA   
1485 C  CA   B VAL A 162 ? 0.1861 0.1246 0.1949 -0.0182 -0.0046 0.0054  163 VAL A CA   
1486 C  C    A VAL A 162 ? 0.1092 0.0661 0.1888 0.0087  -0.0038 -0.0006 163 VAL A C    
1487 C  C    B VAL A 162 ? 0.1728 0.1306 0.1701 -0.0086 0.0151  -0.0005 163 VAL A C    
1488 O  O    A VAL A 162 ? 0.1036 0.0853 0.1712 -0.0225 -0.0005 0.0048  163 VAL A O    
1489 O  O    B VAL A 162 ? 0.1230 0.1054 0.1717 -0.0296 0.0285  -0.0037 163 VAL A O    
1490 C  CB   A VAL A 162 ? 0.1455 0.0964 0.2056 0.0274  0.0092  0.0092  163 VAL A CB   
1491 C  CB   B VAL A 162 ? 0.2145 0.1417 0.1940 0.0076  0.0120  0.0037  163 VAL A CB   
1492 C  CG1  A VAL A 162 ? 0.1588 0.0427 0.2128 -0.0041 -0.0252 -0.0076 163 VAL A CG1  
1493 C  CG1  B VAL A 162 ? 0.2177 0.0564 0.2430 -0.0126 0.0054  0.0339  163 VAL A CG1  
1494 C  CG2  A VAL A 162 ? 0.1406 0.1606 0.1933 0.0401  0.0038  0.0230  163 VAL A CG2  
1495 C  CG2  B VAL A 162 ? 0.2145 0.2060 0.2073 -0.0153 0.0126  0.0086  163 VAL A CG2  
1496 N  N    A LEU A 163 ? 0.0882 0.1119 0.1832 0.0062  -0.0137 0.0085  164 LEU A N    
1497 N  N    B LEU A 163 ? 0.1518 0.1173 0.1679 -0.0162 0.0024  -0.0060 164 LEU A N    
1498 C  CA   A LEU A 163 ? 0.0957 0.1018 0.1502 0.0186  -0.0087 0.0081  164 LEU A CA   
1499 C  CA   B LEU A 163 ? 0.1579 0.0991 0.1685 -0.0192 0.0054  0.0175  164 LEU A CA   
1500 C  C    A LEU A 163 ? 0.0927 0.0654 0.1553 0.0276  -0.0049 0.0038  164 LEU A C    
1501 C  C    B LEU A 163 ? 0.1658 0.1385 0.1780 -0.0208 0.0035  0.0074  164 LEU A C    
1502 O  O    A LEU A 163 ? 0.0954 0.0855 0.1732 0.0119  -0.0370 0.0000  164 LEU A O    
1503 O  O    B LEU A 163 ? 0.1658 0.1146 0.2107 -0.0386 0.0046  0.0175  164 LEU A O    
1504 C  CB   A LEU A 163 ? 0.0909 0.0636 0.1676 -0.0239 0.0135  0.0170  164 LEU A CB   
1505 C  CB   B LEU A 163 ? 0.1412 0.0778 0.1541 -0.0096 0.0108  0.0043  164 LEU A CB   
1506 C  CG   A LEU A 163 ? 0.0613 0.0846 0.1491 0.0010  0.0120  0.0164  164 LEU A CG   
1507 C  CG   B LEU A 163 ? 0.1500 0.0593 0.1615 -0.0199 0.0080  0.0131  164 LEU A CG   
1508 C  CD1  A LEU A 163 ? 0.0927 0.1097 0.1936 -0.0226 0.0137  0.0215  164 LEU A CD1  
1509 C  CD1  B LEU A 163 ? 0.1449 0.0934 0.1847 0.0337  0.0137  0.0537  164 LEU A CD1  
1510 C  CD2  A LEU A 163 ? 0.1489 0.1247 0.1798 0.0154  -0.0065 -0.0115 164 LEU A CD2  
1511 C  CD2  B LEU A 163 ? 0.1333 0.0790 0.1827 0.0307  -0.0337 0.0103  164 LEU A CD2  
1512 N  N    A ASP A 164 ? 0.0982 0.0961 0.1703 -0.0113 0.0003  -0.0231 165 ASP A N    
1513 N  N    B ASP A 164 ? 0.2229 0.1212 0.1959 -0.0208 0.0052  0.0143  165 ASP A N    
1514 C  CA   A ASP A 164 ? 0.1493 0.1065 0.1780 -0.0254 -0.0137 -0.0006 165 ASP A CA   
1515 C  CA   B ASP A 164 ? 0.1879 0.1042 0.1732 -0.0020 0.0214  -0.0249 165 ASP A CA   
1516 C  C    A ASP A 164 ? 0.1225 0.1297 0.1881 -0.0297 -0.0188 -0.0131 165 ASP A C    
1517 C  C    B ASP A 164 ? 0.1647 0.1516 0.1291 0.0153  0.0049  0.0031  165 ASP A C    
1518 O  O    A ASP A 164 ? 0.1342 0.1509 0.1920 -0.0093 -0.0153 -0.0206 165 ASP A O    
1519 O  O    B ASP A 164 ? 0.2189 0.1561 0.1847 0.0076  0.0436  0.0020  165 ASP A O    
1520 C  CB   A ASP A 164 ? 0.0957 0.1376 0.1841 0.0263  -0.0087 -0.0175 165 ASP A CB   
1521 C  CB   B ASP A 164 ? 0.2497 0.1992 0.1800 0.0254  -0.0076 -0.0228 165 ASP A CB   
1522 C  CG   A ASP A 164 ? 0.2319 0.1769 0.2189 0.0359  -0.0361 0.0000  165 ASP A CG   
1523 C  CG   B ASP A 164 ? 0.2245 0.2242 0.2296 0.0403  -0.0052 -0.0467 165 ASP A CG   
1524 O  OD1  A ASP A 164 ? 0.2712 0.2265 0.2538 0.0619  -0.0148 0.0027  165 ASP A OD1  
1525 O  OD1  B ASP A 164 ? 0.2380 0.1787 0.2100 0.0087  0.0015  -0.0599 165 ASP A OD1  
1526 O  OD2  A ASP A 164 ? 0.3179 0.2883 0.2973 0.0494  0.0074  0.0052  165 ASP A OD2  
1527 O  OD2  B ASP A 164 ? 0.3226 0.4221 0.2412 0.0494  0.0087  -0.0230 165 ASP A OD2  
1528 N  N    A SER A 165 ? 0.1225 0.1020 0.1732 -0.0222 -0.0313 -0.0119 166 SER A N    
1529 N  N    B SER A 165 ? 0.1990 0.1180 0.1812 -0.0171 -0.0074 0.0031  166 SER A N    
1530 C  CA   A SER A 165 ? 0.0785 0.1167 0.1852 0.0020  -0.0137 0.0074  166 SER A CA   
1531 C  CA   B SER A 165 ? 0.1870 0.1218 0.1811 0.0046  -0.0115 0.0164  166 SER A CA   
1532 C  C    A SER A 165 ? 0.1040 0.0925 0.1624 -0.0193 0.0000  -0.0038 166 SER A C    
1533 C  C    B SER A 165 ? 0.1873 0.1252 0.1944 -0.0076 0.0015  0.0074  166 SER A C    
1534 O  O    A SER A 165 ? 0.0939 0.0819 0.1868 0.0006  -0.0120 0.0474  166 SER A O    
1535 O  O    B SER A 165 ? 0.1913 0.1186 0.1884 -0.0141 0.0359  0.0384  166 SER A O    
1536 C  CB   A SER A 165 ? 0.0873 0.1083 0.2080 0.0020  0.0161  0.0077  166 SER A CB   
1537 C  CB   B SER A 165 ? 0.1757 0.1574 0.2053 0.0043  -0.0059 0.0165  166 SER A CB   
1538 O  OG   A SER A 165 ? 0.0995 0.1678 0.2240 -0.0293 -0.0243 0.0166  166 SER A OG   
1539 O  OG   B SER A 165 ? 0.2030 0.1593 0.2260 0.0419  0.0063  0.0317  166 SER A OG   
1540 N  N    A ILE A 166 ? 0.0842 0.0431 0.1383 -0.0023 -0.0285 0.0114  167 ILE A N    
1541 N  N    B ILE A 166 ? 0.1758 0.1532 0.1509 0.0129  -0.0007 0.0129  167 ILE A N    
1542 C  CA   A ILE A 166 ? 0.0907 0.0427 0.1439 -0.0104 0.0115  0.0317  167 ILE A CA   
1543 C  CA   B ILE A 166 ? 0.1336 0.1403 0.1839 0.0003  -0.0104 0.0232  167 ILE A CA   
1544 C  C    A ILE A 166 ? 0.0684 0.0411 0.1532 -0.0107 0.0098  0.0003  167 ILE A C    
1545 C  C    B ILE A 166 ? 0.1368 0.1047 0.1545 -0.0156 0.0000  -0.0010 167 ILE A C    
1546 O  O    A ILE A 166 ? 0.0306 0.0758 0.1448 0.0031  0.0035  0.0258  167 ILE A O    
1547 O  O    B ILE A 166 ? 0.1410 0.1347 0.1532 -0.0143 -0.0040 0.0043  167 ILE A O    
1548 C  CB   A ILE A 166 ? 0.0785 0.0534 0.1117 -0.0046 -0.0034 -0.0241 167 ILE A CB   
1549 C  CB   B ILE A 166 ? 0.1494 0.1575 0.1550 -0.0137 -0.0137 0.0288  167 ILE A CB   
1550 C  CG1  A ILE A 166 ? 0.1083 0.0873 0.1304 -0.0020 0.0206  -0.0082 167 ILE A CG1  
1551 C  CG1  B ILE A 166 ? 0.1836 0.1547 0.1509 0.0153  0.0439  0.0109  167 ILE A CG1  
1552 C  CG2  A ILE A 166 ? 0.0552 0.0430 0.1717 0.0051  0.0007  0.0199  167 ILE A CG2  
1553 C  CG2  B ILE A 166 ? 0.1764 0.1832 0.1899 -0.0013 -0.0057 0.0251  167 ILE A CG2  
1554 C  CD1  A ILE A 166 ? 0.2143 0.0984 0.1668 -0.0003 -0.0115 -0.0093 167 ILE A CD1  
1555 C  CD1  B ILE A 166 ? 0.1653 0.0706 0.1519 0.0274  -0.0326 0.0185  167 ILE A CD1  
1556 N  N    A LYS A 167 ? 0.0598 0.0873 0.1536 0.0198  0.0017  -0.0104 168 LYS A N    
1557 N  N    B LYS A 167 ? 0.1464 0.1042 0.1931 -0.0285 0.0031  -0.0049 168 LYS A N    
1558 C  CA   A LYS A 167 ? 0.0904 0.0778 0.1671 0.0041  -0.0219 -0.0023 168 LYS A CA   
1559 C  CA   B LYS A 167 ? 0.1638 0.1054 0.1992 -0.0164 0.0156  -0.0131 168 LYS A CA   
1560 C  C    A LYS A 167 ? 0.0807 0.0571 0.1604 0.0288  -0.0164 -0.0186 168 LYS A C    
1561 C  C    B LYS A 167 ? 0.1631 0.0975 0.1647 -0.0309 0.0238  -0.0258 168 LYS A C    
1562 O  O    A LYS A 167 ? 0.0589 0.0508 0.1708 0.0059  0.0159  -0.0006 168 LYS A O    
1563 O  O    B LYS A 167 ? 0.1308 0.0702 0.1620 -0.0298 0.0518  -0.0195 168 LYS A O    
1564 C  CB   A LYS A 167 ? 0.1072 0.1054 0.1728 -0.0172 -0.0093 -0.0266 168 LYS A CB   
1565 C  CB   B LYS A 167 ? 0.2125 0.0819 0.1905 -0.0217 -0.0049 -0.0233 168 LYS A CB   
1566 C  CG   A LYS A 167 ? 0.2005 0.1176 0.2017 0.0000  0.0165  -0.0186 168 LYS A CG   
1567 C  CG   B LYS A 167 ? 0.2430 0.0806 0.2466 -0.0124 -0.0043 -0.0210 168 LYS A CG   
1568 C  CD   A LYS A 167 ? 0.2170 0.0925 0.2340 -0.0137 -0.0143 -0.0255 168 LYS A CD   
1569 C  CD   B LYS A 167 ? 0.2145 0.2042 0.2214 -0.0020 0.0434  -0.0412 168 LYS A CD   
1570 C  CE   A LYS A 167 ? 0.2480 0.1748 0.2845 0.0054  -0.0099 -0.0917 168 LYS A CE   
1571 C  CE   B LYS A 167 ? 0.2788 0.2451 0.2856 0.0041  0.0051  -0.0230 168 LYS A CE   
1572 N  NZ   A LYS A 167 ? 0.1841 0.2831 0.4211 0.0776  0.0197  -0.0383 168 LYS A NZ   
1573 N  NZ   B LYS A 167 ? 0.2750 0.2721 0.2617 -0.0305 -0.0161 -0.0763 168 LYS A NZ   
1574 N  N    A THR A 168 ? 0.0513 0.0440 0.1448 0.0219  -0.0015 0.0010  169 THR A N    
1575 N  N    B THR A 168 ? 0.1550 0.0835 0.1476 -0.0653 0.0237  -0.0188 169 THR A N    
1576 C  CA   A THR A 168 ? 0.0547 0.0661 0.1353 -0.0038 0.0048  0.0135  169 THR A CA   
1577 C  CA   B THR A 168 ? 0.1729 0.1022 0.1884 -0.0038 0.0193  -0.0275 169 THR A CA   
1578 C  C    A THR A 168 ? 0.0395 0.0476 0.1604 0.0174  0.0049  -0.0051 169 THR A C    
1579 C  C    B THR A 168 ? 0.1764 0.1160 0.1744 -0.0460 0.0208  0.0049  169 THR A C    
1580 O  O    A THR A 168 ? 0.0354 0.0442 0.1917 0.0132  0.0217  0.0161  169 THR A O    
1581 O  O    B THR A 168 ? 0.1592 0.0860 0.2125 -0.0549 0.0167  0.0098  169 THR A O    
1582 C  CB   A THR A 168 ? 0.0617 0.0837 0.1746 0.0120  -0.0070 0.0086  169 THR A CB   
1583 C  CB   B THR A 168 ? 0.1611 0.1399 0.1704 0.0040  0.0159  -0.0183 169 THR A CB   
1584 O  OG1  A THR A 168 ? 0.0437 0.1090 0.1487 0.0124  0.0076  0.0317  169 THR A OG1  
1585 O  OG1  B THR A 168 ? 0.2227 0.1297 0.1712 0.0010  0.0390  -0.0109 169 THR A OG1  
1586 C  CG2  A THR A 168 ? 0.0869 0.0512 0.1773 0.0146  0.0206  -0.0054 169 THR A CG2  
1587 C  CG2  B THR A 168 ? 0.2150 0.0738 0.2574 -0.0340 0.0276  -0.0024 169 THR A CG2  
1588 N  N    A LYS A 169 ? 0.0885 0.0599 0.1317 -0.0298 0.0129  0.0104  170 LYS A N    
1589 N  N    B LYS A 169 ? 0.1297 0.0794 0.2096 -0.0368 0.0221  0.0076  170 LYS A N    
1590 C  CA   A LYS A 169 ? 0.0623 0.0361 0.1397 -0.0104 0.0281  0.0031  170 LYS A CA   
1591 C  CA   B LYS A 169 ? 0.1575 0.0921 0.2048 -0.0296 0.0000  0.0172  170 LYS A CA   
1592 C  C    A LYS A 169 ? 0.0706 0.0505 0.1561 -0.0038 0.0074  -0.0024 170 LYS A C    
1593 C  C    B LYS A 169 ? 0.1482 0.1203 0.1872 -0.0206 0.0024  0.0073  170 LYS A C    
1594 O  O    A LYS A 169 ? 0.0722 0.0688 0.1751 0.0252  0.0143  -0.0074 170 LYS A O    
1595 O  O    B LYS A 169 ? 0.1545 0.1494 0.1945 0.0062  0.0324  0.0215  170 LYS A O    
1596 C  CB   A LYS A 169 ? 0.0436 0.0399 0.1378 -0.0097 0.0162  0.0219  170 LYS A CB   
1597 C  CB   B LYS A 169 ? 0.1776 0.1196 0.1798 -0.0248 0.0030  0.0188  170 LYS A CB   
1598 C  CG   A LYS A 169 ? 0.1191 0.0930 0.1717 -0.0020 -0.0209 0.0160  170 LYS A CG   
1599 C  CG   B LYS A 169 ? 0.1595 0.1076 0.1893 -0.0082 -0.0052 0.0093  170 LYS A CG   
1600 C  CD   A LYS A 169 ? 0.0557 0.1306 0.2159 -0.0126 0.0166  -0.0068 170 LYS A CD   
1601 C  CD   B LYS A 169 ? 0.1778 0.1390 0.2538 -0.0564 0.0183  0.0421  170 LYS A CD   
1602 C  CE   A LYS A 169 ? 0.1498 0.1807 0.2628 0.0406  0.0474  0.0274  170 LYS A CE   
1603 C  CE   B LYS A 169 ? 0.1978 0.2529 0.2933 -0.0582 0.0425  0.0522  170 LYS A CE   
1604 N  NZ   A LYS A 169 ? 0.2578 0.2170 0.2739 0.0151  -0.0172 -0.0099 170 LYS A NZ   
1605 N  NZ   B LYS A 169 ? 0.2175 0.3497 0.4347 -0.0476 0.0163  0.0115  170 LYS A NZ   
1606 N  N    A GLY A 170 ? 0.0639 0.0702 0.1640 -0.0048 0.0206  0.0098  171 GLY A N    
1607 N  N    B GLY A 170 ? 0.1324 0.0995 0.1834 -0.0175 -0.0010 0.0060  171 GLY A N    
1608 C  CA   A GLY A 170 ? 0.0943 0.0548 0.1787 0.0324  -0.0017 0.0187  171 GLY A CA   
1609 C  CA   B GLY A 170 ? 0.1651 0.1288 0.1837 -0.0348 -0.0010 0.0242  171 GLY A CA   
1610 C  C    A GLY A 170 ? 0.0939 0.1214 0.1764 0.0152  0.0120  0.0259  171 GLY A C    
1611 C  C    B GLY A 170 ? 0.1719 0.1247 0.1839 -0.0041 0.0063  0.0099  171 GLY A C    
1612 O  O    A GLY A 170 ? 0.1081 0.0666 0.2109 -0.0151 0.0085  0.0467  171 GLY A O    
1613 O  O    B GLY A 170 ? 0.1780 0.1343 0.2243 -0.0322 0.0379  0.0263  171 GLY A O    
1614 N  N    A LYS A 171 ? 0.0806 0.0469 0.1556 0.0142  -0.0063 0.0147  172 LYS A N    
1615 N  N    B LYS A 171 ? 0.1579 0.1158 0.1401 -0.0351 -0.0104 0.0041  172 LYS A N    
1616 C  CA   A LYS A 171 ? 0.0837 0.0860 0.1342 0.0302  0.0172  0.0208  172 LYS A CA   
1617 C  CA   B LYS A 171 ? 0.1974 0.1340 0.1340 -0.0097 0.0109  -0.0188 172 LYS A CA   
1618 C  C    A LYS A 171 ? 0.0529 0.0736 0.1726 0.0192  0.0065  0.0130  172 LYS A C    
1619 C  C    B LYS A 171 ? 0.2017 0.1324 0.1360 -0.0098 0.0041  0.0006  172 LYS A C    
1620 O  O    A LYS A 171 ? 0.0328 0.0772 0.1890 0.0147  -0.0137 0.0065  172 LYS A O    
1621 O  O    B LYS A 171 ? 0.2021 0.1176 0.1568 -0.0027 0.0266  0.0120  172 LYS A O    
1622 C  CB   A LYS A 171 ? 0.0537 0.0988 0.1877 0.0454  0.0157  0.0161  172 LYS A CB   
1623 C  CB   B LYS A 171 ? 0.1712 0.1288 0.1744 -0.0307 -0.0198 -0.0252 172 LYS A CB   
1624 C  CG   A LYS A 171 ? 0.0710 0.1221 0.1794 0.0359  -0.0092 -0.0274 172 LYS A CG   
1625 C  CG   B LYS A 171 ? 0.2441 0.1194 0.2152 0.0263  0.0124  -0.0662 172 LYS A CG   
1626 C  CD   A LYS A 171 ? 0.1487 0.1768 0.1764 0.0184  0.0126  -0.0073 172 LYS A CD   
1627 C  CD   B LYS A 171 ? 0.2599 0.1949 0.2186 -0.0274 0.0096  -0.0208 172 LYS A CD   
1628 C  CE   A LYS A 171 ? 0.1920 0.1931 0.1739 0.0000  -0.0054 0.0261  172 LYS A CE   
1629 C  CE   B LYS A 171 ? 0.3594 0.2348 0.2046 0.0142  0.0006  -0.0456 172 LYS A CE   
1630 N  NZ   A LYS A 171 ? 0.1780 0.1771 0.2005 0.0287  0.0362  -0.0049 172 LYS A NZ   
1631 N  NZ   B LYS A 171 ? 0.3596 0.3217 0.2933 -0.0287 -0.0068 -0.0465 172 LYS A NZ   
1632 N  N    A SER A 172 ? 0.0496 0.0864 0.1649 0.0252  -0.0015 -0.0049 173 SER A N    
1633 N  N    B SER A 172 ? 0.1811 0.1439 0.1507 0.0003  0.0155  0.0074  173 SER A N    
1634 C  CA   A SER A 172 ? 0.0573 0.1333 0.1311 0.0076  0.0006  0.0262  173 SER A CA   
1635 C  CA   B SER A 172 ? 0.1809 0.0974 0.1187 -0.0093 0.0074  -0.0131 173 SER A CA   
1636 C  C    A SER A 172 ? 0.0375 0.1067 0.1482 0.0272  0.0065  0.0121  173 SER A C    
1637 C  C    B SER A 172 ? 0.2037 0.0769 0.1536 -0.0143 0.0054  -0.0080 173 SER A C    
1638 O  O    A SER A 172 ? 0.0663 0.1579 0.1768 0.0220  0.0048  0.0264  173 SER A O    
1639 O  O    B SER A 172 ? 0.2243 0.1286 0.1446 0.0377  0.0186  0.0142  173 SER A O    
1640 C  CB   A SER A 172 ? 0.0324 0.1345 0.1563 0.0173  -0.0274 -0.0275 173 SER A CB   
1641 C  CB   B SER A 172 ? 0.2193 0.0898 0.1746 -0.0322 0.0185  0.0098  173 SER A CB   
1642 O  OG   A SER A 172 ? 0.0970 0.1920 0.2218 0.0208  -0.0286 0.0649  173 SER A OG   
1643 O  OG   B SER A 172 ? 0.2139 0.0939 0.1863 -0.0193 0.0182  0.0410  173 SER A OG   
1644 N  N    A ALA A 173 ? 0.0494 0.1263 0.1525 -0.0048 0.0126  0.0043  174 ALA A N    
1645 N  N    B ALA A 173 ? 0.1972 0.1074 0.1507 0.0000  0.0041  0.0087  174 ALA A N    
1646 C  CA   A ALA A 173 ? 0.0505 0.0855 0.1732 -0.0285 -0.0115 0.0197  174 ALA A CA   
1647 C  CA   B ALA A 173 ? 0.2028 0.1117 0.1746 -0.0068 -0.0020 -0.0124 174 ALA A CA   
1648 C  C    A ALA A 173 ? 0.0675 0.0754 0.1812 -0.0458 -0.0097 0.0174  174 ALA A C    
1649 C  C    B ALA A 173 ? 0.2042 0.1507 0.1611 0.0077  0.0043  0.0052  174 ALA A C    
1650 O  O    A ALA A 173 ? 0.0741 0.0625 0.1451 -0.0419 -0.0161 0.0245  174 ALA A O    
1651 O  O    B ALA A 173 ? 0.2542 0.1089 0.1261 0.0164  -0.0080 0.0229  174 ALA A O    
1652 C  CB   A ALA A 173 ? 0.1042 0.0864 0.2117 -0.0331 0.0046  -0.0013 174 ALA A CB   
1653 C  CB   B ALA A 173 ? 0.1665 0.1171 0.1870 -0.0606 0.0088  -0.0205 174 ALA A CB   
1654 N  N    A ASP A 174 ? 0.0654 0.1196 0.1755 -0.0487 -0.0392 0.0293  175 ASP A N    
1655 N  N    B ASP A 174 ? 0.2193 0.1593 0.1625 -0.0027 -0.0286 0.0109  175 ASP A N    
1656 C  CA   A ASP A 174 ? 0.0778 0.1006 0.1701 -0.0450 -0.0063 0.0390  175 ASP A CA   
1657 C  CA   B ASP A 174 ? 0.2114 0.1485 0.1399 -0.0170 -0.0331 0.0430  175 ASP A CA   
1658 C  C    A ASP A 174 ? 0.0722 0.1164 0.1843 -0.0399 -0.0060 0.0260  175 ASP A C    
1659 C  C    B ASP A 174 ? 0.2135 0.1775 0.1820 -0.0135 -0.0416 0.0137  175 ASP A C    
1660 O  O    A ASP A 174 ? 0.1024 0.0995 0.2064 -0.0046 -0.0030 -0.0142 175 ASP A O    
1661 O  O    B ASP A 174 ? 0.2071 0.1570 0.1962 -0.0098 -0.0480 0.0031  175 ASP A O    
1662 C  CB   A ASP A 174 ? 0.1437 0.1340 0.2306 -0.0243 -0.0277 0.0511  175 ASP A CB   
1663 C  CB   B ASP A 174 ? 0.2658 0.2171 0.1881 -0.0339 -0.0364 0.0296  175 ASP A CB   
1664 C  CG   A ASP A 174 ? 0.1047 0.1789 0.2039 -0.0471 -0.0688 0.0557  175 ASP A CG   
1665 C  CG   B ASP A 174 ? 0.2939 0.2444 0.2614 0.0175  -0.0566 0.0505  175 ASP A CG   
1666 O  OD1  A ASP A 174 ? 0.2452 0.3009 0.2513 -0.0593 -0.1067 0.0031  175 ASP A OD1  
1667 O  OD1  B ASP A 174 ? 0.4189 0.2888 0.3199 0.0384  -0.0359 0.0060  175 ASP A OD1  
1668 O  OD2  A ASP A 174 ? 0.1809 0.2114 0.1572 -0.0979 -0.0368 0.0526  175 ASP A OD2  
1669 O  OD2  B ASP A 174 ? 0.4020 0.3161 0.3088 -0.0186 -0.0005 -0.0048 175 ASP A OD2  
1670 N  N    A PHE A 175 ? 0.0441 0.1106 0.1640 -0.0109 0.0012  0.0260  176 PHE A N    
1671 N  N    B PHE A 175 ? 0.1944 0.1182 0.1561 -0.0136 -0.0049 0.0186  176 PHE A N    
1672 C  CA   A PHE A 175 ? 0.0351 0.1300 0.1414 -0.0043 0.0172  0.0107  176 PHE A CA   
1673 C  CA   B PHE A 175 ? 0.1796 0.1419 0.1732 -0.0077 -0.0339 0.0073  176 PHE A CA   
1674 C  C    A PHE A 175 ? 0.0476 0.0954 0.1435 -0.0339 0.0175  0.0174  176 PHE A C    
1675 C  C    B PHE A 175 ? 0.1703 0.1279 0.1825 -0.0166 -0.0183 0.0103  176 PHE A C    
1676 O  O    A PHE A 175 ? 0.0923 0.1194 0.1751 -0.0240 -0.0088 0.0076  176 PHE A O    
1677 O  O    B PHE A 175 ? 0.1527 0.1423 0.1816 -0.0124 -0.0193 0.0165  176 PHE A O    
1678 C  CB   A PHE A 175 ? 0.0727 0.0788 0.1538 -0.0293 0.0210  0.0017  176 PHE A CB   
1679 C  CB   B PHE A 175 ? 0.1757 0.0639 0.1872 0.0331  -0.0208 0.0230  176 PHE A CB   
1680 C  CG   A PHE A 175 ? 0.0939 0.0830 0.1683 -0.0142 0.0148  -0.0006 176 PHE A CG   
1681 C  CG   B PHE A 175 ? 0.1176 0.0722 0.1826 0.0260  -0.0081 0.0068  176 PHE A CG   
1682 C  CD1  A PHE A 175 ? 0.1491 0.0431 0.1568 -0.0093 0.0309  0.0114  176 PHE A CD1  
1683 C  CD1  B PHE A 175 ? 0.1775 0.0754 0.1958 0.0171  0.0151  0.0175  176 PHE A CD1  
1684 C  CD2  A PHE A 175 ? 0.0577 0.0431 0.1880 0.0238  0.0108  0.0017  176 PHE A CD2  
1685 C  CD2  B PHE A 175 ? 0.1721 0.1124 0.1841 -0.0171 0.0103  0.0255  176 PHE A CD2  
1686 C  CE1  A PHE A 175 ? 0.1430 0.0756 0.1899 0.0013  0.0529  0.0013  176 PHE A CE1  
1687 C  CE1  B PHE A 175 ? 0.1171 0.0842 0.2143 0.0339  -0.0019 0.0017  176 PHE A CE1  
1688 C  CE2  A PHE A 175 ? 0.0711 0.0819 0.1996 -0.0073 0.0030  0.0164  176 PHE A CE2  
1689 C  CE2  B PHE A 175 ? 0.1230 0.0679 0.1981 0.0458  -0.0006 0.0272  176 PHE A CE2  
1690 C  CZ   A PHE A 175 ? 0.1033 0.0679 0.1604 0.0176  0.0469  -0.0109 176 PHE A CZ   
1691 C  CZ   B PHE A 175 ? 0.1708 0.0681 0.1775 -0.0241 -0.0211 -0.0031 176 PHE A CZ   
1692 N  N    A THR A 176 ? 0.0894 0.1124 0.1744 0.0115  0.0006  0.0164  177 THR A N    
1693 N  N    B THR A 176 ? 0.1234 0.0675 0.1895 -0.0015 -0.0131 0.0131  177 THR A N    
1694 C  CA   A THR A 176 ? 0.1128 0.1027 0.1719 0.0049  0.0038  0.0222  177 THR A CA   
1695 C  CA   B THR A 176 ? 0.1581 0.1250 0.2023 0.0118  -0.0185 0.0146  177 THR A CA   
1696 C  C    A THR A 176 ? 0.1024 0.0842 0.1613 0.0295  0.0093  0.0073  177 THR A C    
1697 C  C    B THR A 176 ? 0.1500 0.1270 0.1701 0.0068  -0.0339 0.0013  177 THR A C    
1698 O  O    A THR A 176 ? 0.0693 0.0979 0.1823 0.0155  0.0208  0.0130  177 THR A O    
1699 O  O    B THR A 176 ? 0.1288 0.1076 0.2010 -0.0183 -0.0219 0.0155  177 THR A O    
1700 C  CB   A THR A 176 ? 0.1230 0.1338 0.1796 -0.0174 0.0288  0.0335  177 THR A CB   
1701 C  CB   B THR A 176 ? 0.1151 0.0837 0.1902 0.0355  -0.0447 0.0185  177 THR A CB   
1702 O  OG1  A THR A 176 ? 0.1437 0.1386 0.1613 0.0401  0.0188  0.0252  177 THR A OG1  
1703 O  OG1  B THR A 176 ? 0.1751 0.1430 0.2013 0.0038  0.0109  0.0175  177 THR A OG1  
1704 C  CG2  A THR A 176 ? 0.1083 0.1387 0.2815 0.0063  0.0307  0.0434  177 THR A CG2  
1705 C  CG2  B THR A 176 ? 0.1162 0.1676 0.2304 0.0414  -0.0160 0.0364  177 THR A CG2  
1706 N  N    A ASN A 177 ? 0.1223 0.0715 0.1694 0.0230  -0.0020 0.0239  178 ASN A N    
1707 N  N    B ASN A 177 ? 0.1960 0.1029 0.1556 0.0137  -0.0348 -0.0038 178 ASN A N    
1708 C  CA   A ASN A 177 ? 0.1649 0.0518 0.1705 0.0204  -0.0119 -0.0006 178 ASN A CA   
1709 C  CA   B ASN A 177 ? 0.2150 0.0900 0.1448 -0.0005 -0.0259 -0.0165 178 ASN A CA   
1710 C  C    A ASN A 177 ? 0.1999 0.1079 0.1647 -0.0203 -0.0197 0.0135  178 ASN A C    
1711 C  C    B ASN A 177 ? 0.2229 0.1150 0.1665 0.0131  -0.0478 -0.0177 178 ASN A C    
1712 O  O    A ASN A 177 ? 0.1908 0.1223 0.1599 0.0059  -0.0276 0.0082  178 ASN A O    
1713 O  O    B ASN A 177 ? 0.2703 0.1243 0.1617 0.0137  -0.0502 0.0373  178 ASN A O    
1714 C  CB   A ASN A 177 ? 0.1875 0.0799 0.1852 -0.0109 -0.0065 0.0434  178 ASN A CB   
1715 C  CB   B ASN A 177 ? 0.1884 0.1067 0.1922 0.0065  -0.0063 0.0489  178 ASN A CB   
1716 C  CG   A ASN A 177 ? 0.1512 0.1608 0.2177 0.0406  -0.0373 0.0073  178 ASN A CG   
1717 C  CG   B ASN A 177 ? 0.2017 0.1421 0.2089 -0.0052 -0.0383 0.0229  178 ASN A CG   
1718 O  OD1  A ASN A 177 ? 0.1751 0.1890 0.2416 0.0623  -0.0271 -0.0031 178 ASN A OD1  
1719 O  OD1  B ASN A 177 ? 0.2202 0.0718 0.2495 -0.0372 -0.0549 0.0388  178 ASN A OD1  
1720 N  ND2  A ASN A 177 ? 0.2515 0.0553 0.1922 0.0171  -0.0361 0.0306  178 ASN A ND2  
1721 N  ND2  B ASN A 177 ? 0.2793 0.1665 0.1978 -0.0344 -0.0904 0.0731  178 ASN A ND2  
1722 N  N    . PHE A 178 ? 0.2694 0.0463 0.1870 0.0153  -0.0500 0.0071  179 PHE A N    
1723 C  CA   . PHE A 178 ? 0.2766 0.0830 0.1880 0.0068  -0.0469 0.0412  179 PHE A CA   
1724 C  C    . PHE A 178 ? 0.2444 0.0866 0.1829 0.0274  -0.0439 0.0148  179 PHE A C    
1725 O  O    . PHE A 178 ? 0.2946 0.1054 0.2078 0.0076  -0.0662 0.0062  179 PHE A O    
1726 C  CB   . PHE A 178 ? 0.2784 0.0970 0.1872 0.0024  -0.0373 0.0357  179 PHE A CB   
1727 C  CG   . PHE A 178 ? 0.2597 0.0474 0.2078 0.0046  -0.0263 0.0315  179 PHE A CG   
1728 C  CD1  . PHE A 178 ? 0.3055 0.0704 0.1987 -0.0342 -0.0518 0.0254  179 PHE A CD1  
1729 C  CD2  . PHE A 178 ? 0.2005 0.0961 0.1721 -0.0220 -0.0410 0.0167  179 PHE A CD2  
1730 C  CE1  . PHE A 178 ? 0.2648 0.0494 0.2195 0.0432  -0.0228 0.0222  179 PHE A CE1  
1731 C  CE2  . PHE A 178 ? 0.2017 0.0754 0.1719 -0.0024 -0.0240 0.0186  179 PHE A CE2  
1732 C  CZ   . PHE A 178 ? 0.2469 0.0880 0.1902 0.0065  -0.0524 0.0200  179 PHE A CZ   
1733 N  N    . ASP A 179 ? 0.2096 0.1186 0.2046 0.0141  -0.0489 0.0175  180 ASP A N    
1734 C  CA   . ASP A 179 ? 0.1826 0.1168 0.2046 0.0153  -0.0527 0.0085  180 ASP A CA   
1735 C  C    . ASP A 179 ? 0.1866 0.0934 0.1879 -0.0173 -0.0606 0.0054  180 ASP A C    
1736 O  O    . ASP A 179 ? 0.2041 0.0769 0.2200 -0.0208 -0.0403 -0.0088 180 ASP A O    
1737 C  CB   . ASP A 179 ? 0.2085 0.1726 0.2017 0.0017  -0.0767 0.0109  180 ASP A CB   
1738 C  CG   . ASP A 179 ? 0.1465 0.1999 0.2676 0.0148  -0.0307 0.0174  180 ASP A CG   
1739 O  OD1  . ASP A 179 ? 0.2012 0.1198 0.2633 0.0062  -0.0403 0.0305  180 ASP A OD1  
1740 O  OD2  . ASP A 179 ? 0.2010 0.3540 0.3298 -0.0087 -0.0527 0.0087  180 ASP A OD2  
1741 N  N    . PRO A 180 ? 0.1608 0.0736 0.2085 0.0000  -0.0590 0.0280  181 PRO A N    
1742 C  CA   . PRO A 180 ? 0.1412 0.0916 0.2186 -0.0260 -0.0359 0.0147  181 PRO A CA   
1743 C  C    . PRO A 180 ? 0.1498 0.0898 0.1992 0.0131  -0.0164 0.0192  181 PRO A C    
1744 O  O    . PRO A 180 ? 0.1704 0.0643 0.2012 -0.0222 -0.0544 0.0250  181 PRO A O    
1745 C  CB   . PRO A 180 ? 0.1299 0.0993 0.2529 -0.0087 -0.0390 -0.0153 181 PRO A CB   
1746 C  CG   . PRO A 180 ? 0.1527 0.1076 0.2283 -0.0074 -0.0467 0.0085  181 PRO A CG   
1747 C  CD   . PRO A 180 ? 0.1654 0.0706 0.2175 -0.0414 -0.0754 0.0147  181 PRO A CD   
1748 N  N    . ARG A 181 ? 0.1106 0.0834 0.1987 0.0153  -0.0082 0.0071  182 ARG A N    
1749 C  CA   . ARG A 181 ? 0.1579 0.0769 0.2199 0.0198  -0.0185 0.0121  182 ARG A CA   
1750 C  C    . ARG A 181 ? 0.1746 0.1225 0.2206 0.0531  -0.0318 0.0255  182 ARG A C    
1751 O  O    . ARG A 181 ? 0.1778 0.0979 0.2470 -0.0010 -0.0474 0.0146  182 ARG A O    
1752 C  CB   . ARG A 181 ? 0.1358 0.1308 0.2448 0.0003  -0.0060 -0.0017 182 ARG A CB   
1753 C  CG   . ARG A 181 ? 0.1690 0.1036 0.2412 0.0109  -0.0219 0.0048  182 ARG A CG   
1754 C  CD   . ARG A 181 ? 0.1426 0.1406 0.3039 0.0108  -0.0070 0.0197  182 ARG A CD   
1755 N  NE   . ARG A 181 ? 0.1164 0.1110 0.3601 0.0052  -0.0447 0.0500  182 ARG A NE   
1756 C  CZ   . ARG A 181 ? 0.2039 0.2033 0.3273 0.0006  -0.0017 0.0566  182 ARG A CZ   
1757 N  NH1  . ARG A 181 ? 0.2716 0.2283 0.3759 0.0171  0.0710  0.0527  182 ARG A NH1  
1758 N  NH2  . ARG A 181 ? 0.2186 0.2597 0.3361 -0.0296 -0.0346 0.0878  182 ARG A NH2  
1759 N  N    . GLY A 182 ? 0.2012 0.0808 0.2278 0.0364  -0.0755 0.0037  183 GLY A N    
1760 C  CA   . GLY A 182 ? 0.2340 0.0534 0.2560 0.0148  -0.0410 0.0263  183 GLY A CA   
1761 C  C    . GLY A 182 ? 0.2048 0.0686 0.2745 0.0276  -0.0452 -0.0071 183 GLY A C    
1762 O  O    . GLY A 182 ? 0.2666 0.0815 0.2737 0.0059  -0.0974 0.0118  183 GLY A O    
1763 N  N    . LEU A 183 ? 0.1686 0.1047 0.2233 0.0013  -0.0520 -0.0082 184 LEU A N    
1764 C  CA   . LEU A 183 ? 0.1538 0.0907 0.2143 -0.0204 -0.0361 -0.0093 184 LEU A CA   
1765 C  C    . LEU A 183 ? 0.1465 0.0860 0.1895 -0.0231 -0.0247 -0.0186 184 LEU A C    
1766 O  O    . LEU A 183 ? 0.1538 0.1133 0.2275 0.0287  -0.0166 0.0054  184 LEU A O    
1767 C  CB   . LEU A 183 ? 0.1286 0.0688 0.2199 0.0115  -0.0182 -0.0015 184 LEU A CB   
1768 C  CG   . LEU A 183 ? 0.1539 0.0537 0.2191 0.0287  -0.0362 -0.0166 184 LEU A CG   
1769 C  CD1  . LEU A 183 ? 0.1780 0.1250 0.2139 -0.0063 -0.0588 0.0395  184 LEU A CD1  
1770 C  CD2  . LEU A 183 ? 0.3348 0.1092 0.2161 0.0549  -0.0137 -0.0273 184 LEU A CD2  
1771 N  N    A LEU A 184 ? 0.1629 0.0794 0.1977 -0.0071 -0.0065 -0.0093 185 LEU A N    
1772 N  N    B LEU A 184 ? 0.1404 0.0697 0.2279 -0.0082 -0.0304 -0.0242 185 LEU A N    
1773 C  CA   A LEU A 184 ? 0.0900 0.0785 0.1999 -0.0333 -0.0037 -0.0006 185 LEU A CA   
1774 C  CA   B LEU A 184 ? 0.1058 0.0684 0.2159 -0.0527 -0.0159 -0.0088 185 LEU A CA   
1775 C  C    A LEU A 184 ? 0.0679 0.0754 0.1538 -0.0166 -0.0080 -0.0020 185 LEU A C    
1776 C  C    B LEU A 184 ? 0.1277 0.0553 0.1938 -0.0076 -0.0414 -0.0035 185 LEU A C    
1777 O  O    A LEU A 184 ? 0.0569 0.0729 0.1732 -0.0091 -0.0362 0.0172  185 LEU A O    
1778 O  O    B LEU A 184 ? 0.1547 0.0936 0.2116 -0.0037 -0.0357 -0.0414 185 LEU A O    
1779 C  CB   A LEU A 184 ? 0.0756 0.0583 0.1904 0.0214  -0.0181 0.0218  185 LEU A CB   
1780 C  CB   B LEU A 184 ? 0.1076 0.0483 0.2196 -0.0199 -0.0255 0.0107  185 LEU A CB   
1781 C  CG   A LEU A 184 ? 0.0261 0.0675 0.1658 -0.0023 -0.0104 0.0264  185 LEU A CG   
1782 C  CG   B LEU A 184 ? 0.0815 0.0851 0.1748 -0.0362 -0.0171 0.0081  185 LEU A CG   
1783 C  CD1  A LEU A 184 ? 0.0499 0.1061 0.2016 -0.0438 -0.0151 0.0065  185 LEU A CD1  
1784 C  CD1  B LEU A 184 ? 0.1690 0.1737 0.2344 -0.0046 0.0198  0.0175  185 LEU A CD1  
1785 C  CD2  A LEU A 184 ? 0.0605 0.1058 0.1351 0.0110  -0.0088 0.0186  185 LEU A CD2  
1786 C  CD2  B LEU A 184 ? 0.1288 0.1570 0.1561 -0.0166 -0.0181 0.0114  185 LEU A CD2  
1787 N  N    A PRO A 185 ? 0.0401 0.0900 0.1712 -0.0174 -0.0027 -0.0015 186 PRO A N    
1788 N  N    B PRO A 185 ? 0.1261 0.0478 0.1811 0.0164  -0.0318 -0.0182 186 PRO A N    
1789 C  CA   A PRO A 185 ? 0.0279 0.0767 0.1762 -0.0071 0.0129  0.0000  186 PRO A CA   
1790 C  CA   B PRO A 185 ? 0.0988 0.0718 0.1764 -0.0065 -0.0200 0.0038  186 PRO A CA   
1791 C  C    A PRO A 185 ? 0.0546 0.0713 0.1748 -0.0357 -0.0086 -0.0087 186 PRO A C    
1792 C  C    B PRO A 185 ? 0.0530 0.0495 0.1850 -0.0237 -0.0225 -0.0040 186 PRO A C    
1793 O  O    A PRO A 185 ? 0.0828 0.0478 0.1661 0.0137  -0.0003 0.0068  186 PRO A O    
1794 O  O    B PRO A 185 ? 0.0480 0.0776 0.1977 -0.0077 -0.0217 0.0068  186 PRO A O    
1795 C  CB   A PRO A 185 ? 0.0437 0.0966 0.1852 0.0151  -0.0126 -0.0005 186 PRO A CB   
1796 C  CB   B PRO A 185 ? 0.0939 0.0763 0.1636 -0.0161 -0.0388 -0.0109 186 PRO A CB   
1797 C  CG   A PRO A 185 ? 0.0742 0.0781 0.1735 -0.0110 -0.0034 -0.0119 186 PRO A CG   
1798 C  CG   B PRO A 185 ? 0.0643 0.0527 0.1687 0.0109  -0.0372 0.0115  186 PRO A CG   
1799 C  CD   A PRO A 185 ? 0.0530 0.1189 0.1809 0.0006  -0.0120 -0.0057 186 PRO A CD   
1800 C  CD   B PRO A 185 ? 0.0927 0.0592 0.2005 0.0443  -0.0263 -0.0065 186 PRO A CD   
1801 N  N    A GLU A 186 ? 0.0722 0.0808 0.2272 -0.0351 0.0155  0.0027  187 GLU A N    
1802 N  N    B GLU A 186 ? 0.1022 0.0736 0.2536 -0.0397 -0.0219 0.0164  187 GLU A N    
1803 C  CA   A GLU A 186 ? 0.0421 0.1158 0.2469 0.0063  -0.0142 0.0125  187 GLU A CA   
1804 C  CA   B GLU A 186 ? 0.0878 0.0952 0.2579 -0.0375 -0.0175 0.0208  187 GLU A CA   
1805 C  C    A GLU A 186 ? 0.0366 0.1022 0.2592 -0.0186 0.0006  0.0302  187 GLU A C    
1806 C  C    B GLU A 186 ? 0.0887 0.0869 0.2511 -0.0368 -0.0027 0.0318  187 GLU A C    
1807 O  O    A GLU A 186 ? 0.0363 0.1325 0.2520 0.0141  0.0353  0.0460  187 GLU A O    
1808 O  O    B GLU A 186 ? 0.0740 0.1010 0.2727 -0.0175 0.0057  0.0408  187 GLU A O    
1809 C  CB   A GLU A 186 ? 0.0767 0.1225 0.2698 0.0068  -0.0252 0.0207  187 GLU A CB   
1810 C  CB   B GLU A 186 ? 0.0873 0.1130 0.2811 -0.0693 -0.0232 0.0275  187 GLU A CB   
1811 C  CG   A GLU A 186 ? 0.1209 0.1315 0.2741 0.0038  -0.0161 0.0432  187 GLU A CG   
1812 C  CG   B GLU A 186 ? 0.1931 0.1171 0.2946 -0.0639 -0.0390 0.0344  187 GLU A CG   
1813 C  CD   A GLU A 186 ? 0.1712 0.1911 0.2587 0.0057  0.0098  0.0504  187 GLU A CD   
1814 C  CD   B GLU A 186 ? 0.0718 0.1547 0.2547 -0.0439 -0.0259 0.0129  187 GLU A CD   
1815 O  OE1  A GLU A 186 ? 0.0765 0.1280 0.3407 0.0337  0.0020  0.0346  187 GLU A OE1  
1816 O  OE1  B GLU A 186 ? 0.1890 0.1942 0.3680 -0.0643 -0.0196 0.0219  187 GLU A OE1  
1817 O  OE2  A GLU A 186 ? 0.2315 0.1755 0.3348 0.0753  0.0907  0.0104  187 GLU A OE2  
1818 O  OE2  B GLU A 186 ? 0.1769 0.1547 0.3957 -0.0273 -0.0498 -0.0432 187 GLU A OE2  
1819 N  N    . SER A 187 ? 0.0495 0.1259 0.2637 -0.0271 -0.0186 0.0243  188 SER A N    
1820 C  CA   . SER A 187 ? 0.0704 0.1403 0.2696 -0.0167 -0.0017 0.0088  188 SER A CA   
1821 C  C    . SER A 187 ? 0.0763 0.1216 0.2657 -0.0373 0.0043  0.0119  188 SER A C    
1822 O  O    . SER A 187 ? 0.0997 0.1146 0.2743 -0.0242 -0.0074 -0.0115 188 SER A O    
1823 C  CB   . SER A 187 ? 0.1185 0.1672 0.2576 -0.0043 -0.0023 0.0153  188 SER A CB   
1824 O  OG   . SER A 187 ? 0.0679 0.1185 0.2976 -0.0297 0.0035  -0.0017 188 SER A OG   
1825 N  N    . LEU A 188 ? 0.0315 0.0859 0.2858 -0.0188 -0.0023 -0.0163 189 LEU A N    
1826 C  CA   . LEU A 188 ? 0.0546 0.0742 0.2894 -0.0007 -0.0216 -0.0110 189 LEU A CA   
1827 C  C    . LEU A 188 ? 0.0538 0.0970 0.2529 0.0142  -0.0041 -0.0160 189 LEU A C    
1828 O  O    . LEU A 188 ? 0.0774 0.1532 0.2617 -0.0351 0.0000  -0.0297 189 LEU A O    
1829 C  CB   . LEU A 188 ? 0.0878 0.0776 0.3082 -0.0031 -0.0052 -0.0003 189 LEU A CB   
1830 C  CG   . LEU A 188 ? 0.0592 0.1622 0.3125 0.0260  -0.0031 0.0020  189 LEU A CG   
1831 C  CD1  . LEU A 188 ? 0.1636 0.1185 0.3556 0.0557  -0.0195 0.0148  189 LEU A CD1  
1832 C  CD2  . LEU A 188 ? 0.0600 0.3149 0.3152 -0.0124 -0.0017 0.0099  189 LEU A CD2  
1833 N  N    . ASP A 189 ? 0.0718 0.1223 0.2486 0.0210  0.0070  -0.0137 190 ASP A N    
1834 C  CA   . ASP A 189 ? 0.0499 0.0984 0.2455 -0.0377 0.0019  -0.0071 190 ASP A CA   
1835 C  C    . ASP A 189 ? 0.0586 0.1124 0.1872 -0.0269 0.0182  -0.0125 190 ASP A C    
1836 O  O    . ASP A 189 ? 0.0458 0.0803 0.2134 -0.0052 0.0076  -0.0046 190 ASP A O    
1837 C  CB   . ASP A 189 ? 0.0891 0.1744 0.2504 -0.0538 0.0208  0.0148  190 ASP A CB   
1838 C  CG   . ASP A 189 ? 0.1863 0.2242 0.3021 -0.0372 0.0000  -0.0265 190 ASP A CG   
1839 O  OD1  . ASP A 189 ? 0.1225 0.3143 0.3325 -0.0392 0.0531  -0.0304 190 ASP A OD1  
1840 O  OD2  . ASP A 189 ? 0.2186 0.3564 0.3391 -0.0966 -0.0092 0.0560  190 ASP A OD2  
1841 N  N    . TYR A 190 ? 0.0442 0.1067 0.1820 -0.0109 0.0156  -0.0099 191 TYR A N    
1842 C  CA   . TYR A 190 ? 0.0654 0.0860 0.1590 -0.0381 0.0142  0.0017  191 TYR A CA   
1843 C  C    . TYR A 190 ? 0.0718 0.0326 0.1575 -0.0107 0.0198  0.0114  191 TYR A C    
1844 O  O    . TYR A 190 ? 0.0693 0.0927 0.1816 -0.0109 0.0361  -0.0027 191 TYR A O    
1845 C  CB   . TYR A 190 ? 0.0945 0.0763 0.1638 -0.0197 -0.0057 -0.0076 191 TYR A CB   
1846 C  CG   . TYR A 190 ? 0.0727 0.0887 0.1735 -0.0474 0.0183  0.0292  191 TYR A CG   
1847 C  CD1  . TYR A 190 ? 0.0986 0.0763 0.1893 -0.0610 0.0068  -0.0088 191 TYR A CD1  
1848 C  CD2  . TYR A 190 ? 0.0837 0.1151 0.1683 0.0031  0.0318  -0.0102 191 TYR A CD2  
1849 C  CE1  . TYR A 190 ? 0.0806 0.0684 0.2170 -0.0443 0.0024  0.0024  191 TYR A CE1  
1850 C  CE2  . TYR A 190 ? 0.0966 0.0921 0.1974 0.0119  0.0035  -0.0272 191 TYR A CE2  
1851 C  CZ   . TYR A 190 ? 0.1439 0.0578 0.1944 -0.0206 0.0068  -0.0166 191 TYR A CZ   
1852 O  OH   . TYR A 190 ? 0.1180 0.1009 0.2312 -0.0277 0.0081  -0.0241 191 TYR A OH   
1853 N  N    . TRP A 191 ? 0.0361 0.0706 0.1751 -0.0087 0.0000  0.0160  192 TRP A N    
1854 C  CA   . TRP A 191 ? 0.0537 0.0397 0.1880 -0.0197 -0.0098 0.0148  192 TRP A CA   
1855 C  C    . TRP A 191 ? 0.0397 0.0583 0.1681 0.0175  0.0026  -0.0052 192 TRP A C    
1856 O  O    . TRP A 191 ? 0.0621 0.0574 0.1830 -0.0155 0.0166  -0.0065 192 TRP A O    
1857 C  CB   . TRP A 191 ? 0.0534 0.0614 0.1806 -0.0316 0.0014  0.0054  192 TRP A CB   
1858 C  CG   . TRP A 191 ? 0.0882 0.0934 0.1692 -0.0197 0.0210  -0.0099 192 TRP A CG   
1859 C  CD1  . TRP A 191 ? 0.1049 0.0406 0.2260 -0.0152 0.0373  -0.0065 192 TRP A CD1  
1860 C  CD2  . TRP A 191 ? 0.0588 0.0666 0.1669 0.0370  0.0082  0.0137  192 TRP A CD2  
1861 N  NE1  . TRP A 191 ? 0.1268 0.0458 0.1895 -0.0238 0.0209  0.0035  192 TRP A NE1  
1862 C  CE2  . TRP A 191 ? 0.1137 0.0704 0.1744 -0.0027 0.0098  0.0027  192 TRP A CE2  
1863 C  CE3  . TRP A 191 ? 0.0587 0.0973 0.1755 0.0243  0.0135  0.0099  192 TRP A CE3  
1864 C  CZ2  . TRP A 191 ? 0.0979 0.0533 0.1954 -0.0109 -0.0228 -0.0052 192 TRP A CZ2  
1865 C  CZ3  . TRP A 191 ? 0.0713 0.1054 0.2035 0.0271  0.0132  -0.0251 192 TRP A CZ3  
1866 C  CH2  . TRP A 191 ? 0.0754 0.0824 0.2152 0.0471  -0.0073 -0.0142 192 TRP A CH2  
1867 N  N    . THR A 192 ? 0.0353 0.0406 0.1640 -0.0093 -0.0093 -0.0082 193 THR A N    
1868 C  CA   . THR A 192 ? 0.0395 0.0463 0.1728 -0.0164 -0.0109 -0.0024 193 THR A CA   
1869 C  C    . THR A 192 ? 0.0693 0.0372 0.1624 -0.0003 0.0052  0.0218  193 THR A C    
1870 O  O    . THR A 192 ? 0.0569 0.0589 0.1650 -0.0087 0.0167  0.0208  193 THR A O    
1871 C  CB   . THR A 192 ? 0.0643 0.0431 0.1696 -0.0258 -0.0027 0.0120  193 THR A CB   
1872 O  OG1  . THR A 192 ? 0.0582 0.0336 0.1941 -0.0154 0.0088  0.0087  193 THR A OG1  
1873 C  CG2  . THR A 192 ? 0.0763 0.0709 0.1841 -0.0340 0.0147  0.0031  193 THR A CG2  
1874 N  N    . TYR A 193 ? 0.0265 0.0397 0.1945 0.0038  0.0000  0.0141  194 TYR A N    
1875 C  CA   . TYR A 193 ? 0.0279 0.0305 0.1790 -0.0005 0.0115  0.0202  194 TYR A CA   
1876 C  C    . TYR A 193 ? 0.0325 0.0291 0.1782 0.0043  0.0078  -0.0076 194 TYR A C    
1877 O  O    . TYR A 193 ? 0.0465 0.0375 0.1615 0.0031  -0.0020 0.0051  194 TYR A O    
1878 C  CB   . TYR A 193 ? 0.0693 0.0504 0.1600 -0.0172 0.0087  -0.0165 194 TYR A CB   
1879 C  CG   . TYR A 193 ? 0.0417 0.0450 0.1553 -0.0126 -0.0010 -0.0027 194 TYR A CG   
1880 C  CD1  . TYR A 193 ? 0.0835 0.0329 0.1422 0.0204  0.0066  0.0096  194 TYR A CD1  
1881 C  CD2  . TYR A 193 ? 0.0515 0.0592 0.1592 0.0065  0.0057  -0.0171 194 TYR A CD2  
1882 C  CE1  . TYR A 193 ? 0.0737 0.0521 0.1448 -0.0359 -0.0006 0.0005  194 TYR A CE1  
1883 C  CE2  . TYR A 193 ? 0.0740 0.0496 0.1376 0.0252  -0.0012 -0.0059 194 TYR A CE2  
1884 C  CZ   . TYR A 193 ? 0.0652 0.0366 0.1480 0.0074  -0.0043 -0.0120 194 TYR A CZ   
1885 O  OH   . TYR A 193 ? 0.0473 0.0339 0.1736 -0.0136 0.0071  -0.0087 194 TYR A OH   
1886 N  N    . PRO A 194 ? 0.0256 0.0561 0.1566 -0.0014 -0.0033 -0.0266 195 PRO A N    
1887 C  CA   . PRO A 194 ? 0.0603 0.0527 0.1408 0.0197  0.0362  -0.0148 195 PRO A CA   
1888 C  C    . PRO A 194 ? 0.0359 0.0259 0.1872 0.0004  0.0149  -0.0080 195 PRO A C    
1889 O  O    . PRO A 194 ? 0.0715 0.0731 0.1712 0.0281  -0.0098 -0.0126 195 PRO A O    
1890 C  CB   . PRO A 194 ? 0.0830 0.0851 0.1832 0.0183  0.0175  -0.0092 195 PRO A CB   
1891 C  CG   . PRO A 194 ? 0.0815 0.0878 0.1872 -0.0230 -0.0115 -0.0046 195 PRO A CG   
1892 C  CD   . PRO A 194 ? 0.0758 0.0839 0.1650 -0.0142 0.0054  -0.0173 195 PRO A CD   
1893 N  N    . GLY A 195 ? 0.0291 0.0648 0.1536 -0.0071 0.0142  0.0000  196 GLY A N    
1894 C  CA   . GLY A 195 ? 0.0442 0.0891 0.1600 0.0199  0.0109  0.0237  196 GLY A CA   
1895 C  C    . GLY A 195 ? 0.0411 0.0885 0.1352 -0.0109 0.0081  -0.0030 196 GLY A C    
1896 O  O    . GLY A 195 ? 0.0690 0.0406 0.1825 0.0082  0.0000  -0.0093 196 GLY A O    
1897 N  N    . SER A 196 ? 0.0715 0.0502 0.1239 0.0313  0.0020  -0.0082 197 SER A N    
1898 C  CA   . SER A 196 ? 0.0432 0.0527 0.1243 0.0186  0.0218  -0.0013 197 SER A CA   
1899 C  C    . SER A 196 ? 0.0625 0.0639 0.1455 0.0375  0.0003  0.0093  197 SER A C    
1900 O  O    . SER A 196 ? 0.0345 0.0494 0.1764 -0.0024 0.0054  -0.0057 197 SER A O    
1901 C  CB   . SER A 196 ? 0.0279 0.0508 0.2027 0.0077  -0.0084 -0.0080 197 SER A CB   
1902 O  OG   . SER A 196 ? 0.0329 0.0379 0.1941 0.0093  0.0040  -0.0087 197 SER A OG   
1903 N  N    . LEU A 197 ? 0.0461 0.0698 0.1486 0.0302  0.0129  0.0108  198 LEU A N    
1904 C  CA   . LEU A 197 ? 0.0375 0.0343 0.1811 0.0010  0.0109  -0.0126 198 LEU A CA   
1905 C  C    . LEU A 197 ? 0.0257 0.0411 0.1809 -0.0001 0.0083  0.0006  198 LEU A C    
1906 O  O    . LEU A 197 ? 0.0459 0.0467 0.1848 -0.0186 -0.0026 -0.0239 198 LEU A O    
1907 C  CB   . LEU A 197 ? 0.0458 0.0614 0.2073 0.0195  0.0115  0.0211  198 LEU A CB   
1908 C  CG   . LEU A 197 ? 0.1036 0.0846 0.2247 0.0051  0.0296  0.0568  198 LEU A CG   
1909 C  CD1  . LEU A 197 ? 0.0914 0.1324 0.2538 -0.0232 0.0498  0.0333  198 LEU A CD1  
1910 C  CD2  . LEU A 197 ? 0.0966 0.0900 0.2822 0.0472  0.0364  0.0674  198 LEU A CD2  
1911 N  N    . THR A 198 ? 0.0447 0.0265 0.1843 0.0020  -0.0071 -0.0135 199 THR A N    
1912 C  CA   . THR A 198 ? 0.0345 0.0293 0.1843 -0.0049 0.0304  -0.0070 199 THR A CA   
1913 C  C    . THR A 198 ? 0.0528 0.0477 0.1868 -0.0020 0.0087  0.0110  199 THR A C    
1914 O  O    . THR A 198 ? 0.0299 0.0393 0.2141 -0.0051 0.0234  -0.0019 199 THR A O    
1915 C  CB   . THR A 198 ? 0.0574 0.0398 0.1826 -0.0215 0.0076  -0.0104 199 THR A CB   
1916 O  OG1  . THR A 198 ? 0.0403 0.0274 0.1629 0.0000  -0.0073 -0.0076 199 THR A OG1  
1917 C  CG2  . THR A 198 ? 0.0609 0.0575 0.1593 -0.0166 0.0280  -0.0148 199 THR A CG2  
1918 N  N    . THR A 199 ? 0.0469 0.0524 0.2066 -0.0241 0.0031  -0.0037 200 THR A N    
1919 C  CA   . THR A 199 ? 0.0722 0.0491 0.1913 -0.0320 0.0263  -0.0013 200 THR A CA   
1920 C  C    . THR A 199 ? 0.0684 0.0763 0.1923 -0.0364 0.0071  0.0070  200 THR A C    
1921 O  O    . THR A 199 ? 0.0496 0.0742 0.2127 -0.0288 0.0109  -0.0186 200 THR A O    
1922 C  CB   . THR A 199 ? 0.0553 0.0593 0.2394 -0.0284 0.0221  0.0027  200 THR A CB   
1923 O  OG1  . THR A 199 ? 0.1617 0.0582 0.2779 0.0263  -0.0342 -0.0109 200 THR A OG1  
1924 C  CG2  . THR A 199 ? 0.0961 0.0812 0.2258 -0.0627 0.0297  -0.0195 200 THR A CG2  
1925 N  N    . PRO A 200 ? 0.0736 0.0670 0.2093 -0.0092 0.0322  -0.0162 201 PRO A N    
1926 C  CA   . PRO A 200 ? 0.0473 0.0696 0.2345 -0.0279 0.0268  0.0050  201 PRO A CA   
1927 C  C    . PRO A 200 ? 0.0943 0.0745 0.2172 -0.0281 0.0160  -0.0205 201 PRO A C    
1928 O  O    . PRO A 200 ? 0.0984 0.0830 0.2130 -0.0274 0.0129  -0.0242 201 PRO A O    
1929 C  CB   . PRO A 200 ? 0.0591 0.0844 0.2168 0.0023  0.0274  -0.0147 201 PRO A CB   
1930 C  CG   . PRO A 200 ? 0.0376 0.0934 0.2531 -0.0227 0.0310  -0.0434 201 PRO A CG   
1931 C  CD   . PRO A 200 ? 0.0727 0.0639 0.2037 -0.0177 0.0186  -0.0120 201 PRO A CD   
1932 N  N    . PRO A 201 ? 0.0702 0.0769 0.2186 -0.0215 0.0230  -0.0071 202 PRO A N    
1933 C  CA   . PRO A 201 ? 0.0907 0.0401 0.2146 -0.0124 -0.0065 0.0077  202 PRO A CA   
1934 C  C    . PRO A 201 ? 0.0790 0.0816 0.2177 0.0205  0.0010  -0.0173 202 PRO A C    
1935 O  O    . PRO A 201 ? 0.0825 0.0792 0.2405 -0.0192 0.0230  -0.0175 202 PRO A O    
1936 C  CB   . PRO A 201 ? 0.1773 0.0794 0.2166 -0.0728 0.0115  0.0017  202 PRO A CB   
1937 C  CG   . PRO A 201 ? 0.1714 0.0806 0.2655 -0.0131 0.0073  -0.0209 202 PRO A CG   
1938 C  CD   . PRO A 201 ? 0.0952 0.0903 0.2382 -0.0060 0.0115  -0.0110 202 PRO A CD   
1939 N  N    . LEU A 202 ? 0.0415 0.0569 0.2171 -0.0006 0.0243  -0.0102 203 LEU A N    
1940 C  CA   . LEU A 202 ? 0.0362 0.0718 0.2023 0.0099  0.0035  -0.0088 203 LEU A CA   
1941 C  C    . LEU A 202 ? 0.0482 0.0663 0.2005 -0.0299 -0.0057 -0.0082 203 LEU A C    
1942 O  O    . LEU A 202 ? 0.0259 0.0335 0.2230 0.0010  0.0100  0.0062  203 LEU A O    
1943 C  CB   . LEU A 202 ? 0.0289 0.0930 0.2163 -0.0155 0.0097  -0.0403 203 LEU A CB   
1944 C  CG   . LEU A 202 ? 0.0271 0.1036 0.2073 -0.0075 0.0164  -0.0325 203 LEU A CG   
1945 C  CD1  . LEU A 202 ? 0.0271 0.1544 0.2430 0.0136  0.0056  -0.0254 203 LEU A CD1  
1946 C  CD2  . LEU A 202 ? 0.0412 0.0788 0.2533 -0.0291 0.0002  0.0018  203 LEU A CD2  
1947 N  N    . LEU A 203 ? 0.0630 0.0551 0.2184 0.0054  0.0183  -0.0165 204 LEU A N    
1948 C  CA   . LEU A 203 ? 0.0517 0.0846 0.2168 -0.0080 0.0007  -0.0188 204 LEU A CA   
1949 C  C    . LEU A 203 ? 0.0397 0.0528 0.2001 -0.0015 0.0148  -0.0035 204 LEU A C    
1950 O  O    . LEU A 203 ? 0.0454 0.0533 0.2121 -0.0154 -0.0119 -0.0087 204 LEU A O    
1951 C  CB   . LEU A 203 ? 0.0806 0.0334 0.2380 -0.0172 0.0452  0.0077  204 LEU A CB   
1952 C  CG   . LEU A 203 ? 0.1189 0.0679 0.2480 0.0026  0.0430  0.0204  204 LEU A CG   
1953 C  CD1  . LEU A 203 ? 0.1106 0.0731 0.2833 -0.0006 0.0544  0.0377  204 LEU A CD1  
1954 C  CD2  . LEU A 203 ? 0.0896 0.1318 0.3851 -0.0795 0.0439  -0.0035 204 LEU A CD2  
1955 N  N    . GLU A 204 ? 0.0417 0.0661 0.1904 0.0046  0.0040  -0.0331 205 GLU A N    
1956 C  CA   . GLU A 204 ? 0.0672 0.1061 0.1710 -0.0020 -0.0113 -0.0109 205 GLU A CA   
1957 C  C    . GLU A 204 ? 0.1115 0.0684 0.1949 0.0003  -0.0188 -0.0054 205 GLU A C    
1958 O  O    . GLU A 204 ? 0.0736 0.1099 0.1895 0.0005  -0.0285 -0.0399 205 GLU A O    
1959 C  CB   . GLU A 204 ? 0.0810 0.0615 0.2051 0.0043  -0.0037 -0.0372 205 GLU A CB   
1960 C  CG   . GLU A 204 ? 0.0738 0.0722 0.2351 -0.0173 -0.0333 -0.0275 205 GLU A CG   
1961 C  CD   . GLU A 204 ? 0.1295 0.1155 0.1913 -0.0200 -0.0109 -0.0173 205 GLU A CD   
1962 O  OE1  . GLU A 204 ? 0.1070 0.1038 0.2635 0.0003  -0.0386 -0.0401 205 GLU A OE1  
1963 O  OE2  . GLU A 204 ? 0.0749 0.0846 0.2437 -0.0173 -0.0292 0.0035  205 GLU A OE2  
1964 N  N    . CYS A 205 ? 0.0557 0.0557 0.1879 -0.0170 -0.0046 -0.0093 206 CYS A N    
1965 C  CA   . CYS A 205 ? 0.0267 0.0560 0.1995 0.0009  -0.0156 -0.0003 206 CYS A CA   
1966 C  C    . CYS A 205 ? 0.0339 0.0377 0.1956 -0.0099 -0.0054 -0.0027 206 CYS A C    
1967 O  O    . CYS A 205 ? 0.0525 0.0293 0.2398 0.0093  -0.0098 0.0098  206 CYS A O    
1968 C  CB   . CYS A 205 ? 0.1268 0.0984 0.1784 -0.0087 0.0253  0.0197  206 CYS A CB   
1969 S  SG   . CYS A 205 ? 0.0970 0.0590 0.2046 -0.0027 -0.0013 -0.0037 206 CYS A SG   
1970 N  N    . VAL A 206 ? 0.0490 0.0419 0.1719 -0.0182 0.0210  -0.0041 207 VAL A N    
1971 C  CA   . VAL A 206 ? 0.0421 0.0552 0.1613 -0.0038 0.0163  -0.0214 207 VAL A CA   
1972 C  C    . VAL A 206 ? 0.0496 0.0335 0.1563 0.0141  0.0071  0.0020  207 VAL A C    
1973 O  O    . VAL A 206 ? 0.0500 0.0599 0.1974 -0.0063 -0.0091 0.0136  207 VAL A O    
1974 C  CB   . VAL A 206 ? 0.0621 0.0406 0.1782 -0.0226 0.0034  -0.0167 207 VAL A CB   
1975 C  CG1  . VAL A 206 ? 0.0299 0.0432 0.1854 0.0080  -0.0229 -0.0260 207 VAL A CG1  
1976 C  CG2  . VAL A 206 ? 0.1018 0.0306 0.1762 0.0054  0.0399  0.0077  207 VAL A CG2  
1977 N  N    . THR A 207 ? 0.0253 0.0257 0.1901 -0.0001 0.0026  -0.0080 208 THR A N    
1978 C  CA   . THR A 207 ? 0.0253 0.0258 0.1865 0.0000  0.0009  -0.0089 208 THR A CA   
1979 C  C    . THR A 207 ? 0.0295 0.0253 0.1773 0.0000  -0.0046 0.0021  208 THR A C    
1980 O  O    . THR A 207 ? 0.0534 0.0265 0.1631 -0.0057 0.0003  -0.0032 208 THR A O    
1981 C  CB   . THR A 207 ? 0.0380 0.0262 0.1942 0.0031  -0.0006 -0.0046 208 THR A CB   
1982 O  OG1  . THR A 207 ? 0.0855 0.0363 0.1830 0.0046  0.0086  -0.0178 208 THR A OG1  
1983 C  CG2  . THR A 207 ? 0.0515 0.0649 0.2116 -0.0253 0.0425  -0.0020 208 THR A CG2  
1984 N  N    . TRP A 208 ? 0.0304 0.0285 0.1756 0.0023  0.0061  -0.0141 209 TRP A N    
1985 C  CA   . TRP A 208 ? 0.0377 0.0449 0.1782 -0.0154 0.0086  -0.0103 209 TRP A CA   
1986 C  C    . TRP A 208 ? 0.0323 0.0424 0.1482 0.0074  0.0074  -0.0065 209 TRP A C    
1987 O  O    . TRP A 208 ? 0.0315 0.0403 0.1827 0.0092  0.0118  0.0066  209 TRP A O    
1988 C  CB   . TRP A 208 ? 0.0596 0.0589 0.1686 -0.0126 0.0197  0.0065  209 TRP A CB   
1989 C  CG   . TRP A 208 ? 0.0370 0.0319 0.1430 -0.0076 0.0209  -0.0031 209 TRP A CG   
1990 C  CD1  . TRP A 208 ? 0.0319 0.0302 0.1683 0.0055  0.0097  0.0027  209 TRP A CD1  
1991 C  CD2  . TRP A 208 ? 0.0417 0.0630 0.1286 -0.0231 0.0135  0.0024  209 TRP A CD2  
1992 N  NE1  . TRP A 208 ? 0.0526 0.0557 0.1597 0.0231  -0.0065 -0.0041 209 TRP A NE1  
1993 C  CE2  . TRP A 208 ? 0.0406 0.0473 0.1480 0.0160  0.0153  0.0109  209 TRP A CE2  
1994 C  CE3  . TRP A 208 ? 0.0419 0.0381 0.1580 -0.0140 -0.0159 0.0038  209 TRP A CE3  
1995 C  CZ2  . TRP A 208 ? 0.0487 0.0440 0.1694 0.0208  0.0182  0.0178  209 TRP A CZ2  
1996 C  CZ3  . TRP A 208 ? 0.0645 0.0528 0.1412 0.0035  -0.0007 -0.0142 209 TRP A CZ3  
1997 C  CH2  . TRP A 208 ? 0.0593 0.0630 0.1527 0.0263  0.0126  -0.0364 209 TRP A CH2  
1998 N  N    . ILE A 209 ? 0.0458 0.0293 0.1632 0.0037  0.0003  -0.0054 210 ILE A N    
1999 C  CA   . ILE A 209 ? 0.0442 0.0575 0.1780 -0.0230 -0.0077 -0.0154 210 ILE A CA   
2000 C  C    . ILE A 209 ? 0.0261 0.0351 0.1667 -0.0024 0.0052  -0.0010 210 ILE A C    
2001 O  O    . ILE A 209 ? 0.0816 0.0465 0.1632 -0.0043 -0.0104 -0.0109 210 ILE A O    
2002 C  CB   . ILE A 209 ? 0.0454 0.0397 0.2024 -0.0006 0.0148  -0.0187 210 ILE A CB   
2003 C  CG1  . ILE A 209 ? 0.0533 0.0571 0.2520 0.0294  -0.0068 -0.0195 210 ILE A CG1  
2004 C  CG2  . ILE A 209 ? 0.0432 0.0900 0.2215 -0.0218 0.0012  0.0148  210 ILE A CG2  
2005 C  CD1  . ILE A 209 ? 0.0820 0.0865 0.2574 0.0574  -0.0081 0.0177  210 ILE A CD1  
2006 N  N    . VAL A 210 ? 0.0538 0.0661 0.1660 0.0035  -0.0063 0.0114  211 VAL A N    
2007 C  CA   . VAL A 210 ? 0.0279 0.0273 0.1831 -0.0022 0.0201  -0.0174 211 VAL A CA   
2008 C  C    . VAL A 210 ? 0.0482 0.0256 0.1581 0.0020  0.0026  -0.0046 211 VAL A C    
2009 O  O    . VAL A 210 ? 0.0785 0.0336 0.1570 -0.0109 0.0046  -0.0068 211 VAL A O    
2010 C  CB   . VAL A 210 ? 0.0287 0.0412 0.1784 -0.0070 0.0104  -0.0104 211 VAL A CB   
2011 C  CG1  . VAL A 210 ? 0.0887 0.0321 0.1698 -0.0008 -0.0025 -0.0311 211 VAL A CG1  
2012 C  CG2  . VAL A 210 ? 0.0767 0.0718 0.1929 -0.0487 -0.0027 -0.0043 211 VAL A CG2  
2013 N  N    . LEU A 211 ? 0.0575 0.0503 0.1687 -0.0088 -0.0041 0.0054  212 LEU A N    
2014 C  CA   . LEU A 211 ? 0.0657 0.0697 0.1606 -0.0366 0.0142  0.0040  212 LEU A CA   
2015 C  C    . LEU A 211 ? 0.0260 0.0501 0.1927 -0.0014 0.0090  0.0116  212 LEU A C    
2016 O  O    . LEU A 211 ? 0.0386 0.0731 0.2041 -0.0041 0.0119  0.0120  212 LEU A O    
2017 C  CB   . LEU A 211 ? 0.0586 0.0558 0.1812 -0.0314 -0.0036 -0.0070 212 LEU A CB   
2018 C  CG   . LEU A 211 ? 0.1216 0.0900 0.1796 0.0065  -0.0007 -0.0197 212 LEU A CG   
2019 C  CD1  . LEU A 211 ? 0.1135 0.1313 0.2145 -0.0093 -0.0364 0.0309  212 LEU A CD1  
2020 C  CD2  . LEU A 211 ? 0.0778 0.0821 0.2150 0.0184  0.0038  -0.0132 212 LEU A CD2  
2021 N  N    . LYS A 212 ? 0.0434 0.0822 0.1956 -0.0311 0.0098  0.0052  213 LYS A N    
2022 C  CA   . LYS A 212 ? 0.1324 0.0679 0.1895 -0.0108 0.0115  0.0164  213 LYS A CA   
2023 C  C    . LYS A 212 ? 0.0639 0.0327 0.1922 -0.0160 -0.0052 0.0129  213 LYS A C    
2024 O  O    . LYS A 212 ? 0.0869 0.0516 0.2416 0.0049  -0.0113 0.0076  213 LYS A O    
2025 C  CB   . LYS A 212 ? 0.0930 0.1065 0.2372 -0.0098 0.0452  0.0207  213 LYS A CB   
2026 C  CG   . LYS A 212 ? 0.1823 0.1342 0.2238 -0.0274 0.0065  0.0253  213 LYS A CG   
2027 C  CD   . LYS A 212 ? 0.3176 0.2042 0.3016 -0.1365 0.0513  0.0474  213 LYS A CD   
2028 C  CE   . LYS A 212 ? 0.3747 0.2790 0.3377 -0.0603 0.0250  0.0421  213 LYS A CE   
2029 N  NZ   . LYS A 212 ? 0.4605 0.4304 0.4039 -0.0983 0.0582  0.0505  213 LYS A NZ   
2030 N  N    . GLU A 213 ? 0.0578 0.0749 0.1780 -0.0196 -0.0070 0.0142  214 GLU A N    
2031 C  CA   . GLU A 213 ? 0.0666 0.0487 0.2064 -0.0291 0.0114  -0.0048 214 GLU A CA   
2032 C  C    . GLU A 213 ? 0.0590 0.0363 0.1977 -0.0118 0.0007  0.0114  214 GLU A C    
2033 O  O    . GLU A 213 ? 0.0652 0.0547 0.1999 -0.0031 0.0027  0.0077  214 GLU A O    
2034 C  CB   . GLU A 213 ? 0.0528 0.1054 0.2084 -0.0099 -0.0052 -0.0041 214 GLU A CB   
2035 C  CG   . GLU A 213 ? 0.0584 0.1286 0.2441 -0.0207 -0.0098 -0.0225 214 GLU A CG   
2036 C  CD   . GLU A 213 ? 0.1397 0.1789 0.3497 -0.0834 0.0071  -0.0414 214 GLU A CD   
2037 O  OE1  . GLU A 213 ? 0.1015 0.0907 0.3436 -0.0107 -0.0275 0.0285  214 GLU A OE1  
2038 O  OE2  . GLU A 213 ? 0.2017 0.3966 0.4038 -0.0584 -0.0381 -0.1023 214 GLU A OE2  
2039 N  N    . PRO A 214 ? 0.0724 0.0283 0.1757 -0.0076 -0.0003 -0.0164 215 PRO A N    
2040 C  CA   . PRO A 214 ? 0.0637 0.0278 0.1692 -0.0094 -0.0076 0.0059  215 PRO A CA   
2041 C  C    . PRO A 214 ? 0.0925 0.0670 0.1926 -0.0230 -0.0148 0.0031  215 PRO A C    
2042 O  O    . PRO A 214 ? 0.0846 0.1049 0.2123 -0.0425 -0.0174 0.0177  215 PRO A O    
2043 C  CB   . PRO A 214 ? 0.0668 0.0327 0.1999 -0.0159 -0.0074 -0.0125 215 PRO A CB   
2044 C  CG   . PRO A 214 ? 0.1823 0.0824 0.2870 0.0269  0.0225  0.0024  215 PRO A CG   
2045 C  CD   . PRO A 214 ? 0.1013 0.0439 0.2053 -0.0034 0.0381  0.0038  215 PRO A CD   
2046 N  N    . ILE A 215 ? 0.1045 0.0588 0.1589 0.0174  -0.0040 -0.0196 216 ILE A N    
2047 C  CA   . ILE A 215 ? 0.1194 0.0543 0.1902 0.0186  -0.0196 -0.0197 216 ILE A CA   
2048 C  C    . ILE A 215 ? 0.0900 0.0353 0.1962 0.0006  0.0048  0.0040  216 ILE A C    
2049 O  O    . ILE A 215 ? 0.0760 0.0517 0.2193 0.0357  0.0010  -0.0142 216 ILE A O    
2050 C  CB   . ILE A 215 ? 0.1011 0.0652 0.1956 -0.0109 -0.0109 0.0077  216 ILE A CB   
2051 C  CG1  . ILE A 215 ? 0.1617 0.0640 0.1890 0.0065  0.0087  -0.0164 216 ILE A CG1  
2052 C  CG2  . ILE A 215 ? 0.1186 0.0833 0.2138 0.0217  -0.0449 -0.0186 216 ILE A CG2  
2053 C  CD1  . ILE A 215 ? 0.2098 0.1002 0.2206 -0.0162 -0.0390 0.0147  216 ILE A CD1  
2054 N  N    . SER A 216 ? 0.1121 0.0370 0.2138 -0.0115 -0.0098 -0.0230 217 SER A N    
2055 C  CA   . SER A 216 ? 0.1239 0.0851 0.2012 -0.0329 0.0012  -0.0236 217 SER A CA   
2056 C  C    . SER A 216 ? 0.1388 0.0480 0.2092 -0.0196 -0.0302 -0.0182 217 SER A C    
2057 O  O    . SER A 216 ? 0.1352 0.0546 0.2206 0.0080  -0.0309 -0.0126 217 SER A O    
2058 C  CB   . SER A 216 ? 0.2333 0.0957 0.2278 -0.0304 0.0259  -0.0049 217 SER A CB   
2059 O  OG   . SER A 216 ? 0.2127 0.1696 0.2709 -0.0087 -0.0017 -0.0109 217 SER A OG   
2060 N  N    . VAL A 217 ? 0.1265 0.0706 0.1826 -0.0098 -0.0052 -0.0051 218 VAL A N    
2061 C  CA   . VAL A 217 ? 0.1315 0.0390 0.2008 0.0006  0.0041  -0.0184 218 VAL A CA   
2062 C  C    . VAL A 217 ? 0.1654 0.0491 0.1866 -0.0131 -0.0197 -0.0006 218 VAL A C    
2063 O  O    . VAL A 217 ? 0.1286 0.0582 0.2109 -0.0388 -0.0287 0.0010  218 VAL A O    
2064 C  CB   . VAL A 217 ? 0.1040 0.0390 0.2421 -0.0208 -0.0228 -0.0263 218 VAL A CB   
2065 C  CG1  . VAL A 217 ? 0.1311 0.0760 0.2193 -0.0137 -0.0177 -0.0452 218 VAL A CG1  
2066 C  CG2  . VAL A 217 ? 0.1151 0.0719 0.2671 -0.0051 -0.0318 -0.0085 218 VAL A CG2  
2067 N  N    . SER A 218 ? 0.1434 0.0310 0.1951 -0.0253 -0.0320 0.0006  219 SER A N    
2068 C  CA   . SER A 218 ? 0.1568 0.0407 0.1814 0.0164  -0.0074 -0.0063 219 SER A CA   
2069 C  C    . SER A 218 ? 0.1394 0.0314 0.2148 -0.0115 -0.0038 -0.0071 219 SER A C    
2070 O  O    . SER A 218 ? 0.1502 0.0548 0.1949 -0.0186 -0.0129 -0.0031 219 SER A O    
2071 C  CB   . SER A 218 ? 0.1746 0.0702 0.1915 0.0104  -0.0230 0.0077  219 SER A CB   
2072 O  OG   . SER A 218 ? 0.1629 0.0844 0.2096 -0.0082 -0.0125 -0.0071 219 SER A OG   
2073 N  N    A SER A 219 ? 0.1685 0.0454 0.1952 0.0161  -0.0161 -0.0063 220 SER A N    
2074 N  N    B SER A 219 ? 0.1708 0.0566 0.1954 0.0176  -0.0159 -0.0074 220 SER A N    
2075 C  CA   A SER A 219 ? 0.1913 0.0745 0.2333 -0.0113 -0.0007 0.0070  220 SER A CA   
2076 C  CA   B SER A 219 ? 0.1965 0.0943 0.2450 -0.0046 0.0013  0.0034  220 SER A CA   
2077 C  C    A SER A 219 ? 0.1764 0.0384 0.2247 -0.0220 -0.0093 -0.0074 220 SER A C    
2078 C  C    B SER A 219 ? 0.1837 0.0587 0.2195 -0.0114 -0.0063 -0.0140 220 SER A C    
2079 O  O    A SER A 219 ? 0.1541 0.0582 0.2380 -0.0452 -0.0010 -0.0135 220 SER A O    
2080 O  O    B SER A 219 ? 0.1685 0.1158 0.2549 -0.0137 0.0160  -0.0026 220 SER A O    
2081 C  CB   A SER A 219 ? 0.1951 0.0948 0.2635 -0.0027 0.0003  0.0057  220 SER A CB   
2082 C  CB   B SER A 219 ? 0.1949 0.1171 0.2623 0.0091  0.0017  -0.0027 220 SER A CB   
2083 O  OG   A SER A 219 ? 0.2166 0.0293 0.2343 0.0128  0.0025  -0.0253 220 SER A OG   
2084 O  OG   B SER A 219 ? 0.2073 0.1058 0.2608 0.0160  0.0074  0.0043  220 SER A OG   
2085 N  N    . GLU A 220 ? 0.2042 0.0436 0.1990 0.0052  0.0048  -0.0063 221 GLU A N    
2086 C  CA   . GLU A 220 ? 0.2168 0.1045 0.2319 0.0200  -0.0161 0.0108  221 GLU A CA   
2087 C  C    . GLU A 220 ? 0.2139 0.0952 0.2012 -0.0076 0.0076  -0.0109 221 GLU A C    
2088 O  O    . GLU A 220 ? 0.2157 0.1045 0.2342 0.0113  0.0498  -0.0068 221 GLU A O    
2089 C  CB   . GLU A 220 ? 0.2942 0.1189 0.2024 -0.0302 -0.0241 -0.0233 221 GLU A CB   
2090 C  CG   . GLU A 220 ? 0.3183 0.1841 0.2576 -0.0171 -0.0148 -0.0474 221 GLU A CG   
2091 C  CD   . GLU A 220 ? 0.3388 0.1764 0.3567 -0.0644 -0.0412 -0.0715 221 GLU A CD   
2092 O  OE1  . GLU A 220 ? 0.2477 0.1228 0.3355 -0.0834 -0.0024 -0.0359 221 GLU A OE1  
2093 O  OE2  . GLU A 220 ? 0.4796 0.2436 0.5130 -0.1237 0.0087  -0.0935 221 GLU A OE2  
2094 N  N    . GLN A 221 ? 0.1701 0.0767 0.1895 -0.0110 0.0046  -0.0068 222 GLN A N    
2095 C  CA   . GLN A 221 ? 0.1604 0.0654 0.2150 -0.0205 0.0197  0.0153  222 GLN A CA   
2096 C  C    . GLN A 221 ? 0.1733 0.0630 0.2161 0.0074  -0.0023 0.0076  222 GLN A C    
2097 O  O    . GLN A 221 ? 0.2056 0.0684 0.1947 -0.0342 0.0132  -0.0013 222 GLN A O    
2098 C  CB   . GLN A 221 ? 0.1633 0.0891 0.1972 -0.0265 -0.0087 -0.0037 222 GLN A CB   
2099 C  CG   . GLN A 221 ? 0.1439 0.1065 0.1927 -0.0379 0.0000  -0.0082 222 GLN A CG   
2100 C  CD   . GLN A 221 ? 0.1837 0.0451 0.2012 -0.0308 -0.0041 0.0173  222 GLN A CD   
2101 O  OE1  . GLN A 221 ? 0.1412 0.0502 0.1999 0.0226  -0.0261 0.0059  222 GLN A OE1  
2102 N  NE2  . GLN A 221 ? 0.1661 0.0341 0.2184 -0.0328 -0.0239 0.0200  222 GLN A NE2  
2103 N  N    . VAL A 222 ? 0.1755 0.0737 0.2096 -0.0262 -0.0328 0.0259  223 VAL A N    
2104 C  CA   . VAL A 222 ? 0.1744 0.0772 0.2141 0.0161  -0.0098 0.0340  223 VAL A CA   
2105 C  C    . VAL A 222 ? 0.1917 0.0487 0.2484 -0.0307 0.0288  0.0109  223 VAL A C    
2106 O  O    . VAL A 222 ? 0.1478 0.0984 0.2421 -0.0333 0.0208  0.0093  223 VAL A O    
2107 C  CB   . VAL A 222 ? 0.2218 0.1259 0.2419 -0.0395 -0.0346 0.0395  223 VAL A CB   
2108 C  CG1  . VAL A 222 ? 0.1615 0.1385 0.3156 -0.0351 0.0000  0.0295  223 VAL A CG1  
2109 C  CG2  . VAL A 222 ? 0.1776 0.1377 0.2691 0.0137  -0.0414 0.0238  223 VAL A CG2  
2110 N  N    . LEU A 223 ? 0.2080 0.0702 0.2572 -0.0182 0.0302  0.0000  224 LEU A N    
2111 C  CA   . LEU A 223 ? 0.2078 0.0718 0.2529 -0.0081 0.0383  -0.0046 224 LEU A CA   
2112 C  C    . LEU A 223 ? 0.2297 0.1108 0.2556 -0.0206 0.0219  -0.0076 224 LEU A C    
2113 O  O    . LEU A 223 ? 0.2114 0.1076 0.2632 -0.0132 0.0401  -0.0194 224 LEU A O    
2114 C  CB   . LEU A 223 ? 0.2962 0.1018 0.3138 -0.0423 0.0258  -0.0057 224 LEU A CB   
2115 C  CG   . LEU A 223 ? 0.3120 0.1694 0.2989 -0.0088 0.0230  -0.0253 224 LEU A CG   
2116 C  CD1  . LEU A 223 ? 0.3012 0.2437 0.3880 -0.0403 -0.0480 -0.0126 224 LEU A CD1  
2117 C  CD2  . LEU A 223 ? 0.2610 0.1811 0.4253 0.0147  0.0671  -0.0364 224 LEU A CD2  
2118 N  N    . LYS A 224 ? 0.1956 0.1092 0.2247 -0.0335 0.0175  0.0038  225 LYS A N    
2119 C  CA   . LYS A 224 ? 0.1956 0.0988 0.2267 -0.0130 -0.0082 0.0054  225 LYS A CA   
2120 C  C    . LYS A 224 ? 0.1701 0.0724 0.2087 -0.0076 -0.0082 0.0092  225 LYS A C    
2121 O  O    . LYS A 224 ? 0.2276 0.0670 0.1992 -0.0277 0.0230  0.0173  225 LYS A O    
2122 C  CB   . LYS A 224 ? 0.2224 0.1368 0.2311 -0.0120 -0.0019 0.0494  225 LYS A CB   
2123 C  CG   . LYS A 224 ? 0.2522 0.2060 0.2646 -0.0099 -0.0439 -0.0359 225 LYS A CG   
2124 C  CD   . LYS A 224 ? 0.2937 0.2191 0.3149 0.0040  -0.0283 -0.0394 225 LYS A CD   
2125 C  CE   . LYS A 224 ? 0.3461 0.2662 0.3251 -0.0395 -0.0776 -0.0390 225 LYS A CE   
2126 N  NZ   . LYS A 224 ? 0.3109 0.3300 0.3819 0.0142  -0.0364 -0.0271 225 LYS A NZ   
2127 N  N    . PHE A 225 ? 0.1484 0.0616 0.2005 0.0216  0.0098  0.0129  226 PHE A N    
2128 C  CA   . PHE A 225 ? 0.1385 0.0271 0.1958 0.0020  0.0297  0.0024  226 PHE A CA   
2129 C  C    . PHE A 225 ? 0.1710 0.0507 0.1553 0.0024  0.0164  -0.0071 226 PHE A C    
2130 O  O    . PHE A 225 ? 0.1773 0.0666 0.1877 -0.0207 0.0318  -0.0003 226 PHE A O    
2131 C  CB   . PHE A 225 ? 0.1216 0.0778 0.2030 0.0043  -0.0093 0.0052  226 PHE A CB   
2132 C  CG   . PHE A 225 ? 0.1547 0.0566 0.1917 -0.0218 0.0121  -0.0194 226 PHE A CG   
2133 C  CD1  . PHE A 225 ? 0.2448 0.0891 0.2035 0.0148  0.0175  0.0136  226 PHE A CD1  
2134 C  CD2  . PHE A 225 ? 0.1737 0.1532 0.2423 -0.0361 0.0208  -0.0683 226 PHE A CD2  
2135 C  CE1  . PHE A 225 ? 0.2170 0.1061 0.2486 0.0096  -0.0146 -0.0020 226 PHE A CE1  
2136 C  CE2  . PHE A 225 ? 0.1789 0.1798 0.2416 -0.0143 -0.0027 -0.0926 226 PHE A CE2  
2137 C  CZ   . PHE A 225 ? 0.1336 0.0715 0.2468 -0.0355 -0.0196 -0.0383 226 PHE A CZ   
2138 N  N    . ARG A 226 ? 0.1852 0.0469 0.1683 0.0137  0.0164  -0.0041 227 ARG A N    
2139 C  CA   . ARG A 226 ? 0.1823 0.0749 0.1654 -0.0232 0.0236  0.0038  227 ARG A CA   
2140 C  C    . ARG A 226 ? 0.1807 0.0328 0.1985 -0.0297 0.0148  0.0049  227 ARG A C    
2141 O  O    . ARG A 226 ? 0.1915 0.0853 0.2199 0.0130  0.0399  0.0020  227 ARG A O    
2142 C  CB   . ARG A 226 ? 0.2207 0.0544 0.1890 -0.0147 0.0228  0.0229  227 ARG A CB   
2143 C  CG   . ARG A 226 ? 0.1791 0.0711 0.2039 -0.0324 0.0239  0.0305  227 ARG A CG   
2144 C  CD   . ARG A 226 ? 0.2062 0.0900 0.1954 -0.0342 0.0324  0.0259  227 ARG A CD   
2145 N  NE   . ARG A 226 ? 0.1877 0.0749 0.2046 -0.0675 0.0200  0.0093  227 ARG A NE   
2146 C  CZ   . ARG A 226 ? 0.2114 0.0749 0.1852 -0.0373 0.0379  0.0017  227 ARG A CZ   
2147 N  NH1  . ARG A 226 ? 0.2696 0.1124 0.2215 -0.0303 0.0098  -0.0719 227 ARG A NH1  
2148 N  NH2  . ARG A 226 ? 0.1967 0.0631 0.2291 -0.0779 0.0565  -0.0049 227 ARG A NH2  
2149 N  N    . LYS A 227 ? 0.2146 0.0657 0.1484 -0.0388 0.0172  -0.0153 228 LYS A N    
2150 C  CA   . LYS A 227 ? 0.2150 0.0663 0.1848 -0.0318 0.0193  -0.0270 228 LYS A CA   
2151 C  C    . LYS A 227 ? 0.2060 0.0900 0.1547 -0.0375 0.0421  -0.0197 228 LYS A C    
2152 O  O    . LYS A 227 ? 0.2470 0.1164 0.1729 -0.0614 0.0368  -0.0165 228 LYS A O    
2153 C  CB   . LYS A 227 ? 0.2475 0.1110 0.1762 -0.0456 -0.0086 -0.0196 228 LYS A CB   
2154 C  CG   . LYS A 227 ? 0.3212 0.1491 0.2087 -0.0819 -0.0225 0.0076  228 LYS A CG   
2155 C  CD   . LYS A 227 ? 0.3476 0.2824 0.3055 -0.0524 0.0063  -0.0208 228 LYS A CD   
2156 C  CE   . LYS A 227 ? 0.4649 0.4027 0.3217 -0.0474 -0.0199 -0.0142 228 LYS A CE   
2157 N  NZ   . LYS A 227 ? 0.4577 0.3928 0.4142 -0.0987 -0.0653 -0.0275 228 LYS A NZ   
2158 N  N    . LEU A 228 ? 0.2222 0.0482 0.1762 -0.0386 0.0230  -0.0247 229 LEU A N    
2159 C  CA   . LEU A 228 ? 0.1888 0.0643 0.2017 -0.0619 0.0288  -0.0038 229 LEU A CA   
2160 C  C    . LEU A 228 ? 0.2127 0.0537 0.1705 -0.0581 0.0377  -0.0359 229 LEU A C    
2161 O  O    . LEU A 228 ? 0.2326 0.0458 0.1823 -0.0305 0.0348  -0.0172 229 LEU A O    
2162 C  CB   . LEU A 228 ? 0.2138 0.0520 0.1635 -0.0579 0.0211  -0.0239 229 LEU A CB   
2163 C  CG   . LEU A 228 ? 0.2193 0.1085 0.1683 -0.0388 0.0153  -0.0046 229 LEU A CG   
2164 C  CD1  . LEU A 228 ? 0.2358 0.1270 0.1647 -0.0627 0.0309  -0.0197 229 LEU A CD1  
2165 C  CD2  . LEU A 228 ? 0.2822 0.0842 0.1848 -0.0397 0.0131  0.0194  229 LEU A CD2  
2166 N  N    . ASN A 229 ? 0.2383 0.0742 0.1782 -0.0878 0.0299  -0.0120 230 ASN A N    
2167 C  CA   . ASN A 229 ? 0.2053 0.1256 0.1538 -0.0524 0.0408  -0.0175 230 ASN A CA   
2168 C  C    . ASN A 229 ? 0.2398 0.0943 0.1658 -0.0373 0.0410  -0.0020 230 ASN A C    
2169 O  O    . ASN A 229 ? 0.2351 0.0799 0.2082 -0.0454 0.0340  -0.0164 230 ASN A O    
2170 C  CB   . ASN A 229 ? 0.2655 0.1110 0.1760 -0.0693 0.0368  -0.0049 230 ASN A CB   
2171 C  CG   . ASN A 229 ? 0.2484 0.1140 0.1884 -0.0454 0.0318  -0.0416 230 ASN A CG   
2172 O  OD1  . ASN A 229 ? 0.3325 0.1306 0.2121 -0.0680 0.0741  -0.0478 230 ASN A OD1  
2173 N  ND2  . ASN A 229 ? 0.2535 0.1256 0.2028 -0.0746 0.0375  -0.0425 230 ASN A ND2  
2174 N  N    . PHE A 230 ? 0.1755 0.1081 0.1782 -0.0953 0.0427  -0.0065 231 PHE A N    
2175 C  CA   . PHE A 230 ? 0.1611 0.1228 0.1893 -0.1054 0.0485  0.0000  231 PHE A CA   
2176 C  C    . PHE A 230 ? 0.2143 0.1351 0.2081 -0.0815 0.0467  -0.0178 231 PHE A C    
2177 O  O    . PHE A 230 ? 0.2563 0.1115 0.2346 -0.1216 0.0573  0.0013  231 PHE A O    
2178 C  CB   . PHE A 230 ? 0.2211 0.1377 0.1647 -0.0658 0.0082  -0.0167 231 PHE A CB   
2179 C  CG   . PHE A 230 ? 0.2121 0.1173 0.1927 -0.0706 0.0395  -0.0163 231 PHE A CG   
2180 C  CD1  . PHE A 230 ? 0.2125 0.1415 0.1651 -0.0249 0.0054  -0.0511 231 PHE A CD1  
2181 C  CD2  . PHE A 230 ? 0.2351 0.1094 0.1735 -0.0040 0.0303  -0.0243 231 PHE A CD2  
2182 C  CE1  . PHE A 230 ? 0.2702 0.1140 0.1751 -0.0478 -0.0024 -0.0445 231 PHE A CE1  
2183 C  CE2  . PHE A 230 ? 0.1956 0.1011 0.1996 -0.0231 0.0483  -0.0370 231 PHE A CE2  
2184 C  CZ   . PHE A 230 ? 0.2056 0.1092 0.1931 -0.0445 0.0274  -0.0307 231 PHE A CZ   
2185 N  N    . ASN A 231 ? 0.2166 0.1334 0.1969 -0.0975 0.0820  -0.0285 232 ASN A N    
2186 C  CA   . ASN A 231 ? 0.2344 0.1412 0.2107 -0.0948 0.0772  -0.0296 232 ASN A CA   
2187 C  C    . ASN A 231 ? 0.1888 0.1218 0.2085 -0.0566 0.0640  -0.0320 232 ASN A C    
2188 O  O    . ASN A 231 ? 0.2536 0.1254 0.2139 -0.0649 0.0549  -0.0240 232 ASN A O    
2189 C  CB   . ASN A 231 ? 0.2227 0.1234 0.2103 -0.0789 0.0825  -0.0340 232 ASN A CB   
2190 C  CG   . ASN A 231 ? 0.2511 0.1550 0.2064 -0.0798 0.0271  0.0182  232 ASN A CG   
2191 O  OD1  . ASN A 231 ? 0.3197 0.1380 0.2114 -0.0794 0.0746  -0.0222 232 ASN A OD1  
2192 N  ND2  . ASN A 231 ? 0.2838 0.1556 0.2087 -0.0482 0.0494  -0.0216 232 ASN A ND2  
2193 N  N    . GLY A 232 ? 0.2818 0.1177 0.2078 -0.0746 0.0577  -0.0153 233 GLY A N    
2194 C  CA   . GLY A 232 ? 0.2518 0.1385 0.2351 -0.0297 0.0601  -0.0012 233 GLY A CA   
2195 C  C    . GLY A 232 ? 0.1938 0.1532 0.2378 -0.0359 -0.0013 0.0263  233 GLY A C    
2196 O  O    . GLY A 232 ? 0.2633 0.1816 0.2408 -0.0366 0.1089  0.0272  233 GLY A O    
2197 N  N    . GLU A 233 ? 0.2231 0.1552 0.2218 -0.0351 0.0467  0.0063  234 GLU A N    
2198 C  CA   . GLU A 233 ? 0.1776 0.1308 0.2179 -0.0092 0.0152  0.0087  234 GLU A CA   
2199 C  C    . GLU A 233 ? 0.2164 0.1922 0.2418 -0.0125 0.0182  -0.0183 234 GLU A C    
2200 O  O    . GLU A 233 ? 0.2380 0.1812 0.2357 -0.0054 0.0140  0.0092  234 GLU A O    
2201 C  CB   . GLU A 233 ? 0.1769 0.1255 0.2443 -0.0263 0.0006  0.0252  234 GLU A CB   
2202 C  CG   . GLU A 233 ? 0.1877 0.2132 0.2055 -0.0768 0.0243  0.0364  234 GLU A CG   
2203 C  CD   . GLU A 233 ? 0.3700 0.2745 0.3503 0.0447  0.0062  -0.0086 234 GLU A CD   
2204 O  OE1  . GLU A 233 ? 0.3535 0.2915 0.3804 0.0076  0.0408  -0.0063 234 GLU A OE1  
2205 O  OE2  . GLU A 233 ? 0.3325 0.2506 0.3242 0.0102  -0.0465 0.0000  234 GLU A OE2  
2206 N  N    . GLY A 234 ? 0.2393 0.1593 0.2364 -0.0085 0.0483  0.0082  235 GLY A N    
2207 C  CA   . GLY A 234 ? 0.2529 0.1708 0.2802 0.0088  0.0065  -0.0076 235 GLY A CA   
2208 C  C    . GLY A 234 ? 0.2547 0.1735 0.2297 0.0027  0.0161  0.0320  235 GLY A C    
2209 O  O    . GLY A 234 ? 0.2745 0.2887 0.2743 0.0559  0.0838  -0.0216 235 GLY A O    
2210 N  N    . GLU A 235 ? 0.2383 0.1746 0.2333 0.0010  0.0397  0.0063  236 GLU A N    
2211 C  CA   . GLU A 235 ? 0.2179 0.1367 0.2376 0.0082  0.0203  0.0275  236 GLU A CA   
2212 C  C    . GLU A 235 ? 0.2150 0.2109 0.2691 -0.0103 0.0553  0.0222  236 GLU A C    
2213 O  O    . GLU A 235 ? 0.3032 0.1956 0.2924 -0.0176 0.0276  0.0136  236 GLU A O    
2214 C  CB   . GLU A 235 ? 0.1956 0.1446 0.2578 0.0143  0.0292  0.0247  236 GLU A CB   
2215 C  CG   . GLU A 235 ? 0.2531 0.1588 0.2560 -0.0326 0.0296  -0.0087 236 GLU A CG   
2216 C  CD   . GLU A 235 ? 0.3388 0.1660 0.3145 0.0164  0.0250  0.0252  236 GLU A CD   
2217 O  OE1  . GLU A 235 ? 0.2788 0.2038 0.3474 -0.0183 0.0456  0.0159  236 GLU A OE1  
2218 O  OE2  . GLU A 235 ? 0.4300 0.2804 0.3946 -0.1071 0.1044  -0.0060 236 GLU A OE2  
2219 N  N    . PRO A 236 ? 0.2100 0.1507 0.2283 -0.0175 0.0895  0.0540  237 PRO A N    
2220 C  CA   . PRO A 236 ? 0.2283 0.1794 0.2606 -0.0096 0.0869  0.0176  237 PRO A CA   
2221 C  C    . PRO A 236 ? 0.2563 0.1600 0.2328 -0.0722 0.1014  -0.0113 237 PRO A C    
2222 O  O    . PRO A 236 ? 0.2572 0.1608 0.2283 -0.0535 0.0812  -0.0339 237 PRO A O    
2223 C  CB   . PRO A 236 ? 0.1543 0.2567 0.2813 -0.0059 0.1014  0.0109  237 PRO A CB   
2224 C  CG   . PRO A 236 ? 0.2971 0.2346 0.3027 0.0263  0.0689  0.0882  237 PRO A CG   
2225 C  CD   . PRO A 236 ? 0.2500 0.2326 0.2808 0.0115  0.0627  0.0187  237 PRO A CD   
2226 N  N    . GLU A 237 ? 0.2383 0.1263 0.2698 -0.0568 0.0649  -0.0060 238 GLU A N    
2227 C  CA   . GLU A 237 ? 0.2842 0.1449 0.2261 -0.0505 0.0671  -0.0155 238 GLU A CA   
2228 C  C    . GLU A 237 ? 0.2303 0.1592 0.2561 -0.1004 0.0482  -0.0273 238 GLU A C    
2229 O  O    . GLU A 237 ? 0.2019 0.1784 0.2236 -0.0384 0.0476  -0.0295 238 GLU A O    
2230 C  CB   . GLU A 237 ? 0.2777 0.1232 0.2624 -0.0087 0.0113  -0.0370 238 GLU A CB   
2231 C  CG   . GLU A 237 ? 0.2833 0.1730 0.2416 -0.0155 0.0218  -0.0243 238 GLU A CG   
2232 C  CD   . GLU A 237 ? 0.2757 0.1388 0.2998 -0.0104 0.0252  -0.0137 238 GLU A CD   
2233 O  OE1  . GLU A 237 ? 0.2838 0.2274 0.3632 0.0062  -0.0254 -0.0938 238 GLU A OE1  
2234 O  OE2  . GLU A 237 ? 0.2504 0.1115 0.2561 -0.0137 0.0379  -0.0410 238 GLU A OE2  
2235 N  N    . GLU A 238 ? 0.2019 0.1254 0.1985 -0.0887 0.0630  -0.0500 239 GLU A N    
2236 C  CA   . GLU A 238 ? 0.1969 0.1905 0.2412 -0.0970 0.0410  -0.0208 239 GLU A CA   
2237 C  C    . GLU A 238 ? 0.1435 0.1428 0.1719 -0.0754 0.0684  -0.0439 239 GLU A C    
2238 O  O    . GLU A 238 ? 0.2581 0.1455 0.2107 -0.0732 0.0428  -0.0458 239 GLU A O    
2239 C  CB   . GLU A 238 ? 0.2125 0.2164 0.2529 -0.1195 0.0507  -0.0531 239 GLU A CB   
2240 C  CG   . GLU A 238 ? 0.2538 0.2955 0.3240 -0.0384 0.0251  0.0082  239 GLU A CG   
2241 C  CD   . GLU A 238 ? 0.1489 0.2344 0.5073 0.0860  0.1360  0.0362  239 GLU A CD   
2242 O  OE1  . GLU A 238 ? 0.4753 0.4067 0.5048 -0.0017 0.0000  0.0297  239 GLU A OE1  
2243 O  OE2  . GLU A 238 ? 0.2662 0.6359 0.3768 -0.1032 0.0165  -0.0182 239 GLU A OE2  
2244 N  N    . LEU A 239 ? 0.1593 0.1340 0.1665 -0.0759 0.0432  -0.0238 240 LEU A N    
2245 C  CA   . LEU A 239 ? 0.1203 0.1256 0.1839 -0.0428 0.0675  -0.0248 240 LEU A CA   
2246 C  C    . LEU A 239 ? 0.1297 0.0846 0.1818 -0.0386 0.0368  -0.0198 240 LEU A C    
2247 O  O    . LEU A 239 ? 0.1342 0.1329 0.1881 -0.0582 0.0353  -0.0262 240 LEU A O    
2248 C  CB   . LEU A 239 ? 0.1819 0.1121 0.1951 -0.0214 -0.0012 -0.0197 240 LEU A CB   
2249 C  CG   . LEU A 239 ? 0.1094 0.1392 0.1976 -0.0445 0.0062  -0.0098 240 LEU A CG   
2250 C  CD1  . LEU A 239 ? 0.2110 0.1304 0.3248 -0.0098 -0.0251 -0.0308 240 LEU A CD1  
2251 C  CD2  . LEU A 239 ? 0.1324 0.1137 0.2251 0.0148  0.0010  -0.0242 240 LEU A CD2  
2252 N  N    . MET A 240 ? 0.1559 0.0819 0.1872 -0.0219 0.0564  -0.0211 241 MET A N    
2253 C  CA   . MET A 240 ? 0.1859 0.0788 0.1732 -0.0293 0.0516  -0.0194 241 MET A CA   
2254 C  C    . MET A 240 ? 0.1203 0.0613 0.1825 -0.0538 0.0241  -0.0164 241 MET A C    
2255 O  O    . MET A 240 ? 0.1553 0.0873 0.1847 -0.0644 0.0460  -0.0126 241 MET A O    
2256 C  CB   . MET A 240 ? 0.2078 0.1378 0.1717 -0.0031 0.0310  -0.0240 241 MET A CB   
2257 C  CG   . MET A 240 ? 0.1599 0.1248 0.1854 -0.0489 0.0832  -0.0355 241 MET A CG   
2258 S  SD   . MET A 240 ? 0.2423 0.0697 0.2102 -0.0412 0.0520  -0.0143 241 MET A SD   
2259 C  CE   . MET A 240 ? 0.2214 0.0781 0.1990 -0.0970 0.0617  -0.0035 241 MET A CE   
2260 N  N    . VAL A 241 ? 0.1500 0.0749 0.1586 -0.0230 0.0285  -0.0054 242 VAL A N    
2261 C  CA   . VAL A 241 ? 0.1313 0.0354 0.1678 0.0027  0.0181  -0.0065 242 VAL A CA   
2262 C  C    . VAL A 241 ? 0.1225 0.0446 0.1692 -0.0192 0.0170  -0.0229 242 VAL A C    
2263 O  O    . VAL A 241 ? 0.1422 0.0733 0.2042 -0.0662 0.0460  -0.0210 242 VAL A O    
2264 C  CB   . VAL A 241 ? 0.1187 0.0803 0.1880 -0.0170 0.0351  0.0057  242 VAL A CB   
2265 C  CG1  . VAL A 241 ? 0.1225 0.1223 0.2030 -0.0754 0.0249  -0.0368 242 VAL A CG1  
2266 C  CG2  . VAL A 241 ? 0.1431 0.0546 0.2204 -0.0287 0.0357  -0.0155 242 VAL A CG2  
2267 N  N    . ASP A 242 ? 0.1067 0.0414 0.1589 -0.0186 0.0281  -0.0076 243 ASP A N    
2268 C  CA   . ASP A 242 ? 0.0871 0.0417 0.1816 0.0099  0.0320  -0.0052 243 ASP A CA   
2269 C  C    . ASP A 242 ? 0.0631 0.0643 0.1940 -0.0353 0.0340  -0.0031 243 ASP A C    
2270 O  O    . ASP A 242 ? 0.0817 0.0579 0.2240 -0.0153 0.0299  -0.0381 243 ASP A O    
2271 C  CB   . ASP A 242 ? 0.0667 0.0255 0.2050 0.0020  0.0066  0.0049  243 ASP A CB   
2272 C  CG   . ASP A 242 ? 0.0954 0.0677 0.1719 0.0000  0.0381  -0.0209 243 ASP A CG   
2273 O  OD1  . ASP A 242 ? 0.1218 0.0320 0.1926 -0.0010 0.0537  -0.0200 243 ASP A OD1  
2274 O  OD2  . ASP A 242 ? 0.1124 0.0623 0.2473 0.0118  0.0414  -0.0253 243 ASP A OD2  
2275 N  N    . ASN A 243 ? 0.1056 0.0322 0.1744 -0.0204 0.0489  -0.0265 244 ASN A N    
2276 C  CA   . ASN A 243 ? 0.0957 0.0334 0.1538 -0.0232 0.0223  -0.0137 244 ASN A CA   
2277 C  C    . ASN A 243 ? 0.0973 0.0595 0.1641 -0.0493 0.0207  -0.0205 244 ASN A C    
2278 O  O    . ASN A 243 ? 0.1036 0.0625 0.1783 0.0109  0.0292  0.0054  244 ASN A O    
2279 C  CB   . ASN A 243 ? 0.1092 0.0876 0.1615 -0.0548 0.0063  -0.0252 244 ASN A CB   
2280 C  CG   . ASN A 243 ? 0.1097 0.0257 0.1843 -0.0024 0.0261  0.0060  244 ASN A CG   
2281 O  OD1  . ASN A 243 ? 0.1338 0.0450 0.2037 -0.0221 0.0315  0.0286  244 ASN A OD1  
2282 N  ND2  . ASN A 243 ? 0.1987 0.1027 0.2164 -0.0812 -0.0146 0.0553  244 ASN A ND2  
2283 N  N    . TRP A 244 ? 0.0634 0.0386 0.1527 -0.0190 0.0165  0.0124  245 TRP A N    
2284 C  CA   . TRP A 244 ? 0.0781 0.0458 0.1388 -0.0313 0.0012  -0.0149 245 TRP A CA   
2285 C  C    . TRP A 244 ? 0.0954 0.0390 0.1448 0.0077  0.0326  0.0048  245 TRP A C    
2286 O  O    . TRP A 244 ? 0.0693 0.0556 0.1762 0.0276  0.0211  -0.0109 245 TRP A O    
2287 C  CB   . TRP A 244 ? 0.0754 0.0307 0.1651 -0.0162 0.0040  -0.0046 245 TRP A CB   
2288 C  CG   . TRP A 244 ? 0.0810 0.0490 0.1689 -0.0010 0.0227  -0.0093 245 TRP A CG   
2289 C  CD1  . TRP A 244 ? 0.0658 0.0582 0.1723 0.0065  0.0344  -0.0115 245 TRP A CD1  
2290 C  CD2  . TRP A 244 ? 0.0873 0.0368 0.1455 -0.0194 0.0074  -0.0152 245 TRP A CD2  
2291 N  NE1  . TRP A 244 ? 0.0618 0.0354 0.1746 0.0171  0.0220  -0.0068 245 TRP A NE1  
2292 C  CE2  . TRP A 244 ? 0.0816 0.0539 0.1732 -0.0399 -0.0031 -0.0043 245 TRP A CE2  
2293 C  CE3  . TRP A 244 ? 0.0894 0.0746 0.1626 -0.0561 -0.0060 0.0095  245 TRP A CE3  
2294 C  CZ2  . TRP A 244 ? 0.0860 0.0258 0.2132 -0.0057 0.0083  -0.0007 245 TRP A CZ2  
2295 C  CZ3  . TRP A 244 ? 0.0842 0.0679 0.1933 -0.0208 0.0379  0.0017  245 TRP A CZ3  
2296 C  CH2  . TRP A 244 ? 0.1013 0.0582 0.2033 -0.0230 0.0012  0.0063  245 TRP A CH2  
2297 N  N    . ARG A 245 ? 0.0583 0.0419 0.1401 -0.0197 0.0054  -0.0263 246 ARG A N    
2298 C  CA   . ARG A 245 ? 0.0797 0.0641 0.1632 0.0046  0.0113  -0.0185 246 ARG A CA   
2299 C  C    . ARG A 245 ? 0.0634 0.0587 0.1607 -0.0052 0.0218  -0.0254 246 ARG A C    
2300 O  O    . ARG A 245 ? 0.0618 0.0528 0.1877 -0.0109 0.0172  0.0153  246 ARG A O    
2301 C  CB   . ARG A 245 ? 0.0575 0.0456 0.1604 -0.0115 0.0102  -0.0317 246 ARG A CB   
2302 C  CG   . ARG A 245 ? 0.0366 0.0524 0.1870 -0.0120 -0.0081 -0.0346 246 ARG A CG   
2303 C  CD   . ARG A 245 ? 0.0431 0.0745 0.2026 -0.0263 0.0020  -0.0450 246 ARG A CD   
2304 N  NE   . ARG A 245 ? 0.0511 0.0785 0.2053 -0.0350 0.0107  -0.0467 246 ARG A NE   
2305 C  CZ   . ARG A 245 ? 0.0427 0.0625 0.1665 -0.0252 0.0148  -0.0264 246 ARG A CZ   
2306 N  NH1  . ARG A 245 ? 0.0706 0.0595 0.2117 0.0163  0.0489  -0.0185 246 ARG A NH1  
2307 N  NH2  . ARG A 245 ? 0.0486 0.1126 0.2153 -0.0443 0.0124  -0.0020 246 ARG A NH2  
2308 N  N    . PRO A 246 ? 0.0776 0.0916 0.1832 0.0092  0.0282  0.0034  247 PRO A N    
2309 C  CA   . PRO A 246 ? 0.0636 0.0681 0.1663 0.0043  0.0276  0.0071  247 PRO A CA   
2310 C  C    . PRO A 246 ? 0.1115 0.0767 0.1505 0.0125  0.0068  0.0091  247 PRO A C    
2311 O  O    . PRO A 246 ? 0.0666 0.0307 0.2181 0.0148  -0.0043 0.0000  247 PRO A O    
2312 C  CB   . PRO A 246 ? 0.0943 0.0772 0.2161 0.0046  0.0384  0.0126  247 PRO A CB   
2313 C  CG   . PRO A 246 ? 0.0948 0.1765 0.3106 0.0478  0.0348  0.1080  247 PRO A CG   
2314 C  CD   . PRO A 246 ? 0.0754 0.0794 0.2288 0.0026  0.0421  0.0148  247 PRO A CD   
2315 N  N    . ALA A 247 ? 0.0776 0.0627 0.1629 0.0035  0.0076  0.0170  248 ALA A N    
2316 C  CA   . ALA A 247 ? 0.0596 0.0557 0.1812 -0.0254 -0.0085 0.0020  248 ALA A CA   
2317 C  C    . ALA A 247 ? 0.0573 0.0636 0.1712 0.0019  0.0027  -0.0092 248 ALA A C    
2318 O  O    . ALA A 247 ? 0.0758 0.0907 0.2117 0.0260  -0.0031 -0.0093 248 ALA A O    
2319 C  CB   . ALA A 247 ? 0.1280 0.0765 0.1689 0.0121  0.0230  0.0087  248 ALA A CB   
2320 N  N    . GLN A 248 ? 0.0592 0.0700 0.1478 -0.0087 0.0051  -0.0194 249 GLN A N    
2321 C  CA   . GLN A 248 ? 0.0848 0.0848 0.1665 0.0142  -0.0027 -0.0115 249 GLN A CA   
2322 C  C    . GLN A 248 ? 0.0964 0.0825 0.1739 0.0494  -0.0259 -0.0013 249 GLN A C    
2323 O  O    . GLN A 248 ? 0.0959 0.1117 0.1841 -0.0003 -0.0007 -0.0074 249 GLN A O    
2324 C  CB   . GLN A 248 ? 0.0697 0.0631 0.2006 -0.0046 -0.0052 -0.0098 249 GLN A CB   
2325 C  CG   . GLN A 248 ? 0.0670 0.0693 0.1956 -0.0175 -0.0137 -0.0175 249 GLN A CG   
2326 C  CD   . GLN A 248 ? 0.0430 0.1331 0.1999 -0.0215 -0.0068 0.0121  249 GLN A CD   
2327 O  OE1  . GLN A 248 ? 0.0769 0.1458 0.2195 -0.0225 0.0031  -0.0302 249 GLN A OE1  
2328 N  NE2  . GLN A 248 ? 0.0749 0.1311 0.1829 -0.0164 -0.0013 -0.0137 249 GLN A NE2  
2329 N  N    . PRO A 249 ? 0.0995 0.1577 0.1888 0.0297  -0.0172 -0.0118 250 PRO A N    
2330 C  CA   . PRO A 249 ? 0.1225 0.1977 0.1959 0.0623  -0.0082 -0.0097 250 PRO A CA   
2331 C  C    . PRO A 249 ? 0.1049 0.0984 0.1830 0.0546  -0.0271 -0.0020 250 PRO A C    
2332 O  O    . PRO A 249 ? 0.1058 0.1126 0.1999 0.0403  -0.0186 0.0098  250 PRO A O    
2333 C  CB   . PRO A 249 ? 0.1128 0.2432 0.2132 0.0675  -0.0305 -0.0351 250 PRO A CB   
2334 C  CG   . PRO A 249 ? 0.1468 0.2651 0.2206 -0.0188 -0.0549 -0.0303 250 PRO A CG   
2335 C  CD   . PRO A 249 ? 0.0612 0.1969 0.2274 0.0487  -0.0458 -0.0103 250 PRO A CD   
2336 N  N    . LEU A 250 ? 0.0943 0.1115 0.2046 0.0768  0.0031  -0.0080 251 LEU A N    
2337 C  CA   . LEU A 250 ? 0.0812 0.1054 0.1811 0.0115  -0.0115 -0.0073 251 LEU A CA   
2338 C  C    . LEU A 250 ? 0.0878 0.1189 0.2211 0.0417  -0.0188 0.0000  251 LEU A C    
2339 O  O    . LEU A 250 ? 0.0704 0.0900 0.2527 0.0306  -0.0118 -0.0013 251 LEU A O    
2340 C  CB   . LEU A 250 ? 0.1324 0.0936 0.2283 0.0131  -0.0076 0.0266  251 LEU A CB   
2341 C  CG   . LEU A 250 ? 0.1246 0.1247 0.1945 -0.0344 0.0265  0.0228  251 LEU A CG   
2342 C  CD1  . LEU A 250 ? 0.1532 0.1133 0.1920 -0.0461 -0.0219 -0.0218 251 LEU A CD1  
2343 C  CD2  . LEU A 250 ? 0.2407 0.1545 0.2504 -0.0379 0.0364  0.0154  251 LEU A CD2  
2344 N  N    . LYS A 251 ? 0.1178 0.1311 0.2275 0.0193  -0.0527 -0.0189 252 LYS A N    
2345 C  CA   . LYS A 251 ? 0.0903 0.1575 0.2227 0.0264  -0.0164 -0.0244 252 LYS A CA   
2346 C  C    . LYS A 251 ? 0.1194 0.1428 0.2432 0.0483  -0.0251 -0.0186 252 LYS A C    
2347 O  O    . LYS A 251 ? 0.1843 0.2229 0.2524 0.0015  0.0294  0.0082  252 LYS A O    
2348 C  CB   . LYS A 251 ? 0.1457 0.1604 0.2615 -0.0054 -0.0232 -0.0329 252 LYS A CB   
2349 C  CG   . LYS A 251 ? 0.2229 0.1615 0.2761 -0.0120 0.0068  -0.0741 252 LYS A CG   
2350 C  CD   . LYS A 251 ? 0.1528 0.3106 0.3278 0.0436  0.0296  -0.0219 252 LYS A CD   
2351 C  CE   . LYS A 251 ? 0.1092 0.2330 0.3862 0.0480  0.0062  0.0156  252 LYS A CE   
2352 N  NZ   . LYS A 251 ? 0.1927 0.2901 0.4465 -0.0154 -0.0315 0.0308  252 LYS A NZ   
2353 N  N    . ASN A 252 ? 0.1458 0.1392 0.2028 0.0494  -0.0143 -0.0535 253 ASN A N    
2354 C  CA   . ASN A 252 ? 0.1669 0.2610 0.3104 0.0182  -0.0189 -0.0230 253 ASN A CA   
2355 C  C    . ASN A 252 ? 0.1981 0.2091 0.2944 0.0294  -0.0031 -0.0294 253 ASN A C    
2356 O  O    . ASN A 252 ? 0.2745 0.2337 0.3314 0.0560  0.0024  0.0102  253 ASN A O    
2357 C  CB   . ASN A 252 ? 0.2581 0.2705 0.3339 0.0273  -0.0076 -0.0701 253 ASN A CB   
2358 C  CG   . ASN A 252 ? 0.2732 0.3079 0.3519 0.0326  -0.0186 0.0003  253 ASN A CG   
2359 O  OD1  . ASN A 252 ? 0.3910 0.4520 0.4099 -0.0017 0.0337  -0.0077 253 ASN A OD1  
2360 N  ND2  . ASN A 252 ? 0.2901 0.3109 0.4278 0.0017  -0.0386 -0.0410 253 ASN A ND2  
2361 N  N    . ARG A 253 ? 0.1318 0.1818 0.2347 0.0148  0.0080  -0.0063 254 ARG A N    
2362 C  CA   . ARG A 253 ? 0.0846 0.0986 0.1758 0.0146  0.0020  -0.0007 254 ARG A CA   
2363 C  C    . ARG A 253 ? 0.1721 0.0846 0.2055 0.0175  -0.0197 -0.0164 254 ARG A C    
2364 O  O    . ARG A 253 ? 0.1791 0.1361 0.2527 0.0170  0.0406  0.0219  254 ARG A O    
2365 C  CB   . ARG A 253 ? 0.0740 0.0688 0.1843 0.0390  -0.0035 -0.0160 254 ARG A CB   
2366 C  CG   . ARG A 253 ? 0.1128 0.0557 0.1604 0.0194  0.0280  -0.0154 254 ARG A CG   
2367 C  CD   . ARG A 253 ? 0.0930 0.0649 0.1611 0.0270  0.0353  -0.0173 254 ARG A CD   
2368 N  NE   . ARG A 253 ? 0.0582 0.0643 0.1554 0.0142  0.0153  -0.0241 254 ARG A NE   
2369 C  CZ   . ARG A 253 ? 0.0609 0.0501 0.1347 -0.0115 0.0240  -0.0031 254 ARG A CZ   
2370 N  NH1  . ARG A 253 ? 0.0454 0.0524 0.1715 -0.0173 -0.0241 0.0214  254 ARG A NH1  
2371 N  NH2  . ARG A 253 ? 0.0402 0.0285 0.1640 -0.0017 -0.0013 -0.0170 254 ARG A NH2  
2372 N  N    . GLN A 254 ? 0.1081 0.1324 0.2107 0.0030  -0.0104 -0.0406 255 GLN A N    
2373 C  CA   . GLN A 254 ? 0.1283 0.1505 0.1852 -0.0068 -0.0208 -0.0560 255 GLN A CA   
2374 C  C    . GLN A 254 ? 0.1401 0.1351 0.1999 0.0085  -0.0113 -0.0126 255 GLN A C    
2375 O  O    . GLN A 254 ? 0.1812 0.1331 0.2459 -0.0115 -0.0524 -0.0049 255 GLN A O    
2376 C  CB   . GLN A 254 ? 0.1683 0.2049 0.2150 -0.0041 -0.0035 -0.0579 255 GLN A CB   
2377 C  CG   . GLN A 254 ? 0.3467 0.4272 0.3750 -0.0549 0.0401  -0.0198 255 GLN A CG   
2378 C  CD   . GLN A 254 ? 0.5371 0.5052 0.5047 -0.0188 -0.0247 0.0342  255 GLN A CD   
2379 O  OE1  . GLN A 254 ? 0.6158 0.6510 0.5716 -0.0174 -0.0780 -0.0006 255 GLN A OE1  
2380 N  NE2  . GLN A 254 ? 0.5726 0.5583 0.3138 -0.0847 0.0082  -0.0230 255 GLN A NE2  
2381 N  N    . ILE A 255 ? 0.1108 0.0898 0.1829 -0.0137 -0.0129 -0.0233 256 ILE A N    
2382 C  CA   . ILE A 255 ? 0.1155 0.0873 0.1690 -0.0143 0.0031  -0.0051 256 ILE A CA   
2383 C  C    . ILE A 255 ? 0.0909 0.0961 0.1737 0.0255  0.0164  0.0164  256 ILE A C    
2384 O  O    . ILE A 255 ? 0.1500 0.0798 0.1888 0.0315  0.0136  0.0230  256 ILE A O    
2385 C  CB   . ILE A 255 ? 0.1230 0.0977 0.1830 -0.0043 -0.0203 -0.0230 256 ILE A CB   
2386 C  CG1  . ILE A 255 ? 0.0943 0.1153 0.2130 0.0482  0.0207  -0.0370 256 ILE A CG1  
2387 C  CG2  . ILE A 255 ? 0.1237 0.1169 0.1649 -0.0274 0.0102  -0.0137 256 ILE A CG2  
2388 C  CD1  . ILE A 255 ? 0.1344 0.1180 0.2132 -0.0414 0.0307  -0.0208 256 ILE A CD1  
2389 N  N    . LYS A 256 ? 0.0654 0.1070 0.1775 0.0249  0.0082  -0.0024 257 LYS A N    
2390 C  CA   . LYS A 256 ? 0.0997 0.0973 0.1825 0.0303  0.0115  0.0099  257 LYS A CA   
2391 C  C    . LYS A 256 ? 0.0848 0.0886 0.1808 0.0068  0.0204  0.0077  257 LYS A C    
2392 O  O    . LYS A 256 ? 0.1088 0.1203 0.1775 -0.0494 0.0219  0.0010  257 LYS A O    
2393 C  CB   . LYS A 256 ? 0.0991 0.0851 0.2150 0.0148  0.0185  -0.0167 257 LYS A CB   
2394 C  CG   . LYS A 256 ? 0.2172 0.1237 0.3030 0.0098  0.0337  -0.0601 257 LYS A CG   
2395 C  CD   . LYS A 256 ? 0.2919 0.2039 0.3221 0.0480  -0.0285 -0.0430 257 LYS A CD   
2396 C  CE   . LYS A 256 ? 0.4498 0.4052 0.4272 0.0329  -0.0284 -0.0533 257 LYS A CE   
2397 N  NZ   . LYS A 256 ? 0.3910 0.4581 0.5156 -0.0124 0.0124  -0.0425 257 LYS A NZ   
2398 N  N    . ALA A 257 ? 0.0769 0.0848 0.1773 -0.0258 0.0416  0.0000  258 ALA A N    
2399 C  CA   . ALA A 257 ? 0.0873 0.0988 0.1870 -0.0019 0.0225  -0.0076 258 ALA A CA   
2400 C  C    . ALA A 257 ? 0.0968 0.0663 0.1649 -0.0296 0.0357  0.0103  258 ALA A C    
2401 O  O    . ALA A 257 ? 0.1024 0.1453 0.1830 -0.0182 0.0282  0.0020  258 ALA A O    
2402 C  CB   . ALA A 257 ? 0.1376 0.0913 0.2211 -0.0273 0.0160  -0.0027 258 ALA A CB   
2403 N  N    . SER A 258 ? 0.0930 0.0844 0.1949 0.0120  0.0364  0.0087  259 SER A N    
2404 C  CA   . SER A 258 ? 0.1191 0.1518 0.2103 0.0037  0.0335  0.0071  259 SER A CA   
2405 C  C    . SER A 258 ? 0.1092 0.1663 0.1962 0.0148  0.0568  -0.0060 259 SER A C    
2406 O  O    . SER A 258 ? 0.1004 0.2110 0.2766 0.0227  0.0535  0.0035  259 SER A O    
2407 C  CB   . SER A 258 ? 0.1234 0.1067 0.2200 -0.0006 -0.0132 0.0151  259 SER A CB   
2408 O  OG   . SER A 258 ? 0.1243 0.1164 0.2188 -0.0270 0.0439  -0.0118 259 SER A OG   
2409 N  N    . PHE A 259 ? 0.0943 0.1545 0.2644 -0.0441 0.0331  0.0241  260 PHE A N    
2410 C  CA   . PHE A 259 ? 0.1288 0.1642 0.2770 -0.0494 0.0299  0.0263  260 PHE A CA   
2411 C  C    . PHE A 259 ? 0.2020 0.2326 0.3048 -0.0753 0.0518  0.0372  260 PHE A C    
2412 O  O    . PHE A 259 ? 0.2448 0.1593 0.2960 -0.0604 0.0114  0.0412  260 PHE A O    
2413 C  CB   . PHE A 259 ? 0.1383 0.2056 0.2865 -0.0244 0.0208  -0.0052 260 PHE A CB   
2414 C  CG   . PHE A 259 ? 0.1070 0.1473 0.3138 -0.0065 0.0052  0.0093  260 PHE A CG   
2415 C  CD1  . PHE A 259 ? 0.1056 0.1194 0.2527 -0.0331 0.0228  -0.0217 260 PHE A CD1  
2416 C  CD2  . PHE A 259 ? 0.1812 0.1744 0.2533 -0.0115 0.0318  0.0216  260 PHE A CD2  
2417 C  CE1  . PHE A 259 ? 0.1180 0.1158 0.3045 -0.0194 0.0052  -0.0131 260 PHE A CE1  
2418 C  CE2  . PHE A 259 ? 0.1464 0.1952 0.3158 -0.0264 -0.0193 -0.0153 260 PHE A CE2  
2419 C  CZ   . PHE A 259 ? 0.1570 0.1740 0.3287 -0.0135 -0.0147 -0.0015 260 PHE A CZ   
2420 N  N    . LYS A 260 ? 0.2698 0.2865 0.3817 -0.1045 0.0366  0.0351  261 LYS A N    
2421 C  CA   . LYS A 260 ? 0.4767 0.4179 0.4678 -0.0342 0.0027  0.0439  261 LYS A CA   
2422 C  C    . LYS A 260 ? 0.5302 0.4616 0.5447 -0.0189 -0.0225 0.0388  261 LYS A C    
2423 O  O    . LYS A 260 ? 0.6212 0.5012 0.6273 0.0003  -0.0109 0.0623  261 LYS A O    
2424 C  CB   . LYS A 260 ? 0.4735 0.3844 0.4692 -0.0441 0.0219  0.0595  261 LYS A CB   
2425 C  CG   . LYS A 260 ? 0.5120 0.4433 0.4951 -0.0619 0.0208  0.0324  261 LYS A CG   
2426 C  CD   . LYS A 260 ? 0.4951 0.4666 0.4871 -0.0093 0.0057  0.0140  261 LYS A CD   
2427 C  CE   . LYS A 260 ? 0.5339 0.5059 0.4964 -0.0218 0.0337  0.0260  261 LYS A CE   
2428 N  NZ   . LYS A 260 ? 0.5625 0.4954 0.5094 0.0080  0.0166  0.0154  261 LYS A NZ   
2429 O  OXT  . LYS A 260 ? 0.6090 0.5133 0.6108 0.0000  -0.0346 0.0487  261 LYS A OXT  
2430 ZN ZN   . ZN  B .   ? 0.0654 0.0283 0.1803 -0.0109 0.0076  -0.0007 262 ZN  A ZN   
2431 S  S    . DMS C .   ? 0.2949 0.1013 0.2572 -0.0471 -0.0082 0.0214  263 DMS A S    
2432 O  O    . DMS C .   ? 0.1981 0.1112 0.3134 -0.0904 -0.0266 -0.0026 263 DMS A O    
2433 C  C1   . DMS C .   ? 0.2994 0.0794 0.2903 -0.0511 -0.0458 0.0210  263 DMS A C1   
2434 C  C2   . DMS C .   ? 0.2186 0.2084 0.2538 -0.0732 0.0471  -0.0115 263 DMS A C2   
2435 S  S    . DMS D .   ? 0.1686 0.1703 0.3519 -0.0265 0.0081  -0.0131 264 DMS A S    
2436 O  O    . DMS D .   ? 0.2838 0.2114 0.3828 0.0957  0.0304  -0.0401 264 DMS A O    
2437 C  C1   . DMS D .   ? 0.1808 0.1326 0.3833 -0.0430 -0.0161 0.0237  264 DMS A C1   
2438 C  C2   . DMS D .   ? 0.1528 0.1967 0.2599 0.0276  0.0333  -0.0474 264 DMS A C2   
2439 N  N1   . BCN E .   ? 0.2890 0.3556 0.3490 -0.0700 -0.0368 0.0164  265 BCN A N1   
2440 C  C1   . BCN E .   ? 0.3203 0.4005 0.2824 -0.0557 -0.0461 0.0197  265 BCN A C1   
2441 C  C2   . BCN E .   ? 0.2899 0.3222 0.3698 -0.0599 0.0060  0.0452  265 BCN A C2   
2442 O  O21  . BCN E .   ? 0.3465 0.3350 0.4692 -0.0842 -0.0135 0.0322  265 BCN A O21  
2443 O  O22  . BCN E .   ? 0.3115 0.3657 0.3697 -0.0531 0.0060  0.0292  265 BCN A O22  
2444 C  C3   . BCN E .   ? 0.2508 0.1899 0.3303 -0.0564 -0.0284 -0.0281 265 BCN A C3   
2445 C  C4   . BCN E .   ? 0.4886 0.3659 0.3975 -0.0068 -0.0007 0.0131  265 BCN A C4   
2446 O  O4   . BCN E .   ? 0.4724 0.2673 0.4307 -0.0922 0.0164  0.0684  265 BCN A O4   
2447 C  C5   . BCN E .   ? 0.1541 0.1556 0.3104 -0.0340 -0.0031 0.0377  265 BCN A C5   
2448 C  C6   . BCN E .   ? 0.4897 0.4441 0.4735 -0.0102 0.0551  -0.0164 265 BCN A C6   
2449 O  O6   . BCN E .   ? 0.3612 0.2702 0.4987 0.0062  0.0841  0.0581  265 BCN A O6   
2450 N  N1   . E49 F .   ? 0.2017 0.2542 0.3072 0.0405  0.0626  -0.0136 266 E49 A N1   
2451 C  C2   . E49 F .   ? 0.2477 0.1708 0.3152 -0.0273 0.0478  -0.0148 266 E49 A C2   
2452 N  N3   . E49 F .   ? 0.1808 0.2281 0.3086 -0.0153 0.0520  -0.0068 266 E49 A N3   
2453 C  C4   . E49 F .   ? 0.3127 0.2477 0.2763 -0.0381 0.0388  -0.0097 266 E49 A C4   
2454 C  C5   . E49 F .   ? 0.2869 0.3046 0.3361 -0.0048 0.0592  -0.0285 266 E49 A C5   
2455 C  C6   . E49 F .   ? 0.3199 0.2800 0.2709 -0.0166 0.0293  -0.0035 266 E49 A C6   
2456 S  S7   . E49 F .   ? 0.2348 0.2107 0.2739 0.0151  0.0606  0.0170  266 E49 A S7   
2457 C  C8   . E49 F .   ? 0.1431 0.1036 0.2389 0.0291  0.0657  0.0174  266 E49 A C8   
2458 C  C9   . E49 F .   ? 0.1525 0.0494 0.2398 -0.0272 0.0170  0.0299  266 E49 A C9   
2459 O  O10  . E49 F .   ? 0.1888 0.1750 0.2335 -0.0219 0.0306  0.0688  266 E49 A O10  
2460 C  C11  . E49 F .   ? 0.2457 0.1931 0.2567 0.0723  0.0619  0.0447  266 E49 A C11  
2461 C  C12  . E49 F .   ? 0.2549 0.2793 0.3316 -0.0386 0.0873  0.0199  266 E49 A C12  
2462 C  C13  . E49 F .   ? 0.0882 0.0837 0.1762 0.0200  0.0294  0.0152  266 E49 A C13  
2463 C  C14  . E49 F .   ? 0.0936 0.0533 0.1958 -0.0288 0.0076  0.0076  266 E49 A C14  
2464 C  C15  . E49 F .   ? 0.0520 0.0553 0.1882 -0.0277 0.0046  0.0077  266 E49 A C15  
2465 C  C16  . E49 F .   ? 0.1058 0.0724 0.2319 -0.0610 0.0333  -0.0377 266 E49 A C16  
2466 C  C17  . E49 F .   ? 0.1031 0.0790 0.2152 -0.0582 0.0450  0.0071  266 E49 A C17  
2467 C  C18  . E49 F .   ? 0.0982 0.0519 0.2340 0.0132  0.0194  0.0295  266 E49 A C18  
2468 S  S19  . E49 F .   ? 0.0754 0.0397 0.1841 -0.0040 -0.0093 0.0020  266 E49 A S19  
2469 O  O20  . E49 F .   ? 0.0907 0.0292 0.1816 -0.0148 0.0054  -0.0099 266 E49 A O20  
2470 O  O22  . E49 F .   ? 0.1022 0.0379 0.2202 0.0307  -0.0091 -0.0102 266 E49 A O22  
2471 N  N23  . E49 F .   ? 0.0436 0.0322 0.2229 0.0007  0.0000  -0.0366 266 E49 A N23  
2472 CL CL21 . E49 F .   ? 0.0943 0.0358 0.2626 0.0027  0.0238  -0.0142 266 E49 A CL21 
2473 O  O    . HOH G .   ? 0.3555 0.2624 0.4691 -0.0015 0.0068  -0.1092 126 HOH A O    
2474 O  O    . HOH G .   ? 0.3546 0.4878 0.6495 0.1703  -0.0559 0.0544  267 HOH A O    
2475 O  O    . HOH G .   ? 0.4569 0.5080 0.3673 0.0146  0.0445  -0.1110 268 HOH A O    
2476 O  O    . HOH G .   ? 0.5170 0.2700 0.6402 0.0186  0.1036  -0.1371 269 HOH A O    
2477 O  O    . HOH G .   ? 0.5000 0.4077 0.4598 0.1212  -0.1502 0.1076  270 HOH A O    
2478 O  O    . HOH G .   ? 0.3172 0.5756 0.5256 0.1445  0.0878  -0.0232 271 HOH A O    
2479 O  O    . HOH G .   ? 0.3476 0.2296 0.5781 -0.1288 -0.0665 0.0260  272 HOH A O    
2480 O  O    . HOH G .   ? 0.3124 0.4685 0.5899 0.0992  0.0165  0.0921  273 HOH A O    
2481 O  O    . HOH G .   ? 0.3709 0.4132 0.6467 -0.0505 -0.1391 -0.0700 274 HOH A O    
2482 O  O    . HOH G .   ? 0.5091 0.2229 0.3973 0.0046  0.0551  -0.0115 275 HOH A O    
2483 O  O    . HOH G .   ? 0.5888 0.5278 0.5212 -0.0671 -0.0288 0.0307  276 HOH A O    
2484 O  O    . HOH G .   ? 0.5134 0.3910 0.4444 0.0920  0.0000  -0.0821 277 HOH A O    
2485 O  O    . HOH G .   ? 0.3163 0.2689 0.4677 -0.0465 0.0335  0.0250  278 HOH A O    
2486 O  O    . HOH G .   ? 0.3916 0.3476 0.4681 -0.1312 -0.0182 -0.0315 279 HOH A O    
2487 O  O    . HOH G .   ? 0.6111 0.3623 0.3562 0.0285  0.0153  -0.0864 280 HOH A O    
2488 O  O    . HOH G .   ? 0.4617 0.2781 0.3973 0.0491  0.0461  -0.0087 281 HOH A O    
2489 O  O    . HOH G .   ? 0.4774 0.3485 0.3941 0.0384  0.1393  -0.0373 282 HOH A O    
2490 O  O    . HOH G .   ? 0.6280 0.3851 0.5375 0.0412  -0.0777 -0.0142 283 HOH A O    
2491 O  O    . HOH G .   ? 0.3625 0.3323 0.5166 0.0595  0.0104  -0.0652 284 HOH A O    
2492 O  O    . HOH G .   ? 0.3953 0.2921 0.5177 0.0527  -0.0436 0.0015  285 HOH A O    
2493 O  O    . HOH G .   ? 0.4405 0.2703 0.4401 0.0043  -0.0584 0.1238  286 HOH A O    
2494 O  O    . HOH G .   ? 0.3388 0.3736 0.4649 0.1289  0.0283  0.0428  287 HOH A O    
2495 O  O    . HOH G .   ? 0.5429 0.1679 0.6118 0.0324  -0.1612 0.1018  288 HOH A O    
2496 O  O    . HOH G .   ? 0.3384 0.2849 0.5332 -0.0689 -0.0129 -0.0666 289 HOH A O    
2497 O  O    . HOH G .   ? 0.5845 0.4659 0.4939 0.0006  -0.0208 -0.0452 290 HOH A O    
2498 O  O    . HOH G .   ? 0.2407 0.3903 0.5726 -0.1421 -0.0886 0.0043  291 HOH A O    
2499 O  O    . HOH G .   ? 0.6344 0.4609 0.3237 0.0142  -0.0012 -0.0091 292 HOH A O    
2500 O  O    . HOH G .   ? 0.4434 0.5705 0.6064 -0.0772 -0.0273 0.0317  293 HOH A O    
2501 O  O    . HOH G .   ? 0.5180 0.2533 0.4588 0.0419  0.0555  0.0408  294 HOH A O    
2502 O  O    . HOH G .   ? 0.4746 0.4207 0.6836 -0.1079 0.0834  0.1432  295 HOH A O    
2503 O  O    . HOH G .   ? 0.3617 0.7609 0.6172 0.0838  -0.0960 0.0346  296 HOH A O    
2504 O  O    . HOH G .   ? 0.4053 0.2148 0.5454 -0.0249 0.0772  -0.0384 297 HOH A O    
2505 O  O    . HOH G .   ? 0.5047 0.2673 0.3107 -0.0162 -0.0533 -0.0194 298 HOH A O    
2506 O  O    . HOH G .   ? 0.4689 0.4703 0.4383 -0.0662 -0.0988 0.0410  299 HOH A O    
2507 O  O    . HOH G .   ? 0.4717 0.3892 0.3009 -0.0403 0.0542  0.0824  300 HOH A O    
2508 O  O    . HOH G .   ? 0.2423 0.3962 0.2727 -0.0724 0.0184  0.0272  301 HOH A O    
2509 O  O    . HOH G .   ? 0.3743 0.2401 0.4128 -0.0285 0.0189  -0.0137 302 HOH A O    
2510 O  O    . HOH G .   ? 0.4886 0.2899 0.3174 0.0274  -0.0266 -0.0375 303 HOH A O    
2511 O  O    . HOH G .   ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  304 HOH A O    
2512 O  O    . HOH G .   ? 0.0420 0.0719 0.1929 0.0156  0.0208  0.0000  305 HOH A O    
2513 O  O    . HOH G .   ? 0.0467 0.0794 0.1987 0.0063  0.0313  0.0121  306 HOH A O    
2514 O  O    . HOH G .   ? 0.0997 0.0433 0.1744 -0.0024 -0.0102 -0.0204 307 HOH A O    
2515 O  O    . HOH G .   ? 0.0487 0.0589 0.2001 0.0046  0.0052  0.0054  308 HOH A O    
2516 O  O    . HOH G .   ? 0.1112 0.0300 0.1873 -0.0046 0.0225  -0.0154 309 HOH A O    
2517 O  O    A HOH G .   ? 0.0528 0.0916 0.2240 0.0043  0.0010  -0.0549 310 HOH A O    
2518 O  O    B HOH G .   ? 0.0354 0.1031 0.1944 -0.0214 -0.0019 0.0252  310 HOH A O    
2519 O  O    . HOH G .   ? 0.0873 0.1022 0.1751 -0.0221 0.0253  -0.0092 311 HOH A O    
2520 O  O    . HOH G .   ? 0.1994 0.0406 0.1444 -0.0238 0.0115  0.0093  312 HOH A O    
2521 O  O    . HOH G .   ? 0.0810 0.0652 0.2250 0.0207  -0.0038 0.0177  313 HOH A O    
2522 O  O    . HOH G .   ? 0.1110 0.0740 0.2344 0.0164  -0.0024 0.0063  314 HOH A O    
2523 O  O    . HOH G .   ? 0.1592 0.0704 0.2398 -0.0146 -0.0282 0.0059  315 HOH A O    
2524 O  O    . HOH G .   ? 0.1001 0.2021 0.2171 -0.0049 -0.0443 0.0408  316 HOH A O    
2525 O  O    . HOH G .   ? 0.0496 0.1049 0.3194 -0.0087 0.0216  -0.0240 317 HOH A O    
2526 O  O    . HOH G .   ? 0.1158 0.0476 0.2434 -0.0274 0.0146  0.0087  318 HOH A O    
2527 O  O    . HOH G .   ? 0.0860 0.1169 0.2272 0.0130  -0.0494 0.0218  319 HOH A O    
2528 O  O    . HOH G .   ? 0.1360 0.0742 0.2364 -0.0087 -0.0237 -0.0006 320 HOH A O    
2529 O  O    . HOH G .   ? 0.0584 0.0327 0.2329 0.0120  -0.0142 0.0052  321 HOH A O    
2530 O  O    . HOH G .   ? 0.1358 0.0305 0.2833 0.0237  -0.0065 -0.0026 322 HOH A O    
2531 O  O    . HOH G .   ? 0.0763 0.1246 0.3043 0.0172  0.0368  0.0253  323 HOH A O    
2532 O  O    . HOH G .   ? 0.1629 0.0900 0.2306 0.0428  -0.0040 -0.0068 324 HOH A O    
2533 O  O    A HOH G .   ? 0.1018 0.1399 0.3185 0.0087  -0.0762 -0.0359 325 HOH A O    
2534 O  O    B HOH G .   ? 0.1189 0.1450 0.3273 -0.0225 -0.0776 -0.0208 325 HOH A O    
2535 O  O    . HOH G .   ? 0.2272 0.1349 0.3163 0.0384  0.0485  0.0397  326 HOH A O    
2536 O  O    . HOH G .   ? 0.1622 0.1805 0.2484 -0.0313 0.0529  -0.0261 327 HOH A O    
2537 O  O    . HOH G .   ? 0.1239 0.1298 0.2382 0.0026  0.0188  0.0208  328 HOH A O    
2538 O  O    . HOH G .   ? 0.1474 0.1376 0.3576 0.0178  -0.0161 -0.0006 329 HOH A O    
2539 O  O    A HOH G .   ? 0.0973 0.1207 0.1581 -0.0509 -0.0174 0.0307  330 HOH A O    
2540 O  O    B HOH G .   ? 0.1816 0.1142 0.2021 -0.0038 0.0000  -0.0074 330 HOH A O    
2541 O  O    . HOH G .   ? 0.2164 0.1632 0.3077 -0.0476 0.0068  -0.0230 331 HOH A O    
2542 O  O    . HOH G .   ? 0.2297 0.1333 0.2390 0.0000  -0.0326 0.0232  332 HOH A O    
2543 O  O    . HOH G .   ? 0.1320 0.1340 0.3095 0.0215  0.0355  -0.0241 333 HOH A O    
2544 O  O    . HOH G .   ? 0.2240 0.1243 0.2578 -0.0192 0.0593  0.0309  334 HOH A O    
2545 O  O    . HOH G .   ? 0.1769 0.1013 0.3235 -0.0732 0.0074  -0.0340 335 HOH A O    
2546 O  O    A HOH G .   ? 0.0648 0.0740 0.1476 0.0093  -0.0040 0.0118  336 HOH A O    
2547 O  O    B HOH G .   ? 0.1952 0.1581 0.1897 -0.0732 0.0126  0.0421  336 HOH A O    
2548 O  O    . HOH G .   ? 0.2840 0.0658 0.2944 -0.0634 0.0046  -0.0522 337 HOH A O    
2549 O  O    . HOH G .   ? 0.1686 0.1130 0.2455 -0.0126 -0.0296 -0.0043 338 HOH A O    
2550 O  O    . HOH G .   ? 0.2730 0.1289 0.2761 0.0478  -0.0615 -0.0136 339 HOH A O    
2551 O  O    . HOH G .   ? 0.1848 0.0876 0.2847 0.0104  0.0249  -0.0219 340 HOH A O    
2552 O  O    . HOH G .   ? 0.1444 0.1042 0.3102 -0.0333 0.0281  -0.0372 341 HOH A O    
2553 O  O    . HOH G .   ? 0.1288 0.0803 0.2130 0.0320  0.0186  0.0040  342 HOH A O    
2554 O  O    A HOH G .   ? 0.2394 0.0316 0.2513 -0.0109 -0.0215 0.0024  343 HOH A O    
2555 O  O    B HOH G .   ? 0.2254 0.0939 0.2473 0.0362  -0.0432 -0.0423 343 HOH A O    
2556 O  O    . HOH G .   ? 0.1532 0.1176 0.2709 -0.0153 0.0456  -0.0210 344 HOH A O    
2557 O  O    . HOH G .   ? 0.1992 0.1340 0.3032 0.0059  0.0342  -0.0509 345 HOH A O    
2558 O  O    . HOH G .   ? 0.1036 0.1168 0.3695 -0.0456 -0.0252 0.0137  346 HOH A O    
2559 O  O    . HOH G .   ? 0.2168 0.0548 0.2809 0.0285  -0.0187 -0.0088 347 HOH A O    
2560 O  O    . HOH G .   ? 0.1401 0.2303 0.1951 0.0746  -0.0088 -0.0175 348 HOH A O    
2561 O  O    . HOH G .   ? 0.1949 0.2017 0.3632 -0.0060 -0.0270 -0.0087 349 HOH A O    
2562 O  O    . HOH G .   ? 0.2493 0.1316 0.3851 -0.0350 0.0465  0.0147  350 HOH A O    
2563 O  O    . HOH G .   ? 0.1911 0.1412 0.3048 -0.0185 -0.0099 0.0533  351 HOH A O    
2564 O  O    . HOH G .   ? 0.1775 0.1825 0.2378 0.0182  0.0020  0.0093  352 HOH A O    
2565 O  O    . HOH G .   ? 0.2526 0.1209 0.2955 -0.0137 -0.0436 -0.0057 353 HOH A O    
2566 O  O    . HOH G .   ? 0.2942 0.1453 0.3504 0.0527  -0.0575 -0.0368 354 HOH A O    
2567 O  O    . HOH G .   ? 0.3210 0.1491 0.3314 0.0878  -0.0401 -0.0082 355 HOH A O    
2568 O  O    . HOH G .   ? 0.1663 0.1171 0.2524 -0.0031 -0.0104 0.0307  356 HOH A O    
2569 O  O    . HOH G .   ? 0.0736 0.1406 0.3707 -0.0151 0.0006  -0.0313 357 HOH A O    
2570 O  O    . HOH G .   ? 0.2522 0.2935 0.3562 0.0553  -0.0281 0.0125  358 HOH A O    
2571 O  O    . HOH G .   ? 0.1432 0.1297 0.2797 -0.0148 -0.0199 -0.0087 359 HOH A O    
2572 O  O    . HOH G .   ? 0.2161 0.1651 0.2617 -0.0975 -0.0137 -0.0148 360 HOH A O    
2573 O  O    . HOH G .   ? 0.2161 0.2466 0.3025 0.0109  -0.0644 -0.1253 361 HOH A O    
2574 O  O    . HOH G .   ? 0.3055 0.2175 0.3488 0.0465  -0.1351 -0.0156 362 HOH A O    
2575 O  O    . HOH G .   ? 0.1459 0.2033 0.4106 0.0878  -0.0755 -0.0208 363 HOH A O    
2576 O  O    . HOH G .   ? 0.2829 0.1608 0.2502 0.0281  -0.0230 0.0229  364 HOH A O    
2577 O  O    . HOH G .   ? 0.2624 0.1237 0.3463 0.0140  -0.0161 -0.0020 365 HOH A O    
2578 O  O    . HOH G .   ? 0.2199 0.1543 0.2319 -0.0027 -0.0395 -0.0030 366 HOH A O    
2579 O  O    . HOH G .   ? 0.1719 0.1557 0.3143 0.0000  0.0166  -0.0573 367 HOH A O    
2580 O  O    . HOH G .   ? 0.1753 0.1042 0.3115 0.0000  -0.0208 0.0381  368 HOH A O    
2581 O  O    . HOH G .   ? 0.1471 0.2574 0.3327 0.0307  0.0124  0.0877  369 HOH A O    
2582 O  O    . HOH G .   ? 0.1300 0.1369 0.2996 -0.0080 0.0167  0.0417  370 HOH A O    
2583 O  O    . HOH G .   ? 0.3233 0.1836 0.2314 -0.0291 -0.0811 0.0146  371 HOH A O    
2584 O  O    . HOH G .   ? 0.1701 0.3152 0.4022 0.0099  -0.0337 -0.0037 372 HOH A O    
2585 O  O    . HOH G .   ? 0.2339 0.1923 0.3388 0.0046  -0.0198 0.0333  373 HOH A O    
2586 O  O    . HOH G .   ? 0.1870 0.1895 0.3230 -0.0346 0.0579  0.0476  374 HOH A O    
2587 O  O    . HOH G .   ? 0.2092 0.1784 0.2845 0.0035  0.0026  0.0136  375 HOH A O    
2588 O  O    . HOH G .   ? 0.2430 0.3801 0.2725 0.1321  0.0342  -0.0535 376 HOH A O    
2589 O  O    . HOH G .   ? 0.1890 0.2026 0.2186 -0.0082 0.0051  -0.0288 377 HOH A O    
2590 O  O    . HOH G .   ? 0.2240 0.3115 0.2554 -0.0921 0.0322  -0.0059 378 HOH A O    
2591 O  O    . HOH G .   ? 0.1606 0.2400 0.3524 -0.0186 -0.0073 -0.0006 379 HOH A O    
2592 O  O    . HOH G .   ? 0.1737 0.2840 0.3774 -0.0939 -0.0491 0.0164  380 HOH A O    
2593 O  O    . HOH G .   ? 0.2515 0.1780 0.2748 0.0342  0.0520  -0.0364 381 HOH A O    
2594 O  O    . HOH G .   ? 0.2680 0.2587 0.2639 -0.0220 0.0439  -0.0722 382 HOH A O    
2595 O  O    . HOH G .   ? 0.2087 0.2795 0.2967 0.0153  -0.0024 -0.0231 383 HOH A O    
2596 O  O    . HOH G .   ? 0.3610 0.1904 0.2236 -0.0241 0.0243  0.0263  384 HOH A O    
2597 O  O    . HOH G .   ? 0.2242 0.1474 0.2594 0.0344  -0.0450 0.0177  385 HOH A O    
2598 O  O    . HOH G .   ? 0.4232 0.2362 0.1854 -0.0344 -0.0062 0.0216  386 HOH A O    
2599 O  O    . HOH G .   ? 0.2958 0.2066 0.2606 -0.0649 0.0851  -0.0706 387 HOH A O    
2600 O  O    . HOH G .   ? 0.1951 0.2517 0.3273 -0.0241 -0.0855 0.0231  388 HOH A O    
2601 O  O    . HOH G .   ? 0.1448 0.1800 0.3231 -0.0615 0.0188  -0.0010 389 HOH A O    
2602 O  O    . HOH G .   ? 0.4163 0.1579 0.3009 -0.0732 -0.0860 -0.0507 390 HOH A O    
2603 O  O    . HOH G .   ? 0.3183 0.1329 0.2870 0.0263  -0.0052 -0.0421 391 HOH A O    
2604 O  O    . HOH G .   ? 0.3876 0.3472 0.3003 -0.0511 -0.0518 -0.0469 392 HOH A O    
2605 O  O    . HOH G .   ? 0.1805 0.2231 0.3438 -0.0507 0.0082  0.0107  393 HOH A O    
2606 O  O    . HOH G .   ? 0.3772 0.1237 0.3273 0.0658  0.0228  0.0408  394 HOH A O    
2607 O  O    . HOH G .   ? 0.3249 0.2279 0.3361 -0.0254 -0.0175 0.0076  395 HOH A O    
2608 O  O    . HOH G .   ? 0.2587 0.1191 0.2775 -0.0172 -0.0237 -0.0099 396 HOH A O    
2609 O  O    . HOH G .   ? 0.1379 0.2606 0.4167 0.1058  0.0434  -0.0054 397 HOH A O    
2610 O  O    . HOH G .   ? 0.1534 0.2587 0.4312 0.0109  0.0518  0.0790  398 HOH A O    
2611 O  O    . HOH G .   ? 0.1872 0.1827 0.3865 0.0142  0.0649  -0.0065 399 HOH A O    
2612 O  O    . HOH G .   ? 0.3235 0.4067 0.2466 -0.0947 -0.0432 0.0430  400 HOH A O    
2613 O  O    . HOH G .   ? 0.3143 0.1999 0.2685 0.0328  0.0934  -0.0252 401 HOH A O    
2614 O  O    . HOH G .   ? 0.3943 0.1938 0.3560 0.0277  0.0059  0.0074  402 HOH A O    
2615 O  O    . HOH G .   ? 0.1595 0.2921 0.4240 0.0509  -0.0193 -0.0226 403 HOH A O    
2616 O  O    . HOH G .   ? 0.2547 0.0758 0.3285 -0.0207 0.0023  -0.0035 404 HOH A O    
2617 O  O    . HOH G .   ? 0.3795 0.2551 0.2001 0.0210  0.0174  -0.0216 405 HOH A O    
2618 O  O    . HOH G .   ? 0.3695 0.3330 0.3476 -0.1133 -0.0408 0.0434  406 HOH A O    
2619 O  O    . HOH G .   ? 0.2899 0.2272 0.3831 -0.0406 0.0203  -0.0579 407 HOH A O    
2620 O  O    . HOH G .   ? 0.2035 0.2073 0.3244 -0.0944 0.0851  -0.0614 408 HOH A O    
2621 O  O    . HOH G .   ? 0.3666 0.1902 0.2468 0.0471  -0.0612 -0.0992 409 HOH A O    
2622 O  O    . HOH G .   ? 0.3129 0.2524 0.3373 -0.0026 0.0255  0.0153  410 HOH A O    
2623 O  O    . HOH G .   ? 0.1676 0.2587 0.2639 -0.0152 0.0280  -0.0227 411 HOH A O    
2624 O  O    . HOH G .   ? 0.2867 0.2973 0.3307 0.0137  -0.0737 -0.0520 412 HOH A O    
2625 O  O    . HOH G .   ? 0.2535 0.1550 0.3089 -0.0136 0.0217  0.0208  413 HOH A O    
2626 O  O    . HOH G .   ? 0.2536 0.2842 0.4135 -0.0606 0.0118  -0.0182 414 HOH A O    
2627 O  O    . HOH G .   ? 0.1758 0.1390 0.3551 0.0741  -0.0458 -0.0280 415 HOH A O    
2628 O  O    . HOH G .   ? 0.2682 0.4933 0.3957 0.1342  0.0318  -0.1280 416 HOH A O    
2629 O  O    . HOH G .   ? 0.2347 0.1739 0.4325 0.0952  -0.0229 -0.0176 417 HOH A O    
2630 O  O    . HOH G .   ? 0.2578 0.1832 0.3120 -0.0366 -0.0627 0.0132  418 HOH A O    
2631 O  O    . HOH G .   ? 0.1836 0.2768 0.4239 0.0024  -0.0557 0.0126  419 HOH A O    
2632 O  O    . HOH G .   ? 0.1895 0.1744 0.3079 0.0176  -0.0494 0.0082  420 HOH A O    
2633 O  O    . HOH G .   ? 0.3415 0.2612 0.4369 0.1052  -0.1225 0.0142  421 HOH A O    
2634 O  O    . HOH G .   ? 0.3309 0.2824 0.2885 0.1877  -0.0820 -0.0132 422 HOH A O    
2635 O  O    . HOH G .   ? 0.2189 0.2301 0.4778 -0.1127 -0.0348 0.0251  423 HOH A O    
2636 O  O    . HOH G .   ? 0.4192 0.2042 0.2973 0.1041  0.0615  -0.0996 424 HOH A O    
2637 O  O    . HOH G .   ? 0.2116 0.3059 0.3955 0.0784  0.0151  -0.0357 425 HOH A O    
2638 O  O    . HOH G .   ? 0.3379 0.4204 0.2790 -0.0093 -0.1171 0.0816  426 HOH A O    
2639 O  O    . HOH G .   ? 0.2716 0.1701 0.3555 0.0153  -0.0515 -0.0236 427 HOH A O    
2640 O  O    . HOH G .   ? 0.5751 0.1940 0.2705 0.0119  0.0305  0.0842  428 HOH A O    
2641 O  O    . HOH G .   ? 0.4100 0.2376 0.4189 0.0926  0.0096  -0.0006 429 HOH A O    
2642 O  O    . HOH G .   ? 0.3152 0.3982 0.3711 -0.1860 -0.0370 0.0575  430 HOH A O    
2643 O  O    . HOH G .   ? 0.3641 0.4368 0.3488 0.1010  0.0003  0.1071  431 HOH A O    
2644 O  O    . HOH G .   ? 0.2815 0.2538 0.3759 -0.0886 0.0657  -0.1106 432 HOH A O    
2645 O  O    . HOH G .   ? 0.3134 0.1624 0.4204 -0.0193 0.0491  -0.0515 433 HOH A O    
2646 O  O    . HOH G .   ? 0.2759 0.1902 0.2455 0.0020  0.0241  0.0156  434 HOH A O    
2647 O  O    . HOH G .   ? 0.1714 0.2473 0.4319 -0.0467 0.0233  -0.0098 435 HOH A O    
2648 O  O    . HOH G .   ? 0.3709 0.3443 0.2800 0.0588  0.0250  0.0881  436 HOH A O    
2649 O  O    . HOH G .   ? 0.3007 0.3185 0.3880 -0.0285 -0.0373 0.0461  437 HOH A O    
2650 O  O    . HOH G .   ? 0.3867 0.2134 0.3003 -0.0509 -0.0485 -0.0491 438 HOH A O    
2651 O  O    . HOH G .   ? 0.3014 0.3402 0.3221 0.1359  0.0318  0.0098  439 HOH A O    
2652 O  O    . HOH G .   ? 0.2578 0.2121 0.4426 0.0270  0.0263  -0.0318 440 HOH A O    
2653 O  O    . HOH G .   ? 0.1863 0.2820 0.3930 -0.0819 0.0876  -0.0109 441 HOH A O    
2654 O  O    . HOH G .   ? 0.2329 0.2770 0.5906 -0.0908 0.0082  -0.0131 442 HOH A O    
2655 O  O    . HOH G .   ? 0.4606 0.1618 0.2457 -0.0261 -0.0465 -0.0024 443 HOH A O    
2656 O  O    . HOH G .   ? 0.3023 0.1775 0.2737 0.0728  -0.0450 -0.0013 444 HOH A O    
2657 O  O    . HOH G .   ? 0.3813 0.3707 0.3077 0.0590  -0.1111 -0.0900 445 HOH A O    
2658 O  O    . HOH G .   ? 0.3134 0.2709 0.4656 0.0274  -0.0750 -0.0575 446 HOH A O    
2659 O  O    . HOH G .   ? 0.4505 0.2466 0.5701 0.0452  -0.0436 -0.1457 447 HOH A O    
2660 O  O    . HOH G .   ? 0.3357 0.2110 0.4775 -0.0443 0.0483  0.0483  448 HOH A O    
2661 O  O    . HOH G .   ? 0.2470 0.3892 0.4846 -0.1096 -0.0649 -0.0436 449 HOH A O    
2662 O  O    . HOH G .   ? 0.3447 0.2301 0.4386 0.0057  -0.0071 -0.0443 450 HOH A O    
2663 O  O    . HOH G .   ? 0.2707 0.1180 0.3555 0.0476  0.0333  -0.0237 451 HOH A O    
2664 O  O    . HOH G .   ? 0.2215 0.3269 0.3856 0.0048  0.1299  0.0829  452 HOH A O    
2665 O  O    . HOH G .   ? 0.3219 0.3601 0.4161 0.0447  -0.0054 0.0361  453 HOH A O    
2666 O  O    . HOH G .   ? 0.2572 0.2153 0.3959 0.0291  0.0059  0.0232  454 HOH A O    
2667 O  O    . HOH G .   ? 0.2056 0.2597 0.3134 0.0098  0.0432  -0.0194 455 HOH A O    
2668 O  O    . HOH G .   ? 0.3517 0.2651 0.4157 0.0461  -0.0697 -0.0241 456 HOH A O    
2669 O  O    . HOH G .   ? 0.2976 0.2937 0.3948 0.1726  0.1010  0.0370  457 HOH A O    
2670 O  O    . HOH G .   ? 0.2903 0.1493 0.4641 -0.0359 0.0403  0.0275  458 HOH A O    
2671 O  O    . HOH G .   ? 0.2989 0.2700 0.3379 -0.0627 0.0192  0.0788  459 HOH A O    
2672 O  O    . HOH G .   ? 0.2935 0.2028 0.4264 -0.0533 0.0120  -0.0970 460 HOH A O    
2673 O  O    . HOH G .   ? 0.2637 0.3833 0.3145 0.0542  -0.0217 -0.0388 461 HOH A O    
2674 O  O    . HOH G .   ? 0.3208 0.4286 0.3632 -0.0087 -0.0555 0.0816  462 HOH A O    
2675 O  O    . HOH G .   ? 0.2157 0.2500 0.3921 -0.0299 0.0362  -0.0113 463 HOH A O    
2676 O  O    . HOH G .   ? 0.3749 0.3260 0.3686 -0.1343 -0.0299 0.0869  464 HOH A O    
2677 O  O    . HOH G .   ? 0.6366 0.2093 0.4081 -0.0063 -0.0082 0.0392  465 HOH A O    
2678 O  O    . HOH G .   ? 0.3700 0.4465 0.6093 0.1837  -0.0366 0.0406  466 HOH A O    
2679 O  O    . HOH G .   ? 0.3851 0.2286 0.3519 0.0615  0.0460  -0.0317 467 HOH A O    
2680 O  O    . HOH G .   ? 0.4300 0.3251 0.5058 0.0221  0.0617  -0.0379 468 HOH A O    
2681 O  O    . HOH G .   ? 0.3914 0.3246 0.3689 0.0000  0.0454  0.0412  469 HOH A O    
2682 O  O    . HOH G .   ? 0.4731 0.2533 0.3217 0.0671  0.0147  0.1022  470 HOH A O    
2683 O  O    . HOH G .   ? 0.3768 0.3158 0.3030 -0.0921 0.0285  0.0740  471 HOH A O    
2684 O  O    . HOH G .   ? 0.3643 0.3368 0.3659 0.0366  0.0794  0.0754  472 HOH A O    
2685 O  O    . HOH G .   ? 0.2727 0.3610 0.5274 0.0767  -0.0965 -0.1464 473 HOH A O    
2686 O  O    . HOH G .   ? 0.4336 0.1642 0.3145 0.0511  0.0392  0.0454  474 HOH A O    
2687 O  O    . HOH G .   ? 0.2484 0.2594 0.5141 -0.0898 0.0395  0.0436  475 HOH A O    
2688 O  O    . HOH G .   ? 0.3327 0.1735 0.4430 -0.1855 -0.0540 0.0626  476 HOH A O    
2689 O  O    . HOH G .   ? 0.1996 0.2231 0.4832 -0.0087 -0.0250 0.0674  477 HOH A O    
2690 O  O    . HOH G .   ? 0.4861 0.2687 0.2991 -0.1061 0.0386  -0.0666 478 HOH A O    
2691 O  O    . HOH G .   ? 0.3140 0.3201 0.3411 -0.0322 -0.0315 -0.0379 479 HOH A O    
2692 O  O    . HOH G .   ? 0.2064 0.2265 0.4059 0.0500  0.0313  0.0000  480 HOH A O    
2693 O  O    . HOH G .   ? 0.2118 0.3359 0.2535 0.0147  -0.0068 -0.0723 481 HOH A O    
2694 O  O    . HOH G .   ? 0.5030 0.3797 0.3165 0.0364  -0.0140 -0.0535 482 HOH A O    
2695 O  O    . HOH G .   ? 0.2283 0.2617 0.4185 -0.0351 0.0438  0.0107  483 HOH A O    
2696 O  O    . HOH G .   ? 0.2991 0.3535 0.4756 0.0274  0.0027  -0.0208 484 HOH A O    
2697 O  O    . HOH G .   ? 0.3975 0.3181 0.3510 0.1027  0.0741  -0.0337 485 HOH A O    
2698 O  O    . HOH G .   ? 0.2157 0.3303 0.4182 -0.0855 0.0174  -0.0031 486 HOH A O    
2699 O  O    . HOH G .   ? 0.3138 0.1881 0.4405 0.0041  0.1615  -0.0206 487 HOH A O    
2700 O  O    . HOH G .   ? 0.4480 0.3659 0.3734 -0.1052 0.0254  0.1211  488 HOH A O    
2701 O  O    . HOH G .   ? 0.3440 0.2301 0.4185 -0.0010 0.0250  0.0714  489 HOH A O    
2702 O  O    . HOH G .   ? 0.5264 0.3734 0.2587 -0.1324 -0.1677 0.1079  490 HOH A O    
2703 O  O    . HOH G .   ? 0.2716 0.3301 0.3596 -0.1172 0.0034  0.0196  491 HOH A O    
2704 O  O    . HOH G .   ? 0.3158 0.2779 0.4009 0.0520  0.0099  -0.0088 492 HOH A O    
2705 O  O    . HOH G .   ? 0.5152 0.1076 0.4509 -0.0833 -0.0386 -0.0265 493 HOH A O    
2706 O  O    . HOH G .   ? 0.2211 0.3418 0.3553 -0.0498 0.0148  0.0427  494 HOH A O    
2707 O  O    . HOH G .   ? 0.3743 0.3249 0.2425 0.0456  0.0099  -0.0081 495 HOH A O    
2708 O  O    . HOH G .   ? 0.2504 0.2527 0.3562 0.0584  0.0049  -0.0318 496 HOH A O    
2709 O  O    . HOH G .   ? 0.4007 0.1870 0.5174 -0.0724 -0.0087 0.0344  497 HOH A O    
2710 O  O    . HOH G .   ? 0.3447 0.1383 0.4922 0.0373  -0.0917 -0.0065 498 HOH A O    
2711 O  O    . HOH G .   ? 0.5320 0.1967 0.3404 0.1230  0.0308  -0.0005 499 HOH A O    
2712 O  O    . HOH G .   ? 0.3637 0.2732 0.3136 0.0361  -0.0161 0.0103  500 HOH A O    
2713 O  O    . HOH G .   ? 0.4358 0.1891 0.3887 0.0131  0.0847  0.0793  501 HOH A O    
2714 O  O    . HOH G .   ? 0.4217 0.1798 0.4290 0.0206  -0.0136 -0.0331 502 HOH A O    
2715 O  O    . HOH G .   ? 0.3219 0.3479 0.3684 -0.0302 -0.0252 -0.0308 503 HOH A O    
2716 O  O    . HOH G .   ? 0.3495 0.2504 0.2969 -0.0702 0.0081  0.0052  504 HOH A O    
2717 O  O    . HOH G .   ? 0.2707 0.2333 0.3714 0.0285  -0.0248 -0.0164 505 HOH A O    
2718 O  O    . HOH G .   ? 0.2080 0.2705 0.5360 -0.0724 0.0441  0.0159  506 HOH A O    
2719 O  O    . HOH G .   ? 0.2906 0.3677 0.4613 -0.0252 0.0000  -0.0198 507 HOH A O    
2720 O  O    . HOH G .   ? 0.4660 0.2673 0.3781 0.0293  -0.1080 0.0394  508 HOH A O    
2721 O  O    . HOH G .   ? 0.5144 0.4013 0.2502 -0.0012 0.0153  -0.0776 509 HOH A O    
2722 O  O    . HOH G .   ? 0.1640 0.3833 0.5264 -0.0377 -0.0071 0.0476  510 HOH A O    
2723 O  O    . HOH G .   ? 0.4502 0.3880 0.4164 -0.0388 -0.0038 -0.0465 511 HOH A O    
2724 O  O    . HOH G .   ? 0.3819 0.2477 0.4361 -0.0284 -0.0476 -0.0274 512 HOH A O    
2725 O  O    . HOH G .   ? 0.3057 0.2283 0.4987 -0.2337 0.0196  0.0454  513 HOH A O    
2726 O  O    . HOH G .   ? 0.3786 0.4879 0.3508 -0.1102 -0.0586 0.0935  514 HOH A O    
2727 O  O    . HOH G .   ? 0.4566 0.2475 0.2497 -0.0564 0.0247  -0.0241 515 HOH A O    
2728 O  O    . HOH G .   ? 0.4232 0.3176 0.3558 -0.0513 0.0337  -0.1576 516 HOH A O    
2729 O  O    . HOH G .   ? 0.3998 0.3646 0.3714 0.0013  -0.0388 0.0306  517 HOH A O    
2730 O  O    . HOH G .   ? 0.2858 0.2030 0.4415 -0.0452 0.0900  -0.0566 518 HOH A O    
2731 O  O    . HOH G .   ? 0.3411 0.4627 0.4276 0.1402  -0.0361 0.0129  519 HOH A O    
2732 O  O    . HOH G .   ? 0.3294 0.1719 0.4229 -0.0173 0.0518  0.0737  520 HOH A O    
2733 O  O    . HOH G .   ? 0.3587 0.3528 0.3763 -0.1474 -0.0136 -0.0710 521 HOH A O    
2734 O  O    . HOH G .   ? 0.1847 0.1539 0.5396 0.0329  0.0904  -0.0153 522 HOH A O    
2735 O  O    . HOH G .   ? 0.3048 0.2863 0.5062 -0.1054 -0.0285 -0.0087 523 HOH A O    
2736 O  O    . HOH G .   ? 0.1550 0.5375 0.4652 0.0652  -0.0043 -0.1819 524 HOH A O    
2737 O  O    . HOH G .   ? 0.2434 0.3528 0.4677 0.0829  0.0335  0.0430  525 HOH A O    
2738 O  O    . HOH G .   ? 0.4653 0.2939 0.3704 0.0282  0.0000  -0.0604 526 HOH A O    
2739 O  O    . HOH G .   ? 0.4803 0.2078 0.3977 -0.0255 0.0873  -0.0850 527 HOH A O    
2740 O  O    . HOH G .   ? 0.5073 0.3916 0.3623 0.0843  -0.0081 0.0394  528 HOH A O    
2741 O  O    . HOH G .   ? 0.2684 0.2791 0.4738 -0.0797 -0.0210 -0.1098 529 HOH A O    
2742 O  O    . HOH G .   ? 0.3154 0.4225 0.4987 0.0171  0.1808  -0.0076 530 HOH A O    
2743 O  O    . HOH G .   ? 0.4372 0.5575 0.3253 0.0636  0.0342  -0.0815 531 HOH A O    
2744 O  O    . HOH G .   ? 0.6945 0.2024 0.4738 -0.2187 0.0798  -0.0935 532 HOH A O    
2745 O  O    . HOH G .   ? 0.5856 0.3262 0.3736 -0.0658 0.0895  -0.0015 533 HOH A O    
2746 O  O    . HOH G .   ? 0.2786 0.3896 0.5483 0.0125  0.0399  -0.0693 534 HOH A O    
2747 O  O    . HOH G .   ? 0.4907 0.4239 0.3093 -0.0390 0.0766  0.1142  535 HOH A O    
2748 O  O    . HOH G .   ? 0.3892 0.3583 0.5874 -0.0714 0.0485  -0.0274 536 HOH A O    
2749 O  O    . HOH G .   ? 0.4512 0.2982 0.4915 -0.0680 0.0727  -0.0590 537 HOH A O    
2750 O  O    . HOH G .   ? 0.2026 0.4451 0.4684 -0.0723 0.0432  0.0688  538 HOH A O    
2751 O  O    . HOH G .   ? 0.3937 0.3941 0.4724 0.0877  -0.0087 -0.0447 539 HOH A O    
2752 O  O    . HOH G .   ? 0.4580 0.3607 0.3925 0.0560  0.0631  -0.0599 540 HOH A O    
2753 O  O    . HOH G .   ? 0.5184 0.2430 0.3901 0.0489  0.1350  0.0478  541 HOH A O    
2754 O  O    . HOH G .   ? 0.2939 0.4620 0.4911 0.1096  0.0154  -0.1032 542 HOH A O    
2755 O  O    . HOH G .   ? 0.3161 0.3375 0.4559 -0.0864 0.0948  0.0696  543 HOH A O    
2756 O  O    . HOH G .   ? 0.4979 0.2585 0.3176 -0.0217 -0.0626 -0.1049 544 HOH A O    
2757 O  O    . HOH G .   ? 0.4142 0.4393 0.3470 -0.0186 -0.0270 -0.0454 545 HOH A O    
2758 O  O    . HOH G .   ? 0.1746 0.3370 0.6158 -0.0807 -0.1207 0.1424  546 HOH A O    
2759 O  O    . HOH G .   ? 0.3409 0.2754 0.5156 0.0249  0.0096  0.1097  547 HOH A O    
2760 O  O    . HOH G .   ? 0.3409 0.3540 0.4096 -0.1349 -0.0071 -0.0306 548 HOH A O    
2761 O  O    . HOH G .   ? 0.3926 0.6151 0.4972 -0.0164 0.0498  0.0636  549 HOH A O    
2762 O  O    . HOH G .   ? 0.3125 0.2150 0.5095 -0.1005 0.0046  0.0080  550 HOH A O    
2763 O  O    . HOH G .   ? 0.4092 0.4125 0.5827 -0.1098 -0.0272 0.0285  551 HOH A O    
2764 O  O    . HOH G .   ? 0.3856 0.3251 0.4591 -0.1324 0.0658  -0.0399 552 HOH A O    
2765 O  O    . HOH G .   ? 0.3889 0.2818 0.4182 -0.0461 0.0364  -0.0228 553 HOH A O    
2766 O  O    . HOH G .   ? 0.4944 0.5440 0.3937 -0.0199 -0.0855 -0.0015 554 HOH A O    
2767 O  O    . HOH G .   ? 0.3479 0.2644 0.4031 0.0372  0.0392  -0.0143 555 HOH A O    
2768 O  O    . HOH G .   ? 0.3167 0.4638 0.6736 -0.0926 -0.0595 -0.0348 556 HOH A O    
2769 O  O    . HOH G .   ? 0.2470 0.2491 0.4814 0.0978  -0.0131 -0.0049 557 HOH A O    
2770 O  O    . HOH G .   ? 0.3569 0.2312 0.3808 0.0759  -0.0140 -0.0903 558 HOH A O    
2771 O  O    . HOH G .   ? 0.6394 0.3052 0.3921 0.1410  0.0441  -0.0575 559 HOH A O    
2772 O  O    . HOH G .   ? 0.3181 0.3276 0.4613 0.0131  0.0403  0.0706  560 HOH A O    
2773 O  O    . HOH G .   ? 0.4199 0.2939 0.4760 -0.1570 0.1128  -0.1071 561 HOH A O    
2774 O  O    . HOH G .   ? 0.3628 0.3393 0.4258 0.0000  -0.0186 0.1141  562 HOH A O    
2775 O  O    . HOH G .   ? 0.5629 0.2763 0.4393 -0.0093 0.0478  -0.0789 563 HOH A O    
2776 O  O    . HOH G .   ? 0.6571 0.6280 0.3609 -0.0197 -0.0966 0.0368  564 HOH A O    
2777 O  O    . HOH G .   ? 0.5447 0.5612 0.6369 0.0062  0.0942  0.0737  565 HOH A O    
2778 O  O    . HOH G .   ? 0.4839 0.5698 0.5364 -0.0869 0.0199  -0.0763 566 HOH A O    
2779 O  O    . HOH G .   ? 0.3258 0.3463 0.6326 -0.0535 -0.1102 -0.0480 567 HOH A O    
2780 O  O    . HOH G .   ? 0.6599 0.1940 0.4649 0.0736  -0.0210 -0.0308 568 HOH A O    
2781 O  O    . HOH G .   ? 0.5120 0.3486 0.3431 -0.0674 0.0285  0.1518  569 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   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   262 1   ZN  ZN  A . 
C 3 DMS 1   263 1   DMS DMS A . 
D 3 DMS 1   264 2   DMS DMS A . 
E 4 BCN 1   265 1   BCN BCN A . 
F 5 E49 1   266 1   E49 E49 A . 
G 6 HOH 1   126 126 HOH HOH A . 
G 6 HOH 2   267 267 HOH HOH A . 
G 6 HOH 3   268 268 HOH HOH A . 
G 6 HOH 4   269 269 HOH HOH A . 
G 6 HOH 5   270 270 HOH HOH A . 
G 6 HOH 6   271 271 HOH HOH A . 
G 6 HOH 7   272 272 HOH HOH A . 
G 6 HOH 8   273 273 HOH HOH A . 
G 6 HOH 9   274 274 HOH HOH A . 
G 6 HOH 10  275 275 HOH HOH A . 
G 6 HOH 11  276 276 HOH HOH A . 
G 6 HOH 12  277 277 HOH HOH A . 
G 6 HOH 13  278 278 HOH HOH A . 
G 6 HOH 14  279 279 HOH HOH A . 
G 6 HOH 15  280 280 HOH HOH A . 
G 6 HOH 16  281 281 HOH HOH A . 
G 6 HOH 17  282 282 HOH HOH A . 
G 6 HOH 18  283 283 HOH HOH A . 
G 6 HOH 19  284 284 HOH HOH A . 
G 6 HOH 20  285 285 HOH HOH A . 
G 6 HOH 21  286 286 HOH HOH A . 
G 6 HOH 22  287 287 HOH HOH A . 
G 6 HOH 23  288 288 HOH HOH A . 
G 6 HOH 24  289 289 HOH HOH A . 
G 6 HOH 25  290 290 HOH HOH A . 
G 6 HOH 26  291 291 HOH HOH A . 
G 6 HOH 27  292 292 HOH HOH A . 
G 6 HOH 28  293 293 HOH HOH A . 
G 6 HOH 29  294 294 HOH HOH A . 
G 6 HOH 30  295 295 HOH HOH A . 
G 6 HOH 31  296 296 HOH HOH A . 
G 6 HOH 32  297 297 HOH HOH A . 
G 6 HOH 33  298 298 HOH HOH A . 
G 6 HOH 34  299 299 HOH HOH A . 
G 6 HOH 35  300 300 HOH HOH A . 
G 6 HOH 36  301 301 HOH HOH A . 
G 6 HOH 37  302 302 HOH HOH A . 
G 6 HOH 38  303 303 HOH HOH A . 
G 6 HOH 39  304 304 HOH HOH A . 
G 6 HOH 40  305 1   HOH HOH A . 
G 6 HOH 41  306 2   HOH HOH A . 
G 6 HOH 42  307 3   HOH HOH A . 
G 6 HOH 43  308 4   HOH HOH A . 
G 6 HOH 44  309 5   HOH HOH A . 
G 6 HOH 45  310 6   HOH HOH A . 
G 6 HOH 46  311 7   HOH HOH A . 
G 6 HOH 47  312 8   HOH HOH A . 
G 6 HOH 48  313 9   HOH HOH A . 
G 6 HOH 49  314 10  HOH HOH A . 
G 6 HOH 50  315 11  HOH HOH A . 
G 6 HOH 51  316 12  HOH HOH A . 
G 6 HOH 52  317 13  HOH HOH A . 
G 6 HOH 53  318 14  HOH HOH A . 
G 6 HOH 54  319 15  HOH HOH A . 
G 6 HOH 55  320 16  HOH HOH A . 
G 6 HOH 56  321 17  HOH HOH A . 
G 6 HOH 57  322 18  HOH HOH A . 
G 6 HOH 58  323 19  HOH HOH A . 
G 6 HOH 59  324 20  HOH HOH A . 
G 6 HOH 60  325 21  HOH HOH A . 
G 6 HOH 61  326 22  HOH HOH A . 
G 6 HOH 62  327 23  HOH HOH A . 
G 6 HOH 63  328 24  HOH HOH A . 
G 6 HOH 64  329 25  HOH HOH A . 
G 6 HOH 65  330 26  HOH HOH A . 
G 6 HOH 66  331 27  HOH HOH A . 
G 6 HOH 67  332 28  HOH HOH A . 
G 6 HOH 68  333 29  HOH HOH A . 
G 6 HOH 69  334 30  HOH HOH A . 
G 6 HOH 70  335 31  HOH HOH A . 
G 6 HOH 71  336 32  HOH HOH A . 
G 6 HOH 72  337 33  HOH HOH A . 
G 6 HOH 73  338 34  HOH HOH A . 
G 6 HOH 74  339 35  HOH HOH A . 
G 6 HOH 75  340 36  HOH HOH A . 
G 6 HOH 76  341 37  HOH HOH A . 
G 6 HOH 77  342 38  HOH HOH A . 
G 6 HOH 78  343 39  HOH HOH A . 
G 6 HOH 79  344 40  HOH HOH A . 
G 6 HOH 80  345 41  HOH HOH A . 
G 6 HOH 81  346 42  HOH HOH A . 
G 6 HOH 82  347 43  HOH HOH A . 
G 6 HOH 83  348 44  HOH HOH A . 
G 6 HOH 84  349 45  HOH HOH A . 
G 6 HOH 85  350 46  HOH HOH A . 
G 6 HOH 86  351 47  HOH HOH A . 
G 6 HOH 87  352 48  HOH HOH A . 
G 6 HOH 88  353 49  HOH HOH A . 
G 6 HOH 89  354 50  HOH HOH A . 
G 6 HOH 90  355 51  HOH HOH A . 
G 6 HOH 91  356 52  HOH HOH A . 
G 6 HOH 92  357 53  HOH HOH A . 
G 6 HOH 93  358 54  HOH HOH A . 
G 6 HOH 94  359 55  HOH HOH A . 
G 6 HOH 95  360 56  HOH HOH A . 
G 6 HOH 96  361 57  HOH HOH A . 
G 6 HOH 97  362 58  HOH HOH A . 
G 6 HOH 98  363 59  HOH HOH A . 
G 6 HOH 99  364 60  HOH HOH A . 
G 6 HOH 100 365 61  HOH HOH A . 
G 6 HOH 101 366 62  HOH HOH A . 
G 6 HOH 102 367 63  HOH HOH A . 
G 6 HOH 103 368 64  HOH HOH A . 
G 6 HOH 104 369 65  HOH HOH A . 
G 6 HOH 105 370 66  HOH HOH A . 
G 6 HOH 106 371 67  HOH HOH A . 
G 6 HOH 107 372 68  HOH HOH A . 
G 6 HOH 108 373 69  HOH HOH A . 
G 6 HOH 109 374 70  HOH HOH A . 
G 6 HOH 110 375 71  HOH HOH A . 
G 6 HOH 111 376 72  HOH HOH A . 
G 6 HOH 112 377 73  HOH HOH A . 
G 6 HOH 113 378 74  HOH HOH A . 
G 6 HOH 114 379 75  HOH HOH A . 
G 6 HOH 115 380 76  HOH HOH A . 
G 6 HOH 116 381 77  HOH HOH A . 
G 6 HOH 117 382 78  HOH HOH A . 
G 6 HOH 118 383 79  HOH HOH A . 
G 6 HOH 119 384 80  HOH HOH A . 
G 6 HOH 120 385 81  HOH HOH A . 
G 6 HOH 121 386 82  HOH HOH A . 
G 6 HOH 122 387 83  HOH HOH A . 
G 6 HOH 123 388 84  HOH HOH A . 
G 6 HOH 124 389 85  HOH HOH A . 
G 6 HOH 125 390 86  HOH HOH A . 
G 6 HOH 126 391 87  HOH HOH A . 
G 6 HOH 127 392 88  HOH HOH A . 
G 6 HOH 128 393 89  HOH HOH A . 
G 6 HOH 129 394 90  HOH HOH A . 
G 6 HOH 130 395 91  HOH HOH A . 
G 6 HOH 131 396 92  HOH HOH A . 
G 6 HOH 132 397 93  HOH HOH A . 
G 6 HOH 133 398 94  HOH HOH A . 
G 6 HOH 134 399 95  HOH HOH A . 
G 6 HOH 135 400 96  HOH HOH A . 
G 6 HOH 136 401 97  HOH HOH A . 
G 6 HOH 137 402 98  HOH HOH A . 
G 6 HOH 138 403 99  HOH HOH A . 
G 6 HOH 139 404 100 HOH HOH A . 
G 6 HOH 140 405 101 HOH HOH A . 
G 6 HOH 141 406 102 HOH HOH A . 
G 6 HOH 142 407 103 HOH HOH A . 
G 6 HOH 143 408 104 HOH HOH A . 
G 6 HOH 144 409 105 HOH HOH A . 
G 6 HOH 145 410 106 HOH HOH A . 
G 6 HOH 146 411 107 HOH HOH A . 
G 6 HOH 147 412 108 HOH HOH A . 
G 6 HOH 148 413 109 HOH HOH A . 
G 6 HOH 149 414 110 HOH HOH A . 
G 6 HOH 150 415 111 HOH HOH A . 
G 6 HOH 151 416 112 HOH HOH A . 
G 6 HOH 152 417 113 HOH HOH A . 
G 6 HOH 153 418 114 HOH HOH A . 
G 6 HOH 154 419 115 HOH HOH A . 
G 6 HOH 155 420 116 HOH HOH A . 
G 6 HOH 156 421 117 HOH HOH A . 
G 6 HOH 157 422 118 HOH HOH A . 
G 6 HOH 158 423 119 HOH HOH A . 
G 6 HOH 159 424 120 HOH HOH A . 
G 6 HOH 160 425 121 HOH HOH A . 
G 6 HOH 161 426 122 HOH HOH A . 
G 6 HOH 162 427 123 HOH HOH A . 
G 6 HOH 163 428 124 HOH HOH A . 
G 6 HOH 164 429 125 HOH HOH A . 
G 6 HOH 165 430 127 HOH HOH A . 
G 6 HOH 166 431 128 HOH HOH A . 
G 6 HOH 167 432 129 HOH HOH A . 
G 6 HOH 168 433 130 HOH HOH A . 
G 6 HOH 169 434 131 HOH HOH A . 
G 6 HOH 170 435 132 HOH HOH A . 
G 6 HOH 171 436 133 HOH HOH A . 
G 6 HOH 172 437 134 HOH HOH A . 
G 6 HOH 173 438 135 HOH HOH A . 
G 6 HOH 174 439 136 HOH HOH A . 
G 6 HOH 175 440 137 HOH HOH A . 
G 6 HOH 176 441 138 HOH HOH A . 
G 6 HOH 177 442 139 HOH HOH A . 
G 6 HOH 178 443 140 HOH HOH A . 
G 6 HOH 179 444 141 HOH HOH A . 
G 6 HOH 180 445 142 HOH HOH A . 
G 6 HOH 181 446 143 HOH HOH A . 
G 6 HOH 182 447 144 HOH HOH A . 
G 6 HOH 183 448 145 HOH HOH A . 
G 6 HOH 184 449 146 HOH HOH A . 
G 6 HOH 185 450 147 HOH HOH A . 
G 6 HOH 186 451 148 HOH HOH A . 
G 6 HOH 187 452 149 HOH HOH A . 
G 6 HOH 188 453 150 HOH HOH A . 
G 6 HOH 189 454 151 HOH HOH A . 
G 6 HOH 190 455 152 HOH HOH A . 
G 6 HOH 191 456 153 HOH HOH A . 
G 6 HOH 192 457 154 HOH HOH A . 
G 6 HOH 193 458 155 HOH HOH A . 
G 6 HOH 194 459 156 HOH HOH A . 
G 6 HOH 195 460 157 HOH HOH A . 
G 6 HOH 196 461 158 HOH HOH A . 
G 6 HOH 197 462 159 HOH HOH A . 
G 6 HOH 198 463 160 HOH HOH A . 
G 6 HOH 199 464 161 HOH HOH A . 
G 6 HOH 200 465 162 HOH HOH A . 
G 6 HOH 201 466 163 HOH HOH A . 
G 6 HOH 202 467 164 HOH HOH A . 
G 6 HOH 203 468 165 HOH HOH A . 
G 6 HOH 204 469 166 HOH HOH A . 
G 6 HOH 205 470 167 HOH HOH A . 
G 6 HOH 206 471 168 HOH HOH A . 
G 6 HOH 207 472 169 HOH HOH A . 
G 6 HOH 208 473 170 HOH HOH A . 
G 6 HOH 209 474 171 HOH HOH A . 
G 6 HOH 210 475 172 HOH HOH A . 
G 6 HOH 211 476 173 HOH HOH A . 
G 6 HOH 212 477 174 HOH HOH A . 
G 6 HOH 213 478 175 HOH HOH A . 
G 6 HOH 214 479 176 HOH HOH A . 
G 6 HOH 215 480 177 HOH HOH A . 
G 6 HOH 216 481 178 HOH HOH A . 
G 6 HOH 217 482 179 HOH HOH A . 
G 6 HOH 218 483 180 HOH HOH A . 
G 6 HOH 219 484 181 HOH HOH A . 
G 6 HOH 220 485 182 HOH HOH A . 
G 6 HOH 221 486 183 HOH HOH A . 
G 6 HOH 222 487 184 HOH HOH A . 
G 6 HOH 223 488 185 HOH HOH A . 
G 6 HOH 224 489 186 HOH HOH A . 
G 6 HOH 225 490 187 HOH HOH A . 
G 6 HOH 226 491 188 HOH HOH A . 
G 6 HOH 227 492 189 HOH HOH A . 
G 6 HOH 228 493 190 HOH HOH A . 
G 6 HOH 229 494 191 HOH HOH A . 
G 6 HOH 230 495 192 HOH HOH A . 
G 6 HOH 231 496 193 HOH HOH A . 
G 6 HOH 232 497 194 HOH HOH A . 
G 6 HOH 233 498 195 HOH HOH A . 
G 6 HOH 234 499 196 HOH HOH A . 
G 6 HOH 235 500 197 HOH HOH A . 
G 6 HOH 236 501 198 HOH HOH A . 
G 6 HOH 237 502 199 HOH HOH A . 
G 6 HOH 238 503 200 HOH HOH A . 
G 6 HOH 239 504 201 HOH HOH A . 
G 6 HOH 240 505 202 HOH HOH A . 
G 6 HOH 241 506 203 HOH HOH A . 
G 6 HOH 242 507 204 HOH HOH A . 
G 6 HOH 243 508 205 HOH HOH A . 
G 6 HOH 244 509 206 HOH HOH A . 
G 6 HOH 245 510 207 HOH HOH A . 
G 6 HOH 246 511 208 HOH HOH A . 
G 6 HOH 247 512 209 HOH HOH A . 
G 6 HOH 248 513 210 HOH HOH A . 
G 6 HOH 249 514 211 HOH HOH A . 
G 6 HOH 250 515 212 HOH HOH A . 
G 6 HOH 251 516 213 HOH HOH A . 
G 6 HOH 252 517 214 HOH HOH A . 
G 6 HOH 253 518 215 HOH HOH A . 
G 6 HOH 254 519 216 HOH HOH A . 
G 6 HOH 255 520 217 HOH HOH A . 
G 6 HOH 256 521 218 HOH HOH A . 
G 6 HOH 257 522 219 HOH HOH A . 
G 6 HOH 258 523 220 HOH HOH A . 
G 6 HOH 259 524 221 HOH HOH A . 
G 6 HOH 260 525 222 HOH HOH A . 
G 6 HOH 261 526 223 HOH HOH A . 
G 6 HOH 262 527 224 HOH HOH A . 
G 6 HOH 263 528 225 HOH HOH A . 
G 6 HOH 264 529 226 HOH HOH A . 
G 6 HOH 265 530 227 HOH HOH A . 
G 6 HOH 266 531 228 HOH HOH A . 
G 6 HOH 267 532 229 HOH HOH A . 
G 6 HOH 268 533 230 HOH HOH A . 
G 6 HOH 269 534 231 HOH HOH A . 
G 6 HOH 270 535 232 HOH HOH A . 
G 6 HOH 271 536 233 HOH HOH A . 
G 6 HOH 272 537 234 HOH HOH A . 
G 6 HOH 273 538 235 HOH HOH A . 
G 6 HOH 274 539 236 HOH HOH A . 
G 6 HOH 275 540 237 HOH HOH A . 
G 6 HOH 276 541 238 HOH HOH A . 
G 6 HOH 277 542 239 HOH HOH A . 
G 6 HOH 278 543 240 HOH HOH A . 
G 6 HOH 279 544 241 HOH HOH A . 
G 6 HOH 280 545 242 HOH HOH A . 
G 6 HOH 281 546 243 HOH HOH A . 
G 6 HOH 282 547 244 HOH HOH A . 
G 6 HOH 283 548 245 HOH HOH A . 
G 6 HOH 284 549 246 HOH HOH A . 
G 6 HOH 285 550 247 HOH HOH A . 
G 6 HOH 286 551 248 HOH HOH A . 
G 6 HOH 287 552 249 HOH HOH A . 
G 6 HOH 288 553 250 HOH HOH A . 
G 6 HOH 289 554 251 HOH HOH A . 
G 6 HOH 290 555 252 HOH HOH A . 
G 6 HOH 291 556 253 HOH HOH A . 
G 6 HOH 292 557 254 HOH HOH A . 
G 6 HOH 293 558 255 HOH HOH A . 
G 6 HOH 294 559 256 HOH HOH A . 
G 6 HOH 295 560 257 HOH HOH A . 
G 6 HOH 296 561 258 HOH HOH A . 
G 6 HOH 297 562 259 HOH HOH A . 
G 6 HOH 298 563 260 HOH HOH A . 
G 6 HOH 299 564 261 HOH HOH A . 
G 6 HOH 300 565 262 HOH HOH A . 
G 6 HOH 301 566 263 HOH HOH A . 
G 6 HOH 302 567 264 HOH HOH A . 
G 6 HOH 303 568 265 HOH HOH A . 
G 6 HOH 304 569 266 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_555 104.0 ? 
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_555 109.7 ? 
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_555 100.0 ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N23 ? F E49 .   ? A E49 266 ? 1_555 110.7 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N23 ? F E49 .   ? A E49 266 ? 1_555 112.6 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N23 ? F E49 .   ? A E49 266 ? 1_555 118.5 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 S19 ? F E49 .   ? A E49 266 ? 1_555 97.0  ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 S19 ? F E49 .   ? A E49 266 ? 1_555 142.6 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 S19 ? F E49 .   ? A E49 266 ? 1_555 101.5 ? 
10 N23 ? F E49 .   ? A E49 266 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 S19 ? F E49 .   ? A E49 266 ? 1_555 30.1  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2012-04-18 
2 'Structure model' 1 1 2012-05-16 
3 'Structure model' 1 2 2017-11-15 
4 'Structure model' 1 3 2023-09-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Database references'    
3 4 'Structure model' 'Data collection'        
4 4 'Structure model' 'Database references'    
5 4 'Structure model' 'Derived calculations'   
6 4 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' pdbx_database_related         
2 4 'Structure model' chem_comp_atom                
3 4 'Structure model' chem_comp_bond                
4 4 'Structure model' database_2                    
5 4 'Structure model' diffrn_source                 
6 4 'Structure model' pdbx_initial_refinement_model 
7 4 'Structure model' pdbx_struct_conn_angle        
8 4 'Structure model' struct_conn                   
9 4 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  3 'Structure model' '_pdbx_database_related.db_name'              
2  4 'Structure model' '_database_2.pdbx_DOI'                        
3  4 'Structure model' '_database_2.pdbx_database_accession'         
4  4 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
15 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
16 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
17 4 'Structure model' '_pdbx_struct_conn_angle.value'               
18 4 'Structure model' '_struct_conn.pdbx_dist_value'                
19 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
20 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
21 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
22 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
23 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
24 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
25 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
26 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
27 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
28 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
29 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
30 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
31 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
32 4 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19 22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345dtb   .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A ASP 162 ? B O A HOH 478 ? ? 2.05 
2 1 OE1 A GLN 136 ? A O A HOH 414 ? ? 2.15 
3 1 OE1 A GLN 103 ? B O A HOH 429 ? ? 2.15 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 297 ? ? 1_555 O A HOH 444 ? ? 2_545 2.15 
2 1 O A HOH 497 ? ? 1_555 O A HOH 521 ? ? 2_546 2.16 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -142.26 58.14   
2 1 ALA A 65  ? ? -158.05 -159.92 
3 1 ALA A 77  ? ? 58.02   80.81   
4 1 LYS A 111 ? ? 75.73   -5.03   
5 1 PHE A 176 ? A -154.18 74.24   
6 1 ASN A 244 ? ? -97.47  49.52   
7 1 LYS A 252 ? ? 52.26   -143.09 
# 
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 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
E49 N1   N  Y N 122 
E49 C2   C  Y N 123 
E49 N3   N  Y N 124 
E49 C4   C  Y N 125 
E49 C5   C  Y N 126 
E49 C6   C  Y N 127 
E49 S7   S  N N 128 
E49 C8   C  N N 129 
E49 C9   C  N N 130 
E49 O10  O  N N 131 
E49 C11  C  N N 132 
E49 C12  C  N N 133 
E49 C13  C  Y N 134 
E49 C14  C  Y N 135 
E49 C15  C  Y N 136 
E49 C16  C  Y N 137 
E49 C17  C  Y N 138 
E49 C18  C  Y N 139 
E49 S19  S  N N 140 
E49 O20  O  N N 141 
E49 O22  O  N N 142 
E49 N23  N  N N 143 
E49 H5   H  N N 144 
E49 H8   H  N N 145 
E49 H8A  H  N N 146 
E49 H11  H  N N 147 
E49 H11A H  N N 148 
E49 H11B H  N N 149 
E49 H12  H  N N 150 
E49 H12A H  N N 151 
E49 H12B H  N N 152 
E49 H14  H  N N 153 
E49 H17  H  N N 154 
E49 H18  H  N N 155 
E49 HN23 H  N N 156 
E49 HN2A H  N N 157 
E49 CL21 CL N N 158 
GLN N    N  N N 159 
GLN CA   C  N S 160 
GLN C    C  N N 161 
GLN O    O  N N 162 
GLN CB   C  N N 163 
GLN CG   C  N N 164 
GLN CD   C  N N 165 
GLN OE1  O  N N 166 
GLN NE2  N  N N 167 
GLN OXT  O  N N 168 
GLN H    H  N N 169 
GLN H2   H  N N 170 
GLN HA   H  N N 171 
GLN HB2  H  N N 172 
GLN HB3  H  N N 173 
GLN HG2  H  N N 174 
GLN HG3  H  N N 175 
GLN HE21 H  N N 176 
GLN HE22 H  N N 177 
GLN HXT  H  N N 178 
GLU N    N  N N 179 
GLU CA   C  N S 180 
GLU C    C  N N 181 
GLU O    O  N N 182 
GLU CB   C  N N 183 
GLU CG   C  N N 184 
GLU CD   C  N N 185 
GLU OE1  O  N N 186 
GLU OE2  O  N N 187 
GLU OXT  O  N N 188 
GLU H    H  N N 189 
GLU H2   H  N N 190 
GLU HA   H  N N 191 
GLU HB2  H  N N 192 
GLU HB3  H  N N 193 
GLU HG2  H  N N 194 
GLU HG3  H  N N 195 
GLU HE2  H  N N 196 
GLU HXT  H  N N 197 
GLY N    N  N N 198 
GLY CA   C  N N 199 
GLY C    C  N N 200 
GLY O    O  N N 201 
GLY OXT  O  N N 202 
GLY H    H  N N 203 
GLY H2   H  N N 204 
GLY HA2  H  N N 205 
GLY HA3  H  N N 206 
GLY HXT  H  N N 207 
HIS N    N  N N 208 
HIS CA   C  N S 209 
HIS C    C  N N 210 
HIS O    O  N N 211 
HIS CB   C  N N 212 
HIS CG   C  Y N 213 
HIS ND1  N  Y N 214 
HIS CD2  C  Y N 215 
HIS CE1  C  Y N 216 
HIS NE2  N  Y N 217 
HIS OXT  O  N N 218 
HIS H    H  N N 219 
HIS H2   H  N N 220 
HIS HA   H  N N 221 
HIS HB2  H  N N 222 
HIS HB3  H  N N 223 
HIS HD1  H  N N 224 
HIS HD2  H  N N 225 
HIS HE1  H  N N 226 
HIS HE2  H  N N 227 
HIS HXT  H  N N 228 
HOH O    O  N N 229 
HOH H1   H  N N 230 
HOH H2   H  N N 231 
ILE N    N  N N 232 
ILE CA   C  N S 233 
ILE C    C  N N 234 
ILE O    O  N N 235 
ILE CB   C  N S 236 
ILE CG1  C  N N 237 
ILE CG2  C  N N 238 
ILE CD1  C  N N 239 
ILE OXT  O  N N 240 
ILE H    H  N N 241 
ILE H2   H  N N 242 
ILE HA   H  N N 243 
ILE HB   H  N N 244 
ILE HG12 H  N N 245 
ILE HG13 H  N N 246 
ILE HG21 H  N N 247 
ILE HG22 H  N N 248 
ILE HG23 H  N N 249 
ILE HD11 H  N N 250 
ILE HD12 H  N N 251 
ILE HD13 H  N N 252 
ILE HXT  H  N N 253 
LEU N    N  N N 254 
LEU CA   C  N S 255 
LEU C    C  N N 256 
LEU O    O  N N 257 
LEU CB   C  N N 258 
LEU CG   C  N N 259 
LEU CD1  C  N N 260 
LEU CD2  C  N N 261 
LEU OXT  O  N N 262 
LEU H    H  N N 263 
LEU H2   H  N N 264 
LEU HA   H  N N 265 
LEU HB2  H  N N 266 
LEU HB3  H  N N 267 
LEU HG   H  N N 268 
LEU HD11 H  N N 269 
LEU HD12 H  N N 270 
LEU HD13 H  N N 271 
LEU HD21 H  N N 272 
LEU HD22 H  N N 273 
LEU HD23 H  N N 274 
LEU HXT  H  N N 275 
LYS N    N  N N 276 
LYS CA   C  N S 277 
LYS C    C  N N 278 
LYS O    O  N N 279 
LYS CB   C  N N 280 
LYS CG   C  N N 281 
LYS CD   C  N N 282 
LYS CE   C  N N 283 
LYS NZ   N  N N 284 
LYS OXT  O  N N 285 
LYS H    H  N N 286 
LYS H2   H  N N 287 
LYS HA   H  N N 288 
LYS HB2  H  N N 289 
LYS HB3  H  N N 290 
LYS HG2  H  N N 291 
LYS HG3  H  N N 292 
LYS HD2  H  N N 293 
LYS HD3  H  N N 294 
LYS HE2  H  N N 295 
LYS HE3  H  N N 296 
LYS HZ1  H  N N 297 
LYS HZ2  H  N N 298 
LYS HZ3  H  N N 299 
LYS HXT  H  N N 300 
MET N    N  N N 301 
MET CA   C  N S 302 
MET C    C  N N 303 
MET O    O  N N 304 
MET CB   C  N N 305 
MET CG   C  N N 306 
MET SD   S  N N 307 
MET CE   C  N N 308 
MET OXT  O  N N 309 
MET H    H  N N 310 
MET H2   H  N N 311 
MET HA   H  N N 312 
MET HB2  H  N N 313 
MET HB3  H  N N 314 
MET HG2  H  N N 315 
MET HG3  H  N N 316 
MET HE1  H  N N 317 
MET HE2  H  N N 318 
MET HE3  H  N N 319 
MET HXT  H  N N 320 
PHE N    N  N N 321 
PHE CA   C  N S 322 
PHE C    C  N N 323 
PHE O    O  N N 324 
PHE CB   C  N N 325 
PHE CG   C  Y N 326 
PHE CD1  C  Y N 327 
PHE CD2  C  Y N 328 
PHE CE1  C  Y N 329 
PHE CE2  C  Y N 330 
PHE CZ   C  Y N 331 
PHE OXT  O  N N 332 
PHE H    H  N N 333 
PHE H2   H  N N 334 
PHE HA   H  N N 335 
PHE HB2  H  N N 336 
PHE HB3  H  N N 337 
PHE HD1  H  N N 338 
PHE HD2  H  N N 339 
PHE HE1  H  N N 340 
PHE HE2  H  N N 341 
PHE HZ   H  N N 342 
PHE HXT  H  N N 343 
PRO N    N  N N 344 
PRO CA   C  N S 345 
PRO C    C  N N 346 
PRO O    O  N N 347 
PRO CB   C  N N 348 
PRO CG   C  N N 349 
PRO CD   C  N N 350 
PRO OXT  O  N N 351 
PRO H    H  N N 352 
PRO HA   H  N N 353 
PRO HB2  H  N N 354 
PRO HB3  H  N N 355 
PRO HG2  H  N N 356 
PRO HG3  H  N N 357 
PRO HD2  H  N N 358 
PRO HD3  H  N N 359 
PRO HXT  H  N N 360 
SER N    N  N N 361 
SER CA   C  N S 362 
SER C    C  N N 363 
SER O    O  N N 364 
SER CB   C  N N 365 
SER OG   O  N N 366 
SER OXT  O  N N 367 
SER H    H  N N 368 
SER H2   H  N N 369 
SER HA   H  N N 370 
SER HB2  H  N N 371 
SER HB3  H  N N 372 
SER HG   H  N N 373 
SER HXT  H  N N 374 
THR N    N  N N 375 
THR CA   C  N S 376 
THR C    C  N N 377 
THR O    O  N N 378 
THR CB   C  N R 379 
THR OG1  O  N N 380 
THR CG2  C  N N 381 
THR OXT  O  N N 382 
THR H    H  N N 383 
THR H2   H  N N 384 
THR HA   H  N N 385 
THR HB   H  N N 386 
THR HG1  H  N N 387 
THR HG21 H  N N 388 
THR HG22 H  N N 389 
THR HG23 H  N N 390 
THR HXT  H  N N 391 
TRP N    N  N N 392 
TRP CA   C  N S 393 
TRP C    C  N N 394 
TRP O    O  N N 395 
TRP CB   C  N N 396 
TRP CG   C  Y N 397 
TRP CD1  C  Y N 398 
TRP CD2  C  Y N 399 
TRP NE1  N  Y N 400 
TRP CE2  C  Y N 401 
TRP CE3  C  Y N 402 
TRP CZ2  C  Y N 403 
TRP CZ3  C  Y N 404 
TRP CH2  C  Y N 405 
TRP OXT  O  N N 406 
TRP H    H  N N 407 
TRP H2   H  N N 408 
TRP HA   H  N N 409 
TRP HB2  H  N N 410 
TRP HB3  H  N N 411 
TRP HD1  H  N N 412 
TRP HE1  H  N N 413 
TRP HE3  H  N N 414 
TRP HZ2  H  N N 415 
TRP HZ3  H  N N 416 
TRP HH2  H  N N 417 
TRP HXT  H  N N 418 
TYR N    N  N N 419 
TYR CA   C  N S 420 
TYR C    C  N N 421 
TYR O    O  N N 422 
TYR CB   C  N N 423 
TYR CG   C  Y N 424 
TYR CD1  C  Y N 425 
TYR CD2  C  Y N 426 
TYR CE1  C  Y N 427 
TYR CE2  C  Y N 428 
TYR CZ   C  Y N 429 
TYR OH   O  N N 430 
TYR OXT  O  N N 431 
TYR H    H  N N 432 
TYR H2   H  N N 433 
TYR HA   H  N N 434 
TYR HB2  H  N N 435 
TYR HB3  H  N N 436 
TYR HD1  H  N N 437 
TYR HD2  H  N N 438 
TYR HE1  H  N N 439 
TYR HE2  H  N N 440 
TYR HH   H  N N 441 
TYR HXT  H  N N 442 
VAL N    N  N N 443 
VAL CA   C  N S 444 
VAL C    C  N N 445 
VAL O    O  N N 446 
VAL CB   C  N N 447 
VAL CG1  C  N N 448 
VAL CG2  C  N N 449 
VAL OXT  O  N N 450 
VAL H    H  N N 451 
VAL H2   H  N N 452 
VAL HA   H  N N 453 
VAL HB   H  N N 454 
VAL HG11 H  N N 455 
VAL HG12 H  N N 456 
VAL HG13 H  N N 457 
VAL HG21 H  N N 458 
VAL HG22 H  N N 459 
VAL HG23 H  N N 460 
VAL HXT  H  N N 461 
ZN  ZN   ZN N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
E49 N1  C6   doub Y N 115 
E49 N1  C2   sing Y N 116 
E49 C2  N3   doub Y N 117 
E49 N3  C4   sing Y N 118 
E49 C4  C11  sing N N 119 
E49 C5  C4   doub Y N 120 
E49 C6  C5   sing Y N 121 
E49 S7  C2   sing N N 122 
E49 S7  C8   sing N N 123 
E49 C8  C9   sing N N 124 
E49 C9  C13  sing N N 125 
E49 O10 C9   doub N N 126 
E49 C12 C6   sing N N 127 
E49 C13 C18  doub Y N 128 
E49 C13 C14  sing Y N 129 
E49 C14 C15  doub Y N 130 
E49 C15 C16  sing Y N 131 
E49 C15 S19  sing N N 132 
E49 C17 C16  doub Y N 133 
E49 C18 C17  sing Y N 134 
E49 S19 O20  doub N N 135 
E49 S19 O22  doub N N 136 
E49 N23 S19  sing N N 137 
E49 C5  H5   sing N N 138 
E49 C8  H8   sing N N 139 
E49 C8  H8A  sing N N 140 
E49 C11 H11  sing N N 141 
E49 C11 H11A sing N N 142 
E49 C11 H11B sing N N 143 
E49 C12 H12  sing N N 144 
E49 C12 H12A sing N N 145 
E49 C12 H12B sing N N 146 
E49 C14 H14  sing N N 147 
E49 C17 H17  sing N N 148 
E49 C18 H18  sing N N 149 
E49 N23 HN23 sing N N 150 
E49 N23 HN2A sing N N 151 
E49 C16 CL21 sing N N 152 
GLN N   CA   sing N N 153 
GLN N   H    sing N N 154 
GLN N   H2   sing N N 155 
GLN CA  C    sing N N 156 
GLN CA  CB   sing N N 157 
GLN CA  HA   sing N N 158 
GLN C   O    doub N N 159 
GLN C   OXT  sing N N 160 
GLN CB  CG   sing N N 161 
GLN CB  HB2  sing N N 162 
GLN CB  HB3  sing N N 163 
GLN CG  CD   sing N N 164 
GLN CG  HG2  sing N N 165 
GLN CG  HG3  sing N N 166 
GLN CD  OE1  doub N N 167 
GLN CD  NE2  sing N N 168 
GLN NE2 HE21 sing N N 169 
GLN NE2 HE22 sing N N 170 
GLN OXT HXT  sing N N 171 
GLU N   CA   sing N N 172 
GLU N   H    sing N N 173 
GLU N   H2   sing N N 174 
GLU CA  C    sing N N 175 
GLU CA  CB   sing N N 176 
GLU CA  HA   sing N N 177 
GLU C   O    doub N N 178 
GLU C   OXT  sing N N 179 
GLU CB  CG   sing N N 180 
GLU CB  HB2  sing N N 181 
GLU CB  HB3  sing N N 182 
GLU CG  CD   sing N N 183 
GLU CG  HG2  sing N N 184 
GLU CG  HG3  sing N N 185 
GLU CD  OE1  doub N N 186 
GLU CD  OE2  sing N N 187 
GLU OE2 HE2  sing N N 188 
GLU OXT HXT  sing N N 189 
GLY N   CA   sing N N 190 
GLY N   H    sing N N 191 
GLY N   H2   sing N N 192 
GLY CA  C    sing N N 193 
GLY CA  HA2  sing N N 194 
GLY CA  HA3  sing N N 195 
GLY C   O    doub N N 196 
GLY C   OXT  sing N N 197 
GLY OXT HXT  sing N N 198 
HIS N   CA   sing N N 199 
HIS N   H    sing N N 200 
HIS N   H2   sing N N 201 
HIS CA  C    sing N N 202 
HIS CA  CB   sing N N 203 
HIS CA  HA   sing N N 204 
HIS C   O    doub N N 205 
HIS C   OXT  sing N N 206 
HIS CB  CG   sing N N 207 
HIS CB  HB2  sing N N 208 
HIS CB  HB3  sing N N 209 
HIS CG  ND1  sing Y N 210 
HIS CG  CD2  doub Y N 211 
HIS ND1 CE1  doub Y N 212 
HIS ND1 HD1  sing N N 213 
HIS CD2 NE2  sing Y N 214 
HIS CD2 HD2  sing N N 215 
HIS CE1 NE2  sing Y N 216 
HIS CE1 HE1  sing N N 217 
HIS NE2 HE2  sing N N 218 
HIS OXT HXT  sing N N 219 
HOH O   H1   sing N N 220 
HOH O   H2   sing N N 221 
ILE N   CA   sing N N 222 
ILE N   H    sing N N 223 
ILE N   H2   sing N N 224 
ILE CA  C    sing N N 225 
ILE CA  CB   sing N N 226 
ILE CA  HA   sing N N 227 
ILE C   O    doub N N 228 
ILE C   OXT  sing N N 229 
ILE CB  CG1  sing N N 230 
ILE CB  CG2  sing N N 231 
ILE CB  HB   sing N N 232 
ILE CG1 CD1  sing N N 233 
ILE CG1 HG12 sing N N 234 
ILE CG1 HG13 sing N N 235 
ILE CG2 HG21 sing N N 236 
ILE CG2 HG22 sing N N 237 
ILE CG2 HG23 sing N N 238 
ILE CD1 HD11 sing N N 239 
ILE CD1 HD12 sing N N 240 
ILE CD1 HD13 sing N N 241 
ILE OXT HXT  sing N N 242 
LEU N   CA   sing N N 243 
LEU N   H    sing N N 244 
LEU N   H2   sing N N 245 
LEU CA  C    sing N N 246 
LEU CA  CB   sing N N 247 
LEU CA  HA   sing N N 248 
LEU C   O    doub N N 249 
LEU C   OXT  sing N N 250 
LEU CB  CG   sing N N 251 
LEU CB  HB2  sing N N 252 
LEU CB  HB3  sing N N 253 
LEU CG  CD1  sing N N 254 
LEU CG  CD2  sing N N 255 
LEU CG  HG   sing N N 256 
LEU CD1 HD11 sing N N 257 
LEU CD1 HD12 sing N N 258 
LEU CD1 HD13 sing N N 259 
LEU CD2 HD21 sing N N 260 
LEU CD2 HD22 sing N N 261 
LEU CD2 HD23 sing N N 262 
LEU OXT HXT  sing N N 263 
LYS N   CA   sing N N 264 
LYS N   H    sing N N 265 
LYS N   H2   sing N N 266 
LYS CA  C    sing N N 267 
LYS CA  CB   sing N N 268 
LYS CA  HA   sing N N 269 
LYS C   O    doub N N 270 
LYS C   OXT  sing N N 271 
LYS CB  CG   sing N N 272 
LYS CB  HB2  sing N N 273 
LYS CB  HB3  sing N N 274 
LYS CG  CD   sing N N 275 
LYS CG  HG2  sing N N 276 
LYS CG  HG3  sing N N 277 
LYS CD  CE   sing N N 278 
LYS CD  HD2  sing N N 279 
LYS CD  HD3  sing N N 280 
LYS CE  NZ   sing N N 281 
LYS CE  HE2  sing N N 282 
LYS CE  HE3  sing N N 283 
LYS NZ  HZ1  sing N N 284 
LYS NZ  HZ2  sing N N 285 
LYS NZ  HZ3  sing N N 286 
LYS OXT HXT  sing N N 287 
MET N   CA   sing N N 288 
MET N   H    sing N N 289 
MET N   H2   sing N N 290 
MET CA  C    sing N N 291 
MET CA  CB   sing N N 292 
MET CA  HA   sing N N 293 
MET C   O    doub N N 294 
MET C   OXT  sing N N 295 
MET CB  CG   sing N N 296 
MET CB  HB2  sing N N 297 
MET CB  HB3  sing N N 298 
MET CG  SD   sing N N 299 
MET CG  HG2  sing N N 300 
MET CG  HG3  sing N N 301 
MET SD  CE   sing N N 302 
MET CE  HE1  sing N N 303 
MET CE  HE2  sing N N 304 
MET CE  HE3  sing N N 305 
MET OXT HXT  sing N N 306 
PHE N   CA   sing N N 307 
PHE N   H    sing N N 308 
PHE N   H2   sing N N 309 
PHE CA  C    sing N N 310 
PHE CA  CB   sing N N 311 
PHE CA  HA   sing N N 312 
PHE C   O    doub N N 313 
PHE C   OXT  sing N N 314 
PHE CB  CG   sing N N 315 
PHE CB  HB2  sing N N 316 
PHE CB  HB3  sing N N 317 
PHE CG  CD1  doub Y N 318 
PHE CG  CD2  sing Y N 319 
PHE CD1 CE1  sing Y N 320 
PHE CD1 HD1  sing N N 321 
PHE CD2 CE2  doub Y N 322 
PHE CD2 HD2  sing N N 323 
PHE CE1 CZ   doub Y N 324 
PHE CE1 HE1  sing N N 325 
PHE CE2 CZ   sing Y N 326 
PHE CE2 HE2  sing N N 327 
PHE CZ  HZ   sing N N 328 
PHE OXT HXT  sing N N 329 
PRO N   CA   sing N N 330 
PRO N   CD   sing N N 331 
PRO N   H    sing N N 332 
PRO CA  C    sing N N 333 
PRO CA  CB   sing N N 334 
PRO CA  HA   sing N N 335 
PRO C   O    doub N N 336 
PRO C   OXT  sing N N 337 
PRO CB  CG   sing N N 338 
PRO CB  HB2  sing N N 339 
PRO CB  HB3  sing N N 340 
PRO CG  CD   sing N N 341 
PRO CG  HG2  sing N N 342 
PRO CG  HG3  sing N N 343 
PRO CD  HD2  sing N N 344 
PRO CD  HD3  sing N N 345 
PRO OXT HXT  sing N N 346 
SER N   CA   sing N N 347 
SER N   H    sing N N 348 
SER N   H2   sing N N 349 
SER CA  C    sing N N 350 
SER CA  CB   sing N N 351 
SER CA  HA   sing N N 352 
SER C   O    doub N N 353 
SER C   OXT  sing N N 354 
SER CB  OG   sing N N 355 
SER CB  HB2  sing N N 356 
SER CB  HB3  sing N N 357 
SER OG  HG   sing N N 358 
SER OXT HXT  sing N N 359 
THR N   CA   sing N N 360 
THR N   H    sing N N 361 
THR N   H2   sing N N 362 
THR CA  C    sing N N 363 
THR CA  CB   sing N N 364 
THR CA  HA   sing N N 365 
THR C   O    doub N N 366 
THR C   OXT  sing N N 367 
THR CB  OG1  sing N N 368 
THR CB  CG2  sing N N 369 
THR CB  HB   sing N N 370 
THR OG1 HG1  sing N N 371 
THR CG2 HG21 sing N N 372 
THR CG2 HG22 sing N N 373 
THR CG2 HG23 sing N N 374 
THR OXT HXT  sing N N 375 
TRP N   CA   sing N N 376 
TRP N   H    sing N N 377 
TRP N   H2   sing N N 378 
TRP CA  C    sing N N 379 
TRP CA  CB   sing N N 380 
TRP CA  HA   sing N N 381 
TRP C   O    doub N N 382 
TRP C   OXT  sing N N 383 
TRP CB  CG   sing N N 384 
TRP CB  HB2  sing N N 385 
TRP CB  HB3  sing N N 386 
TRP CG  CD1  doub Y N 387 
TRP CG  CD2  sing Y N 388 
TRP CD1 NE1  sing Y N 389 
TRP CD1 HD1  sing N N 390 
TRP CD2 CE2  doub Y N 391 
TRP CD2 CE3  sing Y N 392 
TRP NE1 CE2  sing Y N 393 
TRP NE1 HE1  sing N N 394 
TRP CE2 CZ2  sing Y N 395 
TRP CE3 CZ3  doub Y N 396 
TRP CE3 HE3  sing N N 397 
TRP CZ2 CH2  doub Y N 398 
TRP CZ2 HZ2  sing N N 399 
TRP CZ3 CH2  sing Y N 400 
TRP CZ3 HZ3  sing N N 401 
TRP CH2 HH2  sing N N 402 
TRP OXT HXT  sing N N 403 
TYR N   CA   sing N N 404 
TYR N   H    sing N N 405 
TYR N   H2   sing N N 406 
TYR CA  C    sing N N 407 
TYR CA  CB   sing N N 408 
TYR CA  HA   sing N N 409 
TYR C   O    doub N N 410 
TYR C   OXT  sing N N 411 
TYR CB  CG   sing N N 412 
TYR CB  HB2  sing N N 413 
TYR CB  HB3  sing N N 414 
TYR CG  CD1  doub Y N 415 
TYR CG  CD2  sing Y N 416 
TYR CD1 CE1  sing Y N 417 
TYR CD1 HD1  sing N N 418 
TYR CD2 CE2  doub Y N 419 
TYR CD2 HD2  sing N N 420 
TYR CE1 CZ   doub Y N 421 
TYR CE1 HE1  sing N N 422 
TYR CE2 CZ   sing Y N 423 
TYR CE2 HE2  sing N N 424 
TYR CZ  OH   sing N N 425 
TYR OH  HH   sing N N 426 
TYR OXT HXT  sing N N 427 
VAL N   CA   sing N N 428 
VAL N   H    sing N N 429 
VAL N   H2   sing N N 430 
VAL CA  C    sing N N 431 
VAL CA  CB   sing N N 432 
VAL CA  HA   sing N N 433 
VAL C   O    doub N N 434 
VAL C   OXT  sing N N 435 
VAL CB  CG1  sing N N 436 
VAL CB  CG2  sing N N 437 
VAL CB  HB   sing N N 438 
VAL CG1 HG11 sing N N 439 
VAL CG1 HG12 sing N N 440 
VAL CG1 HG13 sing N N 441 
VAL CG2 HG21 sing N N 442 
VAL CG2 HG22 sing N N 443 
VAL CG2 HG23 sing N N 444 
VAL OXT HXT  sing N N 445 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                    ZN  
3 'DIMETHYL SULFOXIDE'                                                          DMS 
4 BICINE                                                                        BCN 
5 '2-chloro-5-{[(4,6-dimethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' E49 
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' 
# 
