data_3MHM
# 
_entry.id   3MHM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.380 
_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   3MHM         pdb_00003mhm 10.2210/pdb3mhm/pdb 
RCSB  RCSB058556   ?            ?                   
WWPDB D_1000058556 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3M2N 'The same protein with other ligand' unspecified 
PDB 3M3X 'The same protein with other ligand' unspecified 
PDB 3M5E 'The same protein with other ligand' unspecified 
PDB 3M40 'The same protein with other ligand' unspecified 
PDB 3MHI 'The same protein with other ligand' unspecified 
PDB 3MHL 'The same protein with other ligand' unspecified 
PDB 3MHO 'The same protein with other ligand' unspecified 
# 
_pdbx_database_status.entry_id                        3MHM 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2010-04-08 
_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.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     
'4-[N-(Substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            18 
_citation.page_first                7413 
_citation.page_last                 7421 
_citation.year                      2010 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20889345 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2010.09.011 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sudzius, J.'       1  ? 
primary 'Baranauskiene, L.' 2  ? 
primary 'Golovenko, D.'     3  ? 
primary 'Matuliene, J.'     4  ? 
primary 'Michailoviene, V.' 5  ? 
primary 'Torresan, J.'      6  ? 
primary 'Jachno, J.'        7  ? 
primary 'Sukackaite, R.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Tumkevicius, S.'   11 ? 
primary 'Matulis, D.'       12 ? 
# 
_cell.entry_id           3MHM 
_cell.length_a           42.250 
_cell.length_b           41.171 
_cell.length_c           72.243 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.10 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
_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                         3MHM 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_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    1   ?       ? ? ? 
4 non-polymer syn '4-({[6-(benzylamino)-5-nitropyrimidin-4-yl]amino}methyl)benzenesulfonamide' 414.438   1   ?       ? ? ? 
5 water       nat water                                                                        18.015    290 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonic anhydrase II, CA-II, Carbonate dehydratase II, Carbonic anhydrase C, CAC' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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              3MHM 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'    121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                         ? 'C2 H6 O S'       78.133  
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 
J75 non-polymer         . '4-({[6-(benzylamino)-5-nitropyrimidin-4-yl]amino}methyl)benzenesulfonamide' 
'4-{[N-(6-benzylamino-5-nitropyrimidin-4-yl)amino]methyl}benzenesulfonamide' 'C18 H18 N6 O4 S' 414.438 
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          3MHM 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   40.88 
_exptl_crystal.density_Matthews      2.08 
_exptl_crystal.pdbx_mosaicity        ? 
_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              8 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    
'0.1M Na-bicine pH 9, 0.2M ammonium sulfate, 2.4M Na-malonate pH 7, VAPOR DIFFUSION, temperature 293K' 
_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                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2009-12-18 
_diffrn_detector.details                'Bent, vertically focussing mirror' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    '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   0.81 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_wavelength_list        0.81 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
# 
_reflns.entry_id                     3MHM 
_reflns.d_resolution_high            1.500 
_reflns.d_resolution_low             70.068 
_reflns.number_all                   38763 
_reflns.number_obs                   37716 
_reflns.pdbx_Rmerge_I_obs            0.033 
_reflns.pdbx_netI_over_sigmaI        25.400 
_reflns.pdbx_Rsym_value              0.033 
_reflns.pdbx_redundancy              4.100 
_reflns.percent_possible_obs         97.300 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        14.2 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.50 
_reflns_shell.d_res_low              1.58 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    20829 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.157 
_reflns_shell.meanI_over_sigI_obs    5.8 
_reflns_shell.pdbx_Rsym_value        0.157 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        3.90 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      5409 
_reflns_shell.percent_possible_all   96.10 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3MHM 
_refine.ls_d_res_high                            1.500 
_refine.ls_d_res_low                             39.86 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    96.990 
_refine.ls_number_reflns_obs                     37698 
_refine.ls_number_reflns_all                     38868 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_obs                          0.13727 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.13179 
_refine.ls_R_factor_R_free                       0.18657 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  3760 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_number_reflns_R_work                  33938 
_refine.B_iso_mean                               15.400 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             anisotropic 
_refine.aniso_B[1][1]                            0.01 
_refine.aniso_B[2][2]                            0.19 
_refine.aniso_B[3][3]                            -0.18 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.04 
_refine.aniso_B[2][3]                            0.00 
_refine.correlation_coeff_Fo_to_Fc               0.971 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       0.097 
_refine.pdbx_overall_ESU_R_Free                  0.079 
_refine.overall_SU_ML                            0.042 
_refine.overall_SU_B                             2.359 
_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          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                45.29 
_refine.B_iso_min                                4.34 
_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_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             290 
_refine_hist.number_atoms_total               2373 
_refine_hist.d_res_high                       1.500 
_refine_hist.d_res_low                        39.86 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.028  0.022  ? 2282 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.158  1.965  ? 3113 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.139  5.000  ? 282  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.961 24.712 ? 104  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.835 15.000 ? 380  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       23.372 15.000 ? 8    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.163  0.200  ? 318  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.013  0.020  ? 1795 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.232  0.200  ? 1073 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.311  0.200  ? 1500 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.147  0.200  ? 215  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          0.079  0.200  ? 3    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.247  0.200  ? 85   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.259  0.200  ? 46   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.568  1.500  ? 1418 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.483  2.000  ? 2228 'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.607  3.000  ? 1025 'X-RAY DIFFRACTION' ? 
r_scangle_it                 6.072  4.500  ? 885  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           2.857  3.000  ? 2443 'X-RAY DIFFRACTION' ? 
r_sphericity_free            12.994 3.000  ? 292  'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          8.281  3.000  ? 2206 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.500 
_refine_ls_shell.d_res_low                        1.539 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               95.750 
_refine_ls_shell.number_reflns_R_work             2474 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.144 
_refine_ls_shell.R_factor_R_free                  0.254 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             272 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2746 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3MHM 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 4-{[N-(6-benzylamino-5-nitropyrimidin-4-yl)amino]methyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3MHM 
_struct_keywords.text            'drug design, carbonic anhydrase, sulfonamide, 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 4 ? 
E N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_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 0.28 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.06 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A DMS 263 ? 4  'BINDING SITE FOR RESIDUE DMS A 263' 
AC3 Software A J75 264 ? 16 'BINDING SITE FOR RESIDUE J75 A 264' 
# 
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  J75 D .   ? J75 A 264 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  HOH E .   ? HOH A 544 . ? 1_555 ? 
9  AC3 16 ILE A 91  ? ILE A 91  . ? 1_555 ? 
10 AC3 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
11 AC3 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
12 AC3 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
13 AC3 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
14 AC3 16 PHE A 130 ? PHE A 131 . ? 1_555 ? 
15 AC3 16 GLY A 131 ? GLY A 132 . ? 1_555 ? 
16 AC3 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
17 AC3 16 THR A 198 ? THR A 199 . ? 1_555 ? 
18 AC3 16 THR A 199 ? THR A 200 . ? 1_555 ? 
19 AC3 16 TRP A 208 ? TRP A 209 . ? 1_555 ? 
20 AC3 16 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
21 AC3 16 HOH E .   ? HOH A 320 . ? 1_555 ? 
22 AC3 16 HOH E .   ? HOH A 464 . ? 1_555 ? 
23 AC3 16 HOH E .   ? HOH A 471 . ? 1_555 ? 
24 AC3 16 HOH E .   ? HOH A 543 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3MHM 
_atom_sites.fract_transf_matrix[1][1]   0.023669 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005945 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024289 
_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]   0.014272 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 9.253   1.054   8.200   1.00 26.32 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.199  0.046   8.796   1.00 25.17 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.422   -1.007  9.596   1.00 21.89 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.553   -2.192  9.386   1.00 22.16 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 11.331  0.617   9.670   1.00 28.53 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 12.464  -0.353  9.826   1.00 32.97 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 12.648  -1.125  10.964  1.00 39.35 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 13.394  -0.774  8.928   1.00 36.56 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 13.673  -1.952  10.771  1.00 39.70 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 14.142  -1.759  9.543   1.00 40.53 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.611   -0.566  10.516  1.00 18.67 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.877   -1.544  11.348  1.00 14.55 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.871   -2.324  10.556  1.00 15.04 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.344   -1.863  9.518   1.00 16.18 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.135   -0.842  12.506  1.00 13.51 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.934   0.021   12.133  1.00 14.34 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.886   1.405   11.751  1.00 14.34 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.586   -0.437  12.069  1.00 14.25 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.602   1.774   11.507  1.00 14.74 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.782   0.676   11.638  1.00 11.85 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.959   -1.702  12.296  1.00 12.79 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.380   0.596   11.523  1.00 14.05 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.558   -1.805  12.119  1.00 11.79 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.776   -0.625  11.789  1.00 14.02 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.562   -3.494  11.091  1.00 13.02 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.527   -4.376  10.470  1.00 12.62 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.238   -5.560  11.389  1.00 14.40 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.262   -5.425  12.644  1.00 14.20 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.943   -6.692  10.763  1.00 15.67 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.562   -7.841  11.605  1.00 17.33 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.538   -9.081  11.641  1.00 19.84 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.307   -10.166 12.390  1.00 22.12 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.106   -8.171  11.269  1.00 15.08 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.148   -7.060  11.777  1.00 11.04 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.726   -7.074  13.143  1.00 11.02 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.691   -6.034  10.957  1.00 12.12 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.849   -6.066  13.656  1.00 9.75  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.784   -5.018  11.455  1.00 8.95  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.368   -5.056  12.791  1.00 9.19  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.471  -4.125  13.294  1.00 9.30  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.626   -8.961  10.870  1.00 20.40 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.651   -10.111 10.775  1.00 19.31 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.653   -10.447 11.885  1.00 23.23 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.794   -9.799  12.988  1.00 23.00 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.491   -11.459 11.572  1.00 25.14 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.592  -11.836 12.471  1.00 25.13 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.472  -10.696 12.802  1.00 24.88 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.850  -10.595 14.014  1.00 25.57 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.458  -12.905 11.896  1.00 26.28 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.494  -13.464 12.852  1.00 29.14 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 13.083  -14.722 12.145  1.00 31.25 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 14.472  -15.138 12.616  1.00 34.49 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 15.068  -16.211 11.619  1.00 35.34 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 11.800  -9.861  11.785  1.00 22.41 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.767  -8.847  12.025  1.00 21.47 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 12.152  -7.502  12.181  1.00 18.14 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.909  -6.637  12.568  1.00 20.32 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.865  -8.836  10.930  1.00 18.62 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 14.506  -10.203 10.718  1.00 20.29 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 15.606  -10.669 11.434  1.00 26.22 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 14.176  -11.176 9.848   1.00 22.53 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 15.903  -11.891 11.011  1.00 27.27 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 15.037  -12.225 10.054  1.00 24.40 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.811  -7.297  11.959  1.00 17.90 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.241  -5.949  12.180  1.00 16.11 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.915   -5.951  12.940  1.00 15.59 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.272   -4.905  13.060  1.00 16.45 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 10.064  -5.170  10.897  1.00 15.46 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 9.058   -5.775  9.987   1.00 16.69 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.455   -6.824  10.316  1.00 19.88 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.782   -5.114  8.884   1.00 20.08 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.567   -7.100  13.538  1.00 15.46 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.276   -7.246  14.178  1.00 15.21 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.233   -6.671  15.580  1.00 14.15 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 8.146   -5.950  16.019  1.00 13.43 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.134   -6.968  16.294  1.00 12.16 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.871   -6.333  17.590  1.00 12.58 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 7.003   -6.300  18.601  1.00 11.57 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.159   -5.314  19.346  1.00 14.49 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.648   -7.111  18.122  1.00 12.89 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.859   -7.441  16.828  1.00 11.61 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.993   -7.768  15.819  1.00 12.36 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 7.812   -7.366  18.654  1.00 12.68 ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 8.894   -7.431  19.609  1.00 14.24 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 10.062  -6.464  19.305  1.00 13.20 ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 10.963  -6.279  20.128  1.00 14.94 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 9.400   -8.895  19.673  1.00 17.71 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 10.048  -9.344  18.342  1.00 21.13 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 9.212   -9.996  17.172  1.00 24.91 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 7.987   -9.643  17.003  1.00 19.44 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 9.907   -10.822 16.385  1.00 26.04 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 10.072  -5.920  18.107  1.00 12.27 ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 11.039  -4.935  17.653  1.00 12.81 ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 10.583  -3.471  17.805  1.00 11.66 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.457  -2.530  17.659  1.00 12.30 ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.422  -5.151  16.148  1.00 12.95 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 12.156  -6.438  15.924  1.00 15.30 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.532  -6.533  16.070  1.00 16.51 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 11.703  -7.677  15.619  1.00 18.33 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 13.890  -7.798  15.852  1.00 20.59 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 12.815  -8.508  15.560  1.00 18.95 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.277   -3.235  18.006  1.00 10.67 ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 8.760   -1.897  17.861  1.00 9.40  ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.388   -0.920  18.891  1.00 10.02 ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.482   0.324   18.626  1.00 11.35 ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.233   -1.915  18.026  1.00 9.39  ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 6.557   -2.595  16.868  1.00 10.56 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 7.121   -3.032  15.686  1.00 8.76  ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 5.162   -2.926  16.801  1.00 9.69  ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 6.135   -3.645  14.885  1.00 8.72  ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 4.918   -3.538  15.527  1.00 8.84  ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 4.082   -2.724  17.682  1.00 8.01  ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 3.628   -4.007  15.148  1.00 8.76  ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 2.827   -3.157  17.304  1.00 9.16  ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 2.583   -3.757  16.026  1.00 10.04 ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 9.759   -1.438  20.067  1.00 12.25 ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.238  -0.554  21.154  1.00 12.57 ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.501  0.227   20.719  1.00 13.26 ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 11.804  1.267   21.332  1.00 14.93 ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.530  -1.287  22.460  1.00 12.00 ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 11.739  -2.197  22.338  1.00 11.37 ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 12.972  -1.827  22.841  1.00 14.69 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 11.929  -3.393  21.741  1.00 15.06 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 13.866  -2.746  22.573  1.00 15.29 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 13.269  -3.722  21.922  1.00 16.69 ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 12.274  -0.315  19.760  1.00 12.34 ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 13.522  0.397   19.377  1.00 12.38 ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 13.187  1.759   18.685  1.00 14.00 ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 13.846  2.806   18.927  1.00 18.75 ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 14.424  -0.434  18.468  1.00 14.25 ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 14.970  -1.676  19.223  1.00 14.79 ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 15.675  -2.671  18.344  1.00 14.72 ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 14.697  -3.591  17.658  1.00 15.87 ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 15.305  -4.486  16.574  1.00 14.66 ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 12.188  1.783   17.820  1.00 14.61 ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 11.753  3.073   17.245  1.00 15.85 ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 10.739  3.814   18.097  1.00 15.27 ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 10.622  5.054   17.942  1.00 17.31 ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 11.149  2.888   15.862  1.00 17.82 ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 12.199  2.878   14.740  1.00 20.71 ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 13.346  3.315   14.939  1.00 24.47 ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 11.891  2.402   13.635  1.00 33.31 ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 9.974   3.065   18.914  1.00 12.81 ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 8.859   3.658   19.661  1.00 12.35 ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 8.945   3.169   21.138  1.00 12.17 ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 8.302   2.169   21.491  1.00 11.19 ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 7.512   3.188   19.040  1.00 13.95 ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 7.385   3.572   17.653  1.00 12.75 ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 7.006   4.887   17.306  1.00 16.02 ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 7.770   2.672   16.654  1.00 14.48 ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 7.002   5.255   15.946  1.00 18.01 ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 7.764   3.026   15.312  1.00 14.33 ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 7.356   4.335   14.951  1.00 15.49 ? 20  PHE A CZ  1 
ATOM   154  N  N   A PRO A 1 21  ? 9.721   3.857   22.028  0.50 12.65 ? 21  PRO A N   1 
ATOM   155  N  N   B PRO A 1 21  ? 9.945   3.699   21.855  0.50 12.67 ? 21  PRO A N   1 
ATOM   156  C  CA  A PRO A 1 21  ? 9.954   3.421   23.426  0.50 11.65 ? 21  PRO A CA  1 
ATOM   157  C  CA  B PRO A 1 21  ? 10.198  3.158   23.160  0.50 10.97 ? 21  PRO A CA  1 
ATOM   158  C  C   A PRO A 1 21  ? 8.744   3.300   24.366  0.50 11.93 ? 21  PRO A C   1 
ATOM   159  C  C   B PRO A 1 21  ? 8.936   3.125   23.989  0.50 10.81 ? 21  PRO A C   1 
ATOM   160  O  O   A PRO A 1 21  ? 8.804   2.542   25.374  0.50 11.92 ? 21  PRO A O   1 
ATOM   161  O  O   B PRO A 1 21  ? 8.912   2.326   24.931  0.50 11.50 ? 21  PRO A O   1 
ATOM   162  C  CB  A PRO A 1 21  ? 10.963  4.462   24.002  0.50 11.85 ? 21  PRO A CB  1 
ATOM   163  C  CB  B PRO A 1 21  ? 11.300  4.060   23.767  0.50 11.67 ? 21  PRO A CB  1 
ATOM   164  C  CG  A PRO A 1 21  ? 10.917  5.569   23.052  0.50 12.66 ? 21  PRO A CG  1 
ATOM   165  C  CG  B PRO A 1 21  ? 11.751  4.968   22.675  0.50 11.48 ? 21  PRO A CG  1 
ATOM   166  C  CD  A PRO A 1 21  ? 10.532  5.052   21.698  0.50 11.55 ? 21  PRO A CD  1 
ATOM   167  C  CD  B PRO A 1 21  ? 10.919  4.731   21.436  0.50 12.06 ? 21  PRO A CD  1 
ATOM   168  N  N   A ILE A 1 22  ? 7.669   4.053   24.077  0.50 10.61 ? 22  ILE A N   1 
ATOM   169  N  N   B ILE A 1 22  ? 7.882   3.912   23.623  0.50 10.21 ? 22  ILE A N   1 
ATOM   170  C  CA  A ILE A 1 22  ? 6.442   3.810   24.797  0.50 10.59 ? 22  ILE A CA  1 
ATOM   171  C  CA  B ILE A 1 22  ? 6.646   3.887   24.422  0.50 9.45  ? 22  ILE A CA  1 
ATOM   172  C  C   A ILE A 1 22  ? 5.916   2.351   24.575  0.50 9.98  ? 22  ILE A C   1 
ATOM   173  C  C   B ILE A 1 22  ? 5.965   2.488   24.447  0.50 9.53  ? 22  ILE A C   1 
ATOM   174  O  O   A ILE A 1 22  ? 4.985   1.902   25.311  0.50 10.51 ? 22  ILE A O   1 
ATOM   175  O  O   B ILE A 1 22  ? 4.981   2.239   25.189  0.50 10.35 ? 22  ILE A O   1 
ATOM   176  C  CB  A ILE A 1 22  ? 5.340   4.855   24.412  0.50 9.55  ? 22  ILE A CB  1 
ATOM   177  C  CB  B ILE A 1 22  ? 5.633   4.975   23.946  0.50 9.49  ? 22  ILE A CB  1 
ATOM   178  C  CG1 A ILE A 1 22  ? 4.330   5.015   25.538  0.50 12.25 ? 22  ILE A CG1 1 
ATOM   179  C  CG1 B ILE A 1 22  ? 4.670   5.332   25.074  0.50 7.24  ? 22  ILE A CG1 1 
ATOM   180  C  CG2 A ILE A 1 22  ? 4.677   4.511   23.061  0.50 11.97 ? 22  ILE A CG2 1 
ATOM   181  C  CG2 B ILE A 1 22  ? 5.022   4.613   22.523  0.50 9.08  ? 22  ILE A CG2 1 
ATOM   182  C  CD1 A ILE A 1 22  ? 4.876   5.800   26.689  0.50 17.84 ? 22  ILE A CD1 1 
ATOM   183  C  CD1 B ILE A 1 22  ? 3.527   6.264   24.758  0.50 9.32  ? 22  ILE A CD1 1 
ATOM   184  N  N   . ALA A 1 23  ? 6.463   1.604   23.594  1.00 9.09  ? 23  ALA A N   1 
ATOM   185  C  CA  . ALA A 1 23  ? 5.958   0.198   23.468  1.00 10.77 ? 23  ALA A CA  1 
ATOM   186  C  C   . ALA A 1 23  ? 6.083   -0.526  24.819  1.00 10.70 ? 23  ALA A C   1 
ATOM   187  O  O   . ALA A 1 23  ? 5.380   -1.559  25.018  1.00 10.61 ? 23  ALA A O   1 
ATOM   188  C  CB  . ALA A 1 23  ? 6.788   -0.606  22.434  1.00 11.27 ? 23  ALA A CB  1 
ATOM   189  N  N   . LYS A 1 24  ? 7.052   -0.086  25.681  1.00 11.24 ? 24  LYS A N   1 
ATOM   190  C  CA  . LYS A 1 24  ? 7.207   -0.708  27.035  1.00 12.66 ? 24  LYS A CA  1 
ATOM   191  C  C   . LYS A 1 24  ? 6.596   0.172   28.098  1.00 13.04 ? 24  LYS A C   1 
ATOM   192  O  O   . LYS A 1 24  ? 6.977   0.031   29.319  1.00 15.47 ? 24  LYS A O   1 
ATOM   193  C  CB  . LYS A 1 24  ? 8.698   -0.986  27.325  1.00 14.03 ? 24  LYS A CB  1 
ATOM   194  C  CG  . LYS A 1 24  ? 9.321   -1.909  26.358  1.00 16.15 ? 24  LYS A CG  1 
ATOM   195  C  CD  . LYS A 1 24  ? 10.835  -2.043  26.747  1.00 22.31 ? 24  LYS A CD  1 
ATOM   196  C  CE  . LYS A 1 24  ? 11.524  -2.973  25.748  1.00 25.47 ? 24  LYS A CE  1 
ATOM   197  N  NZ  . LYS A 1 24  ? 11.182  -4.337  26.094  1.00 26.57 ? 24  LYS A NZ  1 
ATOM   198  N  N   . GLY A 1 25  ? 5.570   0.970   27.716  1.00 12.80 ? 25  GLY A N   1 
ATOM   199  C  CA  . GLY A 1 25  ? 5.018   1.942   28.633  1.00 13.46 ? 25  GLY A CA  1 
ATOM   200  C  C   . GLY A 1 25  ? 4.014   1.396   29.639  1.00 12.38 ? 25  GLY A C   1 
ATOM   201  O  O   . GLY A 1 25  ? 3.828   0.161   29.793  1.00 13.69 ? 25  GLY A O   1 
ATOM   202  N  N   . GLU A 1 26  ? 3.384   2.318   30.365  1.00 13.73 ? 26  GLU A N   1 
ATOM   203  C  CA  . GLU A 1 26  ? 2.529   1.917   31.493  1.00 14.00 ? 26  GLU A CA  1 
ATOM   204  C  C   . GLU A 1 26  ? 1.068   1.603   31.141  1.00 11.73 ? 26  GLU A C   1 
ATOM   205  O  O   . GLU A 1 26  ? 0.299   1.074   31.984  1.00 11.42 ? 26  GLU A O   1 
ATOM   206  C  CB  . GLU A 1 26  ? 2.523   3.011   32.581  1.00 15.78 ? 26  GLU A CB  1 
ATOM   207  C  CG  . GLU A 1 26  ? 3.893   3.330   33.267  1.00 18.15 ? 26  GLU A CG  1 
ATOM   208  C  CD  . GLU A 1 26  ? 4.512   2.033   33.831  1.00 26.76 ? 26  GLU A CD  1 
ATOM   209  O  OE1 . GLU A 1 26  ? 3.869   1.350   34.676  1.00 27.24 ? 26  GLU A OE1 1 
ATOM   210  O  OE2 . GLU A 1 26  ? 5.630   1.692   33.376  1.00 29.87 ? 26  GLU A OE2 1 
ATOM   211  N  N   . ARG A 1 27  ? 0.633   1.966   29.910  1.00 9.35  ? 27  ARG A N   1 
ATOM   212  C  CA  . ARG A 1 27  ? -0.770  1.736   29.558  1.00 8.55  ? 27  ARG A CA  1 
ATOM   213  C  C   . ARG A 1 27  ? -0.852  1.283   28.062  1.00 8.27  ? 27  ARG A C   1 
ATOM   214  O  O   . ARG A 1 27  ? -1.596  1.870   27.261  1.00 8.48  ? 27  ARG A O   1 
ATOM   215  C  CB  . ARG A 1 27  ? -1.700  2.938   29.906  1.00 12.29 ? 27  ARG A CB  1 
ATOM   216  C  CG  . ARG A 1 27  ? -1.368  4.205   29.200  1.00 13.96 ? 27  ARG A CG  1 
ATOM   217  C  CD  . ARG A 1 27  ? -2.403  5.392   29.484  1.00 14.53 ? 27  ARG A CD  1 
ATOM   218  N  NE  . ARG A 1 27  ? -3.568  5.318   28.576  1.00 16.07 ? 27  ARG A NE  1 
ATOM   219  C  CZ  . ARG A 1 27  ? -4.519  6.228   28.501  1.00 9.97  ? 27  ARG A CZ  1 
ATOM   220  N  NH1 . ARG A 1 27  ? -4.466  7.403   29.196  1.00 14.63 ? 27  ARG A NH1 1 
ATOM   221  N  NH2 . ARG A 1 27  ? -5.457  6.064   27.666  1.00 13.86 ? 27  ARG A NH2 1 
ATOM   222  N  N   . GLN A 1 28  ? -0.135  0.191   27.760  1.00 7.74  ? 28  GLN A N   1 
ATOM   223  C  CA  . GLN A 1 28  ? -0.093  -0.337  26.396  1.00 6.70  ? 28  GLN A CA  1 
ATOM   224  C  C   . GLN A 1 28  ? -1.286  -1.343  26.138  1.00 6.01  ? 28  GLN A C   1 
ATOM   225  O  O   . GLN A 1 28  ? -1.780  -2.014  27.092  1.00 7.24  ? 28  GLN A O   1 
ATOM   226  C  CB  . GLN A 1 28  ? 1.240   -1.040  26.147  1.00 7.29  ? 28  GLN A CB  1 
ATOM   227  C  CG  . GLN A 1 28  ? 2.392   0.013   26.059  1.00 7.53  ? 28  GLN A CG  1 
ATOM   228  C  CD  . GLN A 1 28  ? 2.221   0.807   24.752  1.00 8.72  ? 28  GLN A CD  1 
ATOM   229  O  OE1 . GLN A 1 28  ? 2.411   0.262   23.656  1.00 7.92  ? 28  GLN A OE1 1 
ATOM   230  N  NE2 . GLN A 1 28  ? 1.894   2.130   24.891  1.00 8.55  ? 28  GLN A NE2 1 
ATOM   231  N  N   . SER A 1 29  ? -1.684  -1.408  24.846  1.00 5.85  ? 29  SER A N   1 
ATOM   232  C  CA  . SER A 1 29  ? -2.732  -2.322  24.450  1.00 5.75  ? 29  SER A CA  1 
ATOM   233  C  C   . SER A 1 29  ? -2.195  -3.183  23.283  1.00 6.49  ? 29  SER A C   1 
ATOM   234  O  O   . SER A 1 29  ? -1.239  -2.793  22.575  1.00 7.12  ? 29  SER A O   1 
ATOM   235  C  CB  . SER A 1 29  ? -3.901  -1.476  23.866  1.00 6.67  ? 29  SER A CB  1 
ATOM   236  O  OG  . SER A 1 29  ? -4.496  -0.693  24.958  1.00 6.96  ? 29  SER A OG  1 
ATOM   237  N  N   . PRO A 1 30  ? -2.852  -4.313  23.033  1.00 6.49  ? 30  PRO A N   1 
ATOM   238  C  CA  . PRO A 1 30  ? -4.036  -4.855  23.722  1.00 6.39  ? 30  PRO A CA  1 
ATOM   239  C  C   . PRO A 1 30  ? -3.619  -5.510  25.054  1.00 5.88  ? 30  PRO A C   1 
ATOM   240  O  O   . PRO A 1 30  ? -2.404  -5.555  25.381  1.00 7.18  ? 30  PRO A O   1 
ATOM   241  C  CB  . PRO A 1 30  ? -4.491  -5.943  22.743  1.00 6.88  ? 30  PRO A CB  1 
ATOM   242  C  CG  . PRO A 1 30  ? -3.208  -6.525  22.200  1.00 7.63  ? 30  PRO A CG  1 
ATOM   243  C  CD  . PRO A 1 30  ? -2.381  -5.225  21.967  1.00 7.34  ? 30  PRO A CD  1 
ATOM   244  N  N   . VAL A 1 31  ? -4.605  -6.076  25.754  1.00 6.33  ? 31  VAL A N   1 
ATOM   245  C  CA  . VAL A 1 31  ? -4.401  -6.820  26.975  1.00 7.49  ? 31  VAL A CA  1 
ATOM   246  C  C   . VAL A 1 31  ? -5.315  -8.049  26.961  1.00 7.04  ? 31  VAL A C   1 
ATOM   247  O  O   . VAL A 1 31  ? -6.271  -8.124  26.191  1.00 7.49  ? 31  VAL A O   1 
ATOM   248  C  CB  . VAL A 1 31  ? -4.720  -5.988  28.259  1.00 7.77  ? 31  VAL A CB  1 
ATOM   249  C  CG1 . VAL A 1 31  ? -3.737  -4.805  28.366  1.00 7.76  ? 31  VAL A CG1 1 
ATOM   250  C  CG2 . VAL A 1 31  ? -6.228  -5.583  28.285  1.00 7.71  ? 31  VAL A CG2 1 
ATOM   251  N  N   . ASP A 1 32  ? -4.944  -9.038  27.795  1.00 6.82  ? 32  ASP A N   1 
ATOM   252  C  CA  . ASP A 1 32  ? -5.848  -10.141 28.064  1.00 7.11  ? 32  ASP A CA  1 
ATOM   253  C  C   . ASP A 1 32  ? -6.919  -9.630  29.053  1.00 8.15  ? 32  ASP A C   1 
ATOM   254  O  O   . ASP A 1 32  ? -6.619  -9.006  30.100  1.00 9.56  ? 32  ASP A O   1 
ATOM   255  C  CB  . ASP A 1 32  ? -5.099  -11.331 28.699  1.00 9.12  ? 32  ASP A CB  1 
ATOM   256  C  CG  . ASP A 1 32  ? -6.052  -12.537 29.007  1.00 10.36 ? 32  ASP A CG  1 
ATOM   257  O  OD1 . ASP A 1 32  ? -6.773  -12.946 28.070  1.00 9.25  ? 32  ASP A OD1 1 
ATOM   258  O  OD2 . ASP A 1 32  ? -6.128  -12.973 30.224  1.00 13.14 ? 32  ASP A OD2 1 
ATOM   259  N  N   . ILE A 1 33  ? -8.187  -9.943  28.767  1.00 6.64  ? 33  ILE A N   1 
ATOM   260  C  CA  . ILE A 1 33  ? -9.286  -9.585  29.625  1.00 8.61  ? 33  ILE A CA  1 
ATOM   261  C  C   . ILE A 1 33  ? -9.606  -10.830 30.472  1.00 8.53  ? 33  ILE A C   1 
ATOM   262  O  O   . ILE A 1 33  ? -10.178 -11.858 29.982  1.00 10.30 ? 33  ILE A O   1 
ATOM   263  C  CB  . ILE A 1 33  ? -10.518 -9.121  28.817  1.00 9.58  ? 33  ILE A CB  1 
ATOM   264  C  CG1 . ILE A 1 33  ? -10.143 -7.862  28.012  1.00 8.41  ? 33  ILE A CG1 1 
ATOM   265  C  CG2 . ILE A 1 33  ? -11.724 -8.935  29.796  1.00 11.24 ? 33  ILE A CG2 1 
ATOM   266  C  CD1 . ILE A 1 33  ? -11.198 -7.609  26.866  1.00 9.20  ? 33  ILE A CD1 1 
ATOM   267  N  N   . ASP A 1 34  ? -9.182  -10.739 31.728  1.00 9.69  ? 34  ASP A N   1 
ATOM   268  C  CA  . ASP A 1 34  ? -9.476  -11.821 32.695  1.00 10.72 ? 34  ASP A CA  1 
ATOM   269  C  C   . ASP A 1 34  ? -10.904 -11.570 33.248  1.00 11.47 ? 34  ASP A C   1 
ATOM   270  O  O   . ASP A 1 34  ? -11.139 -10.611 34.035  1.00 13.78 ? 34  ASP A O   1 
ATOM   271  C  CB  . ASP A 1 34  ? -8.426  -11.850 33.802  1.00 12.50 ? 34  ASP A CB  1 
ATOM   272  C  CG  . ASP A 1 34  ? -8.595  -13.063 34.642  1.00 17.42 ? 34  ASP A CG  1 
ATOM   273  O  OD1 . ASP A 1 34  ? -9.442  -12.999 35.521  1.00 21.17 ? 34  ASP A OD1 1 
ATOM   274  O  OD2 . ASP A 1 34  ? -8.032  -14.148 34.285  1.00 26.81 ? 34  ASP A OD2 1 
ATOM   275  N  N   . THR A 1 35  ? -11.871 -12.347 32.784  1.00 14.11 ? 35  THR A N   1 
ATOM   276  C  CA  . THR A 1 35  ? -13.292 -11.990 32.994  1.00 13.54 ? 35  THR A CA  1 
ATOM   277  C  C   . THR A 1 35  ? -13.696 -12.129 34.457  1.00 14.53 ? 35  THR A C   1 
ATOM   278  O  O   . THR A 1 35  ? -14.666 -11.477 34.912  1.00 16.31 ? 35  THR A O   1 
ATOM   279  C  CB  . THR A 1 35  ? -14.198 -12.906 32.183  1.00 14.96 ? 35  THR A CB  1 
ATOM   280  O  OG1 . THR A 1 35  ? -14.075 -14.246 32.671  1.00 15.48 ? 35  THR A OG1 1 
ATOM   281  C  CG2 . THR A 1 35  ? -13.916 -12.851 30.692  1.00 14.68 ? 35  THR A CG2 1 
ATOM   282  N  N   . HIS A 1 36  ? -12.948 -12.964 35.193  1.00 14.66 ? 36  HIS A N   1 
ATOM   283  C  CA  . HIS A 1 36  ? -13.258 -13.161 36.627  1.00 15.82 ? 36  HIS A CA  1 
ATOM   284  C  C   . HIS A 1 36  ? -12.718 -12.013 37.465  1.00 17.75 ? 36  HIS A C   1 
ATOM   285  O  O   . HIS A 1 36  ? -13.365 -11.710 38.494  1.00 20.39 ? 36  HIS A O   1 
ATOM   286  C  CB  . HIS A 1 36  ? -12.796 -14.565 37.058  1.00 17.34 ? 36  HIS A CB  1 
ATOM   287  C  CG  . HIS A 1 36  ? -13.720 -15.631 36.555  1.00 20.27 ? 36  HIS A CG  1 
ATOM   288  N  ND1 . HIS A 1 36  ? -13.372 -16.503 35.538  1.00 21.98 ? 36  HIS A ND1 1 
ATOM   289  C  CD2 . HIS A 1 36  ? -15.042 -15.844 36.822  1.00 21.23 ? 36  HIS A CD2 1 
ATOM   290  C  CE1 . HIS A 1 36  ? -14.423 -17.255 35.249  1.00 24.51 ? 36  HIS A CE1 1 
ATOM   291  N  NE2 . HIS A 1 36  ? -15.447 -16.873 35.996  1.00 26.76 ? 36  HIS A NE2 1 
ATOM   292  N  N   . THR A 1 37  ? -11.600 -11.366 37.048  1.00 16.82 ? 37  THR A N   1 
ATOM   293  C  CA  . THR A 1 37  ? -10.973 -10.213 37.700  1.00 17.77 ? 37  THR A CA  1 
ATOM   294  C  C   . THR A 1 37  ? -11.565 -8.786  37.302  1.00 15.24 ? 37  THR A C   1 
ATOM   295  O  O   . THR A 1 37  ? -11.392 -7.795  38.035  1.00 18.21 ? 37  THR A O   1 
ATOM   296  C  CB  . THR A 1 37  ? -9.408  -10.276 37.559  1.00 20.45 ? 37  THR A CB  1 
ATOM   297  O  OG1 . THR A 1 37  ? -8.976  -11.365 38.382  1.00 24.59 ? 37  THR A OG1 1 
ATOM   298  C  CG2 . THR A 1 37  ? -8.718  -8.958  38.087  1.00 24.51 ? 37  THR A CG2 1 
ATOM   299  N  N   . ALA A 1 38  ? -12.302 -8.721  36.196  1.00 15.05 ? 38  ALA A N   1 
ATOM   300  C  CA  . ALA A 1 38  ? -12.849 -7.464  35.691  1.00 13.48 ? 38  ALA A CA  1 
ATOM   301  C  C   . ALA A 1 38  ? -13.891 -7.085  36.770  1.00 16.19 ? 38  ALA A C   1 
ATOM   302  O  O   . ALA A 1 38  ? -14.572 -7.951  37.262  1.00 19.34 ? 38  ALA A O   1 
ATOM   303  C  CB  . ALA A 1 38  ? -13.471 -7.669  34.270  1.00 15.30 ? 38  ALA A CB  1 
ATOM   304  N  N   . LYS A 1 39  ? -13.993 -5.815  37.108  1.00 16.06 ? 39  LYS A N   1 
ATOM   305  C  CA  . LYS A 1 39  ? -14.870 -5.376  38.198  1.00 17.27 ? 39  LYS A CA  1 
ATOM   306  C  C   . LYS A 1 39  ? -16.196 -4.863  37.545  1.00 16.32 ? 39  LYS A C   1 
ATOM   307  O  O   . LYS A 1 39  ? -16.166 -3.916  36.740  1.00 14.60 ? 39  LYS A O   1 
ATOM   308  C  CB  . LYS A 1 39  ? -14.140 -4.222  38.891  1.00 18.50 ? 39  LYS A CB  1 
ATOM   309  C  CG  . LYS A 1 39  ? -14.905 -3.391  39.898  1.00 20.38 ? 39  LYS A CG  1 
ATOM   310  C  CD  . LYS A 1 39  ? -15.192 -4.183  41.158  1.00 20.56 ? 39  LYS A CD  1 
ATOM   311  C  CE  . LYS A 1 39  ? -15.896 -3.322  42.150  1.00 24.20 ? 39  LYS A CE  1 
ATOM   312  N  NZ  . LYS A 1 39  ? -16.332 -4.254  43.193  1.00 24.62 ? 39  LYS A NZ  1 
ATOM   313  N  N   . TYR A 1 40  ? -17.350 -5.449  37.911  1.00 16.44 ? 40  TYR A N   1 
ATOM   314  C  CA  . TYR A 1 40  ? -18.574 -4.831  37.448  1.00 16.51 ? 40  TYR A CA  1 
ATOM   315  C  C   . TYR A 1 40  ? -18.728 -3.430  38.093  1.00 16.61 ? 40  TYR A C   1 
ATOM   316  O  O   . TYR A 1 40  ? -18.540 -3.234  39.362  1.00 16.92 ? 40  TYR A O   1 
ATOM   317  C  CB  . TYR A 1 40  ? -19.784 -5.750  37.775  1.00 18.43 ? 40  TYR A CB  1 
ATOM   318  C  CG  . TYR A 1 40  ? -21.108 -5.076  37.639  1.00 20.41 ? 40  TYR A CG  1 
ATOM   319  C  CD1 . TYR A 1 40  ? -21.561 -4.589  36.400  1.00 19.66 ? 40  TYR A CD1 1 
ATOM   320  C  CD2 . TYR A 1 40  ? -21.965 -4.944  38.760  1.00 26.14 ? 40  TYR A CD2 1 
ATOM   321  C  CE1 . TYR A 1 40  ? -22.818 -4.043  36.250  1.00 23.57 ? 40  TYR A CE1 1 
ATOM   322  C  CE2 . TYR A 1 40  ? -23.254 -4.298  38.630  1.00 25.23 ? 40  TYR A CE2 1 
ATOM   323  C  CZ  . TYR A 1 40  ? -23.648 -3.869  37.376  1.00 24.45 ? 40  TYR A CZ  1 
ATOM   324  O  OH  . TYR A 1 40  ? -24.843 -3.271  37.196  1.00 27.49 ? 40  TYR A OH  1 
ATOM   325  N  N   . ASP A 1 41  ? -19.084 -2.448  37.235  1.00 16.01 ? 41  ASP A N   1 
ATOM   326  C  CA  . ASP A 1 41  ? -19.225 -1.044  37.723  1.00 17.94 ? 41  ASP A CA  1 
ATOM   327  C  C   . ASP A 1 41  ? -20.644 -0.579  37.423  1.00 21.13 ? 41  ASP A C   1 
ATOM   328  O  O   . ASP A 1 41  ? -20.964 -0.319  36.263  1.00 20.45 ? 41  ASP A O   1 
ATOM   329  C  CB  . ASP A 1 41  ? -18.197 -0.144  37.045  1.00 19.58 ? 41  ASP A CB  1 
ATOM   330  C  CG  . ASP A 1 41  ? -18.291 1.303   37.536  1.00 22.95 ? 41  ASP A CG  1 
ATOM   331  O  OD1 . ASP A 1 41  ? -19.286 1.607   38.236  1.00 23.07 ? 41  ASP A OD1 1 
ATOM   332  O  OD2 . ASP A 1 41  ? -17.380 2.124   37.204  1.00 29.11 ? 41  ASP A OD2 1 
ATOM   333  N  N   . PRO A 1 42  ? -21.520 -0.581  38.450  1.00 23.60 ? 42  PRO A N   1 
ATOM   334  C  CA  . PRO A 1 42  ? -22.939 -0.259  38.226  1.00 24.69 ? 42  PRO A CA  1 
ATOM   335  C  C   . PRO A 1 42  ? -23.086 1.177   37.792  1.00 25.46 ? 42  PRO A C   1 
ATOM   336  O  O   . PRO A 1 42  ? -24.155 1.542   37.242  1.00 26.17 ? 42  PRO A O   1 
ATOM   337  C  CB  . PRO A 1 42  ? -23.564 -0.439  39.638  1.00 26.06 ? 42  PRO A CB  1 
ATOM   338  C  CG  . PRO A 1 42  ? -22.400 -0.184  40.561  1.00 24.64 ? 42  PRO A CG  1 
ATOM   339  C  CD  . PRO A 1 42  ? -21.278 -0.933  39.870  1.00 24.30 ? 42  PRO A CD  1 
ATOM   340  N  N   . SER A 1 43  ? -22.055 1.990   37.992  1.00 24.83 ? 43  SER A N   1 
ATOM   341  C  CA  . SER A 1 43  ? -22.156 3.370   37.552  1.00 25.68 ? 43  SER A CA  1 
ATOM   342  C  C   . SER A 1 43  ? -21.796 3.627   36.043  1.00 23.72 ? 43  SER A C   1 
ATOM   343  O  O   . SER A 1 43  ? -21.922 4.831   35.523  1.00 25.83 ? 43  SER A O   1 
ATOM   344  C  CB  . SER A 1 43  ? -21.362 4.269   38.470  1.00 28.11 ? 43  SER A CB  1 
ATOM   345  O  OG  . SER A 1 43  ? -19.997 4.273   38.103  1.00 26.94 ? 43  SER A OG  1 
ATOM   346  N  N   . LEU A 1 44  ? -21.321 2.564   35.342  1.00 22.04 ? 44  LEU A N   1 
ATOM   347  C  CA  . LEU A 1 44  ? -21.066 2.673   33.896  1.00 19.32 ? 44  LEU A CA  1 
ATOM   348  C  C   . LEU A 1 44  ? -22.391 2.795   33.154  1.00 21.13 ? 44  LEU A C   1 
ATOM   349  O  O   . LEU A 1 44  ? -23.338 2.071   33.436  1.00 22.35 ? 44  LEU A O   1 
ATOM   350  C  CB  . LEU A 1 44  ? -20.332 1.440   33.366  1.00 19.35 ? 44  LEU A CB  1 
ATOM   351  C  CG  . LEU A 1 44  ? -18.853 1.427   33.648  1.00 16.68 ? 44  LEU A CG  1 
ATOM   352  C  CD1 . LEU A 1 44  ? -18.300 0.018   33.253  1.00 16.47 ? 44  LEU A CD1 1 
ATOM   353  C  CD2 . LEU A 1 44  ? -18.120 2.580   32.899  1.00 17.99 ? 44  LEU A CD2 1 
ATOM   354  N  N   . LYS A 1 45  ? -22.450 3.688   32.163  1.00 19.58 ? 45  LYS A N   1 
ATOM   355  C  CA  . LYS A 1 45  ? -23.740 3.886   31.410  1.00 19.63 ? 45  LYS A CA  1 
ATOM   356  C  C   . LYS A 1 45  ? -23.784 2.980   30.194  1.00 17.96 ? 45  LYS A C   1 
ATOM   357  O  O   . LYS A 1 45  ? -22.759 2.503   29.750  1.00 18.24 ? 45  LYS A O   1 
ATOM   358  C  CB  . LYS A 1 45  ? -23.850 5.309   30.964  1.00 20.21 ? 45  LYS A CB  1 
ATOM   359  C  CG  . LYS A 1 45  ? -23.614 6.324   32.085  1.00 23.99 ? 45  LYS A CG  1 
ATOM   360  C  CD  . LYS A 1 45  ? -23.621 7.778   31.592  1.00 30.95 ? 45  LYS A CD  1 
ATOM   361  C  CE  . LYS A 1 45  ? -25.035 8.296   31.162  1.00 39.08 ? 45  LYS A CE  1 
ATOM   362  N  NZ  . LYS A 1 45  ? -25.257 8.339   29.622  1.00 41.96 ? 45  LYS A NZ  1 
ATOM   363  N  N   . PRO A 1 46  ? -24.975 2.776   29.610  1.00 16.08 ? 46  PRO A N   1 
ATOM   364  C  CA  . PRO A 1 46  ? -25.089 2.121   28.295  1.00 16.56 ? 46  PRO A CA  1 
ATOM   365  C  C   . PRO A 1 46  ? -24.245 2.879   27.282  1.00 15.73 ? 46  PRO A C   1 
ATOM   366  O  O   . PRO A 1 46  ? -24.190 4.102   27.342  1.00 15.05 ? 46  PRO A O   1 
ATOM   367  C  CB  . PRO A 1 46  ? -26.590 2.261   27.972  1.00 15.43 ? 46  PRO A CB  1 
ATOM   368  C  CG  . PRO A 1 46  ? -27.238 2.408   29.311  1.00 17.63 ? 46  PRO A CG  1 
ATOM   369  C  CD  . PRO A 1 46  ? -26.282 3.157   30.189  1.00 18.27 ? 46  PRO A CD  1 
ATOM   370  N  N   . LEU A 1 47  ? -23.625 2.172   26.328  1.00 15.69 ? 47  LEU A N   1 
ATOM   371  C  CA  . LEU A 1 47  ? -22.881 2.844   25.300  1.00 14.32 ? 47  LEU A CA  1 
ATOM   372  C  C   . LEU A 1 47  ? -23.904 3.422   24.297  1.00 14.26 ? 47  LEU A C   1 
ATOM   373  O  O   . LEU A 1 47  ? -24.949 2.793   24.023  1.00 17.67 ? 47  LEU A O   1 
ATOM   374  C  CB  . LEU A 1 47  ? -22.028 1.822   24.504  1.00 15.91 ? 47  LEU A CB  1 
ATOM   375  C  CG  . LEU A 1 47  ? -20.974 2.267   23.517  1.00 19.98 ? 47  LEU A CG  1 
ATOM   376  C  CD1 . LEU A 1 47  ? -19.882 3.017   24.240  1.00 19.89 ? 47  LEU A CD1 1 
ATOM   377  C  CD2 . LEU A 1 47  ? -20.360 0.983   22.882  1.00 19.66 ? 47  LEU A CD2 1 
ATOM   378  N  N   . SER A 1 48  ? -23.639 4.640   23.825  1.00 12.90 ? 48  SER A N   1 
ATOM   379  C  CA  . SER A 1 48  ? -24.464 5.239   22.806  1.00 14.06 ? 48  SER A CA  1 
ATOM   380  C  C   . SER A 1 48  ? -23.717 5.287   21.483  1.00 13.90 ? 48  SER A C   1 
ATOM   381  O  O   . SER A 1 48  ? -22.735 6.042   21.286  1.00 13.37 ? 48  SER A O   1 
ATOM   382  C  CB  . SER A 1 48  ? -24.860 6.642   23.249  1.00 15.09 ? 48  SER A CB  1 
ATOM   383  O  OG  . SER A 1 48  ? -25.472 7.342   22.184  1.00 18.67 ? 48  SER A OG  1 
ATOM   384  N  N   . VAL A 1 49  ? -24.207 4.499   20.552  1.00 16.13 ? 49  VAL A N   1 
ATOM   385  C  CA  . VAL A 1 49  ? -23.627 4.414   19.218  1.00 16.70 ? 49  VAL A CA  1 
ATOM   386  C  C   . VAL A 1 49  ? -24.606 5.045   18.236  1.00 18.60 ? 49  VAL A C   1 
ATOM   387  O  O   . VAL A 1 49  ? -25.670 4.502   17.995  1.00 20.03 ? 49  VAL A O   1 
ATOM   388  C  CB  . VAL A 1 49  ? -23.372 2.939   18.802  1.00 19.18 ? 49  VAL A CB  1 
ATOM   389  C  CG1 . VAL A 1 49  ? -22.759 2.870   17.376  1.00 22.38 ? 49  VAL A CG1 1 
ATOM   390  C  CG2 . VAL A 1 49  ? -22.554 2.216   19.868  1.00 17.07 ? 49  VAL A CG2 1 
ATOM   391  N  N   . SER A 1 50  ? -24.259 6.175   17.656  1.00 16.33 ? 50  SER A N   1 
ATOM   392  C  CA  . SER A 1 50  ? -25.193 6.901   16.794  1.00 18.87 ? 50  SER A CA  1 
ATOM   393  C  C   . SER A 1 50  ? -24.603 6.989   15.439  1.00 18.78 ? 50  SER A C   1 
ATOM   394  O  O   . SER A 1 50  ? -23.859 7.918   15.146  1.00 18.41 ? 50  SER A O   1 
ATOM   395  C  CB  . SER A 1 50  ? -25.532 8.318   17.341  1.00 19.90 ? 50  SER A CB  1 
ATOM   396  O  OG  . SER A 1 50  ? -26.079 8.222   18.608  1.00 26.04 ? 50  SER A OG  1 
ATOM   397  N  N   . TYR A 1 51  ? -24.859 5.960   14.616  1.00 18.26 ? 51  TYR A N   1 
ATOM   398  C  CA  . TYR A 1 51  ? -24.259 5.834   13.321  1.00 17.33 ? 51  TYR A CA  1 
ATOM   399  C  C   . TYR A 1 51  ? -25.245 6.080   12.136  1.00 17.61 ? 51  TYR A C   1 
ATOM   400  O  O   . TYR A 1 51  ? -24.804 5.925   10.986  1.00 18.07 ? 51  TYR A O   1 
ATOM   401  C  CB  . TYR A 1 51  ? -23.626 4.434   13.164  1.00 16.22 ? 51  TYR A CB  1 
ATOM   402  C  CG  . TYR A 1 51  ? -22.304 4.162   13.915  1.00 13.11 ? 51  TYR A CG  1 
ATOM   403  C  CD1 . TYR A 1 51  ? -21.578 5.176   14.574  1.00 12.81 ? 51  TYR A CD1 1 
ATOM   404  C  CD2 . TYR A 1 51  ? -21.800 2.841   13.977  1.00 11.98 ? 51  TYR A CD2 1 
ATOM   405  C  CE1 . TYR A 1 51  ? -20.362 4.866   15.246  1.00 10.94 ? 51  TYR A CE1 1 
ATOM   406  C  CE2 . TYR A 1 51  ? -20.617 2.513   14.583  1.00 11.11 ? 51  TYR A CE2 1 
ATOM   407  C  CZ  . TYR A 1 51  ? -19.905 3.526   15.265  1.00 10.72 ? 51  TYR A CZ  1 
ATOM   408  O  OH  . TYR A 1 51  ? -18.735 3.202   15.873  1.00 12.10 ? 51  TYR A OH  1 
ATOM   409  N  N   . ASP A 1 52  ? -26.513 6.473   12.426  1.00 19.81 ? 52  ASP A N   1 
ATOM   410  C  CA  . ASP A 1 52  ? -27.514 6.771   11.353  1.00 21.43 ? 52  ASP A CA  1 
ATOM   411  C  C   . ASP A 1 52  ? -27.032 7.695   10.207  1.00 22.80 ? 52  ASP A C   1 
ATOM   412  O  O   . ASP A 1 52  ? -27.357 7.461   9.059   1.00 24.10 ? 52  ASP A O   1 
ATOM   413  C  CB  . ASP A 1 52  ? -28.833 7.291   11.944  1.00 23.28 ? 52  ASP A CB  1 
ATOM   414  C  CG  . ASP A 1 52  ? -28.631 8.239   13.135  1.00 29.47 ? 52  ASP A CG  1 
ATOM   415  O  OD1 . ASP A 1 52  ? -28.046 7.845   14.231  1.00 36.25 ? 52  ASP A OD1 1 
ATOM   416  O  OD2 . ASP A 1 52  ? -29.076 9.400   12.971  1.00 38.84 ? 52  ASP A OD2 1 
ATOM   417  N  N   . GLN A 1 53  ? -26.189 8.666   10.474  1.00 22.55 ? 53  GLN A N   1 
ATOM   418  C  CA  . GLN A 1 53  ? -25.791 9.615   9.404   1.00 21.30 ? 53  GLN A CA  1 
ATOM   419  C  C   . GLN A 1 53  ? -24.335 9.457   8.953   1.00 18.97 ? 53  GLN A C   1 
ATOM   420  O  O   . GLN A 1 53  ? -23.789 10.345  8.346   1.00 19.05 ? 53  GLN A O   1 
ATOM   421  C  CB  . GLN A 1 53  ? -25.935 11.043  9.969   1.00 24.20 ? 53  GLN A CB  1 
ATOM   422  C  CG  . GLN A 1 53  ? -27.388 11.446  10.212  1.00 29.10 ? 53  GLN A CG  1 
ATOM   423  C  CD  . GLN A 1 53  ? -28.171 11.398  8.903   1.00 35.21 ? 53  GLN A CD  1 
ATOM   424  O  OE1 . GLN A 1 53  ? -27.728 11.959  7.832   1.00 38.07 ? 53  GLN A OE1 1 
ATOM   425  N  NE2 . GLN A 1 53  ? -29.314 10.683  8.933   1.00 33.75 ? 53  GLN A NE2 1 
ATOM   426  N  N   . ALA A 1 54  ? -23.704 8.322   9.277   1.00 16.05 ? 54  ALA A N   1 
ATOM   427  C  CA  . ALA A 1 54  ? -22.364 8.024   8.806   1.00 13.91 ? 54  ALA A CA  1 
ATOM   428  C  C   . ALA A 1 54  ? -22.185 8.231   7.307   1.00 15.32 ? 54  ALA A C   1 
ATOM   429  O  O   . ALA A 1 54  ? -23.081 7.845   6.495   1.00 18.96 ? 54  ALA A O   1 
ATOM   430  C  CB  . ALA A 1 54  ? -21.920 6.600   9.220   1.00 16.14 ? 54  ALA A CB  1 
ATOM   431  N  N   . THR A 1 55  ? -21.044 8.797   6.959   1.00 14.38 ? 55  THR A N   1 
ATOM   432  C  CA  . THR A 1 55  ? -20.650 9.003   5.571   1.00 14.46 ? 55  THR A CA  1 
ATOM   433  C  C   . THR A 1 55  ? -19.308 8.365   5.291   1.00 14.34 ? 55  THR A C   1 
ATOM   434  O  O   . THR A 1 55  ? -18.292 8.960   5.595   1.00 14.12 ? 55  THR A O   1 
ATOM   435  C  CB  . THR A 1 55  ? -20.544 10.567  5.190   1.00 14.84 ? 55  THR A CB  1 
ATOM   436  O  OG1 . THR A 1 55  ? -21.818 11.116  5.293   1.00 19.61 ? 55  THR A OG1 1 
ATOM   437  C  CG2 . THR A 1 55  ? -20.047 10.650  3.701   1.00 17.22 ? 55  THR A CG2 1 
ATOM   438  N  N   . SER A 1 56  ? -19.300 7.113   4.790   1.00 13.21 ? 56  SER A N   1 
ATOM   439  C  CA  . SER A 1 56  ? -18.055 6.490   4.457   1.00 14.72 ? 56  SER A CA  1 
ATOM   440  C  C   . SER A 1 56  ? -17.601 7.192   3.163   1.00 15.78 ? 56  SER A C   1 
ATOM   441  O  O   . SER A 1 56  ? -18.465 7.635   2.316   1.00 17.48 ? 56  SER A O   1 
ATOM   442  C  CB  . SER A 1 56  ? -18.176 4.940   4.282   1.00 16.00 ? 56  SER A CB  1 
ATOM   443  O  OG  . SER A 1 56  ? -19.053 4.603   3.158   1.00 17.16 ? 56  SER A OG  1 
ATOM   444  N  N   . LEU A 1 57  ? -16.290 7.279   2.957   1.00 15.77 ? 57  LEU A N   1 
ATOM   445  C  CA  . LEU A 1 57  ? -15.756 7.919   1.729   1.00 18.47 ? 57  LEU A CA  1 
ATOM   446  C  C   . LEU A 1 57  ? -14.890 6.999   0.858   1.00 16.49 ? 57  LEU A C   1 
ATOM   447  O  O   . LEU A 1 57  ? -14.924 7.029   -0.370  1.00 17.23 ? 57  LEU A O   1 
ATOM   448  C  CB  . LEU A 1 57  ? -14.892 9.111   2.145   1.00 19.83 ? 57  LEU A CB  1 
ATOM   449  C  CG  . LEU A 1 57  ? -15.753 10.237  2.789   1.00 21.38 ? 57  LEU A CG  1 
ATOM   450  C  CD1 . LEU A 1 57  ? -14.867 11.382  3.322   1.00 24.36 ? 57  LEU A CD1 1 
ATOM   451  C  CD2 . LEU A 1 57  ? -16.887 10.794  1.861   1.00 21.94 ? 57  LEU A CD2 1 
ATOM   452  N  N   . ARG A 1 58  ? -14.078 6.185   1.523   1.00 16.25 ? 58  ARG A N   1 
ATOM   453  C  CA  . ARG A 1 58  ? -13.017 5.510   0.846   1.00 16.24 ? 58  ARG A CA  1 
ATOM   454  C  C   . ARG A 1 58  ? -12.545 4.329   1.649   1.00 14.74 ? 58  ARG A C   1 
ATOM   455  O  O   . ARG A 1 58  ? -12.668 4.320   2.858   1.00 14.57 ? 58  ARG A O   1 
ATOM   456  C  CB  . ARG A 1 58  ? -11.850 6.464   0.668   1.00 17.06 ? 58  ARG A CB  1 
ATOM   457  C  CG  . ARG A 1 58  ? -10.855 6.134   -0.353  1.00 18.31 ? 58  ARG A CG  1 
ATOM   458  C  CD  . ARG A 1 58  ? -9.960  7.395   -0.493  1.00 23.35 ? 58  ARG A CD  1 
ATOM   459  N  NE  . ARG A 1 58  ? -9.169  7.396   0.743   1.00 19.86 ? 58  ARG A NE  1 
ATOM   460  C  CZ  . ARG A 1 58  ? -7.841  7.446   0.753   1.00 19.85 ? 58  ARG A CZ  1 
ATOM   461  N  NH1 . ARG A 1 58  ? -7.236  7.629   -0.372  1.00 20.21 ? 58  ARG A NH1 1 
ATOM   462  N  NH2 . ARG A 1 58  ? -7.159  7.434   1.904   1.00 18.21 ? 58  ARG A NH2 1 
ATOM   463  N  N   . ILE A 1 59  ? -11.922 3.376   0.929   1.00 14.66 ? 59  ILE A N   1 
ATOM   464  C  CA  . ILE A 1 59  ? -11.234 2.253   1.584   1.00 13.35 ? 59  ILE A CA  1 
ATOM   465  C  C   . ILE A 1 59  ? -9.780  2.222   1.076   1.00 12.89 ? 59  ILE A C   1 
ATOM   466  O  O   . ILE A 1 59  ? -9.502  2.412   -0.146  1.00 14.28 ? 59  ILE A O   1 
ATOM   467  C  CB  . ILE A 1 59  ? -11.972 0.894   1.318   1.00 13.87 ? 59  ILE A CB  1 
ATOM   468  C  CG1 . ILE A 1 59  ? -11.371 -0.271  2.161   1.00 12.51 ? 59  ILE A CG1 1 
ATOM   469  C  CG2 . ILE A 1 59  ? -11.988 0.483   -0.257  1.00 13.40 ? 59  ILE A CG2 1 
ATOM   470  C  CD1 . ILE A 1 59  ? -12.270 -1.522  2.098   1.00 14.24 ? 59  ILE A CD1 1 
ATOM   471  N  N   . LEU A 1 60  ? -8.841  1.969   2.005   1.00 13.74 ? 60  LEU A N   1 
ATOM   472  C  CA  . LEU A 1 60  ? -7.444  2.109   1.731   1.00 14.39 ? 60  LEU A CA  1 
ATOM   473  C  C   . LEU A 1 60  ? -6.651  0.925   2.284   1.00 14.01 ? 60  LEU A C   1 
ATOM   474  O  O   . LEU A 1 60  ? -6.892  0.564   3.435   1.00 12.56 ? 60  LEU A O   1 
ATOM   475  C  CB  . LEU A 1 60  ? -6.930  3.472   2.390   1.00 15.73 ? 60  LEU A CB  1 
ATOM   476  C  CG  . LEU A 1 60  ? -5.429  3.628   2.380   1.00 16.89 ? 60  LEU A CG  1 
ATOM   477  C  CD1 . LEU A 1 60  ? -4.874  3.801   0.942   1.00 19.86 ? 60  LEU A CD1 1 
ATOM   478  C  CD2 . LEU A 1 60  ? -4.955  4.822   3.299   1.00 15.67 ? 60  LEU A CD2 1 
ATOM   479  N  N   . ASN A 1 61  ? -5.763  0.346   1.466   1.00 12.43 ? 61  ASN A N   1 
ATOM   480  C  CA  . ASN A 1 61  ? -4.742  -0.601  1.913   1.00 13.32 ? 61  ASN A CA  1 
ATOM   481  C  C   . ASN A 1 61  ? -3.488  0.186   2.310   1.00 15.23 ? 61  ASN A C   1 
ATOM   482  O  O   . ASN A 1 61  ? -2.836  0.769   1.443   1.00 17.69 ? 61  ASN A O   1 
ATOM   483  C  CB  . ASN A 1 61  ? -4.423  -1.685  0.824   1.00 13.84 ? 61  ASN A CB  1 
ATOM   484  C  CG  . ASN A 1 61  ? -3.355  -2.665  1.249   1.00 13.55 ? 61  ASN A CG  1 
ATOM   485  O  OD1 . ASN A 1 61  ? -2.523  -2.352  2.156   1.00 15.27 ? 61  ASN A OD1 1 
ATOM   486  N  ND2 . ASN A 1 61  ? -3.377  -3.905  0.669   1.00 15.89 ? 61  ASN A ND2 1 
ATOM   487  N  N   . ASN A 1 62  ? -3.178  0.260   3.617   1.00 13.51 ? 62  ASN A N   1 
ATOM   488  C  CA  . ASN A 1 62  ? -2.111  1.184   4.065   1.00 14.24 ? 62  ASN A CA  1 
ATOM   489  C  C   . ASN A 1 62  ? -0.833  0.370   4.313   1.00 15.52 ? 62  ASN A C   1 
ATOM   490  O  O   . ASN A 1 62  ? 0.170   0.877   4.911   1.00 19.49 ? 62  ASN A O   1 
ATOM   491  C  CB  . ASN A 1 62  ? -2.487  2.025   5.286   1.00 15.24 ? 62  ASN A CB  1 
ATOM   492  C  CG  . ASN A 1 62  ? -2.780  1.147   6.521   1.00 15.96 ? 62  ASN A CG  1 
ATOM   493  O  OD1 . ASN A 1 62  ? -2.480  -0.097  6.517   1.00 14.46 ? 62  ASN A OD1 1 
ATOM   494  N  ND2 . ASN A 1 62  ? -3.443  1.734   7.492   1.00 20.06 ? 62  ASN A ND2 1 
ATOM   495  N  N   . GLY A 1 63  ? -0.825  -0.896  3.844   1.00 15.39 ? 63  GLY A N   1 
ATOM   496  C  CA  . GLY A 1 63  ? 0.308   -1.749  4.073   1.00 13.48 ? 63  GLY A CA  1 
ATOM   497  C  C   . GLY A 1 63  ? 0.365   -2.494  5.421   1.00 14.16 ? 63  GLY A C   1 
ATOM   498  O  O   . GLY A 1 63  ? 1.235   -3.330  5.607   1.00 14.60 ? 63  GLY A O   1 
ATOM   499  N  N   A HIS A 1 64  ? -0.620  -2.243  6.293   0.50 12.75 ? 64  HIS A N   1 
ATOM   500  N  N   B HIS A 1 64  ? -0.495  -2.135  6.392   0.50 13.13 ? 64  HIS A N   1 
ATOM   501  C  CA  A HIS A 1 64  ? -0.648  -2.873  7.645   0.50 13.43 ? 64  HIS A CA  1 
ATOM   502  C  CA  B HIS A 1 64  ? -0.616  -2.969  7.634   0.50 13.69 ? 64  HIS A CA  1 
ATOM   503  C  C   A HIS A 1 64  ? -2.044  -3.421  7.966   0.50 11.33 ? 64  HIS A C   1 
ATOM   504  C  C   B HIS A 1 64  ? -2.003  -3.605  7.711   0.50 11.69 ? 64  HIS A C   1 
ATOM   505  O  O   A HIS A 1 64  ? -2.221  -4.292  8.855   0.50 11.13 ? 64  HIS A O   1 
ATOM   506  O  O   B HIS A 1 64  ? -2.110  -4.800  8.123   0.50 11.50 ? 64  HIS A O   1 
ATOM   507  C  CB  A HIS A 1 64  ? -0.272  -1.872  8.725   0.50 12.55 ? 64  HIS A CB  1 
ATOM   508  C  CB  B HIS A 1 64  ? -0.211  -2.321  9.001   0.50 13.13 ? 64  HIS A CB  1 
ATOM   509  C  CG  A HIS A 1 64  ? 1.064   -1.241  8.523   0.50 14.59 ? 64  HIS A CG  1 
ATOM   510  C  CG  B HIS A 1 64  ? -0.551  -0.871  9.157   0.50 13.72 ? 64  HIS A CG  1 
ATOM   511  N  ND1 A HIS A 1 64  ? 2.250   -1.929  8.698   0.50 16.31 ? 64  HIS A ND1 1 
ATOM   512  N  ND1 B HIS A 1 64  ? -1.615  -0.414  9.922   0.50 16.31 ? 64  HIS A ND1 1 
ATOM   513  C  CD2 A HIS A 1 64  ? 1.401   0.035   8.250   0.50 16.67 ? 64  HIS A CD2 1 
ATOM   514  C  CD2 B HIS A 1 64  ? 0.109   0.235   8.721   0.50 12.69 ? 64  HIS A CD2 1 
ATOM   515  C  CE1 A HIS A 1 64  ? 3.263   -1.111  8.489   0.50 17.98 ? 64  HIS A CE1 1 
ATOM   516  C  CE1 B HIS A 1 64  ? -1.614  0.906   9.919   0.50 16.10 ? 64  HIS A CE1 1 
ATOM   517  N  NE2 A HIS A 1 64  ? 2.772   0.085   8.212   0.50 15.80 ? 64  HIS A NE2 1 
ATOM   518  N  NE2 B HIS A 1 64  ? -0.583  1.326   9.204   0.50 17.28 ? 64  HIS A NE2 1 
ATOM   519  N  N   . ALA A 1 65  ? -3.042  -2.849  7.300   1.00 11.57 ? 65  ALA A N   1 
ATOM   520  C  CA  . ALA A 1 65  ? -4.427  -3.353  7.327   1.00 11.16 ? 65  ALA A CA  1 
ATOM   521  C  C   . ALA A 1 65  ? -5.168  -2.629  6.175   1.00 11.07 ? 65  ALA A C   1 
ATOM   522  O  O   . ALA A 1 65  ? -4.528  -1.967  5.328   1.00 12.62 ? 65  ALA A O   1 
ATOM   523  C  CB  . ALA A 1 65  ? -5.111  -3.039  8.716   1.00 10.88 ? 65  ALA A CB  1 
ATOM   524  N  N   . PHE A 1 66  ? -6.491  -2.714  6.164   1.00 10.83 ? 66  PHE A N   1 
ATOM   525  C  CA  . PHE A 1 66  ? -7.274  -1.782  5.295   1.00 11.59 ? 66  PHE A CA  1 
ATOM   526  C  C   . PHE A 1 66  ? -8.193  -0.915  6.180   1.00 11.38 ? 66  PHE A C   1 
ATOM   527  O  O   . PHE A 1 66  ? -8.807  -1.415  7.157   1.00 10.83 ? 66  PHE A O   1 
ATOM   528  C  CB  . PHE A 1 66  ? -8.067  -2.528  4.172   1.00 11.16 ? 66  PHE A CB  1 
ATOM   529  C  CG  . PHE A 1 66  ? -9.103  -3.456  4.708   1.00 10.12 ? 66  PHE A CG  1 
ATOM   530  C  CD1 . PHE A 1 66  ? -10.408 -2.983  5.029   1.00 10.83 ? 66  PHE A CD1 1 
ATOM   531  C  CD2 . PHE A 1 66  ? -8.811  -4.817  4.824   1.00 11.15 ? 66  PHE A CD2 1 
ATOM   532  C  CE1 . PHE A 1 66  ? -11.375 -3.818  5.531   1.00 12.36 ? 66  PHE A CE1 1 
ATOM   533  C  CE2 . PHE A 1 66  ? -9.776  -5.682  5.405   1.00 11.86 ? 66  PHE A CE2 1 
ATOM   534  C  CZ  . PHE A 1 66  ? -11.036 -5.234  5.715   1.00 10.46 ? 66  PHE A CZ  1 
ATOM   535  N  N   . ASN A 1 67  ? -8.259  0.385   5.861   1.00 11.35 ? 67  ASN A N   1 
ATOM   536  C  CA  . ASN A 1 67  ? -9.128  1.343   6.596   1.00 11.94 ? 67  ASN A CA  1 
ATOM   537  C  C   . ASN A 1 67  ? -10.325 1.757   5.777   1.00 11.79 ? 67  ASN A C   1 
ATOM   538  O  O   . ASN A 1 67  ? -10.154 2.132   4.630   1.00 14.07 ? 67  ASN A O   1 
ATOM   539  C  CB  . ASN A 1 67  ? -8.388  2.635   6.946   1.00 11.29 ? 67  ASN A CB  1 
ATOM   540  C  CG  . ASN A 1 67  ? -7.342  2.454   7.995   1.00 14.31 ? 67  ASN A CG  1 
ATOM   541  O  OD1 . ASN A 1 67  ? -7.108  1.346   8.535   1.00 12.88 ? 67  ASN A OD1 1 
ATOM   542  N  ND2 . ASN A 1 67  ? -6.653  3.565   8.297   1.00 18.31 ? 67  ASN A ND2 1 
ATOM   543  N  N   . VAL A 1 68  ? -11.513 1.657   6.355   1.00 11.51 ? 68  VAL A N   1 
ATOM   544  C  CA  . VAL A 1 68  ? -12.691 2.259   5.777   1.00 11.20 ? 68  VAL A CA  1 
ATOM   545  C  C   . VAL A 1 68  ? -12.840 3.634   6.471   1.00 13.12 ? 68  VAL A C   1 
ATOM   546  O  O   . VAL A 1 68  ? -12.986 3.675   7.710   1.00 12.83 ? 68  VAL A O   1 
ATOM   547  C  CB  . VAL A 1 68  ? -13.955 1.382   5.939   1.00 12.64 ? 68  VAL A CB  1 
ATOM   548  C  CG1 . VAL A 1 68  ? -15.275 2.195   5.488   1.00 13.70 ? 68  VAL A CG1 1 
ATOM   549  C  CG2 . VAL A 1 68  ? -13.796 0.084   5.205   1.00 11.37 ? 68  VAL A CG2 1 
ATOM   550  N  N   . GLU A 1 69  ? -12.742 4.717   5.694   1.00 12.99 ? 69  GLU A N   1 
ATOM   551  C  CA  . GLU A 1 69  ? -12.620 6.090   6.225   1.00 13.64 ? 69  GLU A CA  1 
ATOM   552  C  C   . GLU A 1 69  ? -13.952 6.771   6.110   1.00 15.03 ? 69  GLU A C   1 
ATOM   553  O  O   . GLU A 1 69  ? -14.717 6.551   5.125   1.00 17.42 ? 69  GLU A O   1 
ATOM   554  C  CB  . GLU A 1 69  ? -11.699 6.895   5.368   1.00 16.64 ? 69  GLU A CB  1 
ATOM   555  C  CG  . GLU A 1 69  ? -10.316 6.345   5.423   1.00 16.43 ? 69  GLU A CG  1 
ATOM   556  C  CD  . GLU A 1 69  ? -9.536  6.840   4.269   1.00 19.35 ? 69  GLU A CD  1 
ATOM   557  O  OE1 . GLU A 1 69  ? -10.141 7.530   3.365   1.00 18.31 ? 69  GLU A OE1 1 
ATOM   558  O  OE2 . GLU A 1 69  ? -8.329  6.554   4.265   1.00 21.84 ? 69  GLU A OE2 1 
ATOM   559  N  N   . PHE A 1 70  ? -14.186 7.676   7.043   1.00 12.71 ? 70  PHE A N   1 
ATOM   560  C  CA  . PHE A 1 70  ? -15.445 8.396   7.113   1.00 11.95 ? 70  PHE A CA  1 
ATOM   561  C  C   . PHE A 1 70  ? -15.218 9.913   7.046   1.00 12.41 ? 70  PHE A C   1 
ATOM   562  O  O   . PHE A 1 70  ? -14.136 10.412  7.446   1.00 13.05 ? 70  PHE A O   1 
ATOM   563  C  CB  . PHE A 1 70  ? -16.193 8.051   8.399   1.00 11.53 ? 70  PHE A CB  1 
ATOM   564  C  CG  . PHE A 1 70  ? -16.744 6.633   8.378   1.00 10.22 ? 70  PHE A CG  1 
ATOM   565  C  CD1 . PHE A 1 70  ? -15.887 5.547   8.564   1.00 11.38 ? 70  PHE A CD1 1 
ATOM   566  C  CD2 . PHE A 1 70  ? -18.080 6.428   8.077   1.00 11.85 ? 70  PHE A CD2 1 
ATOM   567  C  CE1 . PHE A 1 70  ? -16.374 4.206   8.464   1.00 11.50 ? 70  PHE A CE1 1 
ATOM   568  C  CE2 . PHE A 1 70  ? -18.602 5.088   7.928   1.00 10.89 ? 70  PHE A CE2 1 
ATOM   569  C  CZ  . PHE A 1 70  ? -17.737 4.001   8.124   1.00 12.50 ? 70  PHE A CZ  1 
ATOM   570  N  N   . ASP A 1 71  ? -16.253 10.639  6.641   1.00 13.83 ? 71  ASP A N   1 
ATOM   571  C  CA  . ASP A 1 71  ? -16.190 12.104  6.788   1.00 14.15 ? 71  ASP A CA  1 
ATOM   572  C  C   . ASP A 1 71  ? -16.425 12.424  8.276   1.00 14.30 ? 71  ASP A C   1 
ATOM   573  O  O   . ASP A 1 71  ? -17.552 12.232  8.818   1.00 17.34 ? 71  ASP A O   1 
ATOM   574  C  CB  . ASP A 1 71  ? -17.367 12.647  5.988   1.00 14.82 ? 71  ASP A CB  1 
ATOM   575  C  CG  . ASP A 1 71  ? -17.597 14.181  6.231   1.00 19.22 ? 71  ASP A CG  1 
ATOM   576  O  OD1 . ASP A 1 71  ? -16.648 14.817  6.793   1.00 17.90 ? 71  ASP A OD1 1 
ATOM   577  O  OD2 . ASP A 1 71  ? -18.705 14.726  5.923   1.00 23.45 ? 71  ASP A OD2 1 
ATOM   578  N  N   . ASP A 1 72  ? -15.412 12.967  8.929   1.00 13.01 ? 72  ASP A N   1 
ATOM   579  C  CA  . ASP A 1 72  ? -15.491 13.269  10.375  1.00 13.04 ? 72  ASP A CA  1 
ATOM   580  C  C   . ASP A 1 72  ? -15.436 14.822  10.512  1.00 13.37 ? 72  ASP A C   1 
ATOM   581  O  O   . ASP A 1 72  ? -14.977 15.307  11.536  1.00 14.91 ? 72  ASP A O   1 
ATOM   582  C  CB  . ASP A 1 72  ? -14.277 12.625  11.141  1.00 12.53 ? 72  ASP A CB  1 
ATOM   583  C  CG  . ASP A 1 72  ? -12.922 13.155  10.683  1.00 13.42 ? 72  ASP A CG  1 
ATOM   584  O  OD1 . ASP A 1 72  ? -12.778 13.863  9.619   1.00 15.50 ? 72  ASP A OD1 1 
ATOM   585  O  OD2 . ASP A 1 72  ? -11.914 12.930  11.401  1.00 14.15 ? 72  ASP A OD2 1 
ATOM   586  N  N   . SER A 1 73  ? -15.942 15.561  9.511   1.00 14.21 ? 73  SER A N   1 
ATOM   587  C  CA  . SER A 1 73  ? -15.889 17.070  9.581   1.00 14.05 ? 73  SER A CA  1 
ATOM   588  C  C   . SER A 1 73  ? -17.200 17.628  10.191  1.00 18.20 ? 73  SER A C   1 
ATOM   589  O  O   . SER A 1 73  ? -17.349 18.877  10.302  1.00 19.57 ? 73  SER A O   1 
ATOM   590  C  CB  . SER A 1 73  ? -15.658 17.653  8.178   1.00 17.00 ? 73  SER A CB  1 
ATOM   591  O  OG  . SER A 1 73  ? -16.738 17.377  7.308   1.00 15.81 ? 73  SER A OG  1 
ATOM   592  N  N   . GLN A 1 74  ? -18.112 16.752  10.601  1.00 18.44 ? 74  GLN A N   1 
ATOM   593  C  CA  . GLN A 1 74  ? -19.302 17.112  11.349  1.00 21.18 ? 74  GLN A CA  1 
ATOM   594  C  C   . GLN A 1 74  ? -19.659 15.971  12.245  1.00 20.59 ? 74  GLN A C   1 
ATOM   595  O  O   . GLN A 1 74  ? -19.112 14.911  12.016  1.00 18.12 ? 74  GLN A O   1 
ATOM   596  C  CB  . GLN A 1 74  ? -20.523 17.284  10.441  1.00 23.03 ? 74  GLN A CB  1 
ATOM   597  C  CG  . GLN A 1 74  ? -20.437 18.369  9.501   1.00 25.15 ? 74  GLN A CG  1 
ATOM   598  C  CD  . GLN A 1 74  ? -21.756 18.509  8.792   1.00 28.68 ? 74  GLN A CD  1 
ATOM   599  O  OE1 . GLN A 1 74  ? -22.743 19.012  9.391   1.00 32.51 ? 74  GLN A OE1 1 
ATOM   600  N  NE2 . GLN A 1 74  ? -21.812 18.031  7.548   1.00 24.83 ? 74  GLN A NE2 1 
ATOM   601  N  N   . ASP A 1 75  ? -20.571 16.196  13.236  1.00 21.97 ? 75  ASP A N   1 
ATOM   602  C  CA  . ASP A 1 75  ? -21.040 15.142  14.121  1.00 23.84 ? 75  ASP A CA  1 
ATOM   603  C  C   . ASP A 1 75  ? -22.049 14.376  13.260  1.00 24.48 ? 75  ASP A C   1 
ATOM   604  O  O   . ASP A 1 75  ? -23.218 14.859  13.054  1.00 27.99 ? 75  ASP A O   1 
ATOM   605  C  CB  . ASP A 1 75  ? -21.719 15.629  15.423  1.00 26.66 ? 75  ASP A CB  1 
ATOM   606  C  CG  . ASP A 1 75  ? -20.710 16.163  16.442  1.00 27.64 ? 75  ASP A CG  1 
ATOM   607  O  OD1 . ASP A 1 75  ? -19.472 16.027  16.267  1.00 30.72 ? 75  ASP A OD1 1 
ATOM   608  O  OD2 . ASP A 1 75  ? -21.145 16.728  17.465  1.00 34.02 ? 75  ASP A OD2 1 
ATOM   609  N  N   . LYS A 1 76  ? -21.593 13.276  12.701  1.00 21.28 ? 76  LYS A N   1 
ATOM   610  C  CA  . LYS A 1 76  ? -22.487 12.357  11.908  1.00 21.46 ? 76  LYS A CA  1 
ATOM   611  C  C   . LYS A 1 76  ? -22.514 10.877  12.370  1.00 21.34 ? 76  LYS A C   1 
ATOM   612  O  O   . LYS A 1 76  ? -23.504 10.090  12.148  1.00 24.25 ? 76  LYS A O   1 
ATOM   613  C  CB  . LYS A 1 76  ? -21.966 12.252  10.478  1.00 21.36 ? 76  LYS A CB  1 
ATOM   614  C  CG  . LYS A 1 76  ? -22.137 13.490  9.636   1.00 25.87 ? 76  LYS A CG  1 
ATOM   615  C  CD  . LYS A 1 76  ? -21.489 13.288  8.252   1.00 24.70 ? 76  LYS A CD  1 
ATOM   616  C  CE  . LYS A 1 76  ? -22.049 14.303  7.279   1.00 25.35 ? 76  LYS A CE  1 
ATOM   617  N  NZ  . LYS A 1 76  ? -21.614 13.997  5.914   1.00 24.67 ? 76  LYS A NZ  1 
ATOM   618  N  N   . ALA A 1 77  ? -21.381 10.435  12.807  1.00 18.94 ? 77  ALA A N   1 
ATOM   619  C  CA  . ALA A 1 77  ? -21.261 9.050   13.337  1.00 16.54 ? 77  ALA A CA  1 
ATOM   620  C  C   . ALA A 1 77  ? -20.486 9.226   14.623  1.00 15.21 ? 77  ALA A C   1 
ATOM   621  O  O   . ALA A 1 77  ? -19.255 9.413   14.566  1.00 16.44 ? 77  ALA A O   1 
ATOM   622  C  CB  . ALA A 1 77  ? -20.444 8.218   12.402  1.00 18.47 ? 77  ALA A CB  1 
ATOM   623  N  N   . VAL A 1 78  ? -21.169 9.140   15.765  1.00 12.13 ? 78  VAL A N   1 
ATOM   624  C  CA  . VAL A 1 78  ? -20.518 9.377   17.060  1.00 12.90 ? 78  VAL A CA  1 
ATOM   625  C  C   . VAL A 1 78  ? -20.772 8.343   18.153  1.00 12.12 ? 78  VAL A C   1 
ATOM   626  O  O   . VAL A 1 78  ? -21.811 7.641   18.168  1.00 13.54 ? 78  VAL A O   1 
ATOM   627  C  CB  . VAL A 1 78  ? -20.830 10.758  17.637  1.00 15.69 ? 78  VAL A CB  1 
ATOM   628  C  CG1 . VAL A 1 78  ? -20.641 11.965  16.613  1.00 16.78 ? 78  VAL A CG1 1 
ATOM   629  C  CG2 . VAL A 1 78  ? -22.233 10.702  18.134  1.00 17.39 ? 78  VAL A CG2 1 
ATOM   630  N  N   . LEU A 1 79  ? -19.742 8.218   19.000  1.00 11.40 ? 79  LEU A N   1 
ATOM   631  C  CA  . LEU A 1 79  ? -19.820 7.429   20.178  1.00 11.74 ? 79  LEU A CA  1 
ATOM   632  C  C   . LEU A 1 79  ? -19.846 8.353   21.379  1.00 11.52 ? 79  LEU A C   1 
ATOM   633  O  O   . LEU A 1 79  ? -19.095 9.325   21.455  1.00 12.89 ? 79  LEU A O   1 
ATOM   634  C  CB  . LEU A 1 79  ? -18.597 6.474   20.204  1.00 12.54 ? 79  LEU A CB  1 
ATOM   635  C  CG  . LEU A 1 79  ? -18.451 5.386   21.221  1.00 14.03 ? 79  LEU A CG  1 
ATOM   636  C  CD1 . LEU A 1 79  ? -19.624 4.375   20.943  1.00 16.06 ? 79  LEU A CD1 1 
ATOM   637  C  CD2 . LEU A 1 79  ? -17.086 4.738   21.080  1.00 12.63 ? 79  LEU A CD2 1 
ATOM   638  N  N   . LYS A 1 80  ? -20.732 8.030   22.290  1.00 11.64 ? 80  LYS A N   1 
ATOM   639  C  CA  . LYS A 1 80  ? -20.742 8.676   23.624  1.00 14.40 ? 80  LYS A CA  1 
ATOM   640  C  C   . LYS A 1 80  ? -21.390 7.760   24.665  1.00 12.69 ? 80  LYS A C   1 
ATOM   641  O  O   . LYS A 1 80  ? -21.685 6.571   24.378  1.00 13.38 ? 80  LYS A O   1 
ATOM   642  C  CB  . LYS A 1 80  ? -21.444 9.971   23.615  1.00 18.68 ? 80  LYS A CB  1 
ATOM   643  C  CG  . LYS A 1 80  ? -22.850 9.756   23.350  1.00 19.83 ? 80  LYS A CG  1 
ATOM   644  C  CD  . LYS A 1 80  ? -23.616 11.123  23.329  1.00 28.45 ? 80  LYS A CD  1 
ATOM   645  C  CE  . LYS A 1 80  ? -23.251 11.867  22.095  1.00 33.13 ? 80  LYS A CE  1 
ATOM   646  N  NZ  . LYS A 1 80  ? -21.745 11.914  22.009  1.00 41.32 ? 80  LYS A NZ  1 
ATOM   647  N  N   . GLY A 1 81  ? -21.496 8.287   25.894  1.00 13.35 ? 81  GLY A N   1 
ATOM   648  C  CA  . GLY A 1 81  ? -21.982 7.496   26.999  1.00 13.90 ? 81  GLY A CA  1 
ATOM   649  C  C   . GLY A 1 81  ? -20.999 6.407   27.336  1.00 14.03 ? 81  GLY A C   1 
ATOM   650  O  O   . GLY A 1 81  ? -19.786 6.574   27.120  1.00 14.08 ? 81  GLY A O   1 
ATOM   651  N  N   . GLY A 1 82  ? -21.486 5.269   27.839  1.00 14.81 ? 82  GLY A N   1 
ATOM   652  C  CA  . GLY A 1 82  ? -20.547 4.246   28.225  1.00 14.44 ? 82  GLY A CA  1 
ATOM   653  C  C   . GLY A 1 82  ? -19.646 4.830   29.342  1.00 15.34 ? 82  GLY A C   1 
ATOM   654  O  O   . GLY A 1 82  ? -20.124 5.592   30.231  1.00 18.84 ? 82  GLY A O   1 
ATOM   655  N  N   . PRO A 1 83  ? -18.302 4.615   29.249  1.00 15.42 ? 83  PRO A N   1 
ATOM   656  C  CA  . PRO A 1 83  ? -17.393 5.221   30.220  1.00 14.15 ? 83  PRO A CA  1 
ATOM   657  C  C   . PRO A 1 83  ? -16.939 6.656   29.818  1.00 15.76 ? 83  PRO A C   1 
ATOM   658  O  O   . PRO A 1 83  ? -16.145 7.250   30.527  1.00 17.92 ? 83  PRO A O   1 
ATOM   659  C  CB  . PRO A 1 83  ? -16.143 4.321   30.104  1.00 16.29 ? 83  PRO A CB  1 
ATOM   660  C  CG  . PRO A 1 83  ? -16.087 3.939   28.650  1.00 12.21 ? 83  PRO A CG  1 
ATOM   661  C  CD  . PRO A 1 83  ? -17.564 3.813   28.230  1.00 12.93 ? 83  PRO A CD  1 
ATOM   662  N  N   . LEU A 1 84  ? -17.447 7.178   28.706  1.00 13.39 ? 84  LEU A N   1 
ATOM   663  C  CA  . LEU A 1 84  ? -16.847 8.381   28.068  1.00 13.73 ? 84  LEU A CA  1 
ATOM   664  C  C   . LEU A 1 84  ? -17.511 9.665   28.596  1.00 17.05 ? 84  LEU A C   1 
ATOM   665  O  O   . LEU A 1 84  ? -18.713 9.655   28.927  1.00 17.02 ? 84  LEU A O   1 
ATOM   666  C  CB  . LEU A 1 84  ? -17.142 8.365   26.585  1.00 12.05 ? 84  LEU A CB  1 
ATOM   667  C  CG  . LEU A 1 84  ? -16.512 7.120   25.903  1.00 9.96  ? 84  LEU A CG  1 
ATOM   668  C  CD1 . LEU A 1 84  ? -17.004 7.020   24.420  1.00 12.33 ? 84  LEU A CD1 1 
ATOM   669  C  CD2 . LEU A 1 84  ? -14.945 7.143   26.002  1.00 9.64  ? 84  LEU A CD2 1 
ATOM   670  N  N   . ASP A 1 85  ? -16.738 10.747  28.619  1.00 18.39 ? 85  ASP A N   1 
ATOM   671  C  CA  . ASP A 1 85  ? -17.301 12.098  28.840  1.00 20.80 ? 85  ASP A CA  1 
ATOM   672  C  C   . ASP A 1 85  ? -17.324 12.722  27.441  1.00 20.69 ? 85  ASP A C   1 
ATOM   673  O  O   . ASP A 1 85  ? -16.323 12.674  26.692  1.00 24.39 ? 85  ASP A O   1 
ATOM   674  C  CB  . ASP A 1 85  ? -16.417 12.837  29.866  1.00 23.73 ? 85  ASP A CB  1 
ATOM   675  C  CG  . ASP A 1 85  ? -16.565 12.273  31.289  1.00 29.51 ? 85  ASP A CG  1 
ATOM   676  O  OD1 . ASP A 1 85  ? -17.637 11.695  31.643  1.00 36.11 ? 85  ASP A OD1 1 
ATOM   677  O  OD2 . ASP A 1 85  ? -15.623 12.452  32.110  1.00 36.23 ? 85  ASP A OD2 1 
ATOM   678  N  N   . GLY A 1 86  ? -18.352 13.489  27.101  1.00 22.32 ? 86  GLY A N   1 
ATOM   679  C  CA  . GLY A 1 86  ? -18.280 14.129  25.797  1.00 20.33 ? 86  GLY A CA  1 
ATOM   680  C  C   . GLY A 1 86  ? -18.420 13.140  24.582  1.00 19.25 ? 86  GLY A C   1 
ATOM   681  O  O   . GLY A 1 86  ? -18.854 11.971  24.709  1.00 21.47 ? 86  GLY A O   1 
ATOM   682  N  N   . THR A 1 87  ? -18.071 13.643  23.420  1.00 15.40 ? 87  THR A N   1 
ATOM   683  C  CA  . THR A 1 87  ? -18.515 13.052  22.166  1.00 15.43 ? 87  THR A CA  1 
ATOM   684  C  C   . THR A 1 87  ? -17.352 12.736  21.302  1.00 13.39 ? 87  THR A C   1 
ATOM   685  O  O   . THR A 1 87  ? -16.414 13.516  21.223  1.00 12.86 ? 87  THR A O   1 
ATOM   686  C  CB  . THR A 1 87  ? -19.403 14.142  21.400  1.00 17.49 ? 87  THR A CB  1 
ATOM   687  O  OG1 . THR A 1 87  ? -20.605 14.340  22.162  1.00 22.06 ? 87  THR A OG1 1 
ATOM   688  C  CG2 . THR A 1 87  ? -19.833 13.692  19.944  1.00 18.75 ? 87  THR A CG2 1 
ATOM   689  N  N   . TYR A 1 88  ? -17.372 11.507  20.736  1.00 11.69 ? 88  TYR A N   1 
ATOM   690  C  CA  . TYR A 1 88  ? -16.238 11.066  19.921  1.00 10.27 ? 88  TYR A CA  1 
ATOM   691  C  C   . TYR A 1 88  ? -16.686 10.711  18.502  1.00 10.06 ? 88  TYR A C   1 
ATOM   692  O  O   . TYR A 1 88  ? -17.675 9.962   18.329  1.00 13.27 ? 88  TYR A O   1 
ATOM   693  C  CB  . TYR A 1 88  ? -15.585 9.837   20.529  1.00 10.33 ? 88  TYR A CB  1 
ATOM   694  C  CG  . TYR A 1 88  ? -14.831 10.037  21.855  1.00 7.67  ? 88  TYR A CG  1 
ATOM   695  C  CD1 . TYR A 1 88  ? -15.509 10.346  23.042  1.00 8.55  ? 88  TYR A CD1 1 
ATOM   696  C  CD2 . TYR A 1 88  ? -13.437 9.862   21.931  1.00 7.97  ? 88  TYR A CD2 1 
ATOM   697  C  CE1 . TYR A 1 88  ? -14.839 10.578  24.239  1.00 11.03 ? 88  TYR A CE1 1 
ATOM   698  C  CE2 . TYR A 1 88  ? -12.737 10.033  23.155  1.00 9.39  ? 88  TYR A CE2 1 
ATOM   699  C  CZ  . TYR A 1 88  ? -13.432 10.364  24.304  1.00 9.02  ? 88  TYR A CZ  1 
ATOM   700  O  OH  . TYR A 1 88  ? -12.811 10.507  25.527  1.00 10.23 ? 88  TYR A OH  1 
ATOM   701  N  N   . ARG A 1 89  ? -16.030 11.288  17.508  1.00 8.88  ? 89  ARG A N   1 
ATOM   702  C  CA  . ARG A 1 89  ? -16.419 11.114  16.085  1.00 10.39 ? 89  ARG A CA  1 
ATOM   703  C  C   . ARG A 1 89  ? -15.713 9.965   15.414  1.00 8.45  ? 89  ARG A C   1 
ATOM   704  O  O   . ARG A 1 89  ? -14.490 9.866   15.487  1.00 7.95  ? 89  ARG A O   1 
ATOM   705  C  CB  . ARG A 1 89  ? -16.020 12.321  15.242  1.00 11.44 ? 89  ARG A CB  1 
ATOM   706  C  CG  . ARG A 1 89  ? -16.877 13.445  15.459  1.00 17.60 ? 89  ARG A CG  1 
ATOM   707  C  CD  . ARG A 1 89  ? -16.750 14.415  14.317  1.00 22.63 ? 89  ARG A CD  1 
ATOM   708  N  NE  . ARG A 1 89  ? -17.468 15.504  14.828  1.00 23.18 ? 89  ARG A NE  1 
ATOM   709  C  CZ  . ARG A 1 89  ? -17.193 16.744  14.590  1.00 21.94 ? 89  ARG A CZ  1 
ATOM   710  N  NH1 . ARG A 1 89  ? -16.198 17.065  13.750  1.00 20.60 ? 89  ARG A NH1 1 
ATOM   711  N  NH2 . ARG A 1 89  ? -17.937 17.687  15.208  1.00 24.77 ? 89  ARG A NH2 1 
ATOM   712  N  N   . LEU A 1 90  ? -16.478 9.148   14.691  1.00 7.86  ? 90  LEU A N   1 
ATOM   713  C  CA  . LEU A 1 90  ? -15.871 8.068   13.950  1.00 8.59  ? 90  LEU A CA  1 
ATOM   714  C  C   . LEU A 1 90  ? -15.036 8.618   12.798  1.00 8.71  ? 90  LEU A C   1 
ATOM   715  O  O   . LEU A 1 90  ? -15.529 9.370   11.936  1.00 10.71 ? 90  LEU A O   1 
ATOM   716  C  CB  . LEU A 1 90  ? -16.986 7.152   13.366  1.00 8.56  ? 90  LEU A CB  1 
ATOM   717  C  CG  . LEU A 1 90  ? -16.511 5.967   12.506  1.00 8.48  ? 90  LEU A CG  1 
ATOM   718  C  CD1 . LEU A 1 90  ? -15.716 4.905   13.235  1.00 11.92 ? 90  LEU A CD1 1 
ATOM   719  C  CD2 . LEU A 1 90  ? -17.762 5.286   11.955  1.00 11.05 ? 90  LEU A CD2 1 
ATOM   720  N  N   . ILE A 1 91  ? -13.781 8.169   12.738  1.00 8.64  ? 91  ILE A N   1 
ATOM   721  C  CA  . ILE A 1 91  ? -12.813 8.557   11.647  1.00 8.45  ? 91  ILE A CA  1 
ATOM   722  C  C   . ILE A 1 91  ? -12.497 7.393   10.700  1.00 8.00  ? 91  ILE A C   1 
ATOM   723  O  O   . ILE A 1 91  ? -12.506 7.554   9.479   1.00 7.76  ? 91  ILE A O   1 
ATOM   724  C  CB  . ILE A 1 91  ? -11.504 9.219   12.114  1.00 9.64  ? 91  ILE A CB  1 
ATOM   725  C  CG1 . ILE A 1 91  ? -10.614 9.549   10.907  1.00 10.32 ? 91  ILE A CG1 1 
ATOM   726  C  CG2 . ILE A 1 91  ? -10.755 8.398   13.239  1.00 9.42  ? 91  ILE A CG2 1 
ATOM   727  C  CD1 . ILE A 1 91  ? -9.451  10.579  11.317  1.00 12.71 ? 91  ILE A CD1 1 
ATOM   728  N  N   . GLN A 1 92  ? -12.385 6.160   11.257  1.00 8.34  ? 92  GLN A N   1 
ATOM   729  C  CA  . GLN A 1 92  ? -12.171 5.024   10.353  1.00 8.73  ? 92  GLN A CA  1 
ATOM   730  C  C   . GLN A 1 92  ? -12.400 3.740   11.158  1.00 7.72  ? 92  GLN A C   1 
ATOM   731  O  O   . GLN A 1 92  ? -12.397 3.779   12.379  1.00 7.63  ? 92  GLN A O   1 
ATOM   732  C  CB  . GLN A 1 92  ? -10.755 4.971   9.749   1.00 9.86  ? 92  GLN A CB  1 
ATOM   733  C  CG  . GLN A 1 92  ? -9.596  5.156   10.778  1.00 11.37 ? 92  GLN A CG  1 
ATOM   734  C  CD  . GLN A 1 92  ? -8.925  3.841   11.231  1.00 10.09 ? 92  GLN A CD  1 
ATOM   735  O  OE1 . GLN A 1 92  ? -9.469  2.718   11.156  1.00 10.79 ? 92  GLN A OE1 1 
ATOM   736  N  NE2 . GLN A 1 92  ? -7.785  4.029   11.910  1.00 13.77 ? 92  GLN A NE2 1 
ATOM   737  N  N   . PHE A 1 93  ? -12.624 2.632   10.416  1.00 7.56  ? 93  PHE A N   1 
ATOM   738  C  CA  . PHE A 1 93  ? -12.479 1.334   11.057  1.00 7.05  ? 93  PHE A CA  1 
ATOM   739  C  C   . PHE A 1 93  ? -11.535 0.462   10.225  1.00 8.77  ? 93  PHE A C   1 
ATOM   740  O  O   . PHE A 1 93  ? -11.335 0.649   9.029   1.00 9.25  ? 93  PHE A O   1 
ATOM   741  C  CB  . PHE A 1 93  ? -13.836 0.678   11.344  1.00 7.48  ? 93  PHE A CB  1 
ATOM   742  C  CG  . PHE A 1 93  ? -14.590 0.202   10.088  1.00 9.10  ? 93  PHE A CG  1 
ATOM   743  C  CD1 . PHE A 1 93  ? -14.203 -0.960  9.423   1.00 9.08  ? 93  PHE A CD1 1 
ATOM   744  C  CD2 . PHE A 1 93  ? -15.718 0.901   9.661   1.00 9.72  ? 93  PHE A CD2 1 
ATOM   745  C  CE1 . PHE A 1 93  ? -14.902 -1.427  8.317   1.00 9.47  ? 93  PHE A CE1 1 
ATOM   746  C  CE2 . PHE A 1 93  ? -16.473 0.450   8.540   1.00 10.85 ? 93  PHE A CE2 1 
ATOM   747  C  CZ  . PHE A 1 93  ? -16.045 -0.715  7.859   1.00 10.44 ? 93  PHE A CZ  1 
ATOM   748  N  N   . HIS A 1 94  ? -11.016 -0.558  10.922  1.00 7.54  ? 94  HIS A N   1 
ATOM   749  C  CA  . HIS A 1 94  ? -10.141 -1.539  10.275  1.00 6.84  ? 94  HIS A CA  1 
ATOM   750  C  C   . HIS A 1 94  ? -10.214 -2.799  11.109  1.00 7.26  ? 94  HIS A C   1 
ATOM   751  O  O   . HIS A 1 94  ? -10.841 -2.816  12.187  1.00 7.71  ? 94  HIS A O   1 
ATOM   752  C  CB  . HIS A 1 94  ? -8.670  -1.059  10.199  1.00 7.60  ? 94  HIS A CB  1 
ATOM   753  C  CG  . HIS A 1 94  ? -8.120  -0.764  11.590  1.00 7.27  ? 94  HIS A CG  1 
ATOM   754  N  ND1 . HIS A 1 94  ? -8.313  0.452   12.238  1.00 7.18  ? 94  HIS A ND1 1 
ATOM   755  C  CD2 . HIS A 1 94  ? -7.494  -1.574  12.500  1.00 8.52  ? 94  HIS A CD2 1 
ATOM   756  C  CE1 . HIS A 1 94  ? -7.800  0.362   13.467  1.00 6.69  ? 94  HIS A CE1 1 
ATOM   757  N  NE2 . HIS A 1 94  ? -7.317  -0.862  13.648  1.00 7.02  ? 94  HIS A NE2 1 
ATOM   758  N  N   . PHE A 1 95  ? -9.512  -3.846  10.655  1.00 6.72  ? 95  PHE A N   1 
ATOM   759  C  CA  . PHE A 1 95  ? -9.494  -5.144  11.378  1.00 7.09  ? 95  PHE A CA  1 
ATOM   760  C  C   . PHE A 1 95  ? -8.043  -5.580  11.548  1.00 7.19  ? 95  PHE A C   1 
ATOM   761  O  O   . PHE A 1 95  ? -7.112  -5.104  10.849  1.00 7.50  ? 95  PHE A O   1 
ATOM   762  C  CB  . PHE A 1 95  ? -10.195 -6.238  10.490  1.00 7.18  ? 95  PHE A CB  1 
ATOM   763  C  CG  . PHE A 1 95  ? -11.673 -5.948  10.193  1.00 6.00  ? 95  PHE A CG  1 
ATOM   764  C  CD1 . PHE A 1 95  ? -11.995 -5.088  9.121   1.00 7.41  ? 95  PHE A CD1 1 
ATOM   765  C  CD2 . PHE A 1 95  ? -12.703 -6.616  10.875  1.00 7.57  ? 95  PHE A CD2 1 
ATOM   766  C  CE1 . PHE A 1 95  ? -13.313 -4.851  8.770   1.00 7.06  ? 95  PHE A CE1 1 
ATOM   767  C  CE2 . PHE A 1 95  ? -14.027 -6.402  10.588  1.00 7.38  ? 95  PHE A CE2 1 
ATOM   768  C  CZ  . PHE A 1 95  ? -14.359 -5.527  9.492   1.00 7.47  ? 95  PHE A CZ  1 
ATOM   769  N  N   . HIS A 1 96  ? -7.908  -6.534  12.493  1.00 6.40  ? 96  HIS A N   1 
ATOM   770  C  CA  . HIS A 1 96  ? -6.700  -7.338  12.641  1.00 6.22  ? 96  HIS A CA  1 
ATOM   771  C  C   . HIS A 1 96  ? -7.135  -8.802  12.534  1.00 5.56  ? 96  HIS A C   1 
ATOM   772  O  O   . HIS A 1 96  ? -8.185  -9.185  13.082  1.00 6.62  ? 96  HIS A O   1 
ATOM   773  C  CB  . HIS A 1 96  ? -6.049  -7.098  14.029  1.00 6.45  ? 96  HIS A CB  1 
ATOM   774  C  CG  . HIS A 1 96  ? -5.755  -5.669  14.309  1.00 7.36  ? 96  HIS A CG  1 
ATOM   775  N  ND1 . HIS A 1 96  ? -4.505  -5.098  14.104  1.00 8.38  ? 96  HIS A ND1 1 
ATOM   776  C  CD2 . HIS A 1 96  ? -6.587  -4.656  14.708  1.00 7.21  ? 96  HIS A CD2 1 
ATOM   777  C  CE1 . HIS A 1 96  ? -4.578  -3.796  14.411  1.00 6.77  ? 96  HIS A CE1 1 
ATOM   778  N  NE2 . HIS A 1 96  ? -5.806  -3.500  14.755  1.00 6.08  ? 96  HIS A NE2 1 
ATOM   779  N  N   . TRP A 1 97  ? -6.340  -9.629  11.828  1.00 7.30  ? 97  TRP A N   1 
ATOM   780  C  CA  . TRP A 1 97  ? -6.775  -11.031 11.575  1.00 6.03  ? 97  TRP A CA  1 
ATOM   781  C  C   . TRP A 1 97  ? -5.574  -11.965 11.478  1.00 7.39  ? 97  TRP A C   1 
ATOM   782  O  O   . TRP A 1 97  ? -4.401  -11.515 11.403  1.00 7.99  ? 97  TRP A O   1 
ATOM   783  C  CB  . TRP A 1 97  ? -7.683  -11.174 10.366  1.00 7.82  ? 97  TRP A CB  1 
ATOM   784  C  CG  . TRP A 1 97  ? -7.030  -10.781 9.093   1.00 8.29  ? 97  TRP A CG  1 
ATOM   785  C  CD1 . TRP A 1 97  ? -6.315  -11.616 8.255   1.00 8.51  ? 97  TRP A CD1 1 
ATOM   786  C  CD2 . TRP A 1 97  ? -6.965  -9.464  8.510   1.00 7.32  ? 97  TRP A CD2 1 
ATOM   787  N  NE1 . TRP A 1 97  ? -5.854  -10.884 7.138   1.00 9.20  ? 97  TRP A NE1 1 
ATOM   788  C  CE2 . TRP A 1 97  ? -6.202  -9.567  7.299   1.00 7.39  ? 97  TRP A CE2 1 
ATOM   789  C  CE3 . TRP A 1 97  ? -7.434  -8.198  8.920   1.00 7.53  ? 97  TRP A CE3 1 
ATOM   790  C  CZ2 . TRP A 1 97  ? -5.981  -8.448  6.447   1.00 9.65  ? 97  TRP A CZ2 1 
ATOM   791  C  CZ3 . TRP A 1 97  ? -7.166  -7.061  8.092   1.00 8.98  ? 97  TRP A CZ3 1 
ATOM   792  C  CH2 . TRP A 1 97  ? -6.494  -7.209  6.895   1.00 11.44 ? 97  TRP A CH2 1 
ATOM   793  N  N   . GLY A 1 98  ? -5.891  -13.270 11.501  1.00 7.75  ? 98  GLY A N   1 
ATOM   794  C  CA  . GLY A 1 98  ? -4.848  -14.246 11.505  1.00 8.70  ? 98  GLY A CA  1 
ATOM   795  C  C   . GLY A 1 98  ? -4.618  -14.976 10.190  1.00 7.28  ? 98  GLY A C   1 
ATOM   796  O  O   . GLY A 1 98  ? -5.337  -14.810 9.234   1.00 9.47  ? 98  GLY A O   1 
ATOM   797  N  N   . SER A 1 99  ? -3.578  -15.827 10.220  1.00 8.15  ? 99  SER A N   1 
ATOM   798  C  CA  . SER A 1 99  ? -3.342  -16.761 9.112   1.00 9.45  ? 99  SER A CA  1 
ATOM   799  C  C   . SER A 1 99  ? -4.229  -18.005 9.189   1.00 10.08 ? 99  SER A C   1 
ATOM   800  O  O   . SER A 1 99  ? -4.286  -18.772 8.184   1.00 13.46 ? 99  SER A O   1 
ATOM   801  C  CB  . SER A 1 99  ? -1.864  -17.122 9.075   1.00 11.96 ? 99  SER A CB  1 
ATOM   802  O  OG  . SER A 1 99  ? -1.473  -17.680 10.293  1.00 12.47 ? 99  SER A OG  1 
ATOM   803  N  N   . LEU A 1 100 ? -4.791  -18.220 10.392  1.00 11.53 ? 100 LEU A N   1 
ATOM   804  C  CA  . LEU A 1 100 ? -5.636  -19.365 10.739  1.00 13.07 ? 100 LEU A CA  1 
ATOM   805  C  C   . LEU A 1 100 ? -6.763  -18.888 11.615  1.00 11.59 ? 100 LEU A C   1 
ATOM   806  O  O   . LEU A 1 100 ? -6.609  -17.869 12.315  1.00 10.60 ? 100 LEU A O   1 
ATOM   807  C  CB  . LEU A 1 100 ? -4.831  -20.386 11.635  1.00 17.16 ? 100 LEU A CB  1 
ATOM   808  C  CG  . LEU A 1 100 ? -3.517  -20.799 11.006  1.00 20.53 ? 100 LEU A CG  1 
ATOM   809  C  CD1 . LEU A 1 100 ? -2.444  -21.166 11.985  1.00 25.28 ? 100 LEU A CD1 1 
ATOM   810  C  CD2 . LEU A 1 100 ? -3.837  -22.019 10.149  1.00 24.63 ? 100 LEU A CD2 1 
ATOM   811  N  N   . ASP A 1 101 ? -7.864  -19.671 11.677  1.00 9.96  ? 101 ASP A N   1 
ATOM   812  C  CA  . ASP A 1 101 ? -9.048  -19.170 12.446  1.00 11.32 ? 101 ASP A CA  1 
ATOM   813  C  C   . ASP A 1 101 ? -8.753  -19.085 13.946  1.00 11.12 ? 101 ASP A C   1 
ATOM   814  O  O   . ASP A 1 101 ? -9.410  -18.334 14.648  1.00 13.05 ? 101 ASP A O   1 
ATOM   815  C  CB  . ASP A 1 101 ? -10.278 -20.039 12.202  1.00 11.85 ? 101 ASP A CB  1 
ATOM   816  C  CG  . ASP A 1 101 ? -10.793 -19.989 10.781  1.00 14.17 ? 101 ASP A CG  1 
ATOM   817  O  OD1 . ASP A 1 101 ? -10.376 -19.215 9.925   1.00 14.99 ? 101 ASP A OD1 1 
ATOM   818  O  OD2 . ASP A 1 101 ? -11.694 -20.855 10.541  1.00 19.85 ? 101 ASP A OD2 1 
ATOM   819  N  N   . GLY A 1 102 ? -7.767  -19.874 14.425  1.00 11.39 ? 102 GLY A N   1 
ATOM   820  C  CA  . GLY A 1 102 ? -7.451  -19.849 15.876  1.00 11.20 ? 102 GLY A CA  1 
ATOM   821  C  C   . GLY A 1 102 ? -6.627  -18.687 16.421  1.00 9.82  ? 102 GLY A C   1 
ATOM   822  O  O   . GLY A 1 102 ? -6.274  -18.684 17.598  1.00 11.80 ? 102 GLY A O   1 
ATOM   823  N  N   . GLN A 1 103 ? -6.352  -17.689 15.577  1.00 9.11  ? 103 GLN A N   1 
ATOM   824  C  CA  . GLN A 1 103 ? -5.586  -16.514 16.034  1.00 8.29  ? 103 GLN A CA  1 
ATOM   825  C  C   . GLN A 1 103 ? -5.975  -15.332 15.154  1.00 7.56  ? 103 GLN A C   1 
ATOM   826  O  O   . GLN A 1 103 ? -6.585  -15.561 14.078  1.00 9.01  ? 103 GLN A O   1 
ATOM   827  C  CB  . GLN A 1 103 ? -4.067  -16.776 16.068  1.00 10.95 ? 103 GLN A CB  1 
ATOM   828  C  CG  . GLN A 1 103 ? -3.450  -16.911 14.673  1.00 10.20 ? 103 GLN A CG  1 
ATOM   829  C  CD  . GLN A 1 103 ? -2.062  -17.482 14.766  1.00 15.01 ? 103 GLN A CD  1 
ATOM   830  O  OE1 . GLN A 1 103 ? -1.811  -18.428 15.618  1.00 22.54 ? 103 GLN A OE1 1 
ATOM   831  N  NE2 . GLN A 1 103 ? -1.154  -16.984 13.948  1.00 15.93 ? 103 GLN A NE2 1 
ATOM   832  N  N   . GLY A 1 104 ? -5.675  -14.100 15.640  1.00 7.64  ? 104 GLY A N   1 
ATOM   833  C  CA  . GLY A 1 104 ? -6.003  -12.906 14.823  1.00 6.70  ? 104 GLY A CA  1 
ATOM   834  C  C   . GLY A 1 104 ? -6.449  -11.757 15.697  1.00 6.10  ? 104 GLY A C   1 
ATOM   835  O  O   . GLY A 1 104 ? -6.158  -10.559 15.409  1.00 7.90  ? 104 GLY A O   1 
ATOM   836  N  N   . SER A 1 105 ? -7.165  -12.042 16.820  1.00 5.37  ? 105 SER A N   1 
ATOM   837  C  CA  . SER A 1 105 ? -7.560  -10.920 17.669  1.00 6.52  ? 105 SER A CA  1 
ATOM   838  C  C   . SER A 1 105 ? -6.351  -10.327 18.397  1.00 5.54  ? 105 SER A C   1 
ATOM   839  O  O   . SER A 1 105 ? -5.334  -11.011 18.636  1.00 6.92  ? 105 SER A O   1 
ATOM   840  C  CB  . SER A 1 105 ? -8.703  -11.271 18.593  1.00 7.15  ? 105 SER A CB  1 
ATOM   841  O  OG  . SER A 1 105 ? -8.311  -12.174 19.602  1.00 6.74  ? 105 SER A OG  1 
ATOM   842  N  N   . GLU A 1 106 ? -6.506  -9.083  18.814  1.00 5.95  ? 106 GLU A N   1 
ATOM   843  C  CA  . GLU A 1 106 ? -5.479  -8.414  19.646  1.00 5.83  ? 106 GLU A CA  1 
ATOM   844  C  C   . GLU A 1 106 ? -5.798  -8.582  21.144  1.00 5.58  ? 106 GLU A C   1 
ATOM   845  O  O   . GLU A 1 106 ? -5.010  -9.169  21.939  1.00 6.83  ? 106 GLU A O   1 
ATOM   846  C  CB  . GLU A 1 106 ? -5.431  -6.889  19.207  1.00 6.60  ? 106 GLU A CB  1 
ATOM   847  C  CG  . GLU A 1 106 ? -4.904  -6.794  17.787  1.00 8.06  ? 106 GLU A CG  1 
ATOM   848  C  CD  . GLU A 1 106 ? -4.209  -5.471  17.486  1.00 5.89  ? 106 GLU A CD  1 
ATOM   849  O  OE1 . GLU A 1 106 ? -4.889  -4.419  17.753  1.00 7.02  ? 106 GLU A OE1 1 
ATOM   850  O  OE2 . GLU A 1 106 ? -3.053  -5.519  16.973  1.00 8.28  ? 106 GLU A OE2 1 
ATOM   851  N  N   . HIS A 1 107 ? -7.007  -8.090  21.550  1.00 6.10  ? 107 HIS A N   1 
ATOM   852  C  CA  . HIS A 1 107 ? -7.462  -8.472  22.902  1.00 5.51  ? 107 HIS A CA  1 
ATOM   853  C  C   . HIS A 1 107 ? -7.773  -9.984  22.896  1.00 5.74  ? 107 HIS A C   1 
ATOM   854  O  O   . HIS A 1 107 ? -8.112  -10.604 21.835  1.00 7.00  ? 107 HIS A O   1 
ATOM   855  C  CB  . HIS A 1 107 ? -8.712  -7.653  23.312  1.00 6.20  ? 107 HIS A CB  1 
ATOM   856  C  CG  . HIS A 1 107 ? -8.395  -6.177  23.416  1.00 5.42  ? 107 HIS A CG  1 
ATOM   857  N  ND1 . HIS A 1 107 ? -8.396  -5.283  22.346  1.00 6.95  ? 107 HIS A ND1 1 
ATOM   858  C  CD2 . HIS A 1 107 ? -7.904  -5.486  24.493  1.00 6.13  ? 107 HIS A CD2 1 
ATOM   859  C  CE1 . HIS A 1 107 ? -7.958  -4.089  22.775  1.00 6.42  ? 107 HIS A CE1 1 
ATOM   860  N  NE2 . HIS A 1 107 ? -7.685  -4.169  24.089  1.00 5.02  ? 107 HIS A NE2 1 
ATOM   861  N  N   . THR A 1 108 ? -7.657  -10.546 24.101  1.00 5.94  ? 108 THR A N   1 
ATOM   862  C  CA  . THR A 1 108 ? -8.006  -11.934 24.307  1.00 6.14  ? 108 THR A CA  1 
ATOM   863  C  C   . THR A 1 108 ? -8.972  -11.949 25.514  1.00 6.63  ? 108 THR A C   1 
ATOM   864  O  O   . THR A 1 108 ? -9.006  -11.001 26.338  1.00 7.49  ? 108 THR A O   1 
ATOM   865  C  CB  . THR A 1 108 ? -6.809  -12.839 24.513  1.00 7.41  ? 108 THR A CB  1 
ATOM   866  O  OG1 . THR A 1 108 ? -5.993  -12.363 25.621  1.00 7.98  ? 108 THR A OG1 1 
ATOM   867  C  CG2 . THR A 1 108 ? -5.936  -12.929 23.300  1.00 6.37  ? 108 THR A CG2 1 
ATOM   868  N  N   . VAL A 1 109 ? -9.727  -13.029 25.651  1.00 6.84  ? 109 VAL A N   1 
ATOM   869  C  CA  . VAL A 1 109 ? -10.731 -13.141 26.752  1.00 7.38  ? 109 VAL A CA  1 
ATOM   870  C  C   . VAL A 1 109 ? -10.386 -14.438 27.522  1.00 8.34  ? 109 VAL A C   1 
ATOM   871  O  O   . VAL A 1 109 ? -10.561 -15.512 26.950  1.00 9.09  ? 109 VAL A O   1 
ATOM   872  C  CB  . VAL A 1 109 ? -12.184 -13.134 26.202  1.00 8.61  ? 109 VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 109 ? -13.202 -13.246 27.355  1.00 10.07 ? 109 VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 109 ? -12.499 -11.836 25.319  1.00 10.07 ? 109 VAL A CG2 1 
ATOM   875  N  N   . ASP A 1 110 ? -9.920  -14.332 28.761  1.00 9.04  ? 110 ASP A N   1 
ATOM   876  C  CA  . ASP A 1 110 ? -9.412  -15.527 29.457  1.00 8.86  ? 110 ASP A CA  1 
ATOM   877  C  C   . ASP A 1 110 ? -8.460  -16.334 28.544  1.00 8.74  ? 110 ASP A C   1 
ATOM   878  O  O   . ASP A 1 110 ? -8.499  -17.574 28.486  1.00 10.79 ? 110 ASP A O   1 
ATOM   879  C  CB  . ASP A 1 110 ? -10.582 -16.378 29.982  1.00 10.61 ? 110 ASP A CB  1 
ATOM   880  C  CG  . ASP A 1 110 ? -11.433 -15.616 30.998  1.00 10.03 ? 110 ASP A CG  1 
ATOM   881  O  OD1 . ASP A 1 110 ? -10.886 -14.745 31.679  1.00 12.76 ? 110 ASP A OD1 1 
ATOM   882  O  OD2 . ASP A 1 110 ? -12.651 -15.897 31.082  1.00 14.96 ? 110 ASP A OD2 1 
ATOM   883  N  N   . LYS A 1 111 ? -7.566  -15.603 27.859  1.00 8.93  ? 111 LYS A N   1 
ATOM   884  C  CA  . LYS A 1 111 ? -6.524  -16.121 26.954  1.00 9.60  ? 111 LYS A CA  1 
ATOM   885  C  C   . LYS A 1 111 ? -7.071  -16.669 25.629  1.00 8.62  ? 111 LYS A C   1 
ATOM   886  O  O   . LYS A 1 111 ? -6.273  -17.027 24.757  1.00 9.99  ? 111 LYS A O   1 
ATOM   887  C  CB  . LYS A 1 111 ? -5.603  -17.183 27.632  1.00 11.45 ? 111 LYS A CB  1 
ATOM   888  C  CG  . LYS A 1 111 ? -5.016  -16.640 28.913  1.00 13.30 ? 111 LYS A CG  1 
ATOM   889  C  CD  . LYS A 1 111 ? -3.976  -15.587 28.558  1.00 19.19 ? 111 LYS A CD  1 
ATOM   890  C  CE  . LYS A 1 111 ? -3.212  -14.986 29.830  1.00 21.72 ? 111 LYS A CE  1 
ATOM   891  N  NZ  . LYS A 1 111 ? -1.995  -15.707 29.850  1.00 24.64 ? 111 LYS A NZ  1 
ATOM   892  N  N   . LYS A 1 112 ? -8.396  -16.621 25.435  1.00 8.25  ? 112 LYS A N   1 
ATOM   893  C  CA  . LYS A 1 112 ? -8.971  -17.068 24.158  1.00 9.03  ? 112 LYS A CA  1 
ATOM   894  C  C   . LYS A 1 112 ? -8.659  -15.984 23.068  1.00 8.54  ? 112 LYS A C   1 
ATOM   895  O  O   . LYS A 1 112 ? -8.971  -14.777 23.253  1.00 8.75  ? 112 LYS A O   1 
ATOM   896  C  CB  . LYS A 1 112 ? -10.507 -17.174 24.288  1.00 11.60 ? 112 LYS A CB  1 
ATOM   897  C  CG  . LYS A 1 112 ? -11.238 -17.450 22.946  1.00 10.96 ? 112 LYS A CG  1 
ATOM   898  C  CD  . LYS A 1 112 ? -12.741 -17.517 23.049  1.00 13.93 ? 112 LYS A CD  1 
ATOM   899  C  CE  . LYS A 1 112 ? -13.366 -17.692 21.639  1.00 16.68 ? 112 LYS A CE  1 
ATOM   900  N  NZ  . LYS A 1 112 ? -13.176 -18.983 21.110  1.00 19.70 ? 112 LYS A NZ  1 
ATOM   901  N  N   A LYS A 1 113 ? -8.070  -16.465 21.967  0.50 9.31  ? 113 LYS A N   1 
ATOM   902  N  N   B LYS A 1 113 ? -8.228  -16.488 21.921  0.50 8.89  ? 113 LYS A N   1 
ATOM   903  C  CA  A LYS A 1 113 ? -7.935  -15.680 20.696  0.50 8.01  ? 113 LYS A CA  1 
ATOM   904  C  CA  B LYS A 1 113 ? -7.951  -15.654 20.723  0.50 7.52  ? 113 LYS A CA  1 
ATOM   905  C  C   A LYS A 1 113 ? -9.190  -15.874 19.820  0.50 7.32  ? 113 LYS A C   1 
ATOM   906  C  C   B LYS A 1 113 ? -9.013  -15.861 19.630  0.50 6.63  ? 113 LYS A C   1 
ATOM   907  O  O   A LYS A 1 113 ? -9.718  -17.010 19.717  0.50 6.67  ? 113 LYS A O   1 
ATOM   908  O  O   B LYS A 1 113 ? -9.223  -16.998 19.169  0.50 6.28  ? 113 LYS A O   1 
ATOM   909  C  CB  A LYS A 1 113 ? -6.679  -16.075 19.876  0.50 7.31  ? 113 LYS A CB  1 
ATOM   910  C  CB  B LYS A 1 113 ? -6.581  -15.998 20.160  0.50 7.03  ? 113 LYS A CB  1 
ATOM   911  C  CG  A LYS A 1 113 ? -5.331  -15.723 20.559  0.50 8.86  ? 113 LYS A CG  1 
ATOM   912  C  CG  B LYS A 1 113 ? -5.416  -15.703 21.120  0.50 6.20  ? 113 LYS A CG  1 
ATOM   913  C  CD  A LYS A 1 113 ? -4.107  -16.278 19.776  0.50 7.72  ? 113 LYS A CD  1 
ATOM   914  C  CD  B LYS A 1 113 ? -4.080  -16.296 20.572  0.50 7.26  ? 113 LYS A CD  1 
ATOM   915  C  CE  A LYS A 1 113 ? -2.783  -15.915 20.522  0.50 7.15  ? 113 LYS A CE  1 
ATOM   916  C  CE  B LYS A 1 113 ? -2.869  -15.590 21.195  0.50 9.92  ? 113 LYS A CE  1 
ATOM   917  N  NZ  A LYS A 1 113 ? -2.535  -16.490 21.929  0.50 9.75  ? 113 LYS A NZ  1 
ATOM   918  N  NZ  B LYS A 1 113 ? -1.604  -16.307 20.909  0.50 12.14 ? 113 LYS A NZ  1 
ATOM   919  N  N   . TYR A 1 114 ? -9.673  -14.768 19.220  1.00 7.05  ? 114 TYR A N   1 
ATOM   920  C  CA  . TYR A 1 114 ? -10.653 -14.856 18.172  1.00 6.82  ? 114 TYR A CA  1 
ATOM   921  C  C   . TYR A 1 114 ? -10.011 -14.780 16.791  1.00 7.90  ? 114 TYR A C   1 
ATOM   922  O  O   . TYR A 1 114 ? -8.825  -14.471 16.670  1.00 7.72  ? 114 TYR A O   1 
ATOM   923  C  CB  . TYR A 1 114 ? -11.717 -13.742 18.275  1.00 7.38  ? 114 TYR A CB  1 
ATOM   924  C  CG  . TYR A 1 114 ? -12.641 -13.947 19.432  1.00 7.16  ? 114 TYR A CG  1 
ATOM   925  C  CD1 . TYR A 1 114 ? -12.307 -13.525 20.727  1.00 8.30  ? 114 TYR A CD1 1 
ATOM   926  C  CD2 . TYR A 1 114 ? -13.845 -14.612 19.234  1.00 10.04 ? 114 TYR A CD2 1 
ATOM   927  C  CE1 . TYR A 1 114 ? -13.192 -13.711 21.765  1.00 8.91  ? 114 TYR A CE1 1 
ATOM   928  C  CE2 . TYR A 1 114 ? -14.786 -14.738 20.275  1.00 12.22 ? 114 TYR A CE2 1 
ATOM   929  C  CZ  . TYR A 1 114 ? -14.434 -14.298 21.555  1.00 11.38 ? 114 TYR A CZ  1 
ATOM   930  O  OH  . TYR A 1 114 ? -15.360 -14.460 22.637  1.00 15.76 ? 114 TYR A OH  1 
ATOM   931  N  N   . ALA A 1 115 ? -10.803 -15.120 15.757  1.00 6.82  ? 115 ALA A N   1 
ATOM   932  C  CA  . ALA A 1 115 ? -10.225 -15.080 14.404  1.00 6.82  ? 115 ALA A CA  1 
ATOM   933  C  C   . ALA A 1 115 ? -9.788  -13.706 13.908  1.00 7.22  ? 115 ALA A C   1 
ATOM   934  O  O   . ALA A 1 115 ? -8.990  -13.591 12.989  1.00 8.39  ? 115 ALA A O   1 
ATOM   935  C  CB  . ALA A 1 115 ? -11.237 -15.688 13.390  1.00 9.02  ? 115 ALA A CB  1 
ATOM   936  N  N   . ALA A 1 116 ? -10.477 -12.712 14.450  1.00 6.02  ? 116 ALA A N   1 
ATOM   937  C  CA  . ALA A 1 116 ? -10.143 -11.302 14.000  1.00 5.35  ? 116 ALA A CA  1 
ATOM   938  C  C   . ALA A 1 116 ? -10.751 -10.342 15.051  1.00 7.06  ? 116 ALA A C   1 
ATOM   939  O  O   . ALA A 1 116 ? -11.520 -10.770 15.941  1.00 6.30  ? 116 ALA A O   1 
ATOM   940  C  CB  . ALA A 1 116 ? -10.688 -11.019 12.570  1.00 7.78  ? 116 ALA A CB  1 
ATOM   941  N  N   . GLU A 1 117 ? -10.431 -9.063  14.869  1.00 6.76  ? 117 GLU A N   1 
ATOM   942  C  CA  . GLU A 1 117 ? -11.021 -8.055  15.775  1.00 5.71  ? 117 GLU A CA  1 
ATOM   943  C  C   . GLU A 1 117 ? -11.179 -6.784  14.918  1.00 5.70  ? 117 GLU A C   1 
ATOM   944  O  O   . GLU A 1 117 ? -10.243 -6.380  14.218  1.00 6.98  ? 117 GLU A O   1 
ATOM   945  C  CB  . GLU A 1 117 ? -10.026 -7.772  16.925  1.00 5.65  ? 117 GLU A CB  1 
ATOM   946  C  CG  . GLU A 1 117 ? -10.552 -6.824  17.998  1.00 4.89  ? 117 GLU A CG  1 
ATOM   947  C  CD  . GLU A 1 117 ? -9.613  -6.755  19.239  1.00 6.35  ? 117 GLU A CD  1 
ATOM   948  O  OE1 . GLU A 1 117 ? -8.906  -7.781  19.526  1.00 7.74  ? 117 GLU A OE1 1 
ATOM   949  O  OE2 . GLU A 1 117 ? -9.549  -5.641  19.880  1.00 7.45  ? 117 GLU A OE2 1 
ATOM   950  N  N   . LEU A 1 118 ? -12.357 -6.215  15.024  1.00 6.27  ? 118 LEU A N   1 
ATOM   951  C  CA  . LEU A 1 118 ? -12.681 -4.957  14.354  1.00 5.83  ? 118 LEU A CA  1 
ATOM   952  C  C   . LEU A 1 118 ? -12.420 -3.774  15.344  1.00 5.88  ? 118 LEU A C   1 
ATOM   953  O  O   . LEU A 1 118 ? -12.863 -3.854  16.513  1.00 6.47  ? 118 LEU A O   1 
ATOM   954  C  CB  . LEU A 1 118 ? -14.160 -5.041  14.008  1.00 6.49  ? 118 LEU A CB  1 
ATOM   955  C  CG  . LEU A 1 118 ? -14.927 -3.721  13.614  1.00 8.43  ? 118 LEU A CG  1 
ATOM   956  C  CD1 . LEU A 1 118 ? -14.372 -3.081  12.381  1.00 9.09  ? 118 LEU A CD1 1 
ATOM   957  C  CD2 . LEU A 1 118 ? -16.422 -4.055  13.341  1.00 8.31  ? 118 LEU A CD2 1 
ATOM   958  N  N   . HIS A 1 119 ? -11.825 -2.684  14.815  1.00 5.85  ? 119 HIS A N   1 
ATOM   959  C  CA  . HIS A 1 119 ? -11.588 -1.514  15.642  1.00 6.10  ? 119 HIS A CA  1 
ATOM   960  C  C   . HIS A 1 119 ? -12.279 -0.339  14.934  1.00 5.69  ? 119 HIS A C   1 
ATOM   961  O  O   . HIS A 1 119 ? -11.893 0.027   13.793  1.00 7.66  ? 119 HIS A O   1 
ATOM   962  C  CB  . HIS A 1 119 ? -10.111 -1.237  15.726  1.00 5.62  ? 119 HIS A CB  1 
ATOM   963  C  CG  . HIS A 1 119 ? -9.437  -2.191  16.638  1.00 5.36  ? 119 HIS A CG  1 
ATOM   964  N  ND1 . HIS A 1 119 ? -8.074  -2.435  16.628  1.00 6.34  ? 119 HIS A ND1 1 
ATOM   965  C  CD2 . HIS A 1 119 ? -9.967  -3.014  17.574  1.00 6.69  ? 119 HIS A CD2 1 
ATOM   966  C  CE1 . HIS A 1 119 ? -7.781  -3.354  17.538  1.00 5.82  ? 119 HIS A CE1 1 
ATOM   967  N  NE2 . HIS A 1 119 ? -8.920  -3.745  18.127  1.00 6.53  ? 119 HIS A NE2 1 
ATOM   968  N  N   . LEU A 1 120 ? -13.270 0.261   15.621  1.00 6.12  ? 120 LEU A N   1 
ATOM   969  C  CA  . LEU A 1 120 ? -13.946 1.489   15.161  1.00 6.77  ? 120 LEU A CA  1 
ATOM   970  C  C   . LEU A 1 120 ? -13.349 2.665   15.916  1.00 6.35  ? 120 LEU A C   1 
ATOM   971  O  O   . LEU A 1 120 ? -13.457 2.701   17.159  1.00 6.15  ? 120 LEU A O   1 
ATOM   972  C  CB  . LEU A 1 120 ? -15.451 1.399   15.392  1.00 6.46  ? 120 LEU A CB  1 
ATOM   973  C  CG  . LEU A 1 120 ? -16.141 0.271   14.512  1.00 6.96  ? 120 LEU A CG  1 
ATOM   974  C  CD1 . LEU A 1 120 ? -16.990 -0.645  15.377  1.00 10.50 ? 120 LEU A CD1 1 
ATOM   975  C  CD2 . LEU A 1 120 ? -17.041 0.978   13.429  1.00 10.37 ? 120 LEU A CD2 1 
ATOM   976  N  N   . VAL A 1 121 ? -12.569 3.487   15.188  1.00 5.87  ? 121 VAL A N   1 
ATOM   977  C  CA  . VAL A 1 121 ? -11.687 4.494   15.837  1.00 6.67  ? 121 VAL A CA  1 
ATOM   978  C  C   . VAL A 1 121 ? -12.386 5.831   15.865  1.00 6.70  ? 121 VAL A C   1 
ATOM   979  O  O   . VAL A 1 121 ? -12.836 6.301   14.797  1.00 7.91  ? 121 VAL A O   1 
ATOM   980  C  CB  . VAL A 1 121 ? -10.317 4.587   15.096  1.00 7.07  ? 121 VAL A CB  1 
ATOM   981  C  CG1 . VAL A 1 121 ? -9.412  5.660   15.761  1.00 8.82  ? 121 VAL A CG1 1 
ATOM   982  C  CG2 . VAL A 1 121 ? -9.660  3.196   14.992  1.00 8.95  ? 121 VAL A CG2 1 
ATOM   983  N  N   . HIS A 1 122 ? -12.470 6.436   17.074  1.00 6.20  ? 122 HIS A N   1 
ATOM   984  C  CA  . HIS A 1 122 ? -13.225 7.710   17.234  1.00 6.27  ? 122 HIS A CA  1 
ATOM   985  C  C   . HIS A 1 122 ? -12.324 8.702   17.996  1.00 7.24  ? 122 HIS A C   1 
ATOM   986  O  O   . HIS A 1 122 ? -11.581 8.304   18.909  1.00 7.44  ? 122 HIS A O   1 
ATOM   987  C  CB  . HIS A 1 122 ? -14.516 7.520   18.090  1.00 7.12  ? 122 HIS A CB  1 
ATOM   988  C  CG  . HIS A 1 122 ? -15.380 6.382   17.641  1.00 5.91  ? 122 HIS A CG  1 
ATOM   989  N  ND1 . HIS A 1 122 ? -15.066 5.047   17.917  1.00 6.82  ? 122 HIS A ND1 1 
ATOM   990  C  CD2 . HIS A 1 122 ? -16.618 6.377   17.031  1.00 8.31  ? 122 HIS A CD2 1 
ATOM   991  C  CE1 . HIS A 1 122 ? -16.079 4.289   17.477  1.00 8.44  ? 122 HIS A CE1 1 
ATOM   992  N  NE2 . HIS A 1 122 ? -17.009 5.057   16.916  1.00 9.32  ? 122 HIS A NE2 1 
ATOM   993  N  N   . TRP A 1 123 ? -12.456 9.996   17.655  1.00 6.77  ? 123 TRP A N   1 
ATOM   994  C  CA  . TRP A 1 123 ? -11.629 11.004  18.378  1.00 6.30  ? 123 TRP A CA  1 
ATOM   995  C  C   . TRP A 1 123 ? -12.533 12.006  19.112  1.00 7.35  ? 123 TRP A C   1 
ATOM   996  O  O   . TRP A 1 123 ? -13.654 12.361  18.669  1.00 8.61  ? 123 TRP A O   1 
ATOM   997  C  CB  . TRP A 1 123 ? -10.657 11.780  17.451  1.00 7.84  ? 123 TRP A CB  1 
ATOM   998  C  CG  . TRP A 1 123 ? -11.286 12.350  16.249  1.00 10.60 ? 123 TRP A CG  1 
ATOM   999  C  CD1 . TRP A 1 123 ? -11.469 11.735  15.031  1.00 10.29 ? 123 TRP A CD1 1 
ATOM   1000 C  CD2 . TRP A 1 123 ? -11.749 13.690  16.118  1.00 10.84 ? 123 TRP A CD2 1 
ATOM   1001 N  NE1 . TRP A 1 123 ? -12.066 12.607  14.133  1.00 10.44 ? 123 TRP A NE1 1 
ATOM   1002 C  CE2 . TRP A 1 123 ? -12.267 13.813  14.777  1.00 10.11 ? 123 TRP A CE2 1 
ATOM   1003 C  CE3 . TRP A 1 123 ? -11.787 14.816  17.003  1.00 10.48 ? 123 TRP A CE3 1 
ATOM   1004 C  CZ2 . TRP A 1 123 ? -12.774 14.998  14.311  1.00 12.00 ? 123 TRP A CZ2 1 
ATOM   1005 C  CZ3 . TRP A 1 123 ? -12.329 15.999  16.489  1.00 9.85  ? 123 TRP A CZ3 1 
ATOM   1006 C  CH2 . TRP A 1 123 ? -12.808 16.078  15.154  1.00 12.58 ? 123 TRP A CH2 1 
ATOM   1007 N  N   . ASN A 1 124 ? -11.998 12.504  20.248  1.00 7.28  ? 124 ASN A N   1 
ATOM   1008 C  CA  . ASN A 1 124 ? -12.794 13.365  21.148  1.00 7.47  ? 124 ASN A CA  1 
ATOM   1009 C  C   . ASN A 1 124 ? -12.910 14.783  20.528  1.00 8.77  ? 124 ASN A C   1 
ATOM   1010 O  O   . ASN A 1 124 ? -11.890 15.464  20.296  1.00 9.40  ? 124 ASN A O   1 
ATOM   1011 C  CB  . ASN A 1 124 ? -11.997 13.452  22.461  1.00 7.17  ? 124 ASN A CB  1 
ATOM   1012 C  CG  . ASN A 1 124 ? -12.793 14.076  23.595  1.00 8.83  ? 124 ASN A CG  1 
ATOM   1013 O  OD1 . ASN A 1 124 ? -13.644 14.938  23.364  1.00 10.37 ? 124 ASN A OD1 1 
ATOM   1014 N  ND2 . ASN A 1 124 ? -12.570 13.568  24.822  1.00 11.75 ? 124 ASN A ND2 1 
ATOM   1015 N  N   . THR A 1 125 ? -14.154 15.201  20.291  1.00 9.63  ? 125 THR A N   1 
ATOM   1016 C  CA  . THR A 1 125 ? -14.345 16.449  19.575  1.00 10.85 ? 125 THR A CA  1 
ATOM   1017 C  C   . THR A 1 125 ? -13.821 17.681  20.346  1.00 11.50 ? 125 THR A C   1 
ATOM   1018 O  O   . THR A 1 125 ? -13.664 18.758  19.766  1.00 13.36 ? 125 THR A O   1 
ATOM   1019 C  CB  . THR A 1 125 ? -15.856 16.668  19.261  1.00 12.25 ? 125 THR A CB  1 
ATOM   1020 O  OG1 . THR A 1 125 ? -16.606 16.703  20.496  1.00 16.38 ? 125 THR A OG1 1 
ATOM   1021 C  CG2 . THR A 1 125 ? -16.383 15.510  18.376  1.00 12.45 ? 125 THR A CG2 1 
ATOM   1022 N  N   . LYS A 1 126 ? -13.546 17.453  21.770  1.00 11.35 ? 127 LYS A N   1 
ATOM   1023 C  CA  . LYS A 1 126 ? -13.036 18.661  22.486  1.00 13.98 ? 127 LYS A CA  1 
ATOM   1024 C  C   . LYS A 1 126 ? -11.629 19.026  21.960  1.00 13.05 ? 127 LYS A C   1 
ATOM   1025 O  O   . LYS A 1 126 ? -11.095 20.151  22.288  1.00 15.78 ? 127 LYS A O   1 
ATOM   1026 C  CB  . LYS A 1 126 ? -13.071 18.463  23.964  1.00 17.15 ? 127 LYS A CB  1 
ATOM   1027 C  CG  . LYS A 1 126 ? -12.056 17.573  24.542  1.00 19.80 ? 127 LYS A CG  1 
ATOM   1028 C  CD  . LYS A 1 126 ? -12.352 17.424  26.106  1.00 25.87 ? 127 LYS A CD  1 
ATOM   1029 C  CE  . LYS A 1 126 ? -11.440 16.447  26.796  1.00 30.43 ? 127 LYS A CE  1 
ATOM   1030 N  NZ  . LYS A 1 126 ? -10.583 16.978  27.972  1.00 31.43 ? 127 LYS A NZ  1 
ATOM   1031 N  N   . TYR A 1 127 ? -10.978 18.104  21.197  1.00 10.08 ? 128 TYR A N   1 
ATOM   1032 C  CA  . TYR A 1 127 ? -9.596  18.391  20.702  1.00 10.72 ? 128 TYR A CA  1 
ATOM   1033 C  C   . TYR A 1 127 ? -9.541  18.789  19.199  1.00 10.86 ? 128 TYR A C   1 
ATOM   1034 O  O   . TYR A 1 127 ? -8.416  19.037  18.629  1.00 11.37 ? 128 TYR A O   1 
ATOM   1035 C  CB  . TYR A 1 127 ? -8.583  17.213  20.955  1.00 10.25 ? 128 TYR A CB  1 
ATOM   1036 C  CG  . TYR A 1 127 ? -8.545  16.907  22.387  1.00 8.83  ? 128 TYR A CG  1 
ATOM   1037 C  CD1 . TYR A 1 127 ? -8.143  17.877  23.314  1.00 11.52 ? 128 TYR A CD1 1 
ATOM   1038 C  CD2 . TYR A 1 127 ? -8.872  15.634  22.914  1.00 8.25  ? 128 TYR A CD2 1 
ATOM   1039 C  CE1 . TYR A 1 127 ? -8.118  17.603  24.687  1.00 11.11 ? 128 TYR A CE1 1 
ATOM   1040 C  CE2 . TYR A 1 127 ? -8.778  15.326  24.302  1.00 9.03  ? 128 TYR A CE2 1 
ATOM   1041 C  CZ  . TYR A 1 127 ? -8.381  16.350  25.193  1.00 10.15 ? 128 TYR A CZ  1 
ATOM   1042 O  OH  . TYR A 1 127 ? -8.358  16.201  26.529  1.00 13.31 ? 128 TYR A OH  1 
ATOM   1043 N  N   . GLY A 1 128 ? -10.709 18.857  18.559  1.00 10.75 ? 129 GLY A N   1 
ATOM   1044 C  CA  . GLY A 1 128 ? -10.777 19.511  17.241  1.00 11.66 ? 129 GLY A CA  1 
ATOM   1045 C  C   . GLY A 1 128 ? -10.397 18.670  16.013  1.00 11.42 ? 129 GLY A C   1 
ATOM   1046 O  O   . GLY A 1 128 ? -11.038 18.830  14.926  1.00 14.12 ? 129 GLY A O   1 
ATOM   1047 N  N   . ASP A 1 129 ? -9.348  17.814  16.126  1.00 11.78 ? 130 ASP A N   1 
ATOM   1048 C  CA  . ASP A 1 129 ? -9.017  16.922  15.030  1.00 12.19 ? 130 ASP A CA  1 
ATOM   1049 C  C   . ASP A 1 129 ? -8.285  15.689  15.596  1.00 12.07 ? 130 ASP A C   1 
ATOM   1050 O  O   . ASP A 1 129 ? -7.847  15.712  16.764  1.00 12.86 ? 130 ASP A O   1 
ATOM   1051 C  CB  . ASP A 1 129 ? -8.285  17.633  13.845  1.00 14.68 ? 130 ASP A CB  1 
ATOM   1052 C  CG  . ASP A 1 129 ? -6.879  18.041  14.172  1.00 17.95 ? 130 ASP A CG  1 
ATOM   1053 O  OD1 . ASP A 1 129 ? -6.156  17.432  14.949  1.00 21.69 ? 130 ASP A OD1 1 
ATOM   1054 O  OD2 . ASP A 1 129 ? -6.340  18.959  13.625  1.00 24.02 ? 130 ASP A OD2 1 
ATOM   1055 N  N   . PHE A 1 130 ? -8.167  14.656  14.754  1.00 12.14 ? 131 PHE A N   1 
ATOM   1056 C  CA  . PHE A 1 130 ? -7.513  13.422  15.172  1.00 12.80 ? 131 PHE A CA  1 
ATOM   1057 C  C   . PHE A 1 130 ? -6.099  13.686  15.588  1.00 11.65 ? 131 PHE A C   1 
ATOM   1058 O  O   . PHE A 1 130 ? -5.664  13.079  16.609  1.00 12.25 ? 131 PHE A O   1 
ATOM   1059 C  CB  . PHE A 1 130 ? -7.602  12.386  14.011  1.00 11.67 ? 131 PHE A CB  1 
ATOM   1060 C  CG  . PHE A 1 130 ? -6.995  11.056  14.311  1.00 12.44 ? 131 PHE A CG  1 
ATOM   1061 C  CD1 . PHE A 1 130 ? -7.717  10.020  14.972  1.00 10.43 ? 131 PHE A CD1 1 
ATOM   1062 C  CD2 . PHE A 1 130 ? -5.652  10.854  14.029  1.00 14.47 ? 131 PHE A CD2 1 
ATOM   1063 C  CE1 . PHE A 1 130 ? -7.090  8.851   15.244  1.00 10.95 ? 131 PHE A CE1 1 
ATOM   1064 C  CE2 . PHE A 1 130 ? -5.052  9.648   14.325  1.00 17.92 ? 131 PHE A CE2 1 
ATOM   1065 C  CZ  . PHE A 1 130 ? -5.781  8.646   14.935  1.00 14.54 ? 131 PHE A CZ  1 
ATOM   1066 N  N   . GLY A 1 131 ? -5.341  14.468  14.788  1.00 12.27 ? 132 GLY A N   1 
ATOM   1067 C  CA  . GLY A 1 131 ? -3.935  14.621  15.101  1.00 13.35 ? 132 GLY A CA  1 
ATOM   1068 C  C   . GLY A 1 131 ? -3.684  15.226  16.468  1.00 12.29 ? 132 GLY A C   1 
ATOM   1069 O  O   . GLY A 1 131 ? -2.662  14.923  17.158  1.00 13.73 ? 132 GLY A O   1 
ATOM   1070 N  N   . LYS A 1 132 ? -4.568  16.158  16.860  1.00 11.79 ? 133 LYS A N   1 
ATOM   1071 C  CA  . LYS A 1 132 ? -4.403  16.711  18.207  1.00 10.54 ? 133 LYS A CA  1 
ATOM   1072 C  C   . LYS A 1 132 ? -4.904  15.773  19.299  1.00 9.49  ? 133 LYS A C   1 
ATOM   1073 O  O   . LYS A 1 132 ? -4.322  15.679  20.450  1.00 10.14 ? 133 LYS A O   1 
ATOM   1074 C  CB  . LYS A 1 132 ? -5.139  18.048  18.356  1.00 11.73 ? 133 LYS A CB  1 
ATOM   1075 C  CG  . LYS A 1 132 ? -4.527  19.199  17.583  1.00 15.95 ? 133 LYS A CG  1 
ATOM   1076 C  CD  . LYS A 1 132 ? -3.135  19.581  18.250  1.00 18.55 ? 133 LYS A CD  1 
ATOM   1077 C  CE  . LYS A 1 132 ? -2.731  20.943  17.580  1.00 24.68 ? 133 LYS A CE  1 
ATOM   1078 N  NZ  . LYS A 1 132 ? -3.384  20.722  16.157  1.00 34.90 ? 133 LYS A NZ  1 
ATOM   1079 N  N   . ALA A 1 133 ? -6.016  15.074  19.006  1.00 8.48  ? 134 ALA A N   1 
ATOM   1080 C  CA  . ALA A 1 133 ? -6.559  14.097  19.967  1.00 9.19  ? 134 ALA A CA  1 
ATOM   1081 C  C   . ALA A 1 133 ? -5.552  13.013  20.362  1.00 9.65  ? 134 ALA A C   1 
ATOM   1082 O  O   . ALA A 1 133 ? -5.521  12.646  21.540  1.00 10.21 ? 134 ALA A O   1 
ATOM   1083 C  CB  . ALA A 1 133 ? -7.841  13.388  19.381  1.00 8.00  ? 134 ALA A CB  1 
ATOM   1084 N  N   . VAL A 1 134 ? -4.733  12.532  19.424  1.00 9.01  ? 135 VAL A N   1 
ATOM   1085 C  CA  . VAL A 1 134 ? -3.834  11.408  19.799  1.00 10.42 ? 135 VAL A CA  1 
ATOM   1086 C  C   . VAL A 1 134 ? -2.743  11.858  20.820  1.00 9.68  ? 135 VAL A C   1 
ATOM   1087 O  O   . VAL A 1 134 ? -2.028  11.011  21.368  1.00 10.72 ? 135 VAL A O   1 
ATOM   1088 C  CB  . VAL A 1 134 ? -3.153  10.658  18.594  1.00 10.70 ? 135 VAL A CB  1 
ATOM   1089 C  CG1 . VAL A 1 134 ? -4.182  9.965   17.796  1.00 13.28 ? 135 VAL A CG1 1 
ATOM   1090 C  CG2 . VAL A 1 134 ? -2.267  11.554  17.749  1.00 12.92 ? 135 VAL A CG2 1 
ATOM   1091 N  N   A GLN A 1 135 ? -2.604  13.192  21.011  0.50 10.03 ? 136 GLN A N   1 
ATOM   1092 N  N   B GLN A 1 135 ? -2.594  13.180  21.052  0.50 9.93  ? 136 GLN A N   1 
ATOM   1093 C  CA  A GLN A 1 135 ? -1.617  13.718  21.937  0.50 11.03 ? 136 GLN A CA  1 
ATOM   1094 C  CA  B GLN A 1 135 ? -1.573  13.635  21.988  0.50 10.51 ? 136 GLN A CA  1 
ATOM   1095 C  C   A GLN A 1 135 ? -2.214  13.918  23.326  0.50 9.69  ? 136 GLN A C   1 
ATOM   1096 C  C   B GLN A 1 135 ? -2.134  13.714  23.408  0.50 9.47  ? 136 GLN A C   1 
ATOM   1097 O  O   A GLN A 1 135 ? -1.590  14.608  24.185  0.50 10.48 ? 136 GLN A O   1 
ATOM   1098 O  O   B GLN A 1 135 ? -1.397  14.074  24.370  0.50 10.69 ? 136 GLN A O   1 
ATOM   1099 C  CB  A GLN A 1 135 ? -1.080  15.067  21.367  0.50 11.92 ? 136 GLN A CB  1 
ATOM   1100 C  CB  B GLN A 1 135 ? -1.068  15.013  21.497  0.50 11.59 ? 136 GLN A CB  1 
ATOM   1101 C  CG  A GLN A 1 135 ? -0.256  14.889  20.054  0.50 15.16 ? 136 GLN A CG  1 
ATOM   1102 C  CG  B GLN A 1 135 ? -0.672  14.978  19.996  0.50 13.96 ? 136 GLN A CG  1 
ATOM   1103 C  CD  A GLN A 1 135 ? 0.971   13.986  20.244  0.50 18.73 ? 136 GLN A CD  1 
ATOM   1104 C  CD  B GLN A 1 135 ? -0.036  16.224  19.549  0.50 15.66 ? 136 GLN A CD  1 
ATOM   1105 O  OE1 A GLN A 1 135 ? 1.587   14.004  21.305  0.50 21.53 ? 136 GLN A OE1 1 
ATOM   1106 O  OE1 B GLN A 1 135 ? 0.850   16.753  20.216  0.50 20.14 ? 136 GLN A OE1 1 
ATOM   1107 N  NE2 A GLN A 1 135 ? 1.366   13.236  19.186  0.50 20.05 ? 136 GLN A NE2 1 
ATOM   1108 N  NE2 B GLN A 1 135 ? -0.508  16.743  18.416  0.50 14.70 ? 136 GLN A NE2 1 
ATOM   1109 N  N   . GLN A 1 136 ? -3.420  13.362  23.554  1.00 9.38  ? 137 GLN A N   1 
ATOM   1110 C  CA  . GLN A 1 136 ? -4.117  13.519  24.856  1.00 10.03 ? 137 GLN A CA  1 
ATOM   1111 C  C   . GLN A 1 136 ? -4.538  12.193  25.481  1.00 10.05 ? 137 GLN A C   1 
ATOM   1112 O  O   . GLN A 1 136 ? -4.902  11.263  24.735  1.00 8.83  ? 137 GLN A O   1 
ATOM   1113 C  CB  . GLN A 1 136 ? -5.357  14.362  24.705  1.00 9.54  ? 137 GLN A CB  1 
ATOM   1114 C  CG  . GLN A 1 136 ? -5.082  15.720  23.937  1.00 14.12 ? 137 GLN A CG  1 
ATOM   1115 C  CD  . GLN A 1 136 ? -4.199  16.658  24.779  1.00 16.03 ? 137 GLN A CD  1 
ATOM   1116 O  OE1 . GLN A 1 136 ? -4.116  16.519  25.998  1.00 19.71 ? 137 GLN A OE1 1 
ATOM   1117 N  NE2 . GLN A 1 136 ? -3.511  17.569  24.111  1.00 25.65 ? 137 GLN A NE2 1 
ATOM   1118 N  N   . PRO A 1 137 ? -4.522  12.114  26.821  1.00 9.59  ? 138 PRO A N   1 
ATOM   1119 C  CA  . PRO A 1 137 ? -4.787  10.806  27.466  1.00 11.23 ? 138 PRO A CA  1 
ATOM   1120 C  C   . PRO A 1 137 ? -6.217  10.324  27.273  1.00 10.60 ? 138 PRO A C   1 
ATOM   1121 O  O   . PRO A 1 137 ? -6.459  9.093   27.390  1.00 13.52 ? 138 PRO A O   1 
ATOM   1122 C  CB  . PRO A 1 137 ? -4.464  11.017  28.943  1.00 12.19 ? 138 PRO A CB  1 
ATOM   1123 C  CG  . PRO A 1 137 ? -4.372  12.524  29.093  1.00 14.20 ? 138 PRO A CG  1 
ATOM   1124 C  CD  . PRO A 1 137 ? -4.074  13.142  27.780  1.00 11.70 ? 138 PRO A CD  1 
ATOM   1125 N  N   . ASP A 1 138 ? -7.132  11.260  26.960  1.00 8.58  ? 139 ASP A N   1 
ATOM   1126 C  CA  . ASP A 1 138 ? -8.536  10.872  26.680  1.00 10.05 ? 139 ASP A CA  1 
ATOM   1127 C  C   . ASP A 1 138 ? -8.906  11.282  25.210  1.00 8.89  ? 139 ASP A C   1 
ATOM   1128 O  O   . ASP A 1 138 ? -10.022 11.739  24.951  1.00 10.45 ? 139 ASP A O   1 
ATOM   1129 C  CB  . ASP A 1 138 ? -9.543  11.552  27.670  1.00 10.40 ? 139 ASP A CB  1 
ATOM   1130 C  CG  . ASP A 1 138 ? -9.409  13.085  27.716  1.00 11.73 ? 139 ASP A CG  1 
ATOM   1131 O  OD1 . ASP A 1 138 ? -8.389  13.637  27.123  1.00 13.36 ? 139 ASP A OD1 1 
ATOM   1132 O  OD2 . ASP A 1 138 ? -10.270 13.748  28.365  1.00 16.42 ? 139 ASP A OD2 1 
ATOM   1133 N  N   . GLY A 1 139 ? -7.946  11.184  24.274  1.00 8.30  ? 140 GLY A N   1 
ATOM   1134 C  CA  . GLY A 1 139 ? -8.165  11.669  22.933  1.00 7.04  ? 140 GLY A CA  1 
ATOM   1135 C  C   . GLY A 1 139 ? -9.005  10.779  22.065  1.00 7.02  ? 140 GLY A C   1 
ATOM   1136 O  O   . GLY A 1 139 ? -9.731  11.264  21.186  1.00 7.77  ? 140 GLY A O   1 
ATOM   1137 N  N   . LEU A 1 140 ? -8.849  9.437   22.266  1.00 6.26  ? 141 LEU A N   1 
ATOM   1138 C  CA  . LEU A 1 140 ? -9.549  8.481   21.352  1.00 6.54  ? 141 LEU A CA  1 
ATOM   1139 C  C   . LEU A 1 140 ? -10.416 7.524   22.131  1.00 6.63  ? 141 LEU A C   1 
ATOM   1140 O  O   . LEU A 1 140 ? -10.161 7.275   23.326  1.00 6.75  ? 141 LEU A O   1 
ATOM   1141 C  CB  . LEU A 1 140 ? -8.544  7.579   20.633  1.00 7.80  ? 141 LEU A CB  1 
ATOM   1142 C  CG  . LEU A 1 140 ? -7.659  8.221   19.606  1.00 10.67 ? 141 LEU A CG  1 
ATOM   1143 C  CD1 . LEU A 1 140 ? -6.923  7.166   18.764  1.00 9.71  ? 141 LEU A CD1 1 
ATOM   1144 C  CD2 . LEU A 1 140 ? -8.187  9.356   18.707  1.00 14.13 ? 141 LEU A CD2 1 
ATOM   1145 N  N   . ALA A 1 141 ? -11.486 7.069   21.431  1.00 6.55  ? 142 ALA A N   1 
ATOM   1146 C  CA  . ALA A 1 141 ? -12.273 5.951   22.001  1.00 5.57  ? 142 ALA A CA  1 
ATOM   1147 C  C   . ALA A 1 141 ? -12.338 4.911   20.885  1.00 5.86  ? 142 ALA A C   1 
ATOM   1148 O  O   . ALA A 1 141 ? -12.707 5.263   19.771  1.00 7.85  ? 142 ALA A O   1 
ATOM   1149 C  CB  . ALA A 1 141 ? -13.649 6.396   22.433  1.00 7.71  ? 142 ALA A CB  1 
ATOM   1150 N  N   . VAL A 1 142 ? -11.763 3.685   21.181  1.00 7.19  ? 143 VAL A N   1 
ATOM   1151 C  CA  . VAL A 1 142 ? -11.791 2.655   20.167  1.00 5.88  ? 143 VAL A CA  1 
ATOM   1152 C  C   . VAL A 1 142 ? -12.796 1.570   20.627  1.00 6.70  ? 143 VAL A C   1 
ATOM   1153 O  O   . VAL A 1 142 ? -12.654 1.073   21.739  1.00 6.68  ? 143 VAL A O   1 
ATOM   1154 C  CB  . VAL A 1 142 ? -10.402 2.070   19.808  1.00 6.65  ? 143 VAL A CB  1 
ATOM   1155 C  CG1 . VAL A 1 142 ? -10.536 0.997   18.684  1.00 6.50  ? 143 VAL A CG1 1 
ATOM   1156 C  CG2 . VAL A 1 142 ? -9.420  3.198   19.363  1.00 8.44  ? 143 VAL A CG2 1 
ATOM   1157 N  N   . LEU A 1 143 ? -13.749 1.269   19.723  1.00 5.67  ? 144 LEU A N   1 
ATOM   1158 C  CA  . LEU A 1 143 ? -14.767 0.255   20.023  1.00 6.22  ? 144 LEU A CA  1 
ATOM   1159 C  C   . LEU A 1 143 ? -14.189 -0.993  19.348  1.00 7.16  ? 144 LEU A C   1 
ATOM   1160 O  O   . LEU A 1 143 ? -14.061 -1.063  18.089  1.00 6.95  ? 144 LEU A O   1 
ATOM   1161 C  CB  . LEU A 1 143 ? -16.149 0.690   19.443  1.00 7.42  ? 144 LEU A CB  1 
ATOM   1162 C  CG  . LEU A 1 143 ? -17.278 -0.319  19.575  1.00 8.08  ? 144 LEU A CG  1 
ATOM   1163 C  CD1 . LEU A 1 143 ? -17.459 -0.686  21.064  1.00 10.74 ? 144 LEU A CD1 1 
ATOM   1164 C  CD2 . LEU A 1 143 ? -18.561 0.214   18.916  1.00 9.44  ? 144 LEU A CD2 1 
ATOM   1165 N  N   . GLY A 1 144 ? -13.931 -2.026  20.171  1.00 6.29  ? 145 GLY A N   1 
ATOM   1166 C  CA  . GLY A 1 144 ? -13.358 -3.263  19.635  1.00 6.26  ? 145 GLY A CA  1 
ATOM   1167 C  C   . GLY A 1 144 ? -14.436 -4.362  19.632  1.00 5.51  ? 145 GLY A C   1 
ATOM   1168 O  O   . GLY A 1 144 ? -15.200 -4.517  20.615  1.00 6.79  ? 145 GLY A O   1 
ATOM   1169 N  N   . ILE A 1 145 ? -14.490 -5.134  18.510  1.00 5.63  ? 146 ILE A N   1 
ATOM   1170 C  CA  . ILE A 1 145 ? -15.544 -6.153  18.388  1.00 6.03  ? 146 ILE A CA  1 
ATOM   1171 C  C   . ILE A 1 145 ? -14.798 -7.406  17.864  1.00 6.52  ? 146 ILE A C   1 
ATOM   1172 O  O   . ILE A 1 145 ? -14.151 -7.392  16.828  1.00 7.27  ? 146 ILE A O   1 
ATOM   1173 C  CB  . ILE A 1 145 ? -16.642 -5.671  17.388  1.00 7.47  ? 146 ILE A CB  1 
ATOM   1174 C  CG1 . ILE A 1 145 ? -17.253 -4.361  17.898  1.00 7.70  ? 146 ILE A CG1 1 
ATOM   1175 C  CG2 . ILE A 1 145 ? -17.691 -6.806  17.177  1.00 8.95  ? 146 ILE A CG2 1 
ATOM   1176 C  CD1 . ILE A 1 145 ? -18.410 -3.805  16.968  1.00 7.67  ? 146 ILE A CD1 1 
ATOM   1177 N  N   . PHE A 1 146 ? -15.016 -8.538  18.542  1.00 5.87  ? 147 PHE A N   1 
ATOM   1178 C  CA  . PHE A 1 146 ? -14.341 -9.787  18.124  1.00 6.43  ? 147 PHE A CA  1 
ATOM   1179 C  C   . PHE A 1 146 ? -15.123 -10.403 16.961  1.00 6.08  ? 147 PHE A C   1 
ATOM   1180 O  O   . PHE A 1 146 ? -16.391 -10.316 16.880  1.00 7.23  ? 147 PHE A O   1 
ATOM   1181 C  CB  . PHE A 1 146 ? -14.395 -10.761 19.274  1.00 6.47  ? 147 PHE A CB  1 
ATOM   1182 C  CG  . PHE A 1 146 ? -13.566 -10.307 20.444  1.00 4.34  ? 147 PHE A CG  1 
ATOM   1183 C  CD1 . PHE A 1 146 ? -12.179 -10.146 20.279  1.00 5.32  ? 147 PHE A CD1 1 
ATOM   1184 C  CD2 . PHE A 1 146 ? -14.151 -10.061 21.681  1.00 7.59  ? 147 PHE A CD2 1 
ATOM   1185 C  CE1 . PHE A 1 146 ? -11.364 -9.739  21.349  1.00 5.89  ? 147 PHE A CE1 1 
ATOM   1186 C  CE2 . PHE A 1 146 ? -13.331 -9.660  22.770  1.00 6.19  ? 147 PHE A CE2 1 
ATOM   1187 C  CZ  . PHE A 1 146 ? -11.925 -9.520  22.597  1.00 6.36  ? 147 PHE A CZ  1 
ATOM   1188 N  N   . LEU A 1 147 ? -14.386 -11.103 16.098  1.00 6.98  ? 148 LEU A N   1 
ATOM   1189 C  CA  . LEU A 1 147 ? -15.018 -11.884 15.020  1.00 7.16  ? 148 LEU A CA  1 
ATOM   1190 C  C   . LEU A 1 147 ? -14.682 -13.382 15.265  1.00 7.99  ? 148 LEU A C   1 
ATOM   1191 O  O   . LEU A 1 147 ? -13.495 -13.729 15.434  1.00 7.51  ? 148 LEU A O   1 
ATOM   1192 C  CB  . LEU A 1 147 ? -14.431 -11.540 13.630  1.00 6.85  ? 148 LEU A CB  1 
ATOM   1193 C  CG  . LEU A 1 147 ? -14.972 -10.260 12.950  1.00 7.25  ? 148 LEU A CG  1 
ATOM   1194 C  CD1 . LEU A 1 147 ? -14.769 -9.001  13.877  1.00 9.53  ? 148 LEU A CD1 1 
ATOM   1195 C  CD2 . LEU A 1 147 ? -14.379 -10.029 11.563  1.00 9.91  ? 148 LEU A CD2 1 
ATOM   1196 N  N   . LYS A 1 148 ? -15.721 -14.218 15.216  1.00 7.47  ? 149 LYS A N   1 
ATOM   1197 C  CA  . LYS A 1 148 ? -15.538 -15.646 15.141  1.00 9.30  ? 149 LYS A CA  1 
ATOM   1198 C  C   . LYS A 1 148 ? -16.014 -16.154 13.775  1.00 9.52  ? 149 LYS A C   1 
ATOM   1199 O  O   . LYS A 1 148 ? -16.845 -15.523 13.142  1.00 9.45  ? 149 LYS A O   1 
ATOM   1200 C  CB  . LYS A 1 148 ? -16.337 -16.394 16.274  1.00 9.39  ? 149 LYS A CB  1 
ATOM   1201 C  CG  . LYS A 1 148 ? -17.817 -16.251 16.188  1.00 11.88 ? 149 LYS A CG  1 
ATOM   1202 C  CD  . LYS A 1 148 ? -18.524 -16.886 17.444  1.00 16.16 ? 149 LYS A CD  1 
ATOM   1203 C  CE  . LYS A 1 148 ? -19.975 -17.240 17.185  1.00 23.77 ? 149 LYS A CE  1 
ATOM   1204 N  NZ  . LYS A 1 148 ? -20.579 -17.880 18.460  1.00 24.84 ? 149 LYS A NZ  1 
ATOM   1205 N  N   . VAL A 1 149 ? -15.556 -17.337 13.369  1.00 9.78  ? 150 VAL A N   1 
ATOM   1206 C  CA  . VAL A 1 149 ? -15.914 -17.880 12.068  1.00 9.85  ? 150 VAL A CA  1 
ATOM   1207 C  C   . VAL A 1 149 ? -17.130 -18.847 12.257  1.00 10.81 ? 150 VAL A C   1 
ATOM   1208 O  O   . VAL A 1 149 ? -17.110 -19.814 13.094  1.00 13.16 ? 150 VAL A O   1 
ATOM   1209 C  CB  . VAL A 1 149 ? -14.739 -18.665 11.487  1.00 10.57 ? 150 VAL A CB  1 
ATOM   1210 C  CG1 . VAL A 1 149 ? -15.129 -19.437 10.200  1.00 12.40 ? 150 VAL A CG1 1 
ATOM   1211 C  CG2 . VAL A 1 149 ? -13.689 -17.674 11.123  1.00 13.29 ? 150 VAL A CG2 1 
ATOM   1212 N  N   . GLY A 1 150 ? -18.133 -18.632 11.449  1.00 10.08 ? 151 GLY A N   1 
ATOM   1213 C  CA  . GLY A 1 150 ? -19.398 -19.426 11.547  1.00 11.63 ? 151 GLY A CA  1 
ATOM   1214 C  C   . GLY A 1 150 ? -20.271 -18.976 10.395  1.00 10.50 ? 151 GLY A C   1 
ATOM   1215 O  O   . GLY A 1 150 ? -19.894 -19.088 9.219   1.00 10.75 ? 151 GLY A O   1 
ATOM   1216 N  N   . SER A 1 151 ? -21.457 -18.481 10.743  1.00 12.48 ? 152 SER A N   1 
ATOM   1217 C  CA  . SER A 1 151 ? -22.352 -17.922 9.678   1.00 12.81 ? 152 SER A CA  1 
ATOM   1218 C  C   . SER A 1 151 ? -21.784 -16.587 9.117   1.00 12.90 ? 152 SER A C   1 
ATOM   1219 O  O   . SER A 1 151 ? -21.052 -15.918 9.837   1.00 13.47 ? 152 SER A O   1 
ATOM   1220 C  CB  . SER A 1 151 ? -23.719 -17.710 10.246  1.00 18.68 ? 152 SER A CB  1 
ATOM   1221 O  OG  . SER A 1 151 ? -23.714 -16.717 11.218  1.00 25.60 ? 152 SER A OG  1 
ATOM   1222 N  N   . ALA A 1 152 ? -22.127 -16.243 7.858   1.00 11.00 ? 153 ALA A N   1 
ATOM   1223 C  CA  . ALA A 1 152 ? -21.684 -14.999 7.282   1.00 11.82 ? 153 ALA A CA  1 
ATOM   1224 C  C   . ALA A 1 152 ? -22.299 -13.794 8.020   1.00 11.36 ? 153 ALA A C   1 
ATOM   1225 O  O   . ALA A 1 152 ? -23.420 -13.878 8.550   1.00 12.52 ? 153 ALA A O   1 
ATOM   1226 C  CB  . ALA A 1 152 ? -22.076 -14.891 5.780   1.00 12.69 ? 153 ALA A CB  1 
ATOM   1227 N  N   . LYS A 1 153 ? -21.588 -12.631 7.907   1.00 11.40 ? 154 LYS A N   1 
ATOM   1228 C  CA  . LYS A 1 153 ? -22.139 -11.372 8.393   1.00 12.11 ? 154 LYS A CA  1 
ATOM   1229 C  C   . LYS A 1 153 ? -22.565 -10.620 7.117   1.00 12.72 ? 154 LYS A C   1 
ATOM   1230 O  O   . LYS A 1 153 ? -21.715 -10.166 6.340   1.00 11.40 ? 154 LYS A O   1 
ATOM   1231 C  CB  . LYS A 1 153 ? -21.074 -10.570 9.175   1.00 12.75 ? 154 LYS A CB  1 
ATOM   1232 C  CG  . LYS A 1 153 ? -21.619 -9.351  9.876   1.00 16.31 ? 154 LYS A CG  1 
ATOM   1233 C  CD  . LYS A 1 153 ? -22.551 -9.800  11.030  1.00 14.71 ? 154 LYS A CD  1 
ATOM   1234 C  CE  . LYS A 1 153 ? -22.778 -8.718  12.110  1.00 19.35 ? 154 LYS A CE  1 
ATOM   1235 N  NZ  . LYS A 1 153 ? -23.909 -8.998  13.066  1.00 23.32 ? 154 LYS A NZ  1 
ATOM   1236 N  N   . PRO A 1 154 ? -23.884 -10.566 6.852   1.00 14.57 ? 155 PRO A N   1 
ATOM   1237 C  CA  . PRO A 1 154 ? -24.268 -9.954  5.523   1.00 14.37 ? 155 PRO A CA  1 
ATOM   1238 C  C   . PRO A 1 154 ? -23.768 -8.500  5.387   1.00 13.65 ? 155 PRO A C   1 
ATOM   1239 O  O   . PRO A 1 154 ? -23.323 -8.086  4.299   1.00 16.85 ? 155 PRO A O   1 
ATOM   1240 C  CB  . PRO A 1 154 ? -25.827 -9.970  5.535   1.00 14.64 ? 155 PRO A CB  1 
ATOM   1241 C  CG  . PRO A 1 154 ? -26.118 -11.181 6.582   1.00 18.78 ? 155 PRO A CG  1 
ATOM   1242 C  CD  . PRO A 1 154 ? -25.046 -11.049 7.639   1.00 12.91 ? 155 PRO A CD  1 
ATOM   1243 N  N   . GLY A 1 155 ? -23.721 -7.798  6.515   1.00 13.50 ? 156 GLY A N   1 
ATOM   1244 C  CA  . GLY A 1 155 ? -23.316 -6.354  6.540   1.00 12.92 ? 156 GLY A CA  1 
ATOM   1245 C  C   . GLY A 1 155 ? -21.843 -6.139  6.256   1.00 14.23 ? 156 GLY A C   1 
ATOM   1246 O  O   . GLY A 1 155 ? -21.387 -4.994  6.065   1.00 16.81 ? 156 GLY A O   1 
ATOM   1247 N  N   . LEU A 1 156 ? -21.063 -7.227  6.320   1.00 12.41 ? 157 LEU A N   1 
ATOM   1248 C  CA  . LEU A 1 156 ? -19.643 -7.203  5.947   1.00 11.04 ? 157 LEU A CA  1 
ATOM   1249 C  C   . LEU A 1 156 ? -19.349 -7.408  4.457   1.00 11.73 ? 157 LEU A C   1 
ATOM   1250 O  O   . LEU A 1 156 ? -18.226 -7.119  3.966   1.00 12.04 ? 157 LEU A O   1 
ATOM   1251 C  CB  . LEU A 1 156 ? -18.875 -8.246  6.777   1.00 11.56 ? 157 LEU A CB  1 
ATOM   1252 C  CG  . LEU A 1 156 ? -17.328 -8.346  6.597   1.00 10.87 ? 157 LEU A CG  1 
ATOM   1253 C  CD1 . LEU A 1 156 ? -16.605 -7.025  7.008   1.00 12.06 ? 157 LEU A CD1 1 
ATOM   1254 C  CD2 . LEU A 1 156 ? -16.700 -9.514  7.422   1.00 12.25 ? 157 LEU A CD2 1 
ATOM   1255 N  N   . GLN A 1 157 ? -20.334 -7.959  3.704   1.00 11.91 ? 158 GLN A N   1 
ATOM   1256 C  CA  . GLN A 1 157 ? -20.000 -8.456  2.371   1.00 12.05 ? 158 GLN A CA  1 
ATOM   1257 C  C   . GLN A 1 157 ? -19.562 -7.292  1.430   1.00 11.49 ? 158 GLN A C   1 
ATOM   1258 O  O   . GLN A 1 157 ? -18.681 -7.517  0.594   1.00 13.18 ? 158 GLN A O   1 
ATOM   1259 C  CB  . GLN A 1 157 ? -21.155 -9.271  1.747   1.00 14.56 ? 158 GLN A CB  1 
ATOM   1260 C  CG  . GLN A 1 157 ? -20.714 -9.989  0.436   1.00 16.13 ? 158 GLN A CG  1 
ATOM   1261 C  CD  . GLN A 1 157 ? -19.595 -11.045 0.704   1.00 14.63 ? 158 GLN A CD  1 
ATOM   1262 O  OE1 . GLN A 1 157 ? -19.416 -11.605 1.838   1.00 16.91 ? 158 GLN A OE1 1 
ATOM   1263 N  NE2 . GLN A 1 157 ? -18.799 -11.288 -0.327  1.00 17.23 ? 158 GLN A NE2 1 
ATOM   1264 N  N   A LYS A 1 158 ? -20.158 -6.076  1.525   0.50 13.98 ? 159 LYS A N   1 
ATOM   1265 N  N   B LYS A 1 158 ? -20.180 -6.111  1.601   0.50 13.89 ? 159 LYS A N   1 
ATOM   1266 C  CA  A LYS A 1 158 ? -19.676 -4.988  0.623   0.50 12.97 ? 159 LYS A CA  1 
ATOM   1267 C  CA  B LYS A 1 158 ? -19.809 -4.974  0.772   0.50 14.40 ? 159 LYS A CA  1 
ATOM   1268 C  C   A LYS A 1 158 ? -18.130 -4.752  0.826   0.50 13.01 ? 159 LYS A C   1 
ATOM   1269 C  C   B LYS A 1 158 ? -18.276 -4.609  0.897   0.50 14.27 ? 159 LYS A C   1 
ATOM   1270 O  O   A LYS A 1 158 ? -17.373 -4.508  -0.120  0.50 12.95 ? 159 LYS A O   1 
ATOM   1271 O  O   B LYS A 1 158 ? -17.675 -4.131  -0.054  0.50 14.19 ? 159 LYS A O   1 
ATOM   1272 C  CB  A LYS A 1 158 ? -20.512 -3.687  0.757   0.50 14.59 ? 159 LYS A CB  1 
ATOM   1273 C  CB  B LYS A 1 158 ? -20.765 -3.810  1.072   0.50 15.03 ? 159 LYS A CB  1 
ATOM   1274 C  CG  A LYS A 1 158 ? -20.082 -2.498  -0.167  0.50 15.88 ? 159 LYS A CG  1 
ATOM   1275 C  CG  B LYS A 1 158 ? -22.165 -3.993  0.431   0.50 16.35 ? 159 LYS A CG  1 
ATOM   1276 C  CD  A LYS A 1 158 ? -21.041 -2.002  -1.399  0.50 20.08 ? 159 LYS A CD  1 
ATOM   1277 C  CD  B LYS A 1 158 ? -23.023 -2.713  0.652   0.50 19.17 ? 159 LYS A CD  1 
ATOM   1278 C  CE  A LYS A 1 158 ? -21.078 -0.406  -1.622  0.50 17.49 ? 159 LYS A CE  1 
ATOM   1279 C  CE  B LYS A 1 158 ? -24.564 -2.964  0.528   0.50 20.76 ? 159 LYS A CE  1 
ATOM   1280 N  NZ  A LYS A 1 158 ? -20.836 0.253   -0.242  0.50 21.78 ? 159 LYS A NZ  1 
ATOM   1281 N  NZ  B LYS A 1 158 ? -25.277 -1.705  0.077   0.50 22.22 ? 159 LYS A NZ  1 
ATOM   1282 N  N   . VAL A 1 159 ? -17.685 -4.830  2.091   1.00 12.67 ? 160 VAL A N   1 
ATOM   1283 C  CA  . VAL A 1 159 ? -16.283 -4.576  2.347   1.00 12.63 ? 160 VAL A CA  1 
ATOM   1284 C  C   . VAL A 1 159 ? -15.474 -5.744  1.680   1.00 12.17 ? 160 VAL A C   1 
ATOM   1285 O  O   . VAL A 1 159 ? -14.510 -5.490  0.935   1.00 13.21 ? 160 VAL A O   1 
ATOM   1286 C  CB  . VAL A 1 159 ? -16.006 -4.601  3.856   1.00 12.36 ? 160 VAL A CB  1 
ATOM   1287 C  CG1 . VAL A 1 159 ? -14.438 -4.709  4.138   1.00 14.85 ? 160 VAL A CG1 1 
ATOM   1288 C  CG2 . VAL A 1 159 ? -16.685 -3.432  4.548   1.00 15.54 ? 160 VAL A CG2 1 
ATOM   1289 N  N   . VAL A 1 160 ? -15.878 -7.014  1.938   1.00 12.08 ? 161 VAL A N   1 
ATOM   1290 C  CA  . VAL A 1 160 ? -15.175 -8.131  1.373   1.00 14.38 ? 161 VAL A CA  1 
ATOM   1291 C  C   . VAL A 1 160 ? -15.104 -8.027  -0.141  1.00 14.48 ? 161 VAL A C   1 
ATOM   1292 O  O   . VAL A 1 160 ? -14.076 -8.311  -0.743  1.00 14.38 ? 161 VAL A O   1 
ATOM   1293 C  CB  . VAL A 1 160 ? -15.875 -9.532  1.874   1.00 15.41 ? 161 VAL A CB  1 
ATOM   1294 C  CG1 . VAL A 1 160 ? -15.499 -10.807 0.984   1.00 19.79 ? 161 VAL A CG1 1 
ATOM   1295 C  CG2 . VAL A 1 160 ? -15.605 -9.650  3.387   1.00 17.53 ? 161 VAL A CG2 1 
ATOM   1296 N  N   . ASP A 1 161 ? -16.161 -7.552  -0.774  1.00 14.17 ? 162 ASP A N   1 
ATOM   1297 C  CA  . ASP A 1 161 ? -16.194 -7.675  -2.238  1.00 17.29 ? 162 ASP A CA  1 
ATOM   1298 C  C   . ASP A 1 161 ? -15.312 -6.589  -2.924  1.00 18.53 ? 162 ASP A C   1 
ATOM   1299 O  O   . ASP A 1 161 ? -14.965 -6.775  -4.129  1.00 20.95 ? 162 ASP A O   1 
ATOM   1300 C  CB  . ASP A 1 161 ? -17.611 -7.608  -2.727  1.00 19.57 ? 162 ASP A CB  1 
ATOM   1301 C  CG  . ASP A 1 161 ? -18.302 -8.932  -2.687  1.00 19.47 ? 162 ASP A CG  1 
ATOM   1302 O  OD1 . ASP A 1 161 ? -17.610 -9.998  -2.754  1.00 21.27 ? 162 ASP A OD1 1 
ATOM   1303 O  OD2 . ASP A 1 161 ? -19.549 -8.898  -2.586  1.00 22.91 ? 162 ASP A OD2 1 
ATOM   1304 N  N   . VAL A 1 162 ? -14.931 -5.501  -2.198  1.00 17.24 ? 163 VAL A N   1 
ATOM   1305 C  CA  . VAL A 1 162 ? -14.059 -4.489  -2.795  1.00 17.19 ? 163 VAL A CA  1 
ATOM   1306 C  C   . VAL A 1 162 ? -12.543 -4.786  -2.597  1.00 15.86 ? 163 VAL A C   1 
ATOM   1307 O  O   . VAL A 1 162 ? -11.687 -4.070  -3.170  1.00 15.95 ? 163 VAL A O   1 
ATOM   1308 C  CB  . VAL A 1 162 ? -14.445 -3.066  -2.219  1.00 19.06 ? 163 VAL A CB  1 
ATOM   1309 C  CG1 . VAL A 1 162 ? -13.763 -2.769  -0.975  1.00 17.20 ? 163 VAL A CG1 1 
ATOM   1310 C  CG2 . VAL A 1 162 ? -14.307 -1.885  -3.184  1.00 21.36 ? 163 VAL A CG2 1 
ATOM   1311 N  N   . LEU A 1 163 ? -12.193 -5.766  -1.715  1.00 15.60 ? 164 LEU A N   1 
ATOM   1312 C  CA  . LEU A 1 163 ? -10.798 -6.019  -1.390  1.00 14.79 ? 164 LEU A CA  1 
ATOM   1313 C  C   . LEU A 1 163 ? -9.886  -6.318  -2.593  1.00 15.40 ? 164 LEU A C   1 
ATOM   1314 O  O   . LEU A 1 163 ? -8.674  -5.965  -2.591  1.00 16.94 ? 164 LEU A O   1 
ATOM   1315 C  CB  . LEU A 1 163 ? -10.681 -7.090  -0.280  1.00 14.25 ? 164 LEU A CB  1 
ATOM   1316 C  CG  . LEU A 1 163 ? -11.328 -6.656  1.059   1.00 12.89 ? 164 LEU A CG  1 
ATOM   1317 C  CD1 . LEU A 1 163 ? -11.081 -7.820  2.105   1.00 13.36 ? 164 LEU A CD1 1 
ATOM   1318 C  CD2 . LEU A 1 163 ? -10.719 -5.372  1.615   1.00 12.16 ? 164 LEU A CD2 1 
ATOM   1319 N  N   . ASP A 1 164 ? -10.436 -7.012  -3.602  1.00 18.29 ? 165 ASP A N   1 
ATOM   1320 C  CA  . ASP A 1 164 ? -9.551  -7.354  -4.746  1.00 20.35 ? 165 ASP A CA  1 
ATOM   1321 C  C   . ASP A 1 164 ? -9.118  -6.040  -5.501  1.00 20.37 ? 165 ASP A C   1 
ATOM   1322 O  O   . ASP A 1 164 ? -8.072  -6.042  -6.215  1.00 23.51 ? 165 ASP A O   1 
ATOM   1323 C  CB  . ASP A 1 164 ? -10.293 -8.281  -5.754  1.00 21.31 ? 165 ASP A CB  1 
ATOM   1324 C  CG  . ASP A 1 164 ? -11.283 -7.510  -6.543  1.00 25.24 ? 165 ASP A CG  1 
ATOM   1325 O  OD1 . ASP A 1 164 ? -12.254 -7.002  -5.928  1.00 26.66 ? 165 ASP A OD1 1 
ATOM   1326 O  OD2 . ASP A 1 164 ? -11.088 -7.345  -7.782  1.00 32.40 ? 165 ASP A OD2 1 
ATOM   1327 N  N   . SER A 1 165 ? -9.840  -4.923  -5.278  1.00 18.61 ? 166 SER A N   1 
ATOM   1328 C  CA  . SER A 1 165 ? -9.459  -3.645  -5.926  1.00 20.22 ? 166 SER A CA  1 
ATOM   1329 C  C   . SER A 1 165 ? -8.365  -2.870  -5.158  1.00 17.97 ? 166 SER A C   1 
ATOM   1330 O  O   . SER A 1 165 ? -7.770  -1.855  -5.652  1.00 19.31 ? 166 SER A O   1 
ATOM   1331 C  CB  . SER A 1 165 ? -10.676 -2.775  -6.200  1.00 22.93 ? 166 SER A CB  1 
ATOM   1332 O  OG  . SER A 1 165 ? -11.193 -2.199  -5.047  1.00 24.55 ? 166 SER A OG  1 
ATOM   1333 N  N   . ILE A 1 166 ? -8.120  -3.322  -3.916  1.00 15.30 ? 167 ILE A N   1 
ATOM   1334 C  CA  . ILE A 1 166 ? -7.086  -2.689  -3.081  1.00 15.78 ? 167 ILE A CA  1 
ATOM   1335 C  C   . ILE A 1 166 ? -6.088  -3.758  -2.532  1.00 14.58 ? 167 ILE A C   1 
ATOM   1336 O  O   . ILE A 1 166 ? -5.682  -3.760  -1.340  1.00 14.62 ? 167 ILE A O   1 
ATOM   1337 C  CB  . ILE A 1 166 ? -7.716  -1.849  -1.920  1.00 14.33 ? 167 ILE A CB  1 
ATOM   1338 C  CG1 . ILE A 1 166 ? -8.612  -2.700  -0.988  1.00 12.65 ? 167 ILE A CG1 1 
ATOM   1339 C  CG2 . ILE A 1 166 ? -8.402  -0.606  -2.458  1.00 16.89 ? 167 ILE A CG2 1 
ATOM   1340 C  CD1 . ILE A 1 166 ? -8.626  -2.128  0.409   1.00 13.70 ? 167 ILE A CD1 1 
ATOM   1341 N  N   . LYS A 1 167 ? -5.660  -4.631  -3.462  1.00 16.07 ? 168 LYS A N   1 
ATOM   1342 C  CA  . LYS A 1 167 ? -4.899  -5.786  -3.037  1.00 16.15 ? 168 LYS A CA  1 
ATOM   1343 C  C   . LYS A 1 167 ? -3.568  -5.408  -2.347  1.00 15.50 ? 168 LYS A C   1 
ATOM   1344 O  O   . LYS A 1 167 ? -3.183  -6.040  -1.367  1.00 14.15 ? 168 LYS A O   1 
ATOM   1345 C  CB  . LYS A 1 167 ? -4.634  -6.750  -4.233  1.00 15.94 ? 168 LYS A CB  1 
ATOM   1346 C  CG  . LYS A 1 167 ? -3.845  -7.991  -3.773  1.00 17.36 ? 168 LYS A CG  1 
ATOM   1347 C  CD  . LYS A 1 167 ? -3.469  -8.907  -5.024  1.00 20.55 ? 168 LYS A CD  1 
ATOM   1348 C  CE  . LYS A 1 167 ? -2.886  -10.203 -4.478  1.00 28.00 ? 168 LYS A CE  1 
ATOM   1349 N  NZ  . LYS A 1 167 ? -2.562  -11.121 -5.599  1.00 34.94 ? 168 LYS A NZ  1 
ATOM   1350 N  N   . THR A 1 168 ? -2.901  -4.346  -2.852  1.00 15.09 ? 169 THR A N   1 
ATOM   1351 C  CA  . THR A 1 168 ? -1.527  -4.021  -2.449  1.00 15.61 ? 169 THR A CA  1 
ATOM   1352 C  C   . THR A 1 168 ? -1.442  -2.635  -1.761  1.00 14.40 ? 169 THR A C   1 
ATOM   1353 O  O   . THR A 1 168 ? -2.319  -1.789  -1.880  1.00 16.97 ? 169 THR A O   1 
ATOM   1354 C  CB  . THR A 1 168 ? -0.564  -4.076  -3.691  1.00 16.40 ? 169 THR A CB  1 
ATOM   1355 O  OG1 . THR A 1 168 ? -1.142  -3.326  -4.736  1.00 20.21 ? 169 THR A OG1 1 
ATOM   1356 C  CG2 . THR A 1 168 ? -0.441  -5.537  -4.154  1.00 17.95 ? 169 THR A CG2 1 
ATOM   1357 N  N   . LYS A 1 169 ? -0.386  -2.532  -0.993  1.00 17.43 ? 170 LYS A N   1 
ATOM   1358 C  CA  . LYS A 1 169 ? -0.084  -1.327  -0.208  1.00 17.21 ? 170 LYS A CA  1 
ATOM   1359 C  C   . LYS A 1 169 ? -0.244  -0.022  -1.041  1.00 17.93 ? 170 LYS A C   1 
ATOM   1360 O  O   . LYS A 1 169 ? 0.353   0.043   -2.174  1.00 20.14 ? 170 LYS A O   1 
ATOM   1361 C  CB  . LYS A 1 169 ? 1.334   -1.428  0.319   1.00 16.95 ? 170 LYS A CB  1 
ATOM   1362 C  CG  . LYS A 1 169 ? 1.822   -0.139  1.142   1.00 18.85 ? 170 LYS A CG  1 
ATOM   1363 C  CD  . LYS A 1 169 ? 3.134   -0.390  1.849   1.00 20.54 ? 170 LYS A CD  1 
ATOM   1364 C  CE  . LYS A 1 169 ? 3.510   0.722   2.874   1.00 26.21 ? 170 LYS A CE  1 
ATOM   1365 N  NZ  . LYS A 1 169 ? 4.995   1.155   2.786   1.00 33.58 ? 170 LYS A NZ  1 
ATOM   1366 N  N   . GLY A 1 170 ? -0.966  0.976   -0.544  1.00 19.02 ? 171 GLY A N   1 
ATOM   1367 C  CA  . GLY A 1 170 ? -1.111  2.256   -1.272  1.00 18.40 ? 171 GLY A CA  1 
ATOM   1368 C  C   . GLY A 1 170 ? -2.305  2.324   -2.223  1.00 19.43 ? 171 GLY A C   1 
ATOM   1369 O  O   . GLY A 1 170 ? -2.716  3.442   -2.663  1.00 20.46 ? 171 GLY A O   1 
ATOM   1370 N  N   . LYS A 1 171 ? -2.945  1.179   -2.505  1.00 16.84 ? 172 LYS A N   1 
ATOM   1371 C  CA  . LYS A 1 171 ? -4.198  1.250   -3.237  1.00 18.74 ? 172 LYS A CA  1 
ATOM   1372 C  C   . LYS A 1 171 ? -5.448  1.721   -2.432  1.00 18.03 ? 172 LYS A C   1 
ATOM   1373 O  O   . LYS A 1 171 ? -5.655  1.322   -1.274  1.00 17.54 ? 172 LYS A O   1 
ATOM   1374 C  CB  . LYS A 1 171 ? -4.478  -0.098  -3.945  1.00 17.18 ? 172 LYS A CB  1 
ATOM   1375 C  CG  . LYS A 1 171 ? -3.387  -0.506  -4.994  1.00 22.13 ? 172 LYS A CG  1 
ATOM   1376 C  CD  . LYS A 1 171 ? -3.761  -1.775  -5.907  1.00 22.98 ? 172 LYS A CD  1 
ATOM   1377 C  CE  . LYS A 1 171 ? -4.097  -1.539  -7.373  1.00 29.64 ? 172 LYS A CE  1 
ATOM   1378 N  NZ  . LYS A 1 171 ? -5.517  -2.130  -7.755  1.00 30.26 ? 172 LYS A NZ  1 
ATOM   1379 N  N   A SER A 1 172 ? -6.289  2.514   -3.068  0.50 17.12 ? 173 SER A N   1 
ATOM   1380 N  N   B SER A 1 172 ? -6.282  2.532   -3.059  0.50 16.63 ? 173 SER A N   1 
ATOM   1381 C  CA  A SER A 1 172 ? -7.509  3.014   -2.479  0.50 17.31 ? 173 SER A CA  1 
ATOM   1382 C  CA  B SER A 1 172 ? -7.563  2.912   -2.509  0.50 16.23 ? 173 SER A CA  1 
ATOM   1383 C  C   A SER A 1 172 ? -8.652  2.995   -3.504  0.50 17.26 ? 173 SER A C   1 
ATOM   1384 C  C   B SER A 1 172 ? -8.689  2.780   -3.526  0.50 16.65 ? 173 SER A C   1 
ATOM   1385 O  O   A SER A 1 172 ? -8.397  3.105   -4.758  0.50 18.20 ? 173 SER A O   1 
ATOM   1386 O  O   B SER A 1 172 ? -8.494  2.617   -4.774  0.50 17.91 ? 173 SER A O   1 
ATOM   1387 C  CB  A SER A 1 172 ? -7.273  4.452   -1.924  0.50 16.55 ? 173 SER A CB  1 
ATOM   1388 C  CB  B SER A 1 172 ? -7.542  4.373   -2.012  0.50 15.09 ? 173 SER A CB  1 
ATOM   1389 O  OG  A SER A 1 172 ? -6.583  5.320   -2.840  0.50 17.35 ? 173 SER A OG  1 
ATOM   1390 O  OG  B SER A 1 172 ? -7.576  5.232   -3.132  0.50 13.02 ? 173 SER A OG  1 
ATOM   1391 N  N   . ALA A 1 173 ? -9.892  2.900   -3.004  1.00 18.68 ? 174 ALA A N   1 
ATOM   1392 C  CA  . ALA A 1 173 ? -11.110 2.875   -3.833  1.00 19.00 ? 174 ALA A CA  1 
ATOM   1393 C  C   . ALA A 1 173 ? -12.218 3.714   -3.166  1.00 19.91 ? 174 ALA A C   1 
ATOM   1394 O  O   . ALA A 1 173 ? -12.330 3.771   -1.907  1.00 19.57 ? 174 ALA A O   1 
ATOM   1395 C  CB  . ALA A 1 173 ? -11.526 1.483   -4.103  1.00 18.88 ? 174 ALA A CB  1 
ATOM   1396 N  N   . ASP A 1 174 ? -13.011 4.382   -3.986  1.00 21.92 ? 175 ASP A N   1 
ATOM   1397 C  CA  . ASP A 1 174 ? -14.225 5.015   -3.460  1.00 21.77 ? 175 ASP A CA  1 
ATOM   1398 C  C   . ASP A 1 174 ? -15.025 4.000   -2.703  1.00 20.85 ? 175 ASP A C   1 
ATOM   1399 O  O   . ASP A 1 174 ? -15.116 2.806   -3.138  1.00 21.36 ? 175 ASP A O   1 
ATOM   1400 C  CB  . ASP A 1 174 ? -15.136 5.547   -4.620  1.00 24.43 ? 175 ASP A CB  1 
ATOM   1401 C  CG  . ASP A 1 174 ? -14.431 6.543   -5.473  1.00 29.88 ? 175 ASP A CG  1 
ATOM   1402 O  OD1 . ASP A 1 174 ? -13.593 7.310   -4.957  1.00 32.69 ? 175 ASP A OD1 1 
ATOM   1403 O  OD2 . ASP A 1 174 ? -14.715 6.560   -6.708  1.00 33.05 ? 175 ASP A OD2 1 
ATOM   1404 N  N   . PHE A 1 175 ? -15.536 4.407   -1.534  1.00 17.98 ? 176 PHE A N   1 
ATOM   1405 C  CA  . PHE A 1 175 ? -16.340 3.430   -0.785  1.00 16.27 ? 176 PHE A CA  1 
ATOM   1406 C  C   . PHE A 1 175 ? -17.401 4.204   -0.056  1.00 16.02 ? 176 PHE A C   1 
ATOM   1407 O  O   . PHE A 1 175 ? -17.255 4.512   1.167   1.00 18.57 ? 176 PHE A O   1 
ATOM   1408 C  CB  . PHE A 1 175 ? -15.427 2.644   0.157   1.00 14.79 ? 176 PHE A CB  1 
ATOM   1409 C  CG  . PHE A 1 175 ? -16.051 1.369   0.703   1.00 14.96 ? 176 PHE A CG  1 
ATOM   1410 C  CD1 . PHE A 1 175 ? -16.398 0.305   -0.139  1.00 15.58 ? 176 PHE A CD1 1 
ATOM   1411 C  CD2 . PHE A 1 175 ? -16.324 1.252   2.056   1.00 16.54 ? 176 PHE A CD2 1 
ATOM   1412 C  CE1 . PHE A 1 175 ? -16.935 -0.848  0.420   1.00 15.60 ? 176 PHE A CE1 1 
ATOM   1413 C  CE2 . PHE A 1 175 ? -16.904 0.086   2.582   1.00 18.03 ? 176 PHE A CE2 1 
ATOM   1414 C  CZ  . PHE A 1 175 ? -17.179 -0.954  1.759   1.00 16.36 ? 176 PHE A CZ  1 
ATOM   1415 N  N   . THR A 1 176 ? -18.415 4.627   -0.799  1.00 15.27 ? 177 THR A N   1 
ATOM   1416 C  CA  . THR A 1 176 ? -19.481 5.463   -0.222  1.00 16.71 ? 177 THR A CA  1 
ATOM   1417 C  C   . THR A 1 176 ? -20.660 4.612   0.245   1.00 14.68 ? 177 THR A C   1 
ATOM   1418 O  O   . THR A 1 176 ? -20.828 3.436   -0.240  1.00 16.20 ? 177 THR A O   1 
ATOM   1419 C  CB  . THR A 1 176 ? -19.961 6.538   -1.212  1.00 16.53 ? 177 THR A CB  1 
ATOM   1420 O  OG1 . THR A 1 176 ? -20.398 5.875   -2.398  1.00 20.10 ? 177 THR A OG1 1 
ATOM   1421 C  CG2 . THR A 1 176 ? -18.830 7.546   -1.506  1.00 20.62 ? 177 THR A CG2 1 
ATOM   1422 N  N   . ASN A 1 177 ? -21.480 5.171   1.128   1.00 14.41 ? 178 ASN A N   1 
ATOM   1423 C  CA  . ASN A 1 177 ? -22.800 4.619   1.500   1.00 15.56 ? 178 ASN A CA  1 
ATOM   1424 C  C   . ASN A 1 177 ? -22.638 3.280   2.254   1.00 15.12 ? 178 ASN A C   1 
ATOM   1425 O  O   . ASN A 1 177 ? -23.563 2.488   2.240   1.00 18.76 ? 178 ASN A O   1 
ATOM   1426 C  CB  . ASN A 1 177 ? -23.763 4.485   0.315   1.00 16.34 ? 178 ASN A CB  1 
ATOM   1427 C  CG  . ASN A 1 177 ? -24.060 5.862   -0.283  1.00 17.32 ? 178 ASN A CG  1 
ATOM   1428 O  OD1 . ASN A 1 177 ? -24.782 6.715   0.344   1.00 20.89 ? 178 ASN A OD1 1 
ATOM   1429 N  ND2 . ASN A 1 177 ? -23.385 6.146   -1.408  1.00 16.14 ? 178 ASN A ND2 1 
ATOM   1430 N  N   . PHE A 1 178 ? -21.503 3.098   2.955   1.00 13.53 ? 179 PHE A N   1 
ATOM   1431 C  CA  . PHE A 1 178 ? -21.347 1.860   3.747   1.00 14.11 ? 179 PHE A CA  1 
ATOM   1432 C  C   . PHE A 1 178 ? -21.867 2.134   5.130   1.00 13.53 ? 179 PHE A C   1 
ATOM   1433 O  O   . PHE A 1 178 ? -21.396 3.100   5.768   1.00 14.22 ? 179 PHE A O   1 
ATOM   1434 C  CB  . PHE A 1 178 ? -19.917 1.400   3.865   1.00 11.60 ? 179 PHE A CB  1 
ATOM   1435 C  CG  . PHE A 1 178 ? -19.808 0.166   4.690   1.00 11.74 ? 179 PHE A CG  1 
ATOM   1436 C  CD1 . PHE A 1 178 ? -20.248 -1.081  4.157   1.00 15.39 ? 179 PHE A CD1 1 
ATOM   1437 C  CD2 . PHE A 1 178 ? -19.421 0.240   6.025   1.00 11.99 ? 179 PHE A CD2 1 
ATOM   1438 C  CE1 . PHE A 1 178 ? -20.229 -2.235  4.937   1.00 15.53 ? 179 PHE A CE1 1 
ATOM   1439 C  CE2 . PHE A 1 178 ? -19.413 -0.984  6.821   1.00 12.27 ? 179 PHE A CE2 1 
ATOM   1440 C  CZ  . PHE A 1 178 ? -19.823 -2.177  6.278   1.00 14.11 ? 179 PHE A CZ  1 
ATOM   1441 N  N   . ASP A 1 179 ? -22.767 1.266   5.639   1.00 13.25 ? 180 ASP A N   1 
ATOM   1442 C  CA  . ASP A 1 179 ? -23.391 1.487   6.925   1.00 12.99 ? 180 ASP A CA  1 
ATOM   1443 C  C   . ASP A 1 179 ? -22.725 0.632   8.026   1.00 12.02 ? 180 ASP A C   1 
ATOM   1444 O  O   . ASP A 1 179 ? -22.923 -0.594  8.061   1.00 12.08 ? 180 ASP A O   1 
ATOM   1445 C  CB  . ASP A 1 179 ? -24.879 1.120   6.821   1.00 15.82 ? 180 ASP A CB  1 
ATOM   1446 C  CG  . ASP A 1 179 ? -25.647 1.510   8.031   1.00 17.74 ? 180 ASP A CG  1 
ATOM   1447 O  OD1 . ASP A 1 179 ? -25.075 1.761   9.105   1.00 15.73 ? 180 ASP A OD1 1 
ATOM   1448 O  OD2 . ASP A 1 179 ? -26.890 1.613   7.951   1.00 24.21 ? 180 ASP A OD2 1 
ATOM   1449 N  N   . PRO A 1 180 ? -21.933 1.267   8.926   1.00 10.59 ? 181 PRO A N   1 
ATOM   1450 C  CA  . PRO A 1 180 ? -21.215 0.406   9.925   1.00 10.84 ? 181 PRO A CA  1 
ATOM   1451 C  C   . PRO A 1 180 ? -22.133 -0.231  10.968  1.00 10.49 ? 181 PRO A C   1 
ATOM   1452 O  O   . PRO A 1 180 ? -21.695 -1.131  11.748  1.00 10.25 ? 181 PRO A O   1 
ATOM   1453 C  CB  . PRO A 1 180 ? -20.201 1.366   10.537  1.00 11.93 ? 181 PRO A CB  1 
ATOM   1454 C  CG  . PRO A 1 180 ? -20.880 2.764   10.484  1.00 12.04 ? 181 PRO A CG  1 
ATOM   1455 C  CD  . PRO A 1 180 ? -21.628 2.714   9.103   1.00 11.93 ? 181 PRO A CD  1 
ATOM   1456 N  N   . ARG A 1 181 ? -23.440 0.172   11.013  1.00 9.01  ? 182 ARG A N   1 
ATOM   1457 C  CA  . ARG A 1 181 ? -24.343 -0.532  11.932  1.00 10.90 ? 182 ARG A CA  1 
ATOM   1458 C  C   . ARG A 1 181 ? -24.431 -2.042  11.607  1.00 11.19 ? 182 ARG A C   1 
ATOM   1459 O  O   . ARG A 1 181 ? -24.818 -2.823  12.482  1.00 14.32 ? 182 ARG A O   1 
ATOM   1460 C  CB  . ARG A 1 181 ? -25.754 0.081   11.859  1.00 11.77 ? 182 ARG A CB  1 
ATOM   1461 C  CG  . ARG A 1 181 ? -25.705 1.535   12.452  1.00 14.41 ? 182 ARG A CG  1 
ATOM   1462 C  CD  . ARG A 1 181 ? -27.034 2.243   12.371  1.00 17.01 ? 182 ARG A CD  1 
ATOM   1463 N  NE  . ARG A 1 181 ? -27.421 2.433   10.968  1.00 15.98 ? 182 ARG A NE  1 
ATOM   1464 C  CZ  . ARG A 1 181 ? -28.515 3.116   10.583  1.00 18.81 ? 182 ARG A CZ  1 
ATOM   1465 N  NH1 . ARG A 1 181 ? -29.315 3.662   11.488  1.00 22.71 ? 182 ARG A NH1 1 
ATOM   1466 N  NH2 . ARG A 1 181 ? -28.804 3.234   9.286   1.00 21.74 ? 182 ARG A NH2 1 
ATOM   1467 N  N   . GLY A 1 182 ? -24.216 -2.396  10.329  1.00 11.00 ? 183 GLY A N   1 
ATOM   1468 C  CA  . GLY A 1 182 ? -24.298 -3.810  9.910   1.00 11.61 ? 183 GLY A CA  1 
ATOM   1469 C  C   . GLY A 1 182 ? -23.126 -4.654  10.449  1.00 12.90 ? 183 GLY A C   1 
ATOM   1470 O  O   . GLY A 1 182 ? -23.105 -5.865  10.174  1.00 14.81 ? 183 GLY A O   1 
ATOM   1471 N  N   . LEU A 1 183 ? -22.199 -4.043  11.234  1.00 10.09 ? 184 LEU A N   1 
ATOM   1472 C  CA  . LEU A 1 183 ? -21.069 -4.782  11.856  1.00 11.39 ? 184 LEU A CA  1 
ATOM   1473 C  C   . LEU A 1 183 ? -21.200 -4.952  13.338  1.00 10.71 ? 184 LEU A C   1 
ATOM   1474 O  O   . LEU A 1 183 ? -20.297 -5.572  13.939  1.00 12.15 ? 184 LEU A O   1 
ATOM   1475 C  CB  . LEU A 1 183 ? -19.733 -4.088  11.576  1.00 11.58 ? 184 LEU A CB  1 
ATOM   1476 C  CG  . LEU A 1 183 ? -19.409 -3.874  10.072  1.00 11.04 ? 184 LEU A CG  1 
ATOM   1477 C  CD1 . LEU A 1 183 ? -18.119 -3.138  9.810   1.00 12.88 ? 184 LEU A CD1 1 
ATOM   1478 C  CD2 . LEU A 1 183 ? -19.377 -5.207  9.387   1.00 15.65 ? 184 LEU A CD2 1 
ATOM   1479 N  N   . LEU A 1 184 ? -22.329 -4.531  13.908  1.00 9.55  ? 185 LEU A N   1 
ATOM   1480 C  CA  . LEU A 1 184 ? -22.492 -4.534  15.400  1.00 11.08 ? 185 LEU A CA  1 
ATOM   1481 C  C   . LEU A 1 184 ? -23.278 -5.765  15.880  1.00 12.36 ? 185 LEU A C   1 
ATOM   1482 O  O   . LEU A 1 184 ? -24.375 -6.133  15.305  1.00 16.14 ? 185 LEU A O   1 
ATOM   1483 C  CB  . LEU A 1 184 ? -23.301 -3.300  15.888  1.00 10.46 ? 185 LEU A CB  1 
ATOM   1484 C  CG  . LEU A 1 184 ? -22.715 -1.945  15.496  1.00 10.05 ? 185 LEU A CG  1 
ATOM   1485 C  CD1 . LEU A 1 184 ? -23.589 -0.784  15.910  1.00 11.68 ? 185 LEU A CD1 1 
ATOM   1486 C  CD2 . LEU A 1 184 ? -21.255 -1.816  16.000  1.00 10.41 ? 185 LEU A CD2 1 
ATOM   1487 N  N   . PRO A 1 185 ? -22.837 -6.375  16.964  1.00 11.18 ? 186 PRO A N   1 
ATOM   1488 C  CA  . PRO A 1 185 ? -23.626 -7.531  17.502  1.00 10.43 ? 186 PRO A CA  1 
ATOM   1489 C  C   . PRO A 1 185 ? -24.916 -6.995  18.170  1.00 11.43 ? 186 PRO A C   1 
ATOM   1490 O  O   . PRO A 1 185 ? -25.101 -5.765  18.288  1.00 12.96 ? 186 PRO A O   1 
ATOM   1491 C  CB  . PRO A 1 185 ? -22.649 -8.158  18.513  1.00 8.78  ? 186 PRO A CB  1 
ATOM   1492 C  CG  . PRO A 1 185 ? -21.906 -6.898  19.070  1.00 9.52  ? 186 PRO A CG  1 
ATOM   1493 C  CD  . PRO A 1 185 ? -21.682 -5.997  17.807  1.00 8.74  ? 186 PRO A CD  1 
ATOM   1494 N  N   A GLU A 1 186 ? -25.759 -7.896  18.693  0.50 11.49 ? 187 GLU A N   1 
ATOM   1495 N  N   B GLU A 1 186 ? -25.774 -7.923  18.646  0.50 11.93 ? 187 GLU A N   1 
ATOM   1496 C  CA  A GLU A 1 186 ? -27.032 -7.524  19.263  0.50 12.45 ? 187 GLU A CA  1 
ATOM   1497 C  CA  B GLU A 1 186 ? -27.011 -7.564  19.301  0.50 13.06 ? 187 GLU A CA  1 
ATOM   1498 C  C   A GLU A 1 186 ? -26.833 -6.786  20.627  0.50 12.90 ? 187 GLU A C   1 
ATOM   1499 C  C   B GLU A 1 186 ? -26.685 -6.707  20.499  0.50 12.82 ? 187 GLU A C   1 
ATOM   1500 O  O   A GLU A 1 186 ? -27.589 -5.861  20.995  0.50 13.13 ? 187 GLU A O   1 
ATOM   1501 O  O   B GLU A 1 186 ? -27.206 -5.600  20.593  0.50 13.97 ? 187 GLU A O   1 
ATOM   1502 C  CB  A GLU A 1 186 ? -27.822 -8.830  19.433  0.50 12.78 ? 187 GLU A CB  1 
ATOM   1503 C  CB  B GLU A 1 186 ? -27.736 -8.821  19.787  0.50 13.59 ? 187 GLU A CB  1 
ATOM   1504 C  CG  A GLU A 1 186 ? -28.890 -8.684  20.447  0.50 13.30 ? 187 GLU A CG  1 
ATOM   1505 C  CG  B GLU A 1 186 ? -28.797 -9.228  18.892  0.50 15.76 ? 187 GLU A CG  1 
ATOM   1506 C  CD  A GLU A 1 186 ? -29.616 -10.018 20.749  0.50 13.80 ? 187 GLU A CD  1 
ATOM   1507 C  CD  B GLU A 1 186 ? -29.371 -10.623 19.300  0.50 18.30 ? 187 GLU A CD  1 
ATOM   1508 O  OE1 A GLU A 1 186 ? -29.558 -10.963 19.916  0.50 15.27 ? 187 GLU A OE1 1 
ATOM   1509 O  OE1 B GLU A 1 186 ? -29.131 -11.112 20.436  0.50 19.78 ? 187 GLU A OE1 1 
ATOM   1510 O  OE2 A GLU A 1 186 ? -30.242 -10.063 21.821  0.50 17.46 ? 187 GLU A OE2 1 
ATOM   1511 O  OE2 B GLU A 1 186 ? -30.077 -11.235 18.501  0.50 22.39 ? 187 GLU A OE2 1 
ATOM   1512 N  N   . SER A 1 187 ? -25.880 -7.265  21.429  1.00 12.33 ? 188 SER A N   1 
ATOM   1513 C  CA  . SER A 1 187 ? -25.681 -6.670  22.746  1.00 12.51 ? 188 SER A CA  1 
ATOM   1514 C  C   . SER A 1 187 ? -24.548 -5.624  22.687  1.00 11.96 ? 188 SER A C   1 
ATOM   1515 O  O   . SER A 1 187 ? -23.501 -5.868  22.051  1.00 12.87 ? 188 SER A O   1 
ATOM   1516 C  CB  . SER A 1 187 ? -25.271 -7.729  23.769  1.00 13.90 ? 188 SER A CB  1 
ATOM   1517 O  OG  . SER A 1 187 ? -25.029 -7.154  25.068  1.00 14.17 ? 188 SER A OG  1 
ATOM   1518 N  N   . LEU A 1 188 ? -24.726 -4.528  23.449  1.00 11.67 ? 189 LEU A N   1 
ATOM   1519 C  CA  . LEU A 1 188 ? -23.625 -3.542  23.650  1.00 10.84 ? 189 LEU A CA  1 
ATOM   1520 C  C   . LEU A 1 188 ? -22.970 -3.665  25.053  1.00 10.25 ? 189 LEU A C   1 
ATOM   1521 O  O   . LEU A 1 188 ? -22.292 -2.756  25.485  1.00 12.59 ? 189 LEU A O   1 
ATOM   1522 C  CB  . LEU A 1 188 ? -24.059 -2.067  23.338  1.00 11.12 ? 189 LEU A CB  1 
ATOM   1523 C  CG  . LEU A 1 188 ? -24.556 -1.759  21.939  1.00 14.44 ? 189 LEU A CG  1 
ATOM   1524 C  CD1 . LEU A 1 188 ? -25.078 -0.320  21.735  1.00 15.00 ? 189 LEU A CD1 1 
ATOM   1525 C  CD2 . LEU A 1 188 ? -23.442 -2.006  20.956  1.00 13.24 ? 189 LEU A CD2 1 
ATOM   1526 N  N   . ASP A 1 189 ? -23.125 -4.806  25.746  1.00 11.50 ? 190 ASP A N   1 
ATOM   1527 C  CA  . ASP A 1 189 ? -22.346 -5.048  26.986  1.00 11.91 ? 190 ASP A CA  1 
ATOM   1528 C  C   . ASP A 1 189 ? -20.854 -4.972  26.658  1.00 9.65  ? 190 ASP A C   1 
ATOM   1529 O  O   . ASP A 1 189 ? -20.406 -5.491  25.623  1.00 10.06 ? 190 ASP A O   1 
ATOM   1530 C  CB  . ASP A 1 189 ? -22.643 -6.414  27.588  1.00 12.05 ? 190 ASP A CB  1 
ATOM   1531 C  CG  . ASP A 1 189 ? -24.054 -6.485  28.245  1.00 17.44 ? 190 ASP A CG  1 
ATOM   1532 O  OD1 . ASP A 1 189 ? -24.674 -5.445  28.427  1.00 20.01 ? 190 ASP A OD1 1 
ATOM   1533 O  OD2 . ASP A 1 189 ? -24.500 -7.616  28.536  1.00 23.04 ? 190 ASP A OD2 1 
ATOM   1534 N  N   . TYR A 1 190 ? -20.075 -4.371  27.560  1.00 8.63  ? 191 TYR A N   1 
ATOM   1535 C  CA  . TYR A 1 190 ? -18.662 -4.120  27.211  1.00 8.51  ? 191 TYR A CA  1 
ATOM   1536 C  C   . TYR A 1 190 ? -17.729 -4.215  28.442  1.00 9.06  ? 191 TYR A C   1 
ATOM   1537 O  O   . TYR A 1 190 ? -18.194 -4.068  29.598  1.00 9.84  ? 191 TYR A O   1 
ATOM   1538 C  CB  . TYR A 1 190 ? -18.520 -2.714  26.568  1.00 9.33  ? 191 TYR A CB  1 
ATOM   1539 C  CG  . TYR A 1 190 ? -18.915 -1.573  27.482  1.00 8.14  ? 191 TYR A CG  1 
ATOM   1540 C  CD1 . TYR A 1 190 ? -17.967 -0.948  28.390  1.00 8.70  ? 191 TYR A CD1 1 
ATOM   1541 C  CD2 . TYR A 1 190 ? -20.187 -1.064  27.390  1.00 9.72  ? 191 TYR A CD2 1 
ATOM   1542 C  CE1 . TYR A 1 190 ? -18.381 0.069   29.215  1.00 10.18 ? 191 TYR A CE1 1 
ATOM   1543 C  CE2 . TYR A 1 190 ? -20.602 -0.004  28.198  1.00 11.11 ? 191 TYR A CE2 1 
ATOM   1544 C  CZ  . TYR A 1 190 ? -19.695 0.546   29.116  1.00 11.54 ? 191 TYR A CZ  1 
ATOM   1545 O  OH  . TYR A 1 190 ? -20.107 1.588   29.942  1.00 12.90 ? 191 TYR A OH  1 
ATOM   1546 N  N   . TRP A 1 191 ? -16.441 -4.423  28.147  1.00 7.44  ? 192 TRP A N   1 
ATOM   1547 C  CA  . TRP A 1 191 ? -15.390 -4.125  29.113  1.00 6.09  ? 192 TRP A CA  1 
ATOM   1548 C  C   . TRP A 1 191 ? -14.684 -2.804  28.725  1.00 6.68  ? 192 TRP A C   1 
ATOM   1549 O  O   . TRP A 1 191 ? -14.677 -2.440  27.542  1.00 7.98  ? 192 TRP A O   1 
ATOM   1550 C  CB  . TRP A 1 191 ? -14.299 -5.223  29.064  1.00 8.27  ? 192 TRP A CB  1 
ATOM   1551 C  CG  . TRP A 1 191 ? -14.807 -6.559  29.482  1.00 7.74  ? 192 TRP A CG  1 
ATOM   1552 C  CD1 . TRP A 1 191 ? -15.045 -6.985  30.793  1.00 9.37  ? 192 TRP A CD1 1 
ATOM   1553 C  CD2 . TRP A 1 191 ? -15.093 -7.699  28.632  1.00 8.91  ? 192 TRP A CD2 1 
ATOM   1554 N  NE1 . TRP A 1 191 ? -15.456 -8.334  30.775  1.00 8.68  ? 192 TRP A NE1 1 
ATOM   1555 C  CE2 . TRP A 1 191 ? -15.526 -8.776  29.476  1.00 9.46  ? 192 TRP A CE2 1 
ATOM   1556 C  CE3 . TRP A 1 191 ? -15.005 -7.930  27.243  1.00 8.78  ? 192 TRP A CE3 1 
ATOM   1557 C  CZ2 . TRP A 1 191 ? -15.835 -10.071 28.959  1.00 10.06 ? 192 TRP A CZ2 1 
ATOM   1558 C  CZ3 . TRP A 1 191 ? -15.307 -9.246  26.737  1.00 8.26  ? 192 TRP A CZ3 1 
ATOM   1559 C  CH2 . TRP A 1 191 ? -15.727 -10.249 27.612  1.00 9.49  ? 192 TRP A CH2 1 
ATOM   1560 N  N   . THR A 1 192 ? -14.085 -2.132  29.688  1.00 6.62  ? 193 THR A N   1 
ATOM   1561 C  CA  . THR A 1 192 ? -13.394 -0.895  29.318  1.00 5.74  ? 193 THR A CA  1 
ATOM   1562 C  C   . THR A 1 192 ? -12.129 -0.686  30.219  1.00 7.48  ? 193 THR A C   1 
ATOM   1563 O  O   . THR A 1 192 ? -12.093 -1.132  31.395  1.00 8.66  ? 193 THR A O   1 
ATOM   1564 C  CB  . THR A 1 192 ? -14.315 0.361   29.439  1.00 7.41  ? 193 THR A CB  1 
ATOM   1565 O  OG1 . THR A 1 192 ? -13.663 1.571   29.017  1.00 8.43  ? 193 THR A OG1 1 
ATOM   1566 C  CG2 . THR A 1 192 ? -14.843 0.577   30.898  1.00 9.69  ? 193 THR A CG2 1 
ATOM   1567 N  N   . TYR A 1 193 ? -11.074 -0.098  29.610  1.00 7.43  ? 194 TYR A N   1 
ATOM   1568 C  CA  . TYR A 1 193 ? -9.843  0.150   30.368  1.00 6.05  ? 194 TYR A CA  1 
ATOM   1569 C  C   . TYR A 1 193 ? -9.064  1.215   29.599  1.00 7.02  ? 194 TYR A C   1 
ATOM   1570 O  O   . TYR A 1 193 ? -9.293  1.405   28.395  1.00 7.38  ? 194 TYR A O   1 
ATOM   1571 C  CB  . TYR A 1 193 ? -9.018  -1.156  30.560  1.00 7.19  ? 194 TYR A CB  1 
ATOM   1572 C  CG  . TYR A 1 193 ? -8.335  -1.627  29.294  1.00 6.55  ? 194 TYR A CG  1 
ATOM   1573 C  CD1 . TYR A 1 193 ? -9.017  -2.378  28.269  1.00 6.67  ? 194 TYR A CD1 1 
ATOM   1574 C  CD2 . TYR A 1 193 ? -7.007  -1.272  29.061  1.00 6.68  ? 194 TYR A CD2 1 
ATOM   1575 C  CE1 . TYR A 1 193 ? -8.367  -2.660  27.099  1.00 6.16  ? 194 TYR A CE1 1 
ATOM   1576 C  CE2 . TYR A 1 193 ? -6.317  -1.560  27.896  1.00 7.16  ? 194 TYR A CE2 1 
ATOM   1577 C  CZ  . TYR A 1 193 ? -7.012  -2.277  26.900  1.00 5.54  ? 194 TYR A CZ  1 
ATOM   1578 O  OH  . TYR A 1 193 ? -6.353  -2.616  25.719  1.00 6.97  ? 194 TYR A OH  1 
ATOM   1579 N  N   . PRO A 1 194 ? -8.116  1.911   30.267  1.00 6.43  ? 195 PRO A N   1 
ATOM   1580 C  CA  . PRO A 1 194 ? -7.329  2.932   29.547  1.00 5.92  ? 195 PRO A CA  1 
ATOM   1581 C  C   . PRO A 1 194 ? -6.099  2.268   28.889  1.00 5.94  ? 195 PRO A C   1 
ATOM   1582 O  O   . PRO A 1 194 ? -5.377  1.489   29.569  1.00 7.23  ? 195 PRO A O   1 
ATOM   1583 C  CB  . PRO A 1 194 ? -6.803  3.875   30.691  1.00 8.27  ? 195 PRO A CB  1 
ATOM   1584 C  CG  . PRO A 1 194 ? -6.733  2.933   31.961  1.00 9.11  ? 195 PRO A CG  1 
ATOM   1585 C  CD  . PRO A 1 194 ? -7.928  1.948   31.732  1.00 7.94  ? 195 PRO A CD  1 
ATOM   1586 N  N   . GLY A 1 195 ? -5.826  2.585   27.606  1.00 5.32  ? 196 GLY A N   1 
ATOM   1587 C  CA  . GLY A 1 195 ? -4.725  1.906   26.866  1.00 6.03  ? 196 GLY A CA  1 
ATOM   1588 C  C   . GLY A 1 195 ? -4.181  2.794   25.772  1.00 5.64  ? 196 GLY A C   1 
ATOM   1589 O  O   . GLY A 1 195 ? -4.110  4.035   25.895  1.00 6.08  ? 196 GLY A O   1 
ATOM   1590 N  N   . SER A 1 196 ? -3.769  2.145   24.701  1.00 6.65  ? 197 SER A N   1 
ATOM   1591 C  CA  . SER A 1 196 ? -2.965  2.793   23.687  1.00 6.09  ? 197 SER A CA  1 
ATOM   1592 C  C   . SER A 1 196 ? -3.451  2.398   22.262  1.00 5.95  ? 197 SER A C   1 
ATOM   1593 O  O   . SER A 1 196 ? -4.201  1.402   22.098  1.00 6.40  ? 197 SER A O   1 
ATOM   1594 C  CB  . SER A 1 196 ? -1.500  2.369   23.823  1.00 8.95  ? 197 SER A CB  1 
ATOM   1595 O  OG  . SER A 1 196 ? -1.288  1.020   23.388  1.00 7.82  ? 197 SER A OG  1 
ATOM   1596 N  N   . LEU A 1 197 ? -2.915  3.073   21.253  1.00 6.36  ? 198 LEU A N   1 
ATOM   1597 C  CA  . LEU A 1 197 ? -2.948  2.489   19.887  1.00 6.06  ? 198 LEU A CA  1 
ATOM   1598 C  C   . LEU A 1 197 ? -2.189  1.191   19.916  1.00 6.79  ? 198 LEU A C   1 
ATOM   1599 O  O   . LEU A 1 197 ? -1.154  1.076   20.623  1.00 7.14  ? 198 LEU A O   1 
ATOM   1600 C  CB  . LEU A 1 197 ? -2.282  3.434   18.908  1.00 9.76  ? 198 LEU A CB  1 
ATOM   1601 C  CG  . LEU A 1 197 ? -2.803  4.864   18.835  1.00 12.24 ? 198 LEU A CG  1 
ATOM   1602 C  CD1 . LEU A 1 197 ? -1.995  5.773   17.818  1.00 14.97 ? 198 LEU A CD1 1 
ATOM   1603 C  CD2 . LEU A 1 197 ? -4.181  4.821   18.354  1.00 15.14 ? 198 LEU A CD2 1 
ATOM   1604 N  N   . THR A 1 198 ? -2.633  0.227   19.106  1.00 7.19  ? 199 THR A N   1 
ATOM   1605 C  CA  . THR A 1 198 ? -1.924  -1.049  19.074  1.00 6.81  ? 199 THR A CA  1 
ATOM   1606 C  C   . THR A 1 198 ? -0.926  -1.143  17.898  1.00 8.66  ? 199 THR A C   1 
ATOM   1607 O  O   . THR A 1 198 ? -0.294  -2.211  17.704  1.00 8.34  ? 199 THR A O   1 
ATOM   1608 C  CB  . THR A 1 198 ? -2.951  -2.193  18.952  1.00 6.61  ? 199 THR A CB  1 
ATOM   1609 O  OG1 . THR A 1 198 ? -3.562  -2.113  17.675  1.00 7.18  ? 199 THR A OG1 1 
ATOM   1610 C  CG2 . THR A 1 198 ? -3.963  -2.213  20.117  1.00 6.69  ? 199 THR A CG2 1 
ATOM   1611 N  N   . THR A 1 199 ? -0.830  -0.065  17.092  1.00 8.65  ? 200 THR A N   1 
ATOM   1612 C  CA  . THR A 1 199 ? 0.235   -0.008  16.117  1.00 9.46  ? 200 THR A CA  1 
ATOM   1613 C  C   . THR A 1 199 ? 1.040   1.235   16.410  1.00 9.68  ? 200 THR A C   1 
ATOM   1614 O  O   . THR A 1 199 ? 0.555   2.232   17.001  1.00 9.39  ? 200 THR A O   1 
ATOM   1615 C  CB  . THR A 1 199 ? -0.357  0.141   14.669  1.00 10.39 ? 200 THR A CB  1 
ATOM   1616 O  OG1 . THR A 1 199 ? -1.209  1.322   14.629  1.00 15.18 ? 200 THR A OG1 1 
ATOM   1617 C  CG2 . THR A 1 199 ? -1.115  -1.056  14.225  1.00 11.17 ? 200 THR A CG2 1 
ATOM   1618 N  N   . PRO A 1 200 ? 2.313   1.250   15.959  1.00 9.32  ? 201 PRO A N   1 
ATOM   1619 C  CA  . PRO A 1 200 ? 3.110   2.543   16.084  1.00 10.20 ? 201 PRO A CA  1 
ATOM   1620 C  C   . PRO A 1 200 ? 2.248   3.712   15.545  1.00 9.68  ? 201 PRO A C   1 
ATOM   1621 O  O   . PRO A 1 200 ? 1.616   3.577   14.453  1.00 11.30 ? 201 PRO A O   1 
ATOM   1622 C  CB  . PRO A 1 200 ? 4.329   2.267   15.138  1.00 11.06 ? 201 PRO A CB  1 
ATOM   1623 C  CG  . PRO A 1 200 ? 4.552   0.744   15.429  1.00 11.66 ? 201 PRO A CG  1 
ATOM   1624 C  CD  . PRO A 1 200 ? 3.105   0.154   15.372  1.00 10.37 ? 201 PRO A CD  1 
ATOM   1625 N  N   . PRO A 1 201 ? 2.286   4.882   16.182  1.00 10.51 ? 202 PRO A N   1 
ATOM   1626 C  CA  . PRO A 1 201 ? 3.239   5.259   17.286  1.00 10.50 ? 202 PRO A CA  1 
ATOM   1627 C  C   . PRO A 1 201 ? 2.850   4.799   18.715  1.00 9.07  ? 202 PRO A C   1 
ATOM   1628 O  O   . PRO A 1 201 ? 3.470   5.233   19.684  1.00 9.55  ? 202 PRO A O   1 
ATOM   1629 C  CB  . PRO A 1 201 ? 3.266   6.788   17.189  1.00 11.54 ? 202 PRO A CB  1 
ATOM   1630 C  CG  . PRO A 1 201 ? 1.869   7.169   16.598  1.00 13.64 ? 202 PRO A CG  1 
ATOM   1631 C  CD  . PRO A 1 201 ? 1.518   6.029   15.649  1.00 10.34 ? 202 PRO A CD  1 
ATOM   1632 N  N   . LEU A 1 202 ? 1.865   3.910   18.840  1.00 8.17  ? 203 LEU A N   1 
ATOM   1633 C  CA  . LEU A 1 202 ? 1.596   3.272   20.152  1.00 7.49  ? 203 LEU A CA  1 
ATOM   1634 C  C   . LEU A 1 202 ? 1.190   4.286   21.264  1.00 7.76  ? 203 LEU A C   1 
ATOM   1635 O  O   . LEU A 1 202 ? 1.374   4.045   22.459  1.00 8.50  ? 203 LEU A O   1 
ATOM   1636 C  CB  . LEU A 1 202 ? 2.755   2.360   20.631  1.00 8.85  ? 203 LEU A CB  1 
ATOM   1637 C  CG  . LEU A 1 202 ? 3.065   1.224   19.651  1.00 7.29  ? 203 LEU A CG  1 
ATOM   1638 C  CD1 . LEU A 1 202 ? 4.393   0.599   20.139  1.00 12.10 ? 203 LEU A CD1 1 
ATOM   1639 C  CD2 . LEU A 1 202 ? 2.015   0.143   19.551  1.00 9.29  ? 203 LEU A CD2 1 
ATOM   1640 N  N   . LEU A 1 203 ? 0.640   5.441   20.823  1.00 7.16  ? 204 LEU A N   1 
ATOM   1641 C  CA  . LEU A 1 203 ? 0.348   6.522   21.763  1.00 8.75  ? 204 LEU A CA  1 
ATOM   1642 C  C   . LEU A 1 203 ? -0.692  6.113   22.823  1.00 6.76  ? 204 LEU A C   1 
ATOM   1643 O  O   . LEU A 1 203 ? -1.691  5.446   22.502  1.00 7.95  ? 204 LEU A O   1 
ATOM   1644 C  CB  . LEU A 1 203 ? -0.102  7.788   21.016  1.00 9.22  ? 204 LEU A CB  1 
ATOM   1645 C  CG  . LEU A 1 203 ? 0.983   8.379   20.120  1.00 11.89 ? 204 LEU A CG  1 
ATOM   1646 C  CD1 . LEU A 1 203 ? 0.410   9.431   19.168  1.00 13.95 ? 204 LEU A CD1 1 
ATOM   1647 C  CD2 . LEU A 1 203 ? 2.192   9.005   20.932  1.00 15.92 ? 204 LEU A CD2 1 
ATOM   1648 N  N   . GLU A 1 204 ? -0.466  6.577   24.056  1.00 8.21  ? 205 GLU A N   1 
ATOM   1649 C  CA  . GLU A 1 204 ? -1.288  6.215   25.182  1.00 6.84  ? 205 GLU A CA  1 
ATOM   1650 C  C   . GLU A 1 204 ? -2.465  7.195   25.319  1.00 8.09  ? 205 GLU A C   1 
ATOM   1651 O  O   . GLU A 1 204 ? -2.559  7.922   26.334  1.00 9.24  ? 205 GLU A O   1 
ATOM   1652 C  CB  . GLU A 1 204 ? -0.447  6.034   26.474  1.00 7.43  ? 205 GLU A CB  1 
ATOM   1653 C  CG  . GLU A 1 204 ? 0.450   4.808   26.260  1.00 9.73  ? 205 GLU A CG  1 
ATOM   1654 C  CD  . GLU A 1 204 ? 1.454   4.578   27.458  1.00 9.68  ? 205 GLU A CD  1 
ATOM   1655 O  OE1 . GLU A 1 204 ? 1.760   5.557   28.229  1.00 12.94 ? 205 GLU A OE1 1 
ATOM   1656 O  OE2 . GLU A 1 204 ? 1.859   3.375   27.640  1.00 10.77 ? 205 GLU A OE2 1 
ATOM   1657 N  N   . CYS A 1 205 ? -3.386  7.094   24.351  1.00 7.75  ? 206 CYS A N   1 
ATOM   1658 C  CA  . CYS A 1 205 ? -4.455  8.095   24.200  1.00 7.53  ? 206 CYS A CA  1 
ATOM   1659 C  C   . CYS A 1 205 ? -5.818  7.458   24.068  1.00 7.87  ? 206 CYS A C   1 
ATOM   1660 O  O   . CYS A 1 205 ? -6.777  8.162   23.753  1.00 8.83  ? 206 CYS A O   1 
ATOM   1661 C  CB  . CYS A 1 205 ? -4.194  8.976   22.969  1.00 8.70  ? 206 CYS A CB  1 
ATOM   1662 S  SG  . CYS A 1 205 ? -4.136  7.947   21.396  1.00 9.80  ? 206 CYS A SG  1 
ATOM   1663 N  N   . VAL A 1 206 ? -5.948  6.146   24.375  1.00 6.69  ? 207 VAL A N   1 
ATOM   1664 C  CA  . VAL A 1 206 ? -7.212  5.446   24.021  1.00 5.86  ? 207 VAL A CA  1 
ATOM   1665 C  C   . VAL A 1 206 ? -8.004  4.981   25.235  1.00 7.06  ? 207 VAL A C   1 
ATOM   1666 O  O   . VAL A 1 206 ? -7.443  4.353   26.139  1.00 7.96  ? 207 VAL A O   1 
ATOM   1667 C  CB  . VAL A 1 206 ? -6.914  4.172   23.207  1.00 5.59  ? 207 VAL A CB  1 
ATOM   1668 C  CG1 . VAL A 1 206 ? -8.281  3.421   22.891  1.00 7.25  ? 207 VAL A CG1 1 
ATOM   1669 C  CG2 . VAL A 1 206 ? -6.145  4.535   21.899  1.00 7.00  ? 207 VAL A CG2 1 
ATOM   1670 N  N   . THR A 1 207 ? -9.288  5.329   25.292  1.00 6.82  ? 208 THR A N   1 
ATOM   1671 C  CA  . THR A 1 207 ? -10.238 4.610   26.166  1.00 5.80  ? 208 THR A CA  1 
ATOM   1672 C  C   . THR A 1 207 ? -10.712 3.445   25.336  1.00 5.37  ? 208 THR A C   1 
ATOM   1673 O  O   . THR A 1 207 ? -11.428 3.629   24.307  1.00 6.36  ? 208 THR A O   1 
ATOM   1674 C  CB  . THR A 1 207 ? -11.430 5.445   26.675  1.00 7.23  ? 208 THR A CB  1 
ATOM   1675 O  OG1 . THR A 1 207 ? -10.884 6.619   27.340  1.00 7.24  ? 208 THR A OG1 1 
ATOM   1676 C  CG2 . THR A 1 207 ? -12.346 4.662   27.583  1.00 8.52  ? 208 THR A CG2 1 
ATOM   1677 N  N   . TRP A 1 208 ? -10.364 2.241   25.775  1.00 5.55  ? 209 TRP A N   1 
ATOM   1678 C  CA  . TRP A 1 208 ? -10.831 1.015   25.031  1.00 5.66  ? 209 TRP A CA  1 
ATOM   1679 C  C   . TRP A 1 208 ? -12.233 0.620   25.524  1.00 5.93  ? 209 TRP A C   1 
ATOM   1680 O  O   . TRP A 1 208 ? -12.469 0.537   26.766  1.00 7.21  ? 209 TRP A O   1 
ATOM   1681 C  CB  . TRP A 1 208 ? -9.830  -0.166  25.271  1.00 5.83  ? 209 TRP A CB  1 
ATOM   1682 C  CG  . TRP A 1 208 ? -8.717  -0.056  24.309  1.00 5.10  ? 209 TRP A CG  1 
ATOM   1683 C  CD1 . TRP A 1 208 ? -7.489  0.567   24.502  1.00 6.77  ? 209 TRP A CD1 1 
ATOM   1684 C  CD2 . TRP A 1 208 ? -8.765  -0.457  22.902  1.00 5.16  ? 209 TRP A CD2 1 
ATOM   1685 N  NE1 . TRP A 1 208 ? -6.773  0.521   23.335  1.00 6.45  ? 209 TRP A NE1 1 
ATOM   1686 C  CE2 . TRP A 1 208 ? -7.526  -0.095  22.330  1.00 5.51  ? 209 TRP A CE2 1 
ATOM   1687 C  CE3 . TRP A 1 208 ? -9.762  -1.106  22.090  1.00 5.81  ? 209 TRP A CE3 1 
ATOM   1688 C  CZ2 . TRP A 1 208 ? -7.230  -0.337  20.971  1.00 6.38  ? 209 TRP A CZ2 1 
ATOM   1689 C  CZ3 . TRP A 1 208 ? -9.457  -1.388  20.775  1.00 6.38  ? 209 TRP A CZ3 1 
ATOM   1690 C  CH2 . TRP A 1 208 ? -8.190  -0.991  20.227  1.00 6.88  ? 209 TRP A CH2 1 
ATOM   1691 N  N   . ILE A 1 209 ? -13.097 0.258   24.565  1.00 5.67  ? 210 ILE A N   1 
ATOM   1692 C  CA  . ILE A 1 209 ? -14.401 -0.277  24.922  1.00 5.29  ? 210 ILE A CA  1 
ATOM   1693 C  C   . ILE A 1 209 ? -14.505 -1.552  24.048  1.00 7.26  ? 210 ILE A C   1 
ATOM   1694 O  O   . ILE A 1 209 ? -14.592 -1.478  22.822  1.00 6.89  ? 210 ILE A O   1 
ATOM   1695 C  CB  . ILE A 1 209 ? -15.507 0.745   24.538  1.00 6.78  ? 210 ILE A CB  1 
ATOM   1696 C  CG1 . ILE A 1 209 ? -15.306 2.030   25.341  1.00 8.16  ? 210 ILE A CG1 1 
ATOM   1697 C  CG2 . ILE A 1 209 ? -16.937 0.125   24.762  1.00 8.61  ? 210 ILE A CG2 1 
ATOM   1698 C  CD1 . ILE A 1 209 ? -16.159 3.239   24.791  1.00 10.37 ? 210 ILE A CD1 1 
ATOM   1699 N  N   . VAL A 1 210 ? -14.496 -2.714  24.716  1.00 7.47  ? 211 VAL A N   1 
ATOM   1700 C  CA  . VAL A 1 210 ? -14.446 -4.013  23.965  1.00 6.60  ? 211 VAL A CA  1 
ATOM   1701 C  C   . VAL A 1 210 ? -15.753 -4.760  24.217  1.00 5.84  ? 211 VAL A C   1 
ATOM   1702 O  O   . VAL A 1 210 ? -16.114 -4.982  25.382  1.00 7.96  ? 211 VAL A O   1 
ATOM   1703 C  CB  . VAL A 1 210 ? -13.244 -4.858  24.413  1.00 6.73  ? 211 VAL A CB  1 
ATOM   1704 C  CG1 . VAL A 1 210 ? -13.200 -6.277  23.698  1.00 7.75  ? 211 VAL A CG1 1 
ATOM   1705 C  CG2 . VAL A 1 210 ? -11.906 -4.111  24.151  1.00 6.15  ? 211 VAL A CG2 1 
ATOM   1706 N  N   . LEU A 1 211 ? -16.505 -4.973  23.130  1.00 6.62  ? 212 LEU A N   1 
ATOM   1707 C  CA  . LEU A 1 211 ? -17.778 -5.672  23.301  1.00 6.93  ? 212 LEU A CA  1 
ATOM   1708 C  C   . LEU A 1 211 ? -17.624 -7.130  23.727  1.00 7.41  ? 212 LEU A C   1 
ATOM   1709 O  O   . LEU A 1 211 ? -16.773 -7.851  23.174  1.00 7.48  ? 212 LEU A O   1 
ATOM   1710 C  CB  . LEU A 1 211 ? -18.613 -5.561  21.974  1.00 7.60  ? 212 LEU A CB  1 
ATOM   1711 C  CG  . LEU A 1 211 ? -19.058 -4.137  21.618  1.00 8.52  ? 212 LEU A CG  1 
ATOM   1712 C  CD1 . LEU A 1 211 ? -20.135 -4.151  20.459  1.00 11.80 ? 212 LEU A CD1 1 
ATOM   1713 C  CD2 . LEU A 1 211 ? -19.523 -3.237  22.816  1.00 10.15 ? 212 LEU A CD2 1 
ATOM   1714 N  N   . LYS A 1 212 ? -18.500 -7.561  24.639  1.00 8.53  ? 213 LYS A N   1 
ATOM   1715 C  CA  . LYS A 1 212 ? -18.464 -8.976  25.060  1.00 10.07 ? 213 LYS A CA  1 
ATOM   1716 C  C   . LYS A 1 212 ? -18.914 -9.909  23.944  1.00 9.06  ? 213 LYS A C   1 
ATOM   1717 O  O   . LYS A 1 212 ? -18.421 -11.029 23.868  1.00 9.71  ? 213 LYS A O   1 
ATOM   1718 C  CB  . LYS A 1 212 ? -19.341 -9.181  26.304  1.00 11.83 ? 213 LYS A CB  1 
ATOM   1719 C  CG  . LYS A 1 212 ? -19.484 -10.711 26.705  1.00 15.76 ? 213 LYS A CG  1 
ATOM   1720 C  CD  . LYS A 1 212 ? -20.282 -10.887 27.994  1.00 18.81 ? 213 LYS A CD  1 
ATOM   1721 C  CE  . LYS A 1 212 ? -20.238 -12.320 28.503  1.00 24.74 ? 213 LYS A CE  1 
ATOM   1722 N  NZ  . LYS A 1 212 ? -21.137 -12.416 29.737  1.00 35.27 ? 213 LYS A NZ  1 
ATOM   1723 N  N   . GLU A 1 213 ? -19.929 -9.548  23.149  1.00 8.11  ? 214 GLU A N   1 
ATOM   1724 C  CA  . GLU A 1 213 ? -20.529 -10.463 22.199  1.00 9.37  ? 214 GLU A CA  1 
ATOM   1725 C  C   . GLU A 1 213 ? -19.773 -10.311 20.858  1.00 7.67  ? 214 GLU A C   1 
ATOM   1726 O  O   . GLU A 1 213 ? -19.736 -9.217  20.275  1.00 7.48  ? 214 GLU A O   1 
ATOM   1727 C  CB  . GLU A 1 213 ? -22.007 -10.131 21.965  1.00 8.72  ? 214 GLU A CB  1 
ATOM   1728 C  CG  . GLU A 1 213 ? -22.646 -11.073 20.919  1.00 11.29 ? 214 GLU A CG  1 
ATOM   1729 C  CD  . GLU A 1 213 ? -24.133 -10.866 20.743  1.00 13.95 ? 214 GLU A CD  1 
ATOM   1730 O  OE1 . GLU A 1 213 ? -24.759 -10.003 21.340  1.00 14.19 ? 214 GLU A OE1 1 
ATOM   1731 O  OE2 . GLU A 1 213 ? -24.705 -11.765 20.063  1.00 22.92 ? 214 GLU A OE2 1 
ATOM   1732 N  N   A PRO A 1 214 ? -19.267 -11.441 20.324  0.50 7.10  ? 215 PRO A N   1 
ATOM   1733 N  N   B PRO A 1 214 ? -19.126 -11.397 20.392  0.50 8.53  ? 215 PRO A N   1 
ATOM   1734 C  CA  A PRO A 1 214 ? -18.627 -11.356 19.039  0.50 6.92  ? 215 PRO A CA  1 
ATOM   1735 C  CA  B PRO A 1 214 ? -18.520 -11.426 19.061  0.50 8.82  ? 215 PRO A CA  1 
ATOM   1736 C  C   A PRO A 1 214 ? -19.669 -11.282 17.943  0.50 7.17  ? 215 PRO A C   1 
ATOM   1737 C  C   B PRO A 1 214 ? -19.550 -11.490 17.916  0.50 8.68  ? 215 PRO A C   1 
ATOM   1738 O  O   A PRO A 1 214 ? -20.889 -11.565 18.199  0.50 7.83  ? 215 PRO A O   1 
ATOM   1739 O  O   B PRO A 1 214 ? -20.655 -12.050 18.120  0.50 9.62  ? 215 PRO A O   1 
ATOM   1740 C  CB  A PRO A 1 214 ? -17.866 -12.713 18.908  0.50 7.03  ? 215 PRO A CB  1 
ATOM   1741 C  CB  B PRO A 1 214 ? -17.699 -12.756 19.058  0.50 9.28  ? 215 PRO A CB  1 
ATOM   1742 C  CG  A PRO A 1 214 ? -18.659 -13.681 19.738  0.50 7.26  ? 215 PRO A CG  1 
ATOM   1743 C  CG  B PRO A 1 214 ? -17.638 -13.207 20.510  0.50 10.93 ? 215 PRO A CG  1 
ATOM   1744 C  CD  A PRO A 1 214 ? -19.332 -12.828 20.846  0.50 5.90  ? 215 PRO A CD  1 
ATOM   1745 C  CD  B PRO A 1 214 ? -18.923 -12.663 21.130  0.50 8.33  ? 215 PRO A CD  1 
ATOM   1746 N  N   . ILE A 1 215 ? -19.200 -10.964 16.737  1.00 7.62  ? 216 ILE A N   1 
ATOM   1747 C  CA  . ILE A 1 215 ? -20.025 -11.178 15.546  1.00 8.08  ? 216 ILE A CA  1 
ATOM   1748 C  C   . ILE A 1 215 ? -19.477 -12.419 14.859  1.00 8.38  ? 216 ILE A C   1 
ATOM   1749 O  O   . ILE A 1 215 ? -18.280 -12.780 15.019  1.00 8.98  ? 216 ILE A O   1 
ATOM   1750 C  CB  . ILE A 1 215 ? -20.016 -9.999  14.541  1.00 7.97  ? 216 ILE A CB  1 
ATOM   1751 C  CG1 . ILE A 1 215 ? -18.586 -9.601  14.144  1.00 10.27 ? 216 ILE A CG1 1 
ATOM   1752 C  CG2 . ILE A 1 215 ? -20.687 -8.752  15.182  1.00 11.02 ? 216 ILE A CG2 1 
ATOM   1753 C  CD1 . ILE A 1 215 ? -18.564 -8.555  12.885  1.00 10.39 ? 216 ILE A CD1 1 
ATOM   1754 N  N   A SER A 1 216 ? -20.368 -13.111 14.100  0.50 8.38  ? 217 SER A N   1 
ATOM   1755 N  N   B SER A 1 216 ? -20.315 -13.061 14.039  0.50 9.32  ? 217 SER A N   1 
ATOM   1756 C  CA  A SER A 1 216 ? -19.936 -14.237 13.248  0.50 7.73  ? 217 SER A CA  1 
ATOM   1757 C  CA  B SER A 1 216 ? -19.770 -14.174 13.294  0.50 9.48  ? 217 SER A CA  1 
ATOM   1758 C  C   A SER A 1 216 ? -19.692 -13.726 11.818  0.50 9.45  ? 217 SER A C   1 
ATOM   1759 C  C   B SER A 1 216 ? -19.733 -13.829 11.821  0.50 10.26 ? 217 SER A C   1 
ATOM   1760 O  O   A SER A 1 216 ? -20.439 -12.882 11.282  0.50 10.89 ? 217 SER A O   1 
ATOM   1761 O  O   B SER A 1 216 ? -20.672 -13.225 11.262  0.50 10.45 ? 217 SER A O   1 
ATOM   1762 C  CB  A SER A 1 216 ? -20.964 -15.394 13.245  0.50 8.81  ? 217 SER A CB  1 
ATOM   1763 C  CB  B SER A 1 216 ? -20.560 -15.414 13.555  0.50 11.81 ? 217 SER A CB  1 
ATOM   1764 O  OG  A SER A 1 216 ? -21.133 -15.956 14.554  0.50 10.48 ? 217 SER A OG  1 
ATOM   1765 O  OG  B SER A 1 216 ? -21.876 -15.199 13.119  0.50 14.91 ? 217 SER A OG  1 
ATOM   1766 N  N   . VAL A 1 217 ? -18.615 -14.223 11.215  1.00 8.69  ? 218 VAL A N   1 
ATOM   1767 C  CA  . VAL A 1 217 ? -18.356 -14.022 9.793   1.00 9.31  ? 218 VAL A CA  1 
ATOM   1768 C  C   . VAL A 1 217 ? -18.073 -15.376 9.175   1.00 9.75  ? 218 VAL A C   1 
ATOM   1769 O  O   . VAL A 1 217 ? -17.711 -16.367 9.899   1.00 10.54 ? 218 VAL A O   1 
ATOM   1770 C  CB  . VAL A 1 217 ? -17.169 -13.013 9.586   1.00 9.36  ? 218 VAL A CB  1 
ATOM   1771 C  CG1 . VAL A 1 217 ? -17.442 -11.716 10.267  1.00 11.58 ? 218 VAL A CG1 1 
ATOM   1772 C  CG2 . VAL A 1 217 ? -15.829 -13.609 10.020  1.00 11.50 ? 218 VAL A CG2 1 
ATOM   1773 N  N   . SER A 1 218 ? -18.255 -15.518 7.880   1.00 10.01 ? 219 SER A N   1 
ATOM   1774 C  CA  . SER A 1 218 ? -18.012 -16.877 7.305   1.00 9.73  ? 219 SER A CA  1 
ATOM   1775 C  C   . SER A 1 218 ? -16.533 -17.150 7.016   1.00 10.66 ? 219 SER A C   1 
ATOM   1776 O  O   . SER A 1 218 ? -15.729 -16.224 6.876   1.00 9.05  ? 219 SER A O   1 
ATOM   1777 C  CB  . SER A 1 218 ? -18.849 -17.093 6.028   1.00 10.98 ? 219 SER A CB  1 
ATOM   1778 O  OG  . SER A 1 218 ? -18.372 -16.205 4.994   1.00 12.35 ? 219 SER A OG  1 
ATOM   1779 N  N   . SER A 1 219 ? -16.175 -18.433 6.876   1.00 11.47 ? 220 SER A N   1 
ATOM   1780 C  CA  . SER A 1 219 ? -14.789 -18.809 6.442   1.00 12.19 ? 220 SER A CA  1 
ATOM   1781 C  C   . SER A 1 219 ? -14.471 -18.100 5.102   1.00 12.84 ? 220 SER A C   1 
ATOM   1782 O  O   . SER A 1 219 ? -13.359 -17.590 4.899   1.00 14.44 ? 220 SER A O   1 
ATOM   1783 C  CB  . SER A 1 219 ? -14.585 -20.344 6.385   1.00 14.16 ? 220 SER A CB  1 
ATOM   1784 O  OG  . SER A 1 219 ? -15.659 -20.844 5.548   1.00 18.84 ? 220 SER A OG  1 
ATOM   1785 N  N   . GLU A 1 220 ? -15.461 -17.981 4.189   1.00 11.62 ? 221 GLU A N   1 
ATOM   1786 C  CA  . GLU A 1 220 ? -15.173 -17.350 2.898   1.00 13.72 ? 221 GLU A CA  1 
ATOM   1787 C  C   . GLU A 1 220 ? -14.870 -15.841 3.100   1.00 11.86 ? 221 GLU A C   1 
ATOM   1788 O  O   . GLU A 1 220 ? -14.003 -15.288 2.377   1.00 12.55 ? 221 GLU A O   1 
ATOM   1789 C  CB  . GLU A 1 220 ? -16.309 -17.481 1.919   1.00 15.35 ? 221 GLU A CB  1 
ATOM   1790 C  CG  . GLU A 1 220 ? -16.517 -18.938 1.454   1.00 18.35 ? 221 GLU A CG  1 
ATOM   1791 C  CD  . GLU A 1 220 ? -17.638 -19.658 2.255   1.00 19.78 ? 221 GLU A CD  1 
ATOM   1792 O  OE1 . GLU A 1 220 ? -17.989 -19.227 3.372   1.00 18.27 ? 221 GLU A OE1 1 
ATOM   1793 O  OE2 . GLU A 1 220 ? -18.106 -20.785 1.861   1.00 29.41 ? 221 GLU A OE2 1 
ATOM   1794 N  N   . GLN A 1 221 ? -15.585 -15.173 4.043   1.00 9.90  ? 222 GLN A N   1 
ATOM   1795 C  CA  . GLN A 1 221 ? -15.313 -13.734 4.207   1.00 9.73  ? 222 GLN A CA  1 
ATOM   1796 C  C   . GLN A 1 221 ? -13.877 -13.557 4.769   1.00 10.96 ? 222 GLN A C   1 
ATOM   1797 O  O   . GLN A 1 221 ? -13.124 -12.690 4.261   1.00 10.97 ? 222 GLN A O   1 
ATOM   1798 C  CB  . GLN A 1 221 ? -16.339 -13.162 5.184   1.00 10.60 ? 222 GLN A CB  1 
ATOM   1799 C  CG  . GLN A 1 221 ? -17.741 -13.068 4.484   1.00 10.88 ? 222 GLN A CG  1 
ATOM   1800 C  CD  . GLN A 1 221 ? -18.874 -12.519 5.378   1.00 10.00 ? 222 GLN A CD  1 
ATOM   1801 O  OE1 . GLN A 1 221 ? -18.990 -12.877 6.576   1.00 11.18 ? 222 GLN A OE1 1 
ATOM   1802 N  NE2 . GLN A 1 221 ? -19.699 -11.609 4.803   1.00 10.93 ? 222 GLN A NE2 1 
ATOM   1803 N  N   A VAL A 1 222 ? -13.480 -14.317 5.808   0.50 10.24 ? 223 VAL A N   1 
ATOM   1804 N  N   B VAL A 1 222 ? -13.501 -14.326 5.801   0.50 11.13 ? 223 VAL A N   1 
ATOM   1805 C  CA  A VAL A 1 222 ? -12.122 -14.069 6.372   0.50 10.95 ? 223 VAL A CA  1 
ATOM   1806 C  CA  B VAL A 1 222 ? -12.152 -14.121 6.354   0.50 12.12 ? 223 VAL A CA  1 
ATOM   1807 C  C   A VAL A 1 222 ? -11.002 -14.607 5.425   0.50 11.22 ? 223 VAL A C   1 
ATOM   1808 C  C   B VAL A 1 222 ? -11.083 -14.500 5.314   0.50 11.96 ? 223 VAL A C   1 
ATOM   1809 O  O   A VAL A 1 222 ? -9.845  -14.132 5.444   0.50 10.52 ? 223 VAL A O   1 
ATOM   1810 O  O   B VAL A 1 222 ? -10.042 -13.826 5.177   0.50 11.77 ? 223 VAL A O   1 
ATOM   1811 C  CB  A VAL A 1 222 ? -11.978 -14.578 7.854   0.50 10.93 ? 223 VAL A CB  1 
ATOM   1812 C  CB  B VAL A 1 222 ? -11.922 -14.934 7.638   0.50 11.86 ? 223 VAL A CB  1 
ATOM   1813 C  CG1 A VAL A 1 222 ? -12.116 -16.112 7.956   0.50 11.78 ? 223 VAL A CG1 1 
ATOM   1814 C  CG1 B VAL A 1 222 ? -12.972 -14.617 8.638   0.50 14.50 ? 223 VAL A CG1 1 
ATOM   1815 C  CG2 A VAL A 1 222 ? -10.673 -14.063 8.519   0.50 8.65  ? 223 VAL A CG2 1 
ATOM   1816 C  CG2 B VAL A 1 222 ? -11.907 -16.421 7.349   0.50 12.29 ? 223 VAL A CG2 1 
ATOM   1817 N  N   . LEU A 1 223 ? -11.352 -15.586 4.565   1.00 12.24 ? 224 LEU A N   1 
ATOM   1818 C  CA  . LEU A 1 223 ? -10.452 -15.970 3.491   1.00 13.88 ? 224 LEU A CA  1 
ATOM   1819 C  C   . LEU A 1 223 ? -10.103 -14.804 2.607   1.00 14.88 ? 224 LEU A C   1 
ATOM   1820 O  O   . LEU A 1 223 ? -8.920  -14.712 2.164   1.00 16.11 ? 224 LEU A O   1 
ATOM   1821 C  CB  . LEU A 1 223 ? -10.937 -17.206 2.702   1.00 16.95 ? 224 LEU A CB  1 
ATOM   1822 C  CG  . LEU A 1 223 ? -10.621 -18.490 3.505   1.00 23.67 ? 224 LEU A CG  1 
ATOM   1823 C  CD1 . LEU A 1 223 ? -11.482 -19.718 3.001   1.00 27.71 ? 224 LEU A CD1 1 
ATOM   1824 C  CD2 . LEU A 1 223 ? -9.122  -18.813 3.508   1.00 27.81 ? 224 LEU A CD2 1 
ATOM   1825 N  N   . LYS A 1 224 ? -11.097 -13.960 2.292   1.00 12.52 ? 225 LYS A N   1 
ATOM   1826 C  CA  . LYS A 1 224 ? -10.809 -12.828 1.412   1.00 14.61 ? 225 LYS A CA  1 
ATOM   1827 C  C   . LYS A 1 224 ? -9.900  -11.812 2.098   1.00 12.63 ? 225 LYS A C   1 
ATOM   1828 O  O   . LYS A 1 224 ? -9.090  -11.164 1.430   1.00 13.74 ? 225 LYS A O   1 
ATOM   1829 C  CB  . LYS A 1 224 ? -12.136 -12.235 0.868   1.00 14.74 ? 225 LYS A CB  1 
ATOM   1830 C  CG  . LYS A 1 224 ? -12.710 -13.306 -0.233  1.00 20.30 ? 225 LYS A CG  1 
ATOM   1831 C  CD  . LYS A 1 224 ? -14.096 -12.948 -0.684  1.00 23.97 ? 225 LYS A CD  1 
ATOM   1832 C  CE  . LYS A 1 224 ? -14.137 -11.838 -1.706  1.00 30.87 ? 225 LYS A CE  1 
ATOM   1833 N  NZ  . LYS A 1 224 ? -14.065 -12.476 -3.037  1.00 34.03 ? 225 LYS A NZ  1 
ATOM   1834 N  N   . PHE A 1 225 ? -10.022 -11.635 3.430   1.00 10.35 ? 226 PHE A N   1 
ATOM   1835 C  CA  . PHE A 1 225 ? -9.034  -10.763 4.109   1.00 9.19  ? 226 PHE A CA  1 
ATOM   1836 C  C   . PHE A 1 225 ? -7.636  -11.258 3.867   1.00 10.21 ? 226 PHE A C   1 
ATOM   1837 O  O   . PHE A 1 225 ? -6.697  -10.478 3.672   1.00 11.19 ? 226 PHE A O   1 
ATOM   1838 C  CB  . PHE A 1 225 ? -9.234  -10.776 5.651   1.00 9.69  ? 226 PHE A CB  1 
ATOM   1839 C  CG  . PHE A 1 225 ? -10.455 -10.009 6.184   1.00 8.87  ? 226 PHE A CG  1 
ATOM   1840 C  CD1 . PHE A 1 225 ? -11.514 -9.546  5.382   1.00 12.49 ? 226 PHE A CD1 1 
ATOM   1841 C  CD2 . PHE A 1 225 ? -10.548 -9.821  7.625   1.00 10.98 ? 226 PHE A CD2 1 
ATOM   1842 C  CE1 . PHE A 1 225 ? -12.598 -8.837  6.003   1.00 12.65 ? 226 PHE A CE1 1 
ATOM   1843 C  CE2 . PHE A 1 225 ? -11.624 -9.183  8.238   1.00 12.95 ? 226 PHE A CE2 1 
ATOM   1844 C  CZ  . PHE A 1 225 ? -12.646 -8.689  7.439   1.00 12.14 ? 226 PHE A CZ  1 
ATOM   1845 N  N   . ARG A 1 226 ? -7.453  -12.588 3.937   1.00 10.31 ? 227 ARG A N   1 
ATOM   1846 C  CA  . ARG A 1 226 ? -6.094  -13.152 3.875   1.00 11.83 ? 227 ARG A CA  1 
ATOM   1847 C  C   . ARG A 1 226 ? -5.493  -13.149 2.454   1.00 12.20 ? 227 ARG A C   1 
ATOM   1848 O  O   . ARG A 1 226 ? -4.372  -13.624 2.282   1.00 14.67 ? 227 ARG A O   1 
ATOM   1849 C  CB  . ARG A 1 226 ? -6.133  -14.578 4.395   1.00 11.74 ? 227 ARG A CB  1 
ATOM   1850 C  CG  . ARG A 1 226 ? -6.673  -14.750 5.829   1.00 11.24 ? 227 ARG A CG  1 
ATOM   1851 C  CD  . ARG A 1 226 ? -6.617  -16.250 6.266   1.00 12.50 ? 227 ARG A CD  1 
ATOM   1852 N  NE  . ARG A 1 226 ? -7.110  -16.368 7.629   1.00 12.75 ? 227 ARG A NE  1 
ATOM   1853 C  CZ  . ARG A 1 226 ? -8.051  -17.234 8.014   1.00 12.10 ? 227 ARG A CZ  1 
ATOM   1854 N  NH1 . ARG A 1 226 ? -8.476  -18.202 7.153   1.00 15.21 ? 227 ARG A NH1 1 
ATOM   1855 N  NH2 . ARG A 1 226 ? -8.498  -17.198 9.249   1.00 12.37 ? 227 ARG A NH2 1 
ATOM   1856 N  N   . LYS A 1 227 ? -6.262  -12.697 1.450   1.00 12.88 ? 228 LYS A N   1 
ATOM   1857 C  CA  . LYS A 1 227 ? -5.726  -12.569 0.106   1.00 14.12 ? 228 LYS A CA  1 
ATOM   1858 C  C   . LYS A 1 227 ? -5.105  -11.209 -0.160  1.00 12.98 ? 228 LYS A C   1 
ATOM   1859 O  O   . LYS A 1 227 ? -4.479  -10.994 -1.221  1.00 13.95 ? 228 LYS A O   1 
ATOM   1860 C  CB  . LYS A 1 227 ? -6.827  -12.799 -0.950  1.00 15.72 ? 228 LYS A CB  1 
ATOM   1861 C  CG  . LYS A 1 227 ? -7.208  -14.270 -1.065  1.00 18.57 ? 228 LYS A CG  1 
ATOM   1862 C  CD  . LYS A 1 227 ? -8.450  -14.489 -1.916  1.00 26.05 ? 228 LYS A CD  1 
ATOM   1863 C  CE  . LYS A 1 227 ? -8.125  -14.594 -3.389  1.00 34.47 ? 228 LYS A CE  1 
ATOM   1864 N  NZ  . LYS A 1 227 ? -7.168  -15.767 -3.575  1.00 38.01 ? 228 LYS A NZ  1 
ATOM   1865 N  N   . LEU A 1 228 ? -5.328  -10.285 0.789   1.00 12.62 ? 229 LEU A N   1 
ATOM   1866 C  CA  . LEU A 1 228 ? -4.687  -8.990  0.676   1.00 12.72 ? 229 LEU A CA  1 
ATOM   1867 C  C   . LEU A 1 228 ? -3.134  -9.132  0.798   1.00 13.86 ? 229 LEU A C   1 
ATOM   1868 O  O   . LEU A 1 228 ? -2.613  -10.155 1.243   1.00 13.18 ? 229 LEU A O   1 
ATOM   1869 C  CB  . LEU A 1 228 ? -5.203  -8.049  1.756   1.00 11.60 ? 229 LEU A CB  1 
ATOM   1870 C  CG  . LEU A 1 228 ? -6.646  -7.572  1.617   1.00 11.80 ? 229 LEU A CG  1 
ATOM   1871 C  CD1 . LEU A 1 228 ? -7.134  -6.985  2.908   1.00 10.85 ? 229 LEU A CD1 1 
ATOM   1872 C  CD2 . LEU A 1 228 ? -6.722  -6.496  0.494   1.00 13.70 ? 229 LEU A CD2 1 
ATOM   1873 N  N   . ASN A 1 229 ? -2.424  -8.053  0.467   1.00 13.78 ? 230 ASN A N   1 
ATOM   1874 C  CA  . ASN A 1 229 ? -0.966  -8.076  0.445   1.00 14.01 ? 230 ASN A CA  1 
ATOM   1875 C  C   . ASN A 1 229 ? -0.419  -6.942  1.330   1.00 15.92 ? 230 ASN A C   1 
ATOM   1876 O  O   . ASN A 1 229 ? -0.908  -5.811  1.281   1.00 15.92 ? 230 ASN A O   1 
ATOM   1877 C  CB  . ASN A 1 229 ? -0.430  -7.833  -0.985  1.00 14.93 ? 230 ASN A CB  1 
ATOM   1878 C  CG  . ASN A 1 229 ? -0.390  -9.111  -1.899  1.00 17.44 ? 230 ASN A CG  1 
ATOM   1879 O  OD1 . ASN A 1 229 ? 0.212   -9.022  -2.984  1.00 20.83 ? 230 ASN A OD1 1 
ATOM   1880 N  ND2 . ASN A 1 229 ? -1.052  -10.243 -1.503  1.00 15.40 ? 230 ASN A ND2 1 
ATOM   1881 N  N   . PHE A 1 230 ? 0.620   -7.275  2.076   1.00 15.17 ? 231 PHE A N   1 
ATOM   1882 C  CA  . PHE A 1 230 ? 1.336   -6.168  2.786   1.00 14.91 ? 231 PHE A CA  1 
ATOM   1883 C  C   . PHE A 1 230 ? 2.236   -5.352  1.815   1.00 17.68 ? 231 PHE A C   1 
ATOM   1884 O  O   . PHE A 1 230 ? 2.511   -4.148  2.054   1.00 17.50 ? 231 PHE A O   1 
ATOM   1885 C  CB  . PHE A 1 230 ? 2.336   -6.741  3.778   1.00 15.51 ? 231 PHE A CB  1 
ATOM   1886 C  CG  . PHE A 1 230 ? 1.757   -7.334  5.063   1.00 15.17 ? 231 PHE A CG  1 
ATOM   1887 C  CD1 . PHE A 1 230 ? 0.961   -6.543  5.958   1.00 12.21 ? 231 PHE A CD1 1 
ATOM   1888 C  CD2 . PHE A 1 230 ? 2.142   -8.644  5.438   1.00 13.04 ? 231 PHE A CD2 1 
ATOM   1889 C  CE1 . PHE A 1 230 ? 0.523   -7.077  7.209   1.00 14.09 ? 231 PHE A CE1 1 
ATOM   1890 C  CE2 . PHE A 1 230 ? 1.702   -9.223  6.697   1.00 15.22 ? 231 PHE A CE2 1 
ATOM   1891 C  CZ  . PHE A 1 230 ? 0.891   -8.431  7.549   1.00 14.92 ? 231 PHE A CZ  1 
ATOM   1892 N  N   . ASN A 1 231 ? 2.746   -6.013  0.784   1.00 16.50 ? 232 ASN A N   1 
ATOM   1893 C  CA  . ASN A 1 231 ? 3.595   -5.335  -0.237  1.00 17.48 ? 232 ASN A CA  1 
ATOM   1894 C  C   . ASN A 1 231 ? 2.821   -4.428  -1.188  1.00 17.53 ? 232 ASN A C   1 
ATOM   1895 O  O   . ASN A 1 231 ? 1.585   -4.536  -1.308  1.00 17.49 ? 232 ASN A O   1 
ATOM   1896 C  CB  . ASN A 1 231 ? 4.259   -6.434  -1.046  1.00 18.07 ? 232 ASN A CB  1 
ATOM   1897 C  CG  . ASN A 1 231 ? 3.223   -7.377  -1.602  1.00 18.03 ? 232 ASN A CG  1 
ATOM   1898 O  OD1 . ASN A 1 231 ? 2.799   -8.288  -0.862  1.00 20.15 ? 232 ASN A OD1 1 
ATOM   1899 N  ND2 . ASN A 1 231 ? 2.841   -7.217  -2.916  1.00 18.79 ? 232 ASN A ND2 1 
ATOM   1900 N  N   . GLY A 1 232 ? 3.566   -3.527  -1.899  1.00 19.04 ? 233 GLY A N   1 
ATOM   1901 C  CA  . GLY A 1 232 ? 2.950   -2.716  -2.952  1.00 21.45 ? 233 GLY A CA  1 
ATOM   1902 C  C   . GLY A 1 232 ? 2.971   -3.477  -4.259  1.00 20.78 ? 233 GLY A C   1 
ATOM   1903 O  O   . GLY A 1 232 ? 3.658   -4.505  -4.342  1.00 20.56 ? 233 GLY A O   1 
ATOM   1904 N  N   . GLU A 1 233 ? 2.194   -3.011  -5.254  1.00 21.11 ? 234 GLU A N   1 
ATOM   1905 C  CA  . GLU A 1 233 ? 2.149   -3.629  -6.590  1.00 21.30 ? 234 GLU A CA  1 
ATOM   1906 C  C   . GLU A 1 233 ? 3.532   -3.690  -7.196  1.00 22.53 ? 234 GLU A C   1 
ATOM   1907 O  O   . GLU A 1 233 ? 4.313   -2.725  -7.093  1.00 22.70 ? 234 GLU A O   1 
ATOM   1908 C  CB  . GLU A 1 233 ? 1.237   -2.768  -7.479  1.00 21.16 ? 234 GLU A CB  1 
ATOM   1909 C  CG  . GLU A 1 233 ? 0.872   -3.376  -8.839  1.00 20.10 ? 234 GLU A CG  1 
ATOM   1910 C  CD  . GLU A 1 233 ? -0.011  -2.452  -9.627  1.00 24.20 ? 234 GLU A CD  1 
ATOM   1911 O  OE1 . GLU A 1 233 ? -0.287  -1.286  -9.162  1.00 27.24 ? 234 GLU A OE1 1 
ATOM   1912 O  OE2 . GLU A 1 233 ? -0.410  -2.907  -10.731 1.00 27.96 ? 234 GLU A OE2 1 
ATOM   1913 N  N   . GLY A 1 234 ? 3.833   -4.828  -7.853  1.00 22.23 ? 235 GLY A N   1 
ATOM   1914 C  CA  . GLY A 1 234 ? 5.131   -5.004  -8.478  1.00 24.31 ? 235 GLY A CA  1 
ATOM   1915 C  C   . GLY A 1 234 ? 6.210   -5.386  -7.493  1.00 25.20 ? 235 GLY A C   1 
ATOM   1916 O  O   . GLY A 1 234 ? 7.402   -5.317  -7.830  1.00 26.33 ? 235 GLY A O   1 
ATOM   1917 N  N   . GLU A 1 235 ? 5.814   -5.830  -6.286  1.00 25.34 ? 236 GLU A N   1 
ATOM   1918 C  CA  . GLU A 1 235 ? 6.778   -6.302  -5.276  1.00 26.04 ? 236 GLU A CA  1 
ATOM   1919 C  C   . GLU A 1 235 ? 6.431   -7.766  -4.945  1.00 26.94 ? 236 GLU A C   1 
ATOM   1920 O  O   . GLU A 1 235 ? 5.352   -8.244  -5.306  1.00 27.94 ? 236 GLU A O   1 
ATOM   1921 C  CB  . GLU A 1 235 ? 6.658   -5.429  -3.993  1.00 26.53 ? 236 GLU A CB  1 
ATOM   1922 C  CG  . GLU A 1 235 ? 7.358   -4.115  -4.026  1.00 26.75 ? 236 GLU A CG  1 
ATOM   1923 C  CD  . GLU A 1 235 ? 6.999   -3.224  -2.868  1.00 30.92 ? 236 GLU A CD  1 
ATOM   1924 O  OE1 . GLU A 1 235 ? 6.690   -3.707  -1.722  1.00 35.47 ? 236 GLU A OE1 1 
ATOM   1925 O  OE2 . GLU A 1 235 ? 7.025   -2.008  -3.114  1.00 34.15 ? 236 GLU A OE2 1 
ATOM   1926 N  N   . PRO A 1 236 ? 7.380   -8.506  -4.363  1.00 25.94 ? 237 PRO A N   1 
ATOM   1927 C  CA  . PRO A 1 236 ? 7.182   -9.905  -3.992  1.00 26.59 ? 237 PRO A CA  1 
ATOM   1928 C  C   . PRO A 1 236 ? 5.973   -10.004 -3.045  1.00 24.71 ? 237 PRO A C   1 
ATOM   1929 O  O   . PRO A 1 236 ? 5.851   -9.193  -2.118  1.00 23.75 ? 237 PRO A O   1 
ATOM   1930 C  CB  . PRO A 1 236 ? 8.457   -10.244 -3.256  1.00 27.97 ? 237 PRO A CB  1 
ATOM   1931 C  CG  . PRO A 1 236 ? 9.494   -9.334  -3.867  1.00 27.23 ? 237 PRO A CG  1 
ATOM   1932 C  CD  . PRO A 1 236 ? 8.762   -8.046  -4.095  1.00 28.02 ? 237 PRO A CD  1 
ATOM   1933 N  N   . GLU A 1 237 ? 5.120   -10.982 -3.312  1.00 23.64 ? 238 GLU A N   1 
ATOM   1934 C  CA  . GLU A 1 237 ? 3.849   -11.137 -2.584  1.00 20.47 ? 238 GLU A CA  1 
ATOM   1935 C  C   . GLU A 1 237 ? 4.104   -11.650 -1.148  1.00 20.12 ? 238 GLU A C   1 
ATOM   1936 O  O   . GLU A 1 237 ? 4.633   -12.725 -0.941  1.00 19.97 ? 238 GLU A O   1 
ATOM   1937 C  CB  . GLU A 1 237 ? 2.868   -12.109 -3.297  1.00 21.87 ? 238 GLU A CB  1 
ATOM   1938 C  CG  . GLU A 1 237 ? 1.539   -12.230 -2.540  1.00 20.22 ? 238 GLU A CG  1 
ATOM   1939 C  CD  . GLU A 1 237 ? 0.450   -12.899 -3.337  1.00 21.71 ? 238 GLU A CD  1 
ATOM   1940 O  OE1 . GLU A 1 237 ? 0.796   -13.924 -4.020  1.00 28.22 ? 238 GLU A OE1 1 
ATOM   1941 O  OE2 . GLU A 1 237 ? -0.739  -12.441 -3.310  1.00 19.85 ? 238 GLU A OE2 1 
ATOM   1942 N  N   A GLU A 1 238 ? 3.544   -10.823 -0.261  0.50 16.33 ? 239 GLU A N   1 
ATOM   1943 N  N   B GLU A 1 238 ? 3.745   -10.900 -0.113  0.50 17.60 ? 239 GLU A N   1 
ATOM   1944 C  CA  A GLU A 1 238 ? 3.486   -11.036 1.195   0.50 16.08 ? 239 GLU A CA  1 
ATOM   1945 C  CA  B GLU A 1 238 ? 3.764   -11.438 1.309   0.50 16.01 ? 239 GLU A CA  1 
ATOM   1946 C  C   A GLU A 1 238 ? 2.026   -11.031 1.594   0.50 13.20 ? 239 GLU A C   1 
ATOM   1947 C  C   B GLU A 1 238 ? 2.309   -11.162 1.780   0.50 14.20 ? 239 GLU A C   1 
ATOM   1948 O  O   A GLU A 1 238 ? 1.319   -9.938  1.552   0.50 12.39 ? 239 GLU A O   1 
ATOM   1949 O  O   B GLU A 1 238 ? 1.916   -10.014 1.900   0.50 15.15 ? 239 GLU A O   1 
ATOM   1950 C  CB  A GLU A 1 238 ? 4.145   -9.879  1.942   0.50 13.58 ? 239 GLU A CB  1 
ATOM   1951 C  CB  B GLU A 1 238 ? 4.814   -10.723 2.248   0.50 15.37 ? 239 GLU A CB  1 
ATOM   1952 C  CG  A GLU A 1 238 ? 5.588   -9.628  1.658   0.50 14.41 ? 239 GLU A CG  1 
ATOM   1953 C  CG  B GLU A 1 238 ? 6.359   -11.206 2.114   0.50 16.19 ? 239 GLU A CG  1 
ATOM   1954 C  CD  A GLU A 1 238 ? 6.152   -8.369  2.350   0.50 18.65 ? 239 GLU A CD  1 
ATOM   1955 C  CD  B GLU A 1 238 ? 7.388   -10.434 3.009   0.50 16.91 ? 239 GLU A CD  1 
ATOM   1956 O  OE1 A GLU A 1 238 ? 5.611   -7.860  3.366   0.50 20.23 ? 239 GLU A OE1 1 
ATOM   1957 O  OE1 B GLU A 1 238 ? 7.445   -10.590 4.274   0.50 17.27 ? 239 GLU A OE1 1 
ATOM   1958 O  OE2 A GLU A 1 238 ? 7.185   -7.909  1.863   0.50 24.33 ? 239 GLU A OE2 1 
ATOM   1959 O  OE2 B GLU A 1 238 ? 8.200   -9.665  2.417   0.50 22.06 ? 239 GLU A OE2 1 
ATOM   1960 N  N   . LEU A 1 239 ? 1.497   -12.221 1.962   1.00 13.48 ? 240 LEU A N   1 
ATOM   1961 C  CA  . LEU A 1 239 ? 0.041   -12.123 2.309   1.00 12.09 ? 240 LEU A CA  1 
ATOM   1962 C  C   . LEU A 1 239 ? -0.130  -11.295 3.601   1.00 11.79 ? 240 LEU A C   1 
ATOM   1963 O  O   . LEU A 1 239 ? 0.670   -11.458 4.570   1.00 14.29 ? 240 LEU A O   1 
ATOM   1964 C  CB  . LEU A 1 239 ? -0.556  -13.526 2.548   1.00 12.76 ? 240 LEU A CB  1 
ATOM   1965 C  CG  . LEU A 1 239 ? -0.611  -14.381 1.271   1.00 13.64 ? 240 LEU A CG  1 
ATOM   1966 C  CD1 . LEU A 1 239 ? -1.225  -15.737 1.704   1.00 18.30 ? 240 LEU A CD1 1 
ATOM   1967 C  CD2 . LEU A 1 239 ? -1.380  -13.689 0.142   1.00 13.74 ? 240 LEU A CD2 1 
ATOM   1968 N  N   . MET A 1 240 ? -1.173  -10.477 3.604   1.00 11.69 ? 241 MET A N   1 
ATOM   1969 C  CA  . MET A 1 240 ? -1.503  -9.658  4.767   1.00 12.28 ? 241 MET A CA  1 
ATOM   1970 C  C   . MET A 1 240 ? -2.277  -10.599 5.731   1.00 12.16 ? 241 MET A C   1 
ATOM   1971 O  O   . MET A 1 240 ? -3.478  -10.774 5.605   1.00 11.33 ? 241 MET A O   1 
ATOM   1972 C  CB  . MET A 1 240 ? -2.402  -8.502  4.356   1.00 13.28 ? 241 MET A CB  1 
ATOM   1973 C  CG  . MET A 1 240 ? -2.676  -7.498  5.553   1.00 12.99 ? 241 MET A CG  1 
ATOM   1974 S  SD  . MET A 1 240 ? -3.611  -6.091  5.055   1.00 15.21 ? 241 MET A SD  1 
ATOM   1975 C  CE  . MET A 1 240 ? -2.258  -5.056  4.377   1.00 14.16 ? 241 MET A CE  1 
ATOM   1976 N  N   . VAL A 1 241 ? -1.519  -11.263 6.611   1.00 11.08 ? 242 VAL A N   1 
ATOM   1977 C  CA  . VAL A 1 241 ? -2.081  -12.127 7.675   1.00 9.36  ? 242 VAL A CA  1 
ATOM   1978 C  C   . VAL A 1 241 ? -1.283  -11.869 8.986   1.00 9.56  ? 242 VAL A C   1 
ATOM   1979 O  O   . VAL A 1 241 ? -0.101  -11.462 8.914   1.00 10.68 ? 242 VAL A O   1 
ATOM   1980 C  CB  . VAL A 1 241 ? -2.015  -13.633 7.299   1.00 9.69  ? 242 VAL A CB  1 
ATOM   1981 C  CG1 . VAL A 1 241 ? -2.936  -13.878 6.044   1.00 9.79  ? 242 VAL A CG1 1 
ATOM   1982 C  CG2 . VAL A 1 241 ? -0.582  -14.113 7.113   1.00 10.38 ? 242 VAL A CG2 1 
ATOM   1983 N  N   . ASP A 1 242 ? -1.899  -12.187 10.121  1.00 7.93  ? 243 ASP A N   1 
ATOM   1984 C  CA  . ASP A 1 242 ? -1.253  -12.074 11.420  1.00 8.49  ? 243 ASP A CA  1 
ATOM   1985 C  C   . ASP A 1 242 ? -0.742  -10.623 11.644  1.00 7.88  ? 243 ASP A C   1 
ATOM   1986 O  O   . ASP A 1 242 ? 0.367   -10.379 12.161  1.00 11.09 ? 243 ASP A O   1 
ATOM   1987 C  CB  . ASP A 1 242 ? -0.111  -13.143 11.627  1.00 7.46  ? 243 ASP A CB  1 
ATOM   1988 C  CG  . ASP A 1 242 ? -0.674  -14.554 11.715  1.00 8.61  ? 243 ASP A CG  1 
ATOM   1989 O  OD1 . ASP A 1 242 ? -1.753  -14.707 12.356  1.00 10.86 ? 243 ASP A OD1 1 
ATOM   1990 O  OD2 . ASP A 1 242 ? -0.076  -15.464 11.097  1.00 11.28 ? 243 ASP A OD2 1 
ATOM   1991 N  N   . ASN A 1 243 ? -1.636  -9.671  11.341  1.00 6.84  ? 244 ASN A N   1 
ATOM   1992 C  CA  . ASN A 1 243 ? -1.312  -8.245  11.589  1.00 7.51  ? 244 ASN A CA  1 
ATOM   1993 C  C   . ASN A 1 243 ? -1.896  -7.807  12.959  1.00 6.76  ? 244 ASN A C   1 
ATOM   1994 O  O   . ASN A 1 243 ? -2.610  -6.758  13.039  1.00 8.44  ? 244 ASN A O   1 
ATOM   1995 C  CB  . ASN A 1 243 ? -1.896  -7.394  10.434  1.00 8.69  ? 244 ASN A CB  1 
ATOM   1996 C  CG  . ASN A 1 243 ? -3.394  -7.568  10.219  1.00 8.65  ? 244 ASN A CG  1 
ATOM   1997 O  OD1 . ASN A 1 243 ? -4.054  -8.444  10.806  1.00 9.82  ? 244 ASN A OD1 1 
ATOM   1998 N  ND2 . ASN A 1 243 ? -3.955  -6.676  9.400   1.00 13.27 ? 244 ASN A ND2 1 
ATOM   1999 N  N   . TRP A 1 244 ? -1.606  -8.600  13.989  1.00 6.19  ? 245 TRP A N   1 
ATOM   2000 C  CA  . TRP A 1 244 ? -2.058  -8.352  15.348  1.00 6.08  ? 245 TRP A CA  1 
ATOM   2001 C  C   . TRP A 1 244 ? -0.869  -8.227  16.283  1.00 7.69  ? 245 TRP A C   1 
ATOM   2002 O  O   . TRP A 1 244 ? 0.130   -8.967  16.126  1.00 8.26  ? 245 TRP A O   1 
ATOM   2003 C  CB  . TRP A 1 244 ? -3.057  -9.432  15.864  1.00 6.65  ? 245 TRP A CB  1 
ATOM   2004 C  CG  . TRP A 1 244 ? -2.553  -10.841 15.674  1.00 5.80  ? 245 TRP A CG  1 
ATOM   2005 C  CD1 . TRP A 1 244 ? -2.701  -11.598 14.526  1.00 8.75  ? 245 TRP A CD1 1 
ATOM   2006 C  CD2 . TRP A 1 244 ? -1.982  -11.700 16.664  1.00 7.07  ? 245 TRP A CD2 1 
ATOM   2007 N  NE1 . TRP A 1 244 ? -2.168  -12.896 14.728  1.00 7.21  ? 245 TRP A NE1 1 
ATOM   2008 C  CE2 . TRP A 1 244 ? -1.704  -12.962 16.029  1.00 7.02  ? 245 TRP A CE2 1 
ATOM   2009 C  CE3 . TRP A 1 244 ? -1.672  -11.540 18.031  1.00 8.43  ? 245 TRP A CE3 1 
ATOM   2010 C  CZ2 . TRP A 1 244 ? -1.092  -14.032 16.718  1.00 8.79  ? 245 TRP A CZ2 1 
ATOM   2011 C  CZ3 . TRP A 1 244 ? -1.056  -12.618 18.712  1.00 9.38  ? 245 TRP A CZ3 1 
ATOM   2012 C  CH2 . TRP A 1 244 ? -0.799  -13.850 18.046  1.00 9.33  ? 245 TRP A CH2 1 
ATOM   2013 N  N   . ARG A 1 245 ? -1.019  -7.317  17.251  1.00 7.01  ? 246 ARG A N   1 
ATOM   2014 C  CA  . ARG A 1 245 ? -0.037  -7.221  18.347  1.00 7.03  ? 246 ARG A CA  1 
ATOM   2015 C  C   . ARG A 1 245 ? -0.525  -8.126  19.504  1.00 8.04  ? 246 ARG A C   1 
ATOM   2016 O  O   . ARG A 1 245 ? -1.695  -8.128  19.809  1.00 8.55  ? 246 ARG A O   1 
ATOM   2017 C  CB  . ARG A 1 245 ? 0.015   -5.756  18.863  1.00 7.07  ? 246 ARG A CB  1 
ATOM   2018 C  CG  . ARG A 1 245 ? 1.087   -5.540  19.892  1.00 6.63  ? 246 ARG A CG  1 
ATOM   2019 C  CD  . ARG A 1 245 ? 1.011   -4.144  20.509  1.00 8.16  ? 246 ARG A CD  1 
ATOM   2020 N  NE  . ARG A 1 245 ? 2.301   -3.840  21.225  1.00 9.38  ? 246 ARG A NE  1 
ATOM   2021 C  CZ  . ARG A 1 245 ? 2.506   -2.834  22.078  1.00 7.64  ? 246 ARG A CZ  1 
ATOM   2022 N  NH1 . ARG A 1 245 ? 1.478   -2.019  22.412  1.00 9.04  ? 246 ARG A NH1 1 
ATOM   2023 N  NH2 . ARG A 1 245 ? 3.756   -2.604  22.551  1.00 10.69 ? 246 ARG A NH2 1 
ATOM   2024 N  N   . PRO A 1 246 ? 0.352   -8.916  20.128  1.00 8.87  ? 247 PRO A N   1 
ATOM   2025 C  CA  . PRO A 1 246 ? -0.061  -9.765  21.272  1.00 7.69  ? 247 PRO A CA  1 
ATOM   2026 C  C   . PRO A 1 246 ? -0.398  -8.965  22.514  1.00 7.64  ? 247 PRO A C   1 
ATOM   2027 O  O   . PRO A 1 246 ? -0.014  -7.757  22.635  1.00 8.85  ? 247 PRO A O   1 
ATOM   2028 C  CB  . PRO A 1 246 ? 1.188   -10.605 21.566  1.00 10.07 ? 247 PRO A CB  1 
ATOM   2029 C  CG  . PRO A 1 246 ? 2.092   -10.425 20.432  1.00 13.26 ? 247 PRO A CG  1 
ATOM   2030 C  CD  . PRO A 1 246 ? 1.780   -9.122  19.788  1.00 9.56  ? 247 PRO A CD  1 
ATOM   2031 N  N   . ALA A 1 247 ? -1.050  -9.637  23.482  1.00 8.18  ? 248 ALA A N   1 
ATOM   2032 C  CA  . ALA A 1 247 ? -1.381  -8.977  24.751  1.00 7.64  ? 248 ALA A CA  1 
ATOM   2033 C  C   . ALA A 1 247 ? -0.136  -8.452  25.463  1.00 7.09  ? 248 ALA A C   1 
ATOM   2034 O  O   . ALA A 1 247 ? 0.935   -9.121  25.501  1.00 9.77  ? 248 ALA A O   1 
ATOM   2035 C  CB  . ALA A 1 247 ? -2.156  -9.982  25.650  1.00 9.51  ? 248 ALA A CB  1 
ATOM   2036 N  N   . GLN A 1 248 ? -0.295  -7.262  26.078  1.00 8.39  ? 249 GLN A N   1 
ATOM   2037 C  CA  . GLN A 1 248 ? 0.776   -6.538  26.765  1.00 8.25  ? 249 GLN A CA  1 
ATOM   2038 C  C   . GLN A 1 248 ? 0.504   -6.560  28.297  1.00 9.71  ? 249 GLN A C   1 
ATOM   2039 O  O   . GLN A 1 248 ? -0.651  -6.759  28.724  1.00 9.15  ? 249 GLN A O   1 
ATOM   2040 C  CB  . GLN A 1 248 ? 0.778   -5.089  26.268  1.00 8.21  ? 249 GLN A CB  1 
ATOM   2041 C  CG  . GLN A 1 248 ? 1.105   -5.094  24.751  1.00 9.33  ? 249 GLN A CG  1 
ATOM   2042 C  CD  . GLN A 1 248 ? 2.493   -5.731  24.399  1.00 10.05 ? 249 GLN A CD  1 
ATOM   2043 O  OE1 . GLN A 1 248 ? 3.550   -5.374  24.975  1.00 11.90 ? 249 GLN A OE1 1 
ATOM   2044 N  NE2 . GLN A 1 248 ? 2.492   -6.679  23.432  1.00 10.63 ? 249 GLN A NE2 1 
ATOM   2045 N  N   . PRO A 1 249 ? 1.519   -6.302  29.130  1.00 11.67 ? 250 PRO A N   1 
ATOM   2046 C  CA  . PRO A 1 249 ? 1.316   -6.321  30.562  1.00 11.90 ? 250 PRO A CA  1 
ATOM   2047 C  C   . PRO A 1 249 ? 0.196   -5.334  31.007  1.00 10.87 ? 250 PRO A C   1 
ATOM   2048 O  O   . PRO A 1 249 ? 0.217   -4.151  30.611  1.00 11.53 ? 250 PRO A O   1 
ATOM   2049 C  CB  . PRO A 1 249 ? 2.693   -5.853  31.105  1.00 12.67 ? 250 PRO A CB  1 
ATOM   2050 C  CG  . PRO A 1 249 ? 3.680   -6.339  30.068  1.00 15.76 ? 250 PRO A CG  1 
ATOM   2051 C  CD  . PRO A 1 249 ? 2.910   -6.052  28.749  1.00 13.13 ? 250 PRO A CD  1 
ATOM   2052 N  N   . LEU A 1 250 ? -0.697  -5.804  31.858  1.00 11.42 ? 251 LEU A N   1 
ATOM   2053 C  CA  . LEU A 1 250 ? -1.745  -4.945  32.383  1.00 10.72 ? 251 LEU A CA  1 
ATOM   2054 C  C   . LEU A 1 250 ? -1.195  -3.816  33.321  1.00 12.12 ? 251 LEU A C   1 
ATOM   2055 O  O   . LEU A 1 250 ? -1.772  -2.686  33.401  1.00 10.97 ? 251 LEU A O   1 
ATOM   2056 C  CB  . LEU A 1 250 ? -2.832  -5.774  33.095  1.00 12.16 ? 251 LEU A CB  1 
ATOM   2057 C  CG  . LEU A 1 250 ? -4.093  -5.055  33.552  1.00 13.98 ? 251 LEU A CG  1 
ATOM   2058 C  CD1 . LEU A 1 250 ? -4.894  -4.456  32.361  1.00 12.78 ? 251 LEU A CD1 1 
ATOM   2059 C  CD2 . LEU A 1 250 ? -4.929  -6.118  34.302  1.00 16.53 ? 251 LEU A CD2 1 
ATOM   2060 N  N   A LYS A 1 251 ? -0.197  -4.202  34.126  0.50 12.35 ? 252 LYS A N   1 
ATOM   2061 N  N   B LYS A 1 251 ? -0.034  -4.067  33.954  0.50 9.79  ? 252 LYS A N   1 
ATOM   2062 C  CA  A LYS A 1 251 ? 0.390   -3.290  35.129  0.50 13.84 ? 252 LYS A CA  1 
ATOM   2063 C  CA  B LYS A 1 251 ? 0.575   -3.046  34.869  0.50 9.85  ? 252 LYS A CA  1 
ATOM   2064 C  C   A LYS A 1 251 ? -0.673  -2.836  36.125  0.50 15.41 ? 252 LYS A C   1 
ATOM   2065 C  C   B LYS A 1 251 ? -0.454  -2.459  35.808  0.50 9.53  ? 252 LYS A C   1 
ATOM   2066 O  O   A LYS A 1 251 ? -1.392  -3.692  36.667  0.50 16.71 ? 252 LYS A O   1 
ATOM   2067 O  O   B LYS A 1 251 ? -1.333  -3.195  36.310  0.50 12.55 ? 252 LYS A O   1 
ATOM   2068 C  CB  A LYS A 1 251 ? 1.200   -2.195  34.444  0.50 13.89 ? 252 LYS A CB  1 
ATOM   2069 C  CB  B LYS A 1 251 ? 1.269   -1.949  34.062  0.50 10.45 ? 252 LYS A CB  1 
ATOM   2070 C  CG  A LYS A 1 251 ? 2.335   -2.895  33.649  0.50 16.32 ? 252 LYS A CG  1 
ATOM   2071 C  CG  B LYS A 1 251 ? 2.439   -2.529  33.237  0.50 12.55 ? 252 LYS A CG  1 
ATOM   2072 C  CD  A LYS A 1 251 ? 3.525   -2.030  33.291  0.50 17.23 ? 252 LYS A CD  1 
ATOM   2073 C  CD  B LYS A 1 251 ? 3.362   -1.511  32.583  0.50 12.29 ? 252 LYS A CD  1 
ATOM   2074 C  CE  A LYS A 1 251 ? 4.402   -2.676  32.196  0.50 16.78 ? 252 LYS A CE  1 
ATOM   2075 C  CE  B LYS A 1 251 ? 4.734   -2.107  32.240  0.50 16.01 ? 252 LYS A CE  1 
ATOM   2076 N  NZ  A LYS A 1 251 ? 5.307   -1.654  31.505  0.50 16.20 ? 252 LYS A NZ  1 
ATOM   2077 N  NZ  B LYS A 1 251 ? 5.343   -3.017  33.274  0.50 17.34 ? 252 LYS A NZ  1 
ATOM   2078 N  N   A ASN A 1 252 ? -0.799  -1.538  36.374  0.50 16.19 ? 253 ASN A N   1 
ATOM   2079 N  N   B ASN A 1 252 ? -0.359  -1.157  36.077  0.50 9.31  ? 253 ASN A N   1 
ATOM   2080 C  CA  A ASN A 1 252 ? -1.732  -1.092  37.413  0.50 18.23 ? 253 ASN A CA  1 
ATOM   2081 C  CA  B ASN A 1 252 ? -1.239  -0.628  37.101  0.50 12.90 ? 253 ASN A CA  1 
ATOM   2082 C  C   A ASN A 1 252 ? -3.230  -1.485  37.156  0.50 15.50 ? 253 ASN A C   1 
ATOM   2083 C  C   B ASN A 1 252 ? -2.616  -0.175  36.584  0.50 12.60 ? 253 ASN A C   1 
ATOM   2084 O  O   A ASN A 1 252 ? -4.059  -1.664  38.082  0.50 15.69 ? 253 ASN A O   1 
ATOM   2085 O  O   B ASN A 1 252 ? -2.856  1.029   36.573  0.50 14.38 ? 253 ASN A O   1 
ATOM   2086 C  CB  A ASN A 1 252 ? -1.623  0.455   37.514  0.50 21.18 ? 253 ASN A CB  1 
ATOM   2087 C  CB  B ASN A 1 252 ? -0.583  0.505   37.962  0.50 13.96 ? 253 ASN A CB  1 
ATOM   2088 C  CG  A ASN A 1 252 ? -1.699  0.974   38.940  0.50 24.29 ? 253 ASN A CG  1 
ATOM   2089 C  CG  B ASN A 1 252 ? -1.335  0.760   39.276  0.50 20.11 ? 253 ASN A CG  1 
ATOM   2090 O  OD1 A ASN A 1 252 ? -2.357  0.381   39.824  0.50 28.21 ? 253 ASN A OD1 1 
ATOM   2091 O  OD1 B ASN A 1 252 ? -1.684  -0.187  40.014  0.50 26.79 ? 253 ASN A OD1 1 
ATOM   2092 N  ND2 A ASN A 1 252 ? -1.061  2.120   39.167  0.50 30.14 ? 253 ASN A ND2 1 
ATOM   2093 N  ND2 B ASN A 1 252 ? -1.628  2.036   39.561  0.50 26.32 ? 253 ASN A ND2 1 
ATOM   2094 N  N   A ARG A 1 253 ? -3.525  -1.638  35.879  0.50 12.30 ? 254 ARG A N   1 
ATOM   2095 N  N   B ARG A 1 253 ? -3.432  -1.141  36.106  0.50 11.45 ? 254 ARG A N   1 
ATOM   2096 C  CA  A ARG A 1 253 ? -4.799  -1.156  35.339  0.50 11.01 ? 254 ARG A CA  1 
ATOM   2097 C  CA  B ARG A 1 253 ? -4.785  -0.868  35.591  0.50 9.47  ? 254 ARG A CA  1 
ATOM   2098 C  C   A ARG A 1 253 ? -5.992  -2.060  35.650  0.50 12.97 ? 254 ARG A C   1 
ATOM   2099 C  C   B ARG A 1 253 ? -5.851  -1.877  36.055  0.50 11.02 ? 254 ARG A C   1 
ATOM   2100 O  O   A ARG A 1 253 ? -5.913  -3.280  35.561  0.50 13.76 ? 254 ARG A O   1 
ATOM   2101 O  O   B ARG A 1 253 ? -5.524  -3.017  36.368  0.50 11.65 ? 254 ARG A O   1 
ATOM   2102 C  CB  A ARG A 1 253 ? -4.659  -0.896  33.799  0.50 10.52 ? 254 ARG A CB  1 
ATOM   2103 C  CB  B ARG A 1 253 ? -4.815  -0.898  34.041  0.50 9.48  ? 254 ARG A CB  1 
ATOM   2104 C  CG  A ARG A 1 253 ? -3.568  0.193   33.417  0.50 7.31  ? 254 ARG A CG  1 
ATOM   2105 C  CG  B ARG A 1 253 ? -4.192  0.291   33.362  0.50 7.62  ? 254 ARG A CG  1 
ATOM   2106 C  CD  A ARG A 1 253 ? -3.382  0.314   31.905  0.50 8.03  ? 254 ARG A CD  1 
ATOM   2107 C  CD  B ARG A 1 253 ? -4.176  0.032   31.870  0.50 7.90  ? 254 ARG A CD  1 
ATOM   2108 N  NE  A ARG A 1 253 ? -2.578  -0.821  31.412  0.50 6.64  ? 254 ARG A NE  1 
ATOM   2109 N  NE  B ARG A 1 253 ? -3.200  -1.028  31.527  0.50 5.32  ? 254 ARG A NE  1 
ATOM   2110 C  CZ  A ARG A 1 253 ? -2.427  -1.127  30.117  0.50 5.34  ? 254 ARG A CZ  1 
ATOM   2111 C  CZ  B ARG A 1 253 ? -2.890  -1.355  30.271  0.50 5.28  ? 254 ARG A CZ  1 
ATOM   2112 N  NH1 A ARG A 1 253 ? -3.044  -0.381  29.184  0.50 5.33  ? 254 ARG A NH1 1 
ATOM   2113 N  NH1 B ARG A 1 253 ? -3.518  -0.716  29.253  0.50 5.37  ? 254 ARG A NH1 1 
ATOM   2114 N  NH2 A ARG A 1 253 ? -1.668  -2.170  29.747  0.50 5.23  ? 254 ARG A NH2 1 
ATOM   2115 N  NH2 B ARG A 1 253 ? -1.999  -2.321  30.021  0.50 7.74  ? 254 ARG A NH2 1 
ATOM   2116 N  N   . GLN A 1 254 ? -7.115  -1.439  35.970  1.00 13.05 ? 255 GLN A N   1 
ATOM   2117 C  CA  . GLN A 1 254 ? -8.319  -2.225  36.295  1.00 15.82 ? 255 GLN A CA  1 
ATOM   2118 C  C   . GLN A 1 254 ? -9.237  -2.255  35.082  1.00 15.31 ? 255 GLN A C   1 
ATOM   2119 O  O   . GLN A 1 254 ? -9.508  -1.182  34.458  1.00 17.71 ? 255 GLN A O   1 
ATOM   2120 C  CB  . GLN A 1 254 ? -9.110  -1.532  37.436  1.00 17.65 ? 255 GLN A CB  1 
ATOM   2121 C  CG  . GLN A 1 254 ? -10.357 -2.240  37.743  1.00 26.79 ? 255 GLN A CG  1 
ATOM   2122 C  CD  . GLN A 1 254 ? -10.129 -3.544  38.455  1.00 36.37 ? 255 GLN A CD  1 
ATOM   2123 O  OE1 . GLN A 1 254 ? -9.296  -3.610  39.365  1.00 42.84 ? 255 GLN A OE1 1 
ATOM   2124 N  NE2 . GLN A 1 254 ? -10.889 -4.614  38.056  1.00 39.17 ? 255 GLN A NE2 1 
ATOM   2125 N  N   . ILE A 1 255 ? -9.616  -3.453  34.623  1.00 11.74 ? 256 ILE A N   1 
ATOM   2126 C  CA  . ILE A 1 255 ? -10.664 -3.562  33.592  1.00 10.93 ? 256 ILE A CA  1 
ATOM   2127 C  C   . ILE A 1 255 ? -12.014 -3.586  34.271  1.00 9.72  ? 256 ILE A C   1 
ATOM   2128 O  O   . ILE A 1 255 ? -12.199 -4.292  35.255  1.00 11.80 ? 256 ILE A O   1 
ATOM   2129 C  CB  . ILE A 1 255 ? -10.427 -4.793  32.665  1.00 9.63  ? 256 ILE A CB  1 
ATOM   2130 C  CG1 . ILE A 1 255 ? -8.974  -4.759  32.065  1.00 11.36 ? 256 ILE A CG1 1 
ATOM   2131 C  CG2 . ILE A 1 255 ? -11.561 -4.924  31.648  1.00 10.70 ? 256 ILE A CG2 1 
ATOM   2132 C  CD1 . ILE A 1 255 ? -8.671  -6.086  31.352  1.00 13.76 ? 256 ILE A CD1 1 
ATOM   2133 N  N   . LYS A 1 256 ? -12.937 -2.755  33.766  1.00 9.28  ? 257 LYS A N   1 
ATOM   2134 C  CA  . LYS A 1 256 ? -14.283 -2.619  34.309  1.00 10.18 ? 257 LYS A CA  1 
ATOM   2135 C  C   . LYS A 1 256 ? -15.249 -3.238  33.339  1.00 9.32  ? 257 LYS A C   1 
ATOM   2136 O  O   . LYS A 1 256 ? -15.021 -3.154  32.131  1.00 10.87 ? 257 LYS A O   1 
ATOM   2137 C  CB  . LYS A 1 256 ? -14.609 -1.126  34.550  1.00 13.07 ? 257 LYS A CB  1 
ATOM   2138 C  CG  . LYS A 1 256 ? -13.705 -0.472  35.647  1.00 17.38 ? 257 LYS A CG  1 
ATOM   2139 C  CD  . LYS A 1 256 ? -14.200 0.934   35.833  1.00 26.22 ? 257 LYS A CD  1 
ATOM   2140 C  CE  . LYS A 1 256 ? -13.503 1.621   36.963  1.00 35.44 ? 257 LYS A CE  1 
ATOM   2141 N  NZ  . LYS A 1 256 ? -14.300 1.226   38.154  1.00 39.70 ? 257 LYS A NZ  1 
ATOM   2142 N  N   . ALA A 1 257 ? -16.339 -3.812  33.870  1.00 10.99 ? 258 ALA A N   1 
ATOM   2143 C  CA  . ALA A 1 257 ? -17.363 -4.467  33.064  1.00 10.73 ? 258 ALA A CA  1 
ATOM   2144 C  C   . ALA A 1 257 ? -18.680 -3.693  33.246  1.00 11.00 ? 258 ALA A C   1 
ATOM   2145 O  O   . ALA A 1 257 ? -19.027 -3.285  34.394  1.00 11.97 ? 258 ALA A O   1 
ATOM   2146 C  CB  . ALA A 1 257 ? -17.576 -5.941  33.464  1.00 12.79 ? 258 ALA A CB  1 
ATOM   2147 N  N   . SER A 1 258 ? -19.415 -3.514  32.143  1.00 10.07 ? 259 SER A N   1 
ATOM   2148 C  CA  . SER A 1 258 ? -20.703 -2.864  32.244  1.00 11.98 ? 259 SER A CA  1 
ATOM   2149 C  C   . SER A 1 258 ? -21.837 -3.804  32.610  1.00 12.95 ? 259 SER A C   1 
ATOM   2150 O  O   . SER A 1 258 ? -22.991 -3.352  32.736  1.00 16.49 ? 259 SER A O   1 
ATOM   2151 C  CB  . SER A 1 258 ? -21.079 -2.257  30.875  1.00 12.38 ? 259 SER A CB  1 
ATOM   2152 O  OG  . SER A 1 258 ? -21.465 -3.293  29.907  1.00 10.99 ? 259 SER A OG  1 
ATOM   2153 N  N   . PHE A 1 259 ? -21.539 -5.091  32.794  1.00 12.84 ? 260 PHE A N   1 
ATOM   2154 C  CA  . PHE A 1 259 ? -22.549 -6.121  33.007  1.00 15.19 ? 260 PHE A CA  1 
ATOM   2155 C  C   . PHE A 1 259 ? -22.064 -7.098  34.057  1.00 19.18 ? 260 PHE A C   1 
ATOM   2156 O  O   . PHE A 1 259 ? -20.833 -7.165  34.407  1.00 18.47 ? 260 PHE A O   1 
ATOM   2157 C  CB  . PHE A 1 259 ? -22.742 -6.863  31.690  1.00 15.25 ? 260 PHE A CB  1 
ATOM   2158 C  CG  . PHE A 1 259 ? -21.490 -7.560  31.212  1.00 16.88 ? 260 PHE A CG  1 
ATOM   2159 C  CD1 . PHE A 1 259 ? -20.503 -6.853  30.518  1.00 14.38 ? 260 PHE A CD1 1 
ATOM   2160 C  CD2 . PHE A 1 259 ? -21.261 -8.922  31.555  1.00 16.86 ? 260 PHE A CD2 1 
ATOM   2161 C  CE1 . PHE A 1 259 ? -19.329 -7.488  30.095  1.00 15.34 ? 260 PHE A CE1 1 
ATOM   2162 C  CE2 . PHE A 1 259 ? -20.100 -9.575  31.167  1.00 18.15 ? 260 PHE A CE2 1 
ATOM   2163 C  CZ  . PHE A 1 259 ? -19.105 -8.871  30.427  1.00 17.91 ? 260 PHE A CZ  1 
ATOM   2164 N  N   . LYS A 1 260 ? -23.108 -7.858  34.488  1.00 26.31 ? 261 LYS A N   1 
ATOM   2165 C  CA  . LYS A 1 260 ? -23.188 -9.097  35.318  1.00 33.43 ? 261 LYS A CA  1 
ATOM   2166 C  C   . LYS A 1 260 ? -22.405 -9.179  36.585  1.00 36.69 ? 261 LYS A C   1 
ATOM   2167 O  O   . LYS A 1 260 ? -22.979 -8.893  37.669  1.00 39.50 ? 261 LYS A O   1 
ATOM   2168 C  CB  . LYS A 1 260 ? -23.039 -10.381 34.479  1.00 33.55 ? 261 LYS A CB  1 
ATOM   2169 C  CG  . LYS A 1 260 ? -24.209 -10.548 33.505  1.00 37.44 ? 261 LYS A CG  1 
ATOM   2170 C  CD  . LYS A 1 260 ? -24.368 -11.989 33.048  1.00 42.13 ? 261 LYS A CD  1 
ATOM   2171 C  CE  . LYS A 1 260 ? -23.263 -12.489 32.078  1.00 43.67 ? 261 LYS A CE  1 
ATOM   2172 N  NZ  . LYS A 1 260 ? -21.890 -12.635 32.658  1.00 42.84 ? 261 LYS A NZ  1 
ATOM   2173 O  OXT . LYS A 1 260 ? -21.211 -9.541  36.500  1.00 40.53 ? 261 LYS A OXT 1 
HETATM 2174 ZN ZN  . ZN  B 2 .   ? -6.591  -1.705  15.353  1.00 7.68  ? 262 ZN  A ZN  1 
HETATM 2175 S  S   . DMS C 3 .   ? 1.417   -11.723 15.060  1.00 27.33 ? 263 DMS A S   1 
HETATM 2176 O  O   . DMS C 3 .   ? 2.654   -10.606 14.309  1.00 29.04 ? 263 DMS A O   1 
HETATM 2177 C  C1  . DMS C 3 .   ? 1.920   -13.377 14.491  1.00 22.95 ? 263 DMS A C1  1 
HETATM 2178 C  C2  . DMS C 3 .   ? 1.780   -11.641 16.827  1.00 22.67 ? 263 DMS A C2  1 
HETATM 2179 N  N1  . J75 D 4 .   ? -3.343  9.914   11.121  1.00 36.73 ? 264 J75 A N1  1 
HETATM 2180 C  C2  . J75 D 4 .   ? -2.422  9.254   11.864  1.00 36.99 ? 264 J75 A C2  1 
HETATM 2181 N  N3  . J75 D 4 .   ? -2.735  8.069   12.487  1.00 37.89 ? 264 J75 A N3  1 
HETATM 2182 C  C4  . J75 D 4 .   ? -3.979  7.508   12.382  1.00 37.45 ? 264 J75 A C4  1 
HETATM 2183 C  C5  . J75 D 4 .   ? -4.971  8.177   11.595  1.00 36.84 ? 264 J75 A C5  1 
HETATM 2184 C  C6  . J75 D 4 .   ? -4.613  9.405   10.968  1.00 36.37 ? 264 J75 A C6  1 
HETATM 2185 N  N7  . J75 D 4 .   ? -4.296  6.276   13.047  1.00 34.82 ? 264 J75 A N7  1 
HETATM 2186 C  C8  . J75 D 4 .   ? -4.014  4.465   14.611  1.00 26.75 ? 264 J75 A C8  1 
HETATM 2187 C  C9  . J75 D 4 .   ? -3.250  3.333   14.972  1.00 26.64 ? 264 J75 A C9  1 
HETATM 2188 C  C10 . J75 D 4 .   ? -3.801  2.233   15.674  1.00 25.26 ? 264 J75 A C10 1 
HETATM 2189 C  C11 . J75 D 4 .   ? -5.167  2.230   16.011  1.00 21.53 ? 264 J75 A C11 1 
HETATM 2190 C  C12 . J75 D 4 .   ? -5.977  3.333   15.638  1.00 23.84 ? 264 J75 A C12 1 
HETATM 2191 C  C13 . J75 D 4 .   ? -5.402  4.419   14.914  1.00 25.37 ? 264 J75 A C13 1 
HETATM 2192 S  S14 . J75 D 4 .   ? -5.809  0.764   16.899  1.00 21.51 ? 264 J75 A S14 1 
HETATM 2193 O  O15 . J75 D 4 .   ? -7.337  0.827   16.711  1.00 21.84 ? 264 J75 A O15 1 
HETATM 2194 O  O16 . J75 D 4 .   ? -5.366  0.830   18.305  1.00 13.14 ? 264 J75 A O16 1 
HETATM 2195 N  N17 . J75 D 4 .   ? -5.250  -0.493  16.021  1.00 13.88 ? 264 J75 A N17 1 
HETATM 2196 N  N18 . J75 D 4 .   ? -6.333  7.682   11.433  1.00 36.18 ? 264 J75 A N18 1 
HETATM 2197 O  O19 . J75 D 4 .   ? -7.041  8.160   10.575  1.00 40.44 ? 264 J75 A O19 1 
HETATM 2198 O  O20 . J75 D 4 .   ? -6.867  6.786   12.240  1.00 27.78 ? 264 J75 A O20 1 
HETATM 2199 N  N21 . J75 D 4 .   ? -5.614  10.043  10.192  1.00 36.80 ? 264 J75 A N21 1 
HETATM 2200 C  C22 . J75 D 4 .   ? -5.470  11.337  9.616   1.00 37.39 ? 264 J75 A C22 1 
HETATM 2201 C  C23 . J75 D 4 .   ? -5.758  12.604  10.404  1.00 38.63 ? 264 J75 A C23 1 
HETATM 2202 C  C24 . J75 D 4 .   ? -4.709  13.277  11.104  1.00 39.66 ? 264 J75 A C24 1 
HETATM 2203 C  C25 . J75 D 4 .   ? -4.942  14.506  11.798  1.00 38.38 ? 264 J75 A C25 1 
HETATM 2204 C  C26 . J75 D 4 .   ? -6.224  15.081  11.812  1.00 34.90 ? 264 J75 A C26 1 
HETATM 2205 C  C27 . J75 D 4 .   ? -7.280  14.443  11.079  1.00 38.01 ? 264 J75 A C27 1 
HETATM 2206 C  C28 . J75 D 4 .   ? -7.035  13.216  10.378  1.00 37.57 ? 264 J75 A C28 1 
HETATM 2207 C  C29 . J75 D 4 .   ? -3.344  5.609   13.874  1.00 30.77 ? 264 J75 A C29 1 
HETATM 2208 O  O   . HOH E 5 .   ? -27.584 2.653   23.672  1.00 25.06 ? 126 HOH A O   1 
HETATM 2209 O  O   . HOH E 5 .   ? -24.925 4.513   8.412   1.00 31.71 ? 265 HOH A O   1 
HETATM 2210 O  O   . HOH E 5 .   ? -2.965  -19.016 2.177   1.00 35.68 ? 266 HOH A O   1 
HETATM 2211 O  O   . HOH E 5 .   ? -2.475  -19.175 21.585  1.00 31.42 ? 267 HOH A O   1 
HETATM 2212 O  O   . HOH E 5 .   ? 8.267   -8.992  -7.853  1.00 36.23 ? 268 HOH A O   1 
HETATM 2213 O  O   . HOH E 5 .   ? -7.494  -10.301 -4.377  1.00 34.68 ? 269 HOH A O   1 
HETATM 2214 O  O   . HOH E 5 .   ? -12.701 11.007  -5.204  1.00 30.70 ? 270 HOH A O   1 
HETATM 2215 O  O   . HOH E 5 .   ? -14.234 0.225   42.974  1.00 37.68 ? 271 HOH A O   1 
HETATM 2216 O  O   . HOH E 5 .   ? -10.745 -11.102 -2.903  1.00 35.52 ? 273 HOH A O   1 
HETATM 2217 O  O   . HOH E 5 .   ? -12.280 13.500  5.138   1.00 36.46 ? 274 HOH A O   1 
HETATM 2218 O  O   . HOH E 5 .   ? -17.897 -3.180  45.516  1.00 41.68 ? 275 HOH A O   1 
HETATM 2219 O  O   . HOH E 5 .   ? -4.964  -14.001 38.674  1.00 35.20 ? 276 HOH A O   1 
HETATM 2220 O  O   . HOH E 5 .   ? -7.346  -8.814  -2.371  1.00 30.55 ? 277 HOH A O   1 
HETATM 2221 O  O   . HOH E 5 .   ? 3.251   10.864  16.855  1.00 41.36 ? 278 HOH A O   1 
HETATM 2222 O  O   . HOH E 5 .   ? 8.335   3.175   27.761  1.00 26.09 ? 279 HOH A O   1 
HETATM 2223 O  O   . HOH E 5 .   ? -21.098 -22.221 13.802  1.00 33.11 ? 280 HOH A O   1 
HETATM 2224 O  O   . HOH E 5 .   ? 9.134   -13.824 3.653   1.00 32.78 ? 281 HOH A O   1 
HETATM 2225 O  O   . HOH E 5 .   ? 1.470   -16.165 4.918   1.00 35.07 ? 282 HOH A O   1 
HETATM 2226 O  O   . HOH E 5 .   ? -25.556 -3.257  31.861  1.00 32.57 ? 283 HOH A O   1 
HETATM 2227 O  O   . HOH E 5 .   ? -0.277  -6.932  -7.409  1.00 35.95 ? 284 HOH A O   1 
HETATM 2228 O  O   . HOH E 5 .   ? 6.459   -5.207  27.537  1.00 33.87 ? 285 HOH A O   1 
HETATM 2229 O  O   . HOH E 5 .   ? -14.175 -4.674  -6.421  1.00 31.47 ? 286 HOH A O   1 
HETATM 2230 O  O   . HOH E 5 .   ? 8.928   -11.137 6.333   1.00 32.61 ? 287 HOH A O   1 
HETATM 2231 O  O   . HOH E 5 .   ? -13.526 -16.569 -0.069  1.00 37.33 ? 288 HOH A O   1 
HETATM 2232 O  O   . HOH E 5 .   ? -9.998  15.716  29.958  1.00 33.36 ? 289 HOH A O   1 
HETATM 2233 O  O   . HOH E 5 .   ? -0.813  -3.603  39.743  1.00 40.13 ? 290 HOH A O   1 
HETATM 2234 O  O   . HOH E 5 .   ? -3.136  -20.141 30.101  1.00 36.31 ? 291 HOH A O   1 
HETATM 2235 O  O   . HOH E 5 .   ? 6.705   -5.946  6.476   1.00 44.55 ? 292 HOH A O   1 
HETATM 2236 O  O   . HOH E 5 .   ? -0.401  13.965  16.278  1.00 24.54 ? 293 HOH A O   1 
HETATM 2237 O  O   . HOH E 5 .   ? -1.151  -4.127  15.778  1.00 8.48  ? 294 HOH A O   1 
HETATM 2238 O  O   . HOH E 5 .   ? -16.995 -8.422  20.532  1.00 6.95  ? 295 HOH A O   1 
HETATM 2239 O  O   . HOH E 5 .   ? -4.486  -13.559 18.145  1.00 9.83  ? 296 HOH A O   1 
HETATM 2240 O  O   . HOH E 5 .   ? -21.720 5.708   4.780   1.00 16.31 ? 297 HOH A O   1 
HETATM 2241 O  O   . HOH E 5 .   ? -10.644 8.736   25.732  1.00 10.30 ? 298 HOH A O   1 
HETATM 2242 O  O   . HOH E 5 .   ? -21.588 -7.155  23.716  1.00 11.44 ? 299 HOH A O   1 
HETATM 2243 O  O   . HOH E 5 .   ? -3.407  -13.315 25.317  1.00 11.43 ? 300 HOH A O   1 
HETATM 2244 O  O   . HOH E 5 .   ? -13.949 10.437  27.962  1.00 17.18 ? 301 HOH A O   1 
HETATM 2245 O  O   . HOH E 5 .   ? 3.853   5.062   29.762  1.00 18.02 ? 302 HOH A O   1 
HETATM 2246 O  O   . HOH E 5 .   ? 4.946   -4.921  21.067  1.00 12.50 ? 303 HOH A O   1 
HETATM 2247 O  O   . HOH E 5 .   ? -19.302 10.002  8.979   1.00 14.66 ? 304 HOH A O   1 
HETATM 2248 O  O   . HOH E 5 .   ? -3.432  -11.164 21.023  1.00 9.75  ? 305 HOH A O   1 
HETATM 2249 O  O   . HOH E 5 .   ? -2.395  -8.804  29.260  1.00 10.66 ? 306 HOH A O   1 
HETATM 2250 O  O   . HOH E 5 .   ? -17.891 -20.593 8.069   1.00 13.58 ? 307 HOH A O   1 
HETATM 2251 O  O   . HOH E 5 .   ? -3.745  -15.963 24.536  1.00 11.26 ? 308 HOH A O   1 
HETATM 2252 O  O   . HOH E 5 .   ? -17.872 10.484  11.387  1.00 15.03 ? 309 HOH A O   1 
HETATM 2253 O  O   . HOH E 5 .   ? 1.334   -1.604  29.515  1.00 13.55 ? 310 HOH A O   1 
HETATM 2254 O  O   . HOH E 5 .   ? -2.031  -12.379 23.008  1.00 9.94  ? 311 HOH A O   1 
HETATM 2255 O  O   . HOH E 5 .   ? -16.252 -9.985  33.103  1.00 16.07 ? 312 HOH A O   1 
HETATM 2256 O  O   . HOH E 5 .   ? -8.641  -3.920  7.902   1.00 9.90  ? 313 HOH A O   1 
HETATM 2257 O  O   . HOH E 5 .   ? -24.040 -0.776  26.612  1.00 16.93 ? 314 HOH A O   1 
HETATM 2258 O  O   . HOH E 5 .   ? -7.900  -15.501 11.426  1.00 9.37  ? 315 HOH A O   1 
HETATM 2259 O  O   . HOH E 5 .   ? -16.125 -12.363 24.556  1.00 12.17 ? 316 HOH A O   1 
HETATM 2260 O  O   . HOH E 5 .   ? 8.676   -3.827  21.197  1.00 14.53 ? 317 HOH A O   1 
HETATM 2261 O  O   . HOH E 5 .   ? -0.379  10.844  23.603  1.00 14.77 ? 318 HOH A O   1 
HETATM 2262 O  O   . HOH E 5 .   ? -10.356 -18.373 17.170  1.00 15.23 ? 319 HOH A O   1 
HETATM 2263 O  O   . HOH E 5 .   ? -9.838  14.836  12.229  1.00 20.64 ? 320 HOH A O   1 
HETATM 2264 O  O   . HOH E 5 .   ? -21.149 7.818   1.893   1.00 16.99 ? 321 HOH A O   1 
HETATM 2265 O  O   . HOH E 5 .   ? -13.063 -16.948 26.851  1.00 16.13 ? 322 HOH A O   1 
HETATM 2266 O  O   . HOH E 5 .   ? -13.471 -18.642 14.741  1.00 17.49 ? 323 HOH A O   1 
HETATM 2267 O  O   . HOH E 5 .   ? -9.456  -8.029  34.259  1.00 21.37 ? 324 HOH A O   1 
HETATM 2268 O  O   . HOH E 5 .   ? -12.846 -17.307 16.970  1.00 12.12 ? 325 HOH A O   1 
HETATM 2269 O  O   . HOH E 5 .   ? -23.958 -16.738 3.620   1.00 34.82 ? 326 HOH A O   1 
HETATM 2270 O  O   . HOH E 5 .   ? -28.770 0.296   24.601  1.00 19.37 ? 327 HOH A O   1 
HETATM 2271 O  O   . HOH E 5 .   ? -24.909 -7.764  9.087   1.00 16.70 ? 328 HOH A O   1 
HETATM 2272 O  O   . HOH E 5 .   ? 7.693   6.121   21.764  1.00 15.88 ? 329 HOH A O   1 
HETATM 2273 O  O   . HOH E 5 .   ? -14.624 -18.618 18.849  1.00 17.13 ? 330 HOH A O   1 
HETATM 2274 O  O   . HOH E 5 .   ? -30.884 1.428   26.158  1.00 23.67 ? 331 HOH A O   1 
HETATM 2275 O  O   . HOH E 5 .   ? 4.444   -3.490  26.581  1.00 17.80 ? 332 HOH A O   1 
HETATM 2276 O  O   . HOH E 5 .   ? -6.071  -4.516  -6.415  1.00 24.68 ? 333 HOH A O   1 
HETATM 2277 O  O   . HOH E 5 .   ? -26.776 -2.552  14.453  1.00 18.20 ? 334 HOH A O   1 
HETATM 2278 O  O   . HOH E 5 .   ? 5.458   7.126   20.231  1.00 16.89 ? 335 HOH A O   1 
HETATM 2279 O  O   . HOH E 5 .   ? -22.994 -11.736 14.138  1.00 19.46 ? 336 HOH A O   1 
HETATM 2280 O  O   . HOH E 5 .   ? -2.444  -3.294  11.552  1.00 16.38 ? 337 HOH A O   1 
HETATM 2281 O  O   . HOH E 5 .   ? -23.863 -0.819  3.966   1.00 21.04 ? 338 HOH A O   1 
HETATM 2282 O  O   . HOH E 5 .   ? -4.916  0.694   10.038  1.00 22.45 ? 339 HOH A O   1 
HETATM 2283 O  O   . HOH E 5 .   ? -14.835 -21.138 17.624  1.00 22.24 ? 340 HOH A O   1 
HETATM 2284 O  O   . HOH E 5 .   ? 0.239   -1.031  -4.680  1.00 21.15 ? 341 HOH A O   1 
HETATM 2285 O  O   . HOH E 5 .   ? -8.942  -5.928  36.034  1.00 17.38 ? 342 HOH A O   1 
HETATM 2286 O  O   . HOH E 5 .   ? -22.186 -18.424 13.629  1.00 23.61 ? 343 HOH A O   1 
HETATM 2287 O  O   . HOH E 5 .   ? 4.418   -2.599  29.136  1.00 23.50 ? 344 HOH A O   1 
HETATM 2288 O  O   . HOH E 5 .   ? -29.074 -5.782  24.582  1.00 24.46 ? 345 HOH A O   1 
HETATM 2289 O  O   . HOH E 5 .   ? -19.952 -16.842 2.968   1.00 22.28 ? 346 HOH A O   1 
HETATM 2290 O  O   . HOH E 5 .   ? -29.165 -3.880  13.624  1.00 24.52 ? 347 HOH A O   1 
HETATM 2291 O  O   . HOH E 5 .   ? -14.275 -16.658 29.227  1.00 19.64 ? 348 HOH A O   1 
HETATM 2292 O  O   . HOH E 5 .   ? -16.820 -14.025 26.589  1.00 18.03 ? 349 HOH A O   1 
HETATM 2293 O  O   . HOH E 5 .   ? 1.545   -11.780 25.128  1.00 22.41 ? 350 HOH A O   1 
HETATM 2294 O  O   . HOH E 5 .   ? -8.452  0.616   -6.483  1.00 25.43 ? 351 HOH A O   1 
HETATM 2295 O  O   . HOH E 5 .   ? -17.726 -21.292 17.641  1.00 24.29 ? 352 HOH A O   1 
HETATM 2296 O  O   . HOH E 5 .   ? -12.032 2.849   31.061  1.00 22.87 ? 353 HOH A O   1 
HETATM 2297 O  O   . HOH E 5 .   ? -8.210  18.864  10.442  1.00 23.84 ? 354 HOH A O   1 
HETATM 2298 O  O   . HOH E 5 .   ? -25.665 9.670   13.483  1.00 30.66 ? 355 HOH A O   1 
HETATM 2299 O  O   . HOH E 5 .   ? -22.814 -5.946  2.709   1.00 20.44 ? 356 HOH A O   1 
HETATM 2300 O  O   . HOH E 5 .   ? -6.658  20.896  19.659  1.00 13.94 ? 357 HOH A O   1 
HETATM 2301 O  O   . HOH E 5 .   ? -4.700  0.990   43.633  1.00 22.90 ? 358 HOH A O   1 
HETATM 2302 O  O   . HOH E 5 .   ? 4.482   -6.544  7.789   1.00 24.91 ? 359 HOH A O   1 
HETATM 2303 O  O   . HOH E 5 .   ? 1.333   8.789   24.577  1.00 15.47 ? 360 HOH A O   1 
HETATM 2304 O  O   . HOH E 5 .   ? -23.141 -2.995  6.713   1.00 21.14 ? 361 HOH A O   1 
HETATM 2305 O  O   . HOH E 5 .   ? -7.240  -8.755  32.797  1.00 17.09 ? 362 HOH A O   1 
HETATM 2306 O  O   . HOH E 5 .   ? -4.545  -12.064 32.188  1.00 18.79 ? 363 HOH A O   1 
HETATM 2307 O  O   . HOH E 5 .   ? -17.875 19.066  6.076   1.00 13.25 ? 364 HOH A O   1 
HETATM 2308 O  O   . HOH E 5 .   ? -8.134  -19.447 21.811  1.00 14.81 ? 365 HOH A O   1 
HETATM 2309 O  O   . HOH E 5 .   ? -1.008  -11.198 29.119  1.00 18.45 ? 366 HOH A O   1 
HETATM 2310 O  O   . HOH E 5 .   ? -24.070 8.659   20.173  1.00 20.96 ? 367 HOH A O   1 
HETATM 2311 O  O   . HOH E 5 .   ? -20.455 10.811  26.747  1.00 16.76 ? 368 HOH A O   1 
HETATM 2312 O  O   . HOH E 5 .   ? -19.103 14.180  35.443  1.00 22.23 ? 369 HOH A O   1 
HETATM 2313 O  O   . HOH E 5 .   ? -10.778 5.640   38.342  1.00 18.23 ? 370 HOH A O   1 
HETATM 2314 O  O   . HOH E 5 .   ? -10.992 -15.295 34.325  1.00 25.47 ? 371 HOH A O   1 
HETATM 2315 O  O   . HOH E 5 .   ? -16.210 15.920  23.622  1.00 18.08 ? 372 HOH A O   1 
HETATM 2316 O  O   . HOH E 5 .   ? -15.302 -21.753 13.146  1.00 19.78 ? 373 HOH A O   1 
HETATM 2317 O  O   . HOH E 5 .   ? -23.556 8.302   3.565   1.00 22.78 ? 374 HOH A O   1 
HETATM 2318 O  O   . HOH E 5 .   ? -0.402  -8.639  32.681  1.00 24.38 ? 375 HOH A O   1 
HETATM 2319 O  O   . HOH E 5 .   ? -8.392  -17.472 35.043  1.00 22.32 ? 376 HOH A O   1 
HETATM 2320 O  O   . HOH E 5 .   ? -15.548 -16.508 25.839  1.00 29.13 ? 377 HOH A O   1 
HETATM 2321 O  O   . HOH E 5 .   ? -0.990  -17.627 18.105  1.00 28.64 ? 378 HOH A O   1 
HETATM 2322 O  O   . HOH E 5 .   ? -7.184  5.933   6.627   1.00 21.23 ? 379 HOH A O   1 
HETATM 2323 O  O   . HOH E 5 .   ? -27.708 -0.086  15.168  1.00 25.88 ? 380 HOH A O   1 
HETATM 2324 O  O   . HOH E 5 .   ? -4.816  -20.792 21.628  1.00 20.88 ? 381 HOH A O   1 
HETATM 2325 O  O   . HOH E 5 .   ? 2.794   -4.252  7.881   1.00 21.66 ? 382 HOH A O   1 
HETATM 2326 O  O   . HOH E 5 .   ? -26.889 -3.984  25.182  1.00 19.62 ? 383 HOH A O   1 
HETATM 2327 O  O   . HOH E 5 .   ? -10.556 -19.454 20.149  1.00 18.99 ? 384 HOH A O   1 
HETATM 2328 O  O   . HOH E 5 .   ? -3.500  -13.074 -2.724  1.00 25.57 ? 385 HOH A O   1 
HETATM 2329 O  O   . HOH E 5 .   ? -26.150 -6.444  13.192  1.00 28.61 ? 386 HOH A O   1 
HETATM 2330 O  O   . HOH E 5 .   ? -25.865 6.244   27.064  1.00 22.13 ? 387 HOH A O   1 
HETATM 2331 O  O   . HOH E 5 .   ? -1.548  -13.305 27.352  1.00 22.38 ? 388 HOH A O   1 
HETATM 2332 O  O   . HOH E 5 .   ? -15.682 9.093   -2.026  1.00 24.38 ? 389 HOH A O   1 
HETATM 2333 O  O   . HOH E 5 .   ? -19.545 17.468  6.163   1.00 23.53 ? 390 HOH A O   1 
HETATM 2334 O  O   . HOH E 5 .   ? -18.592 -3.926  -2.641  1.00 24.32 ? 391 HOH A O   1 
HETATM 2335 O  O   . HOH E 5 .   ? -19.403 -20.798 5.049   1.00 20.60 ? 392 HOH A O   1 
HETATM 2336 O  O   . HOH E 5 .   ? -13.637 -21.221 15.128  1.00 17.85 ? 393 HOH A O   1 
HETATM 2337 O  O   . HOH E 5 .   ? -17.744 -12.185 31.648  1.00 27.81 ? 394 HOH A O   1 
HETATM 2338 O  O   . HOH E 5 .   ? -6.234  -19.751 24.031  1.00 20.89 ? 395 HOH A O   1 
HETATM 2339 O  O   . HOH E 5 .   ? -1.956  -17.471 25.719  1.00 25.26 ? 396 HOH A O   1 
HETATM 2340 O  O   . HOH E 5 .   ? -14.149 14.383  27.255  1.00 24.17 ? 397 HOH A O   1 
HETATM 2341 O  O   . HOH E 5 .   ? -1.503  11.297  26.145  1.00 23.95 ? 399 HOH A O   1 
HETATM 2342 O  O   . HOH E 5 .   ? -23.492 -13.329 11.433  1.00 19.01 ? 400 HOH A O   1 
HETATM 2343 O  O   . HOH E 5 .   ? 0.067   1.141   34.659  1.00 25.16 ? 401 HOH A O   1 
HETATM 2344 O  O   . HOH E 5 .   ? -10.436 4.931   31.117  1.00 25.27 ? 402 HOH A O   1 
HETATM 2345 O  O   . HOH E 5 .   ? -11.235 -19.518 7.382   1.00 35.00 ? 403 HOH A O   1 
HETATM 2346 O  O   . HOH E 5 .   ? -26.252 3.398   15.443  1.00 28.46 ? 404 HOH A O   1 
HETATM 2347 O  O   . HOH E 5 .   ? 8.715   -4.809  23.882  1.00 24.50 ? 405 HOH A O   1 
HETATM 2348 O  O   . HOH E 5 .   ? -9.048  0.571   43.225  1.00 22.73 ? 406 HOH A O   1 
HETATM 2349 O  O   . HOH E 5 .   ? 0.347   0.595   -6.680  1.00 28.77 ? 407 HOH A O   1 
HETATM 2350 O  O   . HOH E 5 .   ? 2.058   -14.304 20.707  1.00 31.53 ? 408 HOH A O   1 
HETATM 2351 O  O   . HOH E 5 .   ? -18.832 12.214  13.033  1.00 22.11 ? 409 HOH A O   1 
HETATM 2352 O  O   . HOH E 5 .   ? -18.616 -9.101  34.628  1.00 23.98 ? 410 HOH A O   1 
HETATM 2353 O  O   . HOH E 5 .   ? -31.009 -6.975  22.716  1.00 27.06 ? 411 HOH A O   1 
HETATM 2354 O  O   . HOH E 5 .   ? -13.253 -22.531 11.758  1.00 29.33 ? 412 HOH A O   1 
HETATM 2355 O  O   . HOH E 5 .   ? -8.444  -15.340 37.093  1.00 23.18 ? 413 HOH A O   1 
HETATM 2356 O  O   . HOH E 5 .   ? -17.460 -8.486  -6.415  1.00 25.45 ? 414 HOH A O   1 
HETATM 2357 O  O   . HOH E 5 .   ? -3.890  -0.910  11.713  1.00 23.16 ? 415 HOH A O   1 
HETATM 2358 O  O   . HOH E 5 .   ? -23.289 -0.669  34.481  1.00 25.43 ? 416 HOH A O   1 
HETATM 2359 O  O   . HOH E 5 .   ? -12.257 10.675  5.842   1.00 23.73 ? 417 HOH A O   1 
HETATM 2360 O  O   . HOH E 5 .   ? -15.201 -20.125 23.311  1.00 25.50 ? 418 HOH A O   1 
HETATM 2361 O  O   . HOH E 5 .   ? -7.127  -16.901 1.439   1.00 23.21 ? 419 HOH A O   1 
HETATM 2362 O  O   . HOH E 5 .   ? 1.833   12.405  22.985  1.00 24.78 ? 420 HOH A O   1 
HETATM 2363 O  O   . HOH E 5 .   ? 3.864   9.798   24.022  1.00 24.09 ? 421 HOH A O   1 
HETATM 2364 O  O   . HOH E 5 .   ? -25.709 -10.659 17.806  1.00 21.32 ? 422 HOH A O   1 
HETATM 2365 O  O   . HOH E 5 .   ? -30.533 -0.459  16.216  1.00 25.83 ? 423 HOH A O   1 
HETATM 2366 O  O   . HOH E 5 .   ? 4.614   4.591   -0.795  1.00 26.25 ? 424 HOH A O   1 
HETATM 2367 O  O   . HOH E 5 .   ? -17.434 11.028  -1.952  1.00 24.39 ? 425 HOH A O   1 
HETATM 2368 O  O   . HOH E 5 .   ? -17.405 -23.182 4.154   1.00 28.39 ? 426 HOH A O   1 
HETATM 2369 O  O   . HOH E 5 .   ? -1.930  -12.094 31.643  1.00 28.44 ? 427 HOH A O   1 
HETATM 2370 O  O   . HOH E 5 .   ? 2.609   -13.233 5.256   1.00 24.49 ? 428 HOH A O   1 
HETATM 2371 O  O   . HOH E 5 .   ? 2.694   -11.475 9.522   1.00 22.83 ? 429 HOH A O   1 
HETATM 2372 O  O   . HOH E 5 .   ? -10.885 -23.708 12.191  1.00 24.44 ? 430 HOH A O   1 
HETATM 2373 O  O   . HOH E 5 .   ? -0.133  -14.344 22.444  1.00 23.20 ? 431 HOH A O   1 
HETATM 2374 O  O   . HOH E 5 .   ? -4.973  2.167   37.549  1.00 27.68 ? 432 HOH A O   1 
HETATM 2375 O  O   . HOH E 5 .   ? -2.021  -4.716  -6.857  1.00 29.93 ? 433 HOH A O   1 
HETATM 2376 O  O   . HOH E 5 .   ? -1.110  9.272   28.144  1.00 22.00 ? 434 HOH A O   1 
HETATM 2377 O  O   . HOH E 5 .   ? -9.782  1.401   39.338  1.00 25.52 ? 435 HOH A O   1 
HETATM 2378 O  O   . HOH E 5 .   ? -21.208 -19.697 6.527   1.00 23.23 ? 436 HOH A O   1 
HETATM 2379 O  O   . HOH E 5 .   ? -26.676 -1.270  26.068  1.00 23.10 ? 437 HOH A O   1 
HETATM 2380 O  O   . HOH E 5 .   ? -9.160  5.859   29.218  1.00 21.85 ? 438 HOH A O   1 
HETATM 2381 O  O   . HOH E 5 .   ? -20.933 -6.793  -2.094  1.00 28.78 ? 439 HOH A O   1 
HETATM 2382 O  O   . HOH E 5 .   ? -4.122  -8.673  31.337  1.00 20.80 ? 440 HOH A O   1 
HETATM 2383 O  O   . HOH E 5 .   ? -12.926 7.965   28.910  1.00 24.99 ? 441 HOH A O   1 
HETATM 2384 O  O   . HOH E 5 .   ? -10.497 -20.406 25.077  1.00 24.32 ? 442 HOH A O   1 
HETATM 2385 O  O   . HOH E 5 .   ? 5.535   9.029   21.977  1.00 25.48 ? 443 HOH A O   1 
HETATM 2386 O  O   . HOH E 5 .   ? 1.968   -15.682 9.246   1.00 25.34 ? 444 HOH A O   1 
HETATM 2387 O  O   . HOH E 5 .   ? -6.474  -5.254  37.650  1.00 24.30 ? 445 HOH A O   1 
HETATM 2388 O  O   . HOH E 5 .   ? 11.905  -9.650  -0.880  1.00 26.83 ? 446 HOH A O   1 
HETATM 2389 O  O   . HOH E 5 .   ? -15.218 -10.390 37.590  1.00 27.81 ? 447 HOH A O   1 
HETATM 2390 O  O   . HOH E 5 .   ? -12.414 12.618  29.380  1.00 26.16 ? 448 HOH A O   1 
HETATM 2391 O  O   . HOH E 5 .   ? -3.336  -23.125 21.568  1.00 22.65 ? 449 HOH A O   1 
HETATM 2392 O  O   . HOH E 5 .   ? -25.723 -15.343 7.904   1.00 28.49 ? 450 HOH A O   1 
HETATM 2393 O  O   . HOH E 5 .   ? -24.057 -7.092  0.183   1.00 28.10 ? 451 HOH A O   1 
HETATM 2394 O  O   . HOH E 5 .   ? -31.870 5.708   13.051  1.00 36.17 ? 452 HOH A O   1 
HETATM 2395 O  O   . HOH E 5 .   ? 1.739   -17.658 7.176   1.00 30.66 ? 453 HOH A O   1 
HETATM 2396 O  O   . HOH E 5 .   ? -27.257 -6.731  7.833   1.00 31.37 ? 454 HOH A O   1 
HETATM 2397 O  O   . HOH E 5 .   ? -26.342 -7.645  30.500  1.00 27.68 ? 455 HOH A O   1 
HETATM 2398 O  O   . HOH E 5 .   ? -5.233  3.616   -5.759  1.00 32.15 ? 456 HOH A O   1 
HETATM 2399 O  O   . HOH E 5 .   ? -8.835  -1.230  41.157  1.00 36.87 ? 457 HOH A O   1 
HETATM 2400 O  O   . HOH E 5 .   ? 4.400   -11.528 23.606  1.00 36.71 ? 458 HOH A O   1 
HETATM 2401 O  O   . HOH E 5 .   ? -10.649 -18.957 34.572  1.00 25.29 ? 459 HOH A O   1 
HETATM 2402 O  O   . HOH E 5 .   ? -18.050 -20.626 -1.310  1.00 28.13 ? 460 HOH A O   1 
HETATM 2403 O  O   . HOH E 5 .   ? 0.200   -19.724 10.976  1.00 29.14 ? 461 HOH A O   1 
HETATM 2404 O  O   . HOH E 5 .   ? -16.617 -15.299 33.152  1.00 27.20 ? 462 HOH A O   1 
HETATM 2405 O  O   . HOH E 5 .   ? -16.914 -17.992 20.242  1.00 28.23 ? 463 HOH A O   1 
HETATM 2406 O  O   . HOH E 5 .   ? -3.939  0.603   13.937  1.00 19.62 ? 464 HOH A O   1 
HETATM 2407 O  O   . HOH E 5 .   ? -17.395 -16.269 22.051  1.00 22.79 ? 465 HOH A O   1 
HETATM 2408 O  O   . HOH E 5 .   ? 3.024   -13.577 8.174   1.00 25.43 ? 466 HOH A O   1 
HETATM 2409 O  O   . HOH E 5 .   ? -21.759 -14.188 18.566  1.00 27.02 ? 467 HOH A O   1 
HETATM 2410 O  O   . HOH E 5 .   ? -1.205  -6.182  36.571  1.00 28.17 ? 468 HOH A O   1 
HETATM 2411 O  O   . HOH E 5 .   ? -20.744 8.259   30.290  1.00 28.56 ? 469 HOH A O   1 
HETATM 2412 O  O   . HOH E 5 .   ? 2.186   -9.780  30.635  1.00 33.62 ? 470 HOH A O   1 
HETATM 2413 O  O   . HOH E 5 .   ? -8.344  7.757   8.369   1.00 32.12 ? 471 HOH A O   1 
HETATM 2414 O  O   . HOH E 5 .   ? -32.017 -2.640  13.849  1.00 29.63 ? 472 HOH A O   1 
HETATM 2415 O  O   . HOH E 5 .   ? 1.805   2.981   -5.069  1.00 34.09 ? 473 HOH A O   1 
HETATM 2416 O  O   . HOH E 5 .   ? -19.442 -4.104  41.720  1.00 33.51 ? 474 HOH A O   1 
HETATM 2417 O  O   . HOH E 5 .   ? -17.288 -9.272  36.729  1.00 45.29 ? 475 HOH A O   1 
HETATM 2418 O  O   . HOH E 5 .   ? -16.815 19.550  22.259  1.00 44.46 ? 476 HOH A O   1 
HETATM 2419 O  O   . HOH E 5 .   ? -24.013 -2.457  29.150  1.00 28.33 ? 477 HOH A O   1 
HETATM 2420 O  O   . HOH E 5 .   ? -0.921  -17.390 -1.951  1.00 30.68 ? 478 HOH A O   1 
HETATM 2421 O  O   . HOH E 5 .   ? 5.468   -10.723 18.915  1.00 37.49 ? 479 HOH A O   1 
HETATM 2422 O  O   . HOH E 5 .   ? 6.421   -5.493  3.614   1.00 43.60 ? 480 HOH A O   1 
HETATM 2423 O  O   . HOH E 5 .   ? -17.025 -7.355  39.969  1.00 27.21 ? 481 HOH A O   1 
HETATM 2424 O  O   . HOH E 5 .   ? -28.479 -0.341  6.631   1.00 32.08 ? 482 HOH A O   1 
HETATM 2425 O  O   . HOH E 5 .   ? -22.995 -14.638 16.074  1.00 37.81 ? 483 HOH A O   1 
HETATM 2426 O  O   . HOH E 5 .   ? 6.620   5.237   28.679  1.00 28.57 ? 484 HOH A O   1 
HETATM 2427 O  O   . HOH E 5 .   ? -32.716 1.949   12.165  1.00 29.84 ? 485 HOH A O   1 
HETATM 2428 O  O   . HOH E 5 .   ? -27.051 -12.945 20.370  1.00 32.61 ? 486 HOH A O   1 
HETATM 2429 O  O   . HOH E 5 .   ? 0.646   -9.109  -5.377  1.00 39.09 ? 487 HOH A O   1 
HETATM 2430 O  O   . HOH E 5 .   ? 7.230   -3.448  30.392  1.00 31.70 ? 488 HOH A O   1 
HETATM 2431 O  O   . HOH E 5 .   ? -31.665 6.756   15.408  1.00 35.74 ? 489 HOH A O   1 
HETATM 2432 O  O   . HOH E 5 .   ? 6.526   8.480   18.069  1.00 28.90 ? 490 HOH A O   1 
HETATM 2433 O  O   . HOH E 5 .   ? -27.991 -1.533  28.606  1.00 28.36 ? 491 HOH A O   1 
HETATM 2434 O  O   . HOH E 5 .   ? -11.565 0.987   -7.726  1.00 31.75 ? 492 HOH A O   1 
HETATM 2435 O  O   . HOH E 5 .   ? -12.969 3.487   -6.851  1.00 28.67 ? 493 HOH A O   1 
HETATM 2436 O  O   . HOH E 5 .   ? -25.237 10.997  19.681  1.00 35.06 ? 494 HOH A O   1 
HETATM 2437 O  O   . HOH E 5 .   ? -12.188 9.532   3.267   1.00 24.60 ? 495 HOH A O   1 
HETATM 2438 O  O   . HOH E 5 .   ? -10.282 3.014   37.771  1.00 29.53 ? 496 HOH A O   1 
HETATM 2439 O  O   . HOH E 5 .   ? -12.843 -22.169 8.528   1.00 26.14 ? 497 HOH A O   1 
HETATM 2440 O  O   . HOH E 5 .   ? 2.052   8.188   27.918  1.00 34.03 ? 498 HOH A O   1 
HETATM 2441 O  O   . HOH E 5 .   ? -14.167 3.658   33.485  1.00 34.58 ? 499 HOH A O   1 
HETATM 2442 O  O   . HOH E 5 .   ? -23.958 -3.563  3.996   1.00 29.83 ? 500 HOH A O   1 
HETATM 2443 O  O   . HOH E 5 .   ? -26.756 3.061   21.000  1.00 30.98 ? 501 HOH A O   1 
HETATM 2444 O  O   . HOH E 5 .   ? 5.193   -7.573  25.908  1.00 32.67 ? 502 HOH A O   1 
HETATM 2445 O  O   . HOH E 5 .   ? -25.875 8.067   6.142   1.00 28.59 ? 503 HOH A O   1 
HETATM 2446 O  O   . HOH E 5 .   ? -4.274  -7.108  38.362  1.00 38.49 ? 504 HOH A O   1 
HETATM 2447 O  O   . HOH E 5 .   ? -22.519 -12.408 24.971  1.00 26.97 ? 505 HOH A O   1 
HETATM 2448 O  O   . HOH E 5 .   ? -30.322 -6.610  7.918   1.00 31.94 ? 506 HOH A O   1 
HETATM 2449 O  O   . HOH E 5 .   ? -17.124 -6.652  42.570  1.00 27.88 ? 507 HOH A O   1 
HETATM 2450 O  O   . HOH E 5 .   ? -6.056  17.528  27.682  1.00 28.10 ? 508 HOH A O   1 
HETATM 2451 O  O   . HOH E 5 .   ? -3.573  -15.707 -2.076  1.00 30.84 ? 509 HOH A O   1 
HETATM 2452 O  O   . HOH E 5 .   ? -11.051 1.129   33.739  1.00 24.17 ? 510 HOH A O   1 
HETATM 2453 O  O   . HOH E 5 .   ? -5.203  2.303   12.242  1.00 22.79 ? 511 HOH A O   1 
HETATM 2454 O  O   . HOH E 5 .   ? -11.666 -0.416  43.618  1.00 25.58 ? 512 HOH A O   1 
HETATM 2455 O  O   . HOH E 5 .   ? -22.736 -9.648  25.326  1.00 26.69 ? 513 HOH A O   1 
HETATM 2456 O  O   . HOH E 5 .   ? -27.957 5.004   25.361  1.00 26.36 ? 514 HOH A O   1 
HETATM 2457 O  O   . HOH E 5 .   ? -27.793 6.269   21.618  1.00 30.69 ? 515 HOH A O   1 
HETATM 2458 O  O   . HOH E 5 .   ? -30.300 0.609   28.710  1.00 43.34 ? 516 HOH A O   1 
HETATM 2459 O  O   . HOH E 5 .   ? -3.264  -17.864 -0.073  1.00 36.14 ? 517 HOH A O   1 
HETATM 2460 O  O   . HOH E 5 .   ? 1.269   -16.335 -2.213  1.00 35.92 ? 518 HOH A O   1 
HETATM 2461 O  O   . HOH E 5 .   ? -4.232  3.555   10.602  1.00 34.32 ? 519 HOH A O   1 
HETATM 2462 O  O   . HOH E 5 .   ? -10.755 8.900   7.598   1.00 24.67 ? 520 HOH A O   1 
HETATM 2463 O  O   . HOH E 5 .   ? -18.423 2.571   -6.460  1.00 29.73 ? 521 HOH A O   1 
HETATM 2464 O  O   . HOH E 5 .   ? 3.008   -14.565 1.473   1.00 30.81 ? 522 HOH A O   1 
HETATM 2465 O  O   . HOH E 5 .   ? -29.810 4.126   27.392  1.00 28.90 ? 523 HOH A O   1 
HETATM 2466 O  O   . HOH E 5 .   ? -14.985 9.302   31.777  1.00 36.31 ? 524 HOH A O   1 
HETATM 2467 O  O   . HOH E 5 .   ? 1.961   -4.552  -12.366 1.00 30.80 ? 525 HOH A O   1 
HETATM 2468 O  O   . HOH E 5 .   ? -5.935  -11.655 36.614  1.00 32.31 ? 526 HOH A O   1 
HETATM 2469 O  O   . HOH E 5 .   ? -6.363  -19.537 5.388   1.00 31.07 ? 527 HOH A O   1 
HETATM 2470 O  O   . HOH E 5 .   ? -25.294 8.764   26.104  1.00 41.46 ? 528 HOH A O   1 
HETATM 2471 O  O   . HOH E 5 .   ? 2.675   -14.484 -5.732  1.00 32.19 ? 529 HOH A O   1 
HETATM 2472 O  O   . HOH E 5 .   ? 12.272  -4.166  -9.126  1.00 29.55 ? 530 HOH A O   1 
HETATM 2473 O  O   . HOH E 5 .   ? -18.738 -20.912 14.934  1.00 31.51 ? 531 HOH A O   1 
HETATM 2474 O  O   . HOH E 5 .   ? 5.339   -7.242  22.488  1.00 24.95 ? 532 HOH A O   1 
HETATM 2475 O  O   . HOH E 5 .   ? 4.031   4.334   10.946  1.00 33.18 ? 533 HOH A O   1 
HETATM 2476 O  O   . HOH E 5 .   ? -16.273 16.768  26.813  1.00 31.01 ? 534 HOH A O   1 
HETATM 2477 O  O   . HOH E 5 .   ? 9.899   -4.519  -7.977  1.00 26.95 ? 535 HOH A O   1 
HETATM 2478 O  O   . HOH E 5 .   ? -32.281 -0.005  14.468  1.00 38.55 ? 536 HOH A O   1 
HETATM 2479 O  O   A HOH E 5 .   ? -21.363 -14.060 23.164  0.50 16.74 ? 537 HOH A O   1 
HETATM 2480 O  O   B HOH E 5 .   ? -20.001 -15.482 22.617  0.50 14.50 ? 537 HOH A O   1 
HETATM 2481 O  O   . HOH E 5 .   ? -18.049 6.331   39.040  1.00 33.82 ? 538 HOH A O   1 
HETATM 2482 O  O   . HOH E 5 .   ? -20.898 5.847   32.759  1.00 29.38 ? 539 HOH A O   1 
HETATM 2483 O  O   . HOH E 5 .   ? 10.979  -9.525  9.671   1.00 32.72 ? 540 HOH A O   1 
HETATM 2484 O  O   . HOH E 5 .   ? 10.304  -6.840  -8.911  1.00 32.86 ? 541 HOH A O   1 
HETATM 2485 O  O   . HOH E 5 .   ? 6.373   -11.119 15.309  1.00 30.31 ? 542 HOH A O   1 
HETATM 2486 O  O   . HOH E 5 .   ? -0.968  3.881   13.933  1.00 29.36 ? 543 HOH A O   1 
HETATM 2487 O  O   . HOH E 5 .   ? 3.569   -13.789 12.540  1.00 35.81 ? 544 HOH A O   1 
HETATM 2488 O  O   . HOH E 5 .   ? -28.338 11.817  5.241   1.00 23.44 ? 545 HOH A O   1 
HETATM 2489 O  O   . HOH E 5 .   ? -9.108  -10.031 -1.266  1.00 26.77 ? 546 HOH A O   1 
HETATM 2490 O  O   . HOH E 5 .   ? -12.715 -9.025  -3.163  1.00 25.84 ? 547 HOH A O   1 
HETATM 2491 O  O   . HOH E 5 .   ? -28.171 5.686   19.028  1.00 29.96 ? 548 HOH A O   1 
HETATM 2492 O  O   . HOH E 5 .   ? -17.012 -14.050 37.774  1.00 32.46 ? 549 HOH A O   1 
HETATM 2493 O  O   . HOH E 5 .   ? -19.437 -15.021 26.248  1.00 29.54 ? 550 HOH A O   1 
HETATM 2494 O  O   . HOH E 5 .   ? -5.056  7.474   5.834   1.00 31.54 ? 551 HOH A O   1 
HETATM 2495 O  O   . HOH E 5 .   ? -2.886  17.643  14.385  1.00 31.28 ? 552 HOH A O   1 
HETATM 2496 O  O   . HOH E 5 .   ? 7.817   -8.000  -0.536  1.00 35.27 ? 553 HOH A O   1 
HETATM 2497 O  O   . HOH E 5 .   ? -0.775  6.371   40.901  1.00 32.45 ? 554 HOH A O   1 
HETATM 2498 O  O   . HOH E 5 .   ? 4.164   -0.997  36.694  1.00 38.97 ? 555 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 4   ? 0.3262 0.3114 0.3623 -0.0327 0.0552  0.0626  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.3116 0.2836 0.3608 -0.0327 0.0312  0.0295  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.2612 0.2499 0.3206 -0.0291 0.0552  0.0092  4   HIS A C   
4    O  O   . HIS A 4   ? 0.2692 0.2462 0.3262 -0.0131 0.0559  -0.0041 4   HIS A O   
5    C  CB  . HIS A 4   ? 0.3637 0.3356 0.3845 -0.0278 0.0287  0.0295  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.3881 0.4027 0.4617 -0.0042 -0.0166 0.0166  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.4594 0.4978 0.5379 -0.0282 -0.0035 0.0260  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.4399 0.4627 0.4863 -0.0223 -0.0024 0.0153  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.4573 0.5133 0.5377 -0.0238 -0.0161 0.0064  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.4710 0.5262 0.5424 -0.0057 -0.0293 -0.0050 4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.2043 0.2204 0.2845 -0.0469 0.0583  -0.0076 5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1642 0.1587 0.2299 -0.0393 0.0529  -0.0103 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1722 0.1569 0.2422 -0.0142 0.0491  -0.0246 5   TRP A C   
14   O  O   . TRP A 5   ? 0.2071 0.1738 0.2340 -0.0373 0.0559  -0.0126 5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1333 0.1351 0.2446 -0.0340 0.0468  -0.0187 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1681 0.1392 0.2374 -0.0120 0.0635  -0.0112 5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.1961 0.1496 0.1991 -0.0067 0.0387  0.0060  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1274 0.1844 0.2295 -0.0428 0.0144  -0.0288 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2005 0.1598 0.1998 -0.0370 0.0410  -0.0003 5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1509 0.1333 0.1658 -0.0369 0.0539  -0.0148 5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1282 0.1671 0.1904 -0.0310 0.0285  -0.0389 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1643 0.1842 0.1851 -0.0159 0.0403  -0.0317 5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1411 0.1248 0.1817 0.0126  0.0374  -0.0363 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1682 0.1591 0.2052 0.0094  0.0189  -0.0490 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1523 0.1076 0.2347 -0.0170 0.0554  -0.0414 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1385 0.0844 0.2563 -0.0093 0.0485  -0.0206 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1613 0.1144 0.2713 -0.0011 0.0652  -0.0347 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1303 0.1466 0.2625 0.0027  0.0631  -0.0516 6   GLY A O   
29   N  N   . TYR A 7   ? 0.1673 0.1465 0.2815 -0.0024 0.0827  -0.0450 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1930 0.1303 0.3351 -0.0038 0.0608  -0.0452 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.2061 0.1621 0.3854 -0.0068 0.0552  -0.0377 7   TYR A C   
32   O  O   . TYR A 7   ? 0.2430 0.1560 0.4412 -0.0083 0.0507  -0.0257 7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1533 0.1368 0.2826 0.0139  0.0528  -0.0420 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1063 0.1090 0.2039 -0.0046 0.0399  -0.0307 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.0864 0.1476 0.1847 -0.0248 0.0456  -0.0535 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1273 0.1054 0.2276 0.0065  0.0366  -0.0561 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1031 0.0908 0.1765 -0.0204 -0.0007 -0.0404 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1199 0.1099 0.1101 -0.0182 0.0520  -0.0219 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1106 0.1161 0.1223 -0.0256 0.0271  -0.0670 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1199 0.0971 0.1360 -0.0130 0.0334  -0.0402 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.2232 0.1593 0.3925 -0.0024 0.0792  -0.0568 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.1834 0.1610 0.3891 0.0086  0.0773  -0.0735 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.2703 0.2226 0.3895 0.0105  0.0704  -0.0637 8   GLY A C   
44   O  O   . GLY A 8   ? 0.2413 0.2433 0.3892 0.0019  0.1071  -0.0865 8   GLY A O   
45   N  N   . LYS A 9   ? 0.2512 0.2656 0.4384 0.0269  0.0359  -0.0361 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.2766 0.2752 0.4030 0.0199  0.0006  -0.0351 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.2618 0.2810 0.4025 0.0233  0.0258  -0.0124 9   LYS A C   
48   O  O   . LYS A 9   ? 0.2707 0.2930 0.4075 -0.0099 0.0218  -0.0460 9   LYS A O   
49   C  CB  . LYS A 9   ? 0.2752 0.3102 0.4128 0.0216  0.0115  -0.0235 9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.3430 0.3363 0.4276 0.0105  -0.0167 -0.0107 9   LYS A CG  
51   C  CD  . LYS A 9   ? 0.3760 0.3473 0.4640 0.0115  0.0182  -0.0148 9   LYS A CD  
52   C  CE  . LYS A 9   ? 0.4310 0.3908 0.4885 0.0154  0.0099  -0.0063 9   LYS A CE  
53   N  NZ  . LYS A 9   ? 0.4308 0.3989 0.5131 0.0318  0.0277  -0.0391 9   LYS A NZ  
54   N  N   . HIS A 10  ? 0.2216 0.2270 0.4028 0.0290  0.0589  -0.0338 10  HIS A N   
55   C  CA  . HIS A 10  ? 0.2093 0.2220 0.3842 0.0271  0.0852  -0.0095 10  HIS A CA  
56   C  C   . HIS A 10  ? 0.1484 0.1928 0.3480 0.0348  0.0746  -0.0165 10  HIS A C   
57   O  O   . HIS A 10  ? 0.1873 0.2143 0.3702 0.0437  0.0971  -0.0260 10  HIS A O   
58   C  CB  . HIS A 10  ? 0.1818 0.1687 0.3568 0.0384  0.1071  -0.0065 10  HIS A CB  
59   C  CG  . HIS A 10  ? 0.1986 0.2271 0.3452 0.0166  0.0788  0.0188  10  HIS A CG  
60   N  ND1 . HIS A 10  ? 0.2916 0.3130 0.3914 0.0108  0.0510  -0.0149 10  HIS A ND1 
61   C  CD2 . HIS A 10  ? 0.1803 0.2848 0.3908 -0.0298 0.0971  -0.0017 10  HIS A CD2 
62   C  CE1 . HIS A 10  ? 0.2908 0.3393 0.4059 0.0243  0.0327  -0.0045 10  HIS A CE1 
63   N  NE2 . HIS A 10  ? 0.2392 0.3206 0.3673 0.0084  0.0516  0.0024  10  HIS A NE2 
64   N  N   . ASN A 11  ? 0.1465 0.1982 0.3351 0.0158  0.0907  -0.0093 11  ASN A N   
65   C  CA  . ASN A 11  ? 0.1351 0.1864 0.2904 0.0013  0.0818  -0.0116 11  ASN A CA  
66   C  C   . ASN A 11  ? 0.1388 0.1699 0.2833 0.0033  0.0835  -0.0183 11  ASN A C   
67   O  O   . ASN A 11  ? 0.1585 0.1538 0.3125 0.0054  0.1022  -0.0051 11  ASN A O   
68   C  CB  . ASN A 11  ? 0.1266 0.1689 0.2917 0.0028  0.0803  -0.0127 11  ASN A CB  
69   C  CG  . ASN A 11  ? 0.1649 0.1978 0.2715 0.0009  0.0866  -0.0230 11  ASN A CG  
70   O  OD1 . ASN A 11  ? 0.2044 0.2058 0.3450 -0.0193 0.1072  -0.0186 11  ASN A OD1 
71   N  ND2 . ASN A 11  ? 0.2303 0.2153 0.3171 -0.0099 0.0408  -0.0273 11  ASN A ND2 
72   N  N   . GLY A 12  ? 0.1414 0.1799 0.2659 -0.0127 0.0771  -0.0235 12  GLY A N   
73   C  CA  . GLY A 12  ? 0.1438 0.1910 0.2432 -0.0072 0.0730  -0.0131 12  GLY A CA  
74   C  C   . GLY A 12  ? 0.1239 0.1689 0.2446 -0.0081 0.0485  -0.0156 12  GLY A C   
75   O  O   . GLY A 12  ? 0.0894 0.1572 0.2634 0.0101  0.0578  0.0101  12  GLY A O   
76   N  N   . PRO A 13  ? 0.0954 0.1377 0.2286 0.0089  0.0454  -0.0048 13  PRO A N   
77   C  CA  . PRO A 13  ? 0.0879 0.1639 0.2261 -0.0010 0.0535  -0.0085 13  PRO A CA  
78   C  C   . PRO A 13  ? 0.1037 0.1326 0.2030 0.0000  0.0438  0.0127  13  PRO A C   
79   O  O   . PRO A 13  ? 0.1150 0.1836 0.2518 -0.0029 0.0436  -0.0146 13  PRO A O   
80   C  CB  . PRO A 13  ? 0.0935 0.1544 0.2416 -0.0361 0.0381  0.0045  13  PRO A CB  
81   C  CG  . PRO A 13  ? 0.1233 0.1012 0.2163 0.0133  0.0364  -0.0362 13  PRO A CG  
82   C  CD  . PRO A 13  ? 0.1085 0.1526 0.2082 0.0196  0.0296  -0.0142 13  PRO A CD  
83   N  N   . GLU A 14  ? 0.1007 0.1259 0.2548 -0.0016 0.0341  -0.0136 14  GLU A N   
84   C  CA  . GLU A 14  ? 0.1444 0.1156 0.2809 0.0202  0.0054  0.0221  14  GLU A CA  
85   C  C   . GLU A 14  ? 0.1132 0.1290 0.2593 0.0291  0.0070  0.0087  14  GLU A C   
86   O  O   . GLU A 14  ? 0.1354 0.1476 0.2845 0.0411  0.0160  0.0225  14  GLU A O   
87   C  CB  . GLU A 14  ? 0.1939 0.1692 0.3097 0.0340  -0.0027 0.0279  14  GLU A CB  
88   C  CG  . GLU A 14  ? 0.2176 0.2446 0.3406 0.0092  -0.0074 -0.0247 14  GLU A CG  
89   C  CD  . GLU A 14  ? 0.2894 0.2959 0.3608 0.0319  -0.0025 -0.0409 14  GLU A CD  
90   O  OE1 . GLU A 14  ? 0.1844 0.1959 0.3581 0.0378  -0.0279 -0.0777 14  GLU A OE1 
91   O  OE2 . GLU A 14  ? 0.4300 0.2240 0.3351 0.0359  0.0364  -0.0601 14  GLU A OE2 
92   N  N   . HIS A 15  ? 0.0897 0.1304 0.2461 0.0185  0.0234  0.0089  15  HIS A N   
93   C  CA  . HIS A 15  ? 0.1081 0.1150 0.2633 0.0107  0.0221  -0.0178 15  HIS A CA  
94   C  C   . HIS A 15  ? 0.0786 0.1181 0.2463 0.0142  0.0108  -0.0140 15  HIS A C   
95   O  O   . HIS A 15  ? 0.0543 0.1057 0.3074 0.0003  0.0150  -0.0172 15  HIS A O   
96   C  CB  . HIS A 15  ? 0.1199 0.1084 0.2635 0.0295  0.0188  -0.0189 15  HIS A CB  
97   C  CG  . HIS A 15  ? 0.1473 0.1642 0.2698 0.0435  0.0155  -0.0041 15  HIS A CG  
98   N  ND1 . HIS A 15  ? 0.1543 0.1914 0.2816 0.0479  -0.0159 -0.0116 15  HIS A ND1 
99   C  CD2 . HIS A 15  ? 0.2340 0.1807 0.2818 0.0633  0.0218  -0.0292 15  HIS A CD2 
100  C  CE1 . HIS A 15  ? 0.2156 0.2633 0.3033 0.0602  -0.0172 -0.0245 15  HIS A CE1 
101  N  NE2 . HIS A 15  ? 0.2131 0.1768 0.3298 0.0701  0.0130  -0.0193 15  HIS A NE2 
102  N  N   . TRP A 16  ? 0.0587 0.1001 0.2466 0.0266  -0.0032 -0.0058 16  TRP A N   
103  C  CA  . TRP A 16  ? 0.0399 0.0950 0.2220 0.0257  0.0004  -0.0374 16  TRP A CA  
104  C  C   . TRP A 16  ? 0.0601 0.1033 0.2172 0.0040  0.0038  -0.0184 16  TRP A C   
105  O  O   . TRP A 16  ? 0.0756 0.1050 0.2506 -0.0136 -0.0132 -0.0061 16  TRP A O   
106  C  CB  . TRP A 16  ? 0.0255 0.1294 0.2017 0.0006  -0.0014 -0.0201 16  TRP A CB  
107  C  CG  . TRP A 16  ? 0.0931 0.1027 0.2051 0.0021  0.0059  -0.0134 16  TRP A CG  
108  C  CD1 . TRP A 16  ? 0.0857 0.0769 0.1703 0.0047  -0.0014 0.0058  16  TRP A CD1 
109  C  CD2 . TRP A 16  ? 0.0839 0.0906 0.1936 -0.0223 -0.0102 -0.0033 16  TRP A CD2 
110  N  NE1 . TRP A 16  ? 0.0599 0.1256 0.1455 -0.0023 0.0278  -0.0372 16  TRP A NE1 
111  C  CE2 . TRP A 16  ? 0.0584 0.0967 0.1805 0.0016  0.0145  0.0130  16  TRP A CE2 
112  C  CE3 . TRP A 16  ? 0.0588 0.0627 0.1828 -0.0353 0.0025  0.0035  16  TRP A CE3 
113  C  CZ2 . TRP A 16  ? 0.0731 0.0866 0.1729 -0.0144 0.0081  0.0063  16  TRP A CZ2 
114  C  CZ3 . TRP A 16  ? 0.0367 0.1360 0.1752 -0.0130 0.0111  -0.0121 16  TRP A CZ3 
115  C  CH2 . TRP A 16  ? 0.0965 0.1236 0.1613 0.0120  0.0009  0.0021  16  TRP A CH2 
116  N  N   . HIS A 17  ? 0.0895 0.1438 0.2319 0.0024  0.0149  -0.0148 17  HIS A N   
117  C  CA  . HIS A 17  ? 0.0736 0.1650 0.2389 -0.0037 0.0055  -0.0006 17  HIS A CA  
118  C  C   . HIS A 17  ? 0.0883 0.1617 0.2538 -0.0195 0.0005  0.0014  17  HIS A C   
119  O  O   . HIS A 17  ? 0.0882 0.1908 0.2881 -0.0083 -0.0009 -0.0201 17  HIS A O   
120  C  CB  . HIS A 17  ? 0.0657 0.1607 0.2295 0.0294  0.0046  0.0069  17  HIS A CB  
121  C  CG  . HIS A 17  ? 0.0715 0.1478 0.2125 0.0092  0.0031  0.0413  17  HIS A CG  
122  N  ND1 . HIS A 17  ? 0.0886 0.1988 0.2704 0.0427  -0.0553 0.0637  17  HIS A ND1 
123  C  CD2 . HIS A 17  ? 0.1332 0.1827 0.2560 0.0497  -0.0058 0.0132  17  HIS A CD2 
124  C  CE1 . HIS A 17  ? 0.1157 0.1818 0.2834 0.0789  -0.0031 0.0241  17  HIS A CE1 
125  N  NE2 . HIS A 17  ? 0.1489 0.2103 0.2748 0.0306  -0.0192 0.0445  17  HIS A NE2 
126  N  N   . LYS A 18  ? 0.0413 0.1640 0.2636 -0.0142 -0.0086 0.0045  18  LYS A N   
127  C  CA  . LYS A 18  ? 0.0753 0.1304 0.2643 -0.0148 0.0055  0.0168  18  LYS A CA  
128  C  C   . LYS A 18  ? 0.1131 0.1344 0.2843 -0.0369 -0.0042 0.0226  18  LYS A C   
129  O  O   . LYS A 18  ? 0.1534 0.1890 0.3699 -0.0504 -0.0478 0.0352  18  LYS A O   
130  C  CB  . LYS A 18  ? 0.0949 0.1762 0.2700 -0.0027 -0.0001 0.0170  18  LYS A CB  
131  C  CG  . LYS A 18  ? 0.1219 0.1451 0.2949 0.0566  -0.0132 0.0154  18  LYS A CG  
132  C  CD  . LYS A 18  ? 0.1224 0.2043 0.2323 0.0163  -0.0246 0.0147  18  LYS A CD  
133  C  CE  . LYS A 18  ? 0.1573 0.1566 0.2889 0.0187  -0.0056 0.0051  18  LYS A CE  
134  N  NZ  . LYS A 18  ? 0.1221 0.1480 0.2869 0.0230  0.0100  0.0353  18  LYS A NZ  
135  N  N   . ASP A 19  ? 0.1171 0.1709 0.2668 -0.0208 0.0064  0.0419  19  ASP A N   
136  C  CA  . ASP A 19  ? 0.1171 0.2013 0.2836 -0.0222 0.0115  0.0188  19  ASP A CA  
137  C  C   . ASP A 19  ? 0.1198 0.1623 0.2979 -0.0214 0.0069  0.0068  19  ASP A C   
138  O  O   . ASP A 19  ? 0.1379 0.1690 0.3508 -0.0393 0.0141  0.0116  19  ASP A O   
139  C  CB  . ASP A 19  ? 0.1747 0.2433 0.2589 0.0198  -0.0014 0.0235  19  ASP A CB  
140  C  CG  . ASP A 19  ? 0.1745 0.3149 0.2971 -0.0206 -0.0133 0.0152  19  ASP A CG  
141  O  OD1 . ASP A 19  ? 0.1618 0.3759 0.3919 -0.0194 0.0387  0.0092  19  ASP A OD1 
142  O  OD2 . ASP A 19  ? 0.4001 0.4720 0.3935 -0.0115 0.0111  -0.0106 19  ASP A OD2 
143  N  N   . PHE A 20  ? 0.0830 0.1511 0.2527 -0.0252 0.0077  0.0062  20  PHE A N   
144  C  CA  . PHE A 20  ? 0.0874 0.1470 0.2348 -0.0272 0.0051  -0.0092 20  PHE A CA  
145  C  C   . PHE A 20  ? 0.0949 0.1352 0.2323 -0.0146 -0.0127 -0.0024 20  PHE A C   
146  O  O   . PHE A 20  ? 0.0893 0.0869 0.2487 -0.0072 -0.0074 -0.0099 20  PHE A O   
147  C  CB  . PHE A 20  ? 0.1109 0.1775 0.2416 -0.0432 0.0029  0.0033  20  PHE A CB  
148  C  CG  . PHE A 20  ? 0.0693 0.1711 0.2438 -0.0222 -0.0034 -0.0002 20  PHE A CG  
149  C  CD1 . PHE A 20  ? 0.1236 0.2131 0.2718 0.0044  -0.0050 0.0316  20  PHE A CD1 
150  C  CD2 . PHE A 20  ? 0.1566 0.1844 0.2092 -0.0236 0.0267  0.0019  20  PHE A CD2 
151  C  CE1 . PHE A 20  ? 0.2069 0.2135 0.2638 0.0000  -0.0038 0.0158  20  PHE A CE1 
152  C  CE2 . PHE A 20  ? 0.0927 0.1944 0.2571 -0.0139 -0.0197 0.0076  20  PHE A CE2 
153  C  CZ  . PHE A 20  ? 0.1116 0.2124 0.2645 -0.0397 0.0265  0.0504  20  PHE A CZ  
154  N  N   A PRO A 21  ? 0.1087 0.1255 0.2462 -0.0176 -0.0059 -0.0134 21  PRO A N   
155  N  N   B PRO A 21  ? 0.1135 0.1341 0.2335 -0.0256 -0.0151 -0.0057 21  PRO A N   
156  C  CA  A PRO A 21  ? 0.0910 0.1283 0.2231 -0.0255 -0.0092 -0.0175 21  PRO A CA  
157  C  CA  B PRO A 21  ? 0.0894 0.1391 0.1882 -0.0282 -0.0127 -0.0142 21  PRO A CA  
158  C  C   A PRO A 21  ? 0.0948 0.1318 0.2264 -0.0170 -0.0165 -0.0102 21  PRO A C   
159  C  C   B PRO A 21  ? 0.0979 0.1197 0.1931 -0.0139 -0.0127 -0.0289 21  PRO A C   
160  O  O   A PRO A 21  ? 0.0835 0.1298 0.2395 -0.0294 -0.0233 -0.0140 21  PRO A O   
161  O  O   B PRO A 21  ? 0.1129 0.1192 0.2048 -0.0120 -0.0182 -0.0308 21  PRO A O   
162  C  CB  A PRO A 21  ? 0.0760 0.1427 0.2314 -0.0270 -0.0116 -0.0143 21  PRO A CB  
163  C  CB  B PRO A 21  ? 0.0906 0.1413 0.2115 -0.0292 -0.0197 0.0000  21  PRO A CB  
164  C  CG  A PRO A 21  ? 0.1164 0.1327 0.2319 -0.0336 -0.0198 -0.0163 21  PRO A CG  
165  C  CG  B PRO A 21  ? 0.1019 0.1414 0.1930 -0.0294 -0.0093 -0.0049 21  PRO A CG  
166  C  CD  A PRO A 21  ? 0.0870 0.1176 0.2342 -0.0156 0.0054  -0.0164 21  PRO A CD  
167  C  CD  B PRO A 21  ? 0.0915 0.1461 0.2203 -0.0357 -0.0084 0.0068  21  PRO A CD  
168  N  N   A ILE A 22  ? 0.0869 0.0898 0.2263 0.0004  0.0078  -0.0228 22  ILE A N   
169  N  N   B ILE A 22  ? 0.0994 0.1067 0.1817 -0.0282 -0.0168 -0.0199 22  ILE A N   
170  C  CA  A ILE A 22  ? 0.0933 0.1107 0.1983 -0.0159 -0.0036 -0.0107 22  ILE A CA  
171  C  CA  B ILE A 22  ? 0.0801 0.0951 0.1837 -0.0166 -0.0191 -0.0167 22  ILE A CA  
172  C  C   A ILE A 22  ? 0.1009 0.0955 0.1828 -0.0027 -0.0145 -0.0122 22  ILE A C   
173  C  C   B ILE A 22  ? 0.0996 0.0884 0.1739 -0.0037 -0.0229 -0.0126 22  ILE A C   
174  O  O   A ILE A 22  ? 0.0857 0.1100 0.2034 -0.0046 -0.0181 -0.0159 22  ILE A O   
175  O  O   B ILE A 22  ? 0.0762 0.1121 0.2049 0.0007  -0.0242 -0.0191 22  ILE A O   
176  C  CB  A ILE A 22  ? 0.0958 0.0920 0.1750 -0.0214 0.0058  0.0023  22  ILE A CB  
177  C  CB  B ILE A 22  ? 0.0876 0.1126 0.1603 -0.0053 -0.0179 -0.0089 22  ILE A CB  
178  C  CG1 A ILE A 22  ? 0.1211 0.1515 0.1926 0.0145  0.0011  -0.0172 22  ILE A CG1 
179  C  CG1 B ILE A 22  ? 0.0711 0.0412 0.1625 -0.0269 -0.0034 -0.0020 22  ILE A CG1 
180  C  CG2 A ILE A 22  ? 0.1077 0.1521 0.1947 -0.0246 -0.0088 0.0015  22  ILE A CG2 
181  C  CG2 B ILE A 22  ? 0.0684 0.1293 0.1472 -0.0149 -0.0271 -0.0115 22  ILE A CG2 
182  C  CD1 A ILE A 22  ? 0.2323 0.2504 0.1949 -0.0089 -0.0299 -0.0008 22  ILE A CD1 
183  C  CD1 B ILE A 22  ? 0.0556 0.1044 0.1941 -0.0126 -0.0291 -0.0042 22  ILE A CD1 
184  N  N   . ALA A 23  ? 0.0725 0.0848 0.1879 -0.0104 -0.0266 -0.0280 23  ALA A N   
185  C  CA  . ALA A 23  ? 0.1224 0.0980 0.1886 -0.0151 -0.0161 -0.0285 23  ALA A CA  
186  C  C   . ALA A 23  ? 0.1020 0.1075 0.1968 -0.0076 -0.0242 -0.0125 23  ALA A C   
187  O  O   . ALA A 23  ? 0.0815 0.1164 0.2053 -0.0332 -0.0213 0.0002  23  ALA A O   
188  C  CB  . ALA A 23  ? 0.1200 0.1057 0.2024 0.0069  -0.0105 -0.0340 23  ALA A CB  
189  N  N   . LYS A 24  ? 0.1253 0.1328 0.1687 0.0049  -0.0409 -0.0145 24  LYS A N   
190  C  CA  . LYS A 24  ? 0.0976 0.1998 0.1833 0.0004  -0.0316 -0.0186 24  LYS A CA  
191  C  C   . LYS A 24  ? 0.1236 0.1880 0.1836 0.0063  -0.0438 -0.0162 24  LYS A C   
192  O  O   . LYS A 24  ? 0.1235 0.2448 0.2193 0.0042  -0.0607 -0.0048 24  LYS A O   
193  C  CB  . LYS A 24  ? 0.1256 0.1968 0.2105 0.0162  -0.0319 -0.0054 24  LYS A CB  
194  C  CG  . LYS A 24  ? 0.1100 0.2767 0.2269 0.0011  -0.0054 -0.0008 24  LYS A CG  
195  C  CD  . LYS A 24  ? 0.1915 0.2979 0.3581 0.0213  -0.0117 -0.0051 24  LYS A CD  
196  C  CE  . LYS A 24  ? 0.2361 0.3379 0.3937 -0.0040 0.0374  -0.0129 24  LYS A CE  
197  N  NZ  . LYS A 24  ? 0.3001 0.2998 0.4097 0.0487  0.0280  -0.0242 24  LYS A NZ  
198  N  N   . GLY A 25  ? 0.1015 0.1851 0.1997 0.0113  -0.0087 -0.0128 25  GLY A N   
199  C  CA  . GLY A 25  ? 0.1137 0.2044 0.1933 -0.0054 -0.0062 -0.0080 25  GLY A CA  
200  C  C   . GLY A 25  ? 0.1065 0.2011 0.1626 -0.0147 -0.0246 -0.0158 25  GLY A C   
201  O  O   . GLY A 25  ? 0.1499 0.2055 0.1647 0.0055  -0.0455 -0.0045 25  GLY A O   
202  N  N   . GLU A 26  ? 0.1031 0.2177 0.2006 -0.0036 -0.0454 -0.0192 26  GLU A N   
203  C  CA  . GLU A 26  ? 0.1382 0.2198 0.1738 -0.0073 -0.0373 -0.0355 26  GLU A CA  
204  C  C   . GLU A 26  ? 0.1176 0.1656 0.1625 -0.0219 -0.0203 -0.0135 26  GLU A C   
205  O  O   . GLU A 26  ? 0.1160 0.1740 0.1438 -0.0259 -0.0333 -0.0140 26  GLU A O   
206  C  CB  . GLU A 26  ? 0.1553 0.2610 0.1831 -0.0351 -0.0404 -0.0580 26  GLU A CB  
207  C  CG  . GLU A 26  ? 0.1730 0.2829 0.2336 -0.0073 -0.0330 -0.0414 26  GLU A CG  
208  C  CD  . GLU A 26  ? 0.3068 0.3656 0.3441 -0.0001 -0.0357 0.0129  26  GLU A CD  
209  O  OE1 . GLU A 26  ? 0.3273 0.3941 0.3136 -0.0261 -0.0512 -0.0116 26  GLU A OE1 
210  O  OE2 . GLU A 26  ? 0.3070 0.4134 0.4145 0.0040  -0.0217 0.0026  26  GLU A OE2 
211  N  N   . ARG A 27  ? 0.1088 0.1153 0.1311 -0.0340 -0.0360 -0.0342 27  ARG A N   
212  C  CA  . ARG A 27  ? 0.0992 0.1086 0.1170 -0.0135 -0.0260 -0.0255 27  ARG A CA  
213  C  C   . ARG A 27  ? 0.1005 0.1023 0.1111 -0.0096 -0.0166 -0.0279 27  ARG A C   
214  O  O   . ARG A 27  ? 0.0920 0.0887 0.1412 0.0034  -0.0328 -0.0237 27  ARG A O   
215  C  CB  . ARG A 27  ? 0.1619 0.1394 0.1653 -0.0033 -0.0065 -0.0274 27  ARG A CB  
216  C  CG  . ARG A 27  ? 0.1724 0.1819 0.1761 0.0016  -0.0234 -0.0135 27  ARG A CG  
217  C  CD  . ARG A 27  ? 0.1853 0.1887 0.1781 0.0186  -0.0433 -0.0116 27  ARG A CD  
218  N  NE  . ARG A 27  ? 0.1767 0.1922 0.2415 0.0054  -0.0109 -0.0074 27  ARG A NE  
219  C  CZ  . ARG A 27  ? 0.1023 0.1420 0.1344 -0.0017 -0.0023 0.0056  27  ARG A CZ  
220  N  NH1 . ARG A 27  ? 0.2184 0.1940 0.1432 0.0031  -0.0069 -0.1153 27  ARG A NH1 
221  N  NH2 . ARG A 27  ? 0.1637 0.1908 0.1720 -0.0159 -0.0272 -0.0136 27  ARG A NH2 
222  N  N   . GLN A 28  ? 0.0741 0.0898 0.1299 -0.0086 -0.0097 -0.0386 28  GLN A N   
223  C  CA  . GLN A 28  ? 0.0472 0.0970 0.1101 -0.0122 -0.0145 -0.0369 28  GLN A CA  
224  C  C   . GLN A 28  ? 0.0837 0.0598 0.0847 -0.0143 -0.0156 -0.0227 28  GLN A C   
225  O  O   . GLN A 28  ? 0.0967 0.1081 0.0700 -0.0202 -0.0112 -0.0150 28  GLN A O   
226  C  CB  . GLN A 28  ? 0.0328 0.1195 0.1247 0.0007  -0.0253 -0.0302 28  GLN A CB  
227  C  CG  . GLN A 28  ? 0.0733 0.0951 0.1176 -0.0232 -0.0271 -0.0153 28  GLN A CG  
228  C  CD  . GLN A 28  ? 0.1053 0.0868 0.1389 -0.0051 -0.0161 -0.0251 28  GLN A CD  
229  O  OE1 . GLN A 28  ? 0.0976 0.0627 0.1405 -0.0182 -0.0199 -0.0194 28  GLN A OE1 
230  N  NE2 . GLN A 28  ? 0.0556 0.0885 0.1805 -0.0003 -0.0476 -0.0133 28  GLN A NE2 
231  N  N   . SER A 29  ? 0.0664 0.0659 0.0899 -0.0039 -0.0239 -0.0334 29  SER A N   
232  C  CA  . SER A 29  ? 0.0608 0.0749 0.0826 0.0093  -0.0404 -0.0337 29  SER A CA  
233  C  C   . SER A 29  ? 0.0779 0.0841 0.0845 0.0054  -0.0220 0.0044  29  SER A C   
234  O  O   . SER A 29  ? 0.1033 0.0741 0.0931 0.0021  -0.0022 -0.0096 29  SER A O   
235  C  CB  . SER A 29  ? 0.0704 0.0689 0.1141 0.0074  -0.0339 -0.0132 29  SER A CB  
236  O  OG  . SER A 29  ? 0.0916 0.0496 0.1232 -0.0088 0.0106  -0.0388 29  SER A OG  
237  N  N   . PRO A 30  ? 0.0712 0.0720 0.1031 0.0149  -0.0170 -0.0074 30  PRO A N   
238  C  CA  . PRO A 30  ? 0.0829 0.0706 0.0893 -0.0051 -0.0137 0.0059  30  PRO A CA  
239  C  C   . PRO A 30  ? 0.0541 0.0623 0.1071 -0.0049 -0.0148 0.0135  30  PRO A C   
240  O  O   . PRO A 30  ? 0.0711 0.0580 0.1436 -0.0154 -0.0250 -0.0022 30  PRO A O   
241  C  CB  . PRO A 30  ? 0.0803 0.0574 0.1234 0.0036  -0.0203 -0.0056 30  PRO A CB  
242  C  CG  . PRO A 30  ? 0.0969 0.0805 0.1124 -0.0053 0.0030  -0.0165 30  PRO A CG  
243  C  CD  . PRO A 30  ? 0.0860 0.0843 0.1083 0.0009  -0.0011 -0.0280 30  PRO A CD  
244  N  N   . VAL A 31  ? 0.0778 0.0708 0.0918 -0.0114 0.0029  0.0192  31  VAL A N   
245  C  CA  . VAL A 31  ? 0.1157 0.0682 0.1005 -0.0141 -0.0117 -0.0079 31  VAL A CA  
246  C  C   . VAL A 31  ? 0.1024 0.0713 0.0936 -0.0119 -0.0113 0.0054  31  VAL A C   
247  O  O   . VAL A 31  ? 0.0915 0.0666 0.1263 -0.0202 -0.0107 0.0121  31  VAL A O   
248  C  CB  . VAL A 31  ? 0.0971 0.0985 0.0994 0.0012  -0.0189 -0.0245 31  VAL A CB  
249  C  CG1 . VAL A 31  ? 0.0801 0.0593 0.1551 0.0044  -0.0090 -0.0078 31  VAL A CG1 
250  C  CG2 . VAL A 31  ? 0.0878 0.1004 0.1046 0.0365  -0.0086 -0.0018 31  VAL A CG2 
251  N  N   . ASP A 32  ? 0.1057 0.0598 0.0934 -0.0060 -0.0295 0.0099  32  ASP A N   
252  C  CA  . ASP A 32  ? 0.1002 0.0470 0.1229 0.0225  -0.0037 0.0184  32  ASP A CA  
253  C  C   . ASP A 32  ? 0.1159 0.0894 0.1044 0.0101  -0.0109 -0.0060 32  ASP A C   
254  O  O   . ASP A 32  ? 0.1245 0.1284 0.1100 0.0117  -0.0134 -0.0186 32  ASP A O   
255  C  CB  . ASP A 32  ? 0.1193 0.0481 0.1789 0.0322  -0.0111 0.0127  32  ASP A CB  
256  C  CG  . ASP A 32  ? 0.1609 0.0676 0.1651 0.0036  0.0123  -0.0056 32  ASP A CG  
257  O  OD1 . ASP A 32  ? 0.1389 0.0872 0.1253 -0.0070 -0.0205 0.0017  32  ASP A OD1 
258  O  OD2 . ASP A 32  ? 0.2431 0.1137 0.1425 -0.0148 -0.0341 0.0051  32  ASP A OD2 
259  N  N   . ILE A 33  ? 0.0727 0.0911 0.0884 0.0095  -0.0125 -0.0012 33  ILE A N   
260  C  CA  . ILE A 33  ? 0.0957 0.1087 0.1226 0.0050  -0.0084 0.0246  33  ILE A CA  
261  C  C   . ILE A 33  ? 0.1220 0.0930 0.1089 0.0107  -0.0016 0.0107  33  ILE A C   
262  O  O   . ILE A 33  ? 0.1652 0.0793 0.1467 0.0057  -0.0040 0.0100  33  ILE A O   
263  C  CB  . ILE A 33  ? 0.0975 0.1230 0.1434 0.0301  0.0008  0.0225  33  ILE A CB  
264  C  CG1 . ILE A 33  ? 0.0819 0.1048 0.1326 0.0251  0.0039  0.0392  33  ILE A CG1 
265  C  CG2 . ILE A 33  ? 0.1144 0.1656 0.1469 0.0087  0.0302  -0.0010 33  ILE A CG2 
266  C  CD1 . ILE A 33  ? 0.1063 0.0791 0.1639 0.0412  -0.0139 0.0240  33  ILE A CD1 
267  N  N   . ASP A 34  ? 0.1520 0.1206 0.0956 0.0264  -0.0040 0.0331  34  ASP A N   
268  C  CA  . ASP A 34  ? 0.1675 0.1171 0.1225 0.0465  0.0170  0.0408  34  ASP A CA  
269  C  C   . ASP A 34  ? 0.2013 0.1171 0.1170 0.0309  0.0288  0.0366  34  ASP A C   
270  O  O   . ASP A 34  ? 0.2566 0.1447 0.1220 0.0434  0.0323  0.0081  34  ASP A O   
271  C  CB  . ASP A 34  ? 0.2270 0.1206 0.1271 0.0444  0.0054  0.0377  34  ASP A CB  
272  C  CG  . ASP A 34  ? 0.2438 0.1628 0.2551 0.0241  0.0338  0.0406  34  ASP A CG  
273  O  OD1 . ASP A 34  ? 0.3872 0.1818 0.2351 0.0944  0.0621  0.0733  34  ASP A OD1 
274  O  OD2 . ASP A 34  ? 0.3909 0.2349 0.3927 0.0915  0.0195  0.1171  34  ASP A OD2 
275  N  N   . THR A 35  ? 0.2367 0.1619 0.1375 0.0365  0.0238  0.0424  35  THR A N   
276  C  CA  . THR A 35  ? 0.2332 0.1525 0.1287 0.0383  0.0248  0.0381  35  THR A CA  
277  C  C   . THR A 35  ? 0.2546 0.1557 0.1417 0.0526  0.0252  0.0463  35  THR A C   
278  O  O   . THR A 35  ? 0.2692 0.1846 0.1658 0.0559  0.0396  0.0323  35  THR A O   
279  C  CB  . THR A 35  ? 0.2467 0.1457 0.1761 0.0280  0.0228  0.0406  35  THR A CB  
280  O  OG1 . THR A 35  ? 0.2453 0.1604 0.1824 0.0159  0.0565  0.0608  35  THR A OG1 
281  C  CG2 . THR A 35  ? 0.2411 0.1752 0.1414 0.0301  0.0243  0.0457  35  THR A CG2 
282  N  N   . HIS A 36  ? 0.2713 0.1637 0.1218 0.0436  0.0285  0.0448  36  HIS A N   
283  C  CA  . HIS A 36  ? 0.2959 0.1660 0.1390 0.0415  0.0170  0.0473  36  HIS A CA  
284  C  C   . HIS A 36  ? 0.3086 0.2147 0.1508 0.0350  0.0162  0.0267  36  HIS A C   
285  O  O   . HIS A 36  ? 0.3435 0.2329 0.1982 0.0341  0.0395  0.0308  36  HIS A O   
286  C  CB  . HIS A 36  ? 0.3016 0.1952 0.1619 0.0269  -0.0023 0.0628  36  HIS A CB  
287  C  CG  . HIS A 36  ? 0.3508 0.2413 0.1779 0.0231  -0.0484 0.0502  36  HIS A CG  
288  N  ND1 . HIS A 36  ? 0.3975 0.2266 0.2108 0.0312  -0.0874 0.0716  36  HIS A ND1 
289  C  CD2 . HIS A 36  ? 0.3865 0.2237 0.1963 -0.0108 -0.0444 0.0503  36  HIS A CD2 
290  C  CE1 . HIS A 36  ? 0.4189 0.2447 0.2676 0.0146  -0.0456 0.0485  36  HIS A CE1 
291  N  NE2 . HIS A 36  ? 0.4463 0.2851 0.2852 -0.0076 -0.0519 0.0636  36  HIS A NE2 
292  N  N   . THR A 37  ? 0.3124 0.1903 0.1363 0.0438  0.0166  0.0296  37  THR A N   
293  C  CA  . THR A 37  ? 0.3037 0.1757 0.1958 0.0451  0.0122  0.0363  37  THR A CA  
294  C  C   . THR A 37  ? 0.2850 0.1603 0.1337 0.0529  -0.0041 0.0243  37  THR A C   
295  O  O   . THR A 37  ? 0.3476 0.1953 0.1490 0.0777  -0.0115 0.0092  37  THR A O   
296  C  CB  . THR A 37  ? 0.3197 0.1911 0.2661 0.0436  -0.0397 0.0465  37  THR A CB  
297  O  OG1 . THR A 37  ? 0.3545 0.2180 0.3614 0.0519  -0.0157 0.0300  37  THR A OG1 
298  C  CG2 . THR A 37  ? 0.3448 0.2713 0.3150 0.0090  -0.0151 0.0187  37  THR A CG2 
299  N  N   . ALA A 38  ? 0.2685 0.1831 0.1200 0.0619  0.0088  -0.0010 38  ALA A N   
300  C  CA  . ALA A 38  ? 0.2363 0.1547 0.1209 0.0506  0.0520  -0.0081 38  ALA A CA  
301  C  C   . ALA A 38  ? 0.2446 0.1810 0.1896 0.0374  0.0500  0.0000  38  ALA A C   
302  O  O   . ALA A 38  ? 0.2834 0.2132 0.2381 0.0525  0.0883  0.0332  38  ALA A O   
303  C  CB  . ALA A 38  ? 0.2402 0.1709 0.1700 0.0172  0.0113  0.0015  38  ALA A CB  
304  N  N   . LYS A 39  ? 0.2462 0.1801 0.1838 0.0560  0.0299  0.0132  39  LYS A N   
305  C  CA  . LYS A 39  ? 0.2109 0.2327 0.2125 0.0571  0.0141  -0.0014 39  LYS A CA  
306  C  C   . LYS A 39  ? 0.1888 0.2496 0.1814 0.0381  0.0193  -0.0005 39  LYS A C   
307  O  O   . LYS A 39  ? 0.1812 0.2518 0.1214 0.0264  0.0141  -0.0087 39  LYS A O   
308  C  CB  . LYS A 39  ? 0.2265 0.2468 0.2297 0.0496  0.0217  -0.0254 39  LYS A CB  
309  C  CG  . LYS A 39  ? 0.2388 0.2953 0.2400 0.0298  0.0351  0.0084  39  LYS A CG  
310  C  CD  . LYS A 39  ? 0.2386 0.3059 0.2365 0.0609  0.0043  0.0516  39  LYS A CD  
311  C  CE  . LYS A 39  ? 0.3186 0.3632 0.2376 0.0215  0.0199  0.0279  39  LYS A CE  
312  N  NZ  . LYS A 39  ? 0.2485 0.3835 0.3031 0.0462  0.0270  0.0792  39  LYS A NZ  
313  N  N   . TYR A 40  ? 0.1977 0.2560 0.1706 0.0261  0.0141  -0.0003 40  TYR A N   
314  C  CA  . TYR A 40  ? 0.1934 0.2557 0.1782 0.0004  0.0259  0.0013  40  TYR A CA  
315  C  C   . TYR A 40  ? 0.2100 0.2447 0.1765 0.0192  0.0126  0.0035  40  TYR A C   
316  O  O   . TYR A 40  ? 0.2219 0.2656 0.1553 0.0336  0.0085  -0.0051 40  TYR A O   
317  C  CB  . TYR A 40  ? 0.2057 0.3000 0.1943 -0.0313 0.0262  0.0103  40  TYR A CB  
318  C  CG  . TYR A 40  ? 0.2399 0.3276 0.2078 0.0036  0.0537  0.0246  40  TYR A CG  
319  C  CD1 . TYR A 40  ? 0.2172 0.2499 0.2797 -0.0063 -0.0161 0.0276  40  TYR A CD1 
320  C  CD2 . TYR A 40  ? 0.3191 0.4064 0.2675 0.0280  0.0413  -0.0015 40  TYR A CD2 
321  C  CE1 . TYR A 40  ? 0.2594 0.3500 0.2859 0.0367  0.0375  -0.0103 40  TYR A CE1 
322  C  CE2 . TYR A 40  ? 0.2748 0.4083 0.2755 0.0138  0.0266  0.0046  40  TYR A CE2 
323  C  CZ  . TYR A 40  ? 0.2384 0.3935 0.2968 0.0212  0.0205  0.0155  40  TYR A CZ  
324  O  OH  . TYR A 40  ? 0.2838 0.4292 0.3314 0.0483  0.0139  0.0069  40  TYR A OH  
325  N  N   . ASP A 41  ? 0.2257 0.1980 0.1845 0.0400  0.0191  0.0084  41  ASP A N   
326  C  CA  . ASP A 41  ? 0.2464 0.2355 0.1995 0.0355  0.0025  -0.0027 41  ASP A CA  
327  C  C   . ASP A 41  ? 0.2872 0.2828 0.2328 0.0512  0.0150  0.0012  41  ASP A C   
328  O  O   . ASP A 41  ? 0.2810 0.2888 0.2070 0.0753  0.0133  0.0216  41  ASP A O   
329  C  CB  . ASP A 41  ? 0.2671 0.2380 0.2386 0.0185  -0.0120 -0.0082 41  ASP A CB  
330  C  CG  . ASP A 41  ? 0.3208 0.2611 0.2899 0.0089  -0.0002 -0.0094 41  ASP A CG  
331  O  OD1 . ASP A 41  ? 0.3341 0.2784 0.2640 0.0439  -0.0418 -0.0452 41  ASP A OD1 
332  O  OD2 . ASP A 41  ? 0.3887 0.3248 0.3924 -0.0262 0.0134  -0.0227 41  ASP A OD2 
333  N  N   . PRO A 42  ? 0.2981 0.3425 0.2558 0.0646  0.0185  0.0072  42  PRO A N   
334  C  CA  . PRO A 42  ? 0.3105 0.3642 0.2633 0.0548  0.0226  0.0003  42  PRO A CA  
335  C  C   . PRO A 42  ? 0.3304 0.3673 0.2694 0.0472  0.0227  -0.0014 42  PRO A C   
336  O  O   . PRO A 42  ? 0.3345 0.3950 0.2645 0.0842  0.0190  0.0085  42  PRO A O   
337  C  CB  . PRO A 42  ? 0.3289 0.3913 0.2700 0.0415  0.0339  0.0105  42  PRO A CB  
338  C  CG  . PRO A 42  ? 0.2934 0.3723 0.2702 0.0522  0.0409  -0.0141 42  PRO A CG  
339  C  CD  . PRO A 42  ? 0.3308 0.3446 0.2478 0.0613  0.0362  -0.0054 42  PRO A CD  
340  N  N   . SER A 43  ? 0.3432 0.3385 0.2614 0.0478  0.0198  -0.0165 43  SER A N   
341  C  CA  . SER A 43  ? 0.3623 0.3164 0.2967 0.0390  0.0044  -0.0037 43  SER A CA  
342  C  C   . SER A 43  ? 0.3475 0.2747 0.2790 0.0399  0.0105  0.0007  43  SER A C   
343  O  O   . SER A 43  ? 0.3940 0.2846 0.3028 0.0418  0.0056  0.0138  43  SER A O   
344  C  CB  . SER A 43  ? 0.3785 0.3558 0.3334 0.0315  0.0034  -0.0170 43  SER A CB  
345  O  OG  . SER A 43  ? 0.3775 0.2978 0.3482 -0.0057 -0.0052 -0.0456 43  SER A OG  
346  N  N   . LEU A 44  ? 0.3200 0.2638 0.2535 0.0437  0.0010  0.0000  44  LEU A N   
347  C  CA  . LEU A 44  ? 0.2694 0.2298 0.2348 0.0315  -0.0025 0.0121  44  LEU A CA  
348  C  C   . LEU A 44  ? 0.2702 0.2591 0.2735 0.0172  -0.0040 0.0127  44  LEU A C   
349  O  O   . LEU A 44  ? 0.2576 0.2878 0.3035 0.0178  0.0000  0.0534  44  LEU A O   
350  C  CB  . LEU A 44  ? 0.2705 0.2399 0.2248 0.0169  0.0062  0.0024  44  LEU A CB  
351  C  CG  . LEU A 44  ? 0.2401 0.1822 0.2112 0.0208  0.0065  0.0296  44  LEU A CG  
352  C  CD1 . LEU A 44  ? 0.1928 0.2383 0.1943 0.0533  0.0179  -0.0235 44  LEU A CD1 
353  C  CD2 . LEU A 44  ? 0.2247 0.2248 0.2340 -0.0287 -0.0119 0.0185  44  LEU A CD2 
354  N  N   . LYS A 45  ? 0.2479 0.2364 0.2594 0.0193  -0.0337 0.0197  45  LYS A N   
355  C  CA  . LYS A 45  ? 0.2385 0.2566 0.2504 0.0080  -0.0214 -0.0072 45  LYS A CA  
356  C  C   . LYS A 45  ? 0.2005 0.2239 0.2581 0.0141  -0.0228 -0.0048 45  LYS A C   
357  O  O   . LYS A 45  ? 0.1957 0.2462 0.2511 0.0021  -0.0184 -0.0117 45  LYS A O   
358  C  CB  . LYS A 45  ? 0.2606 0.2488 0.2583 0.0204  -0.0261 -0.0032 45  LYS A CB  
359  C  CG  . LYS A 45  ? 0.3181 0.3062 0.2870 -0.0011 -0.0280 -0.0248 45  LYS A CG  
360  C  CD  . LYS A 45  ? 0.4034 0.3720 0.4004 -0.0032 -0.0078 -0.0098 45  LYS A CD  
361  C  CE  . LYS A 45  ? 0.4819 0.5032 0.4996 0.0072  -0.0297 -0.0012 45  LYS A CE  
362  N  NZ  . LYS A 45  ? 0.5402 0.5423 0.5116 0.0021  -0.0208 0.0162  45  LYS A NZ  
363  N  N   . PRO A 46  ? 0.1592 0.2060 0.2457 -0.0183 -0.0003 -0.0168 46  PRO A N   
364  C  CA  . PRO A 46  ? 0.1530 0.2243 0.2516 -0.0145 -0.0102 -0.0103 46  PRO A CA  
365  C  C   . PRO A 46  ? 0.1455 0.2094 0.2426 -0.0098 -0.0071 -0.0085 46  PRO A C   
366  O  O   . PRO A 46  ? 0.1240 0.1915 0.2562 -0.0238 -0.0169 -0.0160 46  PRO A O   
367  C  CB  . PRO A 46  ? 0.1179 0.2204 0.2479 -0.0322 -0.0176 -0.0320 46  PRO A CB  
368  C  CG  . PRO A 46  ? 0.1304 0.2431 0.2962 -0.0191 0.0030  -0.0184 46  PRO A CG  
369  C  CD  . PRO A 46  ? 0.1704 0.2405 0.2831 0.0247  -0.0093 -0.0257 46  PRO A CD  
370  N  N   . LEU A 47  ? 0.1191 0.2265 0.2506 0.0260  -0.0157 0.0036  47  LEU A N   
371  C  CA  . LEU A 47  ? 0.1069 0.1922 0.2449 0.0029  -0.0198 0.0135  47  LEU A CA  
372  C  C   . LEU A 47  ? 0.0888 0.1924 0.2605 -0.0139 -0.0317 0.0098  47  LEU A C   
373  O  O   . LEU A 47  ? 0.1041 0.2710 0.2963 -0.0360 -0.0519 0.0315  47  LEU A O   
374  C  CB  . LEU A 47  ? 0.1357 0.2168 0.2520 -0.0127 0.0076  -0.0088 47  LEU A CB  
375  C  CG  . LEU A 47  ? 0.2289 0.2395 0.2904 0.0063  -0.0020 -0.0215 47  LEU A CG  
376  C  CD1 . LEU A 47  ? 0.2024 0.2565 0.2968 -0.0060 -0.0351 -0.0543 47  LEU A CD1 
377  C  CD2 . LEU A 47  ? 0.1851 0.2324 0.3293 0.0313  -0.0313 -0.0405 47  LEU A CD2 
378  N  N   . SER A 48  ? 0.1030 0.1657 0.2213 -0.0152 -0.0234 0.0211  48  SER A N   
379  C  CA  . SER A 48  ? 0.1383 0.1762 0.2194 -0.0204 -0.0034 0.0128  48  SER A CA  
380  C  C   . SER A 48  ? 0.1433 0.1730 0.2118 -0.0222 -0.0002 0.0083  48  SER A C   
381  O  O   . SER A 48  ? 0.1383 0.1696 0.1999 -0.0429 0.0152  -0.0238 48  SER A O   
382  C  CB  . SER A 48  ? 0.1533 0.1784 0.2414 -0.0110 -0.0011 0.0241  48  SER A CB  
383  O  OG  . SER A 48  ? 0.2013 0.2387 0.2693 0.0164  0.0064  0.0173  48  SER A OG  
384  N  N   . VAL A 49  ? 0.1623 0.2264 0.2242 -0.0300 -0.0162 0.0058  49  VAL A N   
385  C  CA  . VAL A 49  ? 0.1851 0.2290 0.2203 -0.0456 -0.0199 0.0035  49  VAL A CA  
386  C  C   . VAL A 49  ? 0.1891 0.2609 0.2564 -0.0430 -0.0237 0.0038  49  VAL A C   
387  O  O   . VAL A 49  ? 0.1841 0.3254 0.2513 -0.0952 -0.0186 0.0074  49  VAL A O   
388  C  CB  . VAL A 49  ? 0.2268 0.2532 0.2487 -0.0193 -0.0217 0.0003  49  VAL A CB  
389  C  CG1 . VAL A 49  ? 0.2983 0.2592 0.2926 -0.0550 -0.0121 -0.0178 49  VAL A CG1 
390  C  CG2 . VAL A 49  ? 0.1874 0.1907 0.2702 -0.0360 -0.0394 -0.0092 49  VAL A CG2 
391  N  N   . SER A 50  ? 0.1784 0.2267 0.2152 -0.0409 -0.0145 -0.0050 50  SER A N   
392  C  CA  . SER A 50  ? 0.1929 0.2354 0.2884 -0.0226 -0.0316 -0.0137 50  SER A CA  
393  C  C   . SER A 50  ? 0.1956 0.2374 0.2805 -0.0213 -0.0502 -0.0021 50  SER A C   
394  O  O   . SER A 50  ? 0.1779 0.2278 0.2935 -0.0240 -0.0452 0.0033  50  SER A O   
395  C  CB  . SER A 50  ? 0.2378 0.2411 0.2769 -0.0102 0.0086  -0.0162 50  SER A CB  
396  O  OG  . SER A 50  ? 0.3256 0.3175 0.3461 -0.0134 -0.0153 -0.0403 50  SER A OG  
397  N  N   . TYR A 51  ? 0.1825 0.2234 0.2880 -0.0250 -0.0608 -0.0127 51  TYR A N   
398  C  CA  . TYR A 51  ? 0.1734 0.2253 0.2597 -0.0182 -0.0681 0.0118  51  TYR A CA  
399  C  C   . TYR A 51  ? 0.1964 0.2267 0.2456 -0.0054 -0.0572 0.0252  51  TYR A C   
400  O  O   . TYR A 51  ? 0.2225 0.2139 0.2498 -0.0039 -0.0692 0.0178  51  TYR A O   
401  C  CB  . TYR A 51  ? 0.1628 0.2061 0.2471 -0.0243 -0.0741 0.0108  51  TYR A CB  
402  C  CG  . TYR A 51  ? 0.1468 0.1815 0.1696 -0.0216 -0.0610 0.0098  51  TYR A CG  
403  C  CD1 . TYR A 51  ? 0.1274 0.1321 0.2272 -0.0288 -0.0579 0.0125  51  TYR A CD1 
404  C  CD2 . TYR A 51  ? 0.1326 0.1387 0.1838 -0.0131 -0.0419 0.0036  51  TYR A CD2 
405  C  CE1 . TYR A 51  ? 0.0755 0.1372 0.2029 -0.0098 -0.0346 0.0254  51  TYR A CE1 
406  C  CE2 . TYR A 51  ? 0.1137 0.1058 0.2024 -0.0336 -0.0505 0.0118  51  TYR A CE2 
407  C  CZ  . TYR A 51  ? 0.0976 0.1182 0.1914 -0.0341 -0.0487 -0.0074 51  TYR A CZ  
408  O  OH  . TYR A 51  ? 0.1196 0.1271 0.2131 -0.0422 -0.0381 -0.0112 51  TYR A OH  
409  N  N   . ASP A 52  ? 0.2175 0.2559 0.2791 -0.0239 -0.0493 0.0340  52  ASP A N   
410  C  CA  . ASP A 52  ? 0.2460 0.2782 0.2900 -0.0022 -0.0437 0.0355  52  ASP A CA  
411  C  C   . ASP A 52  ? 0.2802 0.2768 0.3091 -0.0008 -0.0429 0.0234  52  ASP A C   
412  O  O   . ASP A 52  ? 0.3049 0.3008 0.3099 0.0154  -0.0674 0.0419  52  ASP A O   
413  C  CB  . ASP A 52  ? 0.2678 0.3082 0.3083 -0.0030 -0.0410 0.0208  52  ASP A CB  
414  C  CG  . ASP A 52  ? 0.3489 0.3796 0.3912 0.0067  -0.0202 0.0018  52  ASP A CG  
415  O  OD1 . ASP A 52  ? 0.4382 0.4885 0.4505 -0.0009 -0.0133 0.0208  52  ASP A OD1 
416  O  OD2 . ASP A 52  ? 0.5040 0.4630 0.5084 0.0084  -0.0250 0.0089  52  ASP A OD2 
417  N  N   . GLN A 53  ? 0.2664 0.2702 0.3200 -0.0018 -0.0398 0.0211  53  GLN A N   
418  C  CA  . GLN A 53  ? 0.2467 0.2367 0.3257 -0.0021 -0.0403 0.0144  53  GLN A CA  
419  C  C   . GLN A 53  ? 0.2487 0.1984 0.2734 0.0061  -0.0354 0.0089  53  GLN A C   
420  O  O   . GLN A 53  ? 0.2427 0.1992 0.2819 0.0168  -0.0626 0.0269  53  GLN A O   
421  C  CB  . GLN A 53  ? 0.2904 0.2704 0.3587 0.0137  -0.0242 -0.0035 53  GLN A CB  
422  C  CG  . GLN A 53  ? 0.3233 0.3543 0.4280 0.0093  -0.0130 0.0062  53  GLN A CG  
423  C  CD  . GLN A 53  ? 0.4047 0.4770 0.4561 -0.0022 -0.0193 0.0231  53  GLN A CD  
424  O  OE1 . GLN A 53  ? 0.4075 0.5183 0.5204 -0.0069 -0.0083 0.0691  53  GLN A OE1 
425  N  NE2 . GLN A 53  ? 0.4087 0.4305 0.4432 0.0247  -0.0134 0.0625  53  GLN A NE2 
426  N  N   . ALA A 54  ? 0.2333 0.1221 0.2545 -0.0122 -0.0611 0.0128  54  ALA A N   
427  C  CA  . ALA A 54  ? 0.2132 0.1213 0.1938 -0.0203 -0.0589 0.0072  54  ALA A CA  
428  C  C   . ALA A 54  ? 0.2267 0.1413 0.2140 -0.0190 -0.0634 -0.0136 54  ALA A C   
429  O  O   . ALA A 54  ? 0.2766 0.2146 0.2289 -0.0215 -0.1033 -0.0352 54  ALA A O   
430  C  CB  . ALA A 54  ? 0.2241 0.1457 0.2432 -0.0190 -0.0463 -0.0015 54  ALA A CB  
431  N  N   . THR A 55  ? 0.2403 0.1052 0.2007 -0.0173 -0.0595 0.0235  55  THR A N   
432  C  CA  . THR A 55  ? 0.2533 0.1056 0.1905 -0.0108 -0.0593 0.0024  55  THR A CA  
433  C  C   . THR A 55  ? 0.2624 0.1172 0.1651 0.0017  -0.0656 0.0179  55  THR A C   
434  O  O   . THR A 55  ? 0.2722 0.0872 0.1768 0.0083  -0.0668 0.0053  55  THR A O   
435  C  CB  . THR A 55  ? 0.2513 0.1144 0.1982 0.0066  -0.0545 0.0190  55  THR A CB  
436  O  OG1 . THR A 55  ? 0.3242 0.1552 0.2655 0.0191  -0.0712 0.0046  55  THR A OG1 
437  C  CG2 . THR A 55  ? 0.2936 0.1381 0.2225 0.0334  -0.0317 0.0205  55  THR A CG2 
438  N  N   . SER A 56  ? 0.2731 0.0901 0.1384 0.0075  -0.0811 0.0108  56  SER A N   
439  C  CA  . SER A 56  ? 0.3152 0.0993 0.1447 0.0054  -0.0705 -0.0109 56  SER A CA  
440  C  C   . SER A 56  ? 0.3292 0.1089 0.1612 0.0106  -0.0639 -0.0064 56  SER A C   
441  O  O   . SER A 56  ? 0.3600 0.1414 0.1625 0.0257  -0.1081 0.0008  56  SER A O   
442  C  CB  . SER A 56  ? 0.3202 0.1131 0.1746 -0.0191 -0.0909 -0.0087 56  SER A CB  
443  O  OG  . SER A 56  ? 0.3613 0.1132 0.1776 0.0056  -0.0968 0.0072  56  SER A OG  
444  N  N   . LEU A 57  ? 0.3427 0.1037 0.1525 0.0245  -0.0329 0.0132  57  LEU A N   
445  C  CA  . LEU A 57  ? 0.3731 0.1613 0.1674 0.0361  -0.0198 0.0101  57  LEU A CA  
446  C  C   . LEU A 57  ? 0.3723 0.1122 0.1418 0.0310  -0.0219 0.0218  57  LEU A C   
447  O  O   . LEU A 57  ? 0.3903 0.1500 0.1140 0.0282  -0.0505 0.0168  57  LEU A O   
448  C  CB  . LEU A 57  ? 0.3845 0.1663 0.2024 0.0337  -0.0200 0.0193  57  LEU A CB  
449  C  CG  . LEU A 57  ? 0.3869 0.2232 0.2020 0.0280  -0.0276 -0.0393 57  LEU A CG  
450  C  CD1 . LEU A 57  ? 0.4088 0.2527 0.2640 -0.0306 -0.0367 0.0057  57  LEU A CD1 
451  C  CD2 . LEU A 57  ? 0.3927 0.2346 0.2062 0.0213  -0.0113 -0.0250 57  LEU A CD2 
452  N  N   . ARG A 58  ? 0.3442 0.1272 0.1459 0.0551  -0.0321 0.0216  58  ARG A N   
453  C  CA  . ARG A 58  ? 0.3375 0.1245 0.1550 0.0311  -0.0145 0.0489  58  ARG A CA  
454  C  C   . ARG A 58  ? 0.3189 0.1140 0.1271 0.0186  -0.0257 0.0319  58  ARG A C   
455  O  O   . ARG A 58  ? 0.3228 0.1114 0.1191 0.0029  -0.0025 0.0280  58  ARG A O   
456  C  CB  . ARG A 58  ? 0.3169 0.1547 0.1767 0.0243  -0.0440 0.0021  58  ARG A CB  
457  C  CG  . ARG A 58  ? 0.3017 0.1788 0.2151 -0.0091 -0.0363 0.0310  58  ARG A CG  
458  C  CD  . ARG A 58  ? 0.3032 0.2839 0.2999 -0.0483 -0.0568 -0.0172 58  ARG A CD  
459  N  NE  . ARG A 58  ? 0.2326 0.2547 0.2670 -0.0178 -0.0341 0.0298  58  ARG A NE  
460  C  CZ  . ARG A 58  ? 0.2407 0.2688 0.2445 -0.0535 -0.0133 0.0450  58  ARG A CZ  
461  N  NH1 . ARG A 58  ? 0.2368 0.2689 0.2620 -0.0385 0.0342  -0.0254 58  ARG A NH1 
462  N  NH2 . ARG A 58  ? 0.1876 0.2286 0.2756 -0.0061 -0.0035 -0.0005 58  ARG A NH2 
463  N  N   . ILE A 59  ? 0.3388 0.0894 0.1287 0.0081  -0.0349 0.0087  59  ILE A N   
464  C  CA  . ILE A 59  ? 0.2952 0.0781 0.1338 -0.0046 -0.0306 -0.0014 59  ILE A CA  
465  C  C   . ILE A 59  ? 0.2814 0.0880 0.1203 -0.0164 -0.0293 0.0013  59  ILE A C   
466  O  O   . ILE A 59  ? 0.3185 0.1415 0.0825 -0.0144 -0.0154 0.0118  59  ILE A O   
467  C  CB  . ILE A 59  ? 0.3133 0.0880 0.1255 -0.0149 -0.0418 -0.0064 59  ILE A CB  
468  C  CG1 . ILE A 59  ? 0.2776 0.0851 0.1122 -0.0158 -0.0205 0.0721  59  ILE A CG1 
469  C  CG2 . ILE A 59  ? 0.3243 0.1132 0.0713 0.0119  -0.0722 -0.0206 59  ILE A CG2 
470  C  CD1 . ILE A 59  ? 0.2808 0.0880 0.1720 -0.0144 -0.0234 0.0024  59  ILE A CD1 
471  N  N   . LEU A 60  ? 0.2790 0.1339 0.1091 -0.0422 -0.0408 0.0167  60  LEU A N   
472  C  CA  . LEU A 60  ? 0.2603 0.1360 0.1502 -0.0397 -0.0311 0.0238  60  LEU A CA  
473  C  C   . LEU A 60  ? 0.2348 0.1277 0.1697 -0.0692 -0.0122 0.0065  60  LEU A C   
474  O  O   . LEU A 60  ? 0.2289 0.1366 0.1117 -0.0560 -0.0030 0.0209  60  LEU A O   
475  C  CB  . LEU A 60  ? 0.2797 0.1088 0.2089 -0.0574 -0.0136 0.0293  60  LEU A CB  
476  C  CG  . LEU A 60  ? 0.2766 0.1619 0.2031 -0.0128 -0.0541 0.0151  60  LEU A CG  
477  C  CD1 . LEU A 60  ? 0.3500 0.1544 0.2502 -0.0516 -0.0191 0.0184  60  LEU A CD1 
478  C  CD2 . LEU A 60  ? 0.2636 0.1112 0.2205 -0.0454 -0.0237 0.0105  60  LEU A CD2 
479  N  N   . ASN A 61  ? 0.2225 0.1216 0.1281 -0.0708 0.0051  -0.0121 61  ASN A N   
480  C  CA  . ASN A 61  ? 0.2353 0.1354 0.1354 -0.0687 0.0226  -0.0075 61  ASN A CA  
481  C  C   . ASN A 61  ? 0.2676 0.1641 0.1469 -0.0621 0.0257  -0.0182 61  ASN A C   
482  O  O   . ASN A 61  ? 0.3336 0.1912 0.1473 -0.0537 0.0404  0.0069  61  ASN A O   
483  C  CB  . ASN A 61  ? 0.2439 0.1458 0.1360 -0.0452 0.0152  -0.0302 61  ASN A CB  
484  C  CG  . ASN A 61  ? 0.2640 0.1597 0.0912 -0.0493 0.0231  -0.0082 61  ASN A CG  
485  O  OD1 . ASN A 61  ? 0.3061 0.1305 0.1432 -0.0659 -0.0070 -0.0017 61  ASN A OD1 
486  N  ND2 . ASN A 61  ? 0.2947 0.1572 0.1518 -0.0675 0.0346  -0.0117 61  ASN A ND2 
487  N  N   . ASN A 62  ? 0.2595 0.1323 0.1215 -0.0667 0.0104  0.0023  62  ASN A N   
488  C  CA  . ASN A 62  ? 0.2568 0.1633 0.1209 -0.0737 0.0141  -0.0103 62  ASN A CA  
489  C  C   . ASN A 62  ? 0.2391 0.1865 0.1641 -0.0710 0.0298  -0.0077 62  ASN A C   
490  O  O   . ASN A 62  ? 0.2786 0.2347 0.2271 -0.0967 0.0189  -0.0193 62  ASN A O   
491  C  CB  . ASN A 62  ? 0.2731 0.1537 0.1522 -0.0724 0.0346  -0.0043 62  ASN A CB  
492  C  CG  . ASN A 62  ? 0.3051 0.1922 0.1090 -0.0679 0.0219  -0.0051 62  ASN A CG  
493  O  OD1 . ASN A 62  ? 0.2593 0.1665 0.1236 -0.0896 0.0071  0.0315  62  ASN A OD1 
494  N  ND2 . ASN A 62  ? 0.3723 0.2123 0.1776 -0.0286 0.0505  0.0259  62  ASN A ND2 
495  N  N   . GLY A 63  ? 0.2366 0.1580 0.1901 -0.0870 0.0338  0.0064  63  GLY A N   
496  C  CA  . GLY A 63  ? 0.2178 0.1381 0.1560 -0.0622 0.0411  0.0059  63  GLY A CA  
497  C  C   . GLY A 63  ? 0.2119 0.1602 0.1656 -0.0475 0.0096  -0.0111 63  GLY A C   
498  O  O   . GLY A 63  ? 0.2114 0.1682 0.1748 -0.0592 0.0106  -0.0070 63  GLY A O   
499  N  N   A HIS A 64  ? 0.1861 0.1426 0.1557 -0.0404 0.0227  -0.0038 64  HIS A N   
500  N  N   B HIS A 64  ? 0.1804 0.1555 0.1628 -0.0444 0.0192  -0.0045 64  HIS A N   
501  C  CA  A HIS A 64  ? 0.1927 0.1576 0.1599 -0.0273 0.0110  -0.0032 64  HIS A CA  
502  C  CA  B HIS A 64  ? 0.1839 0.1709 0.1652 -0.0347 0.0040  -0.0050 64  HIS A CA  
503  C  C   A HIS A 64  ? 0.1769 0.1161 0.1374 -0.0319 0.0092  -0.0032 64  HIS A C   
504  C  C   B HIS A 64  ? 0.1677 0.1329 0.1433 -0.0416 0.0000  -0.0026 64  HIS A C   
505  O  O   A HIS A 64  ? 0.1745 0.1082 0.1402 -0.0250 0.0230  -0.0044 64  HIS A O   
506  O  O   B HIS A 64  ? 0.1507 0.1455 0.1408 -0.0657 -0.0048 0.0087  64  HIS A O   
507  C  CB  A HIS A 64  ? 0.1715 0.1332 0.1720 -0.0353 -0.0079 0.0048  64  HIS A CB  
508  C  CB  B HIS A 64  ? 0.1540 0.1610 0.1839 -0.0431 -0.0073 -0.0082 64  HIS A CB  
509  C  CG  A HIS A 64  ? 0.1920 0.1973 0.1649 -0.0199 0.0127  0.0088  64  HIS A CG  
510  C  CG  B HIS A 64  ? 0.1788 0.1835 0.1588 -0.0174 -0.0115 -0.0081 64  HIS A CG  
511  N  ND1 A HIS A 64  ? 0.2191 0.2182 0.1825 -0.0204 -0.0181 -0.0173 64  HIS A ND1 
512  N  ND1 B HIS A 64  ? 0.2240 0.1981 0.1975 -0.0092 -0.0564 0.0023  64  HIS A ND1 
513  C  CD2 A HIS A 64  ? 0.2366 0.2103 0.1864 -0.0302 -0.0046 0.0073  64  HIS A CD2 
514  C  CD2 B HIS A 64  ? 0.1569 0.1073 0.2176 -0.0015 -0.0317 -0.0238 64  HIS A CD2 
515  C  CE1 A HIS A 64  ? 0.2274 0.2401 0.2155 -0.0415 0.0018  0.0130  64  HIS A CE1 
516  C  CE1 B HIS A 64  ? 0.2301 0.2013 0.1802 0.0169  -0.0238 -0.0278 64  HIS A CE1 
517  N  NE2 A HIS A 64  ? 0.1656 0.1974 0.2370 -0.0386 0.0239  0.0089  64  HIS A NE2 
518  N  NE2 B HIS A 64  ? 0.2168 0.2003 0.2394 0.0149  -0.0228 -0.0302 64  HIS A NE2 
519  N  N   . ALA A 65  ? 0.1756 0.1253 0.1387 -0.0397 0.0125  -0.0060 65  ALA A N   
520  C  CA  . ALA A 65  ? 0.1794 0.1229 0.1217 -0.0370 0.0023  0.0008  65  ALA A CA  
521  C  C   . ALA A 65  ? 0.1981 0.1196 0.1027 -0.0439 -0.0035 -0.0065 65  ALA A C   
522  O  O   . ALA A 65  ? 0.2015 0.1495 0.1282 -0.0605 0.0243  0.0067  65  ALA A O   
523  C  CB  . ALA A 65  ? 0.1651 0.1321 0.1161 -0.0546 0.0066  0.0108  65  ALA A CB  
524  N  N   . PHE A 66  ? 0.1778 0.1238 0.1097 -0.0409 -0.0120 -0.0052 66  PHE A N   
525  C  CA  . PHE A 66  ? 0.2005 0.1234 0.1162 -0.0297 -0.0076 -0.0049 66  PHE A CA  
526  C  C   . PHE A 66  ? 0.2366 0.1112 0.0846 -0.0298 -0.0170 -0.0058 66  PHE A C   
527  O  O   . PHE A 66  ? 0.2378 0.0766 0.0969 -0.0339 -0.0079 0.0047  66  PHE A O   
528  C  CB  . PHE A 66  ? 0.1935 0.1237 0.1066 -0.0434 -0.0125 0.0096  66  PHE A CB  
529  C  CG  . PHE A 66  ? 0.1863 0.1007 0.0974 -0.0251 -0.0020 0.0103  66  PHE A CG  
530  C  CD1 . PHE A 66  ? 0.2047 0.1202 0.0864 -0.0046 -0.0288 -0.0067 66  PHE A CD1 
531  C  CD2 . PHE A 66  ? 0.2473 0.0751 0.1010 -0.0232 -0.0338 0.0099  66  PHE A CD2 
532  C  CE1 . PHE A 66  ? 0.2267 0.1238 0.1190 -0.0214 -0.0256 -0.0271 66  PHE A CE1 
533  C  CE2 . PHE A 66  ? 0.2262 0.0813 0.1429 -0.0303 -0.0408 0.0070  66  PHE A CE2 
534  C  CZ  . PHE A 66  ? 0.1923 0.0761 0.1288 -0.0342 -0.0534 -0.0212 66  PHE A CZ  
535  N  N   . ASN A 67  ? 0.2351 0.0987 0.0975 -0.0298 -0.0264 0.0171  67  ASN A N   
536  C  CA  . ASN A 67  ? 0.2638 0.0970 0.0926 -0.0299 -0.0386 -0.0052 67  ASN A CA  
537  C  C   . ASN A 67  ? 0.2321 0.0837 0.1322 -0.0282 -0.0270 0.0092  67  ASN A C   
538  O  O   . ASN A 67  ? 0.2636 0.1687 0.1023 -0.0396 -0.0124 0.0146  67  ASN A O   
539  C  CB  . ASN A 67  ? 0.2254 0.0846 0.1187 -0.0576 -0.0452 0.0101  67  ASN A CB  
540  C  CG  . ASN A 67  ? 0.2617 0.1478 0.1341 -0.0298 -0.0282 0.0197  67  ASN A CG  
541  O  OD1 . ASN A 67  ? 0.2379 0.1313 0.1199 -0.0604 -0.0613 0.0476  67  ASN A OD1 
542  N  ND2 . ASN A 67  ? 0.2681 0.1915 0.2359 -0.0704 -0.0508 -0.0202 67  ASN A ND2 
543  N  N   . VAL A 68  ? 0.2421 0.0706 0.1244 0.0001  -0.0296 0.0012  68  VAL A N   
544  C  CA  . VAL A 68  ? 0.2389 0.0846 0.1019 0.0240  -0.0528 -0.0010 68  VAL A CA  
545  C  C   . VAL A 68  ? 0.2889 0.0935 0.1161 0.0134  -0.0428 0.0021  68  VAL A C   
546  O  O   . VAL A 68  ? 0.3141 0.0747 0.0986 0.0211  -0.0564 0.0018  68  VAL A O   
547  C  CB  . VAL A 68  ? 0.2357 0.1036 0.1407 0.0314  -0.0554 0.0055  68  VAL A CB  
548  C  CG1 . VAL A 68  ? 0.2476 0.1358 0.1369 0.0542  -0.0806 -0.0010 68  VAL A CG1 
549  C  CG2 . VAL A 68  ? 0.2192 0.1018 0.1108 0.0353  -0.0612 -0.0165 68  VAL A CG2 
550  N  N   . GLU A 69  ? 0.3021 0.0841 0.1074 0.0093  -0.0496 0.0071  69  GLU A N   
551  C  CA  . GLU A 69  ? 0.2704 0.0994 0.1482 0.0022  -0.0266 0.0005  69  GLU A CA  
552  C  C   . GLU A 69  ? 0.3211 0.0853 0.1644 0.0344  -0.0464 0.0176  69  GLU A C   
553  O  O   . GLU A 69  ? 0.4018 0.0769 0.1831 0.0508  -0.0681 0.0121  69  GLU A O   
554  C  CB  . GLU A 69  ? 0.2907 0.1448 0.1965 0.0116  -0.0161 0.0041  69  GLU A CB  
555  C  CG  . GLU A 69  ? 0.2494 0.1774 0.1972 -0.0054 -0.0013 0.0262  69  GLU A CG  
556  C  CD  . GLU A 69  ? 0.2892 0.1867 0.2591 0.0071  -0.0028 0.0451  69  GLU A CD  
557  O  OE1 . GLU A 69  ? 0.2991 0.1702 0.2263 -0.0115 0.0187  0.0410  69  GLU A OE1 
558  O  OE2 . GLU A 69  ? 0.2736 0.2208 0.3353 0.0535  0.0204  0.0937  69  GLU A OE2 
559  N  N   . PHE A 70  ? 0.3028 0.0607 0.1192 -0.0043 -0.0389 0.0200  70  PHE A N   
560  C  CA  . PHE A 70  ? 0.2581 0.0595 0.1364 0.0093  -0.0572 0.0185  70  PHE A CA  
561  C  C   . PHE A 70  ? 0.2508 0.0756 0.1452 -0.0057 -0.0521 -0.0010 70  PHE A C   
562  O  O   . PHE A 70  ? 0.2714 0.0702 0.1541 -0.0112 -0.0673 -0.0036 70  PHE A O   
563  C  CB  . PHE A 70  ? 0.2382 0.0643 0.1353 -0.0100 -0.0418 0.0095  70  PHE A CB  
564  C  CG  . PHE A 70  ? 0.1783 0.0674 0.1426 0.0069  -0.0867 0.0366  70  PHE A CG  
565  C  CD1 . PHE A 70  ? 0.1950 0.0575 0.1797 0.0069  -0.0614 0.0428  70  PHE A CD1 
566  C  CD2 . PHE A 70  ? 0.1741 0.1193 0.1566 -0.0002 -0.0551 0.0070  70  PHE A CD2 
567  C  CE1 . PHE A 70  ? 0.2395 0.0741 0.1230 -0.0029 -0.0192 0.0190  70  PHE A CE1 
568  C  CE2 . PHE A 70  ? 0.2006 0.0981 0.1148 0.0324  -0.0881 0.0318  70  PHE A CE2 
569  C  CZ  . PHE A 70  ? 0.2487 0.0805 0.1455 0.0114  -0.0527 0.0289  70  PHE A CZ  
570  N  N   . ASP A 71  ? 0.2789 0.0694 0.1769 -0.0052 -0.0574 0.0171  71  ASP A N   
571  C  CA  . ASP A 71  ? 0.2574 0.0848 0.1953 0.0013  -0.0433 0.0114  71  ASP A CA  
572  C  C   . ASP A 71  ? 0.2500 0.0737 0.2194 -0.0144 -0.0547 0.0047  71  ASP A C   
573  O  O   . ASP A 71  ? 0.2655 0.1156 0.2775 -0.0333 -0.0335 -0.0204 71  ASP A O   
574  C  CB  . ASP A 71  ? 0.2466 0.1073 0.2089 0.0254  -0.0722 0.0027  71  ASP A CB  
575  C  CG  . ASP A 71  ? 0.3002 0.1373 0.2926 -0.0014 -0.0695 0.0118  71  ASP A CG  
576  O  OD1 . ASP A 71  ? 0.2979 0.1047 0.2775 0.0008  -0.1078 0.0632  71  ASP A OD1 
577  O  OD2 . ASP A 71  ? 0.3081 0.2137 0.3689 -0.0255 -0.1002 0.0313  71  ASP A OD2 
578  N  N   . ASP A 72  ? 0.2427 0.0550 0.1963 -0.0101 -0.0732 0.0207  72  ASP A N   
579  C  CA  . ASP A 72  ? 0.2163 0.0706 0.2085 -0.0089 -0.0443 0.0105  72  ASP A CA  
580  C  C   . ASP A 72  ? 0.2114 0.0804 0.2160 -0.0039 -0.0553 -0.0075 72  ASP A C   
581  O  O   . ASP A 72  ? 0.2799 0.0634 0.2229 -0.0107 -0.0767 -0.0105 72  ASP A O   
582  C  CB  . ASP A 72  ? 0.2011 0.0813 0.1937 0.0028  -0.0430 0.0161  72  ASP A CB  
583  C  CG  . ASP A 72  ? 0.2238 0.0919 0.1940 0.0074  -0.0336 0.0026  72  ASP A CG  
584  O  OD1 . ASP A 72  ? 0.2232 0.1881 0.1774 -0.0307 -0.0262 0.0569  72  ASP A OD1 
585  O  OD2 . ASP A 72  ? 0.2017 0.1546 0.1813 -0.0014 -0.0576 0.0088  72  ASP A OD2 
586  N  N   . SER A 73  ? 0.2482 0.0466 0.2449 -0.0124 -0.0477 0.0128  73  SER A N   
587  C  CA  . SER A 73  ? 0.2307 0.0908 0.2120 -0.0027 -0.0553 -0.0046 73  SER A CA  
588  C  C   . SER A 73  ? 0.2670 0.1592 0.2650 0.0015  -0.0400 -0.0097 73  SER A C   
589  O  O   . SER A 73  ? 0.2865 0.1366 0.3204 -0.0197 -0.0462 0.0062  73  SER A O   
590  C  CB  . SER A 73  ? 0.2749 0.1421 0.2289 -0.0175 -0.0402 0.0102  73  SER A CB  
591  O  OG  . SER A 73  ? 0.2576 0.1196 0.2233 0.0230  -0.0475 0.0313  73  SER A OG  
592  N  N   . GLN A 74  ? 0.2580 0.1695 0.2732 -0.0097 -0.0421 -0.0124 74  GLN A N   
593  C  CA  . GLN A 74  ? 0.2779 0.2322 0.2945 -0.0042 -0.0409 -0.0126 74  GLN A CA  
594  C  C   . GLN A 74  ? 0.2520 0.2363 0.2939 -0.0026 -0.0499 -0.0166 74  GLN A C   
595  O  O   . GLN A 74  ? 0.2192 0.1935 0.2757 -0.0344 -0.0473 -0.0102 74  GLN A O   
596  C  CB  . GLN A 74  ? 0.3038 0.2356 0.3356 0.0208  -0.0387 -0.0087 74  GLN A CB  
597  C  CG  . GLN A 74  ? 0.3054 0.3107 0.3395 0.0071  -0.0285 0.0123  74  GLN A CG  
598  C  CD  . GLN A 74  ? 0.3519 0.3646 0.3729 0.0056  -0.0359 0.0223  74  GLN A CD  
599  O  OE1 . GLN A 74  ? 0.3898 0.4161 0.4294 0.0325  -0.0364 0.0377  74  GLN A OE1 
600  N  NE2 . GLN A 74  ? 0.3633 0.2249 0.3552 0.0036  -0.0427 0.0154  74  GLN A NE2 
601  N  N   . ASP A 75  ? 0.2658 0.2716 0.2972 -0.0013 -0.0501 -0.0255 75  ASP A N   
602  C  CA  . ASP A 75  ? 0.2915 0.2948 0.3195 0.0033  -0.0385 -0.0250 75  ASP A CA  
603  C  C   . ASP A 75  ? 0.3031 0.2962 0.3308 0.0111  -0.0561 -0.0246 75  ASP A C   
604  O  O   . ASP A 75  ? 0.3372 0.3302 0.3959 0.0109  -0.0450 -0.0206 75  ASP A O   
605  C  CB  . ASP A 75  ? 0.3400 0.3262 0.3466 0.0082  -0.0407 -0.0294 75  ASP A CB  
606  C  CG  . ASP A 75  ? 0.3688 0.3691 0.3123 0.0134  -0.0204 -0.0268 75  ASP A CG  
607  O  OD1 . ASP A 75  ? 0.3899 0.4511 0.3259 0.0114  -0.0469 -0.0668 75  ASP A OD1 
608  O  OD2 . ASP A 75  ? 0.4628 0.4269 0.4027 0.0298  0.0250  -0.0539 75  ASP A OD2 
609  N  N   . LYS A 76  ? 0.2905 0.2251 0.2929 0.0223  -0.0639 0.0220  76  LYS A N   
610  C  CA  . LYS A 76  ? 0.2887 0.2134 0.3132 -0.0090 -0.0447 0.0165  76  LYS A CA  
611  C  C   . LYS A 76  ? 0.2697 0.2241 0.3167 -0.0030 -0.0491 0.0354  76  LYS A C   
612  O  O   . LYS A 76  ? 0.3213 0.2336 0.3662 -0.0093 -0.0675 0.0237  76  LYS A O   
613  C  CB  . LYS A 76  ? 0.3094 0.2123 0.2897 -0.0111 -0.0627 0.0241  76  LYS A CB  
614  C  CG  . LYS A 76  ? 0.3949 0.2646 0.3233 -0.0006 -0.0215 0.0379  76  LYS A CG  
615  C  CD  . LYS A 76  ? 0.3516 0.2579 0.3289 -0.0110 -0.0244 0.0141  76  LYS A CD  
616  C  CE  . LYS A 76  ? 0.3547 0.2791 0.3293 0.0226  -0.0215 0.0225  76  LYS A CE  
617  N  NZ  . LYS A 76  ? 0.3477 0.2567 0.3326 0.0123  -0.0222 0.0058  76  LYS A NZ  
618  N  N   . ALA A 77  ? 0.2298 0.2199 0.2697 0.0055  -0.0692 0.0474  77  ALA A N   
619  C  CA  . ALA A 77  ? 0.2131 0.1931 0.2223 0.0005  -0.0558 0.0236  77  ALA A CA  
620  C  C   . ALA A 77  ? 0.1909 0.1679 0.2190 -0.0265 -0.0490 0.0080  77  ALA A C   
621  O  O   . ALA A 77  ? 0.1826 0.2043 0.2377 -0.0372 -0.0625 -0.0151 77  ALA A O   
622  C  CB  . ALA A 77  ? 0.2409 0.2283 0.2324 0.0080  -0.0595 0.0095  77  ALA A CB  
623  N  N   . VAL A 78  ? 0.1741 0.1220 0.1646 -0.0224 -0.0562 0.0108  78  VAL A N   
624  C  CA  . VAL A 78  ? 0.1736 0.1272 0.1891 -0.0138 -0.0523 0.0195  78  VAL A CA  
625  C  C   . VAL A 78  ? 0.1437 0.1428 0.1737 -0.0184 -0.0385 0.0047  78  VAL A C   
626  O  O   . VAL A 78  ? 0.1444 0.1566 0.2135 -0.0237 -0.0698 0.0179  78  VAL A O   
627  C  CB  . VAL A 78  ? 0.2019 0.1857 0.2085 0.0040  -0.0458 0.0151  78  VAL A CB  
628  C  CG1 . VAL A 78  ? 0.2324 0.1371 0.2681 0.0249  -0.0535 0.0134  78  VAL A CG1 
629  C  CG2 . VAL A 78  ? 0.2053 0.1876 0.2678 0.0156  0.0070  -0.0011 78  VAL A CG2 
630  N  N   . LEU A 79  ? 0.1732 0.1058 0.1542 0.0008  -0.0533 0.0010  79  LEU A N   
631  C  CA  . LEU A 79  ? 0.1361 0.1286 0.1813 -0.0078 -0.0257 -0.0001 79  LEU A CA  
632  C  C   . LEU A 79  ? 0.1562 0.1073 0.1742 0.0036  -0.0122 0.0013  79  LEU A C   
633  O  O   . LEU A 79  ? 0.1567 0.1519 0.1809 -0.0446 -0.0082 -0.0267 79  LEU A O   
634  C  CB  . LEU A 79  ? 0.1010 0.1464 0.2288 0.0006  -0.0444 0.0395  79  LEU A CB  
635  C  CG  . LEU A 79  ? 0.1403 0.1624 0.2304 -0.0257 -0.0031 0.0229  79  LEU A CG  
636  C  CD1 . LEU A 79  ? 0.1293 0.1526 0.3283 -0.0293 -0.0033 0.0383  79  LEU A CD1 
637  C  CD2 . LEU A 79  ? 0.1014 0.1683 0.2100 0.0057  -0.0080 0.0246  79  LEU A CD2 
638  N  N   . LYS A 80  ? 0.1208 0.1397 0.1814 -0.0081 -0.0133 -0.0268 80  LYS A N   
639  C  CA  . LYS A 80  ? 0.1898 0.1529 0.2044 0.0133  0.0065  -0.0059 80  LYS A CA  
640  C  C   . LYS A 80  ? 0.1259 0.1592 0.1968 0.0067  0.0228  -0.0081 80  LYS A C   
641  O  O   . LYS A 80  ? 0.1706 0.1341 0.2034 -0.0187 -0.0067 0.0092  80  LYS A O   
642  C  CB  . LYS A 80  ? 0.2390 0.2045 0.2660 0.0313  -0.0092 -0.0041 80  LYS A CB  
643  C  CG  . LYS A 80  ? 0.2320 0.2010 0.3203 0.0278  0.0137  -0.0061 80  LYS A CG  
644  C  CD  . LYS A 80  ? 0.3399 0.2953 0.4457 0.0381  -0.0063 -0.0047 80  LYS A CD  
645  C  CE  . LYS A 80  ? 0.3737 0.4318 0.4533 0.0242  0.0211  -0.0012 80  LYS A CE  
646  N  NZ  . LYS A 80  ? 0.4432 0.5593 0.5673 0.0177  0.0145  -0.0217 80  LYS A NZ  
647  N  N   . GLY A 81  ? 0.1590 0.1554 0.1929 0.0062  -0.0023 -0.0004 81  GLY A N   
648  C  CA  . GLY A 81  ? 0.1532 0.1693 0.2056 -0.0013 0.0223  0.0133  81  GLY A CA  
649  C  C   . GLY A 81  ? 0.1706 0.1594 0.2029 -0.0080 0.0156  0.0263  81  GLY A C   
650  O  O   . GLY A 81  ? 0.1773 0.1511 0.2066 0.0074  0.0255  0.0256  81  GLY A O   
651  N  N   . GLY A 82  ? 0.1923 0.1350 0.2353 -0.0090 0.0053  -0.0105 82  GLY A N   
652  C  CA  . GLY A 82  ? 0.1848 0.1350 0.2288 0.0034  -0.0062 0.0174  82  GLY A CA  
653  C  C   . GLY A 82  ? 0.2043 0.1457 0.2328 0.0146  0.0078  -0.0092 82  GLY A C   
654  O  O   . GLY A 82  ? 0.2271 0.2154 0.2731 0.0444  0.0384  0.0082  82  GLY A O   
655  N  N   . PRO A 83  ? 0.1935 0.1480 0.2441 0.0069  0.0240  0.0013  83  PRO A N   
656  C  CA  . PRO A 83  ? 0.1804 0.1452 0.2117 0.0302  0.0134  -0.0050 83  PRO A CA  
657  C  C   . PRO A 83  ? 0.2035 0.1836 0.2117 0.0093  0.0238  -0.0268 83  PRO A C   
658  O  O   . PRO A 83  ? 0.2199 0.2350 0.2258 -0.0060 0.0012  -0.0324 83  PRO A O   
659  C  CB  . PRO A 83  ? 0.2008 0.1843 0.2336 0.0321  0.0180  -0.0075 83  PRO A CB  
660  C  CG  . PRO A 83  ? 0.1280 0.1595 0.1764 0.0097  0.0047  0.0199  83  PRO A CG  
661  C  CD  . PRO A 83  ? 0.1227 0.1463 0.2220 0.0084  0.0304  -0.0158 83  PRO A CD  
662  N  N   . LEU A 84  ? 0.1842 0.1543 0.1700 0.0214  0.0207  -0.0383 84  LEU A N   
663  C  CA  . LEU A 84  ? 0.1963 0.1246 0.2007 0.0119  0.0062  -0.0509 84  LEU A CA  
664  C  C   . LEU A 84  ? 0.2114 0.1870 0.2494 0.0165  -0.0020 -0.0501 84  LEU A C   
665  O  O   . LEU A 84  ? 0.2236 0.1722 0.2507 -0.0049 0.0388  -0.0654 84  LEU A O   
666  C  CB  . LEU A 84  ? 0.1570 0.1246 0.1760 0.0196  0.0080  -0.0376 84  LEU A CB  
667  C  CG  . LEU A 84  ? 0.1076 0.0784 0.1921 0.0139  0.0108  -0.0300 84  LEU A CG  
668  C  CD1 . LEU A 84  ? 0.1211 0.1668 0.1804 0.0356  -0.0204 -0.0314 84  LEU A CD1 
669  C  CD2 . LEU A 84  ? 0.0748 0.1183 0.1731 0.0079  -0.0345 -0.0377 84  LEU A CD2 
670  N  N   . ASP A 85  ? 0.2392 0.1637 0.2959 0.0151  -0.0089 -0.0508 85  ASP A N   
671  C  CA  . ASP A 85  ? 0.2720 0.1869 0.3314 -0.0120 -0.0110 -0.0466 85  ASP A CA  
672  C  C   . ASP A 85  ? 0.2508 0.1940 0.3411 -0.0028 -0.0051 -0.0377 85  ASP A C   
673  O  O   . ASP A 85  ? 0.2984 0.2520 0.3761 0.0217  -0.0011 -0.0543 85  ASP A O   
674  C  CB  . ASP A 85  ? 0.3169 0.2385 0.3459 0.0025  -0.0152 -0.0457 85  ASP A CB  
675  C  CG  . ASP A 85  ? 0.3904 0.3160 0.4147 0.0063  -0.0055 -0.0315 85  ASP A CG  
676  O  OD1 . ASP A 85  ? 0.4683 0.4548 0.4489 -0.0146 0.0029  -0.0398 85  ASP A OD1 
677  O  OD2 . ASP A 85  ? 0.4365 0.4425 0.4974 0.0152  -0.0154 -0.0164 85  ASP A OD2 
678  N  N   . GLY A 86  ? 0.2635 0.2398 0.3446 -0.0317 -0.0258 -0.0310 86  GLY A N   
679  C  CA  . GLY A 86  ? 0.2712 0.2294 0.2717 -0.0214 -0.0089 -0.0510 86  GLY A CA  
680  C  C   . GLY A 86  ? 0.2811 0.1963 0.2539 -0.0235 0.0028  -0.0447 86  GLY A C   
681  O  O   . GLY A 86  ? 0.3454 0.2232 0.2472 -0.0730 0.0147  -0.0474 86  GLY A O   
682  N  N   . THR A 87  ? 0.1815 0.1905 0.2131 0.0218  0.0277  -0.0469 87  THR A N   
683  C  CA  . THR A 87  ? 0.1724 0.1822 0.2316 0.0328  0.0237  -0.0368 87  THR A CA  
684  C  C   . THR A 87  ? 0.1413 0.1383 0.2292 0.0246  0.0090  -0.0399 87  THR A C   
685  O  O   . THR A 87  ? 0.1237 0.1107 0.2541 0.0192  0.0233  -0.0585 87  THR A O   
686  C  CB  . THR A 87  ? 0.1736 0.2477 0.2431 0.0642  0.0324  -0.0183 87  THR A CB  
687  O  OG1 . THR A 87  ? 0.1945 0.2977 0.3458 0.0448  0.0352  -0.0895 87  THR A OG1 
688  C  CG2 . THR A 87  ? 0.2345 0.2160 0.2617 0.0397  0.0009  0.0140  87  THR A CG2 
689  N  N   . TYR A 88  ? 0.1264 0.1094 0.2081 0.0154  -0.0022 -0.0369 88  TYR A N   
690  C  CA  . TYR A 88  ? 0.1079 0.1056 0.1765 0.0167  -0.0198 -0.0328 88  TYR A CA  
691  C  C   . TYR A 88  ? 0.0981 0.1029 0.1811 0.0113  -0.0381 -0.0042 88  TYR A C   
692  O  O   . TYR A 88  ? 0.1283 0.1598 0.2159 -0.0319 -0.0561 0.0118  88  TYR A O   
693  C  CB  . TYR A 88  ? 0.1116 0.0934 0.1873 0.0030  -0.0515 -0.0160 88  TYR A CB  
694  C  CG  . TYR A 88  ? 0.1000 0.0696 0.1216 0.0017  -0.0291 -0.0165 88  TYR A CG  
695  C  CD1 . TYR A 88  ? 0.1041 0.0745 0.1461 0.0177  -0.0162 -0.0307 88  TYR A CD1 
696  C  CD2 . TYR A 88  ? 0.0465 0.0890 0.1673 -0.0046 -0.0459 -0.0108 88  TYR A CD2 
697  C  CE1 . TYR A 88  ? 0.1427 0.1230 0.1533 0.0173  0.0016  -0.0027 88  TYR A CE1 
698  C  CE2 . TYR A 88  ? 0.1432 0.0879 0.1255 0.0022  -0.0348 -0.0277 88  TYR A CE2 
699  C  CZ  . TYR A 88  ? 0.1387 0.0572 0.1468 0.0053  -0.0432 -0.0277 88  TYR A CZ  
700  O  OH  . TYR A 88  ? 0.1394 0.1105 0.1387 0.0006  -0.0459 -0.0234 88  TYR A OH  
701  N  N   . ARG A 89  ? 0.1138 0.0913 0.1323 0.0348  -0.0144 -0.0216 89  ARG A N   
702  C  CA  . ARG A 89  ? 0.1464 0.0973 0.1510 0.0081  -0.0270 0.0083  89  ARG A CA  
703  C  C   . ARG A 89  ? 0.1033 0.0748 0.1430 0.0177  -0.0198 -0.0107 89  ARG A C   
704  O  O   . ARG A 89  ? 0.1018 0.0599 0.1402 -0.0035 -0.0144 -0.0070 89  ARG A O   
705  C  CB  . ARG A 89  ? 0.1778 0.0589 0.1977 0.0277  -0.0029 -0.0111 89  ARG A CB  
706  C  CG  . ARG A 89  ? 0.1907 0.2098 0.2681 0.0465  -0.0068 0.0303  89  ARG A CG  
707  C  CD  . ARG A 89  ? 0.3357 0.2092 0.3149 0.0525  -0.0334 0.0467  89  ARG A CD  
708  N  NE  . ARG A 89  ? 0.2905 0.3090 0.2811 0.0189  -0.0237 -0.0245 89  ARG A NE  
709  C  CZ  . ARG A 89  ? 0.2998 0.2269 0.3067 0.0499  -0.0322 -0.0168 89  ARG A CZ  
710  N  NH1 . ARG A 89  ? 0.3253 0.2110 0.2461 0.0763  -0.0239 -0.0507 89  ARG A NH1 
711  N  NH2 . ARG A 89  ? 0.2985 0.3225 0.3200 0.0410  0.0072  -0.0883 89  ARG A NH2 
712  N  N   . LEU A 90  ? 0.1206 0.0533 0.1247 0.0029  -0.0291 -0.0097 90  LEU A N   
713  C  CA  . LEU A 90  ? 0.1265 0.0708 0.1291 -0.0109 -0.0270 -0.0214 90  LEU A CA  
714  C  C   . LEU A 90  ? 0.1649 0.0669 0.0989 -0.0038 -0.0287 0.0037  90  LEU A C   
715  O  O   . LEU A 90  ? 0.1728 0.1021 0.1320 0.0285  -0.0157 0.0189  90  LEU A O   
716  C  CB  . LEU A 90  ? 0.1405 0.0610 0.1235 -0.0185 -0.0542 -0.0194 90  LEU A CB  
717  C  CG  . LEU A 90  ? 0.1422 0.0789 0.1012 -0.0026 -0.0646 -0.0066 90  LEU A CG  
718  C  CD1 . LEU A 90  ? 0.1860 0.0765 0.1904 0.0259  -0.0472 0.0007  90  LEU A CD1 
719  C  CD2 . LEU A 90  ? 0.1623 0.0993 0.1582 -0.0109 -0.0883 -0.0203 90  LEU A CD2 
720  N  N   . ILE A 91  ? 0.1478 0.0640 0.1163 -0.0008 -0.0116 0.0155  91  ILE A N   
721  C  CA  . ILE A 91  ? 0.1363 0.0551 0.1294 -0.0127 -0.0116 0.0076  91  ILE A CA  
722  C  C   . ILE A 91  ? 0.1625 0.0579 0.0835 -0.0232 -0.0007 0.0220  91  ILE A C   
723  O  O   . ILE A 91  ? 0.1508 0.0507 0.0932 -0.0148 -0.0221 0.0245  91  ILE A O   
724  C  CB  . ILE A 91  ? 0.1781 0.0578 0.1304 -0.0280 -0.0050 0.0167  91  ILE A CB  
725  C  CG1 . ILE A 91  ? 0.1609 0.1026 0.1286 -0.0403 0.0075  -0.0132 91  ILE A CG1 
726  C  CG2 . ILE A 91  ? 0.1797 0.0716 0.1066 -0.0025 -0.0289 0.0324  91  ILE A CG2 
727  C  CD1 . ILE A 91  ? 0.1768 0.1410 0.1649 -0.0575 -0.0197 -0.0259 91  ILE A CD1 
728  N  N   . GLN A 92  ? 0.1735 0.0337 0.1097 -0.0063 -0.0229 0.0234  92  GLN A N   
729  C  CA  . GLN A 92  ? 0.1714 0.0340 0.1263 -0.0023 0.0007  0.0292  92  GLN A CA  
730  C  C   . GLN A 92  ? 0.1619 0.0315 0.0997 -0.0083 -0.0216 0.0215  92  GLN A C   
731  O  O   . GLN A 92  ? 0.1711 0.0336 0.0850 -0.0095 -0.0225 0.0222  92  GLN A O   
732  C  CB  . GLN A 92  ? 0.1630 0.0749 0.1365 -0.0152 0.0029  0.0160  92  GLN A CB  
733  C  CG  . GLN A 92  ? 0.1887 0.0686 0.1746 0.0232  -0.0315 0.0268  92  GLN A CG  
734  C  CD  . GLN A 92  ? 0.2083 0.0924 0.0825 -0.0262 -0.0393 0.0353  92  GLN A CD  
735  O  OE1 . GLN A 92  ? 0.2047 0.0552 0.1501 -0.0348 0.0027  0.0274  92  GLN A OE1 
736  N  NE2 . GLN A 92  ? 0.1962 0.1699 0.1568 -0.0084 -0.0643 -0.0006 92  GLN A NE2 
737  N  N   . PHE A 93  ? 0.1714 0.0267 0.0892 0.0049  -0.0450 0.0063  93  PHE A N   
738  C  CA  . PHE A 93  ? 0.1419 0.0264 0.0994 -0.0056 -0.0224 0.0088  93  PHE A CA  
739  C  C   . PHE A 93  ? 0.1651 0.0709 0.0971 -0.0191 -0.0074 0.0160  93  PHE A C   
740  O  O   . PHE A 93  ? 0.2127 0.0645 0.0739 0.0005  -0.0132 0.0037  93  PHE A O   
741  C  CB  . PHE A 93  ? 0.1384 0.0655 0.0800 -0.0096 -0.0617 0.0144  93  PHE A CB  
742  C  CG  . PHE A 93  ? 0.1458 0.0741 0.1258 -0.0017 -0.0446 0.0054  93  PHE A CG  
743  C  CD1 . PHE A 93  ? 0.1792 0.0783 0.0875 -0.0187 -0.0689 -0.0076 93  PHE A CD1 
744  C  CD2 . PHE A 93  ? 0.1049 0.1201 0.1440 -0.0338 -0.0874 0.0212  93  PHE A CD2 
745  C  CE1 . PHE A 93  ? 0.1846 0.0670 0.1079 0.0099  -0.0746 0.0034  93  PHE A CE1 
746  C  CE2 . PHE A 93  ? 0.1916 0.0982 0.1222 0.0468  -0.0745 -0.0050 93  PHE A CE2 
747  C  CZ  . PHE A 93  ? 0.2099 0.0944 0.0922 0.0029  -0.0849 -0.0145 93  PHE A CZ  
748  N  N   . HIS A 94  ? 0.1309 0.0502 0.1052 0.0003  -0.0297 0.0139  94  HIS A N   
749  C  CA  . HIS A 94  ? 0.1182 0.0445 0.0971 0.0047  -0.0231 0.0228  94  HIS A CA  
750  C  C   . HIS A 94  ? 0.1361 0.0560 0.0837 -0.0140 -0.0324 0.0076  94  HIS A C   
751  O  O   . HIS A 94  ? 0.1378 0.0497 0.1053 0.0049  -0.0217 0.0198  94  HIS A O   
752  C  CB  . HIS A 94  ? 0.1425 0.0698 0.0764 -0.0131 -0.0266 0.0053  94  HIS A CB  
753  C  CG  . HIS A 94  ? 0.1398 0.0384 0.0978 0.0146  -0.0157 -0.0070 94  HIS A CG  
754  N  ND1 . HIS A 94  ? 0.1592 0.0618 0.0516 0.0113  0.0000  0.0198  94  HIS A ND1 
755  C  CD2 . HIS A 94  ? 0.1715 0.0570 0.0951 -0.0243 -0.0166 -0.0242 94  HIS A CD2 
756  C  CE1 . HIS A 94  ? 0.1156 0.0575 0.0811 -0.0032 0.0130  0.0271  94  HIS A CE1 
757  N  NE2 . HIS A 94  ? 0.1104 0.0473 0.1090 -0.0219 -0.0127 -0.0313 94  HIS A NE2 
758  N  N   . PHE A 95  ? 0.1179 0.0408 0.0965 0.0066  -0.0175 0.0178  95  PHE A N   
759  C  CA  . PHE A 95  ? 0.1208 0.0586 0.0899 -0.0016 -0.0385 -0.0008 95  PHE A CA  
760  C  C   . PHE A 95  ? 0.1182 0.0563 0.0988 -0.0090 -0.0264 0.0038  95  PHE A C   
761  O  O   . PHE A 95  ? 0.1162 0.0578 0.1109 0.0085  -0.0191 0.0078  95  PHE A O   
762  C  CB  . PHE A 95  ? 0.1249 0.0656 0.0819 -0.0013 -0.0301 -0.0148 95  PHE A CB  
763  C  CG  . PHE A 95  ? 0.0978 0.0441 0.0861 -0.0271 -0.0214 -0.0012 95  PHE A CG  
764  C  CD1 . PHE A 95  ? 0.1331 0.0768 0.0714 0.0041  -0.0391 -0.0065 95  PHE A CD1 
765  C  CD2 . PHE A 95  ? 0.1061 0.0630 0.1182 -0.0422 -0.0325 -0.0183 95  PHE A CD2 
766  C  CE1 . PHE A 95  ? 0.1170 0.0511 0.0999 -0.0215 -0.0300 -0.0034 95  PHE A CE1 
767  C  CE2 . PHE A 95  ? 0.1310 0.0803 0.0688 0.0030  -0.0522 -0.0012 95  PHE A CE2 
768  C  CZ  . PHE A 95  ? 0.1126 0.0474 0.1236 -0.0038 -0.0239 -0.0022 95  PHE A CZ  
769  N  N   . HIS A 96  ? 0.1317 0.0254 0.0860 0.0015  -0.0252 0.0014  96  HIS A N   
770  C  CA  . HIS A 96  ? 0.1153 0.0279 0.0930 0.0033  -0.0399 0.0096  96  HIS A CA  
771  C  C   . HIS A 96  ? 0.0839 0.0374 0.0899 -0.0057 -0.0043 0.0123  96  HIS A C   
772  O  O   . HIS A 96  ? 0.1089 0.0468 0.0956 -0.0081 0.0187  0.0059  96  HIS A O   
773  C  CB  . HIS A 96  ? 0.1130 0.0395 0.0926 0.0004  -0.0220 -0.0286 96  HIS A CB  
774  C  CG  . HIS A 96  ? 0.1170 0.0515 0.1111 -0.0176 -0.0085 -0.0252 96  HIS A CG  
775  N  ND1 . HIS A 96  ? 0.0974 0.0485 0.1724 -0.0178 -0.0038 0.0144  96  HIS A ND1 
776  C  CD2 . HIS A 96  ? 0.1409 0.0313 0.1018 0.0240  -0.0175 -0.0111 96  HIS A CD2 
777  C  CE1 . HIS A 96  ? 0.0589 0.0899 0.1083 -0.0353 0.0387  -0.0082 96  HIS A CE1 
778  N  NE2 . HIS A 96  ? 0.0998 0.0332 0.0977 0.0115  0.0226  -0.0166 96  HIS A NE2 
779  N  N   . TRP A 97  ? 0.1225 0.0295 0.1254 -0.0049 -0.0006 -0.0162 97  TRP A N   
780  C  CA  . TRP A 97  ? 0.0955 0.0449 0.0886 0.0078  -0.0137 -0.0351 97  TRP A CA  
781  C  C   . TRP A 97  ? 0.1082 0.0773 0.0949 0.0094  -0.0106 -0.0230 97  TRP A C   
782  O  O   . TRP A 97  ? 0.1282 0.0578 0.1176 0.0015  0.0187  -0.0063 97  TRP A O   
783  C  CB  . TRP A 97  ? 0.1137 0.0782 0.1050 -0.0183 -0.0334 -0.0105 97  TRP A CB  
784  C  CG  . TRP A 97  ? 0.1245 0.0666 0.1239 -0.0256 0.0054  -0.0061 97  TRP A CG  
785  C  CD1 . TRP A 97  ? 0.1328 0.0790 0.1113 -0.0292 -0.0136 -0.0402 97  TRP A CD1 
786  C  CD2 . TRP A 97  ? 0.1104 0.0812 0.0863 -0.0312 0.0053  -0.0230 97  TRP A CD2 
787  N  NE1 . TRP A 97  ? 0.1592 0.0595 0.1306 -0.0043 0.0320  -0.0137 97  TRP A NE1 
788  C  CE2 . TRP A 97  ? 0.1556 0.0718 0.0532 -0.0109 -0.0073 -0.0177 97  TRP A CE2 
789  C  CE3 . TRP A 97  ? 0.1475 0.0626 0.0760 -0.0083 -0.0131 -0.0020 97  TRP A CE3 
790  C  CZ2 . TRP A 97  ? 0.1673 0.0889 0.1104 0.0031  0.0207  0.0100  97  TRP A CZ2 
791  C  CZ3 . TRP A 97  ? 0.1515 0.0764 0.1132 -0.0147 -0.0217 0.0113  97  TRP A CZ3 
792  C  CH2 . TRP A 97  ? 0.2037 0.1097 0.1210 -0.0066 0.0105  0.0082  97  TRP A CH2 
793  N  N   . GLY A 98  ? 0.1335 0.0635 0.0972 0.0091  0.0055  -0.0183 98  GLY A N   
794  C  CA  . GLY A 98  ? 0.1249 0.0853 0.1203 0.0057  0.0045  -0.0115 98  GLY A CA  
795  C  C   . GLY A 98  ? 0.0866 0.0781 0.1119 -0.0111 -0.0149 -0.0214 98  GLY A C   
796  O  O   . GLY A 98  ? 0.1537 0.0613 0.1447 -0.0104 -0.0232 -0.0335 98  GLY A O   
797  N  N   . SER A 99  ? 0.1115 0.0639 0.1339 -0.0011 0.0161  -0.0421 99  SER A N   
798  C  CA  . SER A 99  ? 0.1329 0.0842 0.1418 -0.0081 0.0247  -0.0392 99  SER A CA  
799  C  C   . SER A 99  ? 0.1736 0.0729 0.1364 -0.0167 0.0138  -0.0340 99  SER A C   
800  O  O   . SER A 99  ? 0.2389 0.1153 0.1571 -0.0142 0.0153  -0.0215 99  SER A O   
801  C  CB  . SER A 99  ? 0.1616 0.1351 0.1574 0.0072  0.0264  -0.0482 99  SER A CB  
802  O  OG  . SER A 99  ? 0.1550 0.1078 0.2108 0.0020  0.0333  -0.0323 99  SER A OG  
803  N  N   . LEU A 100 ? 0.1635 0.1061 0.1685 -0.0205 0.0006  -0.0213 100 LEU A N   
804  C  CA  . LEU A 100 ? 0.1671 0.1258 0.2038 -0.0082 -0.0017 0.0113  100 LEU A CA  
805  C  C   . LEU A 100 ? 0.1568 0.1154 0.1680 -0.0353 -0.0003 -0.0063 100 LEU A C   
806  O  O   . LEU A 100 ? 0.1643 0.0674 0.1707 -0.0210 -0.0054 -0.0132 100 LEU A O   
807  C  CB  . LEU A 100 ? 0.2354 0.1784 0.2382 0.0159  0.0177  0.0284  100 LEU A CB  
808  C  CG  . LEU A 100 ? 0.2664 0.2253 0.2883 -0.0075 0.0248  0.0103  100 LEU A CG  
809  C  CD1 . LEU A 100 ? 0.2533 0.3819 0.3254 0.0338  0.0332  -0.0083 100 LEU A CD1 
810  C  CD2 . LEU A 100 ? 0.3588 0.2819 0.2951 -0.0409 0.0500  -0.0638 100 LEU A CD2 
811  N  N   . ASP A 101 ? 0.1189 0.0755 0.1837 -0.0228 -0.0161 0.0022  101 ASP A N   
812  C  CA  . ASP A 101 ? 0.1526 0.0909 0.1863 -0.0383 -0.0264 0.0018  101 ASP A CA  
813  C  C   . ASP A 101 ? 0.1762 0.0737 0.1725 -0.0127 -0.0180 -0.0021 101 ASP A C   
814  O  O   . ASP A 101 ? 0.2033 0.1017 0.1908 -0.0165 -0.0089 0.0267  101 ASP A O   
815  C  CB  . ASP A 101 ? 0.1290 0.1133 0.2078 -0.0418 -0.0321 0.0000  101 ASP A CB  
816  C  CG  . ASP A 101 ? 0.1611 0.1219 0.2553 -0.0149 -0.0340 0.0286  101 ASP A CG  
817  O  OD1 . ASP A 101 ? 0.2182 0.1076 0.2437 -0.0345 -0.0309 0.0230  101 ASP A OD1 
818  O  OD2 . ASP A 101 ? 0.2629 0.1949 0.2962 -0.0904 -0.0629 -0.0095 101 ASP A OD2 
819  N  N   . GLY A 102 ? 0.2020 0.0583 0.1723 -0.0146 -0.0425 0.0108  102 GLY A N   
820  C  CA  . GLY A 102 ? 0.1883 0.0643 0.1727 -0.0149 -0.0402 -0.0048 102 GLY A CA  
821  C  C   . GLY A 102 ? 0.1570 0.0700 0.1458 -0.0013 -0.0186 0.0062  102 GLY A C   
822  O  O   . GLY A 102 ? 0.1784 0.1262 0.1433 -0.0108 -0.0068 0.0184  102 GLY A O   
823  N  N   . GLN A 103 ? 0.1301 0.0476 0.1681 -0.0073 -0.0059 0.0000  103 GLN A N   
824  C  CA  . GLN A 103 ? 0.1234 0.0327 0.1586 0.0000  -0.0188 -0.0136 103 GLN A CA  
825  C  C   . GLN A 103 ? 0.1107 0.0601 0.1164 -0.0205 0.0028  -0.0066 103 GLN A C   
826  O  O   . GLN A 103 ? 0.1574 0.0652 0.1197 0.0033  -0.0180 -0.0218 103 GLN A O   
827  C  CB  . GLN A 103 ? 0.1410 0.0881 0.1870 -0.0064 0.0015  -0.0164 103 GLN A CB  
828  C  CG  . GLN A 103 ? 0.1291 0.0843 0.1739 0.0274  0.0053  -0.0417 103 GLN A CG  
829  C  CD  . GLN A 103 ? 0.1668 0.1879 0.2155 0.0545  0.0276  0.0567  103 GLN A CD  
830  O  OE1 . GLN A 103 ? 0.2491 0.2949 0.3123 0.1142  0.0599  0.1338  103 GLN A OE1 
831  N  NE2 . GLN A 103 ? 0.2098 0.1860 0.2093 0.0225  0.0384  0.0221  103 GLN A NE2 
832  N  N   . GLY A 104 ? 0.1308 0.0410 0.1183 0.0269  0.0037  -0.0264 104 GLY A N   
833  C  CA  . GLY A 104 ? 0.1104 0.0296 0.1144 0.0067  0.0096  -0.0175 104 GLY A CA  
834  C  C   . GLY A 104 ? 0.0985 0.0400 0.0929 0.0026  -0.0069 -0.0168 104 GLY A C   
835  O  O   . GLY A 104 ? 0.1083 0.0770 0.1149 0.0029  0.0002  0.0056  104 GLY A O   
836  N  N   . SER A 105 ? 0.0911 0.0551 0.0579 0.0077  0.0105  -0.0220 105 SER A N   
837  C  CA  . SER A 105 ? 0.1045 0.0765 0.0666 -0.0089 -0.0063 -0.0138 105 SER A CA  
838  C  C   . SER A 105 ? 0.0640 0.0626 0.0838 -0.0061 -0.0107 -0.0088 105 SER A C   
839  O  O   . SER A 105 ? 0.1220 0.0316 0.1091 -0.0007 -0.0317 -0.0212 105 SER A O   
840  C  CB  . SER A 105 ? 0.0830 0.1138 0.0747 -0.0049 -0.0161 0.0218  105 SER A CB  
841  O  OG  . SER A 105 ? 0.0957 0.0490 0.1112 0.0111  -0.0012 0.0004  105 SER A OG  
842  N  N   . GLU A 106 ? 0.0851 0.0623 0.0783 -0.0037 -0.0236 -0.0263 106 GLU A N   
843  C  CA  . GLU A 106 ? 0.1070 0.0368 0.0775 -0.0100 -0.0049 -0.0041 106 GLU A CA  
844  C  C   . GLU A 106 ? 0.0767 0.0489 0.0863 0.0240  -0.0003 0.0020  106 GLU A C   
845  O  O   . GLU A 106 ? 0.0631 0.0577 0.1385 0.0160  -0.0171 -0.0119 106 GLU A O   
846  C  CB  . GLU A 106 ? 0.1435 0.0267 0.0803 -0.0102 -0.0052 0.0057  106 GLU A CB  
847  C  CG  . GLU A 106 ? 0.1634 0.0514 0.0912 -0.0401 0.0086  0.0281  106 GLU A CG  
848  C  CD  . GLU A 106 ? 0.0951 0.0565 0.0721 -0.0352 0.0098  0.0000  106 GLU A CD  
849  O  OE1 . GLU A 106 ? 0.0799 0.0603 0.1266 0.0076  0.0099  -0.0179 106 GLU A OE1 
850  O  OE2 . GLU A 106 ? 0.0834 0.1056 0.1253 -0.0202 0.0357  -0.0102 106 GLU A OE2 
851  N  N   . HIS A 107 ? 0.0661 0.0658 0.0995 0.0257  0.0125  -0.0075 107 HIS A N   
852  C  CA  . HIS A 107 ? 0.0826 0.0460 0.0808 0.0124  0.0222  -0.0158 107 HIS A CA  
853  C  C   . HIS A 107 ? 0.0826 0.0617 0.0737 0.0050  0.0029  0.0084  107 HIS A C   
854  O  O   . HIS A 107 ? 0.0907 0.0688 0.1064 0.0090  -0.0153 -0.0001 107 HIS A O   
855  C  CB  . HIS A 107 ? 0.0904 0.0599 0.0853 0.0273  -0.0001 -0.0117 107 HIS A CB  
856  C  CG  . HIS A 107 ? 0.0556 0.0435 0.1068 0.0130  -0.0115 0.0029  107 HIS A CG  
857  N  ND1 . HIS A 107 ? 0.0963 0.0819 0.0859 0.0238  -0.0253 0.0011  107 HIS A ND1 
858  C  CD2 . HIS A 107 ? 0.0513 0.1008 0.0805 -0.0120 -0.0039 -0.0256 107 HIS A CD2 
859  C  CE1 . HIS A 107 ? 0.0786 0.0785 0.0867 0.0203  -0.0143 -0.0268 107 HIS A CE1 
860  N  NE2 . HIS A 107 ? 0.0594 0.0406 0.0905 0.0104  -0.0121 0.0162  107 HIS A NE2 
861  N  N   . THR A 108 ? 0.0952 0.0686 0.0619 0.0026  -0.0099 0.0161  108 THR A N   
862  C  CA  . THR A 108 ? 0.0867 0.0500 0.0964 0.0174  0.0030  0.0230  108 THR A CA  
863  C  C   . THR A 108 ? 0.0765 0.0812 0.0940 -0.0007 -0.0053 0.0145  108 THR A C   
864  O  O   . THR A 108 ? 0.1087 0.0767 0.0991 -0.0050 -0.0102 0.0216  108 THR A O   
865  C  CB  . THR A 108 ? 0.1092 0.0633 0.1089 0.0294  -0.0222 0.0045  108 THR A CB  
866  O  OG1 . THR A 108 ? 0.1077 0.0826 0.1130 0.0279  -0.0275 0.0118  108 THR A OG1 
867  C  CG2 . THR A 108 ? 0.1128 0.0907 0.0386 0.0013  -0.0238 -0.0073 108 THR A CG2 
868  N  N   . VAL A 109 ? 0.0783 0.0654 0.1162 -0.0097 0.0012  0.0268  109 VAL A N   
869  C  CA  . VAL A 109 ? 0.0853 0.0588 0.1363 0.0147  0.0030  0.0233  109 VAL A CA  
870  C  C   . VAL A 109 ? 0.1258 0.0612 0.1296 0.0078  0.0033  0.0124  109 VAL A C   
871  O  O   . VAL A 109 ? 0.1328 0.0756 0.1368 0.0004  -0.0104 0.0082  109 VAL A O   
872  C  CB  . VAL A 109 ? 0.0733 0.0799 0.1737 -0.0069 0.0129  0.0141  109 VAL A CB  
873  C  CG1 . VAL A 109 ? 0.0709 0.1183 0.1934 -0.0138 0.0418  0.0150  109 VAL A CG1 
874  C  CG2 . VAL A 109 ? 0.1511 0.0745 0.1569 0.0073  -0.0227 0.0303  109 VAL A CG2 
875  N  N   . ASP A 110 ? 0.1250 0.0738 0.1445 0.0281  -0.0114 0.0360  110 ASP A N   
876  C  CA  . ASP A 110 ? 0.1371 0.0755 0.1237 0.0257  0.0079  0.0180  110 ASP A CA  
877  C  C   . ASP A 110 ? 0.1432 0.0721 0.1167 0.0363  0.0005  0.0107  110 ASP A C   
878  O  O   . ASP A 110 ? 0.1887 0.0830 0.1380 -0.0037 0.0045  0.0359  110 ASP A O   
879  C  CB  . ASP A 110 ? 0.1479 0.0955 0.1594 0.0326  0.0222  0.0286  110 ASP A CB  
880  C  CG  . ASP A 110 ? 0.1653 0.1018 0.1138 -0.0006 0.0137  0.0330  110 ASP A CG  
881  O  OD1 . ASP A 110 ? 0.2219 0.1109 0.1518 0.0199  0.0188  0.0035  110 ASP A OD1 
882  O  OD2 . ASP A 110 ? 0.1860 0.1904 0.1917 0.0121  0.0208  0.0299  110 ASP A OD2 
883  N  N   . LYS A 111 ? 0.1477 0.0771 0.1142 0.0283  0.0044  0.0152  111 LYS A N   
884  C  CA  . LYS A 111 ? 0.1521 0.0909 0.1216 0.0242  -0.0240 0.0067  111 LYS A CA  
885  C  C   . LYS A 111 ? 0.1334 0.0772 0.1165 0.0113  -0.0200 0.0099  111 LYS A C   
886  O  O   . LYS A 111 ? 0.1370 0.0997 0.1427 0.0049  0.0026  -0.0036 111 LYS A O   
887  C  CB  . LYS A 111 ? 0.1613 0.1208 0.1530 0.0497  -0.0251 0.0151  111 LYS A CB  
888  C  CG  . LYS A 111 ? 0.2300 0.1462 0.1291 0.0751  -0.0788 0.0419  111 LYS A CG  
889  C  CD  . LYS A 111 ? 0.2362 0.2582 0.2346 0.0235  -0.0810 -0.0134 111 LYS A CD  
890  C  CE  . LYS A 111 ? 0.2879 0.2799 0.2573 0.0265  -0.0579 -0.0499 111 LYS A CE  
891  N  NZ  . LYS A 111 ? 0.3255 0.3001 0.3103 0.0337  -0.0734 0.0062  111 LYS A NZ  
892  N  N   . LYS A 112 ? 0.1234 0.0771 0.1130 0.0057  -0.0089 0.0239  112 LYS A N   
893  C  CA  . LYS A 112 ? 0.1410 0.1069 0.0949 0.0006  -0.0034 0.0237  112 LYS A CA  
894  C  C   . LYS A 112 ? 0.1308 0.0888 0.1048 0.0010  -0.0092 0.0204  112 LYS A C   
895  O  O   . LYS A 112 ? 0.1488 0.0840 0.0996 0.0200  -0.0137 0.0065  112 LYS A O   
896  C  CB  . LYS A 112 ? 0.1510 0.1410 0.1487 -0.0196 -0.0268 0.0098  112 LYS A CB  
897  C  CG  . LYS A 112 ? 0.1230 0.1631 0.1300 -0.0218 -0.0002 -0.0166 112 LYS A CG  
898  C  CD  . LYS A 112 ? 0.1742 0.1606 0.1944 0.0070  -0.0268 -0.0210 112 LYS A CD  
899  C  CE  . LYS A 112 ? 0.2289 0.2037 0.2009 0.0290  -0.0459 -0.0127 112 LYS A CE  
900  N  NZ  . LYS A 112 ? 0.3441 0.1987 0.2055 -0.0153 -0.0322 0.0131  112 LYS A NZ  
901  N  N   A LYS A 113 ? 0.1363 0.1184 0.0990 -0.0045 -0.0091 0.0195  113 LYS A N   
902  N  N   B LYS A 113 ? 0.1330 0.1076 0.0971 -0.0123 -0.0032 0.0208  113 LYS A N   
903  C  CA  A LYS A 113 ? 0.1137 0.0958 0.0949 0.0013  0.0036  0.0083  113 LYS A CA  
904  C  CA  B LYS A 113 ? 0.1115 0.0881 0.0859 -0.0052 0.0108  0.0119  113 LYS A CA  
905  C  C   A LYS A 113 ? 0.0971 0.0766 0.1042 0.0135  -0.0038 0.0109  113 LYS A C   
906  C  C   B LYS A 113 ? 0.0834 0.0690 0.0994 0.0094  0.0024  0.0099  113 LYS A C   
907  O  O   A LYS A 113 ? 0.1039 0.0615 0.0880 0.0064  0.0156  0.0188  113 LYS A O   
908  O  O   B LYS A 113 ? 0.0708 0.0724 0.0955 -0.0062 0.0132  -0.0192 113 LYS A O   
909  C  CB  A LYS A 113 ? 0.0746 0.0953 0.1079 -0.0058 -0.0050 -0.0043 113 LYS A CB  
910  C  CB  B LYS A 113 ? 0.0744 0.0724 0.1200 -0.0096 -0.0073 0.0167  113 LYS A CB  
911  C  CG  A LYS A 113 ? 0.0776 0.1270 0.1318 0.0124  -0.0169 0.0045  113 LYS A CG  
912  C  CG  B LYS A 113 ? 0.0616 0.1190 0.0547 0.0125  -0.0091 -0.0003 113 LYS A CG  
913  C  CD  A LYS A 113 ? 0.0818 0.1082 0.1034 0.0288  -0.0185 -0.0091 113 LYS A CD  
914  C  CD  B LYS A 113 ? 0.1005 0.0906 0.0845 0.0100  0.0287  0.0185  113 LYS A CD  
915  C  CE  A LYS A 113 ? 0.0731 0.1237 0.0746 0.0117  0.0066  -0.0454 113 LYS A CE  
916  C  CE  B LYS A 113 ? 0.1147 0.0986 0.1636 0.0129  0.0107  0.0026  113 LYS A CE  
917  N  NZ  A LYS A 113 ? 0.0786 0.1616 0.1302 0.0527  0.0011  0.0062  113 LYS A NZ  
918  N  NZ  B LYS A 113 ? 0.1220 0.0755 0.2638 0.0345  0.0086  -0.0221 113 LYS A NZ  
919  N  N   . TYR A 114 ? 0.0811 0.0762 0.1104 0.0067  -0.0071 0.0024  114 TYR A N   
920  C  CA  . TYR A 114 ? 0.0994 0.0642 0.0955 0.0174  -0.0120 0.0062  114 TYR A CA  
921  C  C   . TYR A 114 ? 0.1290 0.0601 0.1111 -0.0023 -0.0084 -0.0038 114 TYR A C   
922  O  O   . TYR A 114 ? 0.1210 0.0690 0.1033 -0.0211 -0.0078 0.0059  114 TYR A O   
923  C  CB  . TYR A 114 ? 0.0722 0.0650 0.1430 0.0160  0.0275  0.0017  114 TYR A CB  
924  C  CG  . TYR A 114 ? 0.1101 0.0483 0.1134 0.0080  0.0061  -0.0074 114 TYR A CG  
925  C  CD1 . TYR A 114 ? 0.1516 0.0692 0.0941 -0.0061 0.0423  0.0063  114 TYR A CD1 
926  C  CD2 . TYR A 114 ? 0.1091 0.0994 0.1727 -0.0321 0.0227  0.0084  114 TYR A CD2 
927  C  CE1 . TYR A 114 ? 0.1422 0.0989 0.0972 -0.0005 0.0038  0.0156  114 TYR A CE1 
928  C  CE2 . TYR A 114 ? 0.1685 0.1449 0.1507 -0.0148 0.0059  0.0032  114 TYR A CE2 
929  C  CZ  . TYR A 114 ? 0.1874 0.1067 0.1382 -0.0097 0.0371  0.0638  114 TYR A CZ  
930  O  OH  . TYR A 114 ? 0.2069 0.1815 0.2104 0.0028  0.0521  0.0149  114 TYR A OH  
931  N  N   . ALA A 115 ? 0.1374 0.0338 0.0878 -0.0053 -0.0296 -0.0016 115 ALA A N   
932  C  CA  . ALA A 115 ? 0.1242 0.0296 0.1051 -0.0039 -0.0160 -0.0118 115 ALA A CA  
933  C  C   . ALA A 115 ? 0.1191 0.0586 0.0964 -0.0011 -0.0127 0.0060  115 ALA A C   
934  O  O   . ALA A 115 ? 0.1416 0.0678 0.1091 -0.0154 -0.0042 0.0044  115 ALA A O   
935  C  CB  . ALA A 115 ? 0.1285 0.0884 0.1258 -0.0070 -0.0404 -0.0223 115 ALA A CB  
936  N  N   . ALA A 116 ? 0.1259 0.0255 0.0773 0.0019  -0.0130 0.0019  116 ALA A N   
937  C  CA  . ALA A 116 ? 0.1027 0.0266 0.0736 0.0060  -0.0120 -0.0073 116 ALA A CA  
938  C  C   . ALA A 116 ? 0.1291 0.0556 0.0834 0.0172  -0.0006 -0.0074 116 ALA A C   
939  O  O   . ALA A 116 ? 0.1046 0.0368 0.0979 0.0076  -0.0035 -0.0073 116 ALA A O   
940  C  CB  . ALA A 116 ? 0.1452 0.0767 0.0735 -0.0088 -0.0193 0.0254  116 ALA A CB  
941  N  N   . GLU A 117 ? 0.1151 0.0543 0.0872 -0.0052 -0.0074 -0.0010 117 GLU A N   
942  C  CA  . GLU A 117 ? 0.1081 0.0275 0.0810 0.0117  -0.0211 0.0023  117 GLU A CA  
943  C  C   . GLU A 117 ? 0.0861 0.0409 0.0894 -0.0071 -0.0016 0.0119  117 GLU A C   
944  O  O   . GLU A 117 ? 0.1033 0.0615 0.1002 0.0005  0.0005  0.0219  117 GLU A O   
945  C  CB  . GLU A 117 ? 0.1108 0.0546 0.0493 0.0086  -0.0012 0.0039  117 GLU A CB  
946  C  CG  . GLU A 117 ? 0.0690 0.0672 0.0495 0.0028  -0.0192 -0.0269 117 GLU A CG  
947  C  CD  . GLU A 117 ? 0.0695 0.0667 0.1048 -0.0160 -0.0101 0.0090  117 GLU A CD  
948  O  OE1 . GLU A 117 ? 0.1038 0.0807 0.1094 0.0159  -0.0317 0.0073  117 GLU A OE1 
949  O  OE2 . GLU A 117 ? 0.1152 0.0714 0.0962 0.0007  -0.0434 -0.0229 117 GLU A OE2 
950  N  N   . LEU A 118 ? 0.0957 0.0397 0.1027 0.0307  -0.0202 -0.0003 118 LEU A N   
951  C  CA  . LEU A 118 ? 0.1040 0.0369 0.0805 0.0043  -0.0254 -0.0158 118 LEU A CA  
952  C  C   . LEU A 118 ? 0.0998 0.0535 0.0701 0.0146  -0.0234 0.0021  118 LEU A C   
953  O  O   . LEU A 118 ? 0.1126 0.0409 0.0921 -0.0083 -0.0086 0.0071  118 LEU A O   
954  C  CB  . LEU A 118 ? 0.0693 0.0555 0.1215 0.0275  -0.0302 -0.0142 118 LEU A CB  
955  C  CG  . LEU A 118 ? 0.1250 0.0842 0.1110 0.0075  -0.0283 0.0016  118 LEU A CG  
956  C  CD1 . LEU A 118 ? 0.1871 0.0662 0.0921 -0.0050 -0.0183 0.0349  118 LEU A CD1 
957  C  CD2 . LEU A 118 ? 0.1114 0.1095 0.0947 -0.0235 -0.0472 0.0205  118 LEU A CD2 
958  N  N   . HIS A 119 ? 0.1134 0.0286 0.0802 0.0146  -0.0175 0.0037  119 HIS A N   
959  C  CA  . HIS A 119 ? 0.0987 0.0497 0.0833 0.0099  -0.0400 0.0044  119 HIS A CA  
960  C  C   . HIS A 119 ? 0.1202 0.0331 0.0628 0.0001  -0.0338 -0.0011 119 HIS A C   
961  O  O   . HIS A 119 ? 0.1448 0.0650 0.0810 0.0077  -0.0282 0.0204  119 HIS A O   
962  C  CB  . HIS A 119 ? 0.0847 0.0601 0.0684 0.0342  -0.0150 0.0157  119 HIS A CB  
963  C  CG  . HIS A 119 ? 0.0758 0.0491 0.0785 0.0282  -0.0312 -0.0009 119 HIS A CG  
964  N  ND1 . HIS A 119 ? 0.0700 0.0533 0.1176 0.0070  -0.0120 0.0000  119 HIS A ND1 
965  C  CD2 . HIS A 119 ? 0.1279 0.0359 0.0901 0.0235  0.0034  0.0191  119 HIS A CD2 
966  C  CE1 . HIS A 119 ? 0.0824 0.0448 0.0937 -0.0074 -0.0408 -0.0036 119 HIS A CE1 
967  N  NE2 . HIS A 119 ? 0.0720 0.0596 0.1162 -0.0154 -0.0189 0.0130  119 HIS A NE2 
968  N  N   . LEU A 120 ? 0.1119 0.0308 0.0895 0.0202  -0.0311 -0.0097 120 LEU A N   
969  C  CA  . LEU A 120 ? 0.1008 0.0403 0.1159 -0.0078 -0.0338 0.0020  120 LEU A CA  
970  C  C   . LEU A 120 ? 0.1089 0.0353 0.0968 -0.0018 -0.0311 0.0042  120 LEU A C   
971  O  O   . LEU A 120 ? 0.1051 0.0414 0.0869 -0.0151 -0.0326 0.0064  120 LEU A O   
972  C  CB  . LEU A 120 ? 0.1016 0.0353 0.1084 -0.0107 -0.0281 -0.0081 120 LEU A CB  
973  C  CG  . LEU A 120 ? 0.1074 0.0553 0.1014 0.0038  -0.0493 0.0162  120 LEU A CG  
974  C  CD1 . LEU A 120 ? 0.2007 0.0706 0.1273 -0.0677 -0.0260 0.0164  120 LEU A CD1 
975  C  CD2 . LEU A 120 ? 0.1843 0.1094 0.1003 0.0115  -0.0605 0.0156  120 LEU A CD2 
976  N  N   . VAL A 121 ? 0.0770 0.0379 0.1079 -0.0023 -0.0147 -0.0089 121 VAL A N   
977  C  CA  . VAL A 121 ? 0.0864 0.0566 0.1102 -0.0008 -0.0164 0.0064  121 VAL A CA  
978  C  C   . VAL A 121 ? 0.0979 0.0582 0.0982 -0.0051 -0.0202 -0.0094 121 VAL A C   
979  O  O   . VAL A 121 ? 0.1347 0.0774 0.0883 0.0119  -0.0474 0.0024  121 VAL A O   
980  C  CB  . VAL A 121 ? 0.1090 0.0474 0.1121 -0.0175 0.0132  0.0221  121 VAL A CB  
981  C  CG1 . VAL A 121 ? 0.1142 0.0706 0.1503 -0.0320 0.0001  -0.0148 121 VAL A CG1 
982  C  CG2 . VAL A 121 ? 0.1276 0.0532 0.1590 0.0255  0.0063  0.0438  121 VAL A CG2 
983  N  N   . HIS A 122 ? 0.1012 0.0476 0.0866 -0.0184 -0.0205 -0.0149 122 HIS A N   
984  C  CA  . HIS A 122 ? 0.0833 0.0425 0.1122 -0.0084 -0.0262 -0.0006 122 HIS A CA  
985  C  C   . HIS A 122 ? 0.1068 0.0443 0.1239 -0.0074 -0.0379 0.0002  122 HIS A C   
986  O  O   . HIS A 122 ? 0.1207 0.0329 0.1291 -0.0098 -0.0372 -0.0112 122 HIS A O   
987  C  CB  . HIS A 122 ? 0.0765 0.0534 0.1405 -0.0063 -0.0120 0.0035  122 HIS A CB  
988  C  CG  . HIS A 122 ? 0.0619 0.0452 0.1172 -0.0254 -0.0119 -0.0060 122 HIS A CG  
989  N  ND1 . HIS A 122 ? 0.0953 0.0254 0.1382 0.0023  -0.0012 0.0013  122 HIS A ND1 
990  C  CD2 . HIS A 122 ? 0.0870 0.1126 0.1160 -0.0152 -0.0265 -0.0064 122 HIS A CD2 
991  C  CE1 . HIS A 122 ? 0.0865 0.1208 0.1133 -0.0011 -0.0334 -0.0143 122 HIS A CE1 
992  N  NE2 . HIS A 122 ? 0.1015 0.1018 0.1506 -0.0237 -0.0459 -0.0135 122 HIS A NE2 
993  N  N   . TRP A 123 ? 0.0901 0.0307 0.1364 0.0026  -0.0247 -0.0242 123 TRP A N   
994  C  CA  . TRP A 123 ? 0.0923 0.0310 0.1160 -0.0147 -0.0093 -0.0127 123 TRP A CA  
995  C  C   . TRP A 123 ? 0.1042 0.0590 0.1160 -0.0024 -0.0273 -0.0145 123 TRP A C   
996  O  O   . TRP A 123 ? 0.1075 0.0798 0.1397 0.0020  -0.0494 0.0014  123 TRP A O   
997  C  CB  . TRP A 123 ? 0.0960 0.0834 0.1184 -0.0047 -0.0329 0.0111  123 TRP A CB  
998  C  CG  . TRP A 123 ? 0.1564 0.0886 0.1576 -0.0008 -0.0273 0.0195  123 TRP A CG  
999  C  CD1 . TRP A 123 ? 0.1691 0.0871 0.1347 -0.0350 -0.0323 0.0208  123 TRP A CD1 
1000 C  CD2 . TRP A 123 ? 0.2221 0.0592 0.1304 -0.0055 -0.0439 -0.0029 123 TRP A CD2 
1001 N  NE1 . TRP A 123 ? 0.1926 0.0454 0.1586 -0.0166 -0.0496 0.0148  123 TRP A NE1 
1002 C  CE2 . TRP A 123 ? 0.1933 0.0434 0.1472 0.0210  -0.0624 0.0035  123 TRP A CE2 
1003 C  CE3 . TRP A 123 ? 0.1620 0.0482 0.1879 -0.0124 -0.0591 0.0030  123 TRP A CE3 
1004 C  CZ2 . TRP A 123 ? 0.2133 0.0925 0.1499 0.0160  -0.0334 0.0104  123 TRP A CZ2 
1005 C  CZ3 . TRP A 123 ? 0.1649 0.0700 0.1391 -0.0095 -0.0582 -0.0183 123 TRP A CZ3 
1006 C  CH2 . TRP A 123 ? 0.2090 0.0983 0.1704 -0.0186 -0.0411 0.0104  123 TRP A CH2 
1007 N  N   . ASN A 124 ? 0.1084 0.0607 0.1074 -0.0122 -0.0129 -0.0500 124 ASN A N   
1008 C  CA  . ASN A 124 ? 0.1367 0.0393 0.1078 0.0140  -0.0141 -0.0332 124 ASN A CA  
1009 C  C   . ASN A 124 ? 0.1334 0.0708 0.1289 0.0052  -0.0191 -0.0262 124 ASN A C   
1010 O  O   . ASN A 124 ? 0.1407 0.0543 0.1619 -0.0027 -0.0126 -0.0258 124 ASN A O   
1011 C  CB  . ASN A 124 ? 0.1307 0.0639 0.0775 0.0101  -0.0147 -0.0354 124 ASN A CB  
1012 C  CG  . ASN A 124 ? 0.1350 0.0663 0.1341 0.0036  -0.0356 -0.0378 124 ASN A CG  
1013 O  OD1 . ASN A 124 ? 0.1462 0.0747 0.1729 0.0040  -0.0037 -0.0333 124 ASN A OD1 
1014 N  ND2 . ASN A 124 ? 0.2244 0.0957 0.1261 -0.0174 -0.0107 -0.0303 124 ASN A ND2 
1015 N  N   . THR A 125 ? 0.1328 0.0578 0.1753 0.0280  -0.0377 -0.0083 125 THR A N   
1016 C  CA  . THR A 125 ? 0.1265 0.0829 0.2027 0.0292  -0.0562 -0.0217 125 THR A CA  
1017 C  C   . THR A 125 ? 0.1329 0.0891 0.2147 0.0472  -0.0356 -0.0176 125 THR A C   
1018 O  O   . THR A 125 ? 0.1864 0.0886 0.2322 0.0221  -0.0493 -0.0111 125 THR A O   
1019 C  CB  . THR A 125 ? 0.1348 0.1063 0.2244 0.0169  -0.0422 -0.0163 125 THR A CB  
1020 O  OG1 . THR A 125 ? 0.1610 0.1678 0.2932 0.0522  -0.0109 -0.0401 125 THR A OG1 
1021 C  CG2 . THR A 125 ? 0.1324 0.1054 0.2352 0.0230  -0.0699 -0.0313 125 THR A CG2 
1022 N  N   . LYS A 126 ? 0.1949 0.0540 0.1823 0.0182  -0.0043 -0.0651 127 LYS A N   
1023 C  CA  . LYS A 126 ? 0.2078 0.1181 0.2051 -0.0215 -0.0124 -0.0570 127 LYS A CA  
1024 C  C   . LYS A 126 ? 0.1861 0.0962 0.2135 -0.0093 -0.0048 -0.0388 127 LYS A C   
1025 O  O   . LYS A 126 ? 0.2078 0.1237 0.2678 -0.0282 -0.0027 -0.0679 127 LYS A O   
1026 C  CB  . LYS A 126 ? 0.2634 0.1411 0.2469 -0.0169 -0.0043 -0.0427 127 LYS A CB  
1027 C  CG  . LYS A 126 ? 0.2792 0.2203 0.2525 -0.0144 -0.0242 -0.0574 127 LYS A CG  
1028 C  CD  . LYS A 126 ? 0.3774 0.3142 0.2912 -0.0186 0.0254  0.0018  127 LYS A CD  
1029 C  CE  . LYS A 126 ? 0.3533 0.3977 0.4051 0.0108  -0.0143 -0.0265 127 LYS A CE  
1030 N  NZ  . LYS A 126 ? 0.3953 0.3983 0.4006 0.0087  0.0072  -0.0452 127 LYS A NZ  
1031 N  N   . TYR A 127 ? 0.1672 0.0546 0.1609 -0.0011 -0.0108 -0.0268 128 TYR A N   
1032 C  CA  . TYR A 127 ? 0.1643 0.0705 0.1723 0.0044  -0.0179 0.0002  128 TYR A CA  
1033 C  C   . TYR A 127 ? 0.1635 0.0723 0.1768 0.0097  -0.0116 0.0020  128 TYR A C   
1034 O  O   . TYR A 127 ? 0.1429 0.0962 0.1926 0.0202  -0.0003 0.0032  128 TYR A O   
1035 C  CB  . TYR A 127 ? 0.1727 0.0572 0.1593 0.0051  -0.0284 -0.0196 128 TYR A CB  
1036 C  CG  . TYR A 127 ? 0.1631 0.0611 0.1113 -0.0173 -0.0502 -0.0101 128 TYR A CG  
1037 C  CD1 . TYR A 127 ? 0.1973 0.0765 0.1636 -0.0023 -0.0502 -0.0605 128 TYR A CD1 
1038 C  CD2 . TYR A 127 ? 0.1449 0.0476 0.1208 0.0116  0.0097  -0.0229 128 TYR A CD2 
1039 C  CE1 . TYR A 127 ? 0.1872 0.0929 0.1420 -0.0142 -0.0660 -0.0507 128 TYR A CE1 
1040 C  CE2 . TYR A 127 ? 0.1247 0.1264 0.0920 -0.0111 -0.0225 -0.0565 128 TYR A CE2 
1041 C  CZ  . TYR A 127 ? 0.1455 0.1289 0.1111 0.0147  -0.0177 -0.0318 128 TYR A CZ  
1042 O  OH  . TYR A 127 ? 0.2607 0.1043 0.1408 0.0399  -0.0277 -0.0538 128 TYR A OH  
1043 N  N   . GLY A 128 ? 0.1703 0.0693 0.1689 -0.0033 -0.0153 0.0106  129 GLY A N   
1044 C  CA  . GLY A 128 ? 0.1944 0.0846 0.1640 0.0109  -0.0134 0.0326  129 GLY A CA  
1045 C  C   . GLY A 128 ? 0.1729 0.0773 0.1836 -0.0052 -0.0207 0.0244  129 GLY A C   
1046 O  O   . GLY A 128 ? 0.2442 0.0883 0.2038 0.0000  -0.0463 0.0475  129 GLY A O   
1047 N  N   . ASP A 129 ? 0.1998 0.0693 0.1783 0.0194  -0.0174 0.0032  130 ASP A N   
1048 C  CA  . ASP A 129 ? 0.2146 0.0456 0.2030 0.0275  -0.0038 0.0204  130 ASP A CA  
1049 C  C   . ASP A 129 ? 0.2033 0.0777 0.1772 0.0179  -0.0188 0.0060  130 ASP A C   
1050 O  O   . ASP A 129 ? 0.2195 0.1098 0.1592 0.0189  -0.0144 -0.0148 130 ASP A O   
1051 C  CB  . ASP A 129 ? 0.2356 0.1126 0.2094 0.0607  0.0046  0.0172  130 ASP A CB  
1052 C  CG  . ASP A 129 ? 0.2667 0.0890 0.3261 0.0481  0.0073  -0.0030 130 ASP A CG  
1053 O  OD1 . ASP A 129 ? 0.3921 0.1079 0.3241 -0.0499 -0.0924 0.0532  130 ASP A OD1 
1054 O  OD2 . ASP A 129 ? 0.2208 0.2249 0.4668 0.0397  0.0769  0.1129  130 ASP A OD2 
1055 N  N   . PHE A 130 ? 0.1975 0.0820 0.1818 0.0006  -0.0218 -0.0125 131 PHE A N   
1056 C  CA  . PHE A 130 ? 0.1932 0.1154 0.1776 -0.0137 -0.0204 -0.0140 131 PHE A CA  
1057 C  C   . PHE A 130 ? 0.1848 0.0990 0.1586 -0.0303 -0.0038 -0.0072 131 PHE A C   
1058 O  O   . PHE A 130 ? 0.2020 0.1170 0.1464 -0.0448 -0.0058 0.0310  131 PHE A O   
1059 C  CB  . PHE A 130 ? 0.2069 0.0830 0.1533 -0.0218 -0.0189 -0.0327 131 PHE A CB  
1060 C  CG  . PHE A 130 ? 0.1579 0.1403 0.1744 -0.0172 -0.0178 0.0005  131 PHE A CG  
1061 C  CD1 . PHE A 130 ? 0.1307 0.1149 0.1504 0.0221  -0.0086 -0.0143 131 PHE A CD1 
1062 C  CD2 . PHE A 130 ? 0.1866 0.1509 0.2123 0.0051  -0.0052 0.0187  131 PHE A CD2 
1063 C  CE1 . PHE A 130 ? 0.1166 0.1343 0.1649 -0.0162 -0.0527 -0.0207 131 PHE A CE1 
1064 C  CE2 . PHE A 130 ? 0.2306 0.1910 0.2593 -0.0114 -0.0190 0.0024  131 PHE A CE2 
1065 C  CZ  . PHE A 130 ? 0.1829 0.1403 0.2291 -0.0565 -0.0368 -0.0414 131 PHE A CZ  
1066 N  N   . GLY A 131 ? 0.1984 0.0968 0.1709 -0.0411 0.0091  -0.0062 132 GLY A N   
1067 C  CA  . GLY A 131 ? 0.2042 0.1343 0.1686 -0.0313 0.0185  0.0130  132 GLY A CA  
1068 C  C   . GLY A 131 ? 0.1859 0.1070 0.1738 -0.0370 0.0196  0.0170  132 GLY A C   
1069 O  O   . GLY A 131 ? 0.2095 0.1080 0.2040 -0.0235 0.0134  -0.0193 132 GLY A O   
1070 N  N   . LYS A 132 ? 0.1766 0.0750 0.1961 -0.0591 0.0238  0.0040  133 LYS A N   
1071 C  CA  . LYS A 132 ? 0.1583 0.0718 0.1702 -0.0315 -0.0169 0.0147  133 LYS A CA  
1072 C  C   . LYS A 132 ? 0.1198 0.0716 0.1690 -0.0312 -0.0043 0.0084  133 LYS A C   
1073 O  O   . LYS A 132 ? 0.1236 0.0981 0.1635 -0.0313 -0.0239 0.0110  133 LYS A O   
1074 C  CB  . LYS A 132 ? 0.1532 0.0970 0.1953 -0.0106 -0.0036 0.0094  133 LYS A CB  
1075 C  CG  . LYS A 132 ? 0.2358 0.1431 0.2268 -0.0359 -0.0288 0.0208  133 LYS A CG  
1076 C  CD  . LYS A 132 ? 0.2190 0.1418 0.3439 0.0091  -0.0028 0.0359  133 LYS A CD  
1077 C  CE  . LYS A 132 ? 0.3364 0.2214 0.3798 -0.0308 -0.0054 0.0627  133 LYS A CE  
1078 N  NZ  . LYS A 132 ? 0.4448 0.4331 0.4480 -0.0051 0.0008  0.0267  133 LYS A NZ  
1079 N  N   . ALA A 133 ? 0.1006 0.0743 0.1472 -0.0321 0.0003  0.0008  134 ALA A N   
1080 C  CA  . ALA A 133 ? 0.1193 0.0775 0.1522 -0.0228 0.0122  0.0134  134 ALA A CA  
1081 C  C   . ALA A 133 ? 0.1113 0.0930 0.1621 -0.0363 0.0025  -0.0078 134 ALA A C   
1082 O  O   . ALA A 133 ? 0.1041 0.1319 0.1519 -0.0157 0.0002  -0.0117 134 ALA A O   
1083 C  CB  . ALA A 133 ? 0.0999 0.0739 0.1300 -0.0326 -0.0099 -0.0071 134 ALA A CB  
1084 N  N   . VAL A 134 ? 0.0970 0.0809 0.1641 -0.0185 0.0058  -0.0170 135 VAL A N   
1085 C  CA  . VAL A 134 ? 0.1314 0.1123 0.1522 -0.0249 0.0053  -0.0121 135 VAL A CA  
1086 C  C   . VAL A 134 ? 0.1087 0.1020 0.1570 -0.0291 0.0078  0.0028  135 VAL A C   
1087 O  O   . VAL A 134 ? 0.1275 0.1046 0.1752 -0.0118 0.0055  0.0027  135 VAL A O   
1088 C  CB  . VAL A 134 ? 0.1424 0.1271 0.1370 -0.0241 0.0221  -0.0181 135 VAL A CB  
1089 C  CG1 . VAL A 134 ? 0.1882 0.1846 0.1315 -0.0311 -0.0100 -0.0049 135 VAL A CG1 
1090 C  CG2 . VAL A 134 ? 0.1421 0.1476 0.2011 -0.0201 0.0197  0.0101  135 VAL A CG2 
1091 N  N   A GLN A 135 ? 0.1269 0.0915 0.1627 -0.0259 0.0017  -0.0029 136 GLN A N   
1092 N  N   B GLN A 135 ? 0.1236 0.0945 0.1591 -0.0287 -0.0007 -0.0065 136 GLN A N   
1093 C  CA  A GLN A 135 ? 0.1348 0.1132 0.1709 -0.0282 -0.0014 0.0048  136 GLN A CA  
1094 C  CA  B GLN A 135 ? 0.1271 0.1117 0.1605 -0.0307 -0.0046 0.0037  136 GLN A CA  
1095 C  C   A GLN A 135 ? 0.1165 0.0868 0.1647 -0.0103 -0.0140 -0.0056 136 GLN A C   
1096 C  C   B GLN A 135 ? 0.1076 0.0951 0.1570 -0.0172 -0.0176 -0.0148 136 GLN A C   
1097 O  O   A GLN A 135 ? 0.1500 0.0953 0.1529 -0.0050 -0.0303 -0.0038 136 GLN A O   
1098 O  O   B GLN A 135 ? 0.1406 0.1260 0.1393 -0.0157 -0.0265 -0.0255 136 GLN A O   
1099 C  CB  A GLN A 135 ? 0.1558 0.1248 0.1723 -0.0292 -0.0003 -0.0063 136 GLN A CB  
1100 C  CB  B GLN A 135 ? 0.1463 0.1241 0.1698 -0.0323 -0.0045 -0.0086 136 GLN A CB  
1101 C  CG  A GLN A 135 ? 0.1519 0.2079 0.2161 -0.0314 0.0297  0.0213  136 GLN A CG  
1102 C  CG  B GLN A 135 ? 0.1531 0.1819 0.1954 -0.0162 0.0181  0.0433  136 GLN A CG  
1103 C  CD  A GLN A 135 ? 0.2224 0.2351 0.2541 -0.0120 0.0199  0.0029  136 GLN A CD  
1104 C  CD  B GLN A 135 ? 0.1593 0.1968 0.2388 -0.0265 -0.0098 0.0108  136 GLN A CD  
1105 O  OE1 A GLN A 135 ? 0.2276 0.3155 0.2749 -0.0096 0.0234  0.0155  136 GLN A OE1 
1106 O  OE1 B GLN A 135 ? 0.2115 0.2570 0.2966 -0.0394 0.0017  0.0055  136 GLN A OE1 
1107 N  NE2 A GLN A 135 ? 0.2627 0.1967 0.3022 -0.0374 0.0196  -0.0124 136 GLN A NE2 
1108 N  NE2 B GLN A 135 ? 0.1438 0.1695 0.2453 -0.0452 0.0345  0.0611  136 GLN A NE2 
1109 N  N   . GLN A 136 ? 0.1052 0.0903 0.1607 -0.0081 -0.0073 -0.0139 137 GLN A N   
1110 C  CA  . GLN A 136 ? 0.1317 0.1176 0.1318 -0.0002 -0.0087 0.0081  137 GLN A CA  
1111 C  C   . GLN A 136 ? 0.1315 0.1358 0.1143 -0.0002 -0.0092 -0.0069 137 GLN A C   
1112 O  O   . GLN A 136 ? 0.1373 0.1070 0.0909 -0.0027 0.0035  -0.0130 137 GLN A O   
1113 C  CB  . GLN A 136 ? 0.1351 0.0964 0.1308 -0.0183 -0.0191 -0.0116 137 GLN A CB  
1114 C  CG  . GLN A 136 ? 0.2228 0.1455 0.1680 0.0189  0.0006  0.0108  137 GLN A CG  
1115 C  CD  . GLN A 136 ? 0.2224 0.1460 0.2405 0.0101  -0.0007 0.0305  137 GLN A CD  
1116 O  OE1 . GLN A 136 ? 0.3211 0.1533 0.2744 -0.0039 -0.0148 -0.0797 137 GLN A OE1 
1117 N  NE2 . GLN A 136 ? 0.3339 0.2338 0.4066 -0.0561 -0.0116 0.0167  137 GLN A NE2 
1118 N  N   . PRO A 137 ? 0.1150 0.1515 0.0976 -0.0056 -0.0070 -0.0204 138 PRO A N   
1119 C  CA  . PRO A 137 ? 0.1624 0.1548 0.1094 -0.0036 -0.0016 -0.0243 138 PRO A CA  
1120 C  C   . PRO A 137 ? 0.1423 0.1379 0.1225 -0.0082 -0.0202 -0.0200 138 PRO A C   
1121 O  O   . PRO A 137 ? 0.1798 0.1362 0.1976 0.0134  -0.0177 -0.0065 138 PRO A O   
1122 C  CB  . PRO A 137 ? 0.1993 0.1690 0.0948 0.0123  -0.0218 -0.0311 138 PRO A CB  
1123 C  CG  . PRO A 137 ? 0.2227 0.1850 0.1317 -0.0089 -0.0251 0.0031  138 PRO A CG  
1124 C  CD  . PRO A 137 ? 0.1616 0.1750 0.1077 -0.0252 -0.0171 -0.0366 138 PRO A CD  
1125 N  N   . ASP A 138 ? 0.1086 0.0875 0.1297 0.0082  -0.0142 -0.0269 139 ASP A N   
1126 C  CA  . ASP A 138 ? 0.1249 0.1371 0.1196 0.0132  0.0069  -0.0126 139 ASP A CA  
1127 C  C   . ASP A 138 ? 0.1130 0.0997 0.1247 -0.0174 -0.0192 -0.0143 139 ASP A C   
1128 O  O   . ASP A 138 ? 0.1090 0.1342 0.1537 -0.0179 -0.0162 -0.0036 139 ASP A O   
1129 C  CB  . ASP A 138 ? 0.1420 0.1204 0.1325 0.0031  0.0112  -0.0225 139 ASP A CB  
1130 C  CG  . ASP A 138 ? 0.1394 0.1363 0.1697 0.0349  -0.0004 -0.0477 139 ASP A CG  
1131 O  OD1 . ASP A 138 ? 0.1650 0.1211 0.2214 0.0356  -0.0030 -0.0685 139 ASP A OD1 
1132 O  OD2 . ASP A 138 ? 0.1985 0.2212 0.2041 0.0388  0.0437  -0.0715 139 ASP A OD2 
1133 N  N   . GLY A 139 ? 0.1176 0.0823 0.1153 -0.0210 -0.0126 -0.0232 140 GLY A N   
1134 C  CA  . GLY A 139 ? 0.1029 0.0675 0.0968 -0.0144 -0.0203 -0.0115 140 GLY A CA  
1135 C  C   . GLY A 139 ? 0.0826 0.0578 0.1263 -0.0157 -0.0233 -0.0024 140 GLY A C   
1136 O  O   . GLY A 139 ? 0.1086 0.0470 0.1394 -0.0071 -0.0284 -0.0115 140 GLY A O   
1137 N  N   . LEU A 140 ? 0.0696 0.0425 0.1255 -0.0254 -0.0069 -0.0120 141 LEU A N   
1138 C  CA  . LEU A 140 ? 0.0848 0.0487 0.1148 -0.0334 -0.0064 -0.0165 141 LEU A CA  
1139 C  C   . LEU A 140 ? 0.0959 0.0520 0.1039 -0.0098 -0.0129 -0.0153 141 LEU A C   
1140 O  O   . LEU A 140 ? 0.1125 0.0401 0.1037 -0.0260 -0.0242 -0.0151 141 LEU A O   
1141 C  CB  . LEU A 140 ? 0.0992 0.0869 0.1101 0.0030  0.0207  -0.0077 141 LEU A CB  
1142 C  CG  . LEU A 140 ? 0.1114 0.1221 0.1715 0.0179  0.0227  0.0043  141 LEU A CG  
1143 C  CD1 . LEU A 140 ? 0.0940 0.1137 0.1612 0.0672  0.0342  0.0055  141 LEU A CD1 
1144 C  CD2 . LEU A 140 ? 0.2367 0.0941 0.2059 0.0334  0.0040  0.0596  141 LEU A CD2 
1145 N  N   . ALA A 141 ? 0.0777 0.0428 0.1282 -0.0212 -0.0169 -0.0225 142 ALA A N   
1146 C  CA  . ALA A 141 ? 0.0702 0.0292 0.1122 -0.0041 -0.0041 -0.0171 142 ALA A CA  
1147 C  C   . ALA A 141 ? 0.0798 0.0452 0.0973 -0.0134 -0.0337 -0.0035 142 ALA A C   
1148 O  O   . ALA A 141 ? 0.1227 0.0765 0.0989 -0.0072 -0.0362 -0.0022 142 ALA A O   
1149 C  CB  . ALA A 141 ? 0.0872 0.0634 0.1420 0.0075  0.0041  -0.0176 142 ALA A CB  
1150 N  N   . VAL A 142 ? 0.1023 0.0458 0.1249 -0.0048 -0.0098 -0.0261 143 VAL A N   
1151 C  CA  . VAL A 142 ? 0.0779 0.0335 0.1119 0.0017  -0.0075 -0.0147 143 VAL A CA  
1152 C  C   . VAL A 142 ? 0.0901 0.0529 0.1116 0.0003  -0.0057 -0.0252 143 VAL A C   
1153 O  O   . VAL A 142 ? 0.0792 0.0717 0.1027 0.0058  -0.0285 -0.0021 143 VAL A O   
1154 C  CB  . VAL A 142 ? 0.0708 0.0692 0.1127 0.0014  -0.0139 -0.0258 143 VAL A CB  
1155 C  CG1 . VAL A 142 ? 0.0818 0.0701 0.0948 -0.0121 -0.0273 -0.0428 143 VAL A CG1 
1156 C  CG2 . VAL A 142 ? 0.0709 0.0940 0.1558 -0.0493 -0.0130 -0.0300 143 VAL A CG2 
1157 N  N   . LEU A 143 ? 0.0700 0.0422 0.1032 -0.0185 -0.0245 -0.0044 144 LEU A N   
1158 C  CA  . LEU A 143 ? 0.0712 0.0503 0.1147 -0.0069 -0.0467 -0.0109 144 LEU A CA  
1159 C  C   . LEU A 143 ? 0.0687 0.0832 0.1201 -0.0244 -0.0298 0.0023  144 LEU A C   
1160 O  O   . LEU A 143 ? 0.1112 0.0482 0.1044 -0.0175 -0.0226 -0.0039 144 LEU A O   
1161 C  CB  . LEU A 143 ? 0.0717 0.0882 0.1217 -0.0220 -0.0372 0.0077  144 LEU A CB  
1162 C  CG  . LEU A 143 ? 0.0791 0.0807 0.1471 -0.0141 -0.0249 0.0038  144 LEU A CG  
1163 C  CD1 . LEU A 143 ? 0.0872 0.1684 0.1522 -0.0144 -0.0112 0.0157  144 LEU A CD1 
1164 C  CD2 . LEU A 143 ? 0.0903 0.1277 0.1407 0.0070  -0.0454 0.0031  144 LEU A CD2 
1165 N  N   . GLY A 144 ? 0.0634 0.0584 0.1170 -0.0170 -0.0259 0.0066  145 GLY A N   
1166 C  CA  . GLY A 144 ? 0.0635 0.0424 0.1317 -0.0238 -0.0314 0.0060  145 GLY A CA  
1167 C  C   . GLY A 144 ? 0.0497 0.0536 0.1057 -0.0027 -0.0156 -0.0006 145 GLY A C   
1168 O  O   . GLY A 144 ? 0.0923 0.0462 0.1195 -0.0006 -0.0080 0.0120  145 GLY A O   
1169 N  N   . ILE A 145 ? 0.0883 0.0302 0.0953 -0.0093 -0.0285 -0.0099 146 ILE A N   
1170 C  CA  . ILE A 145 ? 0.0517 0.0649 0.1123 0.0072  -0.0197 0.0072  146 ILE A CA  
1171 C  C   . ILE A 145 ? 0.0844 0.0721 0.0910 -0.0022 -0.0271 -0.0060 146 ILE A C   
1172 O  O   . ILE A 145 ? 0.1146 0.0672 0.0944 0.0159  -0.0178 -0.0170 146 ILE A O   
1173 C  CB  . ILE A 145 ? 0.0940 0.0685 0.1213 0.0242  -0.0158 0.0283  146 ILE A CB  
1174 C  CG1 . ILE A 145 ? 0.0713 0.0688 0.1521 0.0281  -0.0200 -0.0050 146 ILE A CG1 
1175 C  CG2 . ILE A 145 ? 0.1108 0.0593 0.1699 -0.0074 -0.0314 0.0109  146 ILE A CG2 
1176 C  CD1 . ILE A 145 ? 0.0899 0.0927 0.1086 0.0200  -0.0327 0.0061  146 ILE A CD1 
1177 N  N   . PHE A 146 ? 0.0774 0.0496 0.0958 -0.0025 -0.0243 -0.0120 147 PHE A N   
1178 C  CA  . PHE A 146 ? 0.1004 0.0434 0.1004 0.0144  -0.0401 -0.0007 147 PHE A CA  
1179 C  C   . PHE A 146 ? 0.0638 0.0696 0.0975 -0.0139 -0.0171 -0.0043 147 PHE A C   
1180 O  O   . PHE A 146 ? 0.0763 0.0916 0.1067 0.0008  -0.0270 -0.0361 147 PHE A O   
1181 C  CB  . PHE A 146 ? 0.0804 0.0775 0.0876 -0.0066 -0.0301 0.0112  147 PHE A CB  
1182 C  CG  . PHE A 146 ? 0.0629 0.0286 0.0733 0.0000  -0.0181 0.0113  147 PHE A CG  
1183 C  CD1 . PHE A 146 ? 0.0412 0.0845 0.0763 0.0157  -0.0272 -0.0128 147 PHE A CD1 
1184 C  CD2 . PHE A 146 ? 0.1591 0.0360 0.0930 -0.0294 -0.0126 0.0010  147 PHE A CD2 
1185 C  CE1 . PHE A 146 ? 0.0982 0.0526 0.0727 0.0090  -0.0214 -0.0354 147 PHE A CE1 
1186 C  CE2 . PHE A 146 ? 0.0627 0.0453 0.1269 0.0050  -0.0146 -0.0013 147 PHE A CE2 
1187 C  CZ  . PHE A 146 ? 0.0716 0.0713 0.0986 -0.0057 -0.0326 -0.0027 147 PHE A CZ  
1188 N  N   . LEU A 147 ? 0.1113 0.0611 0.0925 -0.0026 -0.0180 -0.0311 148 LEU A N   
1189 C  CA  . LEU A 147 ? 0.1510 0.0311 0.0899 -0.0051 -0.0177 -0.0071 148 LEU A CA  
1190 C  C   . LEU A 147 ? 0.1239 0.0466 0.1330 0.0189  0.0005  -0.0042 148 LEU A C   
1191 O  O   . LEU A 147 ? 0.1090 0.0440 0.1322 0.0133  -0.0107 -0.0029 148 LEU A O   
1192 C  CB  . LEU A 147 ? 0.1099 0.0420 0.1081 -0.0207 -0.0130 0.0064  148 LEU A CB  
1193 C  CG  . LEU A 147 ? 0.1438 0.0354 0.0960 -0.0292 -0.0170 0.0182  148 LEU A CG  
1194 C  CD1 . LEU A 147 ? 0.1805 0.0619 0.1197 -0.0508 -0.0182 -0.0231 148 LEU A CD1 
1195 C  CD2 . LEU A 147 ? 0.1717 0.1046 0.0999 0.0038  -0.0006 0.0119  148 LEU A CD2 
1196 N  N   . LYS A 148 ? 0.1272 0.0298 0.1266 -0.0022 -0.0227 -0.0103 149 LYS A N   
1197 C  CA  . LYS A 148 ? 0.1441 0.0696 0.1395 0.0077  -0.0189 0.0000  149 LYS A CA  
1198 C  C   . LYS A 148 ? 0.1446 0.0715 0.1454 0.0086  -0.0332 -0.0174 149 LYS A C   
1199 O  O   . LYS A 148 ? 0.1329 0.0868 0.1393 0.0127  -0.0508 -0.0137 149 LYS A O   
1200 C  CB  . LYS A 148 ? 0.1374 0.0569 0.1623 -0.0311 -0.0297 -0.0167 149 LYS A CB  
1201 C  CG  . LYS A 148 ? 0.1500 0.1115 0.1896 -0.0249 0.0044  0.0037  149 LYS A CG  
1202 C  CD  . LYS A 148 ? 0.2066 0.1856 0.2217 -0.0047 -0.0014 0.0440  149 LYS A CD  
1203 C  CE  . LYS A 148 ? 0.2619 0.3509 0.2901 -0.0488 0.0537  0.0452  149 LYS A CE  
1204 N  NZ  . LYS A 148 ? 0.2661 0.3682 0.3095 -0.0638 0.0583  0.0376  149 LYS A NZ  
1205 N  N   . VAL A 149 ? 0.1634 0.0668 0.1414 -0.0104 -0.0335 -0.0324 150 VAL A N   
1206 C  CA  . VAL A 149 ? 0.1603 0.0888 0.1249 -0.0231 -0.0130 -0.0246 150 VAL A CA  
1207 C  C   . VAL A 149 ? 0.1579 0.0996 0.1531 -0.0229 -0.0211 -0.0265 150 VAL A C   
1208 O  O   . VAL A 149 ? 0.1891 0.1163 0.1944 -0.0323 -0.0414 0.0215  150 VAL A O   
1209 C  CB  . VAL A 149 ? 0.1686 0.0934 0.1393 -0.0116 -0.0240 -0.0207 150 VAL A CB  
1210 C  CG1 . VAL A 149 ? 0.1882 0.1421 0.1408 -0.0001 -0.0080 -0.0218 150 VAL A CG1 
1211 C  CG2 . VAL A 149 ? 0.1556 0.1598 0.1893 -0.0286 -0.0015 -0.0382 150 VAL A CG2 
1212 N  N   . GLY A 150 ? 0.1418 0.0778 0.1634 -0.0412 -0.0530 -0.0152 151 GLY A N   
1213 C  CA  . GLY A 150 ? 0.1236 0.1416 0.1764 -0.0395 -0.0422 -0.0024 151 GLY A CA  
1214 C  C   . GLY A 150 ? 0.1290 0.0960 0.1737 -0.0458 -0.0424 -0.0098 151 GLY A C   
1215 O  O   . GLY A 150 ? 0.1208 0.0780 0.2097 -0.0189 -0.0186 -0.0127 151 GLY A O   
1216 N  N   . SER A 151 ? 0.1535 0.1053 0.2151 -0.0129 -0.0486 -0.0071 152 SER A N   
1217 C  CA  . SER A 151 ? 0.1665 0.1014 0.2185 -0.0132 -0.0427 0.0003  152 SER A CA  
1218 C  C   . SER A 151 ? 0.1775 0.1203 0.1923 -0.0085 -0.0336 -0.0122 152 SER A C   
1219 O  O   . SER A 151 ? 0.1772 0.1563 0.1783 -0.0053 -0.0560 -0.0258 152 SER A O   
1220 C  CB  . SER A 151 ? 0.2260 0.2077 0.2757 0.0195  -0.0287 -0.0230 152 SER A CB  
1221 O  OG  . SER A 151 ? 0.2919 0.3289 0.3517 -0.0088 -0.0347 -0.0294 152 SER A OG  
1222 N  N   . ALA A 152 ? 0.1799 0.0974 0.1406 0.0037  -0.0402 -0.0145 153 ALA A N   
1223 C  CA  . ALA A 152 ? 0.2010 0.0835 0.1646 -0.0121 -0.0530 -0.0261 153 ALA A CA  
1224 C  C   . ALA A 152 ? 0.1660 0.1054 0.1600 -0.0216 -0.0485 -0.0285 153 ALA A C   
1225 O  O   . ALA A 152 ? 0.1787 0.0739 0.2230 -0.0045 -0.0367 -0.0265 153 ALA A O   
1226 C  CB  . ALA A 152 ? 0.2217 0.1028 0.1575 0.0113  -0.0455 -0.0379 153 ALA A CB  
1227 N  N   . LYS A 153 ? 0.1817 0.0660 0.1852 -0.0255 -0.0571 -0.0072 154 LYS A N   
1228 C  CA  . LYS A 153 ? 0.1953 0.0920 0.1726 0.0000  -0.0483 -0.0189 154 LYS A CA  
1229 C  C   . LYS A 153 ? 0.1781 0.1196 0.1853 0.0114  -0.0531 -0.0227 154 LYS A C   
1230 O  O   . LYS A 153 ? 0.1689 0.1062 0.1579 -0.0023 -0.0836 -0.0176 154 LYS A O   
1231 C  CB  . LYS A 153 ? 0.2066 0.0939 0.1838 -0.0049 -0.0541 -0.0354 154 LYS A CB  
1232 C  CG  . LYS A 153 ? 0.2911 0.1257 0.2027 -0.0060 -0.0408 -0.0415 154 LYS A CG  
1233 C  CD  . LYS A 153 ? 0.2387 0.1058 0.2142 0.0267  -0.0123 -0.0377 154 LYS A CD  
1234 C  CE  . LYS A 153 ? 0.3120 0.2104 0.2126 0.0421  -0.0241 -0.0075 154 LYS A CE  
1235 N  NZ  . LYS A 153 ? 0.3436 0.2724 0.2701 0.0060  -0.0084 -0.0118 154 LYS A NZ  
1236 N  N   . PRO A 154 ? 0.2016 0.1448 0.2072 0.0086  -0.0554 -0.0071 155 PRO A N   
1237 C  CA  . PRO A 154 ? 0.1821 0.1557 0.2080 0.0076  -0.0686 0.0220  155 PRO A CA  
1238 C  C   . PRO A 154 ? 0.1614 0.1464 0.2107 0.0057  -0.0676 0.0017  155 PRO A C   
1239 O  O   . PRO A 154 ? 0.2165 0.1892 0.2343 -0.0067 -0.0808 -0.0060 155 PRO A O   
1240 C  CB  . PRO A 154 ? 0.1713 0.1461 0.2388 0.0165  -0.0715 0.0087  155 PRO A CB  
1241 C  CG  . PRO A 154 ? 0.2306 0.2317 0.2511 0.0093  -0.0756 0.0266  155 PRO A CG  
1242 C  CD  . PRO A 154 ? 0.1231 0.1473 0.2200 0.0240  -0.0561 -0.0087 155 PRO A CD  
1243 N  N   . GLY A 155 ? 0.1858 0.1079 0.2190 0.0106  -0.0537 0.0020  156 GLY A N   
1244 C  CA  . GLY A 155 ? 0.1743 0.1076 0.2088 -0.0039 -0.0425 -0.0054 156 GLY A CA  
1245 C  C   . GLY A 155 ? 0.1975 0.1266 0.2166 -0.0190 -0.0395 0.0153  156 GLY A C   
1246 O  O   . GLY A 155 ? 0.2282 0.1307 0.2796 -0.0141 -0.0422 0.0217  156 GLY A O   
1247 N  N   . LEU A 156 ? 0.1877 0.0987 0.1848 -0.0111 -0.0573 0.0029  157 LEU A N   
1248 C  CA  . LEU A 156 ? 0.1803 0.0842 0.1547 -0.0146 -0.0654 -0.0022 157 LEU A CA  
1249 C  C   . LEU A 156 ? 0.1847 0.1031 0.1578 -0.0194 -0.0698 0.0013  157 LEU A C   
1250 O  O   . LEU A 156 ? 0.1955 0.0987 0.1632 -0.0157 -0.0866 -0.0006 157 LEU A O   
1251 C  CB  . LEU A 156 ? 0.1904 0.0977 0.1509 -0.0198 -0.0741 -0.0127 157 LEU A CB  
1252 C  CG  . LEU A 156 ? 0.1579 0.1053 0.1495 -0.0192 -0.0544 0.0243  157 LEU A CG  
1253 C  CD1 . LEU A 156 ? 0.1864 0.0959 0.1759 -0.0209 -0.0596 -0.0256 157 LEU A CD1 
1254 C  CD2 . LEU A 156 ? 0.2195 0.1041 0.1418 -0.0083 -0.0650 0.0025  157 LEU A CD2 
1255 N  N   . GLN A 157 ? 0.1987 0.1129 0.1407 -0.0196 -0.0793 -0.0182 158 GLN A N   
1256 C  CA  . GLN A 157 ? 0.1887 0.1071 0.1617 -0.0298 -0.0564 -0.0081 158 GLN A CA  
1257 C  C   . GLN A 157 ? 0.1865 0.1073 0.1428 -0.0123 -0.0649 -0.0058 158 GLN A C   
1258 O  O   . GLN A 157 ? 0.2312 0.1007 0.1688 -0.0087 -0.0784 -0.0151 158 GLN A O   
1259 C  CB  . GLN A 157 ? 0.2212 0.1194 0.2124 -0.0338 -0.0538 -0.0218 158 GLN A CB  
1260 C  CG  . GLN A 157 ? 0.2434 0.1526 0.2169 -0.0026 -0.0330 -0.0257 158 GLN A CG  
1261 C  CD  . GLN A 157 ? 0.2738 0.1001 0.1816 -0.0176 -0.0687 0.0043  158 GLN A CD  
1262 O  OE1 . GLN A 157 ? 0.3259 0.1103 0.2063 -0.0108 -0.0494 0.0105  158 GLN A OE1 
1263 N  NE2 . GLN A 157 ? 0.2987 0.1398 0.2161 -0.0310 -0.0666 -0.0066 158 GLN A NE2 
1264 N  N   A LYS A 158 ? 0.2129 0.1415 0.1766 -0.0181 -0.0700 -0.0171 159 LYS A N   
1265 N  N   B LYS A 158 ? 0.2169 0.1381 0.1725 -0.0197 -0.0697 -0.0080 159 LYS A N   
1266 C  CA  A LYS A 158 ? 0.2049 0.1334 0.1544 -0.0004 -0.0576 -0.0137 159 LYS A CA  
1267 C  CA  B LYS A 158 ? 0.2227 0.1501 0.1741 -0.0001 -0.0450 0.0031  159 LYS A CA  
1268 C  C   A LYS A 158 ? 0.2189 0.1182 0.1572 -0.0030 -0.0509 -0.0176 159 LYS A C   
1269 C  C   B LYS A 158 ? 0.2351 0.1364 0.1705 0.0006  -0.0463 0.0001  159 LYS A C   
1270 O  O   A LYS A 158 ? 0.2195 0.1155 0.1569 -0.0102 -0.0803 -0.0357 159 LYS A O   
1271 O  O   B LYS A 158 ? 0.2402 0.1327 0.1662 0.0095  -0.0544 -0.0019 159 LYS A O   
1272 C  CB  A LYS A 158 ? 0.2083 0.1655 0.1804 0.0098  -0.0523 -0.0148 159 LYS A CB  
1273 C  CB  B LYS A 158 ? 0.2301 0.1579 0.1827 0.0093  -0.0420 0.0083  159 LYS A CB  
1274 C  CG  A LYS A 158 ? 0.2241 0.1690 0.2100 -0.0077 -0.0478 -0.0129 159 LYS A CG  
1275 C  CG  B LYS A 158 ? 0.2398 0.1778 0.2033 0.0005  -0.0178 0.0356  159 LYS A CG  
1276 C  CD  A LYS A 158 ? 0.2635 0.2451 0.2540 -0.0070 -0.0276 -0.0056 159 LYS A CD  
1277 C  CD  B LYS A 158 ? 0.2491 0.2268 0.2523 0.0048  -0.0239 0.0033  159 LYS A CD  
1278 C  CE  A LYS A 158 ? 0.2121 0.2234 0.2291 0.0077  -0.0258 0.0037  159 LYS A CE  
1279 C  CE  B LYS A 158 ? 0.2469 0.2599 0.2818 0.0085  -0.0185 0.0134  159 LYS A CE  
1280 N  NZ  A LYS A 158 ? 0.2920 0.2431 0.2925 -0.0445 -0.0316 -0.0080 159 LYS A NZ  
1281 N  NZ  B LYS A 158 ? 0.2777 0.2805 0.2858 -0.0015 -0.0434 0.0333  159 LYS A NZ  
1282 N  N   . VAL A 159 ? 0.2250 0.0959 0.1602 0.0164  -0.0698 0.0024  160 VAL A N   
1283 C  CA  . VAL A 159 ? 0.2284 0.1010 0.1502 0.0032  -0.0626 -0.0006 160 VAL A CA  
1284 C  C   . VAL A 159 ? 0.2259 0.1006 0.1357 -0.0156 -0.0528 -0.0200 160 VAL A C   
1285 O  O   . VAL A 159 ? 0.2535 0.0820 0.1663 -0.0194 -0.0754 -0.0008 160 VAL A O   
1286 C  CB  . VAL A 159 ? 0.2268 0.0971 0.1454 -0.0112 -0.0624 0.0041  160 VAL A CB  
1287 C  CG1 . VAL A 159 ? 0.2162 0.1512 0.1965 -0.0253 -0.0456 -0.0027 160 VAL A CG1 
1288 C  CG2 . VAL A 159 ? 0.2984 0.1268 0.1652 0.0276  -0.0697 -0.0061 160 VAL A CG2 
1289 N  N   . VAL A 160 ? 0.2500 0.0836 0.1250 -0.0099 -0.0343 -0.0055 161 VAL A N   
1290 C  CA  . VAL A 160 ? 0.2897 0.0994 0.1572 -0.0223 -0.0201 -0.0067 161 VAL A CA  
1291 C  C   . VAL A 160 ? 0.2822 0.0971 0.1706 -0.0134 -0.0210 -0.0047 161 VAL A C   
1292 O  O   . VAL A 160 ? 0.2724 0.1339 0.1400 -0.0115 -0.0209 -0.0056 161 VAL A O   
1293 C  CB  . VAL A 160 ? 0.3215 0.0847 0.1793 0.0121  0.0052  -0.0038 161 VAL A CB  
1294 C  CG1 . VAL A 160 ? 0.3445 0.1522 0.2550 -0.0471 -0.0317 -0.0135 161 VAL A CG1 
1295 C  CG2 . VAL A 160 ? 0.3230 0.1341 0.2089 0.0164  -0.0159 0.0233  161 VAL A CG2 
1296 N  N   . ASP A 161 ? 0.3024 0.1045 0.1313 -0.0441 -0.0383 -0.0080 162 ASP A N   
1297 C  CA  . ASP A 161 ? 0.3275 0.1626 0.1668 -0.0456 -0.0244 0.0034  162 ASP A CA  
1298 C  C   . ASP A 161 ? 0.3617 0.1778 0.1645 -0.0465 -0.0301 0.0171  162 ASP A C   
1299 O  O   . ASP A 161 ? 0.3658 0.2084 0.2217 -0.0741 -0.0139 0.0038  162 ASP A O   
1300 C  CB  . ASP A 161 ? 0.3482 0.2010 0.1942 -0.0321 -0.0173 0.0005  162 ASP A CB  
1301 C  CG  . ASP A 161 ? 0.3125 0.1869 0.2401 -0.0193 -0.0161 -0.0258 162 ASP A CG  
1302 O  OD1 . ASP A 161 ? 0.3935 0.1775 0.2369 -0.0228 -0.0416 -0.0213 162 ASP A OD1 
1303 O  OD2 . ASP A 161 ? 0.3791 0.2106 0.2807 -0.0287 -0.0572 -0.0407 162 ASP A OD2 
1304 N  N   . VAL A 162 ? 0.3396 0.1684 0.1468 -0.0338 -0.0366 0.0002  163 VAL A N   
1305 C  CA  . VAL A 162 ? 0.3306 0.1647 0.1576 -0.0259 -0.0313 0.0041  163 VAL A CA  
1306 C  C   . VAL A 162 ? 0.3211 0.1330 0.1485 -0.0206 -0.0153 0.0113  163 VAL A C   
1307 O  O   . VAL A 162 ? 0.3660 0.1425 0.0976 -0.0268 0.0011  0.0171  163 VAL A O   
1308 C  CB  . VAL A 162 ? 0.3594 0.1561 0.2086 -0.0114 -0.0288 0.0163  163 VAL A CB  
1309 C  CG1 . VAL A 162 ? 0.3337 0.1231 0.1966 -0.0214 -0.0233 0.0006  163 VAL A CG1 
1310 C  CG2 . VAL A 162 ? 0.3544 0.2224 0.2344 -0.0133 0.0038  0.0130  163 VAL A CG2 
1311 N  N   . LEU A 163 ? 0.3107 0.1339 0.1480 -0.0418 -0.0483 -0.0074 164 LEU A N   
1312 C  CA  . LEU A 163 ? 0.3006 0.1228 0.1385 -0.0135 0.0034  0.0059  164 LEU A CA  
1313 C  C   . LEU A 163 ? 0.3221 0.1297 0.1334 -0.0187 -0.0073 0.0100  164 LEU A C   
1314 O  O   . LEU A 163 ? 0.3492 0.1493 0.1449 -0.0338 0.0150  0.0015  164 LEU A O   
1315 C  CB  . LEU A 163 ? 0.3022 0.1154 0.1238 -0.0093 -0.0065 0.0023  164 LEU A CB  
1316 C  CG  . LEU A 163 ? 0.2726 0.0936 0.1234 -0.0351 0.0212  0.0243  164 LEU A CG  
1317 C  CD1 . LEU A 163 ? 0.2262 0.0800 0.2013 -0.0089 0.0019  0.0432  164 LEU A CD1 
1318 C  CD2 . LEU A 163 ? 0.2330 0.0933 0.1357 -0.0093 -0.0113 -0.0061 164 LEU A CD2 
1319 N  N   . ASP A 164 ? 0.3557 0.1650 0.1740 -0.0481 0.0079  -0.0153 165 ASP A N   
1320 C  CA  . ASP A 164 ? 0.3865 0.1958 0.1907 -0.0467 -0.0003 -0.0249 165 ASP A CA  
1321 C  C   . ASP A 164 ? 0.3752 0.2054 0.1934 -0.0335 0.0054  0.0021  165 ASP A C   
1322 O  O   . ASP A 164 ? 0.4163 0.2078 0.2689 -0.0192 0.0276  0.0136  165 ASP A O   
1323 C  CB  . ASP A 164 ? 0.3915 0.2150 0.2029 -0.0586 -0.0117 -0.0274 165 ASP A CB  
1324 C  CG  . ASP A 164 ? 0.3757 0.3157 0.2675 -0.0453 -0.0123 -0.0447 165 ASP A CG  
1325 O  OD1 . ASP A 164 ? 0.4429 0.3208 0.2492 -0.0455 -0.0167 -0.0652 165 ASP A OD1 
1326 O  OD2 . ASP A 164 ? 0.5007 0.4471 0.2833 -0.0192 0.0139  -0.0419 165 ASP A OD2 
1327 N  N   . SER A 165 ? 0.3519 0.1944 0.1606 -0.0333 -0.0174 0.0217  166 SER A N   
1328 C  CA  . SER A 165 ? 0.3710 0.2199 0.1772 -0.0356 -0.0011 0.0234  166 SER A CA  
1329 C  C   . SER A 165 ? 0.3465 0.1918 0.1441 -0.0490 0.0000  0.0227  166 SER A C   
1330 O  O   . SER A 165 ? 0.3982 0.1685 0.1670 -0.0609 -0.0092 0.0116  166 SER A O   
1331 C  CB  . SER A 165 ? 0.3931 0.2491 0.2290 -0.0221 0.0131  0.0245  166 SER A CB  
1332 O  OG  . SER A 165 ? 0.4628 0.2219 0.2481 -0.0143 -0.0015 0.0449  166 SER A OG  
1333 N  N   . ILE A 166 ? 0.3319 0.1474 0.1019 -0.0373 -0.0212 0.0254  167 ILE A N   
1334 C  CA  . ILE A 166 ? 0.2904 0.1655 0.1433 -0.0228 0.0026  0.0074  167 ILE A CA  
1335 C  C   . ILE A 166 ? 0.2616 0.1583 0.1340 -0.0212 0.0144  -0.0094 167 ILE A C   
1336 O  O   . ILE A 166 ? 0.2587 0.1606 0.1362 -0.0362 0.0277  0.0123  167 ILE A O   
1337 C  CB  . ILE A 166 ? 0.2940 0.1136 0.1366 -0.0294 0.0049  -0.0010 167 ILE A CB  
1338 C  CG1 . ILE A 166 ? 0.2726 0.1223 0.0856 -0.0406 -0.0075 -0.0015 167 ILE A CG1 
1339 C  CG2 . ILE A 166 ? 0.3066 0.1449 0.1900 -0.0081 -0.0200 -0.0149 167 ILE A CG2 
1340 C  CD1 . ILE A 166 ? 0.2854 0.1366 0.0985 -0.0115 0.0293  -0.0145 167 ILE A CD1 
1341 N  N   . LYS A 167 ? 0.2889 0.1738 0.1477 -0.0127 0.0448  -0.0034 168 LYS A N   
1342 C  CA  . LYS A 167 ? 0.2842 0.1693 0.1598 -0.0106 0.0205  -0.0255 168 LYS A CA  
1343 C  C   . LYS A 167 ? 0.2833 0.1606 0.1450 -0.0442 0.0277  -0.0110 168 LYS A C   
1344 O  O   . LYS A 167 ? 0.2794 0.1183 0.1399 -0.0518 0.0302  -0.0092 168 LYS A O   
1345 C  CB  . LYS A 167 ? 0.3233 0.1296 0.1527 -0.0195 0.0234  -0.0341 168 LYS A CB  
1346 C  CG  . LYS A 167 ? 0.2932 0.1765 0.1896 -0.0217 0.0034  -0.0221 168 LYS A CG  
1347 C  CD  . LYS A 167 ? 0.3431 0.2194 0.2183 0.0121  -0.0002 -0.0446 168 LYS A CD  
1348 C  CE  . LYS A 167 ? 0.4220 0.2860 0.3556 0.0305  0.0010  -0.0271 168 LYS A CE  
1349 N  NZ  . LYS A 167 ? 0.5006 0.4151 0.4117 0.0177  0.0217  -0.0437 168 LYS A NZ  
1350 N  N   . THR A 168 ? 0.2849 0.1560 0.1321 -0.0569 0.0375  0.0094  169 THR A N   
1351 C  CA  . THR A 168 ? 0.2849 0.1733 0.1346 -0.0490 0.0395  -0.0020 169 THR A CA  
1352 C  C   . THR A 168 ? 0.2588 0.1581 0.1300 -0.0444 0.0463  0.0133  169 THR A C   
1353 O  O   . THR A 168 ? 0.3440 0.1455 0.1550 -0.0742 0.0244  0.0052  169 THR A O   
1354 C  CB  . THR A 168 ? 0.2585 0.1879 0.1764 -0.0318 0.0297  0.0000  169 THR A CB  
1355 O  OG1 . THR A 168 ? 0.3697 0.2526 0.1453 -0.0633 0.0466  0.0075  169 THR A OG1 
1356 C  CG2 . THR A 168 ? 0.3151 0.1917 0.1752 -0.0341 0.0470  -0.0264 169 THR A CG2 
1357 N  N   . LYS A 169 ? 0.3112 0.1931 0.1577 -0.0723 0.0460  -0.0116 170 LYS A N   
1358 C  CA  . LYS A 169 ? 0.3140 0.1518 0.1880 -0.0652 0.0253  0.0094  170 LYS A CA  
1359 C  C   . LYS A 169 ? 0.3063 0.1803 0.1944 -0.0496 0.0384  0.0247  170 LYS A C   
1360 O  O   . LYS A 169 ? 0.3763 0.2131 0.1756 -0.0839 0.0612  0.0086  170 LYS A O   
1361 C  CB  . LYS A 169 ? 0.3002 0.1346 0.2090 -0.0428 0.0407  0.0212  170 LYS A CB  
1362 C  CG  . LYS A 169 ? 0.2830 0.2026 0.2306 -0.0472 0.0046  -0.0070 170 LYS A CG  
1363 C  CD  . LYS A 169 ? 0.3088 0.2278 0.2436 -0.0586 0.0051  0.0102  170 LYS A CD  
1364 C  CE  . LYS A 169 ? 0.3296 0.3054 0.3607 -0.0453 -0.0016 -0.0276 170 LYS A CE  
1365 N  NZ  . LYS A 169 ? 0.3867 0.4217 0.4672 -0.0292 -0.0059 -0.0394 170 LYS A NZ  
1366 N  N   . GLY A 170 ? 0.3478 0.1845 0.1904 -0.0778 0.0198  0.0210  171 GLY A N   
1367 C  CA  . GLY A 170 ? 0.3143 0.1646 0.2201 -0.0632 -0.0083 0.0335  171 GLY A CA  
1368 C  C   . GLY A 170 ? 0.3472 0.1775 0.2133 -0.0629 -0.0081 0.0319  171 GLY A C   
1369 O  O   . GLY A 170 ? 0.3507 0.1655 0.2610 -0.0756 -0.0089 0.0270  171 GLY A O   
1370 N  N   . LYS A 171 ? 0.3215 0.1465 0.1715 -0.0769 0.0153  0.0234  172 LYS A N   
1371 C  CA  . LYS A 171 ? 0.3378 0.1875 0.1865 -0.0378 0.0191  0.0077  172 LYS A CA  
1372 C  C   . LYS A 171 ? 0.3455 0.1739 0.1654 -0.0190 0.0135  0.0088  172 LYS A C   
1373 O  O   . LYS A 171 ? 0.3804 0.1537 0.1321 -0.0240 0.0243  0.0104  172 LYS A O   
1374 C  CB  . LYS A 171 ? 0.3168 0.1601 0.1756 -0.0507 0.0156  0.0040  172 LYS A CB  
1375 C  CG  . LYS A 171 ? 0.3719 0.2233 0.2456 -0.0249 0.0074  -0.0624 172 LYS A CG  
1376 C  CD  . LYS A 171 ? 0.3590 0.2394 0.2745 -0.0543 0.0051  -0.0199 172 LYS A CD  
1377 C  CE  . LYS A 171 ? 0.4034 0.3690 0.3537 -0.0213 -0.0178 -0.0024 172 LYS A CE  
1378 N  NZ  . LYS A 171 ? 0.4082 0.3549 0.3865 -0.0367 0.0400  0.0288  172 LYS A NZ  
1379 N  N   A SER A 172 ? 0.3506 0.1574 0.1425 -0.0209 0.0154  0.0020  173 SER A N   
1380 N  N   B SER A 172 ? 0.3399 0.1526 0.1392 -0.0176 0.0133  0.0057  173 SER A N   
1381 C  CA  A SER A 172 ? 0.3495 0.1454 0.1627 -0.0163 0.0148  0.0089  173 SER A CA  
1382 C  CA  B SER A 172 ? 0.3248 0.1310 0.1607 -0.0110 0.0080  0.0167  173 SER A CA  
1383 C  C   A SER A 172 ? 0.3640 0.1500 0.1417 -0.0025 0.0147  0.0101  173 SER A C   
1384 C  C   B SER A 172 ? 0.3479 0.1464 0.1383 0.0044  0.0113  0.0207  173 SER A C   
1385 O  O   A SER A 172 ? 0.3932 0.1768 0.1214 0.0091  0.0249  -0.0004 173 SER A O   
1386 O  O   B SER A 172 ? 0.3702 0.1735 0.1367 0.0251  0.0190  0.0074  173 SER A O   
1387 C  CB  A SER A 172 ? 0.3490 0.1522 0.1274 -0.0314 0.0253  -0.0006 173 SER A CB  
1388 C  CB  B SER A 172 ? 0.3203 0.1401 0.1127 -0.0135 0.0173  0.0152  173 SER A CB  
1389 O  OG  A SER A 172 ? 0.3372 0.1469 0.1749 -0.0171 0.0276  0.0465  173 SER A OG  
1390 O  OG  B SER A 172 ? 0.2274 0.1095 0.1578 0.0070  -0.0195 0.0902  173 SER A OG  
1391 N  N   . ALA A 173 ? 0.3658 0.1816 0.1621 0.0205  -0.0065 0.0114  174 ALA A N   
1392 C  CA  . ALA A 173 ? 0.3727 0.2123 0.1366 0.0531  -0.0113 0.0163  174 ALA A CA  
1393 C  C   . ALA A 173 ? 0.3833 0.2187 0.1544 0.0711  -0.0195 0.0256  174 ALA A C   
1394 O  O   . ALA A 173 ? 0.4298 0.1927 0.1209 0.0846  -0.0210 0.0384  174 ALA A O   
1395 C  CB  . ALA A 173 ? 0.3696 0.2295 0.1179 0.0428  -0.0325 0.0140  174 ALA A CB  
1396 N  N   . ASP A 174 ? 0.4000 0.2475 0.1853 0.0685  -0.0441 0.0474  175 ASP A N   
1397 C  CA  . ASP A 174 ? 0.3924 0.2391 0.1954 0.0474  -0.0332 0.0430  175 ASP A CA  
1398 C  C   . ASP A 174 ? 0.3947 0.2255 0.1718 0.0402  -0.0513 0.0354  175 ASP A C   
1399 O  O   . ASP A 174 ? 0.4315 0.1990 0.1807 0.0609  -0.0497 0.0050  175 ASP A O   
1400 C  CB  . ASP A 174 ? 0.3920 0.2904 0.2458 0.0628  -0.0334 0.0576  175 ASP A CB  
1401 C  CG  . ASP A 174 ? 0.4319 0.3477 0.3556 0.0017  -0.0222 0.0249  175 ASP A CG  
1402 O  OD1 . ASP A 174 ? 0.4033 0.4680 0.3705 0.0126  -0.0930 -0.0084 175 ASP A OD1 
1403 O  OD2 . ASP A 174 ? 0.4625 0.4322 0.3610 -0.0142 -0.0349 0.0289  175 ASP A OD2 
1404 N  N   . PHE A 175 ? 0.3678 0.1808 0.1346 0.0265  -0.0421 0.0141  176 PHE A N   
1405 C  CA  . PHE A 175 ? 0.3447 0.1562 0.1170 0.0229  -0.0658 0.0223  176 PHE A CA  
1406 C  C   . PHE A 175 ? 0.3293 0.1402 0.1390 0.0065  -0.0704 0.0210  176 PHE A C   
1407 O  O   . PHE A 175 ? 0.3639 0.1887 0.1527 0.0697  -0.0837 0.0311  176 PHE A O   
1408 C  CB  . PHE A 175 ? 0.3364 0.1085 0.1171 0.0078  -0.0647 0.0128  176 PHE A CB  
1409 C  CG  . PHE A 175 ? 0.3176 0.0783 0.1724 0.0131  -0.0384 0.0102  176 PHE A CG  
1410 C  CD1 . PHE A 175 ? 0.3246 0.1468 0.1205 -0.0141 -0.0513 -0.0049 176 PHE A CD1 
1411 C  CD2 . PHE A 175 ? 0.3486 0.1112 0.1685 0.0179  -0.0470 0.0229  176 PHE A CD2 
1412 C  CE1 . PHE A 175 ? 0.3356 0.0965 0.1606 -0.0046 -0.0096 -0.0138 176 PHE A CE1 
1413 C  CE2 . PHE A 175 ? 0.3739 0.1119 0.1989 0.0380  -0.0590 0.0312  176 PHE A CE2 
1414 C  CZ  . PHE A 175 ? 0.3220 0.1127 0.1867 0.0053  -0.0582 0.0158  176 PHE A CZ  
1415 N  N   . THR A 176 ? 0.2935 0.1274 0.1593 0.0171  -0.0663 0.0454  177 THR A N   
1416 C  CA  . THR A 176 ? 0.3140 0.1593 0.1616 0.0116  -0.0767 0.0413  177 THR A CA  
1417 C  C   . THR A 176 ? 0.2978 0.1389 0.1209 0.0079  -0.0808 0.0475  177 THR A C   
1418 O  O   . THR A 176 ? 0.3360 0.1394 0.1399 -0.0078 -0.0708 0.0245  177 THR A O   
1419 C  CB  . THR A 176 ? 0.3276 0.1458 0.1545 0.0034  -0.0700 0.0553  177 THR A CB  
1420 O  OG1 . THR A 176 ? 0.3936 0.1891 0.1808 0.0422  -0.0902 0.0553  177 THR A OG1 
1421 C  CG2 . THR A 176 ? 0.3135 0.2385 0.2311 0.0088  -0.0646 0.0666  177 THR A CG2 
1422 N  N   . ASN A 177 ? 0.2974 0.1164 0.1337 0.0073  -0.0902 0.0489  178 ASN A N   
1423 C  CA  . ASN A 177 ? 0.3050 0.1243 0.1618 0.0156  -0.0819 0.0391  178 ASN A CA  
1424 C  C   . ASN A 177 ? 0.2916 0.1081 0.1748 -0.0014 -0.0791 0.0577  178 ASN A C   
1425 O  O   . ASN A 177 ? 0.3263 0.1590 0.2272 0.0067  -0.1054 0.0712  178 ASN A O   
1426 C  CB  . ASN A 177 ? 0.2963 0.1270 0.1975 0.0118  -0.0812 0.0557  178 ASN A CB  
1427 C  CG  . ASN A 177 ? 0.2862 0.1682 0.2036 0.0291  -0.0593 0.0315  178 ASN A CG  
1428 O  OD1 . ASN A 177 ? 0.3633 0.1552 0.2752 0.0270  -0.0444 0.0003  178 ASN A OD1 
1429 N  ND2 . ASN A 177 ? 0.2934 0.1136 0.2063 0.0061  -0.0538 0.0336  178 ASN A ND2 
1430 N  N   . PHE A 178 ? 0.3031 0.0863 0.1247 0.0098  -0.0802 0.0377  179 PHE A N   
1431 C  CA  . PHE A 178 ? 0.2701 0.1062 0.1596 -0.0006 -0.0605 0.0368  179 PHE A CA  
1432 C  C   . PHE A 178 ? 0.2647 0.0964 0.1527 0.0072  -0.0690 0.0355  179 PHE A C   
1433 O  O   . PHE A 178 ? 0.2744 0.1305 0.1353 -0.0050 -0.0977 0.0146  179 PHE A O   
1434 C  CB  . PHE A 178 ? 0.2619 0.0584 0.1203 0.0345  -0.0611 0.0343  179 PHE A CB  
1435 C  CG  . PHE A 178 ? 0.2533 0.0615 0.1311 -0.0301 -0.0415 0.0352  179 PHE A CG  
1436 C  CD1 . PHE A 178 ? 0.3239 0.1001 0.1605 -0.0025 -0.0544 0.0036  179 PHE A CD1 
1437 C  CD2 . PHE A 178 ? 0.2563 0.0724 0.1267 -0.0129 -0.0476 0.0029  179 PHE A CD2 
1438 C  CE1 . PHE A 178 ? 0.3132 0.0984 0.1783 -0.0191 -0.0452 0.0197  179 PHE A CE1 
1439 C  CE2 . PHE A 178 ? 0.2560 0.0861 0.1240 0.0222  -0.0551 0.0281  179 PHE A CE2 
1440 C  CZ  . PHE A 178 ? 0.2964 0.0952 0.1442 0.0170  -0.0262 0.0106  179 PHE A CZ  
1441 N  N   . ASP A 179 ? 0.2432 0.1122 0.1480 0.0021  -0.0746 0.0212  180 ASP A N   
1442 C  CA  . ASP A 179 ? 0.2093 0.1125 0.1717 0.0165  -0.0585 0.0286  180 ASP A CA  
1443 C  C   . ASP A 179 ? 0.2057 0.1009 0.1501 -0.0012 -0.0527 0.0181  180 ASP A C   
1444 O  O   . ASP A 179 ? 0.2052 0.0903 0.1635 -0.0131 -0.0490 0.0043  180 ASP A O   
1445 C  CB  . ASP A 179 ? 0.2260 0.1656 0.2095 0.0158  -0.0679 0.0382  180 ASP A CB  
1446 C  CG  . ASP A 179 ? 0.2339 0.1990 0.2409 0.0014  -0.0342 0.0415  180 ASP A CG  
1447 O  OD1 . ASP A 179 ? 0.2373 0.1297 0.2304 0.0471  -0.0848 0.0256  180 ASP A OD1 
1448 O  OD2 . ASP A 179 ? 0.2646 0.3667 0.2885 0.0100  -0.0795 -0.0099 180 ASP A OD2 
1449 N  N   . PRO A 180 ? 0.1732 0.0818 0.1472 -0.0009 -0.0657 0.0125  181 PRO A N   
1450 C  CA  . PRO A 180 ? 0.1527 0.1183 0.1406 -0.0020 -0.0567 0.0098  181 PRO A CA  
1451 C  C   . PRO A 180 ? 0.1461 0.1096 0.1427 -0.0021 -0.0529 0.0046  181 PRO A C   
1452 O  O   . PRO A 180 ? 0.1494 0.1069 0.1330 -0.0037 -0.0646 0.0103  181 PRO A O   
1453 C  CB  . PRO A 180 ? 0.1548 0.1253 0.1729 -0.0083 -0.0657 0.0104  181 PRO A CB  
1454 C  CG  . PRO A 180 ? 0.1604 0.1261 0.1707 -0.0458 -0.0792 0.0103  181 PRO A CG  
1455 C  CD  . PRO A 180 ? 0.1957 0.0940 0.1633 0.0023  -0.0559 -0.0057 181 PRO A CD  
1456 N  N   . ARG A 181 ? 0.1147 0.1003 0.1273 0.0036  -0.0417 0.0040  182 ARG A N   
1457 C  CA  . ARG A 181 ? 0.1391 0.1016 0.1734 0.0034  -0.0399 -0.0032 182 ARG A CA  
1458 C  C   . ARG A 181 ? 0.1663 0.1036 0.1550 -0.0019 -0.0556 0.0005  182 ARG A C   
1459 O  O   . ARG A 181 ? 0.2005 0.1714 0.1720 0.0079  -0.0541 0.0357  182 ARG A O   
1460 C  CB  . ARG A 181 ? 0.1278 0.1224 0.1971 0.0156  -0.0397 -0.0067 182 ARG A CB  
1461 C  CG  . ARG A 181 ? 0.1680 0.1108 0.2687 0.0211  -0.0103 0.0082  182 ARG A CG  
1462 C  CD  . ARG A 181 ? 0.1922 0.1506 0.3034 0.0332  0.0061  0.0010  182 ARG A CD  
1463 N  NE  . ARG A 181 ? 0.1638 0.1130 0.3301 0.0428  -0.0283 0.0532  182 ARG A NE  
1464 C  CZ  . ARG A 181 ? 0.1520 0.2294 0.3332 0.0146  -0.0213 0.0282  182 ARG A CZ  
1465 N  NH1 . ARG A 181 ? 0.2531 0.2233 0.3864 0.0113  -0.0112 0.0220  182 ARG A NH1 
1466 N  NH2 . ARG A 181 ? 0.1484 0.2993 0.3782 0.0239  -0.0260 0.0525  182 ARG A NH2 
1467 N  N   . GLY A 182 ? 0.1828 0.0953 0.1399 0.0010  -0.0724 -0.0006 183 GLY A N   
1468 C  CA  . GLY A 182 ? 0.1856 0.0793 0.1759 0.0079  -0.0940 0.0054  183 GLY A CA  
1469 C  C   . GLY A 182 ? 0.1971 0.1055 0.1874 0.0109  -0.0662 0.0069  183 GLY A C   
1470 O  O   . GLY A 182 ? 0.2531 0.0909 0.2187 0.0145  -0.0941 -0.0070 183 GLY A O   
1471 N  N   . LEU A 183 ? 0.1468 0.0959 0.1406 0.0220  -0.0768 0.0105  184 LEU A N   
1472 C  CA  . LEU A 183 ? 0.1727 0.1060 0.1538 0.0135  -0.0425 0.0030  184 LEU A CA  
1473 C  C   . LEU A 183 ? 0.1672 0.0994 0.1401 0.0015  -0.0343 0.0004  184 LEU A C   
1474 O  O   . LEU A 183 ? 0.1749 0.0904 0.1961 0.0374  -0.0246 0.0158  184 LEU A O   
1475 C  CB  . LEU A 183 ? 0.1739 0.0976 0.1682 -0.0111 -0.0263 0.0136  184 LEU A CB  
1476 C  CG  . LEU A 183 ? 0.1615 0.0747 0.1831 0.0019  -0.0025 0.0237  184 LEU A CG  
1477 C  CD1 . LEU A 183 ? 0.1503 0.1625 0.1763 0.0113  0.0095  0.0478  184 LEU A CD1 
1478 C  CD2 . LEU A 183 ? 0.2787 0.1518 0.1642 0.0259  -0.0274 0.0007  184 LEU A CD2 
1479 N  N   . LEU A 184 ? 0.1492 0.0689 0.1446 0.0077  -0.0452 -0.0058 185 LEU A N   
1480 C  CA  . LEU A 184 ? 0.1599 0.1035 0.1573 -0.0164 -0.0425 0.0078  185 LEU A CA  
1481 C  C   . LEU A 184 ? 0.1942 0.1302 0.1450 -0.0380 -0.0688 0.0108  185 LEU A C   
1482 O  O   . LEU A 184 ? 0.2287 0.1807 0.2037 -0.0724 -0.1007 0.0584  185 LEU A O   
1483 C  CB  . LEU A 184 ? 0.1293 0.0887 0.1792 -0.0157 -0.0369 -0.0117 185 LEU A CB  
1484 C  CG  . LEU A 184 ? 0.1124 0.0854 0.1840 -0.0115 -0.0605 -0.0214 185 LEU A CG  
1485 C  CD1 . LEU A 184 ? 0.1296 0.1396 0.1746 -0.0085 -0.0222 -0.0053 185 LEU A CD1 
1486 C  CD2 . LEU A 184 ? 0.0919 0.1327 0.1707 0.0013  -0.0456 0.0178  185 LEU A CD2 
1487 N  N   . PRO A 185 ? 0.1360 0.1178 0.1709 -0.0236 -0.0518 0.0269  186 PRO A N   
1488 C  CA  . PRO A 185 ? 0.1316 0.1018 0.1627 -0.0257 -0.0452 0.0216  186 PRO A CA  
1489 C  C   . PRO A 185 ? 0.1196 0.1150 0.1996 -0.0325 -0.0351 0.0423  186 PRO A C   
1490 O  O   . PRO A 185 ? 0.0982 0.0920 0.3019 -0.0169 -0.0294 0.0471  186 PRO A O   
1491 C  CB  . PRO A 185 ? 0.0630 0.1032 0.1671 0.0029  -0.0385 0.0178  186 PRO A CB  
1492 C  CG  . PRO A 185 ? 0.1094 0.1063 0.1458 0.0115  -0.0266 -0.0028 186 PRO A CG  
1493 C  CD  . PRO A 185 ? 0.1095 0.0939 0.1286 -0.0064 -0.0692 -0.0027 186 PRO A CD  
1494 N  N   A GLU A 186 ? 0.1114 0.1281 0.1968 -0.0350 -0.0162 0.0353  187 GLU A N   
1495 N  N   B GLU A 186 ? 0.1140 0.1349 0.2041 -0.0384 -0.0152 0.0338  187 GLU A N   
1496 C  CA  A GLU A 186 ? 0.1187 0.1351 0.2192 -0.0333 -0.0152 0.0322  187 GLU A CA  
1497 C  CA  B GLU A 186 ? 0.1221 0.1473 0.2269 -0.0396 -0.0149 0.0285  187 GLU A CA  
1498 C  C   A GLU A 186 ? 0.1117 0.1339 0.2444 -0.0276 -0.0120 0.0254  187 GLU A C   
1499 C  C   B GLU A 186 ? 0.1060 0.1368 0.2441 -0.0370 -0.0055 0.0264  187 GLU A C   
1500 O  O   A GLU A 186 ? 0.1163 0.1275 0.2549 -0.0193 -0.0049 0.0287  187 GLU A O   
1501 O  O   B GLU A 186 ? 0.0980 0.1389 0.2938 -0.0368 0.0035  0.0386  187 GLU A O   
1502 C  CB  A GLU A 186 ? 0.1242 0.1291 0.2321 -0.0226 -0.0303 0.0339  187 GLU A CB  
1503 C  CB  B GLU A 186 ? 0.1235 0.1569 0.2357 -0.0328 -0.0292 0.0247  187 GLU A CB  
1504 C  CG  A GLU A 186 ? 0.1274 0.1551 0.2225 -0.0264 -0.0147 0.0293  187 GLU A CG  
1505 C  CG  B GLU A 186 ? 0.1781 0.1786 0.2421 -0.0572 -0.0301 0.0026  187 GLU A CG  
1506 C  CD  A GLU A 186 ? 0.1297 0.1556 0.2388 -0.0012 0.0037  0.0390  187 GLU A CD  
1507 C  CD  B GLU A 186 ? 0.2215 0.1955 0.2782 -0.0527 0.0037  0.0102  187 GLU A CD  
1508 O  OE1 A GLU A 186 ? 0.1081 0.2044 0.2677 -0.0299 -0.0259 0.0307  187 GLU A OE1 
1509 O  OE1 B GLU A 186 ? 0.2307 0.2056 0.3152 -0.0686 -0.0260 0.0031  187 GLU A OE1 
1510 O  OE2 A GLU A 186 ? 0.1608 0.2356 0.2669 0.0161  0.0202  0.0649  187 GLU A OE2 
1511 O  OE2 B GLU A 186 ? 0.2841 0.2740 0.2924 -0.0003 -0.0218 -0.0041 187 GLU A OE2 
1512 N  N   . SER A 187 ? 0.0817 0.1425 0.2440 -0.0358 -0.0228 0.0236  188 SER A N   
1513 C  CA  . SER A 187 ? 0.0826 0.1485 0.2442 -0.0090 -0.0161 0.0320  188 SER A CA  
1514 C  C   . SER A 187 ? 0.0831 0.1232 0.2477 -0.0156 0.0041  0.0115  188 SER A C   
1515 O  O   . SER A 187 ? 0.0734 0.1490 0.2665 0.0074  -0.0199 -0.0081 188 SER A O   
1516 C  CB  . SER A 187 ? 0.1271 0.1561 0.2448 -0.0015 0.0089  0.0416  188 SER A CB  
1517 O  OG  . SER A 187 ? 0.1533 0.1233 0.2616 -0.0193 -0.0161 0.0268  188 SER A OG  
1518 N  N   . LEU A 188 ? 0.0893 0.1140 0.2401 -0.0234 -0.0139 -0.0075 189 LEU A N   
1519 C  CA  . LEU A 188 ? 0.0773 0.1161 0.2183 -0.0082 -0.0151 -0.0030 189 LEU A CA  
1520 C  C   . LEU A 188 ? 0.0707 0.1240 0.1945 -0.0083 0.0058  -0.0110 189 LEU A C   
1521 O  O   . LEU A 188 ? 0.1190 0.1313 0.2279 -0.0116 -0.0248 -0.0418 189 LEU A O   
1522 C  CB  . LEU A 188 ? 0.0990 0.0873 0.2359 -0.0290 -0.0126 0.0127  189 LEU A CB  
1523 C  CG  . LEU A 188 ? 0.1424 0.1663 0.2397 0.0118  -0.0081 -0.0036 189 LEU A CG  
1524 C  CD1 . LEU A 188 ? 0.1500 0.1500 0.2698 0.0050  0.0205  -0.0144 189 LEU A CD1 
1525 C  CD2 . LEU A 188 ? 0.0803 0.1788 0.2439 -0.0166 -0.0183 0.0155  189 LEU A CD2 
1526 N  N   . ASP A 189 ? 0.1017 0.1595 0.1754 0.0042  0.0168  -0.0121 190 ASP A N   
1527 C  CA  . ASP A 189 ? 0.1144 0.1616 0.1763 -0.0033 0.0148  -0.0013 190 ASP A CA  
1528 C  C   . ASP A 189 ? 0.1106 0.1051 0.1508 -0.0003 0.0031  0.0066  190 ASP A C   
1529 O  O   . ASP A 189 ? 0.1020 0.1317 0.1484 0.0082  0.0077  -0.0213 190 ASP A O   
1530 C  CB  . ASP A 189 ? 0.1345 0.1520 0.1713 0.0011  0.0434  -0.0084 190 ASP A CB  
1531 C  CG  . ASP A 189 ? 0.1964 0.2426 0.2234 -0.0241 0.0234  0.0060  190 ASP A CG  
1532 O  OD1 . ASP A 189 ? 0.1390 0.3536 0.2676 -0.0244 0.0666  -0.0317 190 ASP A OD1 
1533 O  OD2 . ASP A 189 ? 0.2077 0.3772 0.2904 -0.0737 0.0285  0.0619  190 ASP A OD2 
1534 N  N   . TYR A 190 ? 0.0720 0.1298 0.1260 -0.0114 -0.0059 -0.0032 191 TYR A N   
1535 C  CA  . TYR A 190 ? 0.0794 0.1158 0.1280 -0.0346 -0.0104 -0.0101 191 TYR A CA  
1536 C  C   . TYR A 190 ? 0.1077 0.1300 0.1064 -0.0172 0.0057  0.0015  191 TYR A C   
1537 O  O   . TYR A 190 ? 0.0947 0.1477 0.1312 -0.0227 0.0186  0.0041  191 TYR A O   
1538 C  CB  . TYR A 190 ? 0.1316 0.1113 0.1114 -0.0224 -0.0109 0.0007  191 TYR A CB  
1539 C  CG  . TYR A 190 ? 0.1000 0.0874 0.1219 -0.0044 0.0021  0.0294  191 TYR A CG  
1540 C  CD1 . TYR A 190 ? 0.1086 0.0983 0.1235 -0.0138 0.0079  -0.0103 191 TYR A CD1 
1541 C  CD2 . TYR A 190 ? 0.0740 0.1293 0.1660 0.0205  0.0169  0.0059  191 TYR A CD2 
1542 C  CE1 . TYR A 190 ? 0.1522 0.1017 0.1326 0.0220  -0.0017 0.0057  191 TYR A CE1 
1543 C  CE2 . TYR A 190 ? 0.1236 0.1218 0.1765 0.0028  -0.0098 -0.0334 191 TYR A CE2 
1544 C  CZ  . TYR A 190 ? 0.1671 0.1116 0.1594 -0.0029 -0.0049 -0.0179 191 TYR A CZ  
1545 O  OH  . TYR A 190 ? 0.1594 0.1671 0.1635 0.0030  0.0092  -0.0152 191 TYR A OH  
1546 N  N   . TRP A 191 ? 0.0808 0.0829 0.1190 -0.0299 -0.0127 -0.0040 192 TRP A N   
1547 C  CA  . TRP A 191 ? 0.0386 0.0611 0.1316 -0.0171 -0.0052 0.0139  192 TRP A CA  
1548 C  C   . TRP A 191 ? 0.0746 0.0637 0.1152 0.0075  -0.0118 -0.0010 192 TRP A C   
1549 O  O   . TRP A 191 ? 0.1208 0.0865 0.0957 -0.0084 -0.0233 -0.0086 192 TRP A O   
1550 C  CB  . TRP A 191 ? 0.0903 0.0898 0.1340 0.0052  -0.0085 0.0337  192 TRP A CB  
1551 C  CG  . TRP A 191 ? 0.1073 0.0655 0.1213 0.0014  -0.0176 0.0223  192 TRP A CG  
1552 C  CD1 . TRP A 191 ? 0.1211 0.0694 0.1653 0.0052  0.0172  0.0035  192 TRP A CD1 
1553 C  CD2 . TRP A 191 ? 0.1040 0.1174 0.1169 0.0095  -0.0001 0.0058  192 TRP A CD2 
1554 N  NE1 . TRP A 191 ? 0.1470 0.0693 0.1134 0.0070  0.0118  0.0090  192 TRP A NE1 
1555 C  CE2 . TRP A 191 ? 0.1192 0.1078 0.1321 0.0096  -0.0090 -0.0197 192 TRP A CE2 
1556 C  CE3 . TRP A 191 ? 0.1026 0.0990 0.1319 -0.0036 0.0048  0.0075  192 TRP A CE3 
1557 C  CZ2 . TRP A 191 ? 0.1345 0.1019 0.1458 -0.0054 0.0006  0.0123  192 TRP A CZ2 
1558 C  CZ3 . TRP A 191 ? 0.1147 0.0699 0.1293 -0.0140 0.0066  0.0071  192 TRP A CZ3 
1559 C  CH2 . TRP A 191 ? 0.1198 0.0717 0.1691 0.0181  -0.0112 0.0244  192 TRP A CH2 
1560 N  N   . THR A 192 ? 0.0985 0.0631 0.0897 -0.0233 -0.0257 0.0032  193 THR A N   
1561 C  CA  . THR A 192 ? 0.0795 0.0457 0.0927 -0.0118 -0.0226 -0.0030 193 THR A CA  
1562 C  C   . THR A 192 ? 0.1001 0.0874 0.0965 -0.0240 -0.0205 0.0028  193 THR A C   
1563 O  O   . THR A 192 ? 0.1206 0.1225 0.0857 -0.0124 0.0211  0.0219  193 THR A O   
1564 C  CB  . THR A 192 ? 0.0956 0.0739 0.1118 0.0086  -0.0115 -0.0026 193 THR A CB  
1565 O  OG1 . THR A 192 ? 0.1104 0.0501 0.1596 -0.0027 -0.0024 -0.0020 193 THR A OG1 
1566 C  CG2 . THR A 192 ? 0.1397 0.1342 0.0940 0.0038  0.0490  0.0103  193 THR A CG2 
1567 N  N   . TYR A 193 ? 0.0989 0.0740 0.1094 -0.0349 -0.0148 0.0044  194 TYR A N   
1568 C  CA  . TYR A 193 ? 0.0568 0.0840 0.0890 -0.0182 -0.0044 0.0157  194 TYR A CA  
1569 C  C   . TYR A 193 ? 0.0946 0.0745 0.0976 -0.0060 0.0056  -0.0082 194 TYR A C   
1570 O  O   . TYR A 193 ? 0.1017 0.1008 0.0779 -0.0047 0.0070  -0.0058 194 TYR A O   
1571 C  CB  . TYR A 193 ? 0.0906 0.0839 0.0984 0.0287  0.0105  -0.0198 194 TYR A CB  
1572 C  CG  . TYR A 193 ? 0.0991 0.0631 0.0864 -0.0072 0.0130  -0.0026 194 TYR A CG  
1573 C  CD1 . TYR A 193 ? 0.0959 0.0543 0.1032 0.0286  -0.0131 -0.0149 194 TYR A CD1 
1574 C  CD2 . TYR A 193 ? 0.0777 0.0412 0.1346 0.0012  0.0209  -0.0191 194 TYR A CD2 
1575 C  CE1 . TYR A 193 ? 0.0723 0.0422 0.1194 -0.0035 0.0324  -0.0085 194 TYR A CE1 
1576 C  CE2 . TYR A 193 ? 0.1339 0.0591 0.0791 0.0492  -0.0099 -0.0291 194 TYR A CE2 
1577 C  CZ  . TYR A 193 ? 0.0757 0.0524 0.0824 0.0008  -0.0026 0.0030  194 TYR A CZ  
1578 O  OH  . TYR A 193 ? 0.1010 0.0616 0.1019 0.0057  -0.0042 -0.0063 194 TYR A OH  
1579 N  N   . PRO A 194 ? 0.0802 0.0877 0.0763 0.0012  -0.0147 -0.0226 195 PRO A N   
1580 C  CA  . PRO A 194 ? 0.0830 0.0737 0.0682 -0.0052 0.0188  -0.0379 195 PRO A CA  
1581 C  C   . PRO A 194 ? 0.0779 0.0404 0.1072 -0.0174 0.0088  -0.0172 195 PRO A C   
1582 O  O   . PRO A 194 ? 0.0929 0.0703 0.1112 0.0171  -0.0097 -0.0099 195 PRO A O   
1583 C  CB  . PRO A 194 ? 0.1385 0.0763 0.0991 -0.0060 0.0034  -0.0253 195 PRO A CB  
1584 C  CG  . PRO A 194 ? 0.1324 0.1156 0.0981 -0.0219 -0.0171 -0.0042 195 PRO A CG  
1585 C  CD  . PRO A 194 ? 0.1311 0.1091 0.0614 -0.0229 -0.0071 -0.0029 195 PRO A CD  
1586 N  N   . GLY A 195 ? 0.0725 0.0702 0.0595 -0.0062 0.0237  -0.0320 196 GLY A N   
1587 C  CA  . GLY A 195 ? 0.1013 0.0754 0.0523 -0.0083 0.0229  -0.0106 196 GLY A CA  
1588 C  C   . GLY A 195 ? 0.0580 0.0774 0.0786 -0.0129 0.0108  -0.0202 196 GLY A C   
1589 O  O   . GLY A 195 ? 0.0842 0.0438 0.1029 0.0115  -0.0096 -0.0017 196 GLY A O   
1590 N  N   . SER A 196 ? 0.0966 0.0783 0.0775 0.0015  -0.0070 -0.0384 197 SER A N   
1591 C  CA  . SER A 196 ? 0.0780 0.0605 0.0926 0.0090  -0.0038 -0.0234 197 SER A CA  
1592 C  C   . SER A 196 ? 0.0643 0.0807 0.0808 0.0108  -0.0113 -0.0061 197 SER A C   
1593 O  O   . SER A 196 ? 0.0860 0.0680 0.0889 0.0010  0.0000  -0.0214 197 SER A O   
1594 C  CB  . SER A 196 ? 0.0991 0.1033 0.1377 0.0216  -0.0147 -0.0308 197 SER A CB  
1595 O  OG  . SER A 196 ? 0.0832 0.0852 0.1285 0.0252  -0.0043 -0.0285 197 SER A OG  
1596 N  N   . LEU A 197 ? 0.0778 0.0838 0.0799 0.0119  0.0006  -0.0115 198 LEU A N   
1597 C  CA  . LEU A 197 ? 0.0714 0.0680 0.0906 0.0043  0.0127  -0.0087 198 LEU A CA  
1598 C  C   . LEU A 197 ? 0.0822 0.0880 0.0876 -0.0055 0.0030  -0.0100 198 LEU A C   
1599 O  O   . LEU A 197 ? 0.0921 0.0579 0.1212 -0.0171 -0.0213 -0.0076 198 LEU A O   
1600 C  CB  . LEU A 197 ? 0.1442 0.0767 0.1499 0.0132  0.0112  0.0161  198 LEU A CB  
1601 C  CG  . LEU A 197 ? 0.2101 0.0931 0.1616 0.0079  0.0032  0.0037  198 LEU A CG  
1602 C  CD1 . LEU A 197 ? 0.2917 0.0768 0.2000 -0.0199 0.0115  0.0285  198 LEU A CD1 
1603 C  CD2 . LEU A 197 ? 0.1309 0.2037 0.2404 0.0470  0.0162  0.0433  198 LEU A CD2 
1604 N  N   . THR A 198 ? 0.0880 0.0578 0.1271 0.0090  -0.0108 -0.0174 199 THR A N   
1605 C  CA  . THR A 198 ? 0.0809 0.0552 0.1224 -0.0066 0.0000  -0.0318 199 THR A CA  
1606 C  C   . THR A 198 ? 0.1098 0.0801 0.1389 -0.0036 0.0000  -0.0196 199 THR A C   
1607 O  O   . THR A 198 ? 0.0742 0.1038 0.1390 -0.0073 0.0115  -0.0366 199 THR A O   
1608 C  CB  . THR A 198 ? 0.0910 0.0550 0.1050 -0.0137 -0.0214 -0.0275 199 THR A CB  
1609 O  OG1 . THR A 198 ? 0.0773 0.0879 0.1074 -0.0078 -0.0226 -0.0115 199 THR A OG1 
1610 C  CG2 . THR A 198 ? 0.0338 0.1038 0.1165 -0.0095 0.0209  -0.0016 199 THR A CG2 
1611 N  N   . THR A 199 ? 0.1073 0.1016 0.1196 -0.0210 0.0085  -0.0044 200 THR A N   
1612 C  CA  . THR A 199 ? 0.1364 0.0812 0.1416 -0.0437 -0.0126 -0.0079 200 THR A CA  
1613 C  C   . THR A 199 ? 0.0989 0.1131 0.1557 -0.0321 0.0046  -0.0057 200 THR A C   
1614 O  O   . THR A 199 ? 0.0915 0.1014 0.1637 -0.0269 0.0131  -0.0367 200 THR A O   
1615 C  CB  . THR A 199 ? 0.1517 0.0732 0.1698 -0.0386 -0.0094 0.0118  200 THR A CB  
1616 O  OG1 . THR A 199 ? 0.2414 0.0995 0.2359 -0.0102 -0.0659 -0.0005 200 THR A OG1 
1617 C  CG2 . THR A 199 ? 0.1731 0.0582 0.1928 -0.0605 -0.0270 -0.0252 200 THR A CG2 
1618 N  N   . PRO A 200 ? 0.0839 0.1215 0.1487 -0.0323 0.0140  -0.0242 201 PRO A N   
1619 C  CA  . PRO A 200 ? 0.1076 0.1171 0.1626 -0.0454 0.0258  -0.0084 201 PRO A CA  
1620 C  C   . PRO A 200 ? 0.1243 0.0949 0.1486 -0.0385 0.0230  -0.0179 201 PRO A C   
1621 O  O   . PRO A 200 ? 0.1558 0.1096 0.1638 -0.0062 0.0055  -0.0327 201 PRO A O   
1622 C  CB  . PRO A 200 ? 0.1128 0.1257 0.1815 -0.0370 0.0211  -0.0191 201 PRO A CB  
1623 C  CG  . PRO A 200 ? 0.1191 0.1522 0.1716 -0.0221 0.0090  -0.0199 201 PRO A CG  
1624 C  CD  . PRO A 200 ? 0.1051 0.1338 0.1552 -0.0302 0.0351  -0.0296 201 PRO A CD  
1625 N  N   . PRO A 201 ? 0.1478 0.1073 0.1438 -0.0222 0.0102  -0.0124 202 PRO A N   
1626 C  CA  . PRO A 201 ? 0.1602 0.0884 0.1500 -0.0226 0.0057  -0.0101 202 PRO A CA  
1627 C  C   . PRO A 201 ? 0.1209 0.0926 0.1311 -0.0078 0.0174  -0.0215 202 PRO A C   
1628 O  O   . PRO A 201 ? 0.1072 0.0816 0.1740 -0.0208 0.0153  -0.0388 202 PRO A O   
1629 C  CB  . PRO A 201 ? 0.1870 0.0867 0.1646 -0.0396 0.0000  -0.0015 202 PRO A CB  
1630 C  CG  . PRO A 201 ? 0.2290 0.0837 0.2054 -0.0322 -0.0253 -0.0098 202 PRO A CG  
1631 C  CD  . PRO A 201 ? 0.1626 0.0792 0.1509 -0.0148 -0.0104 -0.0190 202 PRO A CD  
1632 N  N   . LEU A 202 ? 0.0780 0.0891 0.1433 -0.0036 0.0096  -0.0117 203 LEU A N   
1633 C  CA  . LEU A 202 ? 0.0686 0.0739 0.1420 0.0138  0.0034  -0.0130 203 LEU A CA  
1634 C  C   . LEU A 202 ? 0.0660 0.0740 0.1546 -0.0079 -0.0076 -0.0239 203 LEU A C   
1635 O  O   . LEU A 202 ? 0.0755 0.0816 0.1656 0.0036  -0.0198 -0.0264 203 LEU A O   
1636 C  CB  . LEU A 202 ? 0.0699 0.0941 0.1720 0.0238  -0.0063 -0.0460 203 LEU A CB  
1637 C  CG  . LEU A 202 ? 0.0594 0.0628 0.1548 -0.0093 0.0304  -0.0368 203 LEU A CG  
1638 C  CD1 . LEU A 202 ? 0.0583 0.1514 0.2499 0.0139  -0.0215 -0.0069 203 LEU A CD1 
1639 C  CD2 . LEU A 202 ? 0.0576 0.0908 0.2043 -0.0322 0.0230  -0.0393 203 LEU A CD2 
1640 N  N   . LEU A 203 ? 0.0690 0.0602 0.1427 0.0049  0.0020  -0.0297 204 LEU A N   
1641 C  CA  . LEU A 203 ? 0.0952 0.0797 0.1576 -0.0027 0.0045  -0.0160 204 LEU A CA  
1642 C  C   . LEU A 203 ? 0.0619 0.0658 0.1292 0.0016  -0.0077 -0.0180 204 LEU A C   
1643 O  O   . LEU A 203 ? 0.1077 0.0768 0.1175 -0.0233 -0.0204 -0.0289 204 LEU A O   
1644 C  CB  . LEU A 203 ? 0.1032 0.0893 0.1578 0.0007  0.0049  0.0127  204 LEU A CB  
1645 C  CG  . LEU A 203 ? 0.1605 0.1379 0.1532 -0.0014 0.0243  -0.0077 204 LEU A CG  
1646 C  CD1 . LEU A 203 ? 0.1522 0.1348 0.2427 0.0102  0.0357  0.0407  204 LEU A CD1 
1647 C  CD2 . LEU A 203 ? 0.1642 0.1577 0.2829 -0.0377 0.0076  -0.0234 204 LEU A CD2 
1648 N  N   . GLU A 204 ? 0.1133 0.0793 0.1192 -0.0167 -0.0192 -0.0349 205 GLU A N   
1649 C  CA  . GLU A 204 ? 0.0786 0.0935 0.0876 0.0142  -0.0411 -0.0284 205 GLU A CA  
1650 C  C   . GLU A 204 ? 0.1030 0.0836 0.1207 -0.0002 -0.0315 -0.0168 205 GLU A C   
1651 O  O   . GLU A 204 ? 0.1074 0.0967 0.1467 0.0055  -0.0273 -0.0468 205 GLU A O   
1652 C  CB  . GLU A 204 ? 0.0942 0.0707 0.1172 0.0232  -0.0617 -0.0142 205 GLU A CB  
1653 C  CG  . GLU A 204 ? 0.0746 0.1232 0.1717 0.0420  -0.0612 0.0095  205 GLU A CG  
1654 C  CD  . GLU A 204 ? 0.1428 0.1041 0.1209 0.0024  -0.0531 -0.0038 205 GLU A CD  
1655 O  OE1 . GLU A 204 ? 0.1312 0.1554 0.2050 0.0023  -0.0913 -0.0655 205 GLU A OE1 
1656 O  OE2 . GLU A 204 ? 0.1034 0.0948 0.2107 -0.0130 -0.0539 -0.0151 205 GLU A OE2 
1657 N  N   . CYS A 205 ? 0.0667 0.0958 0.1317 -0.0021 -0.0235 -0.0429 206 CYS A N   
1658 C  CA  . CYS A 205 ? 0.0769 0.0906 0.1185 0.0017  -0.0137 -0.0083 206 CYS A CA  
1659 C  C   . CYS A 205 ? 0.0822 0.0864 0.1302 -0.0023 -0.0041 -0.0089 206 CYS A C   
1660 O  O   . CYS A 205 ? 0.1093 0.0685 0.1575 0.0063  -0.0495 0.0111  206 CYS A O   
1661 C  CB  . CYS A 205 ? 0.1200 0.0847 0.1257 0.0025  -0.0111 0.0068  206 CYS A CB  
1662 S  SG  . CYS A 205 ? 0.1546 0.0845 0.1329 0.0026  -0.0193 -0.0146 206 CYS A SG  
1663 N  N   . VAL A 206 ? 0.0829 0.0659 0.1052 -0.0146 -0.0177 -0.0173 207 VAL A N   
1664 C  CA  . VAL A 206 ? 0.0596 0.0444 0.1184 -0.0119 0.0088  -0.0264 207 VAL A CA  
1665 C  C   . VAL A 206 ? 0.1020 0.0540 0.1121 0.0199  0.0087  -0.0192 207 VAL A C   
1666 O  O   . VAL A 206 ? 0.0803 0.0859 0.1364 0.0083  0.0012  -0.0115 207 VAL A O   
1667 C  CB  . VAL A 206 ? 0.0522 0.0577 0.1023 0.0261  0.0046  -0.0185 207 VAL A CB  
1668 C  CG1 . VAL A 206 ? 0.0763 0.0737 0.1252 -0.0388 -0.0131 -0.0326 207 VAL A CG1 
1669 C  CG2 . VAL A 206 ? 0.0651 0.1088 0.0921 -0.0092 0.0207  -0.0202 207 VAL A CG2 
1670 N  N   . THR A 207 ? 0.0848 0.0630 0.1113 0.0096  0.0017  -0.0105 208 THR A N   
1671 C  CA  . THR A 207 ? 0.0678 0.0611 0.0912 0.0030  -0.0094 -0.0316 208 THR A CA  
1672 C  C   . THR A 207 ? 0.0831 0.0353 0.0856 -0.0109 0.0018  0.0006  208 THR A C   
1673 O  O   . THR A 207 ? 0.0903 0.0497 0.1016 -0.0161 -0.0253 0.0010  208 THR A O   
1674 C  CB  . THR A 207 ? 0.0862 0.0895 0.0989 0.0143  0.0016  -0.0306 208 THR A CB  
1675 O  OG1 . THR A 207 ? 0.1093 0.0426 0.1229 -0.0128 0.0012  -0.0388 208 THR A OG1 
1676 C  CG2 . THR A 207 ? 0.0793 0.0961 0.1480 -0.0117 0.0010  -0.0245 208 THR A CG2 
1677 N  N   . TRP A 208 ? 0.0883 0.0315 0.0908 -0.0068 0.0012  -0.0016 209 TRP A N   
1678 C  CA  . TRP A 208 ? 0.0522 0.0591 0.1037 -0.0076 -0.0029 -0.0086 209 TRP A CA  
1679 C  C   . TRP A 208 ? 0.0505 0.0768 0.0978 -0.0020 -0.0004 -0.0105 209 TRP A C   
1680 O  O   . TRP A 208 ? 0.0772 0.0965 0.1002 -0.0209 0.0079  0.0161  209 TRP A O   
1681 C  CB  . TRP A 208 ? 0.0797 0.0387 0.1029 0.0078  0.0054  0.0066  209 TRP A CB  
1682 C  CG  . TRP A 208 ? 0.0489 0.0652 0.0797 0.0226  -0.0158 -0.0123 209 TRP A CG  
1683 C  CD1 . TRP A 208 ? 0.0646 0.0610 0.1313 0.0335  0.0263  -0.0024 209 TRP A CD1 
1684 C  CD2 . TRP A 208 ? 0.0463 0.0576 0.0920 -0.0039 -0.0053 -0.0175 209 TRP A CD2 
1685 N  NE1 . TRP A 208 ? 0.0695 0.0738 0.1015 0.0305  -0.0241 -0.0275 209 TRP A NE1 
1686 C  CE2 . TRP A 208 ? 0.0454 0.0803 0.0834 0.0233  -0.0325 -0.0255 209 TRP A CE2 
1687 C  CE3 . TRP A 208 ? 0.0670 0.0732 0.0802 0.0020  -0.0322 0.0016  209 TRP A CE3 
1688 C  CZ2 . TRP A 208 ? 0.0623 0.0933 0.0867 0.0435  -0.0348 -0.0192 209 TRP A CZ2 
1689 C  CZ3 . TRP A 208 ? 0.0907 0.0611 0.0905 0.0229  0.0005  -0.0025 209 TRP A CZ3 
1690 C  CH2 . TRP A 208 ? 0.0535 0.0800 0.1279 0.0269  -0.0230 -0.0211 209 TRP A CH2 
1691 N  N   . ILE A 209 ? 0.0524 0.0694 0.0937 -0.0003 -0.0058 -0.0194 210 ILE A N   
1692 C  CA  . ILE A 209 ? 0.0416 0.0444 0.1149 0.0174  -0.0196 -0.0150 210 ILE A CA  
1693 C  C   . ILE A 209 ? 0.0697 0.0906 0.1154 -0.0107 -0.0119 -0.0189 210 ILE A C   
1694 O  O   . ILE A 209 ? 0.1014 0.0747 0.0856 0.0149  -0.0277 -0.0154 210 ILE A O   
1695 C  CB  . ILE A 209 ? 0.0624 0.0370 0.1582 0.0170  0.0089  -0.0181 210 ILE A CB  
1696 C  CG1 . ILE A 209 ? 0.0793 0.0734 0.1573 0.0481  -0.0038 -0.0295 210 ILE A CG1 
1697 C  CG2 . ILE A 209 ? 0.0655 0.1242 0.1374 0.0072  -0.0093 -0.0035 210 ILE A CG2 
1698 C  CD1 . ILE A 209 ? 0.0977 0.1027 0.1934 0.0483  -0.0228 0.0009  210 ILE A CD1 
1699 N  N   . VAL A 210 ? 0.0976 0.0621 0.1240 0.0211  0.0003  -0.0265 211 VAL A N   
1700 C  CA  . VAL A 210 ? 0.0753 0.0663 0.1090 -0.0035 0.0109  -0.0142 211 VAL A CA  
1701 C  C   . VAL A 210 ? 0.0739 0.0439 0.1041 0.0155  -0.0061 -0.0056 211 VAL A C   
1702 O  O   . VAL A 210 ? 0.1114 0.0981 0.0927 0.0054  0.0123  0.0013  211 VAL A O   
1703 C  CB  . VAL A 210 ? 0.0339 0.0938 0.1281 0.0153  0.0009  0.0116  211 VAL A CB  
1704 C  CG1 . VAL A 210 ? 0.1265 0.0472 0.1208 0.0097  0.0073  -0.0278 211 VAL A CG1 
1705 C  CG2 . VAL A 210 ? 0.0338 0.0535 0.1462 -0.0106 -0.0150 0.0032  211 VAL A CG2 
1706 N  N   . LEU A 211 ? 0.0655 0.0674 0.1184 -0.0171 -0.0077 -0.0030 212 LEU A N   
1707 C  CA  . LEU A 211 ? 0.0684 0.0828 0.1121 -0.0217 -0.0202 0.0195  212 LEU A CA  
1708 C  C   . LEU A 211 ? 0.0876 0.1091 0.0847 -0.0295 0.0008  0.0230  212 LEU A C   
1709 O  O   . LEU A 211 ? 0.0817 0.0915 0.1107 -0.0213 -0.0008 0.0048  212 LEU A O   
1710 C  CB  . LEU A 211 ? 0.0876 0.1051 0.0957 -0.0123 -0.0576 0.0419  212 LEU A CB  
1711 C  CG  . LEU A 211 ? 0.1007 0.0834 0.1394 -0.0187 -0.0539 0.0275  212 LEU A CG  
1712 C  CD1 . LEU A 211 ? 0.1124 0.1897 0.1460 -0.0039 -0.0668 0.0116  212 LEU A CD1 
1713 C  CD2 . LEU A 211 ? 0.1246 0.0976 0.1635 -0.0237 -0.0063 -0.0241 212 LEU A CD2 
1714 N  N   . LYS A 212 ? 0.1280 0.0935 0.1026 -0.0393 0.0057  0.0171  213 LYS A N   
1715 C  CA  . LYS A 212 ? 0.1475 0.0989 0.1362 -0.0371 -0.0009 0.0234  213 LYS A CA  
1716 C  C   . LYS A 212 ? 0.1282 0.0830 0.1327 -0.0262 -0.0101 0.0378  213 LYS A C   
1717 O  O   . LYS A 212 ? 0.1156 0.0770 0.1762 -0.0166 -0.0375 0.0288  213 LYS A O   
1718 C  CB  . LYS A 212 ? 0.1730 0.1325 0.1439 -0.0504 -0.0027 0.0191  213 LYS A CB  
1719 C  CG  . LYS A 212 ? 0.2352 0.1547 0.2088 -0.0360 -0.0122 0.0042  213 LYS A CG  
1720 C  CD  . LYS A 212 ? 0.2979 0.1693 0.2472 -0.0749 0.0266  0.0156  213 LYS A CD  
1721 C  CE  . LYS A 212 ? 0.3630 0.2451 0.3318 -0.0680 -0.0056 0.0418  213 LYS A CE  
1722 N  NZ  . LYS A 212 ? 0.4840 0.4338 0.4220 -0.0424 0.0369  0.0120  213 LYS A NZ  
1723 N  N   . GLU A 213 ? 0.1058 0.0788 0.1233 -0.0180 -0.0111 0.0133  214 GLU A N   
1724 C  CA  . GLU A 213 ? 0.0968 0.1096 0.1496 -0.0253 -0.0140 0.0134  214 GLU A CA  
1725 C  C   . GLU A 213 ? 0.0941 0.0747 0.1225 -0.0088 -0.0125 0.0086  214 GLU A C   
1726 O  O   . GLU A 213 ? 0.1102 0.0525 0.1213 -0.0171 -0.0254 0.0159  214 GLU A O   
1727 C  CB  . GLU A 213 ? 0.1007 0.1107 0.1196 -0.0111 -0.0269 0.0044  214 GLU A CB  
1728 C  CG  . GLU A 213 ? 0.1007 0.1275 0.2008 -0.0167 -0.0538 0.0012  214 GLU A CG  
1729 C  CD  . GLU A 213 ? 0.1278 0.1490 0.2529 -0.0376 -0.0054 -0.0208 214 GLU A CD  
1730 O  OE1 . GLU A 213 ? 0.1479 0.1041 0.2869 -0.0378 -0.0360 -0.0018 214 GLU A OE1 
1731 O  OE2 . GLU A 213 ? 0.2140 0.3216 0.3353 -0.0590 -0.0698 -0.0374 214 GLU A OE2 
1732 N  N   A PRO A 214 ? 0.0885 0.0525 0.1287 -0.0052 -0.0113 0.0062  215 PRO A N   
1733 N  N   B PRO A 214 ? 0.1111 0.0745 0.1384 0.0003  -0.0085 0.0130  215 PRO A N   
1734 C  CA  A PRO A 214 ? 0.0824 0.0613 0.1191 -0.0023 -0.0126 -0.0111 215 PRO A CA  
1735 C  CA  B PRO A 214 ? 0.1141 0.0901 0.1307 -0.0010 -0.0134 -0.0044 215 PRO A CA  
1736 C  C   A PRO A 214 ? 0.0794 0.0692 0.1238 -0.0013 -0.0179 0.0005  215 PRO A C   
1737 C  C   B PRO A 214 ? 0.1050 0.0915 0.1331 -0.0031 -0.0187 0.0061  215 PRO A C   
1738 O  O   A PRO A 214 ? 0.0814 0.0764 0.1396 0.0027  -0.0164 -0.0001 215 PRO A O   
1739 O  O   B PRO A 214 ? 0.1196 0.0895 0.1564 -0.0267 -0.0289 -0.0045 215 PRO A O   
1740 C  CB  A PRO A 214 ? 0.0741 0.0524 0.1406 -0.0081 -0.0258 -0.0051 215 PRO A CB  
1741 C  CB  B PRO A 214 ? 0.1114 0.0888 0.1521 -0.0008 -0.0122 -0.0006 215 PRO A CB  
1742 C  CG  A PRO A 214 ? 0.0638 0.0670 0.1450 -0.0078 -0.0095 -0.0169 215 PRO A CG  
1743 C  CG  B PRO A 214 ? 0.1396 0.1183 0.1571 0.0145  -0.0172 -0.0071 215 PRO A CG  
1744 C  CD  A PRO A 214 ? 0.0774 0.0342 0.1124 -0.0055 -0.0006 0.0083  215 PRO A CD  
1745 C  CD  B PRO A 214 ? 0.1126 0.0738 0.1301 -0.0006 -0.0080 0.0165  215 PRO A CD  
1746 N  N   . ILE A 215 ? 0.1018 0.0865 0.1012 -0.0028 -0.0259 -0.0107 216 ILE A N   
1747 C  CA  . ILE A 215 ? 0.1302 0.0773 0.0992 0.0063  -0.0250 -0.0099 216 ILE A CA  
1748 C  C   . ILE A 215 ? 0.1039 0.0807 0.1335 0.0167  -0.0341 -0.0122 216 ILE A C   
1749 O  O   . ILE A 215 ? 0.1067 0.0919 0.1424 0.0086  -0.0366 -0.0261 216 ILE A O   
1750 C  CB  . ILE A 215 ? 0.1136 0.0789 0.1103 0.0200  0.0065  0.0057  216 ILE A CB  
1751 C  CG1 . ILE A 215 ? 0.1603 0.1016 0.1281 -0.0345 0.0097  0.0265  216 ILE A CG1 
1752 C  CG2 . ILE A 215 ? 0.1366 0.0816 0.2004 0.0357  -0.0378 -0.0225 216 ILE A CG2 
1753 C  CD1 . ILE A 215 ? 0.1732 0.0890 0.1322 -0.0137 -0.0203 0.0145  216 ILE A CD1 
1754 N  N   A SER A 216 ? 0.1216 0.0770 0.1196 -0.0011 -0.0282 -0.0288 217 SER A N   
1755 N  N   B SER A 216 ? 0.1374 0.0821 0.1343 0.0046  -0.0277 -0.0338 217 SER A N   
1756 C  CA  A SER A 216 ? 0.0989 0.0810 0.1135 -0.0128 -0.0286 -0.0184 217 SER A CA  
1757 C  CA  B SER A 216 ? 0.1328 0.0850 0.1422 -0.0065 -0.0248 -0.0240 217 SER A CA  
1758 C  C   A SER A 216 ? 0.1403 0.0762 0.1424 -0.0090 -0.0403 -0.0120 217 SER A C   
1759 C  C   B SER A 216 ? 0.1547 0.0771 0.1580 -0.0081 -0.0301 -0.0165 217 SER A C   
1760 O  O   A SER A 216 ? 0.1615 0.0992 0.1530 -0.0120 -0.0567 -0.0071 217 SER A O   
1761 O  O   B SER A 216 ? 0.1518 0.0766 0.1686 -0.0178 -0.0224 -0.0191 217 SER A O   
1762 C  CB  A SER A 216 ? 0.1057 0.0998 0.1291 -0.0038 -0.0234 0.0199  217 SER A CB  
1763 C  CB  B SER A 216 ? 0.1717 0.1101 0.1667 0.0014  -0.0127 -0.0062 217 SER A CB  
1764 O  OG  A SER A 216 ? 0.1716 0.1384 0.0879 -0.0509 -0.0048 0.0135  217 SER A OG  
1765 O  OG  B SER A 216 ? 0.1872 0.1676 0.2114 -0.0248 -0.0522 -0.0191 217 SER A OG  
1766 N  N   . VAL A 217 ? 0.1277 0.0535 0.1489 -0.0133 -0.0313 -0.0116 218 VAL A N   
1767 C  CA  . VAL A 217 ? 0.1326 0.0739 0.1470 0.0030  -0.0318 -0.0156 218 VAL A CA  
1768 C  C   . VAL A 217 ? 0.1446 0.0838 0.1418 -0.0047 -0.0482 -0.0110 218 VAL A C   
1769 O  O   . VAL A 217 ? 0.1653 0.1014 0.1338 0.0132  -0.0797 -0.0206 218 VAL A O   
1770 C  CB  . VAL A 217 ? 0.1372 0.0641 0.1541 0.0037  -0.0564 -0.0085 218 VAL A CB  
1771 C  CG1 . VAL A 217 ? 0.2381 0.0327 0.1690 -0.0022 -0.0332 -0.0316 218 VAL A CG1 
1772 C  CG2 . VAL A 217 ? 0.1601 0.0593 0.2175 0.0081  -0.0573 -0.0518 218 VAL A CG2 
1773 N  N   . SER A 218 ? 0.1624 0.0714 0.1464 -0.0042 -0.0342 -0.0244 219 SER A N   
1774 C  CA  . SER A 218 ? 0.1817 0.0644 0.1234 -0.0045 -0.0218 -0.0184 219 SER A CA  
1775 C  C   . SER A 218 ? 0.1803 0.0694 0.1553 -0.0121 -0.0219 -0.0181 219 SER A C   
1776 O  O   . SER A 218 ? 0.1529 0.0466 0.1441 -0.0104 -0.0189 -0.0036 219 SER A O   
1777 C  CB  . SER A 218 ? 0.2236 0.0562 0.1372 -0.0205 -0.0295 -0.0302 219 SER A CB  
1778 O  OG  . SER A 218 ? 0.1962 0.1013 0.1718 -0.0394 -0.0396 -0.0134 219 SER A OG  
1779 N  N   . SER A 219 ? 0.1974 0.0612 0.1770 -0.0052 -0.0010 -0.0125 220 SER A N   
1780 C  CA  . SER A 219 ? 0.2097 0.0459 0.2075 0.0062  0.0053  -0.0030 220 SER A CA  
1781 C  C   . SER A 219 ? 0.2147 0.0638 0.2092 -0.0052 -0.0001 -0.0209 220 SER A C   
1782 O  O   . SER A 219 ? 0.2227 0.0981 0.2275 -0.0236 0.0218  -0.0032 220 SER A O   
1783 C  CB  . SER A 219 ? 0.2688 0.0436 0.2255 -0.0184 -0.0108 -0.0244 220 SER A CB  
1784 O  OG  . SER A 219 ? 0.3023 0.1174 0.2960 -0.0169 -0.0084 -0.0216 220 SER A OG  
1785 N  N   . GLU A 220 ? 0.2260 0.0577 0.1578 -0.0123 -0.0025 -0.0171 221 GLU A N   
1786 C  CA  . GLU A 220 ? 0.2263 0.1089 0.1860 -0.0033 -0.0099 -0.0038 221 GLU A CA  
1787 C  C   . GLU A 220 ? 0.2080 0.0914 0.1509 -0.0132 0.0003  -0.0096 221 GLU A C   
1788 O  O   . GLU A 220 ? 0.2144 0.1110 0.1515 0.0008  0.0132  -0.0305 221 GLU A O   
1789 C  CB  . GLU A 220 ? 0.2508 0.1297 0.2024 -0.0195 -0.0241 -0.0476 221 GLU A CB  
1790 C  CG  . GLU A 220 ? 0.3188 0.1269 0.2514 -0.0255 -0.0227 -0.0264 221 GLU A CG  
1791 C  CD  . GLU A 220 ? 0.3482 0.0877 0.3156 -0.0234 0.0103  -0.0388 221 GLU A CD  
1792 O  OE1 . GLU A 220 ? 0.2608 0.1734 0.2599 -0.0831 -0.0087 -0.0199 221 GLU A OE1 
1793 O  OE2 . GLU A 220 ? 0.4630 0.2305 0.4237 -0.0575 0.0077  -0.0558 221 GLU A OE2 
1794 N  N   . GLN A 221 ? 0.1816 0.0463 0.1481 -0.0081 -0.0259 -0.0038 222 GLN A N   
1795 C  CA  . GLN A 221 ? 0.1492 0.0591 0.1612 -0.0052 -0.0169 0.0103  222 GLN A CA  
1796 C  C   . GLN A 221 ? 0.1665 0.1002 0.1496 -0.0122 -0.0237 0.0067  222 GLN A C   
1797 O  O   . GLN A 221 ? 0.1730 0.1103 0.1336 -0.0179 -0.0133 0.0236  222 GLN A O   
1798 C  CB  . GLN A 221 ? 0.1325 0.1084 0.1617 0.0137  -0.0277 0.0091  222 GLN A CB  
1799 C  CG  . GLN A 221 ? 0.1571 0.1295 0.1266 -0.0373 -0.0261 -0.0148 222 GLN A CG  
1800 C  CD  . GLN A 221 ? 0.1625 0.0552 0.1621 -0.0234 -0.0048 -0.0144 222 GLN A CD  
1801 O  OE1 . GLN A 221 ? 0.1846 0.1012 0.1388 -0.0071 -0.0128 -0.0238 222 GLN A OE1 
1802 N  NE2 . GLN A 221 ? 0.1768 0.0502 0.1880 -0.0201 -0.0800 0.0013  222 GLN A NE2 
1803 N  N   A VAL A 222 ? 0.1558 0.0924 0.1406 -0.0092 -0.0233 0.0071  223 VAL A N   
1804 N  N   B VAL A 222 ? 0.1760 0.0996 0.1473 -0.0136 -0.0149 0.0090  223 VAL A N   
1805 C  CA  A VAL A 222 ? 0.1655 0.1102 0.1400 0.0022  -0.0210 -0.0002 223 VAL A CA  
1806 C  CA  B VAL A 222 ? 0.1906 0.1249 0.1450 -0.0009 -0.0085 0.0065  223 VAL A CA  
1807 C  C   A VAL A 222 ? 0.1691 0.0979 0.1593 -0.0037 -0.0138 -0.0131 223 VAL A C   
1808 C  C   B VAL A 222 ? 0.1867 0.1087 0.1589 -0.0069 -0.0049 -0.0077 223 VAL A C   
1809 O  O   A VAL A 222 ? 0.1764 0.0950 0.1283 -0.0045 -0.0403 -0.0261 223 VAL A O   
1810 O  O   B VAL A 222 ? 0.1950 0.1183 0.1338 -0.0056 -0.0034 -0.0071 223 VAL A O   
1811 C  CB  A VAL A 222 ? 0.1574 0.1163 0.1416 0.0137  -0.0140 -0.0021 223 VAL A CB  
1812 C  CB  B VAL A 222 ? 0.1887 0.1151 0.1466 0.0002  -0.0073 0.0089  223 VAL A CB  
1813 C  CG1 A VAL A 222 ? 0.1510 0.1268 0.1695 -0.0132 -0.0218 -0.0155 223 VAL A CG1 
1814 C  CG1 B VAL A 222 ? 0.1995 0.1827 0.1684 -0.0132 0.0132  0.0143  223 VAL A CG1 
1815 C  CG2 A VAL A 222 ? 0.1249 0.0758 0.1278 -0.0006 -0.0360 0.0180  223 VAL A CG2 
1816 C  CG2 B VAL A 222 ? 0.2103 0.1020 0.1544 -0.0048 -0.0042 0.0150  223 VAL A CG2 
1817 N  N   . LEU A 223 ? 0.2077 0.1007 0.1564 0.0093  -0.0060 -0.0166 224 LEU A N   
1818 C  CA  . LEU A 223 ? 0.2441 0.1102 0.1728 -0.0124 0.0081  -0.0250 224 LEU A CA  
1819 C  C   . LEU A 223 ? 0.2336 0.1536 0.1781 0.0007  0.0040  -0.0150 224 LEU A C   
1820 O  O   . LEU A 223 ? 0.2333 0.1486 0.2300 -0.0066 -0.0040 -0.0127 224 LEU A O   
1821 C  CB  . LEU A 223 ? 0.2814 0.1442 0.2184 -0.0199 -0.0016 -0.0380 224 LEU A CB  
1822 C  CG  . LEU A 223 ? 0.3244 0.2588 0.3159 -0.0147 -0.0104 -0.0121 224 LEU A CG  
1823 C  CD1 . LEU A 223 ? 0.4003 0.2743 0.3780 -0.0353 -0.0166 0.0076  224 LEU A CD1 
1824 C  CD2 . LEU A 223 ? 0.3371 0.3136 0.4060 0.0149  0.0118  -0.0262 224 LEU A CD2 
1825 N  N   . LYS A 224 ? 0.2144 0.1092 0.1519 -0.0083 -0.0108 -0.0184 225 LYS A N   
1826 C  CA  . LYS A 224 ? 0.2139 0.1663 0.1747 0.0009  -0.0128 0.0040  225 LYS A CA  
1827 C  C   . LYS A 224 ? 0.2061 0.1324 0.1414 -0.0037 -0.0049 0.0007  225 LYS A C   
1828 O  O   . LYS A 224 ? 0.2548 0.1533 0.1137 -0.0328 0.0075  -0.0001 225 LYS A O   
1829 C  CB  . LYS A 224 ? 0.2054 0.1730 0.1814 -0.0097 -0.0331 0.0191  225 LYS A CB  
1830 C  CG  . LYS A 224 ? 0.2597 0.2654 0.2462 -0.0260 -0.0263 -0.0131 225 LYS A CG  
1831 C  CD  . LYS A 224 ? 0.3167 0.3121 0.2820 -0.0042 -0.0212 0.0212  225 LYS A CD  
1832 C  CE  . LYS A 224 ? 0.4261 0.3902 0.3563 -0.0118 -0.0077 0.0293  225 LYS A CE  
1833 N  NZ  . LYS A 224 ? 0.4881 0.4185 0.3864 -0.0132 -0.0040 -0.0121 225 LYS A NZ  
1834 N  N   . PHE A 225 ? 0.1789 0.0986 0.1155 0.0105  -0.0083 -0.0233 226 PHE A N   
1835 C  CA  . PHE A 225 ? 0.1716 0.0674 0.1100 0.0013  0.0040  -0.0201 226 PHE A CA  
1836 C  C   . PHE A 225 ? 0.1844 0.0917 0.1116 -0.0080 -0.0033 -0.0213 226 PHE A C   
1837 O  O   . PHE A 225 ? 0.1838 0.1025 0.1387 -0.0121 0.0108  -0.0193 226 PHE A O   
1838 C  CB  . PHE A 225 ? 0.1677 0.0970 0.1033 0.0032  -0.0064 -0.0227 226 PHE A CB  
1839 C  CG  . PHE A 225 ? 0.1594 0.0714 0.1059 0.0004  -0.0079 0.0117  226 PHE A CG  
1840 C  CD1 . PHE A 225 ? 0.2020 0.1166 0.1559 0.0306  -0.0102 0.0009  226 PHE A CD1 
1841 C  CD2 . PHE A 225 ? 0.1331 0.1345 0.1495 0.0138  0.0139  -0.0384 226 PHE A CD2 
1842 C  CE1 . PHE A 225 ? 0.2005 0.1159 0.1641 0.0031  0.0091  -0.0214 226 PHE A CE1 
1843 C  CE2 . PHE A 225 ? 0.1679 0.1622 0.1619 -0.0005 0.0051  -0.0675 226 PHE A CE2 
1844 C  CZ  . PHE A 225 ? 0.1348 0.1365 0.1899 -0.0224 -0.0011 -0.0309 226 PHE A CZ  
1845 N  N   . ARG A 226 ? 0.1934 0.0845 0.1136 0.0081  0.0087  -0.0128 227 ARG A N   
1846 C  CA  . ARG A 226 ? 0.2009 0.1132 0.1351 0.0035  0.0156  -0.0022 227 ARG A CA  
1847 C  C   . ARG A 226 ? 0.1953 0.1212 0.1467 -0.0080 0.0032  -0.0148 227 ARG A C   
1848 O  O   . ARG A 226 ? 0.2050 0.1665 0.1858 -0.0160 0.0167  -0.0175 227 ARG A O   
1849 C  CB  . ARG A 226 ? 0.2156 0.0943 0.1359 0.0125  0.0062  0.0001  227 ARG A CB  
1850 C  CG  . ARG A 226 ? 0.1848 0.1058 0.1365 -0.0176 0.0176  0.0212  227 ARG A CG  
1851 C  CD  . ARG A 226 ? 0.1638 0.1058 0.2051 -0.0174 0.0250  0.0238  227 ARG A CD  
1852 N  NE  . ARG A 226 ? 0.1998 0.1033 0.1812 -0.0305 -0.0182 -0.0328 227 ARG A NE  
1853 C  CZ  . ARG A 226 ? 0.1666 0.1417 0.1512 0.0092  -0.0233 -0.0299 227 ARG A CZ  
1854 N  NH1 . ARG A 226 ? 0.2142 0.1383 0.2253 -0.0270 -0.0732 -0.0575 227 ARG A NH1 
1855 N  NH2 . ARG A 226 ? 0.2068 0.0908 0.1724 -0.0497 -0.0136 -0.0318 227 ARG A NH2 
1856 N  N   . LYS A 227 ? 0.2330 0.1364 0.1198 -0.0130 0.0050  -0.0142 228 LYS A N   
1857 C  CA  . LYS A 227 ? 0.2457 0.1583 0.1324 -0.0362 0.0238  -0.0275 228 LYS A CA  
1858 C  C   . LYS A 227 ? 0.2306 0.1480 0.1145 -0.0248 0.0397  -0.0333 228 LYS A C   
1859 O  O   . LYS A 227 ? 0.2285 0.1542 0.1473 -0.0275 0.0469  -0.0256 228 LYS A O   
1860 C  CB  . LYS A 227 ? 0.2539 0.1788 0.1645 -0.0258 -0.0143 -0.0002 228 LYS A CB  
1861 C  CG  . LYS A 227 ? 0.2961 0.2144 0.1952 -0.0475 0.0064  -0.0119 228 LYS A CG  
1862 C  CD  . LYS A 227 ? 0.3352 0.3171 0.3374 -0.0157 -0.0024 0.0006  228 LYS A CD  
1863 C  CE  . LYS A 227 ? 0.4527 0.4391 0.4176 -0.0086 0.0348  0.0039  228 LYS A CE  
1864 N  NZ  . LYS A 227 ? 0.4980 0.4340 0.5119 -0.0078 -0.0026 -0.0022 228 LYS A NZ  
1865 N  N   . LEU A 228 ? 0.2308 0.1196 0.1289 -0.0368 0.0202  -0.0303 229 LEU A N   
1866 C  CA  . LEU A 228 ? 0.2406 0.1063 0.1363 -0.0314 0.0277  -0.0342 229 LEU A CA  
1867 C  C   . LEU A 228 ? 0.2506 0.1415 0.1343 -0.0312 0.0319  -0.0331 229 LEU A C   
1868 O  O   . LEU A 228 ? 0.2267 0.1095 0.1644 -0.0423 0.0417  -0.0228 229 LEU A O   
1869 C  CB  . LEU A 228 ? 0.2247 0.1149 0.1010 -0.0045 0.0306  -0.0227 229 LEU A CB  
1870 C  CG  . LEU A 228 ? 0.2059 0.1287 0.1138 -0.0044 0.0213  -0.0039 229 LEU A CG  
1871 C  CD1 . LEU A 228 ? 0.1940 0.1109 0.1073 -0.0179 0.0145  -0.0455 229 LEU A CD1 
1872 C  CD2 . LEU A 228 ? 0.2407 0.1304 0.1494 0.0208  0.0113  0.0389  229 LEU A CD2 
1873 N  N   . ASN A 229 ? 0.2427 0.1574 0.1235 -0.0533 0.0453  -0.0372 230 ASN A N   
1874 C  CA  . ASN A 229 ? 0.2482 0.1728 0.1110 -0.0692 0.0220  -0.0391 230 ASN A CA  
1875 C  C   . ASN A 229 ? 0.2638 0.1878 0.1533 -0.0604 0.0340  -0.0301 230 ASN A C   
1876 O  O   . ASN A 229 ? 0.2639 0.1877 0.1532 -0.0680 0.0354  -0.0127 230 ASN A O   
1877 C  CB  . ASN A 229 ? 0.2768 0.1742 0.1162 -0.0356 0.0359  -0.0224 230 ASN A CB  
1878 C  CG  . ASN A 229 ? 0.3048 0.2074 0.1501 -0.0639 0.0341  -0.0302 230 ASN A CG  
1879 O  OD1 . ASN A 229 ? 0.3648 0.2498 0.1768 -0.0483 0.0616  -0.0574 230 ASN A OD1 
1880 N  ND2 . ASN A 229 ? 0.2841 0.1335 0.1672 -0.0575 0.0131  -0.0559 230 ASN A ND2 
1881 N  N   . PHE A 230 ? 0.2384 0.1840 0.1540 -0.1001 0.0352  -0.0178 231 PHE A N   
1882 C  CA  . PHE A 230 ? 0.2406 0.1783 0.1474 -0.0914 0.0303  -0.0177 231 PHE A CA  
1883 C  C   . PHE A 230 ? 0.2660 0.2305 0.1751 -0.0696 0.0469  -0.0232 231 PHE A C   
1884 O  O   . PHE A 230 ? 0.2795 0.2342 0.1511 -0.0961 0.0201  -0.0167 231 PHE A O   
1885 C  CB  . PHE A 230 ? 0.2631 0.1842 0.1419 -0.0673 0.0181  -0.0143 231 PHE A CB  
1886 C  CG  . PHE A 230 ? 0.2347 0.1923 0.1491 -0.0676 0.0538  -0.0237 231 PHE A CG  
1887 C  CD1 . PHE A 230 ? 0.1641 0.1764 0.1235 -0.0197 0.0268  0.0030  231 PHE A CD1 
1888 C  CD2 . PHE A 230 ? 0.1778 0.1880 0.1294 -0.0420 0.0283  -0.0088 231 PHE A CD2 
1889 C  CE1 . PHE A 230 ? 0.2025 0.1873 0.1453 -0.0772 0.0126  0.0233  231 PHE A CE1 
1890 C  CE2 . PHE A 230 ? 0.2266 0.1783 0.1734 -0.0653 0.0254  -0.0253 231 PHE A CE2 
1891 C  CZ  . PHE A 230 ? 0.2148 0.2112 0.1407 -0.0319 0.0281  -0.0051 231 PHE A CZ  
1892 N  N   . ASN A 231 ? 0.2491 0.2252 0.1527 -0.0921 0.0731  -0.0368 232 ASN A N   
1893 C  CA  . ASN A 231 ? 0.2700 0.2285 0.1657 -0.0618 0.0741  -0.0170 232 ASN A CA  
1894 C  C   . ASN A 231 ? 0.2347 0.2499 0.1811 -0.0559 0.0638  -0.0194 232 ASN A C   
1895 O  O   . ASN A 231 ? 0.2318 0.2474 0.1851 -0.0359 0.0547  -0.0105 232 ASN A O   
1896 C  CB  . ASN A 231 ? 0.2707 0.2392 0.1766 -0.0613 0.0766  -0.0351 232 ASN A CB  
1897 C  CG  . ASN A 231 ? 0.2723 0.2355 0.1773 -0.0562 0.0466  -0.0068 232 ASN A CG  
1898 O  OD1 . ASN A 231 ? 0.3278 0.2500 0.1877 -0.1233 0.0788  -0.0410 232 ASN A OD1 
1899 N  ND2 . ASN A 231 ? 0.2686 0.2536 0.1915 0.0061  0.0602  -0.0203 232 ASN A ND2 
1900 N  N   . GLY A 232 ? 0.2911 0.2161 0.2160 -0.0654 0.0478  -0.0115 233 GLY A N   
1901 C  CA  . GLY A 232 ? 0.3162 0.2656 0.2332 -0.0399 0.0539  -0.0034 233 GLY A CA  
1902 C  C   . GLY A 232 ? 0.2930 0.2649 0.2316 -0.0432 0.0296  0.0029  233 GLY A C   
1903 O  O   . GLY A 232 ? 0.3037 0.2587 0.2187 -0.0472 0.0869  0.0099  233 GLY A O   
1904 N  N   . GLU A 233 ? 0.3031 0.2780 0.2208 -0.0386 0.0391  0.0067  234 GLU A N   
1905 C  CA  . GLU A 233 ? 0.2963 0.2858 0.2268 -0.0287 0.0185  0.0030  234 GLU A CA  
1906 C  C   . GLU A 233 ? 0.3137 0.3013 0.2408 -0.0300 0.0263  -0.0096 234 GLU A C   
1907 O  O   . GLU A 233 ? 0.3349 0.3069 0.2207 -0.0496 0.0361  0.0082  234 GLU A O   
1908 C  CB  . GLU A 233 ? 0.2995 0.2683 0.2359 -0.0131 0.0134  0.0011  234 GLU A CB  
1909 C  CG  . GLU A 233 ? 0.2656 0.2838 0.2142 -0.0319 0.0080  0.0356  234 GLU A CG  
1910 C  CD  . GLU A 233 ? 0.3450 0.3163 0.2580 -0.0188 -0.0106 0.0096  234 GLU A CD  
1911 O  OE1 . GLU A 233 ? 0.3329 0.3429 0.3591 -0.0479 -0.0143 -0.0053 234 GLU A OE1 
1912 O  OE2 . GLU A 233 ? 0.3686 0.3754 0.3184 -0.0742 -0.0202 -0.0089 234 GLU A OE2 
1913 N  N   . GLY A 234 ? 0.2927 0.3065 0.2453 -0.0073 0.0526  -0.0002 235 GLY A N   
1914 C  CA  . GLY A 234 ? 0.3056 0.3416 0.2762 -0.0003 0.0337  0.0011  235 GLY A CA  
1915 C  C   . GLY A 234 ? 0.3212 0.3673 0.2688 -0.0005 0.0306  0.0164  235 GLY A C   
1916 O  O   . GLY A 234 ? 0.3275 0.3924 0.2805 0.0076  0.0454  0.0142  235 GLY A O   
1917 N  N   . GLU A 235 ? 0.3258 0.3636 0.2731 -0.0108 0.0413  0.0048  236 GLU A N   
1918 C  CA  . GLU A 235 ? 0.3349 0.3676 0.2867 -0.0018 0.0365  0.0138  236 GLU A CA  
1919 C  C   . GLU A 235 ? 0.3332 0.3983 0.2921 -0.0087 0.0428  0.0091  236 GLU A C   
1920 O  O   . GLU A 235 ? 0.3435 0.4168 0.3010 -0.0129 0.0684  0.0244  236 GLU A O   
1921 C  CB  . GLU A 235 ? 0.3341 0.3680 0.3058 0.0023  0.0302  0.0069  236 GLU A CB  
1922 C  CG  . GLU A 235 ? 0.3438 0.3658 0.3067 -0.0078 0.0544  0.0196  236 GLU A CG  
1923 C  CD  . GLU A 235 ? 0.4195 0.3945 0.3606 -0.0100 0.0217  0.0063  236 GLU A CD  
1924 O  OE1 . GLU A 235 ? 0.4427 0.4661 0.4387 -0.0596 0.0890  0.0364  236 GLU A OE1 
1925 O  OE2 . GLU A 235 ? 0.4609 0.4329 0.4037 -0.0467 0.0554  0.0367  236 GLU A OE2 
1926 N  N   . PRO A 236 ? 0.3285 0.3844 0.2724 -0.0060 0.0497  0.0261  237 PRO A N   
1927 C  CA  . PRO A 236 ? 0.3222 0.4014 0.2863 -0.0172 0.0552  0.0070  237 PRO A CA  
1928 C  C   . PRO A 236 ? 0.3082 0.3668 0.2638 -0.0207 0.0534  0.0012  237 PRO A C   
1929 O  O   . PRO A 236 ? 0.2939 0.3780 0.2305 -0.0201 0.0657  -0.0032 237 PRO A O   
1930 C  CB  . PRO A 236 ? 0.3350 0.4186 0.3088 -0.0119 0.0450  0.0161  237 PRO A CB  
1931 C  CG  . PRO A 236 ? 0.3545 0.4029 0.2772 -0.0064 0.0360  0.0458  237 PRO A CG  
1932 C  CD  . PRO A 236 ? 0.3639 0.4073 0.2932 -0.0150 0.0271  0.0121  237 PRO A CD  
1933 N  N   . GLU A 237 ? 0.2853 0.3523 0.2606 -0.0148 0.0431  -0.0195 238 GLU A N   
1934 C  CA  . GLU A 237 ? 0.2657 0.2950 0.2169 -0.0279 0.0343  -0.0247 238 GLU A CA  
1935 C  C   . GLU A 237 ? 0.2677 0.2735 0.2232 -0.0243 0.0226  -0.0273 238 GLU A C   
1936 O  O   . GLU A 237 ? 0.2749 0.2801 0.2036 -0.0254 0.0161  -0.0346 238 GLU A O   
1937 C  CB  . GLU A 237 ? 0.2689 0.3111 0.2506 -0.0262 0.0282  -0.0372 238 GLU A CB  
1938 C  CG  . GLU A 237 ? 0.2561 0.2779 0.2341 -0.0105 0.0074  -0.0492 238 GLU A CG  
1939 C  CD  . GLU A 237 ? 0.2842 0.2913 0.2492 -0.0174 0.0156  -0.0462 238 GLU A CD  
1940 O  OE1 . GLU A 237 ? 0.3652 0.3486 0.3581 0.0123  -0.0013 -0.0765 238 GLU A OE1 
1941 O  OE2 . GLU A 237 ? 0.3121 0.1853 0.2564 -0.0245 0.0139  -0.0820 238 GLU A OE2 
1942 N  N   A GLU A 238 ? 0.2327 0.2196 0.1681 -0.0413 0.0215  -0.0352 239 GLU A N   
1943 N  N   B GLU A 238 ? 0.2329 0.2421 0.1935 -0.0408 0.0310  -0.0372 239 GLU A N   
1944 C  CA  A GLU A 238 ? 0.2262 0.2111 0.1737 -0.0266 0.0179  -0.0156 239 GLU A CA  
1945 C  CA  B GLU A 238 ? 0.1968 0.2215 0.1901 -0.0238 0.0308  -0.0231 239 GLU A CA  
1946 C  C   A GLU A 238 ? 0.1872 0.1562 0.1580 -0.0189 0.0193  -0.0265 239 GLU A C   
1947 C  C   B GLU A 238 ? 0.1691 0.1985 0.1718 -0.0305 0.0285  -0.0299 239 GLU A C   
1948 O  O   A GLU A 238 ? 0.2039 0.1285 0.1381 -0.0438 -0.0048 -0.0179 239 GLU A O   
1949 O  O   B GLU A 238 ? 0.1964 0.2072 0.1720 -0.0632 0.0241  -0.0187 239 GLU A O   
1950 C  CB  A GLU A 238 ? 0.1939 0.1489 0.1730 -0.0255 0.0144  -0.0115 239 GLU A CB  
1951 C  CB  B GLU A 238 ? 0.1591 0.2093 0.2155 -0.0231 0.0320  -0.0258 239 GLU A CB  
1952 C  CG  A GLU A 238 ? 0.1995 0.1797 0.1682 0.0106  -0.0084 0.0101  239 GLU A CG  
1953 C  CG  B GLU A 238 ? 0.1782 0.1948 0.2420 0.0017  0.0109  -0.0256 239 GLU A CG  
1954 C  CD  A GLU A 238 ? 0.2422 0.2415 0.2249 -0.0161 0.0078  -0.0206 239 GLU A CD  
1955 C  CD  B GLU A 238 ? 0.2059 0.2429 0.1936 -0.0126 0.0126  -0.0006 239 GLU A CD  
1956 O  OE1 A GLU A 238 ? 0.2507 0.2757 0.2421 0.0306  0.0027  -0.0282 239 GLU A OE1 
1957 O  OE1 B GLU A 238 ? 0.2039 0.2843 0.1678 0.0114  0.0376  -0.0038 239 GLU A OE1 
1958 O  OE2 A GLU A 238 ? 0.3000 0.3280 0.2962 -0.0502 0.0061  0.0093  239 GLU A OE2 
1959 O  OE2 B GLU A 238 ? 0.2614 0.3143 0.2624 -0.0650 0.0198  0.0076  239 GLU A OE2 
1960 N  N   . LEU A 239 ? 0.1919 0.1886 0.1317 -0.0233 0.0538  -0.0152 240 LEU A N   
1961 C  CA  . LEU A 239 ? 0.1641 0.1504 0.1447 -0.0197 0.0352  -0.0259 240 LEU A CA  
1962 C  C   . LEU A 239 ? 0.1746 0.1411 0.1319 -0.0108 0.0305  -0.0097 240 LEU A C   
1963 O  O   . LEU A 239 ? 0.1801 0.2056 0.1570 -0.0340 0.0536  -0.0404 240 LEU A O   
1964 C  CB  . LEU A 239 ? 0.1986 0.1351 0.1509 -0.0050 0.0217  -0.0132 240 LEU A CB  
1965 C  CG  . LEU A 239 ? 0.1792 0.1597 0.1790 0.0108  0.0032  -0.0264 240 LEU A CG  
1966 C  CD1 . LEU A 239 ? 0.2662 0.1493 0.2796 0.0287  -0.0191 -0.0378 240 LEU A CD1 
1967 C  CD2 . LEU A 239 ? 0.2553 0.1129 0.1535 0.0462  -0.0140 -0.0363 240 LEU A CD2 
1968 N  N   . MET A 240 ? 0.1784 0.1367 0.1289 -0.0303 0.0544  -0.0279 241 MET A N   
1969 C  CA  . MET A 240 ? 0.2092 0.1331 0.1242 -0.0178 0.0535  -0.0164 241 MET A CA  
1970 C  C   . MET A 240 ? 0.1951 0.1372 0.1294 -0.0233 0.0496  -0.0223 241 MET A C   
1971 O  O   . MET A 240 ? 0.1891 0.1325 0.1086 -0.0191 0.0271  -0.0185 241 MET A O   
1972 C  CB  . MET A 240 ? 0.2244 0.1443 0.1357 0.0012  0.0568  -0.0110 241 MET A CB  
1973 C  CG  . MET A 240 ? 0.2072 0.1416 0.1444 -0.0379 0.0446  -0.0218 241 MET A CG  
1974 S  SD  . MET A 240 ? 0.2804 0.1292 0.1683 -0.0481 0.0476  -0.0234 241 MET A SD  
1975 C  CE  . MET A 240 ? 0.2662 0.1228 0.1487 -0.0729 0.0712  0.0012  241 MET A CE  
1976 N  N   . VAL A 241 ? 0.1898 0.1016 0.1294 -0.0313 0.0343  -0.0163 242 VAL A N   
1977 C  CA  . VAL A 241 ? 0.1632 0.0846 0.1075 -0.0294 0.0217  -0.0345 242 VAL A CA  
1978 C  C   . VAL A 241 ? 0.1415 0.0925 0.1290 -0.0020 0.0202  -0.0392 242 VAL A C   
1979 O  O   . VAL A 241 ? 0.1390 0.1238 0.1430 -0.0259 0.0443  -0.0352 242 VAL A O   
1980 C  CB  . VAL A 241 ? 0.1285 0.0960 0.1435 -0.0037 0.0223  -0.0365 242 VAL A CB  
1981 C  CG1 . VAL A 241 ? 0.1449 0.1225 0.1044 -0.0376 0.0010  -0.0457 242 VAL A CG1 
1982 C  CG2 . VAL A 241 ? 0.1205 0.0983 0.1754 0.0053  0.0101  -0.0195 242 VAL A CG2 
1983 N  N   . ASP A 242 ? 0.1376 0.0703 0.0932 -0.0085 0.0229  -0.0252 243 ASP A N   
1984 C  CA  . ASP A 242 ? 0.1347 0.0617 0.1262 0.0102  0.0121  -0.0393 243 ASP A CA  
1985 C  C   . ASP A 242 ? 0.1214 0.0702 0.1078 -0.0169 -0.0104 -0.0166 243 ASP A C   
1986 O  O   . ASP A 242 ? 0.1424 0.1100 0.1688 -0.0285 0.0031  -0.0453 243 ASP A O   
1987 C  CB  . ASP A 242 ? 0.0892 0.0596 0.1343 -0.0097 -0.0121 -0.0261 243 ASP A CB  
1988 C  CG  . ASP A 242 ? 0.1291 0.0708 0.1270 0.0185  0.0040  -0.0007 243 ASP A CG  
1989 O  OD1 . ASP A 242 ? 0.1242 0.1503 0.1381 0.0190  0.0103  -0.0676 243 ASP A OD1 
1990 O  OD2 . ASP A 242 ? 0.1313 0.1180 0.1793 0.0136  0.0470  -0.0400 243 ASP A OD2 
1991 N  N   . ASN A 243 ? 0.1136 0.0524 0.0939 0.0150  0.0165  -0.0338 244 ASN A N   
1992 C  CA  . ASN A 243 ? 0.1256 0.0907 0.0689 0.0130  -0.0016 -0.0307 244 ASN A CA  
1993 C  C   . ASN A 243 ? 0.0977 0.0918 0.0670 -0.0087 0.0078  -0.0156 244 ASN A C   
1994 O  O   . ASN A 243 ? 0.1296 0.0915 0.0994 0.0057  0.0035  -0.0154 244 ASN A O   
1995 C  CB  . ASN A 243 ? 0.1363 0.1149 0.0789 -0.0070 -0.0004 -0.0429 244 ASN A CB  
1996 C  CG  . ASN A 243 ? 0.1418 0.1164 0.0702 -0.0215 -0.0172 0.0330  244 ASN A CG  
1997 O  OD1 . ASN A 243 ? 0.1403 0.0831 0.1495 -0.0117 0.0032  0.0233  244 ASN A OD1 
1998 N  ND2 . ASN A 243 ? 0.2122 0.1549 0.1369 -0.0579 -0.0204 0.0584  244 ASN A ND2 
1999 N  N   . TRP A 244 ? 0.1024 0.0702 0.0623 0.0017  0.0028  0.0050  245 TRP A N   
2000 C  CA  . TRP A 244 ? 0.1061 0.0615 0.0631 -0.0156 -0.0228 -0.0157 245 TRP A CA  
2001 C  C   . TRP A 244 ? 0.1016 0.0856 0.1049 -0.0060 -0.0158 0.0061  245 TRP A C   
2002 O  O   . TRP A 244 ? 0.1085 0.0927 0.1125 0.0224  -0.0208 -0.0287 245 TRP A O   
2003 C  CB  . TRP A 244 ? 0.1138 0.0269 0.1119 -0.0026 0.0135  -0.0119 245 TRP A CB  
2004 C  CG  . TRP A 244 ? 0.0634 0.0661 0.0907 -0.0115 -0.0143 0.0018  245 TRP A CG  
2005 C  CD1 . TRP A 244 ? 0.1174 0.0788 0.1363 0.0060  0.0311  -0.0160 245 TRP A CD1 
2006 C  CD2 . TRP A 244 ? 0.0902 0.0631 0.1150 0.0204  0.0151  -0.0048 245 TRP A CD2 
2007 N  NE1 . TRP A 244 ? 0.0951 0.0644 0.1143 -0.0067 0.0050  0.0138  245 TRP A NE1 
2008 C  CE2 . TRP A 244 ? 0.0866 0.0844 0.0956 -0.0063 -0.0063 0.0013  245 TRP A CE2 
2009 C  CE3 . TRP A 244 ? 0.1289 0.0662 0.1248 -0.0094 -0.0138 0.0148  245 TRP A CE3 
2010 C  CZ2 . TRP A 244 ? 0.1165 0.0706 0.1467 -0.0031 -0.0087 0.0030  245 TRP A CZ2 
2011 C  CZ3 . TRP A 244 ? 0.1551 0.0581 0.1432 0.0152  -0.0034 -0.0043 245 TRP A CZ3 
2012 C  CH2 . TRP A 244 ? 0.1331 0.0798 0.1413 0.0192  0.0074  0.0054  245 TRP A CH2 
2013 N  N   . ARG A 245 ? 0.1145 0.0567 0.0949 -0.0199 -0.0136 -0.0038 246 ARG A N   
2014 C  CA  . ARG A 245 ? 0.0996 0.0652 0.1022 -0.0126 -0.0126 -0.0030 246 ARG A CA  
2015 C  C   . ARG A 245 ? 0.1035 0.0772 0.1247 0.0052  -0.0057 -0.0024 246 ARG A C   
2016 O  O   . ARG A 245 ? 0.1063 0.1043 0.1141 0.0186  -0.0037 -0.0097 246 ARG A O   
2017 C  CB  . ARG A 245 ? 0.0983 0.0639 0.1063 -0.0150 0.0057  -0.0352 246 ARG A CB  
2018 C  CG  . ARG A 245 ? 0.0640 0.0537 0.1342 -0.0291 -0.0011 -0.0259 246 ARG A CG  
2019 C  CD  . ARG A 245 ? 0.1009 0.0674 0.1415 -0.0330 -0.0041 -0.0380 246 ARG A CD  
2020 N  NE  . ARG A 245 ? 0.0838 0.1045 0.1678 -0.0257 -0.0061 -0.0633 246 ARG A NE  
2021 C  CZ  . ARG A 245 ? 0.0755 0.1019 0.1126 -0.0463 0.0184  -0.0044 246 ARG A CZ  
2022 N  NH1 . ARG A 245 ? 0.0969 0.0916 0.1547 0.0154  0.0252  -0.0154 246 ARG A NH1 
2023 N  NH2 . ARG A 245 ? 0.0462 0.1688 0.1911 -0.0283 -0.0098 -0.0141 246 ARG A NH2 
2024 N  N   . PRO A 246 ? 0.1026 0.1075 0.1270 0.0043  -0.0132 0.0012  247 PRO A N   
2025 C  CA  . PRO A 246 ? 0.0876 0.0801 0.1245 0.0104  -0.0036 0.0099  247 PRO A CA  
2026 C  C   . PRO A 246 ? 0.0897 0.0932 0.1071 0.0174  -0.0133 0.0248  247 PRO A C   
2027 O  O   . PRO A 246 ? 0.1061 0.0763 0.1537 -0.0009 -0.0091 0.0148  247 PRO A O   
2028 C  CB  . PRO A 246 ? 0.1257 0.1213 0.1357 0.0475  0.0204  -0.0073 247 PRO A CB  
2029 C  CG  . PRO A 246 ? 0.1263 0.1704 0.2068 0.0616  0.0041  0.0455  247 PRO A CG  
2030 C  CD  . PRO A 246 ? 0.0853 0.0997 0.1779 0.0289  -0.0066 0.0089  247 PRO A CD  
2031 N  N   . ALA A 247 ? 0.1068 0.1043 0.0994 0.0114  0.0037  0.0128  248 ALA A N   
2032 C  CA  . ALA A 247 ? 0.1006 0.0943 0.0951 -0.0009 -0.0054 -0.0053 248 ALA A CA  
2033 C  C   . ALA A 247 ? 0.1008 0.0668 0.1017 0.0302  -0.0195 0.0213  248 ALA A C   
2034 O  O   . ALA A 247 ? 0.1434 0.0800 0.1476 0.0353  -0.0154 -0.0128 248 ALA A O   
2035 C  CB  . ALA A 247 ? 0.1425 0.1124 0.1063 0.0096  0.0199  0.0179  248 ALA A CB  
2036 N  N   . GLN A 248 ? 0.1123 0.0795 0.1267 0.0293  -0.0333 -0.0190 249 GLN A N   
2037 C  CA  . GLN A 248 ? 0.0979 0.0813 0.1341 0.0211  -0.0315 0.0007  249 GLN A CA  
2038 C  C   . GLN A 248 ? 0.1047 0.1237 0.1405 0.0381  -0.0329 0.0001  249 GLN A C   
2039 O  O   . GLN A 248 ? 0.0951 0.1208 0.1318 0.0092  -0.0254 0.0158  249 GLN A O   
2040 C  CB  . GLN A 248 ? 0.1343 0.0388 0.1387 0.0279  -0.0269 -0.0200 249 GLN A CB  
2041 C  CG  . GLN A 248 ? 0.1247 0.1056 0.1240 -0.0144 0.0058  -0.0034 249 GLN A CG  
2042 C  CD  . GLN A 248 ? 0.0909 0.1557 0.1352 -0.0348 0.0038  -0.0148 249 GLN A CD  
2043 O  OE1 . GLN A 248 ? 0.1077 0.1884 0.1559 -0.0283 -0.0221 -0.0433 249 GLN A OE1 
2044 N  NE2 . GLN A 248 ? 0.0840 0.1364 0.1835 -0.0032 -0.0256 -0.0289 249 GLN A NE2 
2045 N  N   . PRO A 249 ? 0.1394 0.1619 0.1419 0.0310  -0.0240 -0.0051 250 PRO A N   
2046 C  CA  . PRO A 249 ? 0.1298 0.1891 0.1331 0.0439  -0.0289 -0.0223 250 PRO A CA  
2047 C  C   . PRO A 249 ? 0.1223 0.1591 0.1315 0.0247  -0.0337 -0.0140 250 PRO A C   
2048 O  O   . PRO A 249 ? 0.1134 0.1743 0.1503 0.0144  -0.0179 0.0131  250 PRO A O   
2049 C  CB  . PRO A 249 ? 0.0938 0.2385 0.1487 0.0695  -0.0484 -0.0114 250 PRO A CB  
2050 C  CG  . PRO A 249 ? 0.1701 0.2777 0.1509 0.0327  -0.0635 -0.0255 250 PRO A CG  
2051 C  CD  . PRO A 249 ? 0.1120 0.2151 0.1718 0.0344  -0.0673 -0.0049 250 PRO A CD  
2052 N  N   . LEU A 250 ? 0.1413 0.1624 0.1301 0.0297  -0.0273 0.0020  251 LEU A N   
2053 C  CA  . LEU A 250 ? 0.1393 0.1511 0.1167 0.0117  -0.0086 0.0033  251 LEU A CA  
2054 C  C   . LEU A 250 ? 0.1595 0.1493 0.1516 0.0317  -0.0359 -0.0222 251 LEU A C   
2055 O  O   . LEU A 250 ? 0.1441 0.1203 0.1524 0.0407  -0.0367 -0.0036 251 LEU A O   
2056 C  CB  . LEU A 250 ? 0.1563 0.1487 0.1567 0.0163  -0.0152 0.0322  251 LEU A CB  
2057 C  CG  . LEU A 250 ? 0.1753 0.2016 0.1541 0.0078  0.0019  0.0116  251 LEU A CG  
2058 C  CD1 . LEU A 250 ? 0.1978 0.1203 0.1672 0.0078  -0.0240 -0.0064 251 LEU A CD1 
2059 C  CD2 . LEU A 250 ? 0.2348 0.1724 0.2207 0.0015  0.0496  -0.0172 251 LEU A CD2 
2060 N  N   A LYS A 251 ? 0.1644 0.1528 0.1518 0.0247  -0.0461 -0.0202 252 LYS A N   
2061 N  N   B LYS A 251 ? 0.1364 0.1080 0.1273 0.0209  -0.0505 -0.0246 252 LYS A N   
2062 C  CA  A LYS A 251 ? 0.1805 0.1851 0.1603 0.0142  -0.0283 -0.0120 252 LYS A CA  
2063 C  CA  B LYS A 251 ? 0.1353 0.1213 0.1175 0.0124  -0.0388 -0.0096 252 LYS A CA  
2064 C  C   A LYS A 251 ? 0.1879 0.2101 0.1875 0.0067  -0.0242 -0.0119 252 LYS A C   
2065 C  C   B LYS A 251 ? 0.1244 0.1324 0.1052 0.0089  -0.0458 0.0000  252 LYS A C   
2066 O  O   A LYS A 251 ? 0.2195 0.2185 0.1966 -0.0059 -0.0166 0.0028  252 LYS A O   
2067 O  O   B LYS A 251 ? 0.1658 0.1652 0.1456 0.0066  -0.0215 -0.0002 252 LYS A O   
2068 C  CB  A LYS A 251 ? 0.1672 0.1999 0.1606 0.0023  -0.0298 -0.0157 252 LYS A CB  
2069 C  CB  B LYS A 251 ? 0.1391 0.1276 0.1300 0.0061  -0.0391 -0.0061 252 LYS A CB  
2070 C  CG  A LYS A 251 ? 0.2012 0.2170 0.2018 0.0071  -0.0060 -0.0192 252 LYS A CG  
2071 C  CG  B LYS A 251 ? 0.1735 0.1600 0.1432 0.0000  -0.0113 -0.0114 252 LYS A CG  
2072 C  CD  A LYS A 251 ? 0.1753 0.2554 0.2238 -0.0081 -0.0040 -0.0065 252 LYS A CD  
2073 C  CD  B LYS A 251 ? 0.1563 0.1465 0.1641 0.0017  -0.0245 -0.0135 252 LYS A CD  
2074 C  CE  A LYS A 251 ? 0.1714 0.2374 0.2285 -0.0009 -0.0115 0.0126  252 LYS A CE  
2075 C  CE  B LYS A 251 ? 0.1888 0.2228 0.1966 0.0127  0.0043  -0.0133 252 LYS A CE  
2076 N  NZ  A LYS A 251 ? 0.1623 0.1930 0.2602 0.0208  -0.0071 0.0497  252 LYS A NZ  
2077 N  NZ  B LYS A 251 ? 0.1833 0.2279 0.2476 0.0322  0.0132  -0.0287 252 LYS A NZ  
2078 N  N   A ASN A 252 ? 0.2017 0.2203 0.1930 0.0130  -0.0215 -0.0165 253 ASN A N   
2079 N  N   B ASN A 252 ? 0.1223 0.1292 0.1021 0.0123  -0.0386 -0.0101 253 ASN A N   
2080 C  CA  A ASN A 252 ? 0.2167 0.2465 0.2293 0.0099  -0.0154 -0.0115 253 ASN A CA  
2081 C  CA  B ASN A 252 ? 0.1454 0.1778 0.1670 0.0121  -0.0259 -0.0093 253 ASN A CA  
2082 C  C   A ASN A 252 ? 0.1802 0.2259 0.1827 0.0249  -0.0162 -0.0023 253 ASN A C   
2083 C  C   B ASN A 252 ? 0.1429 0.1780 0.1578 0.0164  -0.0279 -0.0077 253 ASN A C   
2084 O  O   A ASN A 252 ? 0.1736 0.2134 0.2091 0.0121  -0.0297 0.0076  253 ASN A O   
2085 O  O   B ASN A 252 ? 0.1742 0.1668 0.2054 0.0324  -0.0214 0.0039  253 ASN A O   
2086 C  CB  A ASN A 252 ? 0.2678 0.2707 0.2660 0.0053  -0.0039 -0.0094 253 ASN A CB  
2087 C  CB  B ASN A 252 ? 0.1485 0.2049 0.1768 -0.0013 -0.0454 -0.0221 253 ASN A CB  
2088 C  CG  A ASN A 252 ? 0.3076 0.3199 0.2954 0.0058  -0.0146 -0.0107 253 ASN A CG  
2089 C  CG  B ASN A 252 ? 0.2359 0.2656 0.2626 0.0103  -0.0091 -0.0133 253 ASN A CG  
2090 O  OD1 A ASN A 252 ? 0.3418 0.4038 0.3261 -0.0006 0.0060  0.0100  253 ASN A OD1 
2091 O  OD1 B ASN A 252 ? 0.3607 0.3336 0.3236 0.0289  0.0068  0.0077  253 ASN A OD1 
2092 N  ND2 A ASN A 252 ? 0.3706 0.3728 0.4016 -0.0179 0.0004  -0.0039 253 ASN A ND2 
2093 N  ND2 B ASN A 252 ? 0.3166 0.3027 0.3806 0.0121  -0.0087 -0.0140 253 ASN A ND2 
2094 N  N   A ARG A 253 ? 0.1453 0.1798 0.1422 0.0252  -0.0391 0.0004  254 ARG A N   
2095 N  N   B ARG A 253 ? 0.1338 0.1833 0.1176 0.0214  -0.0233 -0.0097 254 ARG A N   
2096 C  CA  A ARG A 253 ? 0.1258 0.1631 0.1293 0.0238  0.0001  -0.0132 254 ARG A CA  
2097 C  CA  B ARG A 253 ? 0.1219 0.1601 0.0776 0.0129  -0.0135 -0.0181 254 ARG A CA  
2098 C  C   A ARG A 253 ? 0.1691 0.1708 0.1528 0.0053  -0.0113 -0.0149 254 ARG A C   
2099 C  C   B ARG A 253 ? 0.1587 0.1716 0.0880 0.0031  -0.0184 -0.0177 254 ARG A C   
2100 O  O   A ARG A 253 ? 0.1859 0.1466 0.1903 -0.0064 0.0006  -0.0146 254 ARG A O   
2101 O  O   B ARG A 253 ? 0.1676 0.1682 0.1067 -0.0017 0.0037  -0.0207 254 ARG A O   
2102 C  CB  A ARG A 253 ? 0.1288 0.1516 0.1191 0.0236  -0.0076 0.0168  254 ARG A CB  
2103 C  CB  B ARG A 253 ? 0.1246 0.1555 0.0800 0.0190  -0.0146 0.0156  254 ARG A CB  
2104 C  CG  A ARG A 253 ? 0.1049 0.0869 0.0857 0.0161  0.0255  -0.0368 254 ARG A CG  
2105 C  CG  B ARG A 253 ? 0.0861 0.0981 0.1053 -0.0111 -0.0296 -0.0320 254 ARG A CG  
2106 C  CD  A ARG A 253 ? 0.0904 0.1205 0.0942 0.0012  -0.0089 -0.0283 254 ARG A CD  
2107 C  CD  B ARG A 253 ? 0.1337 0.0887 0.0775 0.0479  0.0135  -0.0062 254 ARG A CD  
2108 N  NE  A ARG A 253 ? 0.0658 0.0841 0.1020 0.0137  -0.0101 -0.0028 254 ARG A NE  
2109 N  NE  B ARG A 253 ? 0.0536 0.1069 0.0416 0.0154  0.0104  -0.0191 254 ARG A NE  
2110 C  CZ  A ARG A 253 ? 0.0617 0.0526 0.0883 -0.0206 -0.0201 -0.0059 254 ARG A CZ  
2111 C  CZ  B ARG A 253 ? 0.0295 0.1043 0.0669 -0.0182 0.0029  -0.0155 254 ARG A CZ  
2112 N  NH1 A ARG A 253 ? 0.0688 0.0325 0.1011 -0.0161 -0.0257 0.0008  254 ARG A NH1 
2113 N  NH1 B ARG A 253 ? 0.0334 0.0915 0.0789 -0.0139 0.0027  0.0217  254 ARG A NH1 
2114 N  NH2 A ARG A 253 ? 0.0577 0.0563 0.0847 -0.0220 -0.0080 -0.0248 254 ARG A NH2 
2115 N  NH2 B ARG A 253 ? 0.1065 0.0747 0.1128 -0.0107 -0.0004 -0.0015 254 ARG A NH2 
2116 N  N   . GLN A 254 ? 0.1682 0.1908 0.1369 -0.0003 -0.0109 -0.0360 255 GLN A N   
2117 C  CA  . GLN A 254 ? 0.2066 0.2421 0.1523 -0.0066 -0.0122 -0.0404 255 GLN A CA  
2118 C  C   . GLN A 254 ? 0.2199 0.2027 0.1589 -0.0050 -0.0338 -0.0200 255 GLN A C   
2119 O  O   . GLN A 254 ? 0.2665 0.1853 0.2212 -0.0271 -0.0615 -0.0472 255 GLN A O   
2120 C  CB  . GLN A 254 ? 0.2126 0.2883 0.1695 -0.0057 0.0049  -0.0459 255 GLN A CB  
2121 C  CG  . GLN A 254 ? 0.3404 0.3852 0.2921 -0.0245 -0.0013 -0.0328 255 GLN A CG  
2122 C  CD  . GLN A 254 ? 0.4828 0.4652 0.4336 -0.0045 -0.0012 0.0056  255 GLN A CD  
2123 O  OE1 . GLN A 254 ? 0.5366 0.5848 0.5061 0.0001  -0.0310 -0.0279 255 GLN A OE1 
2124 N  NE2 . GLN A 254 ? 0.5277 0.5318 0.4286 -0.0394 0.0042  -0.0421 255 GLN A NE2 
2125 N  N   . ILE A 255 ? 0.1747 0.1718 0.0996 -0.0027 -0.0177 -0.0225 256 ILE A N   
2126 C  CA  . ILE A 255 ? 0.1433 0.1458 0.1261 0.0143  0.0116  -0.0192 256 ILE A CA  
2127 C  C   . ILE A 255 ? 0.1299 0.1298 0.1095 0.0063  0.0087  0.0130  256 ILE A C   
2128 O  O   . ILE A 255 ? 0.1660 0.1363 0.1460 0.0154  0.0253  0.0199  256 ILE A O   
2129 C  CB  . ILE A 255 ? 0.1082 0.1533 0.1042 0.0392  0.0172  -0.0218 256 ILE A CB  
2130 C  CG1 . ILE A 255 ? 0.1014 0.1425 0.1875 0.0542  0.0322  -0.0400 256 ILE A CG1 
2131 C  CG2 . ILE A 255 ? 0.1219 0.1862 0.0983 0.0338  -0.0205 -0.0244 256 ILE A CG2 
2132 C  CD1 . ILE A 255 ? 0.2204 0.1471 0.1552 -0.0078 0.0314  -0.0594 256 ILE A CD1 
2133 N  N   . LYS A 256 ? 0.1078 0.1349 0.1097 -0.0085 -0.0015 0.0149  257 LYS A N   
2134 C  CA  . LYS A 256 ? 0.1357 0.1358 0.1151 0.0055  -0.0004 -0.0069 257 LYS A CA  
2135 C  C   . LYS A 256 ? 0.1257 0.1178 0.1104 -0.0059 0.0182  0.0097  257 LYS A C   
2136 O  O   . LYS A 256 ? 0.1390 0.1774 0.0965 -0.0627 0.0199  0.0165  257 LYS A O   
2137 C  CB  . LYS A 256 ? 0.1775 0.1753 0.1435 0.0058  -0.0003 -0.0079 257 LYS A CB  
2138 C  CG  . LYS A 256 ? 0.2469 0.1857 0.2276 -0.0075 -0.0263 -0.0346 257 LYS A CG  
2139 C  CD  . LYS A 256 ? 0.3562 0.2976 0.3424 0.0091  0.0030  -0.0354 257 LYS A CD  
2140 C  CE  . LYS A 256 ? 0.4740 0.4660 0.4064 -0.0166 -0.0132 -0.0200 257 LYS A CE  
2141 N  NZ  . LYS A 256 ? 0.4865 0.5462 0.4755 -0.0303 0.0230  0.0058  257 LYS A NZ  
2142 N  N   . ALA A 257 ? 0.1327 0.1444 0.1404 -0.0301 0.0241  0.0217  258 ALA A N   
2143 C  CA  . ALA A 257 ? 0.1136 0.1275 0.1664 -0.0152 0.0246  0.0225  258 ALA A CA  
2144 C  C   . ALA A 257 ? 0.1312 0.1509 0.1356 -0.0024 0.0214  0.0064  258 ALA A C   
2145 O  O   . ALA A 257 ? 0.1471 0.1654 0.1424 0.0168  0.0212  -0.0201 258 ALA A O   
2146 C  CB  . ALA A 257 ? 0.1640 0.1157 0.2063 -0.0124 0.0289  0.0307  258 ALA A CB  
2147 N  N   . SER A 258 ? 0.1106 0.1433 0.1286 -0.0036 0.0019  -0.0087 259 SER A N   
2148 C  CA  . SER A 258 ? 0.1219 0.1882 0.1449 -0.0014 -0.0007 -0.0152 259 SER A CA  
2149 C  C   . SER A 258 ? 0.1229 0.1963 0.1726 0.0039  0.0213  0.0011  259 SER A C   
2150 O  O   . SER A 258 ? 0.1307 0.2716 0.2240 0.0051  0.0226  -0.0106 259 SER A O   
2151 C  CB  . SER A 258 ? 0.1496 0.1748 0.1460 -0.0139 -0.0029 -0.0125 259 SER A CB  
2152 O  OG  . SER A 258 ? 0.1308 0.1797 0.1071 -0.0296 0.0158  -0.0179 259 SER A OG  
2153 N  N   . PHE A 259 ? 0.1200 0.1929 0.1749 -0.0338 0.0307  0.0022  260 PHE A N   
2154 C  CA  . PHE A 259 ? 0.1462 0.2184 0.2123 -0.0382 0.0272  0.0147  260 PHE A CA  
2155 C  C   . PHE A 259 ? 0.2027 0.2642 0.2618 -0.0331 0.0145  0.0223  260 PHE A C   
2156 O  O   . PHE A 259 ? 0.2427 0.2177 0.2414 -0.0461 -0.0025 0.0612  260 PHE A O   
2157 C  CB  . PHE A 259 ? 0.1453 0.2089 0.2248 -0.0171 0.0086  -0.0144 260 PHE A CB  
2158 C  CG  . PHE A 259 ? 0.1883 0.2078 0.2452 -0.0061 0.0115  -0.0177 260 PHE A CG  
2159 C  CD1 . PHE A 259 ? 0.1773 0.1833 0.1856 0.0206  0.0265  -0.0152 260 PHE A CD1 
2160 C  CD2 . PHE A 259 ? 0.1972 0.2000 0.2432 0.0082  0.0201  0.0097  260 PHE A CD2 
2161 C  CE1 . PHE A 259 ? 0.1791 0.1877 0.2157 -0.0291 0.0335  -0.0312 260 PHE A CE1 
2162 C  CE2 . PHE A 259 ? 0.1961 0.2435 0.2499 -0.0130 0.0318  -0.0025 260 PHE A CE2 
2163 C  CZ  . PHE A 259 ? 0.1891 0.2314 0.2598 0.0031  0.0238  0.0062  260 PHE A CZ  
2164 N  N   . LYS A 260 ? 0.3135 0.3372 0.3488 -0.0428 0.0184  0.0379  261 LYS A N   
2165 C  CA  . LYS A 260 ? 0.4183 0.4294 0.4223 -0.0187 0.0161  0.0225  261 LYS A CA  
2166 C  C   . LYS A 260 ? 0.4432 0.4823 0.4686 -0.0058 0.0110  0.0142  261 LYS A C   
2167 O  O   . LYS A 260 ? 0.4723 0.5281 0.5001 -0.0061 0.0262  0.0111  261 LYS A O   
2168 C  CB  . LYS A 260 ? 0.4272 0.4208 0.4265 -0.0161 0.0225  0.0230  261 LYS A CB  
2169 C  CG  . LYS A 260 ? 0.4709 0.4786 0.4730 -0.0269 0.0196  0.0149  261 LYS A CG  
2170 C  CD  . LYS A 260 ? 0.5535 0.5324 0.5145 -0.0081 -0.0039 0.0039  261 LYS A CD  
2171 C  CE  . LYS A 260 ? 0.5397 0.5762 0.5434 -0.0022 0.0065  0.0044  261 LYS A CE  
2172 N  NZ  . LYS A 260 ? 0.5517 0.5598 0.5162 -0.0065 0.0042  0.0155  261 LYS A NZ  
2173 O  OXT . LYS A 260 ? 0.4790 0.5377 0.5232 0.0007  0.0281  0.0027  261 LYS A OXT 
2174 ZN ZN  . ZN  B .   ? 0.1136 0.0755 0.1023 -0.0093 -0.0085 -0.0061 262 ZN  A ZN  
2175 S  S   . DMS C .   ? 0.2680 0.3492 0.4211 -0.0028 0.0341  0.0158  263 DMS A S   
2176 O  O   . DMS C .   ? 0.3548 0.3049 0.4435 -0.0231 0.0279  0.0223  263 DMS A O   
2177 C  C1  . DMS C .   ? 0.2969 0.3059 0.2690 0.0214  0.0444  -0.0028 263 DMS A C1  
2178 C  C2  . DMS C .   ? 0.2392 0.2972 0.3249 -0.0153 0.0463  -0.0133 263 DMS A C2  
2179 N  N1  . J75 D .   ? 0.4675 0.4327 0.4953 -0.0167 -0.0079 0.0417  264 J75 A N1  
2180 C  C2  . J75 D .   ? 0.4785 0.4237 0.5031 -0.0244 -0.0027 0.0399  264 J75 A C2  
2181 N  N3  . J75 D .   ? 0.4868 0.4396 0.5132 -0.0035 0.0019  0.0445  264 J75 A N3  
2182 C  C4  . J75 D .   ? 0.4860 0.4410 0.4956 -0.0053 -0.0138 0.0384  264 J75 A C4  
2183 C  C5  . J75 D .   ? 0.4663 0.4483 0.4849 -0.0089 -0.0162 0.0371  264 J75 A C5  
2184 C  C6  . J75 D .   ? 0.4671 0.4293 0.4853 -0.0085 -0.0115 0.0416  264 J75 A C6  
2185 N  N7  . J75 D .   ? 0.4419 0.4064 0.4746 0.0045  0.0122  0.0264  264 J75 A N7  
2186 C  C8  . J75 D .   ? 0.3571 0.3198 0.3395 0.0009  0.0065  0.0086  264 J75 A C8  
2187 C  C9  . J75 D .   ? 0.3401 0.2919 0.3799 -0.0059 0.0191  0.0105  264 J75 A C9  
2188 C  C10 . J75 D .   ? 0.3096 0.2644 0.3856 -0.0275 0.0437  -0.0055 264 J75 A C10 
2189 C  C11 . J75 D .   ? 0.2758 0.2419 0.3003 -0.0113 0.0347  -0.0060 264 J75 A C11 
2190 C  C12 . J75 D .   ? 0.2877 0.2972 0.3206 0.0050  -0.0164 -0.0041 264 J75 A C12 
2191 C  C13 . J75 D .   ? 0.3138 0.3009 0.3493 0.0039  -0.0028 -0.0083 264 J75 A C13 
2192 S  S14 . J75 D .   ? 0.2605 0.2688 0.2878 -0.0060 0.0109  0.0081  264 J75 A S14 
2193 O  O15 . J75 D .   ? 0.2174 0.3494 0.2628 0.0284  0.0250  0.0111  264 J75 A O15 
2194 O  O16 . J75 D .   ? 0.1321 0.1599 0.2070 0.0441  -0.0366 -0.0002 264 J75 A O16 
2195 N  N17 . J75 D .   ? 0.1947 0.1244 0.2080 -0.0502 -0.0102 -0.0114 264 J75 A N17 
2196 N  N18 . J75 D .   ? 0.4737 0.4389 0.4618 -0.0239 -0.0251 0.0337  264 J75 A N18 
2197 O  O19 . J75 D .   ? 0.5090 0.5001 0.5274 -0.0013 -0.0467 0.0216  264 J75 A O19 
2198 O  O20 . J75 D .   ? 0.3851 0.3025 0.3677 -0.0462 -0.0509 -0.0001 264 J75 A O20 
2199 N  N21 . J75 D .   ? 0.4762 0.4293 0.4926 0.0092  0.0002  0.0270  264 J75 A N21 
2200 C  C22 . J75 D .   ? 0.5123 0.4379 0.4704 -0.0223 -0.0007 0.0323  264 J75 A C22 
2201 C  C23 . J75 D .   ? 0.5261 0.4826 0.4589 -0.0008 0.0143  0.0111  264 J75 A C23 
2202 C  C24 . J75 D .   ? 0.5279 0.5129 0.4660 -0.0123 0.0134  0.0082  264 J75 A C24 
2203 C  C25 . J75 D .   ? 0.5214 0.5009 0.4359 -0.0164 0.0001  0.0164  264 J75 A C25 
2204 C  C26 . J75 D .   ? 0.5057 0.4569 0.3632 -0.0019 0.0147  0.0330  264 J75 A C26 
2205 C  C27 . J75 D .   ? 0.5122 0.4680 0.4640 -0.0325 0.0407  0.0096  264 J75 A C27 
2206 C  C28 . J75 D .   ? 0.4939 0.4775 0.4560 -0.0336 0.0322  0.0180  264 J75 A C28 
2207 C  C29 . J75 D .   ? 0.4027 0.3586 0.4078 -0.0215 0.0248  0.0225  264 J75 A C29 
2208 O  O   . HOH E .   ? 0.2857 0.2704 0.3958 0.0471  0.0210  0.0421  126 HOH A O   
2209 O  O   . HOH E .   ? 0.4804 0.2473 0.4771 -0.0016 -0.0402 -0.0655 265 HOH A O   
2210 O  O   . HOH E .   ? 0.4595 0.4415 0.4546 0.0056  0.0633  0.0519  266 HOH A O   
2211 O  O   . HOH E .   ? 0.4578 0.2555 0.4802 0.0088  -0.0609 -0.0158 267 HOH A O   
2212 O  O   . HOH E .   ? 0.5384 0.4962 0.3417 0.0105  0.0663  -0.0223 268 HOH A O   
2213 O  O   . HOH E .   ? 0.5200 0.4052 0.3923 0.0014  -0.0122 0.0027  269 HOH A O   
2214 O  O   . HOH E .   ? 0.3014 0.4536 0.4114 -0.0781 0.0125  0.0619  270 HOH A O   
2215 O  O   . HOH E .   ? 0.4723 0.4328 0.5264 -0.0604 -0.0211 -0.0217 271 HOH A O   
2216 O  O   . HOH E .   ? 0.5740 0.3907 0.3848 0.0836  -0.0744 0.0501  273 HOH A O   
2217 O  O   . HOH E .   ? 0.4400 0.3696 0.5756 -0.0010 -0.0103 -0.0362 274 HOH A O   
2218 O  O   . HOH E .   ? 0.5309 0.5765 0.4760 0.0107  -0.0142 -0.0287 275 HOH A O   
2219 O  O   . HOH E .   ? 0.4184 0.5354 0.3834 -0.0424 0.0317  -0.0168 276 HOH A O   
2220 O  O   . HOH E .   ? 0.3990 0.4302 0.3314 0.0091  -0.0117 -0.0062 277 HOH A O   
2221 O  O   . HOH E .   ? 0.5065 0.5284 0.5366 -0.0122 0.0370  0.0252  278 HOH A O   
2222 O  O   . HOH E .   ? 0.3470 0.3493 0.2948 0.0006  -0.0441 0.0065  279 HOH A O   
2223 O  O   . HOH E .   ? 0.4573 0.3516 0.4488 0.0544  -0.0047 -0.0482 280 HOH A O   
2224 O  O   . HOH E .   ? 0.4547 0.3882 0.4026 0.0543  0.0171  -0.0846 281 HOH A O   
2225 O  O   . HOH E .   ? 0.5134 0.4083 0.4107 0.0792  -0.0075 0.0064  282 HOH A O   
2226 O  O   . HOH E .   ? 0.3535 0.4604 0.4234 0.0409  0.0101  -0.0208 283 HOH A O   
2227 O  O   . HOH E .   ? 0.5474 0.4393 0.3791 0.0071  0.0646  -0.0408 284 HOH A O   
2228 O  O   . HOH E .   ? 0.3767 0.5323 0.3779 0.0407  -0.0340 0.0604  285 HOH A O   
2229 O  O   . HOH E .   ? 0.3590 0.4992 0.3375 -0.0292 -0.0895 0.0255  286 HOH A O   
2230 O  O   . HOH E .   ? 0.4325 0.4458 0.3606 -0.0074 -0.0256 -0.1208 287 HOH A O   
2231 O  O   . HOH E .   ? 0.5424 0.5289 0.3470 0.0165  0.0323  -0.0511 288 HOH A O   
2232 O  O   . HOH E .   ? 0.4962 0.3651 0.4059 -0.0252 0.0481  -0.0666 289 HOH A O   
2233 O  O   . HOH E .   ? 0.5910 0.5612 0.3722 0.0275  0.0338  -0.0532 290 HOH A O   
2234 O  O   . HOH E .   ? 0.5009 0.3893 0.4894 0.0170  -0.0421 -0.0209 291 HOH A O   
2235 O  O   . HOH E .   ? 0.5383 0.5395 0.6146 -0.0407 0.0027  0.0317  292 HOH A O   
2236 O  O   . HOH E .   ? 0.2553 0.3172 0.3598 0.0203  0.1054  0.0372  293 HOH A O   
2237 O  O   . HOH E .   ? 0.1019 0.1072 0.1130 -0.0454 0.0175  -0.0317 294 HOH A O   
2238 O  O   . HOH E .   ? 0.0562 0.1059 0.1019 -0.0005 0.0040  -0.0073 295 HOH A O   
2239 O  O   . HOH E .   ? 0.1448 0.0919 0.1367 0.0406  -0.0216 -0.0265 296 HOH A O   
2240 O  O   . HOH E .   ? 0.3593 0.0974 0.1630 0.0105  -0.0888 -0.0055 297 HOH A O   
2241 O  O   . HOH E .   ? 0.1663 0.0995 0.1254 -0.0187 -0.0127 -0.0274 298 HOH A O   
2242 O  O   . HOH E .   ? 0.0772 0.1304 0.2271 -0.0070 0.0113  0.0005  299 HOH A O   
2243 O  O   . HOH E .   ? 0.1690 0.1171 0.1480 0.0139  -0.0184 0.0124  300 HOH A O   
2244 O  O   . HOH E .   ? 0.2317 0.2001 0.2208 0.0108  0.0493  -0.0576 301 HOH A O   
2245 O  O   . HOH E .   ? 0.1706 0.2136 0.3004 0.0107  -0.1231 -0.0218 302 HOH A O   
2246 O  O   . HOH E .   ? 0.0684 0.1833 0.2232 -0.0003 0.0109  -0.0454 303 HOH A O   
2247 O  O   . HOH E .   ? 0.2528 0.1181 0.1859 -0.0089 -0.0842 0.0410  304 HOH A O   
2248 O  O   . HOH E .   ? 0.1141 0.1298 0.1263 0.0196  -0.0226 -0.0115 305 HOH A O   
2249 O  O   . HOH E .   ? 0.0812 0.1640 0.1597 -0.0103 -0.0527 0.0340  306 HOH A O   
2250 O  O   . HOH E .   ? 0.2209 0.1139 0.1811 -0.0216 -0.0198 -0.0472 307 HOH A O   
2251 O  O   . HOH E .   ? 0.1315 0.0743 0.2221 -0.0012 -0.0065 -0.0278 308 HOH A O   
2252 O  O   . HOH E .   ? 0.1994 0.1963 0.1753 0.0342  -0.0647 0.0034  309 HOH A O   
2253 O  O   . HOH E .   ? 0.1498 0.2067 0.1581 0.0227  -0.0679 0.0363  310 HOH A O   
2254 O  O   . HOH E .   ? 0.1282 0.0738 0.1758 0.0068  -0.0075 0.0246  311 HOH A O   
2255 O  O   . HOH E .   ? 0.2811 0.1552 0.1739 0.0366  0.0275  0.0718  312 HOH A O   
2256 O  O   . HOH E .   ? 0.2247 0.0591 0.0922 -0.0350 -0.0030 0.0031  313 HOH A O   
2257 O  O   . HOH E .   ? 0.2218 0.1543 0.2670 -0.0099 0.0458  -0.0329 314 HOH A O   
2258 O  O   . HOH E .   ? 0.1360 0.0737 0.1462 0.0064  -0.0257 -0.0318 315 HOH A O   
2259 O  O   . HOH E .   ? 0.1488 0.1395 0.1738 0.0288  -0.0179 -0.0128 316 HOH A O   
2260 O  O   . HOH E .   ? 0.0863 0.1549 0.3107 -0.0306 0.0010  -0.0226 317 HOH A O   
2261 O  O   . HOH E .   ? 0.1771 0.1550 0.2290 0.0161  -0.0543 -0.0213 318 HOH A O   
2262 O  O   . HOH E .   ? 0.2818 0.1158 0.1809 -0.0378 -0.0040 0.0311  319 HOH A O   
2263 O  O   . HOH E .   ? 0.3808 0.2332 0.1701 0.0085  -0.0797 -0.0127 320 HOH A O   
2264 O  O   . HOH E .   ? 0.3217 0.1372 0.1867 -0.0021 -0.0905 0.0005  321 HOH A O   
2265 O  O   . HOH E .   ? 0.2144 0.1282 0.2700 -0.0146 0.0131  -0.0125 322 HOH A O   
2266 O  O   . HOH E .   ? 0.1826 0.2848 0.1972 0.0539  -0.0329 -0.0309 323 HOH A O   
2267 O  O   . HOH E .   ? 0.3114 0.1976 0.3027 0.0476  0.0674  0.0480  324 HOH A O   
2268 O  O   . HOH E .   ? 0.1892 0.0927 0.1785 -0.0206 -0.0198 -0.0104 325 HOH A O   
2269 O  O   . HOH E .   ? 0.5336 0.5004 0.2888 -0.0423 -0.0654 0.0170  326 HOH A O   
2270 O  O   . HOH E .   ? 0.1428 0.2778 0.3151 -0.0294 -0.0302 0.0240  327 HOH A O   
2271 O  O   . HOH E .   ? 0.2517 0.1468 0.2358 0.0256  -0.0215 0.0137  328 HOH A O   
2272 O  O   . HOH E .   ? 0.1579 0.1635 0.2818 0.0069  -0.0457 -0.0077 329 HOH A O   
2273 O  O   . HOH E .   ? 0.2119 0.2058 0.2330 -0.0024 -0.0042 0.0498  330 HOH A O   
2274 O  O   . HOH E .   ? 0.2382 0.2999 0.3610 0.0135  -0.0434 -0.0092 331 HOH A O   
2275 O  O   . HOH E .   ? 0.2266 0.2157 0.2339 -0.0816 -0.0340 -0.0558 332 HOH A O   
2276 O  O   . HOH E .   ? 0.5052 0.2840 0.1484 0.0211  0.0165  -0.0013 333 HOH A O   
2277 O  O   . HOH E .   ? 0.0860 0.3040 0.3013 0.0368  -0.0198 0.0728  334 HOH A O   
2278 O  O   . HOH E .   ? 0.1409 0.1921 0.3084 0.0001  -0.0403 0.0113  335 HOH A O   
2279 O  O   . HOH E .   ? 0.2403 0.1691 0.3297 0.0764  -0.0577 -0.0461 336 HOH A O   
2280 O  O   . HOH E .   ? 0.1759 0.2865 0.1599 0.0060  0.0119  -0.0044 337 HOH A O   
2281 O  O   . HOH E .   ? 0.3935 0.1695 0.2362 -0.0728 -0.0910 -0.0140 338 HOH A O   
2282 O  O   . HOH E .   ? 0.2878 0.3195 0.2457 -0.0117 0.0291  0.0100  339 HOH A O   
2283 O  O   . HOH E .   ? 0.2896 0.3272 0.2282 -0.0152 -0.0280 0.0165  340 HOH A O   
2284 O  O   . HOH E .   ? 0.3759 0.2387 0.1890 -0.1007 0.0743  0.0031  341 HOH A O   
2285 O  O   . HOH E .   ? 0.2931 0.1723 0.1946 0.0474  -0.0400 0.0159  342 HOH A O   
2286 O  O   . HOH E .   ? 0.3372 0.2721 0.2877 0.0359  -0.0184 -0.0116 343 HOH A O   
2287 O  O   . HOH E .   ? 0.3501 0.2150 0.3277 -0.0459 0.0531  -0.1095 344 HOH A O   
2288 O  O   . HOH E .   ? 0.2541 0.3009 0.3742 -0.0139 0.0978  0.0326  345 HOH A O   
2289 O  O   . HOH E .   ? 0.2884 0.3482 0.2099 -0.0882 -0.0960 0.0364  346 HOH A O   
2290 O  O   . HOH E .   ? 0.2125 0.3315 0.3875 -0.0330 0.0139  -0.0100 347 HOH A O   
2291 O  O   . HOH E .   ? 0.2257 0.2816 0.2386 -0.0342 0.0129  0.0348  348 HOH A O   
2292 O  O   . HOH E .   ? 0.2159 0.2232 0.2457 -0.0206 -0.0125 0.0753  349 HOH A O   
2293 O  O   . HOH E .   ? 0.3062 0.1617 0.3833 0.1136  -0.0516 0.0425  350 HOH A O   
2294 O  O   . HOH E .   ? 0.5270 0.2242 0.2149 0.0135  0.0347  0.0577  351 HOH A O   
2295 O  O   . HOH E .   ? 0.2501 0.3096 0.3632 0.0063  -0.0144 0.0187  352 HOH A O   
2296 O  O   . HOH E .   ? 0.3773 0.2676 0.2239 -0.0939 -0.0182 -0.0462 353 HOH A O   
2297 O  O   . HOH E .   ? 0.4350 0.1738 0.2970 -0.0662 -0.0528 -0.0817 354 HOH A O   
2298 O  O   . HOH E .   ? 0.3194 0.3567 0.4885 0.0267  -0.0410 -0.0342 355 HOH A O   
2299 O  O   . HOH E .   ? 0.2775 0.2217 0.2772 -0.0526 -0.0411 0.0440  356 HOH A O   
2300 O  O   . HOH E .   ? 0.2035 0.1427 0.1831 -0.0247 -0.0005 0.0161  357 HOH A O   
2301 O  O   . HOH E .   ? 0.3287 0.1226 0.4188 0.0295  0.0651  0.0150  358 HOH A O   
2302 O  O   . HOH E .   ? 0.3620 0.3308 0.2534 -0.0086 0.0673  -0.0148 359 HOH A O   
2303 O  O   . HOH E .   ? 0.1665 0.1479 0.2734 -0.0714 -0.0367 -0.0313 360 HOH A O   
2304 O  O   . HOH E .   ? 0.2747 0.1725 0.3560 -0.0206 -0.0467 -0.0608 361 HOH A O   
2305 O  O   . HOH E .   ? 0.2686 0.2196 0.1610 -0.0396 -0.0193 -0.0255 362 HOH A O   
2306 O  O   . HOH E .   ? 0.2801 0.2833 0.1503 -0.0223 -0.0774 0.0273  363 HOH A O   
2307 O  O   . HOH E .   ? 0.2441 0.0619 0.1972 -0.0163 -0.0429 -0.0117 364 HOH A O   
2308 O  O   . HOH E .   ? 0.2526 0.0963 0.2135 0.0164  0.0106  0.0072  365 HOH A O   
2309 O  O   . HOH E .   ? 0.2876 0.1646 0.2486 0.0536  -0.0404 0.0527  366 HOH A O   
2310 O  O   . HOH E .   ? 0.2459 0.2331 0.3171 -0.0219 -0.0107 0.0335  367 HOH A O   
2311 O  O   . HOH E .   ? 0.1905 0.1402 0.3059 0.0020  0.0095  -0.0384 368 HOH A O   
2312 O  O   . HOH E .   ? 0.3532 0.2823 0.2090 -0.1732 -0.0847 0.0116  369 HOH A O   
2313 O  O   . HOH E .   ? 0.3246 0.1580 0.2100 0.0237  -0.0115 -0.0443 370 HOH A O   
2314 O  O   . HOH E .   ? 0.3478 0.2855 0.3343 -0.0239 -0.0098 0.0264  371 HOH A O   
2315 O  O   . HOH E .   ? 0.2091 0.1186 0.3592 0.0154  0.0421  -0.0190 372 HOH A O   
2316 O  O   . HOH E .   ? 0.2047 0.2165 0.3302 0.0213  -0.0596 0.0225  373 HOH A O   
2317 O  O   . HOH E .   ? 0.3979 0.2528 0.2147 0.0356  -0.0967 -0.0135 374 HOH A O   
2318 O  O   . HOH E .   ? 0.4181 0.2076 0.3007 0.0519  -0.0197 0.0644  375 HOH A O   
2319 O  O   . HOH E .   ? 0.2871 0.2626 0.2981 -0.0285 -0.0103 0.0196  376 HOH A O   
2320 O  O   . HOH E .   ? 0.3318 0.3536 0.4211 0.0678  -0.0397 -0.0300 377 HOH A O   
2321 O  O   . HOH E .   ? 0.3833 0.2803 0.4244 0.1097  -0.0112 -0.0130 378 HOH A O   
2322 O  O   . HOH E .   ? 0.2630 0.2375 0.3061 -0.0125 -0.0306 0.0324  379 HOH A O   
2323 O  O   . HOH E .   ? 0.3371 0.2929 0.3532 0.0586  0.0012  0.0550  380 HOH A O   
2324 O  O   . HOH E .   ? 0.2612 0.2354 0.2967 -0.0156 -0.0776 -0.0080 381 HOH A O   
2325 O  O   . HOH E .   ? 0.2749 0.2305 0.3175 -0.0498 0.0674  -0.0525 382 HOH A O   
2326 O  O   . HOH E .   ? 0.1350 0.2425 0.3679 0.0706  0.0282  -0.0048 383 HOH A O   
2327 O  O   . HOH E .   ? 0.2320 0.1833 0.3062 -0.0196 0.0288  0.0364  384 HOH A O   
2328 O  O   . HOH E .   ? 0.4022 0.3156 0.2536 0.0184  0.0213  -0.0917 385 HOH A O   
2329 O  O   . HOH E .   ? 0.3154 0.4204 0.3511 0.0691  0.0446  -0.0112 386 HOH A O   
2330 O  O   . HOH E .   ? 0.1748 0.2895 0.3765 0.0333  -0.0196 0.0147  387 HOH A O   
2331 O  O   . HOH E .   ? 0.2986 0.1833 0.3684 0.0190  -0.1611 -0.0075 388 HOH A O   
2332 O  O   . HOH E .   ? 0.4319 0.2278 0.2664 0.0137  -0.0295 0.1175  389 HOH A O   
2333 O  O   . HOH E .   ? 0.3052 0.2505 0.3382 -0.0361 -0.0705 0.0139  390 HOH A O   
2334 O  O   . HOH E .   ? 0.3121 0.3759 0.2358 0.0169  -0.0985 0.0474  391 HOH A O   
2335 O  O   . HOH E .   ? 0.3166 0.1882 0.2776 -0.0552 0.0293  0.0043  392 HOH A O   
2336 O  O   . HOH E .   ? 0.2480 0.1314 0.2985 0.0041  -0.0842 -0.0410 393 HOH A O   
2337 O  O   . HOH E .   ? 0.3137 0.2907 0.4522 -0.0032 -0.0021 0.0428  394 HOH A O   
2338 O  O   . HOH E .   ? 0.3279 0.1399 0.3257 0.0252  -0.0464 -0.0599 395 HOH A O   
2339 O  O   . HOH E .   ? 0.2731 0.3406 0.3460 0.0823  -0.0863 -0.0318 396 HOH A O   
2340 O  O   . HOH E .   ? 0.4152 0.2822 0.2209 -0.0591 0.0707  -0.1263 397 HOH A O   
2341 O  O   . HOH E .   ? 0.2830 0.3469 0.2798 0.1153  -0.0163 0.0073  399 HOH A O   
2342 O  O   . HOH E .   ? 0.2167 0.2754 0.2299 -0.0517 -0.0963 0.0397  400 HOH A O   
2343 O  O   . HOH E .   ? 0.5278 0.2751 0.1530 0.0023  -0.0081 -0.0418 401 HOH A O   
2344 O  O   . HOH E .   ? 0.3253 0.2999 0.3349 -0.0346 0.0395  -0.0269 402 HOH A O   
2345 O  O   . HOH E .   ? 0.4642 0.4527 0.4127 -0.0640 -0.0495 -0.0349 403 HOH A O   
2346 O  O   . HOH E .   ? 0.2094 0.5034 0.3686 -0.0382 -0.0972 -0.0924 404 HOH A O   
2347 O  O   . HOH E .   ? 0.2845 0.2776 0.3685 0.0522  -0.1111 -0.0593 405 HOH A O   
2348 O  O   . HOH E .   ? 0.3758 0.2031 0.2846 0.0198  -0.0588 0.0058  406 HOH A O   
2349 O  O   . HOH E .   ? 0.4209 0.3572 0.3149 -0.0709 0.0179  0.1164  407 HOH A O   
2350 O  O   . HOH E .   ? 0.4182 0.3690 0.4107 0.0170  -0.0148 0.0311  408 HOH A O   
2351 O  O   . HOH E .   ? 0.2954 0.2071 0.3372 0.0437  -0.0465 -0.0346 409 HOH A O   
2352 O  O   . HOH E .   ? 0.3477 0.2621 0.3011 0.0618  0.0593  0.0460  410 HOH A O   
2353 O  O   . HOH E .   ? 0.3558 0.3429 0.3292 -0.0714 0.0238  0.0404  411 HOH A O   
2354 O  O   . HOH E .   ? 0.4149 0.1988 0.5006 -0.0522 0.0704  0.0386  412 HOH A O   
2355 O  O   . HOH E .   ? 0.2468 0.2197 0.4142 0.0580  0.0210  0.0889  413 HOH A O   
2356 O  O   . HOH E .   ? 0.4127 0.2433 0.3109 -0.0013 -0.0216 -0.0697 414 HOH A O   
2357 O  O   . HOH E .   ? 0.3062 0.2817 0.2921 0.0194  -0.0247 -0.0336 415 HOH A O   
2358 O  O   . HOH E .   ? 0.3059 0.2990 0.3610 0.0336  -0.0269 0.0452  416 HOH A O   
2359 O  O   . HOH E .   ? 0.2843 0.3526 0.2644 0.0380  0.0341  -0.0338 417 HOH A O   
2360 O  O   . HOH E .   ? 0.3262 0.2377 0.4049 0.0064  0.0152  0.0686  418 HOH A O   
2361 O  O   . HOH E .   ? 0.3196 0.2704 0.2916 0.0473  0.0165  -0.0342 419 HOH A O   
2362 O  O   . HOH E .   ? 0.2502 0.3183 0.3731 -0.0426 -0.0351 -0.0540 420 HOH A O   
2363 O  O   . HOH E .   ? 0.2083 0.2849 0.4219 -0.0685 -0.0398 -0.0241 421 HOH A O   
2364 O  O   . HOH E .   ? 0.2830 0.2117 0.3152 0.0084  -0.0578 0.0217  422 HOH A O   
2365 O  O   . HOH E .   ? 0.2696 0.2911 0.4206 0.0635  0.0297  0.0274  423 HOH A O   
2366 O  O   . HOH E .   ? 0.3047 0.3549 0.3376 0.0179  0.0240  0.0887  424 HOH A O   
2367 O  O   . HOH E .   ? 0.3853 0.2460 0.2952 -0.0122 -0.0013 0.0383  425 HOH A O   
2368 O  O   . HOH E .   ? 0.4713 0.3058 0.3014 -0.0206 -0.0668 -0.0164 426 HOH A O   
2369 O  O   . HOH E .   ? 0.3703 0.3726 0.3375 0.0097  -0.0190 0.0602  427 HOH A O   
2370 O  O   . HOH E .   ? 0.3337 0.3222 0.2743 0.0140  -0.0067 -0.0369 428 HOH A O   
2371 O  O   . HOH E .   ? 0.1980 0.3166 0.3527 0.0208  0.0153  0.0057  429 HOH A O   
2372 O  O   . HOH E .   ? 0.3595 0.1849 0.3843 0.0108  -0.0618 0.0254  430 HOH A O   
2373 O  O   . HOH E .   ? 0.2250 0.2225 0.4339 0.0860  -0.0254 -0.0175 431 HOH A O   
2374 O  O   . HOH E .   ? 0.4242 0.2165 0.4108 0.0028  -0.0488 -0.0699 432 HOH A O   
2375 O  O   . HOH E .   ? 0.4807 0.3967 0.2596 -0.0589 0.0136  -0.0391 433 HOH A O   
2376 O  O   . HOH E .   ? 0.2257 0.2632 0.3468 -0.0255 -0.0529 -0.1330 434 HOH A O   
2377 O  O   . HOH E .   ? 0.4076 0.2686 0.2933 -0.0146 -0.0148 -0.0495 435 HOH A O   
2378 O  O   . HOH E .   ? 0.2728 0.2732 0.3363 0.0338  -0.0999 0.0007  436 HOH A O   
2379 O  O   . HOH E .   ? 0.3464 0.2177 0.3133 0.0729  0.0054  -0.0317 437 HOH A O   
2380 O  O   . HOH E .   ? 0.2426 0.2641 0.3235 0.0265  -0.0768 0.0142  438 HOH A O   
2381 O  O   . HOH E .   ? 0.3150 0.3842 0.3939 -0.0461 -0.1430 -0.0864 439 HOH A O   
2382 O  O   . HOH E .   ? 0.2162 0.2883 0.2857 -0.0452 0.0067  -0.0613 440 HOH A O   
2383 O  O   . HOH E .   ? 0.2677 0.3120 0.3694 0.0539  0.0481  -0.0077 441 HOH A O   
2384 O  O   . HOH E .   ? 0.3674 0.2493 0.3074 0.0282  0.0052  -0.0539 442 HOH A O   
2385 O  O   . HOH E .   ? 0.2493 0.2943 0.4242 -0.0688 -0.0309 -0.0798 443 HOH A O   
2386 O  O   . HOH E .   ? 0.2678 0.3509 0.3439 0.0088  0.0905  -0.0361 444 HOH A O   
2387 O  O   . HOH E .   ? 0.2979 0.3151 0.3103 0.0290  -0.0282 -0.0137 445 HOH A O   
2388 O  O   . HOH E .   ? 0.3284 0.3415 0.3492 0.0434  -0.0418 -0.0503 446 HOH A O   
2389 O  O   . HOH E .   ? 0.4709 0.2066 0.3790 -0.0655 0.0201  0.0860  447 HOH A O   
2390 O  O   . HOH E .   ? 0.2973 0.3552 0.3412 -0.0852 0.0762  -0.0633 448 HOH A O   
2391 O  O   . HOH E .   ? 0.2913 0.2607 0.3085 -0.0355 -0.0224 0.0008  449 HOH A O   
2392 O  O   . HOH E .   ? 0.3565 0.2689 0.4571 -0.0791 -0.0718 0.0214  450 HOH A O   
2393 O  O   . HOH E .   ? 0.3870 0.3691 0.3112 -0.0177 -0.1119 0.0479  451 HOH A O   
2394 O  O   . HOH E .   ? 0.4521 0.4749 0.4472 -0.0737 -0.0042 0.0461  452 HOH A O   
2395 O  O   . HOH E .   ? 0.4027 0.3317 0.4302 0.0097  0.0214  -0.0827 453 HOH A O   
2396 O  O   . HOH E .   ? 0.2755 0.4381 0.4782 0.0848  -0.0482 0.0317  454 HOH A O   
2397 O  O   . HOH E .   ? 0.2227 0.4909 0.3380 -0.0197 0.0423  0.0608  455 HOH A O   
2398 O  O   . HOH E .   ? 0.5396 0.3912 0.2908 -0.0863 0.0393  0.1139  456 HOH A O   
2399 O  O   . HOH E .   ? 0.4661 0.3902 0.5446 -0.0425 0.0353  -0.0279 457 HOH A O   
2400 O  O   . HOH E .   ? 0.3718 0.4739 0.5491 0.0884  -0.0077 0.0151  458 HOH A O   
2401 O  O   . HOH E .   ? 0.3539 0.2681 0.3386 -0.0604 0.0308  -0.0230 459 HOH A O   
2402 O  O   . HOH E .   ? 0.3938 0.3204 0.3545 -0.0632 -0.0838 -0.0589 460 HOH A O   
2403 O  O   . HOH E .   ? 0.3849 0.2715 0.4507 0.1361  -0.0979 -0.0028 461 HOH A O   
2404 O  O   . HOH E .   ? 0.2051 0.4598 0.3683 -0.0034 0.0366  0.0955  462 HOH A O   
2405 O  O   . HOH E .   ? 0.3399 0.3706 0.3619 -0.0547 -0.0463 -0.0212 463 HOH A O   
2406 O  O   . HOH E .   ? 0.2036 0.2904 0.2511 -0.0224 -0.0316 0.0336  464 HOH A O   
2407 O  O   . HOH E .   ? 0.2972 0.2622 0.3064 0.0155  0.0270  0.0435  465 HOH A O   
2408 O  O   . HOH E .   ? 0.3362 0.3395 0.2903 -0.0540 0.0392  -0.0245 466 HOH A O   
2409 O  O   . HOH E .   ? 0.3521 0.1965 0.4781 -0.0627 -0.0161 0.0326  467 HOH A O   
2410 O  O   . HOH E .   ? 0.4651 0.3418 0.2634 0.0264  -0.0506 0.0909  468 HOH A O   
2411 O  O   . HOH E .   ? 0.3463 0.3617 0.3770 0.0415  0.0784  -0.0587 469 HOH A O   
2412 O  O   . HOH E .   ? 0.4750 0.2256 0.5766 0.0196  -0.0807 0.0285  470 HOH A O   
2413 O  O   . HOH E .   ? 0.3687 0.4244 0.4271 0.0661  0.0576  -0.0055 471 HOH A O   
2414 O  O   . HOH E .   ? 0.3381 0.3066 0.4812 -0.0879 -0.0229 -0.0163 472 HOH A O   
2415 O  O   . HOH E .   ? 0.6233 0.2938 0.3780 -0.0258 0.0078  0.1030  473 HOH A O   
2416 O  O   . HOH E .   ? 0.5188 0.4801 0.2743 -0.0376 0.0518  0.0294  474 HOH A O   
2417 O  O   . HOH E .   ? 0.5136 0.5837 0.6235 -0.0274 -0.0383 -0.0162 475 HOH A O   
2418 O  O   . HOH E .   ? 0.4964 0.5692 0.6235 0.0034  -0.0033 -0.0268 476 HOH A O   
2419 O  O   . HOH E .   ? 0.2273 0.4297 0.4192 0.0561  0.0490  -0.0325 477 HOH A O   
2420 O  O   . HOH E .   ? 0.4761 0.2799 0.4094 -0.0256 -0.0339 -0.0572 478 HOH A O   
2421 O  O   . HOH E .   ? 0.5130 0.4295 0.4816 0.0056  0.0324  -0.0155 479 HOH A O   
2422 O  O   . HOH E .   ? 0.5388 0.5113 0.6065 -0.0129 0.0026  0.0498  480 HOH A O   
2423 O  O   . HOH E .   ? 0.3830 0.3108 0.3399 0.0695  0.0774  0.0838  481 HOH A O   
2424 O  O   . HOH E .   ? 0.2541 0.4933 0.4715 0.0506  -0.0329 -0.1017 482 HOH A O   
2425 O  O   . HOH E .   ? 0.5415 0.4272 0.4678 -0.0228 0.0283  -0.0414 483 HOH A O   
2426 O  O   . HOH E .   ? 0.3309 0.3034 0.4511 -0.0533 -0.0643 0.0231  484 HOH A O   
2427 O  O   . HOH E .   ? 0.3175 0.3382 0.4780 -0.0126 0.0967  -0.0415 485 HOH A O   
2428 O  O   . HOH E .   ? 0.3776 0.3694 0.4919 -0.0472 -0.0166 0.0508  486 HOH A O   
2429 O  O   . HOH E .   ? 0.5260 0.6060 0.3531 0.0077  0.0325  0.0195  487 HOH A O   
2430 O  O   . HOH E .   ? 0.3725 0.3847 0.4470 0.0888  -0.0472 0.0263  488 HOH A O   
2431 O  O   . HOH E .   ? 0.4689 0.3813 0.5077 -0.0538 0.0061  0.0010  489 HOH A O   
2432 O  O   . HOH E .   ? 0.3475 0.3133 0.4369 -0.1054 0.0105  0.0885  490 HOH A O   
2433 O  O   . HOH E .   ? 0.3076 0.3841 0.3859 -0.0271 0.0245  -0.0112 491 HOH A O   
2434 O  O   . HOH E .   ? 0.4932 0.4248 0.2882 -0.0041 -0.0337 0.0601  492 HOH A O   
2435 O  O   . HOH E .   ? 0.4031 0.4016 0.2844 0.0163  -0.0060 0.0106  493 HOH A O   
2436 O  O   . HOH E .   ? 0.4372 0.3980 0.4970 0.0246  -0.0284 0.0117  494 HOH A O   
2437 O  O   . HOH E .   ? 0.3661 0.2283 0.3400 0.0036  -0.0333 0.0165  495 HOH A O   
2438 O  O   . HOH E .   ? 0.4846 0.2449 0.3924 -0.0451 -0.0474 -0.1010 496 HOH A O   
2439 O  O   . HOH E .   ? 0.3526 0.2687 0.3716 -0.0582 -0.0225 -0.0087 497 HOH A O   
2440 O  O   . HOH E .   ? 0.4562 0.3393 0.4975 -0.0310 -0.0420 -0.0667 498 HOH A O   
2441 O  O   . HOH E .   ? 0.5009 0.4544 0.3584 -0.0016 -0.0261 -0.0151 499 HOH A O   
2442 O  O   . HOH E .   ? 0.3891 0.2621 0.4818 0.0264  -0.0310 0.0351  500 HOH A O   
2443 O  O   . HOH E .   ? 0.3392 0.4683 0.3694 -0.1560 -0.0626 -0.0167 501 HOH A O   
2444 O  O   . HOH E .   ? 0.4729 0.2975 0.4709 0.0427  -0.0041 -0.0515 502 HOH A O   
2445 O  O   . HOH E .   ? 0.3767 0.3555 0.3541 -0.0176 -0.0754 0.0425  503 HOH A O   
2446 O  O   . HOH E .   ? 0.5027 0.4848 0.4746 0.0110  0.0884  0.0068  504 HOH A O   
2447 O  O   . HOH E .   ? 0.2866 0.3412 0.3968 -0.0009 0.0240  0.0361  505 HOH A O   
2448 O  O   . HOH E .   ? 0.3815 0.3788 0.4533 -0.0054 0.1043  -0.0747 506 HOH A O   
2449 O  O   . HOH E .   ? 0.2952 0.3980 0.3658 0.0416  -0.0380 0.0466  507 HOH A O   
2450 O  O   . HOH E .   ? 0.3382 0.3979 0.3315 0.0012  -0.0336 -0.0189 508 HOH A O   
2451 O  O   . HOH E .   ? 0.4694 0.2667 0.4356 -0.0298 -0.0136 -0.0386 509 HOH A O   
2452 O  O   . HOH E .   ? 0.3517 0.2025 0.3640 -0.0026 0.0721  0.0159  510 HOH A O   
2453 O  O   . HOH E .   ? 0.2222 0.2985 0.3449 0.0510  -0.0541 0.0719  511 HOH A O   
2454 O  O   . HOH E .   ? 0.3871 0.2216 0.3629 -0.0419 -0.0425 0.0727  512 HOH A O   
2455 O  O   . HOH E .   ? 0.3018 0.3759 0.3364 -0.0158 0.0355  0.0251  513 HOH A O   
2456 O  O   . HOH E .   ? 0.2295 0.3270 0.4450 -0.0328 -0.0799 0.0519  514 HOH A O   
2457 O  O   . HOH E .   ? 0.2848 0.3692 0.5122 -0.0132 0.0023  -0.0173 515 HOH A O   
2458 O  O   . HOH E .   ? 0.5525 0.5468 0.5471 -0.0203 -0.0109 -0.0346 516 HOH A O   
2459 O  O   . HOH E .   ? 0.3550 0.4675 0.5505 -0.0035 -0.0078 -0.0233 517 HOH A O   
2460 O  O   . HOH E .   ? 0.4674 0.3766 0.5206 -0.0055 0.0394  -0.0280 518 HOH A O   
2461 O  O   . HOH E .   ? 0.4904 0.4377 0.3757 -0.0359 -0.0500 -0.0577 519 HOH A O   
2462 O  O   . HOH E .   ? 0.3454 0.3749 0.2169 -0.0966 0.0377  -0.0332 520 HOH A O   
2463 O  O   . HOH E .   ? 0.4227 0.3686 0.3380 0.1605  -0.1092 0.0867  521 HOH A O   
2464 O  O   . HOH E .   ? 0.3649 0.2452 0.5605 0.0329  0.0624  -0.0878 522 HOH A O   
2465 O  O   . HOH E .   ? 0.2627 0.4230 0.4123 -0.0891 -0.0157 0.0126  523 HOH A O   
2466 O  O   . HOH E .   ? 0.5681 0.3876 0.4239 -0.0002 0.0047  -0.0186 524 HOH A O   
2467 O  O   . HOH E .   ? 0.4964 0.3440 0.3296 -0.0518 0.0369  -0.0568 525 HOH A O   
2468 O  O   . HOH E .   ? 0.4264 0.4227 0.3783 0.0326  -0.0065 0.0494  526 HOH A O   
2469 O  O   . HOH E .   ? 0.4299 0.3429 0.4075 0.0464  -0.0167 0.0523  527 HOH A O   
2470 O  O   . HOH E .   ? 0.4257 0.5773 0.5721 0.0321  0.0177  -0.0222 528 HOH A O   
2471 O  O   . HOH E .   ? 0.4513 0.3581 0.4134 0.0914  0.0000  -0.0258 529 HOH A O   
2472 O  O   . HOH E .   ? 0.4503 0.2014 0.4710 0.0453  0.0011  -0.0879 530 HOH A O   
2473 O  O   . HOH E .   ? 0.4428 0.3632 0.3912 0.0376  -0.0201 0.0766  531 HOH A O   
2474 O  O   . HOH E .   ? 0.2942 0.3258 0.3279 0.1001  0.0155  0.0197  532 HOH A O   
2475 O  O   . HOH E .   ? 0.4368 0.3552 0.4687 0.0440  0.0205  0.0332  533 HOH A O   
2476 O  O   . HOH E .   ? 0.4546 0.3144 0.4092 0.0612  0.0441  -0.1006 534 HOH A O   
2477 O  O   . HOH E .   ? 0.2625 0.3365 0.4249 -0.0142 0.0064  0.0018  535 HOH A O   
2478 O  O   . HOH E .   ? 0.4045 0.5198 0.5403 -0.0192 -0.0603 -0.0502 536 HOH A O   
2479 O  O   A HOH E .   ? 0.2610 0.1656 0.2093 -0.1049 0.0221  0.0431  537 HOH A O   
2480 O  O   B HOH E .   ? 0.1288 0.1888 0.2333 -0.0260 -0.0009 0.0081  537 HOH A O   
2481 O  O   . HOH E .   ? 0.4775 0.2940 0.5135 -0.0278 -0.0883 -0.0340 538 HOH A O   
2482 O  O   . HOH E .   ? 0.4763 0.3095 0.3304 0.0047  0.0140  -0.0469 539 HOH A O   
2483 O  O   . HOH E .   ? 0.2573 0.4303 0.5555 -0.0771 0.0013  -0.0996 540 HOH A O   
2484 O  O   . HOH E .   ? 0.4088 0.3127 0.5270 0.0333  0.0657  -0.0136 541 HOH A O   
2485 O  O   . HOH E .   ? 0.3184 0.3335 0.4996 0.0000  -0.1062 -0.0301 542 HOH A O   
2486 O  O   . HOH E .   ? 0.2983 0.3033 0.5136 -0.0641 -0.0381 0.0948  543 HOH A O   
2487 O  O   . HOH E .   ? 0.3215 0.5270 0.5120 0.0430  0.0366  -0.0244 544 HOH A O   
2488 O  O   . HOH E .   ? 0.4163 0.2432 0.2309 0.1476  -0.0160 0.0330  545 HOH A O   
2489 O  O   . HOH E .   ? 0.4865 0.2477 0.2827 0.0407  -0.0578 0.0392  546 HOH A O   
2490 O  O   . HOH E .   ? 0.4925 0.2839 0.2053 -0.0552 0.0302  -0.0370 547 HOH A O   
2491 O  O   . HOH E .   ? 0.3613 0.2492 0.5276 -0.0663 0.0581  -0.0056 548 HOH A O   
2492 O  O   . HOH E .   ? 0.3964 0.4294 0.4073 0.0636  0.0280  0.0834  549 HOH A O   
2493 O  O   . HOH E .   ? 0.3956 0.2503 0.4763 0.0116  0.0608  0.0909  550 HOH A O   
2494 O  O   . HOH E .   ? 0.3623 0.4672 0.3688 -0.0403 0.0456  0.0210  551 HOH A O   
2495 O  O   . HOH E .   ? 0.5275 0.3633 0.2977 -0.0334 0.0680  0.0501  552 HOH A O   
2496 O  O   . HOH E .   ? 0.3997 0.5004 0.4399 -0.1108 0.0491  -0.0182 553 HOH A O   
2497 O  O   . HOH E .   ? 0.3661 0.5103 0.3565 0.0547  0.0066  -0.0707 554 HOH A O   
2498 O  O   . HOH E .   ? 0.5294 0.5096 0.4415 0.0245  -0.0790 -0.0158 555 HOH A O   
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   262 262 ZN  ZN  A . 
C 3 DMS 1   263 263 DMS DMS A . 
D 4 J75 1   264 264 J75 J75 A . 
E 5 HOH 1   126 126 HOH HOH A . 
E 5 HOH 2   265 265 HOH HOH A . 
E 5 HOH 3   266 266 HOH HOH A . 
E 5 HOH 4   267 267 HOH HOH A . 
E 5 HOH 5   268 268 HOH HOH A . 
E 5 HOH 6   269 269 HOH HOH A . 
E 5 HOH 7   270 270 HOH HOH A . 
E 5 HOH 8   271 271 HOH HOH A . 
E 5 HOH 9   273 273 HOH HOH A . 
E 5 HOH 10  274 274 HOH HOH A . 
E 5 HOH 11  275 275 HOH HOH A . 
E 5 HOH 12  276 276 HOH HOH A . 
E 5 HOH 13  277 277 HOH HOH A . 
E 5 HOH 14  278 278 HOH HOH A . 
E 5 HOH 15  279 279 HOH HOH A . 
E 5 HOH 16  280 280 HOH HOH A . 
E 5 HOH 17  281 281 HOH HOH A . 
E 5 HOH 18  282 282 HOH HOH A . 
E 5 HOH 19  283 283 HOH HOH A . 
E 5 HOH 20  284 284 HOH HOH A . 
E 5 HOH 21  285 285 HOH HOH A . 
E 5 HOH 22  286 286 HOH HOH A . 
E 5 HOH 23  287 287 HOH HOH A . 
E 5 HOH 24  288 288 HOH HOH A . 
E 5 HOH 25  289 289 HOH HOH A . 
E 5 HOH 26  290 290 HOH HOH A . 
E 5 HOH 27  291 291 HOH HOH A . 
E 5 HOH 28  292 292 HOH HOH A . 
E 5 HOH 29  293 293 HOH HOH A . 
E 5 HOH 30  294 294 HOH HOH A . 
E 5 HOH 31  295 295 HOH HOH A . 
E 5 HOH 32  296 296 HOH HOH A . 
E 5 HOH 33  297 297 HOH HOH A . 
E 5 HOH 34  298 298 HOH HOH A . 
E 5 HOH 35  299 299 HOH HOH A . 
E 5 HOH 36  300 300 HOH HOH A . 
E 5 HOH 37  301 301 HOH HOH A . 
E 5 HOH 38  302 302 HOH HOH A . 
E 5 HOH 39  303 303 HOH HOH A . 
E 5 HOH 40  304 304 HOH HOH A . 
E 5 HOH 41  305 305 HOH HOH A . 
E 5 HOH 42  306 306 HOH HOH A . 
E 5 HOH 43  307 307 HOH HOH A . 
E 5 HOH 44  308 308 HOH HOH A . 
E 5 HOH 45  309 309 HOH HOH A . 
E 5 HOH 46  310 310 HOH HOH A . 
E 5 HOH 47  311 311 HOH HOH A . 
E 5 HOH 48  312 312 HOH HOH A . 
E 5 HOH 49  313 313 HOH HOH A . 
E 5 HOH 50  314 314 HOH HOH A . 
E 5 HOH 51  315 315 HOH HOH A . 
E 5 HOH 52  316 316 HOH HOH A . 
E 5 HOH 53  317 317 HOH HOH A . 
E 5 HOH 54  318 318 HOH HOH A . 
E 5 HOH 55  319 319 HOH HOH A . 
E 5 HOH 56  320 320 HOH HOH A . 
E 5 HOH 57  321 321 HOH HOH A . 
E 5 HOH 58  322 322 HOH HOH A . 
E 5 HOH 59  323 323 HOH HOH A . 
E 5 HOH 60  324 324 HOH HOH A . 
E 5 HOH 61  325 325 HOH HOH A . 
E 5 HOH 62  326 326 HOH HOH A . 
E 5 HOH 63  327 327 HOH HOH A . 
E 5 HOH 64  328 328 HOH HOH A . 
E 5 HOH 65  329 329 HOH HOH A . 
E 5 HOH 66  330 330 HOH HOH A . 
E 5 HOH 67  331 331 HOH HOH A . 
E 5 HOH 68  332 332 HOH HOH A . 
E 5 HOH 69  333 333 HOH HOH A . 
E 5 HOH 70  334 334 HOH HOH A . 
E 5 HOH 71  335 335 HOH HOH A . 
E 5 HOH 72  336 336 HOH HOH A . 
E 5 HOH 73  337 337 HOH HOH A . 
E 5 HOH 74  338 338 HOH HOH A . 
E 5 HOH 75  339 339 HOH HOH A . 
E 5 HOH 76  340 340 HOH HOH A . 
E 5 HOH 77  341 341 HOH HOH A . 
E 5 HOH 78  342 342 HOH HOH A . 
E 5 HOH 79  343 343 HOH HOH A . 
E 5 HOH 80  344 344 HOH HOH A . 
E 5 HOH 81  345 345 HOH HOH A . 
E 5 HOH 82  346 346 HOH HOH A . 
E 5 HOH 83  347 347 HOH HOH A . 
E 5 HOH 84  348 348 HOH HOH A . 
E 5 HOH 85  349 349 HOH HOH A . 
E 5 HOH 86  350 350 HOH HOH A . 
E 5 HOH 87  351 351 HOH HOH A . 
E 5 HOH 88  352 352 HOH HOH A . 
E 5 HOH 89  353 353 HOH HOH A . 
E 5 HOH 90  354 354 HOH HOH A . 
E 5 HOH 91  355 355 HOH HOH A . 
E 5 HOH 92  356 356 HOH HOH A . 
E 5 HOH 93  357 357 HOH HOH A . 
E 5 HOH 94  358 358 HOH HOH A . 
E 5 HOH 95  359 359 HOH HOH A . 
E 5 HOH 96  360 360 HOH HOH A . 
E 5 HOH 97  361 361 HOH HOH A . 
E 5 HOH 98  362 362 HOH HOH A . 
E 5 HOH 99  363 363 HOH HOH A . 
E 5 HOH 100 364 364 HOH HOH A . 
E 5 HOH 101 365 365 HOH HOH A . 
E 5 HOH 102 366 366 HOH HOH A . 
E 5 HOH 103 367 367 HOH HOH A . 
E 5 HOH 104 368 368 HOH HOH A . 
E 5 HOH 105 369 369 HOH HOH A . 
E 5 HOH 106 370 370 HOH HOH A . 
E 5 HOH 107 371 371 HOH HOH A . 
E 5 HOH 108 372 372 HOH HOH A . 
E 5 HOH 109 373 373 HOH HOH A . 
E 5 HOH 110 374 374 HOH HOH A . 
E 5 HOH 111 375 375 HOH HOH A . 
E 5 HOH 112 376 376 HOH HOH A . 
E 5 HOH 113 377 377 HOH HOH A . 
E 5 HOH 114 378 378 HOH HOH A . 
E 5 HOH 115 379 379 HOH HOH A . 
E 5 HOH 116 380 380 HOH HOH A . 
E 5 HOH 117 381 381 HOH HOH A . 
E 5 HOH 118 382 382 HOH HOH A . 
E 5 HOH 119 383 383 HOH HOH A . 
E 5 HOH 120 384 384 HOH HOH A . 
E 5 HOH 121 385 385 HOH HOH A . 
E 5 HOH 122 386 386 HOH HOH A . 
E 5 HOH 123 387 387 HOH HOH A . 
E 5 HOH 124 388 388 HOH HOH A . 
E 5 HOH 125 389 389 HOH HOH A . 
E 5 HOH 126 390 390 HOH HOH A . 
E 5 HOH 127 391 391 HOH HOH A . 
E 5 HOH 128 392 392 HOH HOH A . 
E 5 HOH 129 393 393 HOH HOH A . 
E 5 HOH 130 394 394 HOH HOH A . 
E 5 HOH 131 395 395 HOH HOH A . 
E 5 HOH 132 396 396 HOH HOH A . 
E 5 HOH 133 397 397 HOH HOH A . 
E 5 HOH 134 399 399 HOH HOH A . 
E 5 HOH 135 400 400 HOH HOH A . 
E 5 HOH 136 401 401 HOH HOH A . 
E 5 HOH 137 402 402 HOH HOH A . 
E 5 HOH 138 403 403 HOH HOH A . 
E 5 HOH 139 404 404 HOH HOH A . 
E 5 HOH 140 405 405 HOH HOH A . 
E 5 HOH 141 406 406 HOH HOH A . 
E 5 HOH 142 407 407 HOH HOH A . 
E 5 HOH 143 408 408 HOH HOH A . 
E 5 HOH 144 409 409 HOH HOH A . 
E 5 HOH 145 410 410 HOH HOH A . 
E 5 HOH 146 411 411 HOH HOH A . 
E 5 HOH 147 412 412 HOH HOH A . 
E 5 HOH 148 413 413 HOH HOH A . 
E 5 HOH 149 414 414 HOH HOH A . 
E 5 HOH 150 415 415 HOH HOH A . 
E 5 HOH 151 416 416 HOH HOH A . 
E 5 HOH 152 417 417 HOH HOH A . 
E 5 HOH 153 418 418 HOH HOH A . 
E 5 HOH 154 419 419 HOH HOH A . 
E 5 HOH 155 420 420 HOH HOH A . 
E 5 HOH 156 421 421 HOH HOH A . 
E 5 HOH 157 422 422 HOH HOH A . 
E 5 HOH 158 423 423 HOH HOH A . 
E 5 HOH 159 424 424 HOH HOH A . 
E 5 HOH 160 425 425 HOH HOH A . 
E 5 HOH 161 426 426 HOH HOH A . 
E 5 HOH 162 427 427 HOH HOH A . 
E 5 HOH 163 428 428 HOH HOH A . 
E 5 HOH 164 429 429 HOH HOH A . 
E 5 HOH 165 430 430 HOH HOH A . 
E 5 HOH 166 431 431 HOH HOH A . 
E 5 HOH 167 432 432 HOH HOH A . 
E 5 HOH 168 433 433 HOH HOH A . 
E 5 HOH 169 434 434 HOH HOH A . 
E 5 HOH 170 435 435 HOH HOH A . 
E 5 HOH 171 436 436 HOH HOH A . 
E 5 HOH 172 437 437 HOH HOH A . 
E 5 HOH 173 438 438 HOH HOH A . 
E 5 HOH 174 439 439 HOH HOH A . 
E 5 HOH 175 440 440 HOH HOH A . 
E 5 HOH 176 441 441 HOH HOH A . 
E 5 HOH 177 442 442 HOH HOH A . 
E 5 HOH 178 443 443 HOH HOH A . 
E 5 HOH 179 444 444 HOH HOH A . 
E 5 HOH 180 445 445 HOH HOH A . 
E 5 HOH 181 446 446 HOH HOH A . 
E 5 HOH 182 447 447 HOH HOH A . 
E 5 HOH 183 448 448 HOH HOH A . 
E 5 HOH 184 449 449 HOH HOH A . 
E 5 HOH 185 450 450 HOH HOH A . 
E 5 HOH 186 451 451 HOH HOH A . 
E 5 HOH 187 452 452 HOH HOH A . 
E 5 HOH 188 453 453 HOH HOH A . 
E 5 HOH 189 454 454 HOH HOH A . 
E 5 HOH 190 455 455 HOH HOH A . 
E 5 HOH 191 456 456 HOH HOH A . 
E 5 HOH 192 457 457 HOH HOH A . 
E 5 HOH 193 458 458 HOH HOH A . 
E 5 HOH 194 459 459 HOH HOH A . 
E 5 HOH 195 460 460 HOH HOH A . 
E 5 HOH 196 461 461 HOH HOH A . 
E 5 HOH 197 462 462 HOH HOH A . 
E 5 HOH 198 463 463 HOH HOH A . 
E 5 HOH 199 464 464 HOH HOH A . 
E 5 HOH 200 465 465 HOH HOH A . 
E 5 HOH 201 466 466 HOH HOH A . 
E 5 HOH 202 467 467 HOH HOH A . 
E 5 HOH 203 468 468 HOH HOH A . 
E 5 HOH 204 469 469 HOH HOH A . 
E 5 HOH 205 470 470 HOH HOH A . 
E 5 HOH 206 471 471 HOH HOH A . 
E 5 HOH 207 472 472 HOH HOH A . 
E 5 HOH 208 473 473 HOH HOH A . 
E 5 HOH 209 474 474 HOH HOH A . 
E 5 HOH 210 475 475 HOH HOH A . 
E 5 HOH 211 476 476 HOH HOH A . 
E 5 HOH 212 477 477 HOH HOH A . 
E 5 HOH 213 478 478 HOH HOH A . 
E 5 HOH 214 479 479 HOH HOH A . 
E 5 HOH 215 480 480 HOH HOH A . 
E 5 HOH 216 481 481 HOH HOH A . 
E 5 HOH 217 482 482 HOH HOH A . 
E 5 HOH 218 483 483 HOH HOH A . 
E 5 HOH 219 484 484 HOH HOH A . 
E 5 HOH 220 485 485 HOH HOH A . 
E 5 HOH 221 486 486 HOH HOH A . 
E 5 HOH 222 487 487 HOH HOH A . 
E 5 HOH 223 488 488 HOH HOH A . 
E 5 HOH 224 489 489 HOH HOH A . 
E 5 HOH 225 490 490 HOH HOH A . 
E 5 HOH 226 491 491 HOH HOH A . 
E 5 HOH 227 492 492 HOH HOH A . 
E 5 HOH 228 493 493 HOH HOH A . 
E 5 HOH 229 494 494 HOH HOH A . 
E 5 HOH 230 495 495 HOH HOH A . 
E 5 HOH 231 496 496 HOH HOH A . 
E 5 HOH 232 497 497 HOH HOH A . 
E 5 HOH 233 498 498 HOH HOH A . 
E 5 HOH 234 499 499 HOH HOH A . 
E 5 HOH 235 500 500 HOH HOH A . 
E 5 HOH 236 501 501 HOH HOH A . 
E 5 HOH 237 502 502 HOH HOH A . 
E 5 HOH 238 503 503 HOH HOH A . 
E 5 HOH 239 504 504 HOH HOH A . 
E 5 HOH 240 505 505 HOH HOH A . 
E 5 HOH 241 506 506 HOH HOH A . 
E 5 HOH 242 507 507 HOH HOH A . 
E 5 HOH 243 508 508 HOH HOH A . 
E 5 HOH 244 509 509 HOH HOH A . 
E 5 HOH 245 510 510 HOH HOH A . 
E 5 HOH 246 511 511 HOH HOH A . 
E 5 HOH 247 512 512 HOH HOH A . 
E 5 HOH 248 513 513 HOH HOH A . 
E 5 HOH 249 514 514 HOH HOH A . 
E 5 HOH 250 515 515 HOH HOH A . 
E 5 HOH 251 516 516 HOH HOH A . 
E 5 HOH 252 517 517 HOH HOH A . 
E 5 HOH 253 518 518 HOH HOH A . 
E 5 HOH 254 519 519 HOH HOH A . 
E 5 HOH 255 520 520 HOH HOH A . 
E 5 HOH 256 521 521 HOH HOH A . 
E 5 HOH 257 522 522 HOH HOH A . 
E 5 HOH 258 523 523 HOH HOH A . 
E 5 HOH 259 524 524 HOH HOH A . 
E 5 HOH 260 525 525 HOH HOH A . 
E 5 HOH 261 526 526 HOH HOH A . 
E 5 HOH 262 527 527 HOH HOH A . 
E 5 HOH 263 528 528 HOH HOH A . 
E 5 HOH 264 529 529 HOH HOH A . 
E 5 HOH 265 530 530 HOH HOH A . 
E 5 HOH 266 531 531 HOH HOH A . 
E 5 HOH 267 532 532 HOH HOH A . 
E 5 HOH 268 533 533 HOH HOH A . 
E 5 HOH 269 534 534 HOH HOH A . 
E 5 HOH 270 535 535 HOH HOH A . 
E 5 HOH 271 536 536 HOH HOH A . 
E 5 HOH 272 537 537 HOH HOH A . 
E 5 HOH 273 538 538 HOH HOH A . 
E 5 HOH 274 539 539 HOH HOH A . 
E 5 HOH 275 540 540 HOH HOH A . 
E 5 HOH 276 541 541 HOH HOH A . 
E 5 HOH 277 542 542 HOH HOH A . 
E 5 HOH 278 543 543 HOH HOH A . 
E 5 HOH 279 544 544 HOH HOH A . 
E 5 HOH 280 545 545 HOH HOH A . 
E 5 HOH 281 546 546 HOH HOH A . 
E 5 HOH 282 547 547 HOH HOH A . 
E 5 HOH 283 548 548 HOH HOH A . 
E 5 HOH 284 549 549 HOH HOH A . 
E 5 HOH 285 550 550 HOH HOH A . 
E 5 HOH 286 551 551 HOH HOH A . 
E 5 HOH 287 552 552 HOH HOH A . 
E 5 HOH 288 553 553 HOH HOH A . 
E 5 HOH 289 554 554 HOH HOH A . 
E 5 HOH 290 555 555 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 
# 
_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_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 2010-10-20 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-08 
4 'Structure model' 1 3 2023-11-01 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Refinement description'    
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Derived calculations'      
6 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' software                      
2 4 'Structure model' chem_comp_atom                
3 4 'Structure model' chem_comp_bond                
4 4 'Structure model' database_2                    
5 4 'Structure model' diffrn_source                 
6 4 'Structure model' pdbx_initial_refinement_model 
7 4 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_software.name'                       
2 4 'Structure model' '_database_2.pdbx_DOI'                 
3 4 'Structure model' '_database_2.pdbx_database_accession'  
4 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
5 4 'Structure model' '_struct_site.pdbx_auth_asym_id'       
6 4 'Structure model' '_struct_site.pdbx_auth_comp_id'       
7 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       3.2.25                       21/9/2006       other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006                        'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345      'v. 0.9.7 on RedHat Linux 8' ?               ?       ?                    ?                        'data collection' ? 
?          ? 5 
O           .                            ?               ?       ?                    ?                        'model building'  ? 
?          ? 6 
# 
_pdbx_entry_details.entry_id                 3MHM 
_pdbx_entry_details.nonpolymer_details       'METAL ION NATURALLY OCCURS IN CARBONIC ANHYDRASES.' 
_pdbx_entry_details.sequence_details         '126 IS SKIPPED IN THE NUMBERING.' 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   ? 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NZ 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    LYS 
_pdbx_validate_symm_contact.auth_seq_id_1     257 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     291 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              1.98 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             14 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             14 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.336 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            0.084 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 101 ? ? CG A ASP 101 ? ? OD1 A ASP 101 ? ? 124.10 118.30 5.80 0.90 N 
2 1 CB A ASP 130 ? ? CG A ASP 130 ? ? OD1 A ASP 130 ? ? 123.84 118.30 5.54 0.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -141.77 56.91   
2 1 ALA A 65  ? ? -166.54 -166.86 
3 1 ASN A 244 ? ? -95.89  50.40   
4 1 LYS A 252 ? A 60.11   -129.72 
5 1 LYS A 252 ? B 46.13   -141.68 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    253 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   A 
_pdbx_validate_peptide_omega.auth_comp_id_2   ARG 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    254 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   A 
_pdbx_validate_peptide_omega.omega            -139.95 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
J75 N1   N  Y N 193 
J75 C2   C  Y N 194 
J75 N3   N  Y N 195 
J75 C4   C  Y N 196 
J75 C5   C  Y N 197 
J75 C6   C  Y N 198 
J75 N7   N  N N 199 
J75 C8   C  Y N 200 
J75 C9   C  Y N 201 
J75 C10  C  Y N 202 
J75 C11  C  Y N 203 
J75 C12  C  Y N 204 
J75 C13  C  Y N 205 
J75 S14  S  N N 206 
J75 O15  O  N N 207 
J75 O16  O  N N 208 
J75 N17  N  N N 209 
J75 N18  N  N N 210 
J75 O19  O  N N 211 
J75 O20  O  N N 212 
J75 N21  N  N N 213 
J75 C22  C  N N 214 
J75 C23  C  Y N 215 
J75 C24  C  Y N 216 
J75 C25  C  Y N 217 
J75 C26  C  Y N 218 
J75 C27  C  Y N 219 
J75 C28  C  Y N 220 
J75 C29  C  N N 221 
J75 H2   H  N N 222 
J75 HN7  H  N N 223 
J75 H9   H  N N 224 
J75 H10  H  N N 225 
J75 H12  H  N N 226 
J75 H13  H  N N 227 
J75 HN17 H  N N 228 
J75 HN1A H  N N 229 
J75 HN21 H  N N 230 
J75 H22  H  N N 231 
J75 H22A H  N N 232 
J75 H24  H  N N 233 
J75 H25  H  N N 234 
J75 H26  H  N N 235 
J75 H27  H  N N 236 
J75 H28  H  N N 237 
J75 H29  H  N N 238 
J75 H29A H  N N 239 
LEU N    N  N N 240 
LEU CA   C  N S 241 
LEU C    C  N N 242 
LEU O    O  N N 243 
LEU CB   C  N N 244 
LEU CG   C  N N 245 
LEU CD1  C  N N 246 
LEU CD2  C  N N 247 
LEU OXT  O  N N 248 
LEU H    H  N N 249 
LEU H2   H  N N 250 
LEU HA   H  N N 251 
LEU HB2  H  N N 252 
LEU HB3  H  N N 253 
LEU HG   H  N N 254 
LEU HD11 H  N N 255 
LEU HD12 H  N N 256 
LEU HD13 H  N N 257 
LEU HD21 H  N N 258 
LEU HD22 H  N N 259 
LEU HD23 H  N N 260 
LEU HXT  H  N N 261 
LYS N    N  N N 262 
LYS CA   C  N S 263 
LYS C    C  N N 264 
LYS O    O  N N 265 
LYS CB   C  N N 266 
LYS CG   C  N N 267 
LYS CD   C  N N 268 
LYS CE   C  N N 269 
LYS NZ   N  N N 270 
LYS OXT  O  N N 271 
LYS H    H  N N 272 
LYS H2   H  N N 273 
LYS HA   H  N N 274 
LYS HB2  H  N N 275 
LYS HB3  H  N N 276 
LYS HG2  H  N N 277 
LYS HG3  H  N N 278 
LYS HD2  H  N N 279 
LYS HD3  H  N N 280 
LYS HE2  H  N N 281 
LYS HE3  H  N N 282 
LYS HZ1  H  N N 283 
LYS HZ2  H  N N 284 
LYS HZ3  H  N N 285 
LYS HXT  H  N N 286 
MET N    N  N N 287 
MET CA   C  N S 288 
MET C    C  N N 289 
MET O    O  N N 290 
MET CB   C  N N 291 
MET CG   C  N N 292 
MET SD   S  N N 293 
MET CE   C  N N 294 
MET OXT  O  N N 295 
MET H    H  N N 296 
MET H2   H  N N 297 
MET HA   H  N N 298 
MET HB2  H  N N 299 
MET HB3  H  N N 300 
MET HG2  H  N N 301 
MET HG3  H  N N 302 
MET HE1  H  N N 303 
MET HE2  H  N N 304 
MET HE3  H  N N 305 
MET HXT  H  N N 306 
PHE N    N  N N 307 
PHE CA   C  N S 308 
PHE C    C  N N 309 
PHE O    O  N N 310 
PHE CB   C  N N 311 
PHE CG   C  Y N 312 
PHE CD1  C  Y N 313 
PHE CD2  C  Y N 314 
PHE CE1  C  Y N 315 
PHE CE2  C  Y N 316 
PHE CZ   C  Y N 317 
PHE OXT  O  N N 318 
PHE H    H  N N 319 
PHE H2   H  N N 320 
PHE HA   H  N N 321 
PHE HB2  H  N N 322 
PHE HB3  H  N N 323 
PHE HD1  H  N N 324 
PHE HD2  H  N N 325 
PHE HE1  H  N N 326 
PHE HE2  H  N N 327 
PHE HZ   H  N N 328 
PHE HXT  H  N N 329 
PRO N    N  N N 330 
PRO CA   C  N S 331 
PRO C    C  N N 332 
PRO O    O  N N 333 
PRO CB   C  N N 334 
PRO CG   C  N N 335 
PRO CD   C  N N 336 
PRO OXT  O  N N 337 
PRO H    H  N N 338 
PRO HA   H  N N 339 
PRO HB2  H  N N 340 
PRO HB3  H  N N 341 
PRO HG2  H  N N 342 
PRO HG3  H  N N 343 
PRO HD2  H  N N 344 
PRO HD3  H  N N 345 
PRO HXT  H  N N 346 
SER N    N  N N 347 
SER CA   C  N S 348 
SER C    C  N N 349 
SER O    O  N N 350 
SER CB   C  N N 351 
SER OG   O  N N 352 
SER OXT  O  N N 353 
SER H    H  N N 354 
SER H2   H  N N 355 
SER HA   H  N N 356 
SER HB2  H  N N 357 
SER HB3  H  N N 358 
SER HG   H  N N 359 
SER HXT  H  N N 360 
THR N    N  N N 361 
THR CA   C  N S 362 
THR C    C  N N 363 
THR O    O  N N 364 
THR CB   C  N R 365 
THR OG1  O  N N 366 
THR CG2  C  N N 367 
THR OXT  O  N N 368 
THR H    H  N N 369 
THR H2   H  N N 370 
THR HA   H  N N 371 
THR HB   H  N N 372 
THR HG1  H  N N 373 
THR HG21 H  N N 374 
THR HG22 H  N N 375 
THR HG23 H  N N 376 
THR HXT  H  N N 377 
TRP N    N  N N 378 
TRP CA   C  N S 379 
TRP C    C  N N 380 
TRP O    O  N N 381 
TRP CB   C  N N 382 
TRP CG   C  Y N 383 
TRP CD1  C  Y N 384 
TRP CD2  C  Y N 385 
TRP NE1  N  Y N 386 
TRP CE2  C  Y N 387 
TRP CE3  C  Y N 388 
TRP CZ2  C  Y N 389 
TRP CZ3  C  Y N 390 
TRP CH2  C  Y N 391 
TRP OXT  O  N N 392 
TRP H    H  N N 393 
TRP H2   H  N N 394 
TRP HA   H  N N 395 
TRP HB2  H  N N 396 
TRP HB3  H  N N 397 
TRP HD1  H  N N 398 
TRP HE1  H  N N 399 
TRP HE3  H  N N 400 
TRP HZ2  H  N N 401 
TRP HZ3  H  N N 402 
TRP HH2  H  N N 403 
TRP HXT  H  N N 404 
TYR N    N  N N 405 
TYR CA   C  N S 406 
TYR C    C  N N 407 
TYR O    O  N N 408 
TYR CB   C  N N 409 
TYR CG   C  Y N 410 
TYR CD1  C  Y N 411 
TYR CD2  C  Y N 412 
TYR CE1  C  Y N 413 
TYR CE2  C  Y N 414 
TYR CZ   C  Y N 415 
TYR OH   O  N N 416 
TYR OXT  O  N N 417 
TYR H    H  N N 418 
TYR H2   H  N N 419 
TYR HA   H  N N 420 
TYR HB2  H  N N 421 
TYR HB3  H  N N 422 
TYR HD1  H  N N 423 
TYR HD2  H  N N 424 
TYR HE1  H  N N 425 
TYR HE2  H  N N 426 
TYR HH   H  N N 427 
TYR HXT  H  N N 428 
VAL N    N  N N 429 
VAL CA   C  N S 430 
VAL C    C  N N 431 
VAL O    O  N N 432 
VAL CB   C  N N 433 
VAL CG1  C  N N 434 
VAL CG2  C  N N 435 
VAL OXT  O  N N 436 
VAL H    H  N N 437 
VAL H2   H  N N 438 
VAL HA   H  N N 439 
VAL HB   H  N N 440 
VAL HG11 H  N N 441 
VAL HG12 H  N N 442 
VAL HG13 H  N N 443 
VAL HG21 H  N N 444 
VAL HG22 H  N N 445 
VAL HG23 H  N N 446 
VAL HXT  H  N N 447 
ZN  ZN   ZN N N 448 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
J75 N1  C2   doub Y N 182 
J75 N1  C6   sing Y N 183 
J75 C2  N3   sing Y N 184 
J75 N3  C4   doub Y N 185 
J75 C4  C5   sing Y N 186 
J75 C4  N7   sing N N 187 
J75 C5  C6   doub Y N 188 
J75 C5  N18  sing N N 189 
J75 C6  N21  sing N N 190 
J75 N7  C29  sing N N 191 
J75 C8  C9   doub Y N 192 
J75 C8  C13  sing Y N 193 
J75 C8  C29  sing N N 194 
J75 C9  C10  sing Y N 195 
J75 C10 C11  doub Y N 196 
J75 C11 C12  sing Y N 197 
J75 C11 S14  sing N N 198 
J75 C12 C13  doub Y N 199 
J75 S14 O15  doub N N 200 
J75 S14 O16  doub N N 201 
J75 S14 N17  sing N N 202 
J75 N18 O19  sing N N 203 
J75 N18 O20  doub N N 204 
J75 N21 C22  sing N N 205 
J75 C22 C23  sing N N 206 
J75 C23 C24  doub Y N 207 
J75 C23 C28  sing Y N 208 
J75 C24 C25  sing Y N 209 
J75 C25 C26  doub Y N 210 
J75 C26 C27  sing Y N 211 
J75 C27 C28  doub Y N 212 
J75 C2  H2   sing N N 213 
J75 N7  HN7  sing N N 214 
J75 C9  H9   sing N N 215 
J75 C10 H10  sing N N 216 
J75 C12 H12  sing N N 217 
J75 C13 H13  sing N N 218 
J75 N17 HN17 sing N N 219 
J75 N17 HN1A sing N N 220 
J75 N21 HN21 sing N N 221 
J75 C22 H22  sing N N 222 
J75 C22 H22A sing N N 223 
J75 C24 H24  sing N N 224 
J75 C25 H25  sing N N 225 
J75 C26 H26  sing N N 226 
J75 C27 H27  sing N N 227 
J75 C28 H28  sing N N 228 
J75 C29 H29  sing N N 229 
J75 C29 H29A sing N N 230 
LEU N   CA   sing N N 231 
LEU N   H    sing N N 232 
LEU N   H2   sing N N 233 
LEU CA  C    sing N N 234 
LEU CA  CB   sing N N 235 
LEU CA  HA   sing N N 236 
LEU C   O    doub N N 237 
LEU C   OXT  sing N N 238 
LEU CB  CG   sing N N 239 
LEU CB  HB2  sing N N 240 
LEU CB  HB3  sing N N 241 
LEU CG  CD1  sing N N 242 
LEU CG  CD2  sing N N 243 
LEU CG  HG   sing N N 244 
LEU CD1 HD11 sing N N 245 
LEU CD1 HD12 sing N N 246 
LEU CD1 HD13 sing N N 247 
LEU CD2 HD21 sing N N 248 
LEU CD2 HD22 sing N N 249 
LEU CD2 HD23 sing N N 250 
LEU OXT HXT  sing N N 251 
LYS N   CA   sing N N 252 
LYS N   H    sing N N 253 
LYS N   H2   sing N N 254 
LYS CA  C    sing N N 255 
LYS CA  CB   sing N N 256 
LYS CA  HA   sing N N 257 
LYS C   O    doub N N 258 
LYS C   OXT  sing N N 259 
LYS CB  CG   sing N N 260 
LYS CB  HB2  sing N N 261 
LYS CB  HB3  sing N N 262 
LYS CG  CD   sing N N 263 
LYS CG  HG2  sing N N 264 
LYS CG  HG3  sing N N 265 
LYS CD  CE   sing N N 266 
LYS CD  HD2  sing N N 267 
LYS CD  HD3  sing N N 268 
LYS CE  NZ   sing N N 269 
LYS CE  HE2  sing N N 270 
LYS CE  HE3  sing N N 271 
LYS NZ  HZ1  sing N N 272 
LYS NZ  HZ2  sing N N 273 
LYS NZ  HZ3  sing N N 274 
LYS OXT HXT  sing N N 275 
MET N   CA   sing N N 276 
MET N   H    sing N N 277 
MET N   H2   sing N N 278 
MET CA  C    sing N N 279 
MET CA  CB   sing N N 280 
MET CA  HA   sing N N 281 
MET C   O    doub N N 282 
MET C   OXT  sing N N 283 
MET CB  CG   sing N N 284 
MET CB  HB2  sing N N 285 
MET CB  HB3  sing N N 286 
MET CG  SD   sing N N 287 
MET CG  HG2  sing N N 288 
MET CG  HG3  sing N N 289 
MET SD  CE   sing N N 290 
MET CE  HE1  sing N N 291 
MET CE  HE2  sing N N 292 
MET CE  HE3  sing N N 293 
MET OXT HXT  sing N N 294 
PHE N   CA   sing N N 295 
PHE N   H    sing N N 296 
PHE N   H2   sing N N 297 
PHE CA  C    sing N N 298 
PHE CA  CB   sing N N 299 
PHE CA  HA   sing N N 300 
PHE C   O    doub N N 301 
PHE C   OXT  sing N N 302 
PHE CB  CG   sing N N 303 
PHE CB  HB2  sing N N 304 
PHE CB  HB3  sing N N 305 
PHE CG  CD1  doub Y N 306 
PHE CG  CD2  sing Y N 307 
PHE CD1 CE1  sing Y N 308 
PHE CD1 HD1  sing N N 309 
PHE CD2 CE2  doub Y N 310 
PHE CD2 HD2  sing N N 311 
PHE CE1 CZ   doub Y N 312 
PHE CE1 HE1  sing N N 313 
PHE CE2 CZ   sing Y N 314 
PHE CE2 HE2  sing N N 315 
PHE CZ  HZ   sing N N 316 
PHE OXT HXT  sing N N 317 
PRO N   CA   sing N N 318 
PRO N   CD   sing N N 319 
PRO N   H    sing N N 320 
PRO CA  C    sing N N 321 
PRO CA  CB   sing N N 322 
PRO CA  HA   sing N N 323 
PRO C   O    doub N N 324 
PRO C   OXT  sing N N 325 
PRO CB  CG   sing N N 326 
PRO CB  HB2  sing N N 327 
PRO CB  HB3  sing N N 328 
PRO CG  CD   sing N N 329 
PRO CG  HG2  sing N N 330 
PRO CG  HG3  sing N N 331 
PRO CD  HD2  sing N N 332 
PRO CD  HD3  sing N N 333 
PRO OXT HXT  sing N N 334 
SER N   CA   sing N N 335 
SER N   H    sing N N 336 
SER N   H2   sing N N 337 
SER CA  C    sing N N 338 
SER CA  CB   sing N N 339 
SER CA  HA   sing N N 340 
SER C   O    doub N N 341 
SER C   OXT  sing N N 342 
SER CB  OG   sing N N 343 
SER CB  HB2  sing N N 344 
SER CB  HB3  sing N N 345 
SER OG  HG   sing N N 346 
SER OXT HXT  sing N N 347 
THR N   CA   sing N N 348 
THR N   H    sing N N 349 
THR N   H2   sing N N 350 
THR CA  C    sing N N 351 
THR CA  CB   sing N N 352 
THR CA  HA   sing N N 353 
THR C   O    doub N N 354 
THR C   OXT  sing N N 355 
THR CB  OG1  sing N N 356 
THR CB  CG2  sing N N 357 
THR CB  HB   sing N N 358 
THR OG1 HG1  sing N N 359 
THR CG2 HG21 sing N N 360 
THR CG2 HG22 sing N N 361 
THR CG2 HG23 sing N N 362 
THR OXT HXT  sing N N 363 
TRP N   CA   sing N N 364 
TRP N   H    sing N N 365 
TRP N   H2   sing N N 366 
TRP CA  C    sing N N 367 
TRP CA  CB   sing N N 368 
TRP CA  HA   sing N N 369 
TRP C   O    doub N N 370 
TRP C   OXT  sing N N 371 
TRP CB  CG   sing N N 372 
TRP CB  HB2  sing N N 373 
TRP CB  HB3  sing N N 374 
TRP CG  CD1  doub Y N 375 
TRP CG  CD2  sing Y N 376 
TRP CD1 NE1  sing Y N 377 
TRP CD1 HD1  sing N N 378 
TRP CD2 CE2  doub Y N 379 
TRP CD2 CE3  sing Y N 380 
TRP NE1 CE2  sing Y N 381 
TRP NE1 HE1  sing N N 382 
TRP CE2 CZ2  sing Y N 383 
TRP CE3 CZ3  doub Y N 384 
TRP CE3 HE3  sing N N 385 
TRP CZ2 CH2  doub Y N 386 
TRP CZ2 HZ2  sing N N 387 
TRP CZ3 CH2  sing Y N 388 
TRP CZ3 HZ3  sing N N 389 
TRP CH2 HH2  sing N N 390 
TRP OXT HXT  sing N N 391 
TYR N   CA   sing N N 392 
TYR N   H    sing N N 393 
TYR N   H2   sing N N 394 
TYR CA  C    sing N N 395 
TYR CA  CB   sing N N 396 
TYR CA  HA   sing N N 397 
TYR C   O    doub N N 398 
TYR C   OXT  sing N N 399 
TYR CB  CG   sing N N 400 
TYR CB  HB2  sing N N 401 
TYR CB  HB3  sing N N 402 
TYR CG  CD1  doub Y N 403 
TYR CG  CD2  sing Y N 404 
TYR CD1 CE1  sing Y N 405 
TYR CD1 HD1  sing N N 406 
TYR CD2 CE2  doub Y N 407 
TYR CD2 HD2  sing N N 408 
TYR CE1 CZ   doub Y N 409 
TYR CE1 HE1  sing N N 410 
TYR CE2 CZ   sing Y N 411 
TYR CE2 HE2  sing N N 412 
TYR CZ  OH   sing N N 413 
TYR OH  HH   sing N N 414 
TYR OXT HXT  sing N N 415 
VAL N   CA   sing N N 416 
VAL N   H    sing N N 417 
VAL N   H2   sing N N 418 
VAL CA  C    sing N N 419 
VAL CA  CB   sing N N 420 
VAL CA  HA   sing N N 421 
VAL C   O    doub N N 422 
VAL C   OXT  sing N N 423 
VAL CB  CG1  sing N N 424 
VAL CB  CG2  sing N N 425 
VAL CB  HB   sing N N 426 
VAL CG1 HG11 sing N N 427 
VAL CG1 HG12 sing N N 428 
VAL CG1 HG13 sing N N 429 
VAL CG2 HG21 sing N N 430 
VAL CG2 HG22 sing N N 431 
VAL CG2 HG23 sing N N 432 
VAL OXT HXT  sing N N 433 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                   ZN  
3 'DIMETHYL SULFOXIDE'                                                         DMS 
4 '4-({[6-(benzylamino)-5-nitropyrimidin-4-yl]amino}methyl)benzenesulfonamide' J75 
5 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' 
# 
