data_4Q6D
# 
_entry.id   4Q6D 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4Q6D         pdb_00004q6d 10.2210/pdb4q6d/pdb 
RCSB  RCSB085660   ?            ?                   
WWPDB D_1000085660 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          4Q6E 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        4Q6D 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2014-04-22 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     '4-Amino-substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases.' 
_citation.journal_abbrev            Molecules 
_citation.journal_volume            19 
_citation.page_first                17356 
_citation.page_last                 17380 
_citation.year                      2014 
_citation.journal_id_ASTM           ? 
_citation.country                   CH 
_citation.journal_id_ISSN           1420-3049 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25353386 
_citation.pdbx_database_id_DOI      10.3390/molecules191117356 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rutkauskas, K.'      1  ? 
primary 'Zubriene, A.'        2  ? 
primary 'Tumosiene, I.'       3  ? 
primary 'Kantminiene, K.'     4  ? 
primary 'Kazemekaite, M.'     5  ? 
primary 'Smirnov, A.'         6  ? 
primary 'Kazokaite, J.'       7  ? 
primary 'Morkunaite, V.'      8  ? 
primary 'Capkauskaite, E.'    9  ? 
primary 'Manakova, E.'        10 ? 
primary 'Grazulis, S.'        11 ? 
primary 'Beresnevicius, Z.J.' 12 ? 
primary 'Matulis, D.'         13 ? 
# 
_cell.entry_id           4Q6D 
_cell.length_a           42.125 
_cell.length_b           41.195 
_cell.length_c           71.813 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.190 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4Q6D 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                          29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                      65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                            78.133    1   ?       ? ? ? 
4 non-polymer syn BICINE                                          163.172   1   ?       ? ? ? 
5 non-polymer syn '4-[(E)-azepan-1-yldiazenyl]benzenesulfonamide' 282.362   1   ?       ? ? ? 
6 water       nat water                                           18.015    299 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4Q6D 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                         ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                        ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                      ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                 ? 'C4 H7 N O4'      133.103 
BCN non-polymer         . BICINE                                          ? 'C6 H13 N O4'     163.172 
CYS 'L-peptide linking' y CYSTEINE                                        ? 'C3 H7 N O2 S'    121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                            ? 'C2 H6 O S'       78.133  
GLN 'L-peptide linking' y GLUTAMINE                                       ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                 ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                         ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                       ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                           ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                      ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                         ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                                          ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                                      ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                   ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                                         ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                                          ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                                       ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                      ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                                        ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                          ? 'C5 H11 N O2'     117.146 
WW3 non-polymer         . '4-[(E)-azepan-1-yldiazenyl]benzenesulfonamide' ? 'C12 H18 N4 O2 S' 282.362 
ZN  non-polymer         . 'ZINC ION'                                      ? 'Zn 2'            65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4Q6D 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   38.5 
_exptl_crystal.density_Matthews      2.01 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate, VAPOR DIFFUSION, SITTING DROP, temperature 291K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'PSI PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2014-01-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    
;High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM) 
: Si 311, Si 511
;
_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   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
# 
_reflns.entry_id                     4Q6D 
_reflns.d_resolution_high            1.12 
_reflns.d_resolution_low             41.195 
_reflns.number_all                   ? 
_reflns.number_obs                   87368 
_reflns.pdbx_netI_over_sigmaI        13.600 
_reflns.pdbx_Rsym_value              0.076 
_reflns.pdbx_redundancy              6.500 
_reflns.percent_possible_obs         95.800 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            0.076 
_reflns.B_iso_Wilson_estimate        9.250 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.12 1.18  ? 53700 ? 0.166 3.8 0.166 ? 5.10 ? 10618 80.20 1  1 
1.18 1.26  ? 79911 ? 0.147 4.5 0.147 ? 6.50 ? 12366 98.30 2  1 
1.26 1.34  ? 76967 ? 0.111 6.1 0.111 ? 6.60 ? 11586 98.50 3  1 
1.34 1.45  ? 71609 ? 0.089 7.7 0.089 ? 6.60 ? 10798 98.40 4  1 
1.45 1.59  ? 66401 ? 0.075 9.0 0.075 ? 6.70 ? 9913  98.00 5  1 
1.59 1.78  ? 60285 ? 0.069 9.6 0.069 ? 6.70 ? 9000  98.40 6  1 
1.78 2.05  ? 55651 ? 0.067 9.5 0.067 ? 6.90 ? 8065  99.30 7  1 
2.05 2.51  ? 46562 ? 0.066 9.9 0.066 ? 6.90 ? 6784  99.00 8  1 
2.51 3.55  ? 36564 ? 0.070 7.8 0.070 ? 6.90 ? 5290  99.10 9  1 
3.55 41.19 ? 19514 ? 0.081 6.4 0.081 ? 6.60 ? 2948  98.00 10 1 
# 
_refine.entry_id                                 4Q6D 
_refine.ls_d_res_high                            1.120 
_refine.ls_d_res_low                             39.730 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    95.770 
_refine.ls_number_reflns_obs                     87346 
_refine.ls_number_reflns_all                     87346 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          0.131 
_refine.ls_R_factor_obs                          0.131 
_refine.ls_R_factor_R_work                       0.128 
_refine.ls_wR_factor_R_work                      0.133 
_refine.ls_R_factor_R_free                       0.154 
_refine.ls_wR_factor_R_free                      0.167 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  8792 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               16.965 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.090 
_refine.aniso_B[2][2]                            -0.190 
_refine.aniso_B[3][3]                            0.090 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.010 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.978 
_refine.correlation_coeff_Fo_to_Fc_free          0.974 
_refine.overall_SU_R_Cruickshank_DPI             0.033 
_refine.overall_SU_R_free                        0.033 
_refine.pdbx_overall_ESU_R                       0.033 
_refine.pdbx_overall_ESU_R_Free                  0.033 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          MR 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.938 
_refine.B_iso_max                                248.02 
_refine.B_iso_min                                6.64 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_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         35 
_refine_hist.number_atoms_solvent             299 
_refine_hist.number_atoms_total               2383 
_refine_hist.d_res_high                       1.120 
_refine_hist.d_res_low                        39.730 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       2370 0.025  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3251 2.605  1.961  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 306  6.761  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 102  32.502 24.412 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 379  12.641 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 8    19.990 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         337  0.154  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1878 0.016  0.021  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr     2370 10.008 3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free      300  23.139 5.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded    2283 11.196 5.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.123 
_refine_ls_shell.d_res_low                        1.152 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               66.420 
_refine_ls_shell.number_reflns_R_work             4056 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.126 
_refine_ls_shell.R_factor_R_free                  0.160 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             434 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                4490 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4Q6D 
_struct.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 4-[(Z)-azepan-1-yldiazenyl]benzenesulfonamide' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4Q6D 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E WW3 . N10 ? ? A ZN  301 A WW3 304 1_555 ? ? ? ? ? ? ? 1.944 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -3.88 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 12.64 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A DMS 302 ? 5  'BINDING SITE FOR RESIDUE DMS A 302' 
AC3 Software A BCN 303 ? 9  'BINDING SITE FOR RESIDUE BCN A 303' 
AC4 Software A WW3 304 ? 12 'BINDING SITE FOR RESIDUE WW3 A 304' 
# 
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  WW3 E .   ? WW3 A 304 . ? 1_555 ? 
5  AC2 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 5  PRO A 246 ? PRO A 247 . ? 1_555 ? 
9  AC2 5  HOH F .   ? HOH A 654 . ? 1_555 ? 
10 AC3 9  LYS A 148 ? LYS A 149 . ? 1_555 ? 
11 AC3 9  LYS A 212 ? LYS A 213 . ? 1_555 ? 
12 AC3 9  GLU A 213 ? GLU A 214 . ? 1_555 ? 
13 AC3 9  PRO A 214 ? PRO A 215 . ? 1_555 ? 
14 AC3 9  HOH F .   ? HOH A 413 . ? 1_555 ? 
15 AC3 9  HOH F .   ? HOH A 475 . ? 1_555 ? 
16 AC3 9  HOH F .   ? HOH A 540 . ? 1_555 ? 
17 AC3 9  HOH F .   ? HOH A 650 . ? 1_555 ? 
18 AC3 9  HOH F .   ? HOH A 679 . ? 1_555 ? 
19 AC4 12 HIS A 94  ? HIS A 94  . ? 1_555 ? 
20 AC4 12 HIS A 96  ? HIS A 96  . ? 1_555 ? 
21 AC4 12 HIS A 119 ? HIS A 119 . ? 1_555 ? 
22 AC4 12 PHE A 130 ? PHE A 131 . ? 1_555 ? 
23 AC4 12 LEU A 197 ? LEU A 198 . ? 1_555 ? 
24 AC4 12 THR A 198 ? THR A 199 . ? 1_555 ? 
25 AC4 12 THR A 199 ? THR A 200 . ? 1_555 ? 
26 AC4 12 PRO A 201 ? PRO A 202 . ? 1_555 ? 
27 AC4 12 TRP A 208 ? TRP A 209 . ? 1_555 ? 
28 AC4 12 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
29 AC4 12 HOH F .   ? HOH A 416 . ? 1_555 ? 
30 AC4 12 HOH F .   ? HOH A 427 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4Q6D 
_atom_sites.fract_transf_matrix[1][1]   0.023739 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006004 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024275 
_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]   0.014363 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 11.087  -0.486  7.944   1.00   29.15  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 9.945   0.037   8.655   1.00   24.57  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.252   -1.057  9.448   1.00   21.81  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.497   -2.245  9.222   1.00   21.73  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 9.041   0.747   7.680   1.00   29.31  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 8.564   1.988   8.253   1.00   40.35  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 9.295   2.647   9.164   1.00   56.80  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 7.416   2.725   8.051   1.00   45.01  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 8.646   3.775   9.530   0.0000 77.81  ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 7.492   3.824   8.841   0.0000 71.38  ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.409   -0.701  10.397  1.00   18.01  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.725   -1.687  11.242  1.00   15.19  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.728   -2.462  10.455  1.00   14.54  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.224   -1.975  9.422   1.00   16.53  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.059   -0.926  12.426  1.00   15.09  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.918   -0.075  12.033  1.00   12.96  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.898   1.244   11.722  1.00   15.66  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.552   -0.520  11.952  1.00   12.45  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.660   1.668   11.420  1.00   15.06  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.772   0.611   11.550  1.00   13.73  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.909   -1.742  12.202  1.00   12.96  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.424   0.568   11.408  1.00   14.85  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.515   -1.786  12.012  1.00   13.50  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.804   -0.639  11.650  1.00   14.66  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.433   -3.655  10.950  1.00   14.19  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.392   -4.448  10.287  1.00   14.70  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.080   -5.631  11.200  1.00   14.08  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.104   -5.504  12.417  1.00   13.81  ? 6   GLY A O   1 
ATOM   29   N  N   A TYR A 1 7   ? 4.594   -6.673  10.427  0.50   11.53  ? 7   TYR A N   1 
ATOM   30   N  N   B TYR A 1 7   ? 4.994   -6.901  10.789  0.50   15.55  ? 7   TYR A N   1 
ATOM   31   C  CA  A TYR A 1 7   ? 4.182   -7.983  11.019  0.50   9.61   ? 7   TYR A CA  1 
ATOM   32   C  CA  B TYR A 1 7   ? 4.615   -7.942  11.818  0.50   12.73  ? 7   TYR A CA  1 
ATOM   33   C  C   A TYR A 1 7   ? 4.974   -9.129  10.376  0.50   13.15  ? 7   TYR A C   1 
ATOM   34   C  C   B TYR A 1 7   ? 5.505   -9.195  11.765  0.50   14.70  ? 7   TYR A C   1 
ATOM   35   O  O   A TYR A 1 7   ? 4.542   -10.268 10.420  0.50   16.55  ? 7   TYR A O   1 
ATOM   36   O  O   B TYR A 1 7   ? 5.227   -10.243 12.447  0.50   21.07  ? 7   TYR A O   1 
ATOM   37   C  CB  A TYR A 1 7   ? 2.681   -8.224  10.859  0.50   10.24  ? 7   TYR A CB  1 
ATOM   38   C  CB  B TYR A 1 7   ? 3.178   -8.359  11.573  0.50   13.72  ? 7   TYR A CB  1 
ATOM   39   C  CG  A TYR A 1 7   ? 1.899   -7.110  11.500  0.50   8.37   ? 7   TYR A CG  1 
ATOM   40   C  CG  B TYR A 1 7   ? 2.178   -7.300  12.052  0.50   11.11  ? 7   TYR A CG  1 
ATOM   41   C  CD1 A TYR A 1 7   ? 1.531   -7.173  12.854  0.50   8.19   ? 7   TYR A CD1 1 
ATOM   42   C  CD1 B TYR A 1 7   ? 1.757   -7.288  13.391  0.50   10.46  ? 7   TYR A CD1 1 
ATOM   43   C  CD2 A TYR A 1 7   ? 1.414   -6.036  10.741  0.50   9.16   ? 7   TYR A CD2 1 
ATOM   44   C  CD2 B TYR A 1 7   ? 1.735   -6.308  11.209  0.50   11.89  ? 7   TYR A CD2 1 
ATOM   45   C  CE1 A TYR A 1 7   ? 0.727   -6.169  13.423  0.50   8.13   ? 7   TYR A CE1 1 
ATOM   46   C  CE1 B TYR A 1 7   ? 0.877   -6.287  13.821  0.50   10.50  ? 7   TYR A CE1 1 
ATOM   47   C  CE2 A TYR A 1 7   ? 0.617   -5.052  11.300  0.50   8.74   ? 7   TYR A CE2 1 
ATOM   48   C  CE2 B TYR A 1 7   ? 0.850   -5.330  11.627  0.50   11.15  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  A TYR A 1 7   ? 0.268   -5.152  12.628  0.50   7.72   ? 7   TYR A CZ  1 
ATOM   50   C  CZ  B TYR A 1 7   ? 0.420   -5.347  12.950  0.50   10.34  ? 7   TYR A CZ  1 
ATOM   51   O  OH  A TYR A 1 7   ? -0.557  -4.188  13.091  0.50   8.74   ? 7   TYR A OH  1 
ATOM   52   O  OH  B TYR A 1 7   ? -0.475  -4.401  13.389  0.50   11.49  ? 7   TYR A OH  1 
ATOM   53   N  N   A GLY A 1 8   ? 6.126   -8.818  9.794   0.50   12.03  ? 8   GLY A N   1 
ATOM   54   N  N   B GLY A 1 8   ? 6.585   -9.033  10.970  0.50   15.72  ? 8   GLY A N   1 
ATOM   55   C  CA  A GLY A 1 8   ? 6.933   -9.852  9.160   0.50   13.17  ? 8   GLY A CA  1 
ATOM   56   C  CA  B GLY A 1 8   ? 7.644   -10.009 10.907  0.50   18.12  ? 8   GLY A CA  1 
ATOM   57   C  C   A GLY A 1 8   ? 7.814   -10.582 10.138  0.50   14.63  ? 8   GLY A C   1 
ATOM   58   C  C   B GLY A 1 8   ? 8.609   -10.337 12.039  0.50   16.68  ? 8   GLY A C   1 
ATOM   59   O  O   A GLY A 1 8   ? 7.729   -10.541 11.359  0.50   12.77  ? 8   GLY A O   1 
ATOM   60   O  O   B GLY A 1 8   ? 8.793   -9.760  13.120  0.50   19.56  ? 8   GLY A O   1 
ATOM   61   N  N   A LYS A 1 9   ? 8.784   -11.273 9.563   0.50   12.81  ? 9   LYS A N   1 
ATOM   62   N  N   B LYS A 1 9   ? 9.435   -11.324 11.704  0.50   18.28  ? 9   LYS A N   1 
ATOM   63   C  CA  A LYS A 1 9   ? 9.679   -12.101 10.370  0.50   15.08  ? 9   LYS A CA  1 
ATOM   64   C  CA  B LYS A 1 9   ? 10.463  -11.766 12.629  0.50   19.76  ? 9   LYS A CA  1 
ATOM   65   C  C   A LYS A 1 9   ? 10.753  -11.313 11.078  0.50   14.56  ? 9   LYS A C   1 
ATOM   66   C  C   B LYS A 1 9   ? 11.406  -10.599 12.970  0.50   15.72  ? 9   LYS A C   1 
ATOM   67   O  O   A LYS A 1 9   ? 11.351  -11.906 11.976  0.50   14.71  ? 9   LYS A O   1 
ATOM   68   O  O   B LYS A 1 9   ? 11.802  -10.429 14.136  0.50   19.73  ? 9   LYS A O   1 
ATOM   69   C  CB  A LYS A 1 9   ? 10.326  -13.204 9.536   0.50   19.05  ? 9   LYS A CB  1 
ATOM   70   C  CB  B LYS A 1 9   ? 11.220  -12.937 11.937  0.50   25.04  ? 9   LYS A CB  1 
ATOM   71   C  CG  A LYS A 1 9   ? 9.374   -14.321 9.241   0.50   24.72  ? 9   LYS A CG  1 
ATOM   72   C  CG  B LYS A 1 9   ? 11.600  -14.158 12.740  0.50   33.39  ? 9   LYS A CG  1 
ATOM   73   C  CD  A LYS A 1 9   ? 9.543   -15.453 10.237  0.50   34.14  ? 9   LYS A CD  1 
ATOM   74   C  CD  B LYS A 1 9   ? 12.982  -14.628 12.280  0.50   28.82  ? 9   LYS A CD  1 
ATOM   75   C  CE  A LYS A 1 9   ? 8.767   -16.679 9.743   0.50   47.56  ? 9   LYS A CE  1 
ATOM   76   C  CE  B LYS A 1 9   ? 13.026  -15.642 11.121  0.50   32.40  ? 9   LYS A CE  1 
ATOM   77   N  NZ  A LYS A 1 9   ? 9.062   -17.960 10.464  0.50   49.73  ? 9   LYS A NZ  1 
ATOM   78   N  NZ  B LYS A 1 9   ? 14.453  -15.902 10.632  0.50   26.36  ? 9   LYS A NZ  1 
ATOM   79   N  N   A HIS A 1 10  ? 11.000  -10.036 10.700  0.50   12.46  ? 10  HIS A N   1 
ATOM   80   N  N   B HIS A 1 10  ? 11.743  -9.833  11.932  0.50   15.35  ? 10  HIS A N   1 
ATOM   81   C  CA  A HIS A 1 10  ? 12.055  -9.219  11.153  0.50   12.09  ? 10  HIS A CA  1 
ATOM   82   C  CA  B HIS A 1 10  ? 12.721  -8.784  12.053  0.50   15.41  ? 10  HIS A CA  1 
ATOM   83   C  C   A HIS A 1 10  ? 11.688  -7.896  11.703  0.50   13.16  ? 10  HIS A C   1 
ATOM   84   C  C   B HIS A 1 10  ? 11.955  -7.477  12.037  0.50   20.66  ? 10  HIS A C   1 
ATOM   85   O  O   A HIS A 1 10  ? 12.468  -7.377  12.329  0.50   10.94  ? 10  HIS A O   1 
ATOM   86   O  O   B HIS A 1 10  ? 12.825  -6.554  12.419  0.50   17.20  ? 10  HIS A O   1 
ATOM   87   C  CB  A HIS A 1 10  ? 13.108  -9.049  10.024  0.50   14.24  ? 10  HIS A CB  1 
ATOM   88   C  CB  B HIS A 1 10  ? 13.716  -8.850  10.891  0.50   13.91  ? 10  HIS A CB  1 
ATOM   89   C  CG  A HIS A 1 10  ? 13.646  -10.376 9.619   0.50   13.35  ? 10  HIS A CG  1 
ATOM   90   C  CG  B HIS A 1 10  ? 14.372  -10.196 10.768  0.50   15.46  ? 10  HIS A CG  1 
ATOM   91   N  ND1 A HIS A 1 10  ? 14.498  -11.081 10.361  0.50   16.49  ? 10  HIS A ND1 1 
ATOM   92   N  ND1 B HIS A 1 10  ? 15.400  -10.579 11.570  0.50   18.56  ? 10  HIS A ND1 1 
ATOM   93   C  CD2 A HIS A 1 10  ? 13.319  -11.152 8.535   0.50   16.05  ? 10  HIS A CD2 1 
ATOM   94   C  CD2 B HIS A 1 10  ? 14.101  -11.281 9.930   0.50   17.20  ? 10  HIS A CD2 1 
ATOM   95   C  CE1 A HIS A 1 10  ? 14.740  -12.252 9.741   0.50   14.98  ? 10  HIS A CE1 1 
ATOM   96   C  CE1 B HIS A 1 10  ? 15.755  -11.824 11.276  0.50   19.48  ? 10  HIS A CE1 1 
ATOM   97   N  NE2 A HIS A 1 10  ? 14.040  -12.277 8.604   0.50   18.14  ? 10  HIS A NE2 1 
ATOM   98   N  NE2 B HIS A 1 10  ? 14.972  -12.260 10.266  0.50   20.78  ? 10  HIS A NE2 1 
ATOM   99   N  N   . ASN A 1 11  ? 10.546  -7.367  11.708  1.00   18.66  ? 11  ASN A N   1 
ATOM   100  C  CA  . ASN A 1 11  ? 10.104  -6.055  12.021  1.00   16.70  ? 11  ASN A CA  1 
ATOM   101  C  C   . ASN A 1 11  ? 8.786   -6.028  12.820  1.00   15.36  ? 11  ASN A C   1 
ATOM   102  O  O   . ASN A 1 11  ? 8.154   -4.973  12.887  1.00   15.63  ? 11  ASN A O   1 
ATOM   103  C  CB  . ASN A 1 11  ? 9.900   -5.281  10.719  1.00   16.43  ? 11  ASN A CB  1 
ATOM   104  C  CG  . ASN A 1 11  ? 8.836   -5.833  9.791   1.00   16.29  ? 11  ASN A CG  1 
ATOM   105  O  OD1 . ASN A 1 11  ? 8.206   -6.874  10.073  1.00   19.83  ? 11  ASN A OD1 1 
ATOM   106  N  ND2 . ASN A 1 11  ? 8.578   -5.133  8.689   1.00   19.47  ? 11  ASN A ND2 1 
ATOM   107  N  N   . GLY A 1 12  ? 8.465   -7.154  13.427  1.00   15.94  ? 12  GLY A N   1 
ATOM   108  C  CA  . GLY A 1 12  ? 7.151   -7.316  14.085  1.00   16.12  ? 12  GLY A CA  1 
ATOM   109  C  C   . GLY A 1 12  ? 7.136   -6.736  15.442  1.00   13.44  ? 12  GLY A C   1 
ATOM   110  O  O   . GLY A 1 12  ? 8.062   -6.061  15.917  1.00   14.08  ? 12  GLY A O   1 
ATOM   111  N  N   . PRO A 1 13  ? 6.053   -6.990  16.183  1.00   12.65  ? 13  PRO A N   1 
ATOM   112  C  CA  . PRO A 1 13  ? 5.775   -6.369  17.488  1.00   12.63  ? 13  PRO A CA  1 
ATOM   113  C  C   . PRO A 1 13  ? 6.893   -6.412  18.454  1.00   12.74  ? 13  PRO A C   1 
ATOM   114  O  O   . PRO A 1 13  ? 7.049   -5.425  19.241  1.00   13.33  ? 13  PRO A O   1 
ATOM   115  C  CB  . PRO A 1 13  ? 4.552   -7.157  17.945  1.00   13.78  ? 13  PRO A CB  1 
ATOM   116  C  CG  . PRO A 1 13  ? 3.770   -7.405  16.697  1.00   13.58  ? 13  PRO A CG  1 
ATOM   117  C  CD  . PRO A 1 13  ? 4.874   -7.725  15.722  1.00   14.83  ? 13  PRO A CD  1 
ATOM   118  N  N   . GLU A 1 14  ? 7.693   -7.459  18.482  1.00   13.90  ? 14  GLU A N   1 
ATOM   119  C  CA  . GLU A 1 14  ? 8.728   -7.520  19.496  1.00   16.28  ? 14  GLU A CA  1 
ATOM   120  C  C   . GLU A 1 14  ? 9.896   -6.526  19.171  1.00   14.54  ? 14  GLU A C   1 
ATOM   121  O  O   . GLU A 1 14  ? 10.774  -6.348  20.023  1.00   16.94  ? 14  GLU A O   1 
ATOM   122  C  CB  . GLU A 1 14  ? 9.256   -8.941  19.574  1.00   20.78  ? 14  GLU A CB  1 
ATOM   123  C  CG  . GLU A 1 14  ? 9.831   -9.572  18.295  1.00   20.83  ? 14  GLU A CG  1 
ATOM   124  C  CD  . GLU A 1 14  ? 9.038   -10.076 17.111  1.00   23.44  ? 14  GLU A CD  1 
ATOM   125  O  OE1 . GLU A 1 14  ? 7.909   -9.665  16.840  1.00   21.42  ? 14  GLU A OE1 1 
ATOM   126  O  OE2 . GLU A 1 14  ? 9.614   -10.918 16.370  1.00   31.52  ? 14  GLU A OE2 1 
ATOM   127  N  N   . HIS A 1 15  ? 9.914   -5.953  18.005  1.00   13.89  ? 15  HIS A N   1 
ATOM   128  C  CA  . HIS A 1 15  ? 10.954  -4.960  17.596  1.00   14.11  ? 15  HIS A CA  1 
ATOM   129  C  C   . HIS A 1 15  ? 10.492  -3.551  17.738  1.00   12.96  ? 15  HIS A C   1 
ATOM   130  O  O   . HIS A 1 15  ? 11.306  -2.627  17.657  1.00   14.37  ? 15  HIS A O   1 
ATOM   131  C  CB  . HIS A 1 15  ? 11.316  -5.161  16.119  1.00   15.21  ? 15  HIS A CB  1 
ATOM   132  C  CG  . HIS A 1 15  ? 12.025  -6.422  15.897  1.00   15.76  ? 15  HIS A CG  1 
ATOM   133  N  ND1 . HIS A 1 15  ? 13.377  -6.584  16.091  1.00   18.82  ? 15  HIS A ND1 1 
ATOM   134  C  CD2 . HIS A 1 15  ? 11.533  -7.680  15.523  1.00   17.04  ? 15  HIS A CD2 1 
ATOM   135  C  CE1 . HIS A 1 15  ? 13.681  -7.851  15.825  1.00   22.64  ? 15  HIS A CE1 1 
ATOM   136  N  NE2 . HIS A 1 15  ? 12.590  -8.510  15.439  1.00   22.91  ? 15  HIS A NE2 1 
ATOM   137  N  N   . TRP A 1 16  ? 9.176   -3.292  17.886  1.00   12.61  ? 16  TRP A N   1 
ATOM   138  C  CA  . TRP A 1 16  ? 8.658   -1.947  17.792  1.00   11.53  ? 16  TRP A CA  1 
ATOM   139  C  C   . TRP A 1 16  ? 9.223   -0.966  18.821  1.00   11.61  ? 16  TRP A C   1 
ATOM   140  O  O   . TRP A 1 16  ? 9.321   0.232   18.564  1.00   12.74  ? 16  TRP A O   1 
ATOM   141  C  CB  . TRP A 1 16  ? 7.109   -1.974  17.861  1.00   11.03  ? 16  TRP A CB  1 
ATOM   142  C  CG  . TRP A 1 16  ? 6.446   -2.650  16.731  1.00   10.44  ? 16  TRP A CG  1 
ATOM   143  C  CD1 . TRP A 1 16  ? 6.992   -3.123  15.575  1.00   11.83  ? 16  TRP A CD1 1 
ATOM   144  C  CD2 . TRP A 1 16  ? 5.044   -2.972  16.672  1.00   10.39  ? 16  TRP A CD2 1 
ATOM   145  N  NE1 . TRP A 1 16  ? 6.054   -3.728  14.805  1.00   11.50  ? 16  TRP A NE1 1 
ATOM   146  C  CE2 . TRP A 1 16  ? 4.813   -3.615  15.396  1.00   10.35  ? 16  TRP A CE2 1 
ATOM   147  C  CE3 . TRP A 1 16  ? 3.972   -2.747  17.551  1.00   10.55  ? 16  TRP A CE3 1 
ATOM   148  C  CZ2 . TRP A 1 16  ? 3.557   -4.008  15.030  1.00   11.00  ? 16  TRP A CZ2 1 
ATOM   149  C  CZ3 . TRP A 1 16  ? 2.741   -3.190  17.146  1.00   10.82  ? 16  TRP A CZ3 1 
ATOM   150  C  CH2 . TRP A 1 16  ? 2.515   -3.797  15.922  1.00   10.95  ? 16  TRP A CH2 1 
ATOM   151  N  N   . HIS A 1 17  ? 9.592   -1.498  19.973  1.00   11.65  ? 17  HIS A N   1 
ATOM   152  C  CA  . HIS A 1 17  ? 10.087  -0.665  21.020  1.00   12.11  ? 17  HIS A CA  1 
ATOM   153  C  C   . HIS A 1 17  ? 11.352  0.112   20.656  1.00   13.89  ? 17  HIS A C   1 
ATOM   154  O  O   . HIS A 1 17  ? 11.609  1.152   21.262  1.00   14.44  ? 17  HIS A O   1 
ATOM   155  C  CB  . HIS A 1 17  ? 10.374  -1.391  22.306  1.00   13.76  ? 17  HIS A CB  1 
ATOM   156  C  CG  . HIS A 1 17  ? 11.589  -2.273  22.226  1.00   15.23  ? 17  HIS A CG  1 
ATOM   157  N  ND1 . HIS A 1 17  ? 12.817  -1.901  22.720  1.00   17.81  ? 17  HIS A ND1 1 
ATOM   158  C  CD2 . HIS A 1 17  ? 11.745  -3.472  21.639  1.00   16.30  ? 17  HIS A CD2 1 
ATOM   159  C  CE1 . HIS A 1 17  ? 13.649  -2.839  22.496  1.00   18.92  ? 17  HIS A CE1 1 
ATOM   160  N  NE2 . HIS A 1 17  ? 13.080  -3.810  21.843  1.00   17.77  ? 17  HIS A NE2 1 
ATOM   161  N  N   . LYS A 1 18  ? 12.114  -0.370  19.680  1.00   13.88  ? 18  LYS A N   1 
ATOM   162  C  CA  . LYS A 1 18  ? 13.345  0.341   19.312  1.00   15.57  ? 18  LYS A CA  1 
ATOM   163  C  C   . LYS A 1 18  ? 13.042  1.698   18.678  1.00   16.40  ? 18  LYS A C   1 
ATOM   164  O  O   . LYS A 1 18  ? 13.714  2.704   18.949  1.00   21.32  ? 18  LYS A O   1 
ATOM   165  C  CB  . LYS A 1 18  ? 14.161  -0.551  18.417  1.00   16.34  ? 18  LYS A CB  1 
ATOM   166  C  CG  . LYS A 1 18  ? 14.773  -1.745  19.162  1.00   17.09  ? 18  LYS A CG  1 
ATOM   167  C  CD  . LYS A 1 18  ? 15.530  -2.674  18.186  1.00   17.53  ? 18  LYS A CD  1 
ATOM   168  C  CE  . LYS A 1 18  ? 14.554  -3.649  17.602  1.00   17.45  ? 18  LYS A CE  1 
ATOM   169  N  NZ  . LYS A 1 18  ? 15.200  -4.494  16.536  1.00   18.18  ? 18  LYS A NZ  1 
ATOM   170  N  N   . ASP A 1 19  ? 12.028  1.761   17.829  1.00   15.43  ? 19  ASP A N   1 
ATOM   171  C  CA  . ASP A 1 19  ? 11.616  3.026   17.236  1.00   16.58  ? 19  ASP A CA  1 
ATOM   172  C  C   . ASP A 1 19  ? 10.579  3.750   18.071  1.00   14.41  ? 19  ASP A C   1 
ATOM   173  O  O   . ASP A 1 19  ? 10.490  4.932   17.971  1.00   17.15  ? 19  ASP A O   1 
ATOM   174  C  CB  . ASP A 1 19  ? 11.089  2.818   15.795  1.00   19.09  ? 19  ASP A CB  1 
ATOM   175  C  CG  . ASP A 1 19  ? 12.177  2.791   14.769  1.00   31.67  ? 19  ASP A CG  1 
ATOM   176  O  OD1 . ASP A 1 19  ? 13.201  3.487   14.874  1.00   29.57  ? 19  ASP A OD1 1 
ATOM   177  O  OD2 . ASP A 1 19  ? 11.931  2.035   13.827  0.0000 54.06  ? 19  ASP A OD2 1 
ATOM   178  N  N   . PHE A 1 20  ? 9.807   3.031   18.873  1.00   13.95  ? 20  PHE A N   1 
ATOM   179  C  CA  . PHE A 1 20  ? 8.716   3.602   19.617  1.00   14.42  ? 20  PHE A CA  1 
ATOM   180  C  C   . PHE A 1 20  ? 8.802   3.093   21.051  1.00   13.59  ? 20  PHE A C   1 
ATOM   181  O  O   . PHE A 1 20  ? 8.142   2.121   21.410  1.00   13.08  ? 20  PHE A O   1 
ATOM   182  C  CB  . PHE A 1 20  ? 7.376   3.158   18.995  1.00   13.99  ? 20  PHE A CB  1 
ATOM   183  C  CG  . PHE A 1 20  ? 7.305   3.512   17.511  1.00   14.39  ? 20  PHE A CG  1 
ATOM   184  C  CD1 . PHE A 1 20  ? 6.951   4.755   17.121  1.00   16.58  ? 20  PHE A CD1 1 
ATOM   185  C  CD2 . PHE A 1 20  ? 7.683   2.564   16.570  1.00   16.45  ? 20  PHE A CD2 1 
ATOM   186  C  CE1 . PHE A 1 20  ? 6.967   5.110   15.774  1.00   19.79  ? 20  PHE A CE1 1 
ATOM   187  C  CE2 . PHE A 1 20  ? 7.720   2.849   15.206  1.00   19.11  ? 20  PHE A CE2 1 
ATOM   188  C  CZ  . PHE A 1 20  ? 7.335   4.110   14.835  1.00   18.48  ? 20  PHE A CZ  1 
ATOM   189  N  N   A PRO A 1 21  ? 9.610   3.698   21.987  0.50   13.38  ? 21  PRO A N   1 
ATOM   190  N  N   B PRO A 1 21  ? 9.722   3.714   21.746  0.50   13.69  ? 21  PRO A N   1 
ATOM   191  C  CA  A PRO A 1 21  ? 9.816   3.141   23.389  0.50   15.40  ? 21  PRO A CA  1 
ATOM   192  C  CA  B PRO A 1 21  ? 9.989   3.270   23.063  0.50   13.72  ? 21  PRO A CA  1 
ATOM   193  C  C   A PRO A 1 21  ? 8.627   3.116   24.402  0.50   11.74  ? 21  PRO A C   1 
ATOM   194  C  C   B PRO A 1 21  ? 8.728   3.144   23.903  0.50   12.08  ? 21  PRO A C   1 
ATOM   195  O  O   A PRO A 1 21  ? 8.668   2.413   25.410  0.50   11.10  ? 21  PRO A O   1 
ATOM   196  O  O   B PRO A 1 21  ? 8.731   2.299   24.814  0.50   11.15  ? 21  PRO A O   1 
ATOM   197  C  CB  A PRO A 1 21  ? 11.002  3.979   23.953  0.50   18.02  ? 21  PRO A CB  1 
ATOM   198  C  CB  B PRO A 1 21  ? 11.017  4.301   23.624  0.50   18.08  ? 21  PRO A CB  1 
ATOM   199  C  CG  A PRO A 1 21  ? 10.876  5.260   23.154  0.50   16.02  ? 21  PRO A CG  1 
ATOM   200  C  CG  B PRO A 1 21  ? 11.810  4.617   22.411  0.50   20.15  ? 21  PRO A CG  1 
ATOM   201  C  CD  A PRO A 1 21  ? 10.543  4.856   21.764  0.50   15.06  ? 21  PRO A CD  1 
ATOM   202  C  CD  B PRO A 1 21  ? 10.793  4.638   21.253  0.50   13.78  ? 21  PRO A CD  1 
ATOM   203  N  N   A ILE A 1 22  ? 7.589   3.870   24.123  0.50   10.82  ? 22  ILE A N   1 
ATOM   204  N  N   B ILE A 1 22  ? 7.672   3.915   23.589  0.50   10.80  ? 22  ILE A N   1 
ATOM   205  C  CA  A ILE A 1 22  ? 6.342   3.691   24.851  0.50   12.01  ? 22  ILE A CA  1 
ATOM   206  C  CA  B ILE A 1 22  ? 6.392   3.842   24.376  0.50   10.35  ? 22  ILE A CA  1 
ATOM   207  C  C   A ILE A 1 22  ? 5.765   2.339   24.472  0.50   11.26  ? 22  ILE A C   1 
ATOM   208  C  C   B ILE A 1 22  ? 5.795   2.402   24.455  0.50   11.35  ? 22  ILE A C   1 
ATOM   209  O  O   A ILE A 1 22  ? 4.792   1.982   25.037  0.50   10.66  ? 22  ILE A O   1 
ATOM   210  O  O   B ILE A 1 22  ? 4.974   2.034   25.403  0.50   11.86  ? 22  ILE A O   1 
ATOM   211  C  CB  A ILE A 1 22  ? 5.349   4.755   24.362  0.50   11.10  ? 22  ILE A CB  1 
ATOM   212  C  CB  B ILE A 1 22  ? 5.439   4.935   23.862  0.50   10.19  ? 22  ILE A CB  1 
ATOM   213  C  CG1 A ILE A 1 22  ? 4.254   5.119   25.351  0.50   11.70  ? 22  ILE A CG1 1 
ATOM   214  C  CG1 B ILE A 1 22  ? 4.362   5.294   24.873  0.50   12.52  ? 22  ILE A CG1 1 
ATOM   215  C  CG2 A ILE A 1 22  ? 4.721   4.335   23.029  0.50   11.82  ? 22  ILE A CG2 1 
ATOM   216  C  CG2 B ILE A 1 22  ? 4.872   4.526   22.510  0.50   10.41  ? 22  ILE A CG2 1 
ATOM   217  C  CD1 A ILE A 1 22  ? 3.445   6.255   24.712  0.50   13.64  ? 22  ILE A CD1 1 
ATOM   218  C  CD1 B ILE A 1 22  ? 4.815   5.630   26.300  0.50   19.22  ? 22  ILE A CD1 1 
ATOM   219  N  N   . ALA A 1 23  ? 6.291   1.547   23.549  1.00   11.36  ? 23  ALA A N   1 
ATOM   220  C  CA  . ALA A 1 23  ? 5.855   0.158   23.452  1.00   11.95  ? 23  ALA A CA  1 
ATOM   221  C  C   . ALA A 1 23  ? 5.934   -0.565  24.785  1.00   11.97  ? 23  ALA A C   1 
ATOM   222  O  O   . ALA A 1 23  ? 5.232   -1.568  24.941  1.00   12.51  ? 23  ALA A O   1 
ATOM   223  C  CB  . ALA A 1 23  ? 6.649   -0.617  22.420  1.00   12.57  ? 23  ALA A CB  1 
ATOM   224  N  N   . LYS A 1 24  ? 6.890   -0.158  25.640  1.00   12.65  ? 24  LYS A N   1 
ATOM   225  C  CA  . LYS A 1 24  ? 7.053   -0.753  26.947  1.00   13.43  ? 24  LYS A CA  1 
ATOM   226  C  C   . LYS A 1 24  ? 6.429   0.154   27.999  1.00   14.94  ? 24  LYS A C   1 
ATOM   227  O  O   . LYS A 1 24  ? 6.823   0.051   29.189  1.00   16.93  ? 24  LYS A O   1 
ATOM   228  C  CB  . LYS A 1 24  ? 8.554   -1.058  27.249  1.00   15.38  ? 24  LYS A CB  1 
ATOM   229  C  CG  . LYS A 1 24  ? 9.135   -2.032  26.263  1.00   17.30  ? 24  LYS A CG  1 
ATOM   230  C  CD  . LYS A 1 24  ? 10.629  -2.284  26.591  1.00   22.35  ? 24  LYS A CD  1 
ATOM   231  C  CE  . LYS A 1 24  ? 11.247  -3.294  25.671  1.00   23.73  ? 24  LYS A CE  1 
ATOM   232  N  NZ  . LYS A 1 24  ? 10.954  -4.665  26.039  1.00   34.81  ? 24  LYS A NZ  1 
ATOM   233  N  N   . GLY A 1 25  ? 5.425   0.959   27.652  1.00   14.14  ? 25  GLY A N   1 
ATOM   234  C  CA  . GLY A 1 25  ? 4.833   1.934   28.603  1.00   15.21  ? 25  GLY A CA  1 
ATOM   235  C  C   . GLY A 1 25  ? 3.845   1.285   29.571  1.00   12.93  ? 25  GLY A C   1 
ATOM   236  O  O   . GLY A 1 25  ? 3.665   0.058   29.660  1.00   13.88  ? 25  GLY A O   1 
ATOM   237  N  N   . GLU A 1 26  ? 3.187   2.194   30.278  1.00   13.80  ? 26  GLU A N   1 
ATOM   238  C  CA  . GLU A 1 26  ? 2.313   1.810   31.380  1.00   14.50  ? 26  GLU A CA  1 
ATOM   239  C  C   . GLU A 1 26  ? 0.870   1.583   30.952  1.00   11.90  ? 26  GLU A C   1 
ATOM   240  O  O   . GLU A 1 26  ? 0.099   1.093   31.804  1.00   14.08  ? 26  GLU A O   1 
ATOM   241  C  CB  . GLU A 1 26  ? 2.340   2.928   32.453  1.00   18.34  ? 26  GLU A CB  1 
ATOM   242  C  CG  . GLU A 1 26  ? 3.744   3.103   33.027  1.00   19.65  ? 26  GLU A CG  1 
ATOM   243  C  CD  . GLU A 1 26  ? 4.311   1.836   33.679  1.00   30.81  ? 26  GLU A CD  1 
ATOM   244  O  OE1 . GLU A 1 26  ? 3.589   1.203   34.518  1.00   33.44  ? 26  GLU A OE1 1 
ATOM   245  O  OE2 . GLU A 1 26  ? 5.512   1.501   33.398  1.00   38.97  ? 26  GLU A OE2 1 
ATOM   246  N  N   . ARG A 1 27  ? 0.478   1.908   29.749  1.00   10.41  ? 27  ARG A N   1 
ATOM   247  C  CA  . ARG A 1 27  ? -0.903  1.708   29.359  1.00   9.49   ? 27  ARG A CA  1 
ATOM   248  C  C   . ARG A 1 27  ? -0.979  1.252   27.885  1.00   9.11   ? 27  ARG A C   1 
ATOM   249  O  O   . ARG A 1 27  ? -1.678  1.854   27.066  1.00   9.45   ? 27  ARG A O   1 
ATOM   250  C  CB  . ARG A 1 27  ? -1.805  2.930   29.653  1.00   12.87  ? 27  ARG A CB  1 
ATOM   251  C  CG  . ARG A 1 27  ? -1.452  4.237   29.064  1.00   15.37  ? 27  ARG A CG  1 
ATOM   252  C  CD  . ARG A 1 27  ? -2.458  5.377   29.255  1.00   16.89  ? 27  ARG A CD  1 
ATOM   253  N  NE  . ARG A 1 27  ? -3.602  5.297   28.351  1.00   13.67  ? 27  ARG A NE  1 
ATOM   254  C  CZ  . ARG A 1 27  ? -4.541  6.232   28.253  1.00   12.77  ? 27  ARG A CZ  1 
ATOM   255  N  NH1 . ARG A 1 27  ? -4.473  7.321   29.008  1.00   16.35  ? 27  ARG A NH1 1 
ATOM   256  N  NH2 . ARG A 1 27  ? -5.546  6.080   27.406  1.00   13.87  ? 27  ARG A NH2 1 
ATOM   257  N  N   . GLN A 1 28  ? -0.249  0.178   27.598  1.00   8.75   ? 28  GLN A N   1 
ATOM   258  C  CA  . GLN A 1 28  ? -0.228  -0.366  26.242  1.00   8.11   ? 28  GLN A CA  1 
ATOM   259  C  C   . GLN A 1 28  ? -1.378  -1.315  25.992  1.00   7.72   ? 28  GLN A C   1 
ATOM   260  O  O   . GLN A 1 28  ? -1.863  -2.010  26.887  1.00   8.84   ? 28  GLN A O   1 
ATOM   261  C  CB  . GLN A 1 28  ? 1.127   -1.023  26.002  1.00   9.16   ? 28  GLN A CB  1 
ATOM   262  C  CG  . GLN A 1 28  ? 2.264   0.003   25.892  1.00   9.82   ? 28  GLN A CG  1 
ATOM   263  C  CD  . GLN A 1 28  ? 2.143   0.804   24.613  1.00   8.81   ? 28  GLN A CD  1 
ATOM   264  O  OE1 . GLN A 1 28  ? 2.299   0.242   23.522  1.00   9.25   ? 28  GLN A OE1 1 
ATOM   265  N  NE2 . GLN A 1 28  ? 1.806   2.078   24.718  1.00   9.55   ? 28  GLN A NE2 1 
ATOM   266  N  N   . SER A 1 29  ? -1.755  -1.406  24.708  1.00   7.81   ? 29  SER A N   1 
ATOM   267  C  CA  . SER A 1 29  ? -2.804  -2.287  24.242  1.00   7.60   ? 29  SER A CA  1 
ATOM   268  C  C   . SER A 1 29  ? -2.290  -3.180  23.141  1.00   7.10   ? 29  SER A C   1 
ATOM   269  O  O   . SER A 1 29  ? -1.338  -2.821  22.444  1.00   8.20   ? 29  SER A O   1 
ATOM   270  C  CB  . SER A 1 29  ? -3.961  -1.439  23.724  1.00   7.53   ? 29  SER A CB  1 
ATOM   271  O  OG  . SER A 1 29  ? -4.567  -0.706  24.783  1.00   7.72   ? 29  SER A OG  1 
ATOM   272  N  N   . PRO A 1 30  ? -2.931  -4.312  22.873  1.00   7.18   ? 30  PRO A N   1 
ATOM   273  C  CA  . PRO A 1 30  ? -4.090  -4.859  23.606  1.00   7.45   ? 30  PRO A CA  1 
ATOM   274  C  C   . PRO A 1 30  ? -3.681  -5.521  24.897  1.00   7.39   ? 30  PRO A C   1 
ATOM   275  O  O   . PRO A 1 30  ? -2.494  -5.555  25.229  1.00   8.22   ? 30  PRO A O   1 
ATOM   276  C  CB  . PRO A 1 30  ? -4.636  -5.864  22.596  1.00   7.73   ? 30  PRO A CB  1 
ATOM   277  C  CG  . PRO A 1 30  ? -3.345  -6.426  21.986  1.00   8.43   ? 30  PRO A CG  1 
ATOM   278  C  CD  . PRO A 1 30  ? -2.462  -5.234  21.832  1.00   7.89   ? 30  PRO A CD  1 
ATOM   279  N  N   . VAL A 1 31  ? -4.664  -6.055  25.610  1.00   7.77   ? 31  VAL A N   1 
ATOM   280  C  CA  . VAL A 1 31  ? -4.489  -6.820  26.826  1.00   8.26   ? 31  VAL A CA  1 
ATOM   281  C  C   . VAL A 1 31  ? -5.353  -8.027  26.783  1.00   8.20   ? 31  VAL A C   1 
ATOM   282  O  O   . VAL A 1 31  ? -6.351  -8.102  26.014  1.00   8.85   ? 31  VAL A O   1 
ATOM   283  C  CB  . VAL A 1 31  ? -4.808  -5.956  28.084  1.00   9.15   ? 31  VAL A CB  1 
ATOM   284  C  CG1 . VAL A 1 31  ? -3.883  -4.772  28.176  1.00   10.06  ? 31  VAL A CG1 1 
ATOM   285  C  CG2 . VAL A 1 31  ? -6.283  -5.558  28.120  1.00   9.62   ? 31  VAL A CG2 1 
ATOM   286  N  N   . ASP A 1 32  ? -5.039  -9.007  27.632  1.00   8.44   ? 32  ASP A N   1 
ATOM   287  C  CA  . ASP A 1 32  ? -5.945  -10.090 27.955  1.00   9.02   ? 32  ASP A CA  1 
ATOM   288  C  C   . ASP A 1 32  ? -6.983  -9.585  28.917  1.00   8.96   ? 32  ASP A C   1 
ATOM   289  O  O   . ASP A 1 32  ? -6.682  -8.930  29.928  1.00   10.77  ? 32  ASP A O   1 
ATOM   290  C  CB  . ASP A 1 32  ? -5.203  -11.265 28.537  1.00   10.11  ? 32  ASP A CB  1 
ATOM   291  C  CG  . ASP A 1 32  ? -6.114  -12.426 28.828  1.00   11.33  ? 32  ASP A CG  1 
ATOM   292  O  OD1 . ASP A 1 32  ? -6.827  -12.908 27.898  1.00   10.77  ? 32  ASP A OD1 1 
ATOM   293  O  OD2 . ASP A 1 32  ? -6.178  -12.877 30.002  1.00   13.76  ? 32  ASP A OD2 1 
ATOM   294  N  N   . ILE A 1 33  ? -8.223  -9.886  28.633  1.00   8.88   ? 33  ILE A N   1 
ATOM   295  C  CA  . ILE A 1 33  ? -9.360  -9.515  29.499  1.00   9.30   ? 33  ILE A CA  1 
ATOM   296  C  C   . ILE A 1 33  ? -9.641  -10.751 30.343  1.00   9.61   ? 33  ILE A C   1 
ATOM   297  O  O   . ILE A 1 33  ? -10.169 -11.732 29.874  1.00   10.80  ? 33  ILE A O   1 
ATOM   298  C  CB  . ILE A 1 33  ? -10.550 -9.099  28.687  1.00   9.83   ? 33  ILE A CB  1 
ATOM   299  C  CG1 . ILE A 1 33  ? -10.173 -7.898  27.820  1.00   10.73  ? 33  ILE A CG1 1 
ATOM   300  C  CG2 . ILE A 1 33  ? -11.761 -8.838  29.604  1.00   12.29  ? 33  ILE A CG2 1 
ATOM   301  C  CD1 . ILE A 1 33  ? -11.240 -7.587  26.732  1.00   11.95  ? 33  ILE A CD1 1 
ATOM   302  N  N   A ASP A 1 34  ? -9.200  -10.729 31.592  0.50   12.02  ? 34  ASP A N   1 
ATOM   303  N  N   B ASP A 1 34  ? -9.328  -10.630 31.644  0.50   10.73  ? 34  ASP A N   1 
ATOM   304  C  CA  A ASP A 1 34  ? -9.480  -11.822 32.491  0.50   11.77  ? 34  ASP A CA  1 
ATOM   305  C  CA  B ASP A 1 34  ? -9.607  -11.662 32.656  0.50   12.30  ? 34  ASP A CA  1 
ATOM   306  C  C   A ASP A 1 34  ? -10.890 -11.456 33.046  0.50   12.44  ? 34  ASP A C   1 
ATOM   307  C  C   B ASP A 1 34  ? -11.082 -11.455 33.104  0.50   12.63  ? 34  ASP A C   1 
ATOM   308  O  O   A ASP A 1 34  ? -10.970 -10.435 33.865  0.50   13.42  ? 34  ASP A O   1 
ATOM   309  O  O   B ASP A 1 34  ? -11.489 -10.592 33.818  0.50   12.20  ? 34  ASP A O   1 
ATOM   310  C  CB  A ASP A 1 34  ? -8.436  -11.858 33.580  0.50   14.64  ? 34  ASP A CB  1 
ATOM   311  C  CB  B ASP A 1 34  ? -8.593  -11.607 33.800  0.50   14.74  ? 34  ASP A CB  1 
ATOM   312  C  CG  A ASP A 1 34  ? -8.626  -13.035 34.473  0.50   17.50  ? 34  ASP A CG  1 
ATOM   313  C  CG  B ASP A 1 34  ? -8.802  -12.733 34.812  0.50   14.93  ? 34  ASP A CG  1 
ATOM   314  O  OD1 A ASP A 1 34  ? -9.259  -12.920 35.537  0.50   24.83  ? 34  ASP A OD1 1 
ATOM   315  O  OD1 B ASP A 1 34  ? -9.960  -13.201 34.971  0.50   16.33  ? 34  ASP A OD1 1 
ATOM   316  O  OD2 A ASP A 1 34  ? -8.250  -14.111 34.030  0.50   21.27  ? 34  ASP A OD2 1 
ATOM   317  O  OD2 B ASP A 1 34  ? -7.811  -13.121 35.431  0.50   18.59  ? 34  ASP A OD2 1 
ATOM   318  N  N   . THR A 1 35  ? -11.926 -12.262 32.603  1.00   13.49  ? 35  THR A N   1 
ATOM   319  C  CA  . THR A 1 35  ? -13.310 -11.954 32.829  1.00   14.83  ? 35  THR A CA  1 
ATOM   320  C  C   . THR A 1 35  ? -13.712 -12.097 34.286  1.00   13.88  ? 35  THR A C   1 
ATOM   321  O  O   . THR A 1 35  ? -14.665 -11.417 34.719  1.00   17.64  ? 35  THR A O   1 
ATOM   322  C  CB  . THR A 1 35  ? -14.202 -12.848 32.010  1.00   16.06  ? 35  THR A CB  1 
ATOM   323  O  OG1 . THR A 1 35  ? -14.075 -14.164 32.493  1.00   17.12  ? 35  THR A OG1 1 
ATOM   324  C  CG2 . THR A 1 35  ? -13.991 -12.743 30.528  1.00   17.70  ? 35  THR A CG2 1 
ATOM   325  N  N   A HIS A 1 36  ? -13.028 -12.949 35.010  0.50   10.65  ? 36  HIS A N   1 
ATOM   326  N  N   B HIS A 1 36  ? -12.777 -12.722 35.120  0.50   13.31  ? 36  HIS A N   1 
ATOM   327  C  CA  A HIS A 1 36  ? -13.329 -13.153 36.402  0.50   11.81  ? 36  HIS A CA  1 
ATOM   328  C  CA  B HIS A 1 36  ? -12.871 -12.928 36.623  0.50   14.82  ? 36  HIS A CA  1 
ATOM   329  C  C   A HIS A 1 36  ? -12.857 -12.013 37.258  0.50   11.32  ? 36  HIS A C   1 
ATOM   330  C  C   B HIS A 1 36  ? -12.447 -11.747 37.413  0.50   15.84  ? 36  HIS A C   1 
ATOM   331  O  O   A HIS A 1 36  ? -13.517 -11.716 38.254  0.50   14.23  ? 36  HIS A O   1 
ATOM   332  O  O   B HIS A 1 36  ? -13.152 -11.301 38.348  0.50   24.65  ? 36  HIS A O   1 
ATOM   333  C  CB  A HIS A 1 36  ? -12.873 -14.559 36.816  0.50   14.19  ? 36  HIS A CB  1 
ATOM   334  C  CB  B HIS A 1 36  ? -12.169 -14.236 37.026  0.50   16.05  ? 36  HIS A CB  1 
ATOM   335  C  CG  A HIS A 1 36  ? -13.793 -15.650 36.285  0.50   13.19  ? 36  HIS A CG  1 
ATOM   336  C  CG  B HIS A 1 36  ? -12.641 -15.372 36.208  0.50   18.79  ? 36  HIS A CG  1 
ATOM   337  N  ND1 A HIS A 1 36  ? -13.378 -16.578 35.413  0.50   16.43  ? 36  HIS A ND1 1 
ATOM   338  N  ND1 B HIS A 1 36  ? -11.844 -16.010 35.352  0.50   23.56  ? 36  HIS A ND1 1 
ATOM   339  C  CD2 A HIS A 1 36  ? -15.066 -15.988 36.615  0.50   14.29  ? 36  HIS A CD2 1 
ATOM   340  C  CD2 B HIS A 1 36  ? -13.812 -16.094 36.272  0.50   21.52  ? 36  HIS A CD2 1 
ATOM   341  C  CE1 A HIS A 1 36  ? -14.374 -17.421 35.167  0.50   18.99  ? 36  HIS A CE1 1 
ATOM   342  C  CE1 B HIS A 1 36  ? -12.497 -17.049 34.827  0.50   27.06  ? 36  HIS A CE1 1 
ATOM   343  N  NE2 A HIS A 1 36  ? -15.388 -17.071 35.914  0.50   17.60  ? 36  HIS A NE2 1 
ATOM   344  N  NE2 B HIS A 1 36  ? -13.705 -17.105 35.400  0.50   23.83  ? 36  HIS A NE2 1 
ATOM   345  N  N   A THR A 1 37  ? -11.787 -11.331 36.866  0.50   12.83  ? 37  THR A N   1 
ATOM   346  N  N   B THR A 1 37  ? -11.494 -11.113 36.916  0.50   13.70  ? 37  THR A N   1 
ATOM   347  C  CA  A THR A 1 37  ? -11.293 -10.205 37.608  0.50   14.45  ? 37  THR A CA  1 
ATOM   348  C  CA  B THR A 1 37  ? -11.012 -10.054 37.612  0.50   13.80  ? 37  THR A CA  1 
ATOM   349  C  C   A THR A 1 37  ? -11.747 -8.787  37.172  0.50   14.01  ? 37  THR A C   1 
ATOM   350  C  C   B THR A 1 37  ? -11.678 -8.736  37.165  0.50   15.02  ? 37  THR A C   1 
ATOM   351  O  O   A THR A 1 37  ? -11.612 -7.822  37.907  0.50   13.43  ? 37  THR A O   1 
ATOM   352  O  O   B THR A 1 37  ? -11.623 -7.786  37.907  0.50   18.73  ? 37  THR A O   1 
ATOM   353  C  CB  A THR A 1 37  ? -9.823  -10.202 37.789  0.50   16.58  ? 37  THR A CB  1 
ATOM   354  C  CB  B THR A 1 37  ? -9.566  -10.104 37.394  0.50   17.58  ? 37  THR A CB  1 
ATOM   355  O  OG1 A THR A 1 37  ? -9.206  -10.149 36.583  0.50   20.15  ? 37  THR A OG1 1 
ATOM   356  O  OG1 B THR A 1 37  ? -9.160  -11.334 37.994  0.50   23.20  ? 37  THR A OG1 1 
ATOM   357  C  CG2 A THR A 1 37  ? -9.373  -11.449 38.215  0.50   20.94  ? 37  THR A CG2 1 
ATOM   358  C  CG2 B THR A 1 37  ? -8.922  -8.963  38.063  0.50   18.98  ? 37  THR A CG2 1 
ATOM   359  N  N   . ALA A 1 38  ? -12.334 -8.696  36.005  1.00   15.51  ? 38  ALA A N   1 
ATOM   360  C  CA  . ALA A 1 38  ? -12.969 -7.461  35.595  1.00   14.71  ? 38  ALA A CA  1 
ATOM   361  C  C   . ALA A 1 38  ? -14.112 -7.173  36.506  1.00   17.58  ? 38  ALA A C   1 
ATOM   362  O  O   . ALA A 1 38  ? -14.876 -8.022  36.827  1.00   27.55  ? 38  ALA A O   1 
ATOM   363  C  CB  . ALA A 1 38  ? -13.495 -7.581  34.195  1.00   15.40  ? 38  ALA A CB  1 
ATOM   364  N  N   . LYS A 1 39  ? -14.237 -5.957  36.981  1.00   17.60  ? 39  LYS A N   1 
ATOM   365  C  CA  . LYS A 1 39  ? -15.342 -5.727  37.930  1.00   20.29  ? 39  LYS A CA  1 
ATOM   366  C  C   . LYS A 1 39  ? -16.443 -5.035  37.334  1.00   14.98  ? 39  LYS A C   1 
ATOM   367  O  O   . LYS A 1 39  ? -16.274 -4.084  36.518  1.00   14.42  ? 39  LYS A O   1 
ATOM   368  C  CB  . LYS A 1 39  ? -14.891 -4.953  39.155  1.00   24.38  ? 39  LYS A CB  1 
ATOM   369  C  CG  . LYS A 1 39  ? -15.881 -4.999  40.350  1.00   26.32  ? 39  LYS A CG  1 
ATOM   370  C  CD  . LYS A 1 39  ? -15.256 -4.068  41.379  1.00   26.31  ? 39  LYS A CD  1 
ATOM   371  C  CE  . LYS A 1 39  ? -16.273 -3.326  42.216  1.00   39.63  ? 39  LYS A CE  1 
ATOM   372  N  NZ  . LYS A 1 39  ? -16.522 -4.104  43.457  1.00   36.60  ? 39  LYS A NZ  1 
ATOM   373  N  N   . TYR A 1 40  ? -17.662 -5.477  37.666  1.00   18.02  ? 40  TYR A N   1 
ATOM   374  C  CA  . TYR A 1 40  ? -18.812 -4.805  37.237  1.00   16.79  ? 40  TYR A CA  1 
ATOM   375  C  C   . TYR A 1 40  ? -18.871 -3.443  37.875  1.00   14.71  ? 40  TYR A C   1 
ATOM   376  O  O   . TYR A 1 40  ? -18.700 -3.278  39.113  1.00   16.73  ? 40  TYR A O   1 
ATOM   377  C  CB  . TYR A 1 40  ? -20.099 -5.604  37.655  1.00   18.99  ? 40  TYR A CB  1 
ATOM   378  C  CG  . TYR A 1 40  ? -21.386 -4.818  37.533  1.00   21.05  ? 40  TYR A CG  1 
ATOM   379  C  CD1 . TYR A 1 40  ? -21.800 -4.304  36.330  1.00   18.50  ? 40  TYR A CD1 1 
ATOM   380  C  CD2 . TYR A 1 40  ? -22.223 -4.641  38.606  1.00   26.28  ? 40  TYR A CD2 1 
ATOM   381  C  CE1 . TYR A 1 40  ? -22.982 -3.575  36.166  1.00   24.46  ? 40  TYR A CE1 1 
ATOM   382  C  CE2 . TYR A 1 40  ? -23.426 -3.919  38.433  1.00   26.37  ? 40  TYR A CE2 1 
ATOM   383  C  CZ  . TYR A 1 40  ? -23.786 -3.350  37.252  1.00   24.07  ? 40  TYR A CZ  1 
ATOM   384  O  OH  . TYR A 1 40  ? -24.970 -2.694  37.055  1.00   32.48  ? 40  TYR A OH  1 
ATOM   385  N  N   . ASP A 1 41  ? -19.071 -2.419  37.076  1.00   13.62  ? 41  ASP A N   1 
ATOM   386  C  CA  . ASP A 1 41  ? -19.162 -1.053  37.552  1.00   13.91  ? 41  ASP A CA  1 
ATOM   387  C  C   . ASP A 1 41  ? -20.565 -0.566  37.298  1.00   15.88  ? 41  ASP A C   1 
ATOM   388  O  O   . ASP A 1 41  ? -20.884 -0.192  36.156  1.00   15.53  ? 41  ASP A O   1 
ATOM   389  C  CB  . ASP A 1 41  ? -18.114 -0.214  36.826  1.00   17.80  ? 41  ASP A CB  1 
ATOM   390  C  CG  . ASP A 1 41  ? -18.041 1.188   37.330  1.00   19.53  ? 41  ASP A CG  1 
ATOM   391  O  OD1 . ASP A 1 41  ? -18.945 1.573   38.123  1.00   20.69  ? 41  ASP A OD1 1 
ATOM   392  O  OD2 . ASP A 1 41  ? -17.071 1.916   36.961  1.00   22.59  ? 41  ASP A OD2 1 
ATOM   393  N  N   . PRO A 1 42  ? -21.397 -0.487  38.347  1.00   18.13  ? 42  PRO A N   1 
ATOM   394  C  CA  . PRO A 1 42  ? -22.752 0.031   38.167  1.00   21.67  ? 42  PRO A CA  1 
ATOM   395  C  C   . PRO A 1 42  ? -22.762 1.544   37.779  1.00   19.63  ? 42  PRO A C   1 
ATOM   396  O  O   . PRO A 1 42  ? -23.822 2.015   37.348  1.00   31.27  ? 42  PRO A O   1 
ATOM   397  C  CB  . PRO A 1 42  ? -23.410 -0.233  39.529  1.00   27.70  ? 42  PRO A CB  1 
ATOM   398  C  CG  . PRO A 1 42  ? -22.266 -0.231  40.486  1.00   31.53  ? 42  PRO A CG  1 
ATOM   399  C  CD  . PRO A 1 42  ? -21.135 -0.887  39.770  1.00   21.55  ? 42  PRO A CD  1 
ATOM   400  N  N   . SER A 1 43  ? -21.668 2.280   37.894  1.00   20.53  ? 43  SER A N   1 
ATOM   401  C  CA  . SER A 1 43  ? -21.626 3.657   37.395  1.00   22.11  ? 43  SER A CA  1 
ATOM   402  C  C   . SER A 1 43  ? -21.463 3.789   35.857  1.00   20.73  ? 43  SER A C   1 
ATOM   403  O  O   . SER A 1 43  ? -21.645 4.881   35.250  1.00   26.43  ? 43  SER A O   1 
ATOM   404  C  CB  . SER A 1 43  ? -20.519 4.444   38.076  1.00   23.47  ? 43  SER A CB  1 
ATOM   405  O  OG  . SER A 1 43  ? -19.226 4.124   37.611  1.00   23.92  ? 43  SER A OG  1 
ATOM   406  N  N   . LEU A 1 44  ? -21.070 2.700   35.183  1.00   20.51  ? 44  LEU A N   1 
ATOM   407  C  CA  . LEU A 1 44  ? -20.917 2.686   33.695  1.00   18.97  ? 44  LEU A CA  1 
ATOM   408  C  C   . LEU A 1 44  ? -22.302 2.840   33.071  1.00   20.35  ? 44  LEU A C   1 
ATOM   409  O  O   . LEU A 1 44  ? -23.300 2.345   33.544  1.00   25.98  ? 44  LEU A O   1 
ATOM   410  C  CB  . LEU A 1 44  ? -20.204 1.471   33.201  1.00   17.08  ? 44  LEU A CB  1 
ATOM   411  C  CG  . LEU A 1 44  ? -18.751 1.431   33.430  1.00   16.40  ? 44  LEU A CG  1 
ATOM   412  C  CD1 . LEU A 1 44  ? -18.249 0.017   33.067  1.00   18.67  ? 44  LEU A CD1 1 
ATOM   413  C  CD2 . LEU A 1 44  ? -18.033 2.538   32.660  1.00   17.07  ? 44  LEU A CD2 1 
ATOM   414  N  N   . LYS A 1 45  ? -22.342 3.576   31.965  1.00   20.12  ? 45  LYS A N   1 
ATOM   415  C  CA  . LYS A 1 45  ? -23.612 3.854   31.291  1.00   22.04  ? 45  LYS A CA  1 
ATOM   416  C  C   . LYS A 1 45  ? -23.683 2.984   30.055  1.00   18.52  ? 45  LYS A C   1 
ATOM   417  O  O   . LYS A 1 45  ? -22.671 2.463   29.598  1.00   18.35  ? 45  LYS A O   1 
ATOM   418  C  CB  . LYS A 1 45  ? -23.714 5.269   30.857  1.00   20.37  ? 45  LYS A CB  1 
ATOM   419  C  CG  . LYS A 1 45  ? -23.518 6.417   31.844  1.00   27.00  ? 45  LYS A CG  1 
ATOM   420  C  CD  . LYS A 1 45  ? -24.299 7.660   31.438  0.010  24.04  ? 45  LYS A CD  1 
ATOM   421  C  CE  . LYS A 1 45  ? -23.695 8.352   30.225  0.010  16.32  ? 45  LYS A CE  1 
ATOM   422  N  NZ  . LYS A 1 45  ? -24.490 9.534   29.791  0.010  16.99  ? 45  LYS A NZ  1 
ATOM   423  N  N   . PRO A 1 46  ? -24.944 2.770   29.543  1.00   18.42  ? 46  PRO A N   1 
ATOM   424  C  CA  . PRO A 1 46  ? -25.033 2.076   28.252  1.00   18.59  ? 46  PRO A CA  1 
ATOM   425  C  C   . PRO A 1 46  ? -24.211 2.834   27.232  1.00   14.39  ? 46  PRO A C   1 
ATOM   426  O  O   . PRO A 1 46  ? -24.184 4.050   27.304  1.00   16.19  ? 46  PRO A O   1 
ATOM   427  C  CB  . PRO A 1 46  ? -26.526 2.147   27.921  1.00   19.51  ? 46  PRO A CB  1 
ATOM   428  C  CG  . PRO A 1 46  ? -27.245 2.445   29.197  1.00   29.78  ? 46  PRO A CG  1 
ATOM   429  C  CD  . PRO A 1 46  ? -26.242 3.062   30.133  1.00   21.30  ? 46  PRO A CD  1 
ATOM   430  N  N   . LEU A 1 47  ? -23.646 2.069   26.320  1.00   17.71  ? 47  LEU A N   1 
ATOM   431  C  CA  . LEU A 1 47  ? -22.930 2.700   25.244  1.00   16.10  ? 47  LEU A CA  1 
ATOM   432  C  C   . LEU A 1 47  ? -23.983 3.384   24.313  1.00   16.77  ? 47  LEU A C   1 
ATOM   433  O  O   . LEU A 1 47  ? -24.987 2.721   24.059  1.00   21.31  ? 47  LEU A O   1 
ATOM   434  C  CB  . LEU A 1 47  ? -22.166 1.662   24.449  1.00   19.48  ? 47  LEU A CB  1 
ATOM   435  C  CG  . LEU A 1 47  ? -21.058 2.044   23.626  1.00   19.95  ? 47  LEU A CG  1 
ATOM   436  C  CD1 . LEU A 1 47  ? -20.063 2.919   24.442  1.00   25.42  ? 47  LEU A CD1 1 
ATOM   437  C  CD2 . LEU A 1 47  ? -20.449 0.780   23.002  1.00   20.72  ? 47  LEU A CD2 1 
ATOM   438  N  N   . SER A 1 48  ? -23.746 4.565   23.797  1.00   14.28  ? 48  SER A N   1 
ATOM   439  C  CA  . SER A 1 48  ? -24.571 5.142   22.778  1.00   14.28  ? 48  SER A CA  1 
ATOM   440  C  C   . SER A 1 48  ? -23.801 5.167   21.466  1.00   13.68  ? 48  SER A C   1 
ATOM   441  O  O   . SER A 1 48  ? -22.788 5.902   21.343  1.00   14.44  ? 48  SER A O   1 
ATOM   442  C  CB  . SER A 1 48  ? -24.935 6.549   23.181  1.00   16.18  ? 48  SER A CB  1 
ATOM   443  O  OG  . SER A 1 48  ? -25.536 7.299   22.186  1.00   19.68  ? 48  SER A OG  1 
ATOM   444  N  N   . VAL A 1 49  ? -24.234 4.381   20.514  1.00   14.86  ? 49  VAL A N   1 
ATOM   445  C  CA  . VAL A 1 49  ? -23.633 4.341   19.225  1.00   16.53  ? 49  VAL A CA  1 
ATOM   446  C  C   . VAL A 1 49  ? -24.603 4.924   18.226  1.00   16.18  ? 49  VAL A C   1 
ATOM   447  O  O   . VAL A 1 49  ? -25.663 4.356   18.029  1.00   22.51  ? 49  VAL A O   1 
ATOM   448  C  CB  . VAL A 1 49  ? -23.380 2.868   18.796  1.00   18.83  ? 49  VAL A CB  1 
ATOM   449  C  CG1 . VAL A 1 49  ? -22.642 2.798   17.497  1.00   25.05  ? 49  VAL A CG1 1 
ATOM   450  C  CG2 . VAL A 1 49  ? -22.578 2.135   19.855  1.00   22.27  ? 49  VAL A CG2 1 
ATOM   451  N  N   . SER A 1 50  ? -24.326 6.074   17.629  1.00   16.40  ? 50  SER A N   1 
ATOM   452  C  CA  . SER A 1 50  ? -25.282 6.713   16.747  1.00   19.37  ? 50  SER A CA  1 
ATOM   453  C  C   . SER A 1 50  ? -24.623 6.842   15.401  1.00   16.63  ? 50  SER A C   1 
ATOM   454  O  O   . SER A 1 50  ? -23.937 7.829   15.093  1.00   17.99  ? 50  SER A O   1 
ATOM   455  C  CB  . SER A 1 50  ? -25.651 8.063   17.293  1.00   21.34  ? 50  SER A CB  1 
ATOM   456  O  OG  . SER A 1 50  ? -26.263 7.926   18.554  1.00   26.48  ? 50  SER A OG  1 
ATOM   457  N  N   . TYR A 1 51  ? -24.873 5.848   14.549  1.00   16.64  ? 51  TYR A N   1 
ATOM   458  C  CA  . TYR A 1 51  ? -24.278 5.783   13.262  1.00   16.13  ? 51  TYR A CA  1 
ATOM   459  C  C   . TYR A 1 51  ? -25.282 6.034   12.105  1.00   16.53  ? 51  TYR A C   1 
ATOM   460  O  O   . TYR A 1 51  ? -24.871 5.846   10.983  1.00   18.38  ? 51  TYR A O   1 
ATOM   461  C  CB  . TYR A 1 51  ? -23.623 4.409   13.060  1.00   16.03  ? 51  TYR A CB  1 
ATOM   462  C  CG  . TYR A 1 51  ? -22.383 4.085   13.857  1.00   13.63  ? 51  TYR A CG  1 
ATOM   463  C  CD1 . TYR A 1 51  ? -21.627 5.098   14.487  1.00   14.09  ? 51  TYR A CD1 1 
ATOM   464  C  CD2 . TYR A 1 51  ? -21.906 2.790   13.945  1.00   13.44  ? 51  TYR A CD2 1 
ATOM   465  C  CE1 . TYR A 1 51  ? -20.423 4.779   15.151  1.00   12.86  ? 51  TYR A CE1 1 
ATOM   466  C  CE2 . TYR A 1 51  ? -20.701 2.463   14.613  1.00   12.71  ? 51  TYR A CE2 1 
ATOM   467  C  CZ  . TYR A 1 51  ? -19.957 3.468   15.216  1.00   12.53  ? 51  TYR A CZ  1 
ATOM   468  O  OH  . TYR A 1 51  ? -18.822 3.101   15.870  1.00   12.60  ? 51  TYR A OH  1 
ATOM   469  N  N   . ASP A 1 52  ? -26.480 6.472   12.401  1.00   20.15  ? 52  ASP A N   1 
ATOM   470  C  CA  . ASP A 1 52  ? -27.463 6.708   11.355  1.00   21.11  ? 52  ASP A CA  1 
ATOM   471  C  C   . ASP A 1 52  ? -27.059 7.718   10.284  1.00   21.73  ? 52  ASP A C   1 
ATOM   472  O  O   . ASP A 1 52  ? -27.526 7.546   9.143   1.00   25.07  ? 52  ASP A O   1 
ATOM   473  C  CB  . ASP A 1 52  ? -28.768 7.185   11.992  1.00   25.85  ? 52  ASP A CB  1 
ATOM   474  C  CG  . ASP A 1 52  ? -28.517 8.080   13.291  1.00   39.48  ? 52  ASP A CG  1 
ATOM   475  O  OD1 . ASP A 1 52  ? -27.769 7.698   14.284  1.00   46.25  ? 52  ASP A OD1 1 
ATOM   476  O  OD2 . ASP A 1 52  ? -29.124 9.190   13.306  0.0000 66.91  ? 52  ASP A OD2 1 
ATOM   477  N  N   . GLN A 1 53  ? -26.187 8.648   10.591  1.00   20.63  ? 53  GLN A N   1 
ATOM   478  C  CA  . GLN A 1 53  ? -25.748 9.572   9.491   1.00   22.30  ? 53  GLN A CA  1 
ATOM   479  C  C   . GLN A 1 53  ? -24.317 9.322   9.049   1.00   17.30  ? 53  GLN A C   1 
ATOM   480  O  O   . GLN A 1 53  ? -23.729 10.140  8.374   1.00   19.20  ? 53  GLN A O   1 
ATOM   481  C  CB  . GLN A 1 53  ? -25.918 11.042  9.916   1.00   27.73  ? 53  GLN A CB  1 
ATOM   482  C  CG  . GLN A 1 53  ? -27.407 11.436  9.911   1.00   33.76  ? 53  GLN A CG  1 
ATOM   483  C  CD  . GLN A 1 53  ? -28.066 11.220  8.543   1.00   42.34  ? 53  GLN A CD  1 
ATOM   484  O  OE1 . GLN A 1 53  ? -27.569 11.701  7.477   0.0000 62.27  ? 53  GLN A OE1 1 
ATOM   485  N  NE2 . GLN A 1 53  ? -29.112 10.416  8.536   1.00   44.47  ? 53  GLN A NE2 1 
ATOM   486  N  N   . ALA A 1 54  ? -23.796 8.163   9.366   1.00   17.20  ? 54  ALA A N   1 
ATOM   487  C  CA  . ALA A 1 54  ? -22.393 7.908   8.982   1.00   15.34  ? 54  ALA A CA  1 
ATOM   488  C  C   . ALA A 1 54  ? -22.236 7.986   7.487   1.00   17.08  ? 54  ALA A C   1 
ATOM   489  O  O   . ALA A 1 54  ? -23.092 7.492   6.732   1.00   22.94  ? 54  ALA A O   1 
ATOM   490  C  CB  . ALA A 1 54  ? -21.913 6.533   9.470   1.00   18.90  ? 54  ALA A CB  1 
ATOM   491  N  N   A THR A 1 55  ? -21.158 8.626   7.037   0.50   14.47  ? 55  THR A N   1 
ATOM   492  N  N   B THR A 1 55  ? -21.158 8.614   7.036   0.50   14.74  ? 55  THR A N   1 
ATOM   493  C  CA  A THR A 1 55  ? -20.849 8.821   5.629   0.50   14.88  ? 55  THR A CA  1 
ATOM   494  C  CA  B THR A 1 55  ? -20.878 8.785   5.626   0.50   17.88  ? 55  THR A CA  1 
ATOM   495  C  C   A THR A 1 55  ? -19.488 8.273   5.310   0.50   12.03  ? 55  THR A C   1 
ATOM   496  C  C   B THR A 1 55  ? -19.494 8.276   5.301   0.50   14.50  ? 55  THR A C   1 
ATOM   497  O  O   A THR A 1 55  ? -18.514 8.886   5.524   0.50   10.84  ? 55  THR A O   1 
ATOM   498  O  O   B THR A 1 55  ? -18.522 8.890   5.525   0.50   13.48  ? 55  THR A O   1 
ATOM   499  C  CB  A THR A 1 55  ? -20.907 10.301  5.112   0.50   18.54  ? 55  THR A CB  1 
ATOM   500  C  CB  B THR A 1 55  ? -21.190 10.219  5.090   0.50   16.09  ? 55  THR A CB  1 
ATOM   501  O  OG1 A THR A 1 55  ? -22.116 10.931  5.443   0.50   21.09  ? 55  THR A OG1 1 
ATOM   502  O  OG1 B THR A 1 55  ? -20.953 10.242  3.683   0.50   19.19  ? 55  THR A OG1 1 
ATOM   503  C  CG2 A THR A 1 55  ? -20.893 10.255  3.652   0.50   19.20  ? 55  THR A CG2 1 
ATOM   504  C  CG2 B THR A 1 55  ? -20.380 11.075  5.683   0.50   19.68  ? 55  THR A CG2 1 
ATOM   505  N  N   . SER A 1 56  ? -19.456 7.061   4.795   1.00   15.10  ? 56  SER A N   1 
ATOM   506  C  CA  . SER A 1 56  ? -18.210 6.469   4.371   1.00   14.83  ? 56  SER A CA  1 
ATOM   507  C  C   . SER A 1 56  ? -17.794 7.111   3.080   1.00   15.60  ? 56  SER A C   1 
ATOM   508  O  O   . SER A 1 56  ? -18.522 7.596   2.287   1.00   18.69  ? 56  SER A O   1 
ATOM   509  C  CB  . SER A 1 56  ? -18.252 4.965   4.251   1.00   16.10  ? 56  SER A CB  1 
ATOM   510  O  OG  . SER A 1 56  ? -19.117 4.584   3.163   1.00   16.80  ? 56  SER A OG  1 
ATOM   511  N  N   . LEU A 1 57  ? -16.518 7.169   2.926   1.00   14.19  ? 57  LEU A N   1 
ATOM   512  C  CA  . LEU A 1 57  ? -16.023 7.764   1.699   1.00   15.97  ? 57  LEU A CA  1 
ATOM   513  C  C   . LEU A 1 57  ? -15.161 6.809   0.884   1.00   13.55  ? 57  LEU A C   1 
ATOM   514  O  O   . LEU A 1 57  ? -15.197 6.869   -0.352  1.00   16.25  ? 57  LEU A O   1 
ATOM   515  C  CB  . LEU A 1 57  ? -15.149 8.895   2.096   1.00   18.16  ? 57  LEU A CB  1 
ATOM   516  C  CG  . LEU A 1 57  ? -15.971 10.129  2.650   1.00   20.94  ? 57  LEU A CG  1 
ATOM   517  C  CD1 . LEU A 1 57  ? -14.906 11.131  3.044   1.00   25.68  ? 57  LEU A CD1 1 
ATOM   518  C  CD2 . LEU A 1 57  ? -17.052 10.676  1.717   1.00   27.63  ? 57  LEU A CD2 1 
ATOM   519  N  N   . ARG A 1 58  ? -14.299 6.059   1.539   1.00   14.19  ? 58  ARG A N   1 
ATOM   520  C  CA  . ARG A 1 58  ? -13.252 5.396   0.786   1.00   14.35  ? 58  ARG A CA  1 
ATOM   521  C  C   . ARG A 1 58  ? -12.749 4.222   1.593   1.00   12.64  ? 58  ARG A C   1 
ATOM   522  O  O   . ARG A 1 58  ? -12.891 4.189   2.805   1.00   13.78  ? 58  ARG A O   1 
ATOM   523  C  CB  . ARG A 1 58  ? -12.085 6.397   0.603   1.00   16.73  ? 58  ARG A CB  1 
ATOM   524  C  CG  . ARG A 1 58  ? -11.033 6.066   -0.304  1.00   18.01  ? 58  ARG A CG  1 
ATOM   525  C  CD  . ARG A 1 58  ? -10.024 7.188   -0.484  1.00   21.78  ? 58  ARG A CD  1 
ATOM   526  N  NE  . ARG A 1 58  ? -9.133  7.195   0.666   1.00   18.70  ? 58  ARG A NE  1 
ATOM   527  C  CZ  . ARG A 1 58  ? -7.820  7.392   0.625   1.00   16.34  ? 58  ARG A CZ  1 
ATOM   528  N  NH1 . ARG A 1 58  ? -7.190  7.627   -0.521  1.00   20.60  ? 58  ARG A NH1 1 
ATOM   529  N  NH2 . ARG A 1 58  ? -7.136  7.362   1.757   1.00   17.43  ? 58  ARG A NH2 1 
ATOM   530  N  N   . ILE A 1 59  ? -12.081 3.280   0.909   1.00   13.33  ? 59  ILE A N   1 
ATOM   531  C  CA  . ILE A 1 59  ? -11.453 2.166   1.582   1.00   13.10  ? 59  ILE A CA  1 
ATOM   532  C  C   . ILE A 1 59  ? -9.998  2.170   1.055   1.00   12.19  ? 59  ILE A C   1 
ATOM   533  O  O   . ILE A 1 59  ? -9.717  2.354   -0.159  1.00   15.17  ? 59  ILE A O   1 
ATOM   534  C  CB  . ILE A 1 59  ? -12.130 0.859   1.298   1.00   12.87  ? 59  ILE A CB  1 
ATOM   535  C  CG1 . ILE A 1 59  ? -11.543 -0.257  2.190   1.00   13.06  ? 59  ILE A CG1 1 
ATOM   536  C  CG2 . ILE A 1 59  ? -12.157 0.428   -0.181  1.00   15.28  ? 59  ILE A CG2 1 
ATOM   537  C  CD1 . ILE A 1 59  ? -12.407 -1.508  2.113   1.00   13.80  ? 59  ILE A CD1 1 
ATOM   538  N  N   . LEU A 1 60  ? -9.004  1.976   1.927   1.00   11.93  ? 60  LEU A N   1 
ATOM   539  C  CA  . LEU A 1 60  ? -7.623  2.103   1.698   1.00   11.95  ? 60  LEU A CA  1 
ATOM   540  C  C   . LEU A 1 60  ? -6.791  0.948   2.245   1.00   11.76  ? 60  LEU A C   1 
ATOM   541  O  O   . LEU A 1 60  ? -6.973  0.596   3.418   1.00   11.87  ? 60  LEU A O   1 
ATOM   542  C  CB  . LEU A 1 60  ? -7.083  3.411   2.381   1.00   13.61  ? 60  LEU A CB  1 
ATOM   543  C  CG  . LEU A 1 60  ? -5.572  3.580   2.345   1.00   14.68  ? 60  LEU A CG  1 
ATOM   544  C  CD1 . LEU A 1 60  ? -4.999  3.850   0.909   1.00   16.82  ? 60  LEU A CD1 1 
ATOM   545  C  CD2 . LEU A 1 60  ? -5.076  4.684   3.320   1.00   16.87  ? 60  LEU A CD2 1 
ATOM   546  N  N   . ASN A 1 61  ? -5.936  0.313   1.439   1.00   11.91  ? 61  ASN A N   1 
ATOM   547  C  CA  . ASN A 1 61  ? -4.932  -0.565  1.913   1.00   12.37  ? 61  ASN A CA  1 
ATOM   548  C  C   . ASN A 1 61  ? -3.662  0.203   2.323   1.00   12.31  ? 61  ASN A C   1 
ATOM   549  O  O   . ASN A 1 61  ? -3.072  0.779   1.454   1.00   14.55  ? 61  ASN A O   1 
ATOM   550  C  CB  . ASN A 1 61  ? -4.637  -1.651  0.850   1.00   13.76  ? 61  ASN A CB  1 
ATOM   551  C  CG  . ASN A 1 61  ? -3.559  -2.628  1.268   1.00   12.86  ? 61  ASN A CG  1 
ATOM   552  O  OD1 . ASN A 1 61  ? -2.702  -2.358  2.142   1.00   13.83  ? 61  ASN A OD1 1 
ATOM   553  N  ND2 . ASN A 1 61  ? -3.562  -3.835  0.675   1.00   14.38  ? 61  ASN A ND2 1 
ATOM   554  N  N   . ASN A 1 62  ? -3.429  0.275   3.609   1.00   12.54  ? 62  ASN A N   1 
ATOM   555  C  CA  . ASN A 1 62  ? -2.426  1.146   4.094   1.00   13.70  ? 62  ASN A CA  1 
ATOM   556  C  C   . ASN A 1 62  ? -1.155  0.361   4.318   1.00   13.89  ? 62  ASN A C   1 
ATOM   557  O  O   . ASN A 1 62  ? -0.115  0.835   4.882   1.00   17.21  ? 62  ASN A O   1 
ATOM   558  C  CB  . ASN A 1 62  ? -2.796  1.949   5.317   1.00   15.17  ? 62  ASN A CB  1 
ATOM   559  C  CG  . ASN A 1 62  ? -3.105  1.078   6.487   1.00   13.80  ? 62  ASN A CG  1 
ATOM   560  O  OD1 . ASN A 1 62  ? -2.698  -0.123  6.551   1.00   13.65  ? 62  ASN A OD1 1 
ATOM   561  N  ND2 . ASN A 1 62  ? -3.825  1.619   7.402   1.00   18.21  ? 62  ASN A ND2 1 
ATOM   562  N  N   . GLY A 1 63  ? -1.100  -0.925  3.900   1.00   13.69  ? 63  GLY A N   1 
ATOM   563  C  CA  . GLY A 1 63  ? 0.060   -1.710  4.119   1.00   14.45  ? 63  GLY A CA  1 
ATOM   564  C  C   . GLY A 1 63  ? 0.135   -2.499  5.444   1.00   14.59  ? 63  GLY A C   1 
ATOM   565  O  O   . GLY A 1 63  ? 0.973   -3.364  5.593   1.00   14.98  ? 63  GLY A O   1 
ATOM   566  N  N   . HIS A 1 64  ? -0.743  -2.230  6.367   1.00   13.19  ? 64  HIS A N   1 
ATOM   567  C  CA  . HIS A 1 64  ? -0.811  -2.949  7.662   1.00   13.34  ? 64  HIS A CA  1 
ATOM   568  C  C   . HIS A 1 64  ? -2.274  -3.535  7.817   1.00   11.91  ? 64  HIS A C   1 
ATOM   569  O  O   . HIS A 1 64  ? -2.390  -4.591  8.438   1.00   16.04  ? 64  HIS A O   1 
ATOM   570  C  CB  . HIS A 1 64  ? -0.351  -2.248  8.927   1.00   14.30  ? 64  HIS A CB  1 
ATOM   571  C  CG  . HIS A 1 64  ? -0.767  -0.836  9.114   1.00   17.87  ? 64  HIS A CG  1 
ATOM   572  N  ND1 . HIS A 1 64  ? -0.066  0.176   8.631   1.00   23.11  ? 64  HIS A ND1 1 
ATOM   573  C  CD2 . HIS A 1 64  ? -1.745  -0.284  9.919   1.00   19.27  ? 64  HIS A CD2 1 
ATOM   574  C  CE1 . HIS A 1 64  ? -0.624  1.321   9.028   1.00   25.97  ? 64  HIS A CE1 1 
ATOM   575  N  NE2 . HIS A 1 64  ? -1.624  1.038   9.821   1.00   29.55  ? 64  HIS A NE2 1 
ATOM   576  N  N   . ALA A 1 65  ? -3.267  -2.884  7.293   1.00   11.68  ? 65  ALA A N   1 
ATOM   577  C  CA  . ALA A 1 65  ? -4.642  -3.350  7.277   1.00   11.13  ? 65  ALA A CA  1 
ATOM   578  C  C   . ALA A 1 65  ? -5.336  -2.648  6.132   1.00   10.84  ? 65  ALA A C   1 
ATOM   579  O  O   . ALA A 1 65  ? -4.664  -1.978  5.312   1.00   12.84  ? 65  ALA A O   1 
ATOM   580  C  CB  . ALA A 1 65  ? -5.311  -3.154  8.661   1.00   12.69  ? 65  ALA A CB  1 
ATOM   581  N  N   . PHE A 1 66  ? -6.645  -2.702  6.093   1.00   11.38  ? 66  PHE A N   1 
ATOM   582  C  CA  . PHE A 1 66  ? -7.413  -1.783  5.263   1.00   11.75  ? 66  PHE A CA  1 
ATOM   583  C  C   . PHE A 1 66  ? -8.287  -0.926  6.135   1.00   11.19  ? 66  PHE A C   1 
ATOM   584  O  O   . PHE A 1 66  ? -8.963  -1.424  7.090   1.00   12.33  ? 66  PHE A O   1 
ATOM   585  C  CB  . PHE A 1 66  ? -8.193  -2.530  4.155   1.00   13.33  ? 66  PHE A CB  1 
ATOM   586  C  CG  . PHE A 1 66  ? -9.277  -3.456  4.665   1.00   12.59  ? 66  PHE A CG  1 
ATOM   587  C  CD1 . PHE A 1 66  ? -10.531 -2.967  5.004   1.00   13.19  ? 66  PHE A CD1 1 
ATOM   588  C  CD2 . PHE A 1 66  ? -9.004  -4.826  4.842   1.00   12.86  ? 66  PHE A CD2 1 
ATOM   589  C  CE1 . PHE A 1 66  ? -11.508 -3.831  5.522   1.00   14.56  ? 66  PHE A CE1 1 
ATOM   590  C  CE2 . PHE A 1 66  ? -9.998  -5.683  5.350   1.00   13.58  ? 66  PHE A CE2 1 
ATOM   591  C  CZ  . PHE A 1 66  ? -11.266 -5.170  5.683   1.00   13.65  ? 66  PHE A CZ  1 
ATOM   592  N  N   . ASN A 1 67  ? -8.400  0.350   5.817   1.00   11.45  ? 67  ASN A N   1 
ATOM   593  C  CA  . ASN A 1 67  ? -9.289  1.256   6.568   1.00   10.71  ? 67  ASN A CA  1 
ATOM   594  C  C   . ASN A 1 67  ? -10.499 1.668   5.744   1.00   10.24  ? 67  ASN A C   1 
ATOM   595  O  O   . ASN A 1 67  ? -10.305 2.107   4.576   1.00   12.41  ? 67  ASN A O   1 
ATOM   596  C  CB  . ASN A 1 67  ? -8.533  2.518   6.950   1.00   13.25  ? 67  ASN A CB  1 
ATOM   597  C  CG  . ASN A 1 67  ? -7.501  2.308   7.997   1.00   13.59  ? 67  ASN A CG  1 
ATOM   598  O  OD1 . ASN A 1 67  ? -7.332  1.241   8.561   1.00   15.93  ? 67  ASN A OD1 1 
ATOM   599  N  ND2 . ASN A 1 67  ? -6.777  3.348   8.294   1.00   16.50  ? 67  ASN A ND2 1 
ATOM   600  N  N   . VAL A 1 68  ? -11.680 1.587   6.301   1.00   10.80  ? 68  VAL A N   1 
ATOM   601  C  CA  . VAL A 1 68  ? -12.858 2.203   5.725   1.00   11.81  ? 68  VAL A CA  1 
ATOM   602  C  C   . VAL A 1 68  ? -12.927 3.575   6.392   1.00   11.77  ? 68  VAL A C   1 
ATOM   603  O  O   . VAL A 1 68  ? -13.063 3.669   7.638   1.00   11.58  ? 68  VAL A O   1 
ATOM   604  C  CB  . VAL A 1 68  ? -14.125 1.388   5.930   1.00   12.31  ? 68  VAL A CB  1 
ATOM   605  C  CG1 . VAL A 1 68  ? -15.387 2.189   5.498   1.00   14.07  ? 68  VAL A CG1 1 
ATOM   606  C  CG2 . VAL A 1 68  ? -13.999 0.095   5.173   1.00   13.28  ? 68  VAL A CG2 1 
ATOM   607  N  N   . GLU A 1 69  ? -12.845 4.644   5.614   1.00   12.92  ? 69  GLU A N   1 
ATOM   608  C  CA  . GLU A 1 69  ? -12.751 6.005   6.100   1.00   12.37  ? 69  GLU A CA  1 
ATOM   609  C  C   . GLU A 1 69  ? -14.115 6.705   6.020   1.00   12.65  ? 69  GLU A C   1 
ATOM   610  O  O   . GLU A 1 69  ? -14.867 6.480   5.046   1.00   14.40  ? 69  GLU A O   1 
ATOM   611  C  CB  . GLU A 1 69  ? -11.857 6.766   5.190   1.00   14.43  ? 69  GLU A CB  1 
ATOM   612  C  CG  . GLU A 1 69  ? -10.474 6.206   5.278   1.00   15.50  ? 69  GLU A CG  1 
ATOM   613  C  CD  . GLU A 1 69  ? -9.566  6.722   4.213   1.00   17.96  ? 69  GLU A CD  1 
ATOM   614  O  OE1 . GLU A 1 69  ? -10.007 7.408   3.243   1.00   20.03  ? 69  GLU A OE1 1 
ATOM   615  O  OE2 . GLU A 1 69  ? -8.320  6.429   4.241   1.00   21.74  ? 69  GLU A OE2 1 
ATOM   616  N  N   . PHE A 1 70  ? -14.343 7.587   6.988   1.00   12.63  ? 70  PHE A N   1 
ATOM   617  C  CA  . PHE A 1 70  ? -15.550 8.318   7.044   1.00   11.43  ? 70  PHE A CA  1 
ATOM   618  C  C   . PHE A 1 70  ? -15.350 9.794   6.951   1.00   12.95  ? 70  PHE A C   1 
ATOM   619  O  O   . PHE A 1 70  ? -14.282 10.309  7.323   1.00   13.47  ? 70  PHE A O   1 
ATOM   620  C  CB  . PHE A 1 70  ? -16.294 8.007   8.340   1.00   11.98  ? 70  PHE A CB  1 
ATOM   621  C  CG  . PHE A 1 70  ? -16.845 6.594   8.331   1.00   11.82  ? 70  PHE A CG  1 
ATOM   622  C  CD1 . PHE A 1 70  ? -15.983 5.501   8.577   1.00   12.66  ? 70  PHE A CD1 1 
ATOM   623  C  CD2 . PHE A 1 70  ? -18.165 6.368   8.014   1.00   11.88  ? 70  PHE A CD2 1 
ATOM   624  C  CE1 . PHE A 1 70  ? -16.466 4.236   8.464   1.00   13.63  ? 70  PHE A CE1 1 
ATOM   625  C  CE2 . PHE A 1 70  ? -18.662 5.069   7.901   1.00   13.10  ? 70  PHE A CE2 1 
ATOM   626  C  CZ  . PHE A 1 70  ? -17.820 3.998   8.135   1.00   14.10  ? 70  PHE A CZ  1 
ATOM   627  N  N   A ASP A 1 71  ? -16.463 10.499  6.680   0.50   13.42  ? 71  ASP A N   1 
ATOM   628  N  N   B ASP A 1 71  ? -16.165 10.554  6.279   0.50   13.13  ? 71  ASP A N   1 
ATOM   629  C  CA  A ASP A 1 71  ? -16.523 11.961  6.724   0.50   15.00  ? 71  ASP A CA  1 
ATOM   630  C  CA  B ASP A 1 71  ? -16.068 12.017  6.361   0.50   12.77  ? 71  ASP A CA  1 
ATOM   631  C  C   A ASP A 1 71  ? -16.649 12.294  8.158   0.50   13.48  ? 71  ASP A C   1 
ATOM   632  C  C   B ASP A 1 71  ? -16.544 12.406  7.764   0.50   13.59  ? 71  ASP A C   1 
ATOM   633  O  O   A ASP A 1 71  ? -17.617 12.053  8.855   0.50   16.97  ? 71  ASP A O   1 
ATOM   634  O  O   B ASP A 1 71  ? -17.715 12.262  8.043   0.50   14.06  ? 71  ASP A O   1 
ATOM   635  C  CB  A ASP A 1 71  ? -17.731 12.540  6.023   0.50   16.38  ? 71  ASP A CB  1 
ATOM   636  C  CB  B ASP A 1 71  ? -17.064 12.472  5.306   0.50   13.48  ? 71  ASP A CB  1 
ATOM   637  C  CG  A ASP A 1 71  ? -17.793 14.061  6.141   0.50   17.17  ? 71  ASP A CG  1 
ATOM   638  C  CG  B ASP A 1 71  ? -17.211 13.947  5.200   0.50   17.15  ? 71  ASP A CG  1 
ATOM   639  O  OD1 A ASP A 1 71  ? -16.884 14.685  6.728   0.50   19.96  ? 71  ASP A OD1 1 
ATOM   640  O  OD1 B ASP A 1 71  ? -16.597 14.615  6.025   0.50   17.75  ? 71  ASP A OD1 1 
ATOM   641  O  OD2 A ASP A 1 71  ? -18.731 14.687  5.666   0.50   22.50  ? 71  ASP A OD2 1 
ATOM   642  O  OD2 B ASP A 1 71  ? -17.865 14.393  4.216   0.50   26.02  ? 71  ASP A OD2 1 
ATOM   643  N  N   . ASP A 1 72  ? -15.591 12.861  8.610   1.00   14.42  ? 72  ASP A N   1 
ATOM   644  C  CA  . ASP A 1 72  ? -15.735 13.301  9.996   1.00   15.45  ? 72  ASP A CA  1 
ATOM   645  C  C   . ASP A 1 72  ? -15.680 14.801  10.104  1.00   18.09  ? 72  ASP A C   1 
ATOM   646  O  O   . ASP A 1 72  ? -15.334 15.335  11.155  1.00   19.25  ? 72  ASP A O   1 
ATOM   647  C  CB  . ASP A 1 72  ? -14.677 12.642  10.881  1.00   14.96  ? 72  ASP A CB  1 
ATOM   648  C  CG  . ASP A 1 72  ? -13.321 13.114  10.567  1.00   16.27  ? 72  ASP A CG  1 
ATOM   649  O  OD1 . ASP A 1 72  ? -13.119 13.791  9.484   1.00   19.20  ? 72  ASP A OD1 1 
ATOM   650  O  OD2 . ASP A 1 72  ? -12.397 12.921  11.378  1.00   17.22  ? 72  ASP A OD2 1 
ATOM   651  N  N   . SER A 1 73  ? -16.117 15.539  9.082   1.00   18.51  ? 73  SER A N   1 
ATOM   652  C  CA  . SER A 1 73  ? -16.095 17.050  9.129   1.00   20.48  ? 73  SER A CA  1 
ATOM   653  C  C   . SER A 1 73  ? -17.465 17.602  9.685   1.00   18.85  ? 73  SER A C   1 
ATOM   654  O  O   . SER A 1 73  ? -17.534 18.804  9.880   1.00   18.84  ? 73  SER A O   1 
ATOM   655  C  CB  . SER A 1 73  ? -15.736 17.527  7.753   1.00   25.74  ? 73  SER A CB  1 
ATOM   656  O  OG  . SER A 1 73  ? -16.880 17.330  6.984   1.00   23.38  ? 73  SER A OG  1 
ATOM   657  N  N   . GLN A 1 74  ? -18.451 16.742  9.966   1.00   21.06  ? 74  GLN A N   1 
ATOM   658  C  CA  . GLN A 1 74  ? -19.769 17.195  10.543  1.00   20.02  ? 74  GLN A CA  1 
ATOM   659  C  C   . GLN A 1 74  ? -19.989 16.239  11.759  1.00   20.00  ? 74  GLN A C   1 
ATOM   660  O  O   . GLN A 1 74  ? -19.385 15.112  11.837  1.00   16.82  ? 74  GLN A O   1 
ATOM   661  C  CB  . GLN A 1 74  ? -20.948 17.222  9.542   1.00   21.45  ? 74  GLN A CB  1 
ATOM   662  C  CG  . GLN A 1 74  ? -20.812 18.155  8.348   1.00   27.52  ? 74  GLN A CG  1 
ATOM   663  C  CD  . GLN A 1 74  ? -22.038 18.146  7.490   1.00   27.29  ? 74  GLN A CD  1 
ATOM   664  O  OE1 . GLN A 1 74  ? -23.146 18.317  7.983   1.00   52.11  ? 74  GLN A OE1 1 
ATOM   665  N  NE2 . GLN A 1 74  ? -21.839 17.995  6.187   1.00   48.78  ? 74  GLN A NE2 1 
ATOM   666  N  N   A ASP A 1 75  ? -20.901 16.657  12.587  0.50   28.91  ? 75  ASP A N   1 
ATOM   667  N  N   B ASP A 1 75  ? -21.027 16.674  12.487  0.50   16.32  ? 75  ASP A N   1 
ATOM   668  C  CA  A ASP A 1 75  ? -21.250 15.831  13.648  0.50   23.24  ? 75  ASP A CA  1 
ATOM   669  C  CA  B ASP A 1 75  ? -21.422 15.975  13.629  0.50   13.12  ? 75  ASP A CA  1 
ATOM   670  C  C   A ASP A 1 75  ? -22.230 14.738  13.229  0.50   25.56  ? 75  ASP A C   1 
ATOM   671  C  C   B ASP A 1 75  ? -22.292 14.799  13.165  0.50   18.92  ? 75  ASP A C   1 
ATOM   672  O  O   A ASP A 1 75  ? -23.424 14.959  13.172  0.50   36.39  ? 75  ASP A O   1 
ATOM   673  O  O   B ASP A 1 75  ? -23.531 14.950  13.082  0.50   18.57  ? 75  ASP A O   1 
ATOM   674  C  CB  A ASP A 1 75  ? -21.797 16.624  14.758  0.50   30.49  ? 75  ASP A CB  1 
ATOM   675  C  CB  B ASP A 1 75  ? -22.119 16.982  14.587  0.50   15.67  ? 75  ASP A CB  1 
ATOM   676  C  CG  A ASP A 1 75  ? -21.515 15.944  15.979  0.50   30.04  ? 75  ASP A CG  1 
ATOM   677  C  CG  B ASP A 1 75  ? -22.720 16.323  15.822  0.50   19.17  ? 75  ASP A CG  1 
ATOM   678  O  OD1 A ASP A 1 75  ? -22.397 15.243  16.349  0.50   17.31  ? 75  ASP A OD1 1 
ATOM   679  O  OD1 B ASP A 1 75  ? -22.367 15.156  16.134  0.50   18.94  ? 75  ASP A OD1 1 
ATOM   680  O  OD2 A ASP A 1 75  ? -20.352 15.909  16.429  0.50   32.77  ? 75  ASP A OD2 1 
ATOM   681  O  OD2 B ASP A 1 75  ? -23.526 17.005  16.497  0.50   27.10  ? 75  ASP A OD2 1 
ATOM   682  N  N   . LYS A 1 76  ? -21.687 13.609  12.893  1.00   19.47  ? 76  LYS A N   1 
ATOM   683  C  CA  . LYS A 1 76  ? -22.466 12.487  12.345  1.00   22.43  ? 76  LYS A CA  1 
ATOM   684  C  C   . LYS A 1 76  ? -22.524 11.178  13.169  1.00   41.94  ? 76  LYS A C   1 
ATOM   685  O  O   . LYS A 1 76  ? -23.507 10.928  13.869  1.00   61.78  ? 76  LYS A O   1 
ATOM   686  C  CB  . LYS A 1 76  ? -22.024 12.189  10.899  1.00   21.67  ? 76  LYS A CB  1 
ATOM   687  C  CG  . LYS A 1 76  ? -22.325 13.311  9.912   1.00   34.42  ? 76  LYS A CG  1 
ATOM   688  C  CD  . LYS A 1 76  ? -21.968 12.931  8.482   1.00   38.90  ? 76  LYS A CD  1 
ATOM   689  C  CE  . LYS A 1 76  ? -22.517 13.954  7.496   0.0000 44.79  ? 76  LYS A CE  1 
ATOM   690  N  NZ  . LYS A 1 76  ? -22.237 13.606  6.075   0.0000 46.12  ? 76  LYS A NZ  1 
ATOM   691  N  N   . ALA A 1 77  ? -21.497 10.357  13.014  1.00   27.62  ? 77  ALA A N   1 
ATOM   692  C  CA  . ALA A 1 77  ? -21.460 9.025   13.582  1.00   15.92  ? 77  ALA A CA  1 
ATOM   693  C  C   . ALA A 1 77  ? -20.726 9.221   14.801  1.00   14.75  ? 77  ALA A C   1 
ATOM   694  O  O   . ALA A 1 77  ? -19.550 9.463   14.785  1.00   21.41  ? 77  ALA A O   1 
ATOM   695  C  CB  . ALA A 1 77  ? -20.688 8.108   12.645  1.00   17.98  ? 77  ALA A CB  1 
ATOM   696  N  N   A VAL A 1 78  ? -21.360 9.159   15.909  0.50   14.26  ? 78  VAL A N   1 
ATOM   697  N  N   B VAL A 1 78  ? -21.472 9.136   15.912  0.50   14.30  ? 78  VAL A N   1 
ATOM   698  C  CA  A VAL A 1 78  ? -20.559 9.442   17.059  0.50   13.88  ? 78  VAL A CA  1 
ATOM   699  C  CA  B VAL A 1 78  ? -21.043 9.537   17.327  0.50   11.90  ? 78  VAL A CA  1 
ATOM   700  C  C   A VAL A 1 78  ? -20.845 8.278   18.009  0.50   12.60  ? 78  VAL A C   1 
ATOM   701  C  C   B VAL A 1 78  ? -21.116 8.411   18.343  0.50   10.95  ? 78  VAL A C   1 
ATOM   702  O  O   A VAL A 1 78  ? -21.848 7.555   17.928  0.50   12.03  ? 78  VAL A O   1 
ATOM   703  O  O   B VAL A 1 78  ? -22.160 7.758   18.508  0.50   11.63  ? 78  VAL A O   1 
ATOM   704  C  CB  A VAL A 1 78  ? -20.933 10.814  17.662  0.50   14.41  ? 78  VAL A CB  1 
ATOM   705  C  CB  B VAL A 1 78  ? -21.863 10.695  17.903  0.50   14.14  ? 78  VAL A CB  1 
ATOM   706  C  CG1 A VAL A 1 78  ? -20.673 11.950  16.698  0.50   15.16  ? 78  VAL A CG1 1 
ATOM   707  C  CG1 B VAL A 1 78  ? -21.567 10.982  19.408  0.50   15.70  ? 78  VAL A CG1 1 
ATOM   708  C  CG2 A VAL A 1 78  ? -22.410 10.775  18.099  0.50   21.63  ? 78  VAL A CG2 1 
ATOM   709  C  CG2 B VAL A 1 78  ? -21.581 11.965  17.108  0.50   16.23  ? 78  VAL A CG2 1 
ATOM   710  N  N   . LEU A 1 79  ? -19.976 8.215   19.007  1.00   11.84  ? 79  LEU A N   1 
ATOM   711  C  CA  . LEU A 1 79  ? -19.984 7.329   20.160  1.00   12.17  ? 79  LEU A CA  1 
ATOM   712  C  C   . LEU A 1 79  ? -19.945 8.189   21.409  1.00   12.94  ? 79  LEU A C   1 
ATOM   713  O  O   . LEU A 1 79  ? -19.146 9.128   21.512  1.00   13.56  ? 79  LEU A O   1 
ATOM   714  C  CB  . LEU A 1 79  ? -18.699 6.428   20.073  1.00   12.92  ? 79  LEU A CB  1 
ATOM   715  C  CG  . LEU A 1 79  ? -18.570 5.411   21.117  1.00   13.45  ? 79  LEU A CG  1 
ATOM   716  C  CD1 . LEU A 1 79  ? -19.630 4.324   20.924  1.00   19.15  ? 79  LEU A CD1 1 
ATOM   717  C  CD2 . LEU A 1 79  ? -17.181 4.733   21.024  1.00   13.96  ? 79  LEU A CD2 1 
ATOM   718  N  N   . LYS A 1 80  ? -20.818 7.850   22.361  1.00   13.30  ? 80  LYS A N   1 
ATOM   719  C  CA  . LYS A 1 80  ? -20.875 8.570   23.621  1.00   13.79  ? 80  LYS A CA  1 
ATOM   720  C  C   . LYS A 1 80  ? -21.382 7.631   24.690  1.00   13.12  ? 80  LYS A C   1 
ATOM   721  O  O   . LYS A 1 80  ? -21.654 6.450   24.400  1.00   13.86  ? 80  LYS A O   1 
ATOM   722  C  CB  . LYS A 1 80  ? -21.585 9.892   23.581  1.00   17.88  ? 80  LYS A CB  1 
ATOM   723  C  CG  . LYS A 1 80  ? -22.981 9.672   23.343  1.00   18.61  ? 80  LYS A CG  1 
ATOM   724  C  CD  . LYS A 1 80  ? -23.728 10.996  23.262  1.00   24.08  ? 80  LYS A CD  1 
ATOM   725  C  CE  . LYS A 1 80  ? -23.341 11.806  22.108  1.00   32.17  ? 80  LYS A CE  1 
ATOM   726  N  NZ  . LYS A 1 80  ? -21.986 11.281  21.906  1.00   38.67  ? 80  LYS A NZ  1 
ATOM   727  N  N   . GLY A 1 81  ? -21.477 8.119   25.928  1.00   14.98  ? 81  GLY A N   1 
ATOM   728  C  CA  . GLY A 1 81  ? -21.962 7.275   27.011  1.00   16.08  ? 81  GLY A CA  1 
ATOM   729  C  C   . GLY A 1 81  ? -20.935 6.246   27.313  1.00   15.76  ? 81  GLY A C   1 
ATOM   730  O  O   . GLY A 1 81  ? -19.732 6.459   27.118  1.00   14.33  ? 81  GLY A O   1 
ATOM   731  N  N   . GLY A 1 82  ? -21.380 5.120   27.840  1.00   19.89  ? 82  GLY A N   1 
ATOM   732  C  CA  . GLY A 1 82  ? -20.441 4.121   28.256  1.00   22.33  ? 82  GLY A CA  1 
ATOM   733  C  C   . GLY A 1 82  ? -19.602 4.769   29.351  1.00   18.63  ? 82  GLY A C   1 
ATOM   734  O  O   . GLY A 1 82  ? -20.023 5.481   30.272  1.00   26.07  ? 82  GLY A O   1 
ATOM   735  N  N   . PRO A 1 83  ? -18.234 4.574   29.199  1.00   15.70  ? 83  PRO A N   1 
ATOM   736  C  CA  . PRO A 1 83  ? -17.336 5.148   30.130  1.00   15.81  ? 83  PRO A CA  1 
ATOM   737  C  C   . PRO A 1 83  ? -16.919 6.570   29.742  1.00   14.50  ? 83  PRO A C   1 
ATOM   738  O  O   . PRO A 1 83  ? -16.111 7.143   30.436  1.00   18.50  ? 83  PRO A O   1 
ATOM   739  C  CB  . PRO A 1 83  ? -16.023 4.299   29.963  1.00   15.99  ? 83  PRO A CB  1 
ATOM   740  C  CG  . PRO A 1 83  ? -16.057 3.960   28.507  1.00   14.56  ? 83  PRO A CG  1 
ATOM   741  C  CD  . PRO A 1 83  ? -17.543 3.740   28.224  1.00   14.72  ? 83  PRO A CD  1 
ATOM   742  N  N   . LEU A 1 84  ? -17.383 7.094   28.629  1.00   13.22  ? 84  LEU A N   1 
ATOM   743  C  CA  . LEU A 1 84  ? -16.889 8.291   28.037  1.00   12.39  ? 84  LEU A CA  1 
ATOM   744  C  C   . LEU A 1 84  ? -17.520 9.551   28.624  1.00   14.91  ? 84  LEU A C   1 
ATOM   745  O  O   . LEU A 1 84  ? -18.717 9.595   28.882  1.00   16.68  ? 84  LEU A O   1 
ATOM   746  C  CB  . LEU A 1 84  ? -17.145 8.265   26.557  1.00   12.06  ? 84  LEU A CB  1 
ATOM   747  C  CG  . LEU A 1 84  ? -16.566 7.038   25.832  1.00   11.18  ? 84  LEU A CG  1 
ATOM   748  C  CD1 . LEU A 1 84  ? -17.069 6.999   24.411  1.00   12.74  ? 84  LEU A CD1 1 
ATOM   749  C  CD2 . LEU A 1 84  ? -15.031 7.020   25.899  1.00   12.06  ? 84  LEU A CD2 1 
ATOM   750  N  N   . ASP A 1 85  ? -16.748 10.609  28.632  1.00   15.97  ? 85  ASP A N   1 
ATOM   751  C  CA  . ASP A 1 85  ? -17.254 11.986  28.923  1.00   18.86  ? 85  ASP A CA  1 
ATOM   752  C  C   . ASP A 1 85  ? -17.244 12.644  27.547  1.00   20.04  ? 85  ASP A C   1 
ATOM   753  O  O   . ASP A 1 85  ? -16.202 12.643  26.794  1.00   23.98  ? 85  ASP A O   1 
ATOM   754  C  CB  . ASP A 1 85  ? -16.234 12.645  29.859  1.00   22.51  ? 85  ASP A CB  1 
ATOM   755  C  CG  . ASP A 1 85  ? -16.315 12.137  31.312  1.00   28.59  ? 85  ASP A CG  1 
ATOM   756  O  OD1 . ASP A 1 85  ? -17.387 11.518  31.744  1.00   38.86  ? 85  ASP A OD1 1 
ATOM   757  O  OD2 . ASP A 1 85  ? -15.321 12.454  32.060  1.00   50.27  ? 85  ASP A OD2 1 
ATOM   758  N  N   . GLY A 1 86  ? -18.287 13.294  27.158  1.00   23.74  ? 86  GLY A N   1 
ATOM   759  C  CA  . GLY A 1 86  ? -18.206 13.889  25.892  1.00   24.28  ? 86  GLY A CA  1 
ATOM   760  C  C   . GLY A 1 86  ? -18.470 12.965  24.677  1.00   22.91  ? 86  GLY A C   1 
ATOM   761  O  O   . GLY A 1 86  ? -18.954 11.798  24.768  1.00   27.52  ? 86  GLY A O   1 
ATOM   762  N  N   A THR A 1 87  ? -18.114 13.551  23.513  0.50   18.25  ? 87  THR A N   1 
ATOM   763  N  N   B THR A 1 87  ? -18.257 13.501  23.493  0.50   13.71  ? 87  THR A N   1 
ATOM   764  C  CA  A THR A 1 87  ? -18.566 13.126  22.170  0.50   19.47  ? 87  THR A CA  1 
ATOM   765  C  CA  B THR A 1 87  ? -18.693 12.788  22.323  0.50   11.53  ? 87  THR A CA  1 
ATOM   766  C  C   A THR A 1 87  ? -17.445 12.733  21.188  0.50   15.02  ? 87  THR A C   1 
ATOM   767  C  C   B THR A 1 87  ? -17.441 12.557  21.519  0.50   9.57   ? 87  THR A C   1 
ATOM   768  O  O   A THR A 1 87  ? -16.509 13.540  20.883  0.50   13.75  ? 87  THR A O   1 
ATOM   769  O  O   B THR A 1 87  ? -16.503 13.409  21.491  0.50   9.75   ? 87  THR A O   1 
ATOM   770  C  CB  A THR A 1 87  ? -19.485 14.214  21.598  0.50   19.66  ? 87  THR A CB  1 
ATOM   771  C  CB  B THR A 1 87  ? -19.665 13.709  21.554  0.50   14.06  ? 87  THR A CB  1 
ATOM   772  O  OG1 A THR A 1 87  ? -20.758 14.123  22.297  0.50   19.09  ? 87  THR A OG1 1 
ATOM   773  O  OG1 B THR A 1 87  ? -19.999 13.221  20.238  0.50   24.69  ? 87  THR A OG1 1 
ATOM   774  C  CG2 A THR A 1 87  ? -19.649 14.101  20.035  0.50   24.23  ? 87  THR A CG2 1 
ATOM   775  C  CG2 B THR A 1 87  ? -19.017 14.977  21.412  0.50   9.98   ? 87  THR A CG2 1 
ATOM   776  N  N   . TYR A 1 88  ? -17.479 11.474  20.769  1.00   11.40  ? 88  TYR A N   1 
ATOM   777  C  CA  . TYR A 1 88  ? -16.372 10.965  19.961  1.00   10.83  ? 88  TYR A CA  1 
ATOM   778  C  C   . TYR A 1 88  ? -16.857 10.679  18.599  1.00   10.72  ? 88  TYR A C   1 
ATOM   779  O  O   . TYR A 1 88  ? -17.830 9.947   18.385  1.00   14.35  ? 88  TYR A O   1 
ATOM   780  C  CB  . TYR A 1 88  ? -15.731 9.751   20.587  1.00   10.88  ? 88  TYR A CB  1 
ATOM   781  C  CG  . TYR A 1 88  ? -14.972 9.963   21.885  1.00   10.30  ? 88  TYR A CG  1 
ATOM   782  C  CD1 . TYR A 1 88  ? -15.610 10.309  23.087  1.00   10.97  ? 88  TYR A CD1 1 
ATOM   783  C  CD2 . TYR A 1 88  ? -13.562 9.835   21.918  1.00   9.43   ? 88  TYR A CD2 1 
ATOM   784  C  CE1 . TYR A 1 88  ? -14.912 10.524  24.260  1.00   10.80  ? 88  TYR A CE1 1 
ATOM   785  C  CE2 . TYR A 1 88  ? -12.882 9.957   23.088  1.00   9.54   ? 88  TYR A CE2 1 
ATOM   786  C  CZ  . TYR A 1 88  ? -13.522 10.269  24.255  1.00   9.50   ? 88  TYR A CZ  1 
ATOM   787  O  OH  . TYR A 1 88  ? -12.822 10.392  25.419  1.00   10.40  ? 88  TYR A OH  1 
ATOM   788  N  N   . ARG A 1 89  ? -16.210 11.186  17.596  1.00   9.75   ? 89  ARG A N   1 
ATOM   789  C  CA  . ARG A 1 89  ? -16.630 11.050  16.192  1.00   10.60  ? 89  ARG A CA  1 
ATOM   790  C  C   . ARG A 1 89  ? -15.887 9.956   15.442  1.00   8.88   ? 89  ARG A C   1 
ATOM   791  O  O   . ARG A 1 89  ? -14.666 9.864   15.511  1.00   8.96   ? 89  ARG A O   1 
ATOM   792  C  CB  . ARG A 1 89  ? -16.375 12.368  15.533  1.00   13.08  ? 89  ARG A CB  1 
ATOM   793  C  CG  . ARG A 1 89  ? -17.151 12.509  14.238  1.00   14.28  ? 89  ARG A CG  1 
ATOM   794  C  CD  . ARG A 1 89  ? -16.973 13.900  13.652  1.00   15.28  ? 89  ARG A CD  1 
ATOM   795  N  NE  . ARG A 1 89  ? -17.613 14.917  14.483  1.00   15.31  ? 89  ARG A NE  1 
ATOM   796  C  CZ  . ARG A 1 89  ? -17.471 16.229  14.313  1.00   13.85  ? 89  ARG A CZ  1 
ATOM   797  N  NH1 . ARG A 1 89  ? -16.694 16.702  13.340  1.00   17.92  ? 89  ARG A NH1 1 
ATOM   798  N  NH2 . ARG A 1 89  ? -18.106 17.070  15.119  1.00   17.83  ? 89  ARG A NH2 1 
ATOM   799  N  N   . LEU A 1 90  ? -16.648 9.134   14.716  1.00   9.65   ? 90  LEU A N   1 
ATOM   800  C  CA  . LEU A 1 90  ? -16.067 8.046   13.917  1.00   9.47   ? 90  LEU A CA  1 
ATOM   801  C  C   . LEU A 1 90  ? -15.224 8.603   12.770  1.00   9.50   ? 90  LEU A C   1 
ATOM   802  O  O   . LEU A 1 90  ? -15.688 9.428   11.964  1.00   11.44  ? 90  LEU A O   1 
ATOM   803  C  CB  . LEU A 1 90  ? -17.172 7.184   13.356  1.00   9.95   ? 90  LEU A CB  1 
ATOM   804  C  CG  . LEU A 1 90  ? -16.730 6.004   12.475  1.00   11.36  ? 90  LEU A CG  1 
ATOM   805  C  CD1 . LEU A 1 90  ? -15.964 4.953   13.260  1.00   11.44  ? 90  LEU A CD1 1 
ATOM   806  C  CD2 . LEU A 1 90  ? -17.973 5.348   11.841  1.00   13.07  ? 90  LEU A CD2 1 
ATOM   807  N  N   . ILE A 1 91  ? -13.984 8.148   12.649  1.00   9.20   ? 91  ILE A N   1 
ATOM   808  C  CA  . ILE A 1 91  ? -13.098 8.496   11.558  1.00   9.14   ? 91  ILE A CA  1 
ATOM   809  C  C   . ILE A 1 91  ? -12.823 7.335   10.656  1.00   8.58   ? 91  ILE A C   1 
ATOM   810  O  O   . ILE A 1 91  ? -12.710 7.519   9.437   1.00   9.88   ? 91  ILE A O   1 
ATOM   811  C  CB  . ILE A 1 91  ? -11.830 9.189   12.054  1.00   10.29  ? 91  ILE A CB  1 
ATOM   812  C  CG1 . ILE A 1 91  ? -10.926 9.570   10.884  1.00   13.35  ? 91  ILE A CG1 1 
ATOM   813  C  CG2 . ILE A 1 91  ? -11.063 8.374   13.104  1.00   11.41  ? 91  ILE A CG2 1 
ATOM   814  C  CD1 . ILE A 1 91  ? -9.778  10.493  11.268  1.00   17.40  ? 91  ILE A CD1 1 
ATOM   815  N  N   . GLN A 1 92  ? -12.616 6.108   11.178  1.00   8.69   ? 92  GLN A N   1 
ATOM   816  C  CA  . GLN A 1 92  ? -12.293 4.956   10.338  1.00   9.21   ? 92  GLN A CA  1 
ATOM   817  C  C   . GLN A 1 92  ? -12.566 3.696   11.105  1.00   8.11   ? 92  GLN A C   1 
ATOM   818  O  O   . GLN A 1 92  ? -12.612 3.713   12.335  1.00   8.51   ? 92  GLN A O   1 
ATOM   819  C  CB  . GLN A 1 92  ? -10.848 4.982   9.838   1.00   10.27  ? 92  GLN A CB  1 
ATOM   820  C  CG  . GLN A 1 92  ? -9.778  5.086   10.954  1.00   11.08  ? 92  GLN A CG  1 
ATOM   821  C  CD  . GLN A 1 92  ? -9.085  3.779   11.259  1.00   10.31  ? 92  GLN A CD  1 
ATOM   822  O  OE1 . GLN A 1 92  ? -9.640  2.671   11.132  1.00   10.43  ? 92  GLN A OE1 1 
ATOM   823  N  NE2 . GLN A 1 92  ? -7.828  3.856   11.754  1.00   10.90  ? 92  GLN A NE2 1 
ATOM   824  N  N   . PHE A 1 93  ? -12.739 2.605   10.380  1.00   8.49   ? 93  PHE A N   1 
ATOM   825  C  CA  . PHE A 1 93  ? -12.642 1.291   10.966  1.00   8.29   ? 93  PHE A CA  1 
ATOM   826  C  C   . PHE A 1 93  ? -11.697 0.442   10.179  1.00   8.29   ? 93  PHE A C   1 
ATOM   827  O  O   . PHE A 1 93  ? -11.459 0.647   8.966   1.00   9.75   ? 93  PHE A O   1 
ATOM   828  C  CB  . PHE A 1 93  ? -13.980 0.595   11.208  1.00   8.84   ? 93  PHE A CB  1 
ATOM   829  C  CG  . PHE A 1 93  ? -14.726 0.123   9.999   1.00   9.27   ? 93  PHE A CG  1 
ATOM   830  C  CD1 . PHE A 1 93  ? -14.355 -1.033  9.318   1.00   10.50  ? 93  PHE A CD1 1 
ATOM   831  C  CD2 . PHE A 1 93  ? -15.872 0.817   9.570   1.00   10.30  ? 93  PHE A CD2 1 
ATOM   832  C  CE1 . PHE A 1 93  ? -15.068 -1.476  8.218   1.00   11.31  ? 93  PHE A CE1 1 
ATOM   833  C  CE2 . PHE A 1 93  ? -16.594 0.338   8.464   1.00   11.48  ? 93  PHE A CE2 1 
ATOM   834  C  CZ  . PHE A 1 93  ? -16.202 -0.789  7.804   1.00   11.95  ? 93  PHE A CZ  1 
ATOM   835  N  N   . HIS A 1 94  ? -11.163 -0.596  10.859  1.00   8.10   ? 94  HIS A N   1 
ATOM   836  C  CA  . HIS A 1 94  ? -10.281 -1.563  10.263  1.00   8.39   ? 94  HIS A CA  1 
ATOM   837  C  C   . HIS A 1 94  ? -10.362 -2.834  11.077  1.00   7.62   ? 94  HIS A C   1 
ATOM   838  O  O   . HIS A 1 94  ? -10.971 -2.852  12.144  1.00   8.18   ? 94  HIS A O   1 
ATOM   839  C  CB  . HIS A 1 94  ? -8.845  -1.068  10.192  1.00   8.74   ? 94  HIS A CB  1 
ATOM   840  C  CG  . HIS A 1 94  ? -8.311  -0.776  11.531  1.00   7.92   ? 94  HIS A CG  1 
ATOM   841  N  ND1 . HIS A 1 94  ? -8.497  0.410   12.186  1.00   8.60   ? 94  HIS A ND1 1 
ATOM   842  C  CD2 . HIS A 1 94  ? -7.634  -1.596  12.425  1.00   7.90   ? 94  HIS A CD2 1 
ATOM   843  C  CE1 . HIS A 1 94  ? -7.975  0.314   13.427  1.00   8.21   ? 94  HIS A CE1 1 
ATOM   844  N  NE2 . HIS A 1 94  ? -7.462  -0.916  13.603  1.00   7.53   ? 94  HIS A NE2 1 
ATOM   845  N  N   . PHE A 1 95  ? -9.686  -3.874  10.610  1.00   8.12   ? 95  PHE A N   1 
ATOM   846  C  CA  . PHE A 1 95  ? -9.623  -5.168  11.292  1.00   8.23   ? 95  PHE A CA  1 
ATOM   847  C  C   . PHE A 1 95  ? -8.188  -5.601  11.500  1.00   7.97   ? 95  PHE A C   1 
ATOM   848  O  O   . PHE A 1 95  ? -7.287  -5.138  10.795  1.00   9.02   ? 95  PHE A O   1 
ATOM   849  C  CB  . PHE A 1 95  ? -10.368 -6.252  10.447  1.00   8.64   ? 95  PHE A CB  1 
ATOM   850  C  CG  . PHE A 1 95  ? -11.782 -5.985  10.139  1.00   8.74   ? 95  PHE A CG  1 
ATOM   851  C  CD1 . PHE A 1 95  ? -12.110 -5.132  9.059   1.00   10.02  ? 95  PHE A CD1 1 
ATOM   852  C  CD2 . PHE A 1 95  ? -12.810 -6.580  10.828  1.00   9.44   ? 95  PHE A CD2 1 
ATOM   853  C  CE1 . PHE A 1 95  ? -13.439 -4.913  8.727   1.00   10.65  ? 95  PHE A CE1 1 
ATOM   854  C  CE2 . PHE A 1 95  ? -14.154 -6.388  10.462  1.00   10.45  ? 95  PHE A CE2 1 
ATOM   855  C  CZ  . PHE A 1 95  ? -14.459 -5.550  9.423   1.00   10.57  ? 95  PHE A CZ  1 
ATOM   856  N  N   . HIS A 1 96  ? -8.016  -6.549  12.392  1.00   7.62   ? 96  HIS A N   1 
ATOM   857  C  CA  . HIS A 1 96  ? -6.826  -7.363  12.557  1.00   7.90   ? 96  HIS A CA  1 
ATOM   858  C  C   . HIS A 1 96  ? -7.230  -8.788  12.434  1.00   7.98   ? 96  HIS A C   1 
ATOM   859  O  O   . HIS A 1 96  ? -8.316  -9.147  12.960  1.00   8.34   ? 96  HIS A O   1 
ATOM   860  C  CB  . HIS A 1 96  ? -6.163  -7.094  13.930  1.00   8.51   ? 96  HIS A CB  1 
ATOM   861  C  CG  . HIS A 1 96  ? -5.871  -5.666  14.174  1.00   7.49   ? 96  HIS A CG  1 
ATOM   862  N  ND1 . HIS A 1 96  ? -4.641  -5.086  13.978  1.00   9.05   ? 96  HIS A ND1 1 
ATOM   863  C  CD2 . HIS A 1 96  ? -6.653  -4.643  14.606  1.00   7.55   ? 96  HIS A CD2 1 
ATOM   864  C  CE1 . HIS A 1 96  ? -4.711  -3.795  14.286  1.00   8.71   ? 96  HIS A CE1 1 
ATOM   865  N  NE2 . HIS A 1 96  ? -5.939  -3.480  14.644  1.00   7.69   ? 96  HIS A NE2 1 
ATOM   866  N  N   . TRP A 1 97  ? -6.453  -9.648  11.808  1.00   7.67   ? 97  TRP A N   1 
ATOM   867  C  CA  . TRP A 1 97  ? -6.859  -11.019 11.598  1.00   8.73   ? 97  TRP A CA  1 
ATOM   868  C  C   . TRP A 1 97  ? -5.670  -11.926 11.466  1.00   8.09   ? 97  TRP A C   1 
ATOM   869  O  O   . TRP A 1 97  ? -4.507  -11.509 11.373  1.00   8.77   ? 97  TRP A O   1 
ATOM   870  C  CB  . TRP A 1 97  ? -7.777  -11.130 10.339  1.00   8.95   ? 97  TRP A CB  1 
ATOM   871  C  CG  . TRP A 1 97  ? -7.121  -10.741 9.065   1.00   8.82   ? 97  TRP A CG  1 
ATOM   872  C  CD1 . TRP A 1 97  ? -6.443  -11.571 8.219   1.00   10.22  ? 97  TRP A CD1 1 
ATOM   873  C  CD2 . TRP A 1 97  ? -7.081  -9.446  8.483   1.00   9.62   ? 97  TRP A CD2 1 
ATOM   874  N  NE1 . TRP A 1 97  ? -5.999  -10.837 7.119   1.00   10.58  ? 97  TRP A NE1 1 
ATOM   875  C  CE2 . TRP A 1 97  ? -6.323  -9.531  7.277   1.00   10.00  ? 97  TRP A CE2 1 
ATOM   876  C  CE3 . TRP A 1 97  ? -7.549  -8.160  8.889   1.00   9.27   ? 97  TRP A CE3 1 
ATOM   877  C  CZ2 . TRP A 1 97  ? -6.183  -8.425  6.439   1.00   10.87  ? 97  TRP A CZ2 1 
ATOM   878  C  CZ3 . TRP A 1 97  ? -7.348  -7.073  8.085   1.00   9.72   ? 97  TRP A CZ3 1 
ATOM   879  C  CH2 . TRP A 1 97  ? -6.644  -7.192  6.853   1.00   10.60  ? 97  TRP A CH2 1 
ATOM   880  N  N   . GLY A 1 98  ? -5.954  -13.244 11.470  1.00   8.78   ? 98  GLY A N   1 
ATOM   881  C  CA  . GLY A 1 98  ? -4.948  -14.235 11.496  1.00   9.26   ? 98  GLY A CA  1 
ATOM   882  C  C   . GLY A 1 98  ? -4.714  -14.920 10.176  1.00   10.03  ? 98  GLY A C   1 
ATOM   883  O  O   . GLY A 1 98  ? -5.455  -14.786 9.211   1.00   10.87  ? 98  GLY A O   1 
ATOM   884  N  N   . SER A 1 99  ? -3.681  -15.798 10.199  1.00   11.06  ? 99  SER A N   1 
ATOM   885  C  CA  . SER A 1 99  ? -3.473  -16.737 9.075   1.00   11.71  ? 99  SER A CA  1 
ATOM   886  C  C   . SER A 1 99  ? -4.366  -17.966 9.169   1.00   13.51  ? 99  SER A C   1 
ATOM   887  O  O   . SER A 1 99  ? -4.472  -18.662 8.153   1.00   15.11  ? 99  SER A O   1 
ATOM   888  C  CB  . SER A 1 99  ? -2.035  -17.138 9.052   1.00   13.92  ? 99  SER A CB  1 
ATOM   889  O  OG  . SER A 1 99  ? -1.576  -17.620 10.288  1.00   13.55  ? 99  SER A OG  1 
ATOM   890  N  N   . LEU A 1 100 ? -4.953  -18.207 10.338  1.00   12.36  ? 100 LEU A N   1 
ATOM   891  C  CA  . LEU A 1 100 ? -5.752  -19.354 10.660  1.00   13.98  ? 100 LEU A CA  1 
ATOM   892  C  C   . LEU A 1 100 ? -6.881  -18.877 11.505  1.00   12.07  ? 100 LEU A C   1 
ATOM   893  O  O   . LEU A 1 100 ? -6.720  -17.870 12.221  1.00   12.26  ? 100 LEU A O   1 
ATOM   894  C  CB  . LEU A 1 100 ? -4.958  -20.365 11.549  1.00   22.34  ? 100 LEU A CB  1 
ATOM   895  C  CG  . LEU A 1 100 ? -3.601  -20.709 10.984  1.00   22.13  ? 100 LEU A CG  1 
ATOM   896  C  CD1 . LEU A 1 100 ? -2.486  -21.097 11.939  1.00   31.92  ? 100 LEU A CD1 1 
ATOM   897  C  CD2 . LEU A 1 100 ? -3.913  -21.813 9.986   1.00   33.63  ? 100 LEU A CD2 1 
ATOM   898  N  N   . ASP A 1 101 ? -7.999  -19.619 11.553  1.00   12.99  ? 101 ASP A N   1 
ATOM   899  C  CA  . ASP A 1 101 ? -9.126  -19.167 12.326  1.00   11.53  ? 101 ASP A CA  1 
ATOM   900  C  C   . ASP A 1 101 ? -8.856  -19.077 13.813  1.00   11.89  ? 101 ASP A C   1 
ATOM   901  O  O   . ASP A 1 101 ? -9.537  -18.350 14.516  1.00   14.34  ? 101 ASP A O   1 
ATOM   902  C  CB  . ASP A 1 101 ? -10.361 -20.013 12.135  1.00   14.33  ? 101 ASP A CB  1 
ATOM   903  C  CG  . ASP A 1 101 ? -10.843 -20.115 10.693  1.00   15.42  ? 101 ASP A CG  1 
ATOM   904  O  OD1 . ASP A 1 101 ? -10.544 -19.243 9.849   1.00   15.56  ? 101 ASP A OD1 1 
ATOM   905  O  OD2 . ASP A 1 101 ? -11.710 -20.957 10.474  1.00   19.93  ? 101 ASP A OD2 1 
ATOM   906  N  N   . GLY A 1 102 ? -7.875  -19.851 14.273  1.00   12.90  ? 102 GLY A N   1 
ATOM   907  C  CA  . GLY A 1 102 ? -7.562  -19.853 15.702  1.00   13.51  ? 102 GLY A CA  1 
ATOM   908  C  C   . GLY A 1 102 ? -6.743  -18.682 16.280  1.00   11.99  ? 102 GLY A C   1 
ATOM   909  O  O   . GLY A 1 102 ? -6.391  -18.690 17.468  1.00   13.32  ? 102 GLY A O   1 
ATOM   910  N  N   . GLN A 1 103 ? -6.466  -17.660 15.490  1.00   10.86  ? 103 GLN A N   1 
ATOM   911  C  CA  . GLN A 1 103 ? -5.767  -16.520 15.966  1.00   9.96   ? 103 GLN A CA  1 
ATOM   912  C  C   . GLN A 1 103 ? -6.155  -15.337 15.089  1.00   9.06   ? 103 GLN A C   1 
ATOM   913  O  O   . GLN A 1 103 ? -6.693  -15.528 14.004  1.00   10.29  ? 103 GLN A O   1 
ATOM   914  C  CB  . GLN A 1 103 ? -4.251  -16.695 15.993  1.00   11.94  ? 103 GLN A CB  1 
ATOM   915  C  CG  . GLN A 1 103 ? -3.678  -16.917 14.617  1.00   13.03  ? 103 GLN A CG  1 
ATOM   916  C  CD  . GLN A 1 103 ? -2.274  -17.493 14.681  1.00   15.49  ? 103 GLN A CD  1 
ATOM   917  O  OE1 . GLN A 1 103 ? -2.051  -18.416 15.461  1.00   26.22  ? 103 GLN A OE1 1 
ATOM   918  N  NE2 . GLN A 1 103 ? -1.387  -17.050 13.913  1.00   14.69  ? 103 GLN A NE2 1 
ATOM   919  N  N   . GLY A 1 104 ? -5.861  -14.129 15.563  1.00   8.47   ? 104 GLY A N   1 
ATOM   920  C  CA  . GLY A 1 104 ? -6.139  -12.940 14.777  1.00   8.80   ? 104 GLY A CA  1 
ATOM   921  C  C   . GLY A 1 104 ? -6.544  -11.753 15.607  1.00   8.22   ? 104 GLY A C   1 
ATOM   922  O  O   . GLY A 1 104 ? -6.291  -10.619 15.237  1.00   9.12   ? 104 GLY A O   1 
ATOM   923  N  N   . SER A 1 105 ? -7.279  -11.995 16.736  1.00   8.29   ? 105 SER A N   1 
ATOM   924  C  CA  . SER A 1 105 ? -7.651  -10.893 17.568  1.00   7.87   ? 105 SER A CA  1 
ATOM   925  C  C   . SER A 1 105 ? -6.447  -10.308 18.302  1.00   7.67   ? 105 SER A C   1 
ATOM   926  O  O   . SER A 1 105 ? -5.429  -10.990 18.531  1.00   8.92   ? 105 SER A O   1 
ATOM   927  C  CB  . SER A 1 105 ? -8.778  -11.220 18.515  1.00   8.22   ? 105 SER A CB  1 
ATOM   928  O  OG  . SER A 1 105 ? -8.439  -12.191 19.489  1.00   8.51   ? 105 SER A OG  1 
ATOM   929  N  N   . GLU A 1 106 ? -6.574  -9.067  18.705  1.00   7.72   ? 106 GLU A N   1 
ATOM   930  C  CA  . GLU A 1 106 ? -5.574  -8.349  19.505  1.00   7.82   ? 106 GLU A CA  1 
ATOM   931  C  C   . GLU A 1 106 ? -5.922  -8.536  20.980  1.00   7.76   ? 106 GLU A C   1 
ATOM   932  O  O   . GLU A 1 106 ? -5.101  -9.111  21.759  1.00   8.45   ? 106 GLU A O   1 
ATOM   933  C  CB  . GLU A 1 106 ? -5.513  -6.898  19.069  1.00   8.13   ? 106 GLU A CB  1 
ATOM   934  C  CG  . GLU A 1 106 ? -5.102  -6.763  17.634  1.00   9.63   ? 106 GLU A CG  1 
ATOM   935  C  CD  . GLU A 1 106 ? -4.380  -5.510  17.361  1.00   8.56   ? 106 GLU A CD  1 
ATOM   936  O  OE1 . GLU A 1 106 ? -4.949  -4.412  17.603  1.00   8.55   ? 106 GLU A OE1 1 
ATOM   937  O  OE2 . GLU A 1 106 ? -3.200  -5.556  16.887  1.00   9.83   ? 106 GLU A OE2 1 
ATOM   938  N  N   . HIS A 1 107 ? -7.081  -8.085  21.430  1.00   7.30   ? 107 HIS A N   1 
ATOM   939  C  CA  . HIS A 1 107 ? -7.539  -8.471  22.717  1.00   7.32   ? 107 HIS A CA  1 
ATOM   940  C  C   . HIS A 1 107 ? -7.813  -9.977  22.732  1.00   7.32   ? 107 HIS A C   1 
ATOM   941  O  O   . HIS A 1 107 ? -8.169  -10.588 21.734  1.00   7.95   ? 107 HIS A O   1 
ATOM   942  C  CB  . HIS A 1 107 ? -8.770  -7.669  23.125  1.00   8.04   ? 107 HIS A CB  1 
ATOM   943  C  CG  . HIS A 1 107 ? -8.469  -6.228  23.279  1.00   7.45   ? 107 HIS A CG  1 
ATOM   944  N  ND1 . HIS A 1 107 ? -8.521  -5.322  22.233  1.00   8.07   ? 107 HIS A ND1 1 
ATOM   945  C  CD2 . HIS A 1 107 ? -7.996  -5.522  24.341  1.00   7.50   ? 107 HIS A CD2 1 
ATOM   946  C  CE1 . HIS A 1 107 ? -8.084  -4.148  22.680  1.00   8.32   ? 107 HIS A CE1 1 
ATOM   947  N  NE2 . HIS A 1 107 ? -7.763  -4.218  23.951  1.00   7.94   ? 107 HIS A NE2 1 
ATOM   948  N  N   . THR A 1 108 ? -7.698  -10.539 23.941  1.00   8.43   ? 108 THR A N   1 
ATOM   949  C  CA  . THR A 1 108 ? -8.052  -11.916 24.215  1.00   8.44   ? 108 THR A CA  1 
ATOM   950  C  C   . THR A 1 108 ? -8.989  -11.934 25.406  1.00   7.92   ? 108 THR A C   1 
ATOM   951  O  O   . THR A 1 108 ? -9.010  -10.961 26.195  1.00   8.74   ? 108 THR A O   1 
ATOM   952  C  CB  . THR A 1 108 ? -6.824  -12.807 24.399  1.00   9.21   ? 108 THR A CB  1 
ATOM   953  O  OG1 . THR A 1 108 ? -5.987  -12.342 25.430  1.00   10.01  ? 108 THR A OG1 1 
ATOM   954  C  CG2 . THR A 1 108 ? -6.019  -12.873 23.114  1.00   10.36  ? 108 THR A CG2 1 
ATOM   955  N  N   . VAL A 1 109 ? -9.773  -12.997 25.562  1.00   8.75   ? 109 VAL A N   1 
ATOM   956  C  CA  . VAL A 1 109 ? -10.757 -13.095 26.630  1.00   9.15   ? 109 VAL A CA  1 
ATOM   957  C  C   . VAL A 1 109 ? -10.442 -14.374 27.390  1.00   9.31   ? 109 VAL A C   1 
ATOM   958  O  O   . VAL A 1 109 ? -10.589 -15.487 26.833  1.00   9.75   ? 109 VAL A O   1 
ATOM   959  C  CB  . VAL A 1 109 ? -12.176 -13.090 26.070  1.00   9.90   ? 109 VAL A CB  1 
ATOM   960  C  CG1 . VAL A 1 109 ? -13.198 -13.226 27.230  1.00   11.28  ? 109 VAL A CG1 1 
ATOM   961  C  CG2 . VAL A 1 109 ? -12.460 -11.843 25.277  1.00   10.78  ? 109 VAL A CG2 1 
ATOM   962  N  N   . ASP A 1 110 ? -9.911  -14.251 28.606  1.00   10.34  ? 110 ASP A N   1 
ATOM   963  C  CA  . ASP A 1 110 ? -9.437  -15.486 29.299  1.00   11.44  ? 110 ASP A CA  1 
ATOM   964  C  C   . ASP A 1 110 ? -8.471  -16.276 28.431  1.00   11.08  ? 110 ASP A C   1 
ATOM   965  O  O   . ASP A 1 110 ? -8.556  -17.514 28.363  1.00   11.68  ? 110 ASP A O   1 
ATOM   966  C  CB  . ASP A 1 110 ? -10.586 -16.313 29.830  1.00   13.14  ? 110 ASP A CB  1 
ATOM   967  C  CG  . ASP A 1 110 ? -11.438 -15.550 30.850  1.00   14.41  ? 110 ASP A CG  1 
ATOM   968  O  OD1 . ASP A 1 110 ? -10.871 -14.660 31.547  1.00   15.33  ? 110 ASP A OD1 1 
ATOM   969  O  OD2 . ASP A 1 110 ? -12.637 -15.828 30.949  1.00   16.77  ? 110 ASP A OD2 1 
ATOM   970  N  N   . LYS A 1 111 ? -7.604  -15.560 27.723  1.00   10.14  ? 111 LYS A N   1 
ATOM   971  C  CA  . LYS A 1 111 ? -6.621  -16.110 26.821  1.00   10.84  ? 111 LYS A CA  1 
ATOM   972  C  C   . LYS A 1 111 ? -7.179  -16.620 25.517  1.00   10.52  ? 111 LYS A C   1 
ATOM   973  O  O   . LYS A 1 111 ? -6.398  -16.994 24.609  1.00   12.13  ? 111 LYS A O   1 
ATOM   974  C  CB  . LYS A 1 111 ? -5.693  -17.171 27.461  1.00   12.72  ? 111 LYS A CB  1 
ATOM   975  C  CG  . LYS A 1 111 ? -4.971  -16.605 28.718  1.00   17.02  ? 111 LYS A CG  1 
ATOM   976  C  CD  . LYS A 1 111 ? -4.056  -15.425 28.394  1.00   19.83  ? 111 LYS A CD  1 
ATOM   977  C  CE  . LYS A 1 111 ? -3.214  -14.820 29.529  1.00   25.13  ? 111 LYS A CE  1 
ATOM   978  N  NZ  . LYS A 1 111 ? -2.039  -15.628 29.794  1.00   25.08  ? 111 LYS A NZ  1 
ATOM   979  N  N   . LYS A 1 112 ? -8.483  -16.594 25.292  1.00   10.03  ? 112 LYS A N   1 
ATOM   980  C  CA  . LYS A 1 112 ? -9.058  -16.995 24.013  1.00   10.69  ? 112 LYS A CA  1 
ATOM   981  C  C   . LYS A 1 112 ? -8.735  -15.946 22.940  1.00   9.68   ? 112 LYS A C   1 
ATOM   982  O  O   . LYS A 1 112 ? -8.984  -14.760 23.147  1.00   9.55   ? 112 LYS A O   1 
ATOM   983  C  CB  . LYS A 1 112 ? -10.600 -17.109 24.109  1.00   11.52  ? 112 LYS A CB  1 
ATOM   984  C  CG  . LYS A 1 112 ? -11.275 -17.455 22.812  1.00   13.02  ? 112 LYS A CG  1 
ATOM   985  C  CD  . LYS A 1 112 ? -12.783 -17.410 22.888  1.00   15.45  ? 112 LYS A CD  1 
ATOM   986  C  CE  . LYS A 1 112 ? -13.446 -17.640 21.578  1.00   16.72  ? 112 LYS A CE  1 
ATOM   987  N  NZ  . LYS A 1 112 ? -13.240 -18.938 21.115  1.00   16.36  ? 112 LYS A NZ  1 
ATOM   988  N  N   A LYS A 1 113 ? -8.127  -16.400 21.851  0.50   10.06  ? 113 LYS A N   1 
ATOM   989  N  N   B LYS A 1 113 ? -8.345  -16.460 21.786  0.50   9.26   ? 113 LYS A N   1 
ATOM   990  C  CA  A LYS A 1 113 ? -8.025  -15.618 20.627  0.50   9.76   ? 113 LYS A CA  1 
ATOM   991  C  CA  B LYS A 1 113 ? -8.021  -15.644 20.617  0.50   9.80   ? 113 LYS A CA  1 
ATOM   992  C  C   A LYS A 1 113 ? -9.242  -15.870 19.736  0.50   8.92   ? 113 LYS A C   1 
ATOM   993  C  C   B LYS A 1 113 ? -9.082  -15.875 19.579  0.50   8.95   ? 113 LYS A C   1 
ATOM   994  O  O   A LYS A 1 113 ? -9.730  -16.988 19.593  0.50   9.90   ? 113 LYS A O   1 
ATOM   995  O  O   B LYS A 1 113 ? -9.311  -16.999 19.182  0.50   8.75   ? 113 LYS A O   1 
ATOM   996  C  CB  A LYS A 1 113 ? -6.756  -15.982 19.864  0.50   10.02  ? 113 LYS A CB  1 
ATOM   997  C  CB  B LYS A 1 113 ? -6.679  -16.054 20.019  0.50   10.97  ? 113 LYS A CB  1 
ATOM   998  C  CG  A LYS A 1 113 ? -5.461  -15.887 20.654  0.50   9.92   ? 113 LYS A CG  1 
ATOM   999  C  CG  B LYS A 1 113 ? -5.461  -15.533 20.746  0.50   11.10  ? 113 LYS A CG  1 
ATOM   1000 C  CD  A LYS A 1 113 ? -4.277  -16.298 19.788  0.50   12.20  ? 113 LYS A CD  1 
ATOM   1001 C  CD  B LYS A 1 113 ? -4.193  -16.243 20.263  0.50   11.92  ? 113 LYS A CD  1 
ATOM   1002 C  CE  A LYS A 1 113 ? -2.932  -16.011 20.482  0.50   13.67  ? 113 LYS A CE  1 
ATOM   1003 C  CE  B LYS A 1 113 ? -2.952  -15.544 20.854  0.50   16.16  ? 113 LYS A CE  1 
ATOM   1004 N  NZ  A LYS A 1 113 ? -2.634  -16.543 21.838  0.50   16.01  ? 113 LYS A NZ  1 
ATOM   1005 N  NZ  B LYS A 1 113 ? -1.731  -16.410 20.716  0.50   20.80  ? 113 LYS A NZ  1 
ATOM   1006 N  N   . TYR A 1 114 ? -9.747  -14.784 19.135  1.00   9.09   ? 114 TYR A N   1 
ATOM   1007 C  CA  . TYR A 1 114 ? -10.731 -14.841 18.116  1.00   9.13   ? 114 TYR A CA  1 
ATOM   1008 C  C   . TYR A 1 114 ? -10.062 -14.792 16.725  1.00   8.45   ? 114 TYR A C   1 
ATOM   1009 O  O   . TYR A 1 114 ? -8.863  -14.488 16.612  1.00   9.08   ? 114 TYR A O   1 
ATOM   1010 C  CB  . TYR A 1 114 ? -11.768 -13.731 18.265  1.00   9.04   ? 114 TYR A CB  1 
ATOM   1011 C  CG  . TYR A 1 114 ? -12.708 -13.970 19.426  1.00   8.84   ? 114 TYR A CG  1 
ATOM   1012 C  CD1 . TYR A 1 114 ? -12.444 -13.544 20.737  1.00   10.70  ? 114 TYR A CD1 1 
ATOM   1013 C  CD2 . TYR A 1 114 ? -13.914 -14.571 19.187  1.00   10.37  ? 114 TYR A CD2 1 
ATOM   1014 C  CE1 . TYR A 1 114 ? -13.356 -13.776 21.777  1.00   12.61  ? 114 TYR A CE1 1 
ATOM   1015 C  CE2 . TYR A 1 114 ? -14.892 -14.782 20.191  1.00   12.77  ? 114 TYR A CE2 1 
ATOM   1016 C  CZ  . TYR A 1 114 ? -14.585 -14.325 21.483  1.00   13.40  ? 114 TYR A CZ  1 
ATOM   1017 O  OH  . TYR A 1 114 ? -15.443 -14.474 22.566  1.00   18.23  ? 114 TYR A OH  1 
ATOM   1018 N  N   . ALA A 1 115 ? -10.821 -15.091 15.683  1.00   8.95   ? 115 ALA A N   1 
ATOM   1019 C  CA  . ALA A 1 115 ? -10.299 -15.114 14.331  1.00   9.13   ? 115 ALA A CA  1 
ATOM   1020 C  C   . ALA A 1 115 ? -9.916  -13.730 13.837  1.00   8.81   ? 115 ALA A C   1 
ATOM   1021 O  O   . ALA A 1 115 ? -9.076  -13.580 12.946  1.00   9.27   ? 115 ALA A O   1 
ATOM   1022 C  CB  . ALA A 1 115 ? -11.331 -15.722 13.399  1.00   10.51  ? 115 ALA A CB  1 
ATOM   1023 N  N   . ALA A 1 116 ? -10.563 -12.683 14.372  1.00   8.46   ? 116 ALA A N   1 
ATOM   1024 C  CA  . ALA A 1 116 ? -10.274 -11.331 13.929  1.00   8.56   ? 116 ALA A CA  1 
ATOM   1025 C  C   . ALA A 1 116 ? -10.889 -10.386 14.959  1.00   7.85   ? 116 ALA A C   1 
ATOM   1026 O  O   . ALA A 1 116 ? -11.615 -10.785 15.868  1.00   8.19   ? 116 ALA A O   1 
ATOM   1027 C  CB  . ALA A 1 116 ? -10.802 -11.069 12.513  1.00   9.18   ? 116 ALA A CB  1 
ATOM   1028 N  N   . GLU A 1 117 ? -10.557 -9.100  14.793  1.00   7.79   ? 117 GLU A N   1 
ATOM   1029 C  CA  . GLU A 1 117 ? -11.074 -8.068  15.660  1.00   7.52   ? 117 GLU A CA  1 
ATOM   1030 C  C   . GLU A 1 117 ? -11.280 -6.799  14.826  1.00   7.55   ? 117 GLU A C   1 
ATOM   1031 O  O   . GLU A 1 117 ? -10.347 -6.388  14.109  1.00   9.01   ? 117 GLU A O   1 
ATOM   1032 C  CB  . GLU A 1 117 ? -10.116 -7.815  16.835  1.00   8.40   ? 117 GLU A CB  1 
ATOM   1033 C  CG  . GLU A 1 117 ? -10.592 -6.866  17.901  1.00   8.73   ? 117 GLU A CG  1 
ATOM   1034 C  CD  . GLU A 1 117 ? -9.665  -6.764  19.108  1.00   7.81   ? 117 GLU A CD  1 
ATOM   1035 O  OE1 . GLU A 1 117 ? -9.022  -7.792  19.407  1.00   9.25   ? 117 GLU A OE1 1 
ATOM   1036 O  OE2 . GLU A 1 117 ? -9.631  -5.705  19.745  1.00   8.88   ? 117 GLU A OE2 1 
ATOM   1037 N  N   . LEU A 1 118 ? -12.454 -6.202  14.943  1.00   7.52   ? 118 LEU A N   1 
ATOM   1038 C  CA  . LEU A 1 118 ? -12.819 -4.964  14.300  1.00   7.22   ? 118 LEU A CA  1 
ATOM   1039 C  C   . LEU A 1 118 ? -12.589 -3.830  15.281  1.00   7.27   ? 118 LEU A C   1 
ATOM   1040 O  O   . LEU A 1 118 ? -12.999 -3.912  16.450  1.00   7.30   ? 118 LEU A O   1 
ATOM   1041 C  CB  . LEU A 1 118 ? -14.331 -5.055  13.972  1.00   8.33   ? 118 LEU A CB  1 
ATOM   1042 C  CG  . LEU A 1 118 ? -15.054 -3.791  13.576  1.00   8.64   ? 118 LEU A CG  1 
ATOM   1043 C  CD1 . LEU A 1 118 ? -14.480 -3.112  12.352  1.00   9.37   ? 118 LEU A CD1 1 
ATOM   1044 C  CD2 . LEU A 1 118 ? -16.503 -4.107  13.341  1.00   10.80  ? 118 LEU A CD2 1 
ATOM   1045 N  N   . HIS A 1 119 ? -11.972 -2.756  14.795  1.00   6.86   ? 119 HIS A N   1 
ATOM   1046 C  CA  . HIS A 1 119 ? -11.736 -1.540  15.537  1.00   6.75   ? 119 HIS A CA  1 
ATOM   1047 C  C   . HIS A 1 119 ? -12.421 -0.377  14.877  1.00   7.06   ? 119 HIS A C   1 
ATOM   1048 O  O   . HIS A 1 119 ? -12.041 -0.011  13.743  1.00   8.02   ? 119 HIS A O   1 
ATOM   1049 C  CB  . HIS A 1 119 ? -10.241 -1.248  15.643  1.00   7.30   ? 119 HIS A CB  1 
ATOM   1050 C  CG  . HIS A 1 119 ? -9.514  -2.222  16.519  1.00   7.21   ? 119 HIS A CG  1 
ATOM   1051 N  ND1 . HIS A 1 119 ? -8.158  -2.392  16.488  1.00   6.70   ? 119 HIS A ND1 1 
ATOM   1052 C  CD2 . HIS A 1 119 ? -10.052 -3.052  17.464  1.00   7.12   ? 119 HIS A CD2 1 
ATOM   1053 C  CE1 . HIS A 1 119 ? -7.887  -3.332  17.404  1.00   7.74   ? 119 HIS A CE1 1 
ATOM   1054 N  NE2 . HIS A 1 119 ? -9.001  -3.735  18.024  1.00   7.27   ? 119 HIS A NE2 1 
ATOM   1055 N  N   . LEU A 1 120 ? -13.426 0.194   15.541  1.00   7.12   ? 120 LEU A N   1 
ATOM   1056 C  CA  . LEU A 1 120 ? -14.108 1.408   15.105  1.00   7.89   ? 120 LEU A CA  1 
ATOM   1057 C  C   . LEU A 1 120 ? -13.473 2.554   15.882  1.00   6.99   ? 120 LEU A C   1 
ATOM   1058 O  O   . LEU A 1 120 ? -13.579 2.600   17.106  1.00   7.38   ? 120 LEU A O   1 
ATOM   1059 C  CB  . LEU A 1 120 ? -15.598 1.285   15.321  1.00   8.36   ? 120 LEU A CB  1 
ATOM   1060 C  CG  . LEU A 1 120 ? -16.291 0.230   14.443  1.00   9.57   ? 120 LEU A CG  1 
ATOM   1061 C  CD1 . LEU A 1 120 ? -17.203 -0.631  15.286  1.00   14.74  ? 120 LEU A CD1 1 
ATOM   1062 C  CD2 . LEU A 1 120 ? -17.066 0.908   13.313  1.00   12.24  ? 120 LEU A CD2 1 
ATOM   1063 N  N   . VAL A 1 121 ? -12.797 3.449   15.166  1.00   7.56   ? 121 VAL A N   1 
ATOM   1064 C  CA  . VAL A 1 121 ? -11.937 4.450   15.776  1.00   7.65   ? 121 VAL A CA  1 
ATOM   1065 C  C   . VAL A 1 121 ? -12.629 5.805   15.813  1.00   7.45   ? 121 VAL A C   1 
ATOM   1066 O  O   . VAL A 1 121 ? -13.080 6.293   14.753  1.00   8.41   ? 121 VAL A O   1 
ATOM   1067 C  CB  . VAL A 1 121 ? -10.617 4.546   14.963  1.00   8.27   ? 121 VAL A CB  1 
ATOM   1068 C  CG1 . VAL A 1 121 ? -9.686  5.607   15.585  1.00   9.46   ? 121 VAL A CG1 1 
ATOM   1069 C  CG2 . VAL A 1 121 ? -9.964  3.194   14.828  1.00   8.87   ? 121 VAL A CG2 1 
ATOM   1070 N  N   . HIS A 1 122 ? -12.706 6.424   16.990  1.00   7.65   ? 122 HIS A N   1 
ATOM   1071 C  CA  . HIS A 1 122 ? -13.391 7.675   17.182  1.00   7.88   ? 122 HIS A CA  1 
ATOM   1072 C  C   . HIS A 1 122 ? -12.508 8.658   17.935  1.00   8.06   ? 122 HIS A C   1 
ATOM   1073 O  O   . HIS A 1 122 ? -11.757 8.249   18.811  1.00   8.97   ? 122 HIS A O   1 
ATOM   1074 C  CB  . HIS A 1 122 ? -14.663 7.483   18.023  1.00   8.48   ? 122 HIS A CB  1 
ATOM   1075 C  CG  . HIS A 1 122 ? -15.542 6.361   17.617  1.00   7.99   ? 122 HIS A CG  1 
ATOM   1076 N  ND1 . HIS A 1 122 ? -15.240 5.041   17.879  1.00   8.48   ? 122 HIS A ND1 1 
ATOM   1077 C  CD2 . HIS A 1 122 ? -16.766 6.301   16.976  1.00   9.54   ? 122 HIS A CD2 1 
ATOM   1078 C  CE1 . HIS A 1 122 ? -16.215 4.275   17.435  1.00   9.12   ? 122 HIS A CE1 1 
ATOM   1079 N  NE2 . HIS A 1 122 ? -17.175 4.987   16.884  1.00   9.47   ? 122 HIS A NE2 1 
ATOM   1080 N  N   . TRP A 1 123 ? -12.633 9.945   17.618  1.00   8.00   ? 123 TRP A N   1 
ATOM   1081 C  CA  . TRP A 1 123 ? -11.843 10.961  18.293  1.00   8.31   ? 123 TRP A CA  1 
ATOM   1082 C  C   . TRP A 1 123 ? -12.694 11.932  19.029  1.00   8.43   ? 123 TRP A C   1 
ATOM   1083 O  O   . TRP A 1 123 ? -13.827 12.282  18.633  1.00   9.30   ? 123 TRP A O   1 
ATOM   1084 C  CB  . TRP A 1 123 ? -10.896 11.703  17.308  1.00   10.55  ? 123 TRP A CB  1 
ATOM   1085 C  CG  . TRP A 1 123 ? -11.571 12.351  16.162  1.00   10.55  ? 123 TRP A CG  1 
ATOM   1086 C  CD1 . TRP A 1 123 ? -11.825 11.742  14.951  1.00   10.89  ? 123 TRP A CD1 1 
ATOM   1087 C  CD2 . TRP A 1 123 ? -12.062 13.688  16.058  1.00   10.96  ? 123 TRP A CD2 1 
ATOM   1088 N  NE1 . TRP A 1 123 ? -12.420 12.614  14.094  1.00   12.16  ? 123 TRP A NE1 1 
ATOM   1089 C  CE2 . TRP A 1 123 ? -12.593 13.815  14.733  1.00   11.79  ? 123 TRP A CE2 1 
ATOM   1090 C  CE3 . TRP A 1 123 ? -12.059 14.806  16.887  1.00   12.93  ? 123 TRP A CE3 1 
ATOM   1091 C  CZ2 . TRP A 1 123 ? -13.164 14.990  14.257  1.00   13.88  ? 123 TRP A CZ2 1 
ATOM   1092 C  CZ3 . TRP A 1 123 ? -12.609 15.967  16.396  1.00   14.40  ? 123 TRP A CZ3 1 
ATOM   1093 C  CH2 . TRP A 1 123 ? -13.149 16.058  15.104  1.00   16.02  ? 123 TRP A CH2 1 
ATOM   1094 N  N   . ASN A 1 124 ? -12.176 12.399  20.172  1.00   8.95   ? 124 ASN A N   1 
ATOM   1095 C  CA  . ASN A 1 124 ? -12.911 13.285  21.071  1.00   9.79   ? 124 ASN A CA  1 
ATOM   1096 C  C   . ASN A 1 124 ? -13.045 14.654  20.498  1.00   9.30   ? 124 ASN A C   1 
ATOM   1097 O  O   . ASN A 1 124 ? -12.025 15.331  20.215  1.00   9.80   ? 124 ASN A O   1 
ATOM   1098 C  CB  . ASN A 1 124 ? -12.112 13.335  22.374  1.00   9.97   ? 124 ASN A CB  1 
ATOM   1099 C  CG  . ASN A 1 124 ? -12.869 13.965  23.494  1.00   10.36  ? 124 ASN A CG  1 
ATOM   1100 O  OD1 . ASN A 1 124 ? -13.701 14.834  23.282  1.00   11.53  ? 124 ASN A OD1 1 
ATOM   1101 N  ND2 . ASN A 1 124 ? -12.585 13.542  24.696  1.00   12.58  ? 124 ASN A ND2 1 
ATOM   1102 N  N   . THR A 1 125 ? -14.264 15.104  20.264  1.00   10.52  ? 125 THR A N   1 
ATOM   1103 C  CA  . THR A 1 125 ? -14.488 16.380  19.583  1.00   11.83  ? 125 THR A CA  1 
ATOM   1104 C  C   . THR A 1 125 ? -13.945 17.541  20.329  1.00   11.42  ? 125 THR A C   1 
ATOM   1105 O  O   . THR A 1 125 ? -13.802 18.627  19.771  1.00   13.24  ? 125 THR A O   1 
ATOM   1106 C  CB  . THR A 1 125 ? -16.023 16.490  19.219  1.00   14.81  ? 125 THR A CB  1 
ATOM   1107 O  OG1 . THR A 1 125 ? -16.810 16.461  20.412  1.00   19.60  ? 125 THR A OG1 1 
ATOM   1108 C  CG2 . THR A 1 125 ? -16.423 15.430  18.199  1.00   17.22  ? 125 THR A CG2 1 
ATOM   1109 N  N   A LYS A 1 126 ? -13.605 17.338  21.591  0.50   9.82   ? 127 LYS A N   1 
ATOM   1110 N  N   B LYS A 1 126 ? -13.612 17.367  21.547  0.50   10.69  ? 127 LYS A N   1 
ATOM   1111 C  CA  A LYS A 1 126 ? -13.125 18.508  22.277  0.50   12.23  ? 127 LYS A CA  1 
ATOM   1112 C  CA  B LYS A 1 126 ? -13.136 18.498  22.298  0.50   11.69  ? 127 LYS A CA  1 
ATOM   1113 C  C   A LYS A 1 126 ? -11.760 18.955  21.805  0.50   11.51  ? 127 LYS A C   1 
ATOM   1114 C  C   B LYS A 1 126 ? -11.747 18.928  21.853  0.50   11.97  ? 127 LYS A C   1 
ATOM   1115 O  O   A LYS A 1 126 ? -11.321 20.067  22.096  0.50   9.85   ? 127 LYS A O   1 
ATOM   1116 O  O   B LYS A 1 126 ? -11.273 20.004  22.218  0.50   13.21  ? 127 LYS A O   1 
ATOM   1117 C  CB  A LYS A 1 126 ? -13.193 18.477  23.812  0.50   12.38  ? 127 LYS A CB  1 
ATOM   1118 C  CB  B LYS A 1 126 ? -13.148 18.208  23.802  0.50   12.55  ? 127 LYS A CB  1 
ATOM   1119 C  CG  A LYS A 1 126 ? -12.230 17.483  24.440  0.50   11.38  ? 127 LYS A CG  1 
ATOM   1120 C  CG  B LYS A 1 126 ? -11.954 17.399  24.282  0.50   13.63  ? 127 LYS A CG  1 
ATOM   1121 C  CD  A LYS A 1 126 ? -12.638 17.142  25.864  0.50   16.39  ? 127 LYS A CD  1 
ATOM   1122 C  CD  B LYS A 1 126 ? -12.121 16.977  25.733  0.50   13.92  ? 127 LYS A CD  1 
ATOM   1123 C  CE  A LYS A 1 126 ? -11.525 16.413  26.598  0.50   15.90  ? 127 LYS A CE  1 
ATOM   1124 C  CE  B LYS A 1 126 ? -11.783 18.116  26.682  0.50   20.38  ? 127 LYS A CE  1 
ATOM   1125 N  NZ  A LYS A 1 126 ? -12.012 15.773  27.851  0.0000 19.04  ? 127 LYS A NZ  1 
ATOM   1126 N  NZ  B LYS A 1 126 ? -10.332 18.148  27.015  0.0000 37.21  ? 127 LYS A NZ  1 
ATOM   1127 N  N   . TYR A 1 127 ? -11.101 18.083  21.058  1.00   10.75  ? 128 TYR A N   1 
ATOM   1128 C  CA  . TYR A 1 127 ? -9.759  18.368  20.581  1.00   10.97  ? 128 TYR A CA  1 
ATOM   1129 C  C   . TYR A 1 127 ? -9.738  18.779  19.116  1.00   10.97  ? 128 TYR A C   1 
ATOM   1130 O  O   . TYR A 1 127 ? -8.670  19.020  18.553  1.00   11.75  ? 128 TYR A O   1 
ATOM   1131 C  CB  . TYR A 1 127 ? -8.822  17.191  20.853  1.00   11.94  ? 128 TYR A CB  1 
ATOM   1132 C  CG  . TYR A 1 127 ? -8.697  16.882  22.326  1.00   11.65  ? 128 TYR A CG  1 
ATOM   1133 C  CD1 . TYR A 1 127 ? -8.295  17.858  23.228  1.00   11.82  ? 128 TYR A CD1 1 
ATOM   1134 C  CD2 . TYR A 1 127 ? -9.004  15.622  22.821  1.00   10.80  ? 128 TYR A CD2 1 
ATOM   1135 C  CE1 . TYR A 1 127 ? -8.190  17.587  24.579  1.00   12.22  ? 128 TYR A CE1 1 
ATOM   1136 C  CE2 . TYR A 1 127 ? -8.903  15.340  24.170  1.00   11.05  ? 128 TYR A CE2 1 
ATOM   1137 C  CZ  . TYR A 1 127 ? -8.495  16.326  25.044  1.00   12.28  ? 128 TYR A CZ  1 
ATOM   1138 O  OH  . TYR A 1 127 ? -8.392  16.051  26.387  1.00   13.52  ? 128 TYR A OH  1 
ATOM   1139 N  N   . GLY A 1 128 ? -10.914 18.888  18.503  1.00   11.19  ? 129 GLY A N   1 
ATOM   1140 C  CA  . GLY A 1 128 ? -10.982 19.560  17.196  1.00   12.55  ? 129 GLY A CA  1 
ATOM   1141 C  C   . GLY A 1 128 ? -10.639 18.745  15.984  1.00   12.38  ? 129 GLY A C   1 
ATOM   1142 O  O   . GLY A 1 128 ? -11.309 18.870  14.952  1.00   14.13  ? 129 GLY A O   1 
ATOM   1143 N  N   . ASP A 1 129 ? -9.653  17.854  16.057  1.00   13.01  ? 130 ASP A N   1 
ATOM   1144 C  CA  . ASP A 1 129 ? -9.389  16.959  14.935  1.00   14.01  ? 130 ASP A CA  1 
ATOM   1145 C  C   . ASP A 1 129 ? -8.644  15.731  15.493  1.00   13.50  ? 130 ASP A C   1 
ATOM   1146 O  O   . ASP A 1 129 ? -8.150  15.735  16.635  1.00   14.06  ? 130 ASP A O   1 
ATOM   1147 C  CB  . ASP A 1 129 ? -8.804  17.592  13.699  1.00   17.37  ? 130 ASP A CB  1 
ATOM   1148 C  CG  . ASP A 1 129 ? -7.429  18.033  13.906  1.00   14.73  ? 130 ASP A CG  1 
ATOM   1149 O  OD1 . ASP A 1 129 ? -6.886  17.724  14.985  1.00   22.43  ? 130 ASP A OD1 1 
ATOM   1150 O  OD2 . ASP A 1 129 ? -6.898  18.692  12.999  1.00   21.05  ? 130 ASP A OD2 1 
ATOM   1151 N  N   . PHE A 1 130 ? -8.575  14.698  14.661  1.00   12.81  ? 131 PHE A N   1 
ATOM   1152 C  CA  . PHE A 1 130 ? -7.964  13.448  15.047  1.00   12.22  ? 131 PHE A CA  1 
ATOM   1153 C  C   . PHE A 1 130 ? -6.478  13.641  15.421  1.00   11.93  ? 131 PHE A C   1 
ATOM   1154 O  O   . PHE A 1 130 ? -5.954  13.051  16.398  1.00   12.40  ? 131 PHE A O   1 
ATOM   1155 C  CB  . PHE A 1 130 ? -8.067  12.466  13.910  1.00   12.23  ? 131 PHE A CB  1 
ATOM   1156 C  CG  . PHE A 1 130 ? -7.442  11.159  14.159  1.00   11.96  ? 131 PHE A CG  1 
ATOM   1157 C  CD1 . PHE A 1 130 ? -8.057  10.174  14.874  1.00   11.32  ? 131 PHE A CD1 1 
ATOM   1158 C  CD2 . PHE A 1 130 ? -6.138  10.941  13.832  1.00   19.24  ? 131 PHE A CD2 1 
ATOM   1159 C  CE1 . PHE A 1 130 ? -7.484  8.961   15.089  1.00   12.94  ? 131 PHE A CE1 1 
ATOM   1160 C  CE2 . PHE A 1 130 ? -5.519  9.743   14.033  1.00   21.29  ? 131 PHE A CE2 1 
ATOM   1161 C  CZ  . PHE A 1 130 ? -6.253  8.750   14.659  1.00   18.73  ? 131 PHE A CZ  1 
ATOM   1162 N  N   . GLY A 1 131 ? -5.730  14.431  14.609  1.00   14.11  ? 132 GLY A N   1 
ATOM   1163 C  CA  . GLY A 1 131 ? -4.288  14.555  14.865  1.00   15.45  ? 132 GLY A CA  1 
ATOM   1164 C  C   . GLY A 1 131 ? -3.981  15.210  16.214  1.00   14.25  ? 132 GLY A C   1 
ATOM   1165 O  O   . GLY A 1 131 ? -2.958  14.893  16.850  1.00   16.09  ? 132 GLY A O   1 
ATOM   1166 N  N   A LYS A 1 132 ? -4.838  16.122  16.645  0.50   13.31  ? 133 LYS A N   1 
ATOM   1167 N  N   B LYS A 1 132 ? -4.793  16.154  16.690  0.50   13.70  ? 133 LYS A N   1 
ATOM   1168 C  CA  A LYS A 1 132 ? -4.672  16.703  17.955  0.50   12.01  ? 133 LYS A CA  1 
ATOM   1169 C  CA  B LYS A 1 132 ? -4.556  16.665  18.047  0.50   12.96  ? 133 LYS A CA  1 
ATOM   1170 C  C   A LYS A 1 132 ? -5.184  15.746  19.035  0.50   11.26  ? 133 LYS A C   1 
ATOM   1171 C  C   B LYS A 1 132 ? -5.047  15.616  19.050  0.50   11.54  ? 133 LYS A C   1 
ATOM   1172 O  O   A LYS A 1 132 ? -4.670  15.734  20.153  0.50   9.71   ? 133 LYS A O   1 
ATOM   1173 O  O   B LYS A 1 132 ? -4.374  15.456  20.130  0.50   13.00  ? 133 LYS A O   1 
ATOM   1174 C  CB  A LYS A 1 132 ? -5.385  18.038  17.999  0.50   12.91  ? 133 LYS A CB  1 
ATOM   1175 C  CB  B LYS A 1 132 ? -5.295  17.957  18.281  0.50   13.28  ? 133 LYS A CB  1 
ATOM   1176 C  CG  A LYS A 1 132 ? -4.641  19.138  17.194  0.50   13.36  ? 133 LYS A CG  1 
ATOM   1177 C  CG  B LYS A 1 132 ? -4.550  19.219  17.889  0.50   19.24  ? 133 LYS A CG  1 
ATOM   1178 C  CD  A LYS A 1 132 ? -3.364  19.501  17.965  0.50   17.35  ? 133 LYS A CD  1 
ATOM   1179 C  CD  B LYS A 1 132 ? -3.596  19.510  19.062  0.50   28.66  ? 133 LYS A CD  1 
ATOM   1180 C  CE  A LYS A 1 132 ? -2.879  20.952  17.871  0.50   18.74  ? 133 LYS A CE  1 
ATOM   1181 C  CE  B LYS A 1 132 ? -4.122  20.546  20.060  0.50   21.02  ? 133 LYS A CE  1 
ATOM   1182 N  NZ  A LYS A 1 132 ? -2.001  21.409  19.024  0.50   25.15  ? 133 LYS A NZ  1 
ATOM   1183 N  NZ  B LYS A 1 132 ? -4.882  20.392  21.401  0.50   15.87  ? 133 LYS A NZ  1 
ATOM   1184 N  N   . ALA A 1 133 ? -6.224  14.997  18.764  1.00   11.03  ? 134 ALA A N   1 
ATOM   1185 C  CA  . ALA A 1 133 ? -6.743  14.063  19.755  1.00   10.50  ? 134 ALA A CA  1 
ATOM   1186 C  C   . ALA A 1 133 ? -5.756  12.995  20.142  1.00   10.09  ? 134 ALA A C   1 
ATOM   1187 O  O   . ALA A 1 133 ? -5.719  12.596  21.301  1.00   10.29  ? 134 ALA A O   1 
ATOM   1188 C  CB  . ALA A 1 133 ? -8.037  13.465  19.204  1.00   10.16  ? 134 ALA A CB  1 
ATOM   1189 N  N   . VAL A 1 134 ? -4.978  12.459  19.200  1.00   10.97  ? 135 VAL A N   1 
ATOM   1190 C  CA  . VAL A 1 134 ? -4.073  11.366  19.545  1.00   11.37  ? 135 VAL A CA  1 
ATOM   1191 C  C   . VAL A 1 134 ? -2.960  11.804  20.463  1.00   11.00  ? 135 VAL A C   1 
ATOM   1192 O  O   . VAL A 1 134 ? -2.250  10.909  21.015  1.00   12.54  ? 135 VAL A O   1 
ATOM   1193 C  CB  . VAL A 1 134 ? -3.454  10.691  18.340  1.00   13.84  ? 135 VAL A CB  1 
ATOM   1194 C  CG1 . VAL A 1 134 ? -4.481  9.983   17.500  1.00   15.49  ? 135 VAL A CG1 1 
ATOM   1195 C  CG2 . VAL A 1 134 ? -2.551  11.574  17.510  1.00   13.33  ? 135 VAL A CG2 1 
ATOM   1196 N  N   . GLN A 1 135 ? -2.807  13.111  20.693  1.00   11.26  ? 136 GLN A N   1 
ATOM   1197 C  CA  . GLN A 1 135 ? -1.814  13.612  21.643  1.00   12.45  ? 136 GLN A CA  1 
ATOM   1198 C  C   . GLN A 1 135 ? -2.342  13.751  23.045  1.00   11.54  ? 136 GLN A C   1 
ATOM   1199 O  O   . GLN A 1 135 ? -1.644  14.274  23.921  1.00   14.30  ? 136 GLN A O   1 
ATOM   1200 C  CB  . GLN A 1 135 ? -1.272  14.952  21.104  1.00   14.30  ? 136 GLN A CB  1 
ATOM   1201 C  CG  . GLN A 1 135 ? -0.648  14.815  19.744  1.00   16.65  ? 136 GLN A CG  1 
ATOM   1202 C  CD  . GLN A 1 135 ? -0.180  16.149  19.240  1.00   21.16  ? 136 GLN A CD  1 
ATOM   1203 O  OE1 . GLN A 1 135 ? 0.737   16.761  19.861  1.00   26.91  ? 136 GLN A OE1 1 
ATOM   1204 N  NE2 . GLN A 1 135 ? -0.722  16.644  18.139  1.00   21.34  ? 136 GLN A NE2 1 
ATOM   1205 N  N   . GLN A 1 136 ? -3.569  13.284  23.266  1.00   10.42  ? 137 GLN A N   1 
ATOM   1206 C  CA  . GLN A 1 136 ? -4.226  13.473  24.575  1.00   10.54  ? 137 GLN A CA  1 
ATOM   1207 C  C   . GLN A 1 136 ? -4.550  12.145  25.188  1.00   10.54  ? 137 GLN A C   1 
ATOM   1208 O  O   . GLN A 1 136 ? -4.964  11.231  24.488  1.00   10.60  ? 137 GLN A O   1 
ATOM   1209 C  CB  . GLN A 1 136 ? -5.506  14.285  24.413  1.00   11.40  ? 137 GLN A CB  1 
ATOM   1210 C  CG  . GLN A 1 136 ? -5.420  15.532  23.605  1.00   14.36  ? 137 GLN A CG  1 
ATOM   1211 C  CD  . GLN A 1 136 ? -4.487  16.481  24.082  1.00   17.75  ? 137 GLN A CD  1 
ATOM   1212 O  OE1 . GLN A 1 136 ? -4.238  16.624  25.273  1.00   19.37  ? 137 GLN A OE1 1 
ATOM   1213 N  NE2 . GLN A 1 136 ? -3.920  17.199  23.157  1.00   28.97  ? 137 GLN A NE2 1 
ATOM   1214 N  N   A PRO A 1 137 ? -4.591  12.179  26.543  0.50   11.80  ? 138 PRO A N   1 
ATOM   1215 N  N   B PRO A 1 137 ? -4.524  11.942  26.557  0.50   10.04  ? 138 PRO A N   1 
ATOM   1216 C  CA  A PRO A 1 137 ? -4.803  10.916  27.256  0.50   11.24  ? 138 PRO A CA  1 
ATOM   1217 C  CA  B PRO A 1 137 ? -4.811  10.601  27.088  0.50   9.84   ? 138 PRO A CA  1 
ATOM   1218 C  C   A PRO A 1 137 ? -6.211  10.330  27.081  0.50   11.43  ? 138 PRO A C   1 
ATOM   1219 C  C   B PRO A 1 137 ? -6.275  10.194  26.881  0.50   10.38  ? 138 PRO A C   1 
ATOM   1220 O  O   A PRO A 1 137 ? -6.382  9.149   27.337  0.50   13.73  ? 138 PRO A O   1 
ATOM   1221 O  O   B PRO A 1 137 ? -6.540  8.981   26.875  0.50   11.89  ? 138 PRO A O   1 
ATOM   1222 C  CB  A PRO A 1 137 ? -4.666  11.288  28.749  0.50   13.33  ? 138 PRO A CB  1 
ATOM   1223 C  CB  B PRO A 1 137 ? -4.515  10.746  28.600  0.50   11.51  ? 138 PRO A CB  1 
ATOM   1224 C  CG  A PRO A 1 137 ? -4.424  12.693  28.751  0.50   15.29  ? 138 PRO A CG  1 
ATOM   1225 C  CG  B PRO A 1 137 ? -3.628  11.951  28.698  0.50   13.68  ? 138 PRO A CG  1 
ATOM   1226 C  CD  A PRO A 1 137 ? -4.334  13.351  27.435  0.50   13.02  ? 138 PRO A CD  1 
ATOM   1227 C  CD  B PRO A 1 137 ? -3.921  12.840  27.567  0.50   10.60  ? 138 PRO A CD  1 
ATOM   1228 N  N   . ASP A 1 138 ? -7.203  11.179  26.757  1.00   10.22  ? 139 ASP A N   1 
ATOM   1229 C  CA  . ASP A 1 138 ? -8.570  10.838  26.500  1.00   10.60  ? 139 ASP A CA  1 
ATOM   1230 C  C   . ASP A 1 138 ? -8.934  11.264  25.083  1.00   9.25   ? 139 ASP A C   1 
ATOM   1231 O  O   . ASP A 1 138 ? -10.090 11.687  24.810  1.00   10.39  ? 139 ASP A O   1 
ATOM   1232 C  CB  . ASP A 1 138 ? -9.535  11.468  27.502  1.00   12.55  ? 139 ASP A CB  1 
ATOM   1233 C  CG  . ASP A 1 138 ? -9.438  12.940  27.572  1.00   11.95  ? 139 ASP A CG  1 
ATOM   1234 O  OD1 . ASP A 1 138 ? -8.506  13.549  26.956  1.00   12.69  ? 139 ASP A OD1 1 
ATOM   1235 O  OD2 . ASP A 1 138 ? -10.319 13.524  28.240  1.00   15.09  ? 139 ASP A OD2 1 
ATOM   1236 N  N   . GLY A 1 139 ? -8.015  11.160  24.129  1.00   8.76   ? 140 GLY A N   1 
ATOM   1237 C  CA  . GLY A 1 139 ? -8.266  11.600  22.786  1.00   9.05   ? 140 GLY A CA  1 
ATOM   1238 C  C   . GLY A 1 139 ? -9.122  10.708  21.927  1.00   7.83   ? 140 GLY A C   1 
ATOM   1239 O  O   . GLY A 1 139 ? -9.822  11.204  21.048  1.00   8.74   ? 140 GLY A O   1 
ATOM   1240 N  N   . LEU A 1 140 ? -8.999  9.382   22.122  1.00   7.89   ? 141 LEU A N   1 
ATOM   1241 C  CA  . LEU A 1 140 ? -9.698  8.431   21.247  1.00   7.74   ? 141 LEU A CA  1 
ATOM   1242 C  C   . LEU A 1 140 ? -10.511 7.505   22.034  1.00   7.23   ? 141 LEU A C   1 
ATOM   1243 O  O   . LEU A 1 140 ? -10.250 7.226   23.205  1.00   8.03   ? 141 LEU A O   1 
ATOM   1244 C  CB  . LEU A 1 140 ? -8.684  7.600   20.428  1.00   8.44   ? 141 LEU A CB  1 
ATOM   1245 C  CG  . LEU A 1 140 ? -7.751  8.228   19.371  1.00   10.88  ? 141 LEU A CG  1 
ATOM   1246 C  CD1 . LEU A 1 140 ? -7.122  7.163   18.481  1.00   10.61  ? 141 LEU A CD1 1 
ATOM   1247 C  CD2 . LEU A 1 140 ? -8.429  9.314   18.549  1.00   14.29  ? 141 LEU A CD2 1 
ATOM   1248 N  N   . ALA A 1 141 ? -11.548 6.972   21.384  1.00   7.63   ? 142 ALA A N   1 
ATOM   1249 C  CA  . ALA A 1 141 ? -12.336 5.838   21.906  1.00   8.30   ? 142 ALA A CA  1 
ATOM   1250 C  C   . ALA A 1 141 ? -12.380 4.837   20.770  1.00   7.67   ? 142 ALA A C   1 
ATOM   1251 O  O   . ALA A 1 141 ? -12.809 5.185   19.655  1.00   8.57   ? 142 ALA A O   1 
ATOM   1252 C  CB  . ALA A 1 141 ? -13.714 6.269   22.339  1.00   9.44   ? 142 ALA A CB  1 
ATOM   1253 N  N   . VAL A 1 142 ? -11.884 3.632   21.021  1.00   7.46   ? 143 VAL A N   1 
ATOM   1254 C  CA  . VAL A 1 142 ? -11.923 2.562   20.036  1.00   7.49   ? 143 VAL A CA  1 
ATOM   1255 C  C   . VAL A 1 142 ? -12.863 1.528   20.516  1.00   7.20   ? 143 VAL A C   1 
ATOM   1256 O  O   . VAL A 1 142 ? -12.716 1.009   21.636  1.00   7.62   ? 143 VAL A O   1 
ATOM   1257 C  CB  . VAL A 1 142 ? -10.501 2.025   19.650  1.00   7.83   ? 143 VAL A CB  1 
ATOM   1258 C  CG1 . VAL A 1 142 ? -10.675 0.982   18.545  1.00   8.60   ? 143 VAL A CG1 1 
ATOM   1259 C  CG2 . VAL A 1 142 ? -9.603  3.151   19.205  1.00   9.20   ? 143 VAL A CG2 1 
ATOM   1260 N  N   . LEU A 1 143 ? -13.862 1.230   19.688  1.00   7.13   ? 144 LEU A N   1 
ATOM   1261 C  CA  . LEU A 1 143 ? -14.825 0.183   19.941  1.00   7.47   ? 144 LEU A CA  1 
ATOM   1262 C  C   . LEU A 1 143 ? -14.290 -1.069  19.269  1.00   7.65   ? 144 LEU A C   1 
ATOM   1263 O  O   . LEU A 1 143 ? -14.135 -1.102  18.024  1.00   8.87   ? 144 LEU A O   1 
ATOM   1264 C  CB  . LEU A 1 143 ? -16.185 0.603   19.397  1.00   9.47   ? 144 LEU A CB  1 
ATOM   1265 C  CG  . LEU A 1 143 ? -17.329 -0.348  19.545  1.00   10.49  ? 144 LEU A CG  1 
ATOM   1266 C  CD1 . LEU A 1 143 ? -17.594 -0.659  20.991  1.00   13.28  ? 144 LEU A CD1 1 
ATOM   1267 C  CD2 . LEU A 1 143 ? -18.580 0.248   18.887  1.00   13.28  ? 144 LEU A CD2 1 
ATOM   1268 N  N   . GLY A 1 144 ? -13.994 -2.096  20.059  1.00   7.52   ? 145 GLY A N   1 
ATOM   1269 C  CA  . GLY A 1 144 ? -13.449 -3.347  19.554  1.00   7.92   ? 145 GLY A CA  1 
ATOM   1270 C  C   . GLY A 1 144 ? -14.522 -4.436  19.570  1.00   7.19   ? 145 GLY A C   1 
ATOM   1271 O  O   . GLY A 1 144 ? -15.245 -4.570  20.574  1.00   8.21   ? 145 GLY A O   1 
ATOM   1272 N  N   . ILE A 1 145 ? -14.602 -5.179  18.479  1.00   7.25   ? 146 ILE A N   1 
ATOM   1273 C  CA  . ILE A 1 145 ? -15.610 -6.205  18.289  1.00   7.09   ? 146 ILE A CA  1 
ATOM   1274 C  C   . ILE A 1 145 ? -14.915 -7.442  17.786  1.00   7.20   ? 146 ILE A C   1 
ATOM   1275 O  O   . ILE A 1 145 ? -14.206 -7.400  16.762  1.00   8.22   ? 146 ILE A O   1 
ATOM   1276 C  CB  . ILE A 1 145 ? -16.723 -5.724  17.323  1.00   8.48   ? 146 ILE A CB  1 
ATOM   1277 C  CG1 . ILE A 1 145 ? -17.355 -4.448  17.841  1.00   10.24  ? 146 ILE A CG1 1 
ATOM   1278 C  CG2 . ILE A 1 145 ? -17.774 -6.845  17.123  1.00   10.80  ? 146 ILE A CG2 1 
ATOM   1279 C  CD1 . ILE A 1 145 ? -18.397 -3.834  16.964  1.00   10.27  ? 146 ILE A CD1 1 
ATOM   1280 N  N   . PHE A 1 146 ? -15.084 -8.555  18.472  1.00   7.33   ? 147 PHE A N   1 
ATOM   1281 C  CA  . PHE A 1 146 ? -14.485 -9.811  18.053  1.00   7.96   ? 147 PHE A CA  1 
ATOM   1282 C  C   . PHE A 1 146 ? -15.248 -10.418 16.886  1.00   8.00   ? 147 PHE A C   1 
ATOM   1283 O  O   . PHE A 1 146 ? -16.481 -10.301 16.825  1.00   8.72   ? 147 PHE A O   1 
ATOM   1284 C  CB  . PHE A 1 146 ? -14.466 -10.782 19.219  1.00   8.22   ? 147 PHE A CB  1 
ATOM   1285 C  CG  . PHE A 1 146 ? -13.616 -10.324 20.368  1.00   7.64   ? 147 PHE A CG  1 
ATOM   1286 C  CD1 . PHE A 1 146 ? -12.252 -10.126 20.191  1.00   8.12   ? 147 PHE A CD1 1 
ATOM   1287 C  CD2 . PHE A 1 146 ? -14.140 -10.084 21.614  1.00   8.39   ? 147 PHE A CD2 1 
ATOM   1288 C  CE1 . PHE A 1 146 ? -11.447 -9.759  21.252  1.00   8.56   ? 147 PHE A CE1 1 
ATOM   1289 C  CE2 . PHE A 1 146 ? -13.344 -9.690  22.678  1.00   9.29   ? 147 PHE A CE2 1 
ATOM   1290 C  CZ  . PHE A 1 146 ? -11.974 -9.545  22.483  1.00   8.57   ? 147 PHE A CZ  1 
ATOM   1291 N  N   . LEU A 1 147 ? -14.506 -11.142 16.036  1.00   8.20   ? 148 LEU A N   1 
ATOM   1292 C  CA  . LEU A 1 147 ? -15.099 -11.913 14.946  1.00   8.49   ? 148 LEU A CA  1 
ATOM   1293 C  C   . LEU A 1 147 ? -14.774 -13.410 15.188  1.00   8.42   ? 148 LEU A C   1 
ATOM   1294 O  O   . LEU A 1 147 ? -13.609 -13.735 15.401  1.00   9.24   ? 148 LEU A O   1 
ATOM   1295 C  CB  . LEU A 1 147 ? -14.523 -11.540 13.605  1.00   9.22   ? 148 LEU A CB  1 
ATOM   1296 C  CG  . LEU A 1 147 ? -15.054 -10.280 12.916  1.00   9.30   ? 148 LEU A CG  1 
ATOM   1297 C  CD1 . LEU A 1 147 ? -14.851 -9.004  13.753  1.00   10.86  ? 148 LEU A CD1 1 
ATOM   1298 C  CD2 . LEU A 1 147 ? -14.477 -10.089 11.552  1.00   10.99  ? 148 LEU A CD2 1 
ATOM   1299 N  N   . LYS A 1 148 ? -15.796 -14.225 15.083  1.00   9.05   ? 149 LYS A N   1 
ATOM   1300 C  CA  . LYS A 1 148 ? -15.631 -15.681 15.055  1.00   10.05  ? 149 LYS A CA  1 
ATOM   1301 C  C   . LYS A 1 148 ? -16.111 -16.184 13.702  1.00   10.34  ? 149 LYS A C   1 
ATOM   1302 O  O   . LYS A 1 148 ? -16.959 -15.534 13.053  1.00   11.91  ? 149 LYS A O   1 
ATOM   1303 C  CB  . LYS A 1 148 ? -16.388 -16.364 16.182  1.00   11.76  ? 149 LYS A CB  1 
ATOM   1304 C  CG  . LYS A 1 148 ? -17.871 -16.220 16.157  1.00   13.39  ? 149 LYS A CG  1 
ATOM   1305 C  CD  . LYS A 1 148 ? -18.471 -16.961 17.368  1.00   20.11  ? 149 LYS A CD  1 
ATOM   1306 C  CE  . LYS A 1 148 ? -19.936 -17.030 17.227  1.00   30.35  ? 149 LYS A CE  1 
ATOM   1307 N  NZ  . LYS A 1 148 ? -20.402 -17.945 18.306  0.0000 56.66  ? 149 LYS A NZ  1 
ATOM   1308 N  N   . VAL A 1 149 ? -15.617 -17.320 13.277  1.00   11.21  ? 150 VAL A N   1 
ATOM   1309 C  CA  . VAL A 1 149 ? -16.015 -17.927 12.004  1.00   11.12  ? 150 VAL A CA  1 
ATOM   1310 C  C   . VAL A 1 149 ? -17.233 -18.849 12.209  1.00   11.32  ? 150 VAL A C   1 
ATOM   1311 O  O   . VAL A 1 149 ? -17.178 -19.787 12.979  1.00   13.05  ? 150 VAL A O   1 
ATOM   1312 C  CB  . VAL A 1 149 ? -14.819 -18.682 11.416  1.00   12.12  ? 150 VAL A CB  1 
ATOM   1313 C  CG1 . VAL A 1 149 ? -15.223 -19.475 10.179  1.00   14.20  ? 150 VAL A CG1 1 
ATOM   1314 C  CG2 . VAL A 1 149 ? -13.739 -17.699 11.070  1.00   14.18  ? 150 VAL A CG2 1 
ATOM   1315 N  N   . GLY A 1 150 ? -18.291 -18.558 11.454  1.00   12.29  ? 151 GLY A N   1 
ATOM   1316 C  CA  . GLY A 1 150 ? -19.500 -19.371 11.503  1.00   14.38  ? 151 GLY A CA  1 
ATOM   1317 C  C   . GLY A 1 150 ? -20.380 -18.900 10.384  1.00   12.74  ? 151 GLY A C   1 
ATOM   1318 O  O   . GLY A 1 150 ? -20.010 -18.985 9.205   1.00   14.10  ? 151 GLY A O   1 
ATOM   1319 N  N   A SER A 1 151 ? -21.582 -18.415 10.691  0.50   14.45  ? 152 SER A N   1 
ATOM   1320 N  N   B SER A 1 151 ? -21.562 -18.402 10.727  0.50   14.31  ? 152 SER A N   1 
ATOM   1321 C  CA  A SER A 1 151 ? -22.478 -17.885 9.666   0.50   15.38  ? 152 SER A CA  1 
ATOM   1322 C  CA  B SER A 1 151 ? -22.434 -17.766 9.763   0.50   14.16  ? 152 SER A CA  1 
ATOM   1323 C  C   A SER A 1 151 ? -21.942 -16.561 9.164   0.50   13.04  ? 152 SER A C   1 
ATOM   1324 C  C   B SER A 1 151 ? -21.750 -16.572 9.107   0.50   12.65  ? 152 SER A C   1 
ATOM   1325 O  O   A SER A 1 151 ? -21.344 -15.815 9.935   0.50   11.68  ? 152 SER A O   1 
ATOM   1326 O  O   B SER A 1 151 ? -20.853 -15.929 9.689   0.50   11.99  ? 152 SER A O   1 
ATOM   1327 C  CB  A SER A 1 151 ? -23.873 -17.691 10.250  0.50   20.23  ? 152 SER A CB  1 
ATOM   1328 C  CB  B SER A 1 151 ? -23.746 -17.404 10.440  0.50   15.91  ? 152 SER A CB  1 
ATOM   1329 O  OG  A SER A 1 151 ? -23.867 -16.683 11.265  0.50   21.17  ? 152 SER A OG  1 
ATOM   1330 O  OG  B SER A 1 151 ? -24.395 -18.590 10.872  0.50   19.99  ? 152 SER A OG  1 
ATOM   1331 N  N   . ALA A 1 152 ? -22.173 -16.260 7.877   1.00   13.75  ? 153 ALA A N   1 
ATOM   1332 C  CA  . ALA A 1 152 ? -21.755 -15.038 7.263   1.00   13.67  ? 153 ALA A CA  1 
ATOM   1333 C  C   . ALA A 1 152 ? -22.429 -13.846 7.949   1.00   13.13  ? 153 ALA A C   1 
ATOM   1334 O  O   . ALA A 1 152 ? -23.531 -13.885 8.439   1.00   15.25  ? 153 ALA A O   1 
ATOM   1335 C  CB  . ALA A 1 152 ? -22.115 -15.043 5.781   1.00   16.22  ? 153 ALA A CB  1 
ATOM   1336 N  N   . LYS A 1 153 ? -21.666 -12.710 7.852   1.00   13.79  ? 154 LYS A N   1 
ATOM   1337 C  CA  . LYS A 1 153 ? -22.210 -11.416 8.288   1.00   14.95  ? 154 LYS A CA  1 
ATOM   1338 C  C   . LYS A 1 153 ? -22.655 -10.662 7.032   1.00   13.69  ? 154 LYS A C   1 
ATOM   1339 O  O   . LYS A 1 153 ? -21.775 -10.213 6.266   1.00   13.34  ? 154 LYS A O   1 
ATOM   1340 C  CB  . LYS A 1 153 ? -21.168 -10.630 9.070   1.00   14.91  ? 154 LYS A CB  1 
ATOM   1341 C  CG  . LYS A 1 153 ? -21.661 -9.444  9.812   1.00   18.35  ? 154 LYS A CG  1 
ATOM   1342 C  CD  . LYS A 1 153 ? -22.511 -9.802  11.046  1.00   20.37  ? 154 LYS A CD  1 
ATOM   1343 C  CE  . LYS A 1 153 ? -22.510 -8.563  11.826  1.00   19.72  ? 154 LYS A CE  1 
ATOM   1344 N  NZ  . LYS A 1 153 ? -23.369 -8.999  12.900  1.00   19.86  ? 154 LYS A NZ  1 
ATOM   1345 N  N   . PRO A 1 154 ? -23.972 -10.577 6.785   1.00   15.15  ? 155 PRO A N   1 
ATOM   1346 C  CA  . PRO A 1 154 ? -24.312 -10.006 5.487   1.00   15.72  ? 155 PRO A CA  1 
ATOM   1347 C  C   . PRO A 1 154 ? -23.847 -8.557  5.316   1.00   14.39  ? 155 PRO A C   1 
ATOM   1348 O  O   . PRO A 1 154 ? -23.445 -8.170  4.215   1.00   17.50  ? 155 PRO A O   1 
ATOM   1349 C  CB  . PRO A 1 154 ? -25.839 -10.076 5.541   1.00   19.47  ? 155 PRO A CB  1 
ATOM   1350 C  CG  . PRO A 1 154 ? -26.085 -11.290 6.404   1.00   21.07  ? 155 PRO A CG  1 
ATOM   1351 C  CD  . PRO A 1 154 ? -25.157 -11.122 7.530   1.00   17.80  ? 155 PRO A CD  1 
ATOM   1352 N  N   . GLY A 1 155 ? -23.776 -7.817  6.420   1.00   14.11  ? 156 GLY A N   1 
ATOM   1353 C  CA  . GLY A 1 155 ? -23.393 -6.434  6.360   1.00   15.34  ? 156 GLY A CA  1 
ATOM   1354 C  C   . GLY A 1 155 ? -21.905 -6.215  6.193   1.00   15.13  ? 156 GLY A C   1 
ATOM   1355 O  O   . GLY A 1 155 ? -21.462 -5.096  5.978   1.00   19.02  ? 156 GLY A O   1 
ATOM   1356 N  N   . LEU A 1 156 ? -21.165 -7.292  6.224   1.00   13.98  ? 157 LEU A N   1 
ATOM   1357 C  CA  . LEU A 1 156 ? -19.736 -7.249  5.880   1.00   13.65  ? 157 LEU A CA  1 
ATOM   1358 C  C   . LEU A 1 156 ? -19.445 -7.466  4.419   1.00   13.86  ? 157 LEU A C   1 
ATOM   1359 O  O   . LEU A 1 156 ? -18.343 -7.162  3.940   1.00   13.88  ? 157 LEU A O   1 
ATOM   1360 C  CB  . LEU A 1 156 ? -18.962 -8.275  6.750   1.00   14.10  ? 157 LEU A CB  1 
ATOM   1361 C  CG  . LEU A 1 156 ? -17.447 -8.362  6.584   1.00   14.33  ? 157 LEU A CG  1 
ATOM   1362 C  CD1 . LEU A 1 156 ? -16.715 -7.072  6.942   1.00   15.69  ? 157 LEU A CD1 1 
ATOM   1363 C  CD2 . LEU A 1 156 ? -16.880 -9.557  7.407   1.00   15.93  ? 157 LEU A CD2 1 
ATOM   1364 N  N   . GLN A 1 157 ? -20.373 -8.072  3.645   1.00   13.99  ? 158 GLN A N   1 
ATOM   1365 C  CA  . GLN A 1 157 ? -20.020 -8.537  2.315   1.00   15.40  ? 158 GLN A CA  1 
ATOM   1366 C  C   . GLN A 1 157 ? -19.612 -7.380  1.423   1.00   15.67  ? 158 GLN A C   1 
ATOM   1367 O  O   . GLN A 1 157 ? -18.750 -7.592  0.586   1.00   15.52  ? 158 GLN A O   1 
ATOM   1368 C  CB  . GLN A 1 157 ? -21.170 -9.360  1.759   1.00   17.42  ? 158 GLN A CB  1 
ATOM   1369 C  CG  . GLN A 1 157 ? -20.711 -10.069 0.463   1.00   17.95  ? 158 GLN A CG  1 
ATOM   1370 C  CD  . GLN A 1 157 ? -19.607 -11.095 0.701   1.00   16.42  ? 158 GLN A CD  1 
ATOM   1371 O  OE1 . GLN A 1 157 ? -19.436 -11.642 1.810   1.00   16.61  ? 158 GLN A OE1 1 
ATOM   1372 N  NE2 . GLN A 1 157 ? -18.771 -11.321 -0.361  1.00   18.14  ? 158 GLN A NE2 1 
ATOM   1373 N  N   . LYS A 1 158 ? -20.182 -6.160  1.539   1.00   15.26  ? 159 LYS A N   1 
ATOM   1374 C  CA  . LYS A 1 158 ? -19.753 -5.073  0.668   1.00   15.57  ? 159 LYS A CA  1 
ATOM   1375 C  C   . LYS A 1 158 ? -18.268 -4.762  0.818   1.00   14.83  ? 159 LYS A C   1 
ATOM   1376 O  O   . LYS A 1 158 ? -17.590 -4.384  -0.127  1.00   16.77  ? 159 LYS A O   1 
ATOM   1377 C  CB  . LYS A 1 158 ? -20.605 -3.840  0.893   1.00   17.89  ? 159 LYS A CB  1 
ATOM   1378 C  CG  . LYS A 1 158 ? -21.984 -3.926  0.217   1.00   26.61  ? 159 LYS A CG  1 
ATOM   1379 C  CD  . LYS A 1 158 ? -22.368 -2.464  -0.073  1.00   36.91  ? 159 LYS A CD  1 
ATOM   1380 C  CE  . LYS A 1 158 ? -21.381 -1.472  0.644   0.0000 46.21  ? 159 LYS A CE  1 
ATOM   1381 N  NZ  . LYS A 1 158 ? -20.993 -0.091  0.108   0.0000 52.26  ? 159 LYS A NZ  1 
ATOM   1382 N  N   . VAL A 1 159 ? -17.766 -4.876  2.049   1.00   14.80  ? 160 VAL A N   1 
ATOM   1383 C  CA  . VAL A 1 159 ? -16.347 -4.678  2.317   1.00   14.31  ? 160 VAL A CA  1 
ATOM   1384 C  C   . VAL A 1 159 ? -15.566 -5.787  1.676   1.00   13.82  ? 160 VAL A C   1 
ATOM   1385 O  O   . VAL A 1 159 ? -14.593 -5.528  0.951   1.00   15.18  ? 160 VAL A O   1 
ATOM   1386 C  CB  . VAL A 1 159 ? -16.085 -4.646  3.845   1.00   13.58  ? 160 VAL A CB  1 
ATOM   1387 C  CG1 . VAL A 1 159 ? -14.566 -4.701  4.098   1.00   15.77  ? 160 VAL A CG1 1 
ATOM   1388 C  CG2 . VAL A 1 159 ? -16.744 -3.460  4.499   1.00   15.55  ? 160 VAL A CG2 1 
ATOM   1389 N  N   . VAL A 1 160 ? -15.949 -7.030  1.901   1.00   13.65  ? 161 VAL A N   1 
ATOM   1390 C  CA  . VAL A 1 160 ? -15.262 -8.130  1.310   1.00   14.64  ? 161 VAL A CA  1 
ATOM   1391 C  C   . VAL A 1 160 ? -15.156 -8.057  -0.190  1.00   15.83  ? 161 VAL A C   1 
ATOM   1392 O  O   . VAL A 1 160 ? -14.124 -8.404  -0.765  1.00   17.64  ? 161 VAL A O   1 
ATOM   1393 C  CB  . VAL A 1 160 ? -15.982 -9.442  1.683   1.00   16.54  ? 161 VAL A CB  1 
ATOM   1394 C  CG1 . VAL A 1 160 ? -15.411 -10.605 0.890   1.00   19.66  ? 161 VAL A CG1 1 
ATOM   1395 C  CG2 . VAL A 1 160 ? -15.860 -9.686  3.180   1.00   16.78  ? 161 VAL A CG2 1 
ATOM   1396 N  N   . ASP A 1 161 ? -16.198 -7.625  -0.842  1.00   16.47  ? 162 ASP A N   1 
ATOM   1397 C  CA  . ASP A 1 161 ? -16.161 -7.673  -2.290  1.00   19.05  ? 162 ASP A CA  1 
ATOM   1398 C  C   . ASP A 1 161 ? -15.324 -6.581  -2.907  1.00   19.59  ? 162 ASP A C   1 
ATOM   1399 O  O   . ASP A 1 161 ? -15.003 -6.686  -4.082  1.00   27.27  ? 162 ASP A O   1 
ATOM   1400 C  CB  . ASP A 1 161 ? -17.554 -7.564  -2.678  1.00   23.03  ? 162 ASP A CB  1 
ATOM   1401 C  CG  . ASP A 1 161 ? -18.216 -8.931  -2.692  1.00   29.05  ? 162 ASP A CG  1 
ATOM   1402 O  OD1 . ASP A 1 161 ? -17.526 -10.027 -2.765  1.00   29.68  ? 162 ASP A OD1 1 
ATOM   1403 O  OD2 . ASP A 1 161 ? -19.449 -8.895  -2.548  1.00   33.13  ? 162 ASP A OD2 1 
ATOM   1404 N  N   . VAL A 1 162 ? -14.952 -5.535  -2.179  1.00   17.95  ? 163 VAL A N   1 
ATOM   1405 C  CA  . VAL A 1 162 ? -14.181 -4.465  -2.728  1.00   18.02  ? 163 VAL A CA  1 
ATOM   1406 C  C   . VAL A 1 162 ? -12.699 -4.773  -2.546  1.00   15.64  ? 163 VAL A C   1 
ATOM   1407 O  O   . VAL A 1 162 ? -11.794 -4.110  -3.099  1.00   18.40  ? 163 VAL A O   1 
ATOM   1408 C  CB  . VAL A 1 162 ? -14.579 -3.084  -2.145  1.00   19.27  ? 163 VAL A CB  1 
ATOM   1409 C  CG1 . VAL A 1 162 ? -14.080 -2.884  -0.809  1.00   18.92  ? 163 VAL A CG1 1 
ATOM   1410 C  CG2 . VAL A 1 162 ? -14.208 -1.885  -3.002  1.00   22.01  ? 163 VAL A CG2 1 
ATOM   1411 N  N   . LEU A 1 163 ? -12.413 -5.772  -1.723  1.00   16.92  ? 164 LEU A N   1 
ATOM   1412 C  CA  . LEU A 1 163 ? -11.055 -6.028  -1.422  1.00   16.00  ? 164 LEU A CA  1 
ATOM   1413 C  C   . LEU A 1 163 ? -10.143 -6.370  -2.581  1.00   17.81  ? 164 LEU A C   1 
ATOM   1414 O  O   . LEU A 1 163 ? -8.942  -6.033  -2.608  1.00   17.22  ? 164 LEU A O   1 
ATOM   1415 C  CB  . LEU A 1 163 ? -10.794 -7.055  -0.317  1.00   15.44  ? 164 LEU A CB  1 
ATOM   1416 C  CG  . LEU A 1 163 ? -11.413 -6.721  1.026   1.00   14.44  ? 164 LEU A CG  1 
ATOM   1417 C  CD1 . LEU A 1 163 ? -11.227 -7.843  2.054   1.00   16.76  ? 164 LEU A CD1 1 
ATOM   1418 C  CD2 . LEU A 1 163 ? -10.891 -5.440  1.577   1.00   14.59  ? 164 LEU A CD2 1 
ATOM   1419 N  N   . ASP A 1 164 ? -10.629 -7.058  -3.567  1.00   18.49  ? 165 ASP A N   1 
ATOM   1420 C  CA  . ASP A 1 164 ? -9.790  -7.371  -4.759  1.00   24.79  ? 165 ASP A CA  1 
ATOM   1421 C  C   . ASP A 1 164 ? -9.323  -6.092  -5.436  1.00   23.63  ? 165 ASP A C   1 
ATOM   1422 O  O   . ASP A 1 164 ? -8.365  -6.177  -6.189  1.00   27.14  ? 165 ASP A O   1 
ATOM   1423 C  CB  . ASP A 1 164 ? -10.575 -8.230  -5.787  1.00   34.76  ? 165 ASP A CB  1 
ATOM   1424 C  CG  . ASP A 1 164 ? -11.639 -7.413  -6.577  1.00   67.04  ? 165 ASP A CG  1 
ATOM   1425 O  OD1 . ASP A 1 164 ? -12.483 -6.680  -5.993  0.0000 62.52  ? 165 ASP A OD1 1 
ATOM   1426 O  OD2 . ASP A 1 164 ? -11.650 -7.523  -7.817  0.0000 248.02 ? 165 ASP A OD2 1 
ATOM   1427 N  N   . SER A 1 165 ? -10.014 -4.947  -5.273  1.00   18.47  ? 166 SER A N   1 
ATOM   1428 C  CA  . SER A 1 165 ? -9.605  -3.691  -5.867  1.00   21.66  ? 166 SER A CA  1 
ATOM   1429 C  C   . SER A 1 165 ? -8.538  -2.947  -5.093  1.00   16.83  ? 166 SER A C   1 
ATOM   1430 O  O   . SER A 1 165 ? -8.006  -1.944  -5.596  1.00   19.87  ? 166 SER A O   1 
ATOM   1431 C  CB  . SER A 1 165 ? -10.826 -2.851  -6.222  1.00   25.61  ? 166 SER A CB  1 
ATOM   1432 O  OG  . SER A 1 165 ? -11.241 -2.210  -5.029  1.00   23.82  ? 166 SER A OG  1 
ATOM   1433 N  N   . ILE A 1 166 ? -8.266  -3.383  -3.870  1.00   15.72  ? 167 ILE A N   1 
ATOM   1434 C  CA  . ILE A 1 166 ? -7.264  -2.694  -3.065  1.00   14.31  ? 167 ILE A CA  1 
ATOM   1435 C  C   . ILE A 1 166 ? -6.229  -3.733  -2.550  1.00   13.39  ? 167 ILE A C   1 
ATOM   1436 O  O   . ILE A 1 166 ? -5.838  -3.736  -1.378  1.00   14.33  ? 167 ILE A O   1 
ATOM   1437 C  CB  . ILE A 1 166 ? -7.872  -1.878  -1.905  1.00   14.99  ? 167 ILE A CB  1 
ATOM   1438 C  CG1 . ILE A 1 166 ? -8.684  -2.754  -1.002  1.00   14.73  ? 167 ILE A CG1 1 
ATOM   1439 C  CG2 . ILE A 1 166 ? -8.653  -0.699  -2.497  1.00   15.76  ? 167 ILE A CG2 1 
ATOM   1440 C  CD1 . ILE A 1 166 ? -8.787  -2.162  0.400   1.00   15.09  ? 167 ILE A CD1 1 
ATOM   1441 N  N   . LYS A 1 167 ? -5.852  -4.654  -3.445  1.00   15.37  ? 168 LYS A N   1 
ATOM   1442 C  CA  . LYS A 1 167 ? -5.091  -5.788  -3.009  1.00   14.83  ? 168 LYS A CA  1 
ATOM   1443 C  C   . LYS A 1 167 ? -3.768  -5.427  -2.330  1.00   14.96  ? 168 LYS A C   1 
ATOM   1444 O  O   . LYS A 1 167 ? -3.277  -6.064  -1.370  1.00   14.56  ? 168 LYS A O   1 
ATOM   1445 C  CB  . LYS A 1 167 ? -4.737  -6.712  -4.180  1.00   16.02  ? 168 LYS A CB  1 
ATOM   1446 C  CG  . LYS A 1 167 ? -3.955  -7.978  -3.718  1.00   16.94  ? 168 LYS A CG  1 
ATOM   1447 C  CD  . LYS A 1 167 ? -3.778  -8.895  -4.906  1.00   22.28  ? 168 LYS A CD  1 
ATOM   1448 C  CE  . LYS A 1 167 ? -2.728  -9.954  -4.714  1.00   32.43  ? 168 LYS A CE  1 
ATOM   1449 N  NZ  . LYS A 1 167 ? -3.386  -11.256 -4.423  0.0000 56.66  ? 168 LYS A NZ  1 
ATOM   1450 N  N   . THR A 1 168 ? -3.188  -4.363  -2.820  1.00   13.80  ? 169 THR A N   1 
ATOM   1451 C  CA  . THR A 1 168 ? -1.825  -4.062  -2.439  1.00   14.74  ? 169 THR A CA  1 
ATOM   1452 C  C   . THR A 1 168 ? -1.711  -2.595  -1.772  1.00   12.91  ? 169 THR A C   1 
ATOM   1453 O  O   . THR A 1 168 ? -2.582  -1.770  -1.912  1.00   15.40  ? 169 THR A O   1 
ATOM   1454 C  CB  . THR A 1 168 ? -0.806  -4.084  -3.651  1.00   16.60  ? 169 THR A CB  1 
ATOM   1455 O  OG1 . THR A 1 168 ? -1.360  -3.324  -4.716  1.00   18.13  ? 169 THR A OG1 1 
ATOM   1456 C  CG2 . THR A 1 168 ? -0.630  -5.554  -4.096  1.00   18.82  ? 169 THR A CG2 1 
ATOM   1457 N  N   A LYS A 1 169 ? -0.740  -2.439  -0.965  0.50   15.50  ? 170 LYS A N   1 
ATOM   1458 N  N   B LYS A 1 169 ? -0.530  -2.542  -1.049  0.50   17.10  ? 170 LYS A N   1 
ATOM   1459 C  CA  A LYS A 1 169 ? -0.519  -1.215  -0.279  0.50   11.07  ? 170 LYS A CA  1 
ATOM   1460 C  CA  B LYS A 1 169 ? 0.029   -1.447  -0.175  0.50   16.89  ? 170 LYS A CA  1 
ATOM   1461 C  C   A LYS A 1 169 ? -0.632  0.047   -1.133  0.50   10.31  ? 170 LYS A C   1 
ATOM   1462 C  C   B LYS A 1 169 ? 0.065   -0.270  -1.015  0.50   16.25  ? 170 LYS A C   1 
ATOM   1463 O  O   A LYS A 1 169 ? -0.003  0.119   -2.213  0.50   11.66  ? 170 LYS A O   1 
ATOM   1464 O  O   B LYS A 1 169 ? 0.775   -0.209  -1.996  0.50   18.92  ? 170 LYS A O   1 
ATOM   1465 C  CB  A LYS A 1 169 ? 0.879   -1.304  0.365   0.50   11.10  ? 170 LYS A CB  1 
ATOM   1466 C  CB  B LYS A 1 169 ? 1.480   -1.618  0.404   0.50   16.39  ? 170 LYS A CB  1 
ATOM   1467 C  CG  A LYS A 1 169 ? 1.307   -0.111  1.195   0.50   11.91  ? 170 LYS A CG  1 
ATOM   1468 C  CG  B LYS A 1 169 ? 2.031   -0.440  1.247   0.50   18.21  ? 170 LYS A CG  1 
ATOM   1469 C  CD  A LYS A 1 169 ? 2.631   -0.324  1.854   0.50   13.98  ? 170 LYS A CD  1 
ATOM   1470 C  CD  B LYS A 1 169 ? 3.482   -0.598  1.740   0.50   24.07  ? 170 LYS A CD  1 
ATOM   1471 C  CE  A LYS A 1 169 ? 3.133   0.887   2.687   0.50   26.90  ? 170 LYS A CE  1 
ATOM   1472 C  CE  B LYS A 1 169 ? 4.349   -1.517  0.893   0.50   34.27  ? 170 LYS A CE  1 
ATOM   1473 N  NZ  A LYS A 1 169 ? 4.364   0.649   3.519   0.50   27.55  ? 170 LYS A NZ  1 
ATOM   1474 N  NZ  B LYS A 1 169 ? 5.738   -1.708  1.425   0.50   35.78  ? 170 LYS A NZ  1 
ATOM   1475 N  N   A GLY A 1 170 ? -1.417  1.035   -0.659  0.50   10.53  ? 171 GLY A N   1 
ATOM   1476 N  N   B GLY A 1 170 ? -0.642  0.722   -0.540  0.50   13.48  ? 171 GLY A N   1 
ATOM   1477 C  CA  A GLY A 1 170 ? -1.540  2.335   -1.267  0.50   12.45  ? 171 GLY A CA  1 
ATOM   1478 C  CA  B GLY A 1 170 ? -0.998  1.907   -1.389  0.50   16.43  ? 171 GLY A CA  1 
ATOM   1479 C  C   A GLY A 1 170 ? -2.731  2.356   -2.174  0.50   14.66  ? 171 GLY A C   1 
ATOM   1480 C  C   B GLY A 1 170 ? -2.280  2.116   -2.272  0.50   16.78  ? 171 GLY A C   1 
ATOM   1481 O  O   A GLY A 1 170 ? -3.027  3.407   -2.726  0.50   15.70  ? 171 GLY A O   1 
ATOM   1482 O  O   B GLY A 1 170 ? -2.414  3.254   -2.713  0.50   22.45  ? 171 GLY A O   1 
ATOM   1483 N  N   . LYS A 1 171 ? -3.227  1.164   -2.509  1.00   15.69  ? 172 LYS A N   1 
ATOM   1484 C  CA  . LYS A 1 171 ? -4.435  1.222   -3.307  1.00   16.55  ? 172 LYS A CA  1 
ATOM   1485 C  C   . LYS A 1 171 ? -5.641  1.710   -2.471  1.00   14.00  ? 172 LYS A C   1 
ATOM   1486 O  O   . LYS A 1 171 ? -5.838  1.240   -1.327  1.00   15.08  ? 172 LYS A O   1 
ATOM   1487 C  CB  . LYS A 1 171 ? -4.697  -0.117  -3.952  1.00   15.47  ? 172 LYS A CB  1 
ATOM   1488 C  CG  . LYS A 1 171 ? -3.648  -0.510  -4.948  1.00   19.96  ? 172 LYS A CG  1 
ATOM   1489 C  CD  . LYS A 1 171 ? -4.081  -1.639  -5.920  1.00   27.18  ? 172 LYS A CD  1 
ATOM   1490 C  CE  . LYS A 1 171 ? -5.248  -1.289  -6.869  0.0000 39.61  ? 172 LYS A CE  1 
ATOM   1491 N  NZ  . LYS A 1 171 ? -5.801  -2.313  -7.888  0.0000 40.72  ? 172 LYS A NZ  1 
ATOM   1492 N  N   . SER A 1 172 ? -6.502  2.529   -3.029  1.00   16.30  ? 173 SER A N   1 
ATOM   1493 C  CA  . SER A 1 172 ? -7.782  2.913   -2.458  1.00   16.42  ? 173 SER A CA  1 
ATOM   1494 C  C   . SER A 1 172 ? -8.930  2.761   -3.487  1.00   15.00  ? 173 SER A C   1 
ATOM   1495 O  O   . SER A 1 172 ? -8.680  2.658   -4.686  1.00   18.39  ? 173 SER A O   1 
ATOM   1496 C  CB  . SER A 1 172 ? -7.682  4.355   -1.982  1.00   18.18  ? 173 SER A CB  1 
ATOM   1497 O  OG  . SER A 1 172 ? -7.372  5.237   -3.032  1.00   26.30  ? 173 SER A OG  1 
ATOM   1498 N  N   . ALA A 1 173 ? -10.177 2.741   -3.010  1.00   15.94  ? 174 ALA A N   1 
ATOM   1499 C  CA  . ALA A 1 173 ? -11.328 2.690   -3.826  1.00   18.89  ? 174 ALA A CA  1 
ATOM   1500 C  C   . ALA A 1 173 ? -12.468 3.498   -3.204  1.00   14.88  ? 174 ALA A C   1 
ATOM   1501 O  O   . ALA A 1 173 ? -12.545 3.555   -1.953  1.00   14.76  ? 174 ALA A O   1 
ATOM   1502 C  CB  . ALA A 1 173 ? -11.813 1.253   -4.056  1.00   21.45  ? 174 ALA A CB  1 
ATOM   1503 N  N   . ASP A 1 174 ? -13.243 4.153   -4.013  1.00   18.87  ? 175 ASP A N   1 
ATOM   1504 C  CA  . ASP A 1 174 ? -14.383 4.868   -3.435  1.00   21.05  ? 175 ASP A CA  1 
ATOM   1505 C  C   . ASP A 1 174 ? -15.223 3.837   -2.714  1.00   19.04  ? 175 ASP A C   1 
ATOM   1506 O  O   . ASP A 1 174 ? -15.384 2.655   -3.174  1.00   20.43  ? 175 ASP A O   1 
ATOM   1507 C  CB  . ASP A 1 174 ? -15.255 5.427   -4.581  1.00   26.70  ? 175 ASP A CB  1 
ATOM   1508 C  CG  . ASP A 1 174 ? -14.556 6.499   -5.318  1.00   40.42  ? 175 ASP A CG  1 
ATOM   1509 O  OD1 . ASP A 1 174 ? -13.996 7.350   -4.580  1.00   56.10  ? 175 ASP A OD1 1 
ATOM   1510 O  OD2 . ASP A 1 174 ? -14.514 6.500   -6.594  1.00   31.59  ? 175 ASP A OD2 1 
ATOM   1511 N  N   . PHE A 1 175 ? -15.812 4.267   -1.588  1.00   17.02  ? 176 PHE A N   1 
ATOM   1512 C  CA  . PHE A 1 175 ? -16.599 3.363   -0.765  1.00   17.15  ? 176 PHE A CA  1 
ATOM   1513 C  C   . PHE A 1 175 ? -17.617 4.161   -0.014  1.00   15.91  ? 176 PHE A C   1 
ATOM   1514 O  O   . PHE A 1 175 ? -17.422 4.401   1.160   1.00   18.96  ? 176 PHE A O   1 
ATOM   1515 C  CB  . PHE A 1 175 ? -15.649 2.531   0.119   1.00   17.54  ? 176 PHE A CB  1 
ATOM   1516 C  CG  . PHE A 1 175 ? -16.241 1.290   0.630   1.00   16.10  ? 176 PHE A CG  1 
ATOM   1517 C  CD1 . PHE A 1 175 ? -16.540 0.271   -0.204  1.00   18.62  ? 176 PHE A CD1 1 
ATOM   1518 C  CD2 . PHE A 1 175 ? -16.517 1.160   1.981   1.00   17.02  ? 176 PHE A CD2 1 
ATOM   1519 C  CE1 . PHE A 1 175 ? -17.081 -0.897  0.259   1.00   21.71  ? 176 PHE A CE1 1 
ATOM   1520 C  CE2 . PHE A 1 175 ? -17.012 -0.036  2.475   1.00   18.35  ? 176 PHE A CE2 1 
ATOM   1521 C  CZ  . PHE A 1 175 ? -17.366 -1.039  1.604   1.00   18.84  ? 176 PHE A CZ  1 
ATOM   1522 N  N   . THR A 1 176 ? -18.626 4.585   -0.723  1.00   17.05  ? 177 THR A N   1 
ATOM   1523 C  CA  . THR A 1 176 ? -19.669 5.366   -0.171  1.00   15.82  ? 177 THR A CA  1 
ATOM   1524 C  C   . THR A 1 176 ? -20.796 4.543   0.298   1.00   14.47  ? 177 THR A C   1 
ATOM   1525 O  O   . THR A 1 176 ? -20.994 3.405   -0.187  1.00   15.97  ? 177 THR A O   1 
ATOM   1526 C  CB  . THR A 1 176 ? -20.090 6.411   -1.203  1.00   16.80  ? 177 THR A CB  1 
ATOM   1527 O  OG1 . THR A 1 176 ? -20.429 5.801   -2.454  1.00   22.74  ? 177 THR A OG1 1 
ATOM   1528 C  CG2 . THR A 1 176 ? -18.967 7.444   -1.439  1.00   26.16  ? 177 THR A CG2 1 
ATOM   1529 N  N   . ASN A 1 177 ? -21.617 5.122   1.165   1.00   15.48  ? 178 ASN A N   1 
ATOM   1530 C  CA  . ASN A 1 177 ? -22.877 4.538   1.593   1.00   16.50  ? 178 ASN A CA  1 
ATOM   1531 C  C   . ASN A 1 177 ? -22.745 3.233   2.349   1.00   15.52  ? 178 ASN A C   1 
ATOM   1532 O  O   . ASN A 1 177 ? -23.665 2.487   2.367   1.00   23.57  ? 178 ASN A O   1 
ATOM   1533 C  CB  . ASN A 1 177 ? -23.834 4.455   0.404   1.00   18.31  ? 178 ASN A CB  1 
ATOM   1534 C  CG  . ASN A 1 177 ? -24.071 5.840   -0.180  1.00   17.34  ? 178 ASN A CG  1 
ATOM   1535 O  OD1 . ASN A 1 177 ? -24.676 6.692   0.436   1.00   19.47  ? 178 ASN A OD1 1 
ATOM   1536 N  ND2 . ASN A 1 177 ? -23.460 6.097   -1.313  1.00   18.27  ? 178 ASN A ND2 1 
ATOM   1537 N  N   . PHE A 1 178 ? -21.590 2.997   2.954   1.00   14.77  ? 179 PHE A N   1 
ATOM   1538 C  CA  . PHE A 1 178 ? -21.476 1.812   3.762   1.00   14.70  ? 179 PHE A CA  1 
ATOM   1539 C  C   . PHE A 1 178 ? -21.947 2.071   5.160   1.00   14.33  ? 179 PHE A C   1 
ATOM   1540 O  O   . PHE A 1 178 ? -21.528 3.070   5.763   1.00   15.90  ? 179 PHE A O   1 
ATOM   1541 C  CB  . PHE A 1 178 ? -20.047 1.336   3.815   1.00   15.37  ? 179 PHE A CB  1 
ATOM   1542 C  CG  . PHE A 1 178 ? -19.911 0.086   4.655   1.00   15.13  ? 179 PHE A CG  1 
ATOM   1543 C  CD1 . PHE A 1 178 ? -20.271 -1.184  4.111   1.00   16.89  ? 179 PHE A CD1 1 
ATOM   1544 C  CD2 . PHE A 1 178 ? -19.546 0.147   6.002   1.00   13.36  ? 179 PHE A CD2 1 
ATOM   1545 C  CE1 . PHE A 1 178 ? -20.209 -2.291  4.866   1.00   17.50  ? 179 PHE A CE1 1 
ATOM   1546 C  CE2 . PHE A 1 178 ? -19.545 -1.024  6.761   1.00   12.39  ? 179 PHE A CE2 1 
ATOM   1547 C  CZ  . PHE A 1 178 ? -19.873 -2.224  6.227   1.00   13.76  ? 179 PHE A CZ  1 
ATOM   1548 N  N   . ASP A 1 179 ? -22.826 1.195   5.657   1.00   14.30  ? 180 ASP A N   1 
ATOM   1549 C  CA  . ASP A 1 179 ? -23.454 1.446   6.964   1.00   14.39  ? 180 ASP A CA  1 
ATOM   1550 C  C   . ASP A 1 179 ? -22.822 0.563   8.026   1.00   12.76  ? 180 ASP A C   1 
ATOM   1551 O  O   . ASP A 1 179 ? -22.987 -0.662  8.054   1.00   14.04  ? 180 ASP A O   1 
ATOM   1552 C  CB  . ASP A 1 179 ? -24.922 1.075   6.854   1.00   16.57  ? 180 ASP A CB  1 
ATOM   1553 C  CG  . ASP A 1 179 ? -25.721 1.469   8.067   1.00   18.23  ? 180 ASP A CG  1 
ATOM   1554 O  OD1 . ASP A 1 179 ? -25.151 1.689   9.153   1.00   16.70  ? 180 ASP A OD1 1 
ATOM   1555 O  OD2 . ASP A 1 179 ? -26.928 1.500   7.935   1.00   25.88  ? 180 ASP A OD2 1 
ATOM   1556 N  N   . PRO A 1 180 ? -21.986 1.142   8.935   1.00   12.03  ? 181 PRO A N   1 
ATOM   1557 C  CA  . PRO A 1 180 ? -21.278 0.321   9.927   1.00   12.18  ? 181 PRO A CA  1 
ATOM   1558 C  C   . PRO A 1 180 ? -22.241 -0.303  10.973  1.00   11.98  ? 181 PRO A C   1 
ATOM   1559 O  O   . PRO A 1 180 ? -21.767 -1.156  11.697  1.00   12.44  ? 181 PRO A O   1 
ATOM   1560 C  CB  . PRO A 1 180 ? -20.275 1.331   10.532  1.00   13.48  ? 181 PRO A CB  1 
ATOM   1561 C  CG  . PRO A 1 180 ? -20.908 2.637   10.335  1.00   13.73  ? 181 PRO A CG  1 
ATOM   1562 C  CD  . PRO A 1 180 ? -21.629 2.542   9.000   1.00   13.74  ? 181 PRO A CD  1 
ATOM   1563 N  N   . ARG A 1 181 ? -23.509 0.106   11.000  1.00   12.65  ? 182 ARG A N   1 
ATOM   1564 C  CA  . ARG A 1 181 ? -24.428 -0.567  11.945  1.00   12.35  ? 182 ARG A CA  1 
ATOM   1565 C  C   . ARG A 1 181 ? -24.519 -2.047  11.587  1.00   13.01  ? 182 ARG A C   1 
ATOM   1566 O  O   . ARG A 1 181 ? -24.853 -2.859  12.475  1.00   14.20  ? 182 ARG A O   1 
ATOM   1567 C  CB  . ARG A 1 181 ? -25.805 0.062   11.844  1.00   14.63  ? 182 ARG A CB  1 
ATOM   1568 C  CG  . ARG A 1 181 ? -25.767 1.481   12.426  1.00   15.74  ? 182 ARG A CG  1 
ATOM   1569 C  CD  . ARG A 1 181 ? -27.110 2.158   12.376  1.00   17.66  ? 182 ARG A CD  1 
ATOM   1570 N  NE  . ARG A 1 181 ? -27.473 2.421   10.995  1.00   18.39  ? 182 ARG A NE  1 
ATOM   1571 C  CZ  . ARG A 1 181 ? -28.497 3.178   10.636  1.00   20.21  ? 182 ARG A CZ  1 
ATOM   1572 N  NH1 . ARG A 1 181 ? -29.262 3.738   11.563  1.00   25.85  ? 182 ARG A NH1 1 
ATOM   1573 N  NH2 . ARG A 1 181 ? -28.758 3.365   9.354   1.00   24.46  ? 182 ARG A NH2 1 
ATOM   1574 N  N   . GLY A 1 182 ? -24.284 -2.428  10.319  1.00   13.20  ? 183 GLY A N   1 
ATOM   1575 C  CA  . GLY A 1 182 ? -24.356 -3.812  9.975   1.00   14.42  ? 183 GLY A CA  1 
ATOM   1576 C  C   . GLY A 1 182 ? -23.223 -4.668  10.498  1.00   14.68  ? 183 GLY A C   1 
ATOM   1577 O  O   . GLY A 1 182 ? -23.222 -5.874  10.218  1.00   18.49  ? 183 GLY A O   1 
ATOM   1578 N  N   . LEU A 1 183 ? -22.221 -4.082  11.216  1.00   12.95  ? 184 LEU A N   1 
ATOM   1579 C  CA  . LEU A 1 183 ? -21.114 -4.798  11.820  1.00   12.95  ? 184 LEU A CA  1 
ATOM   1580 C  C   . LEU A 1 183 ? -21.281 -5.004  13.302  1.00   12.03  ? 184 LEU A C   1 
ATOM   1581 O  O   . LEU A 1 183 ? -20.355 -5.534  13.949  1.00   13.96  ? 184 LEU A O   1 
ATOM   1582 C  CB  . LEU A 1 183 ? -19.802 -4.127  11.484  1.00   12.71  ? 184 LEU A CB  1 
ATOM   1583 C  CG  . LEU A 1 183 ? -19.572 -4.063  9.988   1.00   14.54  ? 184 LEU A CG  1 
ATOM   1584 C  CD1 . LEU A 1 183 ? -18.309 -3.284  9.805   1.00   16.97  ? 184 LEU A CD1 1 
ATOM   1585 C  CD2 . LEU A 1 183 ? -19.466 -5.335  9.239   1.00   18.18  ? 184 LEU A CD2 1 
ATOM   1586 N  N   A LEU A 1 184 ? -22.366 -4.481  13.929  0.50   13.16  ? 185 LEU A N   1 
ATOM   1587 N  N   B LEU A 1 184 ? -22.360 -4.597  13.850  0.50   12.78  ? 185 LEU A N   1 
ATOM   1588 C  CA  A LEU A 1 184 ? -22.634 -4.509  15.428  0.50   12.25  ? 185 LEU A CA  1 
ATOM   1589 C  CA  B LEU A 1 184 ? -22.401 -4.665  15.219  0.50   11.12  ? 185 LEU A CA  1 
ATOM   1590 C  C   A LEU A 1 184 ? -23.443 -5.712  15.951  0.50   10.96  ? 185 LEU A C   1 
ATOM   1591 C  C   B LEU A 1 184 ? -23.025 -5.998  15.598  0.50   11.72  ? 185 LEU A C   1 
ATOM   1592 O  O   A LEU A 1 184 ? -24.467 -6.081  15.420  0.50   10.26  ? 185 LEU A O   1 
ATOM   1593 O  O   B LEU A 1 184 ? -23.751 -6.583  14.759  0.50   13.01  ? 185 LEU A O   1 
ATOM   1594 C  CB  A LEU A 1 184 ? -23.342 -3.236  15.934  0.50   11.20  ? 185 LEU A CB  1 
ATOM   1595 C  CB  B LEU A 1 184 ? -23.220 -3.460  15.735  0.50   11.73  ? 185 LEU A CB  1 
ATOM   1596 C  CG  A LEU A 1 184 ? -22.682 -2.032  15.265  0.50   12.04  ? 185 LEU A CG  1 
ATOM   1597 C  CG  B LEU A 1 184 ? -22.733 -1.987  15.561  0.50   11.02  ? 185 LEU A CG  1 
ATOM   1598 C  CD1 A LEU A 1 184 ? -23.439 -0.821  15.751  0.50   12.65  ? 185 LEU A CD1 1 
ATOM   1599 C  CD1 B LEU A 1 184 ? -23.771 -0.990  16.038  0.50   12.35  ? 185 LEU A CD1 1 
ATOM   1600 C  CD2 A LEU A 1 184 ? -21.222 -2.003  15.763  0.50   11.83  ? 185 LEU A CD2 1 
ATOM   1601 C  CD2 B LEU A 1 184 ? -21.387 -1.666  16.246  0.50   11.79  ? 185 LEU A CD2 1 
ATOM   1602 N  N   . PRO A 1 185 ? -22.860 -6.428  16.921  1.00   12.35  ? 186 PRO A N   1 
ATOM   1603 C  CA  . PRO A 1 185 ? -23.601 -7.551  17.507  1.00   13.53  ? 186 PRO A CA  1 
ATOM   1604 C  C   . PRO A 1 185 ? -24.890 -7.010  18.143  1.00   13.18  ? 186 PRO A C   1 
ATOM   1605 O  O   . PRO A 1 185 ? -25.122 -5.818  18.235  1.00   15.78  ? 186 PRO A O   1 
ATOM   1606 C  CB  . PRO A 1 185 ? -22.633 -8.144  18.538  1.00   13.30  ? 186 PRO A CB  1 
ATOM   1607 C  CG  . PRO A 1 185 ? -21.933 -6.913  18.995  1.00   12.15  ? 186 PRO A CG  1 
ATOM   1608 C  CD  . PRO A 1 185 ? -21.734 -6.023  17.774  1.00   11.25  ? 186 PRO A CD  1 
ATOM   1609 N  N   A GLU A 1 186 ? -25.661 -7.987  18.448  0.50   14.14  ? 187 GLU A N   1 
ATOM   1610 N  N   B GLU A 1 186 ? -25.740 -7.836  18.807  0.50   13.10  ? 187 GLU A N   1 
ATOM   1611 C  CA  A GLU A 1 186 ? -26.878 -7.685  19.058  0.50   14.21  ? 187 GLU A CA  1 
ATOM   1612 C  CA  B GLU A 1 186 ? -27.053 -7.404  19.418  0.50   12.32  ? 187 GLU A CA  1 
ATOM   1613 C  C   A GLU A 1 186 ? -26.709 -6.856  20.384  0.50   13.49  ? 187 GLU A C   1 
ATOM   1614 C  C   B GLU A 1 186 ? -26.823 -6.707  20.683  0.50   11.68  ? 187 GLU A C   1 
ATOM   1615 O  O   A GLU A 1 186 ? -27.310 -5.759  20.422  0.50   14.05  ? 187 GLU A O   1 
ATOM   1616 O  O   B GLU A 1 186 ? -27.483 -5.701  21.046  0.50   13.81  ? 187 GLU A O   1 
ATOM   1617 C  CB  A GLU A 1 186 ? -27.593 -8.976  19.223  0.50   13.69  ? 187 GLU A CB  1 
ATOM   1618 C  CB  B GLU A 1 186 ? -27.885 -8.610  19.874  0.50   16.50  ? 187 GLU A CB  1 
ATOM   1619 C  CG  A GLU A 1 186 ? -28.817 -8.805  20.126  0.50   16.34  ? 187 GLU A CG  1 
ATOM   1620 C  CG  B GLU A 1 186 ? -28.855 -9.155  18.848  0.50   18.79  ? 187 GLU A CG  1 
ATOM   1621 C  CD  A GLU A 1 186 ? -29.522 -10.128 20.398  0.50   19.87  ? 187 GLU A CD  1 
ATOM   1622 C  CD  B GLU A 1 186 ? -29.365 -10.563 19.166  0.50   23.56  ? 187 GLU A CD  1 
ATOM   1623 O  OE1 A GLU A 1 186 ? -29.318 -11.116 19.592  0.50   20.92  ? 187 GLU A OE1 1 
ATOM   1624 O  OE1 B GLU A 1 186 ? -29.386 -10.943 20.406  0.50   19.20  ? 187 GLU A OE1 1 
ATOM   1625 O  OE2 A GLU A 1 186 ? -30.245 -10.151 21.420  0.50   21.27  ? 187 GLU A OE2 1 
ATOM   1626 O  OE2 B GLU A 1 186 ? -29.763 -11.287 18.212  0.50   25.28  ? 187 GLU A OE2 1 
ATOM   1627 N  N   . SER A 1 187 ? -25.875 -7.282  21.400  1.00   12.86  ? 188 SER A N   1 
ATOM   1628 C  CA  . SER A 1 187 ? -25.668 -6.683  22.675  1.00   13.42  ? 188 SER A CA  1 
ATOM   1629 C  C   . SER A 1 187 ? -24.538 -5.672  22.666  1.00   12.51  ? 188 SER A C   1 
ATOM   1630 O  O   . SER A 1 187 ? -23.500 -5.940  22.047  1.00   13.53  ? 188 SER A O   1 
ATOM   1631 C  CB  . SER A 1 187 ? -25.281 -7.766  23.675  1.00   14.58  ? 188 SER A CB  1 
ATOM   1632 O  OG  . SER A 1 187 ? -24.978 -7.202  24.983  1.00   15.22  ? 188 SER A OG  1 
ATOM   1633 N  N   . LEU A 1 188 ? -24.689 -4.578  23.382  1.00   12.79  ? 189 LEU A N   1 
ATOM   1634 C  CA  . LEU A 1 188 ? -23.613 -3.615  23.609  1.00   12.48  ? 189 LEU A CA  1 
ATOM   1635 C  C   . LEU A 1 188 ? -22.982 -3.765  24.977  1.00   12.23  ? 189 LEU A C   1 
ATOM   1636 O  O   . LEU A 1 188 ? -22.281 -2.842  25.406  1.00   13.59  ? 189 LEU A O   1 
ATOM   1637 C  CB  . LEU A 1 188 ? -24.113 -2.191  23.321  1.00   15.39  ? 189 LEU A CB  1 
ATOM   1638 C  CG  . LEU A 1 188 ? -24.555 -1.887  21.930  1.00   16.48  ? 189 LEU A CG  1 
ATOM   1639 C  CD1 . LEU A 1 188 ? -25.064 -0.438  21.853  1.00   21.05  ? 189 LEU A CD1 1 
ATOM   1640 C  CD2 . LEU A 1 188 ? -23.484 -2.202  20.882  1.00   18.24  ? 189 LEU A CD2 1 
ATOM   1641 N  N   . ASP A 1 189 ? -23.120 -4.930  25.634  1.00   11.55  ? 190 ASP A N   1 
ATOM   1642 C  CA  . ASP A 1 189 ? -22.372 -5.142  26.871  1.00   12.23  ? 190 ASP A CA  1 
ATOM   1643 C  C   . ASP A 1 189 ? -20.834 -5.084  26.566  1.00   9.98   ? 190 ASP A C   1 
ATOM   1644 O  O   . ASP A 1 189 ? -20.409 -5.604  25.543  1.00   9.99   ? 190 ASP A O   1 
ATOM   1645 C  CB  . ASP A 1 189 ? -22.682 -6.499  27.452  1.00   13.88  ? 190 ASP A CB  1 
ATOM   1646 C  CG  . ASP A 1 189 ? -24.051 -6.623  28.074  1.00   19.74  ? 190 ASP A CG  1 
ATOM   1647 O  OD1 . ASP A 1 189 ? -24.722 -5.591  28.294  1.00   26.07  ? 190 ASP A OD1 1 
ATOM   1648 O  OD2 . ASP A 1 189 ? -24.442 -7.800  28.380  1.00   28.22  ? 190 ASP A OD2 1 
ATOM   1649 N  N   . TYR A 1 190 ? -20.064 -4.496  27.474  1.00   9.93   ? 191 TYR A N   1 
ATOM   1650 C  CA  . TYR A 1 190 ? -18.663 -4.235  27.151  1.00   9.60   ? 191 TYR A CA  1 
ATOM   1651 C  C   . TYR A 1 190 ? -17.796 -4.295  28.365  1.00   9.13   ? 191 TYR A C   1 
ATOM   1652 O  O   . TYR A 1 190 ? -18.228 -4.164  29.528  1.00   9.62   ? 191 TYR A O   1 
ATOM   1653 C  CB  . TYR A 1 190 ? -18.500 -2.863  26.480  1.00   9.85   ? 191 TYR A CB  1 
ATOM   1654 C  CG  . TYR A 1 190 ? -18.920 -1.701  27.305  1.00   9.63   ? 191 TYR A CG  1 
ATOM   1655 C  CD1 . TYR A 1 190 ? -17.977 -1.088  28.168  1.00   10.35  ? 191 TYR A CD1 1 
ATOM   1656 C  CD2 . TYR A 1 190 ? -20.204 -1.173  27.267  1.00   10.72  ? 191 TYR A CD2 1 
ATOM   1657 C  CE1 . TYR A 1 190 ? -18.356 -0.038  28.983  1.00   11.36  ? 191 TYR A CE1 1 
ATOM   1658 C  CE2 . TYR A 1 190 ? -20.595 -0.098  28.077  1.00   11.47  ? 191 TYR A CE2 1 
ATOM   1659 C  CZ  . TYR A 1 190 ? -19.684 0.460   28.943  1.00   11.50  ? 191 TYR A CZ  1 
ATOM   1660 O  OH  . TYR A 1 190 ? -20.015 1.466   29.779  1.00   12.85  ? 191 TYR A OH  1 
ATOM   1661 N  N   . TRP A 1 191 ? -16.499 -4.421  28.074  1.00   8.26   ? 192 TRP A N   1 
ATOM   1662 C  CA  . TRP A 1 191 ? -15.395 -4.150  29.023  1.00   8.36   ? 192 TRP A CA  1 
ATOM   1663 C  C   . TRP A 1 191 ? -14.693 -2.881  28.592  1.00   7.94   ? 192 TRP A C   1 
ATOM   1664 O  O   . TRP A 1 191 ? -14.634 -2.541  27.411  1.00   8.87   ? 192 TRP A O   1 
ATOM   1665 C  CB  . TRP A 1 191 ? -14.367 -5.268  29.012  1.00   8.70   ? 192 TRP A CB  1 
ATOM   1666 C  CG  . TRP A 1 191 ? -14.898 -6.613  29.425  1.00   8.56   ? 192 TRP A CG  1 
ATOM   1667 C  CD1 . TRP A 1 191 ? -15.122 -7.033  30.718  1.00   10.83  ? 192 TRP A CD1 1 
ATOM   1668 C  CD2 . TRP A 1 191 ? -15.166 -7.729  28.579  1.00   9.00   ? 192 TRP A CD2 1 
ATOM   1669 N  NE1 . TRP A 1 191 ? -15.532 -8.345  30.699  1.00   11.31  ? 192 TRP A NE1 1 
ATOM   1670 C  CE2 . TRP A 1 191 ? -15.590 -8.782  29.419  1.00   10.57  ? 192 TRP A CE2 1 
ATOM   1671 C  CE3 . TRP A 1 191 ? -15.084 -7.938  27.188  1.00   9.37   ? 192 TRP A CE3 1 
ATOM   1672 C  CZ2 . TRP A 1 191 ? -15.909 -10.063 28.897  1.00   11.27  ? 192 TRP A CZ2 1 
ATOM   1673 C  CZ3 . TRP A 1 191 ? -15.361 -9.202  26.721  1.00   11.08  ? 192 TRP A CZ3 1 
ATOM   1674 C  CH2 . TRP A 1 191 ? -15.757 -10.238 27.563  1.00   11.92  ? 192 TRP A CH2 1 
ATOM   1675 N  N   . THR A 1 192 ? -14.130 -2.150  29.534  1.00   7.84   ? 193 THR A N   1 
ATOM   1676 C  CA  . THR A 1 192 ? -13.393 -0.927  29.196  1.00   8.21   ? 193 THR A CA  1 
ATOM   1677 C  C   . THR A 1 192 ? -12.168 -0.794  30.071  1.00   7.56   ? 193 THR A C   1 
ATOM   1678 O  O   . THR A 1 192 ? -12.146 -1.150  31.241  1.00   8.66   ? 193 THR A O   1 
ATOM   1679 C  CB  . THR A 1 192 ? -14.337 0.263   29.315  1.00   8.82   ? 193 THR A CB  1 
ATOM   1680 O  OG1 . THR A 1 192 ? -13.648 1.474   28.894  1.00   9.01   ? 193 THR A OG1 1 
ATOM   1681 C  CG2 . THR A 1 192 ? -14.867 0.499   30.715  1.00   10.12  ? 193 THR A CG2 1 
ATOM   1682 N  N   . TYR A 1 193 ? -11.122 -0.172  29.485  1.00   7.82   ? 194 TYR A N   1 
ATOM   1683 C  CA  . TYR A 1 193 ? -9.882  0.115   30.190  1.00   8.26   ? 194 TYR A CA  1 
ATOM   1684 C  C   . TYR A 1 193 ? -9.149  1.186   29.411  1.00   7.56   ? 194 TYR A C   1 
ATOM   1685 O  O   . TYR A 1 193 ? -9.340  1.359   28.220  1.00   7.88   ? 194 TYR A O   1 
ATOM   1686 C  CB  . TYR A 1 193 ? -9.061  -1.178  30.379  1.00   8.54   ? 194 TYR A CB  1 
ATOM   1687 C  CG  . TYR A 1 193 ? -8.369  -1.652  29.127  1.00   8.31   ? 194 TYR A CG  1 
ATOM   1688 C  CD1 . TYR A 1 193 ? -9.038  -2.358  28.162  1.00   7.93   ? 194 TYR A CD1 1 
ATOM   1689 C  CD2 . TYR A 1 193 ? -7.029  -1.302  28.891  1.00   8.48   ? 194 TYR A CD2 1 
ATOM   1690 C  CE1 . TYR A 1 193 ? -8.420  -2.711  26.950  1.00   7.99   ? 194 TYR A CE1 1 
ATOM   1691 C  CE2 . TYR A 1 193 ? -6.423  -1.626  27.695  1.00   8.24   ? 194 TYR A CE2 1 
ATOM   1692 C  CZ  . TYR A 1 193 ? -7.104  -2.329  26.718  1.00   7.64   ? 194 TYR A CZ  1 
ATOM   1693 O  OH  . TYR A 1 193 ? -6.456  -2.610  25.550  1.00   8.10   ? 194 TYR A OH  1 
ATOM   1694 N  N   . PRO A 1 194 ? -8.177  1.859   30.060  1.00   8.02   ? 195 PRO A N   1 
ATOM   1695 C  CA  . PRO A 1 194 ? -7.360  2.887   29.368  1.00   8.61   ? 195 PRO A CA  1 
ATOM   1696 C  C   . PRO A 1 194 ? -6.161  2.216   28.697  1.00   7.46   ? 195 PRO A C   1 
ATOM   1697 O  O   . PRO A 1 194 ? -5.417  1.443   29.346  1.00   8.61   ? 195 PRO A O   1 
ATOM   1698 C  CB  . PRO A 1 194 ? -6.895  3.786   30.512  1.00   9.93   ? 195 PRO A CB  1 
ATOM   1699 C  CG  . PRO A 1 194 ? -6.842  2.847   31.705  1.00   10.95  ? 195 PRO A CG  1 
ATOM   1700 C  CD  . PRO A 1 194 ? -7.962  1.884   31.527  1.00   10.00  ? 195 PRO A CD  1 
ATOM   1701 N  N   . GLY A 1 195 ? -5.933  2.522   27.434  1.00   7.69   ? 196 GLY A N   1 
ATOM   1702 C  CA  . GLY A 1 195 ? -4.812  1.913   26.713  1.00   8.02   ? 196 GLY A CA  1 
ATOM   1703 C  C   . GLY A 1 195 ? -4.283  2.770   25.607  1.00   7.15   ? 196 GLY A C   1 
ATOM   1704 O  O   . GLY A 1 195 ? -4.188  4.015   25.752  1.00   7.81   ? 196 GLY A O   1 
ATOM   1705 N  N   . SER A 1 196 ? -3.859  2.112   24.550  1.00   7.30   ? 197 SER A N   1 
ATOM   1706 C  CA  . SER A 1 196 ? -3.046  2.765   23.508  1.00   7.46   ? 197 SER A CA  1 
ATOM   1707 C  C   . SER A 1 196 ? -3.496  2.349   22.136  1.00   7.11   ? 197 SER A C   1 
ATOM   1708 O  O   . SER A 1 196 ? -4.265  1.380   21.948  1.00   7.46   ? 197 SER A O   1 
ATOM   1709 C  CB  . SER A 1 196 ? -1.574  2.363   23.685  1.00   8.00   ? 197 SER A CB  1 
ATOM   1710 O  OG  . SER A 1 196 ? -1.319  1.026   23.250  1.00   7.89   ? 197 SER A OG  1 
ATOM   1711 N  N   . LEU A 1 197 ? -2.951  3.033   21.133  1.00   7.31   ? 198 LEU A N   1 
ATOM   1712 C  CA  . LEU A 1 197 ? -2.968  2.505   19.775  1.00   7.71   ? 198 LEU A CA  1 
ATOM   1713 C  C   . LEU A 1 197 ? -2.235  1.183   19.784  1.00   7.71   ? 198 LEU A C   1 
ATOM   1714 O  O   . LEU A 1 197 ? -1.200  1.022   20.474  1.00   8.33   ? 198 LEU A O   1 
ATOM   1715 C  CB  . LEU A 1 197 ? -2.235  3.441   18.806  1.00   8.26   ? 198 LEU A CB  1 
ATOM   1716 C  CG  . LEU A 1 197 ? -2.713  4.892   18.777  1.00   8.78   ? 198 LEU A CG  1 
ATOM   1717 C  CD1 . LEU A 1 197 ? -1.879  5.676   17.743  1.00   10.27  ? 198 LEU A CD1 1 
ATOM   1718 C  CD2 . LEU A 1 197 ? -4.166  5.004   18.463  1.00   9.74   ? 198 LEU A CD2 1 
ATOM   1719 N  N   . THR A 1 198 ? -2.667  0.216   18.965  1.00   7.43   ? 199 THR A N   1 
ATOM   1720 C  CA  . THR A 1 198 ? -2.010  -1.068  18.891  1.00   8.17   ? 199 THR A CA  1 
ATOM   1721 C  C   . THR A 1 198 ? -0.995  -1.170  17.733  1.00   8.00   ? 199 THR A C   1 
ATOM   1722 O  O   . THR A 1 198 ? -0.403  -2.260  17.567  1.00   9.02   ? 199 THR A O   1 
ATOM   1723 C  CB  . THR A 1 198 ? -3.010  -2.216  18.797  1.00   7.98   ? 199 THR A CB  1 
ATOM   1724 O  OG1 . THR A 1 198 ? -3.615  -2.181  17.521  1.00   7.97   ? 199 THR A OG1 1 
ATOM   1725 C  CG2 . THR A 1 198 ? -4.038  -2.219  19.944  1.00   8.59   ? 199 THR A CG2 1 
ATOM   1726 N  N   . THR A 1 199 ? -0.828  -0.125  16.975  1.00   9.00   ? 200 THR A N   1 
ATOM   1727 C  CA  . THR A 1 199 ? 0.210   -0.011  15.959  1.00   8.90   ? 200 THR A CA  1 
ATOM   1728 C  C   . THR A 1 199 ? 1.015   1.224   16.256  1.00   9.35   ? 200 THR A C   1 
ATOM   1729 O  O   . THR A 1 199 ? 0.549   2.182   16.836  1.00   9.73   ? 200 THR A O   1 
ATOM   1730 C  CB  . THR A 1 199 ? -0.349  0.051   14.524  1.00   9.34   ? 200 THR A CB  1 
ATOM   1731 O  OG1 . THR A 1 199 ? -1.404  1.032   14.447  1.00   11.06  ? 200 THR A OG1 1 
ATOM   1732 C  CG2 . THR A 1 199 ? -0.930  -1.271  14.127  1.00   11.40  ? 200 THR A CG2 1 
ATOM   1733 N  N   . PRO A 1 200 ? 2.313   1.218   15.818  1.00   10.36  ? 201 PRO A N   1 
ATOM   1734 C  CA  . PRO A 1 200 ? 3.112   2.432   15.903  1.00   10.96  ? 201 PRO A CA  1 
ATOM   1735 C  C   . PRO A 1 200 ? 2.327   3.605   15.376  1.00   11.26  ? 201 PRO A C   1 
ATOM   1736 O  O   . PRO A 1 200 ? 1.727   3.509   14.286  1.00   13.46  ? 201 PRO A O   1 
ATOM   1737 C  CB  . PRO A 1 200 ? 4.344   2.056   15.059  1.00   12.53  ? 201 PRO A CB  1 
ATOM   1738 C  CG  . PRO A 1 200 ? 4.489   0.608   15.308  1.00   12.51  ? 201 PRO A CG  1 
ATOM   1739 C  CD  . PRO A 1 200 ? 3.082   0.094   15.228  1.00   11.01  ? 201 PRO A CD  1 
ATOM   1740 N  N   . PRO A 1 201 ? 2.351   4.741   16.052  1.00   11.21  ? 202 PRO A N   1 
ATOM   1741 C  CA  . PRO A 1 201 ? 3.262   5.127   17.161  1.00   11.02  ? 202 PRO A CA  1 
ATOM   1742 C  C   . PRO A 1 201 ? 2.836   4.697   18.580  1.00   10.71  ? 202 PRO A C   1 
ATOM   1743 O  O   . PRO A 1 201 ? 3.504   5.139   19.540  1.00   11.21  ? 202 PRO A O   1 
ATOM   1744 C  CB  . PRO A 1 201 ? 3.297   6.666   17.042  1.00   14.04  ? 202 PRO A CB  1 
ATOM   1745 C  CG  . PRO A 1 201 ? 1.903   6.998   16.534  1.00   15.56  ? 202 PRO A CG  1 
ATOM   1746 C  CD  . PRO A 1 201 ? 1.616   5.922   15.513  1.00   13.22  ? 202 PRO A CD  1 
ATOM   1747 N  N   . LEU A 1 202 ? 1.806   3.855   18.732  1.00   9.33   ? 203 LEU A N   1 
ATOM   1748 C  CA  . LEU A 1 202 ? 1.554   3.218   20.039  1.00   9.24   ? 203 LEU A CA  1 
ATOM   1749 C  C   . LEU A 1 202 ? 1.166   4.241   21.111  1.00   9.07   ? 203 LEU A C   1 
ATOM   1750 O  O   . LEU A 1 202 ? 1.323   4.016   22.308  1.00   8.82   ? 203 LEU A O   1 
ATOM   1751 C  CB  . LEU A 1 202 ? 2.706   2.335   20.516  1.00   9.46   ? 203 LEU A CB  1 
ATOM   1752 C  CG  . LEU A 1 202 ? 3.063   1.197   19.530  1.00   9.49   ? 203 LEU A CG  1 
ATOM   1753 C  CD1 . LEU A 1 202 ? 4.321   0.533   20.043  1.00   11.55  ? 203 LEU A CD1 1 
ATOM   1754 C  CD2 . LEU A 1 202 ? 1.965   0.168   19.427  1.00   10.68  ? 203 LEU A CD2 1 
ATOM   1755 N  N   . LEU A 1 203 ? 0.577   5.362   20.691  1.00   9.27   ? 204 LEU A N   1 
ATOM   1756 C  CA  . LEU A 1 203 ? 0.296   6.475   21.591  1.00   9.46   ? 204 LEU A CA  1 
ATOM   1757 C  C   . LEU A 1 203 ? -0.732  6.062   22.607  1.00   9.16   ? 204 LEU A C   1 
ATOM   1758 O  O   . LEU A 1 203 ? -1.719  5.344   22.337  1.00   8.76   ? 204 LEU A O   1 
ATOM   1759 C  CB  . LEU A 1 203 ? -0.216  7.686   20.802  1.00   11.05  ? 204 LEU A CB  1 
ATOM   1760 C  CG  . LEU A 1 203 ? 0.820   8.270   19.841  1.00   12.89  ? 204 LEU A CG  1 
ATOM   1761 C  CD1 . LEU A 1 203 ? 0.160   9.283   18.912  1.00   15.06  ? 204 LEU A CD1 1 
ATOM   1762 C  CD2 . LEU A 1 203 ? 2.046   8.856   20.614  1.00   18.70  ? 204 LEU A CD2 1 
ATOM   1763 N  N   . GLU A 1 204 ? -0.556  6.545   23.842  1.00   9.81   ? 205 GLU A N   1 
ATOM   1764 C  CA  . GLU A 1 204 ? -1.391  6.193   24.997  1.00   9.73   ? 205 GLU A CA  1 
ATOM   1765 C  C   . GLU A 1 204 ? -2.570  7.169   25.132  1.00   9.41   ? 205 GLU A C   1 
ATOM   1766 O  O   . GLU A 1 204 ? -2.675  7.932   26.063  1.00   11.96  ? 205 GLU A O   1 
ATOM   1767 C  CB  . GLU A 1 204 ? -0.527  6.073   26.261  1.00   11.20  ? 205 GLU A CB  1 
ATOM   1768 C  CG  . GLU A 1 204 ? 0.343   4.819   26.149  1.00   11.70  ? 205 GLU A CG  1 
ATOM   1769 C  CD  . GLU A 1 204 ? 1.292   4.549   27.315  1.00   11.55  ? 205 GLU A CD  1 
ATOM   1770 O  OE1 . GLU A 1 204 ? 1.602   5.503   28.090  1.00   14.47  ? 205 GLU A OE1 1 
ATOM   1771 O  OE2 . GLU A 1 204 ? 1.683   3.369   27.474  1.00   11.98  ? 205 GLU A OE2 1 
ATOM   1772 N  N   . CYS A 1 205 ? -3.489  7.043   24.201  1.00   8.67   ? 206 CYS A N   1 
ATOM   1773 C  CA  . CYS A 1 205 ? -4.542  8.036   23.982  1.00   8.77   ? 206 CYS A CA  1 
ATOM   1774 C  C   . CYS A 1 205 ? -5.895  7.394   23.873  1.00   8.52   ? 206 CYS A C   1 
ATOM   1775 O  O   . CYS A 1 205 ? -6.853  8.098   23.533  1.00   10.26  ? 206 CYS A O   1 
ATOM   1776 C  CB  . CYS A 1 205 ? -4.243  8.854   22.729  1.00   9.75   ? 206 CYS A CB  1 
ATOM   1777 S  SG  . CYS A 1 205 ? -4.215  7.854   21.189  1.00   10.47  ? 206 CYS A SG  1 
ATOM   1778 N  N   . VAL A 1 206 ? -6.039  6.107   24.174  1.00   7.91   ? 207 VAL A N   1 
ATOM   1779 C  CA  . VAL A 1 206 ? -7.294  5.408   23.835  1.00   7.69   ? 207 VAL A CA  1 
ATOM   1780 C  C   . VAL A 1 206 ? -8.039  4.972   25.080  1.00   7.64   ? 207 VAL A C   1 
ATOM   1781 O  O   . VAL A 1 206 ? -7.488  4.311   25.957  1.00   8.99   ? 207 VAL A O   1 
ATOM   1782 C  CB  . VAL A 1 206 ? -7.005  4.152   22.989  1.00   8.20   ? 207 VAL A CB  1 
ATOM   1783 C  CG1 . VAL A 1 206 ? -8.311  3.430   22.663  1.00   8.53   ? 207 VAL A CG1 1 
ATOM   1784 C  CG2 . VAL A 1 206 ? -6.250  4.506   21.718  1.00   9.37   ? 207 VAL A CG2 1 
ATOM   1785 N  N   . THR A 1 207 ? -9.354  5.262   25.119  1.00   7.29   ? 208 THR A N   1 
ATOM   1786 C  CA  . THR A 1 207 ? -10.291 4.542   25.997  1.00   8.07   ? 208 THR A CA  1 
ATOM   1787 C  C   . THR A 1 207 ? -10.822 3.355   25.167  1.00   7.25   ? 208 THR A C   1 
ATOM   1788 O  O   . THR A 1 207 ? -11.484 3.559   24.144  1.00   8.07   ? 208 THR A O   1 
ATOM   1789 C  CB  . THR A 1 207 ? -11.450 5.407   26.438  1.00   8.61   ? 208 THR A CB  1 
ATOM   1790 O  OG1 . THR A 1 207 ? -10.952 6.538   27.173  1.00   9.62   ? 208 THR A OG1 1 
ATOM   1791 C  CG2 . THR A 1 207 ? -12.390 4.604   27.339  1.00   10.12  ? 208 THR A CG2 1 
ATOM   1792 N  N   . TRP A 1 208 ? -10.442 2.147   25.570  1.00   6.82   ? 209 TRP A N   1 
ATOM   1793 C  CA  . TRP A 1 208 ? -10.874 0.959   24.884  1.00   7.00   ? 209 TRP A CA  1 
ATOM   1794 C  C   . TRP A 1 208 ? -12.255 0.533   25.396  1.00   6.64   ? 209 TRP A C   1 
ATOM   1795 O  O   . TRP A 1 208 ? -12.474 0.489   26.612  1.00   7.45   ? 209 TRP A O   1 
ATOM   1796 C  CB  . TRP A 1 208 ? -9.853  -0.187  25.086  1.00   7.17   ? 209 TRP A CB  1 
ATOM   1797 C  CG  . TRP A 1 208 ? -8.746  -0.084  24.107  1.00   7.03   ? 209 TRP A CG  1 
ATOM   1798 C  CD1 . TRP A 1 208 ? -7.505  0.509   24.269  1.00   7.63   ? 209 TRP A CD1 1 
ATOM   1799 C  CD2 . TRP A 1 208 ? -8.829  -0.475  22.736  1.00   6.73   ? 209 TRP A CD2 1 
ATOM   1800 N  NE1 . TRP A 1 208 ? -6.840  0.493   23.087  1.00   7.77   ? 209 TRP A NE1 1 
ATOM   1801 C  CE2 . TRP A 1 208 ? -7.568  -0.104  22.118  1.00   7.39   ? 209 TRP A CE2 1 
ATOM   1802 C  CE3 . TRP A 1 208 ? -9.785  -1.126  21.961  1.00   6.90   ? 209 TRP A CE3 1 
ATOM   1803 C  CZ2 . TRP A 1 208 ? -7.298  -0.344  20.770  1.00   7.95   ? 209 TRP A CZ2 1 
ATOM   1804 C  CZ3 . TRP A 1 208 ? -9.510  -1.392  20.644  1.00   8.39   ? 209 TRP A CZ3 1 
ATOM   1805 C  CH2 . TRP A 1 208 ? -8.302  -0.996  20.057  1.00   8.82   ? 209 TRP A CH2 1 
ATOM   1806 N  N   . ILE A 1 209 ? -13.106 0.180   24.478  1.00   6.92   ? 210 ILE A N   1 
ATOM   1807 C  CA  . ILE A 1 209 ? -14.465 -0.350  24.775  1.00   7.38   ? 210 ILE A CA  1 
ATOM   1808 C  C   . ILE A 1 209 ? -14.570 -1.622  23.958  1.00   6.72   ? 210 ILE A C   1 
ATOM   1809 O  O   . ILE A 1 209 ? -14.639 -1.538  22.724  1.00   8.41   ? 210 ILE A O   1 
ATOM   1810 C  CB  . ILE A 1 209 ? -15.537 0.654   24.428  1.00   7.93   ? 210 ILE A CB  1 
ATOM   1811 C  CG1 . ILE A 1 209 ? -15.337 1.950   25.246  1.00   9.92   ? 210 ILE A CG1 1 
ATOM   1812 C  CG2 . ILE A 1 209 ? -16.910 0.056   24.646  1.00   9.90   ? 210 ILE A CG2 1 
ATOM   1813 C  CD1 . ILE A 1 209 ? -16.150 3.133   24.718  1.00   11.91  ? 210 ILE A CD1 1 
ATOM   1814 N  N   . VAL A 1 210 ? -14.502 -2.774  24.596  1.00   7.07   ? 211 VAL A N   1 
ATOM   1815 C  CA  . VAL A 1 210 ? -14.461 -4.069  23.889  1.00   6.94   ? 211 VAL A CA  1 
ATOM   1816 C  C   . VAL A 1 210 ? -15.765 -4.763  24.146  1.00   7.00   ? 211 VAL A C   1 
ATOM   1817 O  O   . VAL A 1 210 ? -16.108 -5.054  25.299  1.00   8.02   ? 211 VAL A O   1 
ATOM   1818 C  CB  . VAL A 1 210 ? -13.264 -4.907  24.342  1.00   8.09   ? 211 VAL A CB  1 
ATOM   1819 C  CG1 . VAL A 1 210 ? -13.277 -6.265  23.639  1.00   9.17   ? 211 VAL A CG1 1 
ATOM   1820 C  CG2 . VAL A 1 210 ? -11.956 -4.149  24.044  1.00   9.19   ? 211 VAL A CG2 1 
ATOM   1821 N  N   . LEU A 1 211 ? -16.533 -5.037  23.094  1.00   8.01   ? 212 LEU A N   1 
ATOM   1822 C  CA  . LEU A 1 211 ? -17.835 -5.703  23.266  1.00   8.39   ? 212 LEU A CA  1 
ATOM   1823 C  C   . LEU A 1 211 ? -17.648 -7.160  23.628  1.00   7.99   ? 212 LEU A C   1 
ATOM   1824 O  O   . LEU A 1 211 ? -16.797 -7.873  23.091  1.00   9.07   ? 212 LEU A O   1 
ATOM   1825 C  CB  . LEU A 1 211 ? -18.654 -5.574  21.999  1.00   9.16   ? 212 LEU A CB  1 
ATOM   1826 C  CG  . LEU A 1 211 ? -19.032 -4.167  21.591  1.00   9.90   ? 212 LEU A CG  1 
ATOM   1827 C  CD1 . LEU A 1 211 ? -20.064 -4.254  20.444  1.00   12.35  ? 212 LEU A CD1 1 
ATOM   1828 C  CD2 . LEU A 1 211 ? -19.554 -3.335  22.722  1.00   11.41  ? 212 LEU A CD2 1 
ATOM   1829 N  N   . LYS A 1 212 ? -18.507 -7.657  24.551  1.00   9.00   ? 213 LYS A N   1 
ATOM   1830 C  CA  . LYS A 1 212 ? -18.449 -9.047  24.896  1.00   9.91   ? 213 LYS A CA  1 
ATOM   1831 C  C   . LYS A 1 212 ? -18.940 -9.969  23.822  1.00   9.22   ? 213 LYS A C   1 
ATOM   1832 O  O   . LYS A 1 212 ? -18.403 -11.088 23.667  1.00   11.53  ? 213 LYS A O   1 
ATOM   1833 C  CB  . LYS A 1 212 ? -19.213 -9.256  26.198  1.00   12.53  ? 213 LYS A CB  1 
ATOM   1834 C  CG  . LYS A 1 212 ? -19.317 -10.729 26.625  1.00   14.78  ? 213 LYS A CG  1 
ATOM   1835 C  CD  . LYS A 1 212 ? -20.038 -10.881 27.961  1.00   24.58  ? 213 LYS A CD  1 
ATOM   1836 C  CE  . LYS A 1 212 ? -20.423 -12.242 28.338  1.00   29.62  ? 213 LYS A CE  1 
ATOM   1837 N  NZ  . LYS A 1 212 ? -21.245 -12.256 29.603  0.0000 40.75  ? 213 LYS A NZ  1 
ATOM   1838 N  N   . GLU A 1 213 ? -19.983 -9.607  23.092  1.00   9.50   ? 214 GLU A N   1 
ATOM   1839 C  CA  . GLU A 1 213 ? -20.579 -10.495 22.090  1.00   9.85   ? 214 GLU A CA  1 
ATOM   1840 C  C   . GLU A 1 213 ? -19.813 -10.373 20.783  1.00   9.07   ? 214 GLU A C   1 
ATOM   1841 O  O   . GLU A 1 213 ? -19.746 -9.298  20.209  1.00   9.27   ? 214 GLU A O   1 
ATOM   1842 C  CB  . GLU A 1 213 ? -22.038 -10.118 21.883  1.00   10.59  ? 214 GLU A CB  1 
ATOM   1843 C  CG  . GLU A 1 213 ? -22.729 -11.068 20.939  1.00   13.48  ? 214 GLU A CG  1 
ATOM   1844 C  CD  . GLU A 1 213 ? -24.155 -10.860 20.761  1.00   16.60  ? 214 GLU A CD  1 
ATOM   1845 O  OE1 . GLU A 1 213 ? -24.802 -9.962  21.320  1.00   16.57  ? 214 GLU A OE1 1 
ATOM   1846 O  OE2 . GLU A 1 213 ? -24.719 -11.864 20.122  1.00   27.14  ? 214 GLU A OE2 1 
ATOM   1847 N  N   A PRO A 1 214 ? -19.261 -11.488 20.253  0.50   9.20   ? 215 PRO A N   1 
ATOM   1848 N  N   B PRO A 1 214 ? -19.281 -11.508 20.302  0.50   9.61   ? 215 PRO A N   1 
ATOM   1849 C  CA  A PRO A 1 214 ? -18.639 -11.416 18.946  0.50   9.40   ? 215 PRO A CA  1 
ATOM   1850 C  CA  B PRO A 1 214 ? -18.621 -11.464 19.001  0.50   10.05  ? 215 PRO A CA  1 
ATOM   1851 C  C   A PRO A 1 214 ? -19.695 -11.306 17.878  0.50   9.36   ? 215 PRO A C   1 
ATOM   1852 C  C   B PRO A 1 214 ? -19.598 -11.496 17.836  0.50   10.03  ? 215 PRO A C   1 
ATOM   1853 O  O   A PRO A 1 214 ? -20.902 -11.572 18.130  0.50   10.28  ? 215 PRO A O   1 
ATOM   1854 O  O   B PRO A 1 214 ? -20.689 -12.021 17.975  0.50   11.03  ? 215 PRO A O   1 
ATOM   1855 C  CB  A PRO A 1 214 ? -17.944 -12.767 18.817  0.50   9.47   ? 215 PRO A CB  1 
ATOM   1856 C  CB  B PRO A 1 214 ? -17.795 -12.747 18.978  0.50   11.55  ? 215 PRO A CB  1 
ATOM   1857 C  CG  A PRO A 1 214 ? -18.730 -13.712 19.670  0.50   10.07  ? 215 PRO A CG  1 
ATOM   1858 C  CG  B PRO A 1 214 ? -17.859 -13.319 20.332  0.50   16.31  ? 215 PRO A CG  1 
ATOM   1859 C  CD  A PRO A 1 214 ? -19.368 -12.879 20.750  0.50   10.50  ? 215 PRO A CD  1 
ATOM   1860 C  CD  B PRO A 1 214 ? -19.024 -12.770 21.036  0.50   11.33  ? 215 PRO A CD  1 
ATOM   1861 N  N   . ILE A 1 215 ? -19.250 -10.953 16.697  1.00   9.60   ? 216 ILE A N   1 
ATOM   1862 C  CA  . ILE A 1 215 ? -20.023 -11.174 15.470  1.00   10.51  ? 216 ILE A CA  1 
ATOM   1863 C  C   . ILE A 1 215 ? -19.504 -12.409 14.770  1.00   10.16  ? 216 ILE A C   1 
ATOM   1864 O  O   . ILE A 1 215 ? -18.326 -12.770 14.899  1.00   11.00  ? 216 ILE A O   1 
ATOM   1865 C  CB  . ILE A 1 215 ? -20.032 -9.955  14.562  1.00   11.08  ? 216 ILE A CB  1 
ATOM   1866 C  CG1 . ILE A 1 215 ? -18.655 -9.591  14.045  1.00   12.17  ? 216 ILE A CG1 1 
ATOM   1867 C  CG2 . ILE A 1 215 ? -20.728 -8.764  15.226  1.00   12.56  ? 216 ILE A CG2 1 
ATOM   1868 C  CD1 . ILE A 1 215 ? -18.653 -8.592  12.874  1.00   14.23  ? 216 ILE A CD1 1 
ATOM   1869 N  N   A SER A 1 216 ? -20.396 -13.183 14.182  0.50   9.88   ? 217 SER A N   1 
ATOM   1870 N  N   B SER A 1 216 ? -20.341 -12.959 13.875  0.50   10.52  ? 217 SER A N   1 
ATOM   1871 C  CA  A SER A 1 216 ? -19.862 -14.261 13.342  0.50   11.98  ? 217 SER A CA  1 
ATOM   1872 C  CA  B SER A 1 216 ? -20.034 -14.163 13.109  0.50   9.85   ? 217 SER A CA  1 
ATOM   1873 C  C   A SER A 1 216 ? -19.820 -13.841 11.880  0.50   11.61  ? 217 SER A C   1 
ATOM   1874 C  C   B SER A 1 216 ? -19.777 -13.712 11.710  0.50   10.04  ? 217 SER A C   1 
ATOM   1875 O  O   A SER A 1 216 ? -20.772 -13.160 11.408  0.50   11.43  ? 217 SER A O   1 
ATOM   1876 O  O   B SER A 1 216 ? -20.488 -12.937 11.077  0.50   10.29  ? 217 SER A O   1 
ATOM   1877 C  CB  A SER A 1 216 ? -20.779 -15.447 13.570  0.50   15.16  ? 217 SER A CB  1 
ATOM   1878 C  CB  B SER A 1 216 ? -21.231 -15.198 13.191  0.50   11.05  ? 217 SER A CB  1 
ATOM   1879 O  OG  A SER A 1 216 ? -20.741 -16.371 12.546  0.50   19.49  ? 217 SER A OG  1 
ATOM   1880 O  OG  B SER A 1 216 ? -21.153 -15.959 14.437  0.50   13.19  ? 217 SER A OG  1 
ATOM   1881 N  N   . VAL A 1 217 ? -18.710 -14.234 11.183  1.00   10.94  ? 218 VAL A N   1 
ATOM   1882 C  CA  . VAL A 1 217 ? -18.453 -14.041 9.758   1.00   11.30  ? 218 VAL A CA  1 
ATOM   1883 C  C   . VAL A 1 217 ? -18.170 -15.390 9.161   1.00   10.92  ? 218 VAL A C   1 
ATOM   1884 O  O   . VAL A 1 217 ? -17.816 -16.341 9.887   1.00   11.64  ? 218 VAL A O   1 
ATOM   1885 C  CB  . VAL A 1 217 ? -17.217 -13.091 9.541   1.00   11.64  ? 218 VAL A CB  1 
ATOM   1886 C  CG1 . VAL A 1 217 ? -17.501 -11.765 10.191  1.00   13.73  ? 218 VAL A CG1 1 
ATOM   1887 C  CG2 . VAL A 1 217 ? -15.950 -13.710 10.009  1.00   13.16  ? 218 VAL A CG2 1 
ATOM   1888 N  N   . SER A 1 218 ? -18.324 -15.543 7.862   1.00   11.10  ? 219 SER A N   1 
ATOM   1889 C  CA  . SER A 1 218 ? -18.103 -16.858 7.315   1.00   11.82  ? 219 SER A CA  1 
ATOM   1890 C  C   . SER A 1 218 ? -16.624 -17.124 7.041   1.00   11.61  ? 219 SER A C   1 
ATOM   1891 O  O   . SER A 1 218 ? -15.818 -16.197 6.886   1.00   12.30  ? 219 SER A O   1 
ATOM   1892 C  CB  . SER A 1 218 ? -18.912 -17.072 6.045   1.00   12.31  ? 219 SER A CB  1 
ATOM   1893 O  OG  . SER A 1 218 ? -18.402 -16.216 5.040   1.00   13.72  ? 219 SER A OG  1 
ATOM   1894 N  N   A SER A 1 219 ? -16.246 -18.396 6.821   0.50   12.42  ? 220 SER A N   1 
ATOM   1895 N  N   B SER A 1 219 ? -16.344 -18.394 6.988   0.50   12.33  ? 220 SER A N   1 
ATOM   1896 C  CA  A SER A 1 219 ? -14.838 -18.759 6.433   0.50   13.89  ? 220 SER A CA  1 
ATOM   1897 C  CA  B SER A 1 219 ? -15.025 -18.770 6.634   0.50   12.32  ? 220 SER A CA  1 
ATOM   1898 C  C   A SER A 1 219 ? -14.491 -18.065 5.141   0.50   14.20  ? 220 SER A C   1 
ATOM   1899 C  C   B SER A 1 219 ? -14.595 -18.085 5.305   0.50   12.90  ? 220 SER A C   1 
ATOM   1900 O  O   A SER A 1 219 ? -13.378 -17.596 4.894   0.50   14.86  ? 220 SER A O   1 
ATOM   1901 O  O   B SER A 1 219 ? -13.451 -17.642 5.215   0.50   13.16  ? 220 SER A O   1 
ATOM   1902 C  CB  A SER A 1 219 ? -14.697 -20.265 6.248   0.50   16.12  ? 220 SER A CB  1 
ATOM   1903 C  CB  B SER A 1 219 ? -14.912 -20.277 6.621   0.50   12.94  ? 220 SER A CB  1 
ATOM   1904 O  OG  A SER A 1 219 ? -15.761 -20.864 5.547   0.50   17.29  ? 220 SER A OG  1 
ATOM   1905 O  OG  B SER A 1 219 ? -13.558 -20.658 6.243   0.50   14.19  ? 220 SER A OG  1 
ATOM   1906 N  N   . GLU A 1 220 ? -15.449 -18.036 4.261   1.00   12.80  ? 221 GLU A N   1 
ATOM   1907 C  CA  . GLU A 1 220 ? -15.178 -17.386 2.968   1.00   15.09  ? 221 GLU A CA  1 
ATOM   1908 C  C   . GLU A 1 220 ? -14.891 -15.896 3.123   1.00   13.95  ? 221 GLU A C   1 
ATOM   1909 O  O   . GLU A 1 220 ? -14.017 -15.351 2.398   1.00   14.99  ? 221 GLU A O   1 
ATOM   1910 C  CB  . GLU A 1 220 ? -16.270 -17.594 1.989   1.00   18.49  ? 221 GLU A CB  1 
ATOM   1911 C  CG  . GLU A 1 220 ? -16.457 -19.043 1.566   1.00   23.98  ? 221 GLU A CG  1 
ATOM   1912 C  CD  . GLU A 1 220 ? -17.354 -19.818 2.513   1.00   24.85  ? 221 GLU A CD  1 
ATOM   1913 O  OE1 . GLU A 1 220 ? -17.794 -19.236 3.527   1.00   25.21  ? 221 GLU A OE1 1 
ATOM   1914 O  OE2 . GLU A 1 220 ? -17.618 -21.008 2.244   1.00   40.62  ? 221 GLU A OE2 1 
ATOM   1915 N  N   . GLN A 1 221 ? -15.585 -15.225 4.031   1.00   12.81  ? 222 GLN A N   1 
ATOM   1916 C  CA  . GLN A 1 221 ? -15.350 -13.798 4.245   1.00   13.11  ? 222 GLN A CA  1 
ATOM   1917 C  C   . GLN A 1 221 ? -13.916 -13.576 4.791   1.00   12.34  ? 222 GLN A C   1 
ATOM   1918 O  O   . GLN A 1 221 ? -13.190 -12.712 4.265   1.00   13.41  ? 222 GLN A O   1 
ATOM   1919 C  CB  . GLN A 1 221 ? -16.386 -13.201 5.169   1.00   11.85  ? 222 GLN A CB  1 
ATOM   1920 C  CG  . GLN A 1 221 ? -17.738 -13.129 4.492   1.00   12.91  ? 222 GLN A CG  1 
ATOM   1921 C  CD  . GLN A 1 221 ? -18.885 -12.574 5.305   1.00   11.73  ? 222 GLN A CD  1 
ATOM   1922 O  OE1 . GLN A 1 221 ? -19.038 -12.932 6.494   1.00   12.14  ? 222 GLN A OE1 1 
ATOM   1923 N  NE2 . GLN A 1 221 ? -19.677 -11.679 4.720   1.00   12.75  ? 222 GLN A NE2 1 
ATOM   1924 N  N   A VAL A 1 222 ? -13.586 -14.282 5.866   0.50   11.84  ? 223 VAL A N   1 
ATOM   1925 N  N   B VAL A 1 222 ? -13.428 -14.385 5.742   0.50   12.85  ? 223 VAL A N   1 
ATOM   1926 C  CA  A VAL A 1 222 ? -12.267 -14.074 6.434   0.50   12.40  ? 223 VAL A CA  1 
ATOM   1927 C  CA  B VAL A 1 222 ? -12.078 -14.109 6.341   0.50   13.40  ? 223 VAL A CA  1 
ATOM   1928 C  C   A VAL A 1 222 ? -11.162 -14.532 5.428   0.50   12.66  ? 223 VAL A C   1 
ATOM   1929 C  C   B VAL A 1 222 ? -11.022 -14.556 5.350   0.50   13.58  ? 223 VAL A C   1 
ATOM   1930 O  O   A VAL A 1 222 ? -10.121 -13.874 5.397   0.50   11.86  ? 223 VAL A O   1 
ATOM   1931 O  O   B VAL A 1 222 ? -9.897  -14.026 5.285   0.50   14.10  ? 223 VAL A O   1 
ATOM   1932 C  CB  A VAL A 1 222 ? -12.173 -14.598 7.871   0.50   11.58  ? 223 VAL A CB  1 
ATOM   1933 C  CB  B VAL A 1 222 ? -11.820 -14.820 7.669   0.50   15.60  ? 223 VAL A CB  1 
ATOM   1934 C  CG1 A VAL A 1 222 ? -12.086 -16.097 7.844   0.50   12.66  ? 223 VAL A CG1 1 
ATOM   1935 C  CG1 B VAL A 1 222 ? -10.466 -14.361 8.230   0.50   14.47  ? 223 VAL A CG1 1 
ATOM   1936 C  CG2 A VAL A 1 222 ? -10.982 -13.974 8.618   0.50   13.07  ? 223 VAL A CG2 1 
ATOM   1937 C  CG2 B VAL A 1 222 ? -12.888 -14.442 8.657   0.50   19.65  ? 223 VAL A CG2 1 
ATOM   1938 N  N   . LEU A 1 223 ? -11.373 -15.571 4.609   1.00   13.85  ? 224 LEU A N   1 
ATOM   1939 C  CA  . LEU A 1 223 ? -10.445 -16.014 3.596   1.00   15.54  ? 224 LEU A CA  1 
ATOM   1940 C  C   . LEU A 1 223 ? -10.120 -14.880 2.623   1.00   14.55  ? 224 LEU A C   1 
ATOM   1941 O  O   . LEU A 1 223 ? -8.946  -14.755 2.193   1.00   15.80  ? 224 LEU A O   1 
ATOM   1942 C  CB  . LEU A 1 223 ? -10.910 -17.269 2.899   1.00   17.66  ? 224 LEU A CB  1 
ATOM   1943 C  CG  . LEU A 1 223 ? -10.731 -18.566 3.715   1.00   20.28  ? 224 LEU A CG  1 
ATOM   1944 C  CD1 . LEU A 1 223 ? -11.616 -19.681 3.162   1.00   25.50  ? 224 LEU A CD1 1 
ATOM   1945 C  CD2 . LEU A 1 223 ? -9.249  -18.965 3.740   1.00   24.43  ? 224 LEU A CD2 1 
ATOM   1946 N  N   . LYS A 1 224 ? -11.105 -14.028 2.309   1.00   14.02  ? 225 LYS A N   1 
ATOM   1947 C  CA  . LYS A 1 224 ? -10.859 -12.912 1.402   1.00   14.95  ? 225 LYS A CA  1 
ATOM   1948 C  C   . LYS A 1 224 ? -10.011 -11.828 2.100   1.00   13.62  ? 225 LYS A C   1 
ATOM   1949 O  O   . LYS A 1 224 ? -9.186  -11.218 1.432   1.00   14.70  ? 225 LYS A O   1 
ATOM   1950 C  CB  . LYS A 1 224 ? -12.178 -12.377 0.839   1.00   17.58  ? 225 LYS A CB  1 
ATOM   1951 C  CG  . LYS A 1 224 ? -12.748 -13.471 -0.121  1.00   24.53  ? 225 LYS A CG  1 
ATOM   1952 C  CD  . LYS A 1 224 ? -13.863 -13.097 -1.035  1.00   25.42  ? 225 LYS A CD  1 
ATOM   1953 C  CE  . LYS A 1 224 ? -14.445 -14.314 -1.762  1.00   34.20  ? 225 LYS A CE  1 
ATOM   1954 N  NZ  . LYS A 1 224 ? -15.683 -13.897 -2.526  1.00   32.91  ? 225 LYS A NZ  1 
ATOM   1955 N  N   . PHE A 1 225 ? -10.089 -11.620 3.426   1.00   12.40  ? 226 PHE A N   1 
ATOM   1956 C  CA  . PHE A 1 225 ? -9.178  -10.719 4.088   1.00   12.37  ? 226 PHE A CA  1 
ATOM   1957 C  C   . PHE A 1 225 ? -7.725  -11.248 3.865   1.00   12.12  ? 226 PHE A C   1 
ATOM   1958 O  O   . PHE A 1 225 ? -6.786  -10.459 3.656   1.00   13.02  ? 226 PHE A O   1 
ATOM   1959 C  CB  . PHE A 1 225 ? -9.364  -10.727 5.601   1.00   12.48  ? 226 PHE A CB  1 
ATOM   1960 C  CG  . PHE A 1 225 ? -10.580 -9.995  6.134   1.00   12.33  ? 226 PHE A CG  1 
ATOM   1961 C  CD1 . PHE A 1 225 ? -11.632 -9.571  5.332   1.00   16.48  ? 226 PHE A CD1 1 
ATOM   1962 C  CD2 . PHE A 1 225 ? -10.663 -9.767  7.503   1.00   16.18  ? 226 PHE A CD2 1 
ATOM   1963 C  CE1 . PHE A 1 225 ? -12.726 -8.921  5.902   1.00   17.61  ? 226 PHE A CE1 1 
ATOM   1964 C  CE2 . PHE A 1 225 ? -11.746 -9.125  8.069   1.00   17.06  ? 226 PHE A CE2 1 
ATOM   1965 C  CZ  . PHE A 1 225 ? -12.782 -8.700  7.269   1.00   17.30  ? 226 PHE A CZ  1 
ATOM   1966 N  N   . ARG A 1 226 ? -7.553  -12.563 3.930   1.00   11.83  ? 227 ARG A N   1 
ATOM   1967 C  CA  . ARG A 1 226 ? -6.251  -13.134 3.908   1.00   12.76  ? 227 ARG A CA  1 
ATOM   1968 C  C   . ARG A 1 226 ? -5.639  -13.163 2.486   1.00   13.11  ? 227 ARG A C   1 
ATOM   1969 O  O   . ARG A 1 226 ? -4.469  -13.587 2.361   1.00   14.34  ? 227 ARG A O   1 
ATOM   1970 C  CB  . ARG A 1 226 ? -6.267  -14.601 4.432   1.00   13.03  ? 227 ARG A CB  1 
ATOM   1971 C  CG  . ARG A 1 226 ? -6.773  -14.691 5.845   1.00   13.19  ? 227 ARG A CG  1 
ATOM   1972 C  CD  . ARG A 1 226 ? -6.656  -16.150 6.339   1.00   15.37  ? 227 ARG A CD  1 
ATOM   1973 N  NE  . ARG A 1 226 ? -7.235  -16.322 7.662   1.00   13.62  ? 227 ARG A NE  1 
ATOM   1974 C  CZ  . ARG A 1 226 ? -8.187  -17.180 7.983   1.00   14.29  ? 227 ARG A CZ  1 
ATOM   1975 N  NH1 . ARG A 1 226 ? -8.648  -18.076 7.112   1.00   17.82  ? 227 ARG A NH1 1 
ATOM   1976 N  NH2 . ARG A 1 226 ? -8.734  -17.121 9.167   1.00   14.95  ? 227 ARG A NH2 1 
ATOM   1977 N  N   . LYS A 1 227 ? -6.345  -12.708 1.470   1.00   12.98  ? 228 LYS A N   1 
ATOM   1978 C  CA  . LYS A 1 227 ? -5.786  -12.590 0.112   1.00   14.11  ? 228 LYS A CA  1 
ATOM   1979 C  C   . LYS A 1 227 ? -5.183  -11.209 -0.118  1.00   13.66  ? 228 LYS A C   1 
ATOM   1980 O  O   . LYS A 1 227 ? -4.526  -11.004 -1.146  1.00   15.86  ? 228 LYS A O   1 
ATOM   1981 C  CB  . LYS A 1 227 ? -6.871  -12.818 -0.922  1.00   16.92  ? 228 LYS A CB  1 
ATOM   1982 C  CG  . LYS A 1 227 ? -7.407  -14.196 -0.956  1.00   18.76  ? 228 LYS A CG  1 
ATOM   1983 C  CD  . LYS A 1 227 ? -8.474  -14.345 -2.087  1.00   27.94  ? 228 LYS A CD  1 
ATOM   1984 C  CE  . LYS A 1 227 ? -7.861  -14.635 -3.454  1.00   41.68  ? 228 LYS A CE  1 
ATOM   1985 N  NZ  . LYS A 1 227 ? -8.702  -14.609 -4.701  0.0000 58.68  ? 228 LYS A NZ  1 
ATOM   1986 N  N   . LEU A 1 228 ? -5.405  -10.270 0.803   1.00   13.28  ? 229 LEU A N   1 
ATOM   1987 C  CA  . LEU A 1 228 ? -4.767  -8.983  0.702   1.00   13.10  ? 229 LEU A CA  1 
ATOM   1988 C  C   . LEU A 1 228 ? -3.288  -9.129  0.837   1.00   13.50  ? 229 LEU A C   1 
ATOM   1989 O  O   . LEU A 1 228 ? -2.742  -10.183 1.269   1.00   13.53  ? 229 LEU A O   1 
ATOM   1990 C  CB  . LEU A 1 228 ? -5.342  -8.015  1.779   1.00   13.20  ? 229 LEU A CB  1 
ATOM   1991 C  CG  . LEU A 1 228 ? -6.787  -7.586  1.568   1.00   13.79  ? 229 LEU A CG  1 
ATOM   1992 C  CD1 . LEU A 1 228 ? -7.243  -6.973  2.857   1.00   14.60  ? 229 LEU A CD1 1 
ATOM   1993 C  CD2 . LEU A 1 228 ? -6.817  -6.577  0.423   1.00   16.60  ? 229 LEU A CD2 1 
ATOM   1994 N  N   . ASN A 1 229 ? -2.580  -8.075  0.436   1.00   13.39  ? 230 ASN A N   1 
ATOM   1995 C  CA  . ASN A 1 229 ? -1.129  -8.110  0.514   1.00   13.19  ? 230 ASN A CA  1 
ATOM   1996 C  C   . ASN A 1 229 ? -0.615  -6.887  1.321   1.00   14.53  ? 230 ASN A C   1 
ATOM   1997 O  O   . ASN A 1 229 ? -1.095  -5.775  1.298   1.00   14.71  ? 230 ASN A O   1 
ATOM   1998 C  CB  . ASN A 1 229 ? -0.448  -7.897  -0.881  1.00   16.33  ? 230 ASN A CB  1 
ATOM   1999 C  CG  . ASN A 1 229 ? -0.487  -9.076  -1.814  1.00   16.12  ? 230 ASN A CG  1 
ATOM   2000 O  OD1 . ASN A 1 229 ? 0.067   -8.930  -2.919  1.00   21.61  ? 230 ASN A OD1 1 
ATOM   2001 N  ND2 . ASN A 1 229 ? -1.151  -10.214 -1.478  1.00   17.70  ? 230 ASN A ND2 1 
ATOM   2002 N  N   . PHE A 1 230 ? 0.441   -7.234  2.108   1.00   13.95  ? 231 PHE A N   1 
ATOM   2003 C  CA  . PHE A 1 230 ? 1.147   -6.135  2.783   1.00   13.51  ? 231 PHE A CA  1 
ATOM   2004 C  C   . PHE A 1 230 ? 1.962   -5.308  1.824   1.00   15.41  ? 231 PHE A C   1 
ATOM   2005 O  O   . PHE A 1 230 ? 2.284   -4.161  2.108   1.00   16.94  ? 231 PHE A O   1 
ATOM   2006 C  CB  . PHE A 1 230 ? 2.128   -6.699  3.761   1.00   13.81  ? 231 PHE A CB  1 
ATOM   2007 C  CG  . PHE A 1 230 ? 1.583   -7.303  5.051   1.00   14.03  ? 231 PHE A CG  1 
ATOM   2008 C  CD1 . PHE A 1 230 ? 0.792   -6.555  5.952   1.00   14.11  ? 231 PHE A CD1 1 
ATOM   2009 C  CD2 . PHE A 1 230 ? 1.985   -8.561  5.466   1.00   14.38  ? 231 PHE A CD2 1 
ATOM   2010 C  CE1 . PHE A 1 230 ? 0.365   -7.127  7.179   1.00   13.99  ? 231 PHE A CE1 1 
ATOM   2011 C  CE2 . PHE A 1 230 ? 1.519   -9.137  6.660   1.00   14.39  ? 231 PHE A CE2 1 
ATOM   2012 C  CZ  . PHE A 1 230 ? 0.778   -8.375  7.524   1.00   13.88  ? 231 PHE A CZ  1 
ATOM   2013 N  N   . ASN A 1 231 ? 2.516   -5.946  0.797   1.00   15.57  ? 232 ASN A N   1 
ATOM   2014 C  CA  . ASN A 1 231 ? 3.414   -5.283  -0.188  1.00   15.87  ? 232 ASN A CA  1 
ATOM   2015 C  C   . ASN A 1 231 ? 2.609   -4.429  -1.137  1.00   15.46  ? 232 ASN A C   1 
ATOM   2016 O  O   . ASN A 1 231 ? 1.436   -4.537  -1.337  1.00   16.18  ? 232 ASN A O   1 
ATOM   2017 C  CB  . ASN A 1 231 ? 4.128   -6.372  -0.953  1.00   18.13  ? 232 ASN A CB  1 
ATOM   2018 C  CG  . ASN A 1 231 ? 3.157   -7.306  -1.534  1.00   16.98  ? 232 ASN A CG  1 
ATOM   2019 O  OD1 . ASN A 1 231 ? 2.667   -8.246  -0.861  1.00   21.21  ? 232 ASN A OD1 1 
ATOM   2020 N  ND2 . ASN A 1 231 ? 2.858   -7.132  -2.851  1.00   19.91  ? 232 ASN A ND2 1 
ATOM   2021 N  N   . GLY A 1 232 ? 3.365   -3.558  -1.811  1.00   18.67  ? 233 GLY A N   1 
ATOM   2022 C  CA  . GLY A 1 232 ? 2.817   -2.740  -2.939  1.00   18.08  ? 233 GLY A CA  1 
ATOM   2023 C  C   . GLY A 1 232 ? 2.862   -3.518  -4.224  1.00   17.18  ? 233 GLY A C   1 
ATOM   2024 O  O   . GLY A 1 232 ? 3.567   -4.529  -4.249  1.00   21.16  ? 233 GLY A O   1 
ATOM   2025 N  N   . GLU A 1 233 ? 2.133   -3.027  -5.215  1.00   17.47  ? 234 GLU A N   1 
ATOM   2026 C  CA  . GLU A 1 233 ? 2.072   -3.646  -6.524  1.00   18.46  ? 234 GLU A CA  1 
ATOM   2027 C  C   . GLU A 1 233 ? 3.496   -3.825  -7.115  1.00   20.20  ? 234 GLU A C   1 
ATOM   2028 O  O   . GLU A 1 233 ? 4.309   -2.886  -7.031  1.00   24.22  ? 234 GLU A O   1 
ATOM   2029 C  CB  . GLU A 1 233 ? 1.237   -2.768  -7.452  1.00   20.12  ? 234 GLU A CB  1 
ATOM   2030 C  CG  . GLU A 1 233 ? 0.945   -3.376  -8.809  1.00   20.58  ? 234 GLU A CG  1 
ATOM   2031 C  CD  . GLU A 1 233 ? 0.177   -2.428  -9.703  1.00   29.92  ? 234 GLU A CD  1 
ATOM   2032 O  OE1 . GLU A 1 233 ? -0.155  -1.313  -9.244  1.00   29.05  ? 234 GLU A OE1 1 
ATOM   2033 O  OE2 . GLU A 1 233 ? -0.098  -2.796  -10.863 1.00   30.27  ? 234 GLU A OE2 1 
ATOM   2034 N  N   . GLY A 1 234 ? 3.760   -5.024  -7.686  1.00   25.97  ? 235 GLY A N   1 
ATOM   2035 C  CA  . GLY A 1 234 ? 5.083   -5.359  -8.260  1.00   30.94  ? 235 GLY A CA  1 
ATOM   2036 C  C   . GLY A 1 234 ? 6.223   -5.696  -7.305  1.00   38.24  ? 235 GLY A C   1 
ATOM   2037 O  O   . GLY A 1 234 ? 7.409   -5.863  -7.764  1.00   50.38  ? 235 GLY A O   1 
ATOM   2038 N  N   . GLU A 1 235 ? 5.867   -5.883  -6.036  1.00   27.27  ? 236 GLU A N   1 
ATOM   2039 C  CA  . GLU A 1 235 ? 6.852   -6.261  -5.079  1.00   25.37  ? 236 GLU A CA  1 
ATOM   2040 C  C   . GLU A 1 235 ? 6.540   -7.695  -4.713  1.00   28.73  ? 236 GLU A C   1 
ATOM   2041 O  O   . GLU A 1 235 ? 5.432   -8.210  -5.001  1.00   34.68  ? 236 GLU A O   1 
ATOM   2042 C  CB  . GLU A 1 235 ? 6.738   -5.442  -3.777  1.00   24.10  ? 236 GLU A CB  1 
ATOM   2043 C  CG  . GLU A 1 235 ? 7.034   -3.952  -4.005  1.00   24.04  ? 236 GLU A CG  1 
ATOM   2044 C  CD  . GLU A 1 235 ? 6.898   -3.098  -2.766  1.00   37.60  ? 236 GLU A CD  1 
ATOM   2045 O  OE1 . GLU A 1 235 ? 6.248   -3.592  -1.772  1.00   35.18  ? 236 GLU A OE1 1 
ATOM   2046 O  OE2 . GLU A 1 235 ? 7.476   -1.968  -2.763  1.00   53.01  ? 236 GLU A OE2 1 
ATOM   2047 N  N   . PRO A 1 236 ? 7.463   -8.355  -4.050  1.00   25.48  ? 237 PRO A N   1 
ATOM   2048 C  CA  . PRO A 1 236 ? 7.285   -9.800  -3.732  1.00   29.22  ? 237 PRO A CA  1 
ATOM   2049 C  C   . PRO A 1 236 ? 6.062   -9.980  -2.838  1.00   28.25  ? 237 PRO A C   1 
ATOM   2050 O  O   . PRO A 1 236 ? 5.922   -9.213  -1.883  1.00   27.84  ? 237 PRO A O   1 
ATOM   2051 C  CB  . PRO A 1 236 ? 8.563   -10.160 -2.981  1.00   33.06  ? 237 PRO A CB  1 
ATOM   2052 C  CG  . PRO A 1 236 ? 9.557   -9.181  -3.522  1.00   31.85  ? 237 PRO A CG  1 
ATOM   2053 C  CD  . PRO A 1 236 ? 8.846   -7.899  -3.791  1.00   31.27  ? 237 PRO A CD  1 
ATOM   2054 N  N   . GLU A 1 237 ? 5.213   -10.966 -3.134  1.00   26.85  ? 238 GLU A N   1 
ATOM   2055 C  CA  . GLU A 1 237 ? 3.875   -11.059 -2.486  1.00   25.15  ? 238 GLU A CA  1 
ATOM   2056 C  C   . GLU A 1 237 ? 3.993   -11.517 -1.069  1.00   21.80  ? 238 GLU A C   1 
ATOM   2057 O  O   . GLU A 1 237 ? 4.614   -12.550 -0.834  1.00   19.95  ? 238 GLU A O   1 
ATOM   2058 C  CB  . GLU A 1 237 ? 2.959   -12.029 -3.210  1.00   25.90  ? 238 GLU A CB  1 
ATOM   2059 C  CG  . GLU A 1 237 ? 1.593   -12.104 -2.521  1.00   28.31  ? 238 GLU A CG  1 
ATOM   2060 C  CD  . GLU A 1 237 ? 0.490   -12.777 -3.353  1.00   30.75  ? 238 GLU A CD  1 
ATOM   2061 O  OE1 . GLU A 1 237 ? 0.910   -13.657 -4.136  1.00   44.44  ? 238 GLU A OE1 1 
ATOM   2062 O  OE2 . GLU A 1 237 ? -0.761  -12.443 -3.234  1.00   25.13  ? 238 GLU A OE2 1 
ATOM   2063 N  N   . GLU A 1 238 ? 3.447   -10.754 -0.157  1.00   17.35  ? 239 GLU A N   1 
ATOM   2064 C  CA  . GLU A 1 238 ? 3.429   -11.081 1.278   1.00   17.95  ? 239 GLU A CA  1 
ATOM   2065 C  C   . GLU A 1 238 ? 1.977   -10.974 1.695   1.00   14.83  ? 239 GLU A C   1 
ATOM   2066 O  O   . GLU A 1 238 ? 1.450   -9.880  1.758   1.00   18.31  ? 239 GLU A O   1 
ATOM   2067 C  CB  . GLU A 1 238 ? 4.258   -10.072 2.065   1.00   22.86  ? 239 GLU A CB  1 
ATOM   2068 C  CG  . GLU A 1 238 ? 5.683   -9.901  1.600   1.00   32.86  ? 239 GLU A CG  1 
ATOM   2069 C  CD  . GLU A 1 238 ? 6.549   -9.120  2.571   0.0000 52.05  ? 239 GLU A CD  1 
ATOM   2070 O  OE1 . GLU A 1 238 ? 6.080   -8.100  3.175   0.0000 55.39  ? 239 GLU A OE1 1 
ATOM   2071 O  OE2 . GLU A 1 238 ? 7.700   -9.583  2.723   0.0000 61.87  ? 239 GLU A OE2 1 
ATOM   2072 N  N   . LEU A 1 239 ? 1.358   -12.136 1.972   1.00   14.60  ? 240 LEU A N   1 
ATOM   2073 C  CA  . LEU A 1 239 ? -0.033  -12.094 2.310   1.00   13.09  ? 240 LEU A CA  1 
ATOM   2074 C  C   . LEU A 1 239 ? -0.245  -11.276 3.600   1.00   12.78  ? 240 LEU A C   1 
ATOM   2075 O  O   . LEU A 1 239 ? 0.539   -11.454 4.574   1.00   13.48  ? 240 LEU A O   1 
ATOM   2076 C  CB  . LEU A 1 239 ? -0.580  -13.487 2.516   1.00   13.74  ? 240 LEU A CB  1 
ATOM   2077 C  CG  . LEU A 1 239 ? -0.668  -14.390 1.280   1.00   15.97  ? 240 LEU A CG  1 
ATOM   2078 C  CD1 . LEU A 1 239 ? -1.222  -15.754 1.748   1.00   20.36  ? 240 LEU A CD1 1 
ATOM   2079 C  CD2 . LEU A 1 239 ? -1.439  -13.720 0.207   1.00   17.91  ? 240 LEU A CD2 1 
ATOM   2080 N  N   . MET A 1 240 ? -1.278  -10.445 3.616   1.00   12.60  ? 241 MET A N   1 
ATOM   2081 C  CA  . MET A 1 240 ? -1.643  -9.640  4.808   1.00   13.46  ? 241 MET A CA  1 
ATOM   2082 C  C   . MET A 1 240 ? -2.447  -10.580 5.699   1.00   11.31  ? 241 MET A C   1 
ATOM   2083 O  O   . MET A 1 240 ? -3.622  -10.736 5.617   1.00   12.01  ? 241 MET A O   1 
ATOM   2084 C  CB  . MET A 1 240 ? -2.502  -8.464  4.332   1.00   13.08  ? 241 MET A CB  1 
ATOM   2085 C  CG  . MET A 1 240 ? -2.837  -7.503  5.495   1.00   13.13  ? 241 MET A CG  1 
ATOM   2086 S  SD  . MET A 1 240 ? -3.817  -6.106  5.007   1.00   13.63  ? 241 MET A SD  1 
ATOM   2087 C  CE  . MET A 1 240 ? -2.492  -5.024  4.380   1.00   14.90  ? 241 MET A CE  1 
ATOM   2088 N  N   . VAL A 1 241 ? -1.673  -11.202 6.612   1.00   11.32  ? 242 VAL A N   1 
ATOM   2089 C  CA  . VAL A 1 241 ? -2.205  -12.123 7.674   1.00   10.67  ? 242 VAL A CA  1 
ATOM   2090 C  C   . VAL A 1 241 ? -1.399  -11.891 8.933   1.00   9.75   ? 242 VAL A C   1 
ATOM   2091 O  O   . VAL A 1 241 ? -0.258  -11.452 8.885   1.00   10.87  ? 242 VAL A O   1 
ATOM   2092 C  CB  . VAL A 1 241 ? -2.068  -13.622 7.263   1.00   11.57  ? 242 VAL A CB  1 
ATOM   2093 C  CG1 . VAL A 1 241 ? -3.052  -13.904 6.104   1.00   14.46  ? 242 VAL A CG1 1 
ATOM   2094 C  CG2 . VAL A 1 241 ? -0.672  -14.051 6.982   1.00   13.38  ? 242 VAL A CG2 1 
ATOM   2095 N  N   . ASP A 1 242 ? -1.996  -12.214 10.080  1.00   9.49   ? 243 ASP A N   1 
ATOM   2096 C  CA  . ASP A 1 242 ? -1.353  -12.053 11.357  1.00   9.77   ? 243 ASP A CA  1 
ATOM   2097 C  C   . ASP A 1 242 ? -0.886  -10.647 11.622  1.00   9.40   ? 243 ASP A C   1 
ATOM   2098 O  O   . ASP A 1 242 ? 0.215   -10.390 12.110  1.00   10.89  ? 243 ASP A O   1 
ATOM   2099 C  CB  . ASP A 1 242 ? -0.256  -13.122 11.592  1.00   10.45  ? 243 ASP A CB  1 
ATOM   2100 C  CG  . ASP A 1 242 ? -0.833  -14.505 11.702  1.00   11.04  ? 243 ASP A CG  1 
ATOM   2101 O  OD1 . ASP A 1 242 ? -1.907  -14.684 12.324  1.00   10.47  ? 243 ASP A OD1 1 
ATOM   2102 O  OD2 . ASP A 1 242 ? -0.238  -15.451 11.085  1.00   12.58  ? 243 ASP A OD2 1 
ATOM   2103 N  N   . ASN A 1 243 ? -1.755  -9.701  11.317  1.00   8.72   ? 244 ASN A N   1 
ATOM   2104 C  CA  . ASN A 1 243 ? -1.517  -8.272  11.533  1.00   8.95   ? 244 ASN A CA  1 
ATOM   2105 C  C   . ASN A 1 243 ? -2.030  -7.820  12.892  1.00   8.40   ? 244 ASN A C   1 
ATOM   2106 O  O   . ASN A 1 243 ? -2.689  -6.766  12.986  1.00   9.80   ? 244 ASN A O   1 
ATOM   2107 C  CB  . ASN A 1 243 ? -2.033  -7.424  10.377  1.00   9.70   ? 244 ASN A CB  1 
ATOM   2108 C  CG  . ASN A 1 243 ? -3.510  -7.573  10.175  1.00   9.57   ? 244 ASN A CG  1 
ATOM   2109 O  OD1 . ASN A 1 243 ? -4.155  -8.448  10.742  1.00   10.36  ? 244 ASN A OD1 1 
ATOM   2110 N  ND2 . ASN A 1 243 ? -4.074  -6.676  9.380   1.00   13.01  ? 244 ASN A ND2 1 
ATOM   2111 N  N   . TRP A 1 244 ? -1.764  -8.603  13.925  1.00   8.39   ? 245 TRP A N   1 
ATOM   2112 C  CA  . TRP A 1 244 ? -2.203  -8.340  15.269  1.00   8.30   ? 245 TRP A CA  1 
ATOM   2113 C  C   . TRP A 1 244 ? -0.998  -8.248  16.193  1.00   8.55   ? 245 TRP A C   1 
ATOM   2114 O  O   . TRP A 1 244 ? -0.004  -8.974  16.065  1.00   9.59   ? 245 TRP A O   1 
ATOM   2115 C  CB  . TRP A 1 244 ? -3.160  -9.444  15.796  1.00   8.55   ? 245 TRP A CB  1 
ATOM   2116 C  CG  . TRP A 1 244 ? -2.706  -10.835 15.606  1.00   8.53   ? 245 TRP A CG  1 
ATOM   2117 C  CD1 . TRP A 1 244 ? -2.835  -11.606 14.484  1.00   8.60   ? 245 TRP A CD1 1 
ATOM   2118 C  CD2 . TRP A 1 244 ? -2.079  -11.702 16.566  1.00   8.59   ? 245 TRP A CD2 1 
ATOM   2119 N  NE1 . TRP A 1 244 ? -2.297  -12.864 14.665  1.00   9.19   ? 245 TRP A NE1 1 
ATOM   2120 C  CE2 . TRP A 1 244 ? -1.843  -12.938 15.931  1.00   9.53   ? 245 TRP A CE2 1 
ATOM   2121 C  CE3 . TRP A 1 244 ? -1.774  -11.533 17.927  1.00   10.05  ? 245 TRP A CE3 1 
ATOM   2122 C  CZ2 . TRP A 1 244 ? -1.282  -14.025 16.622  1.00   10.71  ? 245 TRP A CZ2 1 
ATOM   2123 C  CZ3 . TRP A 1 244 ? -1.246  -12.624 18.597  1.00   11.90  ? 245 TRP A CZ3 1 
ATOM   2124 C  CH2 . TRP A 1 244 ? -0.961  -13.856 17.922  1.00   11.92  ? 245 TRP A CH2 1 
ATOM   2125 N  N   . ARG A 1 245 ? -1.101  -7.361  17.166  1.00   8.57   ? 246 ARG A N   1 
ATOM   2126 C  CA  . ARG A 1 245 ? -0.150  -7.239  18.270  1.00   8.54   ? 246 ARG A CA  1 
ATOM   2127 C  C   . ARG A 1 245 ? -0.591  -8.149  19.390  1.00   8.38   ? 246 ARG A C   1 
ATOM   2128 O  O   . ARG A 1 245 ? -1.799  -8.134  19.725  1.00   9.55   ? 246 ARG A O   1 
ATOM   2129 C  CB  . ARG A 1 245 ? -0.075  -5.786  18.755  1.00   8.65   ? 246 ARG A CB  1 
ATOM   2130 C  CG  . ARG A 1 245 ? 1.030   -5.551  19.774  1.00   9.07   ? 246 ARG A CG  1 
ATOM   2131 C  CD  . ARG A 1 245 ? 0.959   -4.162  20.364  1.00   8.82   ? 246 ARG A CD  1 
ATOM   2132 N  NE  . ARG A 1 245 ? 2.174   -3.882  21.108  1.00   9.61   ? 246 ARG A NE  1 
ATOM   2133 C  CZ  . ARG A 1 245 ? 2.366   -2.849  21.911  1.00   9.30   ? 246 ARG A CZ  1 
ATOM   2134 N  NH1 . ARG A 1 245 ? 1.396   -2.074  22.277  1.00   9.85   ? 246 ARG A NH1 1 
ATOM   2135 N  NH2 . ARG A 1 245 ? 3.611   -2.613  22.387  1.00   11.51  ? 246 ARG A NH2 1 
ATOM   2136 N  N   A PRO A 1 246 ? 0.285   -8.952  19.985  0.50   9.68   ? 247 PRO A N   1 
ATOM   2137 N  N   B PRO A 1 246 ? 0.286   -8.927  20.017  0.50   9.22   ? 247 PRO A N   1 
ATOM   2138 C  CA  A PRO A 1 246 ? -0.023  -9.739  21.157  0.50   10.00  ? 247 PRO A CA  1 
ATOM   2139 C  CA  B PRO A 1 246 ? -0.226  -9.773  21.076  0.50   9.81   ? 247 PRO A CA  1 
ATOM   2140 C  C   A PRO A 1 246 ? -0.454  -8.924  22.383  0.50   9.74   ? 247 PRO A C   1 
ATOM   2141 C  C   B PRO A 1 246 ? -0.482  -8.955  22.329  0.50   9.19   ? 247 PRO A C   1 
ATOM   2142 O  O   A PRO A 1 246 ? -0.166  -7.723  22.543  0.50   9.15   ? 247 PRO A O   1 
ATOM   2143 O  O   B PRO A 1 246 ? -0.080  -7.780  22.441  0.50   9.88   ? 247 PRO A O   1 
ATOM   2144 C  CB  A PRO A 1 246 ? 1.279   -10.478 21.457  0.50   12.07  ? 247 PRO A CB  1 
ATOM   2145 C  CB  B PRO A 1 246 ? 0.907   -10.723 21.340  0.50   10.85  ? 247 PRO A CB  1 
ATOM   2146 C  CG  A PRO A 1 246 ? 1.934   -10.582 20.110  0.50   12.03  ? 247 PRO A CG  1 
ATOM   2147 C  CG  B PRO A 1 246 ? 2.144   -9.887  20.982  0.50   13.10  ? 247 PRO A CG  1 
ATOM   2148 C  CD  A PRO A 1 246 ? 1.612   -9.282  19.422  0.50   10.03  ? 247 PRO A CD  1 
ATOM   2149 C  CD  B PRO A 1 246 ? 1.763   -9.039  19.837  0.50   10.47  ? 247 PRO A CD  1 
ATOM   2150 N  N   . ALA A 1 247 ? -1.132  -9.600  23.310  1.00   10.05  ? 248 ALA A N   1 
ATOM   2151 C  CA  . ALA A 1 247 ? -1.477  -8.952  24.599  1.00   9.56   ? 248 ALA A CA  1 
ATOM   2152 C  C   . ALA A 1 247 ? -0.246  -8.437  25.310  1.00   9.29   ? 248 ALA A C   1 
ATOM   2153 O  O   . ALA A 1 247 ? 0.781   -9.122  25.376  1.00   11.36  ? 248 ALA A O   1 
ATOM   2154 C  CB  . ALA A 1 247 ? -2.235  -9.920  25.467  1.00   11.96  ? 248 ALA A CB  1 
ATOM   2155 N  N   . GLN A 1 248 ? -0.384  -7.260  25.913  1.00   9.25   ? 249 GLN A N   1 
ATOM   2156 C  CA  . GLN A 1 248 ? 0.659   -6.538  26.654  1.00   10.05  ? 249 GLN A CA  1 
ATOM   2157 C  C   . GLN A 1 248 ? 0.350   -6.547  28.111  1.00   10.18  ? 249 GLN A C   1 
ATOM   2158 O  O   . GLN A 1 248 ? -0.779  -6.758  28.562  1.00   10.92  ? 249 GLN A O   1 
ATOM   2159 C  CB  . GLN A 1 248 ? 0.672   -5.108  26.130  1.00   10.93  ? 249 GLN A CB  1 
ATOM   2160 C  CG  . GLN A 1 248 ? 1.031   -4.997  24.633  1.00   10.81  ? 249 GLN A CG  1 
ATOM   2161 C  CD  . GLN A 1 248 ? 2.342   -5.681  24.298  1.00   11.40  ? 249 GLN A CD  1 
ATOM   2162 O  OE1 . GLN A 1 248 ? 3.377   -5.352  24.889  1.00   14.67  ? 249 GLN A OE1 1 
ATOM   2163 N  NE2 . GLN A 1 248 ? 2.358   -6.595  23.357  1.00   13.16  ? 249 GLN A NE2 1 
ATOM   2164 N  N   . PRO A 1 249 ? 1.337   -6.251  28.949  1.00   12.37  ? 250 PRO A N   1 
ATOM   2165 C  CA  . PRO A 1 249 ? 1.143   -6.282  30.415  1.00   13.52  ? 250 PRO A CA  1 
ATOM   2166 C  C   . PRO A 1 249 ? 0.087   -5.280  30.843  1.00   11.66  ? 250 PRO A C   1 
ATOM   2167 O  O   . PRO A 1 249 ? 0.120   -4.125  30.491  1.00   11.74  ? 250 PRO A O   1 
ATOM   2168 C  CB  . PRO A 1 249 ? 2.551   -5.897  30.944  1.00   16.52  ? 250 PRO A CB  1 
ATOM   2169 C  CG  . PRO A 1 249 ? 3.489   -6.405  29.914  1.00   18.01  ? 250 PRO A CG  1 
ATOM   2170 C  CD  . PRO A 1 249 ? 2.791   -6.045  28.623  1.00   16.09  ? 250 PRO A CD  1 
ATOM   2171 N  N   . LEU A 1 250 ? -0.798  -5.764  31.725  1.00   12.36  ? 251 LEU A N   1 
ATOM   2172 C  CA  . LEU A 1 250 ? -1.847  -4.890  32.236  1.00   11.66  ? 251 LEU A CA  1 
ATOM   2173 C  C   . LEU A 1 250 ? -1.304  -3.838  33.157  1.00   11.10  ? 251 LEU A C   1 
ATOM   2174 O  O   . LEU A 1 250 ? -1.878  -2.741  33.249  1.00   11.70  ? 251 LEU A O   1 
ATOM   2175 C  CB  . LEU A 1 250 ? -2.872  -5.762  32.977  1.00   14.16  ? 251 LEU A CB  1 
ATOM   2176 C  CG  . LEU A 1 250 ? -4.198  -5.019  33.375  1.00   13.79  ? 251 LEU A CG  1 
ATOM   2177 C  CD1 . LEU A 1 250 ? -4.935  -4.456  32.150  1.00   14.03  ? 251 LEU A CD1 1 
ATOM   2178 C  CD2 . LEU A 1 250 ? -5.109  -5.951  34.150  1.00   17.81  ? 251 LEU A CD2 1 
ATOM   2179 N  N   . LYS A 1 251 ? -0.224  -4.098  33.903  1.00   12.86  ? 252 LYS A N   1 
ATOM   2180 C  CA  . LYS A 1 251 ? 0.421   -3.058  34.785  1.00   13.45  ? 252 LYS A CA  1 
ATOM   2181 C  C   . LYS A 1 251 ? -0.620  -2.499  35.731  1.00   14.79  ? 252 LYS A C   1 
ATOM   2182 O  O   . LYS A 1 251 ? -1.426  -3.315  36.260  1.00   17.37  ? 252 LYS A O   1 
ATOM   2183 C  CB  . LYS A 1 251 ? 1.207   -2.062  33.964  1.00   16.21  ? 252 LYS A CB  1 
ATOM   2184 C  CG  . LYS A 1 251 ? 2.332   -2.783  33.245  1.00   19.68  ? 252 LYS A CG  1 
ATOM   2185 C  CD  . LYS A 1 251 ? 3.295   -1.855  32.637  1.00   23.75  ? 252 LYS A CD  1 
ATOM   2186 C  CE  . LYS A 1 251 ? 4.396   -2.592  32.059  1.00   32.12  ? 252 LYS A CE  1 
ATOM   2187 N  NZ  . LYS A 1 251 ? 5.243   -1.700  31.222  1.00   29.66  ? 252 LYS A NZ  1 
ATOM   2188 N  N   . ASN A 1 252 ? -0.652  -1.241  35.984  1.00   13.70  ? 253 ASN A N   1 
ATOM   2189 C  CA  . ASN A 1 252 ? -1.491  -0.783  36.974  1.00   22.41  ? 253 ASN A CA  1 
ATOM   2190 C  C   . ASN A 1 252 ? -2.796  -0.343  36.382  1.00   18.15  ? 253 ASN A C   1 
ATOM   2191 O  O   . ASN A 1 252 ? -3.036  0.856   36.300  1.00   20.10  ? 253 ASN A O   1 
ATOM   2192 C  CB  . ASN A 1 252 ? -0.713  0.402   37.666  1.00   24.12  ? 253 ASN A CB  1 
ATOM   2193 C  CG  . ASN A 1 252 ? -1.448  0.999   38.853  1.00   26.24  ? 253 ASN A CG  1 
ATOM   2194 O  OD1 . ASN A 1 252 ? -1.998  0.268   39.679  1.00   43.37  ? 253 ASN A OD1 1 
ATOM   2195 N  ND2 . ASN A 1 252 ? -1.441  2.321   38.961  1.00   33.28  ? 253 ASN A ND2 1 
ATOM   2196 N  N   A ARG A 1 253 ? -3.583  -1.336  35.950  0.50   14.62  ? 254 ARG A N   1 
ATOM   2197 N  N   B ARG A 1 253 ? -3.524  -1.212  35.684  0.50   14.61  ? 254 ARG A N   1 
ATOM   2198 C  CA  A ARG A 1 253 ? -4.878  -1.110  35.312  0.50   10.60  ? 254 ARG A CA  1 
ATOM   2199 C  CA  B ARG A 1 253 ? -4.848  -0.848  35.257  0.50   11.86  ? 254 ARG A CA  1 
ATOM   2200 C  C   A ARG A 1 253 ? -6.018  -2.044  35.676  0.50   12.03  ? 254 ARG A C   1 
ATOM   2201 C  C   B ARG A 1 253 ? -5.872  -1.848  35.793  0.50   11.89  ? 254 ARG A C   1 
ATOM   2202 O  O   A ARG A 1 253 ? -5.976  -3.265  35.658  0.50   15.81  ? 254 ARG A O   1 
ATOM   2203 O  O   B ARG A 1 253 ? -5.485  -2.900  36.293  0.50   12.95  ? 254 ARG A O   1 
ATOM   2204 C  CB  A ARG A 1 253 ? -4.789  -1.080  33.781  0.50   10.82  ? 254 ARG A CB  1 
ATOM   2205 C  CB  B ARG A 1 253 ? -4.816  -0.794  33.737  0.50   10.45  ? 254 ARG A CB  1 
ATOM   2206 C  CG  A ARG A 1 253 ? -4.008  0.105   33.276  0.50   9.31   ? 254 ARG A CG  1 
ATOM   2207 C  CG  B ARG A 1 253 ? -3.814  0.224   33.234  0.50   11.98  ? 254 ARG A CG  1 
ATOM   2208 C  CD  A ARG A 1 253 ? -3.940  0.090   31.773  0.50   9.16   ? 254 ARG A CD  1 
ATOM   2209 C  CD  B ARG A 1 253 ? -3.688  0.268   31.718  0.50   10.42  ? 254 ARG A CD  1 
ATOM   2210 N  NE  A ARG A 1 253 ? -3.060  -1.001  31.332  0.50   8.22   ? 254 ARG A NE  1 
ATOM   2211 N  NE  B ARG A 1 253 ? -2.915  -0.906  31.271  0.50   10.79  ? 254 ARG A NE  1 
ATOM   2212 C  CZ  A ARG A 1 253 ? -2.779  -1.226  30.053  0.50   8.04   ? 254 ARG A CZ  1 
ATOM   2213 C  CZ  B ARG A 1 253 ? -2.722  -1.275  30.000  0.50   9.49   ? 254 ARG A CZ  1 
ATOM   2214 N  NH1 A ARG A 1 253 ? -3.397  -0.530  29.086  0.50   8.12   ? 254 ARG A NH1 1 
ATOM   2215 N  NH1 B ARG A 1 253 ? -3.314  -0.625  28.973  0.50   8.73   ? 254 ARG A NH1 1 
ATOM   2216 N  NH2 A ARG A 1 253 ? -1.897  -2.155  29.711  0.50   8.04   ? 254 ARG A NH2 1 
ATOM   2217 N  NH2 B ARG A 1 253 ? -1.946  -2.312  29.719  0.50   10.04  ? 254 ARG A NH2 1 
ATOM   2218 N  N   . GLN A 1 254 ? -7.163  -1.400  35.787  1.00   12.13  ? 255 GLN A N   1 
ATOM   2219 C  CA  . GLN A 1 254 ? -8.347  -2.196  36.027  1.00   14.02  ? 255 GLN A CA  1 
ATOM   2220 C  C   . GLN A 1 254 ? -9.216  -2.224  34.821  1.00   11.85  ? 255 GLN A C   1 
ATOM   2221 O  O   . GLN A 1 254 ? -9.448  -1.172  34.165  1.00   15.93  ? 255 GLN A O   1 
ATOM   2222 C  CB  . GLN A 1 254 ? -9.146  -1.640  37.224  1.00   17.24  ? 255 GLN A CB  1 
ATOM   2223 C  CG  . GLN A 1 254 ? -8.415  -1.802  38.544  1.00   24.51  ? 255 GLN A CG  1 
ATOM   2224 C  CD  . GLN A 1 254 ? -9.194  -1.261  39.709  1.00   37.85  ? 255 GLN A CD  1 
ATOM   2225 O  OE1 . GLN A 1 254 ? -10.344 -0.828  39.524  1.00   38.15  ? 255 GLN A OE1 1 
ATOM   2226 N  NE2 . GLN A 1 254 ? -8.575  -1.199  40.900  1.00   42.35  ? 255 GLN A NE2 1 
ATOM   2227 N  N   . ILE A 1 255 ? -9.713  -3.385  34.477  1.00   10.65  ? 256 ILE A N   1 
ATOM   2228 C  CA  . ILE A 1 255 ? -10.704 -3.526  33.413  1.00   10.16  ? 256 ILE A CA  1 
ATOM   2229 C  C   . ILE A 1 255 ? -12.084 -3.561  34.089  1.00   10.01  ? 256 ILE A C   1 
ATOM   2230 O  O   . ILE A 1 255 ? -12.288 -4.291  35.057  1.00   12.63  ? 256 ILE A O   1 
ATOM   2231 C  CB  . ILE A 1 255 ? -10.474 -4.774  32.605  1.00   10.96  ? 256 ILE A CB  1 
ATOM   2232 C  CG1 . ILE A 1 255 ? -9.021  -4.788  32.031  1.00   11.50  ? 256 ILE A CG1 1 
ATOM   2233 C  CG2 . ILE A 1 255 ? -11.504 -4.917  31.499  1.00   12.38  ? 256 ILE A CG2 1 
ATOM   2234 C  CD1 . ILE A 1 255 ? -8.697  -5.994  31.202  1.00   13.01  ? 256 ILE A CD1 1 
ATOM   2235 N  N   . LYS A 1 256 ? -13.007 -2.744  33.609  1.00   10.10  ? 257 LYS A N   1 
ATOM   2236 C  CA  . LYS A 1 256 ? -14.340 -2.653  34.162  1.00   10.00  ? 257 LYS A CA  1 
ATOM   2237 C  C   . LYS A 1 256 ? -15.338 -3.252  33.230  1.00   9.87   ? 257 LYS A C   1 
ATOM   2238 O  O   . LYS A 1 256 ? -15.176 -3.138  31.995  1.00   12.09  ? 257 LYS A O   1 
ATOM   2239 C  CB  . LYS A 1 256 ? -14.677 -1.174  34.442  1.00   12.11  ? 257 LYS A CB  1 
ATOM   2240 C  CG  . LYS A 1 256 ? -13.715 -0.593  35.476  1.00   16.59  ? 257 LYS A CG  1 
ATOM   2241 C  CD  . LYS A 1 256 ? -13.857 0.782   35.880  1.00   20.59  ? 257 LYS A CD  1 
ATOM   2242 C  CE  . LYS A 1 256 ? -12.684 1.138   36.802  1.00   27.96  ? 257 LYS A CE  1 
ATOM   2243 N  NZ  . LYS A 1 256 ? -12.765 2.582   37.247  1.00   27.30  ? 257 LYS A NZ  1 
ATOM   2244 N  N   . ALA A 1 257 ? -16.354 -3.899  33.746  1.00   10.88  ? 258 ALA A N   1 
ATOM   2245 C  CA  . ALA A 1 257 ? -17.404 -4.496  32.981  1.00   11.50  ? 258 ALA A CA  1 
ATOM   2246 C  C   . ALA A 1 257 ? -18.697 -3.665  33.146  1.00   10.80  ? 258 ALA A C   1 
ATOM   2247 O  O   . ALA A 1 257 ? -19.040 -3.225  34.243  1.00   12.15  ? 258 ALA A O   1 
ATOM   2248 C  CB  . ALA A 1 257 ? -17.680 -5.956  33.452  1.00   13.23  ? 258 ALA A CB  1 
ATOM   2249 N  N   . SER A 1 258 ? -19.450 -3.542  32.037  1.00   10.85  ? 259 SER A N   1 
ATOM   2250 C  CA  . SER A 1 258 ? -20.682 -2.811  32.041  1.00   11.86  ? 259 SER A CA  1 
ATOM   2251 C  C   . SER A 1 258 ? -21.857 -3.710  32.497  1.00   12.87  ? 259 SER A C   1 
ATOM   2252 O  O   . SER A 1 258 ? -22.976 -3.147  32.581  1.00   16.85  ? 259 SER A O   1 
ATOM   2253 C  CB  . SER A 1 258 ? -21.002 -2.297  30.663  1.00   13.18  ? 259 SER A CB  1 
ATOM   2254 O  OG  . SER A 1 258 ? -21.412 -3.319  29.784  1.00   12.00  ? 259 SER A OG  1 
ATOM   2255 N  N   . PHE A 1 259 ? -21.627 -4.978  32.691  1.00   13.95  ? 260 PHE A N   1 
ATOM   2256 C  CA  . PHE A 1 259 ? -22.672 -5.983  32.876  1.00   15.99  ? 260 PHE A CA  1 
ATOM   2257 C  C   . PHE A 1 259 ? -22.282 -6.887  33.988  1.00   20.20  ? 260 PHE A C   1 
ATOM   2258 O  O   . PHE A 1 259 ? -21.088 -7.048  34.349  1.00   21.48  ? 260 PHE A O   1 
ATOM   2259 C  CB  . PHE A 1 259 ? -22.842 -6.792  31.610  1.00   15.82  ? 260 PHE A CB  1 
ATOM   2260 C  CG  . PHE A 1 259 ? -21.569 -7.503  31.209  1.00   14.88  ? 260 PHE A CG  1 
ATOM   2261 C  CD1 . PHE A 1 259 ? -20.559 -6.852  30.485  1.00   14.38  ? 260 PHE A CD1 1 
ATOM   2262 C  CD2 . PHE A 1 259 ? -21.345 -8.782  31.695  1.00   18.75  ? 260 PHE A CD2 1 
ATOM   2263 C  CE1 . PHE A 1 259 ? -19.348 -7.513  30.238  1.00   14.86  ? 260 PHE A CE1 1 
ATOM   2264 C  CE2 . PHE A 1 259 ? -20.145 -9.407  31.450  1.00   20.08  ? 260 PHE A CE2 1 
ATOM   2265 C  CZ  . PHE A 1 259 ? -19.162 -8.785  30.706  1.00   18.69  ? 260 PHE A CZ  1 
ATOM   2266 N  N   . LYS A 1 260 ? -23.357 -7.487  34.552  1.00   28.41  ? 261 LYS A N   1 
ATOM   2267 C  CA  . LYS A 1 260 ? -23.410 -8.713  35.372  1.00   38.26  ? 261 LYS A CA  1 
ATOM   2268 C  C   . LYS A 1 260 ? -22.672 -8.605  36.699  1.00   47.33  ? 261 LYS A C   1 
ATOM   2269 O  O   . LYS A 1 260 ? -23.255 -8.144  37.689  0.010  50.26  ? 261 LYS A O   1 
ATOM   2270 C  CB  . LYS A 1 260 ? -22.977 -9.990  34.592  1.00   38.51  ? 261 LYS A CB  1 
ATOM   2271 C  CG  . LYS A 1 260 ? -23.975 -10.642 33.636  1.00   50.73  ? 261 LYS A CG  1 
ATOM   2272 C  CD  . LYS A 1 260 ? -23.477 -11.750 32.683  0.0000 63.93  ? 261 LYS A CD  1 
ATOM   2273 C  CE  . LYS A 1 260 ? -22.048 -12.244 32.871  0.0000 49.96  ? 261 LYS A CE  1 
ATOM   2274 N  NZ  . LYS A 1 260 ? -21.609 -13.342 31.953  0.0000 55.44  ? 261 LYS A NZ  1 
ATOM   2275 O  OXT . LYS A 1 260 ? -21.501 -8.970  36.801  0.0000 30.00  ? 261 LYS A OXT 1 
HETATM 2276 ZN ZN  . ZN  B 2 .   ? -6.708  -1.703  15.278  1.00   7.15   ? 301 ZN  A ZN  1 
HETATM 2277 S  S   . DMS C 3 .   ? 1.279   -11.618 14.864  1.00   33.06  ? 302 DMS A S   1 
HETATM 2278 O  O   . DMS C 3 .   ? 2.328   -10.983 13.947  1.00   43.81  ? 302 DMS A O   1 
HETATM 2279 C  C1  . DMS C 3 .   ? 1.828   -13.325 14.752  1.00   31.90  ? 302 DMS A C1  1 
HETATM 2280 C  C2  . DMS C 3 .   ? 1.581   -11.308 16.464  1.00   21.04  ? 302 DMS A C2  1 
HETATM 2281 N  N1  . BCN D 4 .   ? -20.636 -14.793 23.479  1.00   34.51  ? 303 BCN A N1  1 
HETATM 2282 C  C1  . BCN D 4 .   ? -19.690 -14.061 24.393  1.00   29.38  ? 303 BCN A C1  1 
HETATM 2283 C  C2  . BCN D 4 .   ? -19.918 -14.989 25.570  1.00   33.22  ? 303 BCN A C2  1 
HETATM 2284 O  O21 . BCN D 4 .   ? -20.873 -15.858 25.538  1.00   46.83  ? 303 BCN A O21 1 
HETATM 2285 O  O22 . BCN D 4 .   ? -19.232 -14.899 26.609  1.00   33.28  ? 303 BCN A O22 1 
HETATM 2286 C  C3  . BCN D 4 .   ? -21.732 -13.931 23.063  1.00   25.03  ? 303 BCN A C3  1 
HETATM 2287 C  C4  . BCN D 4 .   ? -22.885 -14.500 22.182  1.00   47.76  ? 303 BCN A C4  1 
HETATM 2288 O  O4  . BCN D 4 .   ? -24.245 -14.290 22.654  1.00   45.81  ? 303 BCN A O4  1 
HETATM 2289 C  C5  . BCN D 4 .   ? -19.981 -15.631 22.474  1.00   19.10  ? 303 BCN A C5  1 
HETATM 2290 C  C6  . BCN D 4 .   ? -20.485 -16.767 21.579  1.00   41.22  ? 303 BCN A C6  1 
HETATM 2291 O  O6  . BCN D 4 .   ? -20.931 -16.273 20.302  1.00   55.45  ? 303 BCN A O6  1 
HETATM 2292 O  O9  . WW3 E 5 .   ? -7.384  0.853   16.677  1.00   7.91   ? 304 WW3 A O9  1 
HETATM 2293 S  S7  . WW3 E 5 .   ? -5.956  0.810   16.789  1.00   7.51   ? 304 WW3 A S7  1 
HETATM 2294 O  O8  . WW3 E 5 .   ? -5.393  0.894   18.122  1.00   7.97   ? 304 WW3 A O8  1 
HETATM 2295 N  N10 . WW3 E 5 .   ? -5.384  -0.497  16.034  1.00   7.61   ? 304 WW3 A N10 1 
HETATM 2296 C  C3  . WW3 E 5 .   ? -5.408  2.238   15.948  1.00   8.66   ? 304 WW3 A C3  1 
HETATM 2297 C  C2  . WW3 E 5 .   ? -6.284  3.241   15.543  1.00   9.90   ? 304 WW3 A C2  1 
HETATM 2298 C  C4  . WW3 E 5 .   ? -4.016  2.390   15.660  1.00   9.39   ? 304 WW3 A C4  1 
HETATM 2299 C  C5  . WW3 E 5 .   ? -3.580  3.538   14.956  1.00   10.23  ? 304 WW3 A C5  1 
HETATM 2300 C  C6  . WW3 E 5 .   ? -4.506  4.495   14.560  1.00   10.77  ? 304 WW3 A C6  1 
HETATM 2301 C  C1  . WW3 E 5 .   ? -5.832  4.349   14.851  1.00   10.90  ? 304 WW3 A C1  1 
HETATM 2302 N  N11 . WW3 E 5 .   ? -4.119  5.621   13.812  1.00   12.44  ? 304 WW3 A N11 1 
HETATM 2303 N  N12 . WW3 E 5 .   ? -2.892  5.896   13.848  1.00   22.82  ? 304 WW3 A N12 1 
HETATM 2304 N  N13 . WW3 E 5 .   ? -2.392  7.011   13.295  1.00   18.57  ? 304 WW3 A N13 1 
HETATM 2305 C  C16 . WW3 E 5 .   ? -1.326  7.455   14.165  1.00   29.27  ? 304 WW3 A C16 1 
HETATM 2306 C  C15 . WW3 E 5 .   ? -0.313  8.528   13.842  1.00   40.42  ? 304 WW3 A C15 1 
HETATM 2307 C  C17 . WW3 E 5 .   ? -1.093  9.785   14.150  1.00   32.45  ? 304 WW3 A C17 1 
HETATM 2308 C  C18 . WW3 E 5 .   ? -2.135  10.025  13.060  1.00   31.83  ? 304 WW3 A C18 1 
HETATM 2309 C  C19 . WW3 E 5 .   ? -2.382  9.003   11.931  1.00   32.42  ? 304 WW3 A C19 1 
HETATM 2310 C  C14 . WW3 E 5 .   ? -3.136  7.753   12.334  1.00   18.89  ? 304 WW3 A C14 1 
HETATM 2311 O  O   . HOH F 6 .   ? -17.061 -8.479  20.427  1.00   9.60   ? 401 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? 2.914   1.322   -1.991  1.00   42.57  ? 402 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? -21.951 5.649   4.747   1.00   18.21  ? 403 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? -4.591  -13.556 18.054  1.00   10.04  ? 404 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? -1.246  -4.208  15.720  1.00   10.43  ? 405 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? -15.060 20.052  17.703  1.00   16.75  ? 406 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? -3.390  -13.317 25.149  1.00   12.01  ? 407 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? -2.104  -12.334 22.830  1.00   11.09  ? 408 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? -3.811  -15.932 24.379  1.00   14.08  ? 409 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? -21.626 -7.286  23.698  1.00   12.41  ? 410 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? -10.686 8.648   25.563  1.00   10.59  ? 411 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? -4.532  4.094   10.410  1.00   22.32  ? 412 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? -17.388 -16.254 22.136  1.00   21.37  ? 413 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? 1.216   -1.524  29.457  1.00   14.43  ? 414 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? 4.829   -4.913  20.955  1.00   14.84  ? 415 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? -3.961  0.136   13.568  1.00   11.10  ? 416 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? -16.373 -9.954  33.026  1.00   18.03  ? 417 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? -15.196 -20.032 23.092  1.00   34.37  ? 418 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? -6.179  -4.627  -6.389  1.00   25.64  ? 419 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? -13.051 -16.890 26.683  1.00   14.98  ? 420 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? -8.043  -15.513 11.345  1.00   11.21  ? 421 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? -8.208  -22.222 10.452  1.00   22.13  ? 422 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? 7.581   6.029   21.714  1.00   16.97  ? 423 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? -3.533  -11.198 20.875  1.00   10.72  ? 424 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? -8.794  -3.906  7.914   1.00   10.24  ? 425 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? -2.533  -8.754  29.120  1.00   11.83  ? 426 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? -6.060  6.123   11.757  1.00   17.90  ? 427 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? 4.132   -6.607  7.698   1.00   22.67  ? 428 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? 0.067   -1.076  -4.680  1.00   17.76  ? 429 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? -18.008 20.766  8.024   1.00   15.16  ? 430 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? -23.940 -0.877  3.949   1.00   22.41  ? 431 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? -30.907 -7.254  22.441  1.00   31.21  ? 432 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? 5.339   7.047   20.336  1.00   17.29  ? 433 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? -23.074 -11.862 14.104  1.00   22.76  ? 434 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? -19.350 9.986   8.869   1.00   14.18  ? 435 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? -16.084 -12.382 24.478  1.00   14.42  ? 436 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? 3.554   4.956   29.810  1.00   18.62  ? 437 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? -22.829 -5.953  2.685   1.00   22.03  ? 438 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? -12.929 -17.264 16.892  1.00   12.55  ? 439 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? -9.545  -7.949  34.241  1.00   19.84  ? 440 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? -3.627  -13.020 -2.788  1.00   27.78  ? 441 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? -2.619  -3.788  11.507  1.00   14.25  ? 442 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? -17.820 19.909  17.505  1.00   21.71  ? 443 HOH A O   1 
HETATM 2354 O  O   . HOH F 6 .   ? -24.219 8.497   20.229  1.00   19.94  ? 444 HOH A O   1 
HETATM 2355 O  O   . HOH F 6 .   ? 1.778   -15.732 9.346   1.00   25.38  ? 445 HOH A O   1 
HETATM 2356 O  O   . HOH F 6 .   ? -6.823  20.864  19.539  1.00   13.38  ? 446 HOH A O   1 
HETATM 2357 O  O   . HOH F 6 .   ? -18.039 10.667  11.266  1.00   16.33  ? 447 HOH A O   1 
HETATM 2358 O  O   . HOH F 6 .   ? -20.386 10.644  26.797  1.00   18.66  ? 448 HOH A O   1 
HETATM 2359 O  O   . HOH F 6 .   ? -13.893 10.310  27.941  1.00   17.40  ? 449 HOH A O   1 
HETATM 2360 O  O   . HOH F 6 .   ? -1.178  -11.134 28.981  1.00   17.34  ? 450 HOH A O   1 
HETATM 2361 O  O   . HOH F 6 .   ? 8.493   -3.930  21.082  1.00   15.23  ? 451 HOH A O   1 
HETATM 2362 O  O   . HOH F 6 .   ? -1.303  -13.058 26.982  1.00   23.44  ? 452 HOH A O   1 
HETATM 2363 O  O   . HOH F 6 .   ? -14.315 -16.623 29.073  1.00   24.88  ? 453 HOH A O   1 
HETATM 2364 O  O   . HOH F 6 .   ? -13.486 -18.570 14.588  1.00   15.04  ? 454 HOH A O   1 
HETATM 2365 O  O   . HOH F 6 .   ? -24.004 -0.813  26.559  1.00   18.44  ? 455 HOH A O   1 
HETATM 2366 O  O   . HOH F 6 .   ? 10.318  -8.688  8.418   1.00   29.71  ? 456 HOH A O   1 
HETATM 2367 O  O   . HOH F 6 .   ? -5.161  0.454   9.840   1.00   15.05  ? 457 HOH A O   1 
HETATM 2368 O  O   . HOH F 6 .   ? -5.405  2.081   12.061  1.00   12.66  ? 458 HOH A O   1 
HETATM 2369 O  O   . HOH F 6 .   ? -21.126 7.766   1.891   1.00   20.40  ? 459 HOH A O   1 
HETATM 2370 O  O   . HOH F 6 .   ? -11.081 -19.571 7.189   1.00   25.01  ? 460 HOH A O   1 
HETATM 2371 O  O   . HOH F 6 .   ? -11.983 2.677   30.948  1.00   19.53  ? 461 HOH A O   1 
HETATM 2372 O  O   . HOH F 6 .   ? -0.073  1.075   34.484  1.00   26.52  ? 462 HOH A O   1 
HETATM 2373 O  O   . HOH F 6 .   ? -8.227  -19.409 21.688  1.00   14.99  ? 463 HOH A O   1 
HETATM 2374 O  O   . HOH F 6 .   ? -23.331 -3.062  6.645   1.00   21.86  ? 464 HOH A O   1 
HETATM 2375 O  O   . HOH F 6 .   ? -9.311  -10.120 -1.141  1.00   24.50  ? 465 HOH A O   1 
HETATM 2376 O  O   . HOH F 6 .   ? -14.698 -18.594 18.698  1.00   15.20  ? 466 HOH A O   1 
HETATM 2377 O  O   . HOH F 6 .   ? -10.450 -18.332 17.097  1.00   12.60  ? 467 HOH A O   1 
HETATM 2378 O  O   . HOH F 6 .   ? -0.653  -8.580  32.564  1.00   23.99  ? 468 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? -19.944 -16.762 3.004   1.00   29.34  ? 469 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? -22.174 -18.379 13.575  1.00   21.96  ? 470 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? 13.397  0.164   24.498  1.00   22.18  ? 471 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? -13.880 19.915  15.192  1.00   18.00  ? 472 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? -4.728  -11.986 32.118  1.00   20.38  ? 473 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? 1.294   -11.765 25.042  1.00   27.13  ? 474 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? -16.820 -13.992 26.448  1.00   19.41  ? 475 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? 15.294  -2.629  14.474  1.00   20.59  ? 476 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? -10.706 -19.491 20.051  1.00   17.47  ? 477 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? -15.543 19.256  13.121  1.00   14.74  ? 478 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? -24.856 -7.761  9.019   1.00   20.41  ? 479 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? -4.010  -1.454  11.391  1.00   19.71  ? 480 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? -2.092  -17.592 25.617  1.00   25.68  ? 481 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? -7.033  1.492   35.148  1.00   24.91  ? 482 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? -7.419  -8.674  32.670  1.00   16.63  ? 483 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? -0.583  10.733  23.221  1.00   19.25  ? 484 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? -0.228  -14.289 22.136  1.00   22.93  ? 485 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? -9.303  3.055   34.786  1.00   26.53  ? 486 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? 2.496   -13.259 5.220   1.00   24.35  ? 487 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? 4.979   -7.373  22.272  1.00   26.11  ? 488 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? -12.825 7.864   28.869  1.00   21.29  ? 489 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? -9.119  -5.820  35.973  1.00   16.71  ? 490 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? -6.256  -19.779 23.826  1.00   22.38  ? 491 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? -10.376 14.707  12.147  1.00   19.40  ? 492 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? -4.235  -8.510  31.123  1.00   18.79  ? 493 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? 4.177   -3.435  26.580  1.00   20.77  ? 494 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? 4.445   -2.601  29.008  1.00   24.40  ? 495 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? -26.294 3.308   15.508  1.00   26.20  ? 496 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? -8.583  0.608   -6.472  1.00   29.42  ? 497 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? 2.550   -4.326  7.728   1.00   21.31  ? 498 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? -6.556  -15.078 31.550  1.00   28.20  ? 499 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? 1.273   8.743   24.161  1.00   20.98  ? 500 HOH A O   1 
HETATM 2411 O  O   . HOH F 6 .   ? -14.098 14.225  27.201  1.00   23.14  ? 501 HOH A O   1 
HETATM 2412 O  O   . HOH F 6 .   ? -8.460  -15.468 36.589  1.00   30.57  ? 502 HOH A O   1 
HETATM 2413 O  O   . HOH F 6 .   ? -7.262  -16.852 1.545   1.00   20.27  ? 503 HOH A O   1 
HETATM 2414 O  O   . HOH F 6 .   ? -16.267 15.814  23.750  1.00   17.00  ? 504 HOH A O   1 
HETATM 2415 O  O   . HOH F 6 .   ? -0.654  3.205   13.077  1.00   21.38  ? 505 HOH A O   1 
HETATM 2416 O  O   . HOH F 6 .   ? -24.720 -9.538  1.926   1.00   25.18  ? 506 HOH A O   1 
HETATM 2417 O  O   . HOH F 6 .   ? 2.920   -14.593 1.540   1.00   27.56  ? 507 HOH A O   1 
HETATM 2418 O  O   . HOH F 6 .   ? -1.168  9.196   27.927  1.00   27.28  ? 508 HOH A O   1 
HETATM 2419 O  O   . HOH F 6 .   ? -13.059 -22.288 8.542   1.00   24.55  ? 509 HOH A O   1 
HETATM 2420 O  O   . HOH F 6 .   ? -7.014  -8.549  -6.928  1.00   36.07  ? 510 HOH A O   1 
HETATM 2421 O  O   . HOH F 6 .   ? 11.156  1.267   26.007  1.00   25.58  ? 511 HOH A O   1 
HETATM 2422 O  O   . HOH F 6 .   ? -10.584 13.546  8.706   1.00   30.99  ? 512 HOH A O   1 
HETATM 2423 O  O   . HOH F 6 .   ? 0.436   0.611   -6.728  1.00   32.57  ? 513 HOH A O   1 
HETATM 2424 O  O   . HOH F 6 .   ? -9.138  5.880   29.046  1.00   19.40  ? 514 HOH A O   1 
HETATM 2425 O  O   . HOH F 6 .   ? -19.837 -4.306  41.439  1.00   31.64  ? 515 HOH A O   1 
HETATM 2426 O  O   . HOH F 6 .   ? -6.624  -5.288  37.417  1.00   17.90  ? 516 HOH A O   1 
HETATM 2427 O  O   . HOH F 6 .   ? 1.431   -6.322  34.412  1.00   30.32  ? 517 HOH A O   1 
HETATM 2428 O  O   . HOH F 6 .   ? -7.078  5.917   6.606   1.00   24.28  ? 518 HOH A O   1 
HETATM 2429 O  O   . HOH F 6 .   ? -16.962 -17.994 20.160  1.00   23.83  ? 519 HOH A O   1 
HETATM 2430 O  O   . HOH F 6 .   ? -17.549 6.223   38.356  1.00   30.58  ? 520 HOH A O   1 
HETATM 2431 O  O   . HOH F 6 .   ? -17.938 -12.156 31.778  1.00   34.21  ? 521 HOH A O   1 
HETATM 2432 O  O   . HOH F 6 .   ? -21.330 -20.698 14.692  1.00   25.78  ? 522 HOH A O   1 
HETATM 2433 O  O   . HOH F 6 .   ? -6.391  8.351   10.266  1.00   37.30  ? 523 HOH A O   1 
HETATM 2434 O  O   . HOH F 6 .   ? 0.987   14.706  24.130  1.00   31.16  ? 524 HOH A O   1 
HETATM 2435 O  O   . HOH F 6 .   ? -26.389 2.707   20.900  1.00   28.55  ? 525 HOH A O   1 
HETATM 2436 O  O   . HOH F 6 .   ? 8.490   -4.727  23.674  1.00   25.89  ? 526 HOH A O   1 
HETATM 2437 O  O   . HOH F 6 .   ? -15.607 8.872   -2.191  1.00   24.22  ? 527 HOH A O   1 
HETATM 2438 O  O   . HOH F 6 .   ? -6.065  -11.613 36.381  1.00   40.85  ? 528 HOH A O   1 
HETATM 2439 O  O   . HOH F 6 .   ? 8.146   3.312   27.849  1.00   36.85  ? 529 HOH A O   1 
HETATM 2440 O  O   . HOH F 6 .   ? -8.582  -19.875 26.728  1.00   21.16  ? 530 HOH A O   1 
HETATM 2441 O  O   . HOH F 6 .   ? -10.717 8.496   7.731   1.00   24.17  ? 531 HOH A O   1 
HETATM 2442 O  O   . HOH F 6 .   ? -18.657 19.908  14.768  1.00   19.61  ? 532 HOH A O   1 
HETATM 2443 O  O   . HOH F 6 .   ? -16.225 16.739  26.473  1.00   31.53  ? 533 HOH A O   1 
HETATM 2444 O  O   . HOH F 6 .   ? -2.081  -11.842 31.608  1.00   31.00  ? 534 HOH A O   1 
HETATM 2445 O  O   . HOH F 6 .   ? -10.655 20.744  24.975  1.00   18.51  ? 535 HOH A O   1 
HETATM 2446 O  O   . HOH F 6 .   ? 2.525   -11.591 9.387   1.00   20.79  ? 536 HOH A O   1 
HETATM 2447 O  O   . HOH F 6 .   ? 7.633   -7.679  -0.260  1.00   32.63  ? 537 HOH A O   1 
HETATM 2448 O  O   . HOH F 6 .   ? -23.664 -0.277  31.926  1.00   36.19  ? 538 HOH A O   1 
HETATM 2449 O  O   . HOH F 6 .   ? 11.945  -6.508  7.957   1.00   29.56  ? 539 HOH A O   1 
HETATM 2450 O  O   . HOH F 6 .   ? -21.999 -14.170 18.752  1.00   33.04  ? 540 HOH A O   1 
HETATM 2451 O  O   . HOH F 6 .   ? -0.678  -17.426 17.929  1.00   47.17  ? 541 HOH A O   1 
HETATM 2452 O  O   . HOH F 6 .   ? -7.717  -18.999 30.671  1.00   29.23  ? 542 HOH A O   1 
HETATM 2453 O  O   . HOH F 6 .   ? -24.835 4.593   8.383   1.00   38.15  ? 543 HOH A O   1 
HETATM 2454 O  O   . HOH F 6 .   ? -12.479 16.091  8.279   1.00   40.32  ? 544 HOH A O   1 
HETATM 2455 O  O   . HOH F 6 .   ? -6.030  -9.271  35.145  1.00   37.66  ? 545 HOH A O   1 
HETATM 2456 O  O   . HOH F 6 .   ? -7.559  -4.864  40.055  1.00   29.82  ? 546 HOH A O   1 
HETATM 2457 O  O   . HOH F 6 .   ? -23.456 -13.360 11.227  1.00   19.10  ? 547 HOH A O   1 
HETATM 2458 O  O   . HOH F 6 .   ? -19.879 -2.201  42.979  1.00   40.62  ? 548 HOH A O   1 
HETATM 2459 O  O   . HOH F 6 .   ? 6.114   -11.282 15.533  1.00   30.50  ? 549 HOH A O   1 
HETATM 2460 O  O   . HOH F 6 .   ? -12.789 3.439   -6.855  1.00   28.14  ? 550 HOH A O   1 
HETATM 2461 O  O   . HOH F 6 .   ? 12.938  -3.966  13.488  1.00   28.72  ? 551 HOH A O   1 
HETATM 2462 O  O   . HOH F 6 .   ? -12.451 12.487  29.181  1.00   26.69  ? 552 HOH A O   1 
HETATM 2463 O  O   . HOH F 6 .   ? -1.540  11.358  25.748  1.00   28.40  ? 553 HOH A O   1 
HETATM 2464 O  O   . HOH F 6 .   ? 13.949  5.597   19.307  1.00   31.51  ? 554 HOH A O   1 
HETATM 2465 O  O   . HOH F 6 .   ? -23.297 -0.053  34.685  1.00   29.22  ? 555 HOH A O   1 
HETATM 2466 O  O   . HOH F 6 .   ? -10.326 -5.738  38.369  1.00   25.53  ? 556 HOH A O   1 
HETATM 2467 O  O   . HOH F 6 .   ? -19.326 13.998  9.068   1.00   28.00  ? 557 HOH A O   1 
HETATM 2468 O  O   . HOH F 6 .   ? -1.448  -17.339 4.831   1.00   37.15  ? 558 HOH A O   1 
HETATM 2469 O  O   . HOH F 6 .   ? -25.714 -1.291  35.025  1.00   30.50  ? 559 HOH A O   1 
HETATM 2470 O  O   . HOH F 6 .   ? -20.607 13.831  28.843  1.00   38.97  ? 560 HOH A O   1 
HETATM 2471 O  O   . HOH F 6 .   ? -26.335 -7.775  30.442  1.00   38.59  ? 561 HOH A O   1 
HETATM 2472 O  O   . HOH F 6 .   ? 8.356   -5.761  -10.442 1.00   33.19  ? 562 HOH A O   1 
HETATM 2473 O  O   . HOH F 6 .   ? -0.630  13.858  15.897  1.00   27.27  ? 563 HOH A O   1 
HETATM 2474 O  O   . HOH F 6 .   ? -11.345 17.577  12.239  1.00   23.01  ? 564 HOH A O   1 
HETATM 2475 O  O   . HOH F 6 .   ? -14.124 3.544   33.185  1.00   26.87  ? 565 HOH A O   1 
HETATM 2476 O  O   . HOH F 6 .   ? -1.868  -4.719  -6.986  1.00   29.22  ? 566 HOH A O   1 
HETATM 2477 O  O   . HOH F 6 .   ? -25.965 6.045   27.117  1.00   24.81  ? 567 HOH A O   1 
HETATM 2478 O  O   . HOH F 6 .   ? -24.212 -7.130  0.346   1.00   34.51  ? 568 HOH A O   1 
HETATM 2479 O  O   . HOH F 6 .   ? -14.591 6.213   32.817  1.00   40.53  ? 569 HOH A O   1 
HETATM 2480 O  O   . HOH F 6 .   ? 11.653  -0.460  16.109  1.00   23.75  ? 570 HOH A O   1 
HETATM 2481 O  O   . HOH F 6 .   ? -25.322 10.982  19.630  1.00   27.05  ? 571 HOH A O   1 
HETATM 2482 O  O   . HOH F 6 .   ? -4.617  -15.970 0.855   1.00   28.79  ? 572 HOH A O   1 
HETATM 2483 O  O   . HOH F 6 .   ? -17.135 -1.003  40.349  1.00   35.88  ? 573 HOH A O   1 
HETATM 2484 O  O   . HOH F 6 .   ? 1.648   12.393  22.522  1.00   28.94  ? 574 HOH A O   1 
HETATM 2485 O  O   . HOH F 6 .   ? 14.218  2.322   23.348  1.00   40.09  ? 575 HOH A O   1 
HETATM 2486 O  O   . HOH F 6 .   ? -7.471  -8.703  -2.374  1.00   29.79  ? 576 HOH A O   1 
HETATM 2487 O  O   . HOH F 6 .   ? -11.734 -3.318  42.176  1.00   37.38  ? 577 HOH A O   1 
HETATM 2488 O  O   . HOH F 6 .   ? -23.784 -3.572  3.792   1.00   37.45  ? 578 HOH A O   1 
HETATM 2489 O  O   . HOH F 6 .   ? -8.316  7.455   8.501   1.00   25.54  ? 579 HOH A O   1 
HETATM 2490 O  O   . HOH F 6 .   ? 1.030   3.297   1.887   1.00   34.50  ? 580 HOH A O   1 
HETATM 2491 O  O   . HOH F 6 .   ? -1.385  4.350   -4.900  1.00   40.78  ? 581 HOH A O   1 
HETATM 2492 O  O   . HOH F 6 .   ? -23.402 -11.133 17.079  1.00   27.09  ? 582 HOH A O   1 
HETATM 2493 O  O   . HOH F 6 .   ? 9.322   7.456   18.518  1.00   45.39  ? 583 HOH A O   1 
HETATM 2494 O  O   . HOH F 6 .   ? -2.818  -14.978 32.754  1.00   27.64  ? 584 HOH A O   1 
HETATM 2495 O  O   . HOH F 6 .   ? -18.724 1.975   40.900  1.00   39.58  ? 585 HOH A O   1 
HETATM 2496 O  O   . HOH F 6 .   ? -23.754 8.094   3.624   1.00   27.24  ? 586 HOH A O   1 
HETATM 2497 O  O   . HOH F 6 .   ? -0.220  0.952   -10.864 1.00   30.83  ? 587 HOH A O   1 
HETATM 2498 O  O   . HOH F 6 .   ? -12.130 10.661  5.715   1.00   32.01  ? 588 HOH A O   1 
HETATM 2499 O  O   . HOH F 6 .   ? -10.507 4.883   30.832  1.00   25.43  ? 589 HOH A O   1 
HETATM 2500 O  O   . HOH F 6 .   ? -11.119 -15.127 34.170  1.00   28.60  ? 590 HOH A O   1 
HETATM 2501 O  O   . HOH F 6 .   ? -5.078  2.209   37.336  1.00   31.27  ? 591 HOH A O   1 
HETATM 2502 O  O   . HOH F 6 .   ? -23.038 -14.889 16.205  1.00   39.50  ? 592 HOH A O   1 
HETATM 2503 O  O   . HOH F 6 .   ? -13.933 14.571  6.194   1.00   41.40  ? 593 HOH A O   1 
HETATM 2504 O  O   . HOH F 6 .   ? -25.803 -15.329 8.160   1.00   35.96  ? 594 HOH A O   1 
HETATM 2505 O  O   . HOH F 6 .   ? -15.178 11.562  34.883  1.00   43.02  ? 595 HOH A O   1 
HETATM 2506 O  O   . HOH F 6 .   ? 3.401   -1.460  8.576   1.00   26.50  ? 596 HOH A O   1 
HETATM 2507 O  O   . HOH F 6 .   ? -1.553  2.937   -7.206  1.00   36.42  ? 597 HOH A O   1 
HETATM 2508 O  O   . HOH F 6 .   ? -20.520 8.293   30.135  1.00   29.90  ? 598 HOH A O   1 
HETATM 2509 O  O   . HOH F 6 .   ? -25.138 8.651   26.211  1.00   37.49  ? 599 HOH A O   1 
HETATM 2510 O  O   . HOH F 6 .   ? 14.470  0.023   15.086  1.00   31.73  ? 600 HOH A O   1 
HETATM 2511 O  O   . HOH F 6 .   ? -11.483 0.821   -7.817  1.00   35.22  ? 601 HOH A O   1 
HETATM 2512 O  O   . HOH F 6 .   ? 11.380  -3.944  7.674   1.00   35.63  ? 602 HOH A O   1 
HETATM 2513 O  O   . HOH F 6 .   ? -25.586 4.244   3.898   1.00   39.89  ? 603 HOH A O   1 
HETATM 2514 O  O   . HOH F 6 .   ? -17.232 5.910   34.603  1.00   55.49  ? 604 HOH A O   1 
HETATM 2515 O  O   . HOH F 6 .   ? 15.313  -1.337  26.007  1.00   23.55  ? 605 HOH A O   1 
HETATM 2516 O  O   . HOH F 6 .   ? -7.187  -10.295 -4.678  1.00   38.00  ? 606 HOH A O   1 
HETATM 2517 O  O   . HOH F 6 .   ? 9.527   -5.050  -8.172  1.00   46.39  ? 607 HOH A O   1 
HETATM 2518 O  O   . HOH F 6 .   ? 6.317   -5.713  27.443  1.00   42.55  ? 608 HOH A O   1 
HETATM 2519 O  O   . HOH F 6 .   ? -3.855  -15.699 -2.035  1.00   36.44  ? 609 HOH A O   1 
HETATM 2520 O  O   . HOH F 6 .   ? -5.248  -13.540 34.384  1.00   41.20  ? 610 HOH A O   1 
HETATM 2521 O  O   . HOH F 6 .   ? -11.107 1.000   33.438  1.00   22.86  ? 611 HOH A O   1 
HETATM 2522 O  O   . HOH F 6 .   ? -12.884 21.642  26.165  1.00   22.23  ? 612 HOH A O   1 
HETATM 2523 O  O   . HOH F 6 .   ? 1.959   -14.143 20.403  1.00   34.64  ? 613 HOH A O   1 
HETATM 2524 O  O   . HOH F 6 .   ? 4.273   -11.525 23.189  1.00   42.62  ? 614 HOH A O   1 
HETATM 2525 O  O   . HOH F 6 .   ? -0.203  -7.067  -7.361  1.00   42.27  ? 615 HOH A O   1 
HETATM 2526 O  O   . HOH F 6 .   ? 3.928   -13.433 21.420  1.00   51.81  ? 616 HOH A O   1 
HETATM 2527 O  O   . HOH F 6 .   ? 15.215  -4.043  25.077  1.00   21.78  ? 617 HOH A O   1 
HETATM 2528 O  O   . HOH F 6 .   ? -11.814 10.784  0.792   1.00   28.21  ? 618 HOH A O   1 
HETATM 2529 O  O   . HOH F 6 .   ? 6.158   -5.365  -11.812 1.00   28.27  ? 619 HOH A O   1 
HETATM 2530 O  O   . HOH F 6 .   ? 10.108  -2.723  13.863  1.00   24.01  ? 620 HOH A O   1 
HETATM 2531 O  O   . HOH F 6 .   ? 2.958   -13.730 8.170   1.00   31.81  ? 621 HOH A O   1 
HETATM 2532 O  O   . HOH F 6 .   ? 13.000  -5.948  24.372  1.00   25.36  ? 622 HOH A O   1 
HETATM 2533 O  O   . HOH F 6 .   ? 14.165  -1.412  28.475  1.00   31.93  ? 623 HOH A O   1 
HETATM 2534 O  O   . HOH F 6 .   ? 6.905   -3.766  30.165  1.00   41.72  ? 624 HOH A O   1 
HETATM 2535 O  O   . HOH F 6 .   ? 1.677   -9.845  31.589  1.00   38.01  ? 625 HOH A O   1 
HETATM 2536 O  O   . HOH F 6 .   ? -1.156  -13.240 33.101  1.00   24.06  ? 626 HOH A O   1 
HETATM 2537 O  O   . HOH F 6 .   ? -4.599  -9.866  33.472  1.00   31.62  ? 627 HOH A O   1 
HETATM 2538 O  O   . HOH F 6 .   ? -15.657 -10.143 38.248  1.00   39.87  ? 628 HOH A O   1 
HETATM 2539 O  O   . HOH F 6 .   ? -17.009 -14.026 37.547  1.00   28.83  ? 629 HOH A O   1 
HETATM 2540 O  O   . HOH F 6 .   ? -17.590 -7.701  39.434  1.00   40.89  ? 630 HOH A O   1 
HETATM 2541 O  O   . HOH F 6 .   ? -15.761 3.630   35.270  1.00   32.56  ? 631 HOH A O   1 
HETATM 2542 O  O   . HOH F 6 .   ? -15.024 2.470   38.711  1.00   25.39  ? 632 HOH A O   1 
HETATM 2543 O  O   . HOH F 6 .   ? -25.104 9.582   12.956  1.00   27.35  ? 633 HOH A O   1 
HETATM 2544 O  O   . HOH F 6 .   ? -11.995 9.329   3.094   1.00   22.61  ? 634 HOH A O   1 
HETATM 2545 O  O   . HOH F 6 .   ? -21.737 19.448  12.112  1.00   27.98  ? 635 HOH A O   1 
HETATM 2546 O  O   . HOH F 6 .   ? -22.935 15.588  18.976  1.00   41.25  ? 636 HOH A O   1 
HETATM 2547 O  O   . HOH F 6 .   ? -21.865 19.736  17.382  1.00   40.99  ? 637 HOH A O   1 
HETATM 2548 O  O   . HOH F 6 .   ? -24.433 13.483  20.467  1.00   36.09  ? 638 HOH A O   1 
HETATM 2549 O  O   . HOH F 6 .   ? -16.627 -14.505 28.942  1.00   44.62  ? 639 HOH A O   1 
HETATM 2550 O  O   . HOH F 6 .   ? -22.707 -9.664  25.379  1.00   20.79  ? 640 HOH A O   1 
HETATM 2551 O  O   . HOH F 6 .   ? -25.567 -10.690 17.751  1.00   24.62  ? 641 HOH A O   1 
HETATM 2552 O  O   . HOH F 6 .   ? -16.827 -17.798 24.304  1.00   31.37  ? 642 HOH A O   1 
HETATM 2553 O  O   . HOH F 6 .   ? -15.410 -16.232 25.537  1.00   36.51  ? 643 HOH A O   1 
HETATM 2554 O  O   . HOH F 6 .   ? -3.487  18.079  21.038  1.00   22.36  ? 644 HOH A O   1 
HETATM 2555 O  O   . HOH F 6 .   ? -21.273 -19.636 6.612   1.00   25.32  ? 645 HOH A O   1 
HETATM 2556 O  O   . HOH F 6 .   ? -18.483 -3.809  -2.681  1.00   27.83  ? 646 HOH A O   1 
HETATM 2557 O  O   . HOH F 6 .   ? -13.349 -0.905  -6.033  1.00   36.33  ? 647 HOH A O   1 
HETATM 2558 O  O   . HOH F 6 .   ? -25.820 -5.817  13.169  1.00   37.60  ? 648 HOH A O   1 
HETATM 2559 O  O   . HOH F 6 .   ? 7.267   -3.714  -10.453 1.00   35.36  ? 649 HOH A O   1 
HETATM 2560 O  O   . HOH F 6 .   ? -22.347 -12.330 24.982  1.00   29.57  ? 650 HOH A O   1 
HETATM 2561 O  O   . HOH F 6 .   ? 1.803   8.139   27.942  1.00   31.52  ? 651 HOH A O   1 
HETATM 2562 O  O   . HOH F 6 .   ? -31.984 5.368   12.790  1.00   45.93  ? 652 HOH A O   1 
HETATM 2563 O  O   . HOH F 6 .   ? 6.607   -5.980  6.735   1.00   36.05  ? 653 HOH A O   1 
HETATM 2564 O  O   . HOH F 6 .   ? 3.333   -13.929 12.686  1.00   41.00  ? 654 HOH A O   1 
HETATM 2565 O  O   . HOH F 6 .   ? 0.404   7.113   29.868  1.00   31.88  ? 655 HOH A O   1 
HETATM 2566 O  O   . HOH F 6 .   ? -18.060 -9.080  34.953  1.00   44.82  ? 656 HOH A O   1 
HETATM 2567 O  O   . HOH F 6 .   ? -6.114  -20.905 26.358  1.00   27.51  ? 657 HOH A O   1 
HETATM 2568 O  O   . HOH F 6 .   ? -3.480  -20.011 26.938  1.00   30.43  ? 658 HOH A O   1 
HETATM 2569 O  O   . HOH F 6 .   ? -24.184 -0.023  1.304   1.00   33.40  ? 659 HOH A O   1 
HETATM 2570 O  O   . HOH F 6 .   ? 1.972   -4.307  -12.292 1.00   32.69  ? 660 HOH A O   1 
HETATM 2571 O  O   . HOH F 6 .   ? 9.003   -11.511 6.741   1.00   38.96  ? 661 HOH A O   1 
HETATM 2572 O  O   . HOH F 6 .   ? 6.002   -14.143 8.968   1.00   46.57  ? 662 HOH A O   1 
HETATM 2573 O  O   . HOH F 6 .   ? 12.149  -11.389 5.827   1.00   39.21  ? 663 HOH A O   1 
HETATM 2574 O  O   . HOH F 6 .   ? -12.471 13.526  4.825   1.00   33.30  ? 664 HOH A O   1 
HETATM 2575 O  O   . HOH F 6 .   ? -12.185 13.609  1.759   1.00   39.23  ? 665 HOH A O   1 
HETATM 2576 O  O   . HOH F 6 .   ? -17.006 18.180  22.215  1.00   37.57  ? 666 HOH A O   1 
HETATM 2577 O  O   . HOH F 6 .   ? -2.783  -19.344 6.287   1.00   33.72  ? 667 HOH A O   1 
HETATM 2578 O  O   . HOH F 6 .   ? -4.745  -21.714 5.343   1.00   35.29  ? 668 HOH A O   1 
HETATM 2579 O  O   . HOH F 6 .   ? -3.379  -17.821 -0.107  1.00   39.41  ? 669 HOH A O   1 
HETATM 2580 O  O   . HOH F 6 .   ? -0.361  -20.655 14.771  1.00   39.27  ? 670 HOH A O   1 
HETATM 2581 O  O   . HOH F 6 .   ? 6.146   5.498   29.130  1.00   43.33  ? 671 HOH A O   1 
HETATM 2582 O  O   . HOH F 6 .   ? -19.545 -20.731 5.159   1.00   33.69  ? 672 HOH A O   1 
HETATM 2583 O  O   . HOH F 6 .   ? -32.352 -14.349 3.975   1.00   50.72  ? 673 HOH A O   1 
HETATM 2584 O  O   . HOH F 6 .   ? -12.846 -8.918  -3.264  1.00   33.53  ? 674 HOH A O   1 
HETATM 2585 O  O   . HOH F 6 .   ? 10.371  -5.320  -5.706  1.00   43.89  ? 675 HOH A O   1 
HETATM 2586 O  O   . HOH F 6 .   ? -4.429  -1.555  38.050  1.00   24.60  ? 676 HOH A O   1 
HETATM 2587 O  O   . HOH F 6 .   ? -5.124  -2.152  40.640  1.00   41.53  ? 677 HOH A O   1 
HETATM 2588 O  O   . HOH F 6 .   ? -1.144  -6.090  36.511  1.00   28.90  ? 678 HOH A O   1 
HETATM 2589 O  O   . HOH F 6 .   ? -23.086 -18.055 20.571  1.00   48.03  ? 679 HOH A O   1 
HETATM 2590 O  O   . HOH F 6 .   ? 5.659   -12.993 11.192  1.00   39.99  ? 680 HOH A O   1 
HETATM 2591 O  O   . HOH F 6 .   ? 4.012   -1.010  36.341  1.00   41.78  ? 681 HOH A O   1 
HETATM 2592 O  O   . HOH F 6 .   ? -0.832  9.174   33.087  1.00   29.33  ? 682 HOH A O   1 
HETATM 2593 O  O   . HOH F 6 .   ? -12.100 -4.297  37.685  1.00   31.71  ? 683 HOH A O   1 
HETATM 2594 O  O   . HOH F 6 .   ? -13.307 -16.708 -0.089  1.00   40.26  ? 684 HOH A O   1 
HETATM 2595 O  O   . HOH F 6 .   ? -12.488 -24.825 -4.590  1.00   43.58  ? 685 HOH A O   1 
HETATM 2596 O  O   . HOH F 6 .   ? -19.845 17.163  23.022  1.00   39.51  ? 686 HOH A O   1 
HETATM 2597 O  O   . HOH F 6 .   ? -20.090 15.870  18.954  1.00   27.48  ? 687 HOH A O   1 
HETATM 2598 O  O   . HOH F 6 .   ? 9.762   -0.054  14.414  1.00   31.45  ? 688 HOH A O   1 
HETATM 2599 O  O   . HOH F 6 .   ? -8.486  -15.522 32.941  1.00   29.27  ? 689 HOH A O   1 
HETATM 2600 O  O   . HOH F 6 .   ? -3.390  -16.193 3.076   1.00   40.29  ? 690 HOH A O   1 
HETATM 2601 O  O   . HOH F 6 .   ? 8.108   -5.254  -0.198  1.00   46.36  ? 691 HOH A O   1 
HETATM 2602 O  O   . HOH F 6 .   ? 4.300   11.058  21.969  1.00   48.12  ? 692 HOH A O   1 
HETATM 2603 O  O   . HOH F 6 .   ? -23.477 19.909  10.272  1.00   43.87  ? 693 HOH A O   1 
HETATM 2604 O  O   . HOH F 6 .   ? -17.826 -22.065 5.935   1.00   25.11  ? 694 HOH A O   1 
HETATM 2605 O  O   . HOH F 6 .   ? 1.453   -5.956  38.511  1.00   49.85  ? 695 HOH A O   1 
HETATM 2606 O  O   . HOH F 6 .   ? 9.397   1.958   11.870  1.00   35.27  ? 696 HOH A O   1 
HETATM 2607 O  O   . HOH F 6 .   ? 3.694   4.218   10.296  1.00   48.53  ? 697 HOH A O   1 
HETATM 2608 O  O   . HOH F 6 .   ? 4.427   -7.769  -11.448 1.00   41.10  ? 698 HOH A O   1 
HETATM 2609 O  O   . HOH F 6 .   ? 5.949   -9.762  -9.808  1.00   51.87  ? 699 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   ? 0.2754 0.4465 0.3855 0.0080  0.1001  0.1238  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.2055 0.3589 0.3693 -0.0137 0.0908  0.0856  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.2361 0.2626 0.3299 -0.0148 0.0944  0.0074  4   HIS A C   
4    O  O   . HIS A 4   ? 0.2547 0.2716 0.2992 -0.0160 0.1044  -0.0063 4   HIS A O   
5    C  CB  . HIS A 4   ? 0.1718 0.5026 0.4393 0.0081  0.0856  0.1703  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.5655 0.4082 0.5594 0.0006  0.1421  0.2542  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.4282 0.8765 0.8535 -0.1991 0.2361  0.0452  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.6387 0.4181 0.6531 0.0269  -0.2089 0.2046  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.7318 0.7949 1.4299 0.0627  0.0983  0.2232  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.8098 0.5565 1.3459 -0.0115 0.0126  0.0205  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.1641 0.2489 0.2712 -0.0313 0.0559  0.0057  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1428 0.1941 0.2404 -0.0386 0.0483  0.0188  5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1356 0.2201 0.1967 0.0027  0.0454  0.0247  5   TRP A C   
14   O  O   . TRP A 5   ? 0.2002 0.2108 0.2169 -0.0219 0.0573  0.0142  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1361 0.1880 0.2489 -0.0023 0.0390  -0.0215 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1404 0.1650 0.1870 -0.0230 0.0392  0.0035  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.1560 0.1916 0.2474 -0.0192 0.0399  0.0296  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1272 0.1835 0.1624 -0.0153 0.0271  -0.0115 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.1780 0.1897 0.2045 0.0046  0.0285  0.0317  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1414 0.1993 0.1809 0.0000  0.0198  0.0173  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1387 0.1905 0.1632 -0.0188 0.0436  -0.0198 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1562 0.2349 0.1731 -0.0115 0.0218  -0.0118 5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1579 0.1941 0.1611 -0.0057 0.0307  -0.0307 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1560 0.2327 0.1685 -0.0043 0.0259  -0.0275 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1686 0.1668 0.2035 0.0030  0.0586  -0.0019 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1801 0.1781 0.2002 -0.0379 0.0653  -0.0265 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1333 0.1861 0.2152 0.0080  0.0715  -0.0015 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1272 0.1869 0.2108 0.0164  0.0461  0.0024  6   GLY A O   
29   N  N   A TYR A 7   ? 0.1395 0.1423 0.1562 0.0320  0.0197  0.0119  7   TYR A N   
30   N  N   B TYR A 7   ? 0.1290 0.1817 0.2802 -0.0093 0.0649  -0.0261 7   TYR A N   
31   C  CA  A TYR A 7   ? 0.1110 0.1185 0.1356 0.0091  -0.0153 -0.0115 7   TYR A CA  
32   C  CA  B TYR A 7   ? 0.1201 0.1773 0.1861 -0.0120 0.0261  -0.0502 7   TYR A CA  
33   C  C   A TYR A 7   ? 0.1324 0.1208 0.2465 0.0073  0.0540  -0.0182 7   TYR A C   
34   C  C   B TYR A 7   ? 0.1219 0.1960 0.2404 -0.0013 -0.0103 -0.0335 7   TYR A C   
35   O  O   A TYR A 7   ? 0.1316 0.1375 0.3596 0.0109  0.0269  -0.0137 7   TYR A O   
36   O  O   B TYR A 7   ? 0.1334 0.1456 0.5213 -0.0306 0.0423  -0.0900 7   TYR A O   
37   C  CB  A TYR A 7   ? 0.0907 0.1230 0.1754 0.0074  0.0109  0.0006  7   TYR A CB  
38   C  CB  B TYR A 7   ? 0.1332 0.2125 0.1756 0.0109  0.0209  -0.0344 7   TYR A CB  
39   C  CG  A TYR A 7   ? 0.0992 0.1118 0.1070 -0.0074 0.0076  0.0104  7   TYR A CG  
40   C  CG  B TYR A 7   ? 0.1280 0.1395 0.1545 -0.0076 0.0034  -0.0175 7   TYR A CG  
41   C  CD1 A TYR A 7   ? 0.0996 0.1001 0.1113 -0.0109 -0.0062 0.0048  7   TYR A CD1 
42   C  CD1 B TYR A 7   ? 0.0851 0.1797 0.1326 -0.0041 0.0136  -0.0109 7   TYR A CD1 
43   C  CD2 A TYR A 7   ? 0.1131 0.1340 0.1009 -0.0024 0.0093  0.0082  7   TYR A CD2 
44   C  CD2 B TYR A 7   ? 0.1043 0.1553 0.1923 -0.0131 0.0147  0.0010  7   TYR A CD2 
45   C  CE1 A TYR A 7   ? 0.0956 0.1230 0.0904 -0.0131 -0.0003 0.0020  7   TYR A CE1 
46   C  CE1 B TYR A 7   ? 0.1097 0.1465 0.1428 -0.0052 0.0000  0.0059  7   TYR A CE1 
47   C  CE2 A TYR A 7   ? 0.0979 0.1414 0.0925 -0.0140 0.0010  -0.0026 7   TYR A CE2 
48   C  CE2 B TYR A 7   ? 0.1359 0.1527 0.1351 -0.0054 0.0082  0.0195  7   TYR A CE2 
49   C  CZ  A TYR A 7   ? 0.0926 0.1088 0.0920 -0.0109 0.0059  -0.0057 7   TYR A CZ  
50   C  CZ  B TYR A 7   ? 0.1263 0.1297 0.1368 -0.0059 0.0120  0.0003  7   TYR A CZ  
51   O  OH  A TYR A 7   ? 0.1335 0.0988 0.0996 0.0012  0.0043  -0.0020 7   TYR A OH  
52   O  OH  B TYR A 7   ? 0.1462 0.1386 0.1518 0.0093  -0.0109 -0.0006 7   TYR A OH  
53   N  N   A GLY A 8   ? 0.0979 0.1712 0.1879 0.0165  0.0315  0.0040  8   GLY A N   
54   N  N   B GLY A 8   ? 0.1404 0.2117 0.2453 0.0126  0.0192  -0.0204 8   GLY A N   
55   C  CA  A GLY A 8   ? 0.1203 0.1817 0.1985 0.0230  -0.0052 -0.0487 8   GLY A CA  
56   C  CA  B GLY A 8   ? 0.2288 0.1472 0.3125 0.0406  0.0390  0.0098  8   GLY A CA  
57   C  C   A GLY A 8   ? 0.1650 0.2092 0.1814 0.0024  0.0153  -0.0296 8   GLY A C   
58   C  C   B GLY A 8   ? 0.0907 0.2669 0.2763 -0.0454 0.0054  -0.0640 8   GLY A C   
59   O  O   A GLY A 8   ? 0.1429 0.1782 0.1641 0.0438  0.0031  -0.0076 8   GLY A O   
60   O  O   B GLY A 8   ? 0.2428 0.1595 0.3409 -0.0617 0.1791  -0.1168 8   GLY A O   
61   N  N   A LYS A 9   ? 0.1234 0.1693 0.1940 0.0131  -0.0027 -0.0173 9   LYS A N   
62   N  N   B LYS A 9   ? 0.1624 0.1871 0.3449 -0.0439 0.0406  -0.0806 9   LYS A N   
63   C  CA  A LYS A 9   ? 0.1536 0.2288 0.1903 0.0298  -0.0013 -0.0221 9   LYS A CA  
64   C  CA  B LYS A 9   ? 0.1212 0.2935 0.3359 0.0142  0.0208  -0.0623 9   LYS A CA  
65   C  C   A LYS A 9   ? 0.1569 0.1958 0.2003 0.0261  0.0035  0.0052  9   LYS A C   
66   C  C   B LYS A 9   ? 0.1488 0.1983 0.2500 0.0183  0.0450  -0.0023 9   LYS A C   
67   O  O   A LYS A 9   ? 0.1577 0.2125 0.1888 0.0221  -0.0076 -0.0337 9   LYS A O   
68   O  O   B LYS A 9   ? 0.1677 0.3046 0.2773 -0.0231 0.0386  -0.0619 9   LYS A O   
69   C  CB  A LYS A 9   ? 0.2328 0.2343 0.2569 0.0410  -0.0741 -0.1150 9   LYS A CB  
70   C  CB  B LYS A 9   ? 0.3111 0.0983 0.5421 -0.0186 0.0430  -0.0571 9   LYS A CB  
71   C  CG  A LYS A 9   ? 0.3671 0.2222 0.3499 -0.0093 0.0085  -0.1342 9   LYS A CG  
72   C  CG  B LYS A 9   ? 0.3826 0.4077 0.4781 0.0807  0.0282  0.0939  9   LYS A CG  
73   C  CD  A LYS A 9   ? 0.5895 0.5267 0.1808 0.0860  0.1190  -0.0048 9   LYS A CD  
74   C  CD  B LYS A 9   ? 0.3503 0.1897 0.5551 -0.0518 0.0687  0.0093  9   LYS A CD  
75   C  CE  A LYS A 9   ? 0.7706 0.4458 0.5906 0.2538  0.0131  -0.1647 9   LYS A CE  
76   C  CE  B LYS A 9   ? 0.3765 0.5406 0.3140 0.0447  0.0608  -0.0162 9   LYS A CE  
77   N  NZ  A LYS A 9   ? 1.1013 0.5540 0.2342 0.0671  -0.0436 -0.0208 9   LYS A NZ  
78   N  NZ  B LYS A 9   ? 0.3984 0.3208 0.2824 0.0597  0.0666  0.0469  9   LYS A NZ  
79   N  N   A HIS A 10  ? 0.1031 0.1745 0.1958 0.0263  0.0351  -0.0076 10  HIS A N   
80   N  N   B HIS A 10  ? 0.1455 0.1907 0.2471 0.0240  0.0296  -0.0109 10  HIS A N   
81   C  CA  A HIS A 10  ? 0.1298 0.1766 0.1527 0.0296  -0.0120 -0.0104 10  HIS A CA  
82   C  CA  B HIS A 10  ? 0.1246 0.2073 0.2536 0.0054  0.0467  -0.0243 10  HIS A CA  
83   C  C   A HIS A 10  ? 0.0710 0.2544 0.1744 0.0087  -0.0165 -0.0390 10  HIS A C   
84   C  C   B HIS A 10  ? 0.2298 0.2231 0.3319 0.0038  -0.0355 -0.0017 10  HIS A C   
85   O  O   A HIS A 10  ? 0.0627 0.1482 0.2046 0.0148  -0.0125 -0.0405 10  HIS A O   
86   O  O   B HIS A 10  ? 0.1676 0.1449 0.3409 0.0217  0.1080  0.0030  10  HIS A O   
87   C  CB  A HIS A 10  ? 0.0841 0.2558 0.2011 0.0702  0.0087  -0.0328 10  HIS A CB  
88   C  CB  B HIS A 10  ? 0.1190 0.1897 0.2197 0.0027  0.0221  0.0093  10  HIS A CB  
89   C  CG  A HIS A 10  ? 0.1366 0.2117 0.1588 -0.0197 0.0153  -0.0186 10  HIS A CG  
90   C  CG  B HIS A 10  ? 0.1465 0.2002 0.2407 0.0302  0.0366  -0.0043 10  HIS A CG  
91   N  ND1 A HIS A 10  ? 0.2117 0.2270 0.1879 0.0239  0.0241  -0.0135 10  HIS A ND1 
92   N  ND1 B HIS A 10  ? 0.1147 0.2037 0.3869 0.0093  0.0274  -0.0193 10  HIS A ND1 
93   C  CD2 A HIS A 10  ? 0.1281 0.2723 0.2091 -0.0085 0.0085  -0.0771 10  HIS A CD2 
94   C  CD2 B HIS A 10  ? 0.1465 0.2363 0.2709 0.0207  0.0412  -0.0208 10  HIS A CD2 
95   C  CE1 A HIS A 10  ? 0.1185 0.2266 0.2240 0.0449  0.0331  -0.0287 10  HIS A CE1 
96   C  CE1 B HIS A 10  ? 0.2117 0.1779 0.3506 0.0093  0.0789  -0.0438 10  HIS A CE1 
97   N  NE2 A HIS A 10  ? 0.2073 0.2842 0.1976 0.0118  0.0348  -0.1111 10  HIS A NE2 
98   N  NE2 B HIS A 10  ? 0.3036 0.1983 0.2878 0.0666  0.0527  -0.0333 10  HIS A NE2 
99   N  N   . ASN A 11  ? 0.1596 0.2284 0.3208 0.0405  0.1106  0.0109  11  ASN A N   
100  C  CA  . ASN A 11  ? 0.1446 0.2161 0.2737 0.0562  0.0939  0.0175  11  ASN A CA  
101  C  C   . ASN A 11  ? 0.1595 0.1879 0.2361 0.0416  0.0793  0.0162  11  ASN A C   
102  O  O   . ASN A 11  ? 0.1580 0.2043 0.2313 0.0403  0.0842  0.0119  11  ASN A O   
103  C  CB  . ASN A 11  ? 0.1588 0.2065 0.2587 0.0076  0.0970  -0.0059 11  ASN A CB  
104  C  CG  . ASN A 11  ? 0.1580 0.2277 0.2334 0.0046  0.0904  -0.0210 11  ASN A CG  
105  O  OD1 . ASN A 11  ? 0.2171 0.2559 0.2802 -0.0104 0.0869  0.0165  11  ASN A OD1 
106  N  ND2 . ASN A 11  ? 0.2300 0.2374 0.2723 0.0120  0.0816  0.0093  11  ASN A ND2 
107  N  N   . GLY A 12  ? 0.1553 0.1964 0.2540 0.0285  0.0825  0.0054  12  GLY A N   
108  C  CA  . GLY A 12  ? 0.1421 0.2544 0.2159 0.0331  0.0863  -0.0049 12  GLY A CA  
109  C  C   . GLY A 12  ? 0.1395 0.1737 0.1976 0.0252  0.0471  0.0423  12  GLY A C   
110  O  O   . GLY A 12  ? 0.1277 0.1831 0.2240 0.0375  0.0313  0.0263  12  GLY A O   
111  N  N   . PRO A 13  ? 0.1207 0.1535 0.2064 0.0010  0.0498  -0.0027 13  PRO A N   
112  C  CA  . PRO A 13  ? 0.1147 0.1632 0.2020 0.0043  0.0467  0.0057  13  PRO A CA  
113  C  C   . PRO A 13  ? 0.1633 0.1333 0.1875 0.0020  0.0527  0.0057  13  PRO A C   
114  O  O   . PRO A 13  ? 0.1185 0.1735 0.2143 -0.0109 0.0425  -0.0115 13  PRO A O   
115  C  CB  . PRO A 13  ? 0.1488 0.1560 0.2188 -0.0154 0.0665  -0.0063 13  PRO A CB  
116  C  CG  . PRO A 13  ? 0.1401 0.1571 0.2186 -0.0065 0.0542  -0.0060 13  PRO A CG  
117  C  CD  . PRO A 13  ? 0.1500 0.1933 0.2202 0.0350  0.0588  0.0000  13  PRO A CD  
118  N  N   . GLU A 14  ? 0.1695 0.1546 0.2037 0.0368  0.0230  0.0220  14  GLU A N   
119  C  CA  . GLU A 14  ? 0.2222 0.1585 0.2379 0.0423  0.0509  0.0386  14  GLU A CA  
120  C  C   . GLU A 14  ? 0.1493 0.2011 0.2020 0.0709  -0.0120 0.0152  14  GLU A C   
121  O  O   . GLU A 14  ? 0.1999 0.2020 0.2415 0.0643  0.0187  0.0458  14  GLU A O   
122  C  CB  . GLU A 14  ? 0.3574 0.1808 0.2511 0.0430  0.0146  0.0252  14  GLU A CB  
123  C  CG  . GLU A 14  ? 0.2092 0.3105 0.2716 0.0015  -0.0154 0.0181  14  GLU A CG  
124  C  CD  . GLU A 14  ? 0.2637 0.3276 0.2990 0.0741  -0.0405 0.0049  14  GLU A CD  
125  O  OE1 . GLU A 14  ? 0.2428 0.2338 0.3373 0.0922  -0.0841 -0.0908 14  GLU A OE1 
126  O  OE2 . GLU A 14  ? 0.6689 0.2439 0.2849 0.1146  0.1203  -0.0015 14  GLU A OE2 
127  N  N   . HIS A 15  ? 0.1234 0.1735 0.2307 0.0472  0.0449  0.0175  15  HIS A N   
128  C  CA  . HIS A 15  ? 0.1230 0.1744 0.2389 0.0329  0.0230  0.0087  15  HIS A CA  
129  C  C   . HIS A 15  ? 0.0948 0.1770 0.2206 0.0197  0.0419  -0.0051 15  HIS A C   
130  O  O   . HIS A 15  ? 0.0935 0.1915 0.2608 0.0262  0.0296  0.0359  15  HIS A O   
131  C  CB  . HIS A 15  ? 0.1106 0.2065 0.2608 0.0653  0.0331  0.0154  15  HIS A CB  
132  C  CG  . HIS A 15  ? 0.1439 0.2115 0.2433 0.0560  0.0295  0.0252  15  HIS A CG  
133  N  ND1 . HIS A 15  ? 0.1718 0.3057 0.2377 0.1184  0.0216  -0.0006 15  HIS A ND1 
134  C  CD2 . HIS A 15  ? 0.1905 0.2125 0.2446 0.0842  0.0603  0.0197  15  HIS A CD2 
135  C  CE1 . HIS A 15  ? 0.2850 0.3373 0.2377 0.1620  0.0041  -0.0399 15  HIS A CE1 
136  N  NE2 . HIS A 15  ? 0.3032 0.2651 0.3021 0.1712  0.0305  -0.0082 15  HIS A NE2 
137  N  N   . TRP A 16  ? 0.0847 0.1676 0.2266 0.0243  0.0237  0.0142  16  TRP A N   
138  C  CA  . TRP A 16  ? 0.0697 0.1449 0.2232 0.0183  0.0065  -0.0085 16  TRP A CA  
139  C  C   . TRP A 16  ? 0.0662 0.1633 0.2114 0.0283  -0.0013 0.0142  16  TRP A C   
140  O  O   . TRP A 16  ? 0.0882 0.1532 0.2425 0.0120  -0.0131 0.0218  16  TRP A O   
141  C  CB  . TRP A 16  ? 0.0666 0.1562 0.1959 0.0284  0.0163  -0.0074 16  TRP A CB  
142  C  CG  . TRP A 16  ? 0.0812 0.1342 0.1810 -0.0012 0.0098  -0.0109 16  TRP A CG  
143  C  CD1 . TRP A 16  ? 0.1061 0.1659 0.1775 0.0183  0.0270  0.0136  16  TRP A CD1 
144  C  CD2 . TRP A 16  ? 0.0754 0.1313 0.1879 -0.0068 0.0259  0.0031  16  TRP A CD2 
145  N  NE1 . TRP A 16  ? 0.0973 0.1580 0.1815 0.0059  0.0362  -0.0071 16  TRP A NE1 
146  C  CE2 . TRP A 16  ? 0.0970 0.1190 0.1771 0.0081  0.0306  0.0040  16  TRP A CE2 
147  C  CE3 . TRP A 16  ? 0.0754 0.1262 0.1993 0.0049  0.0315  0.0027  16  TRP A CE3 
148  C  CZ2 . TRP A 16  ? 0.1036 0.1298 0.1844 -0.0015 0.0364  0.0087  16  TRP A CZ2 
149  C  CZ3 . TRP A 16  ? 0.0680 0.1446 0.1985 -0.0031 0.0390  -0.0063 16  TRP A CZ3 
150  C  CH2 . TRP A 16  ? 0.1185 0.1350 0.1624 0.0076  0.0340  -0.0006 16  TRP A CH2 
151  N  N   . HIS A 17  ? 0.0627 0.1756 0.2045 0.0073  -0.0082 -0.0076 17  HIS A N   
152  C  CA  . HIS A 17  ? 0.0763 0.1738 0.2099 0.0035  -0.0071 0.0108  17  HIS A CA  
153  C  C   . HIS A 17  ? 0.0969 0.2064 0.2246 -0.0076 0.0063  0.0017  17  HIS A C   
154  O  O   . HIS A 17  ? 0.0750 0.2204 0.2533 -0.0024 -0.0161 0.0120  17  HIS A O   
155  C  CB  . HIS A 17  ? 0.0894 0.2148 0.2187 0.0153  -0.0043 -0.0031 17  HIS A CB  
156  C  CG  . HIS A 17  ? 0.1088 0.2056 0.2640 0.0131  0.0000  0.0417  17  HIS A CG  
157  N  ND1 . HIS A 17  ? 0.0882 0.2967 0.2917 0.0068  -0.0186 0.0542  17  HIS A ND1 
158  C  CD2 . HIS A 17  ? 0.1439 0.2178 0.2576 0.0649  0.0225  0.0658  17  HIS A CD2 
159  C  CE1 . HIS A 17  ? 0.1317 0.2687 0.3183 0.0688  0.0318  0.0601  17  HIS A CE1 
160  N  NE2 . HIS A 17  ? 0.1465 0.2363 0.2924 0.0604  0.0186  0.0728  17  HIS A NE2 
161  N  N   . LYS A 18  ? 0.0702 0.1924 0.2648 0.0086  0.0057  0.0131  18  LYS A N   
162  C  CA  . LYS A 18  ? 0.0626 0.2630 0.2657 -0.0071 0.0104  0.0390  18  LYS A CA  
163  C  C   . LYS A 18  ? 0.0780 0.2407 0.3043 -0.0251 -0.0096 0.0318  18  LYS A C   
164  O  O   . LYS A 18  ? 0.1369 0.2500 0.4232 -0.0513 -0.0577 0.0842  18  LYS A O   
165  C  CB  . LYS A 18  ? 0.0934 0.2666 0.2608 0.0186  0.0317  0.0331  18  LYS A CB  
166  C  CG  . LYS A 18  ? 0.0886 0.2460 0.3147 0.0557  0.0337  0.0540  18  LYS A CG  
167  C  CD  . LYS A 18  ? 0.0834 0.2716 0.3111 0.0230  -0.0048 0.0693  18  LYS A CD  
168  C  CE  . LYS A 18  ? 0.1097 0.2737 0.2795 0.0555  0.0307  0.0586  18  LYS A CE  
169  N  NZ  . LYS A 18  ? 0.0974 0.3362 0.2569 0.0904  0.0238  0.0838  18  LYS A NZ  
170  N  N   . ASP A 19  ? 0.0882 0.2237 0.2745 -0.0031 0.0135  0.0176  19  ASP A N   
171  C  CA  . ASP A 19  ? 0.1221 0.2136 0.2942 0.0048  0.0125  0.0494  19  ASP A CA  
172  C  C   . ASP A 19  ? 0.1106 0.1676 0.2694 -0.0034 0.0141  0.0423  19  ASP A C   
173  O  O   . ASP A 19  ? 0.1312 0.1879 0.3323 -0.0274 0.0263  0.0456  19  ASP A O   
174  C  CB  . ASP A 19  ? 0.1471 0.3014 0.2766 0.0119  -0.0142 0.0606  19  ASP A CB  
175  C  CG  . ASP A 19  ? 0.1050 0.6506 0.4476 0.0052  0.0326  -0.1171 19  ASP A CG  
176  O  OD1 . ASP A 19  ? 0.1984 0.5411 0.3840 -0.0304 0.0768  0.0152  19  ASP A OD1 
177  O  OD2 . ASP A 19  ? 0.3686 0.9937 0.6916 -0.1843 0.1492  -0.3632 19  ASP A OD2 
178  N  N   . PHE A 20  ? 0.0908 0.1888 0.2504 -0.0115 0.0034  0.0335  20  PHE A N   
179  C  CA  . PHE A 20  ? 0.0697 0.1897 0.2885 -0.0049 0.0023  0.0291  20  PHE A CA  
180  C  C   . PHE A 20  ? 0.0688 0.1905 0.2569 -0.0166 0.0082  0.0087  20  PHE A C   
181  O  O   . PHE A 20  ? 0.0934 0.1649 0.2386 -0.0103 0.0041  0.0098  20  PHE A O   
182  C  CB  . PHE A 20  ? 0.0935 0.1959 0.2422 -0.0015 0.0065  0.0326  20  PHE A CB  
183  C  CG  . PHE A 20  ? 0.0724 0.2188 0.2554 -0.0353 -0.0006 0.0465  20  PHE A CG  
184  C  CD1 . PHE A 20  ? 0.1203 0.2313 0.2784 -0.0351 0.0060  0.0557  20  PHE A CD1 
185  C  CD2 . PHE A 20  ? 0.0935 0.2845 0.2471 -0.0364 -0.0070 0.0175  20  PHE A CD2 
186  C  CE1 . PHE A 20  ? 0.1313 0.3377 0.2831 -0.0386 -0.0124 0.0974  20  PHE A CE1 
187  C  CE2 . PHE A 20  ? 0.1106 0.3291 0.2863 -0.0071 -0.0184 0.0430  20  PHE A CE2 
188  C  CZ  . PHE A 20  ? 0.1005 0.3026 0.2989 -0.0436 0.0113  0.0723  20  PHE A CZ  
189  N  N   A PRO A 21  ? 0.0806 0.1791 0.2486 -0.0035 0.0171  0.0227  21  PRO A N   
190  N  N   B PRO A 21  ? 0.0988 0.2052 0.2160 -0.0087 -0.0195 0.0038  21  PRO A N   
191  C  CA  A PRO A 21  ? 0.0653 0.2425 0.2773 -0.0388 -0.0015 0.0295  21  PRO A CA  
192  C  CA  B PRO A 21  ? 0.1052 0.2320 0.1842 -0.0608 -0.0186 0.0146  21  PRO A CA  
193  C  C   A PRO A 21  ? 0.1036 0.1594 0.1831 -0.0210 -0.0206 -0.0041 21  PRO A C   
194  C  C   B PRO A 21  ? 0.1203 0.1941 0.1445 -0.0296 -0.0186 -0.0107 21  PRO A C   
195  O  O   A PRO A 21  ? 0.0649 0.2020 0.1550 -0.0076 -0.0230 -0.0186 21  PRO A O   
196  O  O   B PRO A 21  ? 0.1101 0.1862 0.1272 -0.0163 -0.0197 -0.0176 21  PRO A O   
197  C  CB  A PRO A 21  ? 0.1396 0.2306 0.3143 -0.0846 -0.0315 0.0564  21  PRO A CB  
198  C  CB  B PRO A 21  ? 0.1448 0.2554 0.2867 -0.1172 -0.0524 0.0465  21  PRO A CB  
199  C  CG  A PRO A 21  ? 0.0987 0.2046 0.3054 -0.0943 -0.0403 0.0068  21  PRO A CG  
200  C  CG  B PRO A 21  ? 0.1034 0.3906 0.2716 -0.0423 -0.0274 0.0710  21  PRO A CG  
201  C  CD  A PRO A 21  ? 0.0904 0.2249 0.2569 -0.0399 0.0665  -0.0006 21  PRO A CD  
202  C  CD  B PRO A 21  ? 0.1045 0.2177 0.2012 -0.0172 0.0219  0.0208  21  PRO A CD  
203  N  N   A ILE A 22  ? 0.0903 0.1501 0.1704 -0.0098 -0.0006 -0.0063 22  ILE A N   
204  N  N   B ILE A 22  ? 0.0983 0.1859 0.1261 -0.0269 -0.0265 -0.0192 22  ILE A N   
205  C  CA  A ILE A 22  ? 0.0829 0.1448 0.2288 -0.0065 0.0142  -0.0031 22  ILE A CA  
206  C  CA  B ILE A 22  ? 0.1017 0.1668 0.1246 -0.0082 -0.0241 -0.0091 22  ILE A CA  
207  C  C   A ILE A 22  ? 0.0886 0.1360 0.2030 -0.0131 -0.0068 -0.0197 22  ILE A C   
208  C  C   B ILE A 22  ? 0.0878 0.1360 0.2073 -0.0048 -0.0198 -0.0331 22  ILE A C   
209  O  O   A ILE A 22  ? 0.0807 0.1612 0.1632 -0.0126 -0.0219 -0.0027 22  ILE A O   
210  O  O   B ILE A 22  ? 0.0846 0.1667 0.1993 -0.0030 -0.0204 -0.0489 22  ILE A O   
211  C  CB  A ILE A 22  ? 0.1058 0.1253 0.1905 -0.0282 -0.0093 -0.0142 22  ILE A CB  
212  C  CB  B ILE A 22  ? 0.1133 0.1571 0.1167 0.0020  -0.0185 0.0137  22  ILE A CB  
213  C  CG1 A ILE A 22  ? 0.1057 0.1588 0.1800 -0.0098 -0.0104 -0.0306 22  ILE A CG1 
214  C  CG1 B ILE A 22  ? 0.1395 0.1509 0.1852 0.0165  -0.0015 -0.0153 22  ILE A CG1 
215  C  CG2 A ILE A 22  ? 0.1005 0.1791 0.1694 0.0013  0.0108  0.0163  22  ILE A CG2 
216  C  CG2 B ILE A 22  ? 0.1212 0.1506 0.1237 -0.0597 -0.0197 0.0308  22  ILE A CG2 
217  C  CD1 A ILE A 22  ? 0.1331 0.1392 0.2460 -0.0098 -0.0260 -0.0164 22  ILE A CD1 
218  C  CD1 B ILE A 22  ? 0.2406 0.2020 0.2878 -0.0049 -0.0408 -0.0662 22  ILE A CD1 
219  N  N   . ALA A 23  ? 0.0882 0.1465 0.1968 -0.0091 -0.0175 -0.0113 23  ALA A N   
220  C  CA  . ALA A 23  ? 0.1041 0.1421 0.2079 -0.0043 0.0031  -0.0136 23  ALA A CA  
221  C  C   . ALA A 23  ? 0.0758 0.1563 0.2224 -0.0020 -0.0068 -0.0114 23  ALA A C   
222  O  O   . ALA A 23  ? 0.0973 0.1664 0.2117 -0.0098 0.0000  -0.0038 23  ALA A O   
223  C  CB  . ALA A 23  ? 0.0781 0.1729 0.2266 0.0010  -0.0087 -0.0208 23  ALA A CB  
224  N  N   . LYS A 24  ? 0.1172 0.1762 0.1870 0.0086  -0.0131 -0.0057 24  LYS A N   
225  C  CA  . LYS A 24  ? 0.1027 0.2187 0.1887 0.0017  -0.0254 -0.0076 24  LYS A CA  
226  C  C   . LYS A 24  ? 0.1409 0.2097 0.2171 -0.0062 -0.0359 -0.0262 24  LYS A C   
227  O  O   . LYS A 24  ? 0.1404 0.2809 0.2219 0.0043  -0.0333 -0.0141 24  LYS A O   
228  C  CB  . LYS A 24  ? 0.1282 0.2179 0.2381 0.0357  -0.0240 0.0170  24  LYS A CB  
229  C  CG  . LYS A 24  ? 0.1518 0.2720 0.2334 0.0719  0.0015  0.0197  24  LYS A CG  
230  C  CD  . LYS A 24  ? 0.1606 0.3262 0.3625 0.0577  0.0041  0.0350  24  LYS A CD  
231  C  CE  . LYS A 24  ? 0.1659 0.3901 0.3456 0.0952  0.0076  0.0785  24  LYS A CE  
232  N  NZ  . LYS A 24  ? 0.5062 0.3686 0.4480 -0.0456 0.0549  -0.0856 24  LYS A NZ  
233  N  N   . GLY A 25  ? 0.1251 0.2021 0.2099 0.0093  -0.0197 -0.0199 25  GLY A N   
234  C  CA  . GLY A 25  ? 0.1331 0.2157 0.2291 -0.0306 0.0030  -0.0344 25  GLY A CA  
235  C  C   . GLY A 25  ? 0.1120 0.2055 0.1738 -0.0043 -0.0373 -0.0392 25  GLY A C   
236  O  O   . GLY A 25  ? 0.1342 0.2098 0.1834 -0.0052 -0.0197 -0.0227 25  GLY A O   
237  N  N   . GLU A 26  ? 0.1158 0.2374 0.1712 -0.0013 -0.0423 -0.0463 26  GLU A N   
238  C  CA  . GLU A 26  ? 0.1331 0.2655 0.1524 -0.0086 -0.0337 -0.0518 26  GLU A CA  
239  C  C   . GLU A 26  ? 0.1291 0.1986 0.1242 0.0049  -0.0198 -0.0263 26  GLU A C   
240  O  O   . GLU A 26  ? 0.1756 0.2368 0.1226 -0.0142 -0.0320 -0.0059 26  GLU A O   
241  C  CB  . GLU A 26  ? 0.1826 0.3413 0.1729 -0.0292 -0.0520 -0.1076 26  GLU A CB  
242  C  CG  . GLU A 26  ? 0.2087 0.3700 0.1677 -0.0142 -0.0584 -0.0507 26  GLU A CG  
243  C  CD  . GLU A 26  ? 0.3395 0.5173 0.3140 0.0070  -0.1691 -0.0740 26  GLU A CD  
244  O  OE1 . GLU A 26  ? 0.3610 0.4781 0.4311 -0.0098 -0.1243 -0.0307 26  GLU A OE1 
245  O  OE2 . GLU A 26  ? 0.3151 0.5493 0.6161 0.0649  -0.2294 0.0706  26  GLU A OE2 
246  N  N   . ARG A 27  ? 0.1146 0.1568 0.1243 0.0031  -0.0293 -0.0240 27  ARG A N   
247  C  CA  . ARG A 27  ? 0.1014 0.1356 0.1235 0.0082  -0.0209 -0.0148 27  ARG A CA  
248  C  C   . ARG A 27  ? 0.0922 0.1296 0.1242 -0.0041 -0.0199 -0.0076 27  ARG A C   
249  O  O   . ARG A 27  ? 0.0992 0.1422 0.1176 0.0126  -0.0219 -0.0194 27  ARG A O   
250  C  CB  . ARG A 27  ? 0.1949 0.1580 0.1360 0.0131  -0.0408 -0.0478 27  ARG A CB  
251  C  CG  . ARG A 27  ? 0.2037 0.1993 0.1808 -0.0129 -0.0308 -0.0210 27  ARG A CG  
252  C  CD  . ARG A 27  ? 0.2673 0.2169 0.1577 0.0408  -0.0428 -0.0186 27  ARG A CD  
253  N  NE  . ARG A 27  ? 0.2028 0.1727 0.1439 0.0065  0.0013  -0.0152 27  ARG A NE  
254  C  CZ  . ARG A 27  ? 0.1845 0.1782 0.1224 0.0231  -0.0104 0.0263  27  ARG A CZ  
255  N  NH1 . ARG A 27  ? 0.1780 0.2410 0.2021 0.0425  -0.0194 -0.1221 27  ARG A NH1 
256  N  NH2 . ARG A 27  ? 0.1668 0.1905 0.1694 -0.0003 -0.0013 -0.0120 27  ARG A NH2 
257  N  N   . GLN A 28  ? 0.0908 0.1226 0.1190 0.0012  -0.0154 -0.0164 28  GLN A N   
258  C  CA  . GLN A 28  ? 0.0803 0.1128 0.1150 -0.0102 -0.0076 -0.0124 28  GLN A CA  
259  C  C   . GLN A 28  ? 0.0766 0.1088 0.1077 0.0082  -0.0027 0.0000  28  GLN A C   
260  O  O   . GLN A 28  ? 0.1077 0.1263 0.1018 -0.0120 -0.0153 -0.0115 28  GLN A O   
261  C  CB  . GLN A 28  ? 0.0688 0.1403 0.1391 -0.0043 -0.0154 -0.0131 28  GLN A CB  
262  C  CG  . GLN A 28  ? 0.0873 0.1455 0.1404 0.0024  -0.0097 -0.0175 28  GLN A CG  
263  C  CD  . GLN A 28  ? 0.0706 0.1272 0.1368 -0.0093 -0.0115 -0.0230 28  GLN A CD  
264  O  OE1 . GLN A 28  ? 0.0868 0.1216 0.1430 -0.0082 -0.0003 -0.0176 28  GLN A OE1 
265  N  NE2 . GLN A 28  ? 0.0825 0.1269 0.1536 -0.0126 -0.0109 -0.0208 28  GLN A NE2 
266  N  N   . SER A 29  ? 0.0829 0.1079 0.1058 0.0000  -0.0137 -0.0148 29  SER A N   
267  C  CA  . SER A 29  ? 0.0763 0.0995 0.1128 0.0017  -0.0087 -0.0147 29  SER A CA  
268  C  C   . SER A 29  ? 0.0706 0.0907 0.1084 0.0031  -0.0057 0.0043  29  SER A C   
269  O  O   . SER A 29  ? 0.0798 0.1110 0.1208 -0.0015 0.0060  -0.0109 29  SER A O   
270  C  CB  . SER A 29  ? 0.0724 0.1070 0.1067 0.0115  -0.0074 -0.0219 29  SER A CB  
271  O  OG  . SER A 29  ? 0.0846 0.0948 0.1140 0.0006  0.0003  -0.0087 29  SER A OG  
272  N  N   . PRO A 30  ? 0.0710 0.0948 0.1070 0.0006  -0.0057 -0.0073 30  PRO A N   
273  C  CA  . PRO A 30  ? 0.0798 0.0907 0.1124 -0.0049 -0.0015 0.0049  30  PRO A CA  
274  C  C   . PRO A 30  ? 0.0762 0.0944 0.1102 0.0043  -0.0087 -0.0092 30  PRO A C   
275  O  O   . PRO A 30  ? 0.0863 0.1145 0.1115 0.0051  -0.0082 -0.0024 30  PRO A O   
276  C  CB  . PRO A 30  ? 0.0780 0.1054 0.1102 0.0006  -0.0006 -0.0148 30  PRO A CB  
277  C  CG  . PRO A 30  ? 0.0900 0.1093 0.1210 -0.0034 0.0000  0.0000  30  PRO A CG  
278  C  CD  . PRO A 30  ? 0.0944 0.0966 0.1086 0.0000  0.0068  -0.0120 30  PRO A CD  
279  N  N   . VAL A 31  ? 0.1018 0.1001 0.0934 0.0017  0.0000  0.0081  31  VAL A N   
280  C  CA  . VAL A 31  ? 0.1027 0.1059 0.1054 0.0006  -0.0051 0.0120  31  VAL A CA  
281  C  C   . VAL A 31  ? 0.1000 0.1061 0.1054 0.0068  0.0043  0.0114  31  VAL A C   
282  O  O   . VAL A 31  ? 0.0996 0.1158 0.1206 0.0031  -0.0060 0.0186  31  VAL A O   
283  C  CB  . VAL A 31  ? 0.1208 0.1133 0.1136 0.0015  -0.0031 -0.0142 31  VAL A CB  
284  C  CG1 . VAL A 31  ? 0.1405 0.1145 0.1272 0.0037  -0.0006 -0.0131 31  VAL A CG1 
285  C  CG2 . VAL A 31  ? 0.1097 0.1208 0.1351 0.0010  0.0176  0.0013  31  VAL A CG2 
286  N  N   . ASP A 32  ? 0.1167 0.0995 0.1045 0.0006  -0.0070 0.0142  32  ASP A N   
287  C  CA  . ASP A 32  ? 0.1138 0.1118 0.1172 0.0054  0.0034  0.0115  32  ASP A CA  
288  C  C   . ASP A 32  ? 0.1203 0.1246 0.0957 0.0126  -0.0065 0.0060  32  ASP A C   
289  O  O   . ASP A 32  ? 0.1246 0.1643 0.1203 -0.0006 -0.0091 -0.0109 32  ASP A O   
290  C  CB  . ASP A 32  ? 0.1589 0.0988 0.1263 0.0137  0.0076  0.0203  32  ASP A CB  
291  C  CG  . ASP A 32  ? 0.1629 0.1447 0.1228 0.0206  -0.0098 0.0194  32  ASP A CG  
292  O  OD1 . ASP A 32  ? 0.1508 0.1174 0.1409 0.0063  -0.0176 0.0187  32  ASP A OD1 
293  O  OD2 . ASP A 32  ? 0.2295 0.1629 0.1306 -0.0392 -0.0206 0.0443  32  ASP A OD2 
294  N  N   . ILE A 33  ? 0.1045 0.1224 0.1106 0.0041  0.0065  0.0131  33  ILE A N   
295  C  CA  . ILE A 33  ? 0.1237 0.1190 0.1106 0.0185  0.0087  0.0076  33  ILE A CA  
296  C  C   . ILE A 33  ? 0.1396 0.1104 0.1149 0.0129  0.0109  0.0010  33  ILE A C   
297  O  O   . ILE A 33  ? 0.1569 0.1295 0.1237 0.0046  0.0162  0.0153  33  ILE A O   
298  C  CB  . ILE A 33  ? 0.1312 0.1145 0.1279 0.0274  0.0081  0.0164  33  ILE A CB  
299  C  CG1 . ILE A 33  ? 0.1435 0.1250 0.1391 0.0166  -0.0115 0.0231  33  ILE A CG1 
300  C  CG2 . ILE A 33  ? 0.1396 0.1613 0.1658 0.0220  0.0252  0.0043  33  ILE A CG2 
301  C  CD1 . ILE A 33  ? 0.1315 0.1701 0.1523 0.0175  -0.0177 0.0324  33  ILE A CD1 
302  N  N   A ASP A 34  ? 0.1712 0.1665 0.1190 0.0221  0.0049  0.0166  34  ASP A N   
303  N  N   B ASP A 34  ? 0.1649 0.1421 0.1005 0.0308  0.0177  0.0248  34  ASP A N   
304  C  CA  A ASP A 34  ? 0.1747 0.1603 0.1122 0.0573  0.0166  0.0241  34  ASP A CA  
305  C  CA  B ASP A 34  ? 0.1958 0.1534 0.1183 0.0142  0.0307  0.0355  34  ASP A CA  
306  C  C   A ASP A 34  ? 0.2078 0.1518 0.1129 0.0724  0.0304  0.0631  34  ASP A C   
307  C  C   B ASP A 34  ? 0.2043 0.1563 0.1190 0.0297  0.0579  0.0339  34  ASP A C   
308  O  O   A ASP A 34  ? 0.1518 0.2169 0.1412 0.0337  0.0361  0.0104  34  ASP A O   
309  O  O   B ASP A 34  ? 0.1764 0.1624 0.1246 0.0241  0.0295  0.0120  34  ASP A O   
310  C  CB  A ASP A 34  ? 0.2536 0.1877 0.1149 0.0794  0.0013  0.0476  34  ASP A CB  
311  C  CB  B ASP A 34  ? 0.2428 0.1779 0.1395 0.0392  0.0076  0.0469  34  ASP A CB  
312  C  CG  A ASP A 34  ? 0.2935 0.1888 0.1826 0.0450  0.0093  0.0381  34  ASP A CG  
313  C  CG  B ASP A 34  ? 0.2240 0.1879 0.1551 0.0566  0.0104  0.0427  34  ASP A CG  
314  O  OD1 A ASP A 34  ? 0.3675 0.2892 0.2867 0.0639  0.0944  -0.0825 34  ASP A OD1 
315  O  OD1 B ASP A 34  ? 0.2489 0.2187 0.1527 0.0320  0.0242  0.1053  34  ASP A OD1 
316  O  OD2 A ASP A 34  ? 0.4009 0.2392 0.1678 0.1180  0.0579  0.0505  34  ASP A OD2 
317  O  OD2 B ASP A 34  ? 0.2691 0.2453 0.1921 0.0307  -0.0383 0.1190  34  ASP A OD2 
318  N  N   . THR A 35  ? 0.1942 0.1745 0.1437 0.0335  0.0419  0.0553  35  THR A N   
319  C  CA  . THR A 35  ? 0.2113 0.2083 0.1439 0.0542  0.0296  0.0671  35  THR A CA  
320  C  C   . THR A 35  ? 0.2177 0.1621 0.1474 0.0573  0.0496  0.0445  35  THR A C   
321  O  O   . THR A 35  ? 0.2874 0.2108 0.1720 0.0988  0.0522  0.0560  35  THR A O   
322  C  CB  . THR A 35  ? 0.1937 0.2162 0.2001 0.0500  0.0494  0.0719  35  THR A CB  
323  O  OG1 . THR A 35  ? 0.2270 0.2222 0.2010 0.0193  0.0575  0.0489  35  THR A OG1 
324  C  CG2 . THR A 35  ? 0.2496 0.2494 0.1737 0.0666  0.0372  0.0688  35  THR A CG2 
325  N  N   A HIS A 36  ? 0.1743 0.1133 0.1172 -0.0115 -0.0027 0.0318  36  HIS A N   
326  N  N   B HIS A 36  ? 0.2245 0.1251 0.1562 0.0166  0.0560  0.0359  36  HIS A N   
327  C  CA  A HIS A 36  ? 0.1818 0.1649 0.1018 -0.0296 -0.0098 0.0718  36  HIS A CA  
328  C  CA  B HIS A 36  ? 0.2709 0.1307 0.1615 0.0239  0.0970  0.0226  36  HIS A CA  
329  C  C   A HIS A 36  ? 0.1657 0.1440 0.1203 0.0177  0.0015  0.0384  36  HIS A C   
330  C  C   B HIS A 36  ? 0.2529 0.2328 0.1162 -0.0251 0.0601  0.0171  36  HIS A C   
331  O  O   A HIS A 36  ? 0.1928 0.2349 0.1129 0.0160  -0.0197 0.0102  36  HIS A O   
332  O  O   B HIS A 36  ? 0.3718 0.3986 0.1659 0.0063  0.0882  -0.0621 36  HIS A O   
333  C  CB  A HIS A 36  ? 0.2056 0.1904 0.1430 0.0020  -0.0081 0.0482  36  HIS A CB  
334  C  CB  B HIS A 36  ? 0.2802 0.1844 0.1448 0.0340  0.0379  0.0535  36  HIS A CB  
335  C  CG  A HIS A 36  ? 0.2090 0.1709 0.1212 0.0109  -0.0326 0.0593  36  HIS A CG  
336  C  CG  B HIS A 36  ? 0.3305 0.2140 0.1694 0.0507  -0.0452 0.1106  36  HIS A CG  
337  N  ND1 A HIS A 36  ? 0.2536 0.2205 0.1499 -0.0175 -0.0344 0.0421  36  HIS A ND1 
338  N  ND1 B HIS A 36  ? 0.3097 0.2967 0.2885 0.0410  0.0219  -0.0063 36  HIS A ND1 
339  C  CD2 A HIS A 36  ? 0.2500 0.1731 0.1199 0.0274  -0.0359 0.0456  36  HIS A CD2 
340  C  CD2 B HIS A 36  ? 0.4027 0.2565 0.1581 0.0401  0.0035  0.1142  36  HIS A CD2 
341  C  CE1 A HIS A 36  ? 0.3352 0.2152 0.1711 -0.0065 -0.0731 0.0015  36  HIS A CE1 
342  C  CE1 B HIS A 36  ? 0.3883 0.3603 0.2795 -0.0428 -0.0553 -0.0204 36  HIS A CE1 
343  N  NE2 A HIS A 36  ? 0.2558 0.1887 0.2240 0.0093  -0.0516 0.0399  36  HIS A NE2 
344  N  NE2 B HIS A 36  ? 0.4088 0.1915 0.3050 0.0697  -0.0520 0.0934  36  HIS A NE2 
345  N  N   A THR A 37  ? 0.2046 0.1615 0.1212 -0.0034 0.0270  0.0221  37  THR A N   
346  N  N   B THR A 37  ? 0.1852 0.1651 0.1703 0.0362  0.0037  0.0059  37  THR A N   
347  C  CA  A THR A 37  ? 0.2231 0.1694 0.1567 -0.0153 0.0136  0.0274  37  THR A CA  
348  C  CA  B THR A 37  ? 0.2229 0.1483 0.1532 0.0432  0.0529  0.0405  37  THR A CA  
349  C  C   A THR A 37  ? 0.1851 0.2026 0.1448 0.0395  0.0370  0.0092  37  THR A C   
350  C  C   B THR A 37  ? 0.2291 0.1913 0.1502 0.0727  0.0722  0.0522  37  THR A C   
351  O  O   A THR A 37  ? 0.2176 0.1787 0.1138 0.0093  0.0164  0.0263  37  THR A O   
352  O  O   B THR A 37  ? 0.2809 0.2228 0.2081 -0.0051 0.0439  0.0516  37  THR A O   
353  C  CB  A THR A 37  ? 0.2153 0.2177 0.1967 -0.0232 -0.0019 0.0120  37  THR A CB  
354  C  CB  B THR A 37  ? 0.2770 0.1650 0.2258 0.0715  0.1278  0.0900  37  THR A CB  
355  O  OG1 A THR A 37  ? 0.3693 0.2453 0.1509 0.0697  0.0359  0.0454  37  THR A OG1 
356  O  OG1 B THR A 37  ? 0.3136 0.1942 0.3736 0.0951  0.0463  0.1203  37  THR A OG1 
357  C  CG2 A THR A 37  ? 0.3007 0.2162 0.2788 0.0333  0.0082  0.0326  37  THR A CG2 
358  C  CG2 B THR A 37  ? 0.3528 0.2605 0.1077 0.0744  0.0037  0.0626  37  THR A CG2 
359  N  N   . ALA A 38  ? 0.2838 0.1739 0.1315 0.0535  0.0326  0.0379  38  ALA A N   
360  C  CA  . ALA A 38  ? 0.2468 0.1861 0.1260 0.0526  0.0485  0.0388  38  ALA A CA  
361  C  C   . ALA A 38  ? 0.2451 0.1805 0.2422 0.0351  0.0759  0.0522  38  ALA A C   
362  O  O   . ALA A 38  ? 0.4404 0.2300 0.3761 0.0359  0.2407  0.0175  38  ALA A O   
363  C  CB  . ALA A 38  ? 0.2372 0.1826 0.1655 0.0273  0.0126  0.0137  38  ALA A CB  
364  N  N   . LYS A 39  ? 0.2784 0.2316 0.1586 0.1075  0.0059  -0.0092 39  LYS A N   
365  C  CA  . LYS A 39  ? 0.2777 0.3503 0.1428 0.1499  -0.0065 -0.0230 39  LYS A CA  
366  C  C   . LYS A 39  ? 0.2143 0.2331 0.1219 0.0834  0.0031  -0.0125 39  LYS A C   
367  O  O   . LYS A 39  ? 0.1694 0.2623 0.1163 0.0379  0.0043  0.0137  39  LYS A O   
368  C  CB  . LYS A 39  ? 0.2460 0.4706 0.2096 0.1659  -0.0819 -0.1067 39  LYS A CB  
369  C  CG  . LYS A 39  ? 0.3941 0.4648 0.1410 0.1448  -0.0183 -0.0421 39  LYS A CG  
370  C  CD  . LYS A 39  ? 0.2824 0.5435 0.1738 0.1571  -0.0421 -0.0162 39  LYS A CD  
371  C  CE  . LYS A 39  ? 0.6376 0.5533 0.3147 0.0581  0.1177  -0.0439 39  LYS A CE  
372  N  NZ  . LYS A 39  ? 0.3652 0.7411 0.2842 0.1727  0.1316  0.2045  39  LYS A NZ  
373  N  N   . TYR A 40  ? 0.2752 0.2601 0.1492 0.0467  0.0461  0.0230  40  TYR A N   
374  C  CA  . TYR A 40  ? 0.2483 0.2433 0.1462 0.0331  0.0732  0.0171  40  TYR A CA  
375  C  C   . TYR A 40  ? 0.1781 0.2363 0.1445 0.0182  0.0315  0.0218  40  TYR A C   
376  O  O   . TYR A 40  ? 0.2258 0.2946 0.1150 0.0286  0.0320  -0.0070 40  TYR A O   
377  C  CB  . TYR A 40  ? 0.2705 0.2924 0.1588 -0.0590 0.0377  0.0175  40  TYR A CB  
378  C  CG  . TYR A 40  ? 0.2870 0.3244 0.1880 -0.0562 0.0996  0.0124  40  TYR A CG  
379  C  CD1 . TYR A 40  ? 0.2281 0.3161 0.1587 -0.0702 0.0529  -0.0087 40  TYR A CD1 
380  C  CD2 . TYR A 40  ? 0.3230 0.4781 0.1973 -0.0443 0.1225  -0.0241 40  TYR A CD2 
381  C  CE1 . TYR A 40  ? 0.2116 0.5166 0.2010 -0.0135 0.0364  -0.0604 40  TYR A CE1 
382  C  CE2 . TYR A 40  ? 0.2921 0.4850 0.2249 0.0043  0.1186  0.0114  40  TYR A CE2 
383  C  CZ  . TYR A 40  ? 0.2061 0.5019 0.2065 -0.0013 0.0381  0.0108  40  TYR A CZ  
384  O  OH  . TYR A 40  ? 0.1895 0.6843 0.3603 -0.0082 0.0485  -0.0877 40  TYR A OH  
385  N  N   . ASP A 41  ? 0.1604 0.2061 0.1509 0.0271  0.0388  -0.0027 41  ASP A N   
386  C  CA  . ASP A 41  ? 0.1686 0.2046 0.1552 -0.0013 0.0107  -0.0071 41  ASP A CA  
387  C  C   . ASP A 41  ? 0.1844 0.2644 0.1544 0.0005  0.0076  -0.0274 41  ASP A C   
388  O  O   . ASP A 41  ? 0.1747 0.2431 0.1722 0.0125  -0.0017 -0.0071 41  ASP A O   
389  C  CB  . ASP A 41  ? 0.2282 0.2215 0.2265 -0.0242 0.0006  -0.0043 41  ASP A CB  
390  C  CG  . ASP A 41  ? 0.2029 0.2752 0.2637 -0.0194 -0.0104 -0.0500 41  ASP A CG  
391  O  OD1 . ASP A 41  ? 0.2352 0.2705 0.2802 0.0164  -0.0259 -0.0969 41  ASP A OD1 
392  O  OD2 . ASP A 41  ? 0.2483 0.3379 0.2720 -0.0597 -0.0623 0.0098  41  ASP A OD2 
393  N  N   . PRO A 42  ? 0.2028 0.3025 0.1835 0.0615  0.0436  -0.0284 42  PRO A N   
394  C  CA  . PRO A 42  ? 0.2003 0.3657 0.2572 0.0538  0.0476  0.0251  42  PRO A CA  
395  C  C   . PRO A 42  ? 0.1914 0.3402 0.2141 0.0702  0.0542  -0.0098 42  PRO A C   
396  O  O   . PRO A 42  ? 0.2838 0.5443 0.3600 0.1824  0.0700  -0.0214 42  PRO A O   
397  C  CB  . PRO A 42  ? 0.2302 0.5600 0.2623 0.0688  0.0948  0.0031  42  PRO A CB  
398  C  CG  . PRO A 42  ? 0.3039 0.6758 0.2180 0.1230  0.0781  -0.0324 42  PRO A CG  
399  C  CD  . PRO A 42  ? 0.2788 0.3908 0.1490 0.0741  0.0480  -0.0109 42  PRO A CD  
400  N  N   . SER A 43  ? 0.2052 0.3258 0.2489 0.0551  0.0326  -0.0296 43  SER A N   
401  C  CA  . SER A 43  ? 0.2734 0.2996 0.2669 0.0604  -0.0003 -0.0617 43  SER A CA  
402  C  C   . SER A 43  ? 0.2338 0.3111 0.2428 0.1032  -0.0221 -0.0048 43  SER A C   
403  O  O   . SER A 43  ? 0.4199 0.2809 0.3032 0.1199  -0.0085 0.0052  43  SER A O   
404  C  CB  . SER A 43  ? 0.2791 0.3449 0.2676 0.0000  0.0538  -0.0597 43  SER A CB  
405  O  OG  . SER A 43  ? 0.3115 0.3104 0.2870 -0.0019 -0.0436 -0.0631 43  SER A OG  
406  N  N   . LEU A 44  ? 0.2356 0.3265 0.2169 0.0454  -0.0071 -0.0384 44  LEU A N   
407  C  CA  . LEU A 44  ? 0.1976 0.3230 0.2002 0.0197  -0.0252 0.0003  44  LEU A CA  
408  C  C   . LEU A 44  ? 0.1544 0.3219 0.2967 0.0307  -0.0059 0.0214  44  LEU A C   
409  O  O   . LEU A 44  ? 0.1981 0.4514 0.3377 -0.0430 -0.0540 0.1106  44  LEU A O   
410  C  CB  . LEU A 44  ? 0.1902 0.2698 0.1888 -0.0275 0.0175  -0.0171 44  LEU A CB  
411  C  CG  . LEU A 44  ? 0.1941 0.2748 0.1542 -0.0171 -0.0065 0.0308  44  LEU A CG  
412  C  CD1 . LEU A 44  ? 0.2569 0.2662 0.1861 -0.0198 0.0381  -0.0383 44  LEU A CD1 
413  C  CD2 . LEU A 44  ? 0.2091 0.2363 0.2029 -0.0306 0.0024  0.0174  44  LEU A CD2 
414  N  N   . LYS A 45  ? 0.2142 0.3111 0.2392 0.0344  -0.0322 0.0013  45  LYS A N   
415  C  CA  . LYS A 45  ? 0.1780 0.2930 0.3664 0.0237  -0.0522 -0.0452 45  LYS A CA  
416  C  C   . LYS A 45  ? 0.1791 0.2881 0.2363 0.0702  0.0274  -0.0220 45  LYS A C   
417  O  O   . LYS A 45  ? 0.1677 0.2511 0.2784 0.0238  0.0120  -0.0137 45  LYS A O   
418  C  CB  . LYS A 45  ? 0.2489 0.2626 0.2623 0.0908  0.0030  0.0076  45  LYS A CB  
419  C  CG  . LYS A 45  ? 0.2899 0.4814 0.2544 0.0219  0.0428  -0.0615 45  LYS A CG  
420  C  CD  . LYS A 45  ? 0.2526 0.3970 0.2637 -0.0285 0.0320  -0.0060 45  LYS A CD  
421  C  CE  . LYS A 45  ? 0.1383 0.1796 0.3021 0.0860  -0.0361 0.0644  45  LYS A CE  
422  N  NZ  . LYS A 45  ? 0.1158 0.1931 0.3366 0.0939  -0.0476 0.0557  45  LYS A NZ  
423  N  N   . PRO A 46  ? 0.1421 0.3050 0.2526 -0.0205 0.0232  -0.0130 46  PRO A N   
424  C  CA  . PRO A 46  ? 0.1665 0.3184 0.2214 0.0152  0.0208  0.0219  46  PRO A CA  
425  C  C   . PRO A 46  ? 0.1342 0.2106 0.2018 -0.0057 0.0172  0.0006  46  PRO A C   
426  O  O   . PRO A 46  ? 0.1215 0.2302 0.2633 -0.0181 -0.0188 0.0153  46  PRO A O   
427  C  CB  . PRO A 46  ? 0.1454 0.3185 0.2773 -0.0397 0.0225  0.0215  46  PRO A CB  
428  C  CG  . PRO A 46  ? 0.1263 0.6599 0.3452 0.0102  0.0115  -0.1120 46  PRO A CG  
429  C  CD  . PRO A 46  ? 0.1507 0.3876 0.2709 0.0557  0.0164  -0.0225 46  PRO A CD  
430  N  N   . LEU A 47  ? 0.1219 0.2842 0.2669 0.0035  0.0020  0.0098  47  LEU A N   
431  C  CA  . LEU A 47  ? 0.1049 0.2522 0.2547 -0.0329 0.0320  -0.0082 47  LEU A CA  
432  C  C   . LEU A 47  ? 0.0728 0.2504 0.3140 -0.0186 -0.0219 0.0688  47  LEU A C   
433  O  O   . LEU A 47  ? 0.1287 0.2964 0.3847 -0.0544 -0.0846 0.1280  47  LEU A O   
434  C  CB  . LEU A 47  ? 0.1823 0.2781 0.2799 0.0390  0.0087  -0.0054 47  LEU A CB  
435  C  CG  . LEU A 47  ? 0.1554 0.2601 0.3424 -0.0151 -0.0362 0.0185  47  LEU A CG  
436  C  CD1 . LEU A 47  ? 0.1077 0.3330 0.5252 -0.0702 -0.0164 -0.0104 47  LEU A CD1 
437  C  CD2 . LEU A 47  ? 0.1685 0.2399 0.3786 0.0000  -0.0063 -0.0230 47  LEU A CD2 
438  N  N   . SER A 48  ? 0.1111 0.2293 0.2020 -0.0348 -0.0015 0.0485  48  SER A N   
439  C  CA  . SER A 48  ? 0.1391 0.2201 0.1834 0.0000  -0.0120 0.0322  48  SER A CA  
440  C  C   . SER A 48  ? 0.1194 0.1867 0.2135 -0.0275 -0.0049 0.0153  48  SER A C   
441  O  O   . SER A 48  ? 0.1244 0.2169 0.2073 -0.0353 0.0063  -0.0124 48  SER A O   
442  C  CB  . SER A 48  ? 0.1553 0.2349 0.2246 -0.0091 -0.0006 0.0357  48  SER A CB  
443  O  OG  . SER A 48  ? 0.1842 0.2716 0.2921 0.0241  0.0386  0.0864  48  SER A OG  
444  N  N   . VAL A 49  ? 0.1581 0.1973 0.2092 -0.0303 0.0023  0.0104  49  VAL A N   
445  C  CA  . VAL A 49  ? 0.1773 0.2197 0.2307 -0.0665 -0.0087 -0.0038 49  VAL A CA  
446  C  C   . VAL A 49  ? 0.1605 0.2284 0.2257 -0.0674 -0.0197 -0.0015 49  VAL A C   
447  O  O   . VAL A 49  ? 0.2099 0.4002 0.2451 -0.1430 -0.0601 0.0305  49  VAL A O   
448  C  CB  . VAL A 49  ? 0.2748 0.2476 0.1930 -0.0825 0.0284  -0.0087 49  VAL A CB  
449  C  CG1 . VAL A 49  ? 0.3682 0.3039 0.2795 -0.0467 0.0878  -0.0373 49  VAL A CG1 
450  C  CG2 . VAL A 49  ? 0.2753 0.2648 0.3061 -0.0942 0.0359  0.0131  49  VAL A CG2 
451  N  N   . SER A 50  ? 0.1448 0.2597 0.2185 -0.0653 0.0060  -0.0057 50  SER A N   
452  C  CA  . SER A 50  ? 0.1435 0.2867 0.3057 -0.0175 -0.0160 0.0046  50  SER A CA  
453  C  C   . SER A 50  ? 0.1230 0.2558 0.2529 -0.0104 -0.0408 0.0085  50  SER A C   
454  O  O   . SER A 50  ? 0.1788 0.2476 0.2572 -0.0460 -0.0450 0.0326  50  SER A O   
455  C  CB  . SER A 50  ? 0.2035 0.2896 0.3176 -0.0074 -0.0015 0.0434  50  SER A CB  
456  O  OG  . SER A 50  ? 0.2169 0.4095 0.3797 -0.0198 0.0087  -0.0186 50  SER A OG  
457  N  N   . TYR A 51  ? 0.1615 0.2494 0.2214 -0.0408 -0.0395 0.0076  51  TYR A N   
458  C  CA  . TYR A 51  ? 0.1482 0.2392 0.2256 -0.0186 -0.0566 0.0204  51  TYR A CA  
459  C  C   . TYR A 51  ? 0.1544 0.2378 0.2356 -0.0322 -0.0307 0.0454  51  TYR A C   
460  O  O   . TYR A 51  ? 0.1986 0.2802 0.2195 -0.0197 -0.0428 0.0425  51  TYR A O   
461  C  CB  . TYR A 51  ? 0.1580 0.2368 0.2142 -0.0252 -0.0491 0.0054  51  TYR A CB  
462  C  CG  . TYR A 51  ? 0.1694 0.1922 0.1562 -0.0287 -0.0395 0.0181  51  TYR A CG  
463  C  CD1 . TYR A 51  ? 0.1551 0.1596 0.2205 -0.0164 -0.0461 0.0197  51  TYR A CD1 
464  C  CD2 . TYR A 51  ? 0.1606 0.1886 0.1613 -0.0355 -0.0087 0.0082  51  TYR A CD2 
465  C  CE1 . TYR A 51  ? 0.1448 0.1808 0.1629 -0.0263 -0.0364 0.0231  51  TYR A CE1 
466  C  CE2 . TYR A 51  ? 0.1621 0.1606 0.1604 -0.0306 -0.0249 -0.0003 51  TYR A CE2 
467  C  CZ  . TYR A 51  ? 0.1458 0.1748 0.1552 -0.0381 -0.0194 0.0109  51  TYR A CZ  
468  O  OH  . TYR A 51  ? 0.1332 0.1621 0.1835 -0.0251 -0.0308 -0.0026 51  TYR A OH  
469  N  N   . ASP A 52  ? 0.1199 0.3230 0.3226 -0.0441 -0.0715 0.0908  52  ASP A N   
470  C  CA  . ASP A 52  ? 0.1510 0.3258 0.3251 -0.0403 -0.0776 0.1237  52  ASP A CA  
471  C  C   . ASP A 52  ? 0.2196 0.2978 0.3082 -0.0093 -0.1088 0.0744  52  ASP A C   
472  O  O   . ASP A 52  ? 0.3140 0.3330 0.3054 -0.0251 -0.1036 0.0785  52  ASP A O   
473  C  CB  . ASP A 52  ? 0.1474 0.4569 0.3776 -0.0040 -0.0929 0.1410  52  ASP A CB  
474  C  CG  . ASP A 52  ? 0.2957 0.6244 0.5798 -0.0087 -0.1058 -0.0335 52  ASP A CG  
475  O  OD1 . ASP A 52  ? 0.3513 0.7616 0.6445 -0.0147 -0.1500 -0.0588 52  ASP A OD1 
476  O  OD2 . ASP A 52  ? 0.8180 0.5794 1.1448 0.0450  -0.0285 0.4189  52  ASP A OD2 
477  N  N   . GLN A 53  ? 0.1941 0.2410 0.3488 -0.0020 -0.0546 0.0562  53  GLN A N   
478  C  CA  . GLN A 53  ? 0.2008 0.2522 0.3941 -0.0076 -0.0634 0.0737  53  GLN A CA  
479  C  C   . GLN A 53  ? 0.1993 0.2413 0.2167 -0.0153 -0.0381 0.0355  53  GLN A C   
480  O  O   . GLN A 53  ? 0.2192 0.2392 0.2712 0.0012  -0.0274 0.0390  53  GLN A O   
481  C  CB  . GLN A 53  ? 0.3100 0.2734 0.4702 0.0653  -0.0230 0.0724  53  GLN A CB  
482  C  CG  . GLN A 53  ? 0.2942 0.5396 0.4490 -0.0059 -0.0701 0.0274  53  GLN A CG  
483  C  CD  . GLN A 53  ? 0.2325 0.7261 0.6503 0.0135  -0.1316 -0.1272 53  GLN A CD  
484  O  OE1 . GLN A 53  ? 0.5194 0.8148 1.0319 0.2804  0.2750  0.1045  53  GLN A OE1 
485  N  NE2 . GLN A 53  ? 0.3833 0.3948 0.9114 0.0364  -0.2003 0.1141  53  GLN A NE2 
486  N  N   . ALA A 54  ? 0.2087 0.1974 0.2475 -0.0261 -0.0388 0.0104  54  ALA A N   
487  C  CA  . ALA A 54  ? 0.1870 0.1887 0.2071 -0.0152 -0.0194 -0.0093 54  ALA A CA  
488  C  C   . ALA A 54  ? 0.2451 0.1888 0.2149 -0.0142 -0.0390 -0.0219 54  ALA A C   
489  O  O   . ALA A 54  ? 0.3161 0.3194 0.2363 -0.0816 -0.0524 -0.0652 54  ALA A O   
490  C  CB  . ALA A 54  ? 0.2161 0.1710 0.3309 -0.0087 -0.0355 -0.0113 54  ALA A CB  
491  N  N   A THR A 55  ? 0.1580 0.2257 0.1659 -0.0015 -0.0333 0.0120  55  THR A N   
492  N  N   B THR A 55  ? 0.2161 0.1352 0.2087 0.0531  -0.0292 0.0174  55  THR A N   
493  C  CA  A THR A 55  ? 0.1930 0.1993 0.1729 0.0684  -0.0302 0.0241  55  THR A CA  
494  C  CA  B THR A 55  ? 0.2759 0.1993 0.2039 0.0465  -0.0491 0.0309  55  THR A CA  
495  C  C   A THR A 55  ? 0.1647 0.1699 0.1226 0.0049  -0.0306 0.0098  55  THR A C   
496  C  C   B THR A 55  ? 0.2630 0.1412 0.1467 -0.0219 -0.0776 0.0388  55  THR A C   
497  O  O   A THR A 55  ? 0.1183 0.1483 0.1453 0.0040  -0.0071 0.0052  55  THR A O   
498  O  O   B THR A 55  ? 0.2011 0.1888 0.1221 0.0320  0.0031  0.0361  55  THR A O   
499  C  CB  A THR A 55  ? 0.2870 0.2011 0.2162 -0.0272 -0.0386 -0.0140 55  THR A CB  
500  C  CB  B THR A 55  ? 0.2108 0.1941 0.2064 0.0662  -0.0670 -0.0076 55  THR A CB  
501  O  OG1 A THR A 55  ? 0.2991 0.1948 0.3072 0.0780  -0.1155 -0.0087 55  THR A OG1 
502  O  OG1 B THR A 55  ? 0.2842 0.2331 0.2117 0.0434  -0.0627 -0.0098 55  THR A OG1 
503  C  CG2 A THR A 55  ? 0.3406 0.1897 0.1991 -0.0081 -0.0864 0.0658  55  THR A CG2 
504  C  CG2 B THR A 55  ? 0.3057 0.2161 0.2257 -0.0140 0.0181  -0.0103 55  THR A CG2 
505  N  N   . SER A 56  ? 0.2615 0.1604 0.1516 0.0331  -0.0732 0.0091  56  SER A N   
506  C  CA  . SER A 56  ? 0.2845 0.1536 0.1253 0.0472  -0.0408 0.0071  56  SER A CA  
507  C  C   . SER A 56  ? 0.2608 0.1826 0.1492 0.0445  -0.0526 0.0348  56  SER A C   
508  O  O   . SER A 56  ? 0.3765 0.1826 0.1511 0.0790  -0.0974 0.0126  56  SER A O   
509  C  CB  . SER A 56  ? 0.3215 0.1501 0.1400 0.0086  -0.0881 0.0125  56  SER A CB  
510  O  OG  . SER A 56  ? 0.2935 0.1744 0.1703 0.0131  -0.0872 0.0209  56  SER A OG  
511  N  N   . LEU A 57  ? 0.2522 0.1587 0.1282 0.0326  -0.0153 0.0219  57  LEU A N   
512  C  CA  . LEU A 57  ? 0.2784 0.1659 0.1624 0.0104  -0.0027 0.0331  57  LEU A CA  
513  C  C   . LEU A 57  ? 0.2203 0.1606 0.1339 0.0082  -0.0108 0.0326  57  LEU A C   
514  O  O   . LEU A 57  ? 0.2867 0.2020 0.1287 0.0322  -0.0286 0.0450  57  LEU A O   
515  C  CB  . LEU A 57  ? 0.3072 0.2143 0.1685 -0.0295 -0.0062 0.0920  57  LEU A CB  
516  C  CG  . LEU A 57  ? 0.3309 0.1956 0.2691 0.0020  -0.0471 0.0377  57  LEU A CG  
517  C  CD1 . LEU A 57  ? 0.3115 0.3521 0.3122 -0.1111 -0.0425 0.1220  57  LEU A CD1 
518  C  CD2 . LEU A 57  ? 0.6230 0.1967 0.2302 0.1277  -0.1194 0.0450  57  LEU A CD2 
519  N  N   . ARG A 58  ? 0.2099 0.1729 0.1562 0.0353  -0.0131 0.0357  58  ARG A N   
520  C  CA  . ARG A 58  ? 0.2151 0.1825 0.1475 0.0120  -0.0273 0.0537  58  ARG A CA  
521  C  C   . ARG A 58  ? 0.1863 0.1738 0.1199 -0.0098 -0.0098 0.0186  58  ARG A C   
522  O  O   . ARG A 58  ? 0.2536 0.1692 0.1008 0.0368  0.0019  0.0163  58  ARG A O   
523  C  CB  . ARG A 58  ? 0.2282 0.2500 0.1572 0.0140  0.0085  0.0183  58  ARG A CB  
524  C  CG  . ARG A 58  ? 0.1965 0.2125 0.2753 -0.0403 0.0153  0.0904  58  ARG A CG  
525  C  CD  . ARG A 58  ? 0.3003 0.2813 0.2460 -0.0746 -0.0230 0.0829  58  ARG A CD  
526  N  NE  . ARG A 58  ? 0.2345 0.2544 0.2213 -0.0461 0.0119  0.0207  58  ARG A NE  
527  C  CZ  . ARG A 58  ? 0.1796 0.2698 0.1712 -0.0568 0.0120  0.0515  58  ARG A CZ  
528  N  NH1 . ARG A 58  ? 0.2838 0.2809 0.2179 -0.0661 0.0465  0.0586  58  ARG A NH1 
529  N  NH2 . ARG A 58  ? 0.2249 0.2275 0.2099 -0.0281 0.0131  0.0328  58  ARG A NH2 
530  N  N   . ILE A 59  ? 0.2349 0.1753 0.0961 0.0186  -0.0006 0.0329  59  ILE A N   
531  C  CA  . ILE A 59  ? 0.2090 0.1764 0.1124 -0.0114 0.0068  0.0461  59  ILE A CA  
532  C  C   . ILE A 59  ? 0.2089 0.1439 0.1104 0.0041  -0.0320 0.0307  59  ILE A C   
533  O  O   . ILE A 59  ? 0.2684 0.2194 0.0886 0.0172  -0.0087 0.0295  59  ILE A O   
534  C  CB  . ILE A 59  ? 0.2440 0.1465 0.0983 0.0031  -0.0097 0.0253  59  ILE A CB  
535  C  CG1 . ILE A 59  ? 0.2500 0.1465 0.0996 0.0057  -0.0135 0.0164  59  ILE A CG1 
536  C  CG2 . ILE A 59  ? 0.3043 0.1588 0.1176 0.0229  -0.0533 0.0098  59  ILE A CG2 
537  C  CD1 . ILE A 59  ? 0.2486 0.1524 0.1234 -0.0010 -0.0204 -0.0027 59  ILE A CD1 
538  N  N   . LEU A 60  ? 0.1604 0.1465 0.1465 -0.0120 -0.0038 0.0046  60  LEU A N   
539  C  CA  . LEU A 60  ? 0.2046 0.1325 0.1167 0.0017  -0.0317 0.0340  60  LEU A CA  
540  C  C   . LEU A 60  ? 0.1840 0.1498 0.1131 -0.0219 -0.0020 0.0027  60  LEU A C   
541  O  O   . LEU A 60  ? 0.1816 0.1624 0.1070 -0.0102 0.0120  0.0276  60  LEU A O   
542  C  CB  . LEU A 60  ? 0.2028 0.1395 0.1747 -0.0355 0.0035  0.0068  60  LEU A CB  
543  C  CG  . LEU A 60  ? 0.2240 0.1484 0.1852 -0.0364 -0.0131 0.0171  60  LEU A CG  
544  C  CD1 . LEU A 60  ? 0.2379 0.2034 0.1976 -0.0412 0.0348  0.0307  60  LEU A CD1 
545  C  CD2 . LEU A 60  ? 0.2623 0.1764 0.2020 -0.0386 0.0020  0.0098  60  LEU A CD2 
546  N  N   . ASN A 61  ? 0.2038 0.1181 0.1304 0.0020  0.0086  0.0241  61  ASN A N   
547  C  CA  . ASN A 61  ? 0.1904 0.1580 0.1217 -0.0181 0.0241  -0.0208 61  ASN A CA  
548  C  C   . ASN A 61  ? 0.2099 0.1410 0.1167 -0.0274 0.0142  0.0131  61  ASN A C   
549  O  O   . ASN A 61  ? 0.2496 0.1722 0.1308 -0.0342 0.0285  0.0423  61  ASN A O   
550  C  CB  . ASN A 61  ? 0.2476 0.1482 0.1272 0.0006  0.0362  0.0175  61  ASN A CB  
551  C  CG  . ASN A 61  ? 0.2160 0.1651 0.1076 -0.0390 0.0315  -0.0208 61  ASN A CG  
552  O  OD1 . ASN A 61  ? 0.2368 0.1544 0.1342 -0.0220 0.0337  -0.0010 61  ASN A OD1 
553  N  ND2 . ASN A 61  ? 0.2623 0.1543 0.1298 -0.0410 0.0533  -0.0074 61  ASN A ND2 
554  N  N   . ASN A 62  ? 0.2282 0.1439 0.1045 -0.0421 0.0023  0.0074  62  ASN A N   
555  C  CA  . ASN A 62  ? 0.2029 0.1841 0.1333 -0.0214 0.0165  0.0000  62  ASN A CA  
556  C  C   . ASN A 62  ? 0.1967 0.1994 0.1316 -0.0908 0.0241  0.0087  62  ASN A C   
557  O  O   . ASN A 62  ? 0.2205 0.2417 0.1914 -0.0649 0.0262  0.0261  62  ASN A O   
558  C  CB  . ASN A 62  ? 0.2655 0.1448 0.1659 -0.0498 0.0129  0.0142  62  ASN A CB  
559  C  CG  . ASN A 62  ? 0.2264 0.1569 0.1411 -0.0353 0.0219  -0.0254 62  ASN A CG  
560  O  OD1 . ASN A 62  ? 0.2284 0.1524 0.1376 -0.0368 0.0164  -0.0041 62  ASN A OD1 
561  N  ND2 . ASN A 62  ? 0.3722 0.1580 0.1615 -0.0076 0.0384  -0.0098 62  ASN A ND2 
562  N  N   . GLY A 63  ? 0.1958 0.1691 0.1552 -0.0220 0.0206  0.0263  63  GLY A N   
563  C  CA  . GLY A 63  ? 0.2117 0.1907 0.1465 -0.0573 0.0285  0.0294  63  GLY A CA  
564  C  C   . GLY A 63  ? 0.2171 0.1414 0.1957 -0.0177 0.0120  0.0049  63  GLY A C   
565  O  O   . GLY A 63  ? 0.1993 0.1941 0.1756 -0.0326 0.0401  -0.0057 63  GLY A O   
566  N  N   . HIS A 64  ? 0.1896 0.1695 0.1418 -0.0373 0.0329  0.0142  64  HIS A N   
567  C  CA  . HIS A 64  ? 0.1827 0.1766 0.1474 -0.0318 0.0331  0.0076  64  HIS A CA  
568  C  C   . HIS A 64  ? 0.1597 0.1333 0.1596 -0.0342 0.0197  0.0082  64  HIS A C   
569  O  O   . HIS A 64  ? 0.1995 0.1801 0.2295 -0.0320 0.0074  0.0680  64  HIS A O   
570  C  CB  . HIS A 64  ? 0.1581 0.2088 0.1764 -0.0582 0.0023  0.0262  64  HIS A CB  
571  C  CG  . HIS A 64  ? 0.2179 0.2748 0.1861 -0.0126 0.0186  0.0397  64  HIS A CG  
572  N  ND1 . HIS A 64  ? 0.3503 0.2888 0.2389 -0.0322 -0.0109 -0.0068 64  HIS A ND1 
573  C  CD2 . HIS A 64  ? 0.2572 0.3276 0.1474 0.0225  -0.0155 -0.0460 64  HIS A CD2 
574  C  CE1 . HIS A 64  ? 0.3919 0.2849 0.3100 -0.0640 -0.0054 -0.0788 64  HIS A CE1 
575  N  NE2 . HIS A 64  ? 0.3668 0.3531 0.4027 -0.0285 0.0401  -0.0715 64  HIS A NE2 
576  N  N   . ALA A 65  ? 0.1614 0.1453 0.1369 -0.0249 0.0059  0.0186  65  ALA A N   
577  C  CA  . ALA A 65  ? 0.1694 0.1332 0.1201 -0.0318 0.0126  0.0000  65  ALA A CA  
578  C  C   . ALA A 65  ? 0.1990 0.1172 0.0956 -0.0164 0.0137  0.0027  65  ALA A C   
579  O  O   . ALA A 65  ? 0.2074 0.1542 0.1261 -0.0397 0.0217  0.0148  65  ALA A O   
580  C  CB  . ALA A 65  ? 0.1967 0.1605 0.1246 -0.0348 0.0173  -0.0131 65  ALA A CB  
581  N  N   . PHE A 66  ? 0.1835 0.1412 0.1076 -0.0166 0.0046  0.0142  66  PHE A N   
582  C  CA  . PHE A 66  ? 0.2038 0.1405 0.1018 0.0096  0.0071  0.0263  66  PHE A CA  
583  C  C   . PHE A 66  ? 0.1941 0.1386 0.0922 -0.0159 -0.0040 0.0068  66  PHE A C   
584  O  O   . PHE A 66  ? 0.2334 0.1349 0.1000 -0.0082 0.0142  0.0104  66  PHE A O   
585  C  CB  . PHE A 66  ? 0.2334 0.1796 0.0935 -0.0082 -0.0207 0.0076  66  PHE A CB  
586  C  CG  . PHE A 66  ? 0.2313 0.1632 0.0838 -0.0120 -0.0098 -0.0109 66  PHE A CG  
587  C  CD1 . PHE A 66  ? 0.2169 0.1849 0.0992 0.0137  -0.0176 -0.0098 66  PHE A CD1 
588  C  CD2 . PHE A 66  ? 0.2140 0.1711 0.1034 0.0031  -0.0104 -0.0160 66  PHE A CD2 
589  C  CE1 . PHE A 66  ? 0.2368 0.1947 0.1216 -0.0164 -0.0414 -0.0096 66  PHE A CE1 
590  C  CE2 . PHE A 66  ? 0.2295 0.1797 0.1066 -0.0324 -0.0125 -0.0184 66  PHE A CE2 
591  C  CZ  . PHE A 66  ? 0.2046 0.1950 0.1190 -0.0204 -0.0198 -0.0260 66  PHE A CZ  
592  N  N   . ASN A 67  ? 0.1844 0.1400 0.1106 -0.0082 0.0000  0.0230  67  ASN A N   
593  C  CA  . ASN A 67  ? 0.1623 0.1368 0.1079 -0.0063 -0.0003 -0.0048 67  ASN A CA  
594  C  C   . ASN A 67  ? 0.1721 0.1235 0.0935 -0.0120 -0.0214 0.0054  67  ASN A C   
595  O  O   . ASN A 67  ? 0.2108 0.1659 0.0948 -0.0098 -0.0041 0.0361  67  ASN A O   
596  C  CB  . ASN A 67  ? 0.2277 0.1634 0.1124 -0.0313 -0.0293 0.0080  67  ASN A CB  
597  C  CG  . ASN A 67  ? 0.1712 0.1807 0.1642 -0.0417 0.0015  -0.0051 67  ASN A CG  
598  O  OD1 . ASN A 67  ? 0.2221 0.2197 0.1632 -0.0599 -0.0401 0.0661  67  ASN A OD1 
599  N  ND2 . ASN A 67  ? 0.2096 0.2404 0.1770 -0.0410 -0.0423 -0.0063 67  ASN A ND2 
600  N  N   . VAL A 68  ? 0.1780 0.1277 0.1045 0.0035  0.0017  0.0125  68  VAL A N   
601  C  CA  . VAL A 68  ? 0.2302 0.1350 0.0834 0.0593  -0.0258 0.0120  68  VAL A CA  
602  C  C   . VAL A 68  ? 0.2171 0.1255 0.1045 0.0221  -0.0243 0.0046  68  VAL A C   
603  O  O   . VAL A 68  ? 0.2127 0.1272 0.1001 0.0148  -0.0131 0.0146  68  VAL A O   
604  C  CB  . VAL A 68  ? 0.1976 0.1402 0.1297 0.0082  -0.0142 0.0087  68  VAL A CB  
605  C  CG1 . VAL A 68  ? 0.2061 0.2012 0.1272 0.0417  -0.0447 -0.0031 68  VAL A CG1 
606  C  CG2 . VAL A 68  ? 0.2099 0.1561 0.1386 -0.0093 -0.0174 -0.0197 68  VAL A CG2 
607  N  N   . GLU A 69  ? 0.2417 0.1326 0.1165 0.0285  0.0035  0.0240  69  GLU A N   
608  C  CA  . GLU A 69  ? 0.2180 0.1360 0.1158 0.0096  -0.0006 0.0186  69  GLU A CA  
609  C  C   . GLU A 69  ? 0.2186 0.1387 0.1234 0.0232  -0.0292 0.0307  69  GLU A C   
610  O  O   . GLU A 69  ? 0.2428 0.1482 0.1562 0.0293  -0.0526 0.0135  69  GLU A O   
611  C  CB  . GLU A 69  ? 0.1555 0.1906 0.2018 -0.0031 0.0383  0.0285  69  GLU A CB  
612  C  CG  . GLU A 69  ? 0.1764 0.2187 0.1940 -0.0423 0.0206  0.0329  69  GLU A CG  
613  C  CD  . GLU A 69  ? 0.1967 0.2090 0.2766 0.0131  0.0502  0.0706  69  GLU A CD  
614  O  OE1 . GLU A 69  ? 0.2809 0.2492 0.2309 0.0027  0.0478  0.0838  69  GLU A OE1 
615  O  OE2 . GLU A 69  ? 0.2274 0.2655 0.3330 -0.0208 0.0744  0.0832  69  GLU A OE2 
616  N  N   . PHE A 70  ? 0.2192 0.1377 0.1228 0.0181  -0.0060 0.0182  70  PHE A N   
617  C  CA  . PHE A 70  ? 0.1877 0.1149 0.1315 0.0208  -0.0263 0.0151  70  PHE A CA  
618  C  C   . PHE A 70  ? 0.2010 0.1502 0.1405 0.0031  -0.0390 0.0175  70  PHE A C   
619  O  O   . PHE A 70  ? 0.2118 0.1316 0.1683 0.0152  -0.0302 0.0219  70  PHE A O   
620  C  CB  . PHE A 70  ? 0.1975 0.1291 0.1282 0.0131  -0.0282 0.0161  70  PHE A CB  
621  C  CG  . PHE A 70  ? 0.1827 0.1230 0.1431 0.0142  -0.0260 0.0271  70  PHE A CG  
622  C  CD1 . PHE A 70  ? 0.2108 0.1379 0.1324 0.0315  -0.0153 0.0331  70  PHE A CD1 
623  C  CD2 . PHE A 70  ? 0.1782 0.1456 0.1273 0.0142  -0.0248 0.0230  70  PHE A CD2 
624  C  CE1 . PHE A 70  ? 0.2158 0.1555 0.1465 0.0351  -0.0027 0.0324  70  PHE A CE1 
625  C  CE2 . PHE A 70  ? 0.2117 0.1316 0.1544 0.0091  -0.0250 0.0195  70  PHE A CE2 
626  C  CZ  . PHE A 70  ? 0.2504 0.1465 0.1387 0.0260  -0.0006 0.0049  70  PHE A CZ  
627  N  N   A ASP A 71  ? 0.2037 0.1395 0.1666 0.0129  -0.0292 0.0434  71  ASP A N   
628  N  N   B ASP A 71  ? 0.2331 0.1448 0.1208 0.0219  -0.0368 0.0441  71  ASP A N   
629  C  CA  A ASP A 71  ? 0.2250 0.1351 0.2099 0.0186  0.0208  0.0335  71  ASP A CA  
630  C  CA  B ASP A 71  ? 0.2018 0.1140 0.1694 0.0566  -0.0086 0.0571  71  ASP A CA  
631  C  C   A ASP A 71  ? 0.1527 0.0951 0.2644 0.0126  0.0108  0.0249  71  ASP A C   
632  C  C   B ASP A 71  ? 0.1775 0.1237 0.2149 -0.0046 0.0098  0.0320  71  ASP A C   
633  O  O   A ASP A 71  ? 0.2651 0.1932 0.1862 -0.0125 0.0197  0.0155  71  ASP A O   
634  O  O   B ASP A 71  ? 0.1712 0.2018 0.1613 -0.0113 -0.0060 0.0263  71  ASP A O   
635  C  CB  A ASP A 71  ? 0.2456 0.1739 0.2029 0.0109  -0.0108 0.0504  71  ASP A CB  
636  C  CB  B ASP A 71  ? 0.1861 0.1569 0.1692 0.0209  -0.0232 0.0593  71  ASP A CB  
637  C  CG  A ASP A 71  ? 0.2122 0.1763 0.2637 0.0282  0.0054  0.0351  71  ASP A CG  
638  C  CG  B ASP A 71  ? 0.2770 0.1585 0.2161 0.0229  -0.0335 0.0450  71  ASP A CG  
639  O  OD1 A ASP A 71  ? 0.3111 0.1599 0.2874 0.0197  0.0063  0.0458  71  ASP A OD1 
640  O  OD1 B ASP A 71  ? 0.2870 0.1506 0.2368 0.0566  -0.0098 0.0329  71  ASP A OD1 
641  O  OD2 A ASP A 71  ? 0.3143 0.1739 0.3664 0.0533  -0.0832 -0.0087 71  ASP A OD2 
642  O  OD2 B ASP A 71  ? 0.4314 0.2284 0.3287 0.0342  -0.1289 0.0493  71  ASP A OD2 
643  N  N   . ASP A 72  ? 0.2055 0.1210 0.2213 0.0037  -0.0165 0.0166  72  ASP A N   
644  C  CA  . ASP A 72  ? 0.2126 0.1110 0.2633 0.0000  0.0232  -0.0040 72  ASP A CA  
645  C  C   . ASP A 72  ? 0.3061 0.1210 0.2601 -0.0153 0.0476  -0.0010 72  ASP A C   
646  O  O   . ASP A 72  ? 0.3628 0.1246 0.2442 -0.0353 0.0538  -0.0175 72  ASP A O   
647  C  CB  . ASP A 72  ? 0.1831 0.1810 0.2043 -0.0054 0.0252  0.0164  72  ASP A CB  
648  C  CG  . ASP A 72  ? 0.2250 0.2379 0.1550 0.0054  -0.0142 0.0285  72  ASP A CG  
649  O  OD1 . ASP A 72  ? 0.2020 0.3046 0.2230 -0.0344 -0.0394 0.0869  72  ASP A OD1 
650  O  OD2 . ASP A 72  ? 0.2381 0.2569 0.1590 -0.0286 -0.0166 0.0135  72  ASP A OD2 
651  N  N   . SER A 73  ? 0.2694 0.1272 0.3064 0.0043  0.0259  0.0408  73  SER A N   
652  C  CA  . SER A 73  ? 0.3043 0.1270 0.3470 -0.0087 0.0412  0.0175  73  SER A CA  
653  C  C   . SER A 73  ? 0.2558 0.1404 0.3201 -0.0091 0.0375  -0.0076 73  SER A C   
654  O  O   . SER A 73  ? 0.2784 0.1352 0.3021 0.0175  0.0141  0.0131  73  SER A O   
655  C  CB  . SER A 73  ? 0.3955 0.1805 0.4020 -0.0460 0.0154  0.1084  73  SER A CB  
656  O  OG  . SER A 73  ? 0.4038 0.1650 0.3197 0.0361  0.0679  0.0816  73  SER A OG  
657  N  N   . GLN A 74  ? 0.2399 0.1454 0.4149 0.0113  0.0719  0.0019  74  GLN A N   
658  C  CA  . GLN A 74  ? 0.2899 0.1849 0.2860 0.0206  0.0131  0.0447  74  GLN A CA  
659  C  C   . GLN A 74  ? 0.2141 0.2055 0.3402 0.0303  0.0082  0.0076  74  GLN A C   
660  O  O   . GLN A 74  ? 0.2318 0.1763 0.2310 -0.0322 -0.0531 0.0275  74  GLN A O   
661  C  CB  . GLN A 74  ? 0.2240 0.2374 0.3536 0.0274  -0.0081 0.0392  74  GLN A CB  
662  C  CG  . GLN A 74  ? 0.3294 0.3050 0.4113 0.0172  -0.0197 0.1694  74  GLN A CG  
663  C  CD  . GLN A 74  ? 0.3707 0.3402 0.3258 0.0527  -0.0350 0.1462  74  GLN A CD  
664  O  OE1 . GLN A 74  ? 0.6172 0.5292 0.8335 -0.0236 0.2849  0.0489  74  GLN A OE1 
665  N  NE2 . GLN A 74  ? 0.7124 0.7404 0.4005 0.0996  -0.0666 -0.2194 74  GLN A NE2 
666  N  N   A ASP A 75  ? 0.4451 0.4099 0.2432 -0.1058 0.0403  -0.0560 75  ASP A N   
667  N  N   B ASP A 75  ? 0.1870 0.1781 0.2551 0.0164  -0.0296 0.0460  75  ASP A N   
668  C  CA  A ASP A 75  ? 0.2328 0.2913 0.3589 0.0684  -0.2055 -0.0263 75  ASP A CA  
669  C  CA  B ASP A 75  ? 0.1738 0.1395 0.1852 0.0242  -0.0640 0.0264  75  ASP A CA  
670  C  C   A ASP A 75  ? 0.1914 0.2885 0.4914 0.0608  -0.0161 -0.0208 75  ASP A C   
671  C  C   B ASP A 75  ? 0.1958 0.2378 0.2850 -0.0469 -0.0035 -0.0362 75  ASP A C   
672  O  O   A ASP A 75  ? 0.2478 0.5770 0.5579 0.0498  0.0662  0.1164  75  ASP A O   
673  O  O   B ASP A 75  ? 0.2099 0.1994 0.2960 -0.0010 -0.0326 0.0263  75  ASP A O   
674  C  CB  A ASP A 75  ? 0.4171 0.3730 0.3682 0.1022  0.0829  0.0745  75  ASP A CB  
675  C  CB  B ASP A 75  ? 0.2081 0.1606 0.2265 0.0005  -0.0013 0.0230  75  ASP A CB  
676  C  CG  A ASP A 75  ? 0.5583 0.1423 0.4404 0.0810  -0.0131 -0.0445 75  ASP A CG  
677  C  CG  B ASP A 75  ? 0.2910 0.1816 0.2558 -0.0335 0.0181  0.0140  75  ASP A CG  
678  O  OD1 A ASP A 75  ? 0.1999 0.2522 0.2055 -0.0432 0.0205  0.0487  75  ASP A OD1 
679  O  OD1 B ASP A 75  ? 0.1666 0.2249 0.3280 -0.0129 -0.0359 0.0697  75  ASP A OD1 
680  O  OD2 A ASP A 75  ? 0.5396 0.2982 0.4074 0.0114  0.1278  0.0461  75  ASP A OD2 
681  O  OD2 B ASP A 75  ? 0.4393 0.2917 0.2985 0.0238  0.1172  0.0480  75  ASP A OD2 
682  N  N   . LYS A 76  ? 0.2662 0.2048 0.2684 -0.0384 -0.0496 0.0631  76  LYS A N   
683  C  CA  . LYS A 76  ? 0.3341 0.1861 0.3319 0.0012  -0.0610 0.0276  76  LYS A CA  
684  C  C   . LYS A 76  ? 0.7361 0.1905 0.6668 0.0392  -0.0658 0.0983  76  LYS A C   
685  O  O   . LYS A 76  ? 0.3908 0.9858 0.9706 0.1633  -0.3199 0.1535  76  LYS A O   
686  C  CB  . LYS A 76  ? 0.2896 0.1685 0.3652 -0.0614 -0.1146 0.0346  76  LYS A CB  
687  C  CG  . LYS A 76  ? 0.7530 0.2292 0.3255 -0.0731 -0.2219 0.0553  76  LYS A CG  
688  C  CD  . LYS A 76  ? 0.9872 0.2310 0.2597 -0.1243 -0.2587 0.0573  76  LYS A CD  
689  C  CE  . LYS A 76  ? 0.9225 0.3743 0.4049 -0.0515 -0.1440 0.1280  76  LYS A CE  
690  N  NZ  . LYS A 76  ? 0.9911 0.4045 0.3567 0.1867  0.0649  0.1973  76  LYS A NZ  
691  N  N   . ALA A 77  ? 0.2316 0.3707 0.4469 0.0864  -0.2002 0.0355  77  ALA A N   
692  C  CA  . ALA A 77  ? 0.1687 0.2336 0.2025 0.0109  -0.0566 -0.0049 77  ALA A CA  
693  C  C   . ALA A 77  ? 0.1297 0.1949 0.2356 -0.0103 -0.0658 -0.0062 77  ALA A C   
694  O  O   . ALA A 77  ? 0.1312 0.3776 0.3046 -0.0208 -0.0351 -0.1146 77  ALA A O   
695  C  CB  . ALA A 77  ? 0.2254 0.2806 0.1770 -0.0155 -0.0480 0.0124  77  ALA A CB  
696  N  N   A VAL A 78  ? 0.1545 0.1968 0.1905 -0.0199 -0.0724 0.0040  78  VAL A N   
697  N  N   B VAL A 78  ? 0.1823 0.1567 0.2045 -0.0215 -0.0344 0.0163  78  VAL A N   
698  C  CA  A VAL A 78  ? 0.1756 0.1578 0.1941 0.0166  -0.0912 0.0160  78  VAL A CA  
699  C  CA  B VAL A 78  ? 0.1215 0.1330 0.1976 -0.0285 0.0147  0.0170  78  VAL A CA  
700  C  C   A VAL A 78  ? 0.1333 0.1221 0.2231 0.0020  -0.0604 -0.0153 78  VAL A C   
701  C  C   B VAL A 78  ? 0.0957 0.1676 0.1527 -0.0074 0.0159  -0.0024 78  VAL A C   
702  O  O   A VAL A 78  ? 0.1456 0.1483 0.1632 -0.0107 -0.0307 -0.0115 78  VAL A O   
703  O  O   B VAL A 78  ? 0.0930 0.1783 0.1703 -0.0262 0.0013  -0.0137 78  VAL A O   
704  C  CB  A VAL A 78  ? 0.1447 0.1616 0.2410 0.0081  -0.0205 0.0131  78  VAL A CB  
705  C  CB  B VAL A 78  ? 0.1356 0.1456 0.2558 -0.0274 -0.0098 -0.0142 78  VAL A CB  
706  C  CG1 A VAL A 78  ? 0.1553 0.1620 0.2587 0.0161  0.0114  0.0208  78  VAL A CG1 
707  C  CG1 B VAL A 78  ? 0.1677 0.1967 0.2320 0.0115  0.0538  -0.0489 78  VAL A CG1 
708  C  CG2 A VAL A 78  ? 0.1825 0.3201 0.3190 0.0309  0.0265  0.0237  78  VAL A CG2 
709  C  CG2 B VAL A 78  ? 0.1509 0.1956 0.2702 0.0175  0.0252  0.0461  78  VAL A CG2 
710  N  N   . LEU A 79  ? 0.1254 0.1464 0.1780 -0.0087 -0.0170 0.0030  79  LEU A N   
711  C  CA  . LEU A 79  ? 0.1563 0.1437 0.1622 -0.0126 -0.0173 0.0109  79  LEU A CA  
712  C  C   . LEU A 79  ? 0.1597 0.1632 0.1685 -0.0309 -0.0013 -0.0026 79  LEU A C   
713  O  O   . LEU A 79  ? 0.1712 0.1676 0.1765 -0.0353 0.0080  -0.0164 79  LEU A O   
714  C  CB  . LEU A 79  ? 0.1221 0.1835 0.1852 0.0019  -0.0115 0.0126  79  LEU A CB  
715  C  CG  . LEU A 79  ? 0.1358 0.1884 0.1870 0.0080  -0.0020 0.0225  79  LEU A CG  
716  C  CD1 . LEU A 79  ? 0.1409 0.2018 0.3847 -0.0114 0.0024  0.0785  79  LEU A CD1 
717  C  CD2 . LEU A 79  ? 0.1377 0.2021 0.1905 0.0076  0.0071  0.0026  79  LEU A CD2 
718  N  N   . LYS A 80  ? 0.1464 0.1851 0.1738 -0.0082 0.0182  0.0013  80  LYS A N   
719  C  CA  . LYS A 80  ? 0.1553 0.1553 0.2134 -0.0247 0.0236  0.0003  80  LYS A CA  
720  C  C   . LYS A 80  ? 0.1097 0.1763 0.2125 0.0098  0.0242  0.0120  80  LYS A C   
721  O  O   . LYS A 80  ? 0.1342 0.1722 0.2202 -0.0142 0.0043  0.0208  80  LYS A O   
722  C  CB  . LYS A 80  ? 0.2204 0.2064 0.2526 0.0538  0.0273  0.0412  80  LYS A CB  
723  C  CG  . LYS A 80  ? 0.1977 0.2037 0.3057 0.0274  0.0135  0.0399  80  LYS A CG  
724  C  CD  . LYS A 80  ? 0.2116 0.2942 0.4092 0.0571  -0.0164 0.1057  80  LYS A CD  
725  C  CE  . LYS A 80  ? 0.3546 0.3219 0.5460 0.0559  -0.0296 0.1588  80  LYS A CE  
726  N  NZ  . LYS A 80  ? 0.3488 0.5587 0.5616 -0.0348 -0.0219 -0.2011 80  LYS A NZ  
727  N  N   . GLY A 81  ? 0.1800 0.1950 0.1939 0.0176  0.0247  0.0052  81  GLY A N   
728  C  CA  . GLY A 81  ? 0.1676 0.2159 0.2274 0.0313  0.0560  0.0450  81  GLY A CA  
729  C  C   . GLY A 81  ? 0.1615 0.1985 0.2386 0.0208  0.0568  0.0504  81  GLY A C   
730  O  O   . GLY A 81  ? 0.1412 0.1887 0.2143 -0.0185 0.0296  -0.0148 81  GLY A O   
731  N  N   . GLY A 82  ? 0.1303 0.2389 0.3865 0.0013  0.0522  0.0794  82  GLY A N   
732  C  CA  . GLY A 82  ? 0.1718 0.2467 0.4300 0.0315  0.0364  0.0882  82  GLY A CA  
733  C  C   . GLY A 82  ? 0.1905 0.2345 0.2827 0.0746  0.0526  0.0763  82  GLY A C   
734  O  O   . GLY A 82  ? 0.2511 0.4131 0.3262 0.1623  0.1146  0.1181  82  GLY A O   
735  N  N   . PRO A 83  ? 0.1474 0.1806 0.2684 0.0195  0.0394  0.0351  83  PRO A N   
736  C  CA  . PRO A 83  ? 0.2117 0.1702 0.2187 0.0606  0.0355  0.0329  83  PRO A CA  
737  C  C   . PRO A 83  ? 0.1543 0.2134 0.1834 0.0397  -0.0129 -0.0225 83  PRO A C   
738  O  O   . PRO A 83  ? 0.2399 0.2449 0.2179 0.0172  -0.0582 -0.0063 83  PRO A O   
739  C  CB  . PRO A 83  ? 0.1861 0.1939 0.2275 0.0469  -0.0120 0.0135  83  PRO A CB  
740  C  CG  . PRO A 83  ? 0.1454 0.1877 0.2202 0.0412  0.0186  0.0027  83  PRO A CG  
741  C  CD  . PRO A 83  ? 0.1447 0.1527 0.2619 0.0309  0.0461  0.0252  83  PRO A CD  
742  N  N   . LEU A 84  ? 0.1578 0.1731 0.1712 0.0399  0.0165  -0.0038 84  LEU A N   
743  C  CA  . LEU A 84  ? 0.1604 0.1463 0.1641 0.0335  -0.0035 -0.0281 84  LEU A CA  
744  C  C   . LEU A 84  ? 0.1508 0.1800 0.2356 0.0546  -0.0166 -0.0381 84  LEU A C   
745  O  O   . LEU A 84  ? 0.1782 0.1968 0.2587 0.0505  0.0326  -0.0408 84  LEU A O   
746  C  CB  . LEU A 84  ? 0.1324 0.1360 0.1898 0.0273  0.0166  -0.0049 84  LEU A CB  
747  C  CG  . LEU A 84  ? 0.1246 0.1260 0.1739 0.0142  0.0192  -0.0140 84  LEU A CG  
748  C  CD1 . LEU A 84  ? 0.1519 0.1507 0.1815 0.0236  0.0135  -0.0129 84  LEU A CD1 
749  C  CD2 . LEU A 84  ? 0.1303 0.1323 0.1958 0.0065  0.0186  -0.0109 84  LEU A CD2 
750  N  N   . ASP A 85  ? 0.2082 0.1825 0.2161 0.0274  0.0231  -0.0557 85  ASP A N   
751  C  CA  . ASP A 85  ? 0.3064 0.1465 0.2637 -0.0038 0.0324  -0.0798 85  ASP A CA  
752  C  C   . ASP A 85  ? 0.2108 0.1418 0.4088 0.0401  0.0537  0.0193  85  ASP A C   
753  O  O   . ASP A 85  ? 0.2892 0.2957 0.3262 0.0241  0.0348  -0.0553 85  ASP A O   
754  C  CB  . ASP A 85  ? 0.3851 0.1862 0.2838 0.0281  0.0621  -0.0597 85  ASP A CB  
755  C  CG  . ASP A 85  ? 0.4081 0.2633 0.4146 -0.0026 0.1712  -0.0102 85  ASP A CG  
756  O  OD1 . ASP A 85  ? 0.4401 0.6754 0.3610 -0.1216 0.0974  0.0186  85  ASP A OD1 
757  O  OD2 . ASP A 85  ? 0.5472 0.6517 0.7113 -0.1852 -0.0074 -0.2345 85  ASP A OD2 
758  N  N   . GLY A 86  ? 0.3219 0.2605 0.3197 -0.0062 -0.0511 0.0515  86  GLY A N   
759  C  CA  . GLY A 86  ? 0.3855 0.2867 0.2504 -0.0584 -0.0263 0.0239  86  GLY A CA  
760  C  C   . GLY A 86  ? 0.3434 0.2673 0.2597 -0.0873 -0.0758 0.0187  86  GLY A C   
761  O  O   . GLY A 86  ? 0.3531 0.3822 0.3104 -0.1924 -0.0340 0.0337  86  GLY A O   
762  N  N   A THR A 87  ? 0.2292 0.2169 0.2474 0.0612  0.0511  -0.0103 87  THR A N   
763  N  N   B THR A 87  ? 0.1743 0.1453 0.2011 -0.0027 0.0034  -0.0340 87  THR A N   
764  C  CA  A THR A 87  ? 0.1572 0.2551 0.3273 0.0355  -0.0242 -0.0040 87  THR A CA  
765  C  CA  B THR A 87  ? 0.1269 0.1250 0.1861 0.0076  0.0308  -0.0381 87  THR A CA  
766  C  C   A THR A 87  ? 0.2089 0.1176 0.2442 0.0195  -0.0335 -0.0353 87  THR A C   
767  C  C   B THR A 87  ? 0.0916 0.1079 0.1640 0.0181  0.0038  0.0098  87  THR A C   
768  O  O   A THR A 87  ? 0.1923 0.1428 0.1875 0.0198  -0.0436 -0.0170 87  THR A O   
769  O  O   B THR A 87  ? 0.1339 0.0996 0.1368 -0.0027 0.0252  -0.0113 87  THR A O   
770  C  CB  A THR A 87  ? 0.1572 0.2753 0.3143 0.0493  -0.0247 -0.0173 87  THR A CB  
771  C  CB  B THR A 87  ? 0.1720 0.1145 0.2478 0.0274  0.0176  -0.0159 87  THR A CB  
772  O  OG1 A THR A 87  ? 0.1403 0.2601 0.3248 0.0974  -0.0093 -0.0833 87  THR A OG1 
773  O  OG1 B THR A 87  ? 0.2637 0.2565 0.4178 -0.0307 -0.0812 -0.0627 87  THR A OG1 
774  C  CG2 A THR A 87  ? 0.2662 0.2680 0.3865 0.0683  -0.0148 0.0318  87  THR A CG2 
775  C  CG2 B THR A 87  ? 0.1023 0.1303 0.1465 0.0137  0.0193  0.0324  87  THR A CG2 
776  N  N   . TYR A 88  ? 0.1088 0.1263 0.1982 0.0109  -0.0074 -0.0131 88  TYR A N   
777  C  CA  . TYR A 88  ? 0.1194 0.1273 0.1647 0.0035  -0.0087 -0.0065 88  TYR A CA  
778  C  C   . TYR A 88  ? 0.1133 0.1206 0.1735 -0.0010 -0.0196 -0.0051 88  TYR A C   
779  O  O   . TYR A 88  ? 0.1669 0.1870 0.1914 -0.0474 -0.0417 0.0186  88  TYR A O   
780  C  CB  . TYR A 88  ? 0.1235 0.1079 0.1818 0.0109  -0.0091 -0.0052 88  TYR A CB  
781  C  CG  . TYR A 88  ? 0.1288 0.1025 0.1599 0.0108  -0.0093 -0.0162 88  TYR A CG  
782  C  CD1 . TYR A 88  ? 0.1312 0.1281 0.1572 0.0186  0.0118  0.0043  88  TYR A CD1 
783  C  CD2 . TYR A 88  ? 0.1237 0.0794 0.1551 0.0197  -0.0017 0.0010  88  TYR A CD2 
784  C  CE1 . TYR A 88  ? 0.1252 0.1295 0.1555 0.0154  0.0171  -0.0092 88  TYR A CE1 
785  C  CE2 . TYR A 88  ? 0.1238 0.1014 0.1370 0.0043  0.0000  -0.0035 88  TYR A CE2 
786  C  CZ  . TYR A 88  ? 0.1254 0.0988 0.1367 0.0057  0.0000  -0.0003 88  TYR A CZ  
787  O  OH  . TYR A 88  ? 0.1312 0.1174 0.1465 0.0097  0.0046  -0.0135 88  TYR A OH  
788  N  N   . ARG A 89  ? 0.1101 0.1027 0.1576 0.0115  -0.0136 -0.0087 89  ARG A N   
789  C  CA  . ARG A 89  ? 0.1498 0.0939 0.1589 0.0142  -0.0318 0.0043  89  ARG A CA  
790  C  C   . ARG A 89  ? 0.1246 0.0894 0.1234 -0.0060 -0.0252 0.0294  89  ARG A C   
791  O  O   . ARG A 89  ? 0.1102 0.0966 0.1335 0.0006  -0.0183 0.0093  89  ARG A O   
792  C  CB  . ARG A 89  ? 0.2089 0.0869 0.2011 0.0162  -0.0608 0.0239  89  ARG A CB  
793  C  CG  . ARG A 89  ? 0.2277 0.1323 0.1826 -0.0120 -0.0262 0.0031  89  ARG A CG  
794  C  CD  . ARG A 89  ? 0.2529 0.1335 0.1941 0.0287  -0.0146 0.0012  89  ARG A CD  
795  N  NE  . ARG A 89  ? 0.2206 0.1562 0.2046 0.0035  -0.0076 0.0419  89  ARG A NE  
796  C  CZ  . ARG A 89  ? 0.2149 0.1421 0.1692 0.0005  -0.0161 0.0159  89  ARG A CZ  
797  N  NH1 . ARG A 89  ? 0.2536 0.1765 0.2504 0.0261  0.0395  0.0555  89  ARG A NH1 
798  N  NH2 . ARG A 89  ? 0.2832 0.1571 0.2372 0.0322  -0.0118 0.0230  89  ARG A NH2 
799  N  N   . LEU A 90  ? 0.1298 0.1025 0.1342 -0.0060 -0.0219 0.0107  90  LEU A N   
800  C  CA  . LEU A 90  ? 0.1412 0.1005 0.1183 -0.0031 -0.0230 0.0136  90  LEU A CA  
801  C  C   . LEU A 90  ? 0.1296 0.1176 0.1136 -0.0003 -0.0252 0.0155  90  LEU A C   
802  O  O   . LEU A 90  ? 0.1370 0.1439 0.1536 0.0142  -0.0225 0.0515  90  LEU A O   
803  C  CB  . LEU A 90  ? 0.1333 0.1034 0.1412 -0.0109 -0.0173 0.0063  90  LEU A CB  
804  C  CG  . LEU A 90  ? 0.1676 0.1289 0.1351 -0.0275 -0.0194 -0.0031 90  LEU A CG  
805  C  CD1 . LEU A 90  ? 0.1875 0.0961 0.1511 -0.0065 -0.0107 0.0006  90  LEU A CD1 
806  C  CD2 . LEU A 90  ? 0.1692 0.1720 0.1554 -0.0335 -0.0337 -0.0131 90  LEU A CD2 
807  N  N   . ILE A 91  ? 0.1377 0.0926 0.1194 0.0031  -0.0049 0.0137  91  ILE A N   
808  C  CA  . ILE A 91  ? 0.1333 0.0917 0.1221 -0.0091 0.0043  0.0140  91  ILE A CA  
809  C  C   . ILE A 91  ? 0.1237 0.0930 0.1092 0.0059  -0.0120 0.0126  91  ILE A C   
810  O  O   . ILE A 91  ? 0.1643 0.1014 0.1095 -0.0031 -0.0082 0.0181  91  ILE A O   
811  C  CB  . ILE A 91  ? 0.1536 0.1176 0.1198 -0.0307 0.0046  0.0146  91  ILE A CB  
812  C  CG1 . ILE A 91  ? 0.1976 0.1657 0.1437 -0.0627 0.0109  0.0043  91  ILE A CG1 
813  C  CG2 . ILE A 91  ? 0.1703 0.1176 0.1456 -0.0098 -0.0115 0.0175  91  ILE A CG2 
814  C  CD1 . ILE A 91  ? 0.2626 0.2320 0.1667 -0.1045 -0.0104 0.0087  91  ILE A CD1 
815  N  N   . GLN A 92  ? 0.1333 0.0847 0.1122 -0.0003 -0.0148 0.0148  92  GLN A N   
816  C  CA  . GLN A 92  ? 0.1606 0.0908 0.0987 0.0071  -0.0043 0.0208  92  GLN A CA  
817  C  C   . GLN A 92  ? 0.1260 0.0864 0.0957 0.0037  -0.0034 0.0098  92  GLN A C   
818  O  O   . GLN A 92  ? 0.1419 0.0939 0.0876 -0.0026 -0.0054 0.0087  92  GLN A O   
819  C  CB  . GLN A 92  ? 0.1719 0.1120 0.1062 -0.0027 -0.0017 0.0185  92  GLN A CB  
820  C  CG  . GLN A 92  ? 0.1605 0.0948 0.1657 -0.0065 -0.0052 0.0307  92  GLN A CG  
821  C  CD  . GLN A 92  ? 0.1659 0.1154 0.1106 -0.0142 0.0041  0.0131  92  GLN A CD  
822  O  OE1 . GLN A 92  ? 0.1659 0.1093 0.1210 -0.0031 -0.0164 0.0219  92  GLN A OE1 
823  N  NE2 . GLN A 92  ? 0.1448 0.1339 0.1356 -0.0115 -0.0013 0.0062  92  GLN A NE2 
824  N  N   . PHE A 93  ? 0.1412 0.0873 0.0939 0.0013  -0.0054 0.0068  93  PHE A N   
825  C  CA  . PHE A 93  ? 0.1421 0.0798 0.0929 0.0012  -0.0087 0.0098  93  PHE A CA  
826  C  C   . PHE A 93  ? 0.1269 0.0913 0.0966 -0.0063 -0.0183 0.0141  93  PHE A C   
827  O  O   . PHE A 93  ? 0.1701 0.1070 0.0934 0.0113  -0.0010 0.0175  93  PHE A O   
828  C  CB  . PHE A 93  ? 0.1361 0.1049 0.0947 0.0006  -0.0229 0.0103  93  PHE A CB  
829  C  CG  . PHE A 93  ? 0.1474 0.0988 0.1061 -0.0031 -0.0324 0.0063  93  PHE A CG  
830  C  CD1 . PHE A 93  ? 0.1796 0.1115 0.1077 0.0020  -0.0333 -0.0068 93  PHE A CD1 
831  C  CD2 . PHE A 93  ? 0.1509 0.1174 0.1230 0.0027  -0.0401 0.0217  93  PHE A CD2 
832  C  CE1 . PHE A 93  ? 0.1870 0.1097 0.1330 0.0164  -0.0456 -0.0081 93  PHE A CE1 
833  C  CE2 . PHE A 93  ? 0.1770 0.1377 0.1212 0.0115  -0.0516 0.0038  93  PHE A CE2 
834  C  CZ  . PHE A 93  ? 0.1888 0.1190 0.1464 0.0109  -0.0674 -0.0086 93  PHE A CZ  
835  N  N   . HIS A 94  ? 0.1303 0.0829 0.0944 0.0057  -0.0102 0.0074  94  HIS A N   
836  C  CA  . HIS A 94  ? 0.1280 0.0913 0.0996 -0.0031 -0.0096 0.0108  94  HIS A CA  
837  C  C   . HIS A 94  ? 0.1198 0.0916 0.0781 -0.0065 -0.0166 0.0040  94  HIS A C   
838  O  O   . HIS A 94  ? 0.1326 0.0917 0.0864 0.0052  0.0000  0.0104  94  HIS A O   
839  C  CB  . HIS A 94  ? 0.1357 0.1054 0.0908 -0.0037 -0.0065 0.0115  94  HIS A CB  
840  C  CG  . HIS A 94  ? 0.1228 0.0886 0.0895 -0.0092 -0.0006 0.0054  94  HIS A CG  
841  N  ND1 . HIS A 94  ? 0.1339 0.0988 0.0939 -0.0175 -0.0109 0.0115  94  HIS A ND1 
842  C  CD2 . HIS A 94  ? 0.1054 0.1142 0.0806 -0.0115 -0.0098 -0.0023 94  HIS A CD2 
843  C  CE1 . HIS A 94  ? 0.1070 0.0952 0.1095 -0.0073 0.0006  0.0131  94  HIS A CE1 
844  N  NE2 . HIS A 94  ? 0.1054 0.0957 0.0851 -0.0082 -0.0043 0.0104  94  HIS A NE2 
845  N  N   . PHE A 95  ? 0.1322 0.0886 0.0876 -0.0027 0.0015  0.0000  95  PHE A N   
846  C  CA  . PHE A 95  ? 0.1279 0.0895 0.0952 -0.0034 -0.0074 0.0062  95  PHE A CA  
847  C  C   . PHE A 95  ? 0.1150 0.0873 0.1005 -0.0131 -0.0012 -0.0035 95  PHE A C   
848  O  O   . PHE A 95  ? 0.1296 0.1079 0.1052 -0.0048 0.0010  0.0129  95  PHE A O   
849  C  CB  . PHE A 95  ? 0.1323 0.0982 0.0979 -0.0068 -0.0177 -0.0063 95  PHE A CB  
850  C  CG  . PHE A 95  ? 0.1334 0.1014 0.0973 0.0020  -0.0197 -0.0120 95  PHE A CG  
851  C  CD1 . PHE A 95  ? 0.1642 0.1136 0.1027 0.0046  -0.0137 -0.0109 95  PHE A CD1 
852  C  CD2 . PHE A 95  ? 0.1316 0.1095 0.1176 -0.0261 -0.0109 -0.0173 95  PHE A CD2 
853  C  CE1 . PHE A 95  ? 0.1553 0.1330 0.1164 0.0115  -0.0335 -0.0164 95  PHE A CE1 
854  C  CE2 . PHE A 95  ? 0.1473 0.1226 0.1272 -0.0026 -0.0273 -0.0231 95  PHE A CE2 
855  C  CZ  . PHE A 95  ? 0.1515 0.1272 0.1228 0.0027  -0.0296 -0.0241 95  PHE A CZ  
856  N  N   . HIS A 96  ? 0.1176 0.0825 0.0895 -0.0031 -0.0063 -0.0005 96  HIS A N   
857  C  CA  . HIS A 96  ? 0.1095 0.0873 0.1034 -0.0043 -0.0065 -0.0034 96  HIS A CA  
858  C  C   . HIS A 96  ? 0.1093 0.1018 0.0921 -0.0164 0.0000  -0.0020 96  HIS A C   
859  O  O   . HIS A 96  ? 0.1237 0.0856 0.1075 -0.0065 0.0020  -0.0068 96  HIS A O   
860  C  CB  . HIS A 96  ? 0.1176 0.0926 0.1131 -0.0137 -0.0120 -0.0135 96  HIS A CB  
861  C  CG  . HIS A 96  ? 0.0988 0.0908 0.0948 -0.0030 -0.0071 -0.0041 96  HIS A CG  
862  N  ND1 . HIS A 96  ? 0.1059 0.1010 0.1369 -0.0041 -0.0034 -0.0131 96  HIS A ND1 
863  C  CD2 . HIS A 96  ? 0.1174 0.0762 0.0930 -0.0109 -0.0031 -0.0076 96  HIS A CD2 
864  C  CE1 . HIS A 96  ? 0.0992 0.0860 0.1456 -0.0020 0.0049  -0.0153 96  HIS A CE1 
865  N  NE2 . HIS A 96  ? 0.1043 0.0913 0.0966 -0.0054 -0.0049 -0.0027 96  HIS A NE2 
866  N  N   . TRP A 97  ? 0.1137 0.0784 0.0995 -0.0054 0.0000  -0.0031 97  TRP A N   
867  C  CA  . TRP A 97  ? 0.1314 0.0917 0.1086 -0.0054 -0.0026 -0.0082 97  TRP A CA  
868  C  C   . TRP A 97  ? 0.1212 0.0974 0.0886 -0.0093 0.0076  -0.0097 97  TRP A C   
869  O  O   . TRP A 97  ? 0.1208 0.0961 0.1163 -0.0038 0.0142  -0.0057 97  TRP A O   
870  C  CB  . TRP A 97  ? 0.1474 0.1054 0.0873 -0.0164 -0.0027 -0.0070 97  TRP A CB  
871  C  CG  . TRP A 97  ? 0.1387 0.0983 0.0979 -0.0087 -0.0120 -0.0120 97  TRP A CG  
872  C  CD1 . TRP A 97  ? 0.1648 0.1176 0.1061 -0.0146 0.0120  -0.0182 97  TRP A CD1 
873  C  CD2 . TRP A 97  ? 0.1587 0.1084 0.0983 -0.0228 0.0031  -0.0040 97  TRP A CD2 
874  N  NE1 . TRP A 97  ? 0.1826 0.1088 0.1104 -0.0141 0.0283  -0.0114 97  TRP A NE1 
875  C  CE2 . TRP A 97  ? 0.1676 0.1097 0.1027 -0.0165 0.0070  -0.0131 97  TRP A CE2 
876  C  CE3 . TRP A 97  ? 0.1484 0.1070 0.0966 -0.0031 -0.0142 0.0017  97  TRP A CE3 
877  C  CZ2 . TRP A 97  ? 0.1782 0.1298 0.1048 -0.0175 0.0104  0.0015  97  TRP A CZ2 
878  C  CZ3 . TRP A 97  ? 0.1587 0.1210 0.0895 -0.0219 0.0000  -0.0037 97  TRP A CZ3 
879  C  CH2 . TRP A 97  ? 0.1764 0.1138 0.1124 -0.0107 0.0020  -0.0081 97  TRP A CH2 
880  N  N   . GLY A 98  ? 0.1365 0.0864 0.1106 -0.0035 0.0091  -0.0092 98  GLY A N   
881  C  CA  . GLY A 98  ? 0.1325 0.0986 0.1207 0.0109  0.0060  -0.0109 98  GLY A CA  
882  C  C   . GLY A 98  ? 0.1411 0.1079 0.1321 -0.0031 0.0000  -0.0115 98  GLY A C   
883  O  O   . GLY A 98  ? 0.1675 0.1145 0.1312 -0.0065 0.0017  -0.0197 98  GLY A O   
884  N  N   . SER A 99  ? 0.1747 0.1041 0.1412 -0.0031 0.0240  -0.0248 99  SER A N   
885  C  CA  . SER A 99  ? 0.1738 0.1219 0.1491 0.0000  0.0254  -0.0428 99  SER A CA  
886  C  C   . SER A 99  ? 0.2282 0.1106 0.1743 0.0197  0.0136  -0.0496 99  SER A C   
887  O  O   . SER A 99  ? 0.2422 0.1501 0.1817 -0.0141 0.0108  -0.0566 99  SER A O   
888  C  CB  . SER A 99  ? 0.1999 0.1525 0.1764 -0.0023 0.0298  -0.0463 99  SER A CB  
889  O  OG  . SER A 99  ? 0.1580 0.1282 0.2284 0.0187  0.0205  -0.0259 99  SER A OG  
890  N  N   . LEU A 100 ? 0.1660 0.1307 0.1729 -0.0126 0.0238  -0.0324 100 LEU A N   
891  C  CA  . LEU A 100 ? 0.2157 0.0925 0.2231 0.0071  0.0276  -0.0328 100 LEU A CA  
892  C  C   . LEU A 100 ? 0.1692 0.1163 0.1730 -0.0087 0.0026  -0.0160 100 LEU A C   
893  O  O   . LEU A 100 ? 0.1814 0.1093 0.1752 -0.0098 0.0194  -0.0237 100 LEU A O   
894  C  CB  . LEU A 100 ? 0.2850 0.2029 0.3607 0.0828  0.1102  0.0562  100 LEU A CB  
895  C  CG  . LEU A 100 ? 0.2795 0.2536 0.3075 0.0715  0.0344  0.0160  100 LEU A CG  
896  C  CD1 . LEU A 100 ? 0.3905 0.4174 0.4049 0.2635  0.0137  0.0280  100 LEU A CD1 
897  C  CD2 . LEU A 100 ? 0.5684 0.2910 0.4181 0.0410  0.1620  -0.1110 100 LEU A CD2 
898  N  N   . ASP A 101 ? 0.1605 0.1172 0.2159 0.0012  0.0005  -0.0175 101 ASP A N   
899  C  CA  . ASP A 101 ? 0.1634 0.1070 0.1676 -0.0059 -0.0068 0.0015  101 ASP A CA  
900  C  C   . ASP A 101 ? 0.1542 0.1001 0.1974 -0.0024 0.0131  0.0026  101 ASP A C   
901  O  O   . ASP A 101 ? 0.2124 0.1351 0.1973 0.0060  0.0194  0.0076  101 ASP A O   
902  C  CB  . ASP A 101 ? 0.1967 0.1457 0.2020 -0.0293 -0.0388 0.0254  101 ASP A CB  
903  C  CG  . ASP A 101 ? 0.1985 0.1492 0.2381 -0.0438 -0.0309 0.0024  101 ASP A CG  
904  O  OD1 . ASP A 101 ? 0.2082 0.1782 0.2046 -0.0308 -0.0071 -0.0048 101 ASP A OD1 
905  O  OD2 . ASP A 101 ? 0.2989 0.2336 0.2245 -0.1076 -0.0586 0.0174  101 ASP A OD2 
906  N  N   . GLY A 102 ? 0.1703 0.1225 0.1973 -0.0177 -0.0049 0.0221  102 GLY A N   
907  C  CA  . GLY A 102 ? 0.1831 0.1268 0.2034 -0.0208 -0.0062 0.0296  102 GLY A CA  
908  C  C   . GLY A 102 ? 0.1532 0.1330 0.1694 0.0126  0.0054  0.0194  102 GLY A C   
909  O  O   . GLY A 102 ? 0.2078 0.1254 0.1729 0.0000  0.0086  0.0320  102 GLY A O   
910  N  N   . GLN A 103 ? 0.1501 0.1001 0.1624 -0.0115 0.0052  0.0219  103 GLN A N   
911  C  CA  . GLN A 103 ? 0.1439 0.0992 0.1351 0.0043  0.0040  -0.0046 103 GLN A CA  
912  C  C   . GLN A 103 ? 0.1201 0.0942 0.1298 0.0048  0.0151  -0.0026 103 GLN A C   
913  O  O   . GLN A 103 ? 0.1533 0.1061 0.1316 -0.0010 0.0012  -0.0023 103 GLN A O   
914  C  CB  . GLN A 103 ? 0.1641 0.1421 0.1474 0.0287  0.0107  0.0034  103 GLN A CB  
915  C  CG  . GLN A 103 ? 0.1572 0.1490 0.1886 0.0372  0.0401  0.0177  103 GLN A CG  
916  C  CD  . GLN A 103 ? 0.2168 0.1527 0.2192 0.0304  0.0678  0.0590  103 GLN A CD  
917  O  OE1 . GLN A 103 ? 0.2832 0.3212 0.3916 0.1632  0.1686  0.1972  103 GLN A OE1 
918  N  NE2 . GLN A 103 ? 0.1668 0.1603 0.2310 0.0381  0.0529  0.0335  103 GLN A NE2 
919  N  N   . GLY A 104 ? 0.1101 0.0970 0.1149 0.0057  0.0071  0.0000  104 GLY A N   
920  C  CA  . GLY A 104 ? 0.1246 0.0978 0.1119 -0.0060 -0.0027 0.0000  104 GLY A CA  
921  C  C   . GLY A 104 ? 0.1054 0.0895 0.1176 -0.0062 -0.0012 0.0034  104 GLY A C   
922  O  O   . GLY A 104 ? 0.1133 0.1079 0.1254 -0.0071 0.0027  0.0024  104 GLY A O   
923  N  N   . SER A 105 ? 0.1084 0.1032 0.1032 -0.0031 -0.0027 0.0000  105 SER A N   
924  C  CA  . SER A 105 ? 0.1067 0.0944 0.0979 -0.0074 -0.0030 -0.0087 105 SER A CA  
925  C  C   . SER A 105 ? 0.0947 0.0842 0.1124 -0.0019 0.0038  0.0046  105 SER A C   
926  O  O   . SER A 105 ? 0.1172 0.0978 0.1237 0.0006  -0.0104 -0.0073 105 SER A O   
927  C  CB  . SER A 105 ? 0.1061 0.0974 0.1088 -0.0151 0.0017  0.0137  105 SER A CB  
928  O  OG  . SER A 105 ? 0.1147 0.0913 0.1174 -0.0065 0.0054  0.0068  105 SER A OG  
929  N  N   . GLU A 106 ? 0.0996 0.0935 0.1004 -0.0035 -0.0027 -0.0041 106 GLU A N   
930  C  CA  . GLU A 106 ? 0.1086 0.0957 0.0930 -0.0164 -0.0082 0.0062  106 GLU A CA  
931  C  C   . GLU A 106 ? 0.1039 0.0816 0.1095 -0.0098 -0.0109 0.0068  106 GLU A C   
932  O  O   . GLU A 106 ? 0.1068 0.0992 0.1150 0.0010  -0.0010 -0.0030 106 GLU A O   
933  C  CB  . GLU A 106 ? 0.1115 0.0957 0.1017 -0.0087 -0.0010 0.0054  106 GLU A CB  
934  C  CG  . GLU A 106 ? 0.1463 0.0992 0.1203 -0.0220 0.0318  0.0020  106 GLU A CG  
935  C  CD  . GLU A 106 ? 0.1066 0.1104 0.1084 -0.0043 -0.0017 -0.0098 106 GLU A CD  
936  O  OE1 . GLU A 106 ? 0.0960 0.1025 0.1263 -0.0087 -0.0006 -0.0071 106 GLU A OE1 
937  O  OE2 . GLU A 106 ? 0.1041 0.1262 0.1431 -0.0013 0.0141  -0.0096 106 GLU A OE2 
938  N  N   . HIS A 107 ? 0.0920 0.0922 0.0930 0.0013  -0.0006 0.0003  107 HIS A N   
939  C  CA  . HIS A 107 ? 0.0979 0.0860 0.0942 0.0074  -0.0065 0.0020  107 HIS A CA  
940  C  C   . HIS A 107 ? 0.0904 0.0939 0.0938 0.0097  -0.0030 0.0086  107 HIS A C   
941  O  O   . HIS A 107 ? 0.1018 0.0973 0.1030 -0.0054 -0.0043 -0.0005 107 HIS A O   
942  C  CB  . HIS A 107 ? 0.1018 0.0908 0.1129 0.0093  0.0074  0.0027  107 HIS A CB  
943  C  CG  . HIS A 107 ? 0.0819 0.0979 0.1034 0.0135  -0.0034 0.0038  107 HIS A CG  
944  N  ND1 . HIS A 107 ? 0.1067 0.0907 0.1092 0.0063  -0.0048 0.0013  107 HIS A ND1 
945  C  CD2 . HIS A 107 ? 0.0891 0.0790 0.1167 0.0182  -0.0071 -0.0142 107 HIS A CD2 
946  C  CE1 . HIS A 107 ? 0.1147 0.0943 0.1070 0.0093  -0.0118 -0.0054 107 HIS A CE1 
947  N  NE2 . HIS A 107 ? 0.0979 0.0988 0.1049 0.0183  -0.0129 -0.0109 107 HIS A NE2 
948  N  N   . THR A 108 ? 0.1092 0.0961 0.1149 -0.0006 -0.0012 0.0054  108 THR A N   
949  C  CA  . THR A 108 ? 0.1235 0.0819 0.1154 0.0104  0.0098  0.0098  108 THR A CA  
950  C  C   . THR A 108 ? 0.1008 0.0935 0.1068 0.0092  -0.0043 0.0073  108 THR A C   
951  O  O   . THR A 108 ? 0.1131 0.0983 0.1206 0.0057  0.0000  0.0068  108 THR A O   
952  C  CB  . THR A 108 ? 0.1192 0.1133 0.1174 0.0093  -0.0102 -0.0041 108 THR A CB  
953  O  OG1 . THR A 108 ? 0.1421 0.1115 0.1269 0.0176  -0.0186 0.0041  108 THR A OG1 
954  C  CG2 . THR A 108 ? 0.1237 0.1474 0.1226 0.0208  0.0057  -0.0006 108 THR A CG2 
955  N  N   . VAL A 109 ? 0.1185 0.0966 0.1172 -0.0093 0.0000  0.0170  109 VAL A N   
956  C  CA  . VAL A 109 ? 0.1252 0.1101 0.1124 0.0063  0.0087  0.0242  109 VAL A CA  
957  C  C   . VAL A 109 ? 0.1244 0.1041 0.1251 -0.0082 0.0109  0.0155  109 VAL A C   
958  O  O   . VAL A 109 ? 0.1333 0.1009 0.1361 0.0006  0.0104  0.0186  109 VAL A O   
959  C  CB  . VAL A 109 ? 0.1185 0.1129 0.1446 -0.0019 0.0027  0.0172  109 VAL A CB  
960  C  CG1 . VAL A 109 ? 0.1230 0.1440 0.1614 0.0031  0.0230  0.0186  109 VAL A CG1 
961  C  CG2 . VAL A 109 ? 0.1272 0.1323 0.1500 0.0086  -0.0109 0.0241  109 VAL A CG2 
962  N  N   . ASP A 110 ? 0.1501 0.1210 0.1215 0.0142  0.0082  0.0197  110 ASP A N   
963  C  CA  . ASP A 110 ? 0.1852 0.1088 0.1405 0.0192  0.0130  0.0405  110 ASP A CA  
964  C  C   . ASP A 110 ? 0.1950 0.0982 0.1278 0.0164  0.0098  0.0226  110 ASP A C   
965  O  O   . ASP A 110 ? 0.1893 0.1106 0.1439 0.0176  0.0063  0.0272  110 ASP A O   
966  C  CB  . ASP A 110 ? 0.2046 0.1272 0.1675 0.0272  0.0520  0.0447  110 ASP A CB  
967  C  CG  . ASP A 110 ? 0.2099 0.1805 0.1571 0.0076  0.0210  0.0597  110 ASP A CG  
968  O  OD1 . ASP A 110 ? 0.2356 0.1675 0.1791 0.0317  0.0533  0.0428  110 ASP A OD1 
969  O  OD2 . ASP A 110 ? 0.2037 0.2356 0.1976 0.0271  0.0333  0.0333  110 ASP A OD2 
970  N  N   . LYS A 111 ? 0.1509 0.1201 0.1142 0.0153  -0.0070 0.0230  111 LYS A N   
971  C  CA  . LYS A 111 ? 0.1508 0.1172 0.1439 0.0368  0.0006  0.0177  111 LYS A CA  
972  C  C   . LYS A 111 ? 0.1694 0.1041 0.1261 0.0175  -0.0071 0.0164  111 LYS A C   
973  O  O   . LYS A 111 ? 0.1666 0.1511 0.1430 0.0197  0.0126  -0.0013 111 LYS A O   
974  C  CB  . LYS A 111 ? 0.1791 0.1523 0.1519 0.0381  -0.0137 0.0248  111 LYS A CB  
975  C  CG  . LYS A 111 ? 0.2766 0.2000 0.1702 0.0965  -0.0348 0.0194  111 LYS A CG  
976  C  CD  . LYS A 111 ? 0.2460 0.2478 0.2597 0.0531  -0.1075 -0.0636 111 LYS A CD  
977  C  CE  . LYS A 111 ? 0.2953 0.3840 0.2753 0.0869  -0.1010 -0.0776 111 LYS A CE  
978  N  NZ  . LYS A 111 ? 0.3027 0.3316 0.3185 0.0271  -0.1190 0.0340  111 LYS A NZ  
979  N  N   . LYS A 112 ? 0.1429 0.0996 0.1384 0.0120  -0.0054 0.0164  112 LYS A N   
980  C  CA  . LYS A 112 ? 0.1585 0.1255 0.1221 0.0160  0.0102  0.0096  112 LYS A CA  
981  C  C   . LYS A 112 ? 0.1385 0.0943 0.1350 0.0205  -0.0120 0.0174  112 LYS A C   
982  O  O   . LYS A 112 ? 0.1492 0.0935 0.1201 0.0103  -0.0020 0.0065  112 LYS A O   
983  C  CB  . LYS A 112 ? 0.1508 0.1465 0.1404 -0.0109 0.0035  -0.0148 112 LYS A CB  
984  C  CG  . LYS A 112 ? 0.1525 0.1782 0.1641 -0.0320 -0.0043 -0.0263 112 LYS A CG  
985  C  CD  . LYS A 112 ? 0.1632 0.2185 0.2053 -0.0153 -0.0251 0.0165  112 LYS A CD  
986  C  CE  . LYS A 112 ? 0.2186 0.1791 0.2374 -0.0324 -0.0375 -0.0225 112 LYS A CE  
987  N  NZ  . LYS A 112 ? 0.2238 0.1755 0.2222 -0.0006 -0.0445 0.0048  112 LYS A NZ  
988  N  N   A LYS A 113 ? 0.1307 0.1351 0.1162 0.0175  0.0065  0.0104  113 LYS A N   
989  N  N   B LYS A 113 ? 0.1435 0.1068 0.1014 0.0210  -0.0313 0.0015  113 LYS A N   
990  C  CA  A LYS A 113 ? 0.1233 0.1140 0.1334 0.0164  -0.0065 0.0125  113 LYS A CA  
991  C  CA  B LYS A 113 ? 0.1299 0.1061 0.1360 0.0071  -0.0148 0.0080  113 LYS A CA  
992  C  C   A LYS A 113 ? 0.1216 0.0877 0.1296 -0.0031 0.0225  0.0285  113 LYS A C   
993  C  C   B LYS A 113 ? 0.1465 0.0885 0.1050 0.0027  0.0052  0.0098  113 LYS A C   
994  O  O   A LYS A 113 ? 0.1377 0.0803 0.1580 -0.0065 0.0252  0.0236  113 LYS A O   
995  O  O   B LYS A 113 ? 0.1436 0.0807 0.1083 0.0203  0.0051  0.0059  113 LYS A O   
996  C  CB  A LYS A 113 ? 0.1393 0.1260 0.1156 0.0192  -0.0006 -0.0115 113 LYS A CB  
997  C  CB  B LYS A 113 ? 0.1482 0.1474 0.1212 0.0107  -0.0043 0.0041  113 LYS A CB  
998  C  CG  A LYS A 113 ? 0.1067 0.1254 0.1446 0.0049  -0.0051 0.0130  113 LYS A CG  
999  C  CG  B LYS A 113 ? 0.1386 0.1616 0.1212 0.0175  -0.0082 -0.0346 113 LYS A CG  
1000 C  CD  A LYS A 113 ? 0.1325 0.1632 0.1676 0.0237  0.0082  -0.0263 113 LYS A CD  
1001 C  CD  B LYS A 113 ? 0.1201 0.2037 0.1290 0.0274  0.0006  0.0130  113 LYS A CD  
1002 C  CE  A LYS A 113 ? 0.1552 0.1413 0.2228 0.0160  -0.0113 -0.0285 113 LYS A CE  
1003 C  CE  B LYS A 113 ? 0.1083 0.3201 0.1854 0.0160  -0.0126 -0.0252 113 LYS A CE  
1004 N  NZ  A LYS A 113 ? 0.1061 0.2863 0.2159 0.0441  -0.0531 -0.0335 113 LYS A NZ  
1005 N  NZ  B LYS A 113 ? 0.2046 0.2669 0.3186 0.0538  0.0601  0.0034  113 LYS A NZ  
1006 N  N   . TYR A 114 ? 0.1252 0.0920 0.1280 -0.0040 -0.0046 0.0082  114 TYR A N   
1007 C  CA  . TYR A 114 ? 0.1158 0.1025 0.1286 -0.0024 -0.0164 0.0054  114 TYR A CA  
1008 C  C   . TYR A 114 ? 0.1162 0.0790 0.1259 -0.0035 -0.0043 0.0037  114 TYR A C   
1009 O  O   . TYR A 114 ? 0.1101 0.1027 0.1321 -0.0046 0.0024  -0.0010 114 TYR A O   
1010 C  CB  . TYR A 114 ? 0.1140 0.0996 0.1298 -0.0054 0.0035  0.0074  114 TYR A CB  
1011 C  CG  . TYR A 114 ? 0.1203 0.0917 0.1237 0.0041  -0.0109 0.0142  114 TYR A CG  
1012 C  CD1 . TYR A 114 ? 0.1569 0.1045 0.1449 0.0129  0.0043  0.0137  114 TYR A CD1 
1013 C  CD2 . TYR A 114 ? 0.1133 0.1140 0.1668 0.0000  0.0000  0.0227  114 TYR A CD2 
1014 C  CE1 . TYR A 114 ? 0.2125 0.1412 0.1254 0.0394  0.0120  0.0115  114 TYR A CE1 
1015 C  CE2 . TYR A 114 ? 0.1507 0.1386 0.1958 -0.0015 0.0324  -0.0087 114 TYR A CE2 
1016 C  CZ  . TYR A 114 ? 0.1718 0.1403 0.1972 -0.0041 0.0458  0.0065  114 TYR A CZ  
1017 O  OH  . TYR A 114 ? 0.2465 0.2178 0.2284 0.0208  0.1070  0.0155  114 TYR A OH  
1018 N  N   . ALA A 115 ? 0.1280 0.0864 0.1254 -0.0166 -0.0170 -0.0076 115 ALA A N   
1019 C  CA  . ALA A 115 ? 0.1474 0.0794 0.1201 -0.0027 -0.0065 -0.0052 115 ALA A CA  
1020 C  C   . ALA A 115 ? 0.1395 0.0847 0.1106 -0.0081 -0.0087 -0.0041 115 ALA A C   
1021 O  O   . ALA A 115 ? 0.1277 0.0965 0.1279 -0.0081 0.0071  -0.0052 115 ALA A O   
1022 C  CB  . ALA A 115 ? 0.1515 0.1043 0.1435 -0.0263 -0.0197 -0.0104 115 ALA A CB  
1023 N  N   . ALA A 116 ? 0.1253 0.0772 0.1190 -0.0104 0.0019  0.0013  116 ALA A N   
1024 C  CA  . ALA A 116 ? 0.1199 0.0944 0.1111 -0.0087 0.0031  -0.0046 116 ALA A CA  
1025 C  C   . ALA A 116 ? 0.1124 0.0908 0.0952 -0.0049 -0.0082 0.0046  116 ALA A C   
1026 O  O   . ALA A 116 ? 0.1142 0.0974 0.0995 -0.0103 0.0031  0.0046  116 ALA A O   
1027 C  CB  . ALA A 116 ? 0.1299 0.1165 0.1023 -0.0098 -0.0006 0.0020  116 ALA A CB  
1028 N  N   . GLU A 117 ? 0.1201 0.0753 0.1005 0.0027  0.0000  -0.0005 117 GLU A N   
1029 C  CA  . GLU A 117 ? 0.1146 0.0803 0.0908 -0.0041 -0.0017 0.0026  117 GLU A CA  
1030 C  C   . GLU A 117 ? 0.1124 0.0860 0.0885 0.0013  0.0013  0.0048  117 GLU A C   
1031 O  O   . GLU A 117 ? 0.1158 0.1049 0.1216 0.0087  0.0092  0.0228  117 GLU A O   
1032 C  CB  . GLU A 117 ? 0.1263 0.0957 0.0970 0.0043  -0.0104 -0.0024 117 GLU A CB  
1033 C  CG  . GLU A 117 ? 0.1279 0.1070 0.0966 0.0006  -0.0205 0.0006  117 GLU A CG  
1034 C  CD  . GLU A 117 ? 0.1068 0.0869 0.1032 -0.0097 0.0051  0.0043  117 GLU A CD  
1035 O  OE1 . GLU A 117 ? 0.1189 0.1131 0.1194 0.0086  -0.0076 0.0043  117 GLU A OE1 
1036 O  OE2 . GLU A 117 ? 0.1264 0.1074 0.1034 -0.0087 -0.0131 0.0063  117 GLU A OE2 
1037 N  N   . LEU A 118 ? 0.1050 0.0878 0.0930 -0.0010 -0.0104 0.0003  118 LEU A N   
1038 C  CA  . LEU A 118 ? 0.1025 0.0788 0.0930 0.0006  -0.0148 0.0048  118 LEU A CA  
1039 C  C   . LEU A 118 ? 0.1079 0.0754 0.0930 0.0010  -0.0087 0.0031  118 LEU A C   
1040 O  O   . LEU A 118 ? 0.1036 0.0847 0.0890 -0.0013 -0.0031 -0.0005 118 LEU A O   
1041 C  CB  . LEU A 118 ? 0.1129 0.0929 0.1106 -0.0012 -0.0205 0.0006  118 LEU A CB  
1042 C  CG  . LEU A 118 ? 0.1031 0.1097 0.1156 0.0103  -0.0199 0.0140  118 LEU A CG  
1043 C  CD1 . LEU A 118 ? 0.1377 0.1059 0.1122 -0.0038 -0.0322 0.0171  118 LEU A CD1 
1044 C  CD2 . LEU A 118 ? 0.1268 0.1423 0.1410 -0.0104 -0.0450 0.0114  118 LEU A CD2 
1045 N  N   . HIS A 119 ? 0.1070 0.0724 0.0812 -0.0071 -0.0120 0.0030  119 HIS A N   
1046 C  CA  . HIS A 119 ? 0.0986 0.0785 0.0793 -0.0046 -0.0085 0.0063  119 HIS A CA  
1047 C  C   . HIS A 119 ? 0.1043 0.0794 0.0847 -0.0115 -0.0136 0.0076  119 HIS A C   
1048 O  O   . HIS A 119 ? 0.1237 0.0864 0.0948 -0.0010 -0.0109 0.0076  119 HIS A O   
1049 C  CB  . HIS A 119 ? 0.0934 0.0899 0.0942 0.0074  -0.0063 0.0074  119 HIS A CB  
1050 C  CG  . HIS A 119 ? 0.0878 0.0974 0.0886 -0.0070 0.0054  -0.0005 119 HIS A CG  
1051 N  ND1 . HIS A 119 ? 0.0886 0.0891 0.0768 -0.0037 0.0046  0.0063  119 HIS A ND1 
1052 C  CD2 . HIS A 119 ? 0.0922 0.0878 0.0904 -0.0027 -0.0082 0.0031  119 HIS A CD2 
1053 C  CE1 . HIS A 119 ? 0.1031 0.1010 0.0899 -0.0049 -0.0041 -0.0076 119 HIS A CE1 
1054 N  NE2 . HIS A 119 ? 0.0851 0.0944 0.0966 -0.0035 -0.0087 0.0115  119 HIS A NE2 
1055 N  N   . LEU A 120 ? 0.0944 0.0763 0.1000 0.0065  -0.0120 0.0043  120 LEU A N   
1056 C  CA  . LEU A 120 ? 0.1088 0.0832 0.1079 0.0041  -0.0210 0.0093  120 LEU A CA  
1057 C  C   . LEU A 120 ? 0.0922 0.0776 0.0957 0.0136  -0.0037 0.0130  120 LEU A C   
1058 O  O   . LEU A 120 ? 0.0995 0.0842 0.0966 -0.0057 -0.0093 0.0065  120 LEU A O   
1059 C  CB  . LEU A 120 ? 0.0964 0.0917 0.1296 -0.0038 -0.0261 -0.0017 120 LEU A CB  
1060 C  CG  . LEU A 120 ? 0.1203 0.1115 0.1317 -0.0197 -0.0285 0.0068  120 LEU A CG  
1061 C  CD1 . LEU A 120 ? 0.2399 0.1474 0.1727 -0.1032 -0.0068 -0.0187 120 LEU A CD1 
1062 C  CD2 . LEU A 120 ? 0.1430 0.1844 0.1375 0.0098  -0.0432 -0.0148 120 LEU A CD2 
1063 N  N   . VAL A 121 ? 0.1014 0.0856 0.1001 -0.0076 -0.0068 0.0131  121 VAL A N   
1064 C  CA  . VAL A 121 ? 0.1005 0.0842 0.1059 -0.0040 -0.0131 0.0120  121 VAL A CA  
1065 C  C   . VAL A 121 ? 0.0987 0.0851 0.0992 -0.0153 -0.0017 0.0076  121 VAL A C   
1066 O  O   . VAL A 121 ? 0.1219 0.0891 0.1084 0.0071  -0.0131 0.0074  121 VAL A O   
1067 C  CB  . VAL A 121 ? 0.1076 0.0921 0.1145 -0.0057 -0.0026 0.0043  121 VAL A CB  
1068 C  CG1 . VAL A 121 ? 0.1351 0.1023 0.1219 -0.0219 0.0027  -0.0005 121 VAL A CG1 
1069 C  CG2 . VAL A 121 ? 0.1308 0.1001 0.1059 0.0177  0.0043  0.0129  121 VAL A CG2 
1070 N  N   . HIS A 122 ? 0.0988 0.0793 0.1124 -0.0071 -0.0120 0.0041  122 HIS A N   
1071 C  CA  . HIS A 122 ? 0.1113 0.0737 0.1145 0.0006  -0.0082 0.0040  122 HIS A CA  
1072 C  C   . HIS A 122 ? 0.1010 0.0860 0.1192 0.0065  -0.0071 0.0051  122 HIS A C   
1073 O  O   . HIS A 122 ? 0.1307 0.0868 0.1233 -0.0085 -0.0240 0.0129  122 HIS A O   
1074 C  CB  . HIS A 122 ? 0.1221 0.0741 0.1260 0.0017  0.0027  0.0031  122 HIS A CB  
1075 C  CG  . HIS A 122 ? 0.1014 0.0864 0.1158 0.0074  -0.0024 0.0054  122 HIS A CG  
1076 N  ND1 . HIS A 122 ? 0.1043 0.0916 0.1263 -0.0013 0.0046  0.0065  122 HIS A ND1 
1077 C  CD2 . HIS A 122 ? 0.1079 0.1212 0.1333 -0.0082 -0.0057 0.0052  122 HIS A CD2 
1078 C  CE1 . HIS A 122 ? 0.0996 0.1138 0.1333 -0.0052 -0.0034 0.0024  122 HIS A CE1 
1079 N  NE2 . HIS A 122 ? 0.1005 0.1198 0.1395 -0.0093 -0.0092 0.0052  122 HIS A NE2 
1080 N  N   . TRP A 123 ? 0.1027 0.0768 0.1246 0.0031  -0.0098 -0.0027 123 TRP A N   
1081 C  CA  . TRP A 123 ? 0.1194 0.0829 0.1136 0.0000  -0.0098 -0.0031 123 TRP A CA  
1082 C  C   . TRP A 123 ? 0.1113 0.0766 0.1324 -0.0027 -0.0076 0.0049  123 TRP A C   
1083 O  O   . TRP A 123 ? 0.1118 0.0842 0.1571 0.0046  -0.0151 -0.0019 123 TRP A O   
1084 C  CB  . TRP A 123 ? 0.1342 0.1307 0.1360 -0.0329 0.0015  0.0013  123 TRP A CB  
1085 C  CG  . TRP A 123 ? 0.1525 0.1070 0.1412 -0.0230 0.0063  0.0124  123 TRP A CG  
1086 C  CD1 . TRP A 123 ? 0.1692 0.1115 0.1332 -0.0217 -0.0208 0.0087  123 TRP A CD1 
1087 C  CD2 . TRP A 123 ? 0.1898 0.0842 0.1422 -0.0265 -0.0019 0.0074  123 TRP A CD2 
1088 N  NE1 . TRP A 123 ? 0.2204 0.0882 0.1536 -0.0203 -0.0250 0.0017  123 TRP A NE1 
1089 C  CE2 . TRP A 123 ? 0.1920 0.0982 0.1578 -0.0269 -0.0109 0.0181  123 TRP A CE2 
1090 C  CE3 . TRP A 123 ? 0.2456 0.0798 0.1659 -0.0447 0.0097  0.0010  123 TRP A CE3 
1091 C  CZ2 . TRP A 123 ? 0.2518 0.0964 0.1791 -0.0219 -0.0051 0.0109  123 TRP A CZ2 
1092 C  CZ3 . TRP A 123 ? 0.3043 0.0789 0.1639 -0.0432 0.0052  0.0043  123 TRP A CZ3 
1093 C  CH2 . TRP A 123 ? 0.3276 0.0966 0.1844 -0.0074 0.0124  0.0274  123 TRP A CH2 
1094 N  N   . ASN A 124 ? 0.1254 0.0864 0.1280 0.0046  -0.0126 -0.0082 124 ASN A N   
1095 C  CA  . ASN A 124 ? 0.1439 0.0856 0.1421 0.0204  -0.0109 -0.0098 124 ASN A CA  
1096 C  C   . ASN A 124 ? 0.1147 0.0921 0.1466 0.0109  -0.0013 -0.0217 124 ASN A C   
1097 O  O   . ASN A 124 ? 0.1360 0.1005 0.1360 0.0109  -0.0070 -0.0010 124 ASN A O   
1098 C  CB  . ASN A 124 ? 0.1458 0.1010 0.1321 0.0153  0.0010  -0.0046 124 ASN A CB  
1099 C  CG  . ASN A 124 ? 0.1472 0.1001 0.1464 0.0000  0.0027  -0.0031 124 ASN A CG  
1100 O  OD1 . ASN A 124 ? 0.1563 0.1068 0.1747 0.0195  0.0082  -0.0141 124 ASN A OD1 
1101 N  ND2 . ASN A 124 ? 0.2099 0.1263 0.1419 0.0091  -0.0031 -0.0186 124 ASN A ND2 
1102 N  N   . THR A 125 ? 0.1342 0.0900 0.1756 0.0239  -0.0230 -0.0148 125 THR A N   
1103 C  CA  . THR A 125 ? 0.1571 0.1059 0.1861 0.0023  -0.0283 -0.0012 125 THR A CA  
1104 C  C   . THR A 125 ? 0.1634 0.0886 0.1818 0.0253  -0.0024 0.0035  125 THR A C   
1105 O  O   . THR A 125 ? 0.1994 0.1088 0.1946 0.0263  -0.0324 0.0051  125 THR A O   
1106 C  CB  . THR A 125 ? 0.1710 0.1456 0.2460 0.0193  -0.0666 0.0181  125 THR A CB  
1107 O  OG1 . THR A 125 ? 0.2048 0.1835 0.3560 0.0728  0.0103  0.0082  125 THR A OG1 
1108 C  CG2 . THR A 125 ? 0.2202 0.1484 0.2856 -0.0065 -0.1001 0.0155  125 THR A CG2 
1109 N  N   A LYS A 126 ? 0.1717 0.0706 0.1307 -0.0051 -0.0059 -0.0040 127 LYS A N   
1110 N  N   B LYS A 126 ? 0.1789 0.1052 0.1221 0.0370  0.0093  0.0034  127 LYS A N   
1111 C  CA  A LYS A 126 ? 0.1842 0.1237 0.1569 -0.0141 -0.0209 -0.0425 127 LYS A CA  
1112 C  CA  B LYS A 126 ? 0.1931 0.1001 0.1509 0.0131  0.0219  0.0057  127 LYS A CA  
1113 C  C   A LYS A 126 ? 0.2002 0.0794 0.1579 -0.0027 -0.0082 -0.0170 127 LYS A C   
1114 C  C   B LYS A 126 ? 0.1920 0.0768 0.1861 0.0259  -0.0081 0.0015  127 LYS A C   
1115 O  O   A LYS A 126 ? 0.1700 0.0886 0.1155 -0.0076 -0.0136 0.0019  127 LYS A O   
1116 O  O   B LYS A 126 ? 0.2090 0.0920 0.2008 0.0154  -0.0489 -0.0276 127 LYS A O   
1117 C  CB  A LYS A 126 ? 0.2081 0.1131 0.1492 0.0038  -0.0487 -0.0340 127 LYS A CB  
1118 C  CB  B LYS A 126 ? 0.1632 0.1379 0.1754 -0.0186 -0.0241 -0.0098 127 LYS A CB  
1119 C  CG  A LYS A 126 ? 0.1482 0.1167 0.1673 0.0140  -0.0063 -0.0408 127 LYS A CG  
1120 C  CG  B LYS A 126 ? 0.1826 0.1744 0.1606 0.0476  0.0419  0.0153  127 LYS A CG  
1121 C  CD  A LYS A 126 ? 0.1632 0.2644 0.1948 0.0696  0.0071  -0.0540 127 LYS A CD  
1122 C  CD  B LYS A 126 ? 0.1791 0.1860 0.1639 0.0115  -0.0038 0.0104  127 LYS A CD  
1123 C  CE  A LYS A 126 ? 0.1581 0.2465 0.1993 -0.0076 -0.0286 0.0098  127 LYS A CE  
1124 C  CE  B LYS A 126 ? 0.4864 0.1861 0.1018 0.0333  0.0498  0.0027  127 LYS A CE  
1125 N  NZ  A LYS A 126 ? 0.2824 0.2612 0.1798 0.0758  0.0247  -0.0151 127 LYS A NZ  
1126 N  NZ  B LYS A 126 ? 0.4708 0.4885 0.4544 0.1594  0.0631  0.0331  127 LYS A NZ  
1127 N  N   . TYR A 127 ? 0.1807 0.0899 0.1379 -0.0020 -0.0063 -0.0013 128 TYR A N   
1128 C  CA  . TYR A 127 ? 0.1782 0.0935 0.1449 0.0006  -0.0195 0.0049  128 TYR A CA  
1129 C  C   . TYR A 127 ? 0.1683 0.1032 0.1453 -0.0093 0.0052  -0.0136 128 TYR A C   
1130 O  O   . TYR A 127 ? 0.1799 0.1095 0.1571 -0.0060 -0.0027 -0.0065 128 TYR A O   
1131 C  CB  . TYR A 127 ? 0.1870 0.1149 0.1518 0.0013  -0.0060 0.0109  128 TYR A CB  
1132 C  CG  . TYR A 127 ? 0.1718 0.1102 0.1606 0.0087  -0.0219 -0.0087 128 TYR A CG  
1133 C  CD1 . TYR A 127 ? 0.1693 0.1201 0.1597 0.0027  -0.0275 -0.0104 128 TYR A CD1 
1134 C  CD2 . TYR A 127 ? 0.1492 0.1172 0.1439 0.0087  0.0096  0.0012  128 TYR A CD2 
1135 C  CE1 . TYR A 127 ? 0.1941 0.1263 0.1439 -0.0013 -0.0186 -0.0215 128 TYR A CE1 
1136 C  CE2 . TYR A 127 ? 0.1464 0.1289 0.1447 -0.0010 0.0006  -0.0153 128 TYR A CE2 
1137 C  CZ  . TYR A 127 ? 0.1761 0.1492 0.1412 0.0207  -0.0153 -0.0096 128 TYR A CZ  
1138 O  OH  . TYR A 127 ? 0.2404 0.1409 0.1324 0.0153  -0.0230 -0.0283 128 TYR A OH  
1139 N  N   . GLY A 128 ? 0.1810 0.0986 0.1453 -0.0073 -0.0206 0.0043  129 GLY A N   
1140 C  CA  . GLY A 128 ? 0.2035 0.1142 0.1590 -0.0043 0.0031  0.0000  129 GLY A CA  
1141 C  C   . GLY A 128 ? 0.2240 0.1079 0.1384 -0.0052 -0.0177 0.0210  129 GLY A C   
1142 O  O   . GLY A 128 ? 0.2741 0.1163 0.1465 0.0098  -0.0240 0.0124  129 GLY A O   
1143 N  N   . ASP A 129 ? 0.2565 0.1088 0.1289 0.0166  -0.0174 -0.0006 130 ASP A N   
1144 C  CA  . ASP A 129 ? 0.2885 0.1190 0.1246 0.0236  -0.0038 0.0010  130 ASP A CA  
1145 C  C   . ASP A 129 ? 0.2648 0.1217 0.1263 0.0214  -0.0031 0.0087  130 ASP A C   
1146 O  O   . ASP A 129 ? 0.2833 0.1150 0.1358 0.0197  -0.0152 0.0052  130 ASP A O   
1147 C  CB  . ASP A 129 ? 0.3262 0.1773 0.1562 0.0186  0.0412  0.0065  130 ASP A CB  
1148 C  CG  . ASP A 129 ? 0.2888 0.1237 0.1473 0.0098  0.0362  0.0315  130 ASP A CG  
1149 O  OD1 . ASP A 129 ? 0.3650 0.2107 0.2766 -0.0643 -0.0895 0.0176  130 ASP A OD1 
1150 O  OD2 . ASP A 129 ? 0.3402 0.2037 0.2558 -0.0151 0.0878  0.0136  130 ASP A OD2 
1151 N  N   . PHE A 130 ? 0.2558 0.1079 0.1230 0.0104  0.0076  -0.0006 131 PHE A N   
1152 C  CA  . PHE A 130 ? 0.2310 0.1034 0.1298 0.0013  0.0063  -0.0120 131 PHE A CA  
1153 C  C   . PHE A 130 ? 0.2064 0.1088 0.1379 -0.0017 0.0333  -0.0093 131 PHE A C   
1154 O  O   . PHE A 130 ? 0.2096 0.1324 0.1289 -0.0155 0.0104  0.0087  131 PHE A O   
1155 C  CB  . PHE A 130 ? 0.2180 0.1230 0.1235 0.0048  -0.0027 -0.0208 131 PHE A CB  
1156 C  CG  . PHE A 130 ? 0.2122 0.1070 0.1352 0.0154  0.0346  -0.0265 131 PHE A CG  
1157 C  CD1 . PHE A 130 ? 0.1686 0.1210 0.1404 -0.0098 -0.0109 0.0027  131 PHE A CD1 
1158 C  CD2 . PHE A 130 ? 0.2888 0.1622 0.2799 -0.0142 0.1177  -0.0439 131 PHE A CD2 
1159 C  CE1 . PHE A 130 ? 0.2020 0.1316 0.1580 -0.0241 -0.0020 -0.0194 131 PHE A CE1 
1160 C  CE2 . PHE A 130 ? 0.2533 0.2004 0.3553 0.0197  0.0724  -0.0104 131 PHE A CE2 
1161 C  CZ  . PHE A 130 ? 0.2673 0.1527 0.2917 0.0465  0.0243  -0.0231 131 PHE A CZ  
1162 N  N   . GLY A 131 ? 0.2478 0.1383 0.1499 -0.0307 0.0540  0.0063  132 GLY A N   
1163 C  CA  . GLY A 131 ? 0.2465 0.1699 0.1704 -0.0324 0.0856  0.0166  132 GLY A CA  
1164 C  C   . GLY A 131 ? 0.2011 0.1676 0.1729 -0.0403 0.0474  0.0091  132 GLY A C   
1165 O  O   . GLY A 131 ? 0.1938 0.1691 0.2483 -0.0295 0.0555  -0.0230 132 GLY A O   
1166 N  N   A LYS A 132 ? 0.2009 0.1282 0.1766 -0.0368 0.0313  0.0000  133 LYS A N   
1167 N  N   B LYS A 132 ? 0.2045 0.1307 0.1854 -0.0305 0.0408  0.0098  133 LYS A N   
1168 C  CA  A LYS A 132 ? 0.1747 0.1212 0.1606 -0.0260 -0.0098 0.0119  133 LYS A CA  
1169 C  CA  B LYS A 132 ? 0.2249 0.0834 0.1842 -0.0162 0.0340  0.0024  133 LYS A CA  
1170 C  C   A LYS A 132 ? 0.1676 0.1138 0.1462 -0.0364 0.0065  -0.0230 133 LYS A C   
1171 C  C   B LYS A 132 ? 0.1541 0.1142 0.1703 -0.0242 0.0131  0.0054  133 LYS A C   
1172 O  O   A LYS A 132 ? 0.1181 0.1030 0.1480 -0.0186 0.0076  -0.0131 133 LYS A O   
1173 O  O   B LYS A 132 ? 0.1719 0.1287 0.1932 -0.0208 -0.0147 -0.0315 133 LYS A O   
1174 C  CB  A LYS A 132 ? 0.2124 0.1018 0.1764 -0.0399 -0.0307 0.0006  133 LYS A CB  
1175 C  CB  B LYS A 132 ? 0.1518 0.1419 0.2108 0.0074  0.0041  0.0241  133 LYS A CB  
1176 C  CG  A LYS A 132 ? 0.1781 0.1142 0.2153 -0.0102 0.0126  0.0109  133 LYS A CG  
1177 C  CG  B LYS A 132 ? 0.2270 0.2435 0.2605 -0.0395 0.0275  0.0388  133 LYS A CG  
1178 C  CD  A LYS A 132 ? 0.1533 0.1203 0.3855 -0.0198 0.0091  0.0688  133 LYS A CD  
1179 C  CD  B LYS A 132 ? 0.3208 0.3262 0.4419 0.0869  -0.0926 -0.1421 133 LYS A CD  
1180 C  CE  A LYS A 132 ? 0.1773 0.1664 0.3682 -0.0524 -0.0397 0.0388  133 LYS A CE  
1181 C  CE  B LYS A 132 ? 0.2201 0.2633 0.3154 0.0439  -0.0104 -0.0395 133 LYS A CE  
1182 N  NZ  A LYS A 132 ? 0.3039 0.2410 0.4106 0.0015  -0.0872 -0.0979 133 LYS A NZ  
1183 N  NZ  B LYS A 132 ? 0.2231 0.1562 0.2238 0.0186  -0.0636 -0.0030 133 LYS A NZ  
1184 N  N   . ALA A 133 ? 0.1641 0.1185 0.1365 -0.0449 0.0115  -0.0107 134 ALA A N   
1185 C  CA  . ALA A 133 ? 0.1431 0.1286 0.1272 -0.0252 -0.0006 -0.0013 134 ALA A CA  
1186 C  C   . ALA A 133 ? 0.1369 0.1447 0.1018 -0.0401 0.0013  -0.0076 134 ALA A C   
1187 O  O   . ALA A 133 ? 0.1210 0.1508 0.1190 -0.0164 -0.0012 -0.0086 134 ALA A O   
1188 C  CB  . ALA A 133 ? 0.1430 0.1176 0.1254 -0.0350 -0.0091 0.0013  134 ALA A CB  
1189 N  N   . VAL A 134 ? 0.1568 0.1189 0.1412 -0.0307 0.0298  -0.0035 135 VAL A N   
1190 C  CA  . VAL A 134 ? 0.1818 0.1176 0.1324 -0.0219 0.0159  0.0003  135 VAL A CA  
1191 C  C   . VAL A 134 ? 0.1488 0.1377 0.1313 -0.0104 0.0291  -0.0037 135 VAL A C   
1192 O  O   . VAL A 134 ? 0.1545 0.1412 0.1806 -0.0031 0.0381  0.0063  135 VAL A O   
1193 C  CB  . VAL A 134 ? 0.2030 0.1351 0.1877 -0.0375 0.0593  -0.0162 135 VAL A CB  
1194 C  CG1 . VAL A 134 ? 0.2327 0.1666 0.1894 -0.0592 0.0416  -0.0304 135 VAL A CG1 
1195 C  CG2 . VAL A 134 ? 0.2002 0.1368 0.1693 -0.0187 0.0507  -0.0109 135 VAL A CG2 
1196 N  N   . GLN A 135 ? 0.1474 0.1307 0.1497 -0.0306 0.0295  -0.0102 136 GLN A N   
1197 C  CA  . GLN A 135 ? 0.1386 0.1445 0.1897 -0.0353 0.0027  -0.0252 136 GLN A CA  
1198 C  C   . GLN A 135 ? 0.1404 0.1342 0.1640 -0.0285 -0.0107 -0.0251 136 GLN A C   
1199 O  O   . GLN A 135 ? 0.1429 0.2055 0.1948 -0.0383 -0.0141 -0.0355 136 GLN A O   
1200 C  CB  . GLN A 135 ? 0.1780 0.1677 0.1976 -0.0544 0.0097  0.0006  136 GLN A CB  
1201 C  CG  . GLN A 135 ? 0.2134 0.1949 0.2240 -0.0516 0.0461  0.0315  136 GLN A CG  
1202 C  CD  . GLN A 135 ? 0.2266 0.2850 0.2924 -0.0842 0.0219  0.0593  136 GLN A CD  
1203 O  OE1 . GLN A 135 ? 0.2680 0.3747 0.3797 -0.1254 -0.0131 0.0443  136 GLN A OE1 
1204 N  NE2 . GLN A 135 ? 0.2354 0.2407 0.3348 -0.0249 0.0384  0.0728  136 GLN A NE2 
1205 N  N   . GLN A 136 ? 0.1217 0.1392 0.1351 -0.0192 0.0076  -0.0175 137 GLN A N   
1206 C  CA  . GLN A 136 ? 0.1458 0.1352 0.1192 -0.0160 -0.0197 -0.0164 137 GLN A CA  
1207 C  C   . GLN A 136 ? 0.1208 0.1544 0.1254 0.0068  -0.0082 -0.0263 137 GLN A C   
1208 O  O   . GLN A 136 ? 0.1594 0.1244 0.1190 -0.0031 -0.0063 -0.0098 137 GLN A O   
1209 C  CB  . GLN A 136 ? 0.1506 0.1185 0.1641 -0.0038 -0.0219 -0.0098 137 GLN A CB  
1210 C  CG  . GLN A 136 ? 0.2222 0.1660 0.1572 0.0181  0.0137  -0.0163 137 GLN A CG  
1211 C  CD  . GLN A 136 ? 0.2004 0.1641 0.3097 -0.0153 0.0035  0.0206  137 GLN A CD  
1212 O  OE1 . GLN A 136 ? 0.2368 0.1993 0.2996 0.0019  -0.0219 -0.1036 137 GLN A OE1 
1213 N  NE2 . GLN A 136 ? 0.2935 0.2716 0.5357 -0.0566 0.0096  0.1669  137 GLN A NE2 
1214 N  N   A PRO A 137 ? 0.1402 0.1921 0.1162 0.0307  -0.0197 -0.0216 138 PRO A N   
1215 N  N   B PRO A 137 ? 0.1158 0.1383 0.1273 -0.0054 -0.0207 -0.0203 138 PRO A N   
1216 C  CA  A PRO A 137 ? 0.1463 0.1781 0.1027 0.0439  -0.0074 -0.0074 138 PRO A CA  
1217 C  CA  B PRO A 137 ? 0.1509 0.1154 0.1077 -0.0041 -0.0160 0.0031  138 PRO A CA  
1218 C  C   A PRO A 137 ? 0.1717 0.1708 0.0917 0.0291  -0.0274 -0.0196 138 PRO A C   
1219 C  C   B PRO A 137 ? 0.1571 0.1254 0.1120 -0.0017 0.0197  0.0172  138 PRO A C   
1220 O  O   A PRO A 137 ? 0.2105 0.1832 0.1280 0.0102  -0.0296 0.0054  138 PRO A O   
1221 O  O   B PRO A 137 ? 0.1543 0.1246 0.1726 0.0097  -0.0194 0.0046  138 PRO A O   
1222 C  CB  A PRO A 137 ? 0.1650 0.2433 0.0983 -0.0076 -0.0568 0.0096  138 PRO A CB  
1223 C  CB  B PRO A 137 ? 0.1993 0.1194 0.1185 0.0274  0.0059  -0.0307 138 PRO A CB  
1224 C  CG  A PRO A 137 ? 0.2410 0.2159 0.1238 0.0776  -0.0186 -0.0487 138 PRO A CG  
1225 C  CG  B PRO A 137 ? 0.2177 0.1904 0.1115 0.0214  -0.0430 -0.0170 138 PRO A CG  
1226 C  CD  A PRO A 137 ? 0.1456 0.2379 0.1111 0.0006  -0.0502 -0.0403 138 PRO A CD  
1227 C  CD  B PRO A 137 ? 0.1536 0.1421 0.1070 -0.0048 -0.0151 -0.0303 138 PRO A CD  
1228 N  N   . ASP A 138 ? 0.1273 0.1492 0.1119 0.0131  -0.0060 0.0043  139 ASP A N   
1229 C  CA  . ASP A 138 ? 0.1289 0.1580 0.1158 0.0104  -0.0035 0.0027  139 ASP A CA  
1230 C  C   . ASP A 138 ? 0.1167 0.1136 0.1210 -0.0024 -0.0040 -0.0087 139 ASP A C   
1231 O  O   . ASP A 138 ? 0.1333 0.1263 0.1352 0.0031  0.0081  0.0000  139 ASP A O   
1232 C  CB  . ASP A 138 ? 0.1897 0.1641 0.1230 0.0065  0.0263  -0.0063 139 ASP A CB  
1233 C  CG  . ASP A 138 ? 0.1481 0.1710 0.1348 0.0206  0.0027  -0.0248 139 ASP A CG  
1234 O  OD1 . ASP A 138 ? 0.1895 0.1423 0.1500 0.0082  -0.0024 -0.0339 139 ASP A OD1 
1235 O  OD2 . ASP A 138 ? 0.2011 0.1946 0.1774 0.0293  0.0287  -0.0460 139 ASP A OD2 
1236 N  N   . GLY A 139 ? 0.1167 0.1062 0.1097 -0.0027 -0.0006 -0.0091 140 GLY A N   
1237 C  CA  . GLY A 139 ? 0.1330 0.1040 0.1068 -0.0194 -0.0114 0.0006  140 GLY A CA  
1238 C  C   . GLY A 139 ? 0.1010 0.0842 0.1122 -0.0093 0.0041  0.0013  140 GLY A C   
1239 O  O   . GLY A 139 ? 0.1203 0.0920 0.1198 0.0098  -0.0151 0.0048  140 GLY A O   
1240 N  N   . LEU A 140 ? 0.0930 0.0846 0.1219 -0.0010 -0.0013 0.0020  141 LEU A N   
1241 C  CA  . LEU A 140 ? 0.1031 0.0794 0.1115 -0.0054 -0.0027 0.0027  141 LEU A CA  
1242 C  C   . LEU A 140 ? 0.1030 0.0768 0.0948 0.0096  -0.0170 0.0003  141 LEU A C   
1243 O  O   . LEU A 140 ? 0.1008 0.0895 0.1147 -0.0035 -0.0093 0.0063  141 LEU A O   
1244 C  CB  . LEU A 140 ? 0.1097 0.0943 0.1165 0.0020  0.0062  0.0046  141 LEU A CB  
1245 C  CG  . LEU A 140 ? 0.1370 0.1316 0.1446 0.0351  0.0298  0.0142  141 LEU A CG  
1246 C  CD1 . LEU A 140 ? 0.1277 0.1413 0.1340 0.0265  0.0184  0.0013  141 LEU A CD1 
1247 C  CD2 . LEU A 140 ? 0.2410 0.1185 0.1835 0.0408  0.0680  0.0226  141 LEU A CD2 
1248 N  N   . ALA A 141 ? 0.1045 0.0806 0.1048 0.0012  -0.0071 0.0006  142 ALA A N   
1249 C  CA  . ALA A 141 ? 0.1133 0.0811 0.1210 -0.0119 -0.0012 0.0027  142 ALA A CA  
1250 C  C   . ALA A 141 ? 0.0974 0.0860 0.1079 -0.0109 -0.0043 0.0109  142 ALA A C   
1251 O  O   . ALA A 141 ? 0.1270 0.0935 0.1050 -0.0027 -0.0141 0.0130  142 ALA A O   
1252 C  CB  . ALA A 141 ? 0.0992 0.1228 0.1365 -0.0038 0.0043  0.0049  142 ALA A CB  
1253 N  N   . VAL A 142 ? 0.0961 0.0803 0.1070 -0.0035 -0.0093 0.0054  143 VAL A N   
1254 C  CA  . VAL A 142 ? 0.1054 0.0833 0.0957 0.0013  -0.0076 -0.0006 143 VAL A CA  
1255 C  C   . VAL A 142 ? 0.0952 0.0868 0.0916 0.0026  0.0020  0.0006  143 VAL A C   
1256 O  O   . VAL A 142 ? 0.0970 0.0948 0.0979 -0.0060 -0.0073 0.0085  143 VAL A O   
1257 C  CB  . VAL A 142 ? 0.0898 0.1027 0.1050 0.0020  -0.0037 -0.0057 143 VAL A CB  
1258 C  CG1 . VAL A 142 ? 0.1122 0.1176 0.0970 0.0043  -0.0063 -0.0054 143 VAL A CG1 
1259 C  CG2 . VAL A 142 ? 0.0996 0.1307 0.1194 -0.0171 0.0005  0.0142  143 VAL A CG2 
1260 N  N   . LEU A 143 ? 0.0873 0.0807 0.1030 -0.0098 -0.0062 0.0060  144 LEU A N   
1261 C  CA  . LEU A 143 ? 0.0798 0.0922 0.1118 -0.0048 -0.0082 -0.0038 144 LEU A CA  
1262 C  C   . LEU A 143 ? 0.0957 0.0964 0.0987 -0.0120 -0.0030 0.0120  144 LEU A C   
1263 O  O   . LEU A 143 ? 0.1350 0.0996 0.1025 -0.0046 0.0034  0.0087  144 LEU A O   
1264 C  CB  . LEU A 143 ? 0.1068 0.1335 0.1194 -0.0082 -0.0142 0.0164  144 LEU A CB  
1265 C  CG  . LEU A 143 ? 0.1142 0.1203 0.1640 -0.0081 -0.0129 0.0030  144 LEU A CG  
1266 C  CD1 . LEU A 143 ? 0.1303 0.1941 0.1801 -0.0186 -0.0208 0.0533  144 LEU A CD1 
1267 C  CD2 . LEU A 143 ? 0.1158 0.2034 0.1852 0.0098  -0.0230 -0.0034 144 LEU A CD2 
1268 N  N   . GLY A 144 ? 0.0969 0.0877 0.1010 -0.0119 -0.0060 0.0046  145 GLY A N   
1269 C  CA  . GLY A 144 ? 0.1010 0.0841 0.1158 -0.0006 -0.0049 -0.0065 145 GLY A CA  
1270 C  C   . GLY A 144 ? 0.0828 0.0926 0.0978 0.0020  -0.0057 0.0125  145 GLY A C   
1271 O  O   . GLY A 144 ? 0.1097 0.1052 0.0970 -0.0142 0.0027  -0.0043 145 GLY A O   
1272 N  N   . ILE A 145 ? 0.0966 0.0837 0.0951 -0.0040 -0.0041 -0.0082 146 ILE A N   
1273 C  CA  . ILE A 145 ? 0.0766 0.0812 0.1115 -0.0060 -0.0142 0.0000  146 ILE A CA  
1274 C  C   . ILE A 145 ? 0.0834 0.0850 0.1052 -0.0071 -0.0193 0.0017  146 ILE A C   
1275 O  O   . ILE A 145 ? 0.1127 0.0856 0.1140 -0.0102 0.0063  0.0043  146 ILE A O   
1276 C  CB  . ILE A 145 ? 0.0982 0.0934 0.1307 0.0038  -0.0181 0.0098  146 ILE A CB  
1277 C  CG1 . ILE A 145 ? 0.1172 0.1181 0.1536 0.0241  -0.0386 -0.0052 146 ILE A CG1 
1278 C  CG2 . ILE A 145 ? 0.1025 0.1131 0.1946 -0.0124 -0.0489 0.0017  146 ILE A CG2 
1279 C  CD1 . ILE A 145 ? 0.1158 0.1237 0.1509 0.0130  -0.0265 0.0043  146 ILE A CD1 
1280 N  N   . PHE A 146 ? 0.0951 0.0806 0.1027 -0.0017 -0.0119 0.0074  147 PHE A N   
1281 C  CA  . PHE A 146 ? 0.1088 0.0772 0.1164 0.0076  -0.0148 0.0060  147 PHE A CA  
1282 C  C   . PHE A 146 ? 0.0988 0.0903 0.1149 -0.0071 -0.0126 -0.0031 147 PHE A C   
1283 O  O   . PHE A 146 ? 0.0974 0.1070 0.1271 -0.0071 -0.0173 -0.0087 147 PHE A O   
1284 C  CB  . PHE A 146 ? 0.1018 0.0904 0.1201 -0.0109 -0.0164 0.0087  147 PHE A CB  
1285 C  CG  . PHE A 146 ? 0.1001 0.0855 0.1048 -0.0020 -0.0173 0.0120  147 PHE A CG  
1286 C  CD1 . PHE A 146 ? 0.0970 0.0908 0.1208 0.0013  -0.0131 0.0115  147 PHE A CD1 
1287 C  CD2 . PHE A 146 ? 0.1149 0.0948 0.1092 -0.0092 -0.0131 0.0195  147 PHE A CD2 
1288 C  CE1 . PHE A 146 ? 0.1124 0.1031 0.1097 -0.0120 -0.0130 0.0030  147 PHE A CE1 
1289 C  CE2 . PHE A 146 ? 0.1181 0.1041 0.1306 -0.0109 -0.0070 0.0115  147 PHE A CE2 
1290 C  CZ  . PHE A 146 ? 0.1057 0.0988 0.1210 -0.0046 -0.0197 0.0161  147 PHE A CZ  
1291 N  N   . LEU A 147 ? 0.1070 0.0930 0.1115 -0.0062 -0.0063 -0.0048 148 LEU A N   
1292 C  CA  . LEU A 147 ? 0.1356 0.0781 0.1088 -0.0151 -0.0186 -0.0092 148 LEU A CA  
1293 C  C   . LEU A 147 ? 0.1176 0.1034 0.0987 -0.0060 -0.0076 -0.0019 148 LEU A C   
1294 O  O   . LEU A 147 ? 0.1171 0.0961 0.1379 -0.0043 -0.0148 0.0027  148 LEU A O   
1295 C  CB  . LEU A 147 ? 0.1289 0.0970 0.1243 -0.0176 -0.0060 -0.0057 148 LEU A CB  
1296 C  CG  . LEU A 147 ? 0.1429 0.0947 0.1158 -0.0126 -0.0182 -0.0027 148 LEU A CG  
1297 C  CD1 . LEU A 147 ? 0.1854 0.0974 0.1298 -0.0164 -0.0231 -0.0020 148 LEU A CD1 
1298 C  CD2 . LEU A 147 ? 0.1699 0.1250 0.1228 -0.0166 -0.0197 0.0003  148 LEU A CD2 
1299 N  N   . LYS A 148 ? 0.1246 0.0798 0.1395 -0.0141 -0.0124 -0.0071 149 LYS A N   
1300 C  CA  . LYS A 148 ? 0.1333 0.0873 0.1614 -0.0046 -0.0160 -0.0052 149 LYS A CA  
1301 C  C   . LYS A 148 ? 0.1342 0.1040 0.1544 0.0012  -0.0170 0.0043  149 LYS A C   
1302 O  O   . LYS A 148 ? 0.1694 0.1412 0.1421 0.0115  -0.0296 -0.0154 149 LYS A O   
1303 C  CB  . LYS A 148 ? 0.1719 0.1263 0.1488 -0.0390 -0.0219 0.0142  149 LYS A CB  
1304 C  CG  . LYS A 148 ? 0.1666 0.1738 0.1682 -0.0496 -0.0012 0.0247  149 LYS A CG  
1305 C  CD  . LYS A 148 ? 0.2565 0.2551 0.2522 -0.0447 0.0377  0.0280  149 LYS A CD  
1306 C  CE  . LYS A 148 ? 0.2655 0.5449 0.3427 -0.1510 0.0868  0.1164  149 LYS A CE  
1307 N  NZ  . LYS A 148 ? 0.8511 0.8338 0.4681 -0.4564 -0.0441 0.2901  149 LYS A NZ  
1308 N  N   . VAL A 149 ? 0.1620 0.0996 0.1641 0.0024  -0.0315 -0.0131 150 VAL A N   
1309 C  CA  . VAL A 149 ? 0.1595 0.1181 0.1448 0.0027  -0.0183 -0.0186 150 VAL A CA  
1310 C  C   . VAL A 149 ? 0.1735 0.1050 0.1515 -0.0164 -0.0065 0.0006  150 VAL A C   
1311 O  O   . VAL A 149 ? 0.1842 0.1325 0.1791 -0.0153 -0.0252 0.0041  150 VAL A O   
1312 C  CB  . VAL A 149 ? 0.1604 0.1280 0.1721 0.0030  -0.0142 -0.0098 150 VAL A CB  
1313 C  CG1 . VAL A 149 ? 0.2064 0.1782 0.1551 0.0197  -0.0131 -0.0414 150 VAL A CG1 
1314 C  CG2 . VAL A 149 ? 0.1542 0.1756 0.2090 -0.0232 0.0071  0.0049  150 VAL A CG2 
1315 N  N   . GLY A 150 ? 0.1650 0.1316 0.1702 -0.0240 -0.0439 -0.0043 151 GLY A N   
1316 C  CA  . GLY A 150 ? 0.1787 0.1595 0.2081 -0.0482 -0.0549 0.0065  151 GLY A CA  
1317 C  C   . GLY A 150 ? 0.1780 0.1391 0.1668 -0.0421 -0.0355 -0.0131 151 GLY A C   
1318 O  O   . GLY A 150 ? 0.1941 0.1506 0.1911 -0.0401 -0.0274 -0.0263 151 GLY A O   
1319 N  N   A SER A 151 ? 0.1743 0.1541 0.2205 -0.0248 -0.0372 -0.0164 152 SER A N   
1320 N  N   B SER A 151 ? 0.1649 0.1524 0.2266 -0.0252 -0.0416 -0.0177 152 SER A N   
1321 C  CA  A SER A 151 ? 0.2008 0.1861 0.1976 -0.0207 -0.0395 -0.0013 152 SER A CA  
1322 C  CA  B SER A 151 ? 0.1685 0.1676 0.2018 -0.0017 -0.0296 -0.0098 152 SER A CA  
1323 C  C   A SER A 151 ? 0.1833 0.1544 0.1577 -0.0206 -0.0118 -0.0425 152 SER A C   
1324 C  C   B SER A 151 ? 0.1904 0.1216 0.1685 -0.0035 -0.0449 -0.0199 152 SER A C   
1325 O  O   A SER A 151 ? 0.1431 0.1624 0.1379 -0.0120 0.0000  -0.0399 152 SER A O   
1326 O  O   B SER A 151 ? 0.1588 0.1562 0.1405 -0.0137 -0.0076 -0.0293 152 SER A O   
1327 C  CB  A SER A 151 ? 0.2016 0.2885 0.2784 -0.0891 0.0035  -0.0258 152 SER A CB  
1328 C  CB  B SER A 151 ? 0.1665 0.1967 0.2414 -0.0031 -0.0197 0.0109  152 SER A CB  
1329 O  OG  A SER A 151 ? 0.1841 0.3754 0.2449 -0.0313 -0.0024 -0.0335 152 SER A OG  
1330 O  OG  B SER A 151 ? 0.1656 0.2515 0.3424 -0.0296 -0.0060 0.0758  152 SER A OG  
1331 N  N   . ALA A 152 ? 0.2056 0.1377 0.1791 -0.0109 -0.0494 -0.0346 153 ALA A N   
1332 C  CA  . ALA A 152 ? 0.1879 0.1524 0.1790 -0.0035 -0.0417 -0.0326 153 ALA A CA  
1333 C  C   . ALA A 152 ? 0.1836 0.1492 0.1659 0.0020  -0.0368 -0.0253 153 ALA A C   
1334 O  O   . ALA A 152 ? 0.1911 0.1659 0.2222 0.0049  -0.0274 -0.0250 153 ALA A O   
1335 C  CB  . ALA A 152 ? 0.2508 0.1946 0.1708 0.0208  -0.0439 -0.0287 153 ALA A CB  
1336 N  N   . LYS A 153 ? 0.2099 0.1463 0.1676 -0.0148 -0.0472 -0.0034 154 LYS A N   
1337 C  CA  . LYS A 153 ? 0.2493 0.1237 0.1951 0.0135  -0.0498 -0.0126 154 LYS A CA  
1338 C  C   . LYS A 153 ? 0.1949 0.1554 0.1699 0.0006  -0.0274 -0.0313 154 LYS A C   
1339 O  O   . LYS A 153 ? 0.1766 0.1588 0.1712 0.0065  -0.0520 -0.0183 154 LYS A O   
1340 C  CB  . LYS A 153 ? 0.2300 0.1321 0.2046 -0.0023 -0.0553 0.0043  154 LYS A CB  
1341 C  CG  . LYS A 153 ? 0.3079 0.1448 0.2446 -0.0197 -0.0614 -0.0248 154 LYS A CG  
1342 C  CD  . LYS A 153 ? 0.3438 0.1773 0.2529 -0.0092 -0.0502 -0.0524 154 LYS A CD  
1343 C  CE  . LYS A 153 ? 0.3345 0.2019 0.2127 0.0043  -0.0615 -0.0269 154 LYS A CE  
1344 N  NZ  . LYS A 153 ? 0.2213 0.2583 0.2748 -0.0063 -0.0054 -0.0432 154 LYS A NZ  
1345 N  N   . PRO A 154 ? 0.2028 0.1624 0.2105 -0.0124 -0.0658 -0.0103 155 PRO A N   
1346 C  CA  . PRO A 154 ? 0.1994 0.1870 0.2108 -0.0146 -0.0644 -0.0388 155 PRO A CA  
1347 C  C   . PRO A 154 ? 0.1735 0.2266 0.1466 0.0181  -0.0577 -0.0131 155 PRO A C   
1348 O  O   . PRO A 154 ? 0.2673 0.2171 0.1806 0.0104  -0.0812 0.0034  155 PRO A O   
1349 C  CB  . PRO A 154 ? 0.1836 0.2291 0.3269 -0.0263 -0.0768 0.0068  155 PRO A CB  
1350 C  CG  . PRO A 154 ? 0.2250 0.2302 0.3452 0.0000  -0.0427 0.0197  155 PRO A CG  
1351 C  CD  . PRO A 154 ? 0.1806 0.2320 0.2637 -0.0186 -0.0253 0.0013  155 PRO A CD  
1352 N  N   . GLY A 155 ? 0.2097 0.1515 0.1747 0.0366  -0.0361 0.0000  156 GLY A N   
1353 C  CA  . GLY A 155 ? 0.2231 0.1678 0.1916 0.0020  -0.0373 -0.0197 156 GLY A CA  
1354 C  C   . GLY A 155 ? 0.2594 0.1488 0.1668 -0.0076 -0.0531 0.0302  156 GLY A C   
1355 O  O   . GLY A 155 ? 0.2881 0.1499 0.2845 0.0049  -0.0675 0.0241  156 GLY A O   
1356 N  N   . LEU A 156 ? 0.1903 0.1694 0.1713 -0.0065 -0.0362 -0.0010 157 LEU A N   
1357 C  CA  . LEU A 156 ? 0.2295 0.1356 0.1536 -0.0176 -0.0416 -0.0074 157 LEU A CA  
1358 C  C   . LEU A 156 ? 0.2132 0.1568 0.1567 -0.0225 -0.0610 -0.0035 157 LEU A C   
1359 O  O   . LEU A 156 ? 0.2289 0.1544 0.1440 -0.0199 -0.0631 -0.0153 157 LEU A O   
1360 C  CB  . LEU A 156 ? 0.1859 0.1639 0.1858 -0.0285 -0.0671 -0.0041 157 LEU A CB  
1361 C  CG  . LEU A 156 ? 0.2231 0.1641 0.1571 -0.0152 -0.0485 -0.0048 157 LEU A CG  
1362 C  CD1 . LEU A 156 ? 0.2386 0.1967 0.1606 -0.0610 -0.0562 -0.0197 157 LEU A CD1 
1363 C  CD2 . LEU A 156 ? 0.2338 0.1893 0.1823 -0.0049 -0.0421 0.0125  157 LEU A CD2 
1364 N  N   . GLN A 157 ? 0.2108 0.1639 0.1570 -0.0129 -0.0564 -0.0063 158 GLN A N   
1365 C  CA  . GLN A 157 ? 0.2856 0.1826 0.1167 -0.0478 -0.0467 -0.0305 158 GLN A CA  
1366 C  C   . GLN A 157 ? 0.2407 0.1875 0.1673 -0.0597 -0.0697 -0.0115 158 GLN A C   
1367 O  O   . GLN A 157 ? 0.2257 0.1950 0.1686 -0.0247 -0.0612 -0.0193 158 GLN A O   
1368 C  CB  . GLN A 157 ? 0.2913 0.1992 0.1712 -0.0511 -0.0592 -0.0441 158 GLN A CB  
1369 C  CG  . GLN A 157 ? 0.3309 0.1624 0.1886 -0.0219 -0.0634 -0.0498 158 GLN A CG  
1370 C  CD  . GLN A 157 ? 0.2896 0.1779 0.1563 -0.0513 -0.0535 -0.0241 158 GLN A CD  
1371 O  OE1 . GLN A 157 ? 0.3082 0.1720 0.1508 -0.0219 -0.0593 -0.0227 158 GLN A OE1 
1372 N  NE2 . GLN A 157 ? 0.3000 0.2264 0.1630 -0.0617 -0.0272 -0.0353 158 GLN A NE2 
1373 N  N   . LYS A 158 ? 0.2515 0.1718 0.1563 -0.0205 -0.0812 0.0024  159 LYS A N   
1374 C  CA  . LYS A 158 ? 0.2554 0.1676 0.1685 0.0031  -0.0754 0.0109  159 LYS A CA  
1375 C  C   . LYS A 158 ? 0.2363 0.1833 0.1439 -0.0175 -0.0666 -0.0186 159 LYS A C   
1376 O  O   . LYS A 158 ? 0.2860 0.2029 0.1483 -0.0219 -0.0527 -0.0048 159 LYS A O   
1377 C  CB  . LYS A 158 ? 0.2928 0.1745 0.2123 -0.0120 -0.0697 0.0432  159 LYS A CB  
1378 C  CG  . LYS A 158 ? 0.4038 0.3337 0.2734 -0.0280 -0.1054 0.0498  159 LYS A CG  
1379 C  CD  . LYS A 158 ? 0.3732 0.4602 0.5691 0.0504  -0.1014 0.1647  159 LYS A CD  
1380 C  CE  . LYS A 158 ? 0.7067 0.8130 0.2360 -0.1332 -0.1615 0.1022  159 LYS A CE  
1381 N  NZ  . LYS A 158 ? 0.7569 0.9024 0.3262 -0.1207 -0.0702 0.2648  159 LYS A NZ  
1382 N  N   . VAL A 159 ? 0.2633 0.1658 0.1331 0.0019  -0.0702 -0.0137 160 VAL A N   
1383 C  CA  . VAL A 159 ? 0.2554 0.1594 0.1289 -0.0317 -0.0612 -0.0161 160 VAL A CA  
1384 C  C   . VAL A 159 ? 0.2372 0.1448 0.1430 -0.0148 -0.0436 -0.0229 160 VAL A C   
1385 O  O   . VAL A 159 ? 0.2417 0.1630 0.1720 -0.0013 -0.0469 -0.0068 160 VAL A O   
1386 C  CB  . VAL A 159 ? 0.2161 0.1673 0.1326 -0.0164 -0.0581 -0.0031 160 VAL A CB  
1387 C  CG1 . VAL A 159 ? 0.2451 0.1827 0.1712 -0.0390 -0.0159 0.0000  160 VAL A CG1 
1388 C  CG2 . VAL A 159 ? 0.2630 0.1824 0.1455 0.0027  -0.0529 -0.0340 160 VAL A CG2 
1389 N  N   . VAL A 160 ? 0.2435 0.1436 0.1313 -0.0043 -0.0410 -0.0230 161 VAL A N   
1390 C  CA  . VAL A 160 ? 0.2608 0.1508 0.1448 -0.0013 -0.0252 0.0027  161 VAL A CA  
1391 C  C   . VAL A 160 ? 0.2781 0.1590 0.1641 -0.0204 -0.0003 -0.0443 161 VAL A C   
1392 O  O   . VAL A 160 ? 0.2892 0.1878 0.1932 -0.0253 0.0000  -0.0302 161 VAL A O   
1393 C  CB  . VAL A 160 ? 0.2590 0.1773 0.1921 -0.0115 0.0080  -0.0436 161 VAL A CB  
1394 C  CG1 . VAL A 160 ? 0.3057 0.1854 0.2558 -0.0513 -0.0631 -0.0241 161 VAL A CG1 
1395 C  CG2 . VAL A 160 ? 0.2637 0.1888 0.1852 0.0164  -0.0210 -0.0274 161 VAL A CG2 
1396 N  N   . ASP A 161 ? 0.2949 0.2073 0.1234 -0.0489 -0.0241 -0.0210 162 ASP A N   
1397 C  CA  . ASP A 161 ? 0.3240 0.2716 0.1281 -0.0961 -0.0562 -0.0197 162 ASP A CA  
1398 C  C   . ASP A 161 ? 0.3276 0.2957 0.1210 -0.0863 -0.0275 -0.0261 162 ASP A C   
1399 O  O   . ASP A 161 ? 0.5213 0.3556 0.1589 -0.1490 0.0428  -0.0386 162 ASP A O   
1400 C  CB  . ASP A 161 ? 0.4415 0.2878 0.1457 -0.0732 -0.0688 -0.0619 162 ASP A CB  
1401 C  CG  . ASP A 161 ? 0.5841 0.3370 0.1827 -0.0921 -0.0208 -0.0753 162 ASP A CG  
1402 O  OD1 . ASP A 161 ? 0.4778 0.3610 0.2888 -0.1254 -0.0601 -0.0697 162 ASP A OD1 
1403 O  OD2 . ASP A 161 ? 0.6226 0.4253 0.2107 -0.0196 -0.1304 -0.0617 162 ASP A OD2 
1404 N  N   . VAL A 162 ? 0.3359 0.2099 0.1360 -0.0724 -0.0678 0.0062  163 VAL A N   
1405 C  CA  . VAL A 162 ? 0.2949 0.2356 0.1543 -0.0296 -0.0697 0.0283  163 VAL A CA  
1406 C  C   . VAL A 162 ? 0.3079 0.1720 0.1142 -0.0242 -0.0054 0.0166  163 VAL A C   
1407 O  O   . VAL A 162 ? 0.3574 0.2215 0.1201 -0.0384 -0.0013 -0.0063 163 VAL A O   
1408 C  CB  . VAL A 162 ? 0.3140 0.1985 0.2197 -0.0199 -0.0522 0.0063  163 VAL A CB  
1409 C  CG1 . VAL A 162 ? 0.3201 0.1949 0.2037 -0.0315 -0.0456 0.0012  163 VAL A CG1 
1410 C  CG2 . VAL A 162 ? 0.3679 0.2206 0.2478 0.0439  0.0015  0.0467  163 VAL A CG2 
1411 N  N   . LEU A 163 ? 0.2870 0.2029 0.1528 -0.0193 -0.0520 0.0041  164 LEU A N   
1412 C  CA  . LEU A 163 ? 0.3129 0.1650 0.1298 -0.0215 0.0320  0.0076  164 LEU A CA  
1413 C  C   . LEU A 163 ? 0.3237 0.2011 0.1518 -0.0107 0.0281  -0.0049 164 LEU A C   
1414 O  O   . LEU A 163 ? 0.3219 0.2090 0.1234 0.0194  0.0251  0.0175  164 LEU A O   
1415 C  CB  . LEU A 163 ? 0.2975 0.1563 0.1325 -0.0263 0.0005  0.0000  164 LEU A CB  
1416 C  CG  . LEU A 163 ? 0.2655 0.1492 0.1339 -0.0080 -0.0006 0.0057  164 LEU A CG  
1417 C  CD1 . LEU A 163 ? 0.3136 0.1577 0.1655 0.0081  0.0000  0.0182  164 LEU A CD1 
1418 C  CD2 . LEU A 163 ? 0.2465 0.1880 0.1198 0.0082  -0.0120 -0.0041 164 LEU A CD2 
1419 N  N   . ASP A 164 ? 0.3901 0.1932 0.1194 -0.0386 0.0081  -0.0252 165 ASP A N   
1420 C  CA  . ASP A 164 ? 0.5551 0.2334 0.1533 -0.0487 0.0908  -0.0544 165 ASP A CA  
1421 C  C   . ASP A 164 ? 0.4914 0.2831 0.1235 -0.0130 0.0623  -0.0126 165 ASP A C   
1422 O  O   . ASP A 164 ? 0.5234 0.3021 0.2056 0.0215  0.1208  0.0230  165 ASP A O   
1423 C  CB  . ASP A 164 ? 0.6844 0.3700 0.2662 -0.0548 0.0472  -0.1897 165 ASP A CB  
1424 C  CG  . ASP A 164 ? 0.8302 0.4453 1.2716 -0.2169 -0.3555 -0.1014 165 ASP A CG  
1425 O  OD1 . ASP A 164 ? 0.8644 1.1948 0.3161 -0.6539 0.0562  -0.1348 165 ASP A OD1 
1426 O  OD2 . ASP A 164 ? 3.0336 3.9663 2.4237 -0.3603 -1.2395 -2.5638 165 ASP A OD2 
1427 N  N   . SER A 165 ? 0.3298 0.2342 0.1378 -0.0252 -0.0119 0.0046  166 SER A N   
1428 C  CA  . SER A 165 ? 0.4003 0.2820 0.1404 -0.0359 0.0137  -0.0148 166 SER A CA  
1429 C  C   . SER A 165 ? 0.3212 0.2064 0.1118 0.0148  0.0153  0.0054  166 SER A C   
1430 O  O   . SER A 165 ? 0.3894 0.2395 0.1260 -0.0285 0.0046  0.0272  166 SER A O   
1431 C  CB  . SER A 165 ? 0.4663 0.3233 0.1835 -0.0087 0.0666  0.0135  166 SER A CB  
1432 O  OG  . SER A 165 ? 0.4433 0.2684 0.1932 0.0280  0.0262  0.0478  166 SER A OG  
1433 N  N   . ILE A 166 ? 0.2885 0.2099 0.0988 -0.0076 0.0152  0.0137  167 ILE A N   
1434 C  CA  . ILE A 166 ? 0.2328 0.1774 0.1333 -0.0040 -0.0015 -0.0054 167 ILE A CA  
1435 C  C   . ILE A 166 ? 0.1880 0.2127 0.1079 -0.0076 0.0184  -0.0249 167 ILE A C   
1436 O  O   . ILE A 166 ? 0.2460 0.1870 0.1113 -0.0115 0.0239  0.0041  167 ILE A O   
1437 C  CB  . ILE A 166 ? 0.2727 0.1791 0.1176 -0.0060 0.0137  0.0043  167 ILE A CB  
1438 C  CG1 . ILE A 166 ? 0.2594 0.1958 0.1043 -0.0147 0.0192  0.0027  167 ILE A CG1 
1439 C  CG2 . ILE A 166 ? 0.2644 0.1844 0.1499 0.0176  0.0040  0.0348  167 ILE A CG2 
1440 C  CD1 . ILE A 166 ? 0.2522 0.1974 0.1235 -0.0038 0.0351  -0.0175 167 ILE A CD1 
1441 N  N   . LYS A 167 ? 0.2766 0.1677 0.1395 0.0059  0.0218  0.0113  168 LYS A N   
1442 C  CA  . LYS A 167 ? 0.2187 0.2133 0.1313 0.0162  0.0070  -0.0308 168 LYS A CA  
1443 C  C   . LYS A 167 ? 0.2453 0.1889 0.1342 -0.0054 0.0631  0.0335  168 LYS A C   
1444 O  O   . LYS A 167 ? 0.2565 0.1571 0.1395 -0.0328 0.0229  -0.0098 168 LYS A O   
1445 C  CB  . LYS A 167 ? 0.2985 0.1761 0.1339 -0.0203 0.0012  -0.0388 168 LYS A CB  
1446 C  CG  . LYS A 167 ? 0.2831 0.1955 0.1651 -0.0048 0.0544  -0.0414 168 LYS A CG  
1447 C  CD  . LYS A 167 ? 0.3700 0.2478 0.2289 0.0054  -0.0164 -0.0680 168 LYS A CD  
1448 C  CE  . LYS A 167 ? 0.5813 0.3858 0.2651 0.1253  -0.0741 -0.1597 168 LYS A CE  
1449 N  NZ  . LYS A 167 ? 0.5569 0.5102 1.0858 0.0220  -0.2522 -0.1146 168 LYS A NZ  
1450 N  N   . THR A 168 ? 0.2149 0.1585 0.1509 -0.0226 0.0208  -0.0059 169 THR A N   
1451 C  CA  . THR A 168 ? 0.2465 0.1914 0.1221 0.0035  0.0540  0.0175  169 THR A CA  
1452 C  C   . THR A 168 ? 0.1972 0.1949 0.0983 -0.0043 0.0241  0.0164  169 THR A C   
1453 O  O   . THR A 168 ? 0.2533 0.1844 0.1475 -0.0153 0.0401  0.0250  169 THR A O   
1454 C  CB  . THR A 168 ? 0.2666 0.2177 0.1465 -0.0252 0.0516  -0.0148 169 THR A CB  
1455 O  OG1 . THR A 168 ? 0.3026 0.2597 0.1263 -0.0252 0.0538  -0.0006 169 THR A OG1 
1456 C  CG2 . THR A 168 ? 0.3136 0.2215 0.1798 -0.0049 0.0626  -0.0012 169 THR A CG2 
1457 N  N   A LYS A 169 ? 0.2222 0.2071 0.1597 -0.0675 0.0206  -0.0052 170 LYS A N   
1458 N  N   B LYS A 169 ? 0.3147 0.2196 0.1156 -0.0653 0.1123  0.0093  170 LYS A N   
1459 C  CA  A LYS A 169 ? 0.1158 0.1440 0.1606 -0.0057 0.0296  0.0131  170 LYS A CA  
1460 C  CA  B LYS A 169 ? 0.2389 0.2360 0.1668 -0.0252 0.0741  -0.0098 170 LYS A CA  
1461 C  C   A LYS A 169 ? 0.1206 0.1596 0.1115 -0.0153 0.0291  0.0159  170 LYS A C   
1462 C  C   B LYS A 169 ? 0.2310 0.1923 0.1942 -0.0399 0.0504  -0.0197 170 LYS A C   
1463 O  O   A LYS A 169 ? 0.1465 0.1929 0.1036 0.0124  0.0362  0.0274  170 LYS A O   
1464 O  O   B LYS A 169 ? 0.2770 0.2583 0.1835 -0.0148 0.0533  0.0000  170 LYS A O   
1465 C  CB  A LYS A 169 ? 0.1317 0.1647 0.1253 0.0375  0.0560  0.0271  170 LYS A CB  
1466 C  CB  B LYS A 169 ? 0.2178 0.1307 0.2741 0.0006  0.0854  -0.0040 170 LYS A CB  
1467 C  CG  A LYS A 169 ? 0.1154 0.1976 0.1395 0.0003  0.0174  0.0447  170 LYS A CG  
1468 C  CG  B LYS A 169 ? 0.2153 0.2277 0.2489 -0.0692 0.0337  0.0461  170 LYS A CG  
1469 C  CD  A LYS A 169 ? 0.1412 0.2374 0.1527 0.0241  0.0337  0.0210  170 LYS A CD  
1470 C  CD  B LYS A 169 ? 0.2134 0.2831 0.4178 -0.1159 -0.0174 0.0790  170 LYS A CD  
1471 C  CE  A LYS A 169 ? 0.3287 0.3973 0.2960 -0.1569 -0.0175 0.0076  170 LYS A CE  
1472 C  CE  B LYS A 169 ? 0.2985 0.5695 0.4339 -0.1164 0.1483  0.0119  170 LYS A CE  
1473 N  NZ  A LYS A 169 ? 0.4433 0.3995 0.2039 0.0185  -0.0126 0.0175  170 LYS A NZ  
1474 N  NZ  B LYS A 169 ? 0.4866 0.5181 0.3546 -0.0974 0.0060  0.1845  170 LYS A NZ  
1475 N  N   A GLY A 170 ? 0.0930 0.1342 0.1729 -0.0115 0.0230  0.0218  171 GLY A N   
1476 N  N   B GLY A 170 ? 0.2196 0.1492 0.1431 -0.0361 0.0197  0.0148  171 GLY A N   
1477 C  CA  A GLY A 170 ? 0.1463 0.1149 0.2117 0.0286  0.0164  0.0364  171 GLY A CA  
1478 C  CA  B GLY A 170 ? 0.3147 0.1145 0.1949 -0.0728 0.0421  0.0307  171 GLY A CA  
1479 C  C   A GLY A 170 ? 0.1621 0.1712 0.2239 0.0408  0.0109  0.0842  171 GLY A C   
1480 C  C   B GLY A 170 ? 0.3183 0.1555 0.1638 -0.0505 0.0248  0.0175  171 GLY A C   
1481 O  O   A GLY A 170 ? 0.1981 0.1736 0.2248 0.0098  0.0093  0.0842  171 GLY A O   
1482 O  O   B GLY A 170 ? 0.4135 0.1710 0.2684 -0.0498 0.0608  0.0643  171 GLY A O   
1483 N  N   . LYS A 171 ? 0.2399 0.1632 0.1930 -0.0208 0.0410  0.0476  172 LYS A N   
1484 C  CA  . LYS A 171 ? 0.2389 0.1852 0.2046 -0.0062 0.0324  0.0434  172 LYS A CA  
1485 C  C   . LYS A 171 ? 0.2003 0.2152 0.1164 0.0219  0.0230  0.0006  172 LYS A C   
1486 O  O   . LYS A 171 ? 0.2511 0.2099 0.1120 -0.0175 0.0219  0.0364  172 LYS A O   
1487 C  CB  . LYS A 171 ? 0.2422 0.2052 0.1403 -0.0041 0.0438  0.0073  172 LYS A CB  
1488 C  CG  . LYS A 171 ? 0.2705 0.2957 0.1923 -0.0040 0.0108  -0.0238 172 LYS A CG  
1489 C  CD  . LYS A 171 ? 0.5684 0.2881 0.1763 -0.0020 0.0171  -0.0296 172 LYS A CD  
1490 C  CE  . LYS A 171 ? 0.7300 0.5389 0.2361 -0.0096 -0.0432 0.0926  172 LYS A CE  
1491 N  NZ  . LYS A 171 ? 0.9258 0.3495 0.2720 -0.0938 0.2745  0.0177  172 LYS A NZ  
1492 N  N   . SER A 172 ? 0.2540 0.2002 0.1650 0.0015  -0.0080 0.0790  173 SER A N   
1493 C  CA  . SER A 172 ? 0.1727 0.2307 0.2203 0.0017  0.0291  0.0318  173 SER A CA  
1494 C  C   . SER A 172 ? 0.1764 0.2197 0.1738 -0.0006 -0.0102 0.0710  173 SER A C   
1495 O  O   . SER A 172 ? 0.2946 0.2964 0.1076 0.0249  -0.0087 0.0381  173 SER A O   
1496 C  CB  . SER A 172 ? 0.3118 0.2125 0.1660 -0.0038 0.0357  0.0193  173 SER A CB  
1497 O  OG  . SER A 172 ? 0.5569 0.2440 0.1985 0.0104  0.0619  0.0710  173 SER A OG  
1498 N  N   . ALA A 173 ? 0.1976 0.2425 0.1655 0.0390  -0.0051 0.0038  174 ALA A N   
1499 C  CA  . ALA A 173 ? 0.2282 0.3596 0.1298 0.0434  -0.0340 0.0890  174 ALA A CA  
1500 C  C   . ALA A 173 ? 0.1790 0.2356 0.1507 -0.0131 -0.0296 0.0296  174 ALA A C   
1501 O  O   . ALA A 173 ? 0.2222 0.2203 0.1183 0.0129  -0.0114 0.0291  174 ALA A O   
1502 C  CB  . ALA A 173 ? 0.3574 0.2845 0.1729 0.0175  -0.0038 0.0141  174 ALA A CB  
1503 N  N   . ASP A 174 ? 0.2597 0.3319 0.1253 0.0425  -0.0120 0.0732  175 ASP A N   
1504 C  CA  . ASP A 174 ? 0.3847 0.2960 0.1190 0.0944  0.0031  0.0549  175 ASP A CA  
1505 C  C   . ASP A 174 ? 0.3388 0.2300 0.1545 0.0074  -0.0639 0.0423  175 ASP A C   
1506 O  O   . ASP A 174 ? 0.3008 0.3003 0.1752 0.0263  0.0027  -0.0377 175 ASP A O   
1507 C  CB  . ASP A 174 ? 0.3057 0.4347 0.2741 0.0921  0.0153  0.1676  175 ASP A CB  
1508 C  CG  . ASP A 174 ? 0.7178 0.5666 0.2515 -0.0706 -0.1075 0.2099  175 ASP A CG  
1509 O  OD1 . ASP A 174 ? 1.0643 0.6916 0.3754 0.0104  -0.0555 -0.0478 175 ASP A OD1 
1510 O  OD2 . ASP A 174 ? 0.2967 0.5795 0.3240 -0.0166 -0.0304 0.1509  175 ASP A OD2 
1511 N  N   . PHE A 175 ? 0.2680 0.2460 0.1326 0.0120  -0.0031 0.0086  176 PHE A N   
1512 C  CA  . PHE A 175 ? 0.2673 0.2228 0.1615 0.0076  -0.0274 0.0513  176 PHE A CA  
1513 C  C   . PHE A 175 ? 0.2630 0.1773 0.1641 -0.0052 -0.0467 -0.0010 176 PHE A C   
1514 O  O   . PHE A 175 ? 0.3082 0.2675 0.1446 0.0617  -0.0675 -0.0097 176 PHE A O   
1515 C  CB  . PHE A 175 ? 0.2802 0.1958 0.1904 0.0019  -0.0086 0.0296  176 PHE A CB  
1516 C  CG  . PHE A 175 ? 0.2985 0.1676 0.1456 0.0419  -0.0283 0.0012  176 PHE A CG  
1517 C  CD1 . PHE A 175 ? 0.3470 0.1845 0.1757 0.0357  -0.0012 -0.0172 176 PHE A CD1 
1518 C  CD2 . PHE A 175 ? 0.2885 0.1950 0.1629 0.0076  -0.0767 0.0218  176 PHE A CD2 
1519 C  CE1 . PHE A 175 ? 0.4555 0.1779 0.1914 0.0054  0.0326  0.0085  176 PHE A CE1 
1520 C  CE2 . PHE A 175 ? 0.3452 0.1771 0.1747 0.0296  -0.0746 0.0317  176 PHE A CE2 
1521 C  CZ  . PHE A 175 ? 0.3377 0.1640 0.2140 0.0302  -0.0430 -0.0192 176 PHE A CZ  
1522 N  N   . THR A 176 ? 0.3158 0.2250 0.1068 0.0302  -0.0612 0.0286  177 THR A N   
1523 C  CA  . THR A 176 ? 0.2842 0.1703 0.1465 0.0355  -0.0428 0.0285  177 THR A CA  
1524 C  C   . THR A 176 ? 0.2734 0.1509 0.1254 -0.0031 -0.0606 0.0408  177 THR A C   
1525 O  O   . THR A 176 ? 0.3082 0.1588 0.1395 -0.0148 -0.0693 0.0252  177 THR A O   
1526 C  CB  . THR A 176 ? 0.2410 0.2246 0.1726 0.0024  -0.0557 0.0640  177 THR A CB  
1527 O  OG1 . THR A 176 ? 0.4896 0.2363 0.1379 0.0744  -0.0966 0.0452  177 THR A OG1 
1528 C  CG2 . THR A 176 ? 0.3179 0.3086 0.3671 -0.0017 -0.0631 0.1906  177 THR A CG2 
1529 N  N   . ASN A 177 ? 0.2759 0.1932 0.1190 0.0313  -0.0571 0.0199  178 ASN A N   
1530 C  CA  . ASN A 177 ? 0.2433 0.1984 0.1852 -0.0074 -0.0555 0.0551  178 ASN A CA  
1531 C  C   . ASN A 177 ? 0.2587 0.1810 0.1500 0.0046  -0.0564 0.0487  178 ASN A C   
1532 O  O   . ASN A 177 ? 0.3298 0.2637 0.3021 -0.0329 -0.1084 0.1490  178 ASN A O   
1533 C  CB  . ASN A 177 ? 0.3154 0.1902 0.1902 -0.0005 -0.0900 0.0657  178 ASN A CB  
1534 C  CG  . ASN A 177 ? 0.2691 0.2150 0.1747 0.0253  -0.0719 0.0164  178 ASN A CG  
1535 O  OD1 . ASN A 177 ? 0.3021 0.2180 0.2194 0.0285  -0.0456 0.0575  178 ASN A OD1 
1536 N  ND2 . ASN A 177 ? 0.3057 0.2277 0.1607 0.0052  -0.0766 0.0643  178 ASN A ND2 
1537 N  N   . PHE A 178 ? 0.2500 0.1745 0.1366 0.0219  -0.0644 0.0335  179 PHE A N   
1538 C  CA  . PHE A 178 ? 0.2669 0.1579 0.1335 0.0013  -0.0443 0.0421  179 PHE A CA  
1539 C  C   . PHE A 178 ? 0.2508 0.1613 0.1324 0.0027  -0.0719 0.0305  179 PHE A C   
1540 O  O   . PHE A 178 ? 0.3046 0.1603 0.1391 -0.0181 -0.0666 0.0208  179 PHE A O   
1541 C  CB  . PHE A 178 ? 0.2842 0.1692 0.1307 0.0073  -0.0370 0.0342  179 PHE A CB  
1542 C  CG  . PHE A 178 ? 0.2759 0.1604 0.1385 -0.0062 -0.0460 0.0478  179 PHE A CG  
1543 C  CD1 . PHE A 178 ? 0.3488 0.1660 0.1269 -0.0026 -0.0421 0.0227  179 PHE A CD1 
1544 C  CD2 . PHE A 178 ? 0.2089 0.1647 0.1342 0.0010  -0.0274 0.0287  179 PHE A CD2 
1545 C  CE1 . PHE A 178 ? 0.3510 0.1541 0.1597 0.0137  -0.0515 0.0265  179 PHE A CE1 
1546 C  CE2 . PHE A 178 ? 0.1805 0.1500 0.1404 -0.0081 -0.0280 0.0185  179 PHE A CE2 
1547 C  CZ  . PHE A 178 ? 0.2343 0.1632 0.1253 -0.0063 -0.0232 0.0276  179 PHE A CZ  
1548 N  N   . ASP A 179 ? 0.2354 0.1701 0.1377 0.0102  -0.0595 0.0335  180 ASP A N   
1549 C  CA  . ASP A 179 ? 0.2090 0.2106 0.1270 0.0199  -0.0631 0.0082  180 ASP A CA  
1550 C  C   . ASP A 179 ? 0.1946 0.1384 0.1518 0.0074  -0.0283 0.0052  180 ASP A C   
1551 O  O   . ASP A 179 ? 0.2307 0.1562 0.1465 0.0049  -0.0476 0.0006  180 ASP A O   
1552 C  CB  . ASP A 179 ? 0.2143 0.2310 0.1844 0.0159  -0.0732 0.0282  180 ASP A CB  
1553 C  CG  . ASP A 179 ? 0.2316 0.2619 0.1993 0.0375  -0.0746 0.0273  180 ASP A CG  
1554 O  OD1 . ASP A 179 ? 0.2334 0.2107 0.1905 0.0313  -0.0582 0.0333  180 ASP A OD1 
1555 O  OD2 . ASP A 179 ? 0.2092 0.4727 0.3014 0.0274  -0.0772 0.0274  180 ASP A OD2 
1556 N  N   . PRO A 180 ? 0.1782 0.1502 0.1287 0.0046  -0.0313 0.0136  181 PRO A N   
1557 C  CA  . PRO A 180 ? 0.1798 0.1368 0.1463 0.0120  -0.0487 0.0285  181 PRO A CA  
1558 C  C   . PRO A 180 ? 0.1709 0.1500 0.1341 0.0035  -0.0383 0.0307  181 PRO A C   
1559 O  O   . PRO A 180 ? 0.1762 0.1481 0.1483 -0.0006 -0.0416 0.0229  181 PRO A O   
1560 C  CB  . PRO A 180 ? 0.1695 0.1888 0.1536 -0.0092 -0.0414 0.0162  181 PRO A CB  
1561 C  CG  . PRO A 180 ? 0.1959 0.1720 0.1535 -0.0020 -0.0513 0.0162  181 PRO A CG  
1562 C  CD  . PRO A 180 ? 0.2123 0.1640 0.1456 -0.0031 -0.0529 0.0103  181 PRO A CD  
1563 N  N   . ARG A 181 ? 0.1676 0.1753 0.1376 0.0218  -0.0298 0.0232  182 ARG A N   
1564 C  CA  . ARG A 181 ? 0.1421 0.1620 0.1650 -0.0062 -0.0175 0.0165  182 ARG A CA  
1565 C  C   . ARG A 181 ? 0.1488 0.1657 0.1798 0.0006  -0.0631 0.0238  182 ARG A C   
1566 O  O   . ARG A 181 ? 0.1615 0.1763 0.2018 0.0068  -0.0366 0.0307  182 ARG A O   
1567 C  CB  . ARG A 181 ? 0.1668 0.1845 0.2046 0.0141  -0.0318 0.0000  182 ARG A CB  
1568 C  CG  . ARG A 181 ? 0.1642 0.2004 0.2334 0.0104  -0.0005 -0.0092 182 ARG A CG  
1569 C  CD  . ARG A 181 ? 0.1756 0.2526 0.2428 0.0141  0.0342  0.0203  182 ARG A CD  
1570 N  NE  . ARG A 181 ? 0.2002 0.2108 0.2878 0.0051  -0.0166 0.0665  182 ARG A NE  
1571 C  CZ  . ARG A 181 ? 0.1941 0.2565 0.3172 0.0285  0.0348  0.0802  182 ARG A CZ  
1572 N  NH1 . ARG A 181 ? 0.2011 0.3542 0.4268 0.0754  0.0702  0.0908  182 ARG A NH1 
1573 N  NH2 . ARG A 181 ? 0.2219 0.3761 0.3312 0.0125  0.0151  0.1208  182 ARG A NH2 
1574 N  N   . GLY A 182 ? 0.1693 0.1781 0.1543 0.0217  -0.0573 0.0071  183 GLY A N   
1575 C  CA  . GLY A 182 ? 0.1941 0.1668 0.1870 0.0031  -0.0597 0.0038  183 GLY A CA  
1576 C  C   . GLY A 182 ? 0.1870 0.1483 0.2222 0.0164  -0.0744 0.0188  183 GLY A C   
1577 O  O   . GLY A 182 ? 0.2590 0.1634 0.2799 0.0073  -0.1150 -0.0013 183 GLY A O   
1578 N  N   . LEU A 183 ? 0.1765 0.1606 0.1550 0.0054  -0.0640 0.0063  184 LEU A N   
1579 C  CA  . LEU A 183 ? 0.1817 0.1282 0.1818 0.0237  -0.0511 -0.0076 184 LEU A CA  
1580 C  C   . LEU A 183 ? 0.1606 0.1500 0.1465 0.0027  -0.0533 0.0012  184 LEU A C   
1581 O  O   . LEU A 183 ? 0.1783 0.1886 0.1632 0.0140  -0.0480 0.0359  184 LEU A O   
1582 C  CB  . LEU A 183 ? 0.1844 0.1687 0.1296 0.0292  -0.0329 0.0087  184 LEU A CB  
1583 C  CG  . LEU A 183 ? 0.2127 0.1799 0.1597 0.0263  -0.0285 0.0232  184 LEU A CG  
1584 C  CD1 . LEU A 183 ? 0.1947 0.2967 0.1533 0.0586  -0.0151 0.0617  184 LEU A CD1 
1585 C  CD2 . LEU A 183 ? 0.2989 0.2153 0.1764 0.0449  -0.0274 -0.0281 184 LEU A CD2 
1586 N  N   A LEU A 184 ? 0.1823 0.1537 0.1641 -0.0031 -0.0241 0.0096  185 LEU A N   
1587 N  N   B LEU A 184 ? 0.1691 0.1720 0.1444 0.0087  -0.0549 0.0447  185 LEU A N   
1588 C  CA  A LEU A 184 ? 0.1307 0.1550 0.1799 -0.0148 -0.0071 0.0096  185 LEU A CA  
1589 C  CA  B LEU A 184 ? 0.1194 0.1342 0.1687 -0.0208 -0.0542 0.0175  185 LEU A CA  
1590 C  C   A LEU A 184 ? 0.1025 0.1360 0.1780 0.0228  -0.0230 -0.0003 185 LEU A C   
1591 C  C   B LEU A 184 ? 0.1694 0.1445 0.1315 -0.0225 -0.0160 0.0081  185 LEU A C   
1592 O  O   A LEU A 184 ? 0.1120 0.1491 0.1289 -0.0115 -0.0155 0.0098  185 LEU A O   
1593 O  O   B LEU A 184 ? 0.1588 0.1862 0.1493 -0.0241 -0.0331 0.0082  185 LEU A O   
1594 C  CB  A LEU A 184 ? 0.0744 0.1606 0.1904 -0.0085 -0.0140 0.0000  185 LEU A CB  
1595 C  CB  B LEU A 184 ? 0.1756 0.1500 0.1199 -0.0043 -0.0248 0.0281  185 LEU A CB  
1596 C  CG  A LEU A 184 ? 0.0952 0.1763 0.1860 -0.0208 0.0118  -0.0010 185 LEU A CG  
1597 C  CG  B LEU A 184 ? 0.1264 0.1580 0.1340 -0.0026 -0.0192 0.0113  185 LEU A CG  
1598 C  CD1 A LEU A 184 ? 0.1368 0.2320 0.1120 -0.0273 -0.0074 0.0043  185 LEU A CD1 
1599 C  CD1 B LEU A 184 ? 0.1479 0.1492 0.1720 -0.0003 0.0241  0.0516  185 LEU A CD1 
1600 C  CD2 A LEU A 184 ? 0.1142 0.1553 0.1800 -0.0142 -0.0035 -0.0098 185 LEU A CD2 
1601 C  CD2 B LEU A 184 ? 0.0973 0.1844 0.1660 0.0097  -0.0329 -0.0109 185 LEU A CD2 
1602 N  N   . PRO A 185 ? 0.1289 0.1726 0.1677 -0.0152 -0.0416 0.0252  186 PRO A N   
1603 C  CA  . PRO A 185 ? 0.1571 0.1676 0.1895 -0.0120 -0.0153 0.0505  186 PRO A CA  
1604 C  C   . PRO A 185 ? 0.1316 0.1484 0.2205 -0.0324 -0.0463 0.0350  186 PRO A C   
1605 O  O   . PRO A 185 ? 0.1097 0.1624 0.3273 -0.0198 -0.0640 0.0631  186 PRO A O   
1606 C  CB  . PRO A 185 ? 0.1347 0.1682 0.2026 0.0086  -0.0154 0.0450  186 PRO A CB  
1607 C  CG  . PRO A 185 ? 0.1212 0.1781 0.1623 0.0214  -0.0239 0.0141  186 PRO A CG  
1608 C  CD  . PRO A 185 ? 0.1203 0.1614 0.1457 0.0164  -0.0292 0.0140  186 PRO A CD  
1609 N  N   A GLU A 186 ? 0.1606 0.1756 0.2011 -0.0582 -0.0675 0.0163  187 GLU A N   
1610 N  N   B GLU A 186 ? 0.1509 0.1589 0.1879 -0.0174 -0.0251 0.0487  187 GLU A N   
1611 C  CA  A GLU A 186 ? 0.1045 0.1826 0.2529 -0.0412 -0.0644 -0.0076 187 GLU A CA  
1612 C  CA  B GLU A 186 ? 0.0992 0.1639 0.2048 -0.0203 0.0034  0.0027  187 GLU A CA  
1613 C  C   A GLU A 186 ? 0.1120 0.1720 0.2284 -0.0148 -0.0329 0.0093  187 GLU A C   
1614 C  C   B GLU A 186 ? 0.0636 0.1712 0.2090 -0.0113 -0.0010 0.0221  187 GLU A C   
1615 O  O   A GLU A 186 ? 0.0816 0.2343 0.2180 0.0164  -0.0023 0.0060  187 GLU A O   
1616 O  O   B GLU A 186 ? 0.1176 0.2372 0.1699 0.0421  0.0098  0.0194  187 GLU A O   
1617 C  CB  A GLU A 186 ? 0.1324 0.1939 0.1939 -0.0544 -0.0498 0.0177  187 GLU A CB  
1618 C  CB  B GLU A 186 ? 0.1465 0.2144 0.2658 -0.0978 -0.0171 -0.0135 187 GLU A CB  
1619 C  CG  A GLU A 186 ? 0.1634 0.2082 0.2489 0.0086  -0.0606 0.0177  187 GLU A CG  
1620 C  CG  B GLU A 186 ? 0.2000 0.2799 0.2338 -0.0904 -0.0623 0.0392  187 GLU A CG  
1621 C  CD  A GLU A 186 ? 0.1088 0.2745 0.3714 -0.0046 -0.0104 -0.0240 187 GLU A CD  
1622 C  CD  B GLU A 186 ? 0.2037 0.3384 0.3528 -0.1544 -0.0772 0.0012  187 GLU A CD  
1623 O  OE1 A GLU A 186 ? 0.2097 0.2529 0.3323 -0.0006 -0.0031 0.0027  187 GLU A OE1 
1624 O  OE1 B GLU A 186 ? 0.1977 0.2270 0.3046 -0.0412 -0.0091 0.0071  187 GLU A OE1 
1625 O  OE2 A GLU A 186 ? 0.2213 0.2422 0.3445 0.0461  0.0065  0.0961  187 GLU A OE2 
1626 O  OE2 B GLU A 186 ? 0.2734 0.3021 0.3851 -0.1084 -0.0961 -0.0137 187 GLU A OE2 
1627 N  N   . SER A 187 ? 0.0864 0.1844 0.2178 -0.0164 -0.0250 0.0272  188 SER A N   
1628 C  CA  . SER A 187 ? 0.1097 0.1808 0.2194 -0.0203 -0.0006 0.0186  188 SER A CA  
1629 C  C   . SER A 187 ? 0.0731 0.1914 0.2108 -0.0085 -0.0031 0.0209  188 SER A C   
1630 O  O   . SER A 187 ? 0.1034 0.2018 0.2090 -0.0228 -0.0020 0.0037  188 SER A O   
1631 C  CB  . SER A 187 ? 0.1342 0.2028 0.2169 -0.0177 -0.0109 0.0342  188 SER A CB  
1632 O  OG  . SER A 187 ? 0.1384 0.2195 0.2205 -0.0359 0.0017  0.0430  188 SER A OG  
1633 N  N   . LEU A 188 ? 0.0969 0.1668 0.2221 -0.0092 -0.0114 0.0118  189 LEU A N   
1634 C  CA  . LEU A 188 ? 0.0979 0.1674 0.2090 -0.0026 -0.0335 0.0003  189 LEU A CA  
1635 C  C   . LEU A 188 ? 0.0996 0.1650 0.1999 -0.0115 -0.0006 0.0006  189 LEU A C   
1636 O  O   . LEU A 188 ? 0.1246 0.1815 0.2104 -0.0154 -0.0197 -0.0130 189 LEU A O   
1637 C  CB  . LEU A 188 ? 0.1281 0.2185 0.2379 -0.0115 -0.0357 0.0076  189 LEU A CB  
1638 C  CG  . LEU A 188 ? 0.1066 0.2417 0.2777 0.0120  -0.0260 0.0746  189 LEU A CG  
1639 C  CD1 . LEU A 188 ? 0.2064 0.1995 0.3937 -0.0071 -0.0507 0.0988  189 LEU A CD1 
1640 C  CD2 . LEU A 188 ? 0.1333 0.3072 0.2522 -0.0043 -0.0148 0.0758  189 LEU A CD2 
1641 N  N   . ASP A 189 ? 0.0922 0.1789 0.1676 0.0057  0.0107  -0.0063 190 ASP A N   
1642 C  CA  . ASP A 189 ? 0.0847 0.2012 0.1788 -0.0285 0.0208  0.0082  190 ASP A CA  
1643 C  C   . ASP A 189 ? 0.1077 0.1366 0.1350 -0.0173 0.0054  -0.0049 190 ASP A C   
1644 O  O   . ASP A 189 ? 0.0925 0.1430 0.1439 -0.0104 0.0006  -0.0027 190 ASP A O   
1645 C  CB  . ASP A 189 ? 0.1158 0.2247 0.1867 -0.0535 0.0221  0.0242  190 ASP A CB  
1646 C  CG  . ASP A 189 ? 0.1939 0.3355 0.2205 -0.0815 0.0171  0.0274  190 ASP A CG  
1647 O  OD1 . ASP A 189 ? 0.1577 0.5467 0.2863 -0.0427 0.0820  -0.0337 190 ASP A OD1 
1648 O  OD2 . ASP A 189 ? 0.2292 0.5138 0.3294 -0.1752 0.0070  0.1124  190 ASP A OD2 
1649 N  N   . TYR A 190 ? 0.0876 0.1500 0.1395 -0.0082 0.0120  0.0146  191 TYR A N   
1650 C  CA  . TYR A 190 ? 0.0966 0.1472 0.1208 -0.0231 0.0071  0.0115  191 TYR A CA  
1651 C  C   . TYR A 190 ? 0.1022 0.1272 0.1174 -0.0097 0.0103  0.0093  191 TYR A C   
1652 O  O   . TYR A 190 ? 0.1122 0.1483 0.1050 -0.0003 0.0186  0.0052  191 TYR A O   
1653 C  CB  . TYR A 190 ? 0.1171 0.1272 0.1297 0.0005  -0.0068 0.0263  191 TYR A CB  
1654 C  CG  . TYR A 190 ? 0.0987 0.1350 0.1323 -0.0205 0.0031  0.0232  191 TYR A CG  
1655 C  CD1 . TYR A 190 ? 0.1158 0.1378 0.1395 -0.0102 0.0098  0.0140  191 TYR A CD1 
1656 C  CD2 . TYR A 190 ? 0.1280 0.1453 0.1342 -0.0063 0.0076  0.0174  191 TYR A CD2 
1657 C  CE1 . TYR A 190 ? 0.1272 0.1456 0.1588 -0.0076 0.0071  0.0217  191 TYR A CE1 
1658 C  CE2 . TYR A 190 ? 0.1084 0.1492 0.1781 -0.0052 -0.0027 0.0173  191 TYR A CE2 
1659 C  CZ  . TYR A 190 ? 0.1536 0.1219 0.1615 -0.0076 0.0140  0.0057  191 TYR A CZ  
1660 O  OH  . TYR A 190 ? 0.1536 0.1493 0.1852 0.0260  0.0024  -0.0130 191 TYR A OH  
1661 N  N   . TRP A 191 ? 0.0964 0.1172 0.1001 -0.0006 0.0087  0.0076  192 TRP A N   
1662 C  CA  . TRP A 191 ? 0.0966 0.1088 0.1124 -0.0093 0.0041  0.0120  192 TRP A CA  
1663 C  C   . TRP A 191 ? 0.0930 0.1217 0.0869 0.0054  0.0126  0.0027  192 TRP A C   
1664 O  O   . TRP A 191 ? 0.1185 0.1237 0.0947 -0.0219 0.0096  -0.0010 192 TRP A O   
1665 C  CB  . TRP A 191 ? 0.1115 0.1140 0.1052 -0.0080 0.0097  0.0063  192 TRP A CB  
1666 C  CG  . TRP A 191 ? 0.1034 0.1093 0.1124 0.0085  0.0063  0.0126  192 TRP A CG  
1667 C  CD1 . TRP A 191 ? 0.1571 0.1272 0.1272 0.0035  0.0219  0.0115  192 TRP A CD1 
1668 C  CD2 . TRP A 191 ? 0.0935 0.1149 0.1334 0.0115  -0.0041 0.0195  192 TRP A CD2 
1669 N  NE1 . TRP A 191 ? 0.1666 0.1246 0.1386 -0.0017 0.0080  0.0322  192 TRP A NE1 
1670 C  CE2 . TRP A 191 ? 0.1430 0.1307 0.1280 0.0070  -0.0012 0.0126  192 TRP A CE2 
1671 C  CE3 . TRP A 191 ? 0.0913 0.1384 0.1263 0.0093  -0.0070 -0.0065 192 TRP A CE3 
1672 C  CZ2 . TRP A 191 ? 0.1316 0.1221 0.1744 -0.0006 -0.0252 0.0068  192 TRP A CZ2 
1673 C  CZ3 . TRP A 191 ? 0.1005 0.1623 0.1580 0.0024  -0.0153 -0.0097 192 TRP A CZ3 
1674 C  CH2 . TRP A 191 ? 0.1332 0.1280 0.1915 0.0035  -0.0247 -0.0186 192 TRP A CH2 
1675 N  N   . THR A 192 ? 0.1018 0.1048 0.0913 -0.0052 0.0000  0.0051  193 THR A N   
1676 C  CA  . THR A 192 ? 0.0969 0.1076 0.1075 -0.0049 -0.0038 0.0085  193 THR A CA  
1677 C  C   . THR A 192 ? 0.0898 0.1115 0.0860 0.0115  0.0057  0.0038  193 THR A C   
1678 O  O   . THR A 192 ? 0.1092 0.1342 0.0856 0.0017  0.0040  0.0092  193 THR A O   
1679 C  CB  . THR A 192 ? 0.1246 0.1040 0.1066 0.0062  0.0068  0.0065  193 THR A CB  
1680 O  OG1 . THR A 192 ? 0.1061 0.1172 0.1190 0.0035  0.0057  0.0000  193 THR A OG1 
1681 C  CG2 . THR A 192 ? 0.1377 0.1387 0.1079 0.0175  0.0227  -0.0006 193 THR A CG2 
1682 N  N   . TYR A 193 ? 0.0921 0.1088 0.0960 0.0013  -0.0010 -0.0031 194 TYR A N   
1683 C  CA  . TYR A 193 ? 0.0952 0.1272 0.0913 -0.0024 -0.0074 0.0059  194 TYR A CA  
1684 C  C   . TYR A 193 ? 0.0886 0.1049 0.0935 0.0098  -0.0081 0.0000  194 TYR A C   
1685 O  O   . TYR A 193 ? 0.0970 0.1102 0.0922 0.0013  -0.0074 0.0015  194 TYR A O   
1686 C  CB  . TYR A 193 ? 0.1079 0.1208 0.0957 0.0131  0.0000  -0.0031 194 TYR A CB  
1687 C  CG  . TYR A 193 ? 0.1129 0.1023 0.1005 0.0102  -0.0146 0.0031  194 TYR A CG  
1688 C  CD1 . TYR A 193 ? 0.1027 0.0956 0.1030 0.0065  -0.0038 0.0068  194 TYR A CD1 
1689 C  CD2 . TYR A 193 ? 0.0988 0.1077 0.1158 0.0119  -0.0126 -0.0076 194 TYR A CD2 
1690 C  CE1 . TYR A 193 ? 0.0956 0.0956 0.1124 0.0126  -0.0082 0.0040  194 TYR A CE1 
1691 C  CE2 . TYR A 193 ? 0.0925 0.1005 0.1201 0.0109  -0.0076 0.0027  194 TYR A CE2 
1692 C  CZ  . TYR A 193 ? 0.0913 0.0970 0.1018 0.0126  -0.0093 -0.0015 194 TYR A CZ  
1693 O  OH  . TYR A 193 ? 0.0970 0.1032 0.1077 0.0076  0.0006  -0.0020 194 TYR A OH  
1694 N  N   . PRO A 194 ? 0.0969 0.1171 0.0908 0.0017  -0.0070 -0.0107 195 PRO A N   
1695 C  CA  . PRO A 194 ? 0.1061 0.1027 0.1181 0.0054  -0.0049 -0.0209 195 PRO A CA  
1696 C  C   . PRO A 194 ? 0.0819 0.0974 0.1040 0.0006  -0.0120 -0.0046 195 PRO A C   
1697 O  O   . PRO A 194 ? 0.1129 0.1176 0.0966 0.0153  -0.0097 -0.0035 195 PRO A O   
1698 C  CB  . PRO A 194 ? 0.1351 0.1280 0.1142 -0.0147 -0.0003 -0.0184 195 PRO A CB  
1699 C  CG  . PRO A 194 ? 0.1419 0.1471 0.1272 -0.0093 -0.0114 -0.0306 195 PRO A CG  
1700 C  CD  . PRO A 194 ? 0.1261 0.1598 0.0939 -0.0186 -0.0113 -0.0176 195 PRO A CD  
1701 N  N   . GLY A 195 ? 0.0908 0.0960 0.1052 0.0013  -0.0049 -0.0120 196 GLY A N   
1702 C  CA  . GLY A 195 ? 0.0952 0.1111 0.0983 0.0102  0.0000  -0.0012 196 GLY A CA  
1703 C  C   . GLY A 195 ? 0.0683 0.0922 0.1111 -0.0081 -0.0087 -0.0065 196 GLY A C   
1704 O  O   . GLY A 195 ? 0.0938 0.0904 0.1124 -0.0006 -0.0065 -0.0051 196 GLY A O   
1705 N  N   . SER A 196 ? 0.0820 0.0995 0.0957 0.0031  -0.0043 -0.0131 197 SER A N   
1706 C  CA  . SER A 196 ? 0.0618 0.1104 0.1111 -0.0049 0.0076  -0.0015 197 SER A CA  
1707 C  C   . SER A 196 ? 0.0731 0.0864 0.1106 0.0024  -0.0031 -0.0026 197 SER A C   
1708 O  O   . SER A 196 ? 0.0794 0.0988 0.1054 -0.0093 0.0006  -0.0104 197 SER A O   
1709 C  CB  . SER A 196 ? 0.0829 0.1009 0.1203 -0.0107 0.0013  -0.0114 197 SER A CB  
1710 O  OG  . SER A 196 ? 0.0754 0.1017 0.1228 0.0006  -0.0043 -0.0057 197 SER A OG  
1711 N  N   . LEU A 197 ? 0.0759 0.0925 0.1095 0.0000  0.0076  -0.0054 198 LEU A N   
1712 C  CA  . LEU A 197 ? 0.0899 0.1017 0.1014 -0.0031 0.0043  -0.0162 198 LEU A CA  
1713 C  C   . LEU A 197 ? 0.0812 0.0983 0.1133 -0.0082 0.0017  -0.0051 198 LEU A C   
1714 O  O   . LEU A 197 ? 0.0816 0.1115 0.1235 -0.0006 -0.0026 -0.0126 198 LEU A O   
1715 C  CB  . LEU A 197 ? 0.0922 0.1032 0.1185 -0.0142 0.0148  -0.0010 198 LEU A CB  
1716 C  CG  . LEU A 197 ? 0.0996 0.1119 0.1221 -0.0082 0.0057  -0.0020 198 LEU A CG  
1717 C  CD1 . LEU A 197 ? 0.1149 0.1206 0.1546 -0.0263 0.0060  0.0188  198 LEU A CD1 
1718 C  CD2 . LEU A 197 ? 0.1110 0.1162 0.1428 0.0057  0.0109  0.0104  198 LEU A CD2 
1719 N  N   . THR A 198 ? 0.0828 0.0900 0.1095 0.0005  0.0000  -0.0093 199 THR A N   
1720 C  CA  . THR A 198 ? 0.0885 0.0974 0.1244 -0.0087 0.0054  -0.0063 199 THR A CA  
1721 C  C   . THR A 198 ? 0.0710 0.1004 0.1325 -0.0024 -0.0065 -0.0026 199 THR A C   
1722 O  O   . THR A 198 ? 0.0841 0.1129 0.1456 -0.0043 0.0104  -0.0098 199 THR A O   
1723 C  CB  . THR A 198 ? 0.0929 0.0996 0.1106 -0.0113 -0.0059 -0.0057 199 THR A CB  
1724 O  OG1 . THR A 198 ? 0.0970 0.1009 0.1049 -0.0054 -0.0038 -0.0015 199 THR A OG1 
1725 C  CG2 . THR A 198 ? 0.0960 0.1158 0.1146 -0.0065 0.0164  0.0043  199 THR A CG2 
1726 N  N   . THR A 199 ? 0.0992 0.1201 0.1226 -0.0153 0.0142  -0.0087 200 THR A N   
1727 C  CA  . THR A 199 ? 0.0803 0.1147 0.1430 -0.0186 0.0252  -0.0186 200 THR A CA  
1728 C  C   . THR A 199 ? 0.0939 0.1279 0.1333 -0.0181 0.0175  -0.0164 200 THR A C   
1729 O  O   . THR A 199 ? 0.0995 0.1253 0.1449 -0.0219 0.0187  -0.0186 200 THR A O   
1730 C  CB  . THR A 199 ? 0.1031 0.1333 0.1185 -0.0043 0.0136  0.0000  200 THR A CB  
1731 O  OG1 . THR A 199 ? 0.1367 0.1444 0.1393 0.0015  0.0115  -0.0048 200 THR A OG1 
1732 C  CG2 . THR A 199 ? 0.1351 0.1490 0.1492 -0.0361 0.0092  -0.0082 200 THR A CG2 
1733 N  N   . PRO A 200 ? 0.1049 0.1333 0.1553 -0.0307 0.0217  -0.0102 201 PRO A N   
1734 C  CA  . PRO A 200 ? 0.1054 0.1473 0.1639 -0.0351 0.0131  -0.0035 201 PRO A CA  
1735 C  C   . PRO A 200 ? 0.1185 0.1542 0.1551 -0.0318 0.0153  -0.0035 201 PRO A C   
1736 O  O   . PRO A 200 ? 0.1615 0.1817 0.1682 -0.0263 0.0043  0.0010  201 PRO A O   
1737 C  CB  . PRO A 200 ? 0.1097 0.1826 0.1835 -0.0447 0.0296  -0.0065 201 PRO A CB  
1738 C  CG  . PRO A 200 ? 0.1004 0.1826 0.1923 -0.0186 0.0344  -0.0153 201 PRO A CG  
1739 C  CD  . PRO A 200 ? 0.1050 0.1553 0.1580 -0.0185 0.0307  -0.0274 201 PRO A CD  
1740 N  N   . PRO A 201 ? 0.1163 0.1509 0.1588 -0.0240 0.0237  -0.0037 202 PRO A N   
1741 C  CA  . PRO A 201 ? 0.1352 0.1359 0.1474 -0.0392 0.0060  -0.0010 202 PRO A CA  
1742 C  C   . PRO A 201 ? 0.1061 0.1374 0.1632 -0.0038 0.0020  -0.0010 202 PRO A C   
1743 O  O   . PRO A 201 ? 0.1142 0.1431 0.1685 -0.0247 0.0054  -0.0048 202 PRO A O   
1744 C  CB  . PRO A 201 ? 0.1641 0.1498 0.2196 -0.0373 0.0331  0.0183  202 PRO A CB  
1745 C  CG  . PRO A 201 ? 0.2100 0.1395 0.2415 -0.0177 -0.0108 0.0177  202 PRO A CG  
1746 C  CD  . PRO A 201 ? 0.1676 0.1511 0.1835 0.0131  0.0103  0.0164  202 PRO A CD  
1747 N  N   . LEU A 202 ? 0.0899 0.1077 0.1570 -0.0126 0.0203  0.0052  203 LEU A N   
1748 C  CA  . LEU A 202 ? 0.0868 0.1097 0.1544 -0.0081 -0.0037 -0.0131 203 LEU A CA  
1749 C  C   . LEU A 202 ? 0.0869 0.1185 0.1393 -0.0151 0.0030  0.0010  203 LEU A C   
1750 O  O   . LEU A 202 ? 0.0869 0.1070 0.1412 -0.0049 -0.0046 -0.0126 203 LEU A O   
1751 C  CB  . LEU A 202 ? 0.0878 0.1111 0.1606 -0.0020 -0.0012 -0.0141 203 LEU A CB  
1752 C  CG  . LEU A 202 ? 0.0776 0.1212 0.1615 0.0082  -0.0003 -0.0152 203 LEU A CG  
1753 C  CD1 . LEU A 202 ? 0.0851 0.1421 0.2117 -0.0017 0.0102  -0.0136 203 LEU A CD1 
1754 C  CD2 . LEU A 202 ? 0.0781 0.1378 0.1897 -0.0082 -0.0082 -0.0203 203 LEU A CD2 
1755 N  N   . LEU A 203 ? 0.0891 0.1045 0.1588 -0.0035 0.0027  -0.0026 204 LEU A N   
1756 C  CA  . LEU A 203 ? 0.0838 0.1018 0.1738 -0.0076 0.0113  -0.0031 204 LEU A CA  
1757 C  C   . LEU A 203 ? 0.0960 0.0925 0.1594 0.0026  0.0017  -0.0109 204 LEU A C   
1758 O  O   . LEU A 203 ? 0.0961 0.1018 0.1348 -0.0130 -0.0115 -0.0115 204 LEU A O   
1759 C  CB  . LEU A 203 ? 0.1115 0.1133 0.1949 -0.0080 0.0109  0.0015  204 LEU A CB  
1760 C  CG  . LEU A 203 ? 0.1335 0.1333 0.2230 0.0010  0.0395  0.0263  204 LEU A CG  
1761 C  CD1 . LEU A 203 ? 0.1966 0.1263 0.2493 0.0186  0.0527  0.0293  204 LEU A CD1 
1762 C  CD2 . LEU A 203 ? 0.1268 0.1816 0.4020 -0.0644 0.0215  0.0487  204 LEU A CD2 
1763 N  N   . GLU A 204 ? 0.0916 0.1172 0.1641 -0.0104 -0.0043 -0.0241 205 GLU A N   
1764 C  CA  . GLU A 204 ? 0.1066 0.1228 0.1402 0.0046  -0.0163 -0.0252 205 GLU A CA  
1765 C  C   . GLU A 204 ? 0.1095 0.1043 0.1438 -0.0098 -0.0274 -0.0318 205 GLU A C   
1766 O  O   . GLU A 204 ? 0.1333 0.1604 0.1605 0.0242  -0.0377 -0.0463 205 GLU A O   
1767 C  CB  . GLU A 204 ? 0.1358 0.1422 0.1474 0.0142  -0.0395 -0.0186 205 GLU A CB  
1768 C  CG  . GLU A 204 ? 0.1246 0.1393 0.1805 0.0057  -0.0408 -0.0337 205 GLU A CG  
1769 C  CD  . GLU A 204 ? 0.1367 0.1474 0.1546 -0.0071 -0.0236 -0.0302 205 GLU A CD  
1770 O  OE1 . GLU A 204 ? 0.1500 0.1738 0.2258 0.0120  -0.0762 -0.0454 205 GLU A OE1 
1771 O  OE2 . GLU A 204 ? 0.1307 0.1559 0.1685 -0.0071 -0.0315 -0.0186 205 GLU A OE2 
1772 N  N   . CYS A 205 ? 0.0904 0.0979 0.1412 -0.0120 -0.0109 -0.0104 206 CYS A N   
1773 C  CA  . CYS A 205 ? 0.0922 0.0991 0.1419 0.0071  -0.0185 0.0052  206 CYS A CA  
1774 C  C   . CYS A 205 ? 0.0864 0.1023 0.1351 0.0070  -0.0154 -0.0109 206 CYS A C   
1775 O  O   . CYS A 205 ? 0.1158 0.1005 0.1736 0.0082  -0.0304 0.0038  206 CYS A O   
1776 C  CB  . CYS A 205 ? 0.1198 0.1031 0.1474 -0.0153 0.0082  0.0020  206 CYS A CB  
1777 S  SG  . CYS A 205 ? 0.1411 0.1154 0.1412 0.0005  -0.0097 -0.0043 206 CYS A SG  
1778 N  N   . VAL A 206 ? 0.0926 0.0886 0.1194 -0.0043 -0.0082 -0.0015 207 VAL A N   
1779 C  CA  . VAL A 206 ? 0.0877 0.0873 0.1172 -0.0048 -0.0087 0.0012  207 VAL A CA  
1780 C  C   . VAL A 206 ? 0.0939 0.0868 0.1097 0.0076  -0.0147 0.0030  207 VAL A C   
1781 O  O   . VAL A 206 ? 0.0996 0.1124 0.1296 0.0034  -0.0141 0.0186  207 VAL A O   
1782 C  CB  . VAL A 206 ? 0.0957 0.0929 0.1228 -0.0003 0.0034  -0.0035 207 VAL A CB  
1783 C  CG1 . VAL A 206 ? 0.0882 0.1036 0.1322 -0.0043 -0.0125 -0.0052 207 VAL A CG1 
1784 C  CG2 . VAL A 206 ? 0.1034 0.1198 0.1330 0.0026  0.0153  -0.0120 207 VAL A CG2 
1785 N  N   . THR A 207 ? 0.0828 0.0898 0.1043 0.0027  -0.0049 -0.0006 208 THR A N   
1786 C  CA  . THR A 207 ? 0.0987 0.0986 0.1092 0.0057  0.0006  -0.0031 208 THR A CA  
1787 C  C   . THR A 207 ? 0.0810 0.0957 0.0987 -0.0060 -0.0013 -0.0031 208 THR A C   
1788 O  O   . THR A 207 ? 0.1005 0.0983 0.1077 0.0000  -0.0181 0.0017  208 THR A O   
1789 C  CB  . THR A 207 ? 0.1088 0.0996 0.1185 -0.0013 0.0034  -0.0159 208 THR A CB  
1790 O  OG1 . THR A 207 ? 0.1314 0.1131 0.1212 0.0041  0.0049  -0.0135 208 THR A OG1 
1791 C  CG2 . THR A 207 ? 0.1254 0.1237 0.1356 -0.0163 0.0175  0.0068  208 THR A CG2 
1792 N  N   . TRP A 208 ? 0.0798 0.0832 0.0961 0.0040  -0.0015 0.0000  209 TRP A N   
1793 C  CA  . TRP A 208 ? 0.0890 0.0785 0.0983 0.0000  -0.0082 0.0006  209 TRP A CA  
1794 C  C   . TRP A 208 ? 0.0850 0.0793 0.0878 0.0026  0.0003  0.0020  209 TRP A C   
1795 O  O   . TRP A 208 ? 0.0920 0.1025 0.0886 -0.0052 0.0041  0.0015  209 TRP A O   
1796 C  CB  . TRP A 208 ? 0.0825 0.0948 0.0952 0.0027  -0.0023 0.0010  209 TRP A CB  
1797 C  CG  . TRP A 208 ? 0.0806 0.0864 0.1001 0.0129  -0.0074 0.0035  209 TRP A CG  
1798 C  CD1 . TRP A 208 ? 0.0907 0.0895 0.1097 0.0049  -0.0082 0.0031  209 TRP A CD1 
1799 C  CD2 . TRP A 208 ? 0.0772 0.0731 0.1054 0.0063  0.0013  0.0000  209 TRP A CD2 
1800 N  NE1 . TRP A 208 ? 0.0810 0.1018 0.1124 -0.0003 0.0015  0.0049  209 TRP A NE1 
1801 C  CE2 . TRP A 208 ? 0.0904 0.0812 0.1092 0.0041  -0.0091 0.0082  209 TRP A CE2 
1802 C  CE3 . TRP A 208 ? 0.0864 0.0798 0.0961 0.0046  -0.0076 0.0040  209 TRP A CE3 
1803 C  CZ2 . TRP A 208 ? 0.0930 0.1001 0.1088 0.0241  0.0076  0.0030  209 TRP A CZ2 
1804 C  CZ3 . TRP A 208 ? 0.1146 0.1005 0.1036 0.0082  0.0006  0.0060  209 TRP A CZ3 
1805 C  CH2 . TRP A 208 ? 0.1194 0.1043 0.1115 0.0199  0.0087  0.0048  209 TRP A CH2 
1806 N  N   . ILE A 209 ? 0.0731 0.0850 0.1050 -0.0049 -0.0034 -0.0006 210 ILE A N   
1807 C  CA  . ILE A 209 ? 0.0825 0.0935 0.1045 -0.0041 0.0013  -0.0027 210 ILE A CA  
1808 C  C   . ILE A 209 ? 0.0759 0.0943 0.0851 -0.0020 0.0013  0.0035  210 ILE A C   
1809 O  O   . ILE A 209 ? 0.1199 0.1030 0.0966 -0.0027 0.0000  0.0024  210 ILE A O   
1810 C  CB  . ILE A 209 ? 0.0776 0.0956 0.1280 0.0010  -0.0037 0.0049  210 ILE A CB  
1811 C  CG1 . ILE A 209 ? 0.0965 0.1102 0.1703 0.0065  -0.0175 -0.0196 210 ILE A CG1 
1812 C  CG2 . ILE A 209 ? 0.0842 0.1325 0.1595 0.0131  -0.0048 0.0073  210 ILE A CG2 
1813 C  CD1 . ILE A 209 ? 0.1120 0.1093 0.2313 0.0294  0.0027  0.0108  210 ILE A CD1 
1814 N  N   . VAL A 210 ? 0.0732 0.0847 0.1106 -0.0063 0.0017  0.0052  211 VAL A N   
1815 C  CA  . VAL A 210 ? 0.0763 0.0864 0.1010 0.0000  0.0005  0.0015  211 VAL A CA  
1816 C  C   . VAL A 210 ? 0.0838 0.0895 0.0926 0.0062  0.0015  0.0076  211 VAL A C   
1817 O  O   . VAL A 210 ? 0.0974 0.1104 0.0969 -0.0063 0.0010  0.0093  211 VAL A O   
1818 C  CB  . VAL A 210 ? 0.0828 0.1088 0.1156 -0.0040 0.0035  0.0027  211 VAL A CB  
1819 C  CG1 . VAL A 210 ? 0.1155 0.0961 0.1368 0.0030  -0.0059 0.0031  211 VAL A CG1 
1820 C  CG2 . VAL A 210 ? 0.0934 0.1093 0.1465 -0.0013 -0.0006 0.0010  211 VAL A CG2 
1821 N  N   . LEU A 211 ? 0.0855 0.1176 0.1014 -0.0052 -0.0013 0.0020  212 LEU A N   
1822 C  CA  . LEU A 211 ? 0.0763 0.1185 0.1237 -0.0159 -0.0038 -0.0041 212 LEU A CA  
1823 C  C   . LEU A 211 ? 0.0793 0.1129 0.1115 -0.0057 -0.0041 -0.0003 212 LEU A C   
1824 O  O   . LEU A 211 ? 0.0988 0.1208 0.1251 -0.0120 -0.0041 0.0057  212 LEU A O   
1825 C  CB  . LEU A 211 ? 0.0882 0.1246 0.1351 -0.0120 -0.0137 0.0146  212 LEU A CB  
1826 C  CG  . LEU A 211 ? 0.0926 0.1335 0.1499 -0.0065 -0.0120 0.0174  212 LEU A CG  
1827 C  CD1 . LEU A 211 ? 0.0995 0.1967 0.1729 -0.0131 -0.0412 0.0308  212 LEU A CD1 
1828 C  CD2 . LEU A 211 ? 0.1298 0.1553 0.1483 0.0041  0.0013  0.0031  212 LEU A CD2 
1829 N  N   . LYS A 212 ? 0.0898 0.1246 0.1273 -0.0210 -0.0049 0.0173  213 LYS A N   
1830 C  CA  . LYS A 212 ? 0.1221 0.1289 0.1255 -0.0166 -0.0006 0.0197  213 LYS A CA  
1831 C  C   . LYS A 212 ? 0.0979 0.1111 0.1412 -0.0115 -0.0052 0.0153  213 LYS A C   
1832 O  O   . LYS A 212 ? 0.1208 0.1386 0.1787 -0.0046 -0.0335 0.0164  213 LYS A O   
1833 C  CB  . LYS A 212 ? 0.1586 0.1703 0.1471 -0.0516 0.0186  0.0272  213 LYS A CB  
1834 C  CG  . LYS A 212 ? 0.1941 0.1930 0.1743 -0.0258 -0.0098 0.0384  213 LYS A CG  
1835 C  CD  . LYS A 212 ? 0.4573 0.3039 0.1729 -0.1404 0.0285  0.0679  213 LYS A CD  
1836 C  CE  . LYS A 212 ? 0.5461 0.3424 0.2368 -0.0208 0.0825  0.0986  213 LYS A CE  
1837 N  NZ  . LYS A 212 ? 0.7099 0.4842 0.3542 -0.0425 0.1544  0.0500  213 LYS A NZ  
1838 N  N   . GLU A 213 ? 0.1018 0.1278 0.1313 -0.0057 -0.0070 0.0182  214 GLU A N   
1839 C  CA  . GLU A 213 ? 0.1025 0.1304 0.1414 -0.0226 -0.0187 0.0060  214 GLU A CA  
1840 C  C   . GLU A 213 ? 0.0982 0.1113 0.1351 -0.0152 -0.0154 0.0080  214 GLU A C   
1841 O  O   . GLU A 213 ? 0.0951 0.1158 0.1412 -0.0049 -0.0109 0.0164  214 GLU A O   
1842 C  CB  . GLU A 213 ? 0.1005 0.1465 0.1553 -0.0219 -0.0163 0.0082  214 GLU A CB  
1843 C  CG  . GLU A 213 ? 0.1158 0.1985 0.1976 -0.0210 -0.0335 0.0031  214 GLU A CG  
1844 C  CD  . GLU A 213 ? 0.1632 0.2656 0.2019 -0.0518 -0.0364 -0.0161 214 GLU A CD  
1845 O  OE1 . GLU A 213 ? 0.1370 0.1852 0.3072 -0.0230 -0.0533 0.0154  214 GLU A OE1 
1846 O  OE2 . GLU A 213 ? 0.2540 0.3610 0.4161 -0.0417 -0.0925 -0.0644 214 GLU A OE2 
1847 N  N   A PRO A 214 ? 0.1158 0.1128 0.1210 -0.0098 -0.0137 0.0120  215 PRO A N   
1848 N  N   B PRO A 214 ? 0.1164 0.1181 0.1306 -0.0003 -0.0172 0.0124  215 PRO A N   
1849 C  CA  A PRO A 214 ? 0.1142 0.1212 0.1217 -0.0046 -0.0109 0.0068  215 PRO A CA  
1850 C  CA  B PRO A 214 ? 0.1203 0.1228 0.1387 -0.0109 -0.0119 0.0006  215 PRO A CA  
1851 C  C   A PRO A 214 ? 0.1049 0.1156 0.1351 -0.0051 -0.0208 -0.0153 215 PRO A C   
1852 C  C   B PRO A 214 ? 0.1252 0.1167 0.1393 -0.0188 -0.0187 -0.0081 215 PRO A C   
1853 O  O   A PRO A 214 ? 0.1050 0.1412 0.1444 -0.0043 -0.0164 -0.0109 215 PRO A O   
1854 O  O   B PRO A 214 ? 0.1286 0.1272 0.1632 -0.0240 -0.0252 -0.0124 215 PRO A O   
1855 C  CB  A PRO A 214 ? 0.1111 0.0979 0.1508 -0.0131 -0.0120 0.0049  215 PRO A CB  
1856 C  CB  B PRO A 214 ? 0.1405 0.1061 0.1922 -0.0010 -0.0164 -0.0038 215 PRO A CB  
1857 C  CG  A PRO A 214 ? 0.1023 0.1057 0.1745 -0.0232 -0.0208 -0.0142 215 PRO A CG  
1858 C  CG  B PRO A 214 ? 0.2055 0.2011 0.2131 0.0087  0.0507  -0.0108 215 PRO A CG  
1859 C  CD  A PRO A 214 ? 0.1508 0.1043 0.1439 -0.0231 -0.0238 -0.0164 215 PRO A CD  
1860 C  CD  B PRO A 214 ? 0.1492 0.0948 0.1862 -0.0313 0.0285  0.0252  215 PRO A CD  
1861 N  N   . ILE A 215 ? 0.1234 0.1224 0.1190 -0.0038 -0.0208 -0.0081 216 ILE A N   
1862 C  CA  . ILE A 215 ? 0.1392 0.1171 0.1430 -0.0049 -0.0340 -0.0115 216 ILE A CA  
1863 C  C   . ILE A 215 ? 0.1149 0.1264 0.1446 -0.0043 -0.0232 -0.0153 216 ILE A C   
1864 O  O   . ILE A 215 ? 0.1230 0.1167 0.1783 -0.0104 -0.0209 -0.0241 216 ILE A O   
1865 C  CB  . ILE A 215 ? 0.1491 0.1194 0.1523 0.0006  -0.0274 -0.0113 216 ILE A CB  
1866 C  CG1 . ILE A 215 ? 0.1843 0.1423 0.1357 -0.0024 -0.0412 0.0000  216 ILE A CG1 
1867 C  CG2 . ILE A 215 ? 0.1754 0.1466 0.1552 0.0184  -0.0263 -0.0243 216 ILE A CG2 
1868 C  CD1 . ILE A 215 ? 0.2485 0.1331 0.1588 -0.0006 -0.0243 0.0171  216 ILE A CD1 
1869 N  N   A SER A 216 ? 0.1174 0.1404 0.1174 -0.0082 -0.0131 0.0035  217 SER A N   
1870 N  N   B SER A 216 ? 0.1435 0.0992 0.1571 -0.0087 -0.0379 -0.0131 217 SER A N   
1871 C  CA  A SER A 216 ? 0.1597 0.1368 0.1586 -0.0142 -0.0174 -0.0274 217 SER A CA  
1872 C  CA  B SER A 216 ? 0.1435 0.1074 0.1235 -0.0060 -0.0425 -0.0208 217 SER A CA  
1873 C  C   A SER A 216 ? 0.1615 0.1147 0.1650 -0.0048 -0.0054 -0.0142 217 SER A C   
1874 C  C   B SER A 216 ? 0.1395 0.1076 0.1342 -0.0086 -0.0491 -0.0164 217 SER A C   
1875 O  O   A SER A 216 ? 0.1375 0.1536 0.1430 -0.0096 0.0172  0.0043  217 SER A O   
1876 O  O   B SER A 216 ? 0.1509 0.1234 0.1167 -0.0035 -0.0306 0.0219  217 SER A O   
1877 C  CB  A SER A 216 ? 0.1967 0.1405 0.2386 -0.0076 0.0259  0.0098  217 SER A CB  
1878 C  CB  B SER A 216 ? 0.2080 0.0775 0.1342 -0.0226 -0.0049 0.0003  217 SER A CB  
1879 O  OG  A SER A 216 ? 0.2996 0.1922 0.2486 -0.0549 0.0049  -0.0131 217 SER A OG  
1880 O  OG  B SER A 216 ? 0.2011 0.1493 0.1507 -0.0458 0.0000  0.0126  217 SER A OG  
1881 N  N   . VAL A 217 ? 0.1562 0.1111 0.1483 -0.0165 -0.0230 -0.0193 218 VAL A N   
1882 C  CA  . VAL A 217 ? 0.1932 0.1061 0.1299 -0.0098 -0.0087 -0.0153 218 VAL A CA  
1883 C  C   . VAL A 217 ? 0.1606 0.1070 0.1471 -0.0163 -0.0219 -0.0076 218 VAL A C   
1884 O  O   . VAL A 217 ? 0.1788 0.1129 0.1506 -0.0238 -0.0241 -0.0153 218 VAL A O   
1885 C  CB  . VAL A 217 ? 0.1563 0.0988 0.1871 -0.0097 -0.0353 -0.0115 218 VAL A CB  
1886 C  CG1 . VAL A 217 ? 0.2353 0.1165 0.1700 -0.0151 -0.0421 -0.0136 218 VAL A CG1 
1887 C  CG2 . VAL A 217 ? 0.1623 0.1212 0.2166 -0.0192 -0.0154 -0.0196 218 VAL A CG2 
1888 N  N   . SER A 218 ? 0.1694 0.1138 0.1385 -0.0126 -0.0193 -0.0276 219 SER A N   
1889 C  CA  . SER A 218 ? 0.1826 0.1128 0.1536 -0.0115 -0.0285 -0.0166 219 SER A CA  
1890 C  C   . SER A 218 ? 0.1941 0.0944 0.1527 -0.0199 -0.0197 -0.0208 219 SER A C   
1891 O  O   . SER A 218 ? 0.1916 0.1129 0.1625 -0.0131 -0.0214 -0.0142 219 SER A O   
1892 C  CB  . SER A 218 ? 0.1904 0.1255 0.1518 -0.0052 -0.0263 -0.0054 219 SER A CB  
1893 O  OG  . SER A 218 ? 0.2055 0.1518 0.1641 -0.0153 -0.0296 -0.0186 219 SER A OG  
1894 N  N   A SER A 219 ? 0.1906 0.1005 0.1806 -0.0252 -0.0322 -0.0146 220 SER A N   
1895 N  N   B SER A 219 ? 0.1772 0.1034 0.1877 -0.0093 -0.0037 0.0013  220 SER A N   
1896 C  CA  A SER A 219 ? 0.2108 0.1133 0.2037 -0.0368 -0.0186 0.0114  220 SER A CA  
1897 C  CA  B SER A 219 ? 0.1932 0.1095 0.1651 0.0093  -0.0221 -0.0046 220 SER A CA  
1898 C  C   A SER A 219 ? 0.2052 0.1272 0.2073 -0.0135 -0.0197 0.0017  220 SER A C   
1899 C  C   B SER A 219 ? 0.2169 0.1216 0.1518 -0.0269 -0.0126 -0.0397 220 SER A C   
1900 O  O   A SER A 219 ? 0.2231 0.1158 0.2257 -0.0308 0.0340  0.0006  220 SER A O   
1901 O  O   B SER A 219 ? 0.1729 0.1718 0.1553 0.0020  -0.0153 -0.0063 220 SER A O   
1902 C  CB  A SER A 219 ? 0.2170 0.1430 0.2522 0.0065  0.0082  0.0364  220 SER A CB  
1903 C  CB  B SER A 219 ? 0.1993 0.1312 0.1613 -0.0230 -0.0087 -0.0241 220 SER A CB  
1904 O  OG  A SER A 219 ? 0.2630 0.1544 0.2395 0.0175  -0.0023 -0.0087 220 SER A OG  
1905 O  OG  B SER A 219 ? 0.2053 0.1357 0.1981 0.0027  -0.0225 -0.0151 220 SER A OG  
1906 N  N   . GLU A 220 ? 0.2020 0.1237 0.1606 -0.0142 -0.0076 -0.0184 221 GLU A N   
1907 C  CA  . GLU A 220 ? 0.2486 0.1544 0.1703 -0.0164 -0.0119 -0.0328 221 GLU A CA  
1908 C  C   . GLU A 220 ? 0.2309 0.1395 0.1597 0.0041  -0.0027 -0.0035 221 GLU A C   
1909 O  O   . GLU A 220 ? 0.2397 0.1665 0.1632 -0.0086 0.0275  -0.0135 221 GLU A O   
1910 C  CB  . GLU A 220 ? 0.3330 0.1788 0.1905 -0.0175 -0.0542 -0.0540 221 GLU A CB  
1911 C  CG  . GLU A 220 ? 0.4128 0.2240 0.2745 -0.0243 -0.0922 -0.0661 221 GLU A CG  
1912 C  CD  . GLU A 220 ? 0.4253 0.2331 0.2856 -0.0833 -0.0401 -0.1177 221 GLU A CD  
1913 O  OE1 . GLU A 220 ? 0.3916 0.2356 0.3305 -0.1128 0.0337  -0.0926 221 GLU A OE1 
1914 O  OE2 . GLU A 220 ? 0.8093 0.2694 0.4645 -0.2187 0.0209  -0.1500 221 GLU A OE2 
1915 N  N   . GLN A 221 ? 0.1976 0.1298 0.1590 -0.0052 -0.0161 -0.0129 222 GLN A N   
1916 C  CA  . GLN A 221 ? 0.2166 0.1237 0.1580 -0.0203 -0.0043 -0.0104 222 GLN A CA  
1917 C  C   . GLN A 221 ? 0.1851 0.1386 0.1453 -0.0120 -0.0071 0.0159  222 GLN A C   
1918 O  O   . GLN A 221 ? 0.2134 0.1480 0.1480 -0.0131 -0.0031 0.0115  222 GLN A O   
1919 C  CB  . GLN A 221 ? 0.1755 0.1324 0.1421 -0.0087 -0.0264 -0.0186 222 GLN A CB  
1920 C  CG  . GLN A 221 ? 0.2043 0.1439 0.1421 -0.0241 -0.0287 -0.0113 222 GLN A CG  
1921 C  CD  . GLN A 221 ? 0.1879 0.1158 0.1418 -0.0131 -0.0205 -0.0130 222 GLN A CD  
1922 O  OE1 . GLN A 221 ? 0.1893 0.1244 0.1474 0.0000  -0.0152 -0.0015 222 GLN A OE1 
1923 N  NE2 . GLN A 221 ? 0.1843 0.1270 0.1731 -0.0080 -0.0394 0.0010  222 GLN A NE2 
1924 N  N   A VAL A 222 ? 0.1861 0.1361 0.1277 -0.0020 -0.0285 -0.0098 223 VAL A N   
1925 N  N   B VAL A 222 ? 0.1951 0.1430 0.1498 -0.0162 -0.0043 0.0241  223 VAL A N   
1926 C  CA  A VAL A 222 ? 0.1605 0.1490 0.1615 -0.0086 -0.0230 0.0252  223 VAL A CA  
1927 C  CA  B VAL A 222 ? 0.1878 0.1747 0.1465 -0.0060 -0.0174 0.0027  223 VAL A CA  
1928 C  C   A VAL A 222 ? 0.1792 0.1324 0.1694 -0.0237 -0.0070 0.0238  223 VAL A C   
1929 C  C   B VAL A 222 ? 0.2098 0.1534 0.1528 0.0024  0.0000  0.0000  223 VAL A C   
1930 O  O   A VAL A 222 ? 0.1413 0.1594 0.1497 -0.0092 0.0026  0.0164  223 VAL A O   
1931 O  O   B VAL A 222 ? 0.2108 0.1289 0.1958 -0.0151 0.0051  -0.0080 223 VAL A O   
1932 C  CB  A VAL A 222 ? 0.1242 0.1571 0.1586 -0.0098 -0.0020 0.0259  223 VAL A CB  
1933 C  CB  B VAL A 222 ? 0.2214 0.2222 0.1492 0.0142  0.0076  0.0141  223 VAL A CB  
1934 C  CG1 A VAL A 222 ? 0.1527 0.1457 0.1826 -0.0392 -0.0197 0.0601  223 VAL A CG1 
1935 C  CG1 B VAL A 222 ? 0.2274 0.1668 0.1555 0.0098  0.0046  0.0129  223 VAL A CG1 
1936 C  CG2 A VAL A 222 ? 0.1851 0.1632 0.1483 -0.0024 -0.0177 -0.0439 223 VAL A CG2 
1937 C  CG2 B VAL A 222 ? 0.2090 0.3398 0.1976 0.0096  0.0340  0.0024  223 VAL A CG2 
1938 N  N   . LEU A 223 ? 0.1951 0.1509 0.1800 -0.0086 -0.0012 0.0012  224 LEU A N   
1939 C  CA  . LEU A 223 ? 0.2406 0.1578 0.1920 -0.0304 0.0175  -0.0046 224 LEU A CA  
1940 C  C   . LEU A 223 ? 0.2220 0.1632 0.1675 -0.0026 0.0119  -0.0344 224 LEU A C   
1941 O  O   . LEU A 223 ? 0.1904 0.2108 0.1990 -0.0199 0.0230  -0.0340 224 LEU A O   
1942 C  CB  . LEU A 223 ? 0.2662 0.1552 0.2496 -0.0176 0.0292  -0.0272 224 LEU A CB  
1943 C  CG  . LEU A 223 ? 0.3345 0.1842 0.2518 -0.0142 0.0102  -0.0196 224 LEU A CG  
1944 C  CD1 . LEU A 223 ? 0.4178 0.2196 0.3312 -0.0454 -0.0386 -0.0131 224 LEU A CD1 
1945 C  CD2 . LEU A 223 ? 0.3183 0.2985 0.3115 -0.0114 0.0031  -0.1193 224 LEU A CD2 
1946 N  N   . LYS A 224 ? 0.2107 0.1686 0.1534 -0.0063 0.0006  -0.0046 225 LYS A N   
1947 C  CA  . LYS A 224 ? 0.2169 0.1929 0.1581 -0.0174 0.0038  -0.0041 225 LYS A CA  
1948 C  C   . LYS A 224 ? 0.2081 0.1728 0.1367 0.0043  0.0065  0.0204  225 LYS A C   
1949 O  O   . LYS A 224 ? 0.2460 0.1748 0.1376 -0.0284 0.0205  -0.0027 225 LYS A O   
1950 C  CB  . LYS A 224 ? 0.2249 0.2474 0.1958 -0.0057 -0.0176 0.0513  225 LYS A CB  
1951 C  CG  . LYS A 224 ? 0.2939 0.3844 0.2536 -0.0648 -0.1036 -0.0074 225 LYS A CG  
1952 C  CD  . LYS A 224 ? 0.3736 0.2770 0.3151 -0.0065 -0.0538 -0.0746 225 LYS A CD  
1953 C  CE  . LYS A 224 ? 0.4307 0.3923 0.4763 -0.0480 -0.1701 -0.1180 225 LYS A CE  
1954 N  NZ  . LYS A 224 ? 0.4893 0.3330 0.4282 0.0781  -0.0597 -0.0419 225 LYS A NZ  
1955 N  N   . PHE A 225 ? 0.1999 0.1536 0.1176 -0.0065 0.0140  -0.0012 226 PHE A N   
1956 C  CA  . PHE A 225 ? 0.1868 0.1412 0.1421 -0.0152 0.0175  0.0000  226 PHE A CA  
1957 C  C   . PHE A 225 ? 0.2011 0.1435 0.1158 -0.0098 0.0087  0.0027  226 PHE A C   
1958 O  O   . PHE A 225 ? 0.2134 0.1384 0.1430 -0.0219 0.0344  -0.0148 226 PHE A O   
1959 C  CB  . PHE A 225 ? 0.2046 0.1396 0.1299 -0.0063 0.0373  0.0020  226 PHE A CB  
1960 C  CG  . PHE A 225 ? 0.1914 0.1216 0.1553 -0.0309 0.0275  -0.0291 226 PHE A CG  
1961 C  CD1 . PHE A 225 ? 0.2594 0.2097 0.1571 0.0344  0.0317  0.0218  226 PHE A CD1 
1962 C  CD2 . PHE A 225 ? 0.2166 0.2169 0.1810 -0.0098 0.0425  -0.0595 226 PHE A CD2 
1963 C  CE1 . PHE A 225 ? 0.2496 0.2122 0.2073 0.0397  0.0283  0.0049  226 PHE A CE1 
1964 C  CE2 . PHE A 225 ? 0.1923 0.2345 0.2213 -0.0326 0.0285  -0.0741 226 PHE A CE2 
1965 C  CZ  . PHE A 225 ? 0.1990 0.2142 0.2442 -0.0232 0.0092  -0.0974 226 PHE A CZ  
1966 N  N   . ARG A 226 ? 0.1808 0.1453 0.1234 0.0065  0.0068  -0.0051 227 ARG A N   
1967 C  CA  . ARG A 226 ? 0.1999 0.1571 0.1280 -0.0173 0.0186  -0.0086 227 ARG A CA  
1968 C  C   . ARG A 226 ? 0.1851 0.1509 0.1620 0.0054  0.0285  0.0035  227 ARG A C   
1969 O  O   . ARG A 226 ? 0.2054 0.1852 0.1544 -0.0030 0.0142  -0.0151 227 ARG A O   
1970 C  CB  . ARG A 226 ? 0.2186 0.1430 0.1334 -0.0120 0.0232  0.0103  227 ARG A CB  
1971 C  CG  . ARG A 226 ? 0.2055 0.1624 0.1332 -0.0137 0.0065  0.0071  227 ARG A CG  
1972 C  CD  . ARG A 226 ? 0.2662 0.1527 0.1650 -0.0263 -0.0052 0.0141  227 ARG A CD  
1973 N  NE  . ARG A 226 ? 0.2224 0.1492 0.1457 -0.0505 -0.0164 0.0000  227 ARG A NE  
1974 C  CZ  . ARG A 226 ? 0.2421 0.1571 0.1436 -0.0465 -0.0231 -0.0263 227 ARG A CZ  
1975 N  NH1 . ARG A 226 ? 0.2745 0.2061 0.1966 -0.0688 -0.0452 -0.0450 227 ARG A NH1 
1976 N  NH2 . ARG A 226 ? 0.2619 0.1657 0.1404 -0.0670 -0.0043 -0.0207 227 ARG A NH2 
1977 N  N   . LYS A 227 ? 0.2125 0.1544 0.1260 -0.0264 0.0230  -0.0250 228 LYS A N   
1978 C  CA  . LYS A 227 ? 0.2379 0.1729 0.1252 -0.0395 0.0275  -0.0281 228 LYS A CA  
1979 C  C   . LYS A 227 ? 0.2345 0.1664 0.1181 -0.0303 0.0452  -0.0302 228 LYS A C   
1980 O  O   . LYS A 227 ? 0.2953 0.1852 0.1221 -0.0388 0.0456  -0.0241 228 LYS A O   
1981 C  CB  . LYS A 227 ? 0.2712 0.2453 0.1261 -0.0489 0.0108  -0.0344 228 LYS A CB  
1982 C  CG  . LYS A 227 ? 0.2924 0.2307 0.1897 -0.0869 0.0383  -0.0573 228 LYS A CG  
1983 C  CD  . LYS A 227 ? 0.4185 0.3865 0.2565 -0.0913 -0.0362 -0.0728 228 LYS A CD  
1984 C  CE  . LYS A 227 ? 0.4882 0.7792 0.3161 -0.2892 0.0019  -0.1102 228 LYS A CE  
1985 N  NZ  . LYS A 227 ? 0.8798 0.9592 0.3907 -0.5400 -0.1233 0.1306  228 LYS A NZ  
1986 N  N   . LEU A 228 ? 0.2361 0.1457 0.1228 -0.0399 0.0303  -0.0241 229 LEU A N   
1987 C  CA  . LEU A 228 ? 0.1949 0.1641 0.1387 -0.0161 0.0337  -0.0175 229 LEU A CA  
1988 C  C   . LEU A 228 ? 0.2630 0.1465 0.1034 -0.0241 0.0388  -0.0163 229 LEU A C   
1989 O  O   . LEU A 228 ? 0.2213 0.1606 0.1323 -0.0082 0.0461  -0.0230 229 LEU A O   
1990 C  CB  . LEU A 228 ? 0.2249 0.1588 0.1176 -0.0230 0.0296  -0.0220 229 LEU A CB  
1991 C  CG  . LEU A 228 ? 0.2188 0.1825 0.1226 -0.0038 0.0166  -0.0030 229 LEU A CG  
1992 C  CD1 . LEU A 228 ? 0.2386 0.1960 0.1201 0.0027  0.0203  -0.0250 229 LEU A CD1 
1993 C  CD2 . LEU A 228 ? 0.2921 0.1994 0.1392 0.0228  0.0593  0.0337  229 LEU A CD2 
1994 N  N   . ASN A 229 ? 0.2061 0.1747 0.1279 -0.0291 0.0331  -0.0114 230 ASN A N   
1995 C  CA  . ASN A 229 ? 0.2284 0.1658 0.1067 -0.0193 0.0219  -0.0230 230 ASN A CA  
1996 C  C   . ASN A 229 ? 0.2205 0.2169 0.1147 -0.0020 0.0487  -0.0005 230 ASN A C   
1997 O  O   . ASN A 229 ? 0.2361 0.1764 0.1465 -0.0241 0.0430  -0.0274 230 ASN A O   
1998 C  CB  . ASN A 229 ? 0.2809 0.2000 0.1395 -0.0333 0.0675  -0.0263 230 ASN A CB  
1999 C  CG  . ASN A 229 ? 0.2734 0.2222 0.1167 -0.0237 0.0381  -0.0436 230 ASN A CG  
2000 O  OD1 . ASN A 229 ? 0.4228 0.2515 0.1466 -0.0478 0.1039  -0.0403 230 ASN A OD1 
2001 N  ND2 . ASN A 229 ? 0.3021 0.2090 0.1615 -0.0518 0.0456  -0.0582 230 ASN A ND2 
2002 N  N   . PHE A 230 ? 0.2193 0.1603 0.1506 -0.0507 0.0584  -0.0087 231 PHE A N   
2003 C  CA  . PHE A 230 ? 0.2073 0.1606 0.1456 -0.0281 0.0130  0.0308  231 PHE A CA  
2004 C  C   . PHE A 230 ? 0.2325 0.1889 0.1641 -0.0588 0.0452  -0.0049 231 PHE A C   
2005 O  O   . PHE A 230 ? 0.2856 0.2030 0.1551 -0.0917 0.0489  -0.0030 231 PHE A O   
2006 C  CB  . PHE A 230 ? 0.1884 0.1650 0.1713 -0.0263 0.0570  -0.0026 231 PHE A CB  
2007 C  CG  . PHE A 230 ? 0.1995 0.1666 0.1668 -0.0423 0.0408  -0.0082 231 PHE A CG  
2008 C  CD1 . PHE A 230 ? 0.2205 0.1835 0.1323 -0.0357 0.0344  -0.0251 231 PHE A CD1 
2009 C  CD2 . PHE A 230 ? 0.1990 0.2277 0.1194 0.0221  0.0250  -0.0204 231 PHE A CD2 
2010 C  CE1 . PHE A 230 ? 0.1941 0.1650 0.1722 -0.0348 0.0438  0.0000  231 PHE A CE1 
2011 C  CE2 . PHE A 230 ? 0.2213 0.1746 0.1509 -0.0160 0.0307  -0.0248 231 PHE A CE2 
2012 C  CZ  . PHE A 230 ? 0.1993 0.2030 0.1251 -0.0339 0.0243  -0.0159 231 PHE A CZ  
2013 N  N   . ASN A 231 ? 0.2281 0.2176 0.1458 -0.0467 0.0555  -0.0035 232 ASN A N   
2014 C  CA  . ASN A 231 ? 0.1684 0.2345 0.2002 -0.0263 0.0326  -0.0041 232 ASN A CA  
2015 C  C   . ASN A 231 ? 0.1735 0.2723 0.1414 0.0000  0.0273  0.0054  232 ASN A C   
2016 O  O   . ASN A 231 ? 0.2451 0.2115 0.1580 -0.0142 0.0586  0.0024  232 ASN A O   
2017 C  CB  . ASN A 231 ? 0.2090 0.2310 0.2486 -0.0417 0.0856  0.0087  232 ASN A CB  
2018 C  CG  . ASN A 231 ? 0.2240 0.2162 0.2047 -0.0087 0.0436  -0.0198 232 ASN A CG  
2019 O  OD1 . ASN A 231 ? 0.3258 0.2560 0.2238 -0.0656 0.1203  -0.0412 232 ASN A OD1 
2020 N  ND2 . ASN A 231 ? 0.2597 0.3115 0.1852 0.0238  0.0606  -0.0197 232 ASN A ND2 
2021 N  N   . GLY A 232 ? 0.2626 0.2433 0.2034 -0.0373 0.0662  0.0252  233 GLY A N   
2022 C  CA  . GLY A 232 ? 0.2709 0.2379 0.1781 0.0230  0.0794  0.0241  233 GLY A CA  
2023 C  C   . GLY A 232 ? 0.1764 0.2363 0.2399 0.0328  -0.0024 -0.0051 233 GLY A C   
2024 O  O   . GLY A 232 ? 0.2666 0.3345 0.2029 0.0781  0.1005  0.0776  233 GLY A O   
2025 N  N   . GLU A 233 ? 0.2117 0.2511 0.2010 -0.0175 0.0631  -0.0046 234 GLU A N   
2026 C  CA  . GLU A 233 ? 0.2486 0.2913 0.1613 -0.0037 0.0584  0.0000  234 GLU A CA  
2027 C  C   . GLU A 233 ? 0.2752 0.2939 0.1982 0.0151  0.0502  -0.0177 234 GLU A C   
2028 O  O   . GLU A 233 ? 0.3036 0.4207 0.1960 -0.0353 0.0736  0.0458  234 GLU A O   
2029 C  CB  . GLU A 233 ? 0.3316 0.2619 0.1710 0.0263  0.0502  0.0447  234 GLU A CB  
2030 C  CG  . GLU A 233 ? 0.2551 0.3291 0.1976 -0.0406 0.0709  0.0013  234 GLU A CG  
2031 C  CD  . GLU A 233 ? 0.3485 0.5411 0.2474 0.0957  0.0825  -0.0355 234 GLU A CD  
2032 O  OE1 . GLU A 233 ? 0.4638 0.3524 0.2874 0.0220  0.1439  0.0623  234 GLU A OE1 
2033 O  OE2 . GLU A 233 ? 0.4356 0.4512 0.2630 0.0164  -0.0287 -0.0219 234 GLU A OE2 
2034 N  N   . GLY A 234 ? 0.3697 0.3718 0.2453 0.0768  0.0657  -0.0806 235 GLY A N   
2035 C  CA  . GLY A 234 ? 0.4016 0.5457 0.2284 0.0702  0.0153  -0.1668 235 GLY A CA  
2036 C  C   . GLY A 234 ? 0.4555 0.8963 0.1010 0.1703  0.0003  -0.1039 235 GLY A C   
2037 O  O   . GLY A 234 ? 0.6013 0.8179 0.4950 0.0926  -0.0126 0.0564  235 GLY A O   
2038 N  N   . GLU A 235 ? 0.3700 0.4322 0.2338 -0.0115 0.0926  -0.0562 236 GLU A N   
2039 C  CA  . GLU A 235 ? 0.3359 0.3844 0.2435 0.1062  0.0701  0.0482  236 GLU A CA  
2040 C  C   . GLU A 235 ? 0.4241 0.5000 0.1674 0.0219  0.1076  0.0575  236 GLU A C   
2041 O  O   . GLU A 235 ? 0.3941 0.5763 0.3474 0.0041  0.1814  0.0253  236 GLU A O   
2042 C  CB  . GLU A 235 ? 0.3398 0.3355 0.2403 0.0419  0.1225  0.0362  236 GLU A CB  
2043 C  CG  . GLU A 235 ? 0.2730 0.3237 0.3169 -0.0728 0.0666  0.0304  236 GLU A CG  
2044 C  CD  . GLU A 235 ? 0.5569 0.5867 0.2851 -0.1982 0.1536  -0.0930 236 GLU A CD  
2045 O  OE1 . GLU A 235 ? 0.4404 0.4612 0.4350 -0.1542 0.1590  0.0225  236 GLU A OE1 
2046 O  OE2 . GLU A 235 ? 0.5238 0.6883 0.8022 -0.2524 0.0714  0.3788  236 GLU A OE2 
2047 N  N   . PRO A 236 ? 0.2896 0.4329 0.2456 0.0403  0.1298  0.0612  237 PRO A N   
2048 C  CA  . PRO A 236 ? 0.3028 0.5138 0.2935 -0.0447 0.0920  0.0996  237 PRO A CA  
2049 C  C   . PRO A 236 ? 0.3585 0.5762 0.1385 -0.1005 0.0573  -0.0171 237 PRO A C   
2050 O  O   . PRO A 236 ? 0.2888 0.5424 0.2266 -0.1298 0.0741  -0.0162 237 PRO A O   
2051 C  CB  . PRO A 236 ? 0.2465 0.6643 0.3452 -0.0302 0.0983  0.1164  237 PRO A CB  
2052 C  CG  . PRO A 236 ? 0.3391 0.4361 0.4350 0.0930  0.1713  0.1928  237 PRO A CG  
2053 C  CD  . PRO A 236 ? 0.2698 0.5489 0.3693 0.1049  0.0885  0.1271  237 PRO A CD  
2054 N  N   . GLU A 237 ? 0.2964 0.4616 0.2623 0.0271  0.1054  -0.1123 238 GLU A N   
2055 C  CA  . GLU A 237 ? 0.3202 0.4483 0.1870 -0.0102 0.1386  -0.0683 238 GLU A CA  
2056 C  C   . GLU A 237 ? 0.2071 0.3039 0.3172 -0.0054 0.1247  -0.0636 238 GLU A C   
2057 O  O   . GLU A 237 ? 0.2392 0.3046 0.2143 0.0253  0.0776  -0.0535 238 GLU A O   
2058 C  CB  . GLU A 237 ? 0.2996 0.4160 0.2684 0.1140  -0.0087 -0.1428 238 GLU A CB  
2059 C  CG  . GLU A 237 ? 0.4041 0.3416 0.3299 -0.0283 0.0251  -0.1412 238 GLU A CG  
2060 C  CD  . GLU A 237 ? 0.4232 0.4498 0.2953 0.0038  0.0388  -0.2123 238 GLU A CD  
2061 O  OE1 . GLU A 237 ? 0.3977 0.6728 0.6182 0.1032  -0.0825 -0.4596 238 GLU A OE1 
2062 O  OE2 . GLU A 237 ? 0.4185 0.2644 0.2720 -0.0027 0.0606  -0.1146 238 GLU A OE2 
2063 N  N   . GLU A 238 ? 0.2320 0.2356 0.1914 -0.0383 0.0942  -0.0317 239 GLU A N   
2064 C  CA  . GLU A 238 ? 0.2171 0.2662 0.1985 -0.0496 0.0864  -0.0302 239 GLU A CA  
2065 C  C   . GLU A 238 ? 0.1966 0.2201 0.1467 -0.0240 0.0658  -0.0109 239 GLU A C   
2066 O  O   . GLU A 238 ? 0.2770 0.1791 0.2396 -0.0461 0.0776  -0.0249 239 GLU A O   
2067 C  CB  . GLU A 238 ? 0.2694 0.2996 0.2996 -0.0882 0.0732  -0.0551 239 GLU A CB  
2068 C  CG  . GLU A 238 ? 0.3312 0.4602 0.4569 -0.1571 0.1212  -0.1612 239 GLU A CG  
2069 C  CD  . GLU A 238 ? 0.5827 0.7160 0.6789 -0.0675 -0.0930 -0.3043 239 GLU A CD  
2070 O  OE1 . GLU A 238 ? 0.3898 0.6478 1.0670 -0.1630 -0.0221 -0.3738 239 GLU A OE1 
2071 O  OE2 . GLU A 238 ? 0.3883 1.0951 0.8672 -0.1263 -0.1685 -0.3885 239 GLU A OE2 
2072 N  N   . LEU A 239 ? 0.2117 0.2037 0.1394 -0.0219 0.0540  -0.0185 240 LEU A N   
2073 C  CA  . LEU A 239 ? 0.1703 0.1736 0.1535 -0.0159 0.0524  -0.0115 240 LEU A CA  
2074 C  C   . LEU A 239 ? 0.1958 0.1625 0.1270 -0.0175 0.0326  0.0063  240 LEU A C   
2075 O  O   . LEU A 239 ? 0.1832 0.1747 0.1543 -0.0153 0.0447  -0.0162 240 LEU A O   
2076 C  CB  . LEU A 239 ? 0.1912 0.1500 0.1807 -0.0054 0.0423  -0.0147 240 LEU A CB  
2077 C  CG  . LEU A 239 ? 0.1650 0.2099 0.2317 -0.0250 0.0226  -0.0666 240 LEU A CG  
2078 C  CD1 . LEU A 239 ? 0.2170 0.1458 0.4106 0.0041  -0.0283 -0.0599 240 LEU A CD1 
2079 C  CD2 . LEU A 239 ? 0.2372 0.2222 0.2211 0.0208  -0.0203 -0.0891 240 LEU A CD2 
2080 N  N   . MET A 240 ? 0.1976 0.1479 0.1331 -0.0107 0.0478  -0.0164 241 MET A N   
2081 C  CA  . MET A 240 ? 0.2374 0.1657 0.1084 -0.0049 0.0662  -0.0148 241 MET A CA  
2082 C  C   . MET A 240 ? 0.1712 0.1527 0.1057 -0.0136 0.0243  -0.0170 241 MET A C   
2083 O  O   . MET A 240 ? 0.1770 0.1622 0.1171 -0.0087 0.0296  -0.0104 241 MET A O   
2084 C  CB  . MET A 240 ? 0.2263 0.1387 0.1316 0.0173  0.0383  -0.0057 241 MET A CB  
2085 C  CG  . MET A 240 ? 0.2205 0.1656 0.1128 -0.0291 0.0559  -0.0237 241 MET A CG  
2086 S  SD  . MET A 240 ? 0.2334 0.1395 0.1448 -0.0170 0.0491  -0.0140 241 MET A SD  
2087 C  CE  . MET A 240 ? 0.2638 0.1490 0.1532 -0.0361 0.0693  0.0046  241 MET A CE  
2088 N  N   . VAL A 241 ? 0.1704 0.1395 0.1201 -0.0207 0.0315  -0.0285 242 VAL A N   
2089 C  CA  . VAL A 241 ? 0.1704 0.1280 0.1070 -0.0320 0.0208  -0.0205 242 VAL A CA  
2090 C  C   . VAL A 241 ? 0.1395 0.1111 0.1199 -0.0038 0.0219  -0.0208 242 VAL A C   
2091 O  O   . VAL A 241 ? 0.1325 0.1595 0.1210 -0.0131 0.0281  -0.0226 242 VAL A O   
2092 C  CB  . VAL A 241 ? 0.1685 0.1316 0.1395 -0.0164 0.0131  -0.0324 242 VAL A CB  
2093 C  CG1 . VAL A 241 ? 0.2331 0.1562 0.1599 -0.0377 0.0171  -0.0419 242 VAL A CG1 
2094 C  CG2 . VAL A 241 ? 0.1992 0.1527 0.1562 -0.0087 0.0432  -0.0432 242 VAL A CG2 
2095 N  N   . ASP A 242 ? 0.1430 0.1061 0.1115 -0.0023 0.0261  -0.0141 243 ASP A N   
2096 C  CA  . ASP A 242 ? 0.1299 0.1176 0.1237 0.0071  0.0205  -0.0154 243 ASP A CA  
2097 C  C   . ASP A 242 ? 0.1176 0.1164 0.1233 -0.0125 0.0249  -0.0274 243 ASP A C   
2098 O  O   . ASP A 242 ? 0.1255 0.1242 0.1641 -0.0040 0.0082  -0.0250 243 ASP A O   
2099 C  CB  . ASP A 242 ? 0.1333 0.1142 0.1497 -0.0092 0.0119  -0.0219 243 ASP A CB  
2100 C  CG  . ASP A 242 ? 0.1474 0.1122 0.1599 0.0043  0.0193  -0.0247 243 ASP A CG  
2101 O  OD1 . ASP A 242 ? 0.1356 0.1104 0.1519 0.0086  0.0098  -0.0109 243 ASP A OD1 
2102 O  OD2 . ASP A 242 ? 0.1614 0.1268 0.1897 0.0003  0.0318  -0.0366 243 ASP A OD2 
2103 N  N   . ASN A 243 ? 0.1167 0.0961 0.1185 -0.0087 0.0252  -0.0164 244 ASN A N   
2104 C  CA  . ASN A 243 ? 0.1164 0.1023 0.1212 -0.0046 0.0243  -0.0193 244 ASN A CA  
2105 C  C   . ASN A 243 ? 0.1018 0.1088 0.1084 -0.0181 0.0120  -0.0062 244 ASN A C   
2106 O  O   . ASN A 243 ? 0.1456 0.1172 0.1097 0.0195  0.0294  -0.0054 244 ASN A O   
2107 C  CB  . ASN A 243 ? 0.1306 0.1194 0.1185 -0.0286 0.0269  0.0023  244 ASN A CB  
2108 C  CG  . ASN A 243 ? 0.1430 0.1113 0.1095 -0.0392 0.0087  -0.0043 244 ASN A CG  
2109 O  OD1 . ASN A 243 ? 0.1277 0.1203 0.1456 -0.0209 0.0087  0.0152  244 ASN A OD1 
2110 N  ND2 . ASN A 243 ? 0.1729 0.1597 0.1615 -0.0355 -0.0124 0.0392  244 ASN A ND2 
2111 N  N   . TRP A 244 ? 0.1140 0.1054 0.0995 -0.0092 0.0155  -0.0071 245 TRP A N   
2112 C  CA  . TRP A 244 ? 0.0983 0.1115 0.1054 -0.0087 0.0073  -0.0092 245 TRP A CA  
2113 C  C   . TRP A 244 ? 0.1061 0.1079 0.1106 -0.0082 0.0263  -0.0034 245 TRP A C   
2114 O  O   . TRP A 244 ? 0.1070 0.1277 0.1298 0.0164  0.0057  -0.0247 245 TRP A O   
2115 C  CB  . TRP A 244 ? 0.1059 0.0944 0.1246 -0.0006 0.0126  -0.0087 245 TRP A CB  
2116 C  CG  . TRP A 244 ? 0.0951 0.1142 0.1149 -0.0024 0.0115  -0.0043 245 TRP A CG  
2117 C  CD1 . TRP A 244 ? 0.1018 0.1018 0.1230 -0.0104 0.0254  -0.0109 245 TRP A CD1 
2118 C  CD2 . TRP A 244 ? 0.0996 0.1092 0.1176 -0.0012 0.0115  -0.0120 245 TRP A CD2 
2119 N  NE1 . TRP A 244 ? 0.1253 0.1036 0.1201 0.0000  0.0131  0.0000  245 TRP A NE1 
2120 C  CE2 . TRP A 244 ? 0.1199 0.1017 0.1405 0.0126  0.0054  0.0020  245 TRP A CE2 
2121 C  CE3 . TRP A 244 ? 0.1316 0.1194 0.1307 0.0043  0.0120  -0.0003 245 TRP A CE3 
2122 C  CZ2 . TRP A 244 ? 0.1438 0.1246 0.1384 0.0065  0.0136  -0.0068 245 TRP A CZ2 
2123 C  CZ3 . TRP A 244 ? 0.1483 0.1333 0.1703 0.0135  -0.0031 0.0065  245 TRP A CZ3 
2124 C  CH2 . TRP A 244 ? 0.1588 0.1361 0.1579 0.0196  0.0113  0.0113  245 TRP A CH2 
2125 N  N   . ARG A 245 ? 0.0988 0.1162 0.1106 -0.0057 0.0126  -0.0241 246 ARG A N   
2126 C  CA  . ARG A 245 ? 0.0952 0.1124 0.1167 0.0035  0.0102  -0.0063 246 ARG A CA  
2127 C  C   . ARG A 245 ? 0.0921 0.1162 0.1102 0.0052  -0.0059 -0.0237 246 ARG A C   
2128 O  O   . ARG A 245 ? 0.0988 0.1316 0.1324 0.0013  0.0049  -0.0207 246 ARG A O   
2129 C  CB  . ARG A 245 ? 0.0878 0.1102 0.1305 -0.0013 0.0057  -0.0195 246 ARG A CB  
2130 C  CG  . ARG A 245 ? 0.0882 0.1163 0.1401 -0.0041 0.0006  -0.0155 246 ARG A CG  
2131 C  CD  . ARG A 245 ? 0.0776 0.1253 0.1324 -0.0104 0.0082  -0.0188 246 ARG A CD  
2132 N  NE  . ARG A 245 ? 0.0833 0.1351 0.1465 -0.0161 0.0031  -0.0322 246 ARG A NE  
2133 C  CZ  . ARG A 245 ? 0.0920 0.1235 0.1377 -0.0148 0.0137  -0.0215 246 ARG A CZ  
2134 N  NH1 . ARG A 245 ? 0.1048 0.1230 0.1465 -0.0159 0.0160  -0.0239 246 ARG A NH1 
2135 N  NH2 . ARG A 245 ? 0.0925 0.1701 0.1747 -0.0383 -0.0057 -0.0148 246 ARG A NH2 
2136 N  N   A PRO A 246 ? 0.1110 0.1278 0.1289 0.0003  0.0043  0.0057  247 PRO A N   
2137 N  N   B PRO A 246 ? 0.1101 0.1244 0.1158 0.0005  0.0017  -0.0027 247 PRO A N   
2138 C  CA  A PRO A 246 ? 0.1264 0.1237 0.1298 -0.0006 -0.0177 -0.0148 247 PRO A CA  
2139 C  CA  B PRO A 246 ? 0.1190 0.1375 0.1163 0.0260  0.0115  -0.0108 247 PRO A CA  
2140 C  C   A PRO A 246 ? 0.1201 0.1120 0.1377 0.0054  -0.0031 -0.0013 247 PRO A C   
2141 C  C   B PRO A 246 ? 0.1149 0.1128 0.1212 0.0057  -0.0087 -0.0085 247 PRO A C   
2142 O  O   A PRO A 246 ? 0.1115 0.1164 0.1198 0.0091  -0.0043 -0.0098 247 PRO A O   
2143 O  O   B PRO A 246 ? 0.1192 0.1219 0.1342 0.0031  0.0000  -0.0060 247 PRO A O   
2144 C  CB  A PRO A 246 ? 0.1639 0.1368 0.1578 0.0196  -0.0136 0.0063  247 PRO A CB  
2145 C  CB  B PRO A 246 ? 0.1136 0.1396 0.1588 0.0197  0.0197  -0.0049 247 PRO A CB  
2146 C  CG  A PRO A 246 ? 0.1545 0.1444 0.1581 0.0199  0.0146  0.0220  247 PRO A CG  
2147 C  CG  B PRO A 246 ? 0.1259 0.1411 0.2307 0.0216  -0.0119 0.0071  247 PRO A CG  
2148 C  CD  A PRO A 246 ? 0.0956 0.1307 0.1546 0.0153  0.0086  0.0076  247 PRO A CD  
2149 C  CD  B PRO A 246 ? 0.1050 0.1568 0.1360 0.0388  -0.0104 -0.0430 247 PRO A CD  
2150 N  N   . ALA A 247 ? 0.1307 0.1237 0.1273 0.0098  0.0020  -0.0006 248 ALA A N   
2151 C  CA  . ALA A 247 ? 0.1149 0.1254 0.1228 0.0057  -0.0074 0.0035  248 ALA A CA  
2152 C  C   . ALA A 247 ? 0.0961 0.1271 0.1298 0.0175  0.0027  0.0186  248 ALA A C   
2153 O  O   . ALA A 247 ? 0.1181 0.1544 0.1589 0.0373  -0.0114 0.0076  248 ALA A O   
2154 C  CB  . ALA A 247 ? 0.1535 0.1580 0.1430 -0.0059 0.0283  0.0104  248 ALA A CB  
2155 N  N   . GLN A 248 ? 0.1111 0.1131 0.1272 0.0049  -0.0115 0.0093  249 GLN A N   
2156 C  CA  . GLN A 248 ? 0.0965 0.1536 0.1316 0.0098  -0.0170 0.0074  249 GLN A CA  
2157 C  C   . GLN A 248 ? 0.1097 0.1563 0.1208 0.0276  -0.0253 0.0253  249 GLN A C   
2158 O  O   . GLN A 248 ? 0.1271 0.1430 0.1448 0.0131  -0.0026 0.0109  249 GLN A O   
2159 C  CB  . GLN A 248 ? 0.1316 0.1493 0.1342 -0.0031 -0.0174 0.0073  249 GLN A CB  
2160 C  CG  . GLN A 248 ? 0.1305 0.1472 0.1331 -0.0010 -0.0219 0.0141  249 GLN A CG  
2161 C  CD  . GLN A 248 ? 0.1150 0.1703 0.1479 -0.0175 -0.0115 0.0164  249 GLN A CD  
2162 O  OE1 . GLN A 248 ? 0.1155 0.2471 0.1947 -0.0351 -0.0048 -0.0208 249 GLN A OE1 
2163 N  NE2 . GLN A 248 ? 0.1499 0.1946 0.1553 -0.0017 -0.0015 -0.0076 249 GLN A NE2 
2164 N  N   . PRO A 249 ? 0.1448 0.1832 0.1419 0.0326  -0.0260 0.0082  250 PRO A N   
2165 C  CA  . PRO A 249 ? 0.1509 0.2142 0.1484 0.0571  -0.0296 0.0054  250 PRO A CA  
2166 C  C   . PRO A 249 ? 0.1597 0.1456 0.1378 0.0241  -0.0339 0.0102  250 PRO A C   
2167 O  O   . PRO A 249 ? 0.1288 0.1588 0.1586 0.0324  -0.0292 0.0054  250 PRO A O   
2168 C  CB  . PRO A 249 ? 0.1544 0.2896 0.1836 0.0820  -0.0458 -0.0248 250 PRO A CB  
2169 C  CG  . PRO A 249 ? 0.1691 0.3373 0.1780 0.0373  -0.0472 -0.0216 250 PRO A CG  
2170 C  CD  . PRO A 249 ? 0.1133 0.2906 0.2073 0.0476  -0.0653 -0.0248 250 PRO A CD  
2171 N  N   . LEU A 250 ? 0.1774 0.1701 0.1221 0.0502  -0.0153 0.0104  251 LEU A N   
2172 C  CA  . LEU A 250 ? 0.1581 0.1383 0.1465 0.0102  -0.0040 0.0003  251 LEU A CA  
2173 C  C   . LEU A 250 ? 0.1447 0.1352 0.1419 0.0206  -0.0197 0.0192  251 LEU A C   
2174 O  O   . LEU A 250 ? 0.1473 0.1497 0.1474 0.0164  -0.0436 0.0038  251 LEU A O   
2175 C  CB  . LEU A 250 ? 0.2099 0.1668 0.1614 -0.0010 -0.0024 0.0010  251 LEU A CB  
2176 C  CG  . LEU A 250 ? 0.2036 0.1589 0.1614 -0.0153 0.0273  -0.0142 251 LEU A CG  
2177 C  CD1 . LEU A 250 ? 0.1598 0.2126 0.1606 -0.0049 -0.0274 -0.0285 251 LEU A CD1 
2178 C  CD2 . LEU A 250 ? 0.2745 0.1914 0.2108 -0.0364 0.0419  -0.0263 251 LEU A CD2 
2179 N  N   . LYS A 251 ? 0.1650 0.1884 0.1351 0.0482  -0.0450 0.0093  252 LYS A N   
2180 C  CA  . LYS A 251 ? 0.1687 0.2108 0.1316 0.0362  -0.0283 -0.0225 252 LYS A CA  
2181 C  C   . LYS A 251 ? 0.1630 0.2069 0.1921 0.0115  -0.0450 0.0048  252 LYS A C   
2182 O  O   . LYS A 251 ? 0.2465 0.2451 0.1685 0.0038  0.0188  -0.0198 252 LYS A O   
2183 C  CB  . LYS A 251 ? 0.1964 0.2440 0.1754 -0.0173 -0.0298 -0.0206 252 LYS A CB  
2184 C  CG  . LYS A 251 ? 0.2275 0.3014 0.2188 -0.0153 0.0284  -0.0436 252 LYS A CG  
2185 C  CD  . LYS A 251 ? 0.1879 0.3427 0.3718 0.0165  0.0390  -0.0250 252 LYS A CD  
2186 C  CE  . LYS A 251 ? 0.1133 0.4663 0.6409 0.0467  0.0732  -0.0037 252 LYS A CE  
2187 N  NZ  . LYS A 251 ? 0.2572 0.3585 0.5113 0.0386  0.0193  0.0250  252 LYS A NZ  
2188 N  N   . ASN A 252 ? 0.1875 0.2011 0.1317 0.0148  -0.0421 -0.0333 253 ASN A N   
2189 C  CA  . ASN A 252 ? 0.2219 0.4566 0.1729 0.0542  -0.0718 -0.1133 253 ASN A CA  
2190 C  C   . ASN A 252 ? 0.2414 0.2500 0.1982 0.0274  -0.0159 -0.0496 253 ASN A C   
2191 O  O   . ASN A 252 ? 0.2694 0.2781 0.2162 0.0350  -0.0051 -0.0265 253 ASN A O   
2192 C  CB  . ASN A 252 ? 0.2476 0.4314 0.2374 0.0296  -0.0463 -0.1180 253 ASN A CB  
2193 C  CG  . ASN A 252 ? 0.3388 0.3671 0.2910 0.0096  0.0520  -0.0366 253 ASN A CG  
2194 O  OD1 . ASN A 252 ? 0.6783 0.6176 0.3517 -0.1365 0.0592  0.1800  253 ASN A OD1 
2195 N  ND2 . ASN A 252 ? 0.4289 0.4514 0.3840 0.0509  -0.0544 -0.1731 253 ASN A ND2 
2196 N  N   A ARG A 253 ? 0.1448 0.2450 0.1658 0.0313  0.0262  0.0619  254 ARG A N   
2197 N  N   B ARG A 253 ? 0.1852 0.3172 0.0529 0.0636  -0.0174 0.0031  254 ARG A N   
2198 C  CA  A ARG A 253 ? 0.1474 0.1423 0.1131 0.0087  0.0031  0.0017  254 ARG A CA  
2199 C  CA  B ARG A 253 ? 0.1572 0.1922 0.1013 0.0275  -0.0359 0.0215  254 ARG A CA  
2200 C  C   A ARG A 253 ? 0.1722 0.1620 0.1226 0.0166  0.0086  0.0254  254 ARG A C   
2201 C  C   B ARG A 253 ? 0.1843 0.1518 0.1156 0.0458  0.0108  -0.0188 254 ARG A C   
2202 O  O   A ARG A 253 ? 0.2046 0.1599 0.2361 0.0241  0.0891  0.0104  254 ARG A O   
2203 O  O   B ARG A 253 ? 0.1993 0.1631 0.1295 0.0307  -0.0027 0.0126  254 ARG A O   
2204 C  CB  A ARG A 253 ? 0.1498 0.1519 0.1093 -0.0125 -0.0087 0.0240  254 ARG A CB  
2205 C  CB  B ARG A 253 ? 0.1350 0.1607 0.1014 0.0467  -0.0081 -0.0160 254 ARG A CB  
2206 C  CG  A ARG A 253 ? 0.1136 0.1208 0.1194 0.0006  -0.0023 0.0081  254 ARG A CG  
2207 C  CG  B ARG A 253 ? 0.1687 0.1659 0.1203 0.0035  0.0104  -0.0186 254 ARG A CG  
2208 C  CD  A ARG A 253 ? 0.1458 0.0838 0.1185 0.0041  0.0093  -0.0035 254 ARG A CD  
2209 C  CD  B ARG A 253 ? 0.1342 0.1585 0.1032 0.0087  -0.0228 -0.0161 254 ARG A CD  
2210 N  NE  A ARG A 253 ? 0.1025 0.1086 0.1014 0.0015  -0.0147 0.0020  254 ARG A NE  
2211 N  NE  B ARG A 253 ? 0.1296 0.1596 0.1208 0.0251  -0.0230 0.0031  254 ARG A NE  
2212 C  CZ  A ARG A 253 ? 0.0956 0.1136 0.0961 -0.0108 -0.0006 -0.0034 254 ARG A CZ  
2213 C  CZ  B ARG A 253 ? 0.1335 0.1252 0.1018 -0.0068 -0.0193 0.0006  254 ARG A CZ  
2214 N  NH1 A ARG A 253 ? 0.1101 0.1122 0.0863 -0.0074 -0.0052 0.0034  254 ARG A NH1 
2215 N  NH1 B ARG A 253 ? 0.0900 0.1181 0.1237 0.0040  -0.0271 0.0063  254 ARG A NH1 
2216 N  NH2 A ARG A 253 ? 0.0900 0.1192 0.0964 0.0120  -0.0269 -0.0026 254 ARG A NH2 
2217 N  NH2 B ARG A 253 ? 0.1167 0.1261 0.1386 0.0126  -0.0197 -0.0076 254 ARG A NH2 
2218 N  N   . GLN A 254 ? 0.1527 0.1641 0.1439 0.0057  -0.0148 -0.0302 255 GLN A N   
2219 C  CA  . GLN A 254 ? 0.2055 0.1923 0.1347 0.0052  -0.0035 -0.0359 255 GLN A CA  
2220 C  C   . GLN A 254 ? 0.1685 0.1421 0.1393 0.0074  -0.0249 -0.0081 255 GLN A C   
2221 O  O   . GLN A 254 ? 0.2392 0.1491 0.2169 -0.0142 -0.0644 -0.0017 255 GLN A O   
2222 C  CB  . GLN A 254 ? 0.1897 0.3039 0.1614 -0.0003 0.0013  -0.0562 255 GLN A CB  
2223 C  CG  . GLN A 254 ? 0.2791 0.4530 0.1990 0.0250  -0.0108 -0.0188 255 GLN A CG  
2224 C  CD  . GLN A 254 ? 0.4628 0.7634 0.2117 0.1550  0.0441  -0.0074 255 GLN A CD  
2225 O  OE1 . GLN A 254 ? 0.4192 0.5314 0.4986 0.1005  0.1404  -0.0531 255 GLN A OE1 
2226 N  NE2 . GLN A 254 ? 0.4531 0.7045 0.4514 0.0041  -0.1553 -0.2150 255 GLN A NE2 
2227 N  N   . ILE A 255 ? 0.1412 0.1395 0.1237 0.0109  0.0000  0.0015  256 ILE A N   
2228 C  CA  . ILE A 255 ? 0.1244 0.1493 0.1122 0.0107  -0.0082 -0.0013 256 ILE A CA  
2229 C  C   . ILE A 255 ? 0.1339 0.1368 0.1097 0.0006  0.0059  0.0115  256 ILE A C   
2230 O  O   . ILE A 255 ? 0.1659 0.1737 0.1400 0.0238  0.0197  0.0461  256 ILE A O   
2231 C  CB  . ILE A 255 ? 0.1536 0.1410 0.1217 0.0142  -0.0005 0.0091  256 ILE A CB  
2232 C  CG1 . ILE A 255 ? 0.1342 0.1439 0.1588 0.0186  -0.0076 -0.0035 256 ILE A CG1 
2233 C  CG2 . ILE A 255 ? 0.1375 0.1976 0.1351 -0.0020 -0.0136 -0.0027 256 ILE A CG2 
2234 C  CD1 . ILE A 255 ? 0.1500 0.1755 0.1685 0.0093  0.0082  -0.0296 256 ILE A CD1 
2235 N  N   . LYS A 256 ? 0.1212 0.1612 0.1014 0.0052  0.0060  0.0262  257 LYS A N   
2236 C  CA  . LYS A 256 ? 0.1194 0.1544 0.1061 -0.0035 0.0153  0.0120  257 LYS A CA  
2237 C  C   . LYS A 256 ? 0.1228 0.1465 0.1058 0.0082  0.0063  0.0228  257 LYS A C   
2238 O  O   . LYS A 256 ? 0.1605 0.2012 0.0974 -0.0403 0.0104  0.0080  257 LYS A O   
2239 C  CB  . LYS A 256 ? 0.1392 0.1771 0.1439 -0.0030 0.0107  -0.0195 257 LYS A CB  
2240 C  CG  . LYS A 256 ? 0.2071 0.2160 0.2073 -0.0198 0.0236  -0.0535 257 LYS A CG  
2241 C  CD  . LYS A 256 ? 0.2784 0.2229 0.2809 -0.0185 -0.0262 -0.0184 257 LYS A CD  
2242 C  CE  . LYS A 256 ? 0.3776 0.4368 0.2478 -0.1067 -0.0085 -0.1633 257 LYS A CE  
2243 N  NZ  . LYS A 256 ? 0.3258 0.4004 0.3107 0.0035  -0.0798 -0.1110 257 LYS A NZ  
2244 N  N   . ALA A 257 ? 0.1272 0.1678 0.1181 -0.0063 0.0302  0.0107  258 ALA A N   
2245 C  CA  . ALA A 257 ? 0.1149 0.1730 0.1489 -0.0082 0.0091  -0.0027 258 ALA A CA  
2246 C  C   . ALA A 257 ? 0.1217 0.1580 0.1307 -0.0218 0.0197  0.0043  258 ALA A C   
2247 O  O   . ALA A 257 ? 0.1377 0.2054 0.1183 -0.0104 0.0297  -0.0137 258 ALA A O   
2248 C  CB  . ALA A 257 ? 0.1606 0.1817 0.1603 -0.0227 0.0131  0.0023  258 ALA A CB  
2249 N  N   . SER A 258 ? 0.1212 0.1685 0.1225 -0.0017 0.0175  0.0035  259 SER A N   
2250 C  CA  . SER A 258 ? 0.1277 0.1641 0.1586 0.0013  0.0240  0.0054  259 SER A CA  
2251 C  C   . SER A 258 ? 0.1124 0.2082 0.1683 -0.0231 0.0281  -0.0082 259 SER A C   
2252 O  O   . SER A 258 ? 0.1527 0.2888 0.1986 0.0059  0.0502  0.0000  259 SER A O   
2253 C  CB  . SER A 258 ? 0.1525 0.1844 0.1640 -0.0012 0.0092  0.0126  259 SER A CB  
2254 O  OG  . SER A 258 ? 0.1165 0.2025 0.1368 0.0024  0.0193  -0.0031 259 SER A OG  
2255 N  N   . PHE A 259 ? 0.1569 0.2002 0.1729 -0.0318 0.0511  0.0204  260 PHE A N   
2256 C  CA  . PHE A 259 ? 0.1861 0.2282 0.1932 -0.0531 0.0417  0.0340  260 PHE A CA  
2257 C  C   . PHE A 259 ? 0.2896 0.2705 0.2074 -0.0744 0.0718  0.0342  260 PHE A C   
2258 O  O   . PHE A 259 ? 0.3542 0.2451 0.2169 -0.0812 0.0076  0.0724  260 PHE A O   
2259 C  CB  . PHE A 259 ? 0.1465 0.2407 0.2136 -0.0372 0.0274  -0.0041 260 PHE A CB  
2260 C  CG  . PHE A 259 ? 0.1753 0.1863 0.2035 -0.0445 0.0076  0.0153  260 PHE A CG  
2261 C  CD1 . PHE A 259 ? 0.1632 0.2282 0.1551 -0.0469 0.0000  0.0046  260 PHE A CD1 
2262 C  CD2 . PHE A 259 ? 0.2605 0.1905 0.2612 -0.0060 0.0390  0.0397  260 PHE A CD2 
2263 C  CE1 . PHE A 259 ? 0.1718 0.1977 0.1949 -0.0399 -0.0153 -0.0006 260 PHE A CE1 
2264 C  CE2 . PHE A 259 ? 0.2289 0.1964 0.3377 -0.0115 -0.0120 0.0586  260 PHE A CE2 
2265 C  CZ  . PHE A 259 ? 0.2824 0.1975 0.2302 -0.0207 -0.0034 -0.0194 260 PHE A CZ  
2266 N  N   . LYS A 260 ? 0.3564 0.4332 0.2896 -0.1712 0.0763  0.1083  261 LYS A N   
2267 C  CA  . LYS A 260 ? 0.6539 0.4465 0.3531 -0.0003 0.1685  0.1500  261 LYS A CA  
2268 C  C   . LYS A 260 ? 0.9186 0.4264 0.4531 -0.2743 0.0432  -0.0115 261 LYS A C   
2269 O  O   . LYS A 260 ? 0.8913 0.5077 0.5105 -0.1694 0.1632  0.0680  261 LYS A O   
2270 C  CB  . LYS A 260 ? 0.7185 0.2849 0.4598 -0.0944 0.0656  0.1474  261 LYS A CB  
2271 C  CG  . LYS A 260 ? 0.8161 0.4763 0.6351 -0.3623 0.1465  -0.0467 261 LYS A CG  
2272 C  CD  . LYS A 260 ? 0.8277 0.8155 0.7857 0.0671  0.2012  -0.2442 261 LYS A CD  
2273 C  CE  . LYS A 260 ? 0.8726 0.4185 0.6071 -0.0351 0.3330  0.1673  261 LYS A CE  
2274 N  NZ  . LYS A 260 ? 1.0039 0.5932 0.5095 -0.0917 0.1243  -0.1342 261 LYS A NZ  
2275 O  OXT . LYS A 260 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  261 LYS A OXT 
2276 ZN ZN  . ZN  B .   ? 0.0935 0.0869 0.0913 -0.0062 -0.0017 0.0000  301 ZN  A ZN  
2277 S  S   . DMS C .   ? 0.2874 0.5259 0.4426 -0.0040 0.0472  -0.0860 302 DMS A S   
2278 O  O   . DMS C .   ? 0.2152 0.4009 1.0484 -0.0006 -0.0160 0.3169  302 DMS A O   
2279 C  C1  . DMS C .   ? 0.3671 0.4433 0.4016 0.1863  0.0833  -0.0820 302 DMS A C1  
2280 C  C2  . DMS C .   ? 0.2460 0.2734 0.2802 0.0362  0.0414  -0.0577 302 DMS A C2  
2281 N  N1  . BCN D .   ? 0.4817 0.4724 0.3571 -0.0052 0.0671  -0.1523 303 BCN A N1  
2282 C  C1  . BCN D .   ? 0.3571 0.4964 0.2626 -0.1421 0.0331  -0.0048 303 BCN A C1  
2283 C  C2  . BCN D .   ? 0.3567 0.4875 0.4178 -0.1685 0.0500  0.0430  303 BCN A C2  
2284 O  O21 . BCN D .   ? 0.5946 0.7106 0.4742 -0.2991 -0.1242 0.1738  303 BCN A O21 
2285 O  O22 . BCN D .   ? 0.4623 0.4548 0.3474 -0.0093 0.0130  0.0812  303 BCN A O22 
2286 C  C3  . BCN D .   ? 0.3409 0.2533 0.3567 -0.0487 0.0790  0.0562  303 BCN A C3  
2287 C  C4  . BCN D .   ? 0.4674 0.6646 0.6826 0.0313  -0.0829 -0.0912 303 BCN A C4  
2288 O  O4  . BCN D .   ? 0.3409 0.6430 0.7566 -0.1448 -0.0829 0.2010  303 BCN A O4  
2289 C  C5  . BCN D .   ? 0.2331 0.1878 0.3046 -0.0285 0.0568  0.0241  303 BCN A C5  
2290 C  C6  . BCN D .   ? 0.7203 0.3657 0.4803 -0.1289 0.0763  -0.0692 303 BCN A C6  
2291 O  O6  . BCN D .   ? 1.0384 0.4810 0.5874 -0.2707 0.0000  0.1110  303 BCN A O6  
2292 O  O9  . WW3 E .   ? 0.0934 0.0992 0.1079 -0.0076 -0.0076 -0.0092 304 WW3 A O9  
2293 S  S7  . WW3 E .   ? 0.0900 0.0935 0.1017 -0.0076 -0.0068 -0.0065 304 WW3 A S7  
2294 O  O8  . WW3 E .   ? 0.0926 0.0988 0.1113 -0.0027 0.0065  -0.0031 304 WW3 A O8  
2295 N  N10 . WW3 E .   ? 0.0904 0.0882 0.1106 -0.0186 -0.0108 0.0026  304 WW3 A N10 
2296 C  C3  . WW3 E .   ? 0.1189 0.1156 0.0944 -0.0219 0.0005  -0.0107 304 WW3 A C3  
2297 C  C2  . WW3 E .   ? 0.1316 0.1041 0.1404 -0.0093 -0.0183 0.0006  304 WW3 A C2  
2298 C  C4  . WW3 E .   ? 0.1289 0.1067 0.1212 -0.0186 0.0027  -0.0091 304 WW3 A C4  
2299 C  C5  . WW3 E .   ? 0.1483 0.1142 0.1262 -0.0262 0.0057  0.0003  304 WW3 A C5  
2300 C  C6  . WW3 E .   ? 0.1713 0.1010 0.1368 -0.0107 0.0082  0.0057  304 WW3 A C6  
2301 C  C1  . WW3 E .   ? 0.1431 0.1167 0.1542 -0.0217 -0.0204 0.0131  304 WW3 A C1  
2302 N  N11 . WW3 E .   ? 0.1650 0.1277 0.1798 -0.0181 0.0062  0.0208  304 WW3 A N11 
2303 N  N12 . WW3 E .   ? 0.2302 0.2601 0.3768 -0.0630 -0.0208 0.1334  304 WW3 A N12 
2304 N  N13 . WW3 E .   ? 0.2055 0.2266 0.2734 -0.0706 -0.0043 0.0776  304 WW3 A N13 
2305 C  C16 . WW3 E .   ? 0.2896 0.4307 0.3919 0.0700  -0.1093 0.0307  304 WW3 A C16 
2306 C  C15 . WW3 E .   ? 0.4896 0.3840 0.6621 0.0447  -0.0790 0.0120  304 WW3 A C15 
2307 C  C17 . WW3 E .   ? 0.2967 0.5370 0.3991 0.0553  0.0207  -0.1942 304 WW3 A C17 
2308 C  C18 . WW3 E .   ? 0.3377 0.2270 0.6445 -0.0152 -0.0842 -0.0414 304 WW3 A C18 
2309 C  C19 . WW3 E .   ? 0.5993 0.2601 0.3725 -0.1351 -0.0731 0.1368  304 WW3 A C19 
2310 C  C14 . WW3 E .   ? 0.2860 0.2026 0.2293 -0.0177 -0.0052 0.0317  304 WW3 A C14 
2311 O  O   . HOH F .   ? 0.1061 0.1280 0.1304 -0.0043 0.0153  -0.0006 401 HOH A O   
2312 O  O   . HOH F .   ? 0.4864 0.6539 0.4771 -0.0627 0.2642  -0.0221 402 HOH A O   
2313 O  O   . HOH F .   ? 0.3050 0.1831 0.2036 -0.0054 -0.0944 0.0092  403 HOH A O   
2314 O  O   . HOH F .   ? 0.1333 0.1176 0.1307 0.0120  -0.0098 -0.0060 404 HOH A O   
2315 O  O   . HOH F .   ? 0.1307 0.1295 0.1360 -0.0103 0.0096  -0.0171 405 HOH A O   
2316 O  O   . HOH F .   ? 0.2356 0.1888 0.2122 -0.0155 -0.0573 -0.0027 406 HOH A O   
2317 O  O   . HOH F .   ? 0.1316 0.1536 0.1712 0.0293  -0.0173 0.0166  407 HOH A O   
2318 O  O   . HOH F .   ? 0.1272 0.1208 0.1735 0.0155  -0.0041 -0.0020 408 HOH A O   
2319 O  O   . HOH F .   ? 0.1743 0.1588 0.2019 0.0414  0.0164  0.0193  409 HOH A O   
2320 O  O   . HOH F .   ? 0.0935 0.1641 0.2136 -0.0027 -0.0093 -0.0359 410 HOH A O   
2321 O  O   . HOH F .   ? 0.1526 0.1190 0.1308 -0.0098 0.0087  -0.0097 411 HOH A O   
2322 O  O   . HOH F .   ? 0.2942 0.2748 0.2791 -0.0362 0.0074  -0.0087 412 HOH A O   
2323 O  O   . HOH F .   ? 0.2257 0.2587 0.3276 0.0035  0.0838  0.0644  413 HOH A O   
2324 O  O   . HOH F .   ? 0.1304 0.2482 0.1695 -0.0141 -0.0452 0.0465  414 HOH A O   
2325 O  O   . HOH F .   ? 0.0952 0.2284 0.2403 0.0263  0.0175  -0.0276 415 HOH A O   
2326 O  O   . HOH F .   ? 0.1391 0.1544 0.1281 -0.0126 0.0142  -0.0087 416 HOH A O   
2327 O  O   . HOH F .   ? 0.2494 0.2117 0.2238 0.0439  0.0571  0.0881  417 HOH A O   
2328 O  O   . HOH F .   ? 0.3395 0.2939 0.6725 0.1088  0.1756  0.1414  418 HOH A O   
2329 O  O   . HOH F .   ? 0.4850 0.3438 0.1455 0.0147  0.0152  0.0142  419 HOH A O   
2330 O  O   . HOH F .   ? 0.1712 0.1712 0.2266 -0.0192 0.0362  -0.0096 420 HOH A O   
2331 O  O   . HOH F .   ? 0.1544 0.1277 0.1438 -0.0020 0.0092  -0.0113 421 HOH A O   
2332 O  O   . HOH F .   ? 0.4494 0.1869 0.2046 -0.0619 -0.0394 -0.0046 422 HOH A O   
2333 O  O   . HOH F .   ? 0.1221 0.1756 0.3470 -0.0102 -0.0119 0.0113  423 HOH A O   
2334 O  O   . HOH F .   ? 0.1253 0.1578 0.1244 0.0214  -0.0096 -0.0015 424 HOH A O   
2335 O  O   . HOH F .   ? 0.1713 0.1208 0.0970 -0.0125 -0.0051 0.0057  425 HOH A O   
2336 O  O   . HOH F .   ? 0.1203 0.1808 0.1482 0.0006  -0.0282 0.0231  426 HOH A O   
2337 O  O   . HOH F .   ? 0.2379 0.1897 0.2526 -0.0439 -0.0562 0.0388  427 HOH A O   
2338 O  O   . HOH F .   ? 0.2978 0.3201 0.2435 -0.0114 0.0564  -0.0511 428 HOH A O   
2339 O  O   . HOH F .   ? 0.2662 0.2197 0.1888 -0.0230 0.0710  0.0230  429 HOH A O   
2340 O  O   . HOH F .   ? 0.2114 0.1439 0.2205 -0.0250 -0.0164 -0.0119 430 HOH A O   
2341 O  O   . HOH F .   ? 0.4192 0.2169 0.2152 -0.0807 -0.0662 -0.0006 431 HOH A O   
2342 O  O   . HOH F .   ? 0.4753 0.4189 0.2917 -0.0392 -0.0746 0.0873  432 HOH A O   
2343 O  O   . HOH F .   ? 0.1395 0.1756 0.3420 -0.0329 -0.0741 0.0097  433 HOH A O   
2344 O  O   . HOH F .   ? 0.1825 0.3312 0.3510 0.0693  -0.0781 -0.0626 434 HOH A O   
2345 O  O   . HOH F .   ? 0.1835 0.1755 0.1796 0.0063  -0.0344 -0.0006 435 HOH A O   
2346 O  O   . HOH F .   ? 0.1656 0.1916 0.1905 0.0359  -0.0195 0.0164  436 HOH A O   
2347 O  O   . HOH F .   ? 0.1916 0.2231 0.2928 0.0216  -0.1049 -0.0414 437 HOH A O   
2348 O  O   . HOH F .   ? 0.3215 0.2313 0.2842 -0.0107 -0.0723 0.0623  438 HOH A O   
2349 O  O   . HOH F .   ? 0.1665 0.1314 0.1791 -0.0093 -0.0296 -0.0034 439 HOH A O   
2350 O  O   . HOH F .   ? 0.2899 0.2099 0.2540 0.0430  0.0524  0.0269  440 HOH A O   
2351 O  O   . HOH F .   ? 0.5198 0.2960 0.2397 -0.0339 0.1325  -0.1010 441 HOH A O   
2352 O  O   . HOH F .   ? 0.1782 0.2043 0.1588 0.0038  0.0131  -0.0068 442 HOH A O   
2353 O  O   . HOH F .   ? 0.2662 0.2684 0.2903 0.0052  -0.0184 0.0386  443 HOH A O   
2354 O  O   . HOH F .   ? 0.2117 0.2755 0.2705 0.0071  0.0031  0.0258  444 HOH A O   
2355 O  O   . HOH F .   ? 0.2169 0.5001 0.2474 0.0294  0.0295  -0.0043 445 HOH A O   
2356 O  O   . HOH F .   ? 0.1844 0.1481 0.1756 -0.0026 0.0020  0.0102  446 HOH A O   
2357 O  O   . HOH F .   ? 0.1913 0.2328 0.1965 0.0006  -0.0505 0.0351  447 HOH A O   
2358 O  O   . HOH F .   ? 0.2108 0.2211 0.2770 0.0263  0.0093  -0.0104 448 HOH A O   
2359 O  O   . HOH F .   ? 0.2229 0.2397 0.1984 0.0163  0.0579  -0.0195 449 HOH A O   
2360 O  O   . HOH F .   ? 0.2011 0.2320 0.2258 0.0403  -0.0480 0.0218  450 HOH A O   
2361 O  O   . HOH F .   ? 0.1370 0.1912 0.2504 -0.0046 0.0141  0.0142  451 HOH A O   
2362 O  O   . HOH F .   ? 0.2928 0.2723 0.3255 0.0623  -0.1580 -0.0251 452 HOH A O   
2363 O  O   . HOH F .   ? 0.2982 0.3718 0.2752 -0.0916 0.1048  0.0049  453 HOH A O   
2364 O  O   . HOH F .   ? 0.2299 0.1535 0.1879 0.0177  -0.0093 0.0109  454 HOH A O   
2365 O  O   . HOH F .   ? 0.1834 0.2442 0.2730 -0.0024 0.0104  -0.0186 455 HOH A O   
2366 O  O   . HOH F .   ? 0.3495 0.3707 0.4088 0.0450  0.0776  -0.1186 456 HOH A O   
2367 O  O   . HOH F .   ? 0.2399 0.1984 0.1333 0.0270  -0.0218 -0.0131 457 HOH A O   
2368 O  O   . HOH F .   ? 0.1731 0.1570 0.1509 0.0049  -0.0109 -0.0141 458 HOH A O   
2369 O  O   . HOH F .   ? 0.3901 0.1796 0.2054 0.0326  -0.1342 0.0065  459 HOH A O   
2370 O  O   . HOH F .   ? 0.3104 0.3621 0.2777 -0.1316 0.0249  -0.0829 460 HOH A O   
2371 O  O   . HOH F .   ? 0.2397 0.2257 0.2766 -0.0052 -0.0511 -0.0851 461 HOH A O   
2372 O  O   . HOH F .   ? 0.5630 0.2831 0.1613 -0.0390 -0.0230 -0.0252 462 HOH A O   
2373 O  O   . HOH F .   ? 0.2442 0.1386 0.1868 0.0214  -0.0103 -0.0109 463 HOH A O   
2374 O  O   . HOH F .   ? 0.3147 0.2270 0.2888 -0.0049 -0.0749 -0.0291 464 HOH A O   
2375 O  O   . HOH F .   ? 0.4724 0.2449 0.2134 0.0715  0.0335  0.0333  465 HOH A O   
2376 O  O   . HOH F .   ? 0.2037 0.1842 0.1896 0.0043  -0.0240 0.0015  466 HOH A O   
2377 O  O   . HOH F .   ? 0.1678 0.1287 0.1819 -0.0126 -0.0186 0.0052  467 HOH A O   
2378 O  O   . HOH F .   ? 0.3970 0.2135 0.3009 0.0922  0.0566  0.0908  468 HOH A O   
2379 O  O   . HOH F .   ? 0.3521 0.5554 0.2073 -0.1439 -0.1253 0.0710  469 HOH A O   
2380 O  O   . HOH F .   ? 0.3585 0.2090 0.2669 -0.0452 0.0236  -0.0104 470 HOH A O   
2381 O  O   . HOH F .   ? 0.1342 0.3287 0.3797 -0.0320 -0.0337 0.0524  471 HOH A O   
2382 O  O   . HOH F .   ? 0.3043 0.1377 0.2417 0.0353  -0.1136 -0.0091 472 HOH A O   
2383 O  O   . HOH F .   ? 0.3554 0.2608 0.1579 -0.0239 -0.0515 0.0175  473 HOH A O   
2384 O  O   . HOH F .   ? 0.4778 0.2195 0.3334 0.1562  -0.1084 -0.0302 474 HOH A O   
2385 O  O   . HOH F .   ? 0.2451 0.2178 0.2745 0.0362  0.0194  0.0515  475 HOH A O   
2386 O  O   . HOH F .   ? 0.1457 0.3765 0.2601 0.0188  -0.0046 0.1013  476 HOH A O   
2387 O  O   . HOH F .   ? 0.2888 0.1421 0.2328 -0.0154 0.0017  0.0076  477 HOH A O   
2388 O  O   . HOH F .   ? 0.2144 0.1428 0.2027 0.0065  -0.0177 0.0109  478 HOH A O   
2389 O  O   . HOH F .   ? 0.3172 0.2478 0.2106 0.0142  -0.0886 -0.0417 479 HOH A O   
2390 O  O   . HOH F .   ? 0.3750 0.2071 0.1667 0.0882  -0.0696 -0.0410 480 HOH A O   
2391 O  O   . HOH F .   ? 0.3014 0.3621 0.3122 0.1303  -0.0566 -0.0306 481 HOH A O   
2392 O  O   . HOH F .   ? 0.3068 0.2277 0.4120 0.0388  0.0710  0.0408  482 HOH A O   
2393 O  O   . HOH F .   ? 0.2300 0.2389 0.1629 0.0076  0.0040  -0.0162 483 HOH A O   
2394 O  O   . HOH F .   ? 0.2727 0.2010 0.2576 0.0276  -0.0489 -0.0215 484 HOH A O   
2395 O  O   . HOH F .   ? 0.2442 0.2863 0.3406 0.1307  -0.0026 0.0230  485 HOH A O   
2396 O  O   . HOH F .   ? 0.3894 0.3628 0.2558 0.1439  -0.0176 -0.0982 486 HOH A O   
2397 O  O   . HOH F .   ? 0.3607 0.3348 0.2295 0.0617  0.0136  -0.0577 487 HOH A O   
2398 O  O   . HOH F .   ? 0.2777 0.3650 0.3492 0.0957  0.0750  0.0337  488 HOH A O   
2399 O  O   . HOH F .   ? 0.2996 0.2381 0.2712 0.0568  0.0619  -0.0115 489 HOH A O   
2400 O  O   . HOH F .   ? 0.2496 0.2064 0.1787 0.0381  -0.0096 0.0414  490 HOH A O   
2401 O  O   . HOH F .   ? 0.3876 0.1879 0.2748 0.0551  -0.0226 -0.0287 491 HOH A O   
2402 O  O   . HOH F .   ? 0.2788 0.2511 0.2070 0.0003  -0.0294 0.0366  492 HOH A O   
2403 O  O   . HOH F .   ? 0.2230 0.3093 0.1816 -0.0339 -0.0068 -0.0634 493 HOH A O   
2404 O  O   . HOH F .   ? 0.3151 0.2489 0.2250 -0.0895 -0.0205 -0.0109 494 HOH A O   
2405 O  O   . HOH F .   ? 0.3420 0.2442 0.3409 -0.0397 0.0847  -0.0917 495 HOH A O   
2406 O  O   . HOH F .   ? 0.2674 0.4580 0.2698 -0.1230 -0.0241 -0.0228 496 HOH A O   
2407 O  O   . HOH F .   ? 0.6855 0.2741 0.1580 0.0241  0.0653  0.0065  497 HOH A O   
2408 O  O   . HOH F .   ? 0.2597 0.2680 0.2820 -0.0195 0.0063  -0.0142 498 HOH A O   
2409 O  O   . HOH F .   ? 0.6413 0.2379 0.1922 -0.0908 -0.0020 0.0452  499 HOH A O   
2410 O  O   . HOH F .   ? 0.2777 0.2106 0.3088 -0.1225 -0.0662 -0.0126 500 HOH A O   
2411 O  O   . HOH F .   ? 0.3973 0.2702 0.2116 -0.1054 0.1062  -0.0766 501 HOH A O   
2412 O  O   . HOH F .   ? 0.3416 0.3499 0.4702 0.0040  -0.0329 0.2212  502 HOH A O   
2413 O  O   . HOH F .   ? 0.2471 0.2356 0.2874 0.0115  -0.0065 -0.0403 503 HOH A O   
2414 O  O   . HOH F .   ? 0.2212 0.1756 0.2492 0.0397  -0.0087 -0.0355 504 HOH A O   
2415 O  O   . HOH F .   ? 0.1817 0.2657 0.3646 -0.0696 -0.0249 0.1190  505 HOH A O   
2416 O  O   . HOH F .   ? 0.3847 0.3600 0.2122 -0.1206 -0.0529 -0.0243 506 HOH A O   
2417 O  O   . HOH F .   ? 0.2266 0.2149 0.6057 0.0469  0.0564  -0.0820 507 HOH A O   
2418 O  O   . HOH F .   ? 0.3054 0.3524 0.3786 0.0252  -0.0922 -0.2081 508 HOH A O   
2419 O  O   . HOH F .   ? 0.3639 0.2425 0.3262 -0.0304 -0.1032 -0.0003 509 HOH A O   
2420 O  O   . HOH F .   ? 0.6819 0.3043 0.3844 -0.0126 -0.0898 -0.0930 510 HOH A O   
2421 O  O   . HOH F .   ? 0.1351 0.4239 0.4131 0.0315  0.0046  0.1383  511 HOH A O   
2422 O  O   . HOH F .   ? 0.2838 0.5052 0.3883 0.0631  0.1054  0.0798  512 HOH A O   
2423 O  O   . HOH F .   ? 0.5497 0.3337 0.3542 -0.0237 0.1435  0.1368  513 HOH A O   
2424 O  O   . HOH F .   ? 0.2353 0.2651 0.2367 0.0529  -0.0537 -0.0109 514 HOH A O   
2425 O  O   . HOH F .   ? 0.3470 0.6524 0.2029 0.0071  0.0529  0.1172  515 HOH A O   
2426 O  O   . HOH F .   ? 0.2435 0.2515 0.1849 0.0399  0.0140  0.0335  516 HOH A O   
2427 O  O   . HOH F .   ? 0.5145 0.4020 0.2356 0.2824  -0.0577 0.0174  517 HOH A O   
2428 O  O   . HOH F .   ? 0.3265 0.2011 0.3948 -0.0142 -0.0549 -0.0057 518 HOH A O   
2429 O  O   . HOH F .   ? 0.2673 0.3424 0.2957 -0.0533 0.0684  -0.0829 519 HOH A O   
2430 O  O   . HOH F .   ? 0.4616 0.3395 0.3607 -0.0491 -0.1342 -0.0195 520 HOH A O   
2431 O  O   . HOH F .   ? 0.3377 0.2302 0.7318 0.0000  0.1057  0.0604  521 HOH A O   
2432 O  O   . HOH F .   ? 0.2824 0.2601 0.4372 0.0197  0.0414  0.0635  522 HOH A O   
2433 O  O   . HOH F .   ? 0.6014 0.3420 0.4738 -0.0908 -0.2506 0.1615  523 HOH A O   
2434 O  O   . HOH F .   ? 0.3713 0.4695 0.3431 -0.0575 -0.0230 -0.0500 524 HOH A O   
2435 O  O   . HOH F .   ? 0.2766 0.4063 0.4020 -0.2196 -0.0333 0.0850  525 HOH A O   
2436 O  O   . HOH F .   ? 0.3064 0.4167 0.2605 0.0445  -0.0357 -0.0104 526 HOH A O   
2437 O  O   . HOH F .   ? 0.4016 0.2576 0.2612 -0.0291 -0.0762 0.1356  527 HOH A O   
2438 O  O   . HOH F .   ? 0.7044 0.4318 0.4160 -0.0048 -0.0606 -0.0068 528 HOH A O   
2439 O  O   . HOH F .   ? 0.4045 0.6646 0.3312 -0.1993 0.0581  -0.0403 529 HOH A O   
2440 O  O   . HOH F .   ? 0.3172 0.2197 0.2669 0.0043  -0.0683 -0.0054 530 HOH A O   
2441 O  O   . HOH F .   ? 0.2949 0.3898 0.2338 -0.0754 0.0230  -0.0392 531 HOH A O   
2442 O  O   . HOH F .   ? 0.2748 0.2011 0.2691 0.0185  0.0161  0.0584  532 HOH A O   
2443 O  O   . HOH F .   ? 0.3226 0.5080 0.3675 0.0688  0.0087  -0.1630 533 HOH A O   
2444 O  O   . HOH F .   ? 0.3276 0.6330 0.2170 0.0688  -0.0086 0.0359  534 HOH A O   
2445 O  O   . HOH F .   ? 0.2888 0.1949 0.2195 0.0186  -0.0480 -0.0142 535 HOH A O   
2446 O  O   . HOH F .   ? 0.1959 0.2676 0.3262 0.0087  0.0146  -0.0093 536 HOH A O   
2447 O  O   . HOH F .   ? 0.3280 0.5343 0.3776 -0.0527 0.0493  -0.0265 537 HOH A O   
2448 O  O   . HOH F .   ? 0.5011 0.3944 0.4796 0.0710  0.3055  -0.0043 538 HOH A O   
2449 O  O   . HOH F .   ? 0.3287 0.3671 0.4275 0.1044  0.1448  -0.0131 539 HOH A O   
2450 O  O   . HOH F .   ? 0.4156 0.2852 0.5546 -0.1668 -0.0046 0.0500  540 HOH A O   
2451 O  O   . HOH F .   ? 0.7954 0.2637 0.7329 0.0746  0.1186  0.0263  541 HOH A O   
2452 O  O   . HOH F .   ? 0.6334 0.2410 0.2363 0.0666  -0.0913 0.0500  542 HOH A O   
2453 O  O   . HOH F .   ? 0.5116 0.3158 0.6223 -0.0728 -0.0623 -0.1464 543 HOH A O   
2454 O  O   . HOH F .   ? 0.6280 0.2533 0.6506 0.0263  0.2599  0.0863  544 HOH A O   
2455 O  O   . HOH F .   ? 0.5827 0.3855 0.4627 -0.0362 -0.2143 0.0948  545 HOH A O   
2456 O  O   . HOH F .   ? 0.5540 0.3262 0.2529 0.0653  0.1199  0.0935  546 HOH A O   
2457 O  O   . HOH F .   ? 0.2088 0.2770 0.2399 0.0003  -0.0351 0.0091  547 HOH A O   
2458 O  O   . HOH F .   ? 0.4889 0.6664 0.3880 0.1128  0.0692  -0.0461 548 HOH A O   
2459 O  O   . HOH F .   ? 0.2680 0.3158 0.5748 -0.0054 -0.1040 -0.0146 549 HOH A O   
2460 O  O   . HOH F .   ? 0.4275 0.4980 0.1435 0.1093  0.0124  0.0281  550 HOH A O   
2461 O  O   . HOH F .   ? 0.1612 0.5317 0.3984 -0.0237 0.0057  0.0184  551 HOH A O   
2462 O  O   . HOH F .   ? 0.3244 0.4070 0.2827 -0.0807 0.0759  -0.1590 552 HOH A O   
2463 O  O   . HOH F .   ? 0.2361 0.5623 0.2806 0.0700  0.0342  0.0340  553 HOH A O   
2464 O  O   . HOH F .   ? 0.2018 0.2899 0.7055 -0.0546 0.1206  0.0286  554 HOH A O   
2465 O  O   . HOH F .   ? 0.2293 0.6183 0.2626 -0.0231 -0.0305 0.1098  555 HOH A O   
2466 O  O   . HOH F .   ? 0.3607 0.3517 0.2576 -0.0186 -0.0274 0.0216  556 HOH A O   
2467 O  O   . HOH F .   ? 0.3104 0.3082 0.4451 -0.0219 -0.0003 0.0151  557 HOH A O   
2468 O  O   . HOH F .   ? 0.6478 0.3668 0.3970 -0.0241 0.1403  -0.0696 558 HOH A O   
2469 O  O   . HOH F .   ? 0.2046 0.5985 0.3555 0.0524  0.0010  -0.0068 559 HOH A O   
2470 O  O   . HOH F .   ? 0.4404 0.5055 0.5346 0.1430  0.2116  0.0930  560 HOH A O   
2471 O  O   . HOH F .   ? 0.3154 0.6747 0.4760 -0.0230 0.1298  0.1032  561 HOH A O   
2472 O  O   . HOH F .   ? 0.3212 0.6646 0.2752 0.0118  0.0873  -0.0006 562 HOH A O   
2473 O  O   . HOH F .   ? 0.3054 0.3165 0.4142 0.0035  0.1536  0.0626  563 HOH A O   
2474 O  O   . HOH F .   ? 0.3431 0.2425 0.2888 -0.0057 -0.0494 -0.0082 564 HOH A O   
2475 O  O   . HOH F .   ? 0.4307 0.3574 0.2327 0.0535  -0.0520 -0.0812 565 HOH A O   
2476 O  O   . HOH F .   ? 0.4774 0.3998 0.2331 -0.0951 0.0273  -0.0649 566 HOH A O   
2477 O  O   . HOH F .   ? 0.2004 0.3086 0.4336 0.0445  -0.0140 -0.0219 567 HOH A O   
2478 O  O   . HOH F .   ? 0.6226 0.3564 0.3323 -0.1194 -0.2046 0.0208  568 HOH A O   
2479 O  O   . HOH F .   ? 0.7282 0.4199 0.3919 0.1599  0.0476  0.0318  569 HOH A O   
2480 O  O   . HOH F .   ? 0.2081 0.3521 0.3420 0.0509  0.0445  0.0447  570 HOH A O   
2481 O  O   . HOH F .   ? 0.3603 0.3105 0.3567 0.0206  -0.0091 0.0350  571 HOH A O   
2482 O  O   . HOH F .   ? 0.2820 0.2946 0.5173 -0.0068 0.0153  -0.1067 572 HOH A O   
2483 O  O   . HOH F .   ? 0.4444 0.4932 0.4257 -0.0274 -0.1500 -0.0644 573 HOH A O   
2484 O  O   . HOH F .   ? 0.2576 0.3158 0.5260 -0.0675 0.0390  -0.0060 574 HOH A O   
2485 O  O   . HOH F .   ? 0.3819 0.4731 0.6682 0.1993  0.2554  0.3122  575 HOH A O   
2486 O  O   . HOH F .   ? 0.4610 0.4128 0.2579 -0.0983 0.0375  0.0248  576 HOH A O   
2487 O  O   . HOH F .   ? 0.2435 0.8356 0.3409 -0.0109 -0.0366 0.0368  577 HOH A O   
2488 O  O   . HOH F .   ? 0.5062 0.2270 0.6898 0.0631  -0.0542 0.0575  578 HOH A O   
2489 O  O   . HOH F .   ? 0.2673 0.3977 0.3054 -0.0263 0.0406  0.0965  579 HOH A O   
2490 O  O   . HOH F .   ? 0.5774 0.4074 0.3262 0.0864  0.1014  0.0824  580 HOH A O   
2491 O  O   . HOH F .   ? 0.7085 0.5406 0.3003 -0.1993 0.0174  0.0891  581 HOH A O   
2492 O  O   . HOH F .   ? 0.2615 0.4508 0.3169 -0.0684 -0.1163 0.0546  582 HOH A O   
2493 O  O   . HOH F .   ? 0.2982 0.3722 1.0542 -0.0478 0.0154  0.0164  583 HOH A O   
2494 O  O   . HOH F .   ? 0.4706 0.2892 0.2903 0.0000  0.0432  0.0182  584 HOH A O   
2495 O  O   . HOH F .   ? 0.6527 0.5867 0.2644 -0.1456 0.0125  -0.1254 585 HOH A O   
2496 O  O   . HOH F .   ? 0.4052 0.3718 0.2579 0.1023  -0.1032 0.0337  586 HOH A O   
2497 O  O   . HOH F .   ? 0.4149 0.3158 0.4408 -0.1630 -0.1368 0.0995  587 HOH A O   
2498 O  O   . HOH F .   ? 0.3438 0.3905 0.4817 -0.1421 0.1879  -0.1080 588 HOH A O   
2499 O  O   . HOH F .   ? 0.3481 0.3183 0.2996 -0.0520 -0.0746 -0.0592 589 HOH A O   
2500 O  O   . HOH F .   ? 0.4577 0.3039 0.3251 0.1127  0.0688  0.0428  590 HOH A O   
2501 O  O   . HOH F .   ? 0.3560 0.2518 0.5802 0.0013  0.0658  -0.1825 591 HOH A O   
2502 O  O   . HOH F .   ? 0.5378 0.6384 0.3248 -0.2389 0.0723  -0.1128 592 HOH A O   
2503 O  O   . HOH F .   ? 0.5266 0.2850 0.7613 -0.0639 0.0108  -0.0553 593 HOH A O   
2504 O  O   . HOH F .   ? 0.3768 0.4286 0.5611 -0.1791 -0.2364 0.1914  594 HOH A O   
2505 O  O   . HOH F .   ? 0.6086 0.5457 0.4803 -0.1092 0.1746  -0.1596 595 HOH A O   
2506 O  O   . HOH F .   ? 0.2529 0.4501 0.3039 -0.1234 0.0434  -0.0913 596 HOH A O   
2507 O  O   . HOH F .   ? 0.5166 0.5091 0.3582 -0.0146 0.0944  0.1666  597 HOH A O   
2508 O  O   . HOH F .   ? 0.3129 0.4742 0.3488 0.1350  0.0925  0.0024  598 HOH A O   
2509 O  O   . HOH F .   ? 0.2991 0.3639 0.7613 0.0562  0.0024  0.0966  599 HOH A O   
2510 O  O   . HOH F .   ? 0.4059 0.4717 0.3280 0.1939  0.0904  0.1098  600 HOH A O   
2511 O  O   . HOH F .   ? 0.5921 0.4702 0.2759 0.0754  -0.0781 0.0285  601 HOH A O   
2512 O  O   . HOH F .   ? 0.3488 0.4088 0.5963 -0.0091 -0.0006 0.0794  602 HOH A O   
2513 O  O   . HOH F .   ? 0.5137 0.5454 0.4566 0.1861  0.0379  0.2072  603 HOH A O   
2514 O  O   . HOH F .   ? 0.9161 0.5278 0.6643 0.0961  -0.2558 -0.1613 604 HOH A O   
2515 O  O   . HOH F .   ? 0.2386 0.3294 0.3269 -0.0096 -0.0229 0.0081  605 HOH A O   
2516 O  O   . HOH F .   ? 0.5709 0.4235 0.4494 -0.0430 -0.0046 -0.1234 606 HOH A O   
2517 O  O   . HOH F .   ? 0.6431 0.5120 0.6074 0.1448  0.2256  0.1440  607 HOH A O   
2518 O  O   . HOH F .   ? 0.3300 0.8942 0.3923 -0.0242 -0.0515 0.0186  608 HOH A O   
2519 O  O   . HOH F .   ? 0.4433 0.3889 0.5522 -0.1374 0.0126  -0.1489 609 HOH A O   
2520 O  O   . HOH F .   ? 0.4839 0.6883 0.3930 0.0423  -0.0806 0.2248  610 HOH A O   
2521 O  O   . HOH F .   ? 0.3125 0.3651 0.1906 -0.0020 0.0342  -0.0216 611 HOH A O   
2522 O  O   . HOH F .   ? 0.3147 0.1448 0.3847 -0.0274 0.1254  -0.0171 612 HOH A O   
2523 O  O   . HOH F .   ? 0.2935 0.3190 0.7037 0.1001  0.0912  0.0238  613 HOH A O   
2524 O  O   . HOH F .   ? 0.4361 0.5554 0.6280 0.2700  -0.0656 0.0126  614 HOH A O   
2525 O  O   . HOH F .   ? 0.7968 0.4638 0.3452 0.0219  0.1861  -0.0951 615 HOH A O   
2526 O  O   . HOH F .   ? 0.5515 0.3273 1.0898 0.0339  0.0886  0.0922  616 HOH A O   
2527 O  O   . HOH F .   ? 0.1632 0.3147 0.3495 0.0621  0.0498  0.0035  617 HOH A O   
2528 O  O   . HOH F .   ? 0.4185 0.3524 0.3009 -0.0621 -0.0644 0.1168  618 HOH A O   
2529 O  O   . HOH F .   ? 0.4318 0.4318 0.2106 0.0313  0.0562  -0.1066 619 HOH A O   
2530 O  O   . HOH F .   ? 0.2331 0.3240 0.3553 -0.0038 0.0318  0.0161  620 HOH A O   
2531 O  O   . HOH F .   ? 0.3061 0.5159 0.3865 -0.1712 0.0306  -0.0057 621 HOH A O   
2532 O  O   . HOH F .   ? 0.2196 0.3348 0.4092 0.0368  0.0302  0.0948  622 HOH A O   
2533 O  O   . HOH F .   ? 0.3513 0.4347 0.4271 -0.0051 0.0753  0.0006  623 HOH A O   
2534 O  O   . HOH F .   ? 0.3840 0.5317 0.6693 0.2149  -0.1040 -0.1775 624 HOH A O   
2535 O  O   . HOH F .   ? 0.3883 0.2799 0.7760 0.0965  -0.0115 -0.0706 625 HOH A O   
2536 O  O   . HOH F .   ? 0.4268 0.2748 0.2125 -0.0198 -0.0275 0.0570  626 HOH A O   
2537 O  O   . HOH F .   ? 0.5457 0.3485 0.3072 -0.0465 0.0640  -0.0175 627 HOH A O   
2538 O  O   . HOH F .   ? 0.5199 0.2590 0.7360 -0.0474 -0.3239 0.1150  628 HOH A O   
2539 O  O   . HOH F .   ? 0.3355 0.4081 0.3517 -0.0250 0.0114  0.1044  629 HOH A O   
2540 O  O   . HOH F .   ? 0.7893 0.3840 0.3804 0.2293  0.2336  0.2329  630 HOH A O   
2541 O  O   . HOH F .   ? 0.5170 0.3890 0.3309 -0.1647 -0.0763 0.0333  631 HOH A O   
2542 O  O   . HOH F .   ? 0.3194 0.3574 0.2878 -0.0098 0.0082  -0.0781 632 HOH A O   
2543 O  O   . HOH F .   ? 0.3391 0.2791 0.4210 0.0606  -0.1150 0.0275  633 HOH A O   
2544 O  O   . HOH F .   ? 0.3105 0.2569 0.2917 -0.0049 -0.0137 0.0798  634 HOH A O   
2545 O  O   . HOH F .   ? 0.4135 0.2275 0.4221 -0.0166 0.0912  0.0680  635 HOH A O   
2546 O  O   . HOH F .   ? 0.2910 0.6291 0.6474 -0.0745 0.0935  -0.0193 636 HOH A O   
2547 O  O   . HOH F .   ? 0.4690 0.6786 0.4099 0.0939  0.0979  0.1509  637 HOH A O   
2548 O  O   . HOH F .   ? 0.3499 0.4706 0.5508 0.0454  0.0675  0.0908  638 HOH A O   
2549 O  O   . HOH F .   ? 0.3402 0.8963 0.4587 0.0263  0.0153  0.3271  639 HOH A O   
2550 O  O   . HOH F .   ? 0.2284 0.3273 0.2343 -0.0329 -0.0006 0.0353  640 HOH A O   
2551 O  O   . HOH F .   ? 0.2605 0.2734 0.4013 -0.0483 -0.0680 -0.0238 641 HOH A O   
2552 O  O   . HOH F .   ? 0.3987 0.3129 0.4803 0.0701  -0.0575 0.0597  642 HOH A O   
2553 O  O   . HOH F .   ? 0.3862 0.4307 0.5702 0.2122  -0.1492 -0.1271 643 HOH A O   
2554 O  O   . HOH F .   ? 0.2831 0.1940 0.3725 -0.0318 -0.0917 0.0107  644 HOH A O   
2555 O  O   . HOH F .   ? 0.3431 0.3470 0.2720 -0.0237 -0.0658 -0.0252 645 HOH A O   
2556 O  O   . HOH F .   ? 0.3840 0.4505 0.2228 -0.0593 -0.1221 0.1036  646 HOH A O   
2557 O  O   . HOH F .   ? 0.6819 0.3485 0.3499 0.1071  0.0939  0.0070  647 HOH A O   
2558 O  O   . HOH F .   ? 0.3025 0.7827 0.3434 0.1722  -0.0630 0.0538  648 HOH A O   
2559 O  O   . HOH F .   ? 0.4296 0.6074 0.3064 0.0869  0.0586  -0.0627 649 HOH A O   
2560 O  O   . HOH F .   ? 0.3711 0.3039 0.4483 -0.0671 0.0252  0.0388  650 HOH A O   
2561 O  O   . HOH F .   ? 0.5515 0.2389 0.4070 -0.0974 -0.0922 -0.0496 651 HOH A O   
2562 O  O   . HOH F .   ? 0.4397 0.7128 0.5928 -0.2802 0.0395  0.1631  652 HOH A O   
2563 O  O   . HOH F .   ? 0.4354 0.6018 0.3323 -0.0522 0.1368  -0.0232 653 HOH A O   
2564 O  O   . HOH F .   ? 0.3316 0.4990 0.7271 0.0798  0.0907  -0.2055 654 HOH A O   
2565 O  O   . HOH F .   ? 0.3495 0.4347 0.4271 0.0242  -0.0366 -0.2078 655 HOH A O   
2566 O  O   . HOH F .   ? 0.8597 0.3086 0.5346 0.0238  0.5055  0.0292  656 HOH A O   
2567 O  O   . HOH F .   ? 0.4282 0.2736 0.3434 0.0093  -0.0825 -0.0131 657 HOH A O   
2568 O  O   . HOH F .   ? 0.3912 0.3596 0.4052 0.1368  -0.0988 -0.0364 658 HOH A O   
2569 O  O   . HOH F .   ? 0.5368 0.3582 0.3740 -0.0261 -0.1333 0.0252  659 HOH A O   
2570 O  O   . HOH F .   ? 0.6072 0.3115 0.3233 -0.0164 0.1263  -0.0710 660 HOH A O   
2571 O  O   . HOH F .   ? 0.5630 0.5303 0.3869 -0.0154 -0.0807 -0.2073 661 HOH A O   
2572 O  O   . HOH F .   ? 0.5184 0.4979 0.7530 0.1576  0.2381  0.0263  662 HOH A O   
2573 O  O   . HOH F .   ? 0.5299 0.5654 0.3944 0.0273  -0.0785 0.0384  663 HOH A O   
2574 O  O   . HOH F .   ? 0.3898 0.4289 0.4465 0.0148  0.0776  -0.0353 664 HOH A O   
2575 O  O   . HOH F .   ? 0.4465 0.5090 0.5350 0.0146  0.1359  0.1004  665 HOH A O   
2576 O  O   . HOH F .   ? 0.2651 0.8176 0.3449 0.0812  -0.0443 -0.1014 666 HOH A O   
2577 O  O   . HOH F .   ? 0.3488 0.7110 0.2213 0.0381  -0.0063 -0.1386 667 HOH A O   
2578 O  O   . HOH F .   ? 0.6794 0.3172 0.3440 0.1216  -0.0306 -0.1208 668 HOH A O   
2579 O  O   . HOH F .   ? 0.4210 0.4138 0.6625 0.0249  -0.0207 -0.1124 669 HOH A O   
2580 O  O   . HOH F .   ? 0.4347 0.4034 0.6538 0.2187  0.0662  0.0274  670 HOH A O   
2581 O  O   . HOH F .   ? 0.3169 0.5921 0.7372 -0.1159 -0.0776 -0.0471 671 HOH A O   
2582 O  O   . HOH F .   ? 0.5471 0.3143 0.4185 -0.1316 0.0869  -0.0992 672 HOH A O   
2583 O  O   . HOH F .   ? 1.0671 0.5346 0.3255 -0.3364 0.1965  -0.1788 673 HOH A O   
2584 O  O   . HOH F .   ? 0.5095 0.4803 0.2842 -0.1709 0.1247  -0.2283 674 HOH A O   
2585 O  O   . HOH F .   ? 0.3906 0.4347 0.8424 0.0057  0.0768  0.0185  675 HOH A O   
2586 O  O   . HOH F .   ? 0.3086 0.4426 0.1834 0.1123  0.0000  0.0463  676 HOH A O   
2587 O  O   . HOH F .   ? 0.3416 0.7562 0.4803 0.0966  -0.0886 -0.3707 677 HOH A O   
2588 O  O   . HOH F .   ? 0.5722 0.2619 0.2638 0.0449  0.0262  0.0529  678 HOH A O   
2589 O  O   . HOH F .   ? 0.6247 0.6557 0.5447 -0.0285 -0.1247 0.0120  679 HOH A O   
2590 O  O   . HOH F .   ? 0.3779 0.3377 0.8036 -0.0237 0.0421  -0.0208 680 HOH A O   
2591 O  O   . HOH F .   ? 0.5155 0.6215 0.4505 0.0487  -0.1650 -0.1247 681 HOH A O   
2592 O  O   . HOH F .   ? 0.3546 0.4580 0.3018 -0.1260 0.0917  -0.1049 682 HOH A O   
2593 O  O   . HOH F .   ? 0.4106 0.5946 0.1994 -0.1509 0.0285  0.0262  683 HOH A O   
2594 O  O   . HOH F .   ? 0.5418 0.6674 0.3203 -0.0807 0.1497  -0.2025 684 HOH A O   
2595 O  O   . HOH F .   ? 0.5375 0.6057 0.5127 0.0366  -0.2459 -0.0697 685 HOH A O   
2596 O  O   . HOH F .   ? 0.5181 0.4077 0.5755 0.1736  -0.0480 -0.1357 686 HOH A O   
2597 O  O   . HOH F .   ? 0.2849 0.4179 0.3409 -0.0151 -0.0063 -0.0443 687 HOH A O   
2598 O  O   . HOH F .   ? 0.3661 0.3237 0.5052 0.0903  -0.1501 -0.0606 688 HOH A O   
2599 O  O   . HOH F .   ? 0.5070 0.3244 0.2806 0.0362  -0.0573 0.0812  689 HOH A O   
2600 O  O   . HOH F .   ? 0.6876 0.3592 0.4839 -0.0304 0.1563  0.0063  690 HOH A O   
2601 O  O   . HOH F .   ? 0.6808 0.5698 0.5109 0.0776  -0.1506 -0.2343 691 HOH A O   
2602 O  O   . HOH F .   ? 0.4013 0.5090 0.9182 0.0041  -0.1827 -0.1448 692 HOH A O   
2603 O  O   . HOH F .   ? 0.5830 0.4239 0.6600 -0.1465 -0.1393 0.0465  693 HOH A O   
2604 O  O   . HOH F .   ? 0.3959 0.2263 0.3319 -0.0262 -0.0013 -0.0417 694 HOH A O   
2605 O  O   . HOH F .   ? 0.4523 0.4882 0.9534 -0.0974 -0.0719 -0.1518 695 HOH A O   
2606 O  O   . HOH F .   ? 0.2809 0.4275 0.6315 -0.0856 0.1709  -0.1447 696 HOH A O   
2607 O  O   . HOH F .   ? 0.9779 0.4099 0.4562 0.1712  0.3377  0.1598  697 HOH A O   
2608 O  O   . HOH F .   ? 0.5784 0.3973 0.5860 0.0476  0.1198  -0.0162 698 HOH A O   
2609 O  O   . HOH F .   ? 0.9889 0.5475 0.4343 0.0687  0.2542  -0.1562 699 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   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 BCN 1   303 2   BCN BCN A . 
E 5 WW3 1   304 1   WW3 WW3 A . 
F 6 HOH 1   401 1   HOH HOH A . 
F 6 HOH 2   402 2   HOH HOH A . 
F 6 HOH 3   403 3   HOH HOH A . 
F 6 HOH 4   404 4   HOH HOH A . 
F 6 HOH 5   405 5   HOH HOH A . 
F 6 HOH 6   406 6   HOH HOH A . 
F 6 HOH 7   407 7   HOH HOH A . 
F 6 HOH 8   408 8   HOH HOH A . 
F 6 HOH 9   409 9   HOH HOH A . 
F 6 HOH 10  410 10  HOH HOH A . 
F 6 HOH 11  411 11  HOH HOH A . 
F 6 HOH 12  412 12  HOH HOH A . 
F 6 HOH 13  413 13  HOH HOH A . 
F 6 HOH 14  414 14  HOH HOH A . 
F 6 HOH 15  415 15  HOH HOH A . 
F 6 HOH 16  416 16  HOH HOH A . 
F 6 HOH 17  417 17  HOH HOH A . 
F 6 HOH 18  418 18  HOH HOH A . 
F 6 HOH 19  419 19  HOH HOH A . 
F 6 HOH 20  420 20  HOH HOH A . 
F 6 HOH 21  421 21  HOH HOH A . 
F 6 HOH 22  422 22  HOH HOH A . 
F 6 HOH 23  423 23  HOH HOH A . 
F 6 HOH 24  424 24  HOH HOH A . 
F 6 HOH 25  425 25  HOH HOH A . 
F 6 HOH 26  426 26  HOH HOH A . 
F 6 HOH 27  427 27  HOH HOH A . 
F 6 HOH 28  428 28  HOH HOH A . 
F 6 HOH 29  429 29  HOH HOH A . 
F 6 HOH 30  430 30  HOH HOH A . 
F 6 HOH 31  431 31  HOH HOH A . 
F 6 HOH 32  432 32  HOH HOH A . 
F 6 HOH 33  433 33  HOH HOH A . 
F 6 HOH 34  434 34  HOH HOH A . 
F 6 HOH 35  435 35  HOH HOH A . 
F 6 HOH 36  436 36  HOH HOH A . 
F 6 HOH 37  437 37  HOH HOH A . 
F 6 HOH 38  438 38  HOH HOH A . 
F 6 HOH 39  439 39  HOH HOH A . 
F 6 HOH 40  440 40  HOH HOH A . 
F 6 HOH 41  441 41  HOH HOH A . 
F 6 HOH 42  442 42  HOH HOH A . 
F 6 HOH 43  443 43  HOH HOH A . 
F 6 HOH 44  444 44  HOH HOH A . 
F 6 HOH 45  445 45  HOH HOH A . 
F 6 HOH 46  446 46  HOH HOH A . 
F 6 HOH 47  447 47  HOH HOH A . 
F 6 HOH 48  448 48  HOH HOH A . 
F 6 HOH 49  449 49  HOH HOH A . 
F 6 HOH 50  450 50  HOH HOH A . 
F 6 HOH 51  451 51  HOH HOH A . 
F 6 HOH 52  452 52  HOH HOH A . 
F 6 HOH 53  453 53  HOH HOH A . 
F 6 HOH 54  454 54  HOH HOH A . 
F 6 HOH 55  455 55  HOH HOH A . 
F 6 HOH 56  456 56  HOH HOH A . 
F 6 HOH 57  457 57  HOH HOH A . 
F 6 HOH 58  458 58  HOH HOH A . 
F 6 HOH 59  459 59  HOH HOH A . 
F 6 HOH 60  460 60  HOH HOH A . 
F 6 HOH 61  461 61  HOH HOH A . 
F 6 HOH 62  462 62  HOH HOH A . 
F 6 HOH 63  463 63  HOH HOH A . 
F 6 HOH 64  464 64  HOH HOH A . 
F 6 HOH 65  465 65  HOH HOH A . 
F 6 HOH 66  466 66  HOH HOH A . 
F 6 HOH 67  467 67  HOH HOH A . 
F 6 HOH 68  468 68  HOH HOH A . 
F 6 HOH 69  469 69  HOH HOH A . 
F 6 HOH 70  470 70  HOH HOH A . 
F 6 HOH 71  471 71  HOH HOH A . 
F 6 HOH 72  472 72  HOH HOH A . 
F 6 HOH 73  473 73  HOH HOH A . 
F 6 HOH 74  474 74  HOH HOH A . 
F 6 HOH 75  475 75  HOH HOH A . 
F 6 HOH 76  476 76  HOH HOH A . 
F 6 HOH 77  477 77  HOH HOH A . 
F 6 HOH 78  478 78  HOH HOH A . 
F 6 HOH 79  479 79  HOH HOH A . 
F 6 HOH 80  480 80  HOH HOH A . 
F 6 HOH 81  481 81  HOH HOH A . 
F 6 HOH 82  482 82  HOH HOH A . 
F 6 HOH 83  483 83  HOH HOH A . 
F 6 HOH 84  484 84  HOH HOH A . 
F 6 HOH 85  485 85  HOH HOH A . 
F 6 HOH 86  486 86  HOH HOH A . 
F 6 HOH 87  487 87  HOH HOH A . 
F 6 HOH 88  488 88  HOH HOH A . 
F 6 HOH 89  489 89  HOH HOH A . 
F 6 HOH 90  490 90  HOH HOH A . 
F 6 HOH 91  491 91  HOH HOH A . 
F 6 HOH 92  492 92  HOH HOH A . 
F 6 HOH 93  493 93  HOH HOH A . 
F 6 HOH 94  494 94  HOH HOH A . 
F 6 HOH 95  495 95  HOH HOH A . 
F 6 HOH 96  496 96  HOH HOH A . 
F 6 HOH 97  497 97  HOH HOH A . 
F 6 HOH 98  498 98  HOH HOH A . 
F 6 HOH 99  499 99  HOH HOH A . 
F 6 HOH 100 500 100 HOH HOH A . 
F 6 HOH 101 501 101 HOH HOH A . 
F 6 HOH 102 502 102 HOH HOH A . 
F 6 HOH 103 503 103 HOH HOH A . 
F 6 HOH 104 504 104 HOH HOH A . 
F 6 HOH 105 505 105 HOH HOH A . 
F 6 HOH 106 506 106 HOH HOH A . 
F 6 HOH 107 507 107 HOH HOH A . 
F 6 HOH 108 508 108 HOH HOH A . 
F 6 HOH 109 509 109 HOH HOH A . 
F 6 HOH 110 510 110 HOH HOH A . 
F 6 HOH 111 511 111 HOH HOH A . 
F 6 HOH 112 512 112 HOH HOH A . 
F 6 HOH 113 513 113 HOH HOH A . 
F 6 HOH 114 514 114 HOH HOH A . 
F 6 HOH 115 515 115 HOH HOH A . 
F 6 HOH 116 516 116 HOH HOH A . 
F 6 HOH 117 517 117 HOH HOH A . 
F 6 HOH 118 518 118 HOH HOH A . 
F 6 HOH 119 519 119 HOH HOH A . 
F 6 HOH 120 520 120 HOH HOH A . 
F 6 HOH 121 521 121 HOH HOH A . 
F 6 HOH 122 522 122 HOH HOH A . 
F 6 HOH 123 523 123 HOH HOH A . 
F 6 HOH 124 524 124 HOH HOH A . 
F 6 HOH 125 525 125 HOH HOH A . 
F 6 HOH 126 526 126 HOH HOH A . 
F 6 HOH 127 527 127 HOH HOH A . 
F 6 HOH 128 528 128 HOH HOH A . 
F 6 HOH 129 529 129 HOH HOH A . 
F 6 HOH 130 530 130 HOH HOH A . 
F 6 HOH 131 531 131 HOH HOH A . 
F 6 HOH 132 532 132 HOH HOH A . 
F 6 HOH 133 533 133 HOH HOH A . 
F 6 HOH 134 534 134 HOH HOH A . 
F 6 HOH 135 535 135 HOH HOH A . 
F 6 HOH 136 536 136 HOH HOH A . 
F 6 HOH 137 537 137 HOH HOH A . 
F 6 HOH 138 538 138 HOH HOH A . 
F 6 HOH 139 539 139 HOH HOH A . 
F 6 HOH 140 540 140 HOH HOH A . 
F 6 HOH 141 541 141 HOH HOH A . 
F 6 HOH 142 542 142 HOH HOH A . 
F 6 HOH 143 543 143 HOH HOH A . 
F 6 HOH 144 544 144 HOH HOH A . 
F 6 HOH 145 545 145 HOH HOH A . 
F 6 HOH 146 546 146 HOH HOH A . 
F 6 HOH 147 547 147 HOH HOH A . 
F 6 HOH 148 548 148 HOH HOH A . 
F 6 HOH 149 549 149 HOH HOH A . 
F 6 HOH 150 550 150 HOH HOH A . 
F 6 HOH 151 551 151 HOH HOH A . 
F 6 HOH 152 552 152 HOH HOH A . 
F 6 HOH 153 553 153 HOH HOH A . 
F 6 HOH 154 554 154 HOH HOH A . 
F 6 HOH 155 555 155 HOH HOH A . 
F 6 HOH 156 556 156 HOH HOH A . 
F 6 HOH 157 557 157 HOH HOH A . 
F 6 HOH 158 558 158 HOH HOH A . 
F 6 HOH 159 559 159 HOH HOH A . 
F 6 HOH 160 560 160 HOH HOH A . 
F 6 HOH 161 561 161 HOH HOH A . 
F 6 HOH 162 562 162 HOH HOH A . 
F 6 HOH 163 563 163 HOH HOH A . 
F 6 HOH 164 564 164 HOH HOH A . 
F 6 HOH 165 565 165 HOH HOH A . 
F 6 HOH 166 566 166 HOH HOH A . 
F 6 HOH 167 567 167 HOH HOH A . 
F 6 HOH 168 568 168 HOH HOH A . 
F 6 HOH 169 569 169 HOH HOH A . 
F 6 HOH 170 570 170 HOH HOH A . 
F 6 HOH 171 571 171 HOH HOH A . 
F 6 HOH 172 572 172 HOH HOH A . 
F 6 HOH 173 573 173 HOH HOH A . 
F 6 HOH 174 574 174 HOH HOH A . 
F 6 HOH 175 575 175 HOH HOH A . 
F 6 HOH 176 576 176 HOH HOH A . 
F 6 HOH 177 577 177 HOH HOH A . 
F 6 HOH 178 578 178 HOH HOH A . 
F 6 HOH 179 579 179 HOH HOH A . 
F 6 HOH 180 580 180 HOH HOH A . 
F 6 HOH 181 581 181 HOH HOH A . 
F 6 HOH 182 582 182 HOH HOH A . 
F 6 HOH 183 583 183 HOH HOH A . 
F 6 HOH 184 584 184 HOH HOH A . 
F 6 HOH 185 585 185 HOH HOH A . 
F 6 HOH 186 586 186 HOH HOH A . 
F 6 HOH 187 587 187 HOH HOH A . 
F 6 HOH 188 588 188 HOH HOH A . 
F 6 HOH 189 589 189 HOH HOH A . 
F 6 HOH 190 590 190 HOH HOH A . 
F 6 HOH 191 591 191 HOH HOH A . 
F 6 HOH 192 592 192 HOH HOH A . 
F 6 HOH 193 593 193 HOH HOH A . 
F 6 HOH 194 594 194 HOH HOH A . 
F 6 HOH 195 595 195 HOH HOH A . 
F 6 HOH 196 596 196 HOH HOH A . 
F 6 HOH 197 597 197 HOH HOH A . 
F 6 HOH 198 598 198 HOH HOH A . 
F 6 HOH 199 599 199 HOH HOH A . 
F 6 HOH 200 600 200 HOH HOH A . 
F 6 HOH 201 601 201 HOH HOH A . 
F 6 HOH 202 602 202 HOH HOH A . 
F 6 HOH 203 603 203 HOH HOH A . 
F 6 HOH 204 604 204 HOH HOH A . 
F 6 HOH 205 605 205 HOH HOH A . 
F 6 HOH 206 606 206 HOH HOH A . 
F 6 HOH 207 607 207 HOH HOH A . 
F 6 HOH 208 608 208 HOH HOH A . 
F 6 HOH 209 609 209 HOH HOH A . 
F 6 HOH 210 610 210 HOH HOH A . 
F 6 HOH 211 611 211 HOH HOH A . 
F 6 HOH 212 612 212 HOH HOH A . 
F 6 HOH 213 613 213 HOH HOH A . 
F 6 HOH 214 614 214 HOH HOH A . 
F 6 HOH 215 615 215 HOH HOH A . 
F 6 HOH 216 616 216 HOH HOH A . 
F 6 HOH 217 617 217 HOH HOH A . 
F 6 HOH 218 618 218 HOH HOH A . 
F 6 HOH 219 619 219 HOH HOH A . 
F 6 HOH 220 620 220 HOH HOH A . 
F 6 HOH 221 621 221 HOH HOH A . 
F 6 HOH 222 622 222 HOH HOH A . 
F 6 HOH 223 623 223 HOH HOH A . 
F 6 HOH 224 624 224 HOH HOH A . 
F 6 HOH 225 625 225 HOH HOH A . 
F 6 HOH 226 626 226 HOH HOH A . 
F 6 HOH 227 627 227 HOH HOH A . 
F 6 HOH 228 628 228 HOH HOH A . 
F 6 HOH 229 629 229 HOH HOH A . 
F 6 HOH 230 630 230 HOH HOH A . 
F 6 HOH 231 631 231 HOH HOH A . 
F 6 HOH 232 632 232 HOH HOH A . 
F 6 HOH 233 633 233 HOH HOH A . 
F 6 HOH 234 634 234 HOH HOH A . 
F 6 HOH 235 635 235 HOH HOH A . 
F 6 HOH 236 636 236 HOH HOH A . 
F 6 HOH 237 637 237 HOH HOH A . 
F 6 HOH 238 638 238 HOH HOH A . 
F 6 HOH 239 639 239 HOH HOH A . 
F 6 HOH 240 640 240 HOH HOH A . 
F 6 HOH 241 641 241 HOH HOH A . 
F 6 HOH 242 642 242 HOH HOH A . 
F 6 HOH 243 643 243 HOH HOH A . 
F 6 HOH 244 644 244 HOH HOH A . 
F 6 HOH 245 645 245 HOH HOH A . 
F 6 HOH 246 646 246 HOH HOH A . 
F 6 HOH 247 647 247 HOH HOH A . 
F 6 HOH 248 648 248 HOH HOH A . 
F 6 HOH 249 649 249 HOH HOH A . 
F 6 HOH 250 650 250 HOH HOH A . 
F 6 HOH 251 651 251 HOH HOH A . 
F 6 HOH 252 652 252 HOH HOH A . 
F 6 HOH 253 653 253 HOH HOH A . 
F 6 HOH 254 654 254 HOH HOH A . 
F 6 HOH 255 655 255 HOH HOH A . 
F 6 HOH 256 656 256 HOH HOH A . 
F 6 HOH 257 657 257 HOH HOH A . 
F 6 HOH 258 658 258 HOH HOH A . 
F 6 HOH 259 659 259 HOH HOH A . 
F 6 HOH 260 660 260 HOH HOH A . 
F 6 HOH 261 661 261 HOH HOH A . 
F 6 HOH 262 662 262 HOH HOH A . 
F 6 HOH 263 663 263 HOH HOH A . 
F 6 HOH 264 664 264 HOH HOH A . 
F 6 HOH 265 665 265 HOH HOH A . 
F 6 HOH 266 666 266 HOH HOH A . 
F 6 HOH 267 667 267 HOH HOH A . 
F 6 HOH 268 668 268 HOH HOH A . 
F 6 HOH 269 669 269 HOH HOH A . 
F 6 HOH 270 670 270 HOH HOH A . 
F 6 HOH 271 671 271 HOH HOH A . 
F 6 HOH 272 672 272 HOH HOH A . 
F 6 HOH 273 673 273 HOH HOH A . 
F 6 HOH 274 674 274 HOH HOH A . 
F 6 HOH 275 675 275 HOH HOH A . 
F 6 HOH 276 676 276 HOH HOH A . 
F 6 HOH 277 677 277 HOH HOH A . 
F 6 HOH 278 678 278 HOH HOH A . 
F 6 HOH 279 679 279 HOH HOH A . 
F 6 HOH 280 680 280 HOH HOH A . 
F 6 HOH 281 681 281 HOH HOH A . 
F 6 HOH 282 682 282 HOH HOH A . 
F 6 HOH 283 683 283 HOH HOH A . 
F 6 HOH 284 684 284 HOH HOH A . 
F 6 HOH 285 685 285 HOH HOH A . 
F 6 HOH 286 686 286 HOH HOH A . 
F 6 HOH 287 687 287 HOH HOH A . 
F 6 HOH 288 688 288 HOH HOH A . 
F 6 HOH 289 689 289 HOH HOH A . 
F 6 HOH 290 690 290 HOH HOH A . 
F 6 HOH 291 691 291 HOH HOH A . 
F 6 HOH 292 692 292 HOH HOH A . 
F 6 HOH 293 693 293 HOH HOH A . 
F 6 HOH 294 694 294 HOH HOH A . 
F 6 HOH 295 695 295 HOH HOH A . 
F 6 HOH 296 696 296 HOH HOH A . 
F 6 HOH 297 697 297 HOH HOH A . 
F 6 HOH 298 698 298 HOH HOH A . 
F 6 HOH 299 699 299 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.0 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.6 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.2  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E WW3 .   ? A WW3 304 ? 1_555 109.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E WW3 .   ? A WW3 304 ? 1_555 113.9 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E WW3 .   ? A WW3 304 ? 1_555 118.0 ? 
# 
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 2014-11-26 
2 'Structure model' 1 1 2018-03-07 
3 'Structure model' 1 2 2023-09-20 
# 
_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' Advisory                 
2 2 'Structure model' 'Data collection'        
3 3 'Structure model' Advisory                 
4 3 'Structure model' 'Data collection'        
5 3 'Structure model' 'Database references'    
6 3 'Structure model' 'Derived calculations'   
7 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  2 'Structure model' diffrn_source                 
2  2 'Structure model' pdbx_unobs_or_zero_occ_atoms  
3  3 'Structure model' chem_comp_atom                
4  3 'Structure model' chem_comp_bond                
5  3 'Structure model' database_2                    
6  3 'Structure model' pdbx_initial_refinement_model 
7  3 'Structure model' pdbx_struct_conn_angle        
8  3 'Structure model' pdbx_unobs_or_zero_occ_atoms  
9  3 'Structure model' struct_conn                   
10 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
2  3 'Structure model' '_database_2.pdbx_DOI'                        
3  3 'Structure model' '_database_2.pdbx_database_accession'         
4  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.value'               
17 3 'Structure model' '_struct_conn.pdbx_dist_value'                
18 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
19 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
20 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
21 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
22 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
23 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
24 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
25 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
26 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
27 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
28 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
29 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
30 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
31 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
SCALA       3.3.20 2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk 'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 2 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 3 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND1 A HIS 36 ? B O A HOH 590 ? ? 1.64 
2 1 OD2 A ASP 34 ? A O A HOH 689 ? ? 1.80 
3 1 CG2 A THR 87 ? A O A HOH 687 ? ? 2.12 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            THR 
_pdbx_validate_rmsd_bond.auth_seq_id_1             55 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            B 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CG2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            THR 
_pdbx_validate_rmsd_bond.auth_seq_id_2             55 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.319 
_pdbx_validate_rmsd_bond.bond_target_value         1.519 
_pdbx_validate_rmsd_bond.bond_deviation            -0.200 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.033 
_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 CA A HIS 10  ? B C  A HIS 10  ? B O  A HIS 10  ? B 105.43 120.10 -14.67 2.10 N 
2 1 CD A LYS 133 ? B CE A LYS 133 ? B NZ A LYS 133 ? B 131.71 111.70 20.01  2.30 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  ? ? -142.82 54.34   
2 1 LYS A 76  ? ? -116.40 -83.07  
3 1 LYS A 76  ? ? -119.87 -83.07  
4 1 GLU A 106 ? ? -92.00  -61.50  
5 1 LYS A 111 ? ? 74.29   -2.72   
6 1 PHE A 176 ? ? -153.37 74.55   
7 1 ASN A 244 ? ? -91.76  44.04   
8 1 LYS A 252 ? ? 55.34   -138.96 
9 1 ASN A 253 ? ? -94.55  58.25   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A HIS 4   ? CE1 ? A HIS 4   CE1 
2  1 Y 0 A HIS 4   ? NE2 ? A HIS 4   NE2 
3  1 Y 0 A ASP 19  ? OD2 ? A ASP 19  OD2 
4  1 Y 0 A ASP 52  ? OD2 ? A ASP 52  OD2 
5  1 Y 0 A GLN 53  ? OE1 ? A GLN 53  OE1 
6  1 Y 0 A LYS 76  ? CE  ? A LYS 76  CE  
7  1 Y 0 A LYS 76  ? NZ  ? A LYS 76  NZ  
8  1 Y 0 A LYS 127 ? NZ  A A LYS 126 NZ  
9  1 Y 0 A LYS 127 ? NZ  B A LYS 126 NZ  
10 1 Y 0 A LYS 149 ? NZ  ? A LYS 148 NZ  
11 1 Y 0 A LYS 159 ? CE  ? A LYS 158 CE  
12 1 Y 0 A LYS 159 ? NZ  ? A LYS 158 NZ  
13 1 Y 0 A ASP 165 ? OD1 ? A ASP 164 OD1 
14 1 Y 0 A ASP 165 ? OD2 ? A ASP 164 OD2 
15 1 Y 0 A LYS 168 ? NZ  ? A LYS 167 NZ  
16 1 Y 0 A LYS 172 ? CE  ? A LYS 171 CE  
17 1 Y 0 A LYS 172 ? NZ  ? A LYS 171 NZ  
18 1 Y 0 A LYS 213 ? NZ  ? A LYS 212 NZ  
19 1 Y 0 A LYS 228 ? NZ  ? A LYS 227 NZ  
20 1 Y 0 A GLU 239 ? CD  ? A GLU 238 CD  
21 1 Y 0 A GLU 239 ? OE1 ? A GLU 238 OE1 
22 1 Y 0 A GLU 239 ? OE2 ? A GLU 238 OE2 
23 1 Y 0 A LYS 261 ? CD  ? A LYS 260 CD  
24 1 Y 0 A LYS 261 ? CE  ? A LYS 260 CE  
25 1 Y 0 A LYS 261 ? NZ  ? A LYS 260 NZ  
26 1 Y 0 A LYS 261 ? OXT ? A LYS 260 OXT 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MET N    N  N N 264 
MET CA   C  N S 265 
MET C    C  N N 266 
MET O    O  N N 267 
MET CB   C  N N 268 
MET CG   C  N N 269 
MET SD   S  N N 270 
MET CE   C  N N 271 
MET OXT  O  N N 272 
MET H    H  N N 273 
MET H2   H  N N 274 
MET HA   H  N N 275 
MET HB2  H  N N 276 
MET HB3  H  N N 277 
MET HG2  H  N N 278 
MET HG3  H  N N 279 
MET HE1  H  N N 280 
MET HE2  H  N N 281 
MET HE3  H  N N 282 
MET HXT  H  N N 283 
PHE N    N  N N 284 
PHE CA   C  N S 285 
PHE C    C  N N 286 
PHE O    O  N N 287 
PHE CB   C  N N 288 
PHE CG   C  Y N 289 
PHE CD1  C  Y N 290 
PHE CD2  C  Y N 291 
PHE CE1  C  Y N 292 
PHE CE2  C  Y N 293 
PHE CZ   C  Y N 294 
PHE OXT  O  N N 295 
PHE H    H  N N 296 
PHE H2   H  N N 297 
PHE HA   H  N N 298 
PHE HB2  H  N N 299 
PHE HB3  H  N N 300 
PHE HD1  H  N N 301 
PHE HD2  H  N N 302 
PHE HE1  H  N N 303 
PHE HE2  H  N N 304 
PHE HZ   H  N N 305 
PHE HXT  H  N N 306 
PRO N    N  N N 307 
PRO CA   C  N S 308 
PRO C    C  N N 309 
PRO O    O  N N 310 
PRO CB   C  N N 311 
PRO CG   C  N N 312 
PRO CD   C  N N 313 
PRO OXT  O  N N 314 
PRO H    H  N N 315 
PRO HA   H  N N 316 
PRO HB2  H  N N 317 
PRO HB3  H  N N 318 
PRO HG2  H  N N 319 
PRO HG3  H  N N 320 
PRO HD2  H  N N 321 
PRO HD3  H  N N 322 
PRO HXT  H  N N 323 
SER N    N  N N 324 
SER CA   C  N S 325 
SER C    C  N N 326 
SER O    O  N N 327 
SER CB   C  N N 328 
SER OG   O  N N 329 
SER OXT  O  N N 330 
SER H    H  N N 331 
SER H2   H  N N 332 
SER HA   H  N N 333 
SER HB2  H  N N 334 
SER HB3  H  N N 335 
SER HG   H  N N 336 
SER HXT  H  N N 337 
THR N    N  N N 338 
THR CA   C  N S 339 
THR C    C  N N 340 
THR O    O  N N 341 
THR CB   C  N R 342 
THR OG1  O  N N 343 
THR CG2  C  N N 344 
THR OXT  O  N N 345 
THR H    H  N N 346 
THR H2   H  N N 347 
THR HA   H  N N 348 
THR HB   H  N N 349 
THR HG1  H  N N 350 
THR HG21 H  N N 351 
THR HG22 H  N N 352 
THR HG23 H  N N 353 
THR HXT  H  N N 354 
TRP N    N  N N 355 
TRP CA   C  N S 356 
TRP C    C  N N 357 
TRP O    O  N N 358 
TRP CB   C  N N 359 
TRP CG   C  Y N 360 
TRP CD1  C  Y N 361 
TRP CD2  C  Y N 362 
TRP NE1  N  Y N 363 
TRP CE2  C  Y N 364 
TRP CE3  C  Y N 365 
TRP CZ2  C  Y N 366 
TRP CZ3  C  Y N 367 
TRP CH2  C  Y N 368 
TRP OXT  O  N N 369 
TRP H    H  N N 370 
TRP H2   H  N N 371 
TRP HA   H  N N 372 
TRP HB2  H  N N 373 
TRP HB3  H  N N 374 
TRP HD1  H  N N 375 
TRP HE1  H  N N 376 
TRP HE3  H  N N 377 
TRP HZ2  H  N N 378 
TRP HZ3  H  N N 379 
TRP HH2  H  N N 380 
TRP HXT  H  N N 381 
TYR N    N  N N 382 
TYR CA   C  N S 383 
TYR C    C  N N 384 
TYR O    O  N N 385 
TYR CB   C  N N 386 
TYR CG   C  Y N 387 
TYR CD1  C  Y N 388 
TYR CD2  C  Y N 389 
TYR CE1  C  Y N 390 
TYR CE2  C  Y N 391 
TYR CZ   C  Y N 392 
TYR OH   O  N N 393 
TYR OXT  O  N N 394 
TYR H    H  N N 395 
TYR H2   H  N N 396 
TYR HA   H  N N 397 
TYR HB2  H  N N 398 
TYR HB3  H  N N 399 
TYR HD1  H  N N 400 
TYR HD2  H  N N 401 
TYR HE1  H  N N 402 
TYR HE2  H  N N 403 
TYR HH   H  N N 404 
TYR HXT  H  N N 405 
VAL N    N  N N 406 
VAL CA   C  N S 407 
VAL C    C  N N 408 
VAL O    O  N N 409 
VAL CB   C  N N 410 
VAL CG1  C  N N 411 
VAL CG2  C  N N 412 
VAL OXT  O  N N 413 
VAL H    H  N N 414 
VAL H2   H  N N 415 
VAL HA   H  N N 416 
VAL HB   H  N N 417 
VAL HG11 H  N N 418 
VAL HG12 H  N N 419 
VAL HG13 H  N N 420 
VAL HG21 H  N N 421 
VAL HG22 H  N N 422 
VAL HG23 H  N N 423 
VAL HXT  H  N N 424 
WW3 O9   O  N N 425 
WW3 S7   S  N N 426 
WW3 O8   O  N N 427 
WW3 N10  N  N N 428 
WW3 C3   C  Y N 429 
WW3 C2   C  Y N 430 
WW3 C4   C  Y N 431 
WW3 C5   C  Y N 432 
WW3 C6   C  Y N 433 
WW3 C1   C  Y N 434 
WW3 N11  N  N N 435 
WW3 N12  N  N N 436 
WW3 N13  N  N N 437 
WW3 C16  C  N N 438 
WW3 C15  C  N N 439 
WW3 C17  C  N N 440 
WW3 C18  C  N N 441 
WW3 C19  C  N N 442 
WW3 C14  C  N N 443 
WW3 H1   H  N N 444 
WW3 H2   H  N N 445 
WW3 H3   H  N N 446 
WW3 H4   H  N N 447 
WW3 H5   H  N N 448 
WW3 H6   H  N N 449 
WW3 H7   H  N N 450 
WW3 H8   H  N N 451 
WW3 H9   H  N N 452 
WW3 H10  H  N N 453 
WW3 H11  H  N N 454 
WW3 H12  H  N N 455 
WW3 H13  H  N N 456 
WW3 H14  H  N N 457 
WW3 H15  H  N N 458 
WW3 H16  H  N N 459 
WW3 H17  H  N N 460 
WW3 H18  H  N N 461 
ZN  ZN   ZN N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MET N   CA   sing N N 250 
MET N   H    sing N N 251 
MET N   H2   sing N N 252 
MET CA  C    sing N N 253 
MET CA  CB   sing N N 254 
MET CA  HA   sing N N 255 
MET C   O    doub N N 256 
MET C   OXT  sing N N 257 
MET CB  CG   sing N N 258 
MET CB  HB2  sing N N 259 
MET CB  HB3  sing N N 260 
MET CG  SD   sing N N 261 
MET CG  HG2  sing N N 262 
MET CG  HG3  sing N N 263 
MET SD  CE   sing N N 264 
MET CE  HE1  sing N N 265 
MET CE  HE2  sing N N 266 
MET CE  HE3  sing N N 267 
MET OXT HXT  sing N N 268 
PHE N   CA   sing N N 269 
PHE N   H    sing N N 270 
PHE N   H2   sing N N 271 
PHE CA  C    sing N N 272 
PHE CA  CB   sing N N 273 
PHE CA  HA   sing N N 274 
PHE C   O    doub N N 275 
PHE C   OXT  sing N N 276 
PHE CB  CG   sing N N 277 
PHE CB  HB2  sing N N 278 
PHE CB  HB3  sing N N 279 
PHE CG  CD1  doub Y N 280 
PHE CG  CD2  sing Y N 281 
PHE CD1 CE1  sing Y N 282 
PHE CD1 HD1  sing N N 283 
PHE CD2 CE2  doub Y N 284 
PHE CD2 HD2  sing N N 285 
PHE CE1 CZ   doub Y N 286 
PHE CE1 HE1  sing N N 287 
PHE CE2 CZ   sing Y N 288 
PHE CE2 HE2  sing N N 289 
PHE CZ  HZ   sing N N 290 
PHE OXT HXT  sing N N 291 
PRO N   CA   sing N N 292 
PRO N   CD   sing N N 293 
PRO N   H    sing N N 294 
PRO CA  C    sing N N 295 
PRO CA  CB   sing N N 296 
PRO CA  HA   sing N N 297 
PRO C   O    doub N N 298 
PRO C   OXT  sing N N 299 
PRO CB  CG   sing N N 300 
PRO CB  HB2  sing N N 301 
PRO CB  HB3  sing N N 302 
PRO CG  CD   sing N N 303 
PRO CG  HG2  sing N N 304 
PRO CG  HG3  sing N N 305 
PRO CD  HD2  sing N N 306 
PRO CD  HD3  sing N N 307 
PRO OXT HXT  sing N N 308 
SER N   CA   sing N N 309 
SER N   H    sing N N 310 
SER N   H2   sing N N 311 
SER CA  C    sing N N 312 
SER CA  CB   sing N N 313 
SER CA  HA   sing N N 314 
SER C   O    doub N N 315 
SER C   OXT  sing N N 316 
SER CB  OG   sing N N 317 
SER CB  HB2  sing N N 318 
SER CB  HB3  sing N N 319 
SER OG  HG   sing N N 320 
SER OXT HXT  sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
VAL N   CA   sing N N 390 
VAL N   H    sing N N 391 
VAL N   H2   sing N N 392 
VAL CA  C    sing N N 393 
VAL CA  CB   sing N N 394 
VAL CA  HA   sing N N 395 
VAL C   O    doub N N 396 
VAL C   OXT  sing N N 397 
VAL CB  CG1  sing N N 398 
VAL CB  CG2  sing N N 399 
VAL CB  HB   sing N N 400 
VAL CG1 HG11 sing N N 401 
VAL CG1 HG12 sing N N 402 
VAL CG1 HG13 sing N N 403 
VAL CG2 HG21 sing N N 404 
VAL CG2 HG22 sing N N 405 
VAL CG2 HG23 sing N N 406 
VAL OXT HXT  sing N N 407 
WW3 C19 C14  sing N N 408 
WW3 C19 C18  sing N N 409 
WW3 C14 N13  sing N N 410 
WW3 C18 C17  sing N N 411 
WW3 N13 N12  sing N N 412 
WW3 N13 C16  sing N N 413 
WW3 N11 N12  doub N N 414 
WW3 N11 C6   sing N N 415 
WW3 C15 C17  sing N N 416 
WW3 C15 C16  sing N N 417 
WW3 C6  C1   doub Y N 418 
WW3 C6  C5   sing Y N 419 
WW3 C1  C2   sing Y N 420 
WW3 C5  C4   doub Y N 421 
WW3 C2  C3   doub Y N 422 
WW3 C4  C3   sing Y N 423 
WW3 C3  S7   sing N N 424 
WW3 N10 S7   sing N N 425 
WW3 O9  S7   doub N N 426 
WW3 S7  O8   doub N N 427 
WW3 N10 H1   sing N N 428 
WW3 N10 H2   sing N N 429 
WW3 C2  H3   sing N N 430 
WW3 C4  H4   sing N N 431 
WW3 C5  H5   sing N N 432 
WW3 C1  H6   sing N N 433 
WW3 C16 H7   sing N N 434 
WW3 C16 H8   sing N N 435 
WW3 C15 H9   sing N N 436 
WW3 C15 H10  sing N N 437 
WW3 C17 H11  sing N N 438 
WW3 C17 H12  sing N N 439 
WW3 C18 H13  sing N N 440 
WW3 C18 H14  sing N N 441 
WW3 C19 H15  sing N N 442 
WW3 C19 H16  sing N N 443 
WW3 C14 H17  sing N N 444 
WW3 C14 H18  sing N N 445 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                      ZN  
3 'DIMETHYL SULFOXIDE'                            DMS 
4 BICINE                                          BCN 
5 '4-[(E)-azepan-1-yldiazenyl]benzenesulfonamide' WW3 
6 water                                           HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          'PDB ENTRY 3HLJ' 
# 
