data_3M98
# 
_entry.id   3M98 
# 
_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   3M98         pdb_00003m98 10.2210/pdb3m98/pdb 
RCSB  RCSB058267   ?            ?                   
WWPDB D_1000058267 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          3M96 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        3M98 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2010-03-21 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 5-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide' 
_citation.journal_abbrev            'To be published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1 ? 
primary 'Baranauskiene, L.' 2 ? 
primary 'Grazulis, S.'      3 ? 
primary 'Manakova, E.'      4 ? 
primary 'Golovenko, D.'     5 ? 
primary 'Matulis, D.'       6 ? 
# 
_cell.entry_id           3M98 
_cell.length_a           42.233 
_cell.length_b           41.112 
_cell.length_c           72.109 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.05 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3M98 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                      29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                  65.409    1   ?       ? ? ? 
3 non-polymer syn '5-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide' 349.792   1   ?       ? ? ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                      195.237   1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                        78.133    1   ?       ? ? ? 
6 water       nat water                                                       18.015    223 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonic anhydrase II, CA-II, Carbonate dehydratase II, Carbonic anhydrase C, CAC' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3M98 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                     ? 'C3 H7 N O2'         89.093  
ARG 'L-peptide linking' y ARGININE                                                    ? 'C6 H15 N4 O2 1'     175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                  ? 'C4 H8 N2 O3'        132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                             ? 'C4 H7 N O4'         133.103 
CYS 'L-peptide linking' y CYSTEINE                                                    ? 'C3 H7 N O2 S'       121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                        ? 'C2 H6 O S'          78.133  
E02 non-polymer         . '5-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide' ? 'C15 H12 Cl N3 O3 S' 349.792 
GLN 'L-peptide linking' y GLUTAMINE                                                   ? 'C5 H10 N2 O3'       146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                             ? 'C5 H9 N O4'         147.129 
GLY 'peptide linking'   y GLYCINE                                                     ? 'C2 H5 N O2'         75.067  
HIS 'L-peptide linking' y HISTIDINE                                                   ? 'C6 H10 N3 O2 1'     156.162 
HOH non-polymer         . WATER                                                       ? 'H2 O'               18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                  ? 'C6 H13 N O2'        131.173 
LEU 'L-peptide linking' y LEUCINE                                                     ? 'C6 H13 N O2'        131.173 
LYS 'L-peptide linking' y LYSINE                                                      ? 'C6 H15 N2 O2 1'     147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                      ? 'C6 H13 N O4 S'      195.237 
MET 'L-peptide linking' y METHIONINE                                                  ? 'C5 H11 N O2 S'      149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                               ? 'C9 H11 N O2'        165.189 
PRO 'L-peptide linking' y PROLINE                                                     ? 'C5 H9 N O2'         115.130 
SER 'L-peptide linking' y SERINE                                                      ? 'C3 H7 N O3'         105.093 
THR 'L-peptide linking' y THREONINE                                                   ? 'C4 H9 N O3'         119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                  ? 'C11 H12 N2 O2'      204.225 
TYR 'L-peptide linking' y TYROSINE                                                    ? 'C9 H11 N O3'        181.189 
VAL 'L-peptide linking' y VALINE                                                      ? 'C5 H11 N O2'        117.146 
ZN  non-polymer         . 'ZINC ION'                                                  ? 'Zn 2'               65.409  
# 
_exptl.entry_id          3M98 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.07 
_exptl_crystal.density_percent_sol   40.68 
_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.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9.0, 0.2 M ammonium sulfate and 2M sodium malonate, pH 7.0 made from 1M sodium BICINE and 3.4M sodium malonate, vapor diffusion, sitting drop, temperature 291K
;
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2009-12-21 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si [111], horizontally focussing' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8120 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.8120 
# 
_reflns.entry_id                     3M98 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             39.81 
_reflns.d_resolution_high            1.500 
_reflns.number_obs                   37890 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.000 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_Rsym_value              0.045 
_reflns.pdbx_netI_over_sigmaI        35.900 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              9.900 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.50 
_reflns_shell.d_res_low              1.58 
_reflns_shell.percent_possible_all   97.10 
_reflns_shell.Rmerge_I_obs           0.324 
_reflns_shell.pdbx_Rsym_value        0.324 
_reflns_shell.meanI_over_sigI_obs    6.0 
_reflns_shell.pdbx_redundancy        9.90 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3M98 
_refine.ls_number_reflns_obs                     34084 
_refine.ls_number_reflns_all                     38726 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             39.81 
_refine.ls_d_res_high                            1.50 
_refine.ls_percent_reflns_obs                    97.84 
_refine.ls_R_factor_obs                          0.13976 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.13479 
_refine.ls_R_factor_R_free                       0.18400 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10.0 
_refine.ls_number_reflns_R_free                  3806 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            0.50 
_refine.occupancy_max                            1.00 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.B_iso_mean                               16.463 
_refine.aniso_B[1][1]                            -0.06 
_refine.aniso_B[2][2]                            -0.03 
_refine.aniso_B[3][3]                            0.11 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.04 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB entry 3HLJ' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.090 
_refine.pdbx_overall_ESU_R_Free                  0.076 
_refine.overall_SU_ML                            0.039 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.247 
_refine.overall_SU_R_Cruickshank_DPI             0.090 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
# 
_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         40 
_refine_hist.number_atoms_solvent             223 
_refine_hist.number_atoms_total               2312 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        39.81 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.029  0.022  ? 2191 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.224  1.967  ? 2981 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.344  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.237 24.646 ? 99   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.660 15.000 ? 361  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       23.930 15.000 ? 7    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.192  0.200  ? 308  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.014  0.020  ? 1696 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.219  0.200  ? 1009 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.311  0.200  ? 1446 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.133  0.200  ? 153  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          0.054  0.200  ? 2    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.230  0.200  ? 66   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.299  0.200  ? 54   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.819  1.500  ? 1363 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.685  2.000  ? 2115 'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.887  3.000  ? 1001 'X-RAY DIFFRACTION' ? 
r_scangle_it                 6.550  4.500  ? 865  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           3.029  3.000  ? 2364 'X-RAY DIFFRACTION' ? 
r_sphericity_free            13.164 3.000  ? 224  'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          7.872  3.000  ? 2124 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.500 
_refine_ls_shell.d_res_low                        1.539 
_refine_ls_shell.number_reflns_R_work             2514 
_refine_ls_shell.R_factor_R_work                  0.159 
_refine_ls_shell.percent_reflns_obs               97.00 
_refine_ls_shell.R_factor_R_free                  0.292 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             265 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  3M98 
_struct.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 5-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3M98 
_struct_keywords.text            'drug design, carbonic anhydrase, benzenesulfonamide, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 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_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -0.85 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 5.97  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A E02 263 ? 16 'BINDING SITE FOR RESIDUE E02 A 263' 
AC3 Software A MES 264 ? 7  'BINDING SITE FOR RESIDUE MES A 264' 
AC4 Software A DMS 265 ? 3  'BINDING SITE FOR RESIDUE DMS A 265' 
# 
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  E02 C .   ? E02 A 263 . ? 1_555 ? 
5  AC2 16 TRP A 5   ? TRP A 5   . ? 1_555 ? 
6  AC2 16 ASN A 62  ? ASN A 62  . ? 1_555 ? 
7  AC2 16 HIS A 64  ? HIS A 64  . ? 1_555 ? 
8  AC2 16 ASN A 67  ? ASN A 67  . ? 1_555 ? 
9  AC2 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
10 AC2 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
11 AC2 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
12 AC2 16 LEU A 140 ? LEU A 141 . ? 1_555 ? 
13 AC2 16 VAL A 142 ? VAL A 143 . ? 1_555 ? 
14 AC2 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
15 AC2 16 THR A 198 ? THR A 199 . ? 1_555 ? 
16 AC2 16 THR A 199 ? THR A 200 . ? 1_555 ? 
17 AC2 16 PRO A 200 ? PRO A 201 . ? 1_555 ? 
18 AC2 16 TRP A 208 ? TRP A 209 . ? 1_555 ? 
19 AC2 16 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
20 AC2 16 HOH F .   ? HOH A 343 . ? 1_555 ? 
21 AC3 7  VAL A 160 ? VAL A 161 . ? 1_555 ? 
22 AC3 7  ASP A 161 ? ASP A 162 . ? 1_555 ? 
23 AC3 7  VAL A 162 ? VAL A 163 . ? 1_555 ? 
24 AC3 7  LEU A 163 ? LEU A 164 . ? 1_555 ? 
25 AC3 7  ASP A 164 ? ASP A 165 . ? 1_555 ? 
26 AC3 7  LYS A 224 ? LYS A 225 . ? 1_555 ? 
27 AC3 7  LYS A 227 ? LYS A 228 . ? 1_555 ? 
28 AC4 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
29 AC4 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
30 AC4 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3M98 
_atom_sites.fract_transf_matrix[1][1]   0.023678 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005926 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024324 
_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]   0.014296 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . HIS A 1 4   ? 9.444   1.230   8.441   1.00 27.12 ?  4   HIS A N    1 
ATOM   2    C  CA   . HIS A 1 4   ? 10.301  0.111   8.886   1.00 25.59 ?  4   HIS A CA   1 
ATOM   3    C  C    . HIS A 1 4   ? 9.431   -0.955  9.592   1.00 22.72 ?  4   HIS A C    1 
ATOM   4    O  O    . HIS A 1 4   ? 9.591   -2.155  9.365   1.00 22.89 ?  4   HIS A O    1 
ATOM   5    C  CB   . HIS A 1 4   ? 11.430  0.593   9.837   1.00 29.15 ?  4   HIS A CB   1 
ATOM   6    C  CG   . HIS A 1 4   ? 12.349  -0.506  10.266  1.00 32.23 ?  4   HIS A CG   1 
ATOM   7    N  ND1  . HIS A 1 4   ? 12.336  -1.029  11.554  1.00 37.45 ?  4   HIS A ND1  1 
ATOM   8    C  CD2  . HIS A 1 4   ? 13.236  -1.258  9.558   1.00 36.30 ?  4   HIS A CD2  1 
ATOM   9    C  CE1  . HIS A 1 4   ? 13.195  -2.040  11.622  1.00 38.10 ?  4   HIS A CE1  1 
ATOM   10   N  NE2  . HIS A 1 4   ? 13.756  -2.202  10.427  1.00 37.84 ?  4   HIS A NE2  1 
ATOM   11   N  N    . TRP A 1 5   ? 8.566   -0.522  10.487  1.00 19.99 ?  5   TRP A N    1 
ATOM   12   C  CA   . TRP A 1 5   ? 7.837   -1.479  11.350  1.00 16.07 ?  5   TRP A CA   1 
ATOM   13   C  C    . TRP A 1 5   ? 6.851   -2.257  10.538  1.00 16.23 ?  5   TRP A C    1 
ATOM   14   O  O    . TRP A 1 5   ? 6.380   -1.780  9.489   1.00 16.56 ?  5   TRP A O    1 
ATOM   15   C  CB   . TRP A 1 5   ? 7.128   -0.742  12.522  1.00 15.10 ?  5   TRP A CB   1 
ATOM   16   C  CG   . TRP A 1 5   ? 5.936   0.093   12.135  1.00 16.37 ?  5   TRP A CG   1 
ATOM   17   C  CD1  . TRP A 1 5   ? 5.894   1.454   11.816  1.00 18.20 ?  5   TRP A CD1  1 
ATOM   18   C  CD2  . TRP A 1 5   ? 4.578   -0.365  12.094  1.00 14.36 ?  5   TRP A CD2  1 
ATOM   19   N  NE1  . TRP A 1 5   ? 4.596   1.834   11.573  1.00 17.89 ?  5   TRP A NE1  1 
ATOM   20   C  CE2  . TRP A 1 5   ? 3.765   0.750   11.714  1.00 15.69 ?  5   TRP A CE2  1 
ATOM   21   C  CE3  . TRP A 1 5   ? 3.964   -1.596  12.336  1.00 14.21 ?  5   TRP A CE3  1 
ATOM   22   C  CZ2  . TRP A 1 5   ? 2.343   0.673   11.615  1.00 15.46 ?  5   TRP A CZ2  1 
ATOM   23   C  CZ3  . TRP A 1 5   ? 2.552   -1.693  12.171  1.00 13.72 ?  5   TRP A CZ3  1 
ATOM   24   C  CH2  . TRP A 1 5   ? 1.755   -0.536  11.882  1.00 15.78 ?  5   TRP A CH2  1 
ATOM   25   N  N    . GLY A 1 6   ? 6.511   -3.448  11.035  1.00 14.71 ?  6   GLY A N    1 
ATOM   26   C  CA   . GLY A 1 6   ? 5.491   -4.286  10.388  1.00 14.77 ?  6   GLY A CA   1 
ATOM   27   C  C    . GLY A 1 6   ? 5.212   -5.436  11.314  1.00 14.12 ?  6   GLY A C    1 
ATOM   28   O  O    . GLY A 1 6   ? 5.254   -5.293  12.551  1.00 14.02 ?  6   GLY A O    1 
ATOM   29   N  N    . TYR A 1 7   ? 4.940   -6.595  10.704  1.00 16.48 ?  7   TYR A N    1 
ATOM   30   C  CA   . TYR A 1 7   ? 4.547   -7.734  11.541  1.00 17.20 ?  7   TYR A CA   1 
ATOM   31   C  C    . TYR A 1 7   ? 5.441   -8.974  11.324  1.00 20.73 ?  7   TYR A C    1 
ATOM   32   O  O    . TYR A 1 7   ? 5.164   -10.062 11.961  1.00 25.48 ?  7   TYR A O    1 
ATOM   33   C  CB   . TYR A 1 7   ? 3.064   -8.111  11.268  1.00 14.88 ?  7   TYR A CB   1 
ATOM   34   C  CG   . TYR A 1 7   ? 2.158   -7.010  11.817  1.00 11.04 ?  7   TYR A CG   1 
ATOM   35   C  CD1  . TYR A 1 7   ? 1.719   -7.037  13.198  1.00 12.04 ?  7   TYR A CD1  1 
ATOM   36   C  CD2  . TYR A 1 7   ? 1.647   -5.933  10.962  1.00 11.15 ?  7   TYR A CD2  1 
ATOM   37   C  CE1  . TYR A 1 7   ? 0.866   -5.974  13.710  1.00 11.09 ?  7   TYR A CE1  1 
ATOM   38   C  CE2  . TYR A 1 7   ? 0.766   -4.920  11.479  1.00 10.05 ?  7   TYR A CE2  1 
ATOM   39   C  CZ   . TYR A 1 7   ? 0.379   -4.968  12.853  1.00 9.65  ?  7   TYR A CZ   1 
ATOM   40   O  OH   . TYR A 1 7   ? -0.443  -3.998  13.318  1.00 10.79 ?  7   TYR A OH   1 
ATOM   41   N  N    . GLY A 1 8   ? 6.512   -8.810  10.521  1.00 21.89 ?  8   GLY A N    1 
ATOM   42   C  CA   . GLY A 1 8   ? 7.513   -9.984  10.381  1.00 22.16 ?  8   GLY A CA   1 
ATOM   43   C  C    . GLY A 1 8   ? 8.487   -10.352 11.531  1.00 25.11 ?  8   GLY A C    1 
ATOM   44   O  O    . GLY A 1 8   ? 8.574   -9.676  12.622  1.00 26.40 ?  8   GLY A O    1 
ATOM   45   N  N    . LYS A 1 9   ? 9.409   -11.331 11.284  1.00 27.84 ?  9   LYS A N    1 
ATOM   46   C  CA   . LYS A 1 9   ? 10.447  -11.750 12.299  1.00 27.56 ?  9   LYS A CA   1 
ATOM   47   C  C    . LYS A 1 9   ? 11.367  -10.622 12.568  1.00 27.61 ?  9   LYS A C    1 
ATOM   48   O  O    . LYS A 1 9   ? 11.824  -10.482 13.735  1.00 29.30 ?  9   LYS A O    1 
ATOM   49   C  CB   . LYS A 1 9   ? 11.286  -12.942 11.863  1.00 30.88 ?  9   LYS A CB   1 
ATOM   50   C  CG   . LYS A 1 9   ? 12.348  -13.408 12.896  1.00 30.82 ?  9   LYS A CG   1 
ATOM   51   C  CD   . LYS A 1 9   ? 13.250  -14.555 12.306  1.00 32.42 ?  9   LYS A CD   1 
ATOM   52   C  CE   . LYS A 1 9   ? 14.466  -14.819 13.228  1.00 37.62 ?  9   LYS A CE   1 
ATOM   53   N  NZ   . LYS A 1 9   ? 14.005  -14.848 14.704  1.00 41.67 ?  9   LYS A NZ   1 
ATOM   54   N  N    . HIS A 1 10  ? 11.589  -9.792  11.523  1.00 24.78 ?  10  HIS A N    1 
ATOM   55   C  CA   . HIS A 1 10  ? 12.572  -8.785  11.698  1.00 23.85 ?  10  HIS A CA   1 
ATOM   56   C  C    . HIS A 1 10  ? 12.079  -7.435  12.052  1.00 20.91 ?  10  HIS A C    1 
ATOM   57   O  O    . HIS A 1 10  ? 12.878  -6.633  12.504  1.00 21.88 ?  10  HIS A O    1 
ATOM   58   C  CB   . HIS A 1 10  ? 13.627  -8.786  10.565  1.00 22.68 ?  10  HIS A CB   1 
ATOM   59   C  CG   . HIS A 1 10  ? 14.362  -10.126 10.457  1.00 27.31 ?  10  HIS A CG   1 
ATOM   60   N  ND1  . HIS A 1 10  ? 15.375  -10.524 11.325  1.00 31.64 ?  10  HIS A ND1  1 
ATOM   61   C  CD2  . HIS A 1 10  ? 14.142  -11.183 9.636   1.00 28.91 ?  10  HIS A CD2  1 
ATOM   62   C  CE1  . HIS A 1 10  ? 15.765  -11.748 11.019  1.00 29.21 ?  10  HIS A CE1  1 
ATOM   63   N  NE2  . HIS A 1 10  ? 15.017  -12.179 10.005  1.00 27.83 ?  10  HIS A NE2  1 
ATOM   64   N  N    . ASN A 1 11  ? 10.748  -7.212  11.938  1.00 18.46 ?  11  ASN A N    1 
ATOM   65   C  CA   . ASN A 1 11  ? 10.264  -5.856  12.209  1.00 17.53 ?  11  ASN A CA   1 
ATOM   66   C  C    . ASN A 1 11  ? 8.898   -5.879  12.939  1.00 17.12 ?  11  ASN A C    1 
ATOM   67   O  O    . ASN A 1 11  ? 8.219   -4.846  13.025  1.00 17.48 ?  11  ASN A O    1 
ATOM   68   C  CB   . ASN A 1 11  ? 10.100  -5.077  10.911  1.00 17.12 ?  11  ASN A CB   1 
ATOM   69   C  CG   . ASN A 1 11  ? 9.054   -5.707  9.970   1.00 18.75 ?  11  ASN A CG   1 
ATOM   70   O  OD1  . ASN A 1 11  ? 8.474   -6.792  10.293  1.00 20.09 ?  11  ASN A OD1  1 
ATOM   71   N  ND2  . ASN A 1 11  ? 8.744   -5.022  8.861   1.00 19.75 ?  11  ASN A ND2  1 
ATOM   72   N  N    . GLY A 1 12  ? 8.540   -7.041  13.505  1.00 16.18 ?  12  GLY A N    1 
ATOM   73   C  CA   . GLY A 1 12  ? 7.252   -7.223  14.160  1.00 16.64 ?  12  GLY A CA   1 
ATOM   74   C  C    . GLY A 1 12  ? 7.237   -6.649  15.571  1.00 15.69 ?  12  GLY A C    1 
ATOM   75   O  O    . GLY A 1 12  ? 8.150   -5.889  16.025  1.00 15.28 ?  12  GLY A O    1 
ATOM   76   N  N    . PRO A 1 13  ? 6.126   -6.961  16.289  1.00 14.09 ?  13  PRO A N    1 
ATOM   77   C  CA   . PRO A 1 13  ? 5.903   -6.339  17.589  1.00 13.43 ?  13  PRO A CA   1 
ATOM   78   C  C    . PRO A 1 13  ? 7.025   -6.331  18.577  1.00 12.17 ?  13  PRO A C    1 
ATOM   79   O  O    . PRO A 1 13  ? 7.185   -5.361  19.350  1.00 14.20 ?  13  PRO A O    1 
ATOM   80   C  CB   . PRO A 1 13  ? 4.673   -7.116  18.135  1.00 14.15 ?  13  PRO A CB   1 
ATOM   81   C  CG   . PRO A 1 13  ? 3.881   -7.469  16.851  1.00 13.85 ?  13  PRO A CG   1 
ATOM   82   C  CD   . PRO A 1 13  ? 4.933   -7.688  15.772  1.00 13.72 ?  13  PRO A CD   1 
ATOM   83   N  N    . GLU A 1 14  ? 7.811   -7.409  18.641  1.00 13.13 ?  14  GLU A N    1 
ATOM   84   C  CA   . GLU A 1 14  ? 8.900   -7.444  19.640  1.00 14.88 ?  14  GLU A CA   1 
ATOM   85   C  C    . GLU A 1 14  ? 10.058  -6.465  19.307  1.00 14.31 ?  14  GLU A C    1 
ATOM   86   O  O    . GLU A 1 14  ? 10.972  -6.284  20.107  1.00 15.53 ?  14  GLU A O    1 
ATOM   87   C  CB   . GLU A 1 14  ? 9.442   -8.881  19.664  1.00 17.44 ?  14  GLU A CB   1 
ATOM   88   C  CG   . GLU A 1 14  ? 10.081  -9.360  18.322  1.00 20.72 ?  14  GLU A CG   1 
ATOM   89   C  CD   . GLU A 1 14  ? 9.200   -9.982  17.133  1.00 28.10 ?  14  GLU A CD   1 
ATOM   90   O  OE1  . GLU A 1 14  ? 7.978   -9.620  16.945  1.00 23.55 ?  14  GLU A OE1  1 
ATOM   91   O  OE2  . GLU A 1 14  ? 9.859   -10.806 16.331  1.00 27.42 ?  14  GLU A OE2  1 
ATOM   92   N  N    . HIS A 1 15  ? 10.045  -5.933  18.083  1.00 13.35 ?  15  HIS A N    1 
ATOM   93   C  CA   . HIS A 1 15  ? 11.030  -4.937  17.694  1.00 14.02 ?  15  HIS A CA   1 
ATOM   94   C  C    . HIS A 1 15  ? 10.618  -3.462  17.861  1.00 12.36 ?  15  HIS A C    1 
ATOM   95   O  O    . HIS A 1 15  ? 11.478  -2.551  17.735  1.00 13.57 ?  15  HIS A O    1 
ATOM   96   C  CB   . HIS A 1 15  ? 11.453  -5.087  16.189  1.00 14.29 ?  15  HIS A CB   1 
ATOM   97   C  CG   . HIS A 1 15  ? 12.160  -6.389  15.934  1.00 15.88 ?  15  HIS A CG   1 
ATOM   98   N  ND1  . HIS A 1 15  ? 13.538  -6.525  16.100  1.00 19.06 ?  15  HIS A ND1  1 
ATOM   99   C  CD2  . HIS A 1 15  ? 11.679  -7.620  15.613  1.00 17.13 ?  15  HIS A CD2  1 
ATOM   100  C  CE1  . HIS A 1 15  ? 13.869  -7.784  15.838  1.00 20.62 ?  15  HIS A CE1  1 
ATOM   101  N  NE2  . HIS A 1 15  ? 12.776  -8.453  15.509  1.00 19.15 ?  15  HIS A NE2  1 
ATOM   102  N  N    . TRP A 1 16  ? 9.321   -3.229  17.977  1.00 12.47 ?  16  TRP A N    1 
ATOM   103  C  CA   . TRP A 1 16  ? 8.780   -1.866  17.896  1.00 11.03 ?  16  TRP A CA   1 
ATOM   104  C  C    . TRP A 1 16  ? 9.407   -0.916  18.937  1.00 12.15 ?  16  TRP A C    1 
ATOM   105  O  O    . TRP A 1 16  ? 9.487   0.319   18.669  1.00 12.88 ?  16  TRP A O    1 
ATOM   106  C  CB   . TRP A 1 16  ? 7.237   -1.828  18.064  1.00 10.04 ?  16  TRP A CB   1 
ATOM   107  C  CG   . TRP A 1 16  ? 6.565   -2.575  16.888  1.00 12.16 ?  16  TRP A CG   1 
ATOM   108  C  CD1  . TRP A 1 16  ? 7.119   -2.990  15.660  1.00 9.81  ?  16  TRP A CD1  1 
ATOM   109  C  CD2  . TRP A 1 16  ? 5.166   -2.912  16.819  1.00 10.71 ?  16  TRP A CD2  1 
ATOM   110  N  NE1  . TRP A 1 16  ? 6.143   -3.639  14.903  1.00 9.46  ?  16  TRP A NE1  1 
ATOM   111  C  CE2  . TRP A 1 16  ? 4.923   -3.517  15.536  1.00 8.86  ?  16  TRP A CE2  1 
ATOM   112  C  CE3  . TRP A 1 16  ? 4.089   -2.699  17.690  1.00 8.73  ?  16  TRP A CE3  1 
ATOM   113  C  CZ2  . TRP A 1 16  ? 3.612   -3.965  15.174  1.00 10.89 ?  16  TRP A CZ2  1 
ATOM   114  C  CZ3  . TRP A 1 16  ? 2.853   -3.111  17.359  1.00 10.85 ?  16  TRP A CZ3  1 
ATOM   115  C  CH2  . TRP A 1 16  ? 2.584   -3.740  16.113  1.00 11.93 ?  16  TRP A CH2  1 
ATOM   116  N  N    . HIS A 1 17  ? 9.783   -1.488  20.122  1.00 12.88 ?  17  HIS A N    1 
ATOM   117  C  CA   . HIS A 1 17  ? 10.206  -0.608  21.224  1.00 13.79 ?  17  HIS A CA   1 
ATOM   118  C  C    . HIS A 1 17  ? 11.494  0.201   20.816  1.00 12.97 ?  17  HIS A C    1 
ATOM   119  O  O    . HIS A 1 17  ? 11.755  1.235   21.454  1.00 15.66 ?  17  HIS A O    1 
ATOM   120  C  CB   . HIS A 1 17  ? 10.514  -1.339  22.529  1.00 12.79 ?  17  HIS A CB   1 
ATOM   121  C  CG   . HIS A 1 17  ? 11.719  -2.244  22.414  1.00 13.20 ?  17  HIS A CG   1 
ATOM   122  N  ND1  . HIS A 1 17  ? 12.963  -1.862  22.874  1.00 17.34 ?  17  HIS A ND1  1 
ATOM   123  C  CD2  . HIS A 1 17  ? 11.906  -3.422  21.780  1.00 15.97 ?  17  HIS A CD2  1 
ATOM   124  C  CE1  . HIS A 1 17  ? 13.852  -2.819  22.626  1.00 17.62 ?  17  HIS A CE1  1 
ATOM   125  N  NE2  . HIS A 1 17  ? 13.249  -3.776  21.945  1.00 17.23 ?  17  HIS A NE2  1 
ATOM   126  N  N    . LYS A 1 18  ? 12.279  -0.305  19.857  1.00 13.64 ?  18  LYS A N    1 
ATOM   127  C  CA   . LYS A 1 18  ? 13.539  0.403   19.455  1.00 13.74 ?  18  LYS A CA   1 
ATOM   128  C  C    . LYS A 1 18  ? 13.185  1.751   18.765  1.00 16.98 ?  18  LYS A C    1 
ATOM   129  O  O    . LYS A 1 18  ? 13.849  2.755   18.996  1.00 21.10 ?  18  LYS A O    1 
ATOM   130  C  CB   . LYS A 1 18  ? 14.360  -0.524  18.523  1.00 16.48 ?  18  LYS A CB   1 
ATOM   131  C  CG   . LYS A 1 18  ? 14.967  -1.643  19.291  1.00 17.50 ?  18  LYS A CG   1 
ATOM   132  C  CD   . LYS A 1 18  ? 15.652  -2.617  18.349  1.00 17.78 ?  18  LYS A CD   1 
ATOM   133  C  CE   . LYS A 1 18  ? 14.680  -3.629  17.700  1.00 16.93 ?  18  LYS A CE   1 
ATOM   134  N  NZ   . LYS A 1 18  ? 15.303  -4.483  16.569  1.00 15.78 ?  18  LYS A NZ   1 
ATOM   135  N  N    . ASP A 1 19  ? 12.172  1.783   17.910  1.00 16.08 ?  19  ASP A N    1 
ATOM   136  C  CA   . ASP A 1 19  ? 11.757  3.080   17.350  1.00 16.83 ?  19  ASP A CA   1 
ATOM   137  C  C    . ASP A 1 19  ? 10.731  3.820   18.253  1.00 15.69 ?  19  ASP A C    1 
ATOM   138  O  O    . ASP A 1 19  ? 10.605  5.059   18.129  1.00 18.40 ?  19  ASP A O    1 
ATOM   139  C  CB   . ASP A 1 19  ? 11.170  2.988   15.956  1.00 19.29 ?  19  ASP A CB   1 
ATOM   140  C  CG   . ASP A 1 19  ? 12.225  2.980   14.836  1.00 23.75 ?  19  ASP A CG   1 
ATOM   141  O  OD1  . ASP A 1 19  ? 13.349  3.475   15.011  1.00 25.84 ?  19  ASP A OD1  1 
ATOM   142  O  OD2  . ASP A 1 19  ? 11.907  2.500   13.733  1.00 34.38 ?  19  ASP A OD2  1 
ATOM   143  N  N    . PHE A 1 20  ? 9.951   3.058   19.054  1.00 13.72 ?  20  PHE A N    1 
ATOM   144  C  CA   . PHE A 1 20  ? 8.819   3.682   19.794  1.00 13.33 ?  20  PHE A CA   1 
ATOM   145  C  C    . PHE A 1 20  ? 8.910   3.191   21.256  1.00 13.52 ?  20  PHE A C    1 
ATOM   146  O  O    . PHE A 1 20  ? 8.312   2.159   21.608  1.00 13.69 ?  20  PHE A O    1 
ATOM   147  C  CB   . PHE A 1 20  ? 7.471   3.226   19.155  1.00 14.80 ?  20  PHE A CB   1 
ATOM   148  C  CG   . PHE A 1 20  ? 7.372   3.608   17.731  1.00 14.85 ?  20  PHE A CG   1 
ATOM   149  C  CD1  . PHE A 1 20  ? 7.057   4.937   17.373  1.00 16.74 ?  20  PHE A CD1  1 
ATOM   150  C  CD2  . PHE A 1 20  ? 7.780   2.677   16.744  1.00 15.38 ?  20  PHE A CD2  1 
ATOM   151  C  CE1  . PHE A 1 20  ? 6.978   5.277   16.046  1.00 15.91 ?  20  PHE A CE1  1 
ATOM   152  C  CE2  . PHE A 1 20  ? 7.761   3.004   15.418  1.00 14.81 ?  20  PHE A CE2  1 
ATOM   153  C  CZ   . PHE A 1 20  ? 7.355   4.345   15.049  1.00 16.24 ?  20  PHE A CZ   1 
ATOM   154  N  N    . PRO A 1 21  ? 9.834   3.797   22.059  1.00 14.43 ?  21  PRO A N    1 
ATOM   155  C  CA   . PRO A 1 21  ? 10.054  3.272   23.411  1.00 14.56 ?  21  PRO A CA   1 
ATOM   156  C  C    . PRO A 1 21  ? 8.816   3.140   24.301  1.00 13.28 ?  21  PRO A C    1 
ATOM   157  O  O    . PRO A 1 21  ? 8.870   2.383   25.284  1.00 14.47 ?  21  PRO A O    1 
ATOM   158  C  CB   . PRO A 1 21  ? 11.127  4.224   24.043  1.00 15.06 ?  21  PRO A CB   1 
ATOM   159  C  CG   . PRO A 1 21  ? 11.541  5.181   22.922  1.00 19.48 ?  21  PRO A CG   1 
ATOM   160  C  CD   . PRO A 1 21  ? 10.801  4.867   21.687  1.00 15.73 ?  21  PRO A CD   1 
ATOM   161  N  N    A ILE A 1 22  ? 7.733   3.901   24.024  0.50 13.08 ?  22  ILE A N    1 
ATOM   162  N  N    B ILE A 1 22  ? 7.756   3.899   23.967  0.50 12.38 ?  22  ILE A N    1 
ATOM   163  C  CA   A ILE A 1 22  ? 6.510   3.782   24.830  0.50 12.53 ?  22  ILE A CA   1 
ATOM   164  C  CA   B ILE A 1 22  ? 6.489   3.847   24.666  0.50 10.84 ?  22  ILE A CA   1 
ATOM   165  C  C    A ILE A 1 22  ? 5.935   2.386   24.664  0.50 10.90 ?  22  ILE A C    1 
ATOM   166  C  C    B ILE A 1 22  ? 5.861   2.468   24.529  0.50 10.36 ?  22  ILE A C    1 
ATOM   167  O  O    A ILE A 1 22  ? 5.081   1.979   25.470  0.50 11.66 ?  22  ILE A O    1 
ATOM   168  O  O    B ILE A 1 22  ? 4.878   2.174   25.181  0.50 11.35 ?  22  ILE A O    1 
ATOM   169  C  CB   A ILE A 1 22  ? 5.447   4.894   24.487  0.50 11.97 ?  22  ILE A CB   1 
ATOM   170  C  CB   B ILE A 1 22  ? 5.556   4.952   24.105  0.50 10.04 ?  22  ILE A CB   1 
ATOM   171  C  CG1  A ILE A 1 22  ? 4.423   5.072   25.629  0.50 14.75 ?  22  ILE A CG1  1 
ATOM   172  C  CG1  B ILE A 1 22  ? 4.504   5.345   25.146  0.50 9.64  ?  22  ILE A CG1  1 
ATOM   173  C  CG2  A ILE A 1 22  ? 4.778   4.637   23.115  0.50 13.32 ?  22  ILE A CG2  1 
ATOM   174  C  CG2  B ILE A 1 22  ? 5.046   4.546   22.696  0.50 10.70 ?  22  ILE A CG2  1 
ATOM   175  C  CD1  A ILE A 1 22  ? 4.872   6.061   26.707  0.50 16.48 ?  22  ILE A CD1  1 
ATOM   176  C  CD1  B ILE A 1 22  ? 3.506   6.389   24.760  0.50 9.32  ?  22  ILE A CD1  1 
ATOM   177  N  N    . ALA A 1 23  ? 6.433   1.632   23.663  1.00 10.97 ?  23  ALA A N    1 
ATOM   178  C  CA   . ALA A 1 23  ? 5.963   0.205   23.543  1.00 11.46 ?  23  ALA A CA   1 
ATOM   179  C  C    . ALA A 1 23  ? 6.077   -0.520  24.885  1.00 12.79 ?  23  ALA A C    1 
ATOM   180  O  O    . ALA A 1 23  ? 5.353   -1.558  25.108  1.00 12.23 ?  23  ALA A O    1 
ATOM   181  C  CB   . ALA A 1 23  ? 6.849   -0.600  22.494  1.00 12.46 ?  23  ALA A CB   1 
ATOM   182  N  N    . LYS A 1 24  ? 7.027   -0.078  25.760  1.00 12.94 ?  24  LYS A N    1 
ATOM   183  C  CA   . LYS A 1 24  ? 7.170   -0.739  27.109  1.00 13.60 ?  24  LYS A CA   1 
ATOM   184  C  C    . LYS A 1 24  ? 6.548   0.175   28.189  1.00 13.47 ?  24  LYS A C    1 
ATOM   185  O  O    . LYS A 1 24  ? 6.946   0.103   29.403  1.00 16.25 ?  24  LYS A O    1 
ATOM   186  C  CB   . LYS A 1 24  ? 8.666   -0.986  27.398  1.00 13.78 ?  24  LYS A CB   1 
ATOM   187  C  CG   . LYS A 1 24  ? 9.279   -1.949  26.400  1.00 17.64 ?  24  LYS A CG   1 
ATOM   188  C  CD   . LYS A 1 24  ? 10.784  -2.101  26.733  1.00 21.02 ?  24  LYS A CD   1 
ATOM   189  C  CE   . LYS A 1 24  ? 11.419  -3.100  25.771  1.00 24.90 ?  24  LYS A CE   1 
ATOM   190  N  NZ   . LYS A 1 24  ? 11.321  -4.426  26.357  1.00 28.07 ?  24  LYS A NZ   1 
ATOM   191  N  N    . GLY A 1 25  ? 5.517   0.967   27.805  1.00 14.33 ?  25  GLY A N    1 
ATOM   192  C  CA   . GLY A 1 25  ? 4.929   1.942   28.718  1.00 13.75 ?  25  GLY A CA   1 
ATOM   193  C  C    . GLY A 1 25  ? 3.953   1.361   29.716  1.00 13.73 ?  25  GLY A C    1 
ATOM   194  O  O    . GLY A 1 25  ? 3.773   0.107   29.864  1.00 14.06 ?  25  GLY A O    1 
ATOM   195  N  N    . GLU A 1 26  ? 3.309   2.290   30.453  1.00 14.12 ?  26  GLU A N    1 
ATOM   196  C  CA   . GLU A 1 26  ? 2.445   1.905   31.545  1.00 14.66 ?  26  GLU A CA   1 
ATOM   197  C  C    . GLU A 1 26  ? 0.988   1.601   31.172  1.00 12.66 ?  26  GLU A C    1 
ATOM   198  O  O    . GLU A 1 26  ? 0.249   1.066   32.009  1.00 14.02 ?  26  GLU A O    1 
ATOM   199  C  CB   . GLU A 1 26  ? 2.446   3.021   32.630  1.00 16.08 ?  26  GLU A CB   1 
ATOM   200  C  CG   . GLU A 1 26  ? 3.835   3.317   33.250  1.00 20.14 ?  26  GLU A CG   1 
ATOM   201  C  CD   . GLU A 1 26  ? 4.448   1.993   33.864  1.00 29.48 ?  26  GLU A CD   1 
ATOM   202  O  OE1  . GLU A 1 26  ? 3.767   1.355   34.746  1.00 31.16 ?  26  GLU A OE1  1 
ATOM   203  O  OE2  . GLU A 1 26  ? 5.561   1.555   33.418  1.00 33.79 ?  26  GLU A OE2  1 
ATOM   204  N  N    . ARG A 1 27  ? 0.564   1.911   29.921  1.00 11.42 ?  27  ARG A N    1 
ATOM   205  C  CA   . ARG A 1 27  ? -0.865  1.695   29.590  1.00 10.27 ?  27  ARG A CA   1 
ATOM   206  C  C    . ARG A 1 27  ? -0.925  1.270   28.115  1.00 9.55  ?  27  ARG A C    1 
ATOM   207  O  O    . ARG A 1 27  ? -1.647  1.864   27.261  1.00 10.20 ?  27  ARG A O    1 
ATOM   208  C  CB   . ARG A 1 27  ? -1.780  2.923   29.890  1.00 13.42 ?  27  ARG A CB   1 
ATOM   209  C  CG   . ARG A 1 27  ? -1.413  4.168   29.200  1.00 14.95 ?  27  ARG A CG   1 
ATOM   210  C  CD   . ARG A 1 27  ? -2.405  5.438   29.455  1.00 16.74 ?  27  ARG A CD   1 
ATOM   211  N  NE   . ARG A 1 27  ? -3.606  5.344   28.615  1.00 17.58 ?  27  ARG A NE   1 
ATOM   212  C  CZ   . ARG A 1 27  ? -4.532  6.275   28.469  1.00 14.82 ?  27  ARG A CZ   1 
ATOM   213  N  NH1  . ARG A 1 27  ? -4.501  7.500   29.090  1.00 15.11 ?  27  ARG A NH1  1 
ATOM   214  N  NH2  . ARG A 1 27  ? -5.473  6.010   27.639  1.00 14.35 ?  27  ARG A NH2  1 
ATOM   215  N  N    . GLN A 1 28  ? -0.164  0.175   27.833  1.00 8.84  ?  28  GLN A N    1 
ATOM   216  C  CA   . GLN A 1 28  ? -0.154  -0.341  26.419  1.00 7.20  ?  28  GLN A CA   1 
ATOM   217  C  C    . GLN A 1 28  ? -1.308  -1.330  26.154  1.00 7.77  ?  28  GLN A C    1 
ATOM   218  O  O    . GLN A 1 28  ? -1.824  -2.009  27.085  1.00 9.36  ?  28  GLN A O    1 
ATOM   219  C  CB   . GLN A 1 28  ? 1.157   -1.052  26.157  1.00 8.35  ?  28  GLN A CB   1 
ATOM   220  C  CG   . GLN A 1 28  ? 2.308   -0.013  26.108  1.00 8.62  ?  28  GLN A CG   1 
ATOM   221  C  CD   . GLN A 1 28  ? 2.200   0.820   24.799  1.00 8.89  ?  28  GLN A CD   1 
ATOM   222  O  OE1  . GLN A 1 28  ? 2.441   0.278   23.707  1.00 9.37  ?  28  GLN A OE1  1 
ATOM   223  N  NE2  . GLN A 1 28  ? 1.903   2.134   24.926  1.00 8.82  ?  28  GLN A NE2  1 
ATOM   224  N  N    . SER A 1 29  ? -1.712  -1.394  24.887  1.00 6.61  ?  29  SER A N    1 
ATOM   225  C  CA   . SER A 1 29  ? -2.748  -2.308  24.433  1.00 7.28  ?  29  SER A CA   1 
ATOM   226  C  C    . SER A 1 29  ? -2.197  -3.153  23.274  1.00 7.00  ?  29  SER A C    1 
ATOM   227  O  O    . SER A 1 29  ? -1.242  -2.784  22.602  1.00 8.06  ?  29  SER A O    1 
ATOM   228  C  CB   . SER A 1 29  ? -3.908  -1.457  23.844  1.00 7.52  ?  29  SER A CB   1 
ATOM   229  O  OG   . SER A 1 29  ? -4.531  -0.709  24.928  1.00 8.09  ?  29  SER A OG   1 
ATOM   230  N  N    . PRO A 1 30  ? -2.841  -4.289  23.009  1.00 6.62  ?  30  PRO A N    1 
ATOM   231  C  CA   . PRO A 1 30  ? -4.018  -4.858  23.701  1.00 7.34  ?  30  PRO A CA   1 
ATOM   232  C  C    . PRO A 1 30  ? -3.602  -5.506  25.019  1.00 7.08  ?  30  PRO A C    1 
ATOM   233  O  O    . PRO A 1 30  ? -2.400  -5.571  25.347  1.00 8.16  ?  30  PRO A O    1 
ATOM   234  C  CB   . PRO A 1 30  ? -4.517  -5.903  22.666  1.00 8.19  ?  30  PRO A CB   1 
ATOM   235  C  CG   . PRO A 1 30  ? -3.205  -6.503  22.158  1.00 8.40  ?  30  PRO A CG   1 
ATOM   236  C  CD   . PRO A 1 30  ? -2.350  -5.235  21.967  1.00 8.36  ?  30  PRO A CD   1 
ATOM   237  N  N    . VAL A 1 31  ? -4.597  -6.086  25.706  1.00 7.32  ?  31  VAL A N    1 
ATOM   238  C  CA   . VAL A 1 31  ? -4.387  -6.849  26.921  1.00 8.11  ?  31  VAL A CA   1 
ATOM   239  C  C    . VAL A 1 31  ? -5.292  -8.066  26.916  1.00 8.56  ?  31  VAL A C    1 
ATOM   240  O  O    . VAL A 1 31  ? -6.257  -8.166  26.124  1.00 8.68  ?  31  VAL A O    1 
ATOM   241  C  CB   . VAL A 1 31  ? -4.716  -6.011  28.208  1.00 8.61  ?  31  VAL A CB   1 
ATOM   242  C  CG1  . VAL A 1 31  ? -3.757  -4.832  28.339  1.00 9.57  ?  31  VAL A CG1  1 
ATOM   243  C  CG2  . VAL A 1 31  ? -6.210  -5.611  28.249  1.00 9.29  ?  31  VAL A CG2  1 
ATOM   244  N  N    . ASP A 1 32  ? -4.928  -9.044  27.771  1.00 8.32  ?  32  ASP A N    1 
ATOM   245  C  CA   . ASP A 1 32  ? -5.840  -10.185 28.014  1.00 8.31  ?  32  ASP A CA   1 
ATOM   246  C  C    . ASP A 1 32  ? -6.925  -9.656  28.977  1.00 8.67  ?  32  ASP A C    1 
ATOM   247  O  O    . ASP A 1 32  ? -6.617  -9.038  30.041  1.00 10.14 ?  32  ASP A O    1 
ATOM   248  C  CB   . ASP A 1 32  ? -5.106  -11.373 28.619  1.00 9.74  ?  32  ASP A CB   1 
ATOM   249  C  CG   . ASP A 1 32  ? -6.063  -12.512 28.933  1.00 11.95 ?  32  ASP A CG   1 
ATOM   250  O  OD1  . ASP A 1 32  ? -6.761  -12.937 27.995  1.00 9.85  ?  32  ASP A OD1  1 
ATOM   251  O  OD2  . ASP A 1 32  ? -6.105  -12.986 30.152  1.00 14.08 ?  32  ASP A OD2  1 
ATOM   252  N  N    . ILE A 1 33  ? -8.203  -9.954  28.674  1.00 8.32  ?  33  ILE A N    1 
ATOM   253  C  CA   . ILE A 1 33  ? -9.333  -9.610  29.560  1.00 9.29  ?  33  ILE A CA   1 
ATOM   254  C  C    . ILE A 1 33  ? -9.655  -10.843 30.395  1.00 9.00  ?  33  ILE A C    1 
ATOM   255  O  O    . ILE A 1 33  ? -10.158 -11.884 29.905  1.00 11.47 ?  33  ILE A O    1 
ATOM   256  C  CB   . ILE A 1 33  ? -10.549 -9.129  28.751  1.00 10.87 ?  33  ILE A CB   1 
ATOM   257  C  CG1  . ILE A 1 33  ? -10.174 -7.865  27.929  1.00 8.58  ?  33  ILE A CG1  1 
ATOM   258  C  CG2  . ILE A 1 33  ? -11.736 -8.891  29.708  1.00 12.75 ?  33  ILE A CG2  1 
ATOM   259  C  CD1  . ILE A 1 33  ? -11.225 -7.595  26.761  1.00 10.49 ?  33  ILE A CD1  1 
ATOM   260  N  N    . ASP A 1 34  ? -9.245  -10.725 31.660  1.00 10.69 ?  34  ASP A N    1 
ATOM   261  C  CA   . ASP A 1 34  ? -9.506  -11.821 32.599  1.00 13.56 ?  34  ASP A CA   1 
ATOM   262  C  C    . ASP A 1 34  ? -10.935 -11.612 33.131  1.00 13.52 ?  34  ASP A C    1 
ATOM   263  O  O    . ASP A 1 34  ? -11.171 -10.662 33.914  1.00 15.79 ?  34  ASP A O    1 
ATOM   264  C  CB   . ASP A 1 34  ? -8.498  -11.796 33.741  1.00 14.76 ?  34  ASP A CB   1 
ATOM   265  C  CG   . ASP A 1 34  ? -8.632  -13.050 34.582  1.00 20.70 ?  34  ASP A CG   1 
ATOM   266  O  OD1  . ASP A 1 34  ? -9.564  -13.114 35.330  1.00 23.74 ?  34  ASP A OD1  1 
ATOM   267  O  OD2  . ASP A 1 34  ? -7.964  -14.060 34.254  1.00 28.53 ?  34  ASP A OD2  1 
ATOM   268  N  N    . THR A 1 35  ? -11.891 -12.407 32.632  1.00 14.08 ?  35  THR A N    1 
ATOM   269  C  CA   . THR A 1 35  ? -13.310 -12.058 32.878  1.00 14.99 ?  35  THR A CA   1 
ATOM   270  C  C    . THR A 1 35  ? -13.715 -12.190 34.362  1.00 14.12 ?  35  THR A C    1 
ATOM   271  O  O    . THR A 1 35  ? -14.680 -11.509 34.823  1.00 17.80 ?  35  THR A O    1 
ATOM   272  C  CB   . THR A 1 35  ? -14.228 -12.978 32.090  1.00 16.23 ?  35  THR A CB   1 
ATOM   273  O  OG1  . THR A 1 35  ? -14.080 -14.318 32.589  1.00 18.25 ?  35  THR A OG1  1 
ATOM   274  C  CG2  . THR A 1 35  ? -13.968 -12.943 30.583  1.00 16.54 ?  35  THR A CG2  1 
ATOM   275  N  N    . HIS A 1 36  ? -13.006 -13.037 35.098  1.00 16.17 ?  36  HIS A N    1 
ATOM   276  C  CA   . HIS A 1 36  ? -13.287 -13.250 36.520  1.00 16.74 ?  36  HIS A CA   1 
ATOM   277  C  C    . HIS A 1 36  ? -12.810 -12.097 37.377  1.00 19.07 ?  36  HIS A C    1 
ATOM   278  O  O    . HIS A 1 36  ? -13.543 -11.761 38.374  1.00 21.92 ?  36  HIS A O    1 
ATOM   279  C  CB   . HIS A 1 36  ? -12.780 -14.645 36.899  1.00 19.12 ?  36  HIS A CB   1 
ATOM   280  C  CG   . HIS A 1 36  ? -13.709 -15.698 36.394  1.00 20.52 ?  36  HIS A CG   1 
ATOM   281  N  ND1  . HIS A 1 36  ? -13.398 -16.599 35.376  1.00 23.79 ?  36  HIS A ND1  1 
ATOM   282  C  CD2  . HIS A 1 36  ? -15.023 -15.884 36.679  1.00 22.62 ?  36  HIS A CD2  1 
ATOM   283  C  CE1  . HIS A 1 36  ? -14.468 -17.340 35.120  1.00 24.13 ?  36  HIS A CE1  1 
ATOM   284  N  NE2  . HIS A 1 36  ? -15.465 -16.928 35.885  1.00 28.28 ?  36  HIS A NE2  1 
ATOM   285  N  N    . THR A 1 37  ? -11.694 -11.434 36.994  1.00 18.58 ?  37  THR A N    1 
ATOM   286  C  CA   . THR A 1 37  ? -11.185 -10.304 37.719  1.00 20.54 ?  37  THR A CA   1 
ATOM   287  C  C    . THR A 1 37  ? -11.605 -8.891  37.231  1.00 18.00 ?  37  THR A C    1 
ATOM   288  O  O    . THR A 1 37  ? -11.339 -7.883  37.924  1.00 20.11 ?  37  THR A O    1 
ATOM   289  C  CB   . THR A 1 37  ? -9.715  -10.344 37.941  1.00 21.86 ?  37  THR A CB   1 
ATOM   290  O  OG1  . THR A 1 37  ? -9.071  -10.455 36.692  1.00 27.83 ?  37  THR A OG1  1 
ATOM   291  C  CG2  . THR A 1 37  ? -9.318  -11.555 38.745  1.00 24.54 ?  37  THR A CG2  1 
ATOM   292  N  N    . ALA A 1 38  ? -12.304 -8.822  36.101  1.00 16.38 ?  38  ALA A N    1 
ATOM   293  C  CA   . ALA A 1 38  ? -12.898 -7.535  35.699  1.00 14.43 ?  38  ALA A CA   1 
ATOM   294  C  C    . ALA A 1 38  ? -13.936 -7.150  36.761  1.00 15.75 ?  38  ALA A C    1 
ATOM   295  O  O    . ALA A 1 38  ? -14.664 -7.993  37.291  1.00 18.88 ?  38  ALA A O    1 
ATOM   296  C  CB   . ALA A 1 38  ? -13.529 -7.665  34.318  1.00 16.86 ?  38  ALA A CB   1 
ATOM   297  N  N    . LYS A 1 39  ? -13.981 -5.861  37.078  1.00 15.67 ?  39  LYS A N    1 
ATOM   298  C  CA   . LYS A 1 39  ? -14.837 -5.382  38.167  1.00 17.04 ?  39  LYS A CA   1 
ATOM   299  C  C    . LYS A 1 39  ? -16.143 -4.857  37.508  1.00 16.05 ?  39  LYS A C    1 
ATOM   300  O  O    . LYS A 1 39  ? -16.108 -3.894  36.734  1.00 14.20 ?  39  LYS A O    1 
ATOM   301  C  CB   . LYS A 1 39  ? -14.041 -4.255  38.834  1.00 18.49 ?  39  LYS A CB   1 
ATOM   302  C  CG   . LYS A 1 39  ? -14.800 -3.337  39.813  1.00 20.24 ?  39  LYS A CG   1 
ATOM   303  C  CD   . LYS A 1 39  ? -15.078 -4.039  41.116  1.00 19.38 ?  39  LYS A CD   1 
ATOM   304  C  CE   . LYS A 1 39  ? -15.751 -3.088  42.129  1.00 24.48 ?  39  LYS A CE   1 
ATOM   305  N  NZ   . LYS A 1 39  ? -16.232 -3.945  43.243  1.00 26.82 ?  39  LYS A NZ   1 
ATOM   306  N  N    . TYR A 1 40  ? -17.282 -5.401  37.887  1.00 17.21 ?  40  TYR A N    1 
ATOM   307  C  CA   . TYR A 1 40  ? -18.562 -4.832  37.492  1.00 18.49 ?  40  TYR A CA   1 
ATOM   308  C  C    . TYR A 1 40  ? -18.704 -3.437  38.110  1.00 18.44 ?  40  TYR A C    1 
ATOM   309  O  O    . TYR A 1 40  ? -18.481 -3.256  39.366  1.00 18.73 ?  40  TYR A O    1 
ATOM   310  C  CB   . TYR A 1 40  ? -19.753 -5.787  37.869  1.00 19.96 ?  40  TYR A CB   1 
ATOM   311  C  CG   . TYR A 1 40  ? -21.086 -5.135  37.732  1.00 22.59 ?  40  TYR A CG   1 
ATOM   312  C  CD1  . TYR A 1 40  ? -21.529 -4.681  36.498  1.00 21.40 ?  40  TYR A CD1  1 
ATOM   313  C  CD2  . TYR A 1 40  ? -21.943 -4.958  38.872  1.00 27.18 ?  40  TYR A CD2  1 
ATOM   314  C  CE1  . TYR A 1 40  ? -22.768 -4.089  36.309  1.00 23.14 ?  40  TYR A CE1  1 
ATOM   315  C  CE2  . TYR A 1 40  ? -23.231 -4.313  38.698  1.00 29.05 ?  40  TYR A CE2  1 
ATOM   316  C  CZ   . TYR A 1 40  ? -23.616 -3.903  37.398  1.00 26.04 ?  40  TYR A CZ   1 
ATOM   317  O  OH   . TYR A 1 40  ? -24.825 -3.277  37.221  1.00 29.33 ?  40  TYR A OH   1 
ATOM   318  N  N    . ASP A 1 41  ? -19.042 -2.457  37.252  1.00 17.93 ?  41  ASP A N    1 
ATOM   319  C  CA   . ASP A 1 41  ? -19.197 -1.064  37.726  1.00 19.91 ?  41  ASP A CA   1 
ATOM   320  C  C    . ASP A 1 41  ? -20.652 -0.685  37.425  1.00 23.90 ?  41  ASP A C    1 
ATOM   321  O  O    . ASP A 1 41  ? -20.986 -0.378  36.250  1.00 23.48 ?  41  ASP A O    1 
ATOM   322  C  CB   . ASP A 1 41  ? -18.175 -0.137  37.073  1.00 22.02 ?  41  ASP A CB   1 
ATOM   323  C  CG   . ASP A 1 41  ? -18.293 1.317   37.604  1.00 25.74 ?  41  ASP A CG   1 
ATOM   324  O  OD1  . ASP A 1 41  ? -19.282 1.583   38.304  1.00 26.35 ?  41  ASP A OD1  1 
ATOM   325  O  OD2  . ASP A 1 41  ? -17.387 2.128   37.386  1.00 31.05 ?  41  ASP A OD2  1 
ATOM   326  N  N    . PRO A 1 42  ? -21.548 -0.763  38.457  1.00 26.66 ?  42  PRO A N    1 
ATOM   327  C  CA   . PRO A 1 42  ? -22.956 -0.452  38.186  1.00 26.63 ?  42  PRO A CA   1 
ATOM   328  C  C    . PRO A 1 42  ? -23.152 1.013   37.832  1.00 27.84 ?  42  PRO A C    1 
ATOM   329  O  O    . PRO A 1 42  ? -24.245 1.331   37.331  1.00 30.29 ?  42  PRO A O    1 
ATOM   330  C  CB   . PRO A 1 42  ? -23.652 -0.778  39.532  1.00 28.47 ?  42  PRO A CB   1 
ATOM   331  C  CG   . PRO A 1 42  ? -22.519 -0.505  40.555  1.00 27.65 ?  42  PRO A CG   1 
ATOM   332  C  CD   . PRO A 1 42  ? -21.336 -1.131  39.868  1.00 26.49 ?  42  PRO A CD   1 
ATOM   333  N  N    . SER A 1 43  ? -22.156 1.897   38.048  1.00 26.94 ?  43  SER A N    1 
ATOM   334  C  CA   . SER A 1 43  ? -22.302 3.294   37.582  1.00 27.92 ?  43  SER A CA   1 
ATOM   335  C  C    . SER A 1 43  ? -21.918 3.527   36.068  1.00 27.11 ?  43  SER A C    1 
ATOM   336  O  O    . SER A 1 43  ? -22.065 4.668   35.533  1.00 29.09 ?  43  SER A O    1 
ATOM   337  C  CB   . SER A 1 43  ? -21.487 4.250   38.459  1.00 30.01 ?  43  SER A CB   1 
ATOM   338  O  OG   . SER A 1 43  ? -20.099 4.236   38.093  1.00 29.67 ?  43  SER A OG   1 
ATOM   339  N  N    . LEU A 1 44  ? -21.406 2.486   35.387  1.00 24.45 ?  44  LEU A N    1 
ATOM   340  C  CA   . LEU A 1 44  ? -21.137 2.616   33.936  1.00 22.69 ?  44  LEU A CA   1 
ATOM   341  C  C    . LEU A 1 44  ? -22.456 2.742   33.196  1.00 23.91 ?  44  LEU A C    1 
ATOM   342  O  O    . LEU A 1 44  ? -23.388 2.008   33.436  1.00 25.24 ?  44  LEU A O    1 
ATOM   343  C  CB   . LEU A 1 44  ? -20.386 1.414   33.364  1.00 21.55 ?  44  LEU A CB   1 
ATOM   344  C  CG   . LEU A 1 44  ? -18.904 1.456   33.646  1.00 18.84 ?  44  LEU A CG   1 
ATOM   345  C  CD1  . LEU A 1 44  ? -18.369 0.044   33.253  1.00 17.55 ?  44  LEU A CD1  1 
ATOM   346  C  CD2  . LEU A 1 44  ? -18.175 2.625   32.973  1.00 19.56 ?  44  LEU A CD2  1 
ATOM   347  N  N    . LYS A 1 45  ? -22.504 3.640   32.222  1.00 22.92 ?  45  LYS A N    1 
ATOM   348  C  CA   . LYS A 1 45  ? -23.775 3.879   31.459  1.00 23.30 ?  45  LYS A CA   1 
ATOM   349  C  C    . LYS A 1 45  ? -23.802 2.965   30.225  1.00 22.08 ?  45  LYS A C    1 
ATOM   350  O  O    . LYS A 1 45  ? -22.763 2.436   29.806  1.00 22.44 ?  45  LYS A O    1 
ATOM   351  C  CB   . LYS A 1 45  ? -23.842 5.296   30.993  1.00 23.22 ?  45  LYS A CB   1 
ATOM   352  C  CG   . LYS A 1 45  ? -23.674 6.364   32.102  1.00 29.43 ?  45  LYS A CG   1 
ATOM   353  C  CD   . LYS A 1 45  ? -23.563 7.763   31.503  1.00 36.97 ?  45  LYS A CD   1 
ATOM   354  C  CE   . LYS A 1 45  ? -23.593 8.774   32.616  1.00 43.12 ?  45  LYS A CE   1 
ATOM   355  N  NZ   . LYS A 1 45  ? -24.931 8.511   33.231  1.00 46.65 ?  45  LYS A NZ   1 
ATOM   356  N  N    . PRO A 1 46  ? -25.009 2.742   29.652  1.00 20.40 ?  46  PRO A N    1 
ATOM   357  C  CA   . PRO A 1 46  ? -25.084 2.098   28.356  1.00 19.21 ?  46  PRO A CA   1 
ATOM   358  C  C    . PRO A 1 46  ? -24.251 2.882   27.363  1.00 17.72 ?  46  PRO A C    1 
ATOM   359  O  O    . PRO A 1 46  ? -24.225 4.139   27.412  1.00 17.48 ?  46  PRO A O    1 
ATOM   360  C  CB   . PRO A 1 46  ? -26.566 2.234   27.953  1.00 18.68 ?  46  PRO A CB   1 
ATOM   361  C  CG   . PRO A 1 46  ? -27.292 2.568   29.162  1.00 22.57 ?  46  PRO A CG   1 
ATOM   362  C  CD   . PRO A 1 46  ? -26.326 3.091   30.217  1.00 20.30 ?  46  PRO A CD   1 
ATOM   363  N  N    . LEU A 1 47  ? -23.615 2.149   26.441  1.00 17.84 ?  47  LEU A N    1 
ATOM   364  C  CA   . LEU A 1 47  ? -22.881 2.807   25.382  1.00 15.89 ?  47  LEU A CA   1 
ATOM   365  C  C    . LEU A 1 47  ? -23.942 3.422   24.406  1.00 16.22 ?  47  LEU A C    1 
ATOM   366  O  O    . LEU A 1 47  ? -25.034 2.821   24.181  1.00 17.85 ?  47  LEU A O    1 
ATOM   367  C  CB   . LEU A 1 47  ? -21.996 1.765   24.682  1.00 20.22 ?  47  LEU A CB   1 
ATOM   368  C  CG   . LEU A 1 47  ? -21.080 2.153   23.616  1.00 22.34 ?  47  LEU A CG   1 
ATOM   369  C  CD1  . LEU A 1 47  ? -20.048 3.119   24.215  1.00 23.24 ?  47  LEU A CD1  1 
ATOM   370  C  CD2  . LEU A 1 47  ? -20.462 0.786   23.223  1.00 20.64 ?  47  LEU A CD2  1 
ATOM   371  N  N    . SER A 1 48  ? -23.672 4.635   23.913  1.00 14.08 ?  48  SER A N    1 
ATOM   372  C  CA   . SER A 1 48  ? -24.507 5.289   22.884  1.00 15.11 ?  48  SER A CA   1 
ATOM   373  C  C    . SER A 1 48  ? -23.743 5.275   21.539  1.00 14.51 ?  48  SER A C    1 
ATOM   374  O  O    . SER A 1 48  ? -22.769 6.022   21.333  1.00 14.26 ?  48  SER A O    1 
ATOM   375  C  CB   . SER A 1 48  ? -24.813 6.755   23.293  1.00 15.15 ?  48  SER A CB   1 
ATOM   376  O  OG   . SER A 1 48  ? -25.486 7.449   22.242  1.00 19.95 ?  48  SER A OG   1 
ATOM   377  N  N    . VAL A 1 49  ? -24.237 4.465   20.634  1.00 17.36 ?  49  VAL A N    1 
ATOM   378  C  CA   . VAL A 1 49  ? -23.649 4.363   19.282  1.00 18.83 ?  49  VAL A CA   1 
ATOM   379  C  C    . VAL A 1 49  ? -24.617 5.014   18.298  1.00 19.86 ?  49  VAL A C    1 
ATOM   380  O  O    . VAL A 1 49  ? -25.693 4.518   18.061  1.00 21.44 ?  49  VAL A O    1 
ATOM   381  C  CB   . VAL A 1 49  ? -23.410 2.868   18.863  1.00 20.20 ?  49  VAL A CB   1 
ATOM   382  C  CG1  . VAL A 1 49  ? -22.704 2.782   17.465  1.00 24.40 ?  49  VAL A CG1  1 
ATOM   383  C  CG2  . VAL A 1 49  ? -22.590 2.127   19.943  1.00 21.15 ?  49  VAL A CG2  1 
ATOM   384  N  N    . SER A 1 50  ? -24.262 6.135   17.741  1.00 18.12 ?  50  SER A N    1 
ATOM   385  C  CA   . SER A 1 50  ? -25.155 6.881   16.876  1.00 19.29 ?  50  SER A CA   1 
ATOM   386  C  C    . SER A 1 50  ? -24.599 6.954   15.522  1.00 17.52 ?  50  SER A C    1 
ATOM   387  O  O    . SER A 1 50  ? -23.899 7.891   15.191  1.00 17.56 ?  50  SER A O    1 
ATOM   388  C  CB   . SER A 1 50  ? -25.522 8.291   17.412  1.00 20.72 ?  50  SER A CB   1 
ATOM   389  O  OG   . SER A 1 50  ? -26.131 8.226   18.660  1.00 28.49 ?  50  SER A OG   1 
ATOM   390  N  N    . TYR A 1 51  ? -24.856 5.901   14.740  1.00 17.95 ?  51  TYR A N    1 
ATOM   391  C  CA   . TYR A 1 51  ? -24.274 5.796   13.404  1.00 16.40 ?  51  TYR A CA   1 
ATOM   392  C  C    . TYR A 1 51  ? -25.256 6.067   12.213  1.00 17.32 ?  51  TYR A C    1 
ATOM   393  O  O    . TYR A 1 51  ? -24.830 5.927   11.068  1.00 18.62 ?  51  TYR A O    1 
ATOM   394  C  CB   . TYR A 1 51  ? -23.629 4.389   13.218  1.00 16.12 ?  51  TYR A CB   1 
ATOM   395  C  CG   . TYR A 1 51  ? -22.301 4.136   13.949  1.00 12.75 ?  51  TYR A CG   1 
ATOM   396  C  CD1  . TYR A 1 51  ? -21.574 5.180   14.645  1.00 14.29 ?  51  TYR A CD1  1 
ATOM   397  C  CD2  . TYR A 1 51  ? -21.793 2.823   13.992  1.00 13.06 ?  51  TYR A CD2  1 
ATOM   398  C  CE1  . TYR A 1 51  ? -20.377 4.877   15.330  1.00 12.22 ?  51  TYR A CE1  1 
ATOM   399  C  CE2  . TYR A 1 51  ? -20.601 2.508   14.599  1.00 13.09 ?  51  TYR A CE2  1 
ATOM   400  C  CZ   . TYR A 1 51  ? -19.893 3.563   15.327  1.00 12.80 ?  51  TYR A CZ   1 
ATOM   401  O  OH   . TYR A 1 51  ? -18.714 3.230   15.947  1.00 13.28 ?  51  TYR A OH   1 
ATOM   402  N  N    . ASP A 1 52  ? -26.507 6.486   12.503  1.00 20.55 ?  52  ASP A N    1 
ATOM   403  C  CA   . ASP A 1 52  ? -27.523 6.730   11.448  1.00 21.29 ?  52  ASP A CA   1 
ATOM   404  C  C    . ASP A 1 52  ? -27.062 7.678   10.334  1.00 23.39 ?  52  ASP A C    1 
ATOM   405  O  O    . ASP A 1 52  ? -27.359 7.446   9.145   1.00 24.65 ?  52  ASP A O    1 
ATOM   406  C  CB   . ASP A 1 52  ? -28.858 7.150   12.084  1.00 23.14 ?  52  ASP A CB   1 
ATOM   407  C  CG   . ASP A 1 52  ? -28.686 8.145   13.244  1.00 29.00 ?  52  ASP A CG   1 
ATOM   408  O  OD1  . ASP A 1 52  ? -28.038 7.880   14.358  1.00 35.62 ?  52  ASP A OD1  1 
ATOM   409  O  OD2  . ASP A 1 52  ? -29.237 9.238   13.040  1.00 37.92 ?  52  ASP A OD2  1 
ATOM   410  N  N    . GLN A 1 53  ? -26.298 8.697   10.683  1.00 22.53 ?  53  GLN A N    1 
ATOM   411  C  CA   . GLN A 1 53  ? -25.870 9.657   9.633   1.00 23.43 ?  53  GLN A CA   1 
ATOM   412  C  C    . GLN A 1 53  ? -24.446 9.466   9.099   1.00 20.08 ?  53  GLN A C    1 
ATOM   413  O  O    . GLN A 1 53  ? -23.856 10.388  8.523   1.00 19.41 ?  53  GLN A O    1 
ATOM   414  C  CB   . GLN A 1 53  ? -26.129 11.120  10.069  1.00 25.41 ?  53  GLN A CB   1 
ATOM   415  C  CG   . GLN A 1 53  ? -27.686 11.471  10.187  1.00 31.05 ?  53  GLN A CG   1 
ATOM   416  C  CD   . GLN A 1 53  ? -28.408 11.151  8.871   1.00 37.84 ?  53  GLN A CD   1 
ATOM   417  O  OE1  . GLN A 1 53  ? -27.908 11.494  7.751   1.00 40.94 ?  53  GLN A OE1  1 
ATOM   418  N  NE2  . GLN A 1 53  ? -29.548 10.435  8.974   1.00 40.59 ?  53  GLN A NE2  1 
ATOM   419  N  N    . ALA A 1 54  ? -23.868 8.279   9.329   1.00 18.09 ?  54  ALA A N    1 
ATOM   420  C  CA   . ALA A 1 54  ? -22.489 8.035   8.873   1.00 14.77 ?  54  ALA A CA   1 
ATOM   421  C  C    . ALA A 1 54  ? -22.291 8.279   7.358   1.00 15.35 ?  54  ALA A C    1 
ATOM   422  O  O    . ALA A 1 54  ? -23.155 7.849   6.503   1.00 18.80 ?  54  ALA A O    1 
ATOM   423  C  CB   . ALA A 1 54  ? -21.990 6.591   9.281   1.00 15.86 ?  54  ALA A CB   1 
ATOM   424  N  N    . THR A 1 55  ? -21.150 8.872   7.056   1.00 14.44 ?  55  THR A N    1 
ATOM   425  C  CA   . THR A 1 55  ? -20.763 9.077   5.655   1.00 15.61 ?  55  THR A CA   1 
ATOM   426  C  C    . THR A 1 55  ? -19.455 8.375   5.343   1.00 13.83 ?  55  THR A C    1 
ATOM   427  O  O    . THR A 1 55  ? -18.410 8.940   5.643   1.00 14.72 ?  55  THR A O    1 
ATOM   428  C  CB   . THR A 1 55  ? -20.661 10.601  5.278   1.00 16.44 ?  55  THR A CB   1 
ATOM   429  O  OG1  . THR A 1 55  ? -21.973 11.116  5.438   1.00 20.98 ?  55  THR A OG1  1 
ATOM   430  C  CG2  . THR A 1 55  ? -20.166 10.695  3.790   1.00 20.42 ?  55  THR A CG2  1 
ATOM   431  N  N    . SER A 1 56  ? -19.468 7.120   4.824   1.00 14.28 ?  56  SER A N    1 
ATOM   432  C  CA   . SER A 1 56  ? -18.214 6.511   4.514   1.00 14.57 ?  56  SER A CA   1 
ATOM   433  C  C    . SER A 1 56  ? -17.708 7.192   3.230   1.00 15.63 ?  56  SER A C    1 
ATOM   434  O  O    . SER A 1 56  ? -18.523 7.689   2.388   1.00 16.96 ?  56  SER A O    1 
ATOM   435  C  CB   . SER A 1 56  ? -18.305 4.941   4.316   1.00 14.90 ?  56  SER A CB   1 
ATOM   436  O  OG   . SER A 1 56  ? -19.139 4.638   3.160   1.00 16.38 ?  56  SER A OG   1 
ATOM   437  N  N    . LEU A 1 57  ? -16.394 7.226   3.047   1.00 16.30 ?  57  LEU A N    1 
ATOM   438  C  CA   . LEU A 1 57  ? -15.882 7.892   1.822   1.00 18.89 ?  57  LEU A CA   1 
ATOM   439  C  C    . LEU A 1 57  ? -15.016 6.972   0.929   1.00 16.53 ?  57  LEU A C    1 
ATOM   440  O  O    . LEU A 1 57  ? -15.052 7.007   -0.323  1.00 17.37 ?  57  LEU A O    1 
ATOM   441  C  CB   . LEU A 1 57  ? -15.039 9.102   2.246   1.00 18.65 ?  57  LEU A CB   1 
ATOM   442  C  CG   . LEU A 1 57  ? -15.898 10.206  2.882   1.00 21.70 ?  57  LEU A CG   1 
ATOM   443  C  CD1  . LEU A 1 57  ? -14.977 11.327  3.300   1.00 24.35 ?  57  LEU A CD1  1 
ATOM   444  C  CD2  . LEU A 1 57  ? -17.035 10.741  1.905   1.00 22.84 ?  57  LEU A CD2  1 
ATOM   445  N  N    . ARG A 1 58  ? -14.140 6.198   1.578   1.00 15.72 ?  58  ARG A N    1 
ATOM   446  C  CA   . ARG A 1 58  ? -13.060 5.559   0.866   1.00 15.61 ?  58  ARG A CA   1 
ATOM   447  C  C    . ARG A 1 58  ? -12.591 4.351   1.655   1.00 14.30 ?  58  ARG A C    1 
ATOM   448  O  O    . ARG A 1 58  ? -12.756 4.302   2.865   1.00 14.49 ?  58  ARG A O    1 
ATOM   449  C  CB   . ARG A 1 58  ? -11.893 6.551   0.723   1.00 17.80 ?  58  ARG A CB   1 
ATOM   450  C  CG   . ARG A 1 58  ? -10.957 6.265   -0.324  1.00 19.65 ?  58  ARG A CG   1 
ATOM   451  C  CD   . ARG A 1 58  ? -10.043 7.449   -0.471  1.00 23.67 ?  58  ARG A CD   1 
ATOM   452  N  NE   . ARG A 1 58  ? -9.215  7.438   0.733   1.00 20.44 ?  58  ARG A NE   1 
ATOM   453  C  CZ   . ARG A 1 58  ? -7.882  7.546   0.700   1.00 19.03 ?  58  ARG A CZ   1 
ATOM   454  N  NH1  . ARG A 1 58  ? -7.260  7.792   -0.466  1.00 20.41 ?  58  ARG A NH1  1 
ATOM   455  N  NH2  . ARG A 1 58  ? -7.206  7.510   1.852   1.00 20.42 ?  58  ARG A NH2  1 
ATOM   456  N  N    . ILE A 1 59  ? -11.983 3.419   0.930   1.00 13.10 ?  59  ILE A N    1 
ATOM   457  C  CA   . ILE A 1 59  ? -11.330 2.272   1.562   1.00 13.29 ?  59  ILE A CA   1 
ATOM   458  C  C    . ILE A 1 59  ? -9.884  2.272   1.055   1.00 12.45 ?  59  ILE A C    1 
ATOM   459  O  O    . ILE A 1 59  ? -9.630  2.465   -0.190  1.00 14.56 ?  59  ILE A O    1 
ATOM   460  C  CB   . ILE A 1 59  ? -12.034 0.912   1.252   1.00 12.61 ?  59  ILE A CB   1 
ATOM   461  C  CG1  . ILE A 1 59  ? -11.471 -0.211  2.153   1.00 13.78 ?  59  ILE A CG1  1 
ATOM   462  C  CG2  . ILE A 1 59  ? -11.988 0.501   -0.281  1.00 13.85 ?  59  ILE A CG2  1 
ATOM   463  C  CD1  . ILE A 1 59  ? -12.370 -1.494  2.064   1.00 15.46 ?  59  ILE A CD1  1 
ATOM   464  N  N    . LEU A 1 60  ? -8.931  2.030   1.994   1.00 13.22 ?  60  LEU A N    1 
ATOM   465  C  CA   . LEU A 1 60  ? -7.509  2.191   1.707   1.00 14.61 ?  60  LEU A CA   1 
ATOM   466  C  C    . LEU A 1 60  ? -6.720  0.969   2.252   1.00 13.58 ?  60  LEU A C    1 
ATOM   467  O  O    . LEU A 1 60  ? -6.930  0.643   3.421   1.00 13.11 ?  60  LEU A O    1 
ATOM   468  C  CB   . LEU A 1 60  ? -7.008  3.514   2.472   1.00 15.46 ?  60  LEU A CB   1 
ATOM   469  C  CG   . LEU A 1 60  ? -5.508  3.716   2.403   1.00 17.32 ?  60  LEU A CG   1 
ATOM   470  C  CD1  . LEU A 1 60  ? -4.986  3.915   0.965   1.00 20.62 ?  60  LEU A CD1  1 
ATOM   471  C  CD2  . LEU A 1 60  ? -5.010  4.859   3.317   1.00 16.89 ?  60  LEU A CD2  1 
ATOM   472  N  N    . ASN A 1 61  ? -5.814  0.388   1.442   1.00 13.11 ?  61  ASN A N    1 
ATOM   473  C  CA   . ASN A 1 61  ? -4.791  -0.569  1.869   1.00 13.15 ?  61  ASN A CA   1 
ATOM   474  C  C    . ASN A 1 61  ? -3.561  0.261   2.286   1.00 14.46 ?  61  ASN A C    1 
ATOM   475  O  O    . ASN A 1 61  ? -2.896  0.867   1.451   1.00 16.95 ?  61  ASN A O    1 
ATOM   476  C  CB   . ASN A 1 61  ? -4.454  -1.606  0.782   1.00 13.56 ?  61  ASN A CB   1 
ATOM   477  C  CG   . ASN A 1 61  ? -3.368  -2.577  1.231   1.00 14.85 ?  61  ASN A CG   1 
ATOM   478  O  OD1  . ASN A 1 61  ? -2.557  -2.283  2.158   1.00 16.19 ?  61  ASN A OD1  1 
ATOM   479  N  ND2  . ASN A 1 61  ? -3.382  -3.776  0.663   1.00 16.54 ?  61  ASN A ND2  1 
ATOM   480  N  N    . ASN A 1 62  ? -3.304  0.336   3.601   1.00 14.84 ?  62  ASN A N    1 
ATOM   481  C  CA   . ASN A 1 62  ? -2.219  1.218   4.048   1.00 15.53 ?  62  ASN A CA   1 
ATOM   482  C  C    . ASN A 1 62  ? -0.909  0.456   4.292   1.00 16.33 ?  62  ASN A C    1 
ATOM   483  O  O    . ASN A 1 62  ? 0.092   1.010   4.856   1.00 19.98 ?  62  ASN A O    1 
ATOM   484  C  CB   . ASN A 1 62  ? -2.610  2.022   5.326   1.00 17.54 ?  62  ASN A CB   1 
ATOM   485  C  CG   . ASN A 1 62  ? -2.935  1.103   6.503   1.00 17.66 ?  62  ASN A CG   1 
ATOM   486  O  OD1  . ASN A 1 62  ? -2.483  -0.032  6.534   1.00 14.94 ?  62  ASN A OD1  1 
ATOM   487  N  ND2  . ASN A 1 62  ? -3.778  1.571   7.424   1.00 22.93 ?  62  ASN A ND2  1 
ATOM   488  N  N    . GLY A 1 63  ? -0.872  -0.816  3.886   1.00 15.41 ?  63  GLY A N    1 
ATOM   489  C  CA   . GLY A 1 63  ? 0.279   -1.632  4.074   1.00 14.77 ?  63  GLY A CA   1 
ATOM   490  C  C    . GLY A 1 63  ? 0.336   -2.409  5.398   1.00 14.10 ?  63  GLY A C    1 
ATOM   491  O  O    . GLY A 1 63  ? 1.211   -3.253  5.552   1.00 14.63 ?  63  GLY A O    1 
ATOM   492  N  N    . HIS A 1 64  ? -0.585  -2.114  6.329   1.00 12.63 ?  64  HIS A N    1 
ATOM   493  C  CA   A HIS A 1 64  ? -0.680  -2.803  7.633   0.50 13.88 ?  64  HIS A CA   1 
ATOM   494  C  CA   B HIS A 1 64  ? -0.676  -2.932  7.575   0.50 14.35 ?  64  HIS A CA   1 
ATOM   495  C  C    . HIS A 1 64  ? -2.060  -3.431  7.848   1.00 13.42 ?  64  HIS A C    1 
ATOM   496  O  O    . HIS A 1 64  ? -2.168  -4.455  8.541   1.00 18.01 ?  64  HIS A O    1 
ATOM   497  C  CB   A HIS A 1 64  ? -0.349  -1.824  8.758   0.50 13.57 ?  64  HIS A CB   1 
ATOM   498  C  CB   B HIS A 1 64  ? -0.066  -2.328  8.859   0.50 14.86 ?  64  HIS A CB   1 
ATOM   499  C  CG   A HIS A 1 64  ? 0.986   -1.169  8.580   0.50 13.77 ?  64  HIS A CG   1 
ATOM   500  C  CG   B HIS A 1 64  ? -0.563  -0.969  9.217   0.50 15.90 ?  64  HIS A CG   1 
ATOM   501  N  ND1  A HIS A 1 64  ? 2.175   -1.840  8.783   0.50 15.25 ?  64  HIS A ND1  1 
ATOM   502  N  ND1  B HIS A 1 64  ? 0.029   0.192   8.749   0.50 16.96 ?  64  HIS A ND1  1 
ATOM   503  C  CD2  A HIS A 1 64  ? 1.321   0.094   8.223   0.50 15.71 ?  64  HIS A CD2  1 
ATOM   504  C  CD2  B HIS A 1 64  ? -1.514  -0.581  10.104  0.50 20.60 ?  64  HIS A CD2  1 
ATOM   505  C  CE1  A HIS A 1 64  ? 3.189   -1.013  8.594   0.50 14.19 ?  64  HIS A CE1  1 
ATOM   506  C  CE1  B HIS A 1 64  ? -0.586  1.229   9.303   0.50 21.02 ?  64  HIS A CE1  1 
ATOM   507  N  NE2  A HIS A 1 64  ? 2.694   0.154   8.229   0.50 14.04 ?  64  HIS A NE2  1 
ATOM   508  N  NE2  B HIS A 1 64  ? -1.540  0.788   10.106  0.50 20.75 ?  64  HIS A NE2  1 
ATOM   509  N  N    . ALA A 1 65  ? -3.091  -2.813  7.254   1.00 12.02 ?  65  ALA A N    1 
ATOM   510  C  CA   . ALA A 1 65  ? -4.467  -3.276  7.311   1.00 11.70 ?  65  ALA A CA   1 
ATOM   511  C  C    . ALA A 1 65  ? -5.206  -2.531  6.179   1.00 11.33 ?  65  ALA A C    1 
ATOM   512  O  O    . ALA A 1 65  ? -4.548  -1.872  5.309   1.00 12.45 ?  65  ALA A O    1 
ATOM   513  C  CB   . ALA A 1 65  ? -5.110  -2.979  8.713   1.00 11.37 ?  65  ALA A CB   1 
ATOM   514  N  N    . PHE A 1 66  ? -6.523  -2.677  6.146   1.00 11.79 ?  66  PHE A N    1 
ATOM   515  C  CA   . PHE A 1 66  ? -7.305  -1.723  5.299   1.00 12.90 ?  66  PHE A CA   1 
ATOM   516  C  C    . PHE A 1 66  ? -8.181  -0.876  6.197   1.00 11.95 ?  66  PHE A C    1 
ATOM   517  O  O    . PHE A 1 66  ? -8.764  -1.365  7.202   1.00 12.13 ?  66  PHE A O    1 
ATOM   518  C  CB   . PHE A 1 66  ? -8.125  -2.446  4.137   1.00 11.85 ?  66  PHE A CB   1 
ATOM   519  C  CG   . PHE A 1 66  ? -9.164  -3.409  4.687   1.00 12.70 ?  66  PHE A CG   1 
ATOM   520  C  CD1  . PHE A 1 66  ? -10.462 -2.935  5.030   1.00 14.13 ?  66  PHE A CD1  1 
ATOM   521  C  CD2  . PHE A 1 66  ? -8.852  -4.805  4.855   1.00 12.46 ?  66  PHE A CD2  1 
ATOM   522  C  CE1  . PHE A 1 66  ? -11.410 -3.774  5.518   1.00 14.45 ?  66  PHE A CE1  1 
ATOM   523  C  CE2  . PHE A 1 66  ? -9.833  -5.650  5.388   1.00 13.43 ?  66  PHE A CE2  1 
ATOM   524  C  CZ   . PHE A 1 66  ? -11.109 -5.159  5.708   1.00 13.63 ?  66  PHE A CZ   1 
ATOM   525  N  N    . ASN A 1 67  ? -8.288  0.413   5.846   1.00 12.62 ?  67  ASN A N    1 
ATOM   526  C  CA   . ASN A 1 67  ? -9.162  1.357   6.565   1.00 12.32 ?  67  ASN A CA   1 
ATOM   527  C  C    . ASN A 1 67  ? -10.360 1.755   5.753   1.00 12.95 ?  67  ASN A C    1 
ATOM   528  O  O    . ASN A 1 67  ? -10.192 2.163   4.603   1.00 14.46 ?  67  ASN A O    1 
ATOM   529  C  CB   . ASN A 1 67  ? -8.402  2.649   6.908   1.00 11.77 ?  67  ASN A CB   1 
ATOM   530  C  CG   . ASN A 1 67  ? -7.302  2.459   7.898   1.00 16.72 ?  67  ASN A CG   1 
ATOM   531  O  OD1  . ASN A 1 67  ? -7.167  1.405   8.560   1.00 16.23 ?  67  ASN A OD1  1 
ATOM   532  N  ND2  . ASN A 1 67  ? -6.451  3.527   8.045   1.00 21.25 ?  67  ASN A ND2  1 
ATOM   533  N  N    . VAL A 1 68  ? -11.519 1.700   6.368   1.00 11.73 ?  68  VAL A N    1 
ATOM   534  C  CA   . VAL A 1 68  ? -12.710 2.320   5.773   1.00 10.30 ?  68  VAL A CA   1 
ATOM   535  C  C    . VAL A 1 68  ? -12.849 3.693   6.475   1.00 13.31 ?  68  VAL A C    1 
ATOM   536  O  O    . VAL A 1 68  ? -13.034 3.752   7.726   1.00 11.80 ?  68  VAL A O    1 
ATOM   537  C  CB   . VAL A 1 68  ? -13.976 1.453   5.954   1.00 12.81 ?  68  VAL A CB   1 
ATOM   538  C  CG1  . VAL A 1 68  ? -15.295 2.238   5.491   1.00 13.95 ?  68  VAL A CG1  1 
ATOM   539  C  CG2  . VAL A 1 68  ? -13.837 0.182   5.205   1.00 11.71 ?  68  VAL A CG2  1 
ATOM   540  N  N    . GLU A 1 69  ? -12.788 4.773   5.691   1.00 12.80 ?  69  GLU A N    1 
ATOM   541  C  CA   . GLU A 1 69  ? -12.686 6.128   6.236   1.00 13.90 ?  69  GLU A CA   1 
ATOM   542  C  C    . GLU A 1 69  ? -14.019 6.800   6.109   1.00 14.96 ?  69  GLU A C    1 
ATOM   543  O  O    . GLU A 1 69  ? -14.723 6.559   5.114   1.00 16.52 ?  69  GLU A O    1 
ATOM   544  C  CB   . GLU A 1 69  ? -11.776 6.936   5.388   1.00 16.03 ?  69  GLU A CB   1 
ATOM   545  C  CG   . GLU A 1 69  ? -10.401 6.405   5.420   1.00 17.82 ?  69  GLU A CG   1 
ATOM   546  C  CD   . GLU A 1 69  ? -9.620  6.853   4.244   1.00 22.68 ?  69  GLU A CD   1 
ATOM   547  O  OE1  . GLU A 1 69  ? -10.238 7.557   3.343   1.00 22.98 ?  69  GLU A OE1  1 
ATOM   548  O  OE2  . GLU A 1 69  ? -8.416  6.471   4.220   1.00 22.69 ?  69  GLU A OE2  1 
ATOM   549  N  N    . PHE A 1 70  ? -14.289 7.701   7.055   1.00 12.18 ?  70  PHE A N    1 
ATOM   550  C  CA   . PHE A 1 70  ? -15.553 8.403   7.176   1.00 12.23 ?  70  PHE A CA   1 
ATOM   551  C  C    . PHE A 1 70  ? -15.332 9.912   7.130   1.00 12.79 ?  70  PHE A C    1 
ATOM   552  O  O    . PHE A 1 70  ? -14.245 10.408  7.531   1.00 13.61 ?  70  PHE A O    1 
ATOM   553  C  CB   . PHE A 1 70  ? -16.224 8.017   8.483   1.00 10.98 ?  70  PHE A CB   1 
ATOM   554  C  CG   . PHE A 1 70  ? -16.821 6.610   8.422   1.00 10.91 ?  70  PHE A CG   1 
ATOM   555  C  CD1  . PHE A 1 70  ? -15.995 5.509   8.635   1.00 12.32 ?  70  PHE A CD1  1 
ATOM   556  C  CD2  . PHE A 1 70  ? -18.161 6.402   8.116   1.00 12.93 ?  70  PHE A CD2  1 
ATOM   557  C  CE1  . PHE A 1 70  ? -16.482 4.192   8.471   1.00 13.43 ?  70  PHE A CE1  1 
ATOM   558  C  CE2  . PHE A 1 70  ? -18.689 5.115   7.964   1.00 12.41 ?  70  PHE A CE2  1 
ATOM   559  C  CZ   . PHE A 1 70  ? -17.850 4.010   8.154   1.00 14.80 ?  70  PHE A CZ   1 
ATOM   560  N  N    . ASP A 1 71  ? -16.379 10.657  6.725   1.00 13.53 ?  71  ASP A N    1 
ATOM   561  C  CA   . ASP A 1 71  ? -16.296 12.130  6.871   1.00 13.95 ?  71  ASP A CA   1 
ATOM   562  C  C    . ASP A 1 71  ? -16.526 12.438  8.352   1.00 13.10 ?  71  ASP A C    1 
ATOM   563  O  O    . ASP A 1 71  ? -17.640 12.179  8.940   1.00 17.52 ?  71  ASP A O    1 
ATOM   564  C  CB   . ASP A 1 71  ? -17.457 12.723  6.067   1.00 16.06 ?  71  ASP A CB   1 
ATOM   565  C  CG   . ASP A 1 71  ? -17.666 14.237  6.358   1.00 15.39 ?  71  ASP A CG   1 
ATOM   566  O  OD1  . ASP A 1 71  ? -16.723 14.874  6.912   1.00 16.68 ?  71  ASP A OD1  1 
ATOM   567  O  OD2  . ASP A 1 71  ? -18.760 14.791  6.009   1.00 23.08 ?  71  ASP A OD2  1 
ATOM   568  N  N    . ASP A 1 72  ? -15.525 13.012  8.999   1.00 12.58 ?  72  ASP A N    1 
ATOM   569  C  CA   . ASP A 1 72  ? -15.577 13.343  10.457  1.00 11.86 ?  72  ASP A CA   1 
ATOM   570  C  C    . ASP A 1 72  ? -15.507 14.850  10.614  1.00 15.09 ?  72  ASP A C    1 
ATOM   571  O  O    . ASP A 1 72  ? -14.974 15.327  11.608  1.00 15.69 ?  72  ASP A O    1 
ATOM   572  C  CB   . ASP A 1 72  ? -14.379 12.679  11.205  1.00 13.50 ?  72  ASP A CB   1 
ATOM   573  C  CG   . ASP A 1 72  ? -12.992 13.177  10.703  1.00 14.46 ?  72  ASP A CG   1 
ATOM   574  O  OD1  . ASP A 1 72  ? -12.872 13.905  9.641   1.00 17.10 ?  72  ASP A OD1  1 
ATOM   575  O  OD2  . ASP A 1 72  ? -11.968 12.909  11.384  1.00 15.47 ?  72  ASP A OD2  1 
ATOM   576  N  N    . SER A 1 73  ? -16.054 15.582  9.640   1.00 15.40 ?  73  SER A N    1 
ATOM   577  C  CA   . SER A 1 73  ? -15.981 17.071  9.680   1.00 16.74 ?  73  SER A CA   1 
ATOM   578  C  C    . SER A 1 73  ? -17.287 17.628  10.265  1.00 17.13 ?  73  SER A C    1 
ATOM   579  O  O    . SER A 1 73  ? -17.406 18.885  10.367  1.00 17.04 ?  73  SER A O    1 
ATOM   580  C  CB   . SER A 1 73  ? -15.692 17.660  8.277   1.00 19.22 ?  73  SER A CB   1 
ATOM   581  O  OG   . SER A 1 73  ? -16.821 17.405  7.430   1.00 17.45 ?  73  SER A OG   1 
ATOM   582  N  N    . GLN A 1 74  ? -18.237 16.737  10.668  1.00 17.64 ?  74  GLN A N    1 
ATOM   583  C  CA   . GLN A 1 74  ? -19.415 17.119  11.454  1.00 19.40 ?  74  GLN A CA   1 
ATOM   584  C  C    . GLN A 1 74  ? -19.769 15.945  12.354  1.00 19.70 ?  74  GLN A C    1 
ATOM   585  O  O    . GLN A 1 74  ? -19.257 14.863  12.105  1.00 19.08 ?  74  GLN A O    1 
ATOM   586  C  CB   . GLN A 1 74  ? -20.676 17.324  10.548  1.00 20.83 ?  74  GLN A CB   1 
ATOM   587  C  CG   . GLN A 1 74  ? -20.560 18.444  9.605   1.00 23.30 ?  74  GLN A CG   1 
ATOM   588  C  CD   . GLN A 1 74  ? -21.850 18.561  8.788   1.00 25.03 ?  74  GLN A CD   1 
ATOM   589  O  OE1  . GLN A 1 74  ? -22.850 19.101  9.278   1.00 30.73 ?  74  GLN A OE1  1 
ATOM   590  N  NE2  . GLN A 1 74  ? -21.821 18.086  7.568   1.00 25.03 ?  74  GLN A NE2  1 
ATOM   591  N  N    . ASP A 1 75  ? -20.698 16.154  13.308  1.00 21.63 ?  75  ASP A N    1 
ATOM   592  C  CA   . ASP A 1 75  ? -21.126 15.089  14.231  1.00 24.02 ?  75  ASP A CA   1 
ATOM   593  C  C    . ASP A 1 75  ? -22.119 14.281  13.428  1.00 24.30 ?  75  ASP A C    1 
ATOM   594  O  O    . ASP A 1 75  ? -23.270 14.723  13.305  1.00 29.18 ?  75  ASP A O    1 
ATOM   595  C  CB   . ASP A 1 75  ? -21.801 15.579  15.534  1.00 26.20 ?  75  ASP A CB   1 
ATOM   596  C  CG   . ASP A 1 75  ? -20.785 16.111  16.538  1.00 28.80 ?  75  ASP A CG   1 
ATOM   597  O  OD1  . ASP A 1 75  ? -19.567 15.891  16.349  1.00 31.46 ?  75  ASP A OD1  1 
ATOM   598  O  OD2  . ASP A 1 75  ? -21.205 16.759  17.541  1.00 37.69 ?  75  ASP A OD2  1 
ATOM   599  N  N    . LYS A 1 76  ? -21.653 13.226  12.808  1.00 21.12 ?  76  LYS A N    1 
ATOM   600  C  CA   . LYS A 1 76  ? -22.497 12.364  11.989  1.00 21.25 ?  76  LYS A CA   1 
ATOM   601  C  C    . LYS A 1 76  ? -22.545 10.884  12.442  1.00 21.81 ?  76  LYS A C    1 
ATOM   602  O  O    . LYS A 1 76  ? -23.542 10.111  12.180  1.00 25.04 ?  76  LYS A O    1 
ATOM   603  C  CB   . LYS A 1 76  ? -21.912 12.321  10.579  1.00 19.29 ?  76  LYS A CB   1 
ATOM   604  C  CG   . LYS A 1 76  ? -22.170 13.562  9.701   1.00 21.67 ?  76  LYS A CG   1 
ATOM   605  C  CD   . LYS A 1 76  ? -21.488 13.328  8.340   1.00 22.28 ?  76  LYS A CD   1 
ATOM   606  C  CE   . LYS A 1 76  ? -22.026 14.277  7.289   1.00 22.99 ?  76  LYS A CE   1 
ATOM   607  N  NZ   . LYS A 1 76  ? -21.542 13.995  5.961   1.00 23.45 ?  76  LYS A NZ   1 
ATOM   608  N  N    . ALA A 1 77  ? -21.423 10.405  12.886  1.00 19.67 ?  77  ALA A N    1 
ATOM   609  C  CA   . ALA A 1 77  ? -21.350 9.005   13.404  1.00 17.07 ?  77  ALA A CA   1 
ATOM   610  C  C    . ALA A 1 77  ? -20.549 9.198   14.694  1.00 15.69 ?  77  ALA A C    1 
ATOM   611  O  O    . ALA A 1 77  ? -19.309 9.444   14.646  1.00 17.74 ?  77  ALA A O    1 
ATOM   612  C  CB   . ALA A 1 77  ? -20.533 8.203   12.450  1.00 18.12 ?  77  ALA A CB   1 
ATOM   613  N  N    . VAL A 1 78  ? -21.208 9.107   15.829  1.00 14.87 ?  78  VAL A N    1 
ATOM   614  C  CA   . VAL A 1 78  ? -20.570 9.426   17.128  1.00 15.04 ?  78  VAL A CA   1 
ATOM   615  C  C    . VAL A 1 78  ? -20.814 8.351   18.181  1.00 15.65 ?  78  VAL A C    1 
ATOM   616  O  O    . VAL A 1 78  ? -21.859 7.654   18.198  1.00 16.17 ?  78  VAL A O    1 
ATOM   617  C  CB   . VAL A 1 78  ? -20.948 10.784  17.731  1.00 17.48 ?  78  VAL A CB   1 
ATOM   618  C  CG1  . VAL A 1 78  ? -20.775 11.938  16.671  1.00 18.03 ?  78  VAL A CG1  1 
ATOM   619  C  CG2  . VAL A 1 78  ? -22.358 10.725  18.159  1.00 20.29 ?  78  VAL A CG2  1 
ATOM   620  N  N    . LEU A 1 79  ? -19.807 8.232   19.042  1.00 12.61 ?  79  LEU A N    1 
ATOM   621  C  CA   . LEU A 1 79  ? -19.853 7.395   20.195  1.00 13.50 ?  79  LEU A CA   1 
ATOM   622  C  C    . LEU A 1 79  ? -19.874 8.310   21.420  1.00 12.92 ?  79  LEU A C    1 
ATOM   623  O  O    . LEU A 1 79  ? -19.105 9.263   21.513  1.00 14.15 ?  79  LEU A O    1 
ATOM   624  C  CB   . LEU A 1 79  ? -18.584 6.460   20.172  1.00 13.24 ?  79  LEU A CB   1 
ATOM   625  C  CG   . LEU A 1 79  ? -18.449 5.420   21.224  1.00 13.94 ?  79  LEU A CG   1 
ATOM   626  C  CD1  . LEU A 1 79  ? -19.604 4.389   21.062  1.00 17.36 ?  79  LEU A CD1  1 
ATOM   627  C  CD2  . LEU A 1 79  ? -17.064 4.799   21.164  1.00 14.23 ?  79  LEU A CD2  1 
ATOM   628  N  N    A LYS A 1 80  ? -20.707 7.977   22.394  0.50 13.16 ?  80  LYS A N    1 
ATOM   629  N  N    B LYS A 1 80  ? -20.760 7.954   22.354  0.50 13.14 ?  80  LYS A N    1 
ATOM   630  C  CA   A LYS A 1 80  ? -20.677 8.689   23.685  0.50 13.88 ?  80  LYS A CA   1 
ATOM   631  C  CA   B LYS A 1 80  ? -21.000 8.701   23.603  0.50 14.29 ?  80  LYS A CA   1 
ATOM   632  C  C    A LYS A 1 80  ? -21.388 7.797   24.709  0.50 13.44 ?  80  LYS A C    1 
ATOM   633  C  C    B LYS A 1 80  ? -21.350 7.731   24.731  0.50 13.99 ?  80  LYS A C    1 
ATOM   634  O  O    A LYS A 1 80  ? -21.787 6.656   24.389  0.50 12.84 ?  80  LYS A O    1 
ATOM   635  O  O    B LYS A 1 80  ? -21.492 6.494   24.507  0.50 13.91 ?  80  LYS A O    1 
ATOM   636  C  CB   A LYS A 1 80  ? -21.328 10.085  23.572  0.50 14.61 ?  80  LYS A CB   1 
ATOM   637  C  CB   B LYS A 1 80  ? -22.212 9.627   23.448  0.50 14.77 ?  80  LYS A CB   1 
ATOM   638  C  CG   A LYS A 1 80  ? -22.839 10.026  23.181  0.50 16.59 ?  80  LYS A CG   1 
ATOM   639  C  CG   B LYS A 1 80  ? -22.134 10.633  22.298  0.50 15.67 ?  80  LYS A CG   1 
ATOM   640  C  CD   A LYS A 1 80  ? -23.522 11.439  23.212  0.50 17.06 ?  80  LYS A CD   1 
ATOM   641  C  CD   B LYS A 1 80  ? -23.427 11.465  22.235  0.50 17.05 ?  80  LYS A CD   1 
ATOM   642  C  CE   A LYS A 1 80  ? -23.618 12.053  24.591  0.50 21.38 ?  80  LYS A CE   1 
ATOM   643  C  CE   B LYS A 1 80  ? -23.318 12.603  21.244  0.50 22.78 ?  80  LYS A CE   1 
ATOM   644  N  NZ   A LYS A 1 80  ? -23.571 11.183  25.841  0.50 26.65 ?  80  LYS A NZ   1 
ATOM   645  N  NZ   B LYS A 1 80  ? -24.607 13.220  20.824  0.50 24.53 ?  80  LYS A NZ   1 
ATOM   646  N  N    . GLY A 1 81  ? -21.478 8.277   25.946  1.00 14.23 ?  81  GLY A N    1 
ATOM   647  C  CA   . GLY A 1 81  ? -21.977 7.473   27.048  1.00 15.19 ?  81  GLY A CA   1 
ATOM   648  C  C    . GLY A 1 81  ? -20.973 6.388   27.376  1.00 14.78 ?  81  GLY A C    1 
ATOM   649  O  O    . GLY A 1 81  ? -19.728 6.571   27.187  1.00 14.51 ?  81  GLY A O    1 
ATOM   650  N  N    . GLY A 1 82  ? -21.478 5.265   27.873  1.00 16.57 ?  82  GLY A N    1 
ATOM   651  C  CA   . GLY A 1 82  ? -20.567 4.228   28.296  1.00 17.46 ?  82  GLY A CA   1 
ATOM   652  C  C    . GLY A 1 82  ? -19.651 4.819   29.406  1.00 16.19 ?  82  GLY A C    1 
ATOM   653  O  O    . GLY A 1 82  ? -20.099 5.617   30.283  1.00 21.48 ?  82  GLY A O    1 
ATOM   654  N  N    . PRO A 1 83  ? -18.311 4.593   29.311  1.00 17.17 ?  83  PRO A N    1 
ATOM   655  C  CA   . PRO A 1 83  ? -17.385 5.263   30.287  1.00 15.04 ?  83  PRO A CA   1 
ATOM   656  C  C    . PRO A 1 83  ? -16.953 6.681   29.901  1.00 17.91 ?  83  PRO A C    1 
ATOM   657  O  O    . PRO A 1 83  ? -16.065 7.281   30.590  1.00 18.93 ?  83  PRO A O    1 
ATOM   658  C  CB   . PRO A 1 83  ? -16.099 4.414   30.184  1.00 16.23 ?  83  PRO A CB   1 
ATOM   659  C  CG   . PRO A 1 83  ? -16.132 3.974   28.680  1.00 13.89 ?  83  PRO A CG   1 
ATOM   660  C  CD   . PRO A 1 83  ? -17.580 3.764   28.309  1.00 14.13 ?  83  PRO A CD   1 
ATOM   661  N  N    . LEU A 1 84  ? -17.503 7.167   28.791  1.00 16.27 ?  84  LEU A N    1 
ATOM   662  C  CA   . LEU A 1 84  ? -16.950 8.385   28.193  1.00 15.87 ?  84  LEU A CA   1 
ATOM   663  C  C    . LEU A 1 84  ? -17.599 9.633   28.708  1.00 19.23 ?  84  LEU A C    1 
ATOM   664  O  O    . LEU A 1 84  ? -18.790 9.638   29.004  1.00 19.53 ?  84  LEU A O    1 
ATOM   665  C  CB   . LEU A 1 84  ? -17.121 8.389   26.666  1.00 13.22 ?  84  LEU A CB   1 
ATOM   666  C  CG   . LEU A 1 84  ? -16.519 7.092   26.030  1.00 11.84 ?  84  LEU A CG   1 
ATOM   667  C  CD1  . LEU A 1 84  ? -16.986 7.026   24.506  1.00 13.77 ?  84  LEU A CD1  1 
ATOM   668  C  CD2  . LEU A 1 84  ? -14.954 7.089   26.068  1.00 12.64 ?  84  LEU A CD2  1 
ATOM   669  N  N    . ASP A 1 85  ? -16.789 10.693  28.755  1.00 21.67 ?  85  ASP A N    1 
ATOM   670  C  CA   . ASP A 1 85  ? -17.345 12.002  29.109  1.00 26.07 ?  85  ASP A CA   1 
ATOM   671  C  C    . ASP A 1 85  ? -17.723 12.833  27.931  1.00 26.29 ?  85  ASP A C    1 
ATOM   672  O  O    . ASP A 1 85  ? -18.597 13.712  28.023  1.00 32.44 ?  85  ASP A O    1 
ATOM   673  C  CB   . ASP A 1 85  ? -16.408 12.773  30.017  1.00 26.84 ?  85  ASP A CB   1 
ATOM   674  C  CG   . ASP A 1 85  ? -16.552 12.358  31.436  1.00 34.03 ?  85  ASP A CG   1 
ATOM   675  O  OD1  . ASP A 1 85  ? -17.706 11.937  31.844  1.00 37.28 ?  85  ASP A OD1  1 
ATOM   676  O  OD2  . ASP A 1 85  ? -15.493 12.458  32.140  1.00 38.97 ?  85  ASP A OD2  1 
ATOM   677  N  N    . GLY A 1 86  ? -17.085 12.774  26.807  1.00 23.58 ?  86  GLY A N    1 
ATOM   678  C  CA   . GLY A 1 86  ? -17.794 13.715  25.896  1.00 25.06 ?  86  GLY A CA   1 
ATOM   679  C  C    . GLY A 1 86  ? -18.292 12.951  24.669  1.00 22.90 ?  86  GLY A C    1 
ATOM   680  O  O    . GLY A 1 86  ? -18.841 11.809  24.789  1.00 26.20 ?  86  GLY A O    1 
ATOM   681  N  N    . THR A 1 87  ? -18.082 13.561  23.503  1.00 18.86 ?  87  THR A N    1 
ATOM   682  C  CA   . THR A 1 87  ? -18.574 13.033  22.252  1.00 18.60 ?  87  THR A CA   1 
ATOM   683  C  C    . THR A 1 87  ? -17.386 12.735  21.381  1.00 14.30 ?  87  THR A C    1 
ATOM   684  O  O    . THR A 1 87  ? -16.443 13.514  21.297  1.00 13.75 ?  87  THR A O    1 
ATOM   685  C  CB   . THR A 1 87  ? -19.433 14.094  21.529  1.00 21.04 ?  87  THR A CB   1 
ATOM   686  O  OG1  . THR A 1 87  ? -20.609 14.328  22.310  1.00 26.47 ?  87  THR A OG1  1 
ATOM   687  C  CG2  . THR A 1 87  ? -19.866 13.655  20.049  1.00 20.34 ?  87  THR A CG2  1 
ATOM   688  N  N    . TYR A 1 88  ? -17.378 11.502  20.824  1.00 12.43 ?  88  TYR A N    1 
ATOM   689  C  CA   . TYR A 1 88  ? -16.258 11.066  19.994  1.00 11.39 ?  88  TYR A CA   1 
ATOM   690  C  C    . TYR A 1 88  ? -16.760 10.740  18.570  1.00 11.30 ?  88  TYR A C    1 
ATOM   691  O  O    . TYR A 1 88  ? -17.741 10.034  18.433  1.00 14.20 ?  88  TYR A O    1 
ATOM   692  C  CB   . TYR A 1 88  ? -15.632 9.833   20.550  1.00 12.01 ?  88  TYR A CB   1 
ATOM   693  C  CG   . TYR A 1 88  ? -14.885 10.025  21.900  1.00 8.98  ?  88  TYR A CG   1 
ATOM   694  C  CD1  . TYR A 1 88  ? -15.584 10.333  23.098  1.00 10.65 ?  88  TYR A CD1  1 
ATOM   695  C  CD2  . TYR A 1 88  ? -13.464 9.910   21.972  1.00 9.75  ?  88  TYR A CD2  1 
ATOM   696  C  CE1  . TYR A 1 88  ? -14.935 10.510  24.300  1.00 11.05 ?  88  TYR A CE1  1 
ATOM   697  C  CE2  . TYR A 1 88  ? -12.791 10.063  23.186  1.00 9.31  ?  88  TYR A CE2  1 
ATOM   698  C  CZ   . TYR A 1 88  ? -13.496 10.345  24.344  1.00 11.10 ?  88  TYR A CZ   1 
ATOM   699  O  OH   . TYR A 1 88  ? -12.809 10.467  25.522  1.00 11.09 ?  88  TYR A OH   1 
ATOM   700  N  N    . ARG A 1 89  ? -16.093 11.246  17.527  1.00 9.88  ?  89  ARG A N    1 
ATOM   701  C  CA   . ARG A 1 89  ? -16.527 11.100  16.142  1.00 11.11 ?  89  ARG A CA   1 
ATOM   702  C  C    . ARG A 1 89  ? -15.788 9.973   15.472  1.00 9.04  ?  89  ARG A C    1 
ATOM   703  O  O    . ARG A 1 89  ? -14.534 9.905   15.559  1.00 8.65  ?  89  ARG A O    1 
ATOM   704  C  CB   . ARG A 1 89  ? -16.103 12.382  15.341  1.00 13.17 ?  89  ARG A CB   1 
ATOM   705  C  CG   . ARG A 1 89  ? -17.009 13.422  15.438  1.00 19.10 ?  89  ARG A CG   1 
ATOM   706  C  CD   . ARG A 1 89  ? -16.742 14.489  14.368  1.00 21.31 ?  89  ARG A CD   1 
ATOM   707  N  NE   . ARG A 1 89  ? -17.431 15.620  14.856  1.00 21.86 ?  89  ARG A NE   1 
ATOM   708  C  CZ   . ARG A 1 89  ? -17.183 16.868  14.532  1.00 21.38 ?  89  ARG A CZ   1 
ATOM   709  N  NH1  . ARG A 1 89  ? -16.174 17.179  13.683  1.00 19.38 ?  89  ARG A NH1  1 
ATOM   710  N  NH2  . ARG A 1 89  ? -17.929 17.828  15.109  1.00 25.59 ?  89  ARG A NH2  1 
ATOM   711  N  N    . LEU A 1 90  ? -16.558 9.115   14.774  1.00 9.73  ?  90  LEU A N    1 
ATOM   712  C  CA   . LEU A 1 90  ? -15.951 8.045   14.001  1.00 10.32 ?  90  LEU A CA   1 
ATOM   713  C  C    . LEU A 1 90  ? -15.095 8.615   12.837  1.00 11.01 ?  90  LEU A C    1 
ATOM   714  O  O    . LEU A 1 90  ? -15.576 9.399   11.988  1.00 12.22 ?  90  LEU A O    1 
ATOM   715  C  CB   . LEU A 1 90  ? -17.061 7.173   13.388  1.00 10.16 ?  90  LEU A CB   1 
ATOM   716  C  CG   . LEU A 1 90  ? -16.594 6.003   12.549  1.00 9.45  ?  90  LEU A CG   1 
ATOM   717  C  CD1  . LEU A 1 90  ? -15.850 4.957   13.392  1.00 11.49 ?  90  LEU A CD1  1 
ATOM   718  C  CD2  . LEU A 1 90  ? -17.835 5.323   11.962  1.00 11.26 ?  90  LEU A CD2  1 
ATOM   719  N  N    . ILE A 1 91  ? -13.844 8.178   12.765  1.00 9.58  ?  91  ILE A N    1 
ATOM   720  C  CA   . ILE A 1 91  ? -12.925 8.585   11.658  1.00 9.85  ?  91  ILE A CA   1 
ATOM   721  C  C    . ILE A 1 91  ? -12.645 7.417   10.715  1.00 10.12 ?  91  ILE A C    1 
ATOM   722  O  O    . ILE A 1 91  ? -12.616 7.571   9.488   1.00 10.03 ?  91  ILE A O    1 
ATOM   723  C  CB   . ILE A 1 91  ? -11.573 9.246   12.148  1.00 10.53 ?  91  ILE A CB   1 
ATOM   724  C  CG1  . ILE A 1 91  ? -10.730 9.572   10.932  1.00 11.79 ?  91  ILE A CG1  1 
ATOM   725  C  CG2  . ILE A 1 91  ? -10.845 8.406   13.192  1.00 11.73 ?  91  ILE A CG2  1 
ATOM   726  C  CD1  . ILE A 1 91  ? -9.555  10.499  11.277  1.00 14.70 ?  91  ILE A CD1  1 
ATOM   727  N  N    . GLN A 1 92  ? -12.503 6.193   11.268  1.00 10.63 ?  92  GLN A N    1 
ATOM   728  C  CA   . GLN A 1 92  ? -12.226 5.051   10.380  1.00 10.11 ?  92  GLN A CA   1 
ATOM   729  C  C    . GLN A 1 92  ? -12.494 3.771   11.153  1.00 8.15  ?  92  GLN A C    1 
ATOM   730  O  O    . GLN A 1 92  ? -12.533 3.809   12.401  1.00 9.03  ?  92  GLN A O    1 
ATOM   731  C  CB   . GLN A 1 92  ? -10.791 5.024   9.854   1.00 11.68 ?  92  GLN A CB   1 
ATOM   732  C  CG   . GLN A 1 92  ? -9.678  5.139   10.987  1.00 12.23 ?  92  GLN A CG   1 
ATOM   733  C  CD   . GLN A 1 92  ? -8.936  3.851   11.170  1.00 10.62 ?  92  GLN A CD   1 
ATOM   734  O  OE1  . GLN A 1 92  ? -9.514  2.771   11.183  1.00 12.48 ?  92  GLN A OE1  1 
ATOM   735  N  NE2  . GLN A 1 92  ? -7.653  3.986   11.595  1.00 17.94 ?  92  GLN A NE2  1 
ATOM   736  N  N    . PHE A 1 93  ? -12.673 2.652   10.414  1.00 7.66  ?  93  PHE A N    1 
ATOM   737  C  CA   . PHE A 1 93  ? -12.515 1.368   11.055  1.00 7.30  ?  93  PHE A CA   1 
ATOM   738  C  C    . PHE A 1 93  ? -11.551 0.477   10.229  1.00 8.01  ?  93  PHE A C    1 
ATOM   739  O  O    . PHE A 1 93  ? -11.339 0.669   9.035   1.00 9.38  ?  93  PHE A O    1 
ATOM   740  C  CB   . PHE A 1 93  ? -13.898 0.691   11.355  1.00 7.91  ?  93  PHE A CB   1 
ATOM   741  C  CG   . PHE A 1 93  ? -14.643 0.227   10.103  1.00 9.97  ?  93  PHE A CG   1 
ATOM   742  C  CD1  . PHE A 1 93  ? -14.240 -0.939  9.424   1.00 9.52  ?  93  PHE A CD1  1 
ATOM   743  C  CD2  . PHE A 1 93  ? -15.775 0.935   9.679   1.00 10.47 ?  93  PHE A CD2  1 
ATOM   744  C  CE1  . PHE A 1 93  ? -14.953 -1.424  8.296   1.00 9.41  ?  93  PHE A CE1  1 
ATOM   745  C  CE2  . PHE A 1 93  ? -16.498 0.436   8.544   1.00 11.25 ?  93  PHE A CE2  1 
ATOM   746  C  CZ   . PHE A 1 93  ? -16.042 -0.717  7.831   1.00 11.30 ?  93  PHE A CZ   1 
ATOM   747  N  N    . HIS A 1 94  ? -11.057 -0.556  10.908  1.00 7.90  ?  94  HIS A N    1 
ATOM   748  C  CA   . HIS A 1 94  ? -10.147 -1.521  10.281  1.00 6.57  ?  94  HIS A CA   1 
ATOM   749  C  C    . HIS A 1 94  ? -10.208 -2.783  11.118  1.00 7.94  ?  94  HIS A C    1 
ATOM   750  O  O    . HIS A 1 94  ? -10.885 -2.801  12.184  1.00 8.43  ?  94  HIS A O    1 
ATOM   751  C  CB   . HIS A 1 94  ? -8.690  -0.993  10.219  1.00 7.26  ?  94  HIS A CB   1 
ATOM   752  C  CG   . HIS A 1 94  ? -8.157  -0.713  11.604  1.00 7.37  ?  94  HIS A CG   1 
ATOM   753  N  ND1  . HIS A 1 94  ? -8.353  0.509   12.241  1.00 7.56  ?  94  HIS A ND1  1 
ATOM   754  C  CD2  . HIS A 1 94  ? -7.531  -1.529  12.505  1.00 8.37  ?  94  HIS A CD2  1 
ATOM   755  C  CE1  . HIS A 1 94  ? -7.834  0.409   13.480  1.00 7.80  ?  94  HIS A CE1  1 
ATOM   756  N  NE2  . HIS A 1 94  ? -7.320  -0.810  13.650  1.00 8.46  ?  94  HIS A NE2  1 
ATOM   757  N  N    . PHE A 1 95  ? -9.526  -3.829  10.646  1.00 7.67  ?  95  PHE A N    1 
ATOM   758  C  CA   . PHE A 1 95  ? -9.508  -5.131  11.363  1.00 7.04  ?  95  PHE A CA   1 
ATOM   759  C  C    . PHE A 1 95  ? -8.037  -5.580  11.516  1.00 7.98  ?  95  PHE A C    1 
ATOM   760  O  O    . PHE A 1 95  ? -7.119  -5.073  10.829  1.00 8.35  ?  95  PHE A O    1 
ATOM   761  C  CB   . PHE A 1 95  ? -10.201 -6.206  10.484  1.00 8.26  ?  95  PHE A CB   1 
ATOM   762  C  CG   . PHE A 1 95  ? -11.660 -5.922  10.173  1.00 6.42  ?  95  PHE A CG   1 
ATOM   763  C  CD1  . PHE A 1 95  ? -11.991 -5.053  9.101   1.00 8.33  ?  95  PHE A CD1  1 
ATOM   764  C  CD2  . PHE A 1 95  ? -12.682 -6.570  10.873  1.00 9.00  ?  95  PHE A CD2  1 
ATOM   765  C  CE1  . PHE A 1 95  ? -13.322 -4.803  8.788   1.00 7.37  ?  95  PHE A CE1  1 
ATOM   766  C  CE2  . PHE A 1 95  ? -14.018 -6.345  10.570  1.00 8.14  ?  95  PHE A CE2  1 
ATOM   767  C  CZ   . PHE A 1 95  ? -14.352 -5.509  9.481   1.00 8.48  ?  95  PHE A CZ   1 
ATOM   768  N  N    . HIS A 1 96  ? -7.902  -6.525  12.445  1.00 7.75  ?  96  HIS A N    1 
ATOM   769  C  CA   . HIS A 1 96  ? -6.686  -7.309  12.593  1.00 7.31  ?  96  HIS A CA   1 
ATOM   770  C  C    . HIS A 1 96  ? -7.132  -8.769  12.458  1.00 7.06  ?  96  HIS A C    1 
ATOM   771  O  O    . HIS A 1 96  ? -8.177  -9.143  13.015  1.00 7.97  ?  96  HIS A O    1 
ATOM   772  C  CB   . HIS A 1 96  ? -6.002  -7.120  13.958  1.00 8.47  ?  96  HIS A CB   1 
ATOM   773  C  CG   . HIS A 1 96  ? -5.725  -5.675  14.279  1.00 8.63  ?  96  HIS A CG   1 
ATOM   774  N  ND1  . HIS A 1 96  ? -4.489  -5.095  14.061  1.00 9.04  ?  96  HIS A ND1  1 
ATOM   775  C  CD2  . HIS A 1 96  ? -6.565  -4.652  14.641  1.00 9.49  ?  96  HIS A CD2  1 
ATOM   776  C  CE1  . HIS A 1 96  ? -4.561  -3.796  14.362  1.00 8.41  ?  96  HIS A CE1  1 
ATOM   777  N  NE2  . HIS A 1 96  ? -5.809  -3.501  14.677  1.00 7.17  ?  96  HIS A NE2  1 
ATOM   778  N  N    . TRP A 1 97  ? -6.345  -9.593  11.762  1.00 7.67  ?  97  TRP A N    1 
ATOM   779  C  CA   . TRP A 1 97  ? -6.755  -10.992 11.552  1.00 7.07  ?  97  TRP A CA   1 
ATOM   780  C  C    . TRP A 1 97  ? -5.553  -11.938 11.451  1.00 7.57  ?  97  TRP A C    1 
ATOM   781  O  O    . TRP A 1 97  ? -4.346  -11.465 11.353  1.00 8.69  ?  97  TRP A O    1 
ATOM   782  C  CB   . TRP A 1 97  ? -7.670  -11.129 10.320  1.00 8.95  ?  97  TRP A CB   1 
ATOM   783  C  CG   . TRP A 1 97  ? -6.997  -10.720 9.041   1.00 8.72  ?  97  TRP A CG   1 
ATOM   784  C  CD1  . TRP A 1 97  ? -6.264  -11.524 8.184   1.00 10.07 ?  97  TRP A CD1  1 
ATOM   785  C  CD2  . TRP A 1 97  ? -6.934  -9.375  8.489   1.00 8.16  ?  97  TRP A CD2  1 
ATOM   786  N  NE1  . TRP A 1 97  ? -5.843  -10.767 7.081   1.00 10.86 ?  97  TRP A NE1  1 
ATOM   787  C  CE2  . TRP A 1 97  ? -6.201  -9.455  7.251   1.00 9.38  ?  97  TRP A CE2  1 
ATOM   788  C  CE3  . TRP A 1 97  ? -7.431  -8.126  8.922   1.00 9.48  ?  97  TRP A CE3  1 
ATOM   789  C  CZ2  . TRP A 1 97  ? -5.993  -8.327  6.422   1.00 10.69 ?  97  TRP A CZ2  1 
ATOM   790  C  CZ3  . TRP A 1 97  ? -7.172  -6.957  8.126   1.00 9.07  ?  97  TRP A CZ3  1 
ATOM   791  C  CH2  . TRP A 1 97  ? -6.494  -7.071  6.910   1.00 11.33 ?  97  TRP A CH2  1 
ATOM   792  N  N    . GLY A 1 98  ? -5.877  -13.252 11.460  1.00 9.07  ?  98  GLY A N    1 
ATOM   793  C  CA   . GLY A 1 98  ? -4.772  -14.222 11.506  1.00 9.23  ?  98  GLY A CA   1 
ATOM   794  C  C    . GLY A 1 98  ? -4.529  -14.940 10.180  1.00 9.65  ?  98  GLY A C    1 
ATOM   795  O  O    . GLY A 1 98  ? -5.261  -14.758 9.190   1.00 11.32 ?  98  GLY A O    1 
ATOM   796  N  N    . SER A 1 99  ? -3.486  -15.779 10.169  1.00 10.90 ?  99  SER A N    1 
ATOM   797  C  CA   . SER A 1 99  ? -3.242  -16.670 9.019   1.00 11.26 ?  99  SER A CA   1 
ATOM   798  C  C    . SER A 1 99  ? -4.114  -17.964 9.120   1.00 12.17 ?  99  SER A C    1 
ATOM   799  O  O    . SER A 1 99  ? -4.201  -18.739 8.157   1.00 15.40 ?  99  SER A O    1 
ATOM   800  C  CB   . SER A 1 99  ? -1.767  -16.992 9.006   1.00 14.40 ?  99  SER A CB   1 
ATOM   801  O  OG   . SER A 1 99  ? -1.417  -17.591 10.238  1.00 13.96 ?  99  SER A OG   1 
ATOM   802  N  N    . LEU A 1 100 ? -4.729  -18.154 10.293  1.00 12.50 ?  100 LEU A N    1 
ATOM   803  C  CA   . LEU A 1 100 ? -5.512  -19.336 10.664  1.00 13.89 ?  100 LEU A CA   1 
ATOM   804  C  C    . LEU A 1 100 ? -6.697  -18.861 11.493  1.00 13.32 ?  100 LEU A C    1 
ATOM   805  O  O    . LEU A 1 100 ? -6.556  -17.836 12.210  1.00 11.13 ?  100 LEU A O    1 
ATOM   806  C  CB   . LEU A 1 100 ? -4.669  -20.283 11.628  1.00 18.17 ?  100 LEU A CB   1 
ATOM   807  C  CG   . LEU A 1 100 ? -3.318  -20.668 11.109  1.00 20.55 ?  100 LEU A CG   1 
ATOM   808  C  CD1  . LEU A 1 100 ? -2.301  -20.887 12.241  1.00 28.44 ?  100 LEU A CD1  1 
ATOM   809  C  CD2  . LEU A 1 100 ? -3.488  -21.956 10.244  1.00 28.90 ?  100 LEU A CD2  1 
ATOM   810  N  N    . ASP A 1 101 ? -7.813  -19.634 11.483  1.00 12.03 ?  101 ASP A N    1 
ATOM   811  C  CA   . ASP A 1 101 ? -8.988  -19.196 12.292  1.00 12.69 ?  101 ASP A CA   1 
ATOM   812  C  C    . ASP A 1 101 ? -8.686  -19.126 13.794  1.00 13.15 ?  101 ASP A C    1 
ATOM   813  O  O    . ASP A 1 101 ? -9.358  -18.378 14.507  1.00 15.11 ?  101 ASP A O    1 
ATOM   814  C  CB   . ASP A 1 101 ? -10.255 -20.030 12.049  1.00 12.87 ?  101 ASP A CB   1 
ATOM   815  C  CG   . ASP A 1 101 ? -10.721 -20.016 10.620  1.00 17.24 ?  101 ASP A CG   1 
ATOM   816  O  OD1  . ASP A 1 101 ? -10.392 -19.156 9.755   1.00 15.61 ?  101 ASP A OD1  1 
ATOM   817  O  OD2  . ASP A 1 101 ? -11.534 -20.914 10.370  1.00 22.39 ?  101 ASP A OD2  1 
ATOM   818  N  N    . GLY A 1 102 ? -7.673  -19.863 14.282  1.00 12.66 ?  102 GLY A N    1 
ATOM   819  C  CA   . GLY A 1 102 ? -7.404  -19.896 15.740  1.00 12.38 ?  102 GLY A CA   1 
ATOM   820  C  C    . GLY A 1 102 ? -6.606  -18.703 16.298  1.00 10.44 ?  102 GLY A C    1 
ATOM   821  O  O    . GLY A 1 102 ? -6.269  -18.684 17.488  1.00 12.90 ?  102 GLY A O    1 
ATOM   822  N  N    . GLN A 1 103 ? -6.350  -17.685 15.478  1.00 10.04 ?  103 GLN A N    1 
ATOM   823  C  CA   . GLN A 1 103 ? -5.643  -16.492 15.992  1.00 9.48  ?  103 GLN A CA   1 
ATOM   824  C  C    . GLN A 1 103 ? -6.007  -15.321 15.101  1.00 8.62  ?  103 GLN A C    1 
ATOM   825  O  O    . GLN A 1 103 ? -6.566  -15.498 13.993  1.00 10.24 ?  103 GLN A O    1 
ATOM   826  C  CB   . GLN A 1 103 ? -4.129  -16.706 15.998  1.00 10.96 ?  103 GLN A CB   1 
ATOM   827  C  CG   . GLN A 1 103 ? -3.523  -16.906 14.568  1.00 10.85 ?  103 GLN A CG   1 
ATOM   828  C  CD   . GLN A 1 103 ? -2.084  -17.465 14.676  1.00 12.77 ?  103 GLN A CD   1 
ATOM   829  O  OE1  . GLN A 1 103 ? -1.826  -18.368 15.541  1.00 21.92 ?  103 GLN A OE1  1 
ATOM   830  N  NE2  . GLN A 1 103 ? -1.185  -17.038 13.820  1.00 15.71 ?  103 GLN A NE2  1 
ATOM   831  N  N    . GLY A 1 104 ? -5.680  -14.115 15.588  1.00 8.55  ?  104 GLY A N    1 
ATOM   832  C  CA   . GLY A 1 104 ? -5.952  -12.941 14.775  1.00 9.21  ?  104 GLY A CA   1 
ATOM   833  C  C    . GLY A 1 104 ? -6.418  -11.764 15.653  1.00 8.16  ?  104 GLY A C    1 
ATOM   834  O  O    . GLY A 1 104 ? -6.118  -10.589 15.316  1.00 10.06 ?  104 GLY A O    1 
ATOM   835  N  N    . SER A 1 105 ? -7.141  -12.042 16.777  1.00 7.01  ?  105 SER A N    1 
ATOM   836  C  CA   . SER A 1 105 ? -7.554  -10.921 17.611  1.00 7.62  ?  105 SER A CA   1 
ATOM   837  C  C    . SER A 1 105 ? -6.326  -10.325 18.379  1.00 7.24  ?  105 SER A C    1 
ATOM   838  O  O    . SER A 1 105 ? -5.290  -10.992 18.586  1.00 8.31  ?  105 SER A O    1 
ATOM   839  C  CB   . SER A 1 105 ? -8.667  -11.239 18.583  1.00 7.85  ?  105 SER A CB   1 
ATOM   840  O  OG   . SER A 1 105 ? -8.284  -12.180 19.558  1.00 8.39  ?  105 SER A OG   1 
ATOM   841  N  N    . GLU A 1 106 ? -6.462  -9.047  18.745  1.00 6.93  ?  106 GLU A N    1 
ATOM   842  C  CA   . GLU A 1 106 ? -5.457  -8.342  19.575  1.00 6.63  ?  106 GLU A CA   1 
ATOM   843  C  C    . GLU A 1 106 ? -5.806  -8.575  21.072  1.00 6.40  ?  106 GLU A C    1 
ATOM   844  O  O    . GLU A 1 106 ? -5.006  -9.151  21.859  1.00 8.52  ?  106 GLU A O    1 
ATOM   845  C  CB   . GLU A 1 106 ? -5.392  -6.851  19.218  1.00 8.05  ?  106 GLU A CB   1 
ATOM   846  C  CG   . GLU A 1 106 ? -4.866  -6.763  17.765  1.00 9.48  ?  106 GLU A CG   1 
ATOM   847  C  CD   . GLU A 1 106 ? -4.204  -5.479  17.425  1.00 8.32  ?  106 GLU A CD   1 
ATOM   848  O  OE1  . GLU A 1 106 ? -4.851  -4.405  17.667  1.00 9.10  ?  106 GLU A OE1  1 
ATOM   849  O  OE2  . GLU A 1 106 ? -3.004  -5.517  16.975  1.00 10.41 ?  106 GLU A OE2  1 
ATOM   850  N  N    . HIS A 1 107 ? -6.976  -8.090  21.494  1.00 6.51  ?  107 HIS A N    1 
ATOM   851  C  CA   . HIS A 1 107 ? -7.419  -8.453  22.826  1.00 6.35  ?  107 HIS A CA   1 
ATOM   852  C  C    . HIS A 1 107 ? -7.753  -9.970  22.829  1.00 6.88  ?  107 HIS A C    1 
ATOM   853  O  O    . HIS A 1 107 ? -8.072  -10.580 21.769  1.00 7.86  ?  107 HIS A O    1 
ATOM   854  C  CB   . HIS A 1 107 ? -8.675  -7.656  23.232  1.00 7.06  ?  107 HIS A CB   1 
ATOM   855  C  CG   . HIS A 1 107 ? -8.357  -6.199  23.343  1.00 5.84  ?  107 HIS A CG   1 
ATOM   856  N  ND1  . HIS A 1 107 ? -8.409  -5.317  22.289  1.00 9.07  ?  107 HIS A ND1  1 
ATOM   857  C  CD2  . HIS A 1 107 ? -7.932  -5.480  24.436  1.00 7.48  ?  107 HIS A CD2  1 
ATOM   858  C  CE1  . HIS A 1 107 ? -7.959  -4.132  22.680  1.00 8.49  ?  107 HIS A CE1  1 
ATOM   859  N  NE2  . HIS A 1 107 ? -7.701  -4.170  23.995  1.00 6.41  ?  107 HIS A NE2  1 
ATOM   860  N  N    . THR A 1 108 ? -7.598  -10.539 24.033  1.00 7.77  ?  108 THR A N    1 
ATOM   861  C  CA   . THR A 1 108 ? -7.967  -11.928 24.249  1.00 7.47  ?  108 THR A CA   1 
ATOM   862  C  C    . THR A 1 108 ? -8.957  -11.969 25.442  1.00 7.84  ?  108 THR A C    1 
ATOM   863  O  O    . THR A 1 108 ? -8.961  -11.025 26.241  1.00 9.06  ?  108 THR A O    1 
ATOM   864  C  CB   . THR A 1 108 ? -6.738  -12.856 24.457  1.00 8.56  ?  108 THR A CB   1 
ATOM   865  O  OG1  . THR A 1 108 ? -5.928  -12.389 25.543  1.00 8.55  ?  108 THR A OG1  1 
ATOM   866  C  CG2  . THR A 1 108 ? -5.892  -12.910 23.221  1.00 9.27  ?  108 THR A CG2  1 
ATOM   867  N  N    . VAL A 1 109 ? -9.702  -13.065 25.610  1.00 8.41  ?  109 VAL A N    1 
ATOM   868  C  CA   . VAL A 1 109 ? -10.701 -13.121 26.699  1.00 7.50  ?  109 VAL A CA   1 
ATOM   869  C  C    . VAL A 1 109 ? -10.364 -14.424 27.428  1.00 9.38  ?  109 VAL A C    1 
ATOM   870  O  O    . VAL A 1 109 ? -10.542 -15.486 26.844  1.00 9.88  ?  109 VAL A O    1 
ATOM   871  C  CB   . VAL A 1 109 ? -12.144 -13.160 26.120  1.00 11.05 ?  109 VAL A CB   1 
ATOM   872  C  CG1  . VAL A 1 109 ? -13.136 -13.275 27.263  1.00 12.73 ?  109 VAL A CG1  1 
ATOM   873  C  CG2  . VAL A 1 109 ? -12.420 -11.836 25.296  1.00 10.46 ?  109 VAL A CG2  1 
ATOM   874  N  N    . ASP A 1 110 ? -9.933  -14.332 28.686  1.00 10.03 ?  110 ASP A N    1 
ATOM   875  C  CA   . ASP A 1 110 ? -9.436  -15.568 29.379  1.00 10.50 ?  110 ASP A CA   1 
ATOM   876  C  C    . ASP A 1 110 ? -8.480  -16.375 28.486  1.00 10.16 ?  110 ASP A C    1 
ATOM   877  O  O    . ASP A 1 110 ? -8.533  -17.603 28.423  1.00 12.15 ?  110 ASP A O    1 
ATOM   878  C  CB   . ASP A 1 110 ? -10.651 -16.405 29.860  1.00 12.80 ?  110 ASP A CB   1 
ATOM   879  C  CG   . ASP A 1 110 ? -11.484 -15.651 30.909  1.00 12.36 ?  110 ASP A CG   1 
ATOM   880  O  OD1  . ASP A 1 110 ? -10.906 -14.798 31.633  1.00 15.56 ?  110 ASP A OD1  1 
ATOM   881  O  OD2  . ASP A 1 110 ? -12.702 -15.948 30.981  1.00 19.03 ?  110 ASP A OD2  1 
ATOM   882  N  N    . LYS A 1 111 ? -7.581  -15.633 27.803  1.00 9.87  ?  111 LYS A N    1 
ATOM   883  C  CA   . LYS A 1 111 ? -6.510  -16.127 26.919  1.00 10.98 ?  111 LYS A CA   1 
ATOM   884  C  C    . LYS A 1 111 ? -7.038  -16.686 25.558  1.00 10.71 ?  111 LYS A C    1 
ATOM   885  O  O    . LYS A 1 111 ? -6.213  -17.048 24.690  1.00 12.52 ?  111 LYS A O    1 
ATOM   886  C  CB   . LYS A 1 111 ? -5.584  -17.184 27.598  1.00 13.68 ?  111 LYS A CB   1 
ATOM   887  C  CG   . LYS A 1 111 ? -4.982  -16.639 28.890  1.00 16.10 ?  111 LYS A CG   1 
ATOM   888  C  CD   . LYS A 1 111 ? -3.885  -15.650 28.583  1.00 19.62 ?  111 LYS A CD   1 
ATOM   889  C  CE   . LYS A 1 111 ? -3.189  -14.976 29.833  1.00 23.01 ?  111 LYS A CE   1 
ATOM   890  N  NZ   . LYS A 1 111 ? -2.339  -16.031 30.328  1.00 34.74 ?  111 LYS A NZ   1 
ATOM   891  N  N    . LYS A 1 112 ? -8.358  -16.620 25.326  1.00 9.55  ?  112 LYS A N    1 
ATOM   892  C  CA   . LYS A 1 112 ? -8.953  -17.071 24.061  1.00 10.25 ?  112 LYS A CA   1 
ATOM   893  C  C    . LYS A 1 112 ? -8.636  -15.985 22.996  1.00 9.99  ?  112 LYS A C    1 
ATOM   894  O  O    . LYS A 1 112 ? -8.945  -14.760 23.191  1.00 9.53  ?  112 LYS A O    1 
ATOM   895  C  CB   . LYS A 1 112 ? -10.456 -17.207 24.185  1.00 13.39 ?  112 LYS A CB   1 
ATOM   896  C  CG   . LYS A 1 112 ? -11.155 -17.408 22.836  1.00 14.23 ?  112 LYS A CG   1 
ATOM   897  C  CD   . LYS A 1 112 ? -12.723 -17.441 22.983  1.00 17.40 ?  112 LYS A CD   1 
ATOM   898  C  CE   . LYS A 1 112 ? -13.322 -17.677 21.612  1.00 20.90 ?  112 LYS A CE   1 
ATOM   899  N  NZ   . LYS A 1 112 ? -13.130 -18.945 21.115  1.00 21.48 ?  112 LYS A NZ   1 
ATOM   900  N  N    . LYS A 1 113 ? -8.071  -16.479 21.900  1.00 10.77 ?  113 LYS A N    1 
ATOM   901  C  CA   . LYS A 1 113 ? -7.894  -15.657 20.657  1.00 9.54  ?  113 LYS A CA   1 
ATOM   902  C  C    . LYS A 1 113 ? -9.050  -15.876 19.665  1.00 9.43  ?  113 LYS A C    1 
ATOM   903  O  O    . LYS A 1 113 ? -9.412  -17.041 19.393  1.00 11.50 ?  113 LYS A O    1 
ATOM   904  C  CB   . LYS A 1 113 ? -6.591  -15.983 19.929  1.00 9.19  ?  113 LYS A CB   1 
ATOM   905  C  CG   . LYS A 1 113 ? -5.326  -15.652 20.795  1.00 9.79  ?  113 LYS A CG   1 
ATOM   906  C  CD   . LYS A 1 113 ? -4.066  -16.285 20.066  1.00 11.59 ?  113 LYS A CD   1 
ATOM   907  C  CE   . LYS A 1 113 ? -2.773  -15.727 20.710  1.00 17.48 ?  113 LYS A CE   1 
ATOM   908  N  NZ   . LYS A 1 113 ? -2.365  -16.479 21.823  1.00 21.85 ?  113 LYS A NZ   1 
ATOM   909  N  N    . TYR A 1 114 ? -9.648  -14.758 19.183  1.00 9.04  ?  114 TYR A N    1 
ATOM   910  C  CA   . TYR A 1 114 ? -10.638 -14.862 18.108  1.00 7.79  ?  114 TYR A CA   1 
ATOM   911  C  C    . TYR A 1 114 ? -9.995  -14.813 16.727  1.00 8.72  ?  114 TYR A C    1 
ATOM   912  O  O    . TYR A 1 114 ? -8.802  -14.470 16.608  1.00 8.81  ?  114 TYR A O    1 
ATOM   913  C  CB   . TYR A 1 114 ? -11.691 -13.730 18.260  1.00 9.18  ?  114 TYR A CB   1 
ATOM   914  C  CG   . TYR A 1 114 ? -12.577 -13.951 19.428  1.00 9.34  ?  114 TYR A CG   1 
ATOM   915  C  CD1  . TYR A 1 114 ? -12.264 -13.520 20.744  1.00 10.78 ?  114 TYR A CD1  1 
ATOM   916  C  CD2  . TYR A 1 114 ? -13.786 -14.614 19.227  1.00 10.13 ?  114 TYR A CD2  1 
ATOM   917  C  CE1  . TYR A 1 114 ? -13.152 -13.738 21.765  1.00 13.19 ?  114 TYR A CE1  1 
ATOM   918  C  CE2  . TYR A 1 114 ? -14.704 -14.775 20.230  1.00 10.66 ?  114 TYR A CE2  1 
ATOM   919  C  CZ   . TYR A 1 114 ? -14.378 -14.347 21.516  1.00 11.52 ?  114 TYR A CZ   1 
ATOM   920  O  OH   . TYR A 1 114 ? -15.317 -14.509 22.606  1.00 17.80 ?  114 TYR A OH   1 
ATOM   921  N  N    . ALA A 1 115 ? -10.781 -15.067 15.688  1.00 9.16  ?  115 ALA A N    1 
ATOM   922  C  CA   . ALA A 1 115 ? -10.210 -15.064 14.342  1.00 8.84  ?  115 ALA A CA   1 
ATOM   923  C  C    . ALA A 1 115 ? -9.788  -13.674 13.853  1.00 8.88  ?  115 ALA A C    1 
ATOM   924  O  O    . ALA A 1 115 ? -8.939  -13.542 12.942  1.00 9.07  ?  115 ALA A O    1 
ATOM   925  C  CB   . ALA A 1 115 ? -11.207 -15.661 13.321  1.00 10.07 ?  115 ALA A CB   1 
ATOM   926  N  N    . ALA A 1 116 ? -10.473 -12.660 14.381  1.00 7.84  ?  116 ALA A N    1 
ATOM   927  C  CA   . ALA A 1 116 ? -10.128 -11.279 13.911  1.00 7.59  ?  116 ALA A CA   1 
ATOM   928  C  C    . ALA A 1 116 ? -10.756 -10.314 14.974  1.00 7.52  ?  116 ALA A C    1 
ATOM   929  O  O    . ALA A 1 116 ? -11.508 -10.754 15.889  1.00 8.06  ?  116 ALA A O    1 
ATOM   930  C  CB   . ALA A 1 116 ? -10.731 -11.022 12.492  1.00 9.28  ?  116 ALA A CB   1 
ATOM   931  N  N    . GLU A 1 117 ? -10.436 -9.029  14.814  1.00 7.61  ?  117 GLU A N    1 
ATOM   932  C  CA   . GLU A 1 117 ? -10.981 -8.029  15.745  1.00 7.05  ?  117 GLU A CA   1 
ATOM   933  C  C    . GLU A 1 117 ? -11.148 -6.765  14.890  1.00 7.17  ?  117 GLU A C    1 
ATOM   934  O  O    . GLU A 1 117 ? -10.223 -6.359  14.171  1.00 8.16  ?  117 GLU A O    1 
ATOM   935  C  CB   . GLU A 1 117 ? -9.996  -7.769  16.886  1.00 7.82  ?  117 GLU A CB   1 
ATOM   936  C  CG   . GLU A 1 117 ? -10.538 -6.829  17.967  1.00 7.47  ?  117 GLU A CG   1 
ATOM   937  C  CD   . GLU A 1 117 ? -9.555  -6.757  19.185  1.00 7.89  ?  117 GLU A CD   1 
ATOM   938  O  OE1  . GLU A 1 117 ? -8.915  -7.810  19.479  1.00 8.72  ?  117 GLU A OE1  1 
ATOM   939  O  OE2  . GLU A 1 117 ? -9.502  -5.685  19.849  1.00 8.31  ?  117 GLU A OE2  1 
ATOM   940  N  N    . LEU A 1 118 ? -12.349 -6.219  14.997  1.00 6.79  ?  118 LEU A N    1 
ATOM   941  C  CA   . LEU A 1 118 ? -12.695 -4.943  14.378  1.00 6.03  ?  118 LEU A CA   1 
ATOM   942  C  C    . LEU A 1 118 ? -12.458 -3.756  15.344  1.00 6.21  ?  118 LEU A C    1 
ATOM   943  O  O    . LEU A 1 118 ? -12.895 -3.833  16.497  1.00 7.20  ?  118 LEU A O    1 
ATOM   944  C  CB   . LEU A 1 118 ? -14.189 -5.006  13.972  1.00 7.75  ?  118 LEU A CB   1 
ATOM   945  C  CG   . LEU A 1 118 ? -14.974 -3.707  13.640  1.00 7.61  ?  118 LEU A CG   1 
ATOM   946  C  CD1  . LEU A 1 118 ? -14.417 -3.056  12.397  1.00 9.20  ?  118 LEU A CD1  1 
ATOM   947  C  CD2  . LEU A 1 118 ? -16.471 -4.035  13.373  1.00 8.27  ?  118 LEU A CD2  1 
ATOM   948  N  N    . HIS A 1 119 ? -11.837 -2.670  14.822  1.00 6.65  ?  119 HIS A N    1 
ATOM   949  C  CA   . HIS A 1 119 ? -11.584 -1.478  15.638  1.00 6.50  ?  119 HIS A CA   1 
ATOM   950  C  C    . HIS A 1 119 ? -12.312 -0.318  14.950  1.00 6.33  ?  119 HIS A C    1 
ATOM   951  O  O    . HIS A 1 119 ? -11.926 0.041   13.804  1.00 7.74  ?  119 HIS A O    1 
ATOM   952  C  CB   . HIS A 1 119 ? -10.086 -1.190  15.695  1.00 6.61  ?  119 HIS A CB   1 
ATOM   953  C  CG   . HIS A 1 119 ? -9.421  -2.197  16.595  1.00 6.42  ?  119 HIS A CG   1 
ATOM   954  N  ND1  . HIS A 1 119 ? -8.074  -2.453  16.621  1.00 8.01  ?  119 HIS A ND1  1 
ATOM   955  C  CD2  . HIS A 1 119 ? -9.970  -3.027  17.524  1.00 7.66  ?  119 HIS A CD2  1 
ATOM   956  C  CE1  . HIS A 1 119 ? -7.783  -3.363  17.515  1.00 7.64  ?  119 HIS A CE1  1 
ATOM   957  N  NE2  . HIS A 1 119 ? -8.922  -3.745  18.103  1.00 7.60  ?  119 HIS A NE2  1 
ATOM   958  N  N    . LEU A 1 120 ? -13.339 0.244   15.646  1.00 6.78  ?  120 LEU A N    1 
ATOM   959  C  CA   . LEU A 1 120 ? -14.007 1.479   15.194  1.00 7.44  ?  120 LEU A CA   1 
ATOM   960  C  C    . LEU A 1 120 ? -13.380 2.635   15.942  1.00 6.55  ?  120 LEU A C    1 
ATOM   961  O  O    . LEU A 1 120 ? -13.500 2.715   17.182  1.00 6.13  ?  120 LEU A O    1 
ATOM   962  C  CB   . LEU A 1 120 ? -15.508 1.385   15.399  1.00 7.11  ?  120 LEU A CB   1 
ATOM   963  C  CG   . LEU A 1 120 ? -16.172 0.294   14.512  1.00 8.34  ?  120 LEU A CG   1 
ATOM   964  C  CD1  . LEU A 1 120 ? -17.057 -0.578  15.299  1.00 12.55 ?  120 LEU A CD1  1 
ATOM   965  C  CD2  . LEU A 1 120 ? -17.067 1.021   13.436  1.00 12.23 ?  120 LEU A CD2  1 
ATOM   966  N  N    . VAL A 1 121 ? -12.588 3.448   15.213  1.00 7.48  ?  121 VAL A N    1 
ATOM   967  C  CA   . VAL A 1 121 ? -11.785 4.500   15.866  1.00 7.64  ?  121 VAL A CA   1 
ATOM   968  C  C    . VAL A 1 121 ? -12.465 5.821   15.917  1.00 7.62  ?  121 VAL A C    1 
ATOM   969  O  O    . VAL A 1 121 ? -12.914 6.321   14.836  1.00 9.61  ?  121 VAL A O    1 
ATOM   970  C  CB   . VAL A 1 121 ? -10.379 4.623   15.125  1.00 7.67  ?  121 VAL A CB   1 
ATOM   971  C  CG1  . VAL A 1 121 ? -9.530  5.733   15.712  1.00 9.20  ?  121 VAL A CG1  1 
ATOM   972  C  CG2  . VAL A 1 121 ? -9.639  3.264   15.034  1.00 8.80  ?  121 VAL A CG2  1 
ATOM   973  N  N    . HIS A 1 122 ? -12.524 6.426   17.132  1.00 6.85  ?  122 HIS A N    1 
ATOM   974  C  CA   . HIS A 1 122 ? -13.261 7.718   17.266  1.00 7.61  ?  122 HIS A CA   1 
ATOM   975  C  C    . HIS A 1 122 ? -12.350 8.683   18.014  1.00 8.12  ?  122 HIS A C    1 
ATOM   976  O  O    . HIS A 1 122 ? -11.612 8.301   18.929  1.00 8.86  ?  122 HIS A O    1 
ATOM   977  C  CB   . HIS A 1 122 ? -14.563 7.553   18.077  1.00 8.16  ?  122 HIS A CB   1 
ATOM   978  C  CG   . HIS A 1 122 ? -15.448 6.390   17.670  1.00 8.00  ?  122 HIS A CG   1 
ATOM   979  N  ND1  . HIS A 1 122 ? -15.118 5.062   17.959  1.00 8.73  ?  122 HIS A ND1  1 
ATOM   980  C  CD2  . HIS A 1 122 ? -16.697 6.371   17.091  1.00 9.87  ?  122 HIS A CD2  1 
ATOM   981  C  CE1  . HIS A 1 122 ? -16.123 4.284   17.541  1.00 10.12 ?  122 HIS A CE1  1 
ATOM   982  N  NE2  . HIS A 1 122 ? -17.067 5.040   16.975  1.00 10.04 ?  122 HIS A NE2  1 
ATOM   983  N  N    . TRP A 1 123 ? -12.490 9.978   17.686  1.00 7.74  ?  123 TRP A N    1 
ATOM   984  C  CA   . TRP A 1 123 ? -11.683 11.012  18.403  1.00 7.92  ?  123 TRP A CA   1 
ATOM   985  C  C    . TRP A 1 123 ? -12.574 12.017  19.144  1.00 10.00 ?  123 TRP A C    1 
ATOM   986  O  O    . TRP A 1 123 ? -13.697 12.362  18.699  1.00 9.53  ?  123 TRP A O    1 
ATOM   987  C  CB   . TRP A 1 123 ? -10.704 11.755  17.480  1.00 9.50  ?  123 TRP A CB   1 
ATOM   988  C  CG   . TRP A 1 123 ? -11.356 12.345  16.259  1.00 10.02 ?  123 TRP A CG   1 
ATOM   989  C  CD1  . TRP A 1 123 ? -11.531 11.760  14.995  1.00 10.97 ?  123 TRP A CD1  1 
ATOM   990  C  CD2  . TRP A 1 123 ? -11.814 13.707  16.123  1.00 10.01 ?  123 TRP A CD2  1 
ATOM   991  N  NE1  . TRP A 1 123 ? -12.149 12.663  14.107  1.00 11.95 ?  123 TRP A NE1  1 
ATOM   992  C  CE2  . TRP A 1 123 ? -12.318 13.865  14.783  1.00 11.10 ?  123 TRP A CE2  1 
ATOM   993  C  CE3  . TRP A 1 123 ? -11.874 14.782  17.016  1.00 11.70 ?  123 TRP A CE3  1 
ATOM   994  C  CZ2  . TRP A 1 123 ? -12.819 15.077  14.331  1.00 11.81 ?  123 TRP A CZ2  1 
ATOM   995  C  CZ3  . TRP A 1 123 ? -12.376 16.018  16.538  1.00 12.43 ?  123 TRP A CZ3  1 
ATOM   996  C  CH2  . TRP A 1 123 ? -12.854 16.135  15.219  1.00 12.70 ?  123 TRP A CH2  1 
ATOM   997  N  N    . ASN A 1 124 ? -12.025 12.493  20.279  1.00 9.31  ?  124 ASN A N    1 
ATOM   998  C  CA   . ASN A 1 124 ? -12.797 13.369  21.145  1.00 9.99  ?  124 ASN A CA   1 
ATOM   999  C  C    . ASN A 1 124 ? -12.940 14.748  20.547  1.00 10.03 ?  124 ASN A C    1 
ATOM   1000 O  O    . ASN A 1 124 ? -11.917 15.445  20.319  1.00 10.61 ?  124 ASN A O    1 
ATOM   1001 C  CB   . ASN A 1 124 ? -12.008 13.441  22.451  1.00 9.65  ?  124 ASN A CB   1 
ATOM   1002 C  CG   . ASN A 1 124 ? -12.797 14.051  23.599  1.00 10.68 ?  124 ASN A CG   1 
ATOM   1003 O  OD1  . ASN A 1 124 ? -13.629 14.932  23.380  1.00 13.32 ?  124 ASN A OD1  1 
ATOM   1004 N  ND2  . ASN A 1 124 ? -12.524 13.561  24.870  1.00 13.64 ?  124 ASN A ND2  1 
ATOM   1005 N  N    . THR A 1 125 ? -14.197 15.196  20.365  1.00 10.63 ?  125 THR A N    1 
ATOM   1006 C  CA   . THR A 1 125 ? -14.404 16.451  19.652  1.00 10.78 ?  125 THR A CA   1 
ATOM   1007 C  C    . THR A 1 125 ? -13.809 17.690  20.360  1.00 11.99 ?  125 THR A C    1 
ATOM   1008 O  O    . THR A 1 125 ? -13.729 18.758  19.754  1.00 15.77 ?  125 THR A O    1 
ATOM   1009 C  CB   . THR A 1 125 ? -15.905 16.695  19.326  1.00 14.22 ?  125 THR A CB   1 
ATOM   1010 O  OG1  . THR A 1 125 ? -16.650 16.707  20.565  1.00 17.14 ?  125 THR A OG1  1 
ATOM   1011 C  CG2  . THR A 1 125 ? -16.371 15.541  18.361  1.00 15.23 ?  125 THR A CG2  1 
ATOM   1012 N  N    . LYS A 1 126 ? -13.539 17.463  21.805  1.00 12.39 ?  127 LYS A N    1 
ATOM   1013 C  CA   . LYS A 1 126 ? -13.008 18.672  22.455  1.00 14.68 ?  127 LYS A CA   1 
ATOM   1014 C  C    . LYS A 1 126 ? -11.610 19.023  21.919  1.00 14.51 ?  127 LYS A C    1 
ATOM   1015 O  O    . LYS A 1 126 ? -11.083 20.130  22.238  1.00 17.63 ?  127 LYS A O    1 
ATOM   1016 C  CB   . LYS A 1 126 ? -12.987 18.475  23.931  1.00 18.66 ?  127 LYS A CB   1 
ATOM   1017 C  CG   . LYS A 1 126 ? -12.073 17.572  24.440  1.00 19.92 ?  127 LYS A CG   1 
ATOM   1018 C  CD   . LYS A 1 126 ? -12.510 17.308  25.915  1.00 26.82 ?  127 LYS A CD   1 
ATOM   1019 C  CE   . LYS A 1 126 ? -11.469 16.536  26.566  1.00 30.93 ?  127 LYS A CE   1 
ATOM   1020 N  NZ   . LYS A 1 126 ? -11.111 16.898  28.007  1.00 38.10 ?  127 LYS A NZ   1 
ATOM   1021 N  N    . TYR A 1 127 ? -10.970 18.116  21.167  1.00 12.26 ?  128 TYR A N    1 
ATOM   1022 C  CA   . TYR A 1 127 ? -9.599  18.401  20.639  1.00 11.53 ?  128 TYR A CA   1 
ATOM   1023 C  C    . TYR A 1 127 ? -9.539  18.814  19.156  1.00 11.84 ?  128 TYR A C    1 
ATOM   1024 O  O    . TYR A 1 127 ? -8.428  19.014  18.588  1.00 13.22 ?  128 TYR A O    1 
ATOM   1025 C  CB   . TYR A 1 127 ? -8.621  17.237  20.874  1.00 12.26 ?  128 TYR A CB   1 
ATOM   1026 C  CG   . TYR A 1 127 ? -8.566  16.947  22.327  1.00 9.82  ?  128 TYR A CG   1 
ATOM   1027 C  CD1  . TYR A 1 127 ? -8.149  17.960  23.233  1.00 14.11 ?  128 TYR A CD1  1 
ATOM   1028 C  CD2  . TYR A 1 127 ? -8.846  15.662  22.852  1.00 10.38 ?  128 TYR A CD2  1 
ATOM   1029 C  CE1  . TYR A 1 127 ? -8.100  17.720  24.594  1.00 12.54 ?  128 TYR A CE1  1 
ATOM   1030 C  CE2  . TYR A 1 127 ? -8.780  15.412  24.243  1.00 11.29 ?  128 TYR A CE2  1 
ATOM   1031 C  CZ   . TYR A 1 127 ? -8.344  16.459  25.106  1.00 12.01 ?  128 TYR A CZ   1 
ATOM   1032 O  OH   . TYR A 1 127 ? -8.326  16.232  26.451  1.00 14.66 ?  128 TYR A OH   1 
ATOM   1033 N  N    . GLY A 1 128 ? -10.711 18.886  18.538  1.00 13.48 ?  129 GLY A N    1 
ATOM   1034 C  CA   . GLY A 1 128 ? -10.830 19.555  17.204  1.00 12.84 ?  129 GLY A CA   1 
ATOM   1035 C  C    . GLY A 1 128 ? -10.471 18.676  15.994  1.00 13.24 ?  129 GLY A C    1 
ATOM   1036 O  O    . GLY A 1 128 ? -11.106 18.795  14.916  1.00 16.23 ?  129 GLY A O    1 
ATOM   1037 N  N    . ASP A 1 129 ? -9.451  17.824  16.130  1.00 13.21 ?  130 ASP A N    1 
ATOM   1038 C  CA   . ASP A 1 129 ? -9.166  16.863  15.039  1.00 13.89 ?  130 ASP A CA   1 
ATOM   1039 C  C    . ASP A 1 129 ? -8.388  15.672  15.573  1.00 13.01 ?  130 ASP A C    1 
ATOM   1040 O  O    . ASP A 1 129 ? -7.941  15.659  16.763  1.00 13.60 ?  130 ASP A O    1 
ATOM   1041 C  CB   . ASP A 1 129 ? -8.526  17.499  13.791  1.00 15.88 ?  130 ASP A CB   1 
ATOM   1042 C  CG   . ASP A 1 129 ? -7.095  17.945  14.028  1.00 16.68 ?  130 ASP A CG   1 
ATOM   1043 O  OD1  . ASP A 1 129 ? -6.366  17.491  14.976  1.00 24.02 ?  130 ASP A OD1  1 
ATOM   1044 O  OD2  . ASP A 1 129 ? -6.584  18.692  13.224  1.00 22.89 ?  130 ASP A OD2  1 
ATOM   1045 N  N    . PHE A 1 130 ? -8.307  14.613  14.749  1.00 13.51 ?  131 PHE A N    1 
ATOM   1046 C  CA   . PHE A 1 130 ? -7.630  13.394  15.181  1.00 13.15 ?  131 PHE A CA   1 
ATOM   1047 C  C    . PHE A 1 130 ? -6.164  13.652  15.573  1.00 12.60 ?  131 PHE A C    1 
ATOM   1048 O  O    . PHE A 1 130 ? -5.709  13.058  16.578  1.00 12.40 ?  131 PHE A O    1 
ATOM   1049 C  CB   . PHE A 1 130 ? -7.757  12.397  14.015  1.00 11.64 ?  131 PHE A CB   1 
ATOM   1050 C  CG   . PHE A 1 130 ? -7.066  11.104  14.249  1.00 13.26 ?  131 PHE A CG   1 
ATOM   1051 C  CD1  . PHE A 1 130 ? -7.705  10.020  14.943  1.00 10.54 ?  131 PHE A CD1  1 
ATOM   1052 C  CD2  . PHE A 1 130 ? -5.723  10.961  13.867  1.00 14.85 ?  131 PHE A CD2  1 
ATOM   1053 C  CE1  . PHE A 1 130 ? -6.996  8.852   15.144  1.00 12.39 ?  131 PHE A CE1  1 
ATOM   1054 C  CE2  . PHE A 1 130 ? -5.027  9.777   14.080  1.00 16.12 ?  131 PHE A CE2  1 
ATOM   1055 C  CZ   . PHE A 1 130 ? -5.660  8.715   14.758  1.00 14.75 ?  131 PHE A CZ   1 
ATOM   1056 N  N    . GLY A 1 131 ? -5.429  14.412  14.745  1.00 12.80 ?  132 GLY A N    1 
ATOM   1057 C  CA   . GLY A 1 131 ? -4.034  14.581  15.059  1.00 14.29 ?  132 GLY A CA   1 
ATOM   1058 C  C    . GLY A 1 131 ? -3.787  15.241  16.399  1.00 13.91 ?  132 GLY A C    1 
ATOM   1059 O  O    . GLY A 1 131 ? -2.757  14.973  17.040  1.00 15.00 ?  132 GLY A O    1 
ATOM   1060 N  N    . LYS A 1 132 ? -4.649  16.211  16.789  1.00 13.81 ?  133 LYS A N    1 
ATOM   1061 C  CA   . LYS A 1 132 ? -4.466  16.758  18.100  1.00 13.44 ?  133 LYS A CA   1 
ATOM   1062 C  C    . LYS A 1 132 ? -4.931  15.795  19.191  1.00 11.86 ?  133 LYS A C    1 
ATOM   1063 O  O    . LYS A 1 132 ? -4.362  15.727  20.337  1.00 12.39 ?  133 LYS A O    1 
ATOM   1064 C  CB   . LYS A 1 132 ? -5.207  18.103  18.210  1.00 14.63 ?  133 LYS A CB   1 
ATOM   1065 C  CG   . LYS A 1 132 ? -4.515  19.261  17.498  1.00 19.00 ?  133 LYS A CG   1 
ATOM   1066 C  CD   . LYS A 1 132 ? -3.137  19.512  18.183  1.00 25.49 ?  133 LYS A CD   1 
ATOM   1067 C  CE   . LYS A 1 132 ? -3.187  20.836  19.058  1.00 33.65 ?  133 LYS A CE   1 
ATOM   1068 N  NZ   . LYS A 1 132 ? -1.849  21.520  19.219  1.00 38.37 ?  133 LYS A NZ   1 
ATOM   1069 N  N    . ALA A 1 133 ? -6.019  15.072  18.908  1.00 10.33 ?  134 ALA A N    1 
ATOM   1070 C  CA   . ALA A 1 133 ? -6.562  14.141  19.900  1.00 11.07 ?  134 ALA A CA   1 
ATOM   1071 C  C    . ALA A 1 133 ? -5.571  13.039  20.330  1.00 9.95  ?  134 ALA A C    1 
ATOM   1072 O  O    . ALA A 1 133 ? -5.531  12.682  21.531  1.00 10.96 ?  134 ALA A O    1 
ATOM   1073 C  CB   . ALA A 1 133 ? -7.902  13.458  19.359  1.00 10.23 ?  134 ALA A CB   1 
ATOM   1074 N  N    . VAL A 1 134 ? -4.754  12.543  19.395  1.00 10.33 ?  135 VAL A N    1 
ATOM   1075 C  CA   . VAL A 1 134 ? -3.857  11.441  19.784  1.00 10.40 ?  135 VAL A CA   1 
ATOM   1076 C  C    . VAL A 1 134 ? -2.744  11.881  20.792  1.00 10.22 ?  135 VAL A C    1 
ATOM   1077 O  O    . VAL A 1 134 ? -2.035  11.016  21.362  1.00 11.30 ?  135 VAL A O    1 
ATOM   1078 C  CB   . VAL A 1 134 ? -3.220  10.682  18.590  1.00 12.65 ?  135 VAL A CB   1 
ATOM   1079 C  CG1  . VAL A 1 134 ? -4.298  10.051  17.752  1.00 12.35 ?  135 VAL A CG1  1 
ATOM   1080 C  CG2  . VAL A 1 134 ? -2.286  11.546  17.753  1.00 12.46 ?  135 VAL A CG2  1 
ATOM   1081 N  N    . GLN A 1 135 ? -2.593  13.220  20.966  1.00 11.16 ?  136 GLN A N    1 
ATOM   1082 C  CA   . GLN A 1 135 ? -1.616  13.687  21.922  1.00 12.71 ?  136 GLN A CA   1 
ATOM   1083 C  C    . GLN A 1 135 ? -2.185  13.824  23.332  1.00 12.71 ?  136 GLN A C    1 
ATOM   1084 O  O    . GLN A 1 135 ? -1.504  14.418  24.245  1.00 15.37 ?  136 GLN A O    1 
ATOM   1085 C  CB   . GLN A 1 135 ? -1.106  15.074  21.361  1.00 14.45 ?  136 GLN A CB   1 
ATOM   1086 C  CG   . GLN A 1 135 ? -0.401  14.886  19.996  1.00 18.26 ?  136 GLN A CG   1 
ATOM   1087 C  CD   . GLN A 1 135 ? 0.909   13.983  20.082  1.00 30.74 ?  136 GLN A CD   1 
ATOM   1088 O  OE1  . GLN A 1 135 ? 1.593   13.941  21.137  1.00 35.19 ?  136 GLN A OE1  1 
ATOM   1089 N  NE2  . GLN A 1 135 ? 1.282   13.317  18.959  1.00 32.28 ?  136 GLN A NE2  1 
ATOM   1090 N  N    . GLN A 1 136 ? -3.438  13.365  23.494  1.00 10.57 ?  137 GLN A N    1 
ATOM   1091 C  CA   . GLN A 1 136 ? -4.123  13.605  24.796  1.00 11.62 ?  137 GLN A CA   1 
ATOM   1092 C  C    . GLN A 1 136 ? -4.472  12.242  25.438  1.00 11.36 ?  137 GLN A C    1 
ATOM   1093 O  O    . GLN A 1 136 ? -4.856  11.298  24.704  1.00 10.05 ?  137 GLN A O    1 
ATOM   1094 C  CB   . GLN A 1 136 ? -5.383  14.414  24.642  1.00 11.64 ?  137 GLN A CB   1 
ATOM   1095 C  CG   . GLN A 1 136 ? -5.170  15.727  23.803  1.00 16.33 ?  137 GLN A CG   1 
ATOM   1096 C  CD   . GLN A 1 136 ? -4.277  16.671  24.547  1.00 19.99 ?  137 GLN A CD   1 
ATOM   1097 O  OE1  . GLN A 1 136 ? -4.207  16.589  25.763  1.00 21.41 ?  137 GLN A OE1  1 
ATOM   1098 N  NE2  . GLN A 1 136 ? -3.519  17.506  23.829  1.00 28.13 ?  137 GLN A NE2  1 
ATOM   1099 N  N    . PRO A 1 137 ? -4.493  12.185  26.781  1.00 11.88 ?  138 PRO A N    1 
ATOM   1100 C  CA   . PRO A 1 137 ? -4.741  10.894  27.433  1.00 11.96 ?  138 PRO A CA   1 
ATOM   1101 C  C    . PRO A 1 137 ? -6.186  10.394  27.298  1.00 12.50 ?  138 PRO A C    1 
ATOM   1102 O  O    . PRO A 1 137 ? -6.422  9.155   27.434  1.00 14.49 ?  138 PRO A O    1 
ATOM   1103 C  CB   . PRO A 1 137 ? -4.353  11.126  28.902  1.00 13.91 ?  138 PRO A CB   1 
ATOM   1104 C  CG   . PRO A 1 137 ? -4.386  12.633  29.022  1.00 16.39 ?  138 PRO A CG   1 
ATOM   1105 C  CD   . PRO A 1 137 ? -4.143  13.271  27.711  1.00 11.86 ?  138 PRO A CD   1 
ATOM   1106 N  N    . ASP A 1 138 ? -7.117  11.293  26.910  1.00 9.70  ?  139 ASP A N    1 
ATOM   1107 C  CA   . ASP A 1 138 ? -8.530  10.880  26.675  1.00 11.50 ?  139 ASP A CA   1 
ATOM   1108 C  C    . ASP A 1 138 ? -8.876  11.297  25.213  1.00 10.04 ?  139 ASP A C    1 
ATOM   1109 O  O    . ASP A 1 138 ? -10.016 11.724  24.937  1.00 11.61 ?  139 ASP A O    1 
ATOM   1110 C  CB   . ASP A 1 138 ? -9.501  11.609  27.653  1.00 12.30 ?  139 ASP A CB   1 
ATOM   1111 C  CG   . ASP A 1 138 ? -9.361  13.126  27.611  1.00 13.42 ?  139 ASP A CG   1 
ATOM   1112 O  OD1  . ASP A 1 138 ? -8.374  13.692  26.981  1.00 15.38 ?  139 ASP A OD1  1 
ATOM   1113 O  OD2  . ASP A 1 138 ? -10.188 13.810  28.299  1.00 18.91 ?  139 ASP A OD2  1 
ATOM   1114 N  N    . GLY A 1 139 ? -7.919  11.176  24.252  1.00 9.19  ?  140 GLY A N    1 
ATOM   1115 C  CA   . GLY A 1 139 ? -8.139  11.663  22.887  1.00 8.20  ?  140 GLY A CA   1 
ATOM   1116 C  C    . GLY A 1 139 ? -9.002  10.772  22.032  1.00 8.15  ?  140 GLY A C    1 
ATOM   1117 O  O    . GLY A 1 139 ? -9.757  11.267  21.188  1.00 8.83  ?  140 GLY A O    1 
ATOM   1118 N  N    . LEU A 1 140 ? -8.850  9.438   22.228  1.00 7.19  ?  141 LEU A N    1 
ATOM   1119 C  CA   . LEU A 1 140 ? -9.536  8.486   21.355  1.00 7.04  ?  141 LEU A CA   1 
ATOM   1120 C  C    . LEU A 1 140 ? -10.452 7.570   22.162  1.00 7.73  ?  141 LEU A C    1 
ATOM   1121 O  O    . LEU A 1 140 ? -10.144 7.300   23.341  1.00 7.86  ?  141 LEU A O    1 
ATOM   1122 C  CB   . LEU A 1 140 ? -8.547  7.563   20.619  1.00 8.48  ?  141 LEU A CB   1 
ATOM   1123 C  CG   . LEU A 1 140 ? -7.646  8.284   19.629  1.00 9.19  ?  141 LEU A CG   1 
ATOM   1124 C  CD1  . LEU A 1 140 ? -6.882  7.300   18.768  1.00 9.10  ?  141 LEU A CD1  1 
ATOM   1125 C  CD2  . LEU A 1 140 ? -8.287  9.343   18.690  1.00 11.51 ?  141 LEU A CD2  1 
ATOM   1126 N  N    . ALA A 1 141 ? -11.473 7.053   21.474  1.00 6.89  ?  142 ALA A N    1 
ATOM   1127 C  CA   . ALA A 1 141 ? -12.277 5.940   22.057  1.00 6.76  ?  142 ALA A CA   1 
ATOM   1128 C  C    . ALA A 1 141 ? -12.395 4.917   20.910  1.00 6.66  ?  142 ALA A C    1 
ATOM   1129 O  O    . ALA A 1 141 ? -12.749 5.286   19.798  1.00 9.00  ?  142 ALA A O    1 
ATOM   1130 C  CB   . ALA A 1 141 ? -13.649 6.378   22.470  1.00 8.72  ?  142 ALA A CB   1 
ATOM   1131 N  N    . VAL A 1 142 ? -11.892 3.689   21.184  1.00 7.34  ?  143 VAL A N    1 
ATOM   1132 C  CA   . VAL A 1 142 ? -11.966 2.685   20.173  1.00 6.73  ?  143 VAL A CA   1 
ATOM   1133 C  C    . VAL A 1 142 ? -12.939 1.580   20.632  1.00 7.75  ?  143 VAL A C    1 
ATOM   1134 O  O    . VAL A 1 142 ? -12.812 1.058   21.754  1.00 8.22  ?  143 VAL A O    1 
ATOM   1135 C  CB   . VAL A 1 142 ? -10.572 2.071   19.843  1.00 8.62  ?  143 VAL A CB   1 
ATOM   1136 C  CG1  . VAL A 1 142 ? -10.742 0.994   18.694  1.00 9.36  ?  143 VAL A CG1  1 
ATOM   1137 C  CG2  . VAL A 1 142 ? -9.588  3.123   19.422  1.00 8.72  ?  143 VAL A CG2  1 
ATOM   1138 N  N    . LEU A 1 143 ? -13.883 1.310   19.740  1.00 6.52  ?  144 LEU A N    1 
ATOM   1139 C  CA   . LEU A 1 143 ? -14.880 0.266   20.041  1.00 8.64  ?  144 LEU A CA   1 
ATOM   1140 C  C    . LEU A 1 143 ? -14.303 -0.975  19.373  1.00 7.87  ?  144 LEU A C    1 
ATOM   1141 O  O    . LEU A 1 143 ? -14.177 -1.019  18.120  1.00 8.80  ?  144 LEU A O    1 
ATOM   1142 C  CB   . LEU A 1 143 ? -16.302 0.657   19.443  1.00 8.97  ?  144 LEU A CB   1 
ATOM   1143 C  CG   . LEU A 1 143 ? -17.419 -0.388  19.580  1.00 8.32  ?  144 LEU A CG   1 
ATOM   1144 C  CD1  . LEU A 1 143 ? -17.570 -0.679  21.047  1.00 11.73 ?  144 LEU A CD1  1 
ATOM   1145 C  CD2  . LEU A 1 143 ? -18.727 0.191   18.963  1.00 11.67 ?  144 LEU A CD2  1 
ATOM   1146 N  N    . GLY A 1 144 ? -13.986 -2.009  20.203  1.00 7.22  ?  145 GLY A N    1 
ATOM   1147 C  CA   . GLY A 1 144 ? -13.380 -3.226  19.659  1.00 7.21  ?  145 GLY A CA   1 
ATOM   1148 C  C    . GLY A 1 144 ? -14.431 -4.353  19.616  1.00 7.07  ?  145 GLY A C    1 
ATOM   1149 O  O    . GLY A 1 144 ? -15.165 -4.536  20.628  1.00 7.55  ?  145 GLY A O    1 
ATOM   1150 N  N    . ILE A 1 145 ? -14.499 -5.126  18.488  1.00 5.95  ?  146 ILE A N    1 
ATOM   1151 C  CA   . ILE A 1 145 ? -15.544 -6.176  18.372  1.00 6.72  ?  146 ILE A CA   1 
ATOM   1152 C  C    . ILE A 1 145 ? -14.830 -7.423  17.851  1.00 8.58  ?  146 ILE A C    1 
ATOM   1153 O  O    . ILE A 1 145 ? -14.129 -7.402  16.829  1.00 8.73  ?  146 ILE A O    1 
ATOM   1154 C  CB   . ILE A 1 145 ? -16.642 -5.697  17.333  1.00 8.03  ?  146 ILE A CB   1 
ATOM   1155 C  CG1  . ILE A 1 145 ? -17.229 -4.383  17.847  1.00 8.51  ?  146 ILE A CG1  1 
ATOM   1156 C  CG2  . ILE A 1 145 ? -17.718 -6.774  17.151  1.00 9.97  ?  146 ILE A CG2  1 
ATOM   1157 C  CD1  . ILE A 1 145 ? -18.374 -3.831  17.021  1.00 8.43  ?  146 ILE A CD1  1 
ATOM   1158 N  N    . PHE A 1 146 ? -15.030 -8.559  18.514  1.00 7.24  ?  147 PHE A N    1 
ATOM   1159 C  CA   . PHE A 1 146 ? -14.346 -9.820  18.104  1.00 7.96  ?  147 PHE A CA   1 
ATOM   1160 C  C    . PHE A 1 146 ? -15.107 -10.418 16.939  1.00 7.80  ?  147 PHE A C    1 
ATOM   1161 O  O    . PHE A 1 146 ? -16.379 -10.318 16.896  1.00 8.20  ?  147 PHE A O    1 
ATOM   1162 C  CB   . PHE A 1 146 ? -14.383 -10.772 19.286  1.00 8.03  ?  147 PHE A CB   1 
ATOM   1163 C  CG   . PHE A 1 146 ? -13.533 -10.275 20.433  1.00 6.75  ?  147 PHE A CG   1 
ATOM   1164 C  CD1  . PHE A 1 146 ? -12.147 -10.115 20.223  1.00 6.84  ?  147 PHE A CD1  1 
ATOM   1165 C  CD2  . PHE A 1 146 ? -14.056 -10.035 21.674  1.00 7.81  ?  147 PHE A CD2  1 
ATOM   1166 C  CE1  . PHE A 1 146 ? -11.289 -9.732  21.264  1.00 7.31  ?  147 PHE A CE1  1 
ATOM   1167 C  CE2  . PHE A 1 146 ? -13.240 -9.619  22.755  1.00 7.81  ?  147 PHE A CE2  1 
ATOM   1168 C  CZ   . PHE A 1 146 ? -11.814 -9.509  22.535  1.00 7.12  ?  147 PHE A CZ   1 
ATOM   1169 N  N    . LEU A 1 147 ? -14.380 -11.096 16.042  1.00 8.03  ?  148 LEU A N    1 
ATOM   1170 C  CA   . LEU A 1 147 ? -15.004 -11.854 14.963  1.00 7.52  ?  148 LEU A CA   1 
ATOM   1171 C  C    . LEU A 1 147 ? -14.655 -13.366 15.216  1.00 8.43  ?  148 LEU A C    1 
ATOM   1172 O  O    . LEU A 1 147 ? -13.482 -13.699 15.393  1.00 8.68  ?  148 LEU A O    1 
ATOM   1173 C  CB   . LEU A 1 147 ? -14.392 -11.493 13.569  1.00 7.95  ?  148 LEU A CB   1 
ATOM   1174 C  CG   . LEU A 1 147 ? -14.977 -10.185 12.961  1.00 8.04  ?  148 LEU A CG   1 
ATOM   1175 C  CD1  . LEU A 1 147 ? -14.776 -8.893  13.827  1.00 11.08 ?  148 LEU A CD1  1 
ATOM   1176 C  CD2  . LEU A 1 147 ? -14.369 -9.998  11.590  1.00 10.53 ?  148 LEU A CD2  1 
ATOM   1177 N  N    . LYS A 1 148 ? -15.677 -14.219 15.170  1.00 8.79  ?  149 LYS A N    1 
ATOM   1178 C  CA   . LYS A 1 148 ? -15.498 -15.668 15.117  1.00 10.64 ?  149 LYS A CA   1 
ATOM   1179 C  C    . LYS A 1 148 ? -16.013 -16.173 13.769  1.00 10.60 ?  149 LYS A C    1 
ATOM   1180 O  O    . LYS A 1 148 ? -16.811 -15.533 13.128  1.00 11.52 ?  149 LYS A O    1 
ATOM   1181 C  CB   . LYS A 1 148 ? -16.289 -16.385 16.248  1.00 11.62 ?  149 LYS A CB   1 
ATOM   1182 C  CG   . LYS A 1 148 ? -17.798 -16.178 16.201  1.00 15.29 ?  149 LYS A CG   1 
ATOM   1183 C  CD   . LYS A 1 148 ? -18.448 -16.962 17.420  1.00 18.06 ?  149 LYS A CD   1 
ATOM   1184 C  CE   . LYS A 1 148 ? -19.978 -16.983 17.316  1.00 24.83 ?  149 LYS A CE   1 
ATOM   1185 N  NZ   . LYS A 1 148 ? -20.524 -17.847 18.442  1.00 30.22 ?  149 LYS A NZ   1 
ATOM   1186 N  N    . VAL A 1 149 ? -15.512 -17.304 13.325  1.00 11.48 ?  150 VAL A N    1 
ATOM   1187 C  CA   . VAL A 1 149 ? -15.898 -17.861 12.037  1.00 11.76 ?  150 VAL A CA   1 
ATOM   1188 C  C    . VAL A 1 149 ? -17.115 -18.801 12.262  1.00 12.27 ?  150 VAL A C    1 
ATOM   1189 O  O    . VAL A 1 149 ? -17.053 -19.781 13.079  1.00 13.96 ?  150 VAL A O    1 
ATOM   1190 C  CB   . VAL A 1 149 ? -14.728 -18.682 11.463  1.00 12.27 ?  150 VAL A CB   1 
ATOM   1191 C  CG1  . VAL A 1 149 ? -15.175 -19.444 10.130  1.00 13.43 ?  150 VAL A CG1  1 
ATOM   1192 C  CG2  . VAL A 1 149 ? -13.564 -17.680 11.093  1.00 14.49 ?  150 VAL A CG2  1 
ATOM   1193 N  N    . GLY A 1 150 ? -18.148 -18.584 11.465  1.00 10.72 ?  151 GLY A N    1 
ATOM   1194 C  CA   . GLY A 1 150 ? -19.367 -19.425 11.571  1.00 12.47 ?  151 GLY A CA   1 
ATOM   1195 C  C    . GLY A 1 150 ? -20.260 -18.949 10.405  1.00 12.66 ?  151 GLY A C    1 
ATOM   1196 O  O    . GLY A 1 150 ? -19.851 -19.032 9.227   1.00 13.16 ?  151 GLY A O    1 
ATOM   1197 N  N    A SER A 1 151 ? -21.469 -18.475 10.705  0.50 13.69 ?  152 SER A N    1 
ATOM   1198 N  N    B SER A 1 151 ? -21.451 -18.454 10.757  0.50 13.61 ?  152 SER A N    1 
ATOM   1199 C  CA   A SER A 1 151 ? -22.337 -17.933 9.617   0.50 13.81 ?  152 SER A CA   1 
ATOM   1200 C  CA   B SER A 1 151 ? -22.389 -17.826 9.784   0.50 13.74 ?  152 SER A CA   1 
ATOM   1201 C  C    A SER A 1 151 ? -21.795 -16.587 9.134   0.50 14.22 ?  152 SER A C    1 
ATOM   1202 C  C    B SER A 1 151 ? -21.798 -16.535 9.159   0.50 14.12 ?  152 SER A C    1 
ATOM   1203 O  O    A SER A 1 151 ? -21.059 -15.909 9.883   0.50 14.10 ?  152 SER A O    1 
ATOM   1204 O  O    B SER A 1 151 ? -21.000 -15.846 9.832   0.50 14.34 ?  152 SER A O    1 
ATOM   1205 C  CB   A SER A 1 151 ? -23.734 -17.730 10.127  0.50 16.10 ?  152 SER A CB   1 
ATOM   1206 C  CB   B SER A 1 151 ? -23.663 -17.483 10.522  0.50 15.68 ?  152 SER A CB   1 
ATOM   1207 O  OG   A SER A 1 151 ? -23.691 -16.728 11.144  0.50 15.28 ?  152 SER A OG   1 
ATOM   1208 O  OG   B SER A 1 151 ? -24.317 -18.661 10.945  0.50 16.21 ?  152 SER A OG   1 
ATOM   1209 N  N    . ALA A 1 152 ? -22.127 -16.236 7.883   1.00 13.32 ?  153 ALA A N    1 
ATOM   1210 C  CA   . ALA A 1 152 ? -21.679 -15.000 7.268   1.00 12.11 ?  153 ALA A CA   1 
ATOM   1211 C  C    . ALA A 1 152 ? -22.280 -13.788 7.993   1.00 11.91 ?  153 ALA A C    1 
ATOM   1212 O  O    . ALA A 1 152 ? -23.394 -13.861 8.562   1.00 14.85 ?  153 ALA A O    1 
ATOM   1213 C  CB   . ALA A 1 152 ? -22.117 -14.935 5.761   1.00 13.89 ?  153 ALA A CB   1 
ATOM   1214 N  N    . LYS A 1 153 ? -21.574 -12.639 7.898   1.00 12.37 ?  154 LYS A N    1 
ATOM   1215 C  CA   . LYS A 1 153 ? -22.118 -11.378 8.390   1.00 13.51 ?  154 LYS A CA   1 
ATOM   1216 C  C    . LYS A 1 153 ? -22.528 -10.610 7.120   1.00 13.97 ?  154 LYS A C    1 
ATOM   1217 O  O    . LYS A 1 153 ? -21.714 -10.159 6.387   1.00 12.64 ?  154 LYS A O    1 
ATOM   1218 C  CB   . LYS A 1 153 ? -21.043 -10.550 9.151   1.00 13.21 ?  154 LYS A CB   1 
ATOM   1219 C  CG   . LYS A 1 153 ? -21.604 -9.365  9.913   1.00 16.56 ?  154 LYS A CG   1 
ATOM   1220 C  CD   . LYS A 1 153 ? -22.476 -9.819  11.094  1.00 16.68 ?  154 LYS A CD   1 
ATOM   1221 C  CE   . LYS A 1 153 ? -22.736 -8.633  12.035  1.00 19.17 ?  154 LYS A CE   1 
ATOM   1222 N  NZ   . LYS A 1 153 ? -23.732 -8.965  13.002  1.00 23.10 ?  154 LYS A NZ   1 
ATOM   1223 N  N    . PRO A 1 154 ? -23.838 -10.555 6.842   1.00 14.42 ?  155 PRO A N    1 
ATOM   1224 C  CA   . PRO A 1 154 ? -24.245 -9.917  5.541   1.00 14.63 ?  155 PRO A CA   1 
ATOM   1225 C  C    . PRO A 1 154 ? -23.751 -8.487  5.409   1.00 13.45 ?  155 PRO A C    1 
ATOM   1226 O  O    . PRO A 1 154 ? -23.333 -8.093  4.320   1.00 15.56 ?  155 PRO A O    1 
ATOM   1227 C  CB   . PRO A 1 154 ? -25.812 -9.955  5.572   1.00 16.11 ?  155 PRO A CB   1 
ATOM   1228 C  CG   . PRO A 1 154 ? -26.101 -11.121 6.594   1.00 19.21 ?  155 PRO A CG   1 
ATOM   1229 C  CD   . PRO A 1 154 ? -24.984 -11.089 7.611   1.00 15.43 ?  155 PRO A CD   1 
ATOM   1230 N  N    . GLY A 1 155 ? -23.701 -7.767  6.525   1.00 13.61 ?  156 GLY A N    1 
ATOM   1231 C  CA   . GLY A 1 155 ? -23.300 -6.349  6.549   1.00 14.23 ?  156 GLY A CA   1 
ATOM   1232 C  C    . GLY A 1 155 ? -21.817 -6.125  6.314   1.00 15.23 ?  156 GLY A C    1 
ATOM   1233 O  O    . GLY A 1 155 ? -21.364 -4.985  6.191   1.00 17.94 ?  156 GLY A O    1 
ATOM   1234 N  N    . LEU A 1 156 ? -21.048 -7.222  6.322   1.00 13.23 ?  157 LEU A N    1 
ATOM   1235 C  CA   . LEU A 1 156 ? -19.577 -7.195  5.992   1.00 11.97 ?  157 LEU A CA   1 
ATOM   1236 C  C    . LEU A 1 156 ? -19.320 -7.405  4.506   1.00 12.29 ?  157 LEU A C    1 
ATOM   1237 O  O    . LEU A 1 156 ? -18.200 -7.086  4.006   1.00 12.92 ?  157 LEU A O    1 
ATOM   1238 C  CB   . LEU A 1 156 ? -18.825 -8.280  6.795   1.00 12.45 ?  157 LEU A CB   1 
ATOM   1239 C  CG   . LEU A 1 156 ? -17.288 -8.322  6.663   1.00 11.27 ?  157 LEU A CG   1 
ATOM   1240 C  CD1  . LEU A 1 156 ? -16.618 -6.983  7.069   1.00 14.24 ?  157 LEU A CD1  1 
ATOM   1241 C  CD2  . LEU A 1 156 ? -16.697 -9.467  7.498   1.00 12.51 ?  157 LEU A CD2  1 
ATOM   1242 N  N    . GLN A 1 157 ? -20.327 -7.943  3.754   1.00 12.39 ?  158 GLN A N    1 
ATOM   1243 C  CA   . GLN A 1 157 ? -20.006 -8.455  2.415   1.00 13.44 ?  158 GLN A CA   1 
ATOM   1244 C  C    . GLN A 1 157 ? -19.609 -7.306  1.485   1.00 12.94 ?  158 GLN A C    1 
ATOM   1245 O  O    . GLN A 1 157 ? -18.721 -7.498  0.668   1.00 13.26 ?  158 GLN A O    1 
ATOM   1246 C  CB   . GLN A 1 157 ? -21.120 -9.315  1.823   1.00 14.71 ?  158 GLN A CB   1 
ATOM   1247 C  CG   . GLN A 1 157 ? -20.667 -10.016 0.519   1.00 16.30 ?  158 GLN A CG   1 
ATOM   1248 C  CD   . GLN A 1 157 ? -19.527 -11.023 0.750   1.00 16.53 ?  158 GLN A CD   1 
ATOM   1249 O  OE1  . GLN A 1 157 ? -19.370 -11.625 1.889   1.00 17.79 ?  158 GLN A OE1  1 
ATOM   1250 N  NE2  . GLN A 1 157 ? -18.743 -11.249 -0.307  1.00 18.06 ?  158 GLN A NE2  1 
ATOM   1251 N  N    . LYS A 1 158 ? -20.163 -6.077  1.664   1.00 14.81 ?  159 LYS A N    1 
ATOM   1252 C  CA   . LYS A 1 158 ? -19.744 -4.988  0.737   1.00 15.15 ?  159 LYS A CA   1 
ATOM   1253 C  C    . LYS A 1 158 ? -18.223 -4.676  0.899   1.00 14.66 ?  159 LYS A C    1 
ATOM   1254 O  O    . LYS A 1 158 ? -17.542 -4.282  -0.047  1.00 15.98 ?  159 LYS A O    1 
ATOM   1255 C  CB   . LYS A 1 158 ? -20.642 -3.752  0.983   1.00 17.58 ?  159 LYS A CB   1 
ATOM   1256 C  CG   . LYS A 1 158 ? -20.278 -2.416  0.160   1.00 23.82 ?  159 LYS A CG   1 
ATOM   1257 C  CD   . LYS A 1 158 ? -20.735 -2.388  -1.397  1.00 30.49 ?  159 LYS A CD   1 
ATOM   1258 C  CE   . LYS A 1 158 ? -20.166 -1.161  -2.214  1.00 29.29 ?  159 LYS A CE   1 
ATOM   1259 N  NZ   . LYS A 1 158 ? -20.988 0.064   -1.921  1.00 32.04 ?  159 LYS A NZ   1 
ATOM   1260 N  N    . VAL A 1 159 ? -17.738 -4.799  2.148   1.00 12.95 ?  160 VAL A N    1 
ATOM   1261 C  CA   . VAL A 1 159 ? -16.301 -4.593  2.399   1.00 12.64 ?  160 VAL A CA   1 
ATOM   1262 C  C    . VAL A 1 159 ? -15.492 -5.735  1.723   1.00 13.38 ?  160 VAL A C    1 
ATOM   1263 O  O    . VAL A 1 159 ? -14.542 -5.478  0.966   1.00 13.93 ?  160 VAL A O    1 
ATOM   1264 C  CB   . VAL A 1 159 ? -16.023 -4.626  3.876   1.00 13.16 ?  160 VAL A CB   1 
ATOM   1265 C  CG1  . VAL A 1 159 ? -14.452 -4.701  4.200   1.00 14.66 ?  160 VAL A CG1  1 
ATOM   1266 C  CG2  . VAL A 1 159 ? -16.720 -3.423  4.545   1.00 14.23 ?  160 VAL A CG2  1 
ATOM   1267 N  N    . VAL A 1 160 ? -15.891 -6.997  1.944   1.00 12.83 ?  161 VAL A N    1 
ATOM   1268 C  CA   . VAL A 1 160 ? -15.130 -8.104  1.357   1.00 13.89 ?  161 VAL A CA   1 
ATOM   1269 C  C    . VAL A 1 160 ? -15.057 -8.017  -0.166  1.00 14.78 ?  161 VAL A C    1 
ATOM   1270 O  O    . VAL A 1 160 ? -14.020 -8.296  -0.797  1.00 16.54 ?  161 VAL A O    1 
ATOM   1271 C  CB   . VAL A 1 160 ? -15.771 -9.506  1.846   1.00 15.19 ?  161 VAL A CB   1 
ATOM   1272 C  CG1  . VAL A 1 160 ? -15.371 -10.708 0.966   1.00 21.32 ?  161 VAL A CG1  1 
ATOM   1273 C  CG2  . VAL A 1 160 ? -15.403 -9.568  3.358   1.00 18.08 ?  161 VAL A CG2  1 
ATOM   1274 N  N    . ASP A 1 161 ? -16.155 -7.569  -0.752  1.00 15.53 ?  162 ASP A N    1 
ATOM   1275 C  CA   . ASP A 1 161 ? -16.224 -7.585  -2.250  1.00 17.91 ?  162 ASP A CA   1 
ATOM   1276 C  C    . ASP A 1 161 ? -15.348 -6.554  -2.940  1.00 18.00 ?  162 ASP A C    1 
ATOM   1277 O  O    . ASP A 1 161 ? -15.045 -6.734  -4.163  1.00 23.29 ?  162 ASP A O    1 
ATOM   1278 C  CB   . ASP A 1 161 ? -17.631 -7.504  -2.718  1.00 19.99 ?  162 ASP A CB   1 
ATOM   1279 C  CG   . ASP A 1 161 ? -18.295 -8.856  -2.675  1.00 22.32 ?  162 ASP A CG   1 
ATOM   1280 O  OD1  . ASP A 1 161 ? -17.561 -9.913  -2.732  1.00 24.76 ?  162 ASP A OD1  1 
ATOM   1281 O  OD2  . ASP A 1 161 ? -19.529 -8.860  -2.507  1.00 24.53 ?  162 ASP A OD2  1 
ATOM   1282 N  N    . VAL A 1 162 ? -14.944 -5.480  -2.221  1.00 16.79 ?  163 VAL A N    1 
ATOM   1283 C  CA   . VAL A 1 162 ? -14.095 -4.469  -2.851  1.00 17.40 ?  163 VAL A CA   1 
ATOM   1284 C  C    . VAL A 1 162 ? -12.619 -4.764  -2.626  1.00 15.83 ?  163 VAL A C    1 
ATOM   1285 O  O    . VAL A 1 162 ? -11.751 -4.050  -3.148  1.00 17.68 ?  163 VAL A O    1 
ATOM   1286 C  CB   . VAL A 1 162 ? -14.484 -3.055  -2.231  1.00 18.25 ?  163 VAL A CB   1 
ATOM   1287 C  CG1  . VAL A 1 162 ? -13.866 -2.793  -0.928  1.00 17.94 ?  163 VAL A CG1  1 
ATOM   1288 C  CG2  . VAL A 1 162 ? -14.274 -1.838  -3.151  1.00 20.29 ?  163 VAL A CG2  1 
ATOM   1289 N  N    . LEU A 1 163 ? -12.299 -5.723  -1.725  1.00 15.99 ?  164 LEU A N    1 
ATOM   1290 C  CA   . LEU A 1 163 ? -10.863 -5.983  -1.421  1.00 15.39 ?  164 LEU A CA   1 
ATOM   1291 C  C    . LEU A 1 163 ? -9.943  -6.275  -2.567  1.00 16.08 ?  164 LEU A C    1 
ATOM   1292 O  O    . LEU A 1 163 ? -8.763  -5.883  -2.587  1.00 17.53 ?  164 LEU A O    1 
ATOM   1293 C  CB   . LEU A 1 163 ? -10.650 -6.993  -0.286  1.00 14.88 ?  164 LEU A CB   1 
ATOM   1294 C  CG   . LEU A 1 163 ? -11.389 -6.641  1.046   1.00 15.80 ?  164 LEU A CG   1 
ATOM   1295 C  CD1  . LEU A 1 163 ? -11.134 -7.783  2.049   1.00 15.16 ?  164 LEU A CD1  1 
ATOM   1296 C  CD2  . LEU A 1 163 ? -10.815 -5.340  1.625   1.00 15.31 ?  164 LEU A CD2  1 
ATOM   1297 N  N    . ASP A 1 164 ? -10.497 -6.924  -3.585  1.00 18.80 ?  165 ASP A N    1 
ATOM   1298 C  CA   . ASP A 1 164 ? -9.612  -7.253  -4.718  1.00 20.43 ?  165 ASP A CA   1 
ATOM   1299 C  C    . ASP A 1 164 ? -9.188  -5.959  -5.466  1.00 21.01 ?  165 ASP A C    1 
ATOM   1300 O  O    . ASP A 1 164 ? -8.176  -5.976  -6.227  1.00 24.66 ?  165 ASP A O    1 
ATOM   1301 C  CB   . ASP A 1 164 ? -10.351 -8.206  -5.686  1.00 22.27 ?  165 ASP A CB   1 
ATOM   1302 C  CG   . ASP A 1 164 ? -11.319 -7.454  -6.523  1.00 24.45 ?  165 ASP A CG   1 
ATOM   1303 O  OD1  . ASP A 1 164 ? -12.336 -6.904  -5.992  1.00 27.72 ?  165 ASP A OD1  1 
ATOM   1304 O  OD2  . ASP A 1 164 ? -11.057 -7.370  -7.737  1.00 32.71 ?  165 ASP A OD2  1 
ATOM   1305 N  N    . SER A 1 165 ? -9.932  -4.850  -5.277  1.00 18.77 ?  166 SER A N    1 
ATOM   1306 C  CA   . SER A 1 165 ? -9.527  -3.590  -5.925  1.00 20.03 ?  166 SER A CA   1 
ATOM   1307 C  C    . SER A 1 165 ? -8.456  -2.781  -5.149  1.00 18.66 ?  166 SER A C    1 
ATOM   1308 O  O    . SER A 1 165 ? -7.945  -1.762  -5.677  1.00 19.85 ?  166 SER A O    1 
ATOM   1309 C  CB   . SER A 1 165 ? -10.743 -2.740  -6.181  1.00 21.88 ?  166 SER A CB   1 
ATOM   1310 O  OG   . SER A 1 165 ? -11.290 -2.232  -4.985  1.00 24.08 ?  166 SER A OG   1 
ATOM   1311 N  N    . ILE A 1 166 ? -8.173  -3.235  -3.900  1.00 16.30 ?  167 ILE A N    1 
ATOM   1312 C  CA   . ILE A 1 166 ? -7.159  -2.618  -3.080  1.00 16.09 ?  167 ILE A CA   1 
ATOM   1313 C  C    . ILE A 1 166 ? -6.123  -3.666  -2.534  1.00 14.85 ?  167 ILE A C    1 
ATOM   1314 O  O    . ILE A 1 166 ? -5.731  -3.659  -1.338  1.00 15.73 ?  167 ILE A O    1 
ATOM   1315 C  CB   . ILE A 1 166 ? -7.812  -1.763  -1.897  1.00 14.13 ?  167 ILE A CB   1 
ATOM   1316 C  CG1  . ILE A 1 166 ? -8.663  -2.635  -1.002  1.00 12.92 ?  167 ILE A CG1  1 
ATOM   1317 C  CG2  . ILE A 1 166 ? -8.611  -0.550  -2.489  1.00 16.69 ?  167 ILE A CG2  1 
ATOM   1318 C  CD1  . ILE A 1 166 ? -8.645  -2.120  0.433   1.00 17.39 ?  167 ILE A CD1  1 
ATOM   1319 N  N    . LYS A 1 167 ? -5.685  -4.551  -3.432  1.00 17.44 ?  168 LYS A N    1 
ATOM   1320 C  CA   . LYS A 1 167 ? -4.928  -5.699  -3.008  1.00 17.14 ?  168 LYS A CA   1 
ATOM   1321 C  C    . LYS A 1 167 ? -3.607  -5.323  -2.361  1.00 17.19 ?  168 LYS A C    1 
ATOM   1322 O  O    . LYS A 1 167 ? -3.200  -5.955  -1.406  1.00 16.51 ?  168 LYS A O    1 
ATOM   1323 C  CB   . LYS A 1 167 ? -4.647  -6.618  -4.230  1.00 18.49 ?  168 LYS A CB   1 
ATOM   1324 C  CG   . LYS A 1 167 ? -3.903  -7.923  -3.828  1.00 18.27 ?  168 LYS A CG   1 
ATOM   1325 C  CD   . LYS A 1 167 ? -3.495  -8.774  -5.082  1.00 21.31 ?  168 LYS A CD   1 
ATOM   1326 C  CE   . LYS A 1 167 ? -2.668  -9.966  -4.628  1.00 28.12 ?  168 LYS A CE   1 
ATOM   1327 N  NZ   . LYS A 1 167 ? -2.764  -11.047 -5.680  1.00 34.54 ?  168 LYS A NZ   1 
ATOM   1328 N  N    . THR A 1 168 ? -2.970  -4.263  -2.872  1.00 14.61 ?  169 THR A N    1 
ATOM   1329 C  CA   . THR A 1 168 ? -1.603  -3.909  -2.481  1.00 16.16 ?  169 THR A CA   1 
ATOM   1330 C  C    . THR A 1 168 ? -1.535  -2.501  -1.814  1.00 14.15 ?  169 THR A C    1 
ATOM   1331 O  O    . THR A 1 168 ? -2.455  -1.679  -1.892  1.00 16.96 ?  169 THR A O    1 
ATOM   1332 C  CB   . THR A 1 168 ? -0.683  -3.878  -3.725  1.00 17.94 ?  169 THR A CB   1 
ATOM   1333 O  OG1  . THR A 1 168 ? -1.344  -3.155  -4.759  1.00 18.60 ?  169 THR A OG1  1 
ATOM   1334 C  CG2  . THR A 1 168 ? -0.449  -5.328  -4.223  1.00 16.68 ?  169 THR A CG2  1 
ATOM   1335 N  N    . LYS A 1 169 ? -0.452  -2.342  -1.081  1.00 18.22 ?  170 LYS A N    1 
ATOM   1336 C  CA   . LYS A 1 169 ? -0.129  -1.151  -0.271  1.00 18.01 ?  170 LYS A CA   1 
ATOM   1337 C  C    . LYS A 1 169 ? -0.278  0.144   -1.064  1.00 17.50 ?  170 LYS A C    1 
ATOM   1338 O  O    . LYS A 1 169 ? 0.310   0.256   -2.202  1.00 21.39 ?  170 LYS A O    1 
ATOM   1339 C  CB   . LYS A 1 169 ? 1.291   -1.317  0.284   1.00 18.24 ?  170 LYS A CB   1 
ATOM   1340 C  CG   . LYS A 1 169 ? 1.822   -0.092  1.156   1.00 20.09 ?  170 LYS A CG   1 
ATOM   1341 C  CD   . LYS A 1 169 ? 3.206   -0.366  1.684   1.00 23.43 ?  170 LYS A CD   1 
ATOM   1342 C  CE   . LYS A 1 169 ? 3.582   0.657   2.737   1.00 30.84 ?  170 LYS A CE   1 
ATOM   1343 N  NZ   . LYS A 1 169 ? 5.080   0.904   2.800   1.00 37.65 ?  170 LYS A NZ   1 
ATOM   1344 N  N    . GLY A 1 170 ? -1.094  1.062   -0.578  1.00 19.22 ?  171 GLY A N    1 
ATOM   1345 C  CA   . GLY A 1 170 ? -1.284  2.360   -1.249  1.00 20.04 ?  171 GLY A CA   1 
ATOM   1346 C  C    . GLY A 1 170 ? -2.493  2.420   -2.184  1.00 21.59 ?  171 GLY A C    1 
ATOM   1347 O  O    . GLY A 1 170 ? -2.937  3.554   -2.586  1.00 22.15 ?  171 GLY A O    1 
ATOM   1348 N  N    . LYS A 1 171 ? -3.082  1.264   -2.535  1.00 18.75 ?  172 LYS A N    1 
ATOM   1349 C  CA   . LYS A 1 171 ? -4.308  1.364   -3.279  1.00 19.34 ?  172 LYS A CA   1 
ATOM   1350 C  C    . LYS A 1 171 ? -5.523  1.856   -2.450  1.00 17.93 ?  172 LYS A C    1 
ATOM   1351 O  O    . LYS A 1 171 ? -5.684  1.485   -1.288  1.00 17.48 ?  172 LYS A O    1 
ATOM   1352 C  CB   . LYS A 1 171 ? -4.620  0.022   -3.966  1.00 19.57 ?  172 LYS A CB   1 
ATOM   1353 C  CG   . LYS A 1 171 ? -3.502  -0.368  -5.000  1.00 20.99 ?  172 LYS A CG   1 
ATOM   1354 C  CD   . LYS A 1 171 ? -3.883  -1.560  -5.879  1.00 25.77 ?  172 LYS A CD   1 
ATOM   1355 C  CE   . LYS A 1 171 ? -3.800  -1.272  -7.353  1.00 35.34 ?  172 LYS A CE   1 
ATOM   1356 N  NZ   . LYS A 1 171 ? -4.319  -2.449  -8.113  1.00 39.13 ?  172 LYS A NZ   1 
ATOM   1357 N  N    . SER A 1 172 ? -6.415  2.596   -3.076  1.00 18.22 ?  173 SER A N    1 
ATOM   1358 C  CA   . SER A 1 172 ? -7.671  3.017   -2.487  1.00 17.32 ?  173 SER A CA   1 
ATOM   1359 C  C    . SER A 1 172 ? -8.845  2.922   -3.510  1.00 16.07 ?  173 SER A C    1 
ATOM   1360 O  O    . SER A 1 172 ? -8.636  2.860   -4.791  1.00 18.76 ?  173 SER A O    1 
ATOM   1361 C  CB   . SER A 1 172 ? -7.581  4.464   -1.993  1.00 18.54 ?  173 SER A CB   1 
ATOM   1362 O  OG   . SER A 1 172 ? -7.297  5.325   -3.059  1.00 20.89 ?  173 SER A OG   1 
ATOM   1363 N  N    . ALA A 1 173 ? -10.060 2.927   -2.990  1.00 18.52 ?  174 ALA A N    1 
ATOM   1364 C  CA   . ALA A 1 173 ? -11.244 2.896   -3.815  1.00 18.39 ?  174 ALA A CA   1 
ATOM   1365 C  C    . ALA A 1 173 ? -12.360 3.685   -3.159  1.00 18.82 ?  174 ALA A C    1 
ATOM   1366 O  O    . ALA A 1 173 ? -12.454 3.737   -1.933  1.00 17.84 ?  174 ALA A O    1 
ATOM   1367 C  CB   . ALA A 1 173 ? -11.658 1.479   -4.117  1.00 20.06 ?  174 ALA A CB   1 
ATOM   1368 N  N    . ASP A 1 174 ? -13.168 4.354   -3.967  1.00 19.29 ?  175 ASP A N    1 
ATOM   1369 C  CA   . ASP A 1 174 ? -14.387 5.015   -3.443  1.00 20.56 ?  175 ASP A CA   1 
ATOM   1370 C  C    . ASP A 1 174 ? -15.178 3.971   -2.695  1.00 20.01 ?  175 ASP A C    1 
ATOM   1371 O  O    . ASP A 1 174 ? -15.203 2.756   -3.079  1.00 20.85 ?  175 ASP A O    1 
ATOM   1372 C  CB   . ASP A 1 174 ? -15.237 5.597   -4.637  1.00 22.62 ?  175 ASP A CB   1 
ATOM   1373 C  CG   . ASP A 1 174 ? -14.455 6.585   -5.456  1.00 30.39 ?  175 ASP A CG   1 
ATOM   1374 O  OD1  . ASP A 1 174 ? -13.676 7.395   -4.871  1.00 31.40 ?  175 ASP A OD1  1 
ATOM   1375 O  OD2  . ASP A 1 174 ? -14.657 6.570   -6.712  1.00 33.64 ?  175 ASP A OD2  1 
ATOM   1376 N  N    . PHE A 1 175 ? -15.696 4.385   -1.541  1.00 17.10 ?  176 PHE A N    1 
ATOM   1377 C  CA   . PHE A 1 175 ? -16.469 3.430   -0.713  1.00 14.96 ?  176 PHE A CA   1 
ATOM   1378 C  C    . PHE A 1 175 ? -17.548 4.233   0.040   1.00 15.40 ?  176 PHE A C    1 
ATOM   1379 O  O    . PHE A 1 175 ? -17.477 4.457   1.241   1.00 18.44 ?  176 PHE A O    1 
ATOM   1380 C  CB   . PHE A 1 175 ? -15.517 2.641   0.209   1.00 14.16 ?  176 PHE A CB   1 
ATOM   1381 C  CG   . PHE A 1 175 ? -16.128 1.382   0.741   1.00 15.00 ?  176 PHE A CG   1 
ATOM   1382 C  CD1  . PHE A 1 175 ? -16.399 0.288   -0.110  1.00 15.40 ?  176 PHE A CD1  1 
ATOM   1383 C  CD2  . PHE A 1 175 ? -16.465 1.268   2.074   1.00 15.05 ?  176 PHE A CD2  1 
ATOM   1384 C  CE1  . PHE A 1 175 ? -16.934 -0.867  0.413   1.00 14.08 ?  176 PHE A CE1  1 
ATOM   1385 C  CE2  . PHE A 1 175 ? -17.043 0.096   2.563   1.00 15.40 ?  176 PHE A CE2  1 
ATOM   1386 C  CZ   . PHE A 1 175 ? -17.288 -0.985  1.716   1.00 16.42 ?  176 PHE A CZ   1 
ATOM   1387 N  N    . THR A 1 176 ? -18.565 4.645   -0.693  1.00 15.86 ?  177 THR A N    1 
ATOM   1388 C  CA   . THR A 1 176 ? -19.653 5.466   -0.152  1.00 15.80 ?  177 THR A CA   1 
ATOM   1389 C  C    . THR A 1 176 ? -20.804 4.615   0.281   1.00 14.95 ?  177 THR A C    1 
ATOM   1390 O  O    . THR A 1 176 ? -20.972 3.416   -0.201  1.00 14.39 ?  177 THR A O    1 
ATOM   1391 C  CB   . THR A 1 176 ? -20.095 6.553   -1.184  1.00 16.96 ?  177 THR A CB   1 
ATOM   1392 O  OG1  . THR A 1 176 ? -20.427 5.882   -2.399  1.00 19.41 ?  177 THR A OG1  1 
ATOM   1393 C  CG2  . THR A 1 176 ? -18.967 7.563   -1.452  1.00 19.39 ?  177 THR A CG2  1 
ATOM   1394 N  N    . ASN A 1 177 ? -21.620 5.198   1.155   1.00 14.03 ?  178 ASN A N    1 
ATOM   1395 C  CA   . ASN A 1 177 ? -22.917 4.611   1.514   1.00 15.31 ?  178 ASN A CA   1 
ATOM   1396 C  C    . ASN A 1 177 ? -22.754 3.269   2.264   1.00 15.64 ?  178 ASN A C    1 
ATOM   1397 O  O    . ASN A 1 177 ? -23.676 2.433   2.250   1.00 18.06 ?  178 ASN A O    1 
ATOM   1398 C  CB   . ASN A 1 177 ? -23.844 4.495   0.280   1.00 14.90 ?  178 ASN A CB   1 
ATOM   1399 C  CG   . ASN A 1 177 ? -24.144 5.880   -0.316  1.00 14.82 ?  178 ASN A CG   1 
ATOM   1400 O  OD1  . ASN A 1 177 ? -24.780 6.744   0.325   1.00 19.51 ?  178 ASN A OD1  1 
ATOM   1401 N  ND2  . ASN A 1 177 ? -23.547 6.120   -1.467  1.00 16.88 ?  178 ASN A ND2  1 
ATOM   1402 N  N    . PHE A 1 178 ? -21.601 3.074   2.915   1.00 14.11 ?  179 PHE A N    1 
ATOM   1403 C  CA   . PHE A 1 178 ? -21.447 1.862   3.745   1.00 13.89 ?  179 PHE A CA   1 
ATOM   1404 C  C    . PHE A 1 178 ? -21.955 2.143   5.165   1.00 13.53 ?  179 PHE A C    1 
ATOM   1405 O  O    . PHE A 1 178 ? -21.555 3.133   5.780   1.00 14.63 ?  179 PHE A O    1 
ATOM   1406 C  CB   . PHE A 1 178 ? -20.013 1.419   3.849   1.00 12.75 ?  179 PHE A CB   1 
ATOM   1407 C  CG   . PHE A 1 178 ? -19.864 0.176   4.702   1.00 13.11 ?  179 PHE A CG   1 
ATOM   1408 C  CD1  . PHE A 1 178 ? -20.271 -1.076  4.187   1.00 14.12 ?  179 PHE A CD1  1 
ATOM   1409 C  CD2  . PHE A 1 178 ? -19.534 0.286   6.060   1.00 13.53 ?  179 PHE A CD2  1 
ATOM   1410 C  CE1  . PHE A 1 178 ? -20.198 -2.227  4.984   1.00 14.99 ?  179 PHE A CE1  1 
ATOM   1411 C  CE2  . PHE A 1 178 ? -19.476 -0.904  6.854   1.00 10.64 ?  179 PHE A CE2  1 
ATOM   1412 C  CZ   . PHE A 1 178 ? -19.801 -2.115  6.303   1.00 11.72 ?  179 PHE A CZ   1 
ATOM   1413 N  N    . ASP A 1 179 ? -22.846 1.276   5.681   1.00 14.22 ?  180 ASP A N    1 
ATOM   1414 C  CA   . ASP A 1 179 ? -23.448 1.512   6.996   1.00 14.18 ?  180 ASP A CA   1 
ATOM   1415 C  C    . ASP A 1 179 ? -22.775 0.662   8.057   1.00 12.68 ?  180 ASP A C    1 
ATOM   1416 O  O    . ASP A 1 179 ? -22.978 -0.566  8.090   1.00 13.38 ?  180 ASP A O    1 
ATOM   1417 C  CB   . ASP A 1 179 ? -24.937 1.122   6.922   1.00 14.75 ?  180 ASP A CB   1 
ATOM   1418 C  CG   . ASP A 1 179 ? -25.737 1.498   8.137   1.00 17.86 ?  180 ASP A CG   1 
ATOM   1419 O  OD1  . ASP A 1 179 ? -25.184 1.773   9.214   1.00 15.70 ?  180 ASP A OD1  1 
ATOM   1420 O  OD2  . ASP A 1 179 ? -26.989 1.576   8.035   1.00 25.82 ?  180 ASP A OD2  1 
ATOM   1421 N  N    . PRO A 1 180 ? -21.993 1.304   8.961   1.00 12.11 ?  181 PRO A N    1 
ATOM   1422 C  CA   . PRO A 1 180 ? -21.248 0.439   9.923   1.00 12.24 ?  181 PRO A CA   1 
ATOM   1423 C  C    . PRO A 1 180 ? -22.189 -0.206  10.956  1.00 11.22 ?  181 PRO A C    1 
ATOM   1424 O  O    . PRO A 1 180 ? -21.743 -1.074  11.762  1.00 10.74 ?  181 PRO A O    1 
ATOM   1425 C  CB   . PRO A 1 180 ? -20.233 1.424   10.552  1.00 13.31 ?  181 PRO A CB   1 
ATOM   1426 C  CG   . PRO A 1 180 ? -21.003 2.813   10.523  1.00 13.68 ?  181 PRO A CG   1 
ATOM   1427 C  CD   . PRO A 1 180 ? -21.726 2.748   9.158   1.00 13.38 ?  181 PRO A CD   1 
ATOM   1428 N  N    . ARG A 1 181 ? -23.484 0.204   10.990  1.00 10.35 ?  182 ARG A N    1 
ATOM   1429 C  CA   . ARG A 1 181 ? -24.393 -0.535  11.963  1.00 12.05 ?  182 ARG A CA   1 
ATOM   1430 C  C    . ARG A 1 181 ? -24.468 -2.044  11.629  1.00 11.61 ?  182 ARG A C    1 
ATOM   1431 O  O    . ARG A 1 181 ? -24.836 -2.845  12.507  1.00 13.27 ?  182 ARG A O    1 
ATOM   1432 C  CB   . ARG A 1 181 ? -25.822 0.053   11.941  1.00 13.06 ?  182 ARG A CB   1 
ATOM   1433 C  CG   . ARG A 1 181 ? -25.761 1.505   12.546  1.00 13.33 ?  182 ARG A CG   1 
ATOM   1434 C  CD   . ARG A 1 181 ? -27.090 2.238   12.426  1.00 17.26 ?  182 ARG A CD   1 
ATOM   1435 N  NE   . ARG A 1 181 ? -27.462 2.423   11.017  1.00 16.52 ?  182 ARG A NE   1 
ATOM   1436 C  CZ   . ARG A 1 181 ? -28.546 3.116   10.667  1.00 18.38 ?  182 ARG A CZ   1 
ATOM   1437 N  NH1  . ARG A 1 181 ? -29.291 3.696   11.638  1.00 21.79 ?  182 ARG A NH1  1 
ATOM   1438 N  NH2  . ARG A 1 181 ? -28.859 3.244   9.373   1.00 22.29 ?  182 ARG A NH2  1 
ATOM   1439 N  N    . GLY A 1 182 ? -24.203 -2.390  10.362  1.00 11.66 ?  183 GLY A N    1 
ATOM   1440 C  CA   . GLY A 1 182 ? -24.262 -3.800  9.880   1.00 11.82 ?  183 GLY A CA   1 
ATOM   1441 C  C    . GLY A 1 182 ? -23.104 -4.656  10.433  1.00 13.93 ?  183 GLY A C    1 
ATOM   1442 O  O    . GLY A 1 182 ? -23.043 -5.879  10.159  1.00 14.54 ?  183 GLY A O    1 
ATOM   1443 N  N    . LEU A 1 183 ? -22.200 -4.047  11.211  1.00 12.04 ?  184 LEU A N    1 
ATOM   1444 C  CA   . LEU A 1 183 ? -21.063 -4.797  11.825  1.00 11.68 ?  184 LEU A CA   1 
ATOM   1445 C  C    . LEU A 1 183 ? -21.207 -4.989  13.339  1.00 11.18 ?  184 LEU A C    1 
ATOM   1446 O  O    . LEU A 1 183 ? -20.304 -5.578  13.932  1.00 13.47 ?  184 LEU A O    1 
ATOM   1447 C  CB   . LEU A 1 183 ? -19.755 -4.024  11.563  1.00 11.39 ?  184 LEU A CB   1 
ATOM   1448 C  CG   . LEU A 1 183 ? -19.451 -3.829  10.055  1.00 11.74 ?  184 LEU A CG   1 
ATOM   1449 C  CD1  . LEU A 1 183 ? -18.197 -3.043  9.895   1.00 13.66 ?  184 LEU A CD1  1 
ATOM   1450 C  CD2  . LEU A 1 183 ? -19.212 -5.175  9.437   1.00 15.10 ?  184 LEU A CD2  1 
ATOM   1451 N  N    . LEU A 1 184 ? -22.323 -4.522  13.942  1.00 10.98 ?  185 LEU A N    1 
ATOM   1452 C  CA   . LEU A 1 184 ? -22.461 -4.524  15.407  1.00 10.25 ?  185 LEU A CA   1 
ATOM   1453 C  C    . LEU A 1 184 ? -23.218 -5.799  15.835  1.00 13.19 ?  185 LEU A C    1 
ATOM   1454 O  O    . LEU A 1 184 ? -24.225 -6.210  15.191  1.00 16.61 ?  185 LEU A O    1 
ATOM   1455 C  CB   . LEU A 1 184 ? -23.293 -3.319  15.913  1.00 10.78 ?  185 LEU A CB   1 
ATOM   1456 C  CG   . LEU A 1 184 ? -22.697 -1.965  15.519  1.00 11.28 ?  185 LEU A CG   1 
ATOM   1457 C  CD1  . LEU A 1 184 ? -23.544 -0.743  15.933  1.00 13.34 ?  185 LEU A CD1  1 
ATOM   1458 C  CD2  . LEU A 1 184 ? -21.245 -1.892  16.051  1.00 11.92 ?  185 LEU A CD2  1 
ATOM   1459 N  N    . PRO A 1 185 ? -22.832 -6.372  16.994  1.00 10.99 ?  186 PRO A N    1 
ATOM   1460 C  CA   . PRO A 1 185 ? -23.606 -7.521  17.525  1.00 11.94 ?  186 PRO A CA   1 
ATOM   1461 C  C    . PRO A 1 185 ? -24.889 -7.005  18.199  1.00 13.07 ?  186 PRO A C    1 
ATOM   1462 O  O    . PRO A 1 185 ? -25.115 -5.758  18.343  1.00 14.15 ?  186 PRO A O    1 
ATOM   1463 C  CB   . PRO A 1 185 ? -22.641 -8.117  18.559  1.00 11.83 ?  186 PRO A CB   1 
ATOM   1464 C  CG   . PRO A 1 185 ? -21.887 -6.883  19.110  1.00 9.87  ?  186 PRO A CG   1 
ATOM   1465 C  CD   . PRO A 1 185 ? -21.698 -5.977  17.839  1.00 10.67 ?  186 PRO A CD   1 
ATOM   1466 N  N    . GLU A 1 186 ? -25.718 -7.943  18.687  1.00 14.38 ?  187 GLU A N    1 
ATOM   1467 C  CA   . GLU A 1 186 ? -26.981 -7.540  19.277  1.00 14.50 ?  187 GLU A CA   1 
ATOM   1468 C  C    . GLU A 1 186 ? -26.729 -6.775  20.572  1.00 14.14 ?  187 GLU A C    1 
ATOM   1469 O  O    . GLU A 1 186 ? -27.351 -5.707  20.791  1.00 17.55 ?  187 GLU A O    1 
ATOM   1470 C  CB   . GLU A 1 186 ? -27.759 -8.855  19.534  1.00 15.99 ?  187 GLU A CB   1 
ATOM   1471 C  CG   . GLU A 1 186 ? -28.900 -8.715  20.428  1.00 22.29 ?  187 GLU A CG   1 
ATOM   1472 C  CD   . GLU A 1 186 ? -29.588 -10.104 20.717  1.00 20.11 ?  187 GLU A CD   1 
ATOM   1473 O  OE1  . GLU A 1 186 ? -29.384 -11.096 19.984  1.00 22.09 ?  187 GLU A OE1  1 
ATOM   1474 O  OE2  . GLU A 1 186 ? -30.322 -10.126 21.759  1.00 29.38 ?  187 GLU A OE2  1 
ATOM   1475 N  N    . SER A 1 187 ? -25.843 -7.328  21.435  1.00 12.36 ?  188 SER A N    1 
ATOM   1476 C  CA   . SER A 1 187 ? -25.660 -6.717  22.758  1.00 12.47 ?  188 SER A CA   1 
ATOM   1477 C  C    . SER A 1 187 ? -24.514 -5.662  22.704  1.00 11.85 ?  188 SER A C    1 
ATOM   1478 O  O    . SER A 1 187 ? -23.488 -5.900  22.069  1.00 13.29 ?  188 SER A O    1 
ATOM   1479 C  CB   . SER A 1 187 ? -25.226 -7.781  23.774  1.00 14.43 ?  188 SER A CB   1 
ATOM   1480 O  OG   . SER A 1 187 ? -25.003 -7.170  25.060  1.00 16.40 ?  188 SER A OG   1 
ATOM   1481 N  N    . LEU A 1 188 ? -24.678 -4.573  23.466  1.00 11.79 ?  189 LEU A N    1 
ATOM   1482 C  CA   . LEU A 1 188 ? -23.625 -3.561  23.635  1.00 12.24 ?  189 LEU A CA   1 
ATOM   1483 C  C    . LEU A 1 188 ? -22.974 -3.675  25.058  1.00 11.91 ?  189 LEU A C    1 
ATOM   1484 O  O    . LEU A 1 188 ? -22.284 -2.763  25.502  1.00 13.83 ?  189 LEU A O    1 
ATOM   1485 C  CB   . LEU A 1 188 ? -24.092 -2.079  23.311  1.00 12.85 ?  189 LEU A CB   1 
ATOM   1486 C  CG   . LEU A 1 188 ? -24.579 -1.813  21.894  1.00 16.27 ?  189 LEU A CG   1 
ATOM   1487 C  CD1  . LEU A 1 188 ? -25.127 -0.308  21.787  1.00 16.98 ?  189 LEU A CD1  1 
ATOM   1488 C  CD2  . LEU A 1 188 ? -23.453 -2.076  20.888  1.00 17.56 ?  189 LEU A CD2  1 
ATOM   1489 N  N    . ASP A 1 189 ? -23.104 -4.834  25.706  1.00 13.01 ?  190 ASP A N    1 
ATOM   1490 C  CA   . ASP A 1 189 ? -22.358 -5.079  26.967  1.00 13.07 ?  190 ASP A CA   1 
ATOM   1491 C  C    . ASP A 1 189 ? -20.839 -5.008  26.663  1.00 12.21 ?  190 ASP A C    1 
ATOM   1492 O  O    . ASP A 1 189 ? -20.382 -5.523  25.640  1.00 11.69 ?  190 ASP A O    1 
ATOM   1493 C  CB   . ASP A 1 189 ? -22.660 -6.444  27.558  1.00 13.72 ?  190 ASP A CB   1 
ATOM   1494 C  CG   . ASP A 1 189 ? -24.064 -6.521  28.219  1.00 18.62 ?  190 ASP A CG   1 
ATOM   1495 O  OD1  . ASP A 1 189 ? -24.666 -5.460  28.548  1.00 23.81 ?  190 ASP A OD1  1 
ATOM   1496 O  OD2  . ASP A 1 189 ? -24.558 -7.646  28.422  1.00 24.00 ?  190 ASP A OD2  1 
ATOM   1497 N  N    . TYR A 1 190 ? -20.057 -4.359  27.552  1.00 10.35 ?  191 TYR A N    1 
ATOM   1498 C  CA   . TYR A 1 190 ? -18.642 -4.166  27.206  1.00 9.43  ?  191 TYR A CA   1 
ATOM   1499 C  C    . TYR A 1 190 ? -17.721 -4.234  28.452  1.00 9.12  ?  191 TYR A C    1 
ATOM   1500 O  O    . TYR A 1 190 ? -18.187 -4.097  29.628  1.00 9.95  ?  191 TYR A O    1 
ATOM   1501 C  CB   . TYR A 1 190 ? -18.499 -2.786  26.536  1.00 10.89 ?  191 TYR A CB   1 
ATOM   1502 C  CG   . TYR A 1 190 ? -18.903 -1.621  27.468  1.00 9.56  ?  191 TYR A CG   1 
ATOM   1503 C  CD1  . TYR A 1 190 ? -17.980 -0.993  28.357  1.00 10.17 ?  191 TYR A CD1  1 
ATOM   1504 C  CD2  . TYR A 1 190 ? -20.203 -1.113  27.424  1.00 9.46  ?  191 TYR A CD2  1 
ATOM   1505 C  CE1  . TYR A 1 190 ? -18.384 0.055   29.209  1.00 9.94  ?  191 TYR A CE1  1 
ATOM   1506 C  CE2  . TYR A 1 190 ? -20.619 -0.081  28.217  1.00 12.35 ?  191 TYR A CE2  1 
ATOM   1507 C  CZ   . TYR A 1 190 ? -19.707 0.530   29.126  1.00 11.11 ?  191 TYR A CZ   1 
ATOM   1508 O  OH   . TYR A 1 190 ? -20.091 1.569   29.976  1.00 13.01 ?  191 TYR A OH   1 
ATOM   1509 N  N    . TRP A 1 191 ? -16.439 -4.451  28.139  1.00 8.68  ?  192 TRP A N    1 
ATOM   1510 C  CA   . TRP A 1 191 ? -15.383 -4.134  29.100  1.00 7.41  ?  192 TRP A CA   1 
ATOM   1511 C  C    . TRP A 1 191 ? -14.670 -2.837  28.725  1.00 7.45  ?  192 TRP A C    1 
ATOM   1512 O  O    . TRP A 1 191 ? -14.718 -2.472  27.544  1.00 8.55  ?  192 TRP A O    1 
ATOM   1513 C  CB   . TRP A 1 191 ? -14.330 -5.223  29.076  1.00 9.24  ?  192 TRP A CB   1 
ATOM   1514 C  CG   . TRP A 1 191 ? -14.836 -6.599  29.459  1.00 8.09  ?  192 TRP A CG   1 
ATOM   1515 C  CD1  . TRP A 1 191 ? -15.028 -7.045  30.752  1.00 10.40 ?  192 TRP A CD1  1 
ATOM   1516 C  CD2  . TRP A 1 191 ? -15.087 -7.711  28.607  1.00 8.87  ?  192 TRP A CD2  1 
ATOM   1517 N  NE1  . TRP A 1 191 ? -15.425 -8.389  30.743  1.00 11.25 ?  192 TRP A NE1  1 
ATOM   1518 C  CE2  . TRP A 1 191 ? -15.479 -8.811  29.434  1.00 10.60 ?  192 TRP A CE2  1 
ATOM   1519 C  CE3  . TRP A 1 191 ? -15.038 -7.896  27.210  1.00 9.90  ?  192 TRP A CE3  1 
ATOM   1520 C  CZ2  . TRP A 1 191 ? -15.785 -10.099 28.894  1.00 10.58 ?  192 TRP A CZ2  1 
ATOM   1521 C  CZ3  . TRP A 1 191 ? -15.304 -9.192  26.690  1.00 11.40 ?  192 TRP A CZ3  1 
ATOM   1522 C  CH2  . TRP A 1 191 ? -15.708 -10.243 27.531  1.00 10.50 ?  192 TRP A CH2  1 
ATOM   1523 N  N    . THR A 1 192 ? -14.118 -2.136  29.702  1.00 7.07  ?  193 THR A N    1 
ATOM   1524 C  CA   . THR A 1 192 ? -13.405 -0.933  29.347  1.00 7.65  ?  193 THR A CA   1 
ATOM   1525 C  C    . THR A 1 192 ? -12.125 -0.716  30.230  1.00 7.77  ?  193 THR A C    1 
ATOM   1526 O  O    . THR A 1 192 ? -12.074 -1.176  31.414  1.00 9.80  ?  193 THR A O    1 
ATOM   1527 C  CB   . THR A 1 192 ? -14.330 0.356   29.448  1.00 8.35  ?  193 THR A CB   1 
ATOM   1528 O  OG1  . THR A 1 192 ? -13.629 1.540   29.018  1.00 8.94  ?  193 THR A OG1  1 
ATOM   1529 C  CG2  . THR A 1 192 ? -14.802 0.598   30.879  1.00 9.91  ?  193 THR A CG2  1 
ATOM   1530 N  N    . TYR A 1 193 ? -11.079 -0.111  29.587  1.00 7.72  ?  194 TYR A N    1 
ATOM   1531 C  CA   . TYR A 1 193 ? -9.861  0.155   30.332  1.00 7.29  ?  194 TYR A CA   1 
ATOM   1532 C  C    . TYR A 1 193 ? -9.068  1.186   29.560  1.00 7.60  ?  194 TYR A C    1 
ATOM   1533 O  O    . TYR A 1 193 ? -9.302  1.385   28.380  1.00 8.43  ?  194 TYR A O    1 
ATOM   1534 C  CB   . TYR A 1 193 ? -9.005  -1.139  30.564  1.00 7.99  ?  194 TYR A CB   1 
ATOM   1535 C  CG   . TYR A 1 193 ? -8.338  -1.606  29.269  1.00 6.83  ?  194 TYR A CG   1 
ATOM   1536 C  CD1  . TYR A 1 193 ? -9.020  -2.364  28.261  1.00 8.54  ?  194 TYR A CD1  1 
ATOM   1537 C  CD2  . TYR A 1 193 ? -6.998  -1.228  29.027  1.00 8.28  ?  194 TYR A CD2  1 
ATOM   1538 C  CE1  . TYR A 1 193 ? -8.406  -2.679  27.086  1.00 7.11  ?  194 TYR A CE1  1 
ATOM   1539 C  CE2  . TYR A 1 193 ? -6.306  -1.594  27.802  1.00 8.78  ?  194 TYR A CE2  1 
ATOM   1540 C  CZ   . TYR A 1 193 ? -7.058  -2.329  26.839  1.00 6.47  ?  194 TYR A CZ   1 
ATOM   1541 O  OH   . TYR A 1 193 ? -6.367  -2.607  25.687  1.00 7.61  ?  194 TYR A OH   1 
ATOM   1542 N  N    . PRO A 1 194 ? -8.147  1.908   30.233  1.00 7.63  ?  195 PRO A N    1 
ATOM   1543 C  CA   . PRO A 1 194 ? -7.324  2.894   29.545  1.00 7.56  ?  195 PRO A CA   1 
ATOM   1544 C  C    . PRO A 1 194 ? -6.100  2.238   28.893  1.00 7.73  ?  195 PRO A C    1 
ATOM   1545 O  O    . PRO A 1 194 ? -5.346  1.509   29.552  1.00 8.75  ?  195 PRO A O    1 
ATOM   1546 C  CB   . PRO A 1 194 ? -6.819  3.815   30.690  1.00 8.82  ?  195 PRO A CB   1 
ATOM   1547 C  CG   . PRO A 1 194 ? -6.783  2.950   31.917  1.00 9.99  ?  195 PRO A CG   1 
ATOM   1548 C  CD   . PRO A 1 194 ? -7.966  1.921   31.696  1.00 9.09  ?  195 PRO A CD   1 
ATOM   1549 N  N    . GLY A 1 195 ? -5.864  2.577   27.598  1.00 6.40  ?  196 GLY A N    1 
ATOM   1550 C  CA   . GLY A 1 195 ? -4.738  1.910   26.872  1.00 8.45  ?  196 GLY A CA   1 
ATOM   1551 C  C    . GLY A 1 195 ? -4.159  2.792   25.803  1.00 6.36  ?  196 GLY A C    1 
ATOM   1552 O  O    . GLY A 1 195 ? -4.090  4.046   25.931  1.00 7.44  ?  196 GLY A O    1 
ATOM   1553 N  N    . SER A 1 196 ? -3.766  2.138   24.688  1.00 7.71  ?  197 SER A N    1 
ATOM   1554 C  CA   . SER A 1 196 ? -2.942  2.829   23.689  1.00 7.40  ?  197 SER A CA   1 
ATOM   1555 C  C    . SER A 1 196 ? -3.380  2.432   22.256  1.00 6.66  ?  197 SER A C    1 
ATOM   1556 O  O    . SER A 1 196 ? -4.144  1.425   22.095  1.00 7.37  ?  197 SER A O    1 
ATOM   1557 C  CB   . SER A 1 196 ? -1.489  2.424   23.843  1.00 9.71  ?  197 SER A CB   1 
ATOM   1558 O  OG   . SER A 1 196 ? -1.271  1.053   23.443  1.00 8.10  ?  197 SER A OG   1 
ATOM   1559 N  N    . LEU A 1 197 ? -2.803  3.090   21.257  1.00 8.01  ?  198 LEU A N    1 
ATOM   1560 C  CA   . LEU A 1 197 ? -2.885  2.496   19.899  1.00 7.22  ?  198 LEU A CA   1 
ATOM   1561 C  C    . LEU A 1 197 ? -2.181  1.152   19.969  1.00 7.37  ?  198 LEU A C    1 
ATOM   1562 O  O    . LEU A 1 197 ? -1.155  0.996   20.715  1.00 7.67  ?  198 LEU A O    1 
ATOM   1563 C  CB   . LEU A 1 197 ? -2.129  3.345   18.912  1.00 9.71  ?  198 LEU A CB   1 
ATOM   1564 C  CG   . LEU A 1 197 ? -2.471  4.817   18.825  1.00 15.78 ?  198 LEU A CG   1 
ATOM   1565 C  CD1  . LEU A 1 197 ? -1.612  5.478   17.676  1.00 17.37 ?  198 LEU A CD1  1 
ATOM   1566 C  CD2  . LEU A 1 197 ? -3.766  5.364   18.888  1.00 16.22 ?  198 LEU A CD2  1 
ATOM   1567 N  N    . THR A 1 198 ? -2.619  0.169   19.146  1.00 7.73  ?  199 THR A N    1 
ATOM   1568 C  CA   . THR A 1 198 ? -1.955  -1.104  19.116  1.00 6.93  ?  199 THR A CA   1 
ATOM   1569 C  C    . THR A 1 198 ? -0.933  -1.166  17.991  1.00 9.21  ?  199 THR A C    1 
ATOM   1570 O  O    . THR A 1 198 ? -0.288  -2.223  17.831  1.00 8.58  ?  199 THR A O    1 
ATOM   1571 C  CB   . THR A 1 198 ? -2.988  -2.240  18.957  1.00 7.33  ?  199 THR A CB   1 
ATOM   1572 O  OG1  . THR A 1 198 ? -3.542  -2.182  17.648  1.00 8.24  ?  199 THR A OG1  1 
ATOM   1573 C  CG2  . THR A 1 198 ? -4.011  -2.266  20.081  1.00 8.63  ?  199 THR A CG2  1 
ATOM   1574 N  N    . THR A 1 199 ? -0.822  -0.076  17.208  1.00 9.43  ?  200 THR A N    1 
ATOM   1575 C  CA   . THR A 1 199 ? 0.251   -0.008  16.187  1.00 9.24  ?  200 THR A CA   1 
ATOM   1576 C  C    . THR A 1 199 ? 1.086   1.208   16.495  1.00 9.47  ?  200 THR A C    1 
ATOM   1577 O  O    . THR A 1 199 ? 0.606   2.158   17.134  1.00 9.94  ?  200 THR A O    1 
ATOM   1578 C  CB   . THR A 1 199 ? -0.309  0.269   14.789  1.00 10.04 ?  200 THR A CB   1 
ATOM   1579 O  OG1  . THR A 1 199 ? -1.084  1.489   14.849  1.00 14.76 ?  200 THR A OG1  1 
ATOM   1580 C  CG2  . THR A 1 199 ? -1.180  -0.822  14.310  1.00 11.17 ?  200 THR A CG2  1 
ATOM   1581 N  N    . PRO A 1 200 ? 2.365   1.197   16.041  1.00 9.63  ?  201 PRO A N    1 
ATOM   1582 C  CA   . PRO A 1 200 ? 3.154   2.465   16.165  1.00 10.22 ?  201 PRO A CA   1 
ATOM   1583 C  C    . PRO A 1 200 ? 2.247   3.640   15.643  1.00 10.01 ?  201 PRO A C    1 
ATOM   1584 O  O    . PRO A 1 200 ? 1.564   3.524   14.576  1.00 12.80 ?  201 PRO A O    1 
ATOM   1585 C  CB   . PRO A 1 200 ? 4.355   2.229   15.230  1.00 12.00 ?  201 PRO A CB   1 
ATOM   1586 C  CG   . PRO A 1 200 ? 4.531   0.676   15.382  1.00 11.61 ?  201 PRO A CG   1 
ATOM   1587 C  CD   . PRO A 1 200 ? 3.128   0.109   15.377  1.00 10.54 ?  201 PRO A CD   1 
ATOM   1588 N  N    . PRO A 1 201 ? 2.359   4.819   16.264  1.00 11.02 ?  202 PRO A N    1 
ATOM   1589 C  CA   . PRO A 1 201 ? 3.320   5.218   17.320  1.00 11.58 ?  202 PRO A CA   1 
ATOM   1590 C  C    . PRO A 1 201 ? 2.934   4.790   18.785  1.00 9.46  ?  202 PRO A C    1 
ATOM   1591 O  O    . PRO A 1 201 ? 3.573   5.240   19.752  1.00 10.86 ?  202 PRO A O    1 
ATOM   1592 C  CB   . PRO A 1 201 ? 3.363   6.754   17.157  1.00 11.57 ?  202 PRO A CB   1 
ATOM   1593 C  CG   . PRO A 1 201 ? 1.947   7.095   16.652  1.00 13.73 ?  202 PRO A CG   1 
ATOM   1594 C  CD   . PRO A 1 201 ? 1.582   5.979   15.727  1.00 10.00 ?  202 PRO A CD   1 
ATOM   1595 N  N    . LEU A 1 202 ? 1.928   3.911   18.933  1.00 9.81  ?  203 LEU A N    1 
ATOM   1596 C  CA   . LEU A 1 202 ? 1.668   3.253   20.262  1.00 8.78  ?  203 LEU A CA   1 
ATOM   1597 C  C    . LEU A 1 202 ? 1.250   4.311   21.318  1.00 8.56  ?  203 LEU A C    1 
ATOM   1598 O  O    . LEU A 1 202 ? 1.440   4.090   22.526  1.00 9.49  ?  203 LEU A O    1 
ATOM   1599 C  CB   . LEU A 1 202 ? 2.886   2.405   20.750  1.00 9.21  ?  203 LEU A CB   1 
ATOM   1600 C  CG   . LEU A 1 202 ? 3.176   1.219   19.740  1.00 10.16 ?  203 LEU A CG   1 
ATOM   1601 C  CD1  . LEU A 1 202 ? 4.463   0.579   20.224  1.00 12.08 ?  203 LEU A CD1  1 
ATOM   1602 C  CD2  . LEU A 1 202 ? 2.058   0.133   19.724  1.00 11.36 ?  203 LEU A CD2  1 
ATOM   1603 N  N    . LEU A 1 203 ? 0.676   5.448   20.874  1.00 8.29  ?  204 LEU A N    1 
ATOM   1604 C  CA   . LEU A 1 203 ? 0.383   6.542   21.816  1.00 9.59  ?  204 LEU A CA   1 
ATOM   1605 C  C    . LEU A 1 203 ? -0.687  6.138   22.865  1.00 8.95  ?  204 LEU A C    1 
ATOM   1606 O  O    . LEU A 1 203 ? -1.646  5.422   22.550  1.00 9.09  ?  204 LEU A O    1 
ATOM   1607 C  CB   . LEU A 1 203 ? -0.108  7.773   21.084  1.00 10.01 ?  204 LEU A CB   1 
ATOM   1608 C  CG   . LEU A 1 203 ? 0.942   8.338   20.122  1.00 12.92 ?  204 LEU A CG   1 
ATOM   1609 C  CD1  . LEU A 1 203 ? 0.436   9.529   19.214  1.00 14.21 ?  204 LEU A CD1  1 
ATOM   1610 C  CD2  . LEU A 1 203 ? 2.184   8.895   20.882  1.00 16.30 ?  204 LEU A CD2  1 
ATOM   1611 N  N    . GLU A 1 204 ? -0.505  6.616   24.087  1.00 9.64  ?  205 GLU A N    1 
ATOM   1612 C  CA   . GLU A 1 204 ? -1.327  6.232   25.207  1.00 8.64  ?  205 GLU A CA   1 
ATOM   1613 C  C    . GLU A 1 204 ? -2.493  7.211   25.318  1.00 9.39  ?  205 GLU A C    1 
ATOM   1614 O  O    . GLU A 1 204 ? -2.572  7.946   26.309  1.00 11.36 ?  205 GLU A O    1 
ATOM   1615 C  CB   . GLU A 1 204 ? -0.464  6.077   26.505  1.00 8.79  ?  205 GLU A CB   1 
ATOM   1616 C  CG   . GLU A 1 204 ? 0.466   4.865   26.322  1.00 12.33 ?  205 GLU A CG   1 
ATOM   1617 C  CD   . GLU A 1 204 ? 1.416   4.605   27.505  1.00 10.31 ?  205 GLU A CD   1 
ATOM   1618 O  OE1  . GLU A 1 204 ? 1.678   5.561   28.311  1.00 13.98 ?  205 GLU A OE1  1 
ATOM   1619 O  OE2  . GLU A 1 204 ? 1.793   3.411   27.650  1.00 12.11 ?  205 GLU A OE2  1 
ATOM   1620 N  N    . CYS A 1 205 ? -3.402  7.117   24.374  1.00 8.88  ?  206 CYS A N    1 
ATOM   1621 C  CA   . CYS A 1 205 ? -4.446  8.115   24.198  1.00 8.05  ?  206 CYS A CA   1 
ATOM   1622 C  C    . CYS A 1 205 ? -5.800  7.464   24.059  1.00 8.42  ?  206 CYS A C    1 
ATOM   1623 O  O    . CYS A 1 205 ? -6.784  8.198   23.755  1.00 10.07 ?  206 CYS A O    1 
ATOM   1624 C  CB   . CYS A 1 205 ? -4.166  8.985   22.981  1.00 9.05  ?  206 CYS A CB   1 
ATOM   1625 S  SG   . CYS A 1 205 ? -4.095  7.997   21.425  1.00 10.85 ?  206 CYS A SG   1 
ATOM   1626 N  N    . VAL A 1 206 ? -5.917  6.149   24.352  1.00 8.02  ?  207 VAL A N    1 
ATOM   1627 C  CA   . VAL A 1 206 ? -7.177  5.446   24.023  1.00 7.18  ?  207 VAL A CA   1 
ATOM   1628 C  C    . VAL A 1 206 ? -7.962  4.968   25.228  1.00 7.53  ?  207 VAL A C    1 
ATOM   1629 O  O    . VAL A 1 206 ? -7.405  4.309   26.090  1.00 9.16  ?  207 VAL A O    1 
ATOM   1630 C  CB   . VAL A 1 206 ? -6.928  4.175   23.150  1.00 6.95  ?  207 VAL A CB   1 
ATOM   1631 C  CG1  . VAL A 1 206 ? -8.288  3.486   22.781  1.00 8.87  ?  207 VAL A CG1  1 
ATOM   1632 C  CG2  . VAL A 1 206 ? -6.113  4.530   21.899  1.00 8.68  ?  207 VAL A CG2  1 
ATOM   1633 N  N    . THR A 1 207 ? -9.276  5.298   25.261  1.00 7.34  ?  208 THR A N    1 
ATOM   1634 C  CA   . THR A 1 207 ? -10.221 4.574   26.115  1.00 6.95  ?  208 THR A CA   1 
ATOM   1635 C  C    . THR A 1 207 ? -10.732 3.388   25.290  1.00 6.74  ?  208 THR A C    1 
ATOM   1636 O  O    . THR A 1 207 ? -11.422 3.605   24.272  1.00 7.20  ?  208 THR A O    1 
ATOM   1637 C  CB   . THR A 1 207 ? -11.416 5.476   26.597  1.00 9.36  ?  208 THR A CB   1 
ATOM   1638 O  OG1  . THR A 1 207 ? -10.848 6.597   27.357  1.00 8.66  ?  208 THR A OG1  1 
ATOM   1639 C  CG2  . THR A 1 207 ? -12.346 4.690   27.497  1.00 9.10  ?  208 THR A CG2  1 
ATOM   1640 N  N    . TRP A 1 208 ? -10.353 2.180   25.697  1.00 6.96  ?  209 TRP A N    1 
ATOM   1641 C  CA   . TRP A 1 208 ? -10.815 0.992   24.989  1.00 6.29  ?  209 TRP A CA   1 
ATOM   1642 C  C    . TRP A 1 208 ? -12.205 0.582   25.498  1.00 6.37  ?  209 TRP A C    1 
ATOM   1643 O  O    . TRP A 1 208 ? -12.435 0.513   26.744  1.00 7.61  ?  209 TRP A O    1 
ATOM   1644 C  CB   . TRP A 1 208 ? -9.809  -0.215  25.212  1.00 7.44  ?  209 TRP A CB   1 
ATOM   1645 C  CG   . TRP A 1 208 ? -8.703  -0.080  24.241  1.00 6.17  ?  209 TRP A CG   1 
ATOM   1646 C  CD1  . TRP A 1 208 ? -7.483  0.543   24.437  1.00 6.60  ?  209 TRP A CD1  1 
ATOM   1647 C  CD2  . TRP A 1 208 ? -8.749  -0.475  22.855  1.00 6.73  ?  209 TRP A CD2  1 
ATOM   1648 N  NE1  . TRP A 1 208 ? -6.762  0.579   23.264  1.00 7.89  ?  209 TRP A NE1  1 
ATOM   1649 C  CE2  . TRP A 1 208 ? -7.504  -0.061  22.271  1.00 6.36  ?  209 TRP A CE2  1 
ATOM   1650 C  CE3  . TRP A 1 208 ? -9.741  -1.115  22.029  1.00 6.80  ?  209 TRP A CE3  1 
ATOM   1651 C  CZ2  . TRP A 1 208 ? -7.200  -0.284  20.894  1.00 8.15  ?  209 TRP A CZ2  1 
ATOM   1652 C  CZ3  . TRP A 1 208 ? -9.448  -1.387  20.725  1.00 7.72  ?  209 TRP A CZ3  1 
ATOM   1653 C  CH2  . TRP A 1 208 ? -8.178  -0.962  20.137  1.00 7.56  ?  209 TRP A CH2  1 
ATOM   1654 N  N    . ILE A 1 209 ? -13.074 0.218   24.544  1.00 7.11  ?  210 ILE A N    1 
ATOM   1655 C  CA   . ILE A 1 209 ? -14.385 -0.307  24.912  1.00 6.51  ?  210 ILE A CA   1 
ATOM   1656 C  C    . ILE A 1 209 ? -14.522 -1.576  24.062  1.00 7.26  ?  210 ILE A C    1 
ATOM   1657 O  O    . ILE A 1 209 ? -14.655 -1.475  22.832  1.00 8.18  ?  210 ILE A O    1 
ATOM   1658 C  CB   . ILE A 1 209 ? -15.496 0.754   24.554  1.00 8.05  ?  210 ILE A CB   1 
ATOM   1659 C  CG1  . ILE A 1 209 ? -15.266 1.982   25.410  1.00 9.04  ?  210 ILE A CG1  1 
ATOM   1660 C  CG2  . ILE A 1 209 ? -16.940 0.128   24.771  1.00 9.80  ?  210 ILE A CG2  1 
ATOM   1661 C  CD1  . ILE A 1 209 ? -16.078 3.216   24.869  1.00 12.35 ?  210 ILE A CD1  1 
ATOM   1662 N  N    . VAL A 1 210 ? -14.479 -2.739  24.723  1.00 7.21  ?  211 VAL A N    1 
ATOM   1663 C  CA   . VAL A 1 210 ? -14.430 -4.027  23.969  1.00 6.93  ?  211 VAL A CA   1 
ATOM   1664 C  C    . VAL A 1 210 ? -15.756 -4.748  24.243  1.00 6.51  ?  211 VAL A C    1 
ATOM   1665 O  O    . VAL A 1 210 ? -16.100 -4.974  25.388  1.00 8.32  ?  211 VAL A O    1 
ATOM   1666 C  CB   . VAL A 1 210 ? -13.215 -4.911  24.396  1.00 7.21  ?  211 VAL A CB   1 
ATOM   1667 C  CG1  . VAL A 1 210 ? -13.244 -6.302  23.686  1.00 7.90  ?  211 VAL A CG1  1 
ATOM   1668 C  CG2  . VAL A 1 210 ? -11.886 -4.138  24.120  1.00 7.55  ?  211 VAL A CG2  1 
ATOM   1669 N  N    . LEU A 1 211 ? -16.514 -5.014  23.165  1.00 7.83  ?  212 LEU A N    1 
ATOM   1670 C  CA   . LEU A 1 211 ? -17.804 -5.639  23.329  1.00 7.91  ?  212 LEU A CA   1 
ATOM   1671 C  C    . LEU A 1 211 ? -17.631 -7.134  23.748  1.00 8.91  ?  212 LEU A C    1 
ATOM   1672 O  O    . LEU A 1 211 ? -16.776 -7.871  23.185  1.00 8.13  ?  212 LEU A O    1 
ATOM   1673 C  CB   . LEU A 1 211 ? -18.655 -5.573  21.998  1.00 8.72  ?  212 LEU A CB   1 
ATOM   1674 C  CG   . LEU A 1 211 ? -19.022 -4.139  21.639  1.00 9.64  ?  212 LEU A CG   1 
ATOM   1675 C  CD1  . LEU A 1 211 ? -20.056 -4.192  20.461  1.00 12.84 ?  212 LEU A CD1  1 
ATOM   1676 C  CD2  . LEU A 1 211 ? -19.563 -3.374  22.807  1.00 12.06 ?  212 LEU A CD2  1 
ATOM   1677 N  N    . LYS A 1 212 ? -18.528 -7.590  24.649  1.00 9.56  ?  213 LYS A N    1 
ATOM   1678 C  CA   . LYS A 1 212 ? -18.471 -8.993  25.081  1.00 11.32 ?  213 LYS A CA   1 
ATOM   1679 C  C    . LYS A 1 212 ? -18.907 -9.938  24.013  1.00 10.72 ?  213 LYS A C    1 
ATOM   1680 O  O    . LYS A 1 212 ? -18.406 -11.066 23.899  1.00 11.75 ?  213 LYS A O    1 
ATOM   1681 C  CB   . LYS A 1 212 ? -19.376 -9.179  26.326  1.00 14.08 ?  213 LYS A CB   1 
ATOM   1682 C  CG   . LYS A 1 212 ? -19.665 -10.651 26.735  1.00 18.64 ?  213 LYS A CG   1 
ATOM   1683 C  CD   . LYS A 1 212 ? -20.943 -10.499 27.697  1.00 21.55 ?  213 LYS A CD   1 
ATOM   1684 C  CE   . LYS A 1 212 ? -22.396 -10.349 26.984  1.00 27.77 ?  213 LYS A CE   1 
ATOM   1685 N  NZ   . LYS A 1 212 ? -22.703 -9.780  25.494  1.00 25.66 ?  213 LYS A NZ   1 
ATOM   1686 N  N    . GLU A 1 213 ? -19.916 -9.535  23.204  1.00 8.99  ?  214 GLU A N    1 
ATOM   1687 C  CA   . GLU A 1 213 ? -20.506 -10.458 22.204  1.00 9.48  ?  214 GLU A CA   1 
ATOM   1688 C  C    . GLU A 1 213 ? -19.746 -10.325 20.879  1.00 7.50  ?  214 GLU A C    1 
ATOM   1689 O  O    . GLU A 1 213 ? -19.673 -9.241  20.264  1.00 8.65  ?  214 GLU A O    1 
ATOM   1690 C  CB   . GLU A 1 213 ? -21.974 -10.114 21.976  1.00 9.43  ?  214 GLU A CB   1 
ATOM   1691 C  CG   . GLU A 1 213 ? -22.641 -11.074 20.978  1.00 13.25 ?  214 GLU A CG   1 
ATOM   1692 C  CD   . GLU A 1 213 ? -24.135 -10.889 20.791  1.00 16.59 ?  214 GLU A CD   1 
ATOM   1693 O  OE1  . GLU A 1 213 ? -24.754 -10.006 21.389  1.00 15.25 ?  214 GLU A OE1  1 
ATOM   1694 O  OE2  . GLU A 1 213 ? -24.710 -11.778 20.031  1.00 27.16 ?  214 GLU A OE2  1 
ATOM   1695 N  N    . PRO A 1 214 ? -19.187 -11.449 20.391  1.00 8.46  ?  215 PRO A N    1 
ATOM   1696 C  CA   . PRO A 1 214 ? -18.524 -11.399 19.053  1.00 9.38  ?  215 PRO A CA   1 
ATOM   1697 C  C    . PRO A 1 214 ? -19.566 -11.363 17.931  1.00 10.62 ?  215 PRO A C    1 
ATOM   1698 O  O    . PRO A 1 214 ? -20.750 -11.783 18.151  1.00 12.55 ?  215 PRO A O    1 
ATOM   1699 C  CB   . PRO A 1 214 ? -17.765 -12.726 18.914  1.00 9.35  ?  215 PRO A CB   1 
ATOM   1700 C  CG   . PRO A 1 214 ? -18.534 -13.685 19.833  1.00 16.13 ?  215 PRO A CG   1 
ATOM   1701 C  CD   . PRO A 1 214 ? -19.138 -12.788 20.985  1.00 9.89  ?  215 PRO A CD   1 
ATOM   1702 N  N    . ILE A 1 215 ? -19.162 -10.923 16.733  1.00 8.34  ?  216 ILE A N    1 
ATOM   1703 C  CA   . ILE A 1 215 ? -19.985 -11.162 15.545  1.00 8.92  ?  216 ILE A CA   1 
ATOM   1704 C  C    . ILE A 1 215 ? -19.441 -12.419 14.862  1.00 9.60  ?  216 ILE A C    1 
ATOM   1705 O  O    . ILE A 1 215 ? -18.270 -12.797 15.036  1.00 10.73 ?  216 ILE A O    1 
ATOM   1706 C  CB   . ILE A 1 215 ? -19.969 -9.971  14.569  1.00 10.46 ?  216 ILE A CB   1 
ATOM   1707 C  CG1  . ILE A 1 215 ? -18.569 -9.628  14.111  1.00 10.28 ?  216 ILE A CG1  1 
ATOM   1708 C  CG2  . ILE A 1 215 ? -20.691 -8.753  15.289  1.00 12.21 ?  216 ILE A CG2  1 
ATOM   1709 C  CD1  . ILE A 1 215 ? -18.615 -8.584  12.898  1.00 11.32 ?  216 ILE A CD1  1 
ATOM   1710 N  N    A SER A 1 216 ? -20.327 -13.083 14.094  0.50 10.89 ?  217 SER A N    1 
ATOM   1711 N  N    B SER A 1 216 ? -20.283 -13.083 14.070  0.50 10.98 ?  217 SER A N    1 
ATOM   1712 C  CA   A SER A 1 216 ? -19.899 -14.206 13.242  0.50 10.91 ?  217 SER A CA   1 
ATOM   1713 C  CA   B SER A 1 216 ? -19.756 -14.210 13.310  0.50 10.84 ?  217 SER A CA   1 
ATOM   1714 C  C    A SER A 1 216 ? -19.658 -13.733 11.831  0.50 11.61 ?  217 SER A C    1 
ATOM   1715 C  C    B SER A 1 216 ? -19.708 -13.860 11.855  0.50 11.23 ?  217 SER A C    1 
ATOM   1716 O  O    A SER A 1 216 ? -20.416 -12.882 11.300  0.50 12.26 ?  217 SER A O    1 
ATOM   1717 O  O    B SER A 1 216 ? -20.665 -13.231 11.322  0.50 11.11 ?  217 SER A O    1 
ATOM   1718 C  CB   A SER A 1 216 ? -20.930 -15.364 13.243  0.50 12.68 ?  217 SER A CB   1 
ATOM   1719 C  CB   B SER A 1 216 ? -20.599 -15.452 13.530  0.50 13.11 ?  217 SER A CB   1 
ATOM   1720 O  OG   A SER A 1 216 ? -21.100 -15.843 14.580  0.50 14.32 ?  217 SER A OG   1 
ATOM   1721 O  OG   B SER A 1 216 ? -21.922 -15.172 13.141  0.50 13.46 ?  217 SER A OG   1 
ATOM   1722 N  N    . VAL A 1 217 ? -18.597 -14.257 11.222  1.00 10.59 ?  218 VAL A N    1 
ATOM   1723 C  CA   . VAL A 1 217 ? -18.331 -14.025 9.781   1.00 11.48 ?  218 VAL A CA   1 
ATOM   1724 C  C    . VAL A 1 217 ? -18.046 -15.397 9.176   1.00 11.82 ?  218 VAL A C    1 
ATOM   1725 O  O    . VAL A 1 217 ? -17.651 -16.346 9.893   1.00 12.30 ?  218 VAL A O    1 
ATOM   1726 C  CB   . VAL A 1 217 ? -17.141 -13.024 9.531   1.00 11.38 ?  218 VAL A CB   1 
ATOM   1727 C  CG1  . VAL A 1 217 ? -17.395 -11.699 10.269  1.00 12.48 ?  218 VAL A CG1  1 
ATOM   1728 C  CG2  . VAL A 1 217 ? -15.857 -13.661 10.030  1.00 12.53 ?  218 VAL A CG2  1 
ATOM   1729 N  N    . SER A 1 218 ? -18.231 -15.532 7.873   1.00 11.42 ?  219 SER A N    1 
ATOM   1730 C  CA   . SER A 1 218 ? -17.983 -16.879 7.284   1.00 11.08 ?  219 SER A CA   1 
ATOM   1731 C  C    . SER A 1 218 ? -16.515 -17.136 7.006   1.00 11.28 ?  219 SER A C    1 
ATOM   1732 O  O    . SER A 1 218 ? -15.709 -16.197 6.912   1.00 11.05 ?  219 SER A O    1 
ATOM   1733 C  CB   . SER A 1 218 ? -18.771 -17.067 5.995   1.00 11.96 ?  219 SER A CB   1 
ATOM   1734 O  OG   . SER A 1 218 ? -18.251 -16.193 5.004   1.00 13.87 ?  219 SER A OG   1 
ATOM   1735 N  N    . SER A 1 219 ? -16.158 -18.419 6.837   1.00 13.11 ?  220 SER A N    1 
ATOM   1736 C  CA   . SER A 1 219 ? -14.792 -18.767 6.472   1.00 13.95 ?  220 SER A CA   1 
ATOM   1737 C  C    . SER A 1 219 ? -14.444 -18.074 5.135   1.00 13.97 ?  220 SER A C    1 
ATOM   1738 O  O    . SER A 1 219 ? -13.297 -17.596 4.959   1.00 16.03 ?  220 SER A O    1 
ATOM   1739 C  CB   . SER A 1 219 ? -14.627 -20.300 6.364   1.00 16.27 ?  220 SER A CB   1 
ATOM   1740 O  OG   . SER A 1 219 ? -15.707 -20.827 5.638   1.00 19.44 ?  220 SER A OG   1 
ATOM   1741 N  N    . GLU A 1 220 ? -15.406 -17.986 4.159   1.00 13.30 ?  221 GLU A N    1 
ATOM   1742 C  CA   . GLU A 1 220 ? -15.075 -17.318 2.890   1.00 13.74 ?  221 GLU A CA   1 
ATOM   1743 C  C    . GLU A 1 220 ? -14.809 -15.797 3.091   1.00 12.84 ?  221 GLU A C    1 
ATOM   1744 O  O    . GLU A 1 220 ? -13.930 -15.236 2.402   1.00 14.48 ?  221 GLU A O    1 
ATOM   1745 C  CB   . GLU A 1 220 ? -16.195 -17.455 1.879   1.00 15.78 ?  221 GLU A CB   1 
ATOM   1746 C  CG   . GLU A 1 220 ? -16.378 -18.911 1.453   1.00 18.66 ?  221 GLU A CG   1 
ATOM   1747 C  CD   . GLU A 1 220 ? -17.407 -19.652 2.332   1.00 22.17 ?  221 GLU A CD   1 
ATOM   1748 O  OE1  . GLU A 1 220 ? -17.962 -19.138 3.364   1.00 20.06 ?  221 GLU A OE1  1 
ATOM   1749 O  OE2  . GLU A 1 220 ? -17.635 -20.859 2.034   1.00 30.98 ?  221 GLU A OE2  1 
ATOM   1750 N  N    . GLN A 1 221 ? -15.542 -15.163 4.037   1.00 10.75 ?  222 GLN A N    1 
ATOM   1751 C  CA   . GLN A 1 221 ? -15.286 -13.715 4.214   1.00 11.46 ?  222 GLN A CA   1 
ATOM   1752 C  C    . GLN A 1 221 ? -13.859 -13.502 4.796   1.00 11.75 ?  222 GLN A C    1 
ATOM   1753 O  O    . GLN A 1 221 ? -13.099 -12.649 4.308   1.00 13.66 ?  222 GLN A O    1 
ATOM   1754 C  CB   . GLN A 1 221 ? -16.329 -13.172 5.185   1.00 11.87 ?  222 GLN A CB   1 
ATOM   1755 C  CG   . GLN A 1 221 ? -17.719 -13.097 4.494   1.00 12.36 ?  222 GLN A CG   1 
ATOM   1756 C  CD   . GLN A 1 221 ? -18.832 -12.500 5.383   1.00 10.79 ?  222 GLN A CD   1 
ATOM   1757 O  OE1  . GLN A 1 221 ? -18.958 -12.883 6.572   1.00 11.80 ?  222 GLN A OE1  1 
ATOM   1758 N  NE2  . GLN A 1 221 ? -19.649 -11.562 4.828   1.00 12.14 ?  222 GLN A NE2  1 
ATOM   1759 N  N    . VAL A 1 222 ? -13.468 -14.312 5.810   1.00 13.22 ?  223 VAL A N    1 
ATOM   1760 C  CA   . VAL A 1 222 ? -12.123 -14.063 6.395   1.00 13.99 ?  223 VAL A CA   1 
ATOM   1761 C  C    . VAL A 1 222 ? -11.008 -14.531 5.374   1.00 14.27 ?  223 VAL A C    1 
ATOM   1762 O  O    . VAL A 1 222 ? -9.900  -13.936 5.280   1.00 14.25 ?  223 VAL A O    1 
ATOM   1763 C  CB   . VAL A 1 222 ? -11.974 -14.691 7.797   1.00 14.67 ?  223 VAL A CB   1 
ATOM   1764 C  CG1  . VAL A 1 222 ? -11.954 -16.175 7.708   1.00 19.93 ?  223 VAL A CG1  1 
ATOM   1765 C  CG2  . VAL A 1 222 ? -10.673 -14.117 8.537   1.00 15.54 ?  223 VAL A CG2  1 
ATOM   1766 N  N    . LEU A 1 223 ? -11.333 -15.541 4.544   1.00 14.60 ?  224 LEU A N    1 
ATOM   1767 C  CA   . LEU A 1 223 ? -10.375 -15.943 3.549   1.00 17.47 ?  224 LEU A CA   1 
ATOM   1768 C  C    . LEU A 1 223 ? -10.018 -14.804 2.628   1.00 16.76 ?  224 LEU A C    1 
ATOM   1769 O  O    . LEU A 1 223 ? -8.812  -14.695 2.229   1.00 16.74 ?  224 LEU A O    1 
ATOM   1770 C  CB   . LEU A 1 223 ? -10.855 -17.178 2.740   1.00 19.79 ?  224 LEU A CB   1 
ATOM   1771 C  CG   . LEU A 1 223 ? -10.616 -18.515 3.462   1.00 24.18 ?  224 LEU A CG   1 
ATOM   1772 C  CD1  . LEU A 1 223 ? -11.419 -19.802 2.815   1.00 29.12 ?  224 LEU A CD1  1 
ATOM   1773 C  CD2  . LEU A 1 223 ? -9.078  -18.823 3.510   1.00 30.06 ?  224 LEU A CD2  1 
ATOM   1774 N  N    . LYS A 1 224 ? -11.032 -13.995 2.296   1.00 16.21 ?  225 LYS A N    1 
ATOM   1775 C  CA   . LYS A 1 224 ? -10.801 -12.854 1.404   1.00 17.89 ?  225 LYS A CA   1 
ATOM   1776 C  C    . LYS A 1 224 ? -9.885  -11.800 2.078   1.00 15.09 ?  225 LYS A C    1 
ATOM   1777 O  O    . LYS A 1 224 ? -9.062  -11.205 1.408   1.00 15.30 ?  225 LYS A O    1 
ATOM   1778 C  CB   . LYS A 1 224 ? -12.139 -12.320 0.826   1.00 17.99 ?  225 LYS A CB   1 
ATOM   1779 C  CG   . LYS A 1 224 ? -12.728 -13.419 -0.201  1.00 23.10 ?  225 LYS A CG   1 
ATOM   1780 C  CD   . LYS A 1 224 ? -13.949 -12.946 -0.935  1.00 24.85 ?  225 LYS A CD   1 
ATOM   1781 C  CE   . LYS A 1 224 ? -14.721 -14.129 -1.726  1.00 28.90 ?  225 LYS A CE   1 
ATOM   1782 N  NZ   . LYS A 1 224 ? -16.017 -13.836 -2.612  1.00 30.65 ?  225 LYS A NZ   1 
ATOM   1783 N  N    . PHE A 1 225 ? -10.009 -11.580 3.396   1.00 12.63 ?  226 PHE A N    1 
ATOM   1784 C  CA   . PHE A 1 225 ? -9.035  -10.717 4.062   1.00 11.07 ?  226 PHE A CA   1 
ATOM   1785 C  C    . PHE A 1 225 ? -7.611  -11.184 3.826   1.00 11.95 ?  226 PHE A C    1 
ATOM   1786 O  O    . PHE A 1 225 ? -6.685  -10.374 3.646   1.00 13.07 ?  226 PHE A O    1 
ATOM   1787 C  CB   . PHE A 1 225 ? -9.194  -10.703 5.615   1.00 11.18 ?  226 PHE A CB   1 
ATOM   1788 C  CG   . PHE A 1 225 ? -10.450 -9.969  6.170   1.00 10.24 ?  226 PHE A CG   1 
ATOM   1789 C  CD1  . PHE A 1 225 ? -11.518 -9.541  5.409   1.00 13.90 ?  226 PHE A CD1  1 
ATOM   1790 C  CD2  . PHE A 1 225 ? -10.523 -9.755  7.590   1.00 11.78 ?  226 PHE A CD2  1 
ATOM   1791 C  CE1  . PHE A 1 225 ? -12.611 -8.845  6.022   1.00 15.98 ?  226 PHE A CE1  1 
ATOM   1792 C  CE2  . PHE A 1 225 ? -11.569 -9.112  8.198   1.00 15.34 ?  226 PHE A CE2  1 
ATOM   1793 C  CZ   . PHE A 1 225 ? -12.626 -8.640  7.417   1.00 13.91 ?  226 PHE A CZ   1 
ATOM   1794 N  N    . ARG A 1 226 ? -7.423  -12.515 3.914   1.00 11.56 ?  227 ARG A N    1 
ATOM   1795 C  CA   . ARG A 1 226 ? -6.074  -13.134 3.818   1.00 12.57 ?  227 ARG A CA   1 
ATOM   1796 C  C    . ARG A 1 226 ? -5.460  -13.093 2.406   1.00 12.85 ?  227 ARG A C    1 
ATOM   1797 O  O    . ARG A 1 226 ? -4.309  -13.523 2.239   1.00 15.12 ?  227 ARG A O    1 
ATOM   1798 C  CB   . ARG A 1 226 ? -6.093  -14.548 4.333   1.00 12.96 ?  227 ARG A CB   1 
ATOM   1799 C  CG   . ARG A 1 226 ? -6.580  -14.687 5.802   1.00 13.60 ?  227 ARG A CG   1 
ATOM   1800 C  CD   . ARG A 1 226 ? -6.548  -16.181 6.214   1.00 14.43 ?  227 ARG A CD   1 
ATOM   1801 N  NE   . ARG A 1 226 ? -7.073  -16.327 7.606   1.00 14.12 ?  227 ARG A NE   1 
ATOM   1802 C  CZ   . ARG A 1 226 ? -7.998  -17.194 8.001   1.00 14.46 ?  227 ARG A CZ   1 
ATOM   1803 N  NH1  . ARG A 1 226 ? -8.450  -18.144 7.133   1.00 16.35 ?  227 ARG A NH1  1 
ATOM   1804 N  NH2  . ARG A 1 226 ? -8.452  -17.153 9.233   1.00 14.19 ?  227 ARG A NH2  1 
ATOM   1805 N  N    . LYS A 1 227 ? -6.221  -12.617 1.416   1.00 13.30 ?  228 LYS A N    1 
ATOM   1806 C  CA   . LYS A 1 227 ? -5.671  -12.495 0.075   1.00 15.39 ?  228 LYS A CA   1 
ATOM   1807 C  C    . LYS A 1 227 ? -5.073  -11.130 -0.180  1.00 14.02 ?  228 LYS A C    1 
ATOM   1808 O  O    . LYS A 1 227 ? -4.472  -10.905 -1.241  1.00 14.99 ?  228 LYS A O    1 
ATOM   1809 C  CB   . LYS A 1 227 ? -6.760  -12.787 -0.978  1.00 17.12 ?  228 LYS A CB   1 
ATOM   1810 C  CG   . LYS A 1 227 ? -7.188  -14.258 -1.008  1.00 20.10 ?  228 LYS A CG   1 
ATOM   1811 C  CD   . LYS A 1 227 ? -8.295  -14.474 -2.028  1.00 25.51 ?  228 LYS A CD   1 
ATOM   1812 C  CE   . LYS A 1 227 ? -7.729  -15.170 -3.289  1.00 35.74 ?  228 LYS A CE   1 
ATOM   1813 N  NZ   . LYS A 1 227 ? -8.415  -14.794 -4.603  1.00 39.48 ?  228 LYS A NZ   1 
ATOM   1814 N  N    . LEU A 1 228 ? -5.295  -10.207 0.784   1.00 13.76 ?  229 LEU A N    1 
ATOM   1815 C  CA   . LEU A 1 228 ? -4.681  -8.901  0.643   1.00 13.79 ?  229 LEU A CA   1 
ATOM   1816 C  C    . LEU A 1 228 ? -3.138  -9.019  0.771   1.00 14.87 ?  229 LEU A C    1 
ATOM   1817 O  O    . LEU A 1 228 ? -2.607  -10.042 1.210   1.00 13.36 ?  229 LEU A O    1 
ATOM   1818 C  CB   . LEU A 1 228 ? -5.196  -7.971  1.755   1.00 13.74 ?  229 LEU A CB   1 
ATOM   1819 C  CG   . LEU A 1 228 ? -6.638  -7.479  1.573   1.00 14.15 ?  229 LEU A CG   1 
ATOM   1820 C  CD1  . LEU A 1 228 ? -7.166  -6.837  2.852   1.00 13.97 ?  229 LEU A CD1  1 
ATOM   1821 C  CD2  . LEU A 1 228 ? -6.623  -6.445  0.390   1.00 14.74 ?  229 LEU A CD2  1 
ATOM   1822 N  N    . ASN A 1 229 ? -2.435  -7.922  0.444   1.00 15.87 ?  230 ASN A N    1 
ATOM   1823 C  CA   . ASN A 1 229 ? -0.987  -7.932  0.448   1.00 15.61 ?  230 ASN A CA   1 
ATOM   1824 C  C    . ASN A 1 229 ? -0.435  -6.776  1.301   1.00 16.29 ?  230 ASN A C    1 
ATOM   1825 O  O    . ASN A 1 229 ? -0.955  -5.637  1.227   1.00 16.17 ?  230 ASN A O    1 
ATOM   1826 C  CB   . ASN A 1 229 ? -0.435  -7.705  -0.990  1.00 16.31 ?  230 ASN A CB   1 
ATOM   1827 C  CG   . ASN A 1 229 ? -0.449  -8.961  -1.924  1.00 19.06 ?  230 ASN A CG   1 
ATOM   1828 O  OD1  . ASN A 1 229 ? 0.136   -8.864  -3.050  1.00 22.38 ?  230 ASN A OD1  1 
ATOM   1829 N  ND2  . ASN A 1 229 ? -1.069  -10.101 -1.487  1.00 19.46 ?  230 ASN A ND2  1 
ATOM   1830 N  N    . PHE A 1 230 ? 0.630   -7.084  2.058   1.00 16.11 ?  231 PHE A N    1 
ATOM   1831 C  CA   . PHE A 1 230 ? 1.320   -5.995  2.778   1.00 15.15 ?  231 PHE A CA   1 
ATOM   1832 C  C    . PHE A 1 230 ? 2.207   -5.162  1.814   1.00 18.44 ?  231 PHE A C    1 
ATOM   1833 O  O    . PHE A 1 230 ? 2.459   -3.987  2.075   1.00 18.43 ?  231 PHE A O    1 
ATOM   1834 C  CB   . PHE A 1 230 ? 2.310   -6.573  3.763   1.00 15.43 ?  231 PHE A CB   1 
ATOM   1835 C  CG   . PHE A 1 230 ? 1.722   -7.199  5.031   1.00 13.74 ?  231 PHE A CG   1 
ATOM   1836 C  CD1  . PHE A 1 230 ? 0.939   -6.452  5.916   1.00 12.47 ?  231 PHE A CD1  1 
ATOM   1837 C  CD2  . PHE A 1 230 ? 2.131   -8.507  5.394   1.00 13.97 ?  231 PHE A CD2  1 
ATOM   1838 C  CE1  . PHE A 1 230 ? 0.506   -6.995  7.176   1.00 13.63 ?  231 PHE A CE1  1 
ATOM   1839 C  CE2  . PHE A 1 230 ? 1.691   -9.089  6.646   1.00 15.54 ?  231 PHE A CE2  1 
ATOM   1840 C  CZ   . PHE A 1 230 ? 0.885   -8.316  7.546   1.00 13.40 ?  231 PHE A CZ   1 
ATOM   1841 N  N    . ASN A 1 231 ? 2.705   -5.816  0.765   1.00 17.06 ?  232 ASN A N    1 
ATOM   1842 C  CA   . ASN A 1 231 ? 3.576   -5.164  -0.242  1.00 19.06 ?  232 ASN A CA   1 
ATOM   1843 C  C    . ASN A 1 231 ? 2.817   -4.269  -1.224  1.00 19.27 ?  232 ASN A C    1 
ATOM   1844 O  O    . ASN A 1 231 ? 1.591   -4.378  -1.399  1.00 18.84 ?  232 ASN A O    1 
ATOM   1845 C  CB   . ASN A 1 231 ? 4.302   -6.251  -1.032  1.00 20.61 ?  232 ASN A CB   1 
ATOM   1846 C  CG   . ASN A 1 231 ? 3.325   -7.179  -1.646  1.00 18.24 ?  232 ASN A CG   1 
ATOM   1847 O  OD1  . ASN A 1 231 ? 2.771   -8.058  -0.945  1.00 21.11 ?  232 ASN A OD1  1 
ATOM   1848 N  ND2  . ASN A 1 231 ? 3.044   -6.993  -2.948  1.00 20.91 ?  232 ASN A ND2  1 
ATOM   1849 N  N    . GLY A 1 232 ? 3.582   -3.408  -1.930  1.00 19.30 ?  233 GLY A N    1 
ATOM   1850 C  CA   . GLY A 1 232 ? 2.985   -2.572  -3.002  1.00 20.96 ?  233 GLY A CA   1 
ATOM   1851 C  C    . GLY A 1 232 ? 2.982   -3.381  -4.279  1.00 20.72 ?  233 GLY A C    1 
ATOM   1852 O  O    . GLY A 1 232 ? 3.690   -4.399  -4.383  1.00 20.91 ?  233 GLY A O    1 
ATOM   1853 N  N    . GLU A 1 233 ? 2.199   -2.924  -5.274  1.00 21.19 ?  234 GLU A N    1 
ATOM   1854 C  CA   . GLU A 1 233 ? 2.162   -3.538  -6.620  1.00 22.37 ?  234 GLU A CA   1 
ATOM   1855 C  C    . GLU A 1 233 ? 3.548   -3.602  -7.246  1.00 21.65 ?  234 GLU A C    1 
ATOM   1856 O  O    . GLU A 1 233 ? 4.324   -2.664  -7.105  1.00 21.11 ?  234 GLU A O    1 
ATOM   1857 C  CB   . GLU A 1 233 ? 1.234   -2.687  -7.524  1.00 21.92 ?  234 GLU A CB   1 
ATOM   1858 C  CG   . GLU A 1 233 ? 0.870   -3.311  -8.857  1.00 22.62 ?  234 GLU A CG   1 
ATOM   1859 C  CD   . GLU A 1 233 ? -0.037  -2.449  -9.696  1.00 27.40 ?  234 GLU A CD   1 
ATOM   1860 O  OE1  . GLU A 1 233 ? -0.334  -1.213  -9.298  1.00 30.14 ?  234 GLU A OE1  1 
ATOM   1861 O  OE2  . GLU A 1 233 ? -0.357  -2.985  -10.813 1.00 31.14 ?  234 GLU A OE2  1 
ATOM   1862 N  N    . GLY A 1 234 ? 3.846   -4.737  -7.894  1.00 22.07 ?  235 GLY A N    1 
ATOM   1863 C  CA   . GLY A 1 234 ? 5.134   -4.927  -8.528  1.00 26.48 ?  235 GLY A CA   1 
ATOM   1864 C  C    . GLY A 1 234 ? 6.232   -5.223  -7.542  1.00 28.10 ?  235 GLY A C    1 
ATOM   1865 O  O    . GLY A 1 234 ? 7.425   -5.124  -7.881  1.00 28.58 ?  235 GLY A O    1 
ATOM   1866 N  N    . GLU A 1 235 ? 5.850   -5.568  -6.303  1.00 28.93 ?  236 GLU A N    1 
ATOM   1867 C  CA   . GLU A 1 235 ? 6.816   -6.073  -5.295  1.00 29.08 ?  236 GLU A CA   1 
ATOM   1868 C  C    . GLU A 1 235 ? 6.454   -7.505  -4.990  1.00 28.98 ?  236 GLU A C    1 
ATOM   1869 O  O    . GLU A 1 235 ? 5.295   -7.950  -5.290  1.00 27.96 ?  236 GLU A O    1 
ATOM   1870 C  CB   . GLU A 1 235 ? 6.787   -5.243  -4.009  1.00 29.42 ?  236 GLU A CB   1 
ATOM   1871 C  CG   . GLU A 1 235 ? 7.279   -3.857  -4.128  1.00 30.25 ?  236 GLU A CG   1 
ATOM   1872 C  CD   . GLU A 1 235 ? 7.066   -2.994  -2.853  1.00 34.64 ?  236 GLU A CD   1 
ATOM   1873 O  OE1  . GLU A 1 235 ? 6.471   -3.442  -1.813  1.00 39.18 ?  236 GLU A OE1  1 
ATOM   1874 O  OE2  . GLU A 1 235 ? 7.528   -1.835  -2.865  1.00 43.44 ?  236 GLU A OE2  1 
ATOM   1875 N  N    . PRO A 1 236 ? 7.414   -8.258  -4.405  1.00 26.64 ?  237 PRO A N    1 
ATOM   1876 C  CA   . PRO A 1 236 ? 7.131   -9.628  -4.123  1.00 26.07 ?  237 PRO A CA   1 
ATOM   1877 C  C    . PRO A 1 236 ? 5.905   -9.728  -3.135  1.00 24.02 ?  237 PRO A C    1 
ATOM   1878 O  O    . PRO A 1 236 ? 5.761   -8.898  -2.189  1.00 23.28 ?  237 PRO A O    1 
ATOM   1879 C  CB   . PRO A 1 236 ? 8.379   -10.099 -3.375  1.00 25.79 ?  237 PRO A CB   1 
ATOM   1880 C  CG   . PRO A 1 236 ? 9.480   -9.199  -3.837  1.00 29.02 ?  237 PRO A CG   1 
ATOM   1881 C  CD   . PRO A 1 236 ? 8.805   -7.876  -4.081  1.00 28.38 ?  237 PRO A CD   1 
ATOM   1882 N  N    . GLU A 1 237 ? 5.103   -10.775 -3.357  1.00 24.38 ?  238 GLU A N    1 
ATOM   1883 C  CA   . GLU A 1 237 ? 3.863   -10.943 -2.622  1.00 23.10 ?  238 GLU A CA   1 
ATOM   1884 C  C    . GLU A 1 237 ? 4.121   -11.424 -1.190  1.00 22.56 ?  238 GLU A C    1 
ATOM   1885 O  O    . GLU A 1 237 ? 4.723   -12.492 -0.960  1.00 20.61 ?  238 GLU A O    1 
ATOM   1886 C  CB   . GLU A 1 237 ? 2.900   -11.918 -3.312  1.00 23.66 ?  238 GLU A CB   1 
ATOM   1887 C  CG   . GLU A 1 237 ? 1.576   -11.971 -2.586  1.00 24.67 ?  238 GLU A CG   1 
ATOM   1888 C  CD   . GLU A 1 237 ? 0.476   -12.770 -3.306  1.00 25.35 ?  238 GLU A CD   1 
ATOM   1889 O  OE1  . GLU A 1 237 ? 0.803   -13.784 -4.013  1.00 33.27 ?  238 GLU A OE1  1 
ATOM   1890 O  OE2  . GLU A 1 237 ? -0.698  -12.369 -3.236  1.00 22.75 ?  238 GLU A OE2  1 
ATOM   1891 N  N    . GLU A 1 238 ? 3.575   -10.653 -0.236  1.00 19.31 ?  239 GLU A N    1 
ATOM   1892 C  CA   . GLU A 1 238 ? 3.641   -11.019 1.191   1.00 20.39 ?  239 GLU A CA   1 
ATOM   1893 C  C    . GLU A 1 238 ? 2.171   -10.928 1.637   1.00 16.28 ?  239 GLU A C    1 
ATOM   1894 O  O    . GLU A 1 238 ? 1.614   -9.799  1.689   1.00 17.41 ?  239 GLU A O    1 
ATOM   1895 C  CB   . GLU A 1 238 ? 4.391   -9.964  1.996   1.00 19.81 ?  239 GLU A CB   1 
ATOM   1896 C  CG   . GLU A 1 238 ? 5.804   -9.591  1.591   1.00 24.58 ?  239 GLU A CG   1 
ATOM   1897 C  CD   . GLU A 1 238 ? 6.373   -8.326  2.381   1.00 29.38 ?  239 GLU A CD   1 
ATOM   1898 O  OE1  . GLU A 1 238 ? 5.814   -7.869  3.462   1.00 36.17 ?  239 GLU A OE1  1 
ATOM   1899 O  OE2  . GLU A 1 238 ? 7.432   -7.812  1.925   1.00 39.24 ?  239 GLU A OE2  1 
ATOM   1900 N  N    . LEU A 1 239 ? 1.542   -12.080 1.937   1.00 16.14 ?  240 LEU A N    1 
ATOM   1901 C  CA   . LEU A 1 239 ? 0.099   -12.009 2.274   1.00 14.06 ?  240 LEU A CA   1 
ATOM   1902 C  C    . LEU A 1 239 ? -0.110  -11.197 3.587   1.00 13.69 ?  240 LEU A C    1 
ATOM   1903 O  O    . LEU A 1 239 ? 0.676   -11.305 4.565   1.00 14.94 ?  240 LEU A O    1 
ATOM   1904 C  CB   . LEU A 1 239 ? -0.469  -13.404 2.485   1.00 15.30 ?  240 LEU A CB   1 
ATOM   1905 C  CG   . LEU A 1 239 ? -0.538  -14.267 1.216   1.00 15.23 ?  240 LEU A CG   1 
ATOM   1906 C  CD1  . LEU A 1 239 ? -1.189  -15.581 1.616   1.00 21.10 ?  240 LEU A CD1  1 
ATOM   1907 C  CD2  . LEU A 1 239 ? -1.309  -13.590 0.140   1.00 16.23 ?  240 LEU A CD2  1 
ATOM   1908 N  N    . MET A 1 240 ? -1.152  -10.360 3.577   1.00 12.67 ?  241 MET A N    1 
ATOM   1909 C  CA   . MET A 1 240 ? -1.433  -9.542  4.750   1.00 12.06 ?  241 MET A CA   1 
ATOM   1910 C  C    . MET A 1 240 ? -2.213  -10.492 5.686   1.00 13.52 ?  241 MET A C    1 
ATOM   1911 O  O    . MET A 1 240 ? -3.449  -10.653 5.559   1.00 12.44 ?  241 MET A O    1 
ATOM   1912 C  CB   . MET A 1 240 ? -2.322  -8.381  4.318   1.00 13.69 ?  241 MET A CB   1 
ATOM   1913 C  CG   . MET A 1 240 ? -2.679  -7.416  5.524   1.00 12.99 ?  241 MET A CG   1 
ATOM   1914 S  SD   . MET A 1 240 ? -3.642  -5.981  4.980   1.00 15.65 ?  241 MET A SD   1 
ATOM   1915 C  CE   . MET A 1 240 ? -2.330  -4.889  4.293   1.00 14.60 ?  241 MET A CE   1 
ATOM   1916 N  N    . VAL A 1 241 ? -1.459  -11.119 6.624   1.00 11.96 ?  242 VAL A N    1 
ATOM   1917 C  CA   . VAL A 1 241 ? -2.040  -12.034 7.646   1.00 10.53 ?  242 VAL A CA   1 
ATOM   1918 C  C    . VAL A 1 241 ? -1.243  -11.824 8.929   1.00 11.68 ?  242 VAL A C    1 
ATOM   1919 O  O    . VAL A 1 241 ? -0.065  -11.377 8.879   1.00 11.95 ?  242 VAL A O    1 
ATOM   1920 C  CB   . VAL A 1 241 ? -1.984  -13.576 7.256   1.00 10.94 ?  242 VAL A CB   1 
ATOM   1921 C  CG1  . VAL A 1 241 ? -2.930  -13.867 6.033   1.00 11.96 ?  242 VAL A CG1  1 
ATOM   1922 C  CG2  . VAL A 1 241 ? -0.504  -13.997 7.053   1.00 12.75 ?  242 VAL A CG2  1 
ATOM   1923 N  N    . ASP A 1 242 ? -1.884  -12.129 10.053  1.00 9.38  ?  243 ASP A N    1 
ATOM   1924 C  CA   . ASP A 1 242 ? -1.206  -11.993 11.385  1.00 8.79  ?  243 ASP A CA   1 
ATOM   1925 C  C    . ASP A 1 242 ? -0.718  -10.550 11.630  1.00 8.23  ?  243 ASP A C    1 
ATOM   1926 O  O    . ASP A 1 242 ? 0.396   -10.312 12.115  1.00 11.03 ?  243 ASP A O    1 
ATOM   1927 C  CB   . ASP A 1 242 ? -0.075  -13.050 11.553  1.00 8.78  ?  243 ASP A CB   1 
ATOM   1928 C  CG   . ASP A 1 242 ? -0.631  -14.460 11.672  1.00 9.75  ?  243 ASP A CG   1 
ATOM   1929 O  OD1  . ASP A 1 242 ? -1.741  -14.637 12.283  1.00 11.78 ?  243 ASP A OD1  1 
ATOM   1930 O  OD2  . ASP A 1 242 ? 0.009   -15.384 11.067  1.00 13.52 ?  243 ASP A OD2  1 
ATOM   1931 N  N    . ASN A 1 243 ? -1.581  -9.605  11.289  1.00 8.96  ?  244 ASN A N    1 
ATOM   1932 C  CA   . ASN A 1 243 ? -1.266  -8.170  11.573  1.00 7.52  ?  244 ASN A CA   1 
ATOM   1933 C  C    . ASN A 1 243 ? -1.868  -7.762  12.940  1.00 8.36  ?  244 ASN A C    1 
ATOM   1934 O  O    . ASN A 1 243 ? -2.584  -6.708  13.065  1.00 9.86  ?  244 ASN A O    1 
ATOM   1935 C  CB   . ASN A 1 243 ? -1.825  -7.324  10.431  1.00 9.18  ?  244 ASN A CB   1 
ATOM   1936 C  CG   . ASN A 1 243 ? -3.368  -7.497  10.212  1.00 10.70 ?  244 ASN A CG   1 
ATOM   1937 O  OD1  . ASN A 1 243 ? -4.035  -8.371  10.802  1.00 11.01 ?  244 ASN A OD1  1 
ATOM   1938 N  ND2  . ASN A 1 243 ? -3.932  -6.599  9.374   1.00 14.58 ?  244 ASN A ND2  1 
ATOM   1939 N  N    . TRP A 1 244 ? -1.581  -8.564  13.961  1.00 7.51  ?  245 TRP A N    1 
ATOM   1940 C  CA   . TRP A 1 244 ? -2.048  -8.316  15.322  1.00 7.73  ?  245 TRP A CA   1 
ATOM   1941 C  C    . TRP A 1 244 ? -0.825  -8.205  16.260  1.00 8.29  ?  245 TRP A C    1 
ATOM   1942 O  O    . TRP A 1 244 ? 0.194   -8.914  16.106  1.00 9.19  ?  245 TRP A O    1 
ATOM   1943 C  CB   . TRP A 1 244 ? -3.039  -9.381  15.832  1.00 7.95  ?  245 TRP A CB   1 
ATOM   1944 C  CG   . TRP A 1 244 ? -2.543  -10.808 15.642  1.00 7.04  ?  245 TRP A CG   1 
ATOM   1945 C  CD1  . TRP A 1 244 ? -2.645  -11.564 14.479  1.00 8.03  ?  245 TRP A CD1  1 
ATOM   1946 C  CD2  . TRP A 1 244 ? -1.927  -11.667 16.613  1.00 8.27  ?  245 TRP A CD2  1 
ATOM   1947 N  NE1  . TRP A 1 244 ? -2.119  -12.857 14.647  1.00 8.06  ?  245 TRP A NE1  1 
ATOM   1948 C  CE2  . TRP A 1 244 ? -1.679  -12.953 15.964  1.00 9.45  ?  245 TRP A CE2  1 
ATOM   1949 C  CE3  . TRP A 1 244 ? -1.647  -11.545 17.981  1.00 10.50 ?  245 TRP A CE3  1 
ATOM   1950 C  CZ2  . TRP A 1 244 ? -1.081  -14.040 16.649  1.00 9.51  ?  245 TRP A CZ2  1 
ATOM   1951 C  CZ3  . TRP A 1 244 ? -1.059  -12.631 18.635  1.00 10.32 ?  245 TRP A CZ3  1 
ATOM   1952 C  CH2  . TRP A 1 244 ? -0.788  -13.867 17.970  1.00 10.73 ?  245 TRP A CH2  1 
ATOM   1953 N  N    . ARG A 1 245 ? -0.966  -7.296  17.229  1.00 8.75  ?  246 ARG A N    1 
ATOM   1954 C  CA   . ARG A 1 245 ? -0.034  -7.200  18.352  1.00 8.55  ?  246 ARG A CA   1 
ATOM   1955 C  C    . ARG A 1 245 ? -0.496  -8.120  19.488  1.00 8.10  ?  246 ARG A C    1 
ATOM   1956 O  O    . ARG A 1 245 ? -1.686  -8.131  19.798  1.00 9.02  ?  246 ARG A O    1 
ATOM   1957 C  CB   . ARG A 1 245 ? 0.042   -5.760  18.875  1.00 7.94  ?  246 ARG A CB   1 
ATOM   1958 C  CG   . ARG A 1 245 ? 1.152   -5.540  19.862  1.00 7.50  ?  246 ARG A CG   1 
ATOM   1959 C  CD   . ARG A 1 245 ? 1.077   -4.122  20.521  1.00 8.42  ?  246 ARG A CD   1 
ATOM   1960 N  NE   . ARG A 1 245 ? 2.346   -3.861  21.277  1.00 10.21 ?  246 ARG A NE   1 
ATOM   1961 C  CZ   . ARG A 1 245 ? 2.543   -2.834  22.111  1.00 9.93  ?  246 ARG A CZ   1 
ATOM   1962 N  NH1  . ARG A 1 245 ? 1.487   -2.027  22.485  1.00 9.29  ?  246 ARG A NH1  1 
ATOM   1963 N  NH2  . ARG A 1 245 ? 3.774   -2.630  22.597  1.00 10.47 ?  246 ARG A NH2  1 
ATOM   1964 N  N    . PRO A 1 246 ? 0.387   -8.900  20.096  1.00 10.23 ?  247 PRO A N    1 
ATOM   1965 C  CA   . PRO A 1 246 ? -0.050  -9.768  21.233  1.00 8.84  ?  247 PRO A CA   1 
ATOM   1966 C  C    . PRO A 1 246 ? -0.402  -8.954  22.483  1.00 8.84  ?  247 PRO A C    1 
ATOM   1967 O  O    . PRO A 1 246 ? -0.032  -7.750  22.600  1.00 9.81  ?  247 PRO A O    1 
ATOM   1968 C  CB   . PRO A 1 246 ? 1.187   -10.612 21.546  1.00 12.03 ?  247 PRO A CB   1 
ATOM   1969 C  CG   . PRO A 1 246 ? 2.131   -10.429 20.384  1.00 14.95 ?  247 PRO A CG   1 
ATOM   1970 C  CD   . PRO A 1 246 ? 1.817   -9.081  19.756  1.00 10.50 ?  247 PRO A CD   1 
ATOM   1971 N  N    . ALA A 1 247 ? -1.020  -9.634  23.467  1.00 9.38  ?  248 ALA A N    1 
ATOM   1972 C  CA   . ALA A 1 247 ? -1.414  -9.012  24.741  1.00 7.66  ?  248 ALA A CA   1 
ATOM   1973 C  C    . ALA A 1 247 ? -0.136  -8.473  25.445  1.00 8.83  ?  248 ALA A C    1 
ATOM   1974 O  O    . ALA A 1 247 ? 0.954   -9.118  25.468  1.00 10.82 ?  248 ALA A O    1 
ATOM   1975 C  CB   . ALA A 1 247 ? -2.138  -10.057 25.615  1.00 10.95 ?  248 ALA A CB   1 
ATOM   1976 N  N    . GLN A 1 248 ? -0.316  -7.289  26.051  1.00 9.77  ?  249 GLN A N    1 
ATOM   1977 C  CA   . GLN A 1 248 ? 0.758   -6.552  26.768  1.00 10.11 ?  249 GLN A CA   1 
ATOM   1978 C  C    . GLN A 1 248 ? 0.455   -6.591  28.273  1.00 10.31 ?  249 GLN A C    1 
ATOM   1979 O  O    . GLN A 1 248 ? -0.700  -6.788  28.696  1.00 10.33 ?  249 GLN A O    1 
ATOM   1980 C  CB   . GLN A 1 248 ? 0.803   -5.098  26.272  1.00 10.55 ?  249 GLN A CB   1 
ATOM   1981 C  CG   . GLN A 1 248 ? 1.088   -5.086  24.773  1.00 10.92 ?  249 GLN A CG   1 
ATOM   1982 C  CD   . GLN A 1 248 ? 2.459   -5.733  24.413  1.00 10.35 ?  249 GLN A CD   1 
ATOM   1983 O  OE1  . GLN A 1 248 ? 3.508   -5.376  25.005  1.00 14.66 ?  249 GLN A OE1  1 
ATOM   1984 N  NE2  . GLN A 1 248 ? 2.474   -6.657  23.462  1.00 11.57 ?  249 GLN A NE2  1 
ATOM   1985 N  N    . PRO A 1 249 ? 1.467   -6.315  29.091  1.00 12.82 ?  250 PRO A N    1 
ATOM   1986 C  CA   . PRO A 1 249 ? 1.227   -6.381  30.568  1.00 13.60 ?  250 PRO A CA   1 
ATOM   1987 C  C    . PRO A 1 249 ? 0.147   -5.365  31.004  1.00 11.53 ?  250 PRO A C    1 
ATOM   1988 O  O    . PRO A 1 249 ? 0.158   -4.200  30.590  1.00 13.61 ?  250 PRO A O    1 
ATOM   1989 C  CB   . PRO A 1 249 ? 2.629   -6.056  31.148  1.00 14.77 ?  250 PRO A CB   1 
ATOM   1990 C  CG   . PRO A 1 249 ? 3.581   -6.449  30.062  1.00 16.92 ?  250 PRO A CG   1 
ATOM   1991 C  CD   . PRO A 1 249 ? 2.883   -6.093  28.735  1.00 14.45 ?  250 PRO A CD   1 
ATOM   1992 N  N    . LEU A 1 250 ? -0.742  -5.821  31.884  1.00 12.45 ?  251 LEU A N    1 
ATOM   1993 C  CA   . LEU A 1 250 ? -1.808  -4.972  32.372  1.00 11.90 ?  251 LEU A CA   1 
ATOM   1994 C  C    . LEU A 1 250 ? -1.244  -3.886  33.316  1.00 12.64 ?  251 LEU A C    1 
ATOM   1995 O  O    . LEU A 1 250 ? -1.792  -2.746  33.416  1.00 12.57 ?  251 LEU A O    1 
ATOM   1996 C  CB   . LEU A 1 250 ? -2.871  -5.811  33.106  1.00 13.32 ?  251 LEU A CB   1 
ATOM   1997 C  CG   . LEU A 1 250 ? -4.164  -5.101  33.508  1.00 14.56 ?  251 LEU A CG   1 
ATOM   1998 C  CD1  . LEU A 1 250 ? -4.890  -4.464  32.277  1.00 13.47 ?  251 LEU A CD1  1 
ATOM   1999 C  CD2  . LEU A 1 250 ? -5.095  -6.093  34.227  1.00 16.83 ?  251 LEU A CD2  1 
ATOM   2000 N  N    . LYS A 1 251 ? -0.146  -4.213  34.032  1.00 13.36 ?  252 LYS A N    1 
ATOM   2001 C  CA   . LYS A 1 251 ? 0.473   -3.207  34.945  1.00 14.44 ?  252 LYS A CA   1 
ATOM   2002 C  C    . LYS A 1 251 ? -0.569  -2.675  35.939  1.00 15.63 ?  252 LYS A C    1 
ATOM   2003 O  O    . LYS A 1 251 ? -1.379  -3.457  36.456  1.00 18.23 ?  252 LYS A O    1 
ATOM   2004 C  CB   . LYS A 1 251 ? 1.222   -2.145  34.173  1.00 14.98 ?  252 LYS A CB   1 
ATOM   2005 C  CG   . LYS A 1 251 ? 2.424   -2.861  33.420  1.00 16.74 ?  252 LYS A CG   1 
ATOM   2006 C  CD   . LYS A 1 251 ? 3.353   -1.853  32.841  1.00 20.68 ?  252 LYS A CD   1 
ATOM   2007 C  CE   . LYS A 1 251 ? 4.566   -2.510  32.239  1.00 23.16 ?  252 LYS A CE   1 
ATOM   2008 N  NZ   . LYS A 1 251 ? 5.406   -1.526  31.530  1.00 22.88 ?  252 LYS A NZ   1 
ATOM   2009 N  N    . ASN A 1 252 ? -0.528  -1.374  36.199  1.00 15.91 ?  253 ASN A N    1 
ATOM   2010 C  CA   . ASN A 1 252 ? -1.353  -0.858  37.228  1.00 21.28 ?  253 ASN A CA   1 
ATOM   2011 C  C    . ASN A 1 252 ? -2.737  -0.446  36.664  1.00 21.03 ?  253 ASN A C    1 
ATOM   2012 O  O    . ASN A 1 252 ? -3.043  0.854   36.696  1.00 23.36 ?  253 ASN A O    1 
ATOM   2013 C  CB   . ASN A 1 252 ? -0.644  0.359   37.873  1.00 22.96 ?  253 ASN A CB   1 
ATOM   2014 C  CG   . ASN A 1 252 ? -1.432  0.925   39.018  1.00 28.75 ?  253 ASN A CG   1 
ATOM   2015 O  OD1  . ASN A 1 252 ? -2.021  0.158   39.830  1.00 36.00 ?  253 ASN A OD1  1 
ATOM   2016 N  ND2  . ASN A 1 252 ? -1.488  2.254   39.097  1.00 34.48 ?  253 ASN A ND2  1 
ATOM   2017 N  N    . ARG A 1 253 ? -3.484  -1.429  36.065  1.00 14.76 ?  254 ARG A N    1 
ATOM   2018 C  CA   . ARG A 1 253 ? -4.793  -1.030  35.544  1.00 12.43 ?  254 ARG A CA   1 
ATOM   2019 C  C    . ARG A 1 253 ? -5.883  -1.996  35.994  1.00 15.63 ?  254 ARG A C    1 
ATOM   2020 O  O    . ARG A 1 253 ? -5.585  -3.183  36.144  1.00 19.06 ?  254 ARG A O    1 
ATOM   2021 C  CB   . ARG A 1 253 ? -4.793  -0.971  33.960  1.00 12.28 ?  254 ARG A CB   1 
ATOM   2022 C  CG   . ARG A 1 253 ? -3.929  0.156   33.379  1.00 11.95 ?  254 ARG A CG   1 
ATOM   2023 C  CD   . ARG A 1 253 ? -3.816  0.199   31.888  1.00 12.21 ?  254 ARG A CD   1 
ATOM   2024 N  NE   . ARG A 1 253 ? -2.965  -0.957  31.454  1.00 10.10 ?  254 ARG A NE   1 
ATOM   2025 C  CZ   . ARG A 1 253 ? -2.665  -1.270  30.187  1.00 7.58  ?  254 ARG A CZ   1 
ATOM   2026 N  NH1  . ARG A 1 253 ? -3.304  -0.539  29.247  1.00 9.37  ?  254 ARG A NH1  1 
ATOM   2027 N  NH2  . ARG A 1 253 ? -1.820  -2.283  29.862  1.00 9.02  ?  254 ARG A NH2  1 
ATOM   2028 N  N    . GLN A 1 254 ? -7.153  -1.547  36.024  1.00 16.51 ?  255 GLN A N    1 
ATOM   2029 C  CA   . GLN A 1 254 ? -8.303  -2.441  36.370  1.00 19.45 ?  255 GLN A CA   1 
ATOM   2030 C  C    . GLN A 1 254 ? -9.238  -2.379  35.153  1.00 17.06 ?  255 GLN A C    1 
ATOM   2031 O  O    . GLN A 1 254 ? -9.472  -1.288  34.572  1.00 18.77 ?  255 GLN A O    1 
ATOM   2032 C  CB   . GLN A 1 254 ? -9.097  -2.060  37.658  1.00 21.49 ?  255 GLN A CB   1 
ATOM   2033 C  CG   . GLN A 1 254 ? -9.897  -3.370  38.207  1.00 23.87 ?  255 GLN A CG   1 
ATOM   2034 C  CD   . GLN A 1 254 ? -10.751 -3.189  39.471  1.00 26.61 ?  255 GLN A CD   1 
ATOM   2035 O  OE1  . GLN A 1 254 ? -11.504 -2.191  39.603  1.00 35.00 ?  255 GLN A OE1  1 
ATOM   2036 N  NE2  . GLN A 1 254 ? -10.702 -4.220  40.374  1.00 33.48 ?  255 GLN A NE2  1 
ATOM   2037 N  N    . ILE A 1 255 ? -9.567  -3.549  34.645  1.00 12.24 ?  256 ILE A N    1 
ATOM   2038 C  CA   . ILE A 1 255 ? -10.609 -3.625  33.582  1.00 12.01 ?  256 ILE A CA   1 
ATOM   2039 C  C    . ILE A 1 255 ? -12.013 -3.644  34.247  1.00 10.93 ?  256 ILE A C    1 
ATOM   2040 O  O    . ILE A 1 255 ? -12.217 -4.333  35.256  1.00 12.93 ?  256 ILE A O    1 
ATOM   2041 C  CB   . ILE A 1 255 ? -10.410 -4.861  32.669  1.00 12.86 ?  256 ILE A CB   1 
ATOM   2042 C  CG1  . ILE A 1 255 ? -8.982  -4.818  32.022  1.00 13.68 ?  256 ILE A CG1  1 
ATOM   2043 C  CG2  . ILE A 1 255 ? -11.542 -5.002  31.563  1.00 12.46 ?  256 ILE A CG2  1 
ATOM   2044 C  CD1  . ILE A 1 255 ? -8.642  -6.091  31.281  1.00 14.46 ?  256 ILE A CD1  1 
ATOM   2045 N  N    . LYS A 1 256 ? -12.894 -2.740  33.762  1.00 11.36 ?  257 LYS A N    1 
ATOM   2046 C  CA   . LYS A 1 256 ? -14.235 -2.610  34.311  1.00 11.82 ?  257 LYS A CA   1 
ATOM   2047 C  C    . LYS A 1 256 ? -15.229 -3.243  33.331  1.00 9.27  ?  257 LYS A C    1 
ATOM   2048 O  O    . LYS A 1 256 ? -14.998 -3.183  32.113  1.00 11.33 ?  257 LYS A O    1 
ATOM   2049 C  CB   . LYS A 1 256 ? -14.613 -1.096  34.542  1.00 13.38 ?  257 LYS A CB   1 
ATOM   2050 C  CG   . LYS A 1 256 ? -13.625 -0.291  35.416  1.00 21.28 ?  257 LYS A CG   1 
ATOM   2051 C  CD   . LYS A 1 256 ? -13.495 -0.899  36.735  1.00 30.56 ?  257 LYS A CD   1 
ATOM   2052 C  CE   . LYS A 1 256 ? -13.171 0.204   37.833  1.00 37.74 ?  257 LYS A CE   1 
ATOM   2053 N  NZ   . LYS A 1 256 ? -14.208 1.335   37.770  1.00 40.44 ?  257 LYS A NZ   1 
ATOM   2054 N  N    . ALA A 1 257 ? -16.293 -3.867  33.867  1.00 11.44 ?  258 ALA A N    1 
ATOM   2055 C  CA   . ALA A 1 257 ? -17.367 -4.518  33.080  1.00 12.14 ?  258 ALA A CA   1 
ATOM   2056 C  C    . ALA A 1 257 ? -18.644 -3.725  33.257  1.00 12.15 ?  258 ALA A C    1 
ATOM   2057 O  O    . ALA A 1 257 ? -18.977 -3.275  34.403  1.00 13.28 ?  258 ALA A O    1 
ATOM   2058 C  CB   . ALA A 1 257 ? -17.554 -5.975  33.463  1.00 13.30 ?  258 ALA A CB   1 
ATOM   2059 N  N    . SER A 1 258 ? -19.398 -3.578  32.154  1.00 10.83 ?  259 SER A N    1 
ATOM   2060 C  CA   . SER A 1 258 ? -20.692 -2.884  32.232  1.00 12.07 ?  259 SER A CA   1 
ATOM   2061 C  C    . SER A 1 258 ? -21.821 -3.833  32.641  1.00 13.22 ?  259 SER A C    1 
ATOM   2062 O  O    . SER A 1 258 ? -22.959 -3.400  32.782  1.00 16.43 ?  259 SER A O    1 
ATOM   2063 C  CB   . SER A 1 258 ? -21.060 -2.269  30.875  1.00 12.14 ?  259 SER A CB   1 
ATOM   2064 O  OG   . SER A 1 258 ? -21.432 -3.281  29.940  1.00 13.31 ?  259 SER A OG   1 
ATOM   2065 N  N    . PHE A 1 259 ? -21.484 -5.114  32.858  1.00 13.79 ?  260 PHE A N    1 
ATOM   2066 C  CA   . PHE A 1 259 ? -22.477 -6.174  33.027  1.00 17.15 ?  260 PHE A CA   1 
ATOM   2067 C  C    . PHE A 1 259 ? -21.980 -7.132  34.091  1.00 20.92 ?  260 PHE A C    1 
ATOM   2068 O  O    . PHE A 1 259 ? -20.750 -7.250  34.360  1.00 19.92 ?  260 PHE A O    1 
ATOM   2069 C  CB   . PHE A 1 259 ? -22.730 -6.946  31.727  1.00 17.57 ?  260 PHE A CB   1 
ATOM   2070 C  CG   . PHE A 1 259 ? -21.474 -7.631  31.199  1.00 16.38 ?  260 PHE A CG   1 
ATOM   2071 C  CD1  . PHE A 1 259 ? -20.487 -6.875  30.520  1.00 15.57 ?  260 PHE A CD1  1 
ATOM   2072 C  CD2  . PHE A 1 259 ? -21.207 -8.985  31.489  1.00 18.91 ?  260 PHE A CD2  1 
ATOM   2073 C  CE1  . PHE A 1 259 ? -19.280 -7.484  30.121  1.00 15.68 ?  260 PHE A CE1  1 
ATOM   2074 C  CE2  . PHE A 1 259 ? -19.989 -9.578  31.093  1.00 19.63 ?  260 PHE A CE2  1 
ATOM   2075 C  CZ   . PHE A 1 259 ? -19.036 -8.828  30.379  1.00 20.63 ?  260 PHE A CZ   1 
ATOM   2076 N  N    . LYS A 1 260 ? -22.995 -7.816  34.601  1.00 27.85 ?  261 LYS A N    1 
ATOM   2077 C  CA   . LYS A 1 260 ? -23.062 -8.994  35.512  1.00 35.62 ?  261 LYS A CA   1 
ATOM   2078 C  C    . LYS A 1 260 ? -22.957 -8.865  37.031  1.00 38.38 ?  261 LYS A C    1 
ATOM   2079 O  O    . LYS A 1 260 ? -22.475 -9.763  37.727  1.00 41.29 ?  261 LYS A O    1 
ATOM   2080 C  CB   . LYS A 1 260 ? -22.576 -10.334 34.916  1.00 34.98 ?  261 LYS A CB   1 
ATOM   2081 C  CG   . LYS A 1 260 ? -23.466 -10.775 33.694  1.00 37.23 ?  261 LYS A CG   1 
ATOM   2082 C  CD   . LYS A 1 260 ? -22.950 -12.105 32.981  1.00 39.07 ?  261 LYS A CD   1 
ATOM   2083 C  CE   . LYS A 1 260 ? -21.390 -12.301 33.094  1.00 42.95 ?  261 LYS A CE   1 
ATOM   2084 N  NZ   . LYS A 1 260 ? -20.858 -13.598 32.497  1.00 43.42 ?  261 LYS A NZ   1 
ATOM   2085 O  OXT  . LYS A 1 260 ? -23.480 -7.854  37.599  1.00 41.30 ?  261 LYS A OXT  1 
HETATM 2086 ZN ZN   . ZN  B 2 .   ? -6.598  -1.682  15.342  1.00 8.53  ?  262 ZN  A ZN   1 
HETATM 2087 N  N1   . E02 C 3 .   ? -2.883  4.165   10.204  1.00 45.10 ?  263 E02 A N1   1 
HETATM 2088 C  C2   . E02 C 3 .   ? -3.150  4.489   8.823   1.00 45.56 ?  263 E02 A C2   1 
HETATM 2089 N  N3   . E02 C 3 .   ? -2.018  4.437   8.144   1.00 46.27 ?  263 E02 A N3   1 
HETATM 2090 C  C4   . E02 C 3 .   ? -1.007  4.084   9.094   1.00 46.46 ?  263 E02 A C4   1 
HETATM 2091 C  C5   . E02 C 3 .   ? -1.546  3.934   10.302  1.00 46.71 ?  263 E02 A C5   1 
HETATM 2092 C  C6   . E02 C 3 .   ? -0.817  3.587   11.507  1.00 44.93 ?  263 E02 A C6   1 
HETATM 2093 C  C7   . E02 C 3 .   ? 0.488   3.415   11.364  1.00 45.41 ?  263 E02 A C7   1 
HETATM 2094 C  C8   . E02 C 3 .   ? 1.122   3.585   10.002  1.00 44.25 ?  263 E02 A C8   1 
HETATM 2095 C  C9   . E02 C 3 .   ? 0.419   3.906   8.900   1.00 43.96 ?  263 E02 A C9   1 
HETATM 2096 C  C10  . E02 C 3 .   ? -3.769  4.069   11.402  1.00 39.46 ?  263 E02 A C10  1 
HETATM 2097 C  C11  . E02 C 3 .   ? -3.573  2.978   12.519  1.00 22.87 ?  263 E02 A C11  1 
HETATM 2098 O  O12  . E02 C 3 .   ? -2.950  1.904   12.383  1.00 24.05 ?  263 E02 A O12  1 
HETATM 2099 C  C13  . E02 C 3 .   ? -4.385  3.227   13.846  1.00 17.71 ?  263 E02 A C13  1 
HETATM 2100 C  C14  . E02 C 3 .   ? -4.727  2.103   14.697  1.00 12.39 ?  263 E02 A C14  1 
HETATM 2101 C  C15  . E02 C 3 .   ? -5.402  2.303   15.838  1.00 9.62  ?  263 E02 A C15  1 
HETATM 2102 C  C16  . E02 C 3 .   ? -5.905  3.595   16.181  1.00 13.44 ?  263 E02 A C16  1 
HETATM 2103 C  C17  . E02 C 3 .   ? -5.603  4.662   15.411  1.00 15.17 ?  263 E02 A C17  1 
HETATM 2104 C  C18  . E02 C 3 .   ? -4.857  4.467   14.217  1.00 18.59 ?  263 E02 A C18  1 
HETATM 2105 S  S19  . E02 C 3 .   ? -5.875  0.832   16.852  1.00 11.18 ?  263 E02 A S19  1 
HETATM 2106 O  O20  . E02 C 3 .   ? -5.244  1.038   18.212  1.00 10.43 ?  263 E02 A O20  1 
HETATM 2107 CL CL21 . E02 C 3 .   ? -6.769  3.808   17.633  1.00 13.92 ?  263 E02 A CL21 1 
HETATM 2108 O  O22  . E02 C 3 .   ? -7.379  0.775   16.784  1.00 9.76  ?  263 E02 A O22  1 
HETATM 2109 N  N23  . E02 C 3 .   ? -5.222  -0.476  16.119  1.00 9.79  ?  263 E02 A N23  1 
HETATM 2110 O  O1   . MES D 4 .   ? -7.583  -9.079  -2.759  1.00 33.04 ?  264 MES A O1   1 
HETATM 2111 C  C2   . MES D 4 .   ? -7.357  -10.007 -3.917  1.00 30.45 ?  264 MES A C2   1 
HETATM 2112 C  C3   . MES D 4 .   ? -8.523  -10.993 -4.211  1.00 36.56 ?  264 MES A C3   1 
HETATM 2113 N  N4   . MES D 4 .   ? -9.639  -10.916 -3.213  1.00 38.93 ?  264 MES A N4   1 
HETATM 2114 C  C5   . MES D 4 .   ? -9.636  -10.204 -1.873  1.00 32.39 ?  264 MES A C5   1 
HETATM 2115 C  C6   . MES D 4 .   ? -8.280  -9.617  -1.598  1.00 28.22 ?  264 MES A C6   1 
HETATM 2116 C  C7   . MES D 4 .   ? -10.862 -11.648 -3.533  1.00 49.23 ?  264 MES A C7   1 
HETATM 2117 C  C8   . MES D 4 .   ? -11.935 -11.057 -2.603  1.00 63.48 ?  264 MES A C8   1 
HETATM 2118 S  S    . MES D 4 .   ? -12.797 -9.773  -3.290  1.00 72.72 ?  264 MES A S    1 
HETATM 2119 O  O1S  . MES D 4 .   ? -12.540 -9.846  -4.780  1.00 76.04 ?  264 MES A O1S  1 
HETATM 2120 O  O2S  . MES D 4 .   ? -14.271 -9.973  -3.014  1.00 75.46 -1 264 MES A O2S  1 
HETATM 2121 O  O3S  . MES D 4 .   ? -12.357 -8.444  -2.802  1.00 71.62 ?  264 MES A O3S  1 
HETATM 2122 S  S    . DMS E 5 .   ? 1.435   -11.720 15.026  1.00 29.94 ?  265 DMS A S    1 
HETATM 2123 O  O    . DMS E 5 .   ? 2.472   -10.403 14.410  1.00 30.88 ?  265 DMS A O    1 
HETATM 2124 C  C1   . DMS E 5 .   ? 2.116   -13.351 14.598  1.00 26.72 ?  265 DMS A C1   1 
HETATM 2125 C  C2   . DMS E 5 .   ? 1.839   -11.572 16.771  1.00 26.90 ?  265 DMS A C2   1 
HETATM 2126 O  O    . HOH F 6 .   ? -4.467  -15.918 0.724   1.00 28.37 ?  126 HOH A O    1 
HETATM 2127 O  O    . HOH F 6 .   ? -16.981 -8.442  20.546  1.00 9.17  ?  266 HOH A O    1 
HETATM 2128 O  O    . HOH F 6 .   ? -4.446  -13.561 18.086  1.00 9.96  ?  267 HOH A O    1 
HETATM 2129 O  O    . HOH F 6 .   ? -1.113  -4.042  15.827  1.00 9.41  ?  268 HOH A O    1 
HETATM 2130 O  O    . HOH F 6 .   ? -21.613 -7.123  23.744  1.00 12.84 ?  269 HOH A O    1 
HETATM 2131 O  O    . HOH F 6 .   ? 4.975   -4.956  21.099  1.00 13.22 ?  270 HOH A O    1 
HETATM 2132 O  O    . HOH F 6 .   ? -10.628 8.720   25.758  1.00 11.61 ?  271 HOH A O    1 
HETATM 2133 O  O    . HOH F 6 .   ? -2.442  -8.814  29.298  1.00 12.98 ?  272 HOH A O    1 
HETATM 2134 O  O    . HOH F 6 .   ? -3.344  -13.318 25.279  1.00 11.53 ?  273 HOH A O    1 
HETATM 2135 O  O    . HOH F 6 .   ? 1.309   -1.571  29.638  1.00 15.97 ?  274 HOH A O    1 
HETATM 2136 O  O    . HOH F 6 .   ? -3.411  -11.210 21.004  1.00 11.20 ?  275 HOH A O    1 
HETATM 2137 O  O    . HOH F 6 .   ? -21.973 5.736   4.840   1.00 17.91 ?  276 HOH A O    1 
HETATM 2138 O  O    . HOH F 6 .   ? -17.933 -20.545 8.052   1.00 15.71 ?  277 HOH A O    1 
HETATM 2139 O  O    . HOH F 6 .   ? -7.870  -15.457 11.383  1.00 10.62 ?  278 HOH A O    1 
HETATM 2140 O  O    . HOH F 6 .   ? -3.691  -15.947 24.453  1.00 14.38 ?  279 HOH A O    1 
HETATM 2141 O  O    . HOH F 6 .   ? 8.667   -3.822  21.199  1.00 15.85 ?  280 HOH A O    1 
HETATM 2142 O  O    . HOH F 6 .   ? -8.675  -3.830  7.921   1.00 12.19 ?  281 HOH A O    1 
HETATM 2143 O  O    . HOH F 6 .   ? -16.340 -10.027 33.072  1.00 16.47 ?  282 HOH A O    1 
HETATM 2144 O  O    . HOH F 6 .   ? -21.223 7.859   1.914   1.00 16.28 ?  283 HOH A O    1 
HETATM 2145 O  O    . HOH F 6 .   ? -1.997  -12.378 22.959  1.00 11.04 ?  284 HOH A O    1 
HETATM 2146 O  O    . HOH F 6 .   ? 3.763   5.103   29.874  1.00 19.33 ?  285 HOH A O    1 
HETATM 2147 O  O    . HOH F 6 .   ? 5.559   7.148   20.302  1.00 18.20 ?  286 HOH A O    1 
HETATM 2148 O  O    . HOH F 6 .   ? -24.426 -1.480  -6.031  1.00 12.72 ?  287 HOH A O    1 
HETATM 2149 O  O    . HOH F 6 .   ? -13.962 10.538  27.977  1.00 19.79 ?  288 HOH A O    1 
HETATM 2150 O  O    . HOH F 6 .   ? -19.411 10.049  9.054   1.00 15.23 ?  289 HOH A O    1 
HETATM 2151 O  O    . HOH F 6 .   ? -23.217 -2.990  6.737   1.00 20.13 ?  290 HOH A O    1 
HETATM 2152 O  O    . HOH F 6 .   ? -16.154 -12.400 24.557  1.00 15.48 ?  291 HOH A O    1 
HETATM 2153 O  O    . HOH F 6 .   ? -10.351 -18.324 17.044  1.00 16.89 ?  292 HOH A O    1 
HETATM 2154 O  O    . HOH F 6 .   ? -23.021 -11.822 14.247  1.00 20.80 ?  293 HOH A O    1 
HETATM 2155 O  O    . HOH F 6 .   ? -20.452 10.902  26.731  1.00 19.52 ?  294 HOH A O    1 
HETATM 2156 O  O    . HOH F 6 .   ? -24.911 -7.807  9.092   1.00 18.74 ?  295 HOH A O    1 
HETATM 2157 O  O    . HOH F 6 .   ? -24.143 8.722   20.321  1.00 23.73 ?  296 HOH A O    1 
HETATM 2158 O  O    . HOH F 6 .   ? 7.720   6.137   21.885  1.00 18.20 ?  297 HOH A O    1 
HETATM 2159 O  O    . HOH F 6 .   ? -26.806 -2.630  14.474  1.00 21.03 ?  298 HOH A O    1 
HETATM 2160 O  O    . HOH F 6 .   ? -9.936  14.729  12.228  1.00 19.17 ?  299 HOH A O    1 
HETATM 2161 O  O    . HOH F 6 .   ? -12.720 -17.299 16.921  1.00 15.60 ?  300 HOH A O    1 
HETATM 2162 O  O    . HOH F 6 .   ? -28.708 0.243   24.615  1.00 22.74 ?  301 HOH A O    1 
HETATM 2163 O  O    . HOH F 6 .   ? -0.429  10.895  23.576  1.00 16.53 ?  302 HOH A O    1 
HETATM 2164 O  O    . HOH F 6 .   ? -6.034  -4.429  -6.452  1.00 25.62 ?  303 HOH A O    1 
HETATM 2165 O  O    . HOH F 6 .   ? -17.921 10.528  11.436  1.00 17.95 ?  304 HOH A O    1 
HETATM 2166 O  O    . HOH F 6 .   ? -24.011 -0.803  26.698  1.00 18.68 ?  305 HOH A O    1 
HETATM 2167 O  O    . HOH F 6 .   ? -23.852 -0.866  3.981   1.00 23.42 ?  306 HOH A O    1 
HETATM 2168 O  O    . HOH F 6 .   ? -2.510  -3.092  11.563  1.00 18.20 ?  307 HOH A O    1 
HETATM 2169 O  O    . HOH F 6 .   ? 4.408   -3.522  26.653  1.00 18.55 ?  308 HOH A O    1 
HETATM 2170 O  O    . HOH F 6 .   ? -8.093  -19.442 21.743  1.00 17.72 ?  309 HOH A O    1 
HETATM 2171 O  O    . HOH F 6 .   ? -1.044  -11.201 29.077  1.00 20.13 ?  310 HOH A O    1 
HETATM 2172 O  O    . HOH F 6 .   ? -5.109  0.873   10.206  1.00 26.43 ?  311 HOH A O    1 
HETATM 2173 O  O    . HOH F 6 .   ? -14.283 -16.583 29.110  1.00 25.34 ?  312 HOH A O    1 
HETATM 2174 O  O    . HOH F 6 .   ? 1.257   8.860   24.635  1.00 18.48 ?  313 HOH A O    1 
HETATM 2175 O  O    . HOH F 6 .   ? -12.073 2.938   30.975  1.00 24.01 ?  314 HOH A O    1 
HETATM 2176 O  O    . HOH F 6 .   ? -25.883 -6.080  13.156  1.00 32.72 ?  315 HOH A O    1 
HETATM 2177 O  O    . HOH F 6 .   ? 1.436   -11.889 25.132  1.00 21.53 ?  316 HOH A O    1 
HETATM 2178 O  O    . HOH F 6 .   ? 0.032   1.002   34.712  1.00 24.16 ?  317 HOH A O    1 
HETATM 2179 O  O    . HOH F 6 .   ? -9.560  -8.104  34.082  1.00 26.13 ?  318 HOH A O    1 
HETATM 2180 O  O    . HOH F 6 .   ? -8.968  -6.033  35.977  1.00 20.58 ?  319 HOH A O    1 
HETATM 2181 O  O    . HOH F 6 .   ? -7.320  -8.764  32.702  1.00 20.03 ?  320 HOH A O    1 
HETATM 2182 O  O    . HOH F 6 .   ? -6.866  -14.992 31.752  1.00 19.42 ?  321 HOH A O    1 
HETATM 2183 O  O    . HOH F 6 .   ? -30.842 1.392   26.227  1.00 25.92 ?  322 HOH A O    1 
HETATM 2184 O  O    . HOH F 6 .   ? -29.050 -5.892  24.606  1.00 26.16 ?  323 HOH A O    1 
HETATM 2185 O  O    . HOH F 6 .   ? -22.483 3.693   -2.970  1.00 23.05 ?  324 HOH A O    1 
HETATM 2186 O  O    . HOH F 6 .   ? -29.166 -3.817  13.701  1.00 23.09 ?  325 HOH A O    1 
HETATM 2187 O  O    . HOH F 6 .   ? -13.343 -18.574 14.725  1.00 20.56 ?  326 HOH A O    1 
HETATM 2188 O  O    . HOH F 6 .   ? 0.147   -0.970  -4.667  1.00 21.67 ?  327 HOH A O    1 
HETATM 2189 O  O    . HOH F 6 .   ? -6.619  -20.305 19.563  1.00 17.35 ?  328 HOH A O    1 
HETATM 2190 O  O    . HOH F 6 .   ? -13.186 -22.457 11.464  1.00 30.76 ?  329 HOH A O    1 
HETATM 2191 O  O    . HOH F 6 .   ? -22.790 -5.850  2.817   1.00 21.20 ?  330 HOH A O    1 
HETATM 2192 O  O    . HOH F 6 .   ? -19.401 -20.731 4.935   1.00 21.19 ?  331 HOH A O    1 
HETATM 2193 O  O    . HOH F 6 .   ? -4.610  -12.034 32.153  1.00 20.64 ?  332 HOH A O    1 
HETATM 2194 O  O    . HOH F 6 .   ? -1.595  -13.316 27.430  1.00 24.35 ?  333 HOH A O    1 
HETATM 2195 O  O    . HOH F 6 .   ? -27.687 -0.061  15.188  1.00 27.38 ?  334 HOH A O    1 
HETATM 2196 O  O    . HOH F 6 .   ? -22.761 -3.124  -6.068  1.00 22.67 ?  335 HOH A O    1 
HETATM 2197 O  O    . HOH F 6 .   ? -16.186 15.892  23.707  1.00 20.01 ?  336 HOH A O    1 
HETATM 2198 O  O    . HOH F 6 .   ? 2.707   -11.416 9.521   1.00 24.08 ?  337 HOH A O    1 
HETATM 2199 O  O    . HOH F 6 .   ? 8.130   -5.794  -10.466 1.00 24.38 ?  338 HOH A O    1 
HETATM 2200 O  O    . HOH F 6 .   ? -14.548 -18.554 18.872  1.00 22.49 ?  339 HOH A O    1 
HETATM 2201 O  O    . HOH F 6 .   ? -26.475 -11.423 1.986   1.00 26.78 ?  340 HOH A O    1 
HETATM 2202 O  O    . HOH F 6 .   ? -25.650 -10.738 17.705  1.00 24.48 ?  341 HOH A O    1 
HETATM 2203 O  O    . HOH F 6 .   ? -14.851 -21.042 17.607  1.00 25.18 ?  342 HOH A O    1 
HETATM 2204 O  O    . HOH F 6 .   ? -4.105  -0.896  11.953  1.00 22.97 ?  343 HOH A O    1 
HETATM 2205 O  O    . HOH F 6 .   ? 4.435   -2.546  29.064  1.00 25.48 ?  344 HOH A O    1 
HETATM 2206 O  O    . HOH F 6 .   ? -18.891 14.009  35.278  1.00 24.59 ?  345 HOH A O    1 
HETATM 2207 O  O    . HOH F 6 .   ? -1.458  11.491  26.052  1.00 26.72 ?  346 HOH A O    1 
HETATM 2208 O  O    . HOH F 6 .   ? -12.941 -16.937 26.740  1.00 19.15 ?  347 HOH A O    1 
HETATM 2209 O  O    . HOH F 6 .   ? -16.617 5.267   -7.792  1.00 27.85 ?  348 HOH A O    1 
HETATM 2210 O  O    . HOH F 6 .   ? -26.920 -4.095  25.223  1.00 21.87 ?  349 HOH A O    1 
HETATM 2211 O  O    . HOH F 6 .   ? -8.303  -15.254 37.070  1.00 28.92 ?  350 HOH A O    1 
HETATM 2212 O  O    . HOH F 6 .   ? -0.453  -8.679  32.492  1.00 23.01 ?  351 HOH A O    1 
HETATM 2213 O  O    . HOH F 6 .   ? -3.485  -12.962 -2.793  1.00 23.35 ?  352 HOH A O    1 
HETATM 2214 O  O    . HOH F 6 .   ? -11.066 -19.452 7.083   1.00 31.47 ?  353 HOH A O    1 
HETATM 2215 O  O    . HOH F 6 .   ? -25.096 4.576   8.588   1.00 28.95 ?  354 HOH A O    1 
HETATM 2216 O  O    . HOH F 6 .   ? -25.657 9.666   13.649  1.00 29.58 ?  355 HOH A O    1 
HETATM 2217 O  O    . HOH F 6 .   ? -4.209  -8.663  31.357  1.00 21.84 ?  356 HOH A O    1 
HETATM 2218 O  O    . HOH F 6 .   ? -11.002 -15.286 34.173  1.00 24.53 ?  357 HOH A O    1 
HETATM 2219 O  O    . HOH F 6 .   ? -23.646 -13.170 11.522  1.00 24.29 ?  358 HOH A O    1 
HETATM 2220 O  O    . HOH F 6 .   ? -30.985 -6.908  22.577  1.00 31.91 ?  359 HOH A O    1 
HETATM 2221 O  O    . HOH F 6 .   ? -23.308 -0.748  34.529  1.00 26.06 ?  360 HOH A O    1 
HETATM 2222 O  O    . HOH F 6 .   ? -18.597 -3.742  -2.551  1.00 26.09 ?  361 HOH A O    1 
HETATM 2223 O  O    . HOH F 6 .   ? -18.969 12.147  13.100  1.00 25.59 ?  362 HOH A O    1 
HETATM 2224 O  O    . HOH F 6 .   ? -13.627 -21.148 15.098  1.00 23.63 ?  363 HOH A O    1 
HETATM 2225 O  O    . HOH F 6 .   ? -6.194  -19.833 24.036  1.00 25.99 ?  364 HOH A O    1 
HETATM 2226 O  O    . HOH F 6 .   ? -23.636 8.419   3.569   1.00 25.42 ?  365 HOH A O    1 
HETATM 2227 O  O    . HOH F 6 .   ? -33.386 -4.749  23.746  1.00 23.72 ?  366 HOH A O    1 
HETATM 2228 O  O    . HOH F 6 .   ? -8.470  0.608   -6.499  1.00 29.71 ?  367 HOH A O    1 
HETATM 2229 O  O    . HOH F 6 .   ? -18.711 -9.188  34.579  1.00 27.31 ?  368 HOH A O    1 
HETATM 2230 O  O    . HOH F 6 .   ? -7.182  6.034   6.526   1.00 28.09 ?  369 HOH A O    1 
HETATM 2231 O  O    . HOH F 6 .   ? -31.946 -2.560  13.866  1.00 27.81 ?  370 HOH A O    1 
HETATM 2232 O  O    . HOH F 6 .   ? -1.139  9.305   28.184  1.00 24.00 ?  371 HOH A O    1 
HETATM 2233 O  O    . HOH F 6 .   ? 10.671  -8.728  8.698   1.00 33.98 ?  372 HOH A O    1 
HETATM 2234 O  O    . HOH F 6 .   ? -25.918 6.263   27.120  1.00 24.18 ?  373 HOH A O    1 
HETATM 2235 O  O    . HOH F 6 .   ? 4.556   -6.462  7.862   1.00 25.66 ?  374 HOH A O    1 
HETATM 2236 O  O    . HOH F 6 .   ? -15.303 -21.728 13.219  1.00 22.03 ?  375 HOH A O    1 
HETATM 2237 O  O    . HOH F 6 .   ? 12.190  -9.806  -5.868  1.00 25.79 ?  376 HOH A O    1 
HETATM 2238 O  O    . HOH F 6 .   ? 7.962   -1.737  -10.309 1.00 25.68 ?  377 HOH A O    1 
HETATM 2239 O  O    . HOH F 6 .   ? -0.099  -14.367 22.337  1.00 25.34 ?  378 HOH A O    1 
HETATM 2240 O  O    . HOH F 6 .   ? -30.573 -0.512  16.166  1.00 27.25 ?  379 HOH A O    1 
HETATM 2241 O  O    . HOH F 6 .   ? 5.472   -7.065  22.626  1.00 27.54 ?  380 HOH A O    1 
HETATM 2242 O  O    . HOH F 6 .   ? -8.513  -19.913 26.740  1.00 25.06 ?  381 HOH A O    1 
HETATM 2243 O  O    . HOH F 6 .   ? -28.218 11.945  5.286   1.00 24.06 ?  382 HOH A O    1 
HETATM 2244 O  O    . HOH F 6 .   ? 2.837   -4.182  7.689   1.00 24.72 ?  383 HOH A O    1 
HETATM 2245 O  O    . HOH F 6 .   ? -11.931 10.944  0.870   1.00 29.57 ?  384 HOH A O    1 
HETATM 2246 O  O    . HOH F 6 .   ? -1.042  -17.613 17.920  1.00 33.35 ?  385 HOH A O    1 
HETATM 2247 O  O    . HOH F 6 .   ? -11.060 -23.752 12.358  1.00 26.30 ?  386 HOH A O    1 
HETATM 2248 O  O    . HOH F 6 .   ? -5.962  -25.892 11.995  1.00 30.67 ?  387 HOH A O    1 
HETATM 2249 O  O    . HOH F 6 .   ? -17.630 11.021  -2.053  1.00 28.46 ?  388 HOH A O    1 
HETATM 2250 O  O    . HOH F 6 .   ? -5.563  3.692   -5.855  1.00 28.92 ?  389 HOH A O    1 
HETATM 2251 O  O    . HOH F 6 .   ? -22.152 -18.460 13.646  1.00 24.85 ?  390 HOH A O    1 
HETATM 2252 O  O    . HOH F 6 .   ? -24.989 -2.555  -4.134  1.00 30.12 ?  391 HOH A O    1 
HETATM 2253 O  O    . HOH F 6 .   ? 3.899   9.834   23.917  1.00 28.37 ?  392 HOH A O    1 
HETATM 2254 O  O    . HOH F 6 .   ? -4.996  2.115   37.544  1.00 29.90 ?  393 HOH A O    1 
HETATM 2255 O  O    . HOH F 6 .   ? -26.735 -1.380  26.105  1.00 24.30 ?  394 HOH A O    1 
HETATM 2256 O  O    . HOH F 6 .   ? -13.957 14.103  27.359  1.00 27.40 ?  395 HOH A O    1 
HETATM 2257 O  O    . HOH F 6 .   ? -17.401 -16.318 22.041  1.00 27.85 ?  396 HOH A O    1 
HETATM 2258 O  O    . HOH F 6 .   ? -2.020  -12.115 31.649  1.00 31.69 ?  397 HOH A O    1 
HETATM 2259 O  O    . HOH F 6 .   ? -4.631  0.991   43.492  1.00 26.91 ?  398 HOH A O    1 
HETATM 2260 O  O    . HOH F 6 .   ? -33.885 3.278   27.965  1.00 31.09 ?  399 HOH A O    1 
HETATM 2261 O  O    . HOH F 6 .   ? -10.536 -19.397 20.029  1.00 24.91 ?  400 HOH A O    1 
HETATM 2262 O  O    . HOH F 6 .   ? 2.699   -13.076 5.192   1.00 26.16 ?  401 HOH A O    1 
HETATM 2263 O  O    . HOH F 6 .   ? 10.147  -6.857  -8.867  1.00 30.07 ?  402 HOH A O    1 
HETATM 2264 O  O    . HOH F 6 .   ? 1.703   12.605  23.017  1.00 28.14 ?  403 HOH A O    1 
HETATM 2265 O  O    . HOH F 6 .   ? -21.154 13.744  1.881   1.00 28.64 ?  404 HOH A O    1 
HETATM 2266 O  O    . HOH F 6 .   ? -17.621 -21.179 17.764  1.00 27.39 ?  405 HOH A O    1 
HETATM 2267 O  O    . HOH F 6 .   ? 9.874   -4.534  -8.093  1.00 24.37 ?  406 HOH A O    1 
HETATM 2268 O  O    . HOH F 6 .   ? 19.674  -14.477 11.093  1.00 25.58 ?  407 HOH A O    1 
HETATM 2269 O  O    . HOH F 6 .   ? -0.359  13.173  30.019  1.00 29.70 ?  408 HOH A O    1 
HETATM 2270 O  O    . HOH F 6 .   ? -23.984 -16.712 3.697   1.00 34.65 ?  409 HOH A O    1 
HETATM 2271 O  O    . HOH F 6 .   ? -9.777  1.333   39.311  1.00 29.28 ?  410 HOH A O    1 
HETATM 2272 O  O    . HOH F 6 .   ? -16.912 -14.055 26.611  1.00 25.01 ?  411 HOH A O    1 
HETATM 2273 O  O    . HOH F 6 .   ? -5.920  7.027   11.189  1.00 31.02 ?  412 HOH A O    1 
HETATM 2274 O  O    . HOH F 6 .   ? -7.274  -15.559 39.272  1.00 32.40 ?  413 HOH A O    1 
HETATM 2275 O  O    . HOH F 6 .   ? -27.945 5.012   25.310  1.00 28.53 ?  414 HOH A O    1 
HETATM 2276 O  O    . HOH F 6 .   ? -8.512  -1.430  41.266  1.00 36.48 ?  415 HOH A O    1 
HETATM 2277 O  O    . HOH F 6 .   ? -32.561 2.032   12.332  1.00 30.33 ?  416 HOH A O    1 
HETATM 2278 O  O    . HOH F 6 .   ? -6.377  -28.402 10.370  1.00 39.71 ?  417 HOH A O    1 
HETATM 2279 O  O    . HOH F 6 .   ? -21.238 -19.632 6.475   1.00 28.65 ?  418 HOH A O    1 
HETATM 2280 O  O    . HOH F 6 .   ? 1.975   -14.427 20.663  1.00 33.54 ?  419 HOH A O    1 
HETATM 2281 O  O    . HOH F 6 .   ? -17.419 -8.403  -6.414  1.00 30.07 ?  420 HOH A O    1 
HETATM 2282 O  O    . HOH F 6 .   ? -27.992 -1.678  28.523  1.00 28.92 ?  421 HOH A O    1 
HETATM 2283 O  O    . HOH F 6 .   ? -21.971 -14.139 18.620  1.00 30.07 ?  422 HOH A O    1 
HETATM 2284 O  O    . HOH F 6 .   ? -12.819 -22.221 8.473   1.00 32.22 ?  423 HOH A O    1 
HETATM 2285 O  O    . HOH F 6 .   ? 12.318  -11.012 -3.280  1.00 31.25 ?  424 HOH A O    1 
HETATM 2286 O  O    . HOH F 6 .   ? -7.235  -16.835 1.446   1.00 25.60 ?  425 HOH A O    1 
HETATM 2287 O  O    . HOH F 6 .   ? -18.706 -20.676 15.060  1.00 31.05 ?  426 HOH A O    1 
HETATM 2288 O  O    . HOH F 6 .   ? 1.698   -17.536 7.124   1.00 33.40 ?  427 HOH A O    1 
HETATM 2289 O  O    . HOH F 6 .   ? -1.921  -17.512 25.613  1.00 27.30 ?  428 HOH A O    1 
HETATM 2290 O  O    . HOH F 6 .   ? 4.206   -11.723 23.644  1.00 33.86 ?  429 HOH A O    1 
HETATM 2291 O  O    . HOH F 6 .   ? -31.949 5.755   13.035  1.00 38.00 ?  430 HOH A O    1 
HETATM 2292 O  O    . HOH F 6 .   ? -23.910 -7.161  0.234   1.00 28.93 ?  431 HOH A O    1 
HETATM 2293 O  O    . HOH F 6 .   ? -6.521  -5.257  37.644  1.00 25.45 ?  432 HOH A O    1 
HETATM 2294 O  O    . HOH F 6 .   ? -4.764  -20.715 21.556  1.00 23.42 ?  433 HOH A O    1 
HETATM 2295 O  O    . HOH F 6 .   ? 2.036   -15.633 9.305   1.00 28.81 ?  434 HOH A O    1 
HETATM 2296 O  O    . HOH F 6 .   ? -26.343 3.486   15.539  1.00 31.27 ?  435 HOH A O    1 
HETATM 2297 O  O    . HOH F 6 .   ? 2.089   -9.875  30.744  1.00 31.75 ?  436 HOH A O    1 
HETATM 2298 O  O    . HOH F 6 .   ? 0.226   -19.654 11.071  1.00 32.08 ?  437 HOH A O    1 
HETATM 2299 O  O    . HOH F 6 .   ? -9.399  -13.394 42.088  1.00 29.87 ?  438 HOH A O    1 
HETATM 2300 O  O    . HOH F 6 .   ? 2.318   8.113   28.068  1.00 31.36 ?  439 HOH A O    1 
HETATM 2301 O  O    . HOH F 6 .   ? -23.993 -2.722  29.337  1.00 26.51 ?  440 HOH A O    1 
HETATM 2302 O  O    . HOH F 6 .   ? -17.142 -14.152 37.487  1.00 28.39 ?  441 HOH A O    1 
HETATM 2303 O  O    . HOH F 6 .   ? 6.388   -11.091 15.485  1.00 34.11 ?  442 HOH A O    1 
HETATM 2304 O  O    . HOH F 6 .   ? -26.763 3.173   21.087  1.00 31.69 ?  443 HOH A O    1 
HETATM 2305 O  O    . HOH F 6 .   ? -0.285  14.134  16.237  1.00 26.60 ?  444 HOH A O    1 
HETATM 2306 O  O    . HOH F 6 .   ? -27.726 2.413   23.653  1.00 33.46 ?  445 HOH A O    1 
HETATM 2307 O  O    . HOH F 6 .   ? -2.992  7.080   -8.210  1.00 29.45 ?  446 HOH A O    1 
HETATM 2308 O  O    . HOH F 6 .   ? 7.763   -7.476  -0.736  1.00 31.82 ?  447 HOH A O    1 
HETATM 2309 O  O    . HOH F 6 .   ? -19.913 -13.826 24.648  1.00 34.43 ?  448 HOH A O    1 
HETATM 2310 O  O    . HOH F 6 .   ? -12.748 7.976   28.996  1.00 32.09 ?  449 HOH A O    1 
HETATM 2311 O  O    . HOH F 6 .   ? -2.432  -19.145 21.763  1.00 31.92 ?  450 HOH A O    1 
HETATM 2312 O  O    . HOH F 6 .   ? -12.398 12.682  29.403  1.00 32.60 ?  451 HOH A O    1 
HETATM 2313 O  O    . HOH F 6 .   ? -19.458 -4.313  41.679  1.00 32.10 ?  452 HOH A O    1 
HETATM 2314 O  O    . HOH F 6 .   ? -24.008 -17.983 6.631   1.00 34.28 ?  453 HOH A O    1 
HETATM 2315 O  O    . HOH F 6 .   ? -28.477 -0.181  6.640   1.00 36.28 ?  454 HOH A O    1 
HETATM 2316 O  O    . HOH F 6 .   ? -0.308  -19.701 6.577   1.00 31.85 ?  455 HOH A O    1 
HETATM 2317 O  O    . HOH F 6 .   ? -25.939 7.999   6.206   1.00 30.32 ?  456 HOH A O    1 
HETATM 2318 O  O    . HOH F 6 .   ? -17.153 -6.677  42.522  1.00 30.68 ?  457 HOH A O    1 
HETATM 2319 O  O    . HOH F 6 .   ? -16.558 -15.450 32.784  1.00 33.15 ?  458 HOH A O    1 
HETATM 2320 O  O    . HOH F 6 .   ? 2.020   -4.369  -12.357 1.00 34.13 ?  459 HOH A O    1 
HETATM 2321 O  O    . HOH F 6 .   ? -13.744 -0.814  -6.234  1.00 39.63 ?  460 HOH A O    1 
HETATM 2322 O  O    . HOH F 6 .   ? 9.987   -13.205 9.426   1.00 46.99 ?  461 HOH A O    1 
HETATM 2323 O  O    . HOH F 6 .   ? -27.740 6.160   21.734  1.00 30.75 ?  462 HOH A O    1 
HETATM 2324 O  O    . HOH F 6 .   ? -13.011 3.617   -6.859  1.00 32.34 ?  463 HOH A O    1 
HETATM 2325 O  O    . HOH F 6 .   ? 8.287   -5.211  25.340  1.00 32.90 ?  464 HOH A O    1 
HETATM 2326 O  O    . HOH F 6 .   ? -17.870 -12.235 31.711  1.00 32.30 ?  465 HOH A O    1 
HETATM 2327 O  O    . HOH F 6 .   ? -28.362 10.911  15.642  1.00 46.95 ?  466 HOH A O    1 
HETATM 2328 O  O    . HOH F 6 .   ? -16.799 -18.029 20.352  1.00 30.26 ?  467 HOH A O    1 
HETATM 2329 O  O    . HOH F 6 .   ? -29.766 4.136   27.509  1.00 30.84 ?  468 HOH A O    1 
HETATM 2330 O  O    . HOH F 6 .   ? -25.388 -3.115  31.795  1.00 31.68 ?  469 HOH A O    1 
HETATM 2331 O  O    . HOH F 6 .   ? -4.414  -20.795 5.965   1.00 35.81 ?  470 HOH A O    1 
HETATM 2332 O  O    . HOH F 6 .   ? -15.146 -16.197 25.412  1.00 35.60 ?  471 HOH A O    1 
HETATM 2333 O  O    . HOH F 6 .   ? -8.178  7.859   8.516   1.00 34.52 ?  472 HOH A O    1 
HETATM 2334 O  O    . HOH F 6 .   ? -6.563  -19.550 5.330   1.00 35.06 ?  473 HOH A O    1 
HETATM 2335 O  O    . HOH F 6 .   ? 6.775   -3.010  6.939   1.00 41.33 ?  474 HOH A O    1 
HETATM 2336 O  O    . HOH F 6 .   ? -18.034 6.171   34.027  1.00 41.73 ?  475 HOH A O    1 
HETATM 2337 O  O    . HOH F 6 .   ? -0.468  -7.177  -7.482  1.00 40.73 ?  476 HOH A O    1 
HETATM 2338 O  O    . HOH F 6 .   ? 12.529  7.616   20.446  1.00 43.46 ?  477 HOH A O    1 
HETATM 2339 O  O    . HOH F 6 .   ? -3.328  18.046  21.552  1.00 29.27 ?  478 HOH A O    1 
HETATM 2340 O  O    . HOH F 6 .   ? -1.966  7.302   14.320  1.00 34.59 ?  479 HOH A O    1 
HETATM 2341 O  O    . HOH F 6 .   ? -20.043 -15.537 22.683  1.00 29.86 ?  480 HOH A O    1 
HETATM 2342 O  O    . HOH F 6 .   ? -8.517  -17.305 34.941  1.00 27.62 ?  481 HOH A O    1 
HETATM 2343 O  O    . HOH F 6 .   ? -4.311  -7.060  38.116  1.00 35.96 ?  482 HOH A O    1 
HETATM 2344 O  O    . HOH F 6 .   ? -11.585 1.110   -7.729  1.00 36.14 ?  483 HOH A O    1 
HETATM 2345 O  O    . HOH F 6 .   ? -10.368 -19.076 34.690  1.00 29.32 ?  484 HOH A O    1 
HETATM 2346 O  O    . HOH F 6 .   ? -0.800  -17.176 -2.073  1.00 35.26 ?  485 HOH A O    1 
HETATM 2347 O  O    . HOH F 6 .   ? -3.726  -15.571 -2.022  1.00 34.16 ?  486 HOH A O    1 
HETATM 2348 O  O    . HOH F 6 .   ? -18.477 -24.020 -3.897  1.00 34.88 ?  487 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   ? 0.3198 0.3114 0.3991 -0.0110 0.0667  0.0507  4   HIS A N    
2    C  CA   . HIS A 4   ? 0.2956 0.2906 0.3858 -0.0319 0.0319  0.0346  4   HIS A CA   
3    C  C    . HIS A 4   ? 0.2586 0.2598 0.3448 -0.0281 0.0590  0.0053  4   HIS A C    
4    O  O    . HIS A 4   ? 0.2527 0.2668 0.3500 -0.0082 0.0620  -0.0149 4   HIS A O    
5    C  CB   . HIS A 4   ? 0.3648 0.3418 0.4007 -0.0297 0.0213  0.0184  4   HIS A CB   
6    C  CG   . HIS A 4   ? 0.3563 0.4147 0.4535 -0.0168 -0.0114 0.0162  4   HIS A CG   
7    N  ND1  . HIS A 4   ? 0.4392 0.5254 0.4580 -0.0124 -0.0116 0.0024  4   HIS A ND1  
8    C  CD2  . HIS A 4   ? 0.4419 0.4806 0.4566 -0.0071 -0.0030 -0.0294 4   HIS A CD2  
9    C  CE1  . HIS A 4   ? 0.4736 0.4871 0.4866 -0.0295 -0.0174 0.0028  4   HIS A CE1  
10   N  NE2  . HIS A 4   ? 0.4586 0.4939 0.4851 -0.0301 -0.0074 -0.0281 4   HIS A NE2  
11   N  N    . TRP A 5   ? 0.2234 0.2425 0.2933 -0.0424 0.0636  -0.0014 5   TRP A N    
12   C  CA   . TRP A 5   ? 0.1972 0.1985 0.2147 -0.0320 0.0659  -0.0094 5   TRP A CA   
13   C  C    . TRP A 5   ? 0.1796 0.1943 0.2426 -0.0278 0.0641  -0.0045 5   TRP A C    
14   O  O    . TRP A 5   ? 0.2125 0.1720 0.2445 -0.0317 0.0654  -0.0026 5   TRP A O    
15   C  CB   . TRP A 5   ? 0.1543 0.1855 0.2336 -0.0284 0.0537  -0.0118 5   TRP A CB   
16   C  CG   . TRP A 5   ? 0.1948 0.1662 0.2611 -0.0033 0.0601  -0.0113 5   TRP A CG   
17   C  CD1  . TRP A 5   ? 0.2387 0.1914 0.2611 0.0006  0.0378  0.0053  5   TRP A CD1  
18   C  CD2  . TRP A 5   ? 0.1601 0.1972 0.1880 -0.0292 0.0284  -0.0042 5   TRP A CD2  
19   N  NE1  . TRP A 5   ? 0.2451 0.2068 0.2276 -0.0337 0.0369  -0.0031 5   TRP A NE1  
20   C  CE2  . TRP A 5   ? 0.1950 0.1999 0.2011 -0.0158 0.0377  -0.0118 5   TRP A CE2  
21   C  CE3  . TRP A 5   ? 0.1759 0.1998 0.1639 -0.0329 0.0055  -0.0205 5   TRP A CE3  
22   C  CZ2  . TRP A 5   ? 0.2059 0.1941 0.1871 -0.0296 0.0164  -0.0104 5   TRP A CZ2  
23   C  CZ3  . TRP A 5   ? 0.1742 0.1977 0.1492 0.0009  0.0171  -0.0215 5   TRP A CZ3  
24   C  CH2  . TRP A 5   ? 0.2116 0.1859 0.2018 -0.0007 0.0263  -0.0315 5   TRP A CH2  
25   N  N    . GLY A 6   ? 0.1674 0.1500 0.2416 -0.0208 0.0562  -0.0357 6   GLY A N    
26   C  CA   . GLY A 6   ? 0.1808 0.1475 0.2328 -0.0375 0.0326  -0.0288 6   GLY A CA   
27   C  C    . GLY A 6   ? 0.1531 0.1448 0.2384 -0.0070 0.0582  -0.0403 6   GLY A C    
28   O  O    . GLY A 6   ? 0.1396 0.1638 0.2293 -0.0204 0.0363  -0.0525 6   GLY A O    
29   N  N    . TYR A 7   ? 0.1848 0.1588 0.2826 -0.0065 0.0588  -0.0398 7   TYR A N    
30   C  CA   . TYR A 7   ? 0.1876 0.1361 0.3297 0.0029  0.0659  -0.0440 7   TYR A CA   
31   C  C    . TYR A 7   ? 0.2360 0.1668 0.3847 0.0143  0.0726  -0.0459 7   TYR A C    
32   O  O    . TYR A 7   ? 0.2729 0.2138 0.4814 0.0148  0.0912  -0.0306 7   TYR A O    
33   C  CB   . TYR A 7   ? 0.1525 0.1558 0.2568 0.0196  0.0499  -0.0477 7   TYR A CB   
34   C  CG   . TYR A 7   ? 0.1205 0.1112 0.1875 -0.0033 0.0228  -0.0391 7   TYR A CG   
35   C  CD1  . TYR A 7   ? 0.1317 0.1764 0.1491 -0.0498 0.0098  -0.0578 7   TYR A CD1  
36   C  CD2  . TYR A 7   ? 0.1555 0.1244 0.1436 0.0043  0.0306  -0.0425 7   TYR A CD2  
37   C  CE1  . TYR A 7   ? 0.1303 0.1192 0.1717 -0.0012 0.0246  0.0008  7   TYR A CE1  
38   C  CE2  . TYR A 7   ? 0.1547 0.1140 0.1132 -0.0089 0.0305  -0.0397 7   TYR A CE2  
39   C  CZ   . TYR A 7   ? 0.1250 0.1220 0.1196 -0.0285 0.0322  -0.0487 7   TYR A CZ   
40   O  OH   . TYR A 7   ? 0.1257 0.1037 0.1803 0.0083  0.0136  -0.0439 7   TYR A OH   
41   N  N    . GLY A 8   ? 0.2390 0.1834 0.4092 0.0086  0.0888  -0.0735 8   GLY A N    
42   C  CA   . GLY A 8   ? 0.2456 0.1840 0.4122 0.0100  0.0820  -0.0704 8   GLY A CA   
43   C  C    . GLY A 8   ? 0.3012 0.2347 0.4180 0.0211  0.0686  -0.0521 8   GLY A C    
44   O  O    . GLY A 8   ? 0.2797 0.2734 0.4500 0.0206  0.1099  -0.0533 8   GLY A O    
45   N  N    . LYS A 9   ? 0.3180 0.2865 0.4531 0.0252  0.0351  -0.0346 9   LYS A N    
46   C  CA   . LYS A 9   ? 0.3294 0.2852 0.4325 0.0204  0.0249  -0.0372 9   LYS A CA   
47   C  C    . LYS A 9   ? 0.2849 0.3391 0.4247 0.0290  0.0407  -0.0135 9   LYS A C    
48   O  O    . LYS A 9   ? 0.3111 0.3611 0.4411 -0.0020 0.0431  -0.0366 9   LYS A O    
49   C  CB   . LYS A 9   ? 0.3442 0.3798 0.4490 0.0331  0.0128  -0.0165 9   LYS A CB   
50   C  CG   . LYS A 9   ? 0.3699 0.3399 0.4609 0.0416  0.0033  -0.0173 9   LYS A CG   
51   C  CD   . LYS A 9   ? 0.3883 0.3839 0.4594 0.0420  -0.0010 -0.0196 9   LYS A CD   
52   C  CE   . LYS A 9   ? 0.4331 0.5073 0.4889 0.0231  -0.0290 0.0134  9   LYS A CE   
53   N  NZ   . LYS A 9   ? 0.5266 0.5525 0.5038 0.0193  -0.0121 0.0053  9   LYS A NZ   
54   N  N    . HIS A 10  ? 0.2447 0.2739 0.4230 0.0380  0.0820  -0.0161 10  HIS A N    
55   C  CA   . HIS A 10  ? 0.2332 0.2807 0.3921 0.0362  0.0927  -0.0161 10  HIS A CA   
56   C  C    . HIS A 10  ? 0.1895 0.2533 0.3516 0.0384  0.0798  0.0010  10  HIS A C    
57   O  O    . HIS A 10  ? 0.1834 0.2763 0.3713 0.0570  0.0942  -0.0053 10  HIS A O    
58   C  CB   . HIS A 10  ? 0.2303 0.2597 0.3717 0.0289  0.1309  -0.0241 10  HIS A CB   
59   C  CG   . HIS A 10  ? 0.2856 0.3374 0.4146 0.0284  0.0662  0.0024  10  HIS A CG   
60   N  ND1  . HIS A 10  ? 0.3558 0.3882 0.4579 0.0002  0.0598  -0.0132 10  HIS A ND1  
61   C  CD2  . HIS A 10  ? 0.2936 0.3761 0.4286 -0.0193 0.1075  0.0209  10  HIS A CD2  
62   C  CE1  . HIS A 10  ? 0.3168 0.3640 0.4290 0.0190  0.0539  0.0063  10  HIS A CE1  
63   N  NE2  . HIS A 10  ? 0.2771 0.3811 0.3992 0.0045  0.0627  0.0151  10  HIS A NE2  
64   N  N    . ASN A 11  ? 0.1527 0.2427 0.3060 0.0438  0.0971  0.0099  11  ASN A N    
65   C  CA   . ASN A 11  ? 0.1676 0.2237 0.2745 0.0233  0.0762  -0.0160 11  ASN A CA   
66   C  C    . ASN A 11  ? 0.1611 0.2258 0.2636 -0.0007 0.0676  -0.0230 11  ASN A C    
67   O  O    . ASN A 11  ? 0.1746 0.1977 0.2919 0.0125  0.0583  -0.0045 11  ASN A O    
68   C  CB   . ASN A 11  ? 0.1657 0.2241 0.2605 0.0105  0.0645  -0.0248 11  ASN A CB   
69   C  CG   . ASN A 11  ? 0.1984 0.2261 0.2876 0.0040  0.0709  -0.0351 11  ASN A CG   
70   O  OD1  . ASN A 11  ? 0.2245 0.2246 0.3140 -0.0210 0.0730  -0.0455 11  ASN A OD1  
71   N  ND2  . ASN A 11  ? 0.2477 0.1902 0.3125 -0.0297 0.0440  -0.0219 11  ASN A ND2  
72   N  N    . GLY A 12  ? 0.1451 0.2155 0.2541 0.0160  0.0650  -0.0284 12  GLY A N    
73   C  CA   . GLY A 12  ? 0.1523 0.2419 0.2379 0.0045  0.0646  -0.0188 12  GLY A CA   
74   C  C    . GLY A 12  ? 0.1442 0.1970 0.2550 0.0079  0.0436  -0.0204 12  GLY A C    
75   O  O    . GLY A 12  ? 0.0940 0.2014 0.2850 0.0217  0.0455  -0.0016 12  GLY A O    
76   N  N    . PRO A 13  ? 0.1140 0.1810 0.2402 0.0019  0.0451  -0.0107 13  PRO A N    
77   C  CA   . PRO A 13  ? 0.1096 0.1701 0.2305 0.0038  0.0443  -0.0056 13  PRO A CA   
78   C  C    . PRO A 13  ? 0.1244 0.1307 0.2073 0.0043  0.0322  0.0155  13  PRO A C    
79   O  O    . PRO A 13  ? 0.1138 0.1793 0.2464 0.0236  0.0184  -0.0128 13  PRO A O    
80   C  CB   . PRO A 13  ? 0.1210 0.1985 0.2180 -0.0444 0.0504  -0.0147 13  PRO A CB   
81   C  CG   . PRO A 13  ? 0.1679 0.1461 0.2122 0.0048  0.0257  -0.0479 13  PRO A CG   
82   C  CD   . PRO A 13  ? 0.1265 0.1761 0.2185 0.0134  0.0296  -0.0170 13  PRO A CD   
83   N  N    . GLU A 14  ? 0.1137 0.1321 0.2529 -0.0026 0.0270  0.0116  14  GLU A N    
84   C  CA   . GLU A 14  ? 0.1529 0.1405 0.2717 0.0230  0.0030  0.0256  14  GLU A CA   
85   C  C    . GLU A 14  ? 0.1315 0.1674 0.2447 0.0182  0.0071  0.0143  14  GLU A C    
86   O  O    . GLU A 14  ? 0.1365 0.1824 0.2712 0.0376  0.0067  0.0214  14  GLU A O    
87   C  CB   . GLU A 14  ? 0.2002 0.1740 0.2884 0.0320  -0.0009 0.0293  14  GLU A CB   
88   C  CG   . GLU A 14  ? 0.2140 0.2583 0.3148 0.0439  -0.0076 -0.0184 14  GLU A CG   
89   C  CD   . GLU A 14  ? 0.3302 0.3460 0.3914 0.0378  -0.0079 -0.0290 14  GLU A CD   
90   O  OE1  . GLU A 14  ? 0.2572 0.2421 0.3952 0.0565  -0.0445 -0.1096 14  GLU A OE1  
91   O  OE2  . GLU A 14  ? 0.3969 0.2840 0.3609 0.0197  0.0158  -0.0526 14  GLU A OE2  
92   N  N    . HIS A 15  ? 0.1181 0.1526 0.2366 0.0212  0.0017  0.0254  15  HIS A N    
93   C  CA   . HIS A 15  ? 0.1373 0.1430 0.2524 0.0151  0.0350  -0.0116 15  HIS A CA   
94   C  C    . HIS A 15  ? 0.0989 0.1467 0.2239 0.0284  0.0072  -0.0173 15  HIS A C    
95   O  O    . HIS A 15  ? 0.0660 0.1444 0.3052 0.0209  -0.0101 -0.0194 15  HIS A O    
96   C  CB   . HIS A 15  ? 0.1478 0.1463 0.2485 0.0303  0.0279  -0.0031 15  HIS A CB   
97   C  CG   . HIS A 15  ? 0.1562 0.1789 0.2680 0.0462  0.0324  -0.0417 15  HIS A CG   
98   N  ND1  . HIS A 15  ? 0.1517 0.2742 0.2979 0.0531  -0.0187 -0.0195 15  HIS A ND1  
99   C  CD2  . HIS A 15  ? 0.2048 0.2079 0.2379 0.0537  0.0351  -0.0309 15  HIS A CD2  
100  C  CE1  . HIS A 15  ? 0.2233 0.2800 0.2802 0.0528  -0.0166 -0.0118 15  HIS A CE1  
101  N  NE2  . HIS A 15  ? 0.1983 0.1915 0.3377 0.0787  0.0529  -0.0397 15  HIS A NE2  
102  N  N    . TRP A 16  ? 0.0828 0.1433 0.2476 0.0443  0.0075  -0.0085 16  TRP A N    
103  C  CA   . TRP A 16  ? 0.0640 0.1399 0.2149 0.0207  -0.0100 -0.0228 16  TRP A CA   
104  C  C    . TRP A 16  ? 0.0824 0.1649 0.2143 0.0172  -0.0040 -0.0200 16  TRP A C    
105  O  O    . TRP A 16  ? 0.0973 0.1730 0.2190 -0.0088 -0.0281 -0.0122 16  TRP A O    
106  C  CB   . TRP A 16  ? 0.0469 0.1510 0.1835 -0.0159 -0.0088 -0.0108 16  TRP A CB   
107  C  CG   . TRP A 16  ? 0.1109 0.1430 0.2079 0.0091  -0.0057 -0.0220 16  TRP A CG   
108  C  CD1  . TRP A 16  ? 0.1162 0.0910 0.1652 0.0133  -0.0024 0.0018  16  TRP A CD1  
109  C  CD2  . TRP A 16  ? 0.0818 0.1183 0.2065 -0.0226 -0.0221 -0.0269 16  TRP A CD2  
110  N  NE1  . TRP A 16  ? 0.0513 0.1190 0.1890 -0.0173 0.0256  -0.0611 16  TRP A NE1  
111  C  CE2  . TRP A 16  ? 0.0509 0.1045 0.1811 0.0106  0.0070  0.0055  16  TRP A CE2  
112  C  CE3  . TRP A 16  ? 0.0624 0.1021 0.1671 0.0011  -0.0086 0.0194  16  TRP A CE3  
113  C  CZ2  . TRP A 16  ? 0.0880 0.1486 0.1771 -0.0265 -0.0066 -0.0100 16  TRP A CZ2  
114  C  CZ3  . TRP A 16  ? 0.0550 0.1564 0.2008 -0.0101 0.0009  -0.0216 16  TRP A CZ3  
115  C  CH2  . TRP A 16  ? 0.1244 0.1483 0.1805 0.0070  0.0024  -0.0282 16  TRP A CH2  
116  N  N    . HIS A 17  ? 0.0987 0.1848 0.2055 0.0091  0.0027  0.0011  17  HIS A N    
117  C  CA   . HIS A 17  ? 0.0875 0.1955 0.2407 -0.0020 -0.0045 0.0125  17  HIS A CA   
118  C  C    . HIS A 17  ? 0.0815 0.1941 0.2172 -0.0177 0.0035  0.0125  17  HIS A C    
119  O  O    . HIS A 17  ? 0.0844 0.2094 0.3010 -0.0157 -0.0118 -0.0201 17  HIS A O    
120  C  CB   . HIS A 17  ? 0.0842 0.2184 0.1834 0.0195  0.0073  0.0193  17  HIS A CB   
121  C  CG   . HIS A 17  ? 0.1185 0.1776 0.2054 0.0107  -0.0041 0.0517  17  HIS A CG   
122  N  ND1  . HIS A 17  ? 0.1427 0.2168 0.2992 0.0315  -0.0460 0.0410  17  HIS A ND1  
123  C  CD2  . HIS A 17  ? 0.1462 0.2295 0.2311 0.0678  -0.0106 0.0030  17  HIS A CD2  
124  C  CE1  . HIS A 17  ? 0.1422 0.2396 0.2874 0.0709  0.0052  0.0181  17  HIS A CE1  
125  N  NE2  . HIS A 17  ? 0.1457 0.2246 0.2841 0.0559  -0.0172 0.0588  17  HIS A NE2  
126  N  N    . LYS A 18  ? 0.0535 0.1856 0.2790 -0.0230 0.0016  0.0132  18  LYS A N    
127  C  CA   . LYS A 18  ? 0.0978 0.1636 0.2605 -0.0008 0.0198  0.0130  18  LYS A CA   
128  C  C    . LYS A 18  ? 0.1437 0.1893 0.3120 -0.0213 0.0029  0.0187  18  LYS A C    
129  O  O    . LYS A 18  ? 0.1960 0.2391 0.3665 -0.0352 -0.0389 0.0413  18  LYS A O    
130  C  CB   . LYS A 18  ? 0.1478 0.1813 0.2969 0.0045  0.0167  0.0080  18  LYS A CB   
131  C  CG   . LYS A 18  ? 0.1712 0.2077 0.2859 0.0399  0.0005  0.0250  18  LYS A CG   
132  C  CD   . LYS A 18  ? 0.1522 0.2673 0.2559 0.0100  0.0096  -0.0127 18  LYS A CD   
133  C  CE   . LYS A 18  ? 0.1943 0.1493 0.2993 0.0210  0.0054  -0.0165 18  LYS A CE   
134  N  NZ   . LYS A 18  ? 0.1283 0.2226 0.2485 0.0518  -0.0029 0.0408  18  LYS A NZ   
135  N  N    . ASP A 19  ? 0.1283 0.1951 0.2873 -0.0161 0.0114  0.0246  19  ASP A N    
136  C  CA   . ASP A 19  ? 0.1250 0.2234 0.2909 -0.0176 0.0186  0.0184  19  ASP A CA   
137  C  C    . ASP A 19  ? 0.1159 0.1780 0.3019 -0.0216 0.0126  0.0131  19  ASP A C    
138  O  O    . ASP A 19  ? 0.1736 0.1586 0.3666 -0.0263 0.0099  0.0042  19  ASP A O    
139  C  CB   . ASP A 19  ? 0.1737 0.2770 0.2821 0.0030  0.0202  0.0048  19  ASP A CB   
140  C  CG   . ASP A 19  ? 0.2278 0.3572 0.3172 -0.0281 0.0243  -0.0038 19  ASP A CG   
141  O  OD1  . ASP A 19  ? 0.2274 0.3725 0.3817 -0.0395 0.0378  -0.0153 19  ASP A OD1  
142  O  OD2  . ASP A 19  ? 0.3935 0.4887 0.4238 -0.0507 0.0296  -0.0339 19  ASP A OD2  
143  N  N    . PHE A 20  ? 0.0735 0.1743 0.2735 -0.0307 0.0271  0.0227  20  PHE A N    
144  C  CA   . PHE A 20  ? 0.0930 0.1747 0.2387 -0.0208 0.0022  -0.0202 20  PHE A CA   
145  C  C    . PHE A 20  ? 0.1073 0.1688 0.2373 -0.0207 -0.0090 0.0076  20  PHE A C    
146  O  O    . PHE A 20  ? 0.1042 0.1634 0.2524 -0.0177 -0.0187 -0.0230 20  PHE A O    
147  C  CB   . PHE A 20  ? 0.1023 0.2136 0.2464 -0.0495 -0.0053 0.0074  20  PHE A CB   
148  C  CG   . PHE A 20  ? 0.0906 0.2336 0.2401 -0.0093 0.0091  -0.0123 20  PHE A CG   
149  C  CD1  . PHE A 20  ? 0.1388 0.2636 0.2333 -0.0418 0.0059  0.0245  20  PHE A CD1  
150  C  CD2  . PHE A 20  ? 0.1471 0.2412 0.1961 -0.0377 0.0217  -0.0151 20  PHE A CD2  
151  C  CE1  . PHE A 20  ? 0.1601 0.2148 0.2295 -0.0116 -0.0071 0.0238  20  PHE A CE1  
152  C  CE2  . PHE A 20  ? 0.1214 0.2118 0.2293 -0.0194 -0.0147 -0.0229 20  PHE A CE2  
153  C  CZ   . PHE A 20  ? 0.1314 0.2414 0.2442 -0.0517 0.0126  0.0300  20  PHE A CZ   
154  N  N    . PRO A 21  ? 0.1208 0.1766 0.2507 -0.0341 -0.0131 -0.0051 21  PRO A N    
155  C  CA   . PRO A 21  ? 0.1317 0.1901 0.2312 -0.0462 -0.0188 -0.0115 21  PRO A CA   
156  C  C    . PRO A 21  ? 0.1111 0.1695 0.2239 -0.0137 -0.0258 -0.0208 21  PRO A C    
157  O  O    . PRO A 21  ? 0.1158 0.1862 0.2475 -0.0336 -0.0478 -0.0202 21  PRO A O    
158  C  CB   . PRO A 21  ? 0.1250 0.2092 0.2377 -0.0661 -0.0383 0.0123  21  PRO A CB   
159  C  CG   . PRO A 21  ? 0.2332 0.2426 0.2643 -0.0693 -0.0273 0.0197  21  PRO A CG   
160  C  CD   . PRO A 21  ? 0.1484 0.1847 0.2644 -0.0427 -0.0103 0.0140  21  PRO A CD   
161  N  N    A ILE A 22  ? 0.1101 0.1671 0.2196 -0.0085 -0.0172 -0.0223 22  ILE A N    
162  N  N    B ILE A 22  ? 0.1025 0.1572 0.2107 -0.0112 -0.0174 -0.0253 22  ILE A N    
163  C  CA   A ILE A 22  ? 0.1177 0.1474 0.2110 -0.0048 -0.0134 -0.0157 22  ILE A CA   
164  C  CA   B ILE A 22  ? 0.0988 0.1203 0.1926 -0.0071 -0.0156 -0.0219 22  ILE A CA   
165  C  C    A ILE A 22  ? 0.1027 0.1283 0.1831 0.0036  -0.0146 -0.0142 22  ILE A C    
166  C  C    B ILE A 22  ? 0.1048 0.1084 0.1800 0.0021  -0.0130 -0.0163 22  ILE A C    
167  O  O    A ILE A 22  ? 0.0820 0.1469 0.2142 0.0124  -0.0090 -0.0202 22  ILE A O    
168  O  O    B ILE A 22  ? 0.0905 0.1235 0.2172 0.0089  -0.0092 -0.0267 22  ILE A O    
169  C  CB   A ILE A 22  ? 0.1128 0.1456 0.1963 0.0008  -0.0136 -0.0077 22  ILE A CB   
170  C  CB   B ILE A 22  ? 0.0828 0.1255 0.1728 0.0024  -0.0122 -0.0143 22  ILE A CB   
171  C  CG1  A ILE A 22  ? 0.1608 0.1849 0.2147 0.0209  -0.0186 -0.0157 22  ILE A CG1  
172  C  CG1  B ILE A 22  ? 0.1061 0.0954 0.1645 -0.0205 -0.0123 0.0012  22  ILE A CG1  
173  C  CG2  A ILE A 22  ? 0.1515 0.1793 0.1751 -0.0063 0.0000  -0.0031 22  ILE A CG2  
174  C  CG2  B ILE A 22  ? 0.0791 0.1579 0.1693 -0.0037 -0.0250 -0.0106 22  ILE A CG2  
175  C  CD1  A ILE A 22  ? 0.1952 0.2057 0.2251 -0.0193 -0.0243 -0.0078 22  ILE A CD1  
176  C  CD1  B ILE A 22  ? 0.0816 0.0928 0.1794 0.0066  -0.0111 -0.0383 22  ILE A CD1  
177  N  N    . ALA A 23  ? 0.0949 0.1410 0.1809 -0.0063 -0.0101 -0.0268 23  ALA A N    
178  C  CA   . ALA A 23  ? 0.1233 0.1479 0.1641 -0.0102 -0.0027 -0.0341 23  ALA A CA   
179  C  C    . ALA A 23  ? 0.1352 0.1600 0.1907 -0.0015 -0.0217 -0.0049 23  ALA A C    
180  O  O    . ALA A 23  ? 0.1179 0.1557 0.1909 -0.0115 -0.0131 0.0190  23  ALA A O    
181  C  CB   . ALA A 23  ? 0.1270 0.1687 0.1776 0.0105  -0.0013 -0.0347 23  ALA A CB   
182  N  N    . LYS A 24  ? 0.1089 0.1684 0.2143 0.0168  -0.0258 -0.0197 24  LYS A N    
183  C  CA   . LYS A 24  ? 0.0884 0.2254 0.2026 0.0028  -0.0223 -0.0288 24  LYS A CA   
184  C  C    . LYS A 24  ? 0.1194 0.2043 0.1881 0.0077  -0.0438 -0.0328 24  LYS A C    
185  O  O    . LYS A 24  ? 0.1392 0.2646 0.2137 0.0077  -0.0540 -0.0223 24  LYS A O    
186  C  CB   . LYS A 24  ? 0.1074 0.2025 0.2137 0.0146  -0.0232 0.0010  24  LYS A CB   
187  C  CG   . LYS A 24  ? 0.1269 0.2809 0.2625 0.0225  -0.0008 0.0020  24  LYS A CG   
188  C  CD   . LYS A 24  ? 0.1866 0.2980 0.3139 0.0209  -0.0196 0.0145  24  LYS A CD   
189  C  CE   . LYS A 24  ? 0.2627 0.3420 0.3412 -0.0037 0.0015  -0.0018 24  LYS A CE   
190  N  NZ   . LYS A 24  ? 0.3654 0.3019 0.3990 0.0236  0.0287  -0.0238 24  LYS A NZ   
191  N  N    . GLY A 25  ? 0.1189 0.2052 0.2202 0.0290  0.0053  -0.0284 25  GLY A N    
192  C  CA   . GLY A 25  ? 0.0846 0.2229 0.2150 -0.0022 -0.0112 -0.0534 25  GLY A CA   
193  C  C    . GLY A 25  ? 0.1322 0.2101 0.1794 -0.0015 -0.0319 -0.0491 25  GLY A C    
194  O  O    . GLY A 25  ? 0.1520 0.2246 0.1574 0.0091  -0.0370 -0.0262 25  GLY A O    
195  N  N    . GLU A 26  ? 0.1119 0.2400 0.1846 0.0156  -0.0491 -0.0504 26  GLU A N    
196  C  CA   . GLU A 26  ? 0.1409 0.2318 0.1842 0.0084  -0.0310 -0.0475 26  GLU A CA   
197  C  C    . GLU A 26  ? 0.1372 0.1819 0.1619 -0.0165 -0.0197 -0.0350 26  GLU A C    
198  O  O    . GLU A 26  ? 0.1422 0.2321 0.1584 -0.0124 -0.0309 -0.0254 26  GLU A O    
199  C  CB   . GLU A 26  ? 0.1605 0.2656 0.1849 -0.0245 -0.0386 -0.0571 26  GLU A CB   
200  C  CG   . GLU A 26  ? 0.2087 0.3143 0.2419 -0.0197 -0.0292 -0.0480 26  GLU A CG   
201  C  CD   . GLU A 26  ? 0.3464 0.4193 0.3543 -0.0025 -0.0357 -0.0027 26  GLU A CD   
202  O  OE1  . GLU A 26  ? 0.3795 0.4670 0.3373 -0.0180 -0.0430 -0.0126 26  GLU A OE1  
203  O  OE2  . GLU A 26  ? 0.3307 0.5026 0.4503 0.0184  -0.0258 -0.0049 26  GLU A OE2  
204  N  N    . ARG A 27  ? 0.1311 0.1585 0.1441 -0.0120 -0.0406 -0.0356 27  ARG A N    
205  C  CA   . ARG A 27  ? 0.1090 0.1572 0.1237 -0.0060 -0.0184 -0.0333 27  ARG A CA   
206  C  C    . ARG A 27  ? 0.1194 0.1311 0.1122 -0.0007 -0.0012 -0.0220 27  ARG A C    
207  O  O    . ARG A 27  ? 0.1263 0.1315 0.1296 0.0163  -0.0149 -0.0212 27  ARG A O    
208  C  CB   . ARG A 27  ? 0.1749 0.1848 0.1500 0.0012  0.0010  -0.0407 27  ARG A CB   
209  C  CG   . ARG A 27  ? 0.1831 0.1989 0.1858 0.0208  -0.0384 -0.0096 27  ARG A CG   
210  C  CD   . ARG A 27  ? 0.1987 0.2456 0.1918 0.0135  -0.0177 -0.0276 27  ARG A CD   
211  N  NE   . ARG A 27  ? 0.2125 0.2270 0.2282 0.0081  -0.0025 -0.0099 27  ARG A NE   
212  C  CZ   . ARG A 27  ? 0.1822 0.2121 0.1688 0.0045  0.0175  0.0013  27  ARG A CZ   
213  N  NH1  . ARG A 27  ? 0.2076 0.2177 0.1484 0.0309  -0.0168 -0.0992 27  ARG A NH1  
214  N  NH2  . ARG A 27  ? 0.1878 0.1661 0.1910 -0.0378 0.0318  -0.0126 27  ARG A NH2  
215  N  N    . GLN A 28  ? 0.0836 0.1265 0.1256 0.0090  -0.0233 -0.0502 28  GLN A N    
216  C  CA   . GLN A 28  ? 0.0632 0.1171 0.0929 0.0009  -0.0018 -0.0451 28  GLN A CA   
217  C  C    . GLN A 28  ? 0.1142 0.0837 0.0972 0.0000  -0.0236 -0.0278 28  GLN A C    
218  O  O    . GLN A 28  ? 0.1166 0.1380 0.1007 -0.0225 -0.0124 -0.0228 28  GLN A O    
219  C  CB   . GLN A 28  ? 0.0385 0.1413 0.1372 0.0065  -0.0122 -0.0447 28  GLN A CB   
220  C  CG   . GLN A 28  ? 0.0793 0.1368 0.1111 -0.0187 0.0050  -0.0045 28  GLN A CG   
221  C  CD   . GLN A 28  ? 0.0949 0.1226 0.1203 0.0069  0.0084  -0.0216 28  GLN A CD   
222  O  OE1  . GLN A 28  ? 0.0983 0.1094 0.1480 -0.0069 -0.0016 -0.0276 28  GLN A OE1  
223  N  NE2  . GLN A 28  ? 0.0745 0.1004 0.1600 0.0109  -0.0222 -0.0136 28  GLN A NE2  
224  N  N    . SER A 29  ? 0.0769 0.0713 0.1029 0.0048  -0.0227 -0.0303 29  SER A N    
225  C  CA   . SER A 29  ? 0.0819 0.0917 0.1030 0.0032  -0.0429 -0.0382 29  SER A CA   
226  C  C    . SER A 29  ? 0.0764 0.0871 0.1023 0.0036  -0.0145 -0.0017 29  SER A C    
227  O  O    . SER A 29  ? 0.0982 0.1172 0.0906 0.0043  0.0179  -0.0320 29  SER A O    
228  C  CB   . SER A 29  ? 0.0578 0.0997 0.1283 0.0181  -0.0323 -0.0136 29  SER A CB   
229  O  OG   . SER A 29  ? 0.0910 0.0847 0.1317 -0.0035 0.0044  -0.0282 29  SER A OG   
230  N  N    . PRO A 30  ? 0.0848 0.0785 0.0880 0.0038  -0.0194 -0.0150 30  PRO A N    
231  C  CA   . PRO A 30  ? 0.1031 0.0952 0.0806 -0.0005 0.0032  0.0144  30  PRO A CA   
232  C  C    . PRO A 30  ? 0.0679 0.1028 0.0982 0.0047  -0.0063 -0.0010 30  PRO A C    
233  O  O    . PRO A 30  ? 0.0995 0.0855 0.1248 -0.0109 -0.0288 -0.0075 30  PRO A O    
234  C  CB   . PRO A 30  ? 0.0954 0.0860 0.1297 0.0099  -0.0118 -0.0337 30  PRO A CB   
235  C  CG   . PRO A 30  ? 0.1176 0.1212 0.0802 0.0070  0.0118  -0.0142 30  PRO A CG   
236  C  CD   . PRO A 30  ? 0.1056 0.1094 0.1026 0.0076  0.0170  -0.0165 30  PRO A CD   
237  N  N    . VAL A 31  ? 0.0888 0.0760 0.1133 -0.0013 0.0087  0.0090  31  VAL A N    
238  C  CA   . VAL A 31  ? 0.1234 0.0782 0.1066 -0.0218 0.0110  -0.0039 31  VAL A CA   
239  C  C    . VAL A 31  ? 0.1180 0.0856 0.1215 0.0007  0.0048  -0.0043 31  VAL A C    
240  O  O    . VAL A 31  ? 0.1193 0.0896 0.1206 -0.0093 -0.0140 0.0130  31  VAL A O    
241  C  CB   . VAL A 31  ? 0.1247 0.0902 0.1121 0.0036  -0.0016 -0.0031 31  VAL A CB   
242  C  CG1  . VAL A 31  ? 0.1339 0.0754 0.1543 -0.0333 -0.0109 -0.0047 31  VAL A CG1  
243  C  CG2  . VAL A 31  ? 0.1020 0.1049 0.1457 0.0214  0.0050  0.0077  31  VAL A CG2  
244  N  N    . ASP A 32  ? 0.1418 0.0761 0.0980 -0.0139 -0.0169 0.0248  32  ASP A N    
245  C  CA   . ASP A 32  ? 0.1228 0.0760 0.1169 0.0199  -0.0102 0.0272  32  ASP A CA   
246  C  C    . ASP A 32  ? 0.1279 0.1035 0.0979 0.0003  -0.0126 0.0249  32  ASP A C    
247  O  O    . ASP A 32  ? 0.1350 0.1320 0.1182 0.0095  -0.0094 -0.0103 32  ASP A O    
248  C  CB   . ASP A 32  ? 0.1474 0.0813 0.1412 0.0186  0.0027  0.0231  32  ASP A CB   
249  C  CG   . ASP A 32  ? 0.1609 0.1264 0.1666 0.0037  -0.0019 0.0146  32  ASP A CG   
250  O  OD1  . ASP A 32  ? 0.1597 0.0946 0.1198 0.0021  -0.0099 -0.0013 32  ASP A OD1  
251  O  OD2  . ASP A 32  ? 0.2298 0.1456 0.1596 -0.0149 -0.0147 0.0421  32  ASP A OD2  
252  N  N    . ILE A 33  ? 0.1019 0.1074 0.1067 0.0170  -0.0118 0.0093  33  ILE A N    
253  C  CA   . ILE A 33  ? 0.1191 0.1185 0.1152 0.0086  -0.0011 0.0396  33  ILE A CA   
254  C  C    . ILE A 33  ? 0.1436 0.1035 0.0947 -0.0004 -0.0005 0.0076  33  ILE A C    
255  O  O    . ILE A 33  ? 0.2037 0.0974 0.1346 0.0006  0.0140  0.0149  33  ILE A O    
256  C  CB   . ILE A 33  ? 0.1318 0.1275 0.1537 0.0225  -0.0040 0.0438  33  ILE A CB   
257  C  CG1  . ILE A 33  ? 0.0904 0.1102 0.1252 -0.0043 -0.0020 0.0598  33  ILE A CG1  
258  C  CG2  . ILE A 33  ? 0.1432 0.1887 0.1523 -0.0250 0.0330  0.0119  33  ILE A CG2  
259  C  CD1  . ILE A 33  ? 0.1113 0.1295 0.1576 0.0381  -0.0337 0.0119  33  ILE A CD1  
260  N  N    . ASP A 34  ? 0.1799 0.1368 0.0895 0.0218  -0.0008 0.0164  34  ASP A N    
261  C  CA   . ASP A 34  ? 0.2078 0.1706 0.1367 0.0394  0.0137  0.0392  34  ASP A CA   
262  C  C    . ASP A 34  ? 0.2201 0.1649 0.1287 0.0170  0.0180  0.0388  34  ASP A C    
263  O  O    . ASP A 34  ? 0.2857 0.1866 0.1275 0.0345  0.0288  0.0254  34  ASP A O    
264  C  CB   . ASP A 34  ? 0.2471 0.1525 0.1610 0.0239  0.0020  0.0519  34  ASP A CB   
265  C  CG   . ASP A 34  ? 0.2857 0.2155 0.2851 0.0200  0.0303  0.0616  34  ASP A CG   
266  O  OD1  . ASP A 34  ? 0.4232 0.2511 0.2277 0.0655  0.0883  0.0952  34  ASP A OD1  
267  O  OD2  . ASP A 34  ? 0.4177 0.2641 0.4021 0.1160  0.0293  0.1155  34  ASP A OD2  
268  N  N    . THR A 35  ? 0.2252 0.1768 0.1330 0.0339  0.0256  0.0500  35  THR A N    
269  C  CA   . THR A 35  ? 0.2319 0.2074 0.1302 0.0380  0.0263  0.0446  35  THR A CA   
270  C  C    . THR A 35  ? 0.2354 0.1829 0.1182 0.0543  0.0319  0.0465  35  THR A C    
271  O  O    . THR A 35  ? 0.2750 0.2363 0.1650 0.0793  0.0452  0.0411  35  THR A O    
272  C  CB   . THR A 35  ? 0.2566 0.1941 0.1660 0.0367  0.0195  0.0301  35  THR A CB   
273  O  OG1  . THR A 35  ? 0.3015 0.2091 0.1827 0.0065  0.0408  0.0424  35  THR A OG1  
274  C  CG2  . THR A 35  ? 0.2513 0.2257 0.1511 0.0448  0.0246  0.0600  35  THR A CG2  
275  N  N    . HIS A 36  ? 0.2769 0.1952 0.1422 0.0498  0.0534  0.0534  36  HIS A N    
276  C  CA   . HIS A 36  ? 0.3042 0.1743 0.1574 0.0454  0.0246  0.0673  36  HIS A CA   
277  C  C    . HIS A 36  ? 0.3154 0.2396 0.1694 0.0360  0.0302  0.0434  36  HIS A C    
278  O  O    . HIS A 36  ? 0.3481 0.2734 0.2111 0.0386  0.0501  0.0541  36  HIS A O    
279  C  CB   . HIS A 36  ? 0.3279 0.2016 0.1970 0.0369  0.0116  0.0721  36  HIS A CB   
280  C  CG   . HIS A 36  ? 0.3530 0.2352 0.1913 0.0349  -0.0337 0.0565  36  HIS A CG   
281  N  ND1  . HIS A 36  ? 0.4366 0.2301 0.2371 0.0308  -0.0624 0.0759  36  HIS A ND1  
282  C  CD2  . HIS A 36  ? 0.3684 0.2848 0.2061 0.0167  -0.0660 0.0856  36  HIS A CD2  
283  C  CE1  . HIS A 36  ? 0.4320 0.2103 0.2745 0.0494  -0.0393 0.0675  36  HIS A CE1  
284  N  NE2  . HIS A 36  ? 0.4499 0.2999 0.3245 0.0152  -0.0503 0.0566  36  HIS A NE2  
285  N  N    . THR A 37  ? 0.3128 0.2255 0.1674 0.0505  0.0385  0.0325  37  THR A N    
286  C  CA   . THR A 37  ? 0.3361 0.2376 0.2067 0.0399  0.0033  0.0410  37  THR A CA   
287  C  C    . THR A 37  ? 0.2973 0.2094 0.1771 0.0552  -0.0036 0.0298  37  THR A C    
288  O  O    . THR A 37  ? 0.3583 0.2166 0.1890 0.0556  -0.0231 0.0221  37  THR A O    
289  C  CB   . THR A 37  ? 0.3350 0.2587 0.2369 0.0369  -0.0097 0.0394  37  THR A CB   
290  O  OG1  . THR A 37  ? 0.4005 0.3487 0.3082 0.0459  -0.0053 0.0361  37  THR A OG1  
291  C  CG2  . THR A 37  ? 0.3963 0.2772 0.2587 0.0624  -0.0379 0.0264  37  THR A CG2  
292  N  N    . ALA A 38  ? 0.2797 0.2043 0.1383 0.0493  0.0240  0.0222  38  ALA A N    
293  C  CA   . ALA A 38  ? 0.2458 0.1717 0.1307 0.0505  0.0425  0.0074  38  ALA A CA   
294  C  C    . ALA A 38  ? 0.2536 0.1706 0.1739 0.0218  0.0504  0.0158  38  ALA A C    
295  O  O    . ALA A 38  ? 0.2968 0.1772 0.2433 0.0256  0.0669  0.0342  38  ALA A O    
296  C  CB   . ALA A 38  ? 0.2832 0.2014 0.1557 0.0310  0.0289  0.0196  38  ALA A CB   
297  N  N    . LYS A 39  ? 0.2576 0.1849 0.1528 0.0320  0.0366  0.0242  39  LYS A N    
298  C  CA   . LYS A 39  ? 0.2372 0.2212 0.1891 0.0489  0.0134  -0.0012 39  LYS A CA   
299  C  C    . LYS A 39  ? 0.2101 0.2392 0.1604 0.0252  0.0197  0.0005  39  LYS A C    
300  O  O    . LYS A 39  ? 0.1935 0.2174 0.1285 0.0117  0.0216  0.0169  39  LYS A O    
301  C  CB   . LYS A 39  ? 0.2624 0.2371 0.2026 0.0322  0.0160  -0.0073 39  LYS A CB   
302  C  CG   . LYS A 39  ? 0.2647 0.3098 0.1943 0.0434  0.0215  0.0271  39  LYS A CG   
303  C  CD   . LYS A 39  ? 0.2746 0.2742 0.1875 0.0551  0.0126  0.0519  39  LYS A CD   
304  C  CE   . LYS A 39  ? 0.3281 0.3867 0.2152 0.0268  0.0316  0.0206  39  LYS A CE   
305  N  NZ   . LYS A 39  ? 0.3438 0.4050 0.2702 -0.0057 0.0042  0.0652  39  LYS A NZ   
306  N  N    . TYR A 40  ? 0.2333 0.2531 0.1673 0.0138  0.0038  0.0257  40  TYR A N    
307  C  CA   . TYR A 40  ? 0.2172 0.2860 0.1993 0.0039  0.0225  0.0087  40  TYR A CA   
308  C  C    . TYR A 40  ? 0.2129 0.2893 0.1982 0.0215  0.0139  0.0023  40  TYR A C    
309  O  O    . TYR A 40  ? 0.2301 0.3054 0.1760 0.0549  0.0072  -0.0187 40  TYR A O    
310  C  CB   . TYR A 40  ? 0.2178 0.3407 0.1997 -0.0160 0.0424  0.0313  40  TYR A CB   
311  C  CG   . TYR A 40  ? 0.2734 0.3489 0.2358 0.0077  0.0414  0.0200  40  TYR A CG   
312  C  CD1  . TYR A 40  ? 0.2537 0.3142 0.2451 -0.0078 -0.0071 0.0170  40  TYR A CD1  
313  C  CD2  . TYR A 40  ? 0.3327 0.4273 0.2727 0.0191  0.0423  -0.0001 40  TYR A CD2  
314  C  CE1  . TYR A 40  ? 0.2524 0.3687 0.2580 0.0295  0.0103  0.0135  40  TYR A CE1  
315  C  CE2  . TYR A 40  ? 0.3394 0.4610 0.3032 0.0261  0.0135  0.0091  40  TYR A CE2  
316  C  CZ   . TYR A 40  ? 0.2615 0.4141 0.3137 0.0156  0.0009  0.0081  40  TYR A CZ   
317  O  OH   . TYR A 40  ? 0.3059 0.4577 0.3506 0.0492  0.0265  0.0244  40  TYR A OH   
318  N  N    . ASP A 41  ? 0.2368 0.2534 0.1911 0.0374  0.0295  -0.0063 41  ASP A N    
319  C  CA   . ASP A 41  ? 0.2696 0.2911 0.1958 0.0366  0.0069  -0.0124 41  ASP A CA   
320  C  C    . ASP A 41  ? 0.3041 0.3558 0.2482 0.0506  0.0307  0.0018  41  ASP A C    
321  O  O    . ASP A 41  ? 0.3000 0.3615 0.2306 0.0711  0.0325  0.0112  41  ASP A O    
322  C  CB   . ASP A 41  ? 0.3098 0.2876 0.2391 0.0315  -0.0116 -0.0192 41  ASP A CB   
323  C  CG   . ASP A 41  ? 0.3587 0.3092 0.3099 0.0081  0.0085  -0.0174 41  ASP A CG   
324  O  OD1  . ASP A 41  ? 0.4373 0.2549 0.3090 0.0909  -0.0323 -0.0734 41  ASP A OD1  
325  O  OD2  . ASP A 41  ? 0.4545 0.3382 0.3868 -0.0427 0.0120  -0.0150 41  ASP A OD2  
326  N  N    . PRO A 42  ? 0.3262 0.4107 0.2758 0.0588  0.0310  0.0030  42  PRO A N    
327  C  CA   . PRO A 42  ? 0.3247 0.4067 0.2801 0.0457  0.0499  0.0000  42  PRO A CA   
328  C  C    . PRO A 42  ? 0.3569 0.4176 0.2831 0.0366  0.0379  -0.0050 42  PRO A C    
329  O  O    . PRO A 42  ? 0.3638 0.4482 0.3388 0.0386  0.0429  -0.0022 42  PRO A O    
330  C  CB   . PRO A 42  ? 0.3465 0.4443 0.2908 0.0362  0.0542  0.0025  42  PRO A CB   
331  C  CG   . PRO A 42  ? 0.3145 0.4537 0.2824 0.0643  0.0569  -0.0062 42  PRO A CG   
332  C  CD   . PRO A 42  ? 0.3295 0.4060 0.2708 0.0767  0.0481  0.0032  42  PRO A CD   
333  N  N    . SER A 43  ? 0.3814 0.3919 0.2500 0.0349  0.0370  -0.0339 43  SER A N    
334  C  CA   . SER A 43  ? 0.4096 0.3794 0.2718 0.0291  0.0154  -0.0256 43  SER A CA   
335  C  C    . SER A 43  ? 0.4048 0.3510 0.2740 0.0399  0.0127  -0.0127 43  SER A C    
336  O  O    . SER A 43  ? 0.4326 0.3600 0.3127 0.0519  0.0009  -0.0250 43  SER A O    
337  C  CB   . SER A 43  ? 0.4124 0.4089 0.3190 0.0227  0.0110  -0.0277 43  SER A CB   
338  O  OG   . SER A 43  ? 0.4188 0.4082 0.3000 -0.0052 0.0248  -0.0751 43  SER A OG   
339  N  N    . LEU A 44  ? 0.3561 0.3264 0.2462 0.0625  -0.0016 -0.0144 44  LEU A N    
340  C  CA   . LEU A 44  ? 0.3144 0.2920 0.2555 0.0495  0.0023  0.0049  44  LEU A CA   
341  C  C    . LEU A 44  ? 0.3035 0.3155 0.2893 0.0339  0.0004  0.0069  44  LEU A C    
342  O  O    . LEU A 44  ? 0.2929 0.3385 0.3273 0.0328  -0.0081 0.0457  44  LEU A O    
343  C  CB   . LEU A 44  ? 0.2898 0.3049 0.2239 0.0482  0.0231  -0.0168 44  LEU A CB   
344  C  CG   . LEU A 44  ? 0.2749 0.2284 0.2125 0.0264  0.0121  0.0110  44  LEU A CG   
345  C  CD1  . LEU A 44  ? 0.2046 0.2771 0.1848 -0.0007 0.0242  -0.0178 44  LEU A CD1  
346  C  CD2  . LEU A 44  ? 0.3010 0.2257 0.2162 -0.0021 -0.0104 -0.0063 44  LEU A CD2  
347  N  N    . LYS A 45  ? 0.2953 0.3058 0.2698 0.0320  -0.0132 0.0191  45  LYS A N    
348  C  CA   . LYS A 45  ? 0.2865 0.3079 0.2909 0.0133  -0.0139 -0.0172 45  LYS A CA   
349  C  C    . LYS A 45  ? 0.2512 0.3043 0.2832 0.0174  -0.0132 -0.0086 45  LYS A C    
350  O  O    . LYS A 45  ? 0.2433 0.3219 0.2873 0.0037  -0.0189 -0.0317 45  LYS A O    
351  C  CB   . LYS A 45  ? 0.3078 0.2946 0.2797 0.0412  -0.0067 -0.0069 45  LYS A CB   
352  C  CG   . LYS A 45  ? 0.3774 0.3952 0.3455 0.0017  -0.0129 -0.0258 45  LYS A CG   
353  C  CD   . LYS A 45  ? 0.4677 0.4517 0.4851 -0.0016 -0.0045 -0.0210 45  LYS A CD   
354  C  CE   . LYS A 45  ? 0.5730 0.5319 0.5332 0.0178  0.0213  -0.0338 45  LYS A CE   
355  N  NZ   . LYS A 45  ? 0.5809 0.5928 0.5986 0.0095  0.0153  -0.0228 45  LYS A NZ   
356  N  N    . PRO A 46  ? 0.2058 0.2933 0.2758 0.0093  -0.0029 -0.0014 46  PRO A N    
357  C  CA   . PRO A 46  ? 0.1863 0.2797 0.2638 0.0058  -0.0036 0.0050  46  PRO A CA   
358  C  C    . PRO A 46  ? 0.1792 0.2582 0.2357 0.0101  0.0021  0.0044  46  PRO A C    
359  O  O    . PRO A 46  ? 0.1445 0.2655 0.2542 -0.0040 0.0246  -0.0001 46  PRO A O    
360  C  CB   . PRO A 46  ? 0.1591 0.2803 0.2703 -0.0048 -0.0087 -0.0021 46  PRO A CB   
361  C  CG   . PRO A 46  ? 0.1943 0.3459 0.3172 -0.0023 -0.0009 -0.0261 46  PRO A CG   
362  C  CD   . PRO A 46  ? 0.1927 0.2959 0.2824 0.0614  -0.0069 -0.0315 46  PRO A CD   
363  N  N    . LEU A 47  ? 0.1638 0.2659 0.2478 0.0231  -0.0144 0.0089  47  LEU A N    
364  C  CA   . LEU A 47  ? 0.1400 0.2292 0.2345 0.0125  0.0003  0.0049  47  LEU A CA   
365  C  C    . LEU A 47  ? 0.1201 0.2275 0.2685 -0.0041 -0.0120 0.0132  47  LEU A C    
366  O  O    . LEU A 47  ? 0.1134 0.2617 0.3028 -0.0345 -0.0503 0.0513  47  LEU A O    
367  C  CB   . LEU A 47  ? 0.2239 0.2616 0.2827 -0.0151 0.0029  -0.0236 47  LEU A CB   
368  C  CG   . LEU A 47  ? 0.2487 0.2699 0.3299 0.0048  -0.0156 -0.0435 47  LEU A CG   
369  C  CD1  . LEU A 47  ? 0.2852 0.2631 0.3346 -0.0222 -0.0158 -0.0710 47  LEU A CD1  
370  C  CD2  . LEU A 47  ? 0.2281 0.1960 0.3599 0.0386  -0.0461 -0.0731 47  LEU A CD2  
371  N  N    . SER A 48  ? 0.1035 0.1924 0.2388 0.0056  -0.0095 0.0168  48  SER A N    
372  C  CA   . SER A 48  ? 0.1425 0.2019 0.2297 -0.0157 0.0023  -0.0005 48  SER A CA   
373  C  C    . SER A 48  ? 0.1477 0.1943 0.2090 -0.0212 0.0092  -0.0004 48  SER A C    
374  O  O    . SER A 48  ? 0.1511 0.1867 0.2040 -0.0568 0.0171  -0.0286 48  SER A O    
375  C  CB   . SER A 48  ? 0.1553 0.1781 0.2421 0.0077  -0.0149 0.0126  48  SER A CB   
376  O  OG   . SER A 48  ? 0.2190 0.2487 0.2902 0.0398  -0.0356 0.0008  48  SER A OG   
377  N  N    . VAL A 49  ? 0.2102 0.2280 0.2213 -0.0258 0.0077  -0.0121 49  VAL A N    
378  C  CA   . VAL A 49  ? 0.2168 0.2505 0.2480 -0.0482 0.0044  -0.0078 49  VAL A CA   
379  C  C    . VAL A 49  ? 0.2174 0.2840 0.2531 -0.0508 -0.0031 0.0000  49  VAL A C    
380  O  O    . VAL A 49  ? 0.2109 0.3319 0.2717 -0.0924 -0.0238 0.0133  49  VAL A O    
381  C  CB   . VAL A 49  ? 0.2663 0.2445 0.2566 -0.0171 0.0070  -0.0166 49  VAL A CB   
382  C  CG1  . VAL A 49  ? 0.3333 0.2860 0.3076 -0.0491 0.0148  -0.0305 49  VAL A CG1  
383  C  CG2  . VAL A 49  ? 0.2416 0.2620 0.3000 -0.0137 -0.0102 -0.0154 49  VAL A CG2  
384  N  N    . SER A 50  ? 0.2002 0.2449 0.2430 -0.0560 -0.0279 0.0030  50  SER A N    
385  C  CA   . SER A 50  ? 0.1855 0.2531 0.2943 -0.0230 -0.0211 -0.0082 50  SER A CA   
386  C  C    . SER A 50  ? 0.1625 0.2292 0.2739 -0.0177 -0.0333 0.0020  50  SER A C    
387  O  O    . SER A 50  ? 0.1579 0.2168 0.2924 -0.0308 -0.0229 -0.0069 50  SER A O    
388  C  CB   . SER A 50  ? 0.2502 0.2498 0.2871 -0.0155 0.0166  -0.0054 50  SER A CB   
389  O  OG   . SER A 50  ? 0.3474 0.3592 0.3759 -0.0229 0.0024  -0.0266 50  SER A OG   
390  N  N    . TYR A 51  ? 0.1686 0.2316 0.2816 -0.0135 -0.0281 -0.0155 51  TYR A N    
391  C  CA   . TYR A 51  ? 0.1599 0.2198 0.2433 -0.0056 -0.0401 0.0093  51  TYR A CA   
392  C  C    . TYR A 51  ? 0.1675 0.2290 0.2615 -0.0056 -0.0301 0.0141  51  TYR A C    
393  O  O    . TYR A 51  ? 0.2001 0.2208 0.2863 -0.0021 -0.0549 0.0252  51  TYR A O    
394  C  CB   . TYR A 51  ? 0.1573 0.2073 0.2476 -0.0136 -0.0485 -0.0061 51  TYR A CB   
395  C  CG   . TYR A 51  ? 0.1395 0.1501 0.1947 -0.0304 -0.0726 -0.0110 51  TYR A CG   
396  C  CD1  . TYR A 51  ? 0.1290 0.1603 0.2536 -0.0314 -0.0457 -0.0337 51  TYR A CD1  
397  C  CD2  . TYR A 51  ? 0.1507 0.1250 0.2205 -0.0223 -0.0402 -0.0331 51  TYR A CD2  
398  C  CE1  . TYR A 51  ? 0.1254 0.1116 0.2271 -0.0015 -0.0313 0.0244  51  TYR A CE1  
399  C  CE2  . TYR A 51  ? 0.1643 0.1272 0.2056 -0.0437 -0.0457 0.0033  51  TYR A CE2  
400  C  CZ   . TYR A 51  ? 0.1549 0.1344 0.1969 -0.0178 -0.0244 -0.0352 51  TYR A CZ   
401  O  OH   . TYR A 51  ? 0.1574 0.1528 0.1941 -0.0226 -0.0311 -0.0174 51  TYR A OH   
402  N  N    . ASP A 52  ? 0.1972 0.2652 0.3181 -0.0092 -0.0401 0.0301  52  ASP A N    
403  C  CA   . ASP A 52  ? 0.2296 0.2783 0.3007 0.0026  -0.0220 0.0293  52  ASP A CA   
404  C  C    . ASP A 52  ? 0.2714 0.2855 0.3317 0.0109  -0.0272 0.0239  52  ASP A C    
405  O  O    . ASP A 52  ? 0.3039 0.3001 0.3324 0.0217  -0.0377 0.0341  52  ASP A O    
406  C  CB   . ASP A 52  ? 0.2169 0.3198 0.3423 0.0127  -0.0429 0.0117  52  ASP A CB   
407  C  CG   . ASP A 52  ? 0.3200 0.3889 0.3928 0.0240  -0.0054 -0.0004 52  ASP A CG   
408  O  OD1  . ASP A 52  ? 0.3804 0.4957 0.4771 0.0207  -0.0274 0.0287  52  ASP A OD1  
409  O  OD2  . ASP A 52  ? 0.4532 0.4515 0.5359 0.0231  -0.0299 0.0382  52  ASP A OD2  
410  N  N    . GLN A 53  ? 0.2515 0.2678 0.3366 0.0229  -0.0116 0.0171  53  GLN A N    
411  C  CA   . GLN A 53  ? 0.2708 0.2596 0.3597 0.0076  -0.0101 0.0149  53  GLN A CA   
412  C  C    . GLN A 53  ? 0.2547 0.2109 0.2970 0.0237  -0.0078 0.0016  53  GLN A C    
413  O  O    . GLN A 53  ? 0.2200 0.2153 0.3021 0.0076  -0.0283 0.0013  53  GLN A O    
414  C  CB   . GLN A 53  ? 0.3065 0.2685 0.3903 0.0222  -0.0025 0.0010  53  GLN A CB   
415  C  CG   . GLN A 53  ? 0.3411 0.3847 0.4536 -0.0051 0.0069  0.0193  53  GLN A CG   
416  C  CD   . GLN A 53  ? 0.4324 0.5013 0.5038 0.0152  -0.0217 0.0323  53  GLN A CD   
417  O  OE1  . GLN A 53  ? 0.4510 0.5415 0.5629 0.0636  -0.0167 0.0557  53  GLN A OE1  
418  N  NE2  . GLN A 53  ? 0.4725 0.5128 0.5569 0.0121  -0.0121 0.0347  53  GLN A NE2  
419  N  N    . ALA A 54  ? 0.2448 0.1740 0.2683 0.0060  -0.0323 0.0039  54  ALA A N    
420  C  CA   . ALA A 54  ? 0.2204 0.1448 0.1959 -0.0020 -0.0419 -0.0093 54  ALA A CA   
421  C  C    . ALA A 54  ? 0.2377 0.1405 0.2050 0.0018  -0.0525 0.0034  54  ALA A C    
422  O  O    . ALA A 54  ? 0.2565 0.2178 0.2397 -0.0177 -0.0778 -0.0239 54  ALA A O    
423  C  CB   . ALA A 54  ? 0.2409 0.1284 0.2332 -0.0064 -0.0349 0.0109  54  ALA A CB   
424  N  N    . THR A 55  ? 0.2352 0.1263 0.1871 -0.0043 -0.0452 0.0232  55  THR A N    
425  C  CA   . THR A 55  ? 0.2745 0.1195 0.1988 -0.0028 -0.0516 0.0120  55  THR A CA   
426  C  C    . THR A 55  ? 0.2676 0.1090 0.1488 0.0012  -0.0643 -0.0009 55  THR A C    
427  O  O    . THR A 55  ? 0.2889 0.0751 0.1950 -0.0084 -0.0577 -0.0092 55  THR A O    
428  C  CB   . THR A 55  ? 0.2829 0.1240 0.2178 0.0197  -0.0409 0.0075  55  THR A CB   
429  O  OG1  . THR A 55  ? 0.3416 0.1376 0.3177 0.0203  -0.1004 0.0042  55  THR A OG1  
430  C  CG2  . THR A 55  ? 0.3439 0.1859 0.2460 0.0388  -0.0276 0.0449  55  THR A CG2  
431  N  N    . SER A 56  ? 0.2957 0.0744 0.1722 0.0178  -0.0534 0.0015  56  SER A N    
432  C  CA   . SER A 56  ? 0.3061 0.1096 0.1378 0.0037  -0.0418 -0.0025 56  SER A CA   
433  C  C    . SER A 56  ? 0.3089 0.1344 0.1506 0.0092  -0.0422 0.0105  56  SER A C    
434  O  O    . SER A 56  ? 0.3162 0.1845 0.1437 0.0240  -0.0797 -0.0037 56  SER A O    
435  C  CB   . SER A 56  ? 0.3009 0.1139 0.1512 -0.0106 -0.0801 -0.0199 56  SER A CB   
436  O  OG   . SER A 56  ? 0.3482 0.1244 0.1498 -0.0099 -0.0841 0.0185  56  SER A OG   
437  N  N    . LEU A 57  ? 0.3106 0.1599 0.1487 0.0257  -0.0128 0.0295  57  LEU A N    
438  C  CA   . LEU A 57  ? 0.3465 0.1890 0.1819 0.0196  -0.0286 0.0161  57  LEU A CA   
439  C  C    . LEU A 57  ? 0.3312 0.1435 0.1533 0.0302  -0.0329 0.0155  57  LEU A C    
440  O  O    . LEU A 57  ? 0.3506 0.1730 0.1362 0.0150  -0.0631 0.0075  57  LEU A O    
441  C  CB   . LEU A 57  ? 0.3343 0.1729 0.2013 0.0209  -0.0217 0.0259  57  LEU A CB   
442  C  CG   . LEU A 57  ? 0.3714 0.2242 0.2289 0.0035  -0.0244 -0.0314 57  LEU A CG   
443  C  CD1  . LEU A 57  ? 0.3770 0.2388 0.3092 -0.0564 0.0010  -0.0010 57  LEU A CD1  
444  C  CD2  . LEU A 57  ? 0.4054 0.2214 0.2408 0.0340  -0.0389 -0.0246 57  LEU A CD2  
445  N  N    . ARG A 58  ? 0.3055 0.1397 0.1519 0.0431  -0.0424 0.0222  58  ARG A N    
446  C  CA   . ARG A 58  ? 0.2802 0.1558 0.1568 0.0207  -0.0212 0.0379  58  ARG A CA   
447  C  C    . ARG A 58  ? 0.2639 0.1393 0.1401 0.0193  -0.0197 0.0257  58  ARG A C    
448  O  O    . ARG A 58  ? 0.2685 0.1473 0.1347 0.0178  0.0057  0.0369  58  ARG A O    
449  C  CB   . ARG A 58  ? 0.3071 0.1699 0.1992 0.0075  -0.0087 0.0244  58  ARG A CB   
450  C  CG   . ARG A 58  ? 0.2700 0.2310 0.2455 -0.0059 -0.0345 0.0209  58  ARG A CG   
451  C  CD   . ARG A 58  ? 0.3386 0.2545 0.3059 -0.0401 -0.0456 -0.0405 58  ARG A CD   
452  N  NE   . ARG A 58  ? 0.2468 0.2499 0.2799 -0.0036 -0.0256 0.0071  58  ARG A NE   
453  C  CZ   . ARG A 58  ? 0.2409 0.2225 0.2594 -0.0310 -0.0133 0.0223  58  ARG A CZ   
454  N  NH1  . ARG A 58  ? 0.2619 0.2272 0.2860 -0.0369 0.0469  -0.0103 58  ARG A NH1  
455  N  NH2  . ARG A 58  ? 0.2374 0.2397 0.2986 -0.0300 -0.0212 0.0020  58  ARG A NH2  
456  N  N    . ILE A 59  ? 0.2725 0.0976 0.1274 0.0115  -0.0262 0.0090  59  ILE A N    
457  C  CA   . ILE A 59  ? 0.2505 0.1169 0.1374 -0.0114 -0.0310 0.0066  59  ILE A CA   
458  C  C    . ILE A 59  ? 0.2279 0.1261 0.1188 -0.0318 -0.0230 0.0073  59  ILE A C    
459  O  O    . ILE A 59  ? 0.2713 0.1849 0.0969 -0.0087 -0.0129 0.0296  59  ILE A O    
460  C  CB   . ILE A 59  ? 0.2599 0.1017 0.1176 -0.0280 -0.0487 0.0155  59  ILE A CB   
461  C  CG1  . ILE A 59  ? 0.2899 0.1208 0.1129 -0.0019 -0.0256 0.0474  59  ILE A CG1  
462  C  CG2  . ILE A 59  ? 0.2770 0.1680 0.0811 -0.0088 -0.0731 -0.0236 59  ILE A CG2  
463  C  CD1  . ILE A 59  ? 0.2720 0.1367 0.1786 -0.0334 -0.0277 0.0212  59  ILE A CD1  
464  N  N    . LEU A 60  ? 0.2098 0.1703 0.1221 -0.0343 -0.0309 0.0188  60  LEU A N    
465  C  CA   . LEU A 60  ? 0.2313 0.1672 0.1566 -0.0272 -0.0211 0.0191  60  LEU A CA   
466  C  C    . LEU A 60  ? 0.2188 0.1485 0.1484 -0.0371 0.0027  0.0094  60  LEU A C    
467  O  O    . LEU A 60  ? 0.2469 0.1549 0.0961 -0.0293 0.0025  0.0198  60  LEU A O    
468  C  CB   . LEU A 60  ? 0.2332 0.1421 0.2121 -0.0372 -0.0279 0.0162  60  LEU A CB   
469  C  CG   . LEU A 60  ? 0.2521 0.2065 0.1993 -0.0096 -0.0242 0.0014  60  LEU A CG   
470  C  CD1  . LEU A 60  ? 0.3305 0.2030 0.2499 -0.0507 0.0161  0.0415  60  LEU A CD1  
471  C  CD2  . LEU A 60  ? 0.2615 0.1797 0.2003 -0.0457 -0.0037 -0.0206 60  LEU A CD2  
472  N  N    . ASN A 61  ? 0.2078 0.1410 0.1493 -0.0392 0.0044  0.0030  61  ASN A N    
473  C  CA   . ASN A 61  ? 0.2136 0.1432 0.1428 -0.0479 0.0253  -0.0103 61  ASN A CA   
474  C  C    . ASN A 61  ? 0.2242 0.1755 0.1496 -0.0368 0.0141  -0.0146 61  ASN A C    
475  O  O    . ASN A 61  ? 0.2625 0.2061 0.1752 -0.0369 0.0324  0.0226  61  ASN A O    
476  C  CB   . ASN A 61  ? 0.2385 0.1543 0.1225 -0.0268 0.0109  -0.0375 61  ASN A CB   
477  C  CG   . ASN A 61  ? 0.2382 0.1896 0.1363 -0.0220 0.0088  -0.0132 61  ASN A CG   
478  O  OD1  . ASN A 61  ? 0.2838 0.1546 0.1765 -0.0564 0.0316  0.0034  61  ASN A OD1  
479  N  ND2  . ASN A 61  ? 0.3075 0.2078 0.1131 -0.0414 -0.0008 -0.0326 61  ASN A ND2  
480  N  N    . ASN A 62  ? 0.2572 0.1728 0.1338 -0.0503 0.0080  0.0065  62  ASN A N    
481  C  CA   . ASN A 62  ? 0.2232 0.2040 0.1628 -0.0534 0.0046  -0.0050 62  ASN A CA   
482  C  C    . ASN A 62  ? 0.2319 0.1911 0.1972 -0.0578 0.0104  0.0069  62  ASN A C    
483  O  O    . ASN A 62  ? 0.2607 0.2593 0.2389 -0.0682 -0.0002 0.0156  62  ASN A O    
484  C  CB   . ASN A 62  ? 0.2608 0.2156 0.1898 -0.0396 0.0091  -0.0105 62  ASN A CB   
485  C  CG   . ASN A 62  ? 0.2643 0.2561 0.1506 -0.0245 0.0092  -0.0194 62  ASN A CG   
486  O  OD1  . ASN A 62  ? 0.2451 0.1919 0.1306 -0.0813 0.0114  0.0253  62  ASN A OD1  
487  N  ND2  . ASN A 62  ? 0.4203 0.2473 0.2035 0.0144  0.0528  -0.0214 62  ASN A ND2  
488  N  N    . GLY A 63  ? 0.2144 0.1721 0.1990 -0.0578 0.0105  0.0109  63  GLY A N    
489  C  CA   . GLY A 63  ? 0.1935 0.1780 0.1895 -0.0349 0.0246  0.0274  63  GLY A CA   
490  C  C    . GLY A 63  ? 0.1863 0.1604 0.1887 -0.0376 0.0036  0.0083  63  GLY A C    
491  O  O    . GLY A 63  ? 0.1940 0.1792 0.1826 -0.0266 0.0191  0.0112  63  GLY A O    
492  N  N    . HIS A 64  ? 0.1699 0.1554 0.1543 -0.0395 0.0147  0.0086  64  HIS A N    
493  C  CA   A HIS A 64  ? 0.1768 0.1803 0.1700 -0.0237 -0.0014 0.0045  64  HIS A CA   
494  C  CA   B HIS A 64  ? 0.1813 0.1841 0.1797 -0.0219 -0.0035 0.0061  64  HIS A CA   
495  C  C    . HIS A 64  ? 0.1830 0.1449 0.1820 -0.0248 -0.0002 0.0153  64  HIS A C    
496  O  O    . HIS A 64  ? 0.1935 0.2241 0.2666 -0.0418 -0.0015 0.0743  64  HIS A O    
497  C  CB   A HIS A 64  ? 0.1615 0.1660 0.1882 -0.0275 -0.0137 -0.0080 64  HIS A CB   
498  C  CB   B HIS A 64  ? 0.1762 0.1840 0.2043 -0.0251 -0.0266 0.0000  64  HIS A CB   
499  C  CG   A HIS A 64  ? 0.1961 0.1800 0.1469 -0.0422 -0.0062 0.0063  64  HIS A CG   
500  C  CG   B HIS A 64  ? 0.2118 0.2046 0.1877 -0.0058 -0.0253 0.0040  64  HIS A CG   
501  N  ND1  A HIS A 64  ? 0.2181 0.2063 0.1551 -0.0544 -0.0354 -0.0270 64  HIS A ND1  
502  N  ND1  B HIS A 64  ? 0.2181 0.1713 0.2549 0.0009  -0.0247 -0.0134 64  HIS A ND1  
503  C  CD2  A HIS A 64  ? 0.2313 0.1966 0.1690 -0.0380 -0.0066 -0.0091 64  HIS A CD2  
504  C  CD2  B HIS A 64  ? 0.2705 0.2496 0.2623 -0.0083 -0.0102 0.0127  64  HIS A CD2  
505  C  CE1  A HIS A 64  ? 0.1837 0.1817 0.1735 -0.0768 0.0099  0.0218  64  HIS A CE1  
506  C  CE1  B HIS A 64  ? 0.2700 0.2599 0.2687 0.0028  0.0077  -0.0189 64  HIS A CE1  
507  N  NE2  A HIS A 64  ? 0.1660 0.1721 0.1951 -0.0689 0.0345  -0.0220 64  HIS A NE2  
508  N  NE2  B HIS A 64  ? 0.3169 0.2586 0.2128 0.0126  -0.0193 -0.0074 64  HIS A NE2  
509  N  N    . ALA A 65  ? 0.1592 0.1570 0.1405 -0.0303 0.0075  0.0187  65  ALA A N    
510  C  CA   . ALA A 65  ? 0.1708 0.1304 0.1431 -0.0188 -0.0030 0.0110  65  ALA A CA   
511  C  C    . ALA A 65  ? 0.1796 0.1456 0.1053 -0.0171 0.0038  0.0028  65  ALA A C    
512  O  O    . ALA A 65  ? 0.1797 0.1633 0.1299 -0.0332 0.0271  -0.0031 65  ALA A O    
513  C  CB   . ALA A 65  ? 0.1505 0.1433 0.1381 -0.0218 0.0329  0.0130  65  ALA A CB   
514  N  N    . PHE A 66  ? 0.1766 0.1438 0.1276 0.0011  -0.0067 -0.0037 66  PHE A N    
515  C  CA   . PHE A 66  ? 0.2061 0.1587 0.1253 -0.0081 -0.0105 0.0030  66  PHE A CA   
516  C  C    . PHE A 66  ? 0.2033 0.1296 0.1211 -0.0133 -0.0060 0.0086  66  PHE A C    
517  O  O    . PHE A 66  ? 0.2349 0.1215 0.1043 -0.0278 -0.0206 0.0075  66  PHE A O    
518  C  CB   . PHE A 66  ? 0.1697 0.1665 0.1140 -0.0237 -0.0193 0.0066  66  PHE A CB   
519  C  CG   . PHE A 66  ? 0.2101 0.1590 0.1132 -0.0236 -0.0013 -0.0132 66  PHE A CG   
520  C  CD1  . PHE A 66  ? 0.2424 0.2066 0.0877 0.0030  -0.0232 0.0006  66  PHE A CD1  
521  C  CD2  . PHE A 66  ? 0.2857 0.1192 0.0684 -0.0159 -0.0289 0.0166  66  PHE A CD2  
522  C  CE1  . PHE A 66  ? 0.2292 0.1722 0.1476 -0.0161 -0.0396 -0.0240 66  PHE A CE1  
523  C  CE2  . PHE A 66  ? 0.2550 0.1298 0.1254 -0.0022 -0.0023 -0.0108 66  PHE A CE2  
524  C  CZ   . PHE A 66  ? 0.2457 0.1464 0.1254 -0.0174 -0.0297 -0.0055 66  PHE A CZ   
525  N  N    . ASN A 67  ? 0.2185 0.1366 0.1242 -0.0008 -0.0221 0.0305  67  ASN A N    
526  C  CA   . ASN A 67  ? 0.2213 0.1155 0.1312 -0.0052 -0.0376 -0.0031 67  ASN A CA   
527  C  C    . ASN A 67  ? 0.2200 0.1316 0.1404 -0.0159 -0.0256 0.0081  67  ASN A C    
528  O  O    . ASN A 67  ? 0.2274 0.2047 0.1172 -0.0193 -0.0113 0.0199  67  ASN A O    
529  C  CB   . ASN A 67  ? 0.1821 0.1224 0.1427 -0.0251 -0.0346 -0.0125 67  ASN A CB   
530  C  CG   . ASN A 67  ? 0.2455 0.1830 0.2066 -0.0033 -0.0457 0.0301  67  ASN A CG   
531  O  OD1  . ASN A 67  ? 0.2146 0.2086 0.1933 -0.0532 -0.0792 0.0695  67  ASN A OD1  
532  N  ND2  . ASN A 67  ? 0.3196 0.2431 0.2446 -0.0602 -0.0505 0.0062  67  ASN A ND2  
533  N  N    . VAL A 68  ? 0.1951 0.0974 0.1532 0.0196  -0.0388 -0.0187 68  VAL A N    
534  C  CA   . VAL A 68  ? 0.1952 0.0986 0.0974 0.0271  -0.0432 -0.0142 68  VAL A CA   
535  C  C    . VAL A 68  ? 0.2555 0.1197 0.1303 0.0315  -0.0339 -0.0022 68  VAL A C    
536  O  O    . VAL A 68  ? 0.2730 0.0918 0.0835 0.0029  -0.0324 0.0033  68  VAL A O    
537  C  CB   . VAL A 68  ? 0.2221 0.1093 0.1551 0.0173  -0.0692 -0.0206 68  VAL A CB   
538  C  CG1  . VAL A 68  ? 0.2481 0.1297 0.1519 0.0491  -0.0483 -0.0312 68  VAL A CG1  
539  C  CG2  . VAL A 68  ? 0.2098 0.1046 0.1305 -0.0213 -0.0425 -0.0505 68  VAL A CG2  
540  N  N    . GLU A 69  ? 0.2811 0.0884 0.1165 0.0136  -0.0233 0.0036  69  GLU A N    
541  C  CA   . GLU A 69  ? 0.2506 0.1195 0.1580 0.0081  -0.0322 0.0128  69  GLU A CA   
542  C  C    . GLU A 69  ? 0.2875 0.1117 0.1689 0.0279  -0.0294 0.0104  69  GLU A C    
543  O  O    . GLU A 69  ? 0.3466 0.0971 0.1838 0.0502  -0.0696 0.0031  69  GLU A O    
544  C  CB   . GLU A 69  ? 0.2643 0.1453 0.1994 0.0024  -0.0106 0.0099  69  GLU A CB   
545  C  CG   . GLU A 69  ? 0.2258 0.1934 0.2575 -0.0071 -0.0154 0.0252  69  GLU A CG   
546  C  CD   . GLU A 69  ? 0.2959 0.2663 0.2994 0.0184  0.0050  0.0286  69  GLU A CD   
547  O  OE1  . GLU A 69  ? 0.2880 0.2585 0.3265 -0.0016 0.0281  0.0754  69  GLU A OE1  
548  O  OE2  . GLU A 69  ? 0.2563 0.2854 0.3202 0.0068  0.0250  0.0652  69  GLU A OE2  
549  N  N    . PHE A 70  ? 0.2707 0.0756 0.1162 0.0108  -0.0226 0.0239  70  PHE A N    
550  C  CA   . PHE A 70  ? 0.2451 0.0875 0.1319 0.0076  -0.0340 0.0065  70  PHE A CA   
551  C  C    . PHE A 70  ? 0.2430 0.1049 0.1380 -0.0041 -0.0325 0.0142  70  PHE A C    
552  O  O    . PHE A 70  ? 0.2676 0.0931 0.1562 -0.0208 -0.0390 -0.0019 70  PHE A O    
553  C  CB   . PHE A 70  ? 0.2300 0.0797 0.1075 0.0039  -0.0283 0.0031  70  PHE A CB   
554  C  CG   . PHE A 70  ? 0.1930 0.0881 0.1332 -0.0146 -0.0336 0.0347  70  PHE A CG   
555  C  CD1  . PHE A 70  ? 0.2054 0.1128 0.1499 0.0071  -0.0581 0.0364  70  PHE A CD1  
556  C  CD2  . PHE A 70  ? 0.2027 0.1276 0.1610 0.0033  -0.0362 0.0198  70  PHE A CD2  
557  C  CE1  . PHE A 70  ? 0.2222 0.1305 0.1573 -0.0255 0.0082  0.0228  70  PHE A CE1  
558  C  CE2  . PHE A 70  ? 0.1883 0.1389 0.1441 -0.0059 -0.0728 0.0121  70  PHE A CE2  
559  C  CZ   . PHE A 70  ? 0.2411 0.1518 0.1694 -0.0107 -0.0281 0.0323  70  PHE A CZ   
560  N  N    . ASP A 71  ? 0.2644 0.0938 0.1556 0.0018  -0.0351 0.0050  71  ASP A N    
561  C  CA   . ASP A 71  ? 0.2579 0.0891 0.1831 -0.0032 -0.0468 0.0241  71  ASP A CA   
562  C  C    . ASP A 71  ? 0.2418 0.0680 0.1878 -0.0193 -0.0435 0.0179  71  ASP A C    
563  O  O    . ASP A 71  ? 0.2883 0.1454 0.2319 -0.0340 -0.0362 -0.0102 71  ASP A O    
564  C  CB   . ASP A 71  ? 0.2623 0.1172 0.2304 0.0195  -0.0764 0.0122  71  ASP A CB   
565  C  CG   . ASP A 71  ? 0.2694 0.1293 0.1858 0.0028  -0.0955 0.0257  71  ASP A CG   
566  O  OD1  . ASP A 71  ? 0.2763 0.1112 0.2462 -0.0007 -0.1171 0.0424  71  ASP A OD1  
567  O  OD2  . ASP A 71  ? 0.3237 0.1429 0.4101 0.0141  -0.1018 0.0206  71  ASP A OD2  
568  N  N    . ASP A 72  ? 0.2202 0.0792 0.1783 -0.0229 -0.0606 0.0280  72  ASP A N    
569  C  CA   . ASP A 72  ? 0.2136 0.0602 0.1768 -0.0132 -0.0584 0.0122  72  ASP A CA   
570  C  C    . ASP A 72  ? 0.2374 0.1153 0.2206 -0.0087 -0.0707 0.0035  72  ASP A C    
571  O  O    . ASP A 72  ? 0.2757 0.0983 0.2218 -0.0067 -0.0854 -0.0023 72  ASP A O    
572  C  CB   . ASP A 72  ? 0.2340 0.1043 0.1744 -0.0072 -0.0514 0.0239  72  ASP A CB   
573  C  CG   . ASP A 72  ? 0.2535 0.0967 0.1990 -0.0080 -0.0443 -0.0069 72  ASP A CG   
574  O  OD1  . ASP A 72  ? 0.2635 0.1755 0.2107 -0.0376 -0.0570 0.0556  72  ASP A OD1  
575  O  OD2  . ASP A 72  ? 0.2216 0.1839 0.1823 0.0027  -0.0659 -0.0029 72  ASP A OD2  
576  N  N    . SER A 73  ? 0.2655 0.0854 0.2342 -0.0082 -0.0530 0.0232  73  SER A N    
577  C  CA   . SER A 73  ? 0.2676 0.1371 0.2311 -0.0113 -0.0549 -0.0007 73  SER A CA   
578  C  C    . SER A 73  ? 0.2535 0.1498 0.2473 -0.0079 -0.0437 0.0017  73  SER A C    
579  O  O    . SER A 73  ? 0.2602 0.1286 0.2587 -0.0117 -0.0542 0.0151  73  SER A O    
580  C  CB   . SER A 73  ? 0.3086 0.1618 0.2597 -0.0368 -0.0482 0.0244  73  SER A CB   
581  O  OG   . SER A 73  ? 0.2818 0.1536 0.2275 0.0204  -0.0631 0.0447  73  SER A OG   
582  N  N    . GLN A 74  ? 0.2428 0.1587 0.2684 0.0010  -0.0416 0.0008  74  GLN A N    
583  C  CA   . GLN A 74  ? 0.2486 0.2216 0.2667 0.0001  -0.0362 0.0111  74  GLN A CA   
584  C  C    . GLN A 74  ? 0.2444 0.2283 0.2756 -0.0064 -0.0479 -0.0029 74  GLN A C    
585  O  O    . GLN A 74  ? 0.2219 0.2240 0.2791 -0.0188 -0.0408 -0.0150 74  GLN A O    
586  C  CB   . GLN A 74  ? 0.2631 0.2325 0.2957 0.0191  -0.0349 0.0077  74  GLN A CB   
587  C  CG   . GLN A 74  ? 0.2528 0.3109 0.3216 0.0099  -0.0537 0.0196  74  GLN A CG   
588  C  CD   . GLN A 74  ? 0.2809 0.3245 0.3456 -0.0082 -0.0722 0.0215  74  GLN A CD   
589  O  OE1  . GLN A 74  ? 0.3334 0.4446 0.3893 -0.0197 -0.0467 0.0050  74  GLN A OE1  
590  N  NE2  . GLN A 74  ? 0.3199 0.2504 0.3804 0.0026  -0.0443 0.0080  74  GLN A NE2  
591  N  N    . ASP A 75  ? 0.2698 0.2686 0.2833 -0.0006 -0.0555 -0.0089 75  ASP A N    
592  C  CA   . ASP A 75  ? 0.2902 0.2965 0.3257 -0.0068 -0.0420 -0.0140 75  ASP A CA   
593  C  C    . ASP A 75  ? 0.2883 0.3083 0.3264 0.0085  -0.0651 -0.0195 75  ASP A C    
594  O  O    . ASP A 75  ? 0.3073 0.3732 0.4278 -0.0042 -0.0605 -0.0220 75  ASP A O    
595  C  CB   . ASP A 75  ? 0.3369 0.3310 0.3273 0.0131  -0.0458 -0.0178 75  ASP A CB   
596  C  CG   . ASP A 75  ? 0.3755 0.3663 0.3524 -0.0149 -0.0187 -0.0414 75  ASP A CG   
597  O  OD1  . ASP A 75  ? 0.4077 0.4075 0.3799 0.0042  -0.0545 -0.0667 75  ASP A OD1  
598  O  OD2  . ASP A 75  ? 0.4909 0.4932 0.4479 0.0175  0.0337  -0.0370 75  ASP A OD2  
599  N  N    . LYS A 76  ? 0.2749 0.2355 0.2919 0.0263  -0.0724 0.0262  76  LYS A N    
600  C  CA   . LYS A 76  ? 0.2901 0.2145 0.3025 -0.0029 -0.0433 0.0202  76  LYS A CA   
601  C  C    . LYS A 76  ? 0.2867 0.2433 0.2984 0.0001  -0.0528 0.0341  76  LYS A C    
602  O  O    . LYS A 76  ? 0.3348 0.2596 0.3569 -0.0248 -0.0691 0.0199  76  LYS A O    
603  C  CB   . LYS A 76  ? 0.2739 0.2036 0.2553 -0.0095 -0.0645 0.0502  76  LYS A CB   
604  C  CG   . LYS A 76  ? 0.3386 0.1787 0.3059 -0.0056 -0.0232 0.0394  76  LYS A CG   
605  C  CD   . LYS A 76  ? 0.3332 0.2082 0.3051 -0.0184 -0.0204 0.0341  76  LYS A CD   
606  C  CE   . LYS A 76  ? 0.3269 0.2245 0.3219 0.0035  -0.0206 0.0181  76  LYS A CE   
607  N  NZ   . LYS A 76  ? 0.3435 0.2158 0.3317 0.0210  -0.0027 -0.0151 76  LYS A NZ   
608  N  N    . ALA A 77  ? 0.2558 0.2184 0.2731 0.0194  -0.0757 0.0371  77  ALA A N    
609  C  CA   . ALA A 77  ? 0.2299 0.2011 0.2175 -0.0014 -0.0612 0.0279  77  ALA A CA   
610  C  C    . ALA A 77  ? 0.1843 0.1927 0.2191 -0.0108 -0.0626 0.0157  77  ALA A C    
611  O  O    . ALA A 77  ? 0.1868 0.2440 0.2431 -0.0342 -0.0541 -0.0041 77  ALA A O    
612  C  CB   . ALA A 77  ? 0.2674 0.2055 0.2153 0.0178  -0.0650 -0.0021 77  ALA A CB   
613  N  N    . VAL A 78  ? 0.1706 0.1825 0.2117 -0.0092 -0.0550 0.0038  78  VAL A N    
614  C  CA   . VAL A 78  ? 0.1866 0.1717 0.2129 -0.0004 -0.0532 0.0161  78  VAL A CA   
615  C  C    . VAL A 78  ? 0.1797 0.2022 0.2127 -0.0140 -0.0321 0.0166  78  VAL A C    
616  O  O    . VAL A 78  ? 0.1875 0.2003 0.2262 -0.0192 -0.0569 0.0315  78  VAL A O    
617  C  CB   . VAL A 78  ? 0.2053 0.2089 0.2498 0.0155  -0.0378 0.0266  78  VAL A CB   
618  C  CG1  . VAL A 78  ? 0.2694 0.1357 0.2797 0.0225  -0.0336 0.0327  78  VAL A CG1  
619  C  CG2  . VAL A 78  ? 0.2280 0.2220 0.3206 0.0226  0.0166  0.0076  78  VAL A CG2  
620  N  N    . LEU A 79  ? 0.1805 0.1462 0.1522 -0.0141 -0.0469 0.0058  79  LEU A N    
621  C  CA   . LEU A 79  ? 0.1706 0.1563 0.1859 0.0019  -0.0264 -0.0055 79  LEU A CA   
622  C  C    . LEU A 79  ? 0.1893 0.1408 0.1607 -0.0057 -0.0105 0.0020  79  LEU A C    
623  O  O    . LEU A 79  ? 0.1902 0.1760 0.1712 -0.0368 -0.0049 -0.0189 79  LEU A O    
624  C  CB   . LEU A 79  ? 0.1090 0.1725 0.2216 0.0034  -0.0486 0.0291  79  LEU A CB   
625  C  CG   . LEU A 79  ? 0.1702 0.1530 0.2062 -0.0134 -0.0278 -0.0081 79  LEU A CG   
626  C  CD1  . LEU A 79  ? 0.1520 0.1922 0.3151 -0.0134 -0.0231 0.0445  79  LEU A CD1  
627  C  CD2  . LEU A 79  ? 0.1319 0.1841 0.2243 0.0059  -0.0092 0.0236  79  LEU A CD2  
628  N  N    A LYS A 80  ? 0.1683 0.1626 0.1689 -0.0078 -0.0070 -0.0082 80  LYS A N    
629  N  N    B LYS A 80  ? 0.1758 0.1576 0.1658 -0.0073 -0.0078 -0.0169 80  LYS A N    
630  C  CA   A LYS A 80  ? 0.1724 0.1599 0.1951 0.0054  -0.0031 -0.0003 80  LYS A CA   
631  C  CA   B LYS A 80  ? 0.1911 0.1548 0.1969 0.0080  0.0037  -0.0117 80  LYS A CA   
632  C  C    A LYS A 80  ? 0.1495 0.1747 0.1862 0.0070  0.0072  -0.0032 80  LYS A C    
633  C  C    B LYS A 80  ? 0.1730 0.1661 0.1922 0.0077  0.0117  -0.0075 80  LYS A C    
634  O  O    A LYS A 80  ? 0.1164 0.1820 0.1892 -0.0110 -0.0106 -0.0121 80  LYS A O    
635  O  O    B LYS A 80  ? 0.1776 0.1424 0.2084 0.0012  -0.0019 0.0001  80  LYS A O    
636  C  CB   A LYS A 80  ? 0.1717 0.1618 0.2214 0.0180  -0.0216 0.0089  80  LYS A CB   
637  C  CB   B LYS A 80  ? 0.2045 0.1370 0.2197 0.0177  -0.0099 -0.0158 80  LYS A CB   
638  C  CG   A LYS A 80  ? 0.1885 0.1938 0.2480 0.0185  -0.0107 -0.0211 80  LYS A CG   
639  C  CG   B LYS A 80  ? 0.2215 0.1747 0.1990 0.0200  0.0122  -0.0195 80  LYS A CG   
640  C  CD   A LYS A 80  ? 0.2127 0.1899 0.2454 0.0172  -0.0005 0.0214  80  LYS A CD   
641  C  CD   B LYS A 80  ? 0.2256 0.1940 0.2282 0.0207  -0.0071 -0.0081 80  LYS A CD   
642  C  CE   A LYS A 80  ? 0.2536 0.2529 0.3055 0.0126  0.0022  0.0000  80  LYS A CE   
643  C  CE   B LYS A 80  ? 0.2866 0.2755 0.3032 -0.0158 0.0170  0.0096  80  LYS A CE   
644  N  NZ   A LYS A 80  ? 0.3442 0.3372 0.3311 0.0282  0.0025  0.0247  80  LYS A NZ   
645  N  NZ   B LYS A 80  ? 0.2914 0.2981 0.3422 0.0235  0.0183  -0.0009 80  LYS A NZ   
646  N  N    . GLY A 81  ? 0.1658 0.1929 0.1817 0.0060  0.0082  0.0081  81  GLY A N    
647  C  CA   . GLY A 81  ? 0.1769 0.1910 0.2092 0.0185  0.0282  0.0206  81  GLY A CA   
648  C  C    . GLY A 81  ? 0.1879 0.1872 0.1864 0.0110  0.0247  0.0173  81  GLY A C    
649  O  O    . GLY A 81  ? 0.1853 0.1674 0.1986 -0.0035 0.0263  0.0000  81  GLY A O    
650  N  N    . GLY A 82  ? 0.2210 0.1767 0.2318 0.0069  0.0236  -0.0068 82  GLY A N    
651  C  CA   . GLY A 82  ? 0.2074 0.2060 0.2498 0.0108  0.0105  0.0138  82  GLY A CA   
652  C  C    . GLY A 82  ? 0.2211 0.1825 0.2115 0.0304  0.0144  -0.0266 82  GLY A C    
653  O  O    . GLY A 82  ? 0.2638 0.2721 0.2803 0.0626  0.0504  -0.0036 82  GLY A O    
654  N  N    . PRO A 83  ? 0.2203 0.2031 0.2287 0.0277  0.0219  -0.0010 83  PRO A N    
655  C  CA   . PRO A 83  ? 0.1966 0.1729 0.2018 0.0362  0.0182  -0.0129 83  PRO A CA   
656  C  C    . PRO A 83  ? 0.2424 0.2124 0.2254 0.0293  0.0068  -0.0262 83  PRO A C    
657  O  O    . PRO A 83  ? 0.2354 0.2566 0.2271 0.0311  -0.0221 -0.0080 83  PRO A O    
658  C  CB   . PRO A 83  ? 0.1986 0.2071 0.2110 0.0448  0.0030  0.0068  83  PRO A CB   
659  C  CG   . PRO A 83  ? 0.1523 0.1853 0.1899 0.0481  -0.0017 -0.0029 83  PRO A CG   
660  C  CD   . PRO A 83  ? 0.1504 0.1729 0.2135 0.0321  0.0135  -0.0311 83  PRO A CD   
661  N  N    . LEU A 84  ? 0.2316 0.1945 0.1920 0.0372  0.0178  -0.0297 84  LEU A N    
662  C  CA   . LEU A 84  ? 0.2369 0.1522 0.2139 0.0235  0.0094  -0.0477 84  LEU A CA   
663  C  C    . LEU A 84  ? 0.2579 0.2040 0.2686 0.0250  -0.0085 -0.0439 84  LEU A C    
664  O  O    . LEU A 84  ? 0.2823 0.2006 0.2588 0.0284  0.0329  -0.0673 84  LEU A O    
665  C  CB   . LEU A 84  ? 0.1834 0.1395 0.1793 0.0317  0.0119  -0.0365 84  LEU A CB   
666  C  CG   . LEU A 84  ? 0.1296 0.1368 0.1833 0.0101  0.0269  -0.0452 84  LEU A CG   
667  C  CD1  . LEU A 84  ? 0.1542 0.1900 0.1787 0.0364  0.0119  -0.0356 84  LEU A CD1  
668  C  CD2  . LEU A 84  ? 0.1334 0.1189 0.2279 0.0026  -0.0100 -0.0373 84  LEU A CD2  
669  N  N    . ASP A 85  ? 0.3307 0.1750 0.3175 0.0158  -0.0227 -0.0428 85  ASP A N    
670  C  CA   . ASP A 85  ? 0.3965 0.2262 0.3678 0.0085  -0.0144 -0.0452 85  ASP A CA   
671  C  C    . ASP A 85  ? 0.3984 0.2234 0.3770 0.0028  -0.0100 -0.0448 85  ASP A C    
672  O  O    . ASP A 85  ? 0.4480 0.3084 0.4761 0.0326  -0.0072 -0.0215 85  ASP A O    
673  C  CB   . ASP A 85  ? 0.4109 0.2473 0.3613 0.0077  -0.0187 -0.0410 85  ASP A CB   
674  C  CG   . ASP A 85  ? 0.4701 0.3790 0.4438 0.0131  -0.0093 -0.0231 85  ASP A CG   
675  O  OD1  . ASP A 85  ? 0.4630 0.4819 0.4715 -0.0118 -0.0241 -0.0220 85  ASP A OD1  
676  O  OD2  . ASP A 85  ? 0.4474 0.4724 0.5608 0.0166  -0.0141 -0.0418 85  ASP A OD2  
677  N  N    . GLY A 86  ? 0.4229 0.1436 0.3292 -0.0218 -0.0239 -0.0634 86  GLY A N    
678  C  CA   . GLY A 86  ? 0.3845 0.2408 0.3266 -0.0300 -0.0197 -0.0464 86  GLY A CA   
679  C  C    . GLY A 86  ? 0.3744 0.2051 0.2905 -0.0258 0.0126  -0.0599 86  GLY A C    
680  O  O    . GLY A 86  ? 0.3929 0.2834 0.3190 -0.0725 0.0356  -0.0338 86  GLY A O    
681  N  N    . THR A 87  ? 0.2747 0.1894 0.2522 0.0114  0.0322  -0.0451 87  THR A N    
682  C  CA   . THR A 87  ? 0.2369 0.2009 0.2687 0.0214  0.0303  -0.0439 87  THR A CA   
683  C  C    . THR A 87  ? 0.1674 0.1300 0.2456 0.0165  0.0090  -0.0313 87  THR A C    
684  O  O    . THR A 87  ? 0.1874 0.0939 0.2410 0.0052  0.0201  -0.0311 87  THR A O    
685  C  CB   . THR A 87  ? 0.2540 0.2730 0.2724 0.0407  0.0396  -0.0416 87  THR A CB   
686  O  OG1  . THR A 87  ? 0.2738 0.3104 0.4213 0.0521  0.0499  -0.0972 87  THR A OG1  
687  C  CG2  . THR A 87  ? 0.2105 0.2706 0.2916 0.0607  -0.0084 -0.0362 87  THR A CG2  
688  N  N    . TYR A 88  ? 0.1469 0.1123 0.2128 0.0062  0.0005  -0.0330 88  TYR A N    
689  C  CA   . TYR A 88  ? 0.1304 0.1163 0.1857 0.0174  -0.0174 -0.0157 88  TYR A CA   
690  C  C    . TYR A 88  ? 0.1148 0.1245 0.1898 0.0151  -0.0425 0.0149  88  TYR A C    
691  O  O    . TYR A 88  ? 0.1422 0.1819 0.2154 -0.0515 -0.0503 0.0141  88  TYR A O    
692  C  CB   . TYR A 88  ? 0.1205 0.1324 0.2033 0.0091  -0.0444 0.0095  88  TYR A CB   
693  C  CG   . TYR A 88  ? 0.1159 0.1060 0.1192 -0.0025 -0.0248 -0.0045 88  TYR A CG   
694  C  CD1  . TYR A 88  ? 0.1222 0.1293 0.1530 -0.0106 -0.0197 -0.0155 88  TYR A CD1  
695  C  CD2  . TYR A 88  ? 0.0716 0.1367 0.1619 -0.0063 -0.0310 -0.0333 88  TYR A CD2  
696  C  CE1  . TYR A 88  ? 0.1415 0.1217 0.1564 0.0392  0.0010  -0.0052 88  TYR A CE1  
697  C  CE2  . TYR A 88  ? 0.1304 0.0778 0.1453 -0.0041 -0.0108 -0.0164 88  TYR A CE2  
698  C  CZ   . TYR A 88  ? 0.1514 0.1029 0.1673 -0.0100 -0.0288 -0.0145 88  TYR A CZ   
699  O  OH   . TYR A 88  ? 0.1458 0.1400 0.1354 0.0073  -0.0142 -0.0158 88  TYR A OH   
700  N  N    . ARG A 89  ? 0.1247 0.1054 0.1452 0.0282  -0.0159 -0.0090 89  ARG A N    
701  C  CA   . ARG A 89  ? 0.1768 0.0866 0.1587 0.0237  -0.0365 0.0257  89  ARG A CA   
702  C  C    . ARG A 89  ? 0.1137 0.0861 0.1436 0.0113  -0.0294 0.0095  89  ARG A C    
703  O  O    . ARG A 89  ? 0.1052 0.0664 0.1567 -0.0008 -0.0246 0.0081  89  ARG A O    
704  C  CB   . ARG A 89  ? 0.2050 0.0687 0.2264 0.0363  -0.0053 0.0281  89  ARG A CB   
705  C  CG   . ARG A 89  ? 0.2529 0.1978 0.2748 0.0620  -0.0363 0.0535  89  ARG A CG   
706  C  CD   . ARG A 89  ? 0.2889 0.2071 0.3136 0.0660  -0.0482 0.0713  89  ARG A CD   
707  N  NE   . ARG A 89  ? 0.2853 0.3078 0.2373 0.0195  -0.0452 0.0194  89  ARG A NE   
708  C  CZ   . ARG A 89  ? 0.2403 0.2240 0.3480 0.0233  -0.0469 -0.0131 89  ARG A CZ   
709  N  NH1  . ARG A 89  ? 0.3479 0.1758 0.2126 0.0698  -0.0191 -0.0118 89  ARG A NH1  
710  N  NH2  . ARG A 89  ? 0.3097 0.2816 0.3809 0.0088  -0.0056 -0.0897 89  ARG A NH2  
711  N  N    . LEU A 90  ? 0.1549 0.0733 0.1413 -0.0069 -0.0428 -0.0169 90  LEU A N    
712  C  CA   . LEU A 90  ? 0.1612 0.0887 0.1422 -0.0125 -0.0339 -0.0226 90  LEU A CA   
713  C  C    . LEU A 90  ? 0.1759 0.0999 0.1422 -0.0082 -0.0438 0.0056  90  LEU A C    
714  O  O    . LEU A 90  ? 0.1936 0.1136 0.1571 0.0241  -0.0259 0.0325  90  LEU A O    
715  C  CB   . LEU A 90  ? 0.1370 0.0946 0.1542 -0.0108 -0.0434 -0.0221 90  LEU A CB   
716  C  CG   . LEU A 90  ? 0.1729 0.1128 0.0734 0.0039  -0.0674 0.0074  90  LEU A CG   
717  C  CD1  . LEU A 90  ? 0.1508 0.1302 0.1555 0.0166  -0.0560 0.0062  90  LEU A CD1  
718  C  CD2  . LEU A 90  ? 0.1935 0.1341 0.1002 -0.0123 -0.0767 -0.0064 90  LEU A CD2  
719  N  N    . ILE A 91  ? 0.1487 0.0901 0.1251 -0.0208 -0.0145 0.0043  91  ILE A N    
720  C  CA   . ILE A 91  ? 0.1755 0.0745 0.1242 -0.0200 -0.0235 0.0092  91  ILE A CA   
721  C  C    . ILE A 91  ? 0.1881 0.0804 0.1159 -0.0169 -0.0257 0.0146  91  ILE A C    
722  O  O    . ILE A 91  ? 0.1925 0.0761 0.1125 -0.0066 -0.0553 0.0168  91  ILE A O    
723  C  CB   . ILE A 91  ? 0.1868 0.0828 0.1303 -0.0210 -0.0143 0.0276  91  ILE A CB   
724  C  CG1  . ILE A 91  ? 0.1850 0.1216 0.1412 -0.0423 0.0055  0.0064  91  ILE A CG1  
725  C  CG2  . ILE A 91  ? 0.1974 0.1254 0.1227 0.0010  -0.0279 0.0274  91  ILE A CG2  
726  C  CD1  . ILE A 91  ? 0.2042 0.1920 0.1624 -0.0495 -0.0222 -0.0247 91  ILE A CD1  
727  N  N    . GLN A 92  ? 0.1975 0.0639 0.1425 -0.0129 -0.0150 0.0170  92  GLN A N    
728  C  CA   . GLN A 92  ? 0.2007 0.0496 0.1338 -0.0080 -0.0039 0.0263  92  GLN A CA   
729  C  C    . GLN A 92  ? 0.1638 0.0435 0.1021 -0.0016 -0.0039 0.0118  92  GLN A C    
730  O  O    . GLN A 92  ? 0.2157 0.0518 0.0754 -0.0139 -0.0222 0.0175  92  GLN A O    
731  C  CB   . GLN A 92  ? 0.2155 0.0870 0.1413 -0.0116 -0.0085 0.0187  92  GLN A CB   
732  C  CG   . GLN A 92  ? 0.1840 0.0998 0.1807 0.0350  -0.0446 0.0457  92  GLN A CG   
733  C  CD   . GLN A 92  ? 0.1997 0.0989 0.1047 -0.0300 -0.0333 0.0195  92  GLN A CD   
734  O  OE1  . GLN A 92  ? 0.2027 0.1058 0.1657 -0.0328 -0.0209 0.0347  92  GLN A OE1  
735  N  NE2  . GLN A 92  ? 0.2035 0.2413 0.2366 -0.0216 -0.0447 0.0321  92  GLN A NE2  
736  N  N    . PHE A 93  ? 0.1720 0.0254 0.0934 0.0048  -0.0447 -0.0015 93  PHE A N    
737  C  CA   . PHE A 93  ? 0.1389 0.0330 0.1054 0.0008  -0.0180 -0.0095 93  PHE A CA   
738  C  C    . PHE A 93  ? 0.1448 0.0619 0.0973 -0.0223 -0.0092 0.0090  93  PHE A C    
739  O  O    . PHE A 93  ? 0.1865 0.0875 0.0822 0.0141  -0.0353 0.0038  93  PHE A O    
740  C  CB   . PHE A 93  ? 0.1346 0.0943 0.0714 -0.0260 -0.0503 0.0162  93  PHE A CB   
741  C  CG   . PHE A 93  ? 0.1832 0.0808 0.1148 0.0011  -0.0343 -0.0208 93  PHE A CG   
742  C  CD1  . PHE A 93  ? 0.1642 0.1167 0.0807 0.0036  -0.0485 -0.0291 93  PHE A CD1  
743  C  CD2  . PHE A 93  ? 0.1611 0.1004 0.1360 -0.0021 -0.1004 0.0457  93  PHE A CD2  
744  C  CE1  . PHE A 93  ? 0.2045 0.0699 0.0828 0.0005  -0.0605 -0.0135 93  PHE A CE1  
745  C  CE2  . PHE A 93  ? 0.2089 0.0990 0.1196 0.0122  -0.0636 0.0261  93  PHE A CE2  
746  C  CZ   . PHE A 93  ? 0.2118 0.1221 0.0953 0.0033  -0.0791 0.0133  93  PHE A CZ   
747  N  N    . HIS A 94  ? 0.1297 0.0597 0.1107 -0.0053 -0.0251 0.0229  94  HIS A N    
748  C  CA   . HIS A 94  ? 0.1056 0.0492 0.0948 -0.0075 -0.0184 0.0169  94  HIS A CA   
749  C  C    . HIS A 94  ? 0.1342 0.0781 0.0894 -0.0064 -0.0311 0.0094  94  HIS A C    
750  O  O    . HIS A 94  ? 0.1376 0.0797 0.1030 0.0083  -0.0081 0.0200  94  HIS A O    
751  C  CB   . HIS A 94  ? 0.1380 0.0805 0.0571 -0.0149 -0.0269 -0.0027 94  HIS A CB   
752  C  CG   . HIS A 94  ? 0.1340 0.0905 0.0552 0.0136  -0.0174 -0.0005 94  HIS A CG   
753  N  ND1  . HIS A 94  ? 0.1637 0.0685 0.0548 0.0063  -0.0172 0.0110  94  HIS A ND1  
754  C  CD2  . HIS A 94  ? 0.1399 0.0657 0.1122 -0.0259 -0.0361 -0.0187 94  HIS A CD2  
755  C  CE1  . HIS A 94  ? 0.1344 0.0877 0.0740 -0.0176 -0.0094 0.0236  94  HIS A CE1  
756  N  NE2  . HIS A 94  ? 0.1480 0.0697 0.1035 -0.0386 -0.0354 -0.0295 94  HIS A NE2  
757  N  N    . PHE A 95  ? 0.1113 0.0638 0.1159 0.0237  -0.0270 0.0159  95  PHE A N    
758  C  CA   . PHE A 95  ? 0.1045 0.0600 0.1027 0.0172  -0.0282 -0.0089 95  PHE A CA   
759  C  C    . PHE A 95  ? 0.1204 0.0669 0.1156 -0.0102 -0.0448 -0.0018 95  PHE A C    
760  O  O    . PHE A 95  ? 0.1263 0.0595 0.1314 -0.0065 -0.0220 0.0158  95  PHE A O    
761  C  CB   . PHE A 95  ? 0.1291 0.0965 0.0879 -0.0149 -0.0552 -0.0122 95  PHE A CB   
762  C  CG   . PHE A 95  ? 0.1147 0.0768 0.0524 -0.0257 -0.0315 0.0064  95  PHE A CG   
763  C  CD1  . PHE A 95  ? 0.1473 0.0750 0.0942 0.0153  -0.0178 -0.0158 95  PHE A CD1  
764  C  CD2  . PHE A 95  ? 0.1033 0.0846 0.1538 -0.0500 -0.0370 -0.0312 95  PHE A CD2  
765  C  CE1  . PHE A 95  ? 0.1201 0.0571 0.1027 0.0069  -0.0343 -0.0052 95  PHE A CE1  
766  C  CE2  . PHE A 95  ? 0.1567 0.0581 0.0942 -0.0102 -0.0583 0.0087  95  PHE A CE2  
767  C  CZ   . PHE A 95  ? 0.1292 0.0689 0.1238 -0.0009 -0.0356 0.0072  95  PHE A CZ   
768  N  N    . HIS A 96  ? 0.1394 0.0617 0.0930 -0.0036 -0.0386 0.0059  96  HIS A N    
769  C  CA   . HIS A 96  ? 0.1067 0.0631 0.1079 0.0012  -0.0510 0.0071  96  HIS A CA   
770  C  C    . HIS A 96  ? 0.1012 0.0705 0.0965 -0.0083 -0.0297 0.0047  96  HIS A C    
771  O  O    . HIS A 96  ? 0.1298 0.0825 0.0905 -0.0204 0.0194  -0.0268 96  HIS A O    
772  C  CB   . HIS A 96  ? 0.1224 0.0877 0.1113 -0.0131 -0.0269 -0.0243 96  HIS A CB   
773  C  CG   . HIS A 96  ? 0.1234 0.0792 0.1253 -0.0097 -0.0176 -0.0131 96  HIS A CG   
774  N  ND1  . HIS A 96  ? 0.1133 0.0665 0.1637 -0.0296 -0.0128 0.0100  96  HIS A ND1  
775  C  CD2  . HIS A 96  ? 0.1441 0.0728 0.1437 -0.0072 -0.0177 0.0289  96  HIS A CD2  
776  C  CE1  . HIS A 96  ? 0.0671 0.1124 0.1398 -0.0448 0.0391  -0.0006 96  HIS A CE1  
777  N  NE2  . HIS A 96  ? 0.0906 0.0643 0.1172 -0.0010 0.0111  -0.0057 96  HIS A NE2  
778  N  N    . TRP A 97  ? 0.1097 0.0458 0.1358 -0.0020 -0.0181 -0.0204 97  TRP A N    
779  C  CA   . TRP A 97  ? 0.1213 0.0458 0.1016 0.0189  -0.0293 -0.0365 97  TRP A CA   
780  C  C    . TRP A 97  ? 0.1187 0.0807 0.0882 0.0057  -0.0062 -0.0283 97  TRP A C    
781  O  O    . TRP A 97  ? 0.1246 0.1018 0.1035 -0.0007 0.0095  -0.0161 97  TRP A O    
782  C  CB   . TRP A 97  ? 0.1284 0.0945 0.1170 -0.0093 -0.0453 -0.0193 97  TRP A CB   
783  C  CG   . TRP A 97  ? 0.1441 0.0840 0.1031 -0.0038 0.0000  -0.0134 97  TRP A CG   
784  C  CD1  . TRP A 97  ? 0.1689 0.1060 0.1075 -0.0399 -0.0016 -0.0451 97  TRP A CD1  
785  C  CD2  . TRP A 97  ? 0.1212 0.1118 0.0767 -0.0268 -0.0266 -0.0084 97  TRP A CD2  
786  N  NE1  . TRP A 97  ? 0.1882 0.1060 0.1185 0.0108  0.0153  0.0005  97  TRP A NE1  
787  C  CE2  . TRP A 97  ? 0.1663 0.0895 0.1005 -0.0253 -0.0093 -0.0310 97  TRP A CE2  
788  C  CE3  . TRP A 97  ? 0.1602 0.1183 0.0815 -0.0043 -0.0054 -0.0255 97  TRP A CE3  
789  C  CZ2  . TRP A 97  ? 0.1729 0.1146 0.1187 -0.0150 0.0063  -0.0044 97  TRP A CZ2  
790  C  CZ3  . TRP A 97  ? 0.1392 0.1139 0.0914 -0.0108 -0.0115 0.0002  97  TRP A CZ3  
791  C  CH2  . TRP A 97  ? 0.1633 0.1303 0.1368 -0.0004 0.0275  -0.0171 97  TRP A CH2  
792  N  N    . GLY A 98  ? 0.1543 0.0745 0.1157 0.0086  -0.0083 -0.0250 98  GLY A N    
793  C  CA   . GLY A 98  ? 0.1312 0.1065 0.1129 0.0121  0.0052  -0.0427 98  GLY A CA   
794  C  C    . GLY A 98  ? 0.1416 0.1056 0.1192 0.0027  0.0132  -0.0377 98  GLY A C    
795  O  O    . GLY A 98  ? 0.1834 0.1111 0.1355 0.0097  0.0110  -0.0341 98  GLY A O    
796  N  N    . SER A 99  ? 0.1504 0.1073 0.1564 0.0005  0.0202  -0.0599 99  SER A N    
797  C  CA   . SER A 99  ? 0.1568 0.1151 0.1559 -0.0006 0.0178  -0.0532 99  SER A CA   
798  C  C    . SER A 99  ? 0.1837 0.1037 0.1748 0.0037  0.0135  -0.0537 99  SER A C    
799  O  O    . SER A 99  ? 0.2506 0.1378 0.1965 -0.0078 0.0199  -0.0580 99  SER A O    
800  C  CB   . SER A 99  ? 0.1942 0.1727 0.1802 0.0079  0.0257  -0.0699 99  SER A CB   
801  O  OG   . SER A 99  ? 0.1669 0.1403 0.2232 0.0058  0.0291  -0.0509 99  SER A OG   
802  N  N    . LEU A 100 ? 0.1487 0.1266 0.1996 -0.0005 0.0046  -0.0379 100 LEU A N    
803  C  CA   . LEU A 100 ? 0.1548 0.1519 0.2208 0.0064  0.0127  -0.0046 100 LEU A CA   
804  C  C    . LEU A 100 ? 0.1766 0.1452 0.1841 -0.0151 0.0087  -0.0258 100 LEU A C    
805  O  O    . LEU A 100 ? 0.1653 0.1030 0.1545 -0.0020 -0.0003 -0.0256 100 LEU A O    
806  C  CB   . LEU A 100 ? 0.2335 0.1898 0.2670 0.0073  0.0100  0.0177  100 LEU A CB   
807  C  CG   . LEU A 100 ? 0.2838 0.2455 0.2514 0.0141  0.0171  -0.0096 100 LEU A CG   
808  C  CD1  . LEU A 100 ? 0.3208 0.4092 0.3506 0.0287  0.0004  -0.0120 100 LEU A CD1  
809  C  CD2  . LEU A 100 ? 0.4127 0.3154 0.3698 0.0102  0.0253  -0.0537 100 LEU A CD2  
810  N  N    . ASP A 101 ? 0.1462 0.1185 0.1924 -0.0095 -0.0036 -0.0112 101 ASP A N    
811  C  CA   . ASP A 101 ? 0.1743 0.1165 0.1911 -0.0364 -0.0028 -0.0054 101 ASP A CA   
812  C  C    . ASP A 101 ? 0.1836 0.1169 0.1990 -0.0202 -0.0052 -0.0076 101 ASP A C    
813  O  O    . ASP A 101 ? 0.2551 0.1094 0.2096 0.0061  -0.0040 0.0030  101 ASP A O    
814  C  CB   . ASP A 101 ? 0.1768 0.1230 0.1891 -0.0353 -0.0191 -0.0081 101 ASP A CB   
815  C  CG   . ASP A 101 ? 0.2423 0.1761 0.2365 -0.0318 -0.0100 0.0007  101 ASP A CG   
816  O  OD1  . ASP A 101 ? 0.2239 0.1416 0.2275 -0.0490 -0.0125 0.0069  101 ASP A OD1  
817  O  OD2  . ASP A 101 ? 0.3747 0.1672 0.3088 -0.0875 -0.0542 -0.0145 101 ASP A OD2  
818  N  N    . GLY A 102 ? 0.2111 0.0829 0.1868 -0.0191 -0.0246 -0.0008 102 GLY A N    
819  C  CA   . GLY A 102 ? 0.1870 0.0993 0.1838 -0.0277 -0.0320 0.0094  102 GLY A CA   
820  C  C    . GLY A 102 ? 0.1727 0.0721 0.1519 -0.0111 -0.0128 0.0010  102 GLY A C    
821  O  O    . GLY A 102 ? 0.1999 0.1230 0.1670 -0.0270 -0.0142 0.0155  102 GLY A O    
822  N  N    . GLN A 103 ? 0.1612 0.0565 0.1636 -0.0055 -0.0099 0.0026  103 GLN A N    
823  C  CA   . GLN A 103 ? 0.1469 0.0593 0.1539 0.0044  -0.0092 -0.0077 103 GLN A CA   
824  C  C    . GLN A 103 ? 0.1261 0.0668 0.1344 -0.0009 -0.0018 -0.0135 103 GLN A C    
825  O  O    . GLN A 103 ? 0.1706 0.0757 0.1426 0.0125  -0.0182 0.0000  103 GLN A O    
826  C  CB   . GLN A 103 ? 0.1655 0.0884 0.1624 0.0044  0.0199  -0.0087 103 GLN A CB   
827  C  CG   . GLN A 103 ? 0.1334 0.1247 0.1540 0.0230  0.0370  -0.0255 103 GLN A CG   
828  C  CD   . GLN A 103 ? 0.1655 0.1304 0.1893 0.0292  0.0147  0.0068  103 GLN A CD   
829  O  OE1  . GLN A 103 ? 0.2651 0.2773 0.2903 0.0910  0.0523  0.1146  103 GLN A OE1  
830  N  NE2  . GLN A 103 ? 0.1995 0.1456 0.2518 0.0124  0.0500  0.0556  103 GLN A NE2  
831  N  N    . GLY A 104 ? 0.1359 0.0609 0.1278 0.0231  -0.0094 -0.0272 104 GLY A N    
832  C  CA   . GLY A 104 ? 0.1408 0.0587 0.1505 0.0047  0.0055  -0.0274 104 GLY A CA   
833  C  C    . GLY A 104 ? 0.1017 0.0857 0.1224 0.0015  -0.0177 -0.0214 104 GLY A C    
834  O  O    . GLY A 104 ? 0.1396 0.1120 0.1306 0.0127  0.0033  0.0021  104 GLY A O    
835  N  N    . SER A 105 ? 0.0992 0.0831 0.0841 0.0035  0.0210  -0.0354 105 SER A N    
836  C  CA   . SER A 105 ? 0.1101 0.0918 0.0874 -0.0133 -0.0073 -0.0177 105 SER A CA   
837  C  C    . SER A 105 ? 0.0949 0.0741 0.1060 -0.0253 -0.0106 -0.0139 105 SER A C    
838  O  O    . SER A 105 ? 0.1403 0.0566 0.1186 0.0062  -0.0298 -0.0382 105 SER A O    
839  C  CB   . SER A 105 ? 0.1024 0.1054 0.0903 -0.0286 0.0048  0.0097  105 SER A CB   
840  O  OG   . SER A 105 ? 0.1390 0.0635 0.1162 -0.0070 0.0051  0.0116  105 SER A OG   
841  N  N    . GLU A 106 ? 0.1002 0.0802 0.0827 -0.0098 -0.0129 -0.0386 106 GLU A N    
842  C  CA   . GLU A 106 ? 0.1273 0.0561 0.0683 -0.0267 -0.0021 -0.0071 106 GLU A CA   
843  C  C    . GLU A 106 ? 0.0953 0.0599 0.0880 0.0096  0.0099  0.0087  106 GLU A C    
844  O  O    . GLU A 106 ? 0.0934 0.0901 0.1399 0.0195  -0.0152 -0.0078 106 GLU A O    
845  C  CB   . GLU A 106 ? 0.1539 0.0613 0.0906 -0.0256 0.0157  0.0141  106 GLU A CB   
846  C  CG   . GLU A 106 ? 0.1809 0.0736 0.1055 -0.0560 -0.0123 0.0099  106 GLU A CG   
847  C  CD   . GLU A 106 ? 0.0923 0.0990 0.1247 -0.0178 -0.0276 -0.0151 106 GLU A CD   
848  O  OE1  . GLU A 106 ? 0.0917 0.0853 0.1687 0.0049  0.0043  0.0064  106 GLU A OE1  
849  O  OE2  . GLU A 106 ? 0.1039 0.1078 0.1836 -0.0027 0.0025  0.0108  106 GLU A OE2  
850  N  N    . HIS A 107 ? 0.0885 0.0518 0.1070 0.0165  0.0310  -0.0227 107 HIS A N    
851  C  CA   . HIS A 107 ? 0.0957 0.0503 0.0953 0.0153  0.0208  -0.0117 107 HIS A CA   
852  C  C    . HIS A 107 ? 0.0954 0.0659 0.1001 0.0164  -0.0133 -0.0034 107 HIS A C    
853  O  O    . HIS A 107 ? 0.1138 0.0656 0.1190 -0.0064 -0.0202 -0.0171 107 HIS A O    
854  C  CB   . HIS A 107 ? 0.1036 0.0759 0.0887 0.0313  0.0133  -0.0042 107 HIS A CB   
855  C  CG   . HIS A 107 ? 0.0762 0.0450 0.1007 0.0204  0.0015  -0.0155 107 HIS A CG   
856  N  ND1  . HIS A 107 ? 0.1357 0.0885 0.1203 0.0238  -0.0352 0.0167  107 HIS A ND1  
857  C  CD2  . HIS A 107 ? 0.1026 0.0972 0.0842 -0.0191 -0.0142 -0.0173 107 HIS A CD2  
858  C  CE1  . HIS A 107 ? 0.1076 0.1300 0.0850 0.0329  -0.0344 -0.0230 107 HIS A CE1  
859  N  NE2  . HIS A 107 ? 0.0962 0.0525 0.0948 0.0015  -0.0132 0.0020  107 HIS A NE2  
860  N  N    . THR A 108 ? 0.1292 0.0797 0.0863 0.0005  -0.0198 0.0238  108 THR A N    
861  C  CA   . THR A 108 ? 0.1139 0.0716 0.0982 0.0154  0.0085  0.0078  108 THR A CA   
862  C  C    . THR A 108 ? 0.1144 0.0877 0.0957 -0.0022 0.0081  0.0285  108 THR A C    
863  O  O    . THR A 108 ? 0.1308 0.0942 0.1190 -0.0023 -0.0081 0.0261  108 THR A O    
864  C  CB   . THR A 108 ? 0.1148 0.0982 0.1121 0.0272  -0.0279 0.0051  108 THR A CB   
865  O  OG1  . THR A 108 ? 0.1282 0.0969 0.0997 0.0114  -0.0284 0.0034  108 THR A OG1  
866  C  CG2  . THR A 108 ? 0.1595 0.1100 0.0825 0.0032  0.0042  -0.0023 108 THR A CG2  
867  N  N    . VAL A 109 ? 0.1123 0.0773 0.1299 -0.0017 0.0148  0.0326  109 VAL A N    
868  C  CA   . VAL A 109 ? 0.0942 0.0766 0.1139 0.0243  -0.0019 0.0402  109 VAL A CA   
869  C  C    . VAL A 109 ? 0.1460 0.0808 0.1296 0.0153  0.0101  0.0052  109 VAL A C    
870  O  O    . VAL A 109 ? 0.1624 0.0632 0.1496 -0.0044 -0.0027 -0.0028 109 VAL A O    
871  C  CB   . VAL A 109 ? 0.0994 0.1263 0.1942 0.0174  0.0195  0.0221  109 VAL A CB   
872  C  CG1  . VAL A 109 ? 0.1058 0.2011 0.1767 -0.0014 0.0166  0.0492  109 VAL A CG1  
873  C  CG2  . VAL A 109 ? 0.1150 0.0992 0.1831 0.0227  -0.0150 0.0450  109 VAL A CG2  
874  N  N    . ASP A 110 ? 0.1499 0.0876 0.1434 0.0182  -0.0124 0.0267  110 ASP A N    
875  C  CA   . ASP A 110 ? 0.1630 0.1079 0.1279 0.0111  0.0150  0.0255  110 ASP A CA   
876  C  C    . ASP A 110 ? 0.1729 0.0950 0.1181 0.0232  0.0049  0.0218  110 ASP A C    
877  O  O    . ASP A 110 ? 0.1964 0.0999 0.1652 -0.0017 0.0055  0.0191  110 ASP A O    
878  C  CB   . ASP A 110 ? 0.1952 0.1401 0.1509 0.0142  0.0229  0.0330  110 ASP A CB   
879  C  CG   . ASP A 110 ? 0.2309 0.1024 0.1363 -0.0067 0.0300  0.0535  110 ASP A CG   
880  O  OD1  . ASP A 110 ? 0.2910 0.1313 0.1688 0.0094  0.0324  0.0173  110 ASP A OD1  
881  O  OD2  . ASP A 110 ? 0.2606 0.2657 0.1967 -0.0238 0.0233  0.0399  110 ASP A OD2  
882  N  N    . LYS A 111 ? 0.1791 0.0742 0.1218 0.0121  0.0032  0.0104  111 LYS A N    
883  C  CA   . LYS A 111 ? 0.1798 0.1089 0.1284 0.0269  -0.0275 0.0140  111 LYS A CA   
884  C  C    . LYS A 111 ? 0.1783 0.0905 0.1379 0.0072  -0.0091 0.0004  111 LYS A C    
885  O  O    . LYS A 111 ? 0.1938 0.1334 0.1484 0.0069  0.0083  -0.0201 111 LYS A O    
886  C  CB   . LYS A 111 ? 0.1991 0.1344 0.1860 0.0340  -0.0254 0.0283  111 LYS A CB   
887  C  CG   . LYS A 111 ? 0.2482 0.1787 0.1848 0.0627  -0.0562 0.0304  111 LYS A CG   
888  C  CD   . LYS A 111 ? 0.2188 0.2749 0.2516 0.0150  -0.0628 -0.0150 111 LYS A CD   
889  C  CE   . LYS A 111 ? 0.3098 0.3177 0.2467 0.0309  -0.0474 -0.0316 111 LYS A CE   
890  N  NZ   . LYS A 111 ? 0.3937 0.4799 0.4463 0.0274  -0.0635 0.0048  111 LYS A NZ   
891  N  N    . LYS A 112 ? 0.1529 0.0943 0.1156 -0.0063 -0.0195 0.0062  112 LYS A N    
892  C  CA   . LYS A 112 ? 0.1543 0.1273 0.1076 -0.0019 -0.0229 0.0325  112 LYS A CA   
893  C  C    . LYS A 112 ? 0.1384 0.1232 0.1177 -0.0012 -0.0122 0.0226  112 LYS A C    
894  O  O    . LYS A 112 ? 0.1541 0.1016 0.1063 0.0037  0.0018  -0.0108 112 LYS A O    
895  C  CB   . LYS A 112 ? 0.1860 0.1654 0.1571 -0.0540 -0.0252 0.0189  112 LYS A CB   
896  C  CG   . LYS A 112 ? 0.1573 0.2090 0.1741 -0.0307 0.0038  -0.0288 112 LYS A CG   
897  C  CD   . LYS A 112 ? 0.1989 0.2246 0.2375 -0.0143 -0.0477 0.0205  112 LYS A CD   
898  C  CE   . LYS A 112 ? 0.3296 0.2307 0.2336 -0.0021 -0.0257 -0.0154 112 LYS A CE   
899  N  NZ   . LYS A 112 ? 0.3817 0.2231 0.2110 -0.0057 -0.0569 0.0067  112 LYS A NZ   
900  N  N    . LYS A 113 ? 0.1484 0.1285 0.1321 -0.0009 -0.0060 0.0112  113 LYS A N    
901  C  CA   . LYS A 113 ? 0.1330 0.1046 0.1250 0.0063  -0.0026 0.0017  113 LYS A CA   
902  C  C    . LYS A 113 ? 0.1254 0.1098 0.1231 0.0260  -0.0093 0.0036  113 LYS A C    
903  O  O    . LYS A 113 ? 0.1737 0.0890 0.1740 0.0112  -0.0440 -0.0054 113 LYS A O    
904  C  CB   . LYS A 113 ? 0.1064 0.1141 0.1285 0.0207  -0.0157 -0.0154 113 LYS A CB   
905  C  CG   . LYS A 113 ? 0.0949 0.1474 0.1294 -0.0040 -0.0329 -0.0009 113 LYS A CG   
906  C  CD   . LYS A 113 ? 0.1046 0.1243 0.2115 0.0362  0.0011  0.0124  113 LYS A CD   
907  C  CE   . LYS A 113 ? 0.2190 0.2527 0.1923 -0.0199 -0.0587 0.0027  113 LYS A CE   
908  N  NZ   . LYS A 113 ? 0.2892 0.2477 0.2930 0.0195  -0.0955 -0.0106 113 LYS A NZ   
909  N  N    . TYR A 114 ? 0.1229 0.0973 0.1234 0.0113  -0.0074 0.0136  114 TYR A N    
910  C  CA   . TYR A 114 ? 0.0981 0.0803 0.1176 0.0207  0.0008  0.0219  114 TYR A CA   
911  C  C    . TYR A 114 ? 0.1071 0.0909 0.1331 0.0153  0.0002  -0.0106 114 TYR A C    
912  O  O    . TYR A 114 ? 0.1162 0.0851 0.1333 -0.0094 -0.0015 -0.0071 114 TYR A O    
913  C  CB   . TYR A 114 ? 0.0894 0.1081 0.1512 0.0239  0.0213  -0.0073 114 TYR A CB   
914  C  CG   . TYR A 114 ? 0.1517 0.0718 0.1312 0.0070  -0.0006 -0.0019 114 TYR A CG   
915  C  CD1  . TYR A 114 ? 0.1666 0.0996 0.1432 -0.0049 0.0248  0.0102  114 TYR A CD1  
916  C  CD2  . TYR A 114 ? 0.1223 0.1064 0.1562 -0.0288 0.0187  0.0059  114 TYR A CD2  
917  C  CE1  . TYR A 114 ? 0.1929 0.1476 0.1605 0.0044  0.0159  -0.0069 114 TYR A CE1  
918  C  CE2  . TYR A 114 ? 0.1490 0.1298 0.1262 -0.0374 -0.0071 0.0060  114 TYR A CE2  
919  C  CZ   . TYR A 114 ? 0.1950 0.1346 0.1080 0.0151  0.0363  0.0259  114 TYR A CZ   
920  O  OH   . TYR A 114 ? 0.2352 0.2241 0.2169 -0.0048 0.0827  0.0073  114 TYR A OH   
921  N  N    . ALA A 115 ? 0.1642 0.0704 0.1131 -0.0032 -0.0220 0.0008  115 ALA A N    
922  C  CA   . ALA A 115 ? 0.1549 0.0684 0.1124 -0.0120 -0.0249 -0.0149 115 ALA A CA   
923  C  C    . ALA A 115 ? 0.1511 0.0739 0.1124 -0.0081 -0.0121 -0.0154 115 ALA A C    
924  O  O    . ALA A 115 ? 0.1536 0.0862 0.1045 -0.0202 -0.0005 -0.0062 115 ALA A O    
925  C  CB   . ALA A 115 ? 0.1503 0.0731 0.1592 -0.0119 -0.0421 -0.0224 115 ALA A CB   
926  N  N    . ALA A 116 ? 0.1353 0.0541 0.1083 0.0040  -0.0109 -0.0169 116 ALA A N    
927  C  CA   . ALA A 116 ? 0.1524 0.0451 0.0908 0.0180  -0.0059 -0.0201 116 ALA A CA   
928  C  C    . ALA A 116 ? 0.1130 0.0677 0.1050 0.0194  -0.0169 -0.0135 116 ALA A C    
929  O  O    . ALA A 116 ? 0.1409 0.0490 0.1162 0.0090  -0.0004 0.0001  116 ALA A O    
930  C  CB   . ALA A 116 ? 0.1807 0.1180 0.0535 0.0102  -0.0261 -0.0098 116 ALA A CB   
931  N  N    . GLU A 117 ? 0.1192 0.0462 0.1237 0.0039  -0.0133 -0.0025 117 GLU A N    
932  C  CA   . GLU A 117 ? 0.1216 0.0319 0.1144 0.0150  -0.0234 -0.0002 117 GLU A CA   
933  C  C    . GLU A 117 ? 0.1038 0.0507 0.1179 -0.0064 -0.0097 0.0096  117 GLU A C    
934  O  O    . GLU A 117 ? 0.1057 0.0749 0.1294 0.0025  -0.0090 0.0279  117 GLU A O    
935  C  CB   . GLU A 117 ? 0.1110 0.0776 0.1083 0.0054  -0.0092 -0.0059 117 GLU A CB   
936  C  CG   . GLU A 117 ? 0.1003 0.0949 0.0886 -0.0014 -0.0291 -0.0360 117 GLU A CG   
937  C  CD   . GLU A 117 ? 0.1130 0.0791 0.1078 -0.0294 0.0122  0.0018  117 GLU A CD   
938  O  OE1  . GLU A 117 ? 0.1308 0.0806 0.1197 0.0008  -0.0115 -0.0024 117 GLU A OE1  
939  O  OE2  . GLU A 117 ? 0.1316 0.0732 0.1108 -0.0039 -0.0418 -0.0199 117 GLU A OE2  
940  N  N    . LEU A 118 ? 0.0996 0.0581 0.1002 0.0300  -0.0229 0.0059  118 LEU A N    
941  C  CA   . LEU A 118 ? 0.0813 0.0471 0.1005 0.0202  -0.0297 -0.0141 118 LEU A CA   
942  C  C    . LEU A 118 ? 0.0967 0.0584 0.0805 0.0276  -0.0048 -0.0140 118 LEU A C    
943  O  O    . LEU A 118 ? 0.1207 0.0623 0.0905 -0.0162 0.0114  0.0017  118 LEU A O    
944  C  CB   . LEU A 118 ? 0.0739 0.0982 0.1221 0.0340  -0.0453 -0.0047 118 LEU A CB   
945  C  CG   . LEU A 118 ? 0.0746 0.0886 0.1258 0.0166  -0.0257 0.0252  118 LEU A CG   
946  C  CD1  . LEU A 118 ? 0.1401 0.1060 0.1031 -0.0121 -0.0061 0.0514  118 LEU A CD1  
947  C  CD2  . LEU A 118 ? 0.0783 0.1321 0.1037 -0.0149 -0.0177 0.0329  118 LEU A CD2  
948  N  N    . HIS A 119 ? 0.1299 0.0295 0.0932 0.0200  -0.0242 0.0000  119 HIS A N    
949  C  CA   . HIS A 119 ? 0.1107 0.0670 0.0692 -0.0043 -0.0280 0.0125  119 HIS A CA   
950  C  C    . HIS A 119 ? 0.1098 0.0673 0.0635 -0.0082 -0.0194 0.0049  119 HIS A C    
951  O  O    . HIS A 119 ? 0.1176 0.0924 0.0838 0.0097  -0.0093 0.0167  119 HIS A O    
952  C  CB   . HIS A 119 ? 0.1008 0.0924 0.0578 0.0300  -0.0258 0.0258  119 HIS A CB   
953  C  CG   . HIS A 119 ? 0.0972 0.0856 0.0608 0.0243  -0.0318 -0.0038 119 HIS A CG   
954  N  ND1  . HIS A 119 ? 0.0932 0.0913 0.1198 -0.0242 -0.0075 -0.0064 119 HIS A ND1  
955  C  CD2  . HIS A 119 ? 0.1391 0.0812 0.0706 0.0079  -0.0124 0.0190  119 HIS A CD2  
956  C  CE1  . HIS A 119 ? 0.1180 0.0559 0.1164 -0.0226 -0.0266 -0.0074 119 HIS A CE1  
957  N  NE2  . HIS A 119 ? 0.0791 0.1008 0.1086 -0.0096 -0.0001 0.0080  119 HIS A NE2  
958  N  N    . LEU A 120 ? 0.1057 0.0386 0.1133 0.0111  -0.0311 -0.0077 120 LEU A N    
959  C  CA   . LEU A 120 ? 0.1130 0.0548 0.1149 -0.0066 -0.0299 -0.0220 120 LEU A CA   
960  C  C    . LEU A 120 ? 0.1062 0.0494 0.0931 -0.0032 -0.0393 0.0036  120 LEU A C    
961  O  O    . LEU A 120 ? 0.0995 0.0560 0.0774 -0.0073 -0.0299 0.0018  120 LEU A O    
962  C  CB   . LEU A 120 ? 0.0913 0.0554 0.1235 -0.0188 -0.0517 -0.0093 120 LEU A CB   
963  C  CG   . LEU A 120 ? 0.1288 0.0826 0.1054 -0.0264 -0.0592 0.0095  120 LEU A CG   
964  C  CD1  . LEU A 120 ? 0.2538 0.0781 0.1448 -0.0377 0.0013  0.0124  120 LEU A CD1  
965  C  CD2  . LEU A 120 ? 0.1524 0.1669 0.1452 -0.0039 -0.0688 0.0251  120 LEU A CD2  
966  N  N    . VAL A 121 ? 0.1018 0.0737 0.1085 -0.0156 -0.0375 -0.0103 121 VAL A N    
967  C  CA   . VAL A 121 ? 0.1141 0.0549 0.1212 -0.0066 -0.0203 0.0115  121 VAL A CA   
968  C  C    . VAL A 121 ? 0.0820 0.0860 0.1214 -0.0072 -0.0293 -0.0195 121 VAL A C    
969  O  O    . VAL A 121 ? 0.1539 0.1004 0.1108 0.0028  -0.0604 -0.0081 121 VAL A O    
970  C  CB   . VAL A 121 ? 0.0882 0.0818 0.1213 0.0004  -0.0115 0.0206  121 VAL A CB   
971  C  CG1  . VAL A 121 ? 0.1171 0.1030 0.1293 -0.0608 0.0047  -0.0035 121 VAL A CG1  
972  C  CG2  . VAL A 121 ? 0.1234 0.0737 0.1372 0.0188  -0.0015 0.0185  121 VAL A CG2  
973  N  N    . HIS A 122 ? 0.0875 0.0746 0.0980 -0.0146 -0.0112 -0.0135 122 HIS A N    
974  C  CA   . HIS A 122 ? 0.0826 0.0793 0.1269 -0.0081 -0.0226 -0.0153 122 HIS A CA   
975  C  C    . HIS A 122 ? 0.1367 0.0589 0.1126 -0.0115 -0.0131 -0.0076 122 HIS A C    
976  O  O    . HIS A 122 ? 0.1613 0.0527 0.1225 -0.0145 -0.0323 -0.0206 122 HIS A O    
977  C  CB   . HIS A 122 ? 0.0983 0.0804 0.1313 -0.0062 -0.0024 -0.0087 122 HIS A CB   
978  C  CG   . HIS A 122 ? 0.0850 0.0575 0.1612 -0.0222 -0.0044 0.0022  122 HIS A CG   
979  N  ND1  . HIS A 122 ? 0.0964 0.0469 0.1883 0.0146  0.0031  0.0136  122 HIS A ND1  
980  C  CD2  . HIS A 122 ? 0.1128 0.1198 0.1424 0.0016  0.0096  0.0242  122 HIS A CD2  
981  C  CE1  . HIS A 122 ? 0.0834 0.1408 0.1602 -0.0083 0.0035  -0.0038 122 HIS A CE1  
982  N  NE2  . HIS A 122 ? 0.1370 0.1039 0.1407 -0.0068 -0.0157 -0.0035 122 HIS A NE2  
983  N  N    . TRP A 123 ? 0.1359 0.0317 0.1262 -0.0053 -0.0235 -0.0230 123 TRP A N    
984  C  CA   . TRP A 123 ? 0.1344 0.0352 0.1312 -0.0191 -0.0149 -0.0195 123 TRP A CA   
985  C  C    . TRP A 123 ? 0.1493 0.0977 0.1330 0.0076  -0.0235 -0.0275 123 TRP A C    
986  O  O    . TRP A 123 ? 0.1173 0.0782 0.1663 0.0018  -0.0568 -0.0113 123 TRP A O    
987  C  CB   . TRP A 123 ? 0.1335 0.0931 0.1342 -0.0117 -0.0277 0.0140  123 TRP A CB   
988  C  CG   . TRP A 123 ? 0.1856 0.0589 0.1361 0.0041  -0.0402 0.0186  123 TRP A CG   
989  C  CD1  . TRP A 123 ? 0.1716 0.0959 0.1491 -0.0089 -0.0631 -0.0104 123 TRP A CD1  
990  C  CD2  . TRP A 123 ? 0.2051 0.0499 0.1252 -0.0109 -0.0553 -0.0118 123 TRP A CD2  
991  N  NE1  . TRP A 123 ? 0.2191 0.0796 0.1553 0.0094  -0.0411 0.0014  123 TRP A NE1  
992  C  CE2  . TRP A 123 ? 0.2009 0.0781 0.1425 0.0250  -0.0556 -0.0214 123 TRP A CE2  
993  C  CE3  . TRP A 123 ? 0.2057 0.0320 0.2068 -0.0326 -0.0130 -0.0100 123 TRP A CE3  
994  C  CZ2  . TRP A 123 ? 0.2299 0.0675 0.1512 0.0072  -0.0212 -0.0008 123 TRP A CZ2  
995  C  CZ3  . TRP A 123 ? 0.2314 0.0848 0.1558 -0.0115 -0.0356 -0.0085 123 TRP A CZ3  
996  C  CH2  . TRP A 123 ? 0.2091 0.0949 0.1782 -0.0077 -0.0388 0.0074  123 TRP A CH2  
997  N  N    . ASN A 124 ? 0.1495 0.0885 0.1157 0.0017  -0.0164 -0.0367 124 ASN A N    
998  C  CA   . ASN A 124 ? 0.1595 0.0786 0.1412 0.0092  -0.0167 -0.0379 124 ASN A CA   
999  C  C    . ASN A 124 ? 0.1425 0.0848 0.1535 0.0237  -0.0130 -0.0311 124 ASN A C    
1000 O  O    . ASN A 124 ? 0.1413 0.0722 0.1893 0.0086  -0.0176 -0.0276 124 ASN A O    
1001 C  CB   . ASN A 124 ? 0.1676 0.1025 0.0966 0.0255  -0.0039 -0.0234 124 ASN A CB   
1002 C  CG   . ASN A 124 ? 0.1618 0.0934 0.1505 -0.0271 -0.0254 -0.0454 124 ASN A CG   
1003 O  OD1  . ASN A 124 ? 0.1737 0.1300 0.2024 0.0238  0.0174  -0.0548 124 ASN A OD1  
1004 N  ND2  . ASN A 124 ? 0.2667 0.1245 0.1268 -0.0120 -0.0118 -0.0204 124 ASN A ND2  
1005 N  N    . THR A 125 ? 0.1549 0.0662 0.1825 0.0160  -0.0306 -0.0288 125 THR A N    
1006 C  CA   . THR A 125 ? 0.1422 0.0624 0.2050 0.0230  -0.0539 -0.0090 125 THR A CA   
1007 C  C    . THR A 125 ? 0.1546 0.0673 0.2335 0.0736  -0.0318 -0.0192 125 THR A C    
1008 O  O    . THR A 125 ? 0.2281 0.0954 0.2754 0.0211  -0.0315 0.0176  125 THR A O    
1009 C  CB   . THR A 125 ? 0.1796 0.1185 0.2419 0.0279  -0.0300 -0.0185 125 THR A CB   
1010 O  OG1  . THR A 125 ? 0.2320 0.1650 0.2540 0.0535  -0.0052 -0.0206 125 THR A OG1  
1011 C  CG2  . THR A 125 ? 0.2102 0.1175 0.2508 0.0223  -0.0584 0.0058  125 THR A CG2  
1012 N  N    . LYS A 126 ? 0.1846 0.0946 0.1913 0.0146  0.0154  -0.0546 127 LYS A N    
1013 C  CA   . LYS A 126 ? 0.2245 0.1320 0.2011 -0.0257 0.0022  -0.0615 127 LYS A CA   
1014 C  C    . LYS A 126 ? 0.2091 0.1320 0.2099 -0.0248 -0.0051 -0.0453 127 LYS A C    
1015 O  O    . LYS A 126 ? 0.2652 0.1428 0.2619 -0.0378 0.0109  -0.0741 127 LYS A O    
1016 C  CB   . LYS A 126 ? 0.2840 0.1758 0.2493 -0.0192 -0.0094 -0.0452 127 LYS A CB   
1017 C  CG   . LYS A 126 ? 0.2668 0.2470 0.2431 -0.0192 -0.0329 -0.0512 127 LYS A CG   
1018 C  CD   . LYS A 126 ? 0.4034 0.3164 0.2991 -0.0378 0.0118  -0.0308 127 LYS A CD   
1019 C  CE   . LYS A 126 ? 0.4100 0.4175 0.3475 -0.0014 0.0016  -0.0346 127 LYS A CE   
1020 N  NZ   . LYS A 126 ? 0.5621 0.4767 0.4085 -0.0009 0.0129  -0.0695 127 LYS A NZ   
1021 N  N    . TYR A 127 ? 0.2022 0.1061 0.1575 -0.0098 -0.0120 -0.0189 128 TYR A N    
1022 C  CA   . TYR A 127 ? 0.1767 0.1161 0.1450 -0.0086 -0.0238 0.0035  128 TYR A CA   
1023 C  C    . TYR A 127 ? 0.1901 0.0987 0.1608 0.0013  -0.0114 -0.0071 128 TYR A C    
1024 O  O    . TYR A 127 ? 0.1789 0.1264 0.1969 -0.0035 0.0045  0.0156  128 TYR A O    
1025 C  CB   . TYR A 127 ? 0.2102 0.1104 0.1451 -0.0036 -0.0132 -0.0104 128 TYR A CB   
1026 C  CG   . TYR A 127 ? 0.1639 0.0909 0.1182 -0.0081 -0.0183 -0.0118 128 TYR A CG   
1027 C  CD1  . TYR A 127 ? 0.2353 0.1352 0.1655 -0.0269 -0.0488 -0.0531 128 TYR A CD1  
1028 C  CD2  . TYR A 127 ? 0.1426 0.0963 0.1555 0.0045  -0.0151 0.0151  128 TYR A CD2  
1029 C  CE1  . TYR A 127 ? 0.2186 0.1064 0.1512 0.0131  -0.0508 -0.0215 128 TYR A CE1  
1030 C  CE2  . TYR A 127 ? 0.1636 0.1299 0.1355 0.0036  -0.0172 -0.0297 128 TYR A CE2  
1031 C  CZ   . TYR A 127 ? 0.2200 0.1339 0.1023 0.0139  -0.0144 -0.0177 128 TYR A CZ   
1032 O  OH   . TYR A 127 ? 0.3016 0.1243 0.1310 0.0304  0.0036  -0.0332 128 TYR A OH   
1033 N  N    . GLY A 128 ? 0.2090 0.1044 0.1986 0.0005  -0.0309 0.0112  129 GLY A N    
1034 C  CA   . GLY A 128 ? 0.2082 0.1265 0.1530 -0.0141 -0.0028 0.0044  129 GLY A CA   
1035 C  C    . GLY A 128 ? 0.2097 0.1060 0.1871 -0.0206 -0.0157 -0.0014 129 GLY A C    
1036 O  O    . GLY A 128 ? 0.2446 0.1475 0.2245 -0.0232 -0.0304 0.0323  129 GLY A O    
1037 N  N    . ASP A 129 ? 0.2151 0.1170 0.1698 0.0013  -0.0180 0.0155  130 ASP A N    
1038 C  CA   . ASP A 129 ? 0.2396 0.0996 0.1886 0.0140  -0.0053 0.0195  130 ASP A CA   
1039 C  C    . ASP A 129 ? 0.2226 0.1019 0.1695 0.0131  -0.0228 0.0006  130 ASP A C    
1040 O  O    . ASP A 129 ? 0.2500 0.1204 0.1464 0.0086  -0.0280 -0.0113 130 ASP A O    
1041 C  CB   . ASP A 129 ? 0.2598 0.1311 0.2123 0.0367  0.0054  0.0090  130 ASP A CB   
1042 C  CG   . ASP A 129 ? 0.2824 0.0954 0.2558 0.0250  0.0013  0.0405  130 ASP A CG   
1043 O  OD1  . ASP A 129 ? 0.3850 0.2069 0.3204 -0.0300 -0.0535 0.0650  130 ASP A OD1  
1044 O  OD2  . ASP A 129 ? 0.3216 0.1873 0.3605 0.0221  0.0961  0.0571  130 ASP A OD2  
1045 N  N    . PHE A 130 ? 0.2446 0.0825 0.1858 0.0147  -0.0254 0.0055  131 PHE A N    
1046 C  CA   . PHE A 130 ? 0.2077 0.1112 0.1807 -0.0061 -0.0196 -0.0039 131 PHE A CA   
1047 C  C    . PHE A 130 ? 0.2117 0.1021 0.1649 -0.0221 -0.0056 -0.0009 131 PHE A C    
1048 O  O    . PHE A 130 ? 0.2261 0.1279 0.1171 -0.0434 0.0010  0.0133  131 PHE A O    
1049 C  CB   . PHE A 130 ? 0.2229 0.0788 0.1403 -0.0225 -0.0153 -0.0065 131 PHE A CB   
1050 C  CG   . PHE A 130 ? 0.1700 0.1485 0.1851 -0.0187 -0.0158 -0.0002 131 PHE A CG   
1051 C  CD1  . PHE A 130 ? 0.1553 0.0862 0.1588 0.0008  -0.0155 -0.0197 131 PHE A CD1  
1052 C  CD2  . PHE A 130 ? 0.1982 0.1460 0.2197 -0.0115 0.0004  0.0100  131 PHE A CD2  
1053 C  CE1  . PHE A 130 ? 0.1779 0.1326 0.1603 -0.0203 -0.0345 -0.0006 131 PHE A CE1  
1054 C  CE2  . PHE A 130 ? 0.2177 0.1816 0.2130 -0.0222 -0.0067 0.0092  131 PHE A CE2  
1055 C  CZ   . PHE A 130 ? 0.2196 0.1215 0.2192 -0.0332 -0.0207 0.0033  131 PHE A CZ   
1056 N  N    . GLY A 131 ? 0.1971 0.1158 0.1735 -0.0324 0.0123  -0.0150 132 GLY A N    
1057 C  CA   . GLY A 131 ? 0.2159 0.1527 0.1741 -0.0548 0.0117  0.0134  132 GLY A CA   
1058 C  C    . GLY A 131 ? 0.2000 0.1365 0.1918 -0.0434 0.0151  0.0069  132 GLY A C    
1059 O  O    . GLY A 131 ? 0.2281 0.1348 0.2070 -0.0218 0.0068  0.0056  132 GLY A O    
1060 N  N    . LYS A 132 ? 0.2177 0.1192 0.1877 -0.0533 0.0183  0.0071  133 LYS A N    
1061 C  CA   . LYS A 132 ? 0.2159 0.1093 0.1852 -0.0452 -0.0120 0.0070  133 LYS A CA   
1062 C  C    . LYS A 132 ? 0.1863 0.0941 0.1701 -0.0315 -0.0118 0.0020  133 LYS A C    
1063 O  O    . LYS A 132 ? 0.1955 0.1089 0.1661 -0.0442 -0.0291 -0.0049 133 LYS A O    
1064 C  CB   . LYS A 132 ? 0.2089 0.1390 0.2078 -0.0289 -0.0067 0.0077  133 LYS A CB   
1065 C  CG   . LYS A 132 ? 0.2859 0.1622 0.2737 -0.0499 -0.0430 0.0313  133 LYS A CG   
1066 C  CD   . LYS A 132 ? 0.3261 0.1999 0.4422 -0.0392 -0.0305 0.0326  133 LYS A CD   
1067 C  CE   . LYS A 132 ? 0.4488 0.3429 0.4865 0.0054  -0.0282 -0.0317 133 LYS A CE   
1068 N  NZ   . LYS A 132 ? 0.4628 0.4416 0.5533 0.0065  -0.0187 0.0031  133 LYS A NZ   
1069 N  N    . ALA A 133 ? 0.1420 0.0924 0.1580 -0.0333 -0.0036 0.0099  134 ALA A N    
1070 C  CA   . ALA A 133 ? 0.1600 0.1191 0.1412 -0.0176 -0.0050 0.0106  134 ALA A CA   
1071 C  C    . ALA A 133 ? 0.1227 0.1175 0.1379 -0.0104 -0.0049 0.0028  134 ALA A C    
1072 O  O    . ALA A 133 ? 0.1244 0.1597 0.1323 0.0052  0.0008  -0.0234 134 ALA A O    
1073 C  CB   . ALA A 133 ? 0.1608 0.0837 0.1443 -0.0465 -0.0227 0.0004  134 ALA A CB   
1074 N  N    . VAL A 134 ? 0.1379 0.1146 0.1399 0.0002  -0.0044 -0.0150 135 VAL A N    
1075 C  CA   . VAL A 134 ? 0.1433 0.1221 0.1295 -0.0181 0.0005  -0.0032 135 VAL A CA   
1076 C  C    . VAL A 134 ? 0.1247 0.1170 0.1463 -0.0196 0.0123  -0.0036 135 VAL A C    
1077 O  O    . VAL A 134 ? 0.1201 0.1197 0.1893 -0.0026 0.0041  -0.0123 135 VAL A O    
1078 C  CB   . VAL A 134 ? 0.1814 0.1583 0.1408 -0.0260 0.0136  -0.0234 135 VAL A CB   
1079 C  CG1  . VAL A 134 ? 0.1905 0.1556 0.1229 -0.0467 -0.0309 -0.0115 135 VAL A CG1  
1080 C  CG2  . VAL A 134 ? 0.1517 0.1538 0.1679 -0.0419 0.0366  -0.0145 135 VAL A CG2  
1081 N  N    . GLN A 135 ? 0.1467 0.1150 0.1623 -0.0252 -0.0032 -0.0106 136 GLN A N    
1082 C  CA   . GLN A 135 ? 0.1578 0.1307 0.1945 -0.0454 0.0009  -0.0259 136 GLN A CA   
1083 C  C    . GLN A 135 ? 0.1409 0.1453 0.1964 -0.0309 -0.0309 -0.0110 136 GLN A C    
1084 O  O    . GLN A 135 ? 0.1889 0.1935 0.2017 -0.0345 -0.0412 -0.0444 136 GLN A O    
1085 C  CB   . GLN A 135 ? 0.1896 0.1596 0.1996 -0.0526 -0.0031 -0.0025 136 GLN A CB   
1086 C  CG   . GLN A 135 ? 0.2419 0.2178 0.2341 -0.0519 0.0136  0.0335  136 GLN A CG   
1087 C  CD   . GLN A 135 ? 0.3737 0.4079 0.3861 0.0013  0.0107  0.0000  136 GLN A CD   
1088 O  OE1  . GLN A 135 ? 0.3898 0.5139 0.4334 -0.0182 0.0027  0.0167  136 GLN A OE1  
1089 N  NE2  . GLN A 135 ? 0.4309 0.3735 0.4221 -0.0330 0.0205  -0.0343 136 GLN A NE2  
1090 N  N    . GLN A 136 ? 0.1143 0.1202 0.1671 -0.0164 -0.0005 -0.0159 137 GLN A N    
1091 C  CA   . GLN A 136 ? 0.1442 0.1540 0.1431 0.0092  -0.0167 -0.0006 137 GLN A CA   
1092 C  C    . GLN A 136 ? 0.1340 0.1621 0.1353 0.0099  -0.0150 -0.0078 137 GLN A C    
1093 O  O    . GLN A 136 ? 0.1625 0.1111 0.1082 0.0047  -0.0265 -0.0122 137 GLN A O    
1094 C  CB   . GLN A 136 ? 0.1478 0.1332 0.1612 0.0086  -0.0315 -0.0172 137 GLN A CB   
1095 C  CG   . GLN A 136 ? 0.2306 0.2021 0.1876 0.0281  -0.0054 -0.0003 137 GLN A CG   
1096 C  CD   . GLN A 136 ? 0.2743 0.2138 0.2712 -0.0159 -0.0196 0.0417  137 GLN A CD   
1097 O  OE1  . GLN A 136 ? 0.3494 0.1718 0.2922 -0.0268 -0.0374 -0.0597 137 GLN A OE1  
1098 N  NE2  . GLN A 136 ? 0.3621 0.2800 0.4267 -0.0249 -0.0204 0.0520  137 GLN A NE2  
1099 N  N    . PRO A 137 ? 0.1561 0.1810 0.1141 -0.0167 -0.0134 -0.0301 138 PRO A N    
1100 C  CA   . PRO A 137 ? 0.1791 0.1793 0.0959 -0.0111 -0.0201 -0.0077 138 PRO A CA   
1101 C  C    . PRO A 137 ? 0.1713 0.1734 0.1301 -0.0104 -0.0086 -0.0146 138 PRO A C    
1102 O  O    . PRO A 137 ? 0.1891 0.1822 0.1789 0.0000  -0.0262 0.0186  138 PRO A O    
1103 C  CB   . PRO A 137 ? 0.2412 0.1947 0.0924 -0.0007 -0.0236 -0.0196 138 PRO A CB   
1104 C  CG   . PRO A 137 ? 0.2949 0.1949 0.1328 -0.0449 -0.0274 -0.0352 138 PRO A CG   
1105 C  CD   . PRO A 137 ? 0.1794 0.1697 0.1016 -0.0384 -0.0078 -0.0467 138 PRO A CD   
1106 N  N    . ASP A 138 ? 0.1510 0.1267 0.0908 -0.0024 -0.0138 -0.0118 139 ASP A N    
1107 C  CA   . ASP A 138 ? 0.1582 0.1597 0.1190 -0.0032 0.0093  -0.0186 139 ASP A CA   
1108 C  C    . ASP A 138 ? 0.1354 0.1093 0.1368 -0.0400 -0.0116 -0.0136 139 ASP A C    
1109 O  O    . ASP A 138 ? 0.1385 0.1529 0.1496 -0.0045 -0.0118 -0.0153 139 ASP A O    
1110 C  CB   . ASP A 138 ? 0.1774 0.1615 0.1284 0.0020  0.0210  -0.0066 139 ASP A CB   
1111 C  CG   . ASP A 138 ? 0.1541 0.1937 0.1621 -0.0043 0.0186  -0.0597 139 ASP A CG   
1112 O  OD1  . ASP A 138 ? 0.2291 0.1327 0.2226 0.0297  -0.0017 -0.0478 139 ASP A OD1  
1113 O  OD2  . ASP A 138 ? 0.2490 0.2464 0.2230 0.0320  0.0635  -0.0966 139 ASP A OD2  
1114 N  N    . GLY A 139 ? 0.1223 0.1087 0.1179 -0.0294 -0.0167 -0.0290 140 GLY A N    
1115 C  CA   . GLY A 139 ? 0.1194 0.0974 0.0945 -0.0139 -0.0162 -0.0314 140 GLY A CA   
1116 C  C    . GLY A 139 ? 0.0986 0.0811 0.1297 -0.0189 -0.0112 -0.0114 140 GLY A C    
1117 O  O    . GLY A 139 ? 0.1385 0.0598 0.1372 0.0068  -0.0297 -0.0180 140 GLY A O    
1118 N  N    . LEU A 140 ? 0.0971 0.0492 0.1268 -0.0195 -0.0006 -0.0188 141 LEU A N    
1119 C  CA   . LEU A 140 ? 0.1151 0.0644 0.0877 -0.0232 0.0073  -0.0270 141 LEU A CA   
1120 C  C    . LEU A 140 ? 0.1195 0.0709 0.1033 -0.0226 -0.0073 -0.0197 141 LEU A C    
1121 O  O    . LEU A 140 ? 0.1477 0.0608 0.0900 -0.0363 -0.0250 0.0028  141 LEU A O    
1122 C  CB   . LEU A 140 ? 0.1189 0.0779 0.1251 0.0033  0.0219  -0.0024 141 LEU A CB   
1123 C  CG   . LEU A 140 ? 0.0851 0.1085 0.1555 -0.0026 0.0218  0.0039  141 LEU A CG   
1124 C  CD1  . LEU A 140 ? 0.1231 0.0728 0.1498 0.0463  0.0261  -0.0117 141 LEU A CD1  
1125 C  CD2  . LEU A 140 ? 0.2015 0.0949 0.1408 0.0198  0.0166  0.0507  141 LEU A CD2  
1126 N  N    . ALA A 141 ? 0.0913 0.0522 0.1183 -0.0353 -0.0043 -0.0249 142 ALA A N    
1127 C  CA   . ALA A 141 ? 0.1076 0.0361 0.1131 -0.0209 -0.0090 -0.0194 142 ALA A CA   
1128 C  C    . ALA A 141 ? 0.1099 0.0503 0.0927 -0.0149 -0.0266 -0.0088 142 ALA A C    
1129 O  O    . ALA A 141 ? 0.1744 0.0684 0.0989 -0.0123 -0.0451 -0.0035 142 ALA A O    
1130 C  CB   . ALA A 141 ? 0.0836 0.0929 0.1546 0.0040  0.0120  -0.0330 142 ALA A CB   
1131 N  N    . VAL A 142 ? 0.1173 0.0455 0.1159 -0.0165 -0.0094 -0.0133 143 VAL A N    
1132 C  CA   . VAL A 142 ? 0.1047 0.0498 0.1011 -0.0042 -0.0102 -0.0094 143 VAL A CA   
1133 C  C    . VAL A 142 ? 0.1263 0.0631 0.1050 -0.0088 -0.0171 -0.0126 143 VAL A C    
1134 O  O    . VAL A 142 ? 0.1231 0.0828 0.1063 -0.0024 -0.0180 0.0147  143 VAL A O    
1135 C  CB   . VAL A 142 ? 0.0937 0.1063 0.1274 0.0147  -0.0063 -0.0305 143 VAL A CB   
1136 C  CG1  . VAL A 142 ? 0.1376 0.0993 0.1184 0.0055  -0.0134 -0.0389 143 VAL A CG1  
1137 C  CG2  . VAL A 142 ? 0.0703 0.1541 0.1066 -0.0310 -0.0253 0.0091  143 VAL A CG2  
1138 N  N    . LEU A 143 ? 0.0753 0.0590 0.1134 -0.0170 -0.0217 -0.0050 144 LEU A N    
1139 C  CA   . LEU A 143 ? 0.0936 0.0974 0.1371 -0.0146 -0.0354 -0.0263 144 LEU A CA   
1140 C  C    . LEU A 143 ? 0.0944 0.0824 0.1222 -0.0088 -0.0132 0.0054  144 LEU A C    
1141 O  O    . LEU A 143 ? 0.1500 0.0605 0.1236 -0.0283 -0.0174 0.0048  144 LEU A O    
1142 C  CB   . LEU A 143 ? 0.0717 0.1182 0.1508 -0.0187 -0.0316 0.0096  144 LEU A CB   
1143 C  CG   . LEU A 143 ? 0.0911 0.0938 0.1309 -0.0144 -0.0164 -0.0142 144 LEU A CG   
1144 C  CD1  . LEU A 143 ? 0.1488 0.1600 0.1368 -0.0449 0.0052  0.0213  144 LEU A CD1  
1145 C  CD2  . LEU A 143 ? 0.1113 0.1893 0.1427 0.0003  -0.0527 -0.0215 144 LEU A CD2  
1146 N  N    . GLY A 144 ? 0.0963 0.0572 0.1206 -0.0041 -0.0278 -0.0075 145 GLY A N    
1147 C  CA   . GLY A 144 ? 0.0971 0.0348 0.1418 -0.0257 -0.0301 0.0054  145 GLY A CA   
1148 C  C    . GLY A 144 ? 0.0972 0.0607 0.1107 0.0032  -0.0032 0.0017  145 GLY A C    
1149 O  O    . GLY A 144 ? 0.1124 0.0768 0.0976 -0.0030 -0.0098 0.0059  145 GLY A O    
1150 N  N    . ILE A 145 ? 0.0898 0.0334 0.1025 -0.0121 -0.0140 -0.0141 146 ILE A N    
1151 C  CA   . ILE A 145 ? 0.0800 0.0575 0.1179 0.0056  -0.0221 -0.0055 146 ILE A CA   
1152 C  C    . ILE A 145 ? 0.1280 0.0884 0.1094 0.0051  -0.0306 0.0003  146 ILE A C    
1153 O  O    . ILE A 145 ? 0.1478 0.0701 0.1135 0.0014  0.0008  -0.0035 146 ILE A O    
1154 C  CB   . ILE A 145 ? 0.1001 0.0685 0.1362 0.0297  -0.0231 0.0065  146 ILE A CB   
1155 C  CG1  . ILE A 145 ? 0.0688 0.0910 0.1635 0.0184  -0.0083 -0.0009 146 ILE A CG1  
1156 C  CG2  . ILE A 145 ? 0.1327 0.0799 0.1659 -0.0074 -0.0407 -0.0144 146 ILE A CG2  
1157 C  CD1  . ILE A 145 ? 0.1134 0.0757 0.1312 0.0400  -0.0209 0.0115  146 ILE A CD1  
1158 N  N    . PHE A 146 ? 0.1152 0.0665 0.0932 -0.0034 -0.0098 -0.0031 147 PHE A N    
1159 C  CA   . PHE A 146 ? 0.1432 0.0516 0.1074 0.0159  -0.0416 0.0094  147 PHE A CA   
1160 C  C    . PHE A 146 ? 0.1263 0.0622 0.1076 -0.0060 -0.0067 0.0011  147 PHE A C    
1161 O  O    . PHE A 146 ? 0.0998 0.0968 0.1150 0.0005  -0.0150 -0.0279 147 PHE A O    
1162 C  CB   . PHE A 146 ? 0.1211 0.0731 0.1110 -0.0022 -0.0397 0.0211  147 PHE A CB   
1163 C  CG   . PHE A 146 ? 0.0947 0.0526 0.1090 0.0141  -0.0203 -0.0145 147 PHE A CG   
1164 C  CD1  . PHE A 146 ? 0.0767 0.0748 0.1081 0.0011  -0.0305 -0.0044 147 PHE A CD1  
1165 C  CD2  . PHE A 146 ? 0.1101 0.0649 0.1216 -0.0175 -0.0120 0.0065  147 PHE A CD2  
1166 C  CE1  . PHE A 146 ? 0.1249 0.0860 0.0666 0.0076  -0.0247 -0.0260 147 PHE A CE1  
1167 C  CE2  . PHE A 146 ? 0.1148 0.0484 0.1332 0.0182  -0.0211 0.0006  147 PHE A CE2  
1168 C  CZ   . PHE A 146 ? 0.0954 0.0947 0.0803 -0.0076 -0.0218 0.0066  147 PHE A CZ   
1169 N  N    . LEU A 147 ? 0.1333 0.0705 0.1009 -0.0005 -0.0084 -0.0298 148 LEU A N    
1170 C  CA   . LEU A 147 ? 0.1397 0.0568 0.0889 -0.0081 -0.0133 -0.0116 148 LEU A CA   
1171 C  C    . LEU A 147 ? 0.1387 0.0686 0.1128 -0.0006 -0.0119 -0.0012 148 LEU A C    
1172 O  O    . LEU A 147 ? 0.1155 0.0739 0.1402 0.0165  -0.0188 -0.0140 148 LEU A O    
1173 C  CB   . LEU A 147 ? 0.1442 0.0640 0.0937 -0.0324 -0.0051 0.0209  148 LEU A CB   
1174 C  CG   . LEU A 147 ? 0.1485 0.0574 0.0994 -0.0084 -0.0241 0.0288  148 LEU A CG   
1175 C  CD1  . LEU A 147 ? 0.2072 0.0572 0.1566 -0.0507 0.0011  -0.0485 148 LEU A CD1  
1176 C  CD2  . LEU A 147 ? 0.1835 0.1273 0.0890 -0.0300 0.0049  -0.0145 148 LEU A CD2  
1177 N  N    . LYS A 148 ? 0.1511 0.0628 0.1200 -0.0291 -0.0225 -0.0309 149 LYS A N    
1178 C  CA   . LYS A 148 ? 0.1633 0.0958 0.1448 -0.0077 -0.0199 0.0056  149 LYS A CA   
1179 C  C    . LYS A 148 ? 0.1549 0.0955 0.1522 0.0009  -0.0346 -0.0138 149 LYS A C    
1180 O  O    . LYS A 148 ? 0.1695 0.1050 0.1632 0.0245  -0.0583 -0.0238 149 LYS A O    
1181 C  CB   . LYS A 148 ? 0.1789 0.1164 0.1462 -0.0230 -0.0319 -0.0113 149 LYS A CB   
1182 C  CG   . LYS A 148 ? 0.2046 0.1533 0.2230 -0.0469 0.0252  -0.0044 149 LYS A CG   
1183 C  CD   . LYS A 148 ? 0.2016 0.2448 0.2398 -0.0243 0.0220  0.0355  149 LYS A CD   
1184 C  CE   . LYS A 148 ? 0.2740 0.3601 0.3093 -0.0198 0.0458  0.0210  149 LYS A CE   
1185 N  NZ   . LYS A 148 ? 0.3771 0.4108 0.3600 -0.0638 0.0552  0.0204  149 LYS A NZ   
1186 N  N    . VAL A 149 ? 0.1824 0.1063 0.1475 -0.0004 -0.0335 -0.0154 150 VAL A N    
1187 C  CA   . VAL A 149 ? 0.1706 0.1133 0.1628 -0.0184 -0.0158 -0.0310 150 VAL A CA   
1188 C  C    . VAL A 149 ? 0.1804 0.1068 0.1788 -0.0181 -0.0323 -0.0187 150 VAL A C    
1189 O  O    . VAL A 149 ? 0.2278 0.1234 0.1792 -0.0227 -0.0561 0.0005  150 VAL A O    
1190 C  CB   . VAL A 149 ? 0.1889 0.1196 0.1576 -0.0001 -0.0023 -0.0028 150 VAL A CB   
1191 C  CG1  . VAL A 149 ? 0.1844 0.1668 0.1591 0.0230  -0.0083 -0.0323 150 VAL A CG1  
1192 C  CG2  . VAL A 149 ? 0.1411 0.1840 0.2252 -0.0140 0.0008  -0.0327 150 VAL A CG2  
1193 N  N    . GLY A 150 ? 0.1558 0.0794 0.1721 -0.0368 -0.0663 -0.0158 151 GLY A N    
1194 C  CA   . GLY A 150 ? 0.1506 0.1373 0.1859 -0.0337 -0.0564 0.0014  151 GLY A CA   
1195 C  C    . GLY A 150 ? 0.1624 0.1297 0.1886 -0.0382 -0.0459 0.0063  151 GLY A C    
1196 O  O    . GLY A 150 ? 0.1826 0.1080 0.2091 -0.0505 -0.0434 -0.0015 151 GLY A O    
1197 N  N    A SER A 151 ? 0.1855 0.1288 0.2055 -0.0302 -0.0496 -0.0007 152 SER A N    
1198 N  N    B SER A 151 ? 0.1807 0.1265 0.2097 -0.0315 -0.0473 -0.0009 152 SER A N    
1199 C  CA   A SER A 151 ? 0.1995 0.1270 0.1979 -0.0153 -0.0467 -0.0009 152 SER A CA   
1200 C  CA   B SER A 151 ? 0.1881 0.1225 0.2111 -0.0166 -0.0355 0.0029  152 SER A CA   
1201 C  C    A SER A 151 ? 0.2095 0.1441 0.1864 -0.0125 -0.0391 -0.0018 152 SER A C    
1202 C  C    B SER A 151 ? 0.2043 0.1399 0.1920 -0.0137 -0.0354 -0.0009 152 SER A C    
1203 O  O    A SER A 151 ? 0.2066 0.1573 0.1718 -0.0086 -0.0517 -0.0266 152 SER A O    
1204 O  O    B SER A 151 ? 0.2030 0.1578 0.1837 -0.0072 -0.0514 -0.0250 152 SER A O    
1205 C  CB   A SER A 151 ? 0.2247 0.1649 0.2219 -0.0165 -0.0269 0.0053  152 SER A CB   
1206 C  CB   B SER A 151 ? 0.2044 0.1578 0.2336 -0.0232 -0.0245 0.0015  152 SER A CB   
1207 O  OG   A SER A 151 ? 0.1862 0.2078 0.1866 -0.0054 -0.0460 -0.0239 152 SER A OG   
1208 O  OG   B SER A 151 ? 0.1702 0.2032 0.2424 -0.0420 0.0203  0.0353  152 SER A OG   
1209 N  N    . ALA A 152 ? 0.2160 0.1233 0.1665 -0.0096 -0.0580 0.0011  153 ALA A N    
1210 C  CA   . ALA A 152 ? 0.1998 0.1027 0.1574 -0.0133 -0.0508 -0.0064 153 ALA A CA   
1211 C  C    . ALA A 152 ? 0.1673 0.1311 0.1538 -0.0110 -0.0555 -0.0110 153 ALA A C    
1212 O  O    . ALA A 152 ? 0.1808 0.1159 0.2672 0.0016  -0.0403 -0.0039 153 ALA A O    
1213 C  CB   . ALA A 152 ? 0.2205 0.1334 0.1736 0.0044  -0.0587 -0.0052 153 ALA A CB   
1214 N  N    . LYS A 153 ? 0.1943 0.0879 0.1877 -0.0255 -0.0536 -0.0055 154 LYS A N    
1215 C  CA   . LYS A 153 ? 0.1970 0.1284 0.1879 0.0037  -0.0516 -0.0144 154 LYS A CA   
1216 C  C    . LYS A 153 ? 0.1827 0.1438 0.2043 -0.0012 -0.0497 -0.0164 154 LYS A C    
1217 O  O    . LYS A 153 ? 0.1846 0.1223 0.1732 0.0082  -0.0721 -0.0008 154 LYS A O    
1218 C  CB   . LYS A 153 ? 0.1869 0.1253 0.1897 -0.0075 -0.0451 -0.0281 154 LYS A CB   
1219 C  CG   . LYS A 153 ? 0.2670 0.1463 0.2156 -0.0101 -0.0528 -0.0330 154 LYS A CG   
1220 C  CD   . LYS A 153 ? 0.2589 0.1475 0.2271 0.0320  -0.0182 -0.0435 154 LYS A CD   
1221 C  CE   . LYS A 153 ? 0.3088 0.1971 0.2224 0.0364  -0.0501 -0.0124 154 LYS A CE   
1222 N  NZ   . LYS A 153 ? 0.3445 0.2543 0.2787 -0.0093 -0.0016 -0.0319 154 LYS A NZ   
1223 N  N    . PRO A 154 ? 0.1858 0.1522 0.2099 0.0019  -0.0670 -0.0032 155 PRO A N    
1224 C  CA   . PRO A 154 ? 0.1597 0.1760 0.2201 -0.0009 -0.0700 0.0338  155 PRO A CA   
1225 C  C    . PRO A 154 ? 0.1498 0.1597 0.2016 0.0018  -0.0789 0.0131  155 PRO A C    
1226 O  O    . PRO A 154 ? 0.1964 0.1870 0.2077 -0.0188 -0.0739 0.0034  155 PRO A O    
1227 C  CB   . PRO A 154 ? 0.1582 0.1840 0.2700 -0.0156 -0.0670 0.0137  155 PRO A CB   
1228 C  CG   . PRO A 154 ? 0.1998 0.2657 0.2642 0.0104  -0.0524 0.0436  155 PRO A CG   
1229 C  CD   . PRO A 154 ? 0.1431 0.2073 0.2358 -0.0144 -0.0482 0.0036  155 PRO A CD   
1230 N  N    . GLY A 155 ? 0.1644 0.1251 0.2276 0.0016  -0.0605 -0.0075 156 GLY A N    
1231 C  CA   . GLY A 155 ? 0.1680 0.1436 0.2289 -0.0020 -0.0314 -0.0104 156 GLY A CA   
1232 C  C    . GLY A 155 ? 0.2053 0.1573 0.2161 -0.0279 -0.0383 0.0008  156 GLY A C    
1233 O  O    . GLY A 155 ? 0.2383 0.1434 0.3000 -0.0187 -0.0512 0.0040  156 GLY A O    
1234 N  N    . LEU A 156 ? 0.1864 0.1248 0.1913 -0.0139 -0.0558 -0.0083 157 LEU A N    
1235 C  CA   . LEU A 156 ? 0.1952 0.0938 0.1658 -0.0228 -0.0684 -0.0068 157 LEU A CA   
1236 C  C    . LEU A 156 ? 0.1915 0.1213 0.1540 -0.0314 -0.0649 0.0164  157 LEU A C    
1237 O  O    . LEU A 156 ? 0.1971 0.1007 0.1930 -0.0354 -0.0826 -0.0061 157 LEU A O    
1238 C  CB   . LEU A 156 ? 0.2161 0.0967 0.1601 -0.0175 -0.0570 0.0036  157 LEU A CB   
1239 C  CG   . LEU A 156 ? 0.1738 0.1048 0.1495 -0.0407 -0.0321 0.0125  157 LEU A CG   
1240 C  CD1  . LEU A 156 ? 0.1761 0.1546 0.2102 -0.0466 -0.0723 -0.0422 157 LEU A CD1  
1241 C  CD2  . LEU A 156 ? 0.1910 0.1266 0.1577 -0.0059 -0.0592 0.0075  157 LEU A CD2  
1242 N  N    . GLN A 157 ? 0.1961 0.1213 0.1531 -0.0374 -0.0648 -0.0163 158 GLN A N    
1243 C  CA   . GLN A 157 ? 0.2067 0.1465 0.1572 -0.0374 -0.0546 -0.0069 158 GLN A CA   
1244 C  C    . GLN A 157 ? 0.2013 0.1442 0.1461 -0.0219 -0.0647 -0.0011 158 GLN A C    
1245 O  O    . GLN A 157 ? 0.2199 0.1415 0.1421 -0.0167 -0.0731 -0.0080 158 GLN A O    
1246 C  CB   . GLN A 157 ? 0.2351 0.1505 0.1731 -0.0401 -0.0555 -0.0084 158 GLN A CB   
1247 C  CG   . GLN A 157 ? 0.2688 0.1627 0.1877 -0.0117 -0.0482 -0.0216 158 GLN A CG   
1248 C  CD   . GLN A 157 ? 0.2893 0.1569 0.1817 -0.0178 -0.0414 0.0009  158 GLN A CD   
1249 O  OE1  . GLN A 157 ? 0.3700 0.1323 0.1735 -0.0078 -0.0628 0.0001  158 GLN A OE1  
1250 N  NE2  . GLN A 157 ? 0.3152 0.1645 0.2062 -0.0348 -0.0374 -0.0568 158 GLN A NE2  
1251 N  N    . LYS A 158 ? 0.2327 0.1517 0.1783 -0.0454 -0.0663 -0.0204 159 LYS A N    
1252 C  CA   . LYS A 158 ? 0.2349 0.1777 0.1628 -0.0236 -0.0617 -0.0077 159 LYS A CA   
1253 C  C    . LYS A 158 ? 0.2499 0.1524 0.1544 -0.0200 -0.0529 -0.0118 159 LYS A C    
1254 O  O    . LYS A 158 ? 0.2691 0.1768 0.1612 -0.0338 -0.0788 -0.0198 159 LYS A O    
1255 C  CB   . LYS A 158 ? 0.2843 0.1658 0.2179 0.0043  -0.0490 0.0003  159 LYS A CB   
1256 C  CG   . LYS A 158 ? 0.3473 0.2849 0.2726 -0.0386 -0.0481 0.0165  159 LYS A CG   
1257 C  CD   . LYS A 158 ? 0.4615 0.3737 0.3232 0.0013  -0.0213 0.0090  159 LYS A CD   
1258 C  CE   . LYS A 158 ? 0.4678 0.2970 0.3480 0.0026  -0.0242 0.0210  159 LYS A CE   
1259 N  NZ   . LYS A 158 ? 0.4631 0.3354 0.4189 0.0401  -0.0303 0.0255  159 LYS A NZ   
1260 N  N    . VAL A 159 ? 0.2236 0.1430 0.1254 -0.0151 -0.0676 -0.0003 160 VAL A N    
1261 C  CA   . VAL A 159 ? 0.2198 0.1408 0.1197 -0.0269 -0.0636 -0.0098 160 VAL A CA   
1262 C  C    . VAL A 159 ? 0.2395 0.1437 0.1252 -0.0244 -0.0521 -0.0007 160 VAL A C    
1263 O  O    . VAL A 159 ? 0.2490 0.1132 0.1669 -0.0391 -0.0540 0.0069  160 VAL A O    
1264 C  CB   . VAL A 159 ? 0.2420 0.1490 0.1091 -0.0104 -0.0619 0.0030  160 VAL A CB   
1265 C  CG1  . VAL A 159 ? 0.2201 0.1918 0.1449 -0.0269 -0.0684 0.0080  160 VAL A CG1  
1266 C  CG2  . VAL A 159 ? 0.2937 0.1379 0.1090 0.0105  -0.0813 -0.0165 160 VAL A CG2  
1267 N  N    . VAL A 160 ? 0.2631 0.0982 0.1261 -0.0267 -0.0446 -0.0165 161 VAL A N    
1268 C  CA   . VAL A 160 ? 0.2863 0.1023 0.1392 -0.0309 -0.0295 -0.0101 161 VAL A CA   
1269 C  C    . VAL A 160 ? 0.2879 0.1082 0.1652 -0.0314 -0.0286 -0.0053 161 VAL A C    
1270 O  O    . VAL A 160 ? 0.3182 0.1332 0.1769 -0.0209 -0.0306 -0.0251 161 VAL A O    
1271 C  CB   . VAL A 160 ? 0.3251 0.0911 0.1607 0.0121  -0.0039 0.0036  161 VAL A CB   
1272 C  CG1  . VAL A 160 ? 0.3484 0.2149 0.2464 -0.0293 -0.0299 -0.0207 161 VAL A CG1  
1273 C  CG2  . VAL A 160 ? 0.3606 0.1500 0.1760 0.0130  -0.0171 0.0352  161 VAL A CG2  
1274 N  N    . ASP A 161 ? 0.2886 0.1732 0.1280 -0.0611 -0.0519 -0.0176 162 ASP A N    
1275 C  CA   . ASP A 161 ? 0.3064 0.2217 0.1521 -0.0586 -0.0389 -0.0021 162 ASP A CA   
1276 C  C    . ASP A 161 ? 0.3301 0.2204 0.1332 -0.0652 -0.0395 0.0004  162 ASP A C    
1277 O  O    . ASP A 161 ? 0.3886 0.2980 0.1981 -0.0720 -0.0521 -0.0265 162 ASP A O    
1278 C  CB   . ASP A 161 ? 0.3233 0.2489 0.1873 -0.0430 -0.0272 0.0020  162 ASP A CB   
1279 C  CG   . ASP A 161 ? 0.3057 0.2625 0.2798 -0.0425 -0.0093 -0.0068 162 ASP A CG   
1280 O  OD1  . ASP A 161 ? 0.4038 0.2774 0.2596 -0.0283 -0.0010 -0.0101 162 ASP A OD1  
1281 O  OD2  . ASP A 161 ? 0.3222 0.2626 0.3469 -0.0756 -0.0675 -0.0328 162 ASP A OD2  
1282 N  N    . VAL A 162 ? 0.3157 0.1855 0.1367 -0.0581 -0.0511 -0.0080 163 VAL A N    
1283 C  CA   . VAL A 162 ? 0.3082 0.2102 0.1426 -0.0439 -0.0368 -0.0020 163 VAL A CA   
1284 C  C    . VAL A 162 ? 0.2988 0.1688 0.1339 -0.0228 -0.0108 0.0008  163 VAL A C    
1285 O  O    . VAL A 162 ? 0.3351 0.2144 0.1221 -0.0358 -0.0105 -0.0003 163 VAL A O    
1286 C  CB   . VAL A 162 ? 0.3192 0.1726 0.2015 -0.0263 -0.0127 0.0183  163 VAL A CB   
1287 C  CG1  . VAL A 162 ? 0.3337 0.1443 0.2034 0.0001  -0.0093 -0.0053 163 VAL A CG1  
1288 C  CG2  . VAL A 162 ? 0.3190 0.2224 0.2294 -0.0251 -0.0158 0.0271  163 VAL A CG2  
1289 N  N    . LEU A 163 ? 0.2978 0.1679 0.1417 -0.0387 -0.0438 -0.0140 164 LEU A N    
1290 C  CA   . LEU A 163 ? 0.2828 0.1858 0.1162 -0.0265 -0.0182 -0.0063 164 LEU A CA   
1291 C  C    . LEU A 163 ? 0.3029 0.1781 0.1296 -0.0264 -0.0175 -0.0005 164 LEU A C    
1292 O  O    . LEU A 163 ? 0.3403 0.1816 0.1440 -0.0395 0.0083  -0.0024 164 LEU A O    
1293 C  CB   . LEU A 163 ? 0.2916 0.1541 0.1193 -0.0115 -0.0145 -0.0097 164 LEU A CB   
1294 C  CG   . LEU A 163 ? 0.3067 0.1935 0.0999 -0.0284 0.0192  0.0162  164 LEU A CG   
1295 C  CD1  . LEU A 163 ? 0.2420 0.1541 0.1799 -0.0110 0.0010  0.0466  164 LEU A CD1  
1296 C  CD2  . LEU A 163 ? 0.2547 0.1792 0.1478 -0.0310 0.0172  -0.0184 164 LEU A CD2  
1297 N  N    . ASP A 164 ? 0.3527 0.2181 0.1435 -0.0526 0.0171  -0.0248 165 ASP A N    
1298 C  CA   . ASP A 164 ? 0.3597 0.2463 0.1702 -0.0429 0.0133  -0.0343 165 ASP A CA   
1299 C  C    . ASP A 164 ? 0.3536 0.2565 0.1881 -0.0264 0.0138  -0.0113 165 ASP A C    
1300 O  O    . ASP A 164 ? 0.3944 0.3079 0.2344 -0.0281 0.0251  0.0120  165 ASP A O    
1301 C  CB   . ASP A 164 ? 0.3984 0.2826 0.1650 -0.0434 0.0081  -0.0372 165 ASP A CB   
1302 C  CG   . ASP A 164 ? 0.3797 0.3201 0.2291 -0.0544 -0.0121 -0.0564 165 ASP A CG   
1303 O  OD1  . ASP A 164 ? 0.4730 0.3708 0.2094 -0.0465 0.0023  -0.0476 165 ASP A OD1  
1304 O  OD2  . ASP A 164 ? 0.5171 0.4591 0.2663 -0.0444 0.0500  -0.0122 165 ASP A OD2  
1305 N  N    . SER A 165 ? 0.3168 0.2358 0.1605 -0.0311 0.0037  -0.0048 166 SER A N    
1306 C  CA   . SER A 165 ? 0.3396 0.2487 0.1726 -0.0280 0.0026  0.0077  166 SER A CA   
1307 C  C    . SER A 165 ? 0.3289 0.2360 0.1440 -0.0349 0.0209  0.0217  166 SER A C    
1308 O  O    . SER A 165 ? 0.3644 0.2138 0.1759 -0.0289 0.0057  0.0184  166 SER A O    
1309 C  CB   . SER A 165 ? 0.3637 0.2537 0.2137 -0.0099 0.0328  0.0253  166 SER A CB   
1310 O  OG   . SER A 165 ? 0.3900 0.2689 0.2557 0.0171  -0.0184 -0.0059 166 SER A OG   
1311 N  N    . ILE A 166 ? 0.2996 0.2029 0.1165 -0.0099 -0.0111 0.0110  167 ILE A N    
1312 C  CA   . ILE A 166 ? 0.2940 0.1779 0.1394 -0.0156 0.0067  -0.0012 167 ILE A CA   
1313 C  C    . ILE A 166 ? 0.2492 0.1664 0.1485 -0.0151 0.0155  -0.0227 167 ILE A C    
1314 O  O    . ILE A 166 ? 0.2654 0.1831 0.1491 -0.0361 0.0071  -0.0011 167 ILE A O    
1315 C  CB   . ILE A 166 ? 0.2473 0.1470 0.1425 -0.0115 0.0191  -0.0013 167 ILE A CB   
1316 C  CG1  . ILE A 166 ? 0.2722 0.1291 0.0895 -0.0199 0.0171  0.0082  167 ILE A CG1  
1317 C  CG2  . ILE A 166 ? 0.2858 0.1614 0.1869 0.0171  -0.0303 0.0202  167 ILE A CG2  
1318 C  CD1  . ILE A 166 ? 0.2989 0.2210 0.1407 -0.0066 0.0234  -0.0220 167 ILE A CD1  
1319 N  N    . LYS A 167 ? 0.2882 0.1965 0.1776 -0.0227 0.0188  -0.0182 168 LYS A N    
1320 C  CA   . LYS A 167 ? 0.2956 0.1908 0.1645 -0.0022 0.0145  -0.0379 168 LYS A CA   
1321 C  C    . LYS A 167 ? 0.2996 0.1932 0.1603 -0.0147 0.0263  -0.0239 168 LYS A C    
1322 O  O    . LYS A 167 ? 0.3038 0.1730 0.1505 -0.0103 0.0238  -0.0076 168 LYS A O    
1323 C  CB   . LYS A 167 ? 0.3412 0.1961 0.1649 -0.0014 0.0161  -0.0561 168 LYS A CB   
1324 C  CG   . LYS A 167 ? 0.2964 0.2136 0.1839 0.0067  0.0024  -0.0331 168 LYS A CG   
1325 C  CD   . LYS A 167 ? 0.3648 0.2168 0.2281 0.0181  -0.0102 -0.0510 168 LYS A CD   
1326 C  CE   . LYS A 167 ? 0.4188 0.2991 0.3506 0.0315  -0.0170 -0.0399 168 LYS A CE   
1327 N  NZ   . LYS A 167 ? 0.4713 0.4390 0.4019 0.0168  -0.0206 -0.0778 168 LYS A NZ   
1328 N  N    . THR A 168 ? 0.2703 0.1529 0.1316 -0.0210 0.0393  0.0044  169 THR A N    
1329 C  CA   . THR A 168 ? 0.2603 0.1938 0.1599 -0.0270 0.0425  -0.0083 169 THR A CA   
1330 C  C    . THR A 168 ? 0.2286 0.1838 0.1251 -0.0110 0.0371  0.0103  169 THR A C    
1331 O  O    . THR A 168 ? 0.2780 0.2036 0.1625 -0.0361 0.0285  0.0096  169 THR A O    
1332 C  CB   . THR A 168 ? 0.2676 0.2130 0.2007 -0.0021 0.0250  0.0013  169 THR A CB   
1333 O  OG1  . THR A 168 ? 0.2947 0.2497 0.1624 -0.0325 0.0345  0.0213  169 THR A OG1  
1334 C  CG2  . THR A 168 ? 0.2464 0.2002 0.1869 -0.0373 0.0672  -0.0367 169 THR A CG2  
1335 N  N    . LYS A 169 ? 0.2719 0.2408 0.1792 -0.0515 0.0352  -0.0059 170 LYS A N    
1336 C  CA   . LYS A 169 ? 0.2838 0.2174 0.1830 -0.0448 0.0268  0.0102  170 LYS A CA   
1337 C  C    . LYS A 169 ? 0.2659 0.2170 0.1817 -0.0496 0.0355  0.0171  170 LYS A C    
1338 O  O    . LYS A 169 ? 0.3209 0.2877 0.2041 -0.0554 0.0663  0.0197  170 LYS A O    
1339 C  CB   . LYS A 169 ? 0.2873 0.2155 0.1902 -0.0317 0.0349  0.0023  170 LYS A CB   
1340 C  CG   . LYS A 169 ? 0.2776 0.2601 0.2255 -0.0385 0.0270  -0.0139 170 LYS A CG   
1341 C  CD   . LYS A 169 ? 0.3283 0.2829 0.2788 -0.0490 -0.0225 0.0058  170 LYS A CD   
1342 C  CE   . LYS A 169 ? 0.3676 0.4051 0.3991 -0.0578 -0.0266 -0.0298 170 LYS A CE   
1343 N  NZ   . LYS A 169 ? 0.3816 0.5467 0.5020 -0.0034 -0.0096 -0.0015 170 LYS A NZ   
1344 N  N    . GLY A 170 ? 0.3062 0.2156 0.2084 -0.0539 0.0273  0.0327  171 GLY A N    
1345 C  CA   . GLY A 170 ? 0.3068 0.2153 0.2392 -0.0468 0.0049  0.0407  171 GLY A CA   
1346 C  C    . GLY A 170 ? 0.3400 0.2284 0.2516 -0.0434 0.0108  0.0366  171 GLY A C    
1347 O  O    . GLY A 170 ? 0.3514 0.1959 0.2940 -0.0421 -0.0033 0.0466  171 GLY A O    
1348 N  N    . LYS A 171 ? 0.3230 0.1881 0.2010 -0.0605 0.0350  0.0395  172 LYS A N    
1349 C  CA   . LYS A 171 ? 0.3069 0.2091 0.2187 -0.0325 0.0317  0.0253  172 LYS A CA   
1350 C  C    . LYS A 171 ? 0.3064 0.1922 0.1826 -0.0267 0.0277  0.0324  172 LYS A C    
1351 O  O    . LYS A 171 ? 0.3056 0.2181 0.1404 -0.0316 0.0239  0.0345  172 LYS A O    
1352 C  CB   . LYS A 171 ? 0.3106 0.2171 0.2156 -0.0445 0.0317  0.0317  172 LYS A CB   
1353 C  CG   . LYS A 171 ? 0.2849 0.2436 0.2689 -0.0233 0.0295  -0.0476 172 LYS A CG   
1354 C  CD   . LYS A 171 ? 0.3819 0.2788 0.3183 -0.0311 0.0157  0.0028  172 LYS A CD   
1355 C  CE   . LYS A 171 ? 0.5193 0.4262 0.3970 -0.0059 -0.0101 -0.0049 172 LYS A CE   
1356 N  NZ   . LYS A 171 ? 0.5824 0.4365 0.4677 -0.0373 -0.0199 -0.0100 172 LYS A NZ   
1357 N  N    . SER A 172 ? 0.3122 0.2107 0.1693 -0.0247 0.0171  0.0373  173 SER A N    
1358 C  CA   . SER A 172 ? 0.3121 0.2076 0.1383 -0.0083 0.0074  0.0227  173 SER A CA   
1359 C  C    . SER A 172 ? 0.3051 0.1832 0.1224 0.0147  0.0075  0.0325  173 SER A C    
1360 O  O    . SER A 172 ? 0.3534 0.2679 0.0912 0.0345  0.0037  0.0286  173 SER A O    
1361 C  CB   . SER A 172 ? 0.3233 0.2157 0.1651 0.0009  0.0018  0.0414  173 SER A CB   
1362 O  OG   . SER A 172 ? 0.4068 0.1750 0.2116 0.0120  -0.0037 0.0767  173 SER A OG   
1363 N  N    . ALA A 173 ? 0.3397 0.2174 0.1463 0.0304  -0.0065 0.0220  174 ALA A N    
1364 C  CA   . ALA A 173 ? 0.3239 0.2296 0.1451 0.0497  -0.0163 0.0252  174 ALA A CA   
1365 C  C    . ALA A 173 ? 0.3190 0.2353 0.1606 0.0661  -0.0311 0.0252  174 ALA A C    
1366 O  O    . ALA A 173 ? 0.3397 0.2350 0.1030 0.0885  -0.0368 0.0464  174 ALA A O    
1367 C  CB   . ALA A 173 ? 0.3411 0.2543 0.1665 0.0290  -0.0395 -0.0010 174 ALA A CB   
1368 N  N    . ASP A 174 ? 0.3468 0.2274 0.1584 0.0648  -0.0486 0.0598  175 ASP A N    
1369 C  CA   . ASP A 174 ? 0.3412 0.2563 0.1836 0.0402  -0.0373 0.0450  175 ASP A CA   
1370 C  C    . ASP A 174 ? 0.3420 0.2334 0.1849 0.0429  -0.0527 0.0298  175 ASP A C    
1371 O  O    . ASP A 174 ? 0.3692 0.2165 0.2062 0.0824  -0.0326 -0.0321 175 ASP A O    
1372 C  CB   . ASP A 174 ? 0.3489 0.2801 0.2304 0.0550  -0.0305 0.0675  175 ASP A CB   
1373 C  CG   . ASP A 174 ? 0.4334 0.3864 0.3346 -0.0046 -0.0217 0.0235  175 ASP A CG   
1374 O  OD1  . ASP A 174 ? 0.3885 0.4641 0.3402 -0.0006 -0.0814 0.0135  175 ASP A OD1  
1375 O  OD2  . ASP A 174 ? 0.4754 0.4838 0.3189 -0.0207 -0.0246 0.0182  175 ASP A OD2  
1376 N  N    . PHE A 175 ? 0.3244 0.1886 0.1366 0.0285  -0.0388 0.0214  176 PHE A N    
1377 C  CA   . PHE A 175 ? 0.2764 0.1676 0.1242 0.0168  -0.0677 0.0077  176 PHE A CA   
1378 C  C    . PHE A 175 ? 0.2913 0.1457 0.1481 0.0111  -0.0717 0.0017  176 PHE A C    
1379 O  O    . PHE A 175 ? 0.3180 0.2201 0.1623 0.0591  -0.0873 0.0028  176 PHE A O    
1380 C  CB   . PHE A 175 ? 0.2886 0.1139 0.1354 -0.0002 -0.0705 -0.0010 176 PHE A CB   
1381 C  CG   . PHE A 175 ? 0.2788 0.1207 0.1701 0.0181  -0.0398 0.0123  176 PHE A CG   
1382 C  CD1  . PHE A 175 ? 0.2470 0.1392 0.1987 -0.0282 -0.0195 -0.0160 176 PHE A CD1  
1383 C  CD2  . PHE A 175 ? 0.2602 0.1492 0.1622 -0.0127 -0.0302 0.0370  176 PHE A CD2  
1384 C  CE1  . PHE A 175 ? 0.2625 0.1199 0.1523 -0.0242 -0.0193 -0.0029 176 PHE A CE1  
1385 C  CE2  . PHE A 175 ? 0.2957 0.1471 0.1423 -0.0236 -0.0708 0.0275  176 PHE A CE2  
1386 C  CZ   . PHE A 175 ? 0.3302 0.1359 0.1578 -0.0208 -0.0518 0.0065  176 PHE A CZ   
1387 N  N    . THR A 176 ? 0.2750 0.1631 0.1642 0.0324  -0.0722 0.0185  177 THR A N    
1388 C  CA   . THR A 176 ? 0.2648 0.1729 0.1623 0.0147  -0.0687 0.0284  177 THR A CA   
1389 C  C    . THR A 176 ? 0.2668 0.1665 0.1346 0.0152  -0.0744 0.0332  177 THR A C    
1390 O  O    . THR A 176 ? 0.2769 0.1202 0.1496 -0.0186 -0.0718 0.0358  177 THR A O    
1391 C  CB   . THR A 176 ? 0.2636 0.1920 0.1885 0.0171  -0.0709 0.0340  177 THR A CB   
1392 O  OG1  . THR A 176 ? 0.3380 0.2210 0.1784 0.0565  -0.0846 0.0290  177 THR A OG1  
1393 C  CG2  . THR A 176 ? 0.2587 0.2355 0.2422 0.0229  -0.0454 0.0508  177 THR A CG2  
1394 N  N    . ASN A 177 ? 0.2807 0.1137 0.1386 0.0192  -0.0746 0.0397  178 ASN A N    
1395 C  CA   . ASN A 177 ? 0.2798 0.1411 0.1607 0.0250  -0.0628 0.0443  178 ASN A CA   
1396 C  C    . ASN A 177 ? 0.2820 0.1253 0.1867 0.0038  -0.0655 0.0558  178 ASN A C    
1397 O  O    . ASN A 177 ? 0.3062 0.1517 0.2283 0.0152  -0.0794 0.0878  178 ASN A O    
1398 C  CB   . ASN A 177 ? 0.2639 0.1158 0.1861 0.0322  -0.0739 0.0639  178 ASN A CB   
1399 C  CG   . ASN A 177 ? 0.2515 0.1561 0.1555 0.0538  -0.0705 0.0419  178 ASN A CG   
1400 O  OD1  . ASN A 177 ? 0.3447 0.1326 0.2637 0.0446  -0.0076 0.0254  178 ASN A OD1  
1401 N  ND2  . ASN A 177 ? 0.3110 0.1786 0.1516 0.0265  -0.0368 0.0317  178 ASN A ND2  
1402 N  N    . PHE A 178 ? 0.2951 0.0909 0.1501 0.0080  -0.0789 0.0445  179 PHE A N    
1403 C  CA   . PHE A 178 ? 0.2716 0.1129 0.1433 0.0103  -0.0491 0.0423  179 PHE A CA   
1404 C  C    . PHE A 178 ? 0.2598 0.1268 0.1274 0.0029  -0.0563 0.0336  179 PHE A C    
1405 O  O    . PHE A 178 ? 0.2814 0.1308 0.1436 -0.0155 -0.0824 0.0211  179 PHE A O    
1406 C  CB   . PHE A 178 ? 0.2565 0.1083 0.1195 -0.0016 -0.0535 0.0568  179 PHE A CB   
1407 C  CG   . PHE A 178 ? 0.2569 0.0810 0.1603 0.0005  -0.0398 0.0469  179 PHE A CG   
1408 C  CD1  . PHE A 178 ? 0.2996 0.1217 0.1151 0.0048  -0.0501 0.0145  179 PHE A CD1  
1409 C  CD2  . PHE A 178 ? 0.2224 0.1406 0.1510 -0.0020 -0.0401 0.0138  179 PHE A CD2  
1410 C  CE1  . PHE A 178 ? 0.2917 0.1347 0.1430 -0.0237 -0.0603 0.0389  179 PHE A CE1  
1411 C  CE2  . PHE A 178 ? 0.1697 0.1198 0.1147 -0.0105 -0.0684 0.0023  179 PHE A CE2  
1412 C  CZ   . PHE A 178 ? 0.2492 0.0861 0.1098 0.0166  -0.0429 0.0229  179 PHE A CZ   
1413 N  N    . ASP A 179 ? 0.2497 0.1397 0.1509 0.0023  -0.0525 0.0280  180 ASP A N    
1414 C  CA   . ASP A 179 ? 0.2261 0.1631 0.1495 0.0095  -0.0459 0.0327  180 ASP A CA   
1415 C  C    . ASP A 179 ? 0.2007 0.1316 0.1494 -0.0017 -0.0467 0.0240  180 ASP A C    
1416 O  O    . ASP A 179 ? 0.2116 0.1341 0.1625 -0.0172 -0.0492 0.0145  180 ASP A O    
1417 C  CB   . ASP A 179 ? 0.2233 0.1479 0.1892 0.0187  -0.0558 0.0282  180 ASP A CB   
1418 C  CG   . ASP A 179 ? 0.2233 0.2445 0.2108 -0.0004 -0.0280 0.0377  180 ASP A CG   
1419 O  OD1  . ASP A 179 ? 0.2157 0.1411 0.2398 0.0188  -0.0893 0.0147  180 ASP A OD1  
1420 O  OD2  . ASP A 179 ? 0.2722 0.4040 0.3046 -0.0037 -0.0496 -0.0337 180 ASP A OD2  
1421 N  N    . PRO A 180 ? 0.1924 0.1244 0.1432 0.0008  -0.0616 0.0139  181 PRO A N    
1422 C  CA   . PRO A 180 ? 0.1725 0.1406 0.1519 0.0005  -0.0406 0.0137  181 PRO A CA   
1423 C  C    . PRO A 180 ? 0.1515 0.1196 0.1551 0.0020  -0.0363 0.0142  181 PRO A C    
1424 O  O    . PRO A 180 ? 0.1440 0.1197 0.1443 -0.0057 -0.0580 0.0167  181 PRO A O    
1425 C  CB   . PRO A 180 ? 0.1749 0.1577 0.1729 -0.0006 -0.0602 0.0157  181 PRO A CB   
1426 C  CG   . PRO A 180 ? 0.1922 0.1405 0.1871 -0.0389 -0.0720 0.0127  181 PRO A CG   
1427 C  CD   . PRO A 180 ? 0.2068 0.1429 0.1587 -0.0125 -0.0510 0.0123  181 PRO A CD   
1428 N  N    . ARG A 181 ? 0.1367 0.1229 0.1336 -0.0028 -0.0106 -0.0112 182 ARG A N    
1429 C  CA   . ARG A 181 ? 0.1575 0.1314 0.1689 0.0021  -0.0106 -0.0092 182 ARG A CA   
1430 C  C    . ARG A 181 ? 0.1584 0.1252 0.1573 -0.0031 -0.0253 0.0073  182 ARG A C    
1431 O  O    . ARG A 181 ? 0.1874 0.1493 0.1674 -0.0082 -0.0370 0.0326  182 ARG A O    
1432 C  CB   . ARG A 181 ? 0.1593 0.1280 0.2087 0.0371  -0.0193 -0.0105 182 ARG A CB   
1433 C  CG   . ARG A 181 ? 0.1627 0.1365 0.2073 0.0247  -0.0302 -0.0146 182 ARG A CG   
1434 C  CD   . ARG A 181 ? 0.1967 0.1892 0.2697 0.0483  -0.0191 -0.0060 182 ARG A CD   
1435 N  NE   . ARG A 181 ? 0.1407 0.1680 0.3189 0.0189  -0.0478 0.0405  182 ARG A NE   
1436 C  CZ   . ARG A 181 ? 0.1811 0.2231 0.2940 0.0405  -0.0133 0.0052  182 ARG A CZ   
1437 N  NH1  . ARG A 181 ? 0.2267 0.2273 0.3736 0.0389  0.0170  0.0318  182 ARG A NH1  
1438 N  NH2  . ARG A 181 ? 0.2160 0.2866 0.3440 0.0188  -0.0062 0.0334  182 ARG A NH2  
1439 N  N    . GLY A 182 ? 0.1804 0.1199 0.1424 -0.0082 -0.0509 -0.0149 183 GLY A N    
1440 C  CA   . GLY A 182 ? 0.1775 0.1003 0.1709 0.0064  -0.0746 0.0039  183 GLY A CA   
1441 C  C    . GLY A 182 ? 0.2078 0.1304 0.1910 0.0135  -0.0654 0.0066  183 GLY A C    
1442 O  O    . GLY A 182 ? 0.2502 0.0923 0.2098 0.0122  -0.0880 0.0252  183 GLY A O    
1443 N  N    . LEU A 183 ? 0.1726 0.1199 0.1649 0.0090  -0.0575 0.0165  184 LEU A N    
1444 C  CA   . LEU A 183 ? 0.1821 0.1155 0.1462 0.0033  -0.0425 0.0069  184 LEU A CA   
1445 C  C    . LEU A 183 ? 0.1613 0.1248 0.1384 -0.0047 -0.0253 -0.0029 184 LEU A C    
1446 O  O    . LEU A 183 ? 0.1797 0.1421 0.1899 0.0288  -0.0302 0.0258  184 LEU A O    
1447 C  CB   . LEU A 183 ? 0.1539 0.1309 0.1476 0.0040  -0.0345 0.0191  184 LEU A CB   
1448 C  CG   . LEU A 183 ? 0.1688 0.0904 0.1868 0.0004  -0.0142 0.0275  184 LEU A CG   
1449 C  CD1  . LEU A 183 ? 0.1398 0.1826 0.1964 -0.0115 -0.0413 0.0674  184 LEU A CD1  
1450 C  CD2  . LEU A 183 ? 0.2874 0.1591 0.1271 0.0203  -0.0316 -0.0142 184 LEU A CD2  
1451 N  N    . LEU A 184 ? 0.1614 0.1128 0.1429 0.0111  -0.0249 -0.0058 185 LEU A N    
1452 C  CA   . LEU A 184 ? 0.1305 0.1172 0.1417 -0.0140 -0.0251 0.0303  185 LEU A CA   
1453 C  C    . LEU A 184 ? 0.1941 0.1605 0.1465 -0.0402 -0.0575 0.0252  185 LEU A C    
1454 O  O    . LEU A 184 ? 0.2046 0.2105 0.2160 -0.0900 -0.0995 0.0729  185 LEU A O    
1455 C  CB   . LEU A 184 ? 0.1270 0.1317 0.1509 -0.0031 -0.0261 0.0029  185 LEU A CB   
1456 C  CG   . LEU A 184 ? 0.1133 0.1396 0.1757 -0.0052 -0.0240 0.0126  185 LEU A CG   
1457 C  CD1  . LEU A 184 ? 0.1027 0.1934 0.2106 0.0027  -0.0233 -0.0160 185 LEU A CD1  
1458 C  CD2  . LEU A 184 ? 0.1418 0.1394 0.1715 -0.0382 -0.0545 -0.0079 185 LEU A CD2  
1459 N  N    . PRO A 185 ? 0.1242 0.1339 0.1593 -0.0195 -0.0492 0.0598  186 PRO A N    
1460 C  CA   . PRO A 185 ? 0.1523 0.1319 0.1695 -0.0215 -0.0403 0.0470  186 PRO A CA   
1461 C  C    . PRO A 185 ? 0.1349 0.1570 0.2045 -0.0245 -0.0441 0.0495  186 PRO A C    
1462 O  O    . PRO A 185 ? 0.1067 0.1434 0.2875 -0.0049 -0.0359 0.0490  186 PRO A O    
1463 C  CB   . PRO A 185 ? 0.1286 0.1651 0.1556 -0.0025 -0.0262 0.0383  186 PRO A CB   
1464 C  CG   . PRO A 185 ? 0.1226 0.1282 0.1240 -0.0032 -0.0291 0.0000  186 PRO A CG   
1465 C  CD   . PRO A 185 ? 0.1398 0.1311 0.1343 -0.0134 -0.0700 0.0122  186 PRO A CD   
1466 N  N    . GLU A 186 ? 0.1476 0.1828 0.2157 -0.0345 -0.0312 0.0422  187 GLU A N    
1467 C  CA   . GLU A 186 ? 0.1501 0.1592 0.2416 -0.0393 -0.0221 0.0252  187 GLU A CA   
1468 C  C    . GLU A 186 ? 0.1251 0.1537 0.2582 -0.0308 -0.0229 0.0205  187 GLU A C    
1469 O  O    . GLU A 186 ? 0.1688 0.1917 0.3060 0.0121  -0.0308 0.0167  187 GLU A O    
1470 C  CB   . GLU A 186 ? 0.1493 0.1614 0.2965 -0.0339 -0.0328 0.0435  187 GLU A CB   
1471 C  CG   . GLU A 186 ? 0.2521 0.2403 0.3543 -0.0402 -0.0036 0.0120  187 GLU A CG   
1472 C  CD   . GLU A 186 ? 0.2160 0.2191 0.3287 -0.0207 0.0015  0.0284  187 GLU A CD   
1473 O  OE1  . GLU A 186 ? 0.1916 0.2152 0.4325 -0.0324 0.0062  -0.0352 187 GLU A OE1  
1474 O  OE2  . GLU A 186 ? 0.3346 0.3556 0.4259 -0.0446 0.0721  0.0672  187 GLU A OE2  
1475 N  N    . SER A 187 ? 0.0682 0.1766 0.2246 -0.0329 -0.0232 0.0064  188 SER A N    
1476 C  CA   . SER A 187 ? 0.0978 0.1698 0.2059 -0.0074 0.0011  0.0126  188 SER A CA   
1477 C  C    . SER A 187 ? 0.0869 0.1641 0.1990 -0.0146 0.0139  0.0028  188 SER A C    
1478 O  O    . SER A 187 ? 0.1062 0.1845 0.2143 -0.0020 0.0034  -0.0063 188 SER A O    
1479 C  CB   . SER A 187 ? 0.1370 0.1925 0.2186 0.0002  -0.0079 0.0271  188 SER A CB   
1480 O  OG   . SER A 187 ? 0.1841 0.1926 0.2461 -0.0238 -0.0264 0.0121  188 SER A OG   
1481 N  N    . LEU A 188 ? 0.1094 0.1307 0.2079 -0.0413 0.0082  -0.0047 189 LEU A N    
1482 C  CA   . LEU A 188 ? 0.1315 0.1294 0.2042 -0.0117 -0.0208 -0.0066 189 LEU A CA   
1483 C  C    . LEU A 188 ? 0.1093 0.1510 0.1922 -0.0150 -0.0122 -0.0064 189 LEU A C    
1484 O  O    . LEU A 188 ? 0.1215 0.1894 0.2143 -0.0181 -0.0334 -0.0423 189 LEU A O    
1485 C  CB   . LEU A 188 ? 0.1590 0.1066 0.2224 -0.0128 -0.0227 0.0335  189 LEU A CB   
1486 C  CG   . LEU A 188 ? 0.1803 0.1952 0.2427 0.0143  -0.0173 -0.0107 189 LEU A CG   
1487 C  CD1  . LEU A 188 ? 0.1813 0.1600 0.3036 0.0239  -0.0023 -0.0102 189 LEU A CD1  
1488 C  CD2  . LEU A 188 ? 0.1603 0.2414 0.2655 0.0067  -0.0281 0.0024  189 LEU A CD2  
1489 N  N    . ASP A 189 ? 0.1312 0.1827 0.1803 0.0179  0.0104  -0.0141 190 ASP A N    
1490 C  CA   . ASP A 189 ? 0.1327 0.1785 0.1854 0.0026  0.0062  -0.0017 190 ASP A CA   
1491 C  C    . ASP A 189 ? 0.1331 0.1556 0.1753 -0.0010 0.0108  0.0072  190 ASP A C    
1492 O  O    . ASP A 189 ? 0.1182 0.1620 0.1640 0.0072  0.0007  -0.0297 190 ASP A O    
1493 C  CB   . ASP A 189 ? 0.1433 0.1873 0.1904 -0.0011 0.0329  0.0144  190 ASP A CB   
1494 C  CG   . ASP A 189 ? 0.1942 0.2591 0.2539 -0.0408 0.0152  0.0133  190 ASP A CG   
1495 O  OD1  . ASP A 189 ? 0.2068 0.3688 0.3291 -0.0492 0.0443  -0.0450 190 ASP A OD1  
1496 O  OD2  . ASP A 189 ? 0.2244 0.3693 0.3180 -0.0667 0.0137  0.0706  190 ASP A OD2  
1497 N  N    . TYR A 190 ? 0.0881 0.1659 0.1393 -0.0083 0.0107  -0.0061 191 TYR A N    
1498 C  CA   . TYR A 190 ? 0.1039 0.1341 0.1202 -0.0153 -0.0022 0.0076  191 TYR A CA   
1499 C  C    . TYR A 190 ? 0.1100 0.1180 0.1185 -0.0130 0.0029  -0.0124 191 TYR A C    
1500 O  O    . TYR A 190 ? 0.1134 0.1452 0.1192 -0.0059 0.0328  -0.0009 191 TYR A O    
1501 C  CB   . TYR A 190 ? 0.1662 0.1240 0.1236 0.0023  0.0079  -0.0023 191 TYR A CB   
1502 C  CG   . TYR A 190 ? 0.1405 0.0860 0.1368 0.0105  -0.0231 0.0157  191 TYR A CG   
1503 C  CD1  . TYR A 190 ? 0.1217 0.1010 0.1636 -0.0292 -0.0113 -0.0047 191 TYR A CD1  
1504 C  CD2  . TYR A 190 ? 0.1059 0.1179 0.1356 0.0087  0.0060  0.0167  191 TYR A CD2  
1505 C  CE1  . TYR A 190 ? 0.1440 0.1011 0.1327 0.0089  -0.0211 0.0168  191 TYR A CE1  
1506 C  CE2  . TYR A 190 ? 0.1684 0.1458 0.1551 -0.0048 -0.0076 -0.0252 191 TYR A CE2  
1507 C  CZ   . TYR A 190 ? 0.1766 0.1221 0.1235 0.0226  -0.0049 -0.0163 191 TYR A CZ   
1508 O  OH   . TYR A 190 ? 0.2045 0.1508 0.1389 0.0084  -0.0059 -0.0169 191 TYR A OH   
1509 N  N    . TRP A 191 ? 0.0845 0.1220 0.1232 -0.0172 -0.0011 0.0038  192 TRP A N    
1510 C  CA   . TRP A 191 ? 0.0750 0.0816 0.1247 -0.0183 0.0004  0.0103  192 TRP A CA   
1511 C  C    . TRP A 191 ? 0.0791 0.0966 0.1072 -0.0071 -0.0028 0.0014  192 TRP A C    
1512 O  O    . TRP A 191 ? 0.1385 0.0948 0.0913 -0.0125 -0.0027 -0.0058 192 TRP A O    
1513 C  CB   . TRP A 191 ? 0.1116 0.1082 0.1312 -0.0107 0.0114  0.0307  192 TRP A CB   
1514 C  CG   . TRP A 191 ? 0.1171 0.0826 0.1074 0.0073  0.0082  0.0020  192 TRP A CG   
1515 C  CD1  . TRP A 191 ? 0.1320 0.1162 0.1468 0.0104  0.0377  0.0161  192 TRP A CD1  
1516 C  CD2  . TRP A 191 ? 0.1042 0.1028 0.1300 0.0166  -0.0006 0.0100  192 TRP A CD2  
1517 N  NE1  . TRP A 191 ? 0.1690 0.1270 0.1312 0.0015  0.0227  0.0273  192 TRP A NE1  
1518 C  CE2  . TRP A 191 ? 0.1357 0.1337 0.1334 0.0200  -0.0168 0.0007  192 TRP A CE2  
1519 C  CE3  . TRP A 191 ? 0.0869 0.1497 0.1396 -0.0130 -0.0090 0.0100  192 TRP A CE3  
1520 C  CZ2  . TRP A 191 ? 0.1641 0.1127 0.1249 -0.0108 -0.0275 0.0413  192 TRP A CZ2  
1521 C  CZ3  . TRP A 191 ? 0.1068 0.1583 0.1680 -0.0113 0.0034  -0.0048 192 TRP A CZ3  
1522 C  CH2  . TRP A 191 ? 0.1332 0.1101 0.1554 -0.0084 -0.0170 0.0027  192 TRP A CH2  
1523 N  N    . THR A 192 ? 0.0940 0.0661 0.1086 -0.0224 -0.0202 0.0061  193 THR A N    
1524 C  CA   . THR A 192 ? 0.0957 0.0998 0.0950 -0.0047 -0.0203 0.0044  193 THR A CA   
1525 C  C    . THR A 192 ? 0.0919 0.0980 0.1052 -0.0263 -0.0160 0.0086  193 THR A C    
1526 O  O    . THR A 192 ? 0.1285 0.1373 0.1063 -0.0045 0.0093  0.0236  193 THR A O    
1527 C  CB   . THR A 192 ? 0.1225 0.1049 0.0898 0.0054  0.0184  -0.0089 193 THR A CB   
1528 O  OG1  . THR A 192 ? 0.1145 0.1003 0.1246 0.0022  0.0040  -0.0127 193 THR A OG1  
1529 C  CG2  . THR A 192 ? 0.1720 0.1163 0.0883 0.0165  0.0390  -0.0113 193 THR A CG2  
1530 N  N    . TYR A 193 ? 0.1001 0.0827 0.1102 -0.0309 -0.0015 -0.0002 194 TYR A N    
1531 C  CA   . TYR A 193 ? 0.0942 0.0767 0.1059 -0.0171 -0.0127 0.0108  194 TYR A CA   
1532 C  C    . TYR A 193 ? 0.1104 0.0759 0.1023 -0.0024 -0.0045 -0.0087 194 TYR A C    
1533 O  O    . TYR A 193 ? 0.1196 0.1070 0.0936 0.0076  0.0060  -0.0168 194 TYR A O    
1534 C  CB   . TYR A 193 ? 0.1242 0.1024 0.0768 0.0091  0.0102  -0.0061 194 TYR A CB   
1535 C  CG   . TYR A 193 ? 0.1077 0.0949 0.0568 -0.0003 0.0122  -0.0051 194 TYR A CG   
1536 C  CD1  . TYR A 193 ? 0.1502 0.0844 0.0897 0.0100  -0.0232 -0.0241 194 TYR A CD1  
1537 C  CD2  . TYR A 193 ? 0.1002 0.0982 0.1161 -0.0098 -0.0025 0.0000  194 TYR A CD2  
1538 C  CE1  . TYR A 193 ? 0.0757 0.0900 0.1045 -0.0104 0.0312  -0.0124 194 TYR A CE1  
1539 C  CE2  . TYR A 193 ? 0.1365 0.0864 0.1105 0.0691  -0.0278 -0.0160 194 TYR A CE2  
1540 C  CZ   . TYR A 193 ? 0.0951 0.0664 0.0842 0.0111  0.0023  -0.0066 194 TYR A CZ   
1541 O  OH   . TYR A 193 ? 0.0931 0.0900 0.1059 0.0043  0.0163  -0.0112 194 TYR A OH   
1542 N  N    . PRO A 194 ? 0.0993 0.1166 0.0740 -0.0082 -0.0277 -0.0077 195 PRO A N    
1543 C  CA   . PRO A 194 ? 0.1067 0.0987 0.0816 -0.0127 0.0041  -0.0244 195 PRO A CA   
1544 C  C    . PRO A 194 ? 0.1200 0.0762 0.0975 -0.0063 -0.0047 -0.0061 195 PRO A C    
1545 O  O    . PRO A 194 ? 0.1154 0.1076 0.1094 -0.0025 -0.0062 -0.0026 195 PRO A O    
1546 C  CB   . PRO A 194 ? 0.1340 0.1271 0.0738 0.0039  -0.0090 -0.0019 195 PRO A CB   
1547 C  CG   . PRO A 194 ? 0.1498 0.1441 0.0855 -0.0197 -0.0251 -0.0205 195 PRO A CG   
1548 C  CD   . PRO A 194 ? 0.1309 0.1587 0.0557 -0.0469 -0.0458 -0.0073 195 PRO A CD   
1549 N  N    . GLY A 195 ? 0.0911 0.1077 0.0443 -0.0033 0.0077  -0.0158 196 GLY A N    
1550 C  CA   . GLY A 195 ? 0.1085 0.1247 0.0877 -0.0071 0.0127  0.0056  196 GLY A CA   
1551 C  C    . GLY A 195 ? 0.0655 0.0860 0.0900 -0.0243 -0.0025 -0.0120 196 GLY A C    
1552 O  O    . GLY A 195 ? 0.1003 0.0590 0.1231 0.0013  -0.0126 0.0034  196 GLY A O    
1553 N  N    . SER A 196 ? 0.0995 0.1032 0.0900 0.0090  -0.0143 -0.0196 197 SER A N    
1554 C  CA   . SER A 196 ? 0.0949 0.0975 0.0885 0.0080  0.0021  -0.0249 197 SER A CA   
1555 C  C    . SER A 196 ? 0.0714 0.0807 0.1010 0.0235  -0.0035 -0.0095 197 SER A C    
1556 O  O    . SER A 196 ? 0.0920 0.0765 0.1115 0.0000  0.0022  -0.0069 197 SER A O    
1557 C  CB   . SER A 196 ? 0.1083 0.1135 0.1469 0.0288  -0.0133 -0.0268 197 SER A CB   
1558 O  OG   . SER A 196 ? 0.0768 0.0868 0.1440 0.0066  -0.0188 -0.0078 197 SER A OG   
1559 N  N    . LEU A 197 ? 0.0941 0.1243 0.0858 0.0094  0.0027  -0.0109 198 LEU A N    
1560 C  CA   . LEU A 197 ? 0.0830 0.0697 0.1216 -0.0191 0.0270  -0.0132 198 LEU A CA   
1561 C  C    . LEU A 197 ? 0.0722 0.1036 0.1043 -0.0092 0.0082  -0.0240 198 LEU A C    
1562 O  O    . LEU A 197 ? 0.0822 0.0854 0.1236 -0.0191 -0.0201 -0.0036 198 LEU A O    
1563 C  CB   . LEU A 197 ? 0.1210 0.0897 0.1580 -0.0112 0.0158  0.0129  198 LEU A CB   
1564 C  CG   . LEU A 197 ? 0.1932 0.1656 0.2407 -0.0114 0.0344  0.0605  198 LEU A CG   
1565 C  CD1  . LEU A 197 ? 0.1717 0.2183 0.2698 -0.0362 0.0757  0.0889  198 LEU A CD1  
1566 C  CD2  . LEU A 197 ? 0.1589 0.2391 0.2180 -0.0131 0.0511  0.0404  198 LEU A CD2  
1567 N  N    . THR A 198 ? 0.1049 0.0770 0.1116 -0.0058 -0.0161 -0.0164 199 THR A N    
1568 C  CA   . THR A 198 ? 0.0967 0.0705 0.0961 -0.0106 0.0025  -0.0368 199 THR A CA   
1569 C  C    . THR A 198 ? 0.1021 0.1033 0.1445 -0.0173 -0.0117 -0.0149 199 THR A C    
1570 O  O    . THR A 198 ? 0.1041 0.0989 0.1229 -0.0085 0.0124  -0.0254 199 THR A O    
1571 C  CB   . THR A 198 ? 0.1007 0.0491 0.1284 0.0029  -0.0185 -0.0435 199 THR A CB   
1572 O  OG1  . THR A 198 ? 0.1026 0.1126 0.0978 -0.0117 -0.0281 -0.0111 199 THR A OG1  
1573 C  CG2  . THR A 198 ? 0.0977 0.1145 0.1155 0.0110  0.0288  -0.0412 199 THR A CG2  
1574 N  N    . THR A 199 ? 0.1403 0.1149 0.1029 -0.0378 0.0149  -0.0102 200 THR A N    
1575 C  CA   . THR A 199 ? 0.1224 0.1044 0.1240 -0.0510 0.0037  -0.0023 200 THR A CA   
1576 C  C    . THR A 199 ? 0.1150 0.1225 0.1223 -0.0268 0.0089  0.0001  200 THR A C    
1577 O  O    . THR A 199 ? 0.1134 0.1047 0.1596 -0.0376 0.0281  -0.0365 200 THR A O    
1578 C  CB   . THR A 199 ? 0.1323 0.1148 0.1343 -0.0411 -0.0073 -0.0053 200 THR A CB   
1579 O  OG1  . THR A 199 ? 0.2555 0.1416 0.1636 0.0076  -0.0156 -0.0116 200 THR A OG1  
1580 C  CG2  . THR A 199 ? 0.1573 0.1124 0.1546 -0.0610 0.0070  -0.0321 200 THR A CG2  
1581 N  N    . PRO A 200 ? 0.0954 0.1310 0.1393 -0.0295 0.0199  -0.0211 201 PRO A N    
1582 C  CA   . PRO A 200 ? 0.0976 0.1287 0.1616 -0.0251 0.0249  0.0179  201 PRO A CA   
1583 C  C    . PRO A 200 ? 0.1097 0.1145 0.1559 -0.0254 0.0216  0.0051  201 PRO A C    
1584 O  O    . PRO A 200 ? 0.1662 0.1462 0.1739 0.0117  0.0056  -0.0263 201 PRO A O    
1585 C  CB   . PRO A 200 ? 0.1206 0.1576 0.1775 -0.0200 0.0217  0.0021  201 PRO A CB   
1586 C  CG   . PRO A 200 ? 0.1210 0.1676 0.1523 -0.0179 -0.0026 -0.0209 201 PRO A CG   
1587 C  CD   . PRO A 200 ? 0.0944 0.1483 0.1576 -0.0311 0.0267  -0.0308 201 PRO A CD   
1588 N  N    . PRO A 201 ? 0.1407 0.1323 0.1457 -0.0189 0.0133  -0.0021 202 PRO A N    
1589 C  CA   . PRO A 201 ? 0.1541 0.1226 0.1629 -0.0328 0.0144  -0.0047 202 PRO A CA   
1590 C  C    . PRO A 201 ? 0.1248 0.1121 0.1225 -0.0082 0.0122  -0.0106 202 PRO A C    
1591 O  O    . PRO A 201 ? 0.1346 0.1125 0.1656 -0.0294 0.0118  -0.0289 202 PRO A O    
1592 C  CB   . PRO A 201 ? 0.1593 0.0986 0.1814 -0.0383 0.0140  -0.0099 202 PRO A CB   
1593 C  CG   . PRO A 201 ? 0.1886 0.1338 0.1992 -0.0415 -0.0300 -0.0169 202 PRO A CG   
1594 C  CD   . PRO A 201 ? 0.1363 0.1015 0.1420 -0.0268 -0.0035 0.0043  202 PRO A CD   
1595 N  N    . LEU A 202 ? 0.1009 0.1440 0.1275 -0.0201 0.0235  -0.0195 203 LEU A N    
1596 C  CA   . LEU A 202 ? 0.1020 0.1064 0.1250 0.0009  0.0102  -0.0125 203 LEU A CA   
1597 C  C    . LEU A 202 ? 0.0806 0.0935 0.1510 -0.0166 0.0032  -0.0225 203 LEU A C    
1598 O  O    . LEU A 202 ? 0.0968 0.1012 0.1624 -0.0007 -0.0021 -0.0267 203 LEU A O    
1599 C  CB   . LEU A 202 ? 0.0586 0.1177 0.1736 0.0194  -0.0093 -0.0682 203 LEU A CB   
1600 C  CG   . LEU A 202 ? 0.0709 0.1239 0.1911 -0.0262 0.0147  -0.0545 203 LEU A CG   
1601 C  CD1  . LEU A 202 ? 0.0919 0.1438 0.2232 0.0059  -0.0186 -0.0303 203 LEU A CD1  
1602 C  CD2  . LEU A 202 ? 0.1042 0.1173 0.2099 -0.0301 -0.0217 -0.0327 203 LEU A CD2  
1603 N  N    . LEU A 203 ? 0.0938 0.0902 0.1310 0.0050  0.0139  -0.0263 204 LEU A N    
1604 C  CA   . LEU A 203 ? 0.0988 0.1095 0.1561 -0.0014 0.0103  -0.0191 204 LEU A CA   
1605 C  C    . LEU A 203 ? 0.0864 0.1099 0.1437 0.0151  0.0001  -0.0172 204 LEU A C    
1606 O  O    . LEU A 203 ? 0.1081 0.0933 0.1439 -0.0251 -0.0026 -0.0232 204 LEU A O    
1607 C  CB   . LEU A 203 ? 0.1385 0.0895 0.1522 -0.0056 0.0187  0.0037  204 LEU A CB   
1608 C  CG   . LEU A 203 ? 0.1698 0.1313 0.1896 -0.0237 0.0199  0.0046  204 LEU A CG   
1609 C  CD1  . LEU A 203 ? 0.1853 0.1368 0.2178 -0.0147 -0.0007 0.0221  204 LEU A CD1  
1610 C  CD2  . LEU A 203 ? 0.1894 0.1691 0.2607 -0.0493 0.0139  -0.0108 204 LEU A CD2  
1611 N  N    . GLU A 204 ? 0.0933 0.1225 0.1502 -0.0082 -0.0228 -0.0286 205 GLU A N    
1612 C  CA   . GLU A 204 ? 0.1012 0.1138 0.1130 0.0229  -0.0347 -0.0294 205 GLU A CA   
1613 C  C    . GLU A 204 ? 0.0919 0.1099 0.1546 0.0042  -0.0313 -0.0154 205 GLU A C    
1614 O  O    . GLU A 204 ? 0.1411 0.1397 0.1505 0.0280  -0.0356 -0.0496 205 GLU A O    
1615 C  CB   . GLU A 204 ? 0.0839 0.1080 0.1418 0.0064  -0.0470 0.0011  205 GLU A CB   
1616 C  CG   . GLU A 204 ? 0.1027 0.1805 0.1853 0.0085  -0.0590 0.0060  205 GLU A CG   
1617 C  CD   . GLU A 204 ? 0.1278 0.1334 0.1305 0.0077  -0.0319 -0.0051 205 GLU A CD   
1618 O  OE1  . GLU A 204 ? 0.1749 0.1561 0.1999 0.0066  -0.0707 -0.0685 205 GLU A OE1  
1619 O  OE2  . GLU A 204 ? 0.1019 0.1693 0.1889 0.0022  -0.0348 -0.0067 205 GLU A OE2  
1620 N  N    . CYS A 205 ? 0.0779 0.1030 0.1564 0.0031  -0.0277 -0.0296 206 CYS A N    
1621 C  CA   . CYS A 205 ? 0.0903 0.0960 0.1195 0.0062  -0.0093 -0.0002 206 CYS A CA   
1622 C  C    . CYS A 205 ? 0.1083 0.0880 0.1233 -0.0014 -0.0225 0.0004  206 CYS A C    
1623 O  O    . CYS A 205 ? 0.1331 0.0881 0.1612 -0.0075 -0.0207 -0.0116 206 CYS A O    
1624 C  CB   . CYS A 205 ? 0.1305 0.0892 0.1240 -0.0031 -0.0182 -0.0072 206 CYS A CB   
1625 S  SG   . CYS A 205 ? 0.1734 0.1051 0.1337 0.0000  -0.0261 -0.0082 206 CYS A SG   
1626 N  N    . VAL A 206 ? 0.1091 0.0822 0.1131 -0.0124 -0.0035 -0.0106 207 VAL A N    
1627 C  CA   . VAL A 206 ? 0.0889 0.0727 0.1111 -0.0024 0.0037  -0.0167 207 VAL A CA   
1628 C  C    . VAL A 206 ? 0.0966 0.0713 0.1181 0.0053  0.0066  -0.0102 207 VAL A C    
1629 O  O    . VAL A 206 ? 0.1121 0.0956 0.1403 0.0095  0.0000  -0.0060 207 VAL A O    
1630 C  CB   . VAL A 206 ? 0.0843 0.0691 0.1105 0.0037  0.0038  -0.0251 207 VAL A CB   
1631 C  CG1  . VAL A 206 ? 0.0991 0.1110 0.1268 -0.0484 -0.0119 -0.0307 207 VAL A CG1  
1632 C  CG2  . VAL A 206 ? 0.1203 0.1098 0.0997 -0.0171 0.0139  -0.0229 207 VAL A CG2  
1633 N  N    . THR A 207 ? 0.0977 0.0722 0.1087 0.0083  0.0099  -0.0109 208 THR A N    
1634 C  CA   . THR A 207 ? 0.0888 0.0699 0.1052 -0.0052 0.0067  -0.0309 208 THR A CA   
1635 C  C    . THR A 207 ? 0.1028 0.0470 0.1062 -0.0010 0.0077  -0.0029 208 THR A C    
1636 O  O    . THR A 207 ? 0.1143 0.0609 0.0982 -0.0022 -0.0178 0.0062  208 THR A O    
1637 C  CB   . THR A 207 ? 0.1044 0.1127 0.1385 0.0068  0.0264  -0.0277 208 THR A CB   
1638 O  OG1  . THR A 207 ? 0.1254 0.0752 0.1284 -0.0048 -0.0028 -0.0309 208 THR A OG1  
1639 C  CG2  . THR A 207 ? 0.1193 0.0779 0.1484 -0.0306 0.0026  -0.0101 208 THR A CG2  
1640 N  N    . TRP A 208 ? 0.1055 0.0348 0.1241 -0.0016 -0.0075 -0.0063 209 TRP A N    
1641 C  CA   . TRP A 208 ? 0.0714 0.0637 0.1039 -0.0078 -0.0108 -0.0196 209 TRP A CA   
1642 C  C    . TRP A 208 ? 0.0663 0.0736 0.1021 -0.0024 0.0012  -0.0196 209 TRP A C    
1643 O  O    . TRP A 208 ? 0.0847 0.0940 0.1100 -0.0216 -0.0026 -0.0110 209 TRP A O    
1644 C  CB   . TRP A 208 ? 0.0901 0.0742 0.1183 0.0248  0.0000  -0.0007 209 TRP A CB   
1645 C  CG   . TRP A 208 ? 0.0730 0.0880 0.0731 0.0103  -0.0264 -0.0002 209 TRP A CG   
1646 C  CD1  . TRP A 208 ? 0.0709 0.0924 0.0873 0.0269  0.0157  0.0000  209 TRP A CD1  
1647 C  CD2  . TRP A 208 ? 0.0857 0.0730 0.0970 0.0023  -0.0159 -0.0048 209 TRP A CD2  
1648 N  NE1  . TRP A 208 ? 0.0986 0.1071 0.0938 -0.0059 -0.0076 -0.0354 209 TRP A NE1  
1649 C  CE2  . TRP A 208 ? 0.0679 0.0590 0.1144 -0.0086 -0.0261 -0.0231 209 TRP A CE2  
1650 C  CE3  . TRP A 208 ? 0.0867 0.0914 0.0800 -0.0143 -0.0422 -0.0054 209 TRP A CE3  
1651 C  CZ2  . TRP A 208 ? 0.1196 0.0867 0.1033 0.0480  -0.0336 -0.0176 209 TRP A CZ2  
1652 C  CZ3  . TRP A 208 ? 0.1086 0.0750 0.1095 -0.0008 -0.0128 -0.0154 209 TRP A CZ3  
1653 C  CH2  . TRP A 208 ? 0.0804 0.0977 0.1090 0.0137  -0.0194 -0.0088 209 TRP A CH2  
1654 N  N    . ILE A 209 ? 0.0802 0.0812 0.1088 -0.0224 -0.0046 -0.0219 210 ILE A N    
1655 C  CA   . ILE A 209 ? 0.0743 0.0548 0.1182 0.0018  -0.0171 -0.0218 210 ILE A CA   
1656 C  C    . ILE A 209 ? 0.0842 0.0841 0.1072 -0.0128 0.0049  -0.0090 210 ILE A C    
1657 O  O    . ILE A 209 ? 0.1196 0.0948 0.0964 0.0109  -0.0200 0.0074  210 ILE A O    
1658 C  CB   . ILE A 209 ? 0.0954 0.0447 0.1655 0.0117  0.0093  -0.0204 210 ILE A CB   
1659 C  CG1  . ILE A 209 ? 0.1148 0.0745 0.1540 0.0330  0.0117  -0.0398 210 ILE A CG1  
1660 C  CG2  . ILE A 209 ? 0.0846 0.1459 0.1419 0.0030  -0.0056 0.0270  210 ILE A CG2  
1661 C  CD1  . ILE A 209 ? 0.1589 0.1072 0.2028 0.0326  -0.0343 -0.0292 210 ILE A CD1  
1662 N  N    . VAL A 210 ? 0.0899 0.0562 0.1276 -0.0025 0.0079  -0.0160 211 VAL A N    
1663 C  CA   . VAL A 210 ? 0.0944 0.0714 0.0975 0.0074  0.0020  -0.0056 211 VAL A CA   
1664 C  C    . VAL A 210 ? 0.0961 0.0651 0.0859 0.0030  -0.0024 0.0044  211 VAL A C    
1665 O  O    . VAL A 210 ? 0.1150 0.0976 0.1033 -0.0062 0.0117  0.0192  211 VAL A O    
1666 C  CB   . VAL A 210 ? 0.0763 0.0857 0.1118 0.0079  0.0037  0.0127  211 VAL A CB   
1667 C  CG1  . VAL A 210 ? 0.1582 0.0508 0.0909 0.0098  -0.0308 -0.0286 211 VAL A CG1  
1668 C  CG2  . VAL A 210 ? 0.0781 0.0796 0.1291 -0.0148 0.0044  0.0025  211 VAL A CG2  
1669 N  N    . LEU A 211 ? 0.0969 0.0954 0.1051 -0.0251 -0.0137 -0.0065 212 LEU A N    
1670 C  CA   . LEU A 211 ? 0.1001 0.0869 0.1133 -0.0239 -0.0170 0.0184  212 LEU A CA   
1671 C  C    . LEU A 211 ? 0.1019 0.1249 0.1115 -0.0188 -0.0112 0.0327  212 LEU A C    
1672 O  O    . LEU A 211 ? 0.1003 0.0902 0.1182 0.0004  -0.0032 0.0067  212 LEU A O    
1673 C  CB   . LEU A 211 ? 0.1051 0.1205 0.1055 -0.0133 -0.0299 0.0244  212 LEU A CB   
1674 C  CG   . LEU A 211 ? 0.1233 0.1195 0.1233 -0.0187 -0.0287 0.0250  212 LEU A CG   
1675 C  CD1  . LEU A 211 ? 0.1497 0.1956 0.1425 -0.0106 -0.0412 0.0249  212 LEU A CD1  
1676 C  CD2  . LEU A 211 ? 0.1562 0.1203 0.1816 0.0149  -0.0071 0.0049  212 LEU A CD2  
1677 N  N    . LYS A 212 ? 0.1201 0.1354 0.1075 -0.0360 0.0047  0.0312  213 LYS A N    
1678 C  CA   . LYS A 212 ? 0.1380 0.1436 0.1482 -0.0187 0.0028  0.0273  213 LYS A CA   
1679 C  C    . LYS A 212 ? 0.1318 0.1293 0.1459 -0.0012 -0.0085 0.0195  213 LYS A C    
1680 O  O    . LYS A 212 ? 0.1135 0.1499 0.1827 0.0024  -0.0181 0.0042  213 LYS A O    
1681 C  CB   . LYS A 212 ? 0.2053 0.1626 0.1668 -0.0364 0.0194  0.0324  213 LYS A CB   
1682 C  CG   . LYS A 212 ? 0.2468 0.2249 0.2364 -0.0394 -0.0049 0.0041  213 LYS A CG   
1683 C  CD   . LYS A 212 ? 0.2666 0.2960 0.2559 -0.0587 0.0343  -0.0015 213 LYS A CD   
1684 C  CE   . LYS A 212 ? 0.3625 0.3664 0.3261 -0.0276 -0.0192 0.0290  213 LYS A CE   
1685 N  NZ   . LYS A 212 ? 0.3151 0.3435 0.3163 -0.0139 -0.0083 -0.0030 213 LYS A NZ   
1686 N  N    . GLU A 213 ? 0.1100 0.0996 0.1317 -0.0058 -0.0027 0.0114  214 GLU A N    
1687 C  CA   . GLU A 213 ? 0.0856 0.1400 0.1346 -0.0273 0.0017  -0.0006 214 GLU A CA   
1688 C  C    . GLU A 213 ? 0.0974 0.0853 0.1020 -0.0156 -0.0039 0.0123  214 GLU A C    
1689 O  O    . GLU A 213 ? 0.1243 0.0969 0.1071 0.0061  -0.0116 0.0187  214 GLU A O    
1690 C  CB   . GLU A 213 ? 0.0720 0.1491 0.1371 -0.0386 -0.0077 0.0050  214 GLU A CB   
1691 C  CG   . GLU A 213 ? 0.0967 0.1978 0.2090 -0.0374 -0.0567 -0.0083 214 GLU A CG   
1692 C  CD   . GLU A 213 ? 0.1465 0.2420 0.2419 -0.0187 0.0078  -0.0392 214 GLU A CD   
1693 O  OE1  . GLU A 213 ? 0.1657 0.1570 0.2566 -0.0059 -0.0281 -0.0043 214 GLU A OE1  
1694 O  OE2  . GLU A 213 ? 0.2650 0.3956 0.3714 -0.0353 -0.0687 -0.0546 214 GLU A OE2  
1695 N  N    . PRO A 214 ? 0.1163 0.0774 0.1275 0.0041  -0.0014 0.0033  215 PRO A N    
1696 C  CA   . PRO A 214 ? 0.1251 0.0897 0.1413 0.0127  0.0042  -0.0177 215 PRO A CA   
1697 C  C    . PRO A 214 ? 0.1413 0.1161 0.1458 -0.0190 -0.0247 -0.0129 215 PRO A C    
1698 O  O    . PRO A 214 ? 0.1395 0.1763 0.1609 -0.0422 -0.0291 -0.0016 215 PRO A O    
1699 C  CB   . PRO A 214 ? 0.1323 0.0583 0.1646 0.0024  0.0064  -0.0113 215 PRO A CB   
1700 C  CG   . PRO A 214 ? 0.2157 0.1545 0.2424 0.0123  0.0346  0.0031  215 PRO A CG   
1701 C  CD   . PRO A 214 ? 0.1497 0.0654 0.1607 0.0091  0.0281  0.0115  215 PRO A CD   
1702 N  N    . ILE A 215 ? 0.1116 0.0984 0.1069 -0.0063 -0.0159 -0.0230 216 ILE A N    
1703 C  CA   . ILE A 215 ? 0.1422 0.0735 0.1229 -0.0070 -0.0296 -0.0080 216 ILE A CA   
1704 C  C    . ILE A 215 ? 0.1353 0.0960 0.1333 0.0057  -0.0375 0.0001  216 ILE A C    
1705 O  O    . ILE A 215 ? 0.1381 0.0967 0.1730 -0.0109 -0.0224 -0.0258 216 ILE A O    
1706 C  CB   . ILE A 215 ? 0.1204 0.1189 0.1581 0.0144  -0.0160 -0.0005 216 ILE A CB   
1707 C  CG1  . ILE A 215 ? 0.1571 0.1069 0.1263 -0.0332 0.0046  0.0023  216 ILE A CG1  
1708 C  CG2  . ILE A 215 ? 0.1175 0.1395 0.2069 0.0414  -0.0351 -0.0041 216 ILE A CG2  
1709 C  CD1  . ILE A 215 ? 0.1761 0.1139 0.1399 -0.0303 -0.0221 0.0200  216 ILE A CD1  
1710 N  N    A SER A 216 ? 0.1621 0.0934 0.1581 -0.0166 -0.0346 -0.0228 217 SER A N    
1711 N  N    B SER A 216 ? 0.1607 0.0898 0.1664 -0.0183 -0.0337 -0.0216 217 SER A N    
1712 C  CA   A SER A 216 ? 0.1489 0.1108 0.1547 -0.0192 -0.0339 -0.0212 217 SER A CA   
1713 C  CA   B SER A 216 ? 0.1424 0.1029 0.1667 -0.0281 -0.0350 -0.0173 217 SER A CA   
1714 C  C    A SER A 216 ? 0.1680 0.1015 0.1713 -0.0167 -0.0341 -0.0165 217 SER A C    
1715 C  C    B SER A 216 ? 0.1603 0.0864 0.1800 -0.0241 -0.0263 -0.0105 217 SER A C    
1716 O  O    A SER A 216 ? 0.1880 0.1205 0.1572 -0.0080 -0.0508 -0.0141 217 SER A O    
1717 O  O    B SER A 216 ? 0.1441 0.0977 0.1803 -0.0337 -0.0218 -0.0082 217 SER A O    
1718 C  CB   A SER A 216 ? 0.1481 0.1497 0.1837 -0.0188 -0.0163 0.0151  217 SER A CB   
1719 C  CB   B SER A 216 ? 0.1687 0.1268 0.2027 -0.0161 -0.0071 0.0162  217 SER A CB   
1720 O  OG   A SER A 216 ? 0.1981 0.1981 0.1476 -0.0344 0.0013  -0.0157 217 SER A OG   
1721 O  OG   B SER A 216 ? 0.1426 0.1919 0.1765 -0.0522 -0.0778 0.0043  217 SER A OG   
1722 N  N    . VAL A 217 ? 0.1548 0.0938 0.1537 -0.0262 -0.0331 -0.0104 218 VAL A N    
1723 C  CA   . VAL A 217 ? 0.1811 0.0966 0.1585 -0.0139 -0.0120 -0.0203 218 VAL A CA   
1724 C  C    . VAL A 217 ? 0.1851 0.1061 0.1578 -0.0202 -0.0373 -0.0208 218 VAL A C    
1725 O  O    . VAL A 217 ? 0.1973 0.1238 0.1460 0.0084  -0.0648 -0.0332 218 VAL A O    
1726 C  CB   . VAL A 217 ? 0.1565 0.1133 0.1625 -0.0053 -0.0425 -0.0055 218 VAL A CB   
1727 C  CG1  . VAL A 217 ? 0.2063 0.0913 0.1765 0.0273  -0.0568 -0.0281 218 VAL A CG1  
1728 C  CG2  . VAL A 217 ? 0.1766 0.0892 0.2100 -0.0168 -0.0413 -0.0597 218 VAL A CG2  
1729 N  N    . SER A 218 ? 0.1822 0.1029 0.1488 -0.0076 -0.0377 -0.0317 219 SER A N    
1730 C  CA   . SER A 218 ? 0.1844 0.0903 0.1461 -0.0008 -0.0257 -0.0362 219 SER A CA   
1731 C  C    . SER A 218 ? 0.1792 0.0863 0.1628 -0.0076 -0.0209 -0.0180 219 SER A C    
1732 O  O    . SER A 218 ? 0.1922 0.0832 0.1441 -0.0161 -0.0293 -0.0076 219 SER A O    
1733 C  CB   . SER A 218 ? 0.2354 0.0829 0.1361 -0.0272 -0.0392 -0.0288 219 SER A CB   
1734 O  OG   . SER A 218 ? 0.2304 0.1109 0.1855 -0.0447 -0.0295 -0.0275 219 SER A OG   
1735 N  N    . SER A 219 ? 0.2153 0.0842 0.1986 -0.0020 0.0061  -0.0146 220 SER A N    
1736 C  CA   . SER A 219 ? 0.2256 0.0755 0.2286 0.0009  -0.0097 -0.0104 220 SER A CA   
1737 C  C    . SER A 219 ? 0.2147 0.0952 0.2209 -0.0045 -0.0200 -0.0179 220 SER A C    
1738 O  O    . SER A 219 ? 0.2340 0.1148 0.2602 -0.0024 -0.0111 -0.0127 220 SER A O    
1739 C  CB   . SER A 219 ? 0.2642 0.0839 0.2700 -0.0137 -0.0223 -0.0116 220 SER A CB   
1740 O  OG   . SER A 219 ? 0.2943 0.1296 0.3145 0.0130  -0.0168 -0.0210 220 SER A OG   
1741 N  N    . GLU A 220 ? 0.2347 0.0981 0.1725 -0.0056 -0.0185 -0.0175 221 GLU A N    
1742 C  CA   . GLU A 220 ? 0.2492 0.0995 0.1731 -0.0131 -0.0207 -0.0176 221 GLU A CA   
1743 C  C    . GLU A 220 ? 0.2347 0.0981 0.1549 -0.0193 -0.0092 -0.0248 221 GLU A C    
1744 O  O    . GLU A 220 ? 0.2206 0.1323 0.1972 0.0000  0.0033  -0.0266 221 GLU A O    
1745 C  CB   . GLU A 220 ? 0.2821 0.1336 0.1836 -0.0320 -0.0236 -0.0560 221 GLU A CB   
1746 C  CG   . GLU A 220 ? 0.3397 0.1409 0.2284 -0.0315 -0.0190 -0.0364 221 GLU A CG   
1747 C  CD   . GLU A 220 ? 0.3928 0.1583 0.2910 -0.0376 0.0041  -0.0340 221 GLU A CD   
1748 O  OE1  . GLU A 220 ? 0.3164 0.2180 0.2276 -0.0653 -0.0121 -0.0339 221 GLU A OE1  
1749 O  OE2  . GLU A 220 ? 0.5184 0.2600 0.3986 -0.0748 -0.0106 -0.0855 221 GLU A OE2  
1750 N  N    . GLN A 221 ? 0.1834 0.0625 0.1623 -0.0056 -0.0117 -0.0098 222 GLN A N    
1751 C  CA   . GLN A 221 ? 0.1663 0.0835 0.1856 -0.0060 -0.0182 -0.0199 222 GLN A CA   
1752 C  C    . GLN A 221 ? 0.1822 0.0920 0.1719 -0.0104 -0.0210 0.0000  222 GLN A C    
1753 O  O    . GLN A 221 ? 0.2092 0.1461 0.1635 -0.0260 -0.0047 0.0287  222 GLN A O    
1754 C  CB   . GLN A 221 ? 0.1396 0.1108 0.2003 0.0060  -0.0225 -0.0388 222 GLN A CB   
1755 C  CG   . GLN A 221 ? 0.1560 0.1501 0.1634 -0.0117 -0.0258 0.0070  222 GLN A CG   
1756 C  CD   . GLN A 221 ? 0.1531 0.0835 0.1732 -0.0359 -0.0263 -0.0352 222 GLN A CD   
1757 O  OE1  . GLN A 221 ? 0.1969 0.1198 0.1315 0.0056  -0.0051 0.0020  222 GLN A OE1  
1758 N  NE2  . GLN A 221 ? 0.1770 0.0825 0.2017 -0.0346 -0.0582 0.0055  222 GLN A NE2  
1759 N  N    . VAL A 222 ? 0.1988 0.1174 0.1861 -0.0047 -0.0385 0.0189  223 VAL A N    
1760 C  CA   . VAL A 222 ? 0.2060 0.1564 0.1689 0.0190  -0.0369 0.0162  223 VAL A CA   
1761 C  C    . VAL A 222 ? 0.1992 0.1473 0.1957 0.0000  -0.0245 -0.0059 223 VAL A C    
1762 O  O    . VAL A 222 ? 0.2190 0.1348 0.1877 -0.0137 -0.0141 -0.0204 223 VAL A O    
1763 C  CB   . VAL A 222 ? 0.2165 0.1685 0.1721 0.0094  -0.0530 0.0236  223 VAL A CB   
1764 C  CG1  . VAL A 222 ? 0.2669 0.2001 0.2900 -0.0129 -0.0248 0.0226  223 VAL A CG1  
1765 C  CG2  . VAL A 222 ? 0.2133 0.1731 0.2039 -0.0213 -0.0616 0.0046  223 VAL A CG2  
1766 N  N    . LEU A 223 ? 0.2428 0.1176 0.1940 0.0163  -0.0075 -0.0155 224 LEU A N    
1767 C  CA   . LEU A 223 ? 0.2549 0.1819 0.2270 -0.0156 0.0052  -0.0089 224 LEU A CA   
1768 C  C    . LEU A 223 ? 0.2504 0.1894 0.1970 -0.0234 -0.0097 -0.0193 224 LEU A C    
1769 O  O    . LEU A 223 ? 0.2181 0.1999 0.2178 -0.0279 0.0038  -0.0092 224 LEU A O    
1770 C  CB   . LEU A 223 ? 0.3001 0.1906 0.2610 -0.0257 -0.0064 -0.0384 224 LEU A CB   
1771 C  CG   . LEU A 223 ? 0.3195 0.2693 0.3297 -0.0171 -0.0156 -0.0259 224 LEU A CG   
1772 C  CD1  . LEU A 223 ? 0.4061 0.3005 0.3994 -0.0172 -0.0384 -0.0376 224 LEU A CD1  
1773 C  CD2  . LEU A 223 ? 0.3366 0.3576 0.4478 -0.0219 -0.0138 -0.0459 224 LEU A CD2  
1774 N  N    . LYS A 224 ? 0.2550 0.1760 0.1848 -0.0327 -0.0022 -0.0185 225 LYS A N    
1775 C  CA   . LYS A 224 ? 0.2619 0.2172 0.2004 -0.0194 -0.0133 -0.0086 225 LYS A CA   
1776 C  C    . LYS A 224 ? 0.2306 0.1906 0.1519 -0.0185 0.0004  -0.0184 225 LYS A C    
1777 O  O    . LYS A 224 ? 0.2730 0.1793 0.1289 -0.0383 0.0046  -0.0409 225 LYS A O    
1778 C  CB   . LYS A 224 ? 0.2601 0.2415 0.1816 -0.0065 -0.0055 0.0111  225 LYS A CB   
1779 C  CG   . LYS A 224 ? 0.2895 0.2991 0.2891 -0.0308 -0.0073 -0.0004 225 LYS A CG   
1780 C  CD   . LYS A 224 ? 0.3257 0.3250 0.2933 -0.0114 -0.0411 -0.0095 225 LYS A CD   
1781 C  CE   . LYS A 224 ? 0.3990 0.3876 0.3112 -0.0192 -0.0638 -0.0220 225 LYS A CE   
1782 N  NZ   . LYS A 224 ? 0.3769 0.3856 0.4020 0.0296  -0.0156 0.0177  225 LYS A NZ   
1783 N  N    . PHE A 225 ? 0.1985 0.1475 0.1338 0.0000  -0.0041 -0.0139 226 PHE A N    
1784 C  CA   . PHE A 225 ? 0.1723 0.1325 0.1158 -0.0035 0.0115  -0.0251 226 PHE A CA   
1785 C  C    . PHE A 225 ? 0.1947 0.1275 0.1317 0.0003  0.0076  -0.0152 226 PHE A C    
1786 O  O    . PHE A 225 ? 0.2032 0.1418 0.1513 -0.0052 0.0218  -0.0308 226 PHE A O    
1787 C  CB   . PHE A 225 ? 0.1736 0.1398 0.1111 0.0003  0.0070  -0.0249 226 PHE A CB   
1788 C  CG   . PHE A 225 ? 0.1647 0.1151 0.1090 -0.0076 0.0018  -0.0231 226 PHE A CG   
1789 C  CD1  . PHE A 225 ? 0.1928 0.1832 0.1519 0.0205  -0.0103 -0.0284 226 PHE A CD1  
1790 C  CD2  . PHE A 225 ? 0.1356 0.1682 0.1436 -0.0140 0.0059  -0.0591 226 PHE A CD2  
1791 C  CE1  . PHE A 225 ? 0.2121 0.2145 0.1805 0.0085  0.0185  -0.0049 226 PHE A CE1  
1792 C  CE2  . PHE A 225 ? 0.1581 0.2301 0.1945 0.0209  -0.0005 -0.0758 226 PHE A CE2  
1793 C  CZ   . PHE A 225 ? 0.1576 0.1569 0.2139 0.0002  -0.0092 -0.0635 226 PHE A CZ   
1794 N  N    . ARG A 226 ? 0.2036 0.1176 0.1179 0.0055  0.0039  -0.0106 227 ARG A N    
1795 C  CA   . ARG A 226 ? 0.2117 0.1346 0.1311 0.0065  0.0267  0.0085  227 ARG A CA   
1796 C  C    . ARG A 226 ? 0.2099 0.1395 0.1388 0.0030  0.0243  -0.0134 227 ARG A C    
1797 O  O    . ARG A 226 ? 0.2182 0.1907 0.1656 -0.0005 0.0300  -0.0257 227 ARG A O    
1798 C  CB   . ARG A 226 ? 0.2408 0.1047 0.1466 0.0309  0.0348  0.0141  227 ARG A CB   
1799 C  CG   . ARG A 226 ? 0.2243 0.1362 0.1562 -0.0167 0.0156  0.0346  227 ARG A CG   
1800 C  CD   . ARG A 226 ? 0.2246 0.1347 0.1888 -0.0061 0.0192  0.0302  227 ARG A CD   
1801 N  NE   . ARG A 226 ? 0.2381 0.1275 0.1706 -0.0197 -0.0208 0.0128  227 ARG A NE   
1802 C  CZ   . ARG A 226 ? 0.2121 0.1491 0.1880 0.0021  -0.0242 -0.0211 227 ARG A CZ   
1803 N  NH1  . ARG A 226 ? 0.2358 0.1304 0.2550 -0.0400 -0.0511 -0.0526 227 ARG A NH1  
1804 N  NH2  . ARG A 226 ? 0.2354 0.1286 0.1748 -0.0577 -0.0100 -0.0165 227 ARG A NH2  
1805 N  N    . LYS A 227 ? 0.2211 0.1567 0.1275 -0.0162 0.0202  -0.0205 228 LYS A N    
1806 C  CA   . LYS A 227 ? 0.2530 0.1758 0.1557 -0.0222 0.0180  -0.0273 228 LYS A CA   
1807 C  C    . LYS A 227 ? 0.2273 0.1692 0.1360 -0.0266 0.0229  -0.0460 228 LYS A C    
1808 O  O    . LYS A 227 ? 0.2430 0.1639 0.1626 -0.0376 0.0440  -0.0416 228 LYS A O    
1809 C  CB   . LYS A 227 ? 0.2670 0.1969 0.1863 -0.0182 -0.0142 -0.0080 228 LYS A CB   
1810 C  CG   . LYS A 227 ? 0.3050 0.2477 0.2108 -0.0418 -0.0081 -0.0211 228 LYS A CG   
1811 C  CD   . LYS A 227 ? 0.3509 0.3268 0.2914 -0.0259 -0.0173 -0.0072 228 LYS A CD   
1812 C  CE   . LYS A 227 ? 0.4826 0.4749 0.4002 0.0084  0.0056  -0.0383 228 LYS A CE   
1813 N  NZ   . LYS A 227 ? 0.5210 0.5110 0.4680 -0.0063 -0.0384 -0.0149 228 LYS A NZ   
1814 N  N    . LEU A 228 ? 0.2622 0.1169 0.1435 -0.0181 0.0092  -0.0534 229 LEU A N    
1815 C  CA   . LEU A 228 ? 0.2377 0.1421 0.1438 -0.0249 0.0131  -0.0400 229 LEU A CA   
1816 C  C    . LEU A 228 ? 0.2460 0.1544 0.1644 -0.0189 0.0244  -0.0291 229 LEU A C    
1817 O  O    . LEU A 228 ? 0.2331 0.1189 0.1555 -0.0205 0.0270  -0.0220 229 LEU A O    
1818 C  CB   . LEU A 228 ? 0.2399 0.1488 0.1334 -0.0019 0.0303  -0.0359 229 LEU A CB   
1819 C  CG   . LEU A 228 ? 0.2328 0.1775 0.1273 -0.0070 0.0299  -0.0267 229 LEU A CG   
1820 C  CD1  . LEU A 228 ? 0.2589 0.1617 0.1103 -0.0198 0.0120  -0.0495 229 LEU A CD1  
1821 C  CD2  . LEU A 228 ? 0.2350 0.1671 0.1580 0.0065  0.0448  0.0383  229 LEU A CD2  
1822 N  N    . ASN A 229 ? 0.2705 0.1802 0.1523 -0.0232 0.0313  -0.0282 230 ASN A N    
1823 C  CA   . ASN A 229 ? 0.2645 0.1971 0.1315 -0.0368 0.0275  -0.0400 230 ASN A CA   
1824 C  C    . ASN A 229 ? 0.2657 0.1970 0.1559 -0.0314 0.0315  -0.0182 230 ASN A C    
1825 O  O    . ASN A 229 ? 0.2672 0.2028 0.1443 -0.0195 0.0451  0.0026  230 ASN A O    
1826 C  CB   . ASN A 229 ? 0.3041 0.2075 0.1081 -0.0052 0.0377  -0.0360 230 ASN A CB   
1827 C  CG   . ASN A 229 ? 0.2721 0.2741 0.1780 -0.0394 0.0133  -0.0547 230 ASN A CG   
1828 O  OD1  . ASN A 229 ? 0.3686 0.2986 0.1831 -0.0245 0.0559  -0.0684 230 ASN A OD1  
1829 N  ND2  . ASN A 229 ? 0.3118 0.2450 0.1824 -0.0269 0.0189  -0.0719 230 ASN A ND2  
1830 N  N    . PHE A 230 ? 0.2491 0.2157 0.1470 -0.0662 0.0396  -0.0130 231 PHE A N    
1831 C  CA   . PHE A 230 ? 0.2449 0.1904 0.1401 -0.0672 0.0331  0.0148  231 PHE A CA   
1832 C  C    . PHE A 230 ? 0.2688 0.2456 0.1861 -0.0531 0.0391  -0.0026 231 PHE A C    
1833 O  O    . PHE A 230 ? 0.2748 0.2363 0.1889 -0.0824 0.0422  0.0050  231 PHE A O    
1834 C  CB   . PHE A 230 ? 0.2600 0.1903 0.1358 -0.0350 0.0170  0.0041  231 PHE A CB   
1835 C  CG   . PHE A 230 ? 0.2247 0.1646 0.1324 -0.0140 0.0693  0.0130  231 PHE A CG   
1836 C  CD1  . PHE A 230 ? 0.1804 0.1670 0.1264 0.0101  0.0464  0.0059  231 PHE A CD1  
1837 C  CD2  . PHE A 230 ? 0.2121 0.1635 0.1550 0.0093  0.0362  0.0128  231 PHE A CD2  
1838 C  CE1  . PHE A 230 ? 0.2304 0.1626 0.1249 -0.0585 0.0053  0.0050  231 PHE A CE1  
1839 C  CE2  . PHE A 230 ? 0.2419 0.1731 0.1751 -0.0150 0.0286  -0.0079 231 PHE A CE2  
1840 C  CZ   . PHE A 230 ? 0.1816 0.1902 0.1371 -0.0076 -0.0102 -0.0099 231 PHE A CZ   
1841 N  N    . ASN A 231 ? 0.2486 0.2549 0.1448 -0.0579 0.0662  -0.0101 232 ASN A N    
1842 C  CA   . ASN A 231 ? 0.2792 0.2563 0.1883 -0.0328 0.0637  -0.0061 232 ASN A CA   
1843 C  C    . ASN A 231 ? 0.2540 0.2828 0.1953 -0.0251 0.0467  -0.0074 232 ASN A C    
1844 O  O    . ASN A 231 ? 0.2485 0.2678 0.1993 0.0116  0.0468  0.0000  232 ASN A O    
1845 C  CB   . ASN A 231 ? 0.2838 0.2828 0.2161 -0.0228 0.0720  -0.0188 232 ASN A CB   
1846 C  CG   . ASN A 231 ? 0.2535 0.2684 0.1711 -0.0156 0.0412  0.0113  232 ASN A CG   
1847 O  OD1  . ASN A 231 ? 0.3237 0.2997 0.1786 -0.0642 0.0487  -0.0267 232 ASN A OD1  
1848 N  ND2  . ASN A 231 ? 0.3164 0.3262 0.1516 0.0328  0.0450  -0.0136 232 ASN A ND2  
1849 N  N    . GLY A 232 ? 0.2784 0.2578 0.1968 -0.0322 0.0415  0.0094  233 GLY A N    
1850 C  CA   . GLY A 232 ? 0.2807 0.2888 0.2267 -0.0166 0.0260  0.0086  233 GLY A CA   
1851 C  C    . GLY A 232 ? 0.2903 0.2740 0.2228 -0.0103 0.0226  0.0130  233 GLY A C    
1852 O  O    . GLY A 232 ? 0.2643 0.2905 0.2393 -0.0169 0.0635  0.0009  233 GLY A O    
1853 N  N    . GLU A 233 ? 0.2702 0.3083 0.2264 -0.0091 0.0195  0.0050  234 GLU A N    
1854 C  CA   . GLU A 233 ? 0.2934 0.3145 0.2419 -0.0020 0.0183  0.0037  234 GLU A CA   
1855 C  C    . GLU A 233 ? 0.2937 0.3115 0.2173 -0.0051 0.0229  0.0157  234 GLU A C    
1856 O  O    . GLU A 233 ? 0.2977 0.3357 0.1684 -0.0098 0.0443  0.0298  234 GLU A O    
1857 C  CB   . GLU A 233 ? 0.2910 0.3101 0.2319 0.0083  0.0106  0.0072  234 GLU A CB   
1858 C  CG   . GLU A 233 ? 0.3100 0.3061 0.2430 -0.0290 0.0326  0.0352  234 GLU A CG   
1859 C  CD   . GLU A 233 ? 0.3653 0.3658 0.3097 0.0032  -0.0189 -0.0085 234 GLU A CD   
1860 O  OE1  . GLU A 233 ? 0.3719 0.3598 0.4135 -0.0150 0.0123  0.0111  234 GLU A OE1  
1861 O  OE2  . GLU A 233 ? 0.3666 0.4180 0.3984 -0.0499 -0.0548 -0.0428 234 GLU A OE2  
1862 N  N    . GLY A 234 ? 0.2795 0.3327 0.2262 0.0121  0.0512  0.0227  235 GLY A N    
1863 C  CA   . GLY A 234 ? 0.3191 0.3923 0.2948 0.0122  0.0298  0.0201  235 GLY A CA   
1864 C  C    . GLY A 234 ? 0.3420 0.4266 0.2988 0.0136  0.0264  0.0331  235 GLY A C    
1865 O  O    . GLY A 234 ? 0.3511 0.4403 0.2944 0.0229  0.0554  0.0407  235 GLY A O    
1866 N  N    . GLU A 235 ? 0.3427 0.4431 0.3134 0.0130  0.0446  0.0205  236 GLU A N    
1867 C  CA   . GLU A 235 ? 0.3535 0.4367 0.3145 0.0108  0.0344  0.0207  236 GLU A CA   
1868 C  C    . GLU A 235 ? 0.3421 0.4425 0.3161 0.0161  0.0381  0.0137  236 GLU A C    
1869 O  O    . GLU A 235 ? 0.3381 0.4384 0.2858 0.0166  0.0392  0.0355  236 GLU A O    
1870 C  CB   . GLU A 235 ? 0.3431 0.4389 0.3355 0.0135  0.0345  0.0036  236 GLU A CB   
1871 C  CG   . GLU A 235 ? 0.3825 0.4275 0.3392 -0.0072 0.0425  0.0226  236 GLU A CG   
1872 C  CD   . GLU A 235 ? 0.4440 0.4694 0.4025 -0.0026 0.0259  0.0042  236 GLU A CD   
1873 O  OE1  . GLU A 235 ? 0.4741 0.4995 0.5150 -0.0463 0.0617  0.0450  236 GLU A OE1  
1874 O  OE2  . GLU A 235 ? 0.5770 0.5278 0.5454 -0.0289 0.0395  0.0342  236 GLU A OE2  
1875 N  N    . PRO A 236 ? 0.3091 0.4214 0.2815 0.0204  0.0585  0.0216  237 PRO A N    
1876 C  CA   . PRO A 236 ? 0.2888 0.4212 0.2806 0.0103  0.0751  0.0171  237 PRO A CA   
1877 C  C    . PRO A 236 ? 0.2763 0.3839 0.2524 0.0112  0.0618  0.0191  237 PRO A C    
1878 O  O    . PRO A 236 ? 0.2631 0.4004 0.2207 0.0261  0.0386  0.0322  237 PRO A O    
1879 C  CB   . PRO A 236 ? 0.2790 0.4184 0.2824 0.0162  0.0814  0.0215  237 PRO A CB   
1880 C  CG   . PRO A 236 ? 0.3371 0.4308 0.3347 0.0072  0.0603  0.0375  237 PRO A CG   
1881 C  CD   . PRO A 236 ? 0.3419 0.4269 0.3091 0.0168  0.0428  0.0127  237 PRO A CD   
1882 N  N    . GLU A 237 ? 0.2726 0.3793 0.2744 0.0040  0.0478  0.0052  238 GLU A N    
1883 C  CA   . GLU A 237 ? 0.2853 0.3481 0.2442 0.0033  0.0439  -0.0122 238 GLU A CA   
1884 C  C    . GLU A 237 ? 0.2895 0.3204 0.2470 -0.0001 0.0384  -0.0135 238 GLU A C    
1885 O  O    . GLU A 237 ? 0.2870 0.2922 0.2037 0.0106  0.0218  -0.0067 238 GLU A O    
1886 C  CB   . GLU A 237 ? 0.2776 0.3568 0.2642 0.0094  0.0309  -0.0175 238 GLU A CB   
1887 C  CG   . GLU A 237 ? 0.2961 0.3750 0.2661 -0.0104 0.0224  -0.0271 238 GLU A CG   
1888 C  CD   . GLU A 237 ? 0.3285 0.3529 0.2814 -0.0026 0.0260  -0.0391 238 GLU A CD   
1889 O  OE1  . GLU A 237 ? 0.4607 0.4068 0.3966 -0.0042 -0.0190 -0.0683 238 GLU A OE1  
1890 O  OE2  . GLU A 237 ? 0.3564 0.2575 0.2502 -0.0181 0.0302  -0.0774 238 GLU A OE2  
1891 N  N    . GLU A 238 ? 0.2681 0.2803 0.1853 -0.0215 0.0301  -0.0384 239 GLU A N    
1892 C  CA   . GLU A 238 ? 0.2741 0.2942 0.2062 -0.0212 0.0500  -0.0317 239 GLU A CA   
1893 C  C    . GLU A 238 ? 0.2245 0.2164 0.1777 -0.0043 0.0583  -0.0396 239 GLU A C    
1894 O  O    . GLU A 238 ? 0.2739 0.1952 0.1924 -0.0164 0.0557  -0.0400 239 GLU A O    
1895 C  CB   . GLU A 238 ? 0.2424 0.2779 0.2325 -0.0516 0.0508  -0.0233 239 GLU A CB   
1896 C  CG   . GLU A 238 ? 0.2911 0.3725 0.2702 -0.0381 0.0212  -0.0153 239 GLU A CG   
1897 C  CD   . GLU A 238 ? 0.3620 0.4113 0.3427 -0.0353 0.0194  -0.0296 239 GLU A CD   
1898 O  OE1  . GLU A 238 ? 0.4465 0.4953 0.4325 -0.0031 0.0304  -0.0645 239 GLU A OE1  
1899 O  OE2  . GLU A 238 ? 0.4600 0.5696 0.4611 -0.0711 0.0438  0.0121  239 GLU A OE2  
1900 N  N    . LEU A 239 ? 0.2240 0.2440 0.1453 -0.0018 0.0572  -0.0370 240 LEU A N    
1901 C  CA   . LEU A 239 ? 0.1895 0.1769 0.1677 0.0074  0.0418  -0.0253 240 LEU A CA   
1902 C  C    . LEU A 239 ? 0.2048 0.1619 0.1534 0.0116  0.0324  -0.0144 240 LEU A C    
1903 O  O    . LEU A 239 ? 0.2158 0.2031 0.1485 0.0106  0.0429  -0.0297 240 LEU A O    
1904 C  CB   . LEU A 239 ? 0.2168 0.1651 0.1994 0.0163  0.0212  -0.0262 240 LEU A CB   
1905 C  CG   . LEU A 239 ? 0.2368 0.1968 0.1451 0.0250  0.0242  -0.0092 240 LEU A CG   
1906 C  CD1  . LEU A 239 ? 0.2672 0.2204 0.3140 0.0182  -0.0189 -0.0182 240 LEU A CD1  
1907 C  CD2  . LEU A 239 ? 0.2136 0.2086 0.1944 0.0608  0.0001  -0.0336 240 LEU A CD2  
1908 N  N    . MET A 240 ? 0.2113 0.1491 0.1210 0.0233  0.0405  -0.0208 241 MET A N    
1909 C  CA   . MET A 240 ? 0.2270 0.1228 0.1083 -0.0012 0.0422  -0.0242 241 MET A CA   
1910 C  C    . MET A 240 ? 0.2251 0.1743 0.1141 -0.0131 0.0278  -0.0237 241 MET A C    
1911 O  O    . MET A 240 ? 0.1984 0.1633 0.1110 -0.0103 0.0229  0.0016  241 MET A O    
1912 C  CB   . MET A 240 ? 0.2343 0.1686 0.1171 0.0090  0.0356  -0.0128 241 MET A CB   
1913 C  CG   . MET A 240 ? 0.2031 0.1375 0.1529 -0.0358 0.0346  -0.0354 241 MET A CG   
1914 S  SD   . MET A 240 ? 0.2716 0.1528 0.1703 -0.0281 0.0338  -0.0235 241 MET A SD   
1915 C  CE   . MET A 240 ? 0.3002 0.1177 0.1366 -0.0673 0.0687  0.0120  241 MET A CE   
1916 N  N    . VAL A 241 ? 0.2035 0.1347 0.1159 -0.0336 0.0234  -0.0036 242 VAL A N    
1917 C  CA   . VAL A 241 ? 0.1981 0.1158 0.0860 -0.0143 0.0056  -0.0190 242 VAL A CA   
1918 C  C    . VAL A 241 ? 0.1830 0.1298 0.1309 0.0000  0.0100  -0.0331 242 VAL A C    
1919 O  O    . VAL A 241 ? 0.1690 0.1401 0.1447 -0.0269 0.0136  -0.0338 242 VAL A O    
1920 C  CB   . VAL A 241 ? 0.1575 0.1244 0.1335 -0.0178 0.0061  -0.0384 242 VAL A CB   
1921 C  CG1  . VAL A 241 ? 0.1758 0.1815 0.0971 -0.0074 0.0010  -0.0393 242 VAL A CG1  
1922 C  CG2  . VAL A 241 ? 0.1835 0.1462 0.1546 -0.0005 0.0264  -0.0230 242 VAL A CG2  
1923 N  N    . ASP A 242 ? 0.1711 0.0963 0.0886 0.0004  0.0060  -0.0153 243 ASP A N    
1924 C  CA   . ASP A 242 ? 0.1393 0.0690 0.1256 0.0140  0.0136  -0.0276 243 ASP A CA   
1925 C  C    . ASP A 242 ? 0.1219 0.0710 0.1197 -0.0011 -0.0078 -0.0032 243 ASP A C    
1926 O  O    . ASP A 242 ? 0.1270 0.1080 0.1840 -0.0089 -0.0069 -0.0383 243 ASP A O    
1927 C  CB   . ASP A 242 ? 0.0961 0.0865 0.1507 0.0005  -0.0042 -0.0009 243 ASP A CB   
1928 C  CG   . ASP A 242 ? 0.1345 0.0956 0.1400 0.0224  0.0003  -0.0116 243 ASP A CG   
1929 O  OD1  . ASP A 242 ? 0.1255 0.1443 0.1775 0.0254  0.0017  -0.0525 243 ASP A OD1  
1930 O  OD2  . ASP A 242 ? 0.1694 0.1259 0.2182 0.0411  0.0339  -0.0444 243 ASP A OD2  
1931 N  N    . ASN A 243 ? 0.1442 0.0836 0.1125 0.0179  0.0063  -0.0270 244 ASN A N    
1932 C  CA   . ASN A 243 ? 0.1274 0.0807 0.0775 0.0155  0.0027  -0.0198 244 ASN A CA   
1933 C  C    . ASN A 243 ? 0.1128 0.0990 0.1057 -0.0194 0.0080  -0.0093 244 ASN A C    
1934 O  O    . ASN A 243 ? 0.1400 0.1178 0.1168 0.0248  0.0066  0.0001  244 ASN A O    
1935 C  CB   . ASN A 243 ? 0.1143 0.1420 0.0924 -0.0119 -0.0225 -0.0339 244 ASN A CB   
1936 C  CG   . ASN A 243 ? 0.1234 0.1697 0.1132 -0.0143 -0.0003 0.0010  244 ASN A CG   
1937 O  OD1  . ASN A 243 ? 0.1202 0.1306 0.1674 -0.0119 0.0010  0.0077  244 ASN A OD1  
1938 N  ND2  . ASN A 243 ? 0.2033 0.1752 0.1752 -0.0451 -0.0248 0.0608  244 ASN A ND2  
1939 N  N    . TRP A 244 ? 0.1281 0.0866 0.0706 -0.0109 0.0055  0.0082  245 TRP A N    
1940 C  CA   . TRP A 244 ? 0.1222 0.0784 0.0930 -0.0142 -0.0187 -0.0265 245 TRP A CA   
1941 C  C    . TRP A 244 ? 0.1099 0.0913 0.1138 -0.0126 -0.0132 0.0021  245 TRP A C    
1942 O  O    . TRP A 244 ? 0.1177 0.1128 0.1186 0.0092  -0.0268 -0.0270 245 TRP A O    
1943 C  CB   . TRP A 244 ? 0.1264 0.0652 0.1103 -0.0077 0.0041  -0.0098 245 TRP A CB   
1944 C  CG   . TRP A 244 ? 0.0992 0.0856 0.0824 -0.0064 -0.0198 -0.0054 245 TRP A CG   
1945 C  CD1  . TRP A 244 ? 0.1143 0.0711 0.1195 -0.0030 0.0174  -0.0187 245 TRP A CD1  
1946 C  CD2  . TRP A 244 ? 0.1310 0.0775 0.1054 -0.0090 -0.0113 0.0062  245 TRP A CD2  
1947 N  NE1  . TRP A 244 ? 0.1079 0.0597 0.1383 0.0222  -0.0144 0.0171  245 TRP A NE1  
1948 C  CE2  . TRP A 244 ? 0.1110 0.1051 0.1428 0.0038  -0.0129 -0.0034 245 TRP A CE2  
1949 C  CE3  . TRP A 244 ? 0.1659 0.1054 0.1276 -0.0032 -0.0068 0.0010  245 TRP A CE3  
1950 C  CZ2  . TRP A 244 ? 0.1489 0.0859 0.1264 -0.0106 -0.0272 -0.0230 245 TRP A CZ2  
1951 C  CZ3  . TRP A 244 ? 0.1564 0.0706 0.1649 0.0222  -0.0132 -0.0098 245 TRP A CZ3  
1952 C  CH2  . TRP A 244 ? 0.1802 0.0985 0.1289 0.0236  0.0002  0.0001  245 TRP A CH2  
1953 N  N    . ARG A 245 ? 0.1276 0.0930 0.1118 -0.0186 -0.0224 -0.0055 246 ARG A N    
1954 C  CA   . ARG A 245 ? 0.1131 0.0966 0.1149 -0.0297 -0.0216 -0.0143 246 ARG A CA   
1955 C  C    . ARG A 245 ? 0.1172 0.0799 0.1104 0.0030  -0.0177 -0.0106 246 ARG A C    
1956 O  O    . ARG A 245 ? 0.1187 0.0942 0.1298 0.0014  -0.0002 -0.0138 246 ARG A O    
1957 C  CB   . ARG A 245 ? 0.0761 0.0992 0.1264 -0.0374 -0.0154 -0.0407 246 ARG A CB   
1958 C  CG   . ARG A 245 ? 0.0705 0.0936 0.1208 -0.0331 -0.0279 -0.0381 246 ARG A CG   
1959 C  CD   . ARG A 245 ? 0.1245 0.0897 0.1054 -0.0313 -0.0224 -0.0402 246 ARG A CD   
1960 N  NE   . ARG A 245 ? 0.1426 0.1004 0.1447 -0.0125 -0.0273 -0.0454 246 ARG A NE   
1961 C  CZ   . ARG A 245 ? 0.0961 0.1301 0.1510 -0.0365 0.0122  -0.0327 246 ARG A CZ   
1962 N  NH1  . ARG A 245 ? 0.1034 0.1041 0.1453 0.0058  0.0086  -0.0239 246 ARG A NH1  
1963 N  NH2  . ARG A 245 ? 0.0913 0.1675 0.1388 -0.0380 -0.0070 -0.0171 246 ARG A NH2  
1964 N  N    . PRO A 246 ? 0.1302 0.1245 0.1340 0.0054  -0.0145 -0.0241 247 PRO A N    
1965 C  CA   . PRO A 246 ? 0.1092 0.1067 0.1198 0.0124  0.0039  -0.0103 247 PRO A CA   
1966 C  C    . PRO A 246 ? 0.1145 0.1093 0.1120 0.0205  0.0059  0.0084  247 PRO A C    
1967 O  O    . PRO A 246 ? 0.1420 0.0872 0.1433 -0.0061 0.0111  -0.0057 247 PRO A O    
1968 C  CB   . PRO A 246 ? 0.1559 0.1638 0.1372 0.0516  0.0134  -0.0167 247 PRO A CB   
1969 C  CG   . PRO A 246 ? 0.1523 0.1860 0.2295 0.0595  0.0063  0.0358  247 PRO A CG   
1970 C  CD   . PRO A 246 ? 0.0999 0.1253 0.1736 0.0141  -0.0085 0.0252  247 PRO A CD   
1971 N  N    . ALA A 247 ? 0.1325 0.1336 0.0901 0.0058  0.0192  0.0171  248 ALA A N    
1972 C  CA   . ALA A 247 ? 0.0985 0.1046 0.0878 -0.0037 0.0099  -0.0039 248 ALA A CA   
1973 C  C    . ALA A 247 ? 0.1192 0.1060 0.1102 0.0227  -0.0021 0.0037  248 ALA A C    
1974 O  O    . ALA A 247 ? 0.1575 0.1012 0.1524 0.0397  0.0065  -0.0264 248 ALA A O    
1975 C  CB   . ALA A 247 ? 0.1636 0.1175 0.1348 0.0005  0.0261  0.0341  248 ALA A CB   
1976 N  N    . GLN A 248 ? 0.1441 0.0907 0.1364 0.0194  -0.0265 -0.0025 249 GLN A N    
1977 C  CA   . GLN A 248 ? 0.1330 0.1247 0.1264 0.0277  -0.0418 0.0111  249 GLN A CA   
1978 C  C    . GLN A 248 ? 0.1280 0.1326 0.1310 0.0330  -0.0320 0.0097  249 GLN A C    
1979 O  O    . GLN A 248 ? 0.1123 0.1451 0.1349 0.0113  -0.0237 0.0089  249 GLN A O    
1980 C  CB   . GLN A 248 ? 0.1722 0.0804 0.1481 0.0333  -0.0285 0.0087  249 GLN A CB   
1981 C  CG   . GLN A 248 ? 0.1588 0.1150 0.1409 0.0200  -0.0074 0.0036  249 GLN A CG   
1982 C  CD   . GLN A 248 ? 0.1491 0.1431 0.1009 0.0077  0.0059  -0.0081 249 GLN A CD   
1983 O  OE1  . GLN A 248 ? 0.1327 0.2440 0.1800 -0.0352 -0.0130 -0.0179 249 GLN A OE1  
1984 N  NE2  . GLN A 248 ? 0.1495 0.1372 0.1529 0.0188  -0.0149 -0.0570 249 GLN A NE2  
1985 N  N    . PRO A 249 ? 0.1462 0.2084 0.1322 0.0265  -0.0233 0.0017  250 PRO A N    
1986 C  CA   . PRO A 249 ? 0.1394 0.2324 0.1447 0.0489  -0.0255 -0.0073 250 PRO A CA   
1987 C  C    . PRO A 249 ? 0.1454 0.1741 0.1184 0.0279  -0.0268 -0.0188 250 PRO A C    
1988 O  O    . PRO A 249 ? 0.1395 0.2036 0.1739 0.0336  -0.0052 -0.0011 250 PRO A O    
1989 C  CB   . PRO A 249 ? 0.1459 0.2692 0.1459 0.0572  -0.0434 -0.0242 250 PRO A CB   
1990 C  CG   . PRO A 249 ? 0.1849 0.3095 0.1484 0.0258  -0.0476 -0.0198 250 PRO A CG   
1991 C  CD   . PRO A 249 ? 0.1238 0.2500 0.1751 0.0347  -0.0621 -0.0084 250 PRO A CD   
1992 N  N    . LEU A 250 ? 0.1645 0.1658 0.1425 0.0333  -0.0106 -0.0064 251 LEU A N    
1993 C  CA   . LEU A 250 ? 0.1371 0.1727 0.1423 0.0202  -0.0062 0.0010  251 LEU A CA   
1994 C  C    . LEU A 250 ? 0.1618 0.1673 0.1509 0.0342  -0.0252 -0.0145 251 LEU A C    
1995 O  O    . LEU A 250 ? 0.1593 0.1501 0.1681 0.0469  -0.0388 0.0035  251 LEU A O    
1996 C  CB   . LEU A 250 ? 0.1702 0.1834 0.1523 0.0172  0.0009  0.0312  251 LEU A CB   
1997 C  CG   . LEU A 250 ? 0.1900 0.2077 0.1554 0.0058  0.0196  0.0011  251 LEU A CG   
1998 C  CD1  . LEU A 250 ? 0.1633 0.1887 0.1599 0.0137  -0.0181 -0.0420 251 LEU A CD1  
1999 C  CD2  . LEU A 250 ? 0.2165 0.1856 0.2371 0.0087  0.0295  0.0306  251 LEU A CD2  
2000 N  N    . LYS A 251 ? 0.1793 0.1726 0.1555 0.0372  -0.0473 -0.0209 252 LYS A N    
2001 C  CA   . LYS A 251 ? 0.1981 0.1880 0.1626 0.0230  -0.0223 -0.0168 252 LYS A CA   
2002 C  C    . LYS A 251 ? 0.1986 0.2122 0.1829 0.0222  -0.0340 -0.0179 252 LYS A C    
2003 O  O    . LYS A 251 ? 0.2384 0.2645 0.1896 0.0119  -0.0220 -0.0233 252 LYS A O    
2004 C  CB   . LYS A 251 ? 0.1925 0.1796 0.1969 -0.0076 -0.0353 -0.0405 252 LYS A CB   
2005 C  CG   . LYS A 251 ? 0.1944 0.1994 0.2422 -0.0123 0.0060  -0.0556 252 LYS A CG   
2006 C  CD   . LYS A 251 ? 0.2329 0.2724 0.2803 -0.0046 0.0072  -0.0143 252 LYS A CD   
2007 C  CE   . LYS A 251 ? 0.2894 0.2998 0.2904 0.0113  0.0295  -0.0166 252 LYS A CE   
2008 N  NZ   . LYS A 251 ? 0.2215 0.3127 0.3348 0.0291  0.0090  0.0361  252 LYS A NZ   
2009 N  N    . ASN A 252 ? 0.1916 0.2440 0.1687 0.0405  -0.0451 -0.0384 253 ASN A N    
2010 C  CA   . ASN A 252 ? 0.2360 0.3117 0.2608 0.0245  -0.0231 -0.0378 253 ASN A CA   
2011 C  C    . ASN A 252 ? 0.2335 0.2993 0.2659 0.0304  -0.0323 -0.0379 253 ASN A C    
2012 O  O    . ASN A 252 ? 0.2698 0.2927 0.3249 0.0385  -0.0330 -0.0582 253 ASN A O    
2013 C  CB   . ASN A 252 ? 0.2795 0.3313 0.2613 0.0130  -0.0245 -0.0555 253 ASN A CB   
2014 C  CG   . ASN A 252 ? 0.3562 0.4077 0.3284 0.0216  -0.0083 -0.0381 253 ASN A CG   
2015 O  OD1  . ASN A 252 ? 0.4683 0.4587 0.4408 -0.0092 0.0197  -0.0177 253 ASN A OD1  
2016 N  ND2  . ASN A 252 ? 0.4539 0.4232 0.4329 -0.0034 -0.0126 -0.0056 253 ASN A ND2  
2017 N  N    . ARG A 253 ? 0.1377 0.2568 0.1660 0.0243  -0.0222 -0.0238 254 ARG A N    
2018 C  CA   . ARG A 253 ? 0.1486 0.2181 0.1054 0.0409  -0.0020 -0.0237 254 ARG A CA   
2019 C  C    . ARG A 253 ? 0.2020 0.2297 0.1622 0.0219  -0.0024 -0.0195 254 ARG A C    
2020 O  O    . ARG A 253 ? 0.2327 0.2507 0.2405 0.0380  0.0157  -0.0015 254 ARG A O    
2021 C  CB   . ARG A 253 ? 0.1547 0.2278 0.0841 0.0212  -0.0043 -0.0027 254 ARG A CB   
2022 C  CG   . ARG A 253 ? 0.1645 0.1850 0.1042 0.0111  0.0003  -0.0243 254 ARG A CG   
2023 C  CD   . ARG A 253 ? 0.2134 0.1833 0.0670 0.0487  0.0047  -0.0418 254 ARG A CD   
2024 N  NE   . ARG A 253 ? 0.1469 0.1665 0.0701 0.0473  0.0205  -0.0246 254 ARG A NE   
2025 C  CZ   . ARG A 253 ? 0.0868 0.1185 0.0825 -0.0097 0.0157  -0.0221 254 ARG A CZ   
2026 N  NH1  . ARG A 253 ? 0.1262 0.1117 0.1180 0.0455  -0.0185 0.0035  254 ARG A NH1  
2027 N  NH2  . ARG A 253 ? 0.1215 0.1057 0.1154 0.0237  -0.0302 -0.0279 254 ARG A NH2  
2028 N  N    . GLN A 254 ? 0.1848 0.2612 0.1811 0.0143  -0.0089 -0.0352 255 GLN A N    
2029 C  CA   . GLN A 254 ? 0.2409 0.3027 0.1951 0.0023  -0.0223 -0.0340 255 GLN A CA   
2030 C  C    . GLN A 254 ? 0.2150 0.2438 0.1892 0.0000  -0.0410 -0.0193 255 GLN A C    
2031 O  O    . GLN A 254 ? 0.2402 0.2117 0.2611 -0.0020 -0.0822 -0.0543 255 GLN A O    
2032 C  CB   . GLN A 254 ? 0.2520 0.3259 0.2386 -0.0110 0.0069  -0.0340 255 GLN A CB   
2033 C  CG   . GLN A 254 ? 0.2945 0.3449 0.2674 0.0054  0.0291  -0.0145 255 GLN A CG   
2034 C  CD   . GLN A 254 ? 0.3342 0.3827 0.2939 0.0258  -0.0050 -0.0106 255 GLN A CD   
2035 O  OE1  . GLN A 254 ? 0.4958 0.4152 0.4189 0.0545  0.0388  -0.0699 255 GLN A OE1  
2036 N  NE2  . GLN A 254 ? 0.4449 0.4498 0.3771 0.0061  0.0030  0.0223  255 GLN A NE2  
2037 N  N    . ILE A 255 ? 0.1474 0.1847 0.1327 0.0161  -0.0041 -0.0333 256 ILE A N    
2038 C  CA   . ILE A 255 ? 0.1518 0.1757 0.1287 0.0154  0.0044  -0.0208 256 ILE A CA   
2039 C  C    . ILE A 255 ? 0.1392 0.1457 0.1302 0.0256  0.0205  0.0072  256 ILE A C    
2040 O  O    . ILE A 255 ? 0.2065 0.1571 0.1276 0.0247  0.0066  0.0221  256 ILE A O    
2041 C  CB   . ILE A 255 ? 0.1750 0.1683 0.1451 0.0348  0.0057  -0.0304 256 ILE A CB   
2042 C  CG1  . ILE A 255 ? 0.1572 0.1773 0.1852 0.0392  0.0222  -0.0452 256 ILE A CG1  
2043 C  CG2  . ILE A 255 ? 0.1457 0.1716 0.1559 0.0104  -0.0119 -0.0170 256 ILE A CG2  
2044 C  CD1  . ILE A 255 ? 0.2055 0.1602 0.1838 0.0072  -0.0105 -0.0587 256 ILE A CD1  
2045 N  N    . LYS A 256 ? 0.1340 0.1678 0.1298 0.0146  -0.0096 -0.0075 257 LYS A N    
2046 C  CA   . LYS A 256 ? 0.1479 0.1624 0.1384 0.0075  0.0050  -0.0214 257 LYS A CA   
2047 C  C    . LYS A 256 ? 0.0993 0.1406 0.1120 -0.0013 0.0091  0.0014  257 LYS A C    
2048 O  O    . LYS A 256 ? 0.1589 0.1743 0.0969 -0.0398 0.0197  0.0096  257 LYS A O    
2049 C  CB   . LYS A 256 ? 0.1824 0.1644 0.1613 0.0194  -0.0014 -0.0168 257 LYS A CB   
2050 C  CG   . LYS A 256 ? 0.2724 0.2591 0.2769 -0.0181 -0.0178 -0.0218 257 LYS A CG   
2051 C  CD   . LYS A 256 ? 0.4114 0.3739 0.3758 -0.0012 -0.0219 0.0110  257 LYS A CD   
2052 C  CE   . LYS A 256 ? 0.5320 0.4133 0.4886 0.0018  -0.0145 -0.0310 257 LYS A CE   
2053 N  NZ   . LYS A 256 ? 0.5092 0.4702 0.5570 0.0084  -0.0022 -0.0166 257 LYS A NZ   
2054 N  N    . ALA A 257 ? 0.1346 0.1788 0.1212 -0.0167 0.0153  0.0262  258 ALA A N    
2055 C  CA   . ALA A 257 ? 0.1483 0.1592 0.1538 -0.0082 0.0173  0.0237  258 ALA A CA   
2056 C  C    . ALA A 257 ? 0.1647 0.1653 0.1313 -0.0050 0.0141  0.0094  258 ALA A C    
2057 O  O    . ALA A 257 ? 0.1796 0.2071 0.1179 0.0328  0.0102  -0.0123 258 ALA A O    
2058 C  CB   . ALA A 257 ? 0.1931 0.1411 0.1710 -0.0160 0.0280  0.0356  258 ALA A CB   
2059 N  N    . SER A 258 ? 0.1204 0.1590 0.1319 0.0113  -0.0119 0.0000  259 SER A N    
2060 C  CA   . SER A 258 ? 0.1310 0.1894 0.1379 0.0058  -0.0028 -0.0077 259 SER A CA   
2061 C  C    . SER A 258 ? 0.1303 0.1998 0.1720 0.0133  0.0194  0.0135  259 SER A C    
2062 O  O    . SER A 258 ? 0.1534 0.2775 0.1931 0.0238  -0.0040 0.0100  259 SER A O    
2063 C  CB   . SER A 258 ? 0.1704 0.1581 0.1328 0.0015  -0.0036 -0.0043 259 SER A CB   
2064 O  OG   . SER A 258 ? 0.1554 0.2224 0.1279 -0.0052 0.0209  -0.0265 259 SER A OG   
2065 N  N    . PHE A 259 ? 0.1476 0.1778 0.1982 -0.0056 0.0287  0.0198  260 PHE A N    
2066 C  CA   . PHE A 259 ? 0.1820 0.2279 0.2416 -0.0095 0.0204  0.0305  260 PHE A CA   
2067 C  C    . PHE A 259 ? 0.2518 0.2651 0.2777 -0.0182 0.0095  0.0341  260 PHE A C    
2068 O  O    . PHE A 259 ? 0.2511 0.2412 0.2645 -0.0312 0.0111  0.0815  260 PHE A O    
2069 C  CB   . PHE A 259 ? 0.1847 0.2265 0.2563 -0.0098 0.0166  0.0119  260 PHE A CB   
2070 C  CG   . PHE A 259 ? 0.1832 0.2164 0.2227 0.0276  0.0076  0.0130  260 PHE A CG   
2071 C  CD1  . PHE A 259 ? 0.1546 0.2480 0.1889 0.0000  0.0229  -0.0136 260 PHE A CD1  
2072 C  CD2  . PHE A 259 ? 0.1919 0.2441 0.2822 0.0077  0.0024  0.0278  260 PHE A CD2  
2073 C  CE1  . PHE A 259 ? 0.1786 0.2302 0.1868 -0.0088 -0.0058 -0.0074 260 PHE A CE1  
2074 C  CE2  . PHE A 259 ? 0.2493 0.2402 0.2563 0.0093  0.0282  0.0026  260 PHE A CE2  
2075 C  CZ   . PHE A 259 ? 0.2326 0.2727 0.2783 0.0037  0.0008  -0.0062 260 PHE A CZ   
2076 N  N    . LYS A 260 ? 0.3574 0.3434 0.3572 -0.0219 0.0217  0.0388  261 LYS A N    
2077 C  CA   . LYS A 260 ? 0.4787 0.4289 0.4457 -0.0019 0.0189  0.0321  261 LYS A CA   
2078 C  C    . LYS A 260 ? 0.5136 0.4623 0.4820 0.0054  0.0080  0.0253  261 LYS A C    
2079 O  O    . LYS A 260 ? 0.5554 0.4765 0.5367 0.0183  0.0067  0.0337  261 LYS A O    
2080 C  CB   . LYS A 260 ? 0.4640 0.4212 0.4436 -0.0045 0.0265  0.0301  261 LYS A CB   
2081 C  CG   . LYS A 260 ? 0.5088 0.4312 0.4745 -0.0213 0.0197  0.0205  261 LYS A CG   
2082 C  CD   . LYS A 260 ? 0.5173 0.4794 0.4874 0.0000  0.0200  0.0137  261 LYS A CD   
2083 C  CE   . LYS A 260 ? 0.5477 0.5354 0.5488 0.0197  0.0294  0.0063  261 LYS A CE   
2084 N  NZ   . LYS A 260 ? 0.5456 0.5432 0.5609 0.0220  0.0191  -0.0080 261 LYS A NZ   
2085 O  OXT  . LYS A 260 ? 0.5533 0.4899 0.5257 0.0113  0.0211  0.0223  261 LYS A OXT  
2086 ZN ZN   . ZN  B .   ? 0.1257 0.0968 0.1014 -0.0095 -0.0108 -0.0041 262 ZN  A ZN   
2087 N  N1   . E02 C .   ? 0.5719 0.5953 0.5462 0.0034  0.0345  0.0011  263 E02 A N1   
2088 C  C2   . E02 C .   ? 0.5721 0.5852 0.5735 0.0053  -0.0035 -0.0004 263 E02 A C2   
2089 N  N3   . E02 C .   ? 0.5930 0.5849 0.5800 -0.0048 -0.0016 -0.0088 263 E02 A N3   
2090 C  C4   . E02 C .   ? 0.5679 0.6028 0.5945 0.0143  0.0123  -0.0036 263 E02 A C4   
2091 C  C5   . E02 C .   ? 0.5794 0.6112 0.5838 0.0131  0.0030  -0.0006 263 E02 A C5   
2092 C  C6   . E02 C .   ? 0.5734 0.5725 0.5612 0.0247  0.0172  0.0175  263 E02 A C6   
2093 C  C7   . E02 C .   ? 0.5676 0.5779 0.5799 0.0178  0.0095  0.0119  263 E02 A C7   
2094 C  C8   . E02 C .   ? 0.5739 0.5632 0.5442 0.0190  0.0105  0.0023  263 E02 A C8   
2095 C  C9   . E02 C .   ? 0.5516 0.5425 0.5758 0.0161  0.0055  0.0026  263 E02 A C9   
2096 C  C10  . E02 C .   ? 0.5459 0.4855 0.4677 0.0185  0.0191  0.0392  263 E02 A C10  
2097 C  C11  . E02 C .   ? 0.3185 0.2727 0.2776 0.0315  0.0615  -0.0159 263 E02 A C11  
2098 O  O12  . E02 C .   ? 0.3441 0.2871 0.2823 0.0345  0.0229  -0.0185 263 E02 A O12  
2099 C  C13  . E02 C .   ? 0.2600 0.2006 0.2121 -0.0182 0.0385  0.0090  263 E02 A C13  
2100 C  C14  . E02 C .   ? 0.1876 0.1298 0.1531 0.0038  -0.0192 0.0027  263 E02 A C14  
2101 C  C15  . E02 C .   ? 0.1151 0.1144 0.1358 -0.0053 -0.0008 0.0266  263 E02 A C15  
2102 C  C16  . E02 C .   ? 0.1510 0.1621 0.1975 0.0174  -0.0295 -0.0017 263 E02 A C16  
2103 C  C17  . E02 C .   ? 0.2533 0.1256 0.1973 -0.0114 0.0202  0.0116  263 E02 A C17  
2104 C  C18  . E02 C .   ? 0.2772 0.2008 0.2281 0.0262  0.0222  0.0295  263 E02 A C18  
2105 S  S19  . E02 C .   ? 0.1562 0.1217 0.1469 0.0026  -0.0087 -0.0024 263 E02 A S19  
2106 O  O20  . E02 C .   ? 0.1239 0.1433 0.1289 -0.0154 -0.0286 -0.0303 263 E02 A O20  
2107 CL CL21 . E02 C .   ? 0.1736 0.1297 0.2255 0.0018  -0.0087 -0.0219 263 E02 A CL21 
2108 O  O22  . E02 C .   ? 0.0936 0.1398 0.1372 0.0011  -0.0156 -0.0040 263 E02 A O22  
2109 N  N23  . E02 C .   ? 0.1382 0.1060 0.1277 0.0026  -0.0219 -0.0313 263 E02 A N23  
2110 O  O1   . MES D .   ? 0.4834 0.3930 0.3790 -0.0082 0.0388  -0.0204 264 MES A O1   
2111 C  C2   . MES D .   ? 0.4427 0.3265 0.3878 -0.0038 0.0163  -0.0075 264 MES A C2   
2112 C  C3   . MES D .   ? 0.4983 0.4315 0.4590 -0.0096 -0.0060 -0.0163 264 MES A C3   
2113 N  N4   . MES D .   ? 0.5374 0.4817 0.4600 -0.0166 0.0004  0.0031  264 MES A N4   
2114 C  C5   . MES D .   ? 0.4532 0.3435 0.4338 0.0074  0.0303  0.0013  264 MES A C5   
2115 C  C6   . MES D .   ? 0.4685 0.3256 0.2779 0.0158  -0.0342 -0.0356 264 MES A C6   
2116 C  C7   . MES D .   ? 0.6247 0.6029 0.6429 -0.0346 -0.0363 0.0166  264 MES A C7   
2117 C  C8   . MES D .   ? 0.7944 0.8260 0.7913 -0.0033 0.0158  -0.0151 264 MES A C8   
2118 S  S    . MES D .   ? 0.9187 0.9439 0.9004 -0.0009 -0.0013 0.0000  264 MES A S    
2119 O  O1S  . MES D .   ? 0.9655 0.9796 0.9439 -0.0084 0.0074  -0.0012 264 MES A O1S  
2120 O  O2S  . MES D .   ? 0.9334 0.9969 0.9367 0.0050  0.0166  -0.0117 264 MES A O2S  
2121 O  O3S  . MES D .   ? 0.9127 0.9176 0.8909 -0.0028 0.0163  -0.0041 264 MES A O3S  
2122 S  S    . DMS E .   ? 0.3027 0.4074 0.4276 -0.0377 0.0131  0.0121  265 DMS A S    
2123 O  O    . DMS E .   ? 0.3591 0.3474 0.4667 -0.0499 0.0023  0.0220  265 DMS A O    
2124 C  C1   . DMS E .   ? 0.2998 0.3350 0.3801 0.0096  0.0231  0.0106  265 DMS A C1   
2125 C  C2   . DMS E .   ? 0.3048 0.3541 0.3630 -0.0310 0.0110  -0.0150 265 DMS A C2   
2126 O  O    . HOH F .   ? 0.3293 0.3286 0.4198 0.0028  0.0491  -0.0525 126 HOH A O    
2127 O  O    . HOH F .   ? 0.0826 0.1290 0.1369 -0.0110 0.0136  -0.0082 266 HOH A O    
2128 O  O    . HOH F .   ? 0.1685 0.0886 0.1214 0.0259  -0.0017 -0.0115 267 HOH A O    
2129 O  O    . HOH F .   ? 0.1316 0.1096 0.1161 -0.0248 -0.0002 -0.0225 268 HOH A O    
2130 O  O    . HOH F .   ? 0.1082 0.1429 0.2366 0.0045  -0.0149 -0.0165 269 HOH A O    
2131 O  O    . HOH F .   ? 0.1041 0.1967 0.2012 -0.0004 0.0030  -0.0384 270 HOH A O    
2132 O  O    . HOH F .   ? 0.1866 0.1359 0.1183 -0.0255 0.0205  -0.0032 271 HOH A O    
2133 O  O    . HOH F .   ? 0.1605 0.1700 0.1624 -0.0086 -0.0491 0.0170  272 HOH A O    
2134 O  O    . HOH F .   ? 0.1550 0.1213 0.1617 0.0012  -0.0099 0.0262  273 HOH A O    
2135 O  O    . HOH F .   ? 0.1569 0.2495 0.2003 0.0062  -0.0801 0.0465  274 HOH A O    
2136 O  O    . HOH F .   ? 0.1335 0.1326 0.1592 0.0310  -0.0053 -0.0078 275 HOH A O    
2137 O  O    . HOH F .   ? 0.3811 0.1283 0.1709 -0.0297 -0.0773 -0.0062 276 HOH A O    
2138 O  O    . HOH F .   ? 0.2641 0.1281 0.2045 -0.0339 -0.0103 -0.0663 277 HOH A O    
2139 O  O    . HOH F .   ? 0.1606 0.0999 0.1428 0.0023  -0.0265 -0.0292 278 HOH A O    
2140 O  O    . HOH F .   ? 0.1880 0.1128 0.2455 0.0039  -0.0107 -0.0177 279 HOH A O    
2141 O  O    . HOH F .   ? 0.1321 0.1948 0.2750 -0.0260 -0.0182 -0.0025 280 HOH A O    
2142 O  O    . HOH F .   ? 0.2184 0.1379 0.1066 -0.0303 -0.0012 0.0220  281 HOH A O    
2143 O  O    . HOH F .   ? 0.2527 0.1710 0.2017 0.0191  0.0434  0.0738  282 HOH A O    
2144 O  O    . HOH F .   ? 0.3091 0.1430 0.1665 0.0130  -0.0863 0.0072  283 HOH A O    
2145 O  O    . HOH F .   ? 0.1159 0.1322 0.1711 0.0081  -0.0063 0.0295  284 HOH A O    
2146 O  O    . HOH F .   ? 0.2085 0.2250 0.3007 -0.0023 -0.1283 -0.0288 285 HOH A O    
2147 O  O    . HOH F .   ? 0.1909 0.1500 0.3505 -0.0652 -0.0475 -0.0149 286 HOH A O    
2148 O  O    . HOH F .   ? 0.2889 0.0724 0.1217 0.0031  -0.0654 -0.0002 287 HOH A O    
2149 O  O    . HOH F .   ? 0.3089 0.2491 0.1938 -0.0109 0.1067  -0.0768 288 HOH A O    
2150 O  O    . HOH F .   ? 0.2120 0.1650 0.2017 0.0069  -0.0714 0.0236  289 HOH A O    
2151 O  O    . HOH F .   ? 0.2988 0.1612 0.3049 -0.0198 -0.0177 -0.0534 290 HOH A O    
2152 O  O    . HOH F .   ? 0.2099 0.1867 0.1914 0.0340  -0.0094 0.0014  291 HOH A O    
2153 O  O    . HOH F .   ? 0.3310 0.1212 0.1896 -0.0517 -0.0125 0.0115  292 HOH A O    
2154 O  O    . HOH F .   ? 0.2406 0.2270 0.3225 0.0470  -0.1317 -0.0427 293 HOH A O    
2155 O  O    . HOH F .   ? 0.2040 0.2432 0.2945 0.0141  0.0222  -0.0434 294 HOH A O    
2156 O  O    . HOH F .   ? 0.2739 0.2047 0.2334 0.0324  -0.0092 -0.0016 295 HOH A O    
2157 O  O    . HOH F .   ? 0.3076 0.2565 0.3374 -0.0257 -0.0042 0.0275  296 HOH A O    
2158 O  O    . HOH F .   ? 0.1805 0.2015 0.3093 -0.0314 -0.0327 -0.0065 297 HOH A O    
2159 O  O    . HOH F .   ? 0.1946 0.3142 0.2900 0.0690  0.0008  0.1152  298 HOH A O    
2160 O  O    . HOH F .   ? 0.2929 0.2340 0.2012 0.0266  -0.0423 -0.0224 299 HOH A O    
2161 O  O    . HOH F .   ? 0.2177 0.1450 0.2299 -0.0334 -0.0374 -0.0156 300 HOH A O    
2162 O  O    . HOH F .   ? 0.1717 0.3621 0.3300 -0.0320 -0.0178 -0.0309 301 HOH A O    
2163 O  O    . HOH F .   ? 0.2077 0.1618 0.2582 0.0333  -0.0340 -0.0318 302 HOH A O    
2164 O  O    . HOH F .   ? 0.4834 0.2987 0.1912 0.0367  0.0421  0.0166  303 HOH A O    
2165 O  O    . HOH F .   ? 0.2727 0.2123 0.1970 0.0619  -0.1148 -0.0002 304 HOH A O    
2166 O  O    . HOH F .   ? 0.2491 0.2219 0.2385 0.0113  0.0133  -0.0330 305 HOH A O    
2167 O  O    . HOH F .   ? 0.4238 0.2011 0.2649 -0.0416 -0.0754 -0.0533 306 HOH A O    
2168 O  O    . HOH F .   ? 0.2130 0.3400 0.1384 0.0471  0.0094  0.0102  307 HOH A O    
2169 O  O    . HOH F .   ? 0.2827 0.1965 0.2254 -0.0319 -0.0298 0.0377  308 HOH A O    
2170 O  O    . HOH F .   ? 0.3025 0.1053 0.2655 0.0502  0.0010  0.0062  309 HOH A O    
2171 O  O    . HOH F .   ? 0.3416 0.1836 0.2396 0.0135  -0.0565 0.0208  310 HOH A O    
2172 O  O    . HOH F .   ? 0.3100 0.3866 0.3074 -0.0605 -0.0922 0.0943  311 HOH A O    
2173 O  O    . HOH F .   ? 0.3176 0.3972 0.2478 -0.0081 0.0358  0.0795  312 HOH A O    
2174 O  O    . HOH F .   ? 0.2135 0.1902 0.2984 -0.0862 -0.0469 -0.0426 313 HOH A O    
2175 O  O    . HOH F .   ? 0.3987 0.2835 0.2300 -0.1172 -0.0435 -0.0401 314 HOH A O    
2176 O  O    . HOH F .   ? 0.3719 0.5502 0.3209 0.0582  -0.0759 0.0178  315 HOH A O    
2177 O  O    . HOH F .   ? 0.3184 0.1933 0.3062 0.1171  -0.0366 0.0262  316 HOH A O    
2178 O  O    . HOH F .   ? 0.4827 0.2862 0.1488 0.0151  -0.0026 -0.0372 317 HOH A O    
2179 O  O    . HOH F .   ? 0.3707 0.2835 0.3384 0.0693  0.0207  0.1037  318 HOH A O    
2180 O  O    . HOH F .   ? 0.3073 0.2741 0.2003 0.0339  -0.0395 0.0437  319 HOH A O    
2181 O  O    . HOH F .   ? 0.2989 0.2505 0.2117 -0.0209 0.0057  -0.0288 320 HOH A O    
2182 O  O    . HOH F .   ? 0.3878 0.1870 0.1628 -0.0072 -0.0336 0.0651  321 HOH A O    
2183 O  O    . HOH F .   ? 0.2341 0.3448 0.4059 -0.0270 -0.0117 0.0391  322 HOH A O    
2184 O  O    . HOH F .   ? 0.2611 0.3451 0.3876 -0.0056 0.0755  0.0425  323 HOH A O    
2185 O  O    . HOH F .   ? 0.3355 0.3359 0.2042 0.0874  -0.0913 -0.0196 324 HOH A O    
2186 O  O    . HOH F .   ? 0.2303 0.2931 0.3537 0.0142  0.0290  -0.0059 325 HOH A O    
2187 O  O    . HOH F .   ? 0.2348 0.3144 0.2320 0.0650  -0.0578 0.0031  326 HOH A O    
2188 O  O    . HOH F .   ? 0.3733 0.2808 0.1692 -0.0313 0.0518  0.0086  327 HOH A O    
2189 O  O    . HOH F .   ? 0.2416 0.2140 0.2035 -0.0274 -0.0089 0.0323  328 HOH A O    
2190 O  O    . HOH F .   ? 0.4132 0.2215 0.5341 0.0002  0.0263  0.0209  329 HOH A O    
2191 O  O    . HOH F .   ? 0.2618 0.2331 0.3103 -0.0068 0.0020  0.0199  330 HOH A O    
2192 O  O    . HOH F .   ? 0.3473 0.2025 0.2554 -0.0620 -0.0205 0.0278  331 HOH A O    
2193 O  O    . HOH F .   ? 0.3396 0.2662 0.1782 -0.0418 -0.1085 0.0108  332 HOH A O    
2194 O  O    . HOH F .   ? 0.2818 0.2655 0.3777 0.0711  -0.1338 -0.0474 333 HOH A O    
2195 O  O    . HOH F .   ? 0.3944 0.3323 0.3135 0.0095  0.0425  0.0239  334 HOH A O    
2196 O  O    . HOH F .   ? 0.2927 0.2349 0.3337 0.0392  -0.0846 -0.0375 335 HOH A O    
2197 O  O    . HOH F .   ? 0.2617 0.1406 0.3577 0.0074  0.0488  -0.0396 336 HOH A O    
2198 O  O    . HOH F .   ? 0.1992 0.3244 0.3914 -0.0005 -0.0153 0.0209  337 HOH A O    
2199 O  O    . HOH F .   ? 0.2906 0.3362 0.2994 0.0066  0.0534  0.0078  338 HOH A O    
2200 O  O    . HOH F .   ? 0.3232 0.2850 0.2463 0.0086  -0.0055 0.0397  339 HOH A O    
2201 O  O    . HOH F .   ? 0.4280 0.2772 0.3122 -0.0089 -0.0104 -0.1349 340 HOH A O    
2202 O  O    . HOH F .   ? 0.2834 0.2724 0.3741 0.0047  -0.0581 -0.0175 341 HOH A O    
2203 O  O    . HOH F .   ? 0.3099 0.3517 0.2949 -0.0111 -0.0706 0.0451  342 HOH A O    
2204 O  O    . HOH F .   ? 0.3162 0.2985 0.2577 -0.0164 0.0071  0.0200  343 HOH A O    
2205 O  O    . HOH F .   ? 0.4053 0.3004 0.2623 -0.0601 0.0636  -0.0782 344 HOH A O    
2206 O  O    . HOH F .   ? 0.3619 0.3440 0.2282 -0.1423 -0.1125 -0.0249 345 HOH A O    
2207 O  O    . HOH F .   ? 0.2593 0.4665 0.2895 0.0583  0.0017  0.0254  346 HOH A O    
2208 O  O    . HOH F .   ? 0.2278 0.2210 0.2788 -0.0319 0.0090  0.0011  347 HOH A O    
2209 O  O    . HOH F .   ? 0.3321 0.2830 0.4427 0.0448  -0.0785 0.0176  348 HOH A O    
2210 O  O    . HOH F .   ? 0.1602 0.2907 0.3797 0.0431  0.0132  -0.0168 349 HOH A O    
2211 O  O    . HOH F .   ? 0.3924 0.2834 0.4228 0.0063  0.0206  0.1309  350 HOH A O    
2212 O  O    . HOH F .   ? 0.4095 0.1706 0.2941 0.0382  -0.0016 0.0854  351 HOH A O    
2213 O  O    . HOH F .   ? 0.3102 0.3255 0.2513 0.0039  0.0642  -0.0804 352 HOH A O    
2214 O  O    . HOH F .   ? 0.4058 0.3556 0.4343 -0.0654 -0.0396 -0.0958 353 HOH A O    
2215 O  O    . HOH F .   ? 0.4384 0.2286 0.4329 -0.0126 -0.0604 -0.0373 354 HOH A O    
2216 O  O    . HOH F .   ? 0.2619 0.3057 0.5561 0.0272  -0.0656 -0.0343 355 HOH A O    
2217 O  O    . HOH F .   ? 0.2246 0.3596 0.2455 -0.0381 -0.0363 -0.0574 356 HOH A O    
2218 O  O    . HOH F .   ? 0.3136 0.2766 0.3419 -0.0288 0.0382  0.0183  357 HOH A O    
2219 O  O    . HOH F .   ? 0.3588 0.2814 0.2825 0.0613  -0.0962 -0.0055 358 HOH A O    
2220 O  O    . HOH F .   ? 0.4199 0.4381 0.3543 -0.0391 -0.0183 0.0203  359 HOH A O    
2221 O  O    . HOH F .   ? 0.2973 0.3317 0.3611 0.0342  -0.0716 0.0619  360 HOH A O    
2222 O  O    . HOH F .   ? 0.3640 0.3923 0.2350 0.0264  -0.1198 0.0704  361 HOH A O    
2223 O  O    . HOH F .   ? 0.3352 0.2411 0.3957 -0.0142 -0.0086 -0.0210 362 HOH A O    
2224 O  O    . HOH F .   ? 0.3704 0.1761 0.3511 -0.0027 -0.0816 -0.0355 363 HOH A O    
2225 O  O    . HOH F .   ? 0.3933 0.2186 0.3755 0.0428  -0.0402 -0.0447 364 HOH A O    
2226 O  O    . HOH F .   ? 0.3665 0.3508 0.2483 0.0298  -0.0809 0.0040  365 HOH A O    
2227 O  O    . HOH F .   ? 0.3201 0.3089 0.2722 -0.0056 -0.0383 0.0037  366 HOH A O    
2228 O  O    . HOH F .   ? 0.5334 0.3441 0.2510 -0.0055 0.0073  0.0558  367 HOH A O    
2229 O  O    . HOH F .   ? 0.3793 0.2665 0.3917 0.0832  0.0760  0.0790  368 HOH A O    
2230 O  O    . HOH F .   ? 0.3390 0.3224 0.4059 -0.0539 -0.0224 0.0079  369 HOH A O    
2231 O  O    . HOH F .   ? 0.2851 0.3195 0.4518 -0.0433 0.0278  -0.0435 370 HOH A O    
2232 O  O    . HOH F .   ? 0.2902 0.2654 0.3560 -0.0181 -0.0585 -0.1406 371 HOH A O    
2233 O  O    . HOH F .   ? 0.3782 0.4118 0.5010 0.0304  0.0645  -0.0496 372 HOH A O    
2234 O  O    . HOH F .   ? 0.2190 0.3229 0.3767 0.0299  -0.0396 -0.0126 373 HOH A O    
2235 O  O    . HOH F .   ? 0.3767 0.3319 0.2661 0.0145  0.0267  -0.0741 374 HOH A O    
2236 O  O    . HOH F .   ? 0.2771 0.2186 0.3411 0.0188  -0.0702 0.0511  375 HOH A O    
2237 O  O    . HOH F .   ? 0.3248 0.2695 0.3854 -0.0226 0.0363  0.0255  376 HOH A O    
2238 O  O    . HOH F .   ? 0.4779 0.2023 0.2954 0.0499  -0.0228 0.0829  377 HOH A O    
2239 O  O    . HOH F .   ? 0.2774 0.2361 0.4494 0.0955  -0.0056 -0.0158 378 HOH A O    
2240 O  O    . HOH F .   ? 0.2616 0.3314 0.4424 0.0586  0.0510  0.0572  379 HOH A O    
2241 O  O    . HOH F .   ? 0.3808 0.3050 0.3603 0.0955  0.0268  0.0475  380 HOH A O    
2242 O  O    . HOH F .   ? 0.4281 0.1983 0.3258 0.0057  -0.0500 -0.0391 381 HOH A O    
2243 O  O    . HOH F .   ? 0.4286 0.3149 0.1707 0.1457  -0.0099 0.0520  382 HOH A O    
2244 O  O    . HOH F .   ? 0.3864 0.2456 0.3071 -0.0276 -0.0371 -0.0482 383 HOH A O    
2245 O  O    . HOH F .   ? 0.3776 0.3158 0.4298 -0.0314 -0.0543 0.0471  384 HOH A O    
2246 O  O    . HOH F .   ? 0.4827 0.3058 0.4786 0.0640  -0.0029 -0.0015 385 HOH A O    
2247 O  O    . HOH F .   ? 0.3466 0.2727 0.3798 0.0064  -0.0418 0.0856  386 HOH A O    
2248 O  O    . HOH F .   ? 0.4777 0.4499 0.2376 0.0422  0.0582  0.0327  387 HOH A O    
2249 O  O    . HOH F .   ? 0.4253 0.2598 0.3960 0.0447  -0.0352 0.0786  388 HOH A O    
2250 O  O    . HOH F .   ? 0.4480 0.4099 0.2409 -0.0270 0.0693  0.1238  389 HOH A O    
2251 O  O    . HOH F .   ? 0.3459 0.2762 0.3219 -0.0050 0.0436  -0.0178 390 HOH A O    
2252 O  O    . HOH F .   ? 0.4221 0.3118 0.4103 -0.0051 -0.0457 0.0273  391 HOH A O    
2253 O  O    . HOH F .   ? 0.2639 0.3307 0.4834 -0.0513 -0.0177 -0.0762 392 HOH A O    
2254 O  O    . HOH F .   ? 0.3549 0.2769 0.5043 0.0232  -0.0273 -0.1343 393 HOH A O    
2255 O  O    . HOH F .   ? 0.3430 0.2575 0.3226 0.0301  -0.0165 -0.0132 394 HOH A O    
2256 O  O    . HOH F .   ? 0.4280 0.4039 0.2089 -0.0611 0.1305  -0.1084 395 HOH A O    
2257 O  O    . HOH F .   ? 0.3589 0.3372 0.3617 -0.0352 0.0282  0.0692  396 HOH A O    
2258 O  O    . HOH F .   ? 0.4106 0.4396 0.3535 0.0107  -0.0080 0.0925  397 HOH A O    
2259 O  O    . HOH F .   ? 0.3466 0.2309 0.4447 0.0298  0.0625  -0.0584 398 HOH A O    
2260 O  O    . HOH F .   ? 0.3412 0.4526 0.3872 -0.0083 -0.0261 -0.0027 399 HOH A O    
2261 O  O    . HOH F .   ? 0.3281 0.2196 0.3988 -0.0314 0.0261  -0.0298 400 HOH A O    
2262 O  O    . HOH F .   ? 0.3053 0.3591 0.3295 0.0535  0.0208  -0.0249 401 HOH A O    
2263 O  O    . HOH F .   ? 0.3751 0.3781 0.3891 -0.0447 0.0615  0.0186  402 HOH A O    
2264 O  O    . HOH F .   ? 0.2958 0.3355 0.4378 -0.0766 -0.0040 -0.0241 403 HOH A O    
2265 O  O    . HOH F .   ? 0.3839 0.3178 0.3865 0.0293  -0.1342 0.1513  404 HOH A O    
2266 O  O    . HOH F .   ? 0.3396 0.2985 0.4024 0.0186  -0.0420 0.0124  405 HOH A O    
2267 O  O    . HOH F .   ? 0.2543 0.2775 0.3939 0.0860  0.0526  0.0545  406 HOH A O    
2268 O  O    . HOH F .   ? 0.3272 0.2925 0.3520 -0.0900 -0.0376 0.0177  407 HOH A O    
2269 O  O    . HOH F .   ? 0.4163 0.3262 0.3857 -0.0173 0.0420  -0.1386 408 HOH A O    
2270 O  O    . HOH F .   ? 0.4772 0.4824 0.3568 -0.0515 -0.0788 -0.0187 409 HOH A O    
2271 O  O    . HOH F .   ? 0.5218 0.2891 0.3016 0.0018  -0.0315 -0.0826 410 HOH A O    
2272 O  O    . HOH F .   ? 0.3581 0.3063 0.2857 -0.0033 0.0167  0.0550  411 HOH A O    
2273 O  O    . HOH F .   ? 0.4063 0.4157 0.3564 -0.0179 -0.0391 0.0149  412 HOH A O    
2274 O  O    . HOH F .   ? 0.3537 0.3956 0.4816 0.0080  -0.1002 0.0853  413 HOH A O    
2275 O  O    . HOH F .   ? 0.1576 0.4348 0.4915 -0.0816 -0.0635 0.1012  414 HOH A O    
2276 O  O    . HOH F .   ? 0.4327 0.4648 0.4883 0.0148  0.0617  -0.0196 415 HOH A O    
2277 O  O    . HOH F .   ? 0.3893 0.2754 0.4875 -0.0825 0.0638  -0.0379 416 HOH A O    
2278 O  O    . HOH F .   ? 0.5297 0.5509 0.4282 -0.0195 0.0483  0.0547  417 HOH A O    
2279 O  O    . HOH F .   ? 0.3061 0.3453 0.4370 -0.0015 -0.0741 -0.0055 418 HOH A O    
2280 O  O    . HOH F .   ? 0.4334 0.3893 0.4515 0.0428  0.0305  0.0198  419 HOH A O    
2281 O  O    . HOH F .   ? 0.4165 0.3188 0.4072 -0.0036 -0.0351 -0.0477 420 HOH A O    
2282 O  O    . HOH F .   ? 0.2687 0.4518 0.3780 0.0207  0.0367  -0.0054 421 HOH A O    
2283 O  O    . HOH F .   ? 0.3423 0.3006 0.4995 -0.0764 -0.0470 0.0609  422 HOH A O    
2284 O  O    . HOH F .   ? 0.4494 0.3510 0.4237 -0.0371 -0.0606 -0.0235 423 HOH A O    
2285 O  O    . HOH F .   ? 0.4257 0.3425 0.4191 -0.0225 -0.0219 -0.0459 424 HOH A O    
2286 O  O    . HOH F .   ? 0.3911 0.2545 0.3268 0.0092  -0.0112 -0.0112 425 HOH A O    
2287 O  O    . HOH F .   ? 0.4621 0.3795 0.3381 -0.0005 -0.0008 0.1208  426 HOH A O    
2288 O  O    . HOH F .   ? 0.5127 0.3074 0.4488 -0.0017 -0.0103 -0.0942 427 HOH A O    
2289 O  O    . HOH F .   ? 0.3600 0.2937 0.3833 0.0667  -0.0498 0.0066  428 HOH A O    
2290 O  O    . HOH F .   ? 0.3380 0.4218 0.5265 0.1251  0.0043  0.0189  429 HOH A O    
2291 O  O    . HOH F .   ? 0.5041 0.4685 0.4712 -0.0639 0.0234  0.0722  430 HOH A O    
2292 O  O    . HOH F .   ? 0.3870 0.3850 0.3272 0.0022  -0.0897 -0.0047 431 HOH A O    
2293 O  O    . HOH F .   ? 0.3080 0.3227 0.3362 0.0263  0.0123  -0.0049 432 HOH A O    
2294 O  O    . HOH F .   ? 0.3433 0.2727 0.2739 -0.0026 -0.0503 -0.0119 433 HOH A O    
2295 O  O    . HOH F .   ? 0.2786 0.3759 0.4400 -0.0055 0.0619  -0.0099 434 HOH A O    
2296 O  O    . HOH F .   ? 0.2498 0.5397 0.3983 -0.0689 -0.0819 -0.0736 435 HOH A O    
2297 O  O    . HOH F .   ? 0.4111 0.2354 0.5596 0.0425  -0.1307 -0.0054 436 HOH A O    
2298 O  O    . HOH F .   ? 0.4133 0.2723 0.5332 0.1562  -0.0789 -0.0488 437 HOH A O    
2299 O  O    . HOH F .   ? 0.3986 0.3066 0.4296 0.0480  -0.0158 -0.0235 438 HOH A O    
2300 O  O    . HOH F .   ? 0.5124 0.2708 0.4081 -0.0185 -0.0150 -0.0654 439 HOH A O    
2301 O  O    . HOH F .   ? 0.1700 0.5068 0.3305 0.0422  -0.0013 -0.1081 440 HOH A O    
2302 O  O    . HOH F .   ? 0.3855 0.4036 0.2895 0.0362  0.0267  0.0508  441 HOH A O    
2303 O  O    . HOH F .   ? 0.3694 0.3715 0.5550 -0.0059 -0.0954 -0.0505 442 HOH A O    
2304 O  O    . HOH F .   ? 0.2898 0.4760 0.4381 -0.1917 -0.0035 -0.0118 443 HOH A O    
2305 O  O    . HOH F .   ? 0.2956 0.3625 0.3524 0.0296  0.0687  0.0183  444 HOH A O    
2306 O  O    . HOH F .   ? 0.3953 0.3900 0.4858 0.1203  0.0162  0.0757  445 HOH A O    
2307 O  O    . HOH F .   ? 0.3465 0.4027 0.3698 0.0622  0.0060  -0.0223 446 HOH A O    
2308 O  O    . HOH F .   ? 0.3459 0.4096 0.4532 -0.0229 -0.0006 0.0374  447 HOH A O    
2309 O  O    . HOH F .   ? 0.4139 0.4709 0.4235 -0.0484 -0.0025 0.0219  448 HOH A O    
2310 O  O    . HOH F .   ? 0.3504 0.3926 0.4762 0.0603  0.0448  0.0163  449 HOH A O    
2311 O  O    . HOH F .   ? 0.4355 0.2650 0.5120 0.0195  -0.0636 -0.0081 450 HOH A O    
2312 O  O    . HOH F .   ? 0.4431 0.4253 0.3701 -0.0844 0.0525  -0.0557 451 HOH A O    
2313 O  O    . HOH F .   ? 0.4844 0.4898 0.2454 -0.0385 0.0298  0.0841  452 HOH A O    
2314 O  O    . HOH F .   ? 0.4819 0.4270 0.3936 -0.1069 -0.1301 -0.0867 453 HOH A O    
2315 O  O    . HOH F .   ? 0.4214 0.4684 0.4884 0.0248  -0.0254 -0.0680 454 HOH A O    
2316 O  O    . HOH F .   ? 0.5104 0.3982 0.3015 0.0781  0.0477  -0.1581 455 HOH A O    
2317 O  O    . HOH F .   ? 0.3114 0.4168 0.4238 0.0305  -0.0809 0.0539  456 HOH A O    
2318 O  O    . HOH F .   ? 0.3198 0.4348 0.4111 0.0365  -0.0185 0.0608  457 HOH A O    
2319 O  O    . HOH F .   ? 0.3314 0.5646 0.3632 -0.0361 0.0240  0.0458  458 HOH A O    
2320 O  O    . HOH F .   ? 0.5340 0.4054 0.3573 0.0027  0.0263  -0.0499 459 HOH A O    
2321 O  O    . HOH F .   ? 0.5610 0.4747 0.4700 0.0261  0.0258  0.0039  460 HOH A O    
2322 O  O    . HOH F .   ? 0.5521 0.6285 0.6047 -0.0039 0.0168  -0.0129 461 HOH A O    
2323 O  O    . HOH F .   ? 0.3661 0.3560 0.4462 0.0203  -0.0030 0.0178  462 HOH A O    
2324 O  O    . HOH F .   ? 0.4435 0.4992 0.2860 0.0397  -0.0349 0.0057  463 HOH A O    
2325 O  O    . HOH F .   ? 0.3966 0.3502 0.5030 -0.0737 0.0708  0.0288  464 HOH A O    
2326 O  O    . HOH F .   ? 0.3422 0.3322 0.5527 0.0142  -0.0029 0.0118  465 HOH A O    
2327 O  O    . HOH F .   ? 0.5513 0.6428 0.5897 -0.0005 -0.0081 0.0235  466 HOH A O    
2328 O  O    . HOH F .   ? 0.3861 0.3462 0.4172 -0.0357 -0.0174 0.0261  467 HOH A O    
2329 O  O    . HOH F .   ? 0.3021 0.4490 0.4205 -0.0421 -0.0357 0.0550  468 HOH A O    
2330 O  O    . HOH F .   ? 0.2394 0.5378 0.4264 0.0558  0.0199  -0.0257 469 HOH A O    
2331 O  O    . HOH F .   ? 0.4368 0.4708 0.4530 0.0344  -0.0289 0.0978  470 HOH A O    
2332 O  O    . HOH F .   ? 0.4152 0.4334 0.5037 0.0248  -0.0739 -0.0401 471 HOH A O    
2333 O  O    . HOH F .   ? 0.3799 0.4632 0.4684 0.0122  0.0956  -0.0016 472 HOH A O    
2334 O  O    . HOH F .   ? 0.4874 0.4180 0.4265 0.0504  0.0487  -0.0046 473 HOH A O    
2335 O  O    . HOH F .   ? 0.6192 0.5496 0.4014 -0.0032 0.0160  -0.0006 474 HOH A O    
2336 O  O    . HOH F .   ? 0.5990 0.4458 0.5408 0.0145  0.0035  -0.0310 475 HOH A O    
2337 O  O    . HOH F .   ? 0.5394 0.5633 0.4448 0.0116  0.0146  -0.0089 476 HOH A O    
2338 O  O    . HOH F .   ? 0.5655 0.4918 0.5939 0.0159  0.0055  0.0536  477 HOH A O    
2339 O  O    . HOH F .   ? 0.3785 0.3066 0.4267 -0.0422 -0.0047 -0.0518 478 HOH A O    
2340 O  O    . HOH F .   ? 0.3932 0.4710 0.4499 0.0768  0.0126  0.0739  479 HOH A O    
2341 O  O    . HOH F .   ? 0.3240 0.4005 0.4100 -0.1030 0.0107  0.0632  480 HOH A O    
2342 O  O    . HOH F .   ? 0.3993 0.3357 0.3141 -0.0147 0.0767  0.0797  481 HOH A O    
2343 O  O    . HOH F .   ? 0.4955 0.4517 0.4190 0.0162  0.0465  0.0623  482 HOH A O    
2344 O  O    . HOH F .   ? 0.5289 0.5063 0.3378 -0.0024 -0.0250 -0.0039 483 HOH A O    
2345 O  O    . HOH F .   ? 0.4552 0.2946 0.3640 -0.0489 0.0506  -0.0501 484 HOH A O    
2346 O  O    . HOH F .   ? 0.5334 0.4415 0.3648 -0.0319 0.0032  -0.0790 485 HOH A O    
2347 O  O    . HOH F .   ? 0.4833 0.3818 0.4328 -0.0220 0.0229  -0.0490 486 HOH A O    
2348 O  O    . HOH F .   ? 0.4629 0.3143 0.5478 -0.0488 -0.0154 -0.0311 487 HOH A O    
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   262 1   ZN  ZN  A . 
C 3 E02 1   263 1   E02 E02 A . 
D 4 MES 1   264 1   MES MES A . 
E 5 DMS 1   265 1   DMS DMS A . 
F 6 HOH 1   126 126 HOH HOH A . 
F 6 HOH 2   266 1   HOH HOH A . 
F 6 HOH 3   267 2   HOH HOH A . 
F 6 HOH 4   268 3   HOH HOH A . 
F 6 HOH 5   269 4   HOH HOH A . 
F 6 HOH 6   270 5   HOH HOH A . 
F 6 HOH 7   271 6   HOH HOH A . 
F 6 HOH 8   272 7   HOH HOH A . 
F 6 HOH 9   273 8   HOH HOH A . 
F 6 HOH 10  274 9   HOH HOH A . 
F 6 HOH 11  275 10  HOH HOH A . 
F 6 HOH 12  276 11  HOH HOH A . 
F 6 HOH 13  277 12  HOH HOH A . 
F 6 HOH 14  278 13  HOH HOH A . 
F 6 HOH 15  279 14  HOH HOH A . 
F 6 HOH 16  280 15  HOH HOH A . 
F 6 HOH 17  281 16  HOH HOH A . 
F 6 HOH 18  282 17  HOH HOH A . 
F 6 HOH 19  283 18  HOH HOH A . 
F 6 HOH 20  284 19  HOH HOH A . 
F 6 HOH 21  285 20  HOH HOH A . 
F 6 HOH 22  286 21  HOH HOH A . 
F 6 HOH 23  287 22  HOH HOH A . 
F 6 HOH 24  288 23  HOH HOH A . 
F 6 HOH 25  289 24  HOH HOH A . 
F 6 HOH 26  290 25  HOH HOH A . 
F 6 HOH 27  291 26  HOH HOH A . 
F 6 HOH 28  292 27  HOH HOH A . 
F 6 HOH 29  293 28  HOH HOH A . 
F 6 HOH 30  294 29  HOH HOH A . 
F 6 HOH 31  295 30  HOH HOH A . 
F 6 HOH 32  296 31  HOH HOH A . 
F 6 HOH 33  297 32  HOH HOH A . 
F 6 HOH 34  298 33  HOH HOH A . 
F 6 HOH 35  299 34  HOH HOH A . 
F 6 HOH 36  300 35  HOH HOH A . 
F 6 HOH 37  301 36  HOH HOH A . 
F 6 HOH 38  302 37  HOH HOH A . 
F 6 HOH 39  303 38  HOH HOH A . 
F 6 HOH 40  304 39  HOH HOH A . 
F 6 HOH 41  305 40  HOH HOH A . 
F 6 HOH 42  306 41  HOH HOH A . 
F 6 HOH 43  307 42  HOH HOH A . 
F 6 HOH 44  308 43  HOH HOH A . 
F 6 HOH 45  309 44  HOH HOH A . 
F 6 HOH 46  310 45  HOH HOH A . 
F 6 HOH 47  311 46  HOH HOH A . 
F 6 HOH 48  312 47  HOH HOH A . 
F 6 HOH 49  313 48  HOH HOH A . 
F 6 HOH 50  314 49  HOH HOH A . 
F 6 HOH 51  315 50  HOH HOH A . 
F 6 HOH 52  316 51  HOH HOH A . 
F 6 HOH 53  317 52  HOH HOH A . 
F 6 HOH 54  318 53  HOH HOH A . 
F 6 HOH 55  319 54  HOH HOH A . 
F 6 HOH 56  320 55  HOH HOH A . 
F 6 HOH 57  321 56  HOH HOH A . 
F 6 HOH 58  322 57  HOH HOH A . 
F 6 HOH 59  323 58  HOH HOH A . 
F 6 HOH 60  324 59  HOH HOH A . 
F 6 HOH 61  325 60  HOH HOH A . 
F 6 HOH 62  326 61  HOH HOH A . 
F 6 HOH 63  327 62  HOH HOH A . 
F 6 HOH 64  328 63  HOH HOH A . 
F 6 HOH 65  329 64  HOH HOH A . 
F 6 HOH 66  330 65  HOH HOH A . 
F 6 HOH 67  331 66  HOH HOH A . 
F 6 HOH 68  332 67  HOH HOH A . 
F 6 HOH 69  333 68  HOH HOH A . 
F 6 HOH 70  334 69  HOH HOH A . 
F 6 HOH 71  335 70  HOH HOH A . 
F 6 HOH 72  336 71  HOH HOH A . 
F 6 HOH 73  337 72  HOH HOH A . 
F 6 HOH 74  338 73  HOH HOH A . 
F 6 HOH 75  339 74  HOH HOH A . 
F 6 HOH 76  340 75  HOH HOH A . 
F 6 HOH 77  341 76  HOH HOH A . 
F 6 HOH 78  342 77  HOH HOH A . 
F 6 HOH 79  343 78  HOH HOH A . 
F 6 HOH 80  344 79  HOH HOH A . 
F 6 HOH 81  345 80  HOH HOH A . 
F 6 HOH 82  346 81  HOH HOH A . 
F 6 HOH 83  347 82  HOH HOH A . 
F 6 HOH 84  348 83  HOH HOH A . 
F 6 HOH 85  349 84  HOH HOH A . 
F 6 HOH 86  350 85  HOH HOH A . 
F 6 HOH 87  351 86  HOH HOH A . 
F 6 HOH 88  352 87  HOH HOH A . 
F 6 HOH 89  353 88  HOH HOH A . 
F 6 HOH 90  354 89  HOH HOH A . 
F 6 HOH 91  355 90  HOH HOH A . 
F 6 HOH 92  356 91  HOH HOH A . 
F 6 HOH 93  357 92  HOH HOH A . 
F 6 HOH 94  358 93  HOH HOH A . 
F 6 HOH 95  359 94  HOH HOH A . 
F 6 HOH 96  360 95  HOH HOH A . 
F 6 HOH 97  361 96  HOH HOH A . 
F 6 HOH 98  362 97  HOH HOH A . 
F 6 HOH 99  363 98  HOH HOH A . 
F 6 HOH 100 364 99  HOH HOH A . 
F 6 HOH 101 365 100 HOH HOH A . 
F 6 HOH 102 366 101 HOH HOH A . 
F 6 HOH 103 367 102 HOH HOH A . 
F 6 HOH 104 368 103 HOH HOH A . 
F 6 HOH 105 369 104 HOH HOH A . 
F 6 HOH 106 370 105 HOH HOH A . 
F 6 HOH 107 371 106 HOH HOH A . 
F 6 HOH 108 372 107 HOH HOH A . 
F 6 HOH 109 373 108 HOH HOH A . 
F 6 HOH 110 374 109 HOH HOH A . 
F 6 HOH 111 375 110 HOH HOH A . 
F 6 HOH 112 376 111 HOH HOH A . 
F 6 HOH 113 377 112 HOH HOH A . 
F 6 HOH 114 378 113 HOH HOH A . 
F 6 HOH 115 379 114 HOH HOH A . 
F 6 HOH 116 380 115 HOH HOH A . 
F 6 HOH 117 381 116 HOH HOH A . 
F 6 HOH 118 382 117 HOH HOH A . 
F 6 HOH 119 383 118 HOH HOH A . 
F 6 HOH 120 384 119 HOH HOH A . 
F 6 HOH 121 385 120 HOH HOH A . 
F 6 HOH 122 386 121 HOH HOH A . 
F 6 HOH 123 387 122 HOH HOH A . 
F 6 HOH 124 388 123 HOH HOH A . 
F 6 HOH 125 389 124 HOH HOH A . 
F 6 HOH 126 390 125 HOH HOH A . 
F 6 HOH 127 391 127 HOH HOH A . 
F 6 HOH 128 392 128 HOH HOH A . 
F 6 HOH 129 393 129 HOH HOH A . 
F 6 HOH 130 394 130 HOH HOH A . 
F 6 HOH 131 395 131 HOH HOH A . 
F 6 HOH 132 396 132 HOH HOH A . 
F 6 HOH 133 397 133 HOH HOH A . 
F 6 HOH 134 398 134 HOH HOH A . 
F 6 HOH 135 399 135 HOH HOH A . 
F 6 HOH 136 400 136 HOH HOH A . 
F 6 HOH 137 401 137 HOH HOH A . 
F 6 HOH 138 402 138 HOH HOH A . 
F 6 HOH 139 403 139 HOH HOH A . 
F 6 HOH 140 404 140 HOH HOH A . 
F 6 HOH 141 405 141 HOH HOH A . 
F 6 HOH 142 406 142 HOH HOH A . 
F 6 HOH 143 407 143 HOH HOH A . 
F 6 HOH 144 408 144 HOH HOH A . 
F 6 HOH 145 409 145 HOH HOH A . 
F 6 HOH 146 410 146 HOH HOH A . 
F 6 HOH 147 411 147 HOH HOH A . 
F 6 HOH 148 412 148 HOH HOH A . 
F 6 HOH 149 413 149 HOH HOH A . 
F 6 HOH 150 414 150 HOH HOH A . 
F 6 HOH 151 415 151 HOH HOH A . 
F 6 HOH 152 416 152 HOH HOH A . 
F 6 HOH 153 417 153 HOH HOH A . 
F 6 HOH 154 418 154 HOH HOH A . 
F 6 HOH 155 419 155 HOH HOH A . 
F 6 HOH 156 420 156 HOH HOH A . 
F 6 HOH 157 421 157 HOH HOH A . 
F 6 HOH 158 422 158 HOH HOH A . 
F 6 HOH 159 423 159 HOH HOH A . 
F 6 HOH 160 424 160 HOH HOH A . 
F 6 HOH 161 425 161 HOH HOH A . 
F 6 HOH 162 426 162 HOH HOH A . 
F 6 HOH 163 427 163 HOH HOH A . 
F 6 HOH 164 428 164 HOH HOH A . 
F 6 HOH 165 429 165 HOH HOH A . 
F 6 HOH 166 430 166 HOH HOH A . 
F 6 HOH 167 431 167 HOH HOH A . 
F 6 HOH 168 432 168 HOH HOH A . 
F 6 HOH 169 433 169 HOH HOH A . 
F 6 HOH 170 434 170 HOH HOH A . 
F 6 HOH 171 435 171 HOH HOH A . 
F 6 HOH 172 436 172 HOH HOH A . 
F 6 HOH 173 437 173 HOH HOH A . 
F 6 HOH 174 438 174 HOH HOH A . 
F 6 HOH 175 439 175 HOH HOH A . 
F 6 HOH 176 440 176 HOH HOH A . 
F 6 HOH 177 441 177 HOH HOH A . 
F 6 HOH 178 442 178 HOH HOH A . 
F 6 HOH 179 443 179 HOH HOH A . 
F 6 HOH 180 444 180 HOH HOH A . 
F 6 HOH 181 445 181 HOH HOH A . 
F 6 HOH 182 446 182 HOH HOH A . 
F 6 HOH 183 447 183 HOH HOH A . 
F 6 HOH 184 448 184 HOH HOH A . 
F 6 HOH 185 449 185 HOH HOH A . 
F 6 HOH 186 450 186 HOH HOH A . 
F 6 HOH 187 451 187 HOH HOH A . 
F 6 HOH 188 452 188 HOH HOH A . 
F 6 HOH 189 453 189 HOH HOH A . 
F 6 HOH 190 454 190 HOH HOH A . 
F 6 HOH 191 455 191 HOH HOH A . 
F 6 HOH 192 456 192 HOH HOH A . 
F 6 HOH 193 457 193 HOH HOH A . 
F 6 HOH 194 458 194 HOH HOH A . 
F 6 HOH 195 459 195 HOH HOH A . 
F 6 HOH 196 460 196 HOH HOH A . 
F 6 HOH 197 461 197 HOH HOH A . 
F 6 HOH 198 462 198 HOH HOH A . 
F 6 HOH 199 463 199 HOH HOH A . 
F 6 HOH 200 464 200 HOH HOH A . 
F 6 HOH 201 465 201 HOH HOH A . 
F 6 HOH 202 466 202 HOH HOH A . 
F 6 HOH 203 467 203 HOH HOH A . 
F 6 HOH 204 468 204 HOH HOH A . 
F 6 HOH 205 469 205 HOH HOH A . 
F 6 HOH 206 470 206 HOH HOH A . 
F 6 HOH 207 471 207 HOH HOH A . 
F 6 HOH 208 472 208 HOH HOH A . 
F 6 HOH 209 473 209 HOH HOH A . 
F 6 HOH 210 474 210 HOH HOH A . 
F 6 HOH 211 475 211 HOH HOH A . 
F 6 HOH 212 476 212 HOH HOH A . 
F 6 HOH 213 477 213 HOH HOH A . 
F 6 HOH 214 478 214 HOH HOH A . 
F 6 HOH 215 479 215 HOH HOH A . 
F 6 HOH 216 480 216 HOH HOH A . 
F 6 HOH 217 481 217 HOH HOH A . 
F 6 HOH 218 482 218 HOH HOH A . 
F 6 HOH 219 483 219 HOH HOH A . 
F 6 HOH 220 484 220 HOH HOH A . 
F 6 HOH 221 485 221 HOH HOH A . 
F 6 HOH 222 486 222 HOH HOH A . 
F 6 HOH 223 487 223 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_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2011-03-02 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-08 
4 'Structure model' 1 3 2023-09-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Refinement description'    
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Derived calculations'      
6 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' software                      
2 4 'Structure model' chem_comp_atom                
3 4 'Structure model' chem_comp_bond                
4 4 'Structure model' database_2                    
5 4 'Structure model' diffrn_source                 
6 4 'Structure model' pdbx_initial_refinement_model 
7 4 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_software.name'                       
2 4 'Structure model' '_database_2.pdbx_DOI'                 
3 4 'Structure model' '_database_2.pdbx_database_accession'  
4 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
5 4 'Structure model' '_struct_site.pdbx_auth_asym_id'       
6 4 'Structure model' '_struct_site.pdbx_auth_comp_id'       
7 4 'Structure model' '_struct_site.pdbx_auth_seq_id'        
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19 22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345      .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 366 ? ? 1_555 O A HOH 464 ? ? 1_455 1.75 
2 1 O   A HOH 358 ? ? 1_555 O A HOH 407 ? ? 1_455 1.75 
3 1 O1S A MES 264 ? ? 1_555 O A HOH 382 ? ? 2_445 1.99 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A TYR 7   ? ? CD2 A TYR 7   ? ? 1.467 1.387 0.080 0.013 N 
2 1 N  A GLY 8   ? ? CA  A GLY 8   ? ? 1.549 1.456 0.093 0.015 N 
3 1 CG A GLU 14  ? ? CD  A GLU 14  ? ? 1.605 1.515 0.090 0.015 N 
4 1 CD A GLU 14  ? ? OE2 A GLU 14  ? ? 1.325 1.252 0.073 0.011 N 
5 1 CZ A TYR 51  ? ? CE2 A TYR 51  ? ? 1.464 1.381 0.083 0.013 N 
6 1 C  A THR 125 ? ? N   A LYS 127 ? ? 1.487 1.336 0.151 0.023 Y 
7 1 CD A GLU 234 ? ? OE1 A GLU 234 ? ? 1.332 1.252 0.080 0.011 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 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH1 A ARG 27  ? ? 124.24 120.30 3.94   0.50 N 
2 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH2 A ARG 27  ? ? 116.12 120.30 -4.18  0.50 N 
3 1 CB A ASP 52  ? ? CG A ASP 52  ? ? OD1 A ASP 52  ? ? 124.29 118.30 5.99   0.90 N 
4 1 C  A ASP 85  ? ? N  A GLY 86  ? ? CA  A GLY 86  ? ? 105.54 122.30 -16.76 2.10 Y 
5 1 CB A ASP 101 ? ? CG A ASP 101 ? ? OD1 A ASP 101 ? ? 125.21 118.30 6.91   0.90 N 
6 1 CB A LEU 198 ? ? CG A LEU 198 ? ? CD2 A LEU 198 ? ? 125.69 111.00 14.69  1.70 N 
7 1 CD A LYS 213 ? ? CE A LYS 213 ? ? NZ  A LYS 213 ? ? 127.13 111.70 15.43  2.30 N 
8 1 CB A PHE 226 ? ? CG A PHE 226 ? ? CD1 A PHE 226 ? ? 125.04 120.80 4.24   0.70 N 
9 1 NE A ARG 254 ? ? CZ A ARG 254 ? ? NH1 A ARG 254 ? ? 115.20 120.30 -5.10  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -142.60 16.45   
2 1 ARG A 27  ? ? -145.71 55.90   
3 1 ASN A 244 ? ? -93.19  50.89   
4 1 LYS A 252 ? ? 55.05   -139.48 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
E02 N1   N  Y N 98  
E02 C2   C  Y N 99  
E02 N3   N  Y N 100 
E02 C4   C  Y N 101 
E02 C5   C  Y N 102 
E02 C6   C  Y N 103 
E02 C7   C  Y N 104 
E02 C8   C  Y N 105 
E02 C9   C  Y N 106 
E02 C10  C  N N 107 
E02 C11  C  N N 108 
E02 O12  O  N N 109 
E02 C13  C  Y N 110 
E02 C14  C  Y N 111 
E02 C15  C  Y N 112 
E02 C16  C  Y N 113 
E02 C17  C  Y N 114 
E02 C18  C  Y N 115 
E02 S19  S  N N 116 
E02 O20  O  N N 117 
E02 CL21 CL N N 118 
E02 O22  O  N N 119 
E02 N23  N  N N 120 
E02 H2   H  N N 121 
E02 H6   H  N N 122 
E02 H7   H  N N 123 
E02 H8   H  N N 124 
E02 H9   H  N N 125 
E02 H10  H  N N 126 
E02 H10A H  N N 127 
E02 H14  H  N N 128 
E02 H17  H  N N 129 
E02 H18  H  N N 130 
E02 HN23 H  N N 131 
E02 HN2A H  N N 132 
GLN N    N  N N 133 
GLN CA   C  N S 134 
GLN C    C  N N 135 
GLN O    O  N N 136 
GLN CB   C  N N 137 
GLN CG   C  N N 138 
GLN CD   C  N N 139 
GLN OE1  O  N N 140 
GLN NE2  N  N N 141 
GLN OXT  O  N N 142 
GLN H    H  N N 143 
GLN H2   H  N N 144 
GLN HA   H  N N 145 
GLN HB2  H  N N 146 
GLN HB3  H  N N 147 
GLN HG2  H  N N 148 
GLN HG3  H  N N 149 
GLN HE21 H  N N 150 
GLN HE22 H  N N 151 
GLN HXT  H  N N 152 
GLU N    N  N N 153 
GLU CA   C  N S 154 
GLU C    C  N N 155 
GLU O    O  N N 156 
GLU CB   C  N N 157 
GLU CG   C  N N 158 
GLU CD   C  N N 159 
GLU OE1  O  N N 160 
GLU OE2  O  N N 161 
GLU OXT  O  N N 162 
GLU H    H  N N 163 
GLU H2   H  N N 164 
GLU HA   H  N N 165 
GLU HB2  H  N N 166 
GLU HB3  H  N N 167 
GLU HG2  H  N N 168 
GLU HG3  H  N N 169 
GLU HE2  H  N N 170 
GLU HXT  H  N N 171 
GLY N    N  N N 172 
GLY CA   C  N N 173 
GLY C    C  N N 174 
GLY O    O  N N 175 
GLY OXT  O  N N 176 
GLY H    H  N N 177 
GLY H2   H  N N 178 
GLY HA2  H  N N 179 
GLY HA3  H  N N 180 
GLY HXT  H  N N 181 
HIS N    N  N N 182 
HIS CA   C  N S 183 
HIS C    C  N N 184 
HIS O    O  N N 185 
HIS CB   C  N N 186 
HIS CG   C  Y N 187 
HIS ND1  N  Y N 188 
HIS CD2  C  Y N 189 
HIS CE1  C  Y N 190 
HIS NE2  N  Y N 191 
HIS OXT  O  N N 192 
HIS H    H  N N 193 
HIS H2   H  N N 194 
HIS HA   H  N N 195 
HIS HB2  H  N N 196 
HIS HB3  H  N N 197 
HIS HD1  H  N N 198 
HIS HD2  H  N N 199 
HIS HE1  H  N N 200 
HIS HE2  H  N N 201 
HIS HXT  H  N N 202 
HOH O    O  N N 203 
HOH H1   H  N N 204 
HOH H2   H  N N 205 
ILE N    N  N N 206 
ILE CA   C  N S 207 
ILE C    C  N N 208 
ILE O    O  N N 209 
ILE CB   C  N S 210 
ILE CG1  C  N N 211 
ILE CG2  C  N N 212 
ILE CD1  C  N N 213 
ILE OXT  O  N N 214 
ILE H    H  N N 215 
ILE H2   H  N N 216 
ILE HA   H  N N 217 
ILE HB   H  N N 218 
ILE HG12 H  N N 219 
ILE HG13 H  N N 220 
ILE HG21 H  N N 221 
ILE HG22 H  N N 222 
ILE HG23 H  N N 223 
ILE HD11 H  N N 224 
ILE HD12 H  N N 225 
ILE HD13 H  N N 226 
ILE HXT  H  N N 227 
LEU N    N  N N 228 
LEU CA   C  N S 229 
LEU C    C  N N 230 
LEU O    O  N N 231 
LEU CB   C  N N 232 
LEU CG   C  N N 233 
LEU CD1  C  N N 234 
LEU CD2  C  N N 235 
LEU OXT  O  N N 236 
LEU H    H  N N 237 
LEU H2   H  N N 238 
LEU HA   H  N N 239 
LEU HB2  H  N N 240 
LEU HB3  H  N N 241 
LEU HG   H  N N 242 
LEU HD11 H  N N 243 
LEU HD12 H  N N 244 
LEU HD13 H  N N 245 
LEU HD21 H  N N 246 
LEU HD22 H  N N 247 
LEU HD23 H  N N 248 
LEU HXT  H  N N 249 
LYS N    N  N N 250 
LYS CA   C  N S 251 
LYS C    C  N N 252 
LYS O    O  N N 253 
LYS CB   C  N N 254 
LYS CG   C  N N 255 
LYS CD   C  N N 256 
LYS CE   C  N N 257 
LYS NZ   N  N N 258 
LYS OXT  O  N N 259 
LYS H    H  N N 260 
LYS H2   H  N N 261 
LYS HA   H  N N 262 
LYS HB2  H  N N 263 
LYS HB3  H  N N 264 
LYS HG2  H  N N 265 
LYS HG3  H  N N 266 
LYS HD2  H  N N 267 
LYS HD3  H  N N 268 
LYS HE2  H  N N 269 
LYS HE3  H  N N 270 
LYS HZ1  H  N N 271 
LYS HZ2  H  N N 272 
LYS HZ3  H  N N 273 
LYS HXT  H  N N 274 
MES O1   O  N N 275 
MES C2   C  N N 276 
MES C3   C  N N 277 
MES N4   N  N N 278 
MES C5   C  N N 279 
MES C6   C  N N 280 
MES C7   C  N N 281 
MES C8   C  N N 282 
MES S    S  N N 283 
MES O1S  O  N N 284 
MES O2S  O  N N 285 
MES O3S  O  N N 286 
MES H21  H  N N 287 
MES H22  H  N N 288 
MES H31  H  N N 289 
MES H32  H  N N 290 
MES HN4  H  N N 291 
MES H51  H  N N 292 
MES H52  H  N N 293 
MES H61  H  N N 294 
MES H62  H  N N 295 
MES H71  H  N N 296 
MES H72  H  N N 297 
MES H81  H  N N 298 
MES H82  H  N N 299 
MET N    N  N N 300 
MET CA   C  N S 301 
MET C    C  N N 302 
MET O    O  N N 303 
MET CB   C  N N 304 
MET CG   C  N N 305 
MET SD   S  N N 306 
MET CE   C  N N 307 
MET OXT  O  N N 308 
MET H    H  N N 309 
MET H2   H  N N 310 
MET HA   H  N N 311 
MET HB2  H  N N 312 
MET HB3  H  N N 313 
MET HG2  H  N N 314 
MET HG3  H  N N 315 
MET HE1  H  N N 316 
MET HE2  H  N N 317 
MET HE3  H  N N 318 
MET HXT  H  N N 319 
PHE N    N  N N 320 
PHE CA   C  N S 321 
PHE C    C  N N 322 
PHE O    O  N N 323 
PHE CB   C  N N 324 
PHE CG   C  Y N 325 
PHE CD1  C  Y N 326 
PHE CD2  C  Y N 327 
PHE CE1  C  Y N 328 
PHE CE2  C  Y N 329 
PHE CZ   C  Y N 330 
PHE OXT  O  N N 331 
PHE H    H  N N 332 
PHE H2   H  N N 333 
PHE HA   H  N N 334 
PHE HB2  H  N N 335 
PHE HB3  H  N N 336 
PHE HD1  H  N N 337 
PHE HD2  H  N N 338 
PHE HE1  H  N N 339 
PHE HE2  H  N N 340 
PHE HZ   H  N N 341 
PHE HXT  H  N N 342 
PRO N    N  N N 343 
PRO CA   C  N S 344 
PRO C    C  N N 345 
PRO O    O  N N 346 
PRO CB   C  N N 347 
PRO CG   C  N N 348 
PRO CD   C  N N 349 
PRO OXT  O  N N 350 
PRO H    H  N N 351 
PRO HA   H  N N 352 
PRO HB2  H  N N 353 
PRO HB3  H  N N 354 
PRO HG2  H  N N 355 
PRO HG3  H  N N 356 
PRO HD2  H  N N 357 
PRO HD3  H  N N 358 
PRO HXT  H  N N 359 
SER N    N  N N 360 
SER CA   C  N S 361 
SER C    C  N N 362 
SER O    O  N N 363 
SER CB   C  N N 364 
SER OG   O  N N 365 
SER OXT  O  N N 366 
SER H    H  N N 367 
SER H2   H  N N 368 
SER HA   H  N N 369 
SER HB2  H  N N 370 
SER HB3  H  N N 371 
SER HG   H  N N 372 
SER HXT  H  N N 373 
THR N    N  N N 374 
THR CA   C  N S 375 
THR C    C  N N 376 
THR O    O  N N 377 
THR CB   C  N R 378 
THR OG1  O  N N 379 
THR CG2  C  N N 380 
THR OXT  O  N N 381 
THR H    H  N N 382 
THR H2   H  N N 383 
THR HA   H  N N 384 
THR HB   H  N N 385 
THR HG1  H  N N 386 
THR HG21 H  N N 387 
THR HG22 H  N N 388 
THR HG23 H  N N 389 
THR HXT  H  N N 390 
TRP N    N  N N 391 
TRP CA   C  N S 392 
TRP C    C  N N 393 
TRP O    O  N N 394 
TRP CB   C  N N 395 
TRP CG   C  Y N 396 
TRP CD1  C  Y N 397 
TRP CD2  C  Y N 398 
TRP NE1  N  Y N 399 
TRP CE2  C  Y N 400 
TRP CE3  C  Y N 401 
TRP CZ2  C  Y N 402 
TRP CZ3  C  Y N 403 
TRP CH2  C  Y N 404 
TRP OXT  O  N N 405 
TRP H    H  N N 406 
TRP H2   H  N N 407 
TRP HA   H  N N 408 
TRP HB2  H  N N 409 
TRP HB3  H  N N 410 
TRP HD1  H  N N 411 
TRP HE1  H  N N 412 
TRP HE3  H  N N 413 
TRP HZ2  H  N N 414 
TRP HZ3  H  N N 415 
TRP HH2  H  N N 416 
TRP HXT  H  N N 417 
TYR N    N  N N 418 
TYR CA   C  N S 419 
TYR C    C  N N 420 
TYR O    O  N N 421 
TYR CB   C  N N 422 
TYR CG   C  Y N 423 
TYR CD1  C  Y N 424 
TYR CD2  C  Y N 425 
TYR CE1  C  Y N 426 
TYR CE2  C  Y N 427 
TYR CZ   C  Y N 428 
TYR OH   O  N N 429 
TYR OXT  O  N N 430 
TYR H    H  N N 431 
TYR H2   H  N N 432 
TYR HA   H  N N 433 
TYR HB2  H  N N 434 
TYR HB3  H  N N 435 
TYR HD1  H  N N 436 
TYR HD2  H  N N 437 
TYR HE1  H  N N 438 
TYR HE2  H  N N 439 
TYR HH   H  N N 440 
TYR HXT  H  N N 441 
VAL N    N  N N 442 
VAL CA   C  N S 443 
VAL C    C  N N 444 
VAL O    O  N N 445 
VAL CB   C  N N 446 
VAL CG1  C  N N 447 
VAL CG2  C  N N 448 
VAL OXT  O  N N 449 
VAL H    H  N N 450 
VAL H2   H  N N 451 
VAL HA   H  N N 452 
VAL HB   H  N N 453 
VAL HG11 H  N N 454 
VAL HG12 H  N N 455 
VAL HG13 H  N N 456 
VAL HG21 H  N N 457 
VAL HG22 H  N N 458 
VAL HG23 H  N N 459 
VAL HXT  H  N N 460 
ZN  ZN   ZN N N 461 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
E02 C5  N1   sing Y N 92  
E02 N1  C2   sing Y N 93  
E02 N1  C10  sing N N 94  
E02 N3  C2   doub Y N 95  
E02 C2  H2   sing N N 96  
E02 C4  N3   sing Y N 97  
E02 C9  C4   doub Y N 98  
E02 C4  C5   sing Y N 99  
E02 C6  C5   doub Y N 100 
E02 C7  C6   sing Y N 101 
E02 C6  H6   sing N N 102 
E02 C8  C7   doub Y N 103 
E02 C7  H7   sing N N 104 
E02 C8  C9   sing Y N 105 
E02 C8  H8   sing N N 106 
E02 C9  H9   sing N N 107 
E02 C10 C11  sing N N 108 
E02 C10 H10  sing N N 109 
E02 C10 H10A sing N N 110 
E02 O12 C11  doub N N 111 
E02 C11 C13  sing N N 112 
E02 C13 C18  doub Y N 113 
E02 C13 C14  sing Y N 114 
E02 C14 C15  doub Y N 115 
E02 C14 H14  sing N N 116 
E02 C15 C16  sing Y N 117 
E02 C15 S19  sing N N 118 
E02 C17 C16  doub Y N 119 
E02 C16 CL21 sing N N 120 
E02 C18 C17  sing Y N 121 
E02 C17 H17  sing N N 122 
E02 C18 H18  sing N N 123 
E02 N23 S19  sing N N 124 
E02 O22 S19  doub N N 125 
E02 S19 O20  doub N N 126 
E02 N23 HN23 sing N N 127 
E02 N23 HN2A sing N N 128 
GLN N   CA   sing N N 129 
GLN N   H    sing N N 130 
GLN N   H2   sing N N 131 
GLN CA  C    sing N N 132 
GLN CA  CB   sing N N 133 
GLN CA  HA   sing N N 134 
GLN C   O    doub N N 135 
GLN C   OXT  sing N N 136 
GLN CB  CG   sing N N 137 
GLN CB  HB2  sing N N 138 
GLN CB  HB3  sing N N 139 
GLN CG  CD   sing N N 140 
GLN CG  HG2  sing N N 141 
GLN CG  HG3  sing N N 142 
GLN CD  OE1  doub N N 143 
GLN CD  NE2  sing N N 144 
GLN NE2 HE21 sing N N 145 
GLN NE2 HE22 sing N N 146 
GLN OXT HXT  sing N N 147 
GLU N   CA   sing N N 148 
GLU N   H    sing N N 149 
GLU N   H2   sing N N 150 
GLU CA  C    sing N N 151 
GLU CA  CB   sing N N 152 
GLU CA  HA   sing N N 153 
GLU C   O    doub N N 154 
GLU C   OXT  sing N N 155 
GLU CB  CG   sing N N 156 
GLU CB  HB2  sing N N 157 
GLU CB  HB3  sing N N 158 
GLU CG  CD   sing N N 159 
GLU CG  HG2  sing N N 160 
GLU CG  HG3  sing N N 161 
GLU CD  OE1  doub N N 162 
GLU CD  OE2  sing N N 163 
GLU OE2 HE2  sing N N 164 
GLU OXT HXT  sing N N 165 
GLY N   CA   sing N N 166 
GLY N   H    sing N N 167 
GLY N   H2   sing N N 168 
GLY CA  C    sing N N 169 
GLY CA  HA2  sing N N 170 
GLY CA  HA3  sing N N 171 
GLY C   O    doub N N 172 
GLY C   OXT  sing N N 173 
GLY OXT HXT  sing N N 174 
HIS N   CA   sing N N 175 
HIS N   H    sing N N 176 
HIS N   H2   sing N N 177 
HIS CA  C    sing N N 178 
HIS CA  CB   sing N N 179 
HIS CA  HA   sing N N 180 
HIS C   O    doub N N 181 
HIS C   OXT  sing N N 182 
HIS CB  CG   sing N N 183 
HIS CB  HB2  sing N N 184 
HIS CB  HB3  sing N N 185 
HIS CG  ND1  sing Y N 186 
HIS CG  CD2  doub Y N 187 
HIS ND1 CE1  doub Y N 188 
HIS ND1 HD1  sing N N 189 
HIS CD2 NE2  sing Y N 190 
HIS CD2 HD2  sing N N 191 
HIS CE1 NE2  sing Y N 192 
HIS CE1 HE1  sing N N 193 
HIS NE2 HE2  sing N N 194 
HIS OXT HXT  sing N N 195 
HOH O   H1   sing N N 196 
HOH O   H2   sing N N 197 
ILE N   CA   sing N N 198 
ILE N   H    sing N N 199 
ILE N   H2   sing N N 200 
ILE CA  C    sing N N 201 
ILE CA  CB   sing N N 202 
ILE CA  HA   sing N N 203 
ILE C   O    doub N N 204 
ILE C   OXT  sing N N 205 
ILE CB  CG1  sing N N 206 
ILE CB  CG2  sing N N 207 
ILE CB  HB   sing N N 208 
ILE CG1 CD1  sing N N 209 
ILE CG1 HG12 sing N N 210 
ILE CG1 HG13 sing N N 211 
ILE CG2 HG21 sing N N 212 
ILE CG2 HG22 sing N N 213 
ILE CG2 HG23 sing N N 214 
ILE CD1 HD11 sing N N 215 
ILE CD1 HD12 sing N N 216 
ILE CD1 HD13 sing N N 217 
ILE OXT HXT  sing N N 218 
LEU N   CA   sing N N 219 
LEU N   H    sing N N 220 
LEU N   H2   sing N N 221 
LEU CA  C    sing N N 222 
LEU CA  CB   sing N N 223 
LEU CA  HA   sing N N 224 
LEU C   O    doub N N 225 
LEU C   OXT  sing N N 226 
LEU CB  CG   sing N N 227 
LEU CB  HB2  sing N N 228 
LEU CB  HB3  sing N N 229 
LEU CG  CD1  sing N N 230 
LEU CG  CD2  sing N N 231 
LEU CG  HG   sing N N 232 
LEU CD1 HD11 sing N N 233 
LEU CD1 HD12 sing N N 234 
LEU CD1 HD13 sing N N 235 
LEU CD2 HD21 sing N N 236 
LEU CD2 HD22 sing N N 237 
LEU CD2 HD23 sing N N 238 
LEU OXT HXT  sing N N 239 
LYS N   CA   sing N N 240 
LYS N   H    sing N N 241 
LYS N   H2   sing N N 242 
LYS CA  C    sing N N 243 
LYS CA  CB   sing N N 244 
LYS CA  HA   sing N N 245 
LYS C   O    doub N N 246 
LYS C   OXT  sing N N 247 
LYS CB  CG   sing N N 248 
LYS CB  HB2  sing N N 249 
LYS CB  HB3  sing N N 250 
LYS CG  CD   sing N N 251 
LYS CG  HG2  sing N N 252 
LYS CG  HG3  sing N N 253 
LYS CD  CE   sing N N 254 
LYS CD  HD2  sing N N 255 
LYS CD  HD3  sing N N 256 
LYS CE  NZ   sing N N 257 
LYS CE  HE2  sing N N 258 
LYS CE  HE3  sing N N 259 
LYS NZ  HZ1  sing N N 260 
LYS NZ  HZ2  sing N N 261 
LYS NZ  HZ3  sing N N 262 
LYS OXT HXT  sing N N 263 
MES O1  C2   sing N N 264 
MES O1  C6   sing N N 265 
MES C2  C3   sing N N 266 
MES C2  H21  sing N N 267 
MES C2  H22  sing N N 268 
MES C3  N4   sing N N 269 
MES C3  H31  sing N N 270 
MES C3  H32  sing N N 271 
MES N4  C5   sing N N 272 
MES N4  C7   sing N N 273 
MES N4  HN4  sing N N 274 
MES C5  C6   sing N N 275 
MES C5  H51  sing N N 276 
MES C5  H52  sing N N 277 
MES C6  H61  sing N N 278 
MES C6  H62  sing N N 279 
MES C7  C8   sing N N 280 
MES C7  H71  sing N N 281 
MES C7  H72  sing N N 282 
MES C8  S    sing N N 283 
MES C8  H81  sing N N 284 
MES C8  H82  sing N N 285 
MES S   O1S  doub N N 286 
MES S   O2S  doub N N 287 
MES S   O3S  sing N N 288 
MET N   CA   sing N N 289 
MET N   H    sing N N 290 
MET N   H2   sing N N 291 
MET CA  C    sing N N 292 
MET CA  CB   sing N N 293 
MET CA  HA   sing N N 294 
MET C   O    doub N N 295 
MET C   OXT  sing N N 296 
MET CB  CG   sing N N 297 
MET CB  HB2  sing N N 298 
MET CB  HB3  sing N N 299 
MET CG  SD   sing N N 300 
MET CG  HG2  sing N N 301 
MET CG  HG3  sing N N 302 
MET SD  CE   sing N N 303 
MET CE  HE1  sing N N 304 
MET CE  HE2  sing N N 305 
MET CE  HE3  sing N N 306 
MET OXT HXT  sing N N 307 
PHE N   CA   sing N N 308 
PHE N   H    sing N N 309 
PHE N   H2   sing N N 310 
PHE CA  C    sing N N 311 
PHE CA  CB   sing N N 312 
PHE CA  HA   sing N N 313 
PHE C   O    doub N N 314 
PHE C   OXT  sing N N 315 
PHE CB  CG   sing N N 316 
PHE CB  HB2  sing N N 317 
PHE CB  HB3  sing N N 318 
PHE CG  CD1  doub Y N 319 
PHE CG  CD2  sing Y N 320 
PHE CD1 CE1  sing Y N 321 
PHE CD1 HD1  sing N N 322 
PHE CD2 CE2  doub Y N 323 
PHE CD2 HD2  sing N N 324 
PHE CE1 CZ   doub Y N 325 
PHE CE1 HE1  sing N N 326 
PHE CE2 CZ   sing Y N 327 
PHE CE2 HE2  sing N N 328 
PHE CZ  HZ   sing N N 329 
PHE OXT HXT  sing N N 330 
PRO N   CA   sing N N 331 
PRO N   CD   sing N N 332 
PRO N   H    sing N N 333 
PRO CA  C    sing N N 334 
PRO CA  CB   sing N N 335 
PRO CA  HA   sing N N 336 
PRO C   O    doub N N 337 
PRO C   OXT  sing N N 338 
PRO CB  CG   sing N N 339 
PRO CB  HB2  sing N N 340 
PRO CB  HB3  sing N N 341 
PRO CG  CD   sing N N 342 
PRO CG  HG2  sing N N 343 
PRO CG  HG3  sing N N 344 
PRO CD  HD2  sing N N 345 
PRO CD  HD3  sing N N 346 
PRO OXT HXT  sing N N 347 
SER N   CA   sing N N 348 
SER N   H    sing N N 349 
SER N   H2   sing N N 350 
SER CA  C    sing N N 351 
SER CA  CB   sing N N 352 
SER CA  HA   sing N N 353 
SER C   O    doub N N 354 
SER C   OXT  sing N N 355 
SER CB  OG   sing N N 356 
SER CB  HB2  sing N N 357 
SER CB  HB3  sing N N 358 
SER OG  HG   sing N N 359 
SER OXT HXT  sing N N 360 
THR N   CA   sing N N 361 
THR N   H    sing N N 362 
THR N   H2   sing N N 363 
THR CA  C    sing N N 364 
THR CA  CB   sing N N 365 
THR CA  HA   sing N N 366 
THR C   O    doub N N 367 
THR C   OXT  sing N N 368 
THR CB  OG1  sing N N 369 
THR CB  CG2  sing N N 370 
THR CB  HB   sing N N 371 
THR OG1 HG1  sing N N 372 
THR CG2 HG21 sing N N 373 
THR CG2 HG22 sing N N 374 
THR CG2 HG23 sing N N 375 
THR OXT HXT  sing N N 376 
TRP N   CA   sing N N 377 
TRP N   H    sing N N 378 
TRP N   H2   sing N N 379 
TRP CA  C    sing N N 380 
TRP CA  CB   sing N N 381 
TRP CA  HA   sing N N 382 
TRP C   O    doub N N 383 
TRP C   OXT  sing N N 384 
TRP CB  CG   sing N N 385 
TRP CB  HB2  sing N N 386 
TRP CB  HB3  sing N N 387 
TRP CG  CD1  doub Y N 388 
TRP CG  CD2  sing Y N 389 
TRP CD1 NE1  sing Y N 390 
TRP CD1 HD1  sing N N 391 
TRP CD2 CE2  doub Y N 392 
TRP CD2 CE3  sing Y N 393 
TRP NE1 CE2  sing Y N 394 
TRP NE1 HE1  sing N N 395 
TRP CE2 CZ2  sing Y N 396 
TRP CE3 CZ3  doub Y N 397 
TRP CE3 HE3  sing N N 398 
TRP CZ2 CH2  doub Y N 399 
TRP CZ2 HZ2  sing N N 400 
TRP CZ3 CH2  sing Y N 401 
TRP CZ3 HZ3  sing N N 402 
TRP CH2 HH2  sing N N 403 
TRP OXT HXT  sing N N 404 
TYR N   CA   sing N N 405 
TYR N   H    sing N N 406 
TYR N   H2   sing N N 407 
TYR CA  C    sing N N 408 
TYR CA  CB   sing N N 409 
TYR CA  HA   sing N N 410 
TYR C   O    doub N N 411 
TYR C   OXT  sing N N 412 
TYR CB  CG   sing N N 413 
TYR CB  HB2  sing N N 414 
TYR CB  HB3  sing N N 415 
TYR CG  CD1  doub Y N 416 
TYR CG  CD2  sing Y N 417 
TYR CD1 CE1  sing Y N 418 
TYR CD1 HD1  sing N N 419 
TYR CD2 CE2  doub Y N 420 
TYR CD2 HD2  sing N N 421 
TYR CE1 CZ   doub Y N 422 
TYR CE1 HE1  sing N N 423 
TYR CE2 CZ   sing Y N 424 
TYR CE2 HE2  sing N N 425 
TYR CZ  OH   sing N N 426 
TYR OH  HH   sing N N 427 
TYR OXT HXT  sing N N 428 
VAL N   CA   sing N N 429 
VAL N   H    sing N N 430 
VAL N   H2   sing N N 431 
VAL CA  C    sing N N 432 
VAL CA  CB   sing N N 433 
VAL CA  HA   sing N N 434 
VAL C   O    doub N N 435 
VAL C   OXT  sing N N 436 
VAL CB  CG1  sing N N 437 
VAL CB  CG2  sing N N 438 
VAL CB  HB   sing N N 439 
VAL CG1 HG11 sing N N 440 
VAL CG1 HG12 sing N N 441 
VAL CG1 HG13 sing N N 442 
VAL CG2 HG21 sing N N 443 
VAL CG2 HG22 sing N N 444 
VAL CG2 HG23 sing N N 445 
VAL OXT HXT  sing N N 446 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                  ZN  
3 '5-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide' E02 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                      MES 
5 'DIMETHYL SULFOXIDE'                                        DMS 
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' 
# 
