data_4Q6E
# 
_entry.id   4Q6E 
# 
_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   4Q6E         pdb_00004q6e 10.2210/pdb4q6e/pdb 
RCSB  RCSB085661   ?            ?                   
WWPDB D_1000085661 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          4Q6D 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        4Q6E 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2014-04-22 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     '4-Amino-substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases.' 
_citation.journal_abbrev            Molecules 
_citation.journal_volume            19 
_citation.page_first                17356 
_citation.page_last                 17380 
_citation.year                      2014 
_citation.journal_id_ASTM           ? 
_citation.country                   CH 
_citation.journal_id_ISSN           1420-3049 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25353386 
_citation.pdbx_database_id_DOI      10.3390/molecules191117356 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rutkauskas, K.'      1  ? 
primary 'Zubriene, A.'        2  ? 
primary 'Tumosiene, I.'       3  ? 
primary 'Kantminiene, K.'     4  ? 
primary 'Kazemekaite, M.'     5  ? 
primary 'Smirnov, A.'         6  ? 
primary 'Kazokaite, J.'       7  ? 
primary 'Morkunaite, V.'      8  ? 
primary 'Capkauskaite, E.'    9  ? 
primary 'Manakova, E.'        10 ? 
primary 'Grazulis, S.'        11 ? 
primary 'Beresnevicius, Z.J.' 12 ? 
primary 'Matulis, D.'         13 ? 
# 
_cell.entry_id           4Q6E 
_cell.length_a           42.237 
_cell.length_b           41.241 
_cell.length_c           72.189 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.300 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4Q6E 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                      29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                  65.409    1   ?       ? ? ? 
3 non-polymer syn BICINE                                                                      163.172   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                        78.133    2   ?       ? ? ? 
5 non-polymer syn '4-{[3-(3,5-dimethyl-1H-pyrazol-1-yl)-3-oxopropyl]amino}benzenesulfonamide' 322.383   1   ?       ? ? ? 
6 water       nat water                                                                       18.015    321 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4Q6E 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                     ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                    ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                  ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                             ? 'C4 H7 N O4'      133.103 
BCN non-polymer         . BICINE                                                                      ? 'C6 H13 N O4'     163.172 
CYS 'L-peptide linking' y CYSTEINE                                                                    ? 'C3 H7 N O2 S'    121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                        ? 'C2 H6 O S'       78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                   ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                             ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                                                     ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                   ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                                                       ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                  ? 'C6 H13 N O2'     131.173 
KR5 non-polymer         . '4-{[3-(3,5-dimethyl-1H-pyrazol-1-yl)-3-oxopropyl]amino}benzenesulfonamide' ? 'C14 H18 N4 O3 S' 322.383 
LEU 'L-peptide linking' y LEUCINE                                                                     ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                                                                      ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                                                                  ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                               ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                                                                     ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                                                                      ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                                                                   ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                  ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                                                                    ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                                                      ? 'C5 H11 N O2'     117.146 
ZN  non-polymer         . 'ZINC ION'                                                                  ? 'Zn 2'            65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4Q6E 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.0 
_exptl_crystal.density_Matthews      2.03 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate, VAPOR DIFFUSION, SITTING DROP, temperature 291K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'PSI PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2014-01-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    
;High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM) 
: Si 311, Si 511
;
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
# 
_reflns.entry_id                     4Q6E 
_reflns.d_resolution_high            1.12 
_reflns.d_resolution_low             41.241 
_reflns.number_all                   ? 
_reflns.number_obs                   85569 
_reflns.pdbx_netI_over_sigmaI        14.400 
_reflns.pdbx_Rsym_value              0.063 
_reflns.pdbx_redundancy              6.500 
_reflns.percent_possible_obs         92.800 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        8.915 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.12 1.18  ? 46827 ? 0.193 3.6  0.193 ? 5.20 ? 8952  66.70 1  1 
1.18 1.25  ? 67542 ? 0.167 4.2  0.167 ? 5.90 ? 11389 89.90 2  1 
1.25 1.34  ? 77973 ? 0.130 5.5  0.130 ? 6.60 ? 11779 98.80 3  1 
1.34 1.45  ? 72218 ? 0.095 7.5  0.095 ? 6.60 ? 10928 98.50 4  1 
1.45 1.59  ? 67407 ? 0.072 9.5  0.072 ? 6.70 ? 10116 98.60 5  1 
1.59 1.77  ? 61068 ? 0.062 10.7 0.062 ? 6.70 ? 9078  97.90 6  1 
1.77 2.05  ? 56141 ? 0.058 10.8 0.058 ? 6.90 ? 8098  99.00 7  1 
2.05 2.51  ? 47242 ? 0.057 11.5 0.057 ? 6.80 ? 6901  99.20 8  1 
2.51 3.55  ? 37006 ? 0.058 10.0 0.058 ? 6.90 ? 5333  98.80 9  1 
3.55 41.24 ? 19798 ? 0.061 8.2  0.061 ? 6.60 ? 2995  98.40 10 1 
# 
_refine.entry_id                                 4Q6E 
_refine.ls_d_res_high                            1.120 
_refine.ls_d_res_low                             39.880 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    92.610 
_refine.ls_number_reflns_obs                     85523 
_refine.ls_number_reflns_all                     85523 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          0.133 
_refine.ls_R_factor_obs                          0.133 
_refine.ls_R_factor_R_work                       0.130 
_refine.ls_wR_factor_R_work                      0.134 
_refine.ls_R_factor_R_free                       0.158 
_refine.ls_wR_factor_R_free                      0.168 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  8572 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               15.119 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.030 
_refine.aniso_B[2][2]                            -0.190 
_refine.aniso_B[3][3]                            0.160 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.120 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.978 
_refine.correlation_coeff_Fo_to_Fc_free          0.971 
_refine.overall_SU_R_Cruickshank_DPI             0.034 
_refine.overall_SU_R_free                        0.034 
_refine.pdbx_overall_ESU_R                       0.034 
_refine.pdbx_overall_ESU_R_Free                  0.034 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          MR 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.936 
_refine.B_iso_max                                74.68 
_refine.B_iso_min                                5.85 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             321 
_refine_hist.number_atoms_total               2412 
_refine_hist.d_res_high                       1.120 
_refine_hist.d_res_low                        39.880 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       2309 0.024  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3155 2.362  1.968  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 292  6.765  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 96   32.815 24.375 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 374  11.663 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 7    20.828 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         327  0.177  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1799 0.015  0.021  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr     2309 8.457  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free      322  17.834 5.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded    2230 8.400  5.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.121 
_refine_ls_shell.d_res_low                        1.151 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               54.540 
_refine_ls_shell.number_reflns_R_work             3349 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.132 
_refine_ls_shell.R_factor_R_free                  0.165 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             348 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                3697 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4Q6E 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 4-{[3-(3,5-Dimethyl-1H-pyrazol-1-yl)-3-oxopropyl]amino}benzene-1-sulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4Q6E 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F KR5 . N1 ? ? A ZN  301 A KR5 305 1_555 ? ? ? ? ? ? ? 1.934 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.12 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 11.40 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A BCN 302 ? 9  'BINDING SITE FOR RESIDUE BCN A 302' 
AC3 Software A DMS 303 ? 5  'BINDING SITE FOR RESIDUE DMS A 303' 
AC4 Software A DMS 304 ? 5  'BINDING SITE FOR RESIDUE DMS A 304' 
AC5 Software A KR5 305 ? 12 'BINDING SITE FOR RESIDUE KR5 A 305' 
# 
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  KR5 F .   ? KR5 A 305 . ? 1_555 ? 
5  AC2 9  LYS A 148 ? LYS A 149 . ? 1_555 ? 
6  AC2 9  LYS A 212 ? LYS A 213 . ? 1_555 ? 
7  AC2 9  GLU A 213 ? GLU A 214 . ? 1_555 ? 
8  AC2 9  PRO A 214 ? PRO A 215 . ? 1_555 ? 
9  AC2 9  HOH G .   ? HOH A 445 . ? 1_555 ? 
10 AC2 9  HOH G .   ? HOH A 473 . ? 1_555 ? 
11 AC2 9  HOH G .   ? HOH A 474 . ? 1_555 ? 
12 AC2 9  HOH G .   ? HOH A 541 . ? 1_555 ? 
13 AC2 9  HOH G .   ? HOH A 603 . ? 1_555 ? 
14 AC3 5  ILE A 91  ? ILE A 91  . ? 1_555 ? 
15 AC3 5  GLN A 92  ? GLN A 92  . ? 1_555 ? 
16 AC3 5  PHE A 130 ? PHE A 131 . ? 1_555 ? 
17 AC3 5  KR5 F .   ? KR5 A 305 . ? 1_555 ? 
18 AC3 5  HOH G .   ? HOH A 443 . ? 1_555 ? 
19 AC4 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
20 AC4 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
21 AC4 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
22 AC4 5  PRO A 246 ? PRO A 247 . ? 1_555 ? 
23 AC4 5  HOH G .   ? HOH A 616 . ? 1_555 ? 
24 AC5 12 HIS A 94  ? HIS A 94  . ? 1_555 ? 
25 AC5 12 HIS A 96  ? HIS A 96  . ? 1_555 ? 
26 AC5 12 HIS A 119 ? HIS A 119 . ? 1_555 ? 
27 AC5 12 PHE A 130 ? PHE A 131 . ? 1_555 ? 
28 AC5 12 LEU A 197 ? LEU A 198 . ? 1_555 ? 
29 AC5 12 THR A 198 ? THR A 199 . ? 1_555 ? 
30 AC5 12 THR A 199 ? THR A 200 . ? 1_555 ? 
31 AC5 12 PRO A 201 ? PRO A 202 . ? 1_555 ? 
32 AC5 12 TRP A 208 ? TRP A 209 . ? 1_555 ? 
33 AC5 12 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
34 AC5 12 DMS D .   ? DMS A 303 . ? 1_555 ? 
35 AC5 12 HOH G .   ? HOH A 415 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4Q6E 
_atom_sites.fract_transf_matrix[1][1]   0.023676 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006035 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024248 
_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]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 11.084  -0.437  8.140   1.00   25.60 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 9.890   0.127   8.786   1.00   23.29 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.184   -1.011  9.518   1.00   19.95 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.364   -2.188  9.209   1.00   20.17 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 8.973   0.889   7.803   1.00   25.56 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 8.483   2.151   8.420   1.00   40.58 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 7.214   2.554   8.348   1.00   42.71 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 9.152   3.071   9.243   0.0000 59.89 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 7.072   3.717   9.029   0.0000 69.88 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 8.265   4.025   9.586   0.0000 71.58 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.338   -0.672  10.447  1.00   16.41 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.648   -1.653  11.281  1.00   13.12 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.625   -2.423  10.486  1.00   12.21 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.114   -1.926  9.465   1.00   14.10 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.015   -0.900  12.474  1.00   12.58 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.864   -0.059  12.091  1.00   11.27 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.869   1.274   11.790  1.00   12.95 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.483   -0.470  11.991  1.00   10.75 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.630   1.738   11.513  1.00   13.63 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.740   0.675   11.617  1.00   11.86 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.817   -1.685  12.241  1.00   11.72 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.361   0.635   11.475  1.00   12.60 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.427   -1.726  12.030  1.00   11.91 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.734   -0.573  11.658  1.00   12.80 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.321   -3.628  10.973  1.00   11.69 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.299   -4.426  10.320  1.00   12.17 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 4.970   -5.599  11.200  1.00   11.43 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.019   -5.475  12.423  1.00   12.03 ? 6   GLY A O   1 
ATOM   29   N  N   A TYR A 1 7   ? 4.563   -6.641  10.432  0.50   10.47 ? 7   TYR A N   1 
ATOM   30   N  N   B TYR A 1 7   ? 4.751   -6.782  10.677  0.50   14.29 ? 7   TYR A N   1 
ATOM   31   C  CA  A TYR A 1 7   ? 4.115   -7.938  10.971  0.50   9.72  ? 7   TYR A CA  1 
ATOM   32   C  CA  B TYR A 1 7   ? 4.444   -7.890  11.572  0.50   13.59 ? 7   TYR A CA  1 
ATOM   33   C  C   A TYR A 1 7   ? 4.924   -9.132  10.431  0.50   11.26 ? 7   TYR A C   1 
ATOM   34   C  C   B TYR A 1 7   ? 5.292   -8.998  11.004  0.50   20.58 ? 7   TYR A C   1 
ATOM   35   O  O   A TYR A 1 7   ? 4.441   -10.276 10.425  0.50   11.70 ? 7   TYR A O   1 
ATOM   36   O  O   B TYR A 1 7   ? 5.137   -10.060 11.575  0.50   22.65 ? 7   TYR A O   1 
ATOM   37   C  CB  A TYR A 1 7   ? 2.616   -8.112  10.886  0.50   8.69  ? 7   TYR A CB  1 
ATOM   38   C  CB  B TYR A 1 7   ? 2.952   -8.318  11.468  0.50   13.08 ? 7   TYR A CB  1 
ATOM   39   C  CG  A TYR A 1 7   ? 1.825   -7.012  11.551  0.50   7.64  ? 7   TYR A CG  1 
ATOM   40   C  CG  B TYR A 1 7   ? 2.035   -7.298  11.994  0.50   10.32 ? 7   TYR A CG  1 
ATOM   41   C  CD1 A TYR A 1 7   ? 1.453   -7.090  12.911  0.50   8.15  ? 7   TYR A CD1 1 
ATOM   42   C  CD1 B TYR A 1 7   ? 1.654   -7.310  13.346  0.50   8.99  ? 7   TYR A CD1 1 
ATOM   43   C  CD2 A TYR A 1 7   ? 1.338   -5.942  10.794  0.50   7.33  ? 7   TYR A CD2 1 
ATOM   44   C  CD2 B TYR A 1 7   ? 1.576   -6.299  11.158  0.50   10.79 ? 7   TYR A CD2 1 
ATOM   45   C  CE1 A TYR A 1 7   ? 0.652   -6.098  13.466  0.50   7.03  ? 7   TYR A CE1 1 
ATOM   46   C  CE1 B TYR A 1 7   ? 0.759   -6.323  13.797  0.50   9.25  ? 7   TYR A CE1 1 
ATOM   47   C  CE2 A TYR A 1 7   ? 0.549   -4.946  11.353  0.50   8.25  ? 7   TYR A CE2 1 
ATOM   48   C  CE2 B TYR A 1 7   ? 0.733   -5.331  11.609  0.50   10.38 ? 7   TYR A CE2 1 
ATOM   49   C  CZ  A TYR A 1 7   ? 0.179   -5.062  12.674  0.50   7.68  ? 7   TYR A CZ  1 
ATOM   50   C  CZ  B TYR A 1 7   ? 0.332   -5.345  12.949  0.50   8.75  ? 7   TYR A CZ  1 
ATOM   51   O  OH  A TYR A 1 7   ? -0.643  -4.102  13.163  0.50   8.25  ? 7   TYR A OH  1 
ATOM   52   O  OH  B TYR A 1 7   ? -0.535  -4.382  13.356  0.50   10.04 ? 7   TYR A OH  1 
ATOM   53   N  N   A GLY A 1 8   ? 6.259   -8.904  10.317  0.50   18.22 ? 8   GLY A N   1 
ATOM   54   N  N   B GLY A 1 8   ? 6.007   -8.811  9.822   0.50   13.19 ? 8   GLY A N   1 
ATOM   55   C  CA  A GLY A 1 8   ? 7.195   -9.963  9.956   0.50   23.85 ? 8   GLY A CA  1 
ATOM   56   C  CA  B GLY A 1 8   ? 6.881   -9.850  9.174   0.50   12.98 ? 8   GLY A CA  1 
ATOM   57   C  C   A GLY A 1 8   ? 8.172   -10.377 11.026  0.50   25.67 ? 8   GLY A C   1 
ATOM   58   C  C   B GLY A 1 8   ? 7.753   -10.587 10.162  0.50   12.24 ? 8   GLY A C   1 
ATOM   59   O  O   A GLY A 1 8   ? 8.313   -9.825  12.137  0.50   22.88 ? 8   GLY A O   1 
ATOM   60   O  O   B GLY A 1 8   ? 7.624   -10.469 11.383  0.50   11.34 ? 8   GLY A O   1 
ATOM   61   N  N   A LYS A 1 9   ? 8.947   -11.352 10.626  0.50   29.47 ? 9   LYS A N   1 
ATOM   62   N  N   B LYS A 1 9   ? 8.722   -11.292 9.578   0.50   11.61 ? 9   LYS A N   1 
ATOM   63   C  CA  A LYS A 1 9   ? 9.803   -11.986 11.555  0.50   28.45 ? 9   LYS A CA  1 
ATOM   64   C  CA  B LYS A 1 9   ? 9.661   -12.124 10.392  0.50   11.24 ? 9   LYS A CA  1 
ATOM   65   C  C   A LYS A 1 9   ? 10.904  -11.033 11.986  0.50   26.26 ? 9   LYS A C   1 
ATOM   66   C  C   B LYS A 1 9   ? 10.685  -11.326 11.140  0.50   10.72 ? 9   LYS A C   1 
ATOM   67   O  O   A LYS A 1 9   ? 11.500  -11.292 12.983  0.50   39.23 ? 9   LYS A O   1 
ATOM   68   O  O   B LYS A 1 9   ? 11.323  -11.912 12.027  0.50   12.50 ? 9   LYS A O   1 
ATOM   69   C  CB  A LYS A 1 9   ? 10.378  -13.311 10.988  0.50   36.74 ? 9   LYS A CB  1 
ATOM   70   C  CB  B LYS A 1 9   ? 10.379  -13.146 9.538   0.50   16.88 ? 9   LYS A CB  1 
ATOM   71   C  CG  A LYS A 1 9   ? 10.362  -13.470 9.463   0.50   38.74 ? 9   LYS A CG  1 
ATOM   72   C  CG  B LYS A 1 9   ? 9.502   -14.145 8.824   0.50   24.79 ? 9   LYS A CG  1 
ATOM   73   C  CD  A LYS A 1 9   ? 9.317   -14.465 8.931   0.50   40.01 ? 9   LYS A CD  1 
ATOM   74   C  CD  B LYS A 1 9   ? 10.465  -15.148 8.170   0.50   24.20 ? 9   LYS A CD  1 
ATOM   75   C  CE  A LYS A 1 9   ? 9.689   -14.918 7.502   0.50   28.92 ? 9   LYS A CE  1 
ATOM   76   C  CE  B LYS A 1 9   ? 9.897   -16.083 7.104   0.50   22.26 ? 9   LYS A CE  1 
ATOM   77   N  NZ  A LYS A 1 9   ? 8.679   -15.583 6.600   0.50   41.18 ? 9   LYS A NZ  1 
ATOM   78   N  NZ  B LYS A 1 9   ? 8.551   -16.510 7.533   0.50   24.83 ? 9   LYS A NZ  1 
ATOM   79   N  N   A HIS A 1 10  ? 11.194  -9.952  11.246  0.50   28.32 ? 10  HIS A N   1 
ATOM   80   N  N   B HIS A 1 10  ? 10.892  -10.066 10.742  0.50   11.84 ? 10  HIS A N   1 
ATOM   81   C  CA  A HIS A 1 10  ? 12.277  -8.997  11.585  0.50   22.57 ? 10  HIS A CA  1 
ATOM   82   C  CA  B HIS A 1 10  ? 11.982  -9.241  11.219  0.50   12.60 ? 10  HIS A CA  1 
ATOM   83   C  C   A HIS A 1 10  ? 11.746  -7.609  11.813  0.50   18.56 ? 10  HIS A C   1 
ATOM   84   C  C   B HIS A 1 10  ? 11.615  -7.918  11.789  0.50   12.43 ? 10  HIS A C   1 
ATOM   85   O  O   A HIS A 1 10  ? 12.597  -6.704  12.168  0.50   15.45 ? 10  HIS A O   1 
ATOM   86   O  O   B HIS A 1 10  ? 12.443  -7.366  12.395  0.50   9.60  ? 10  HIS A O   1 
ATOM   87   C  CB  A HIS A 1 10  ? 13.429  -8.991  10.530  0.50   20.77 ? 10  HIS A CB  1 
ATOM   88   C  CB  B HIS A 1 10  ? 13.009  -9.053  10.055  0.50   13.60 ? 10  HIS A CB  1 
ATOM   89   C  CG  A HIS A 1 10  ? 14.003  -10.368 10.312  0.50   24.09 ? 10  HIS A CG  1 
ATOM   90   C  CG  B HIS A 1 10  ? 13.551  -10.360 9.599   0.50   12.26 ? 10  HIS A CG  1 
ATOM   91   N  ND1 A HIS A 1 10  ? 15.046  -10.844 11.016  0.50   26.10 ? 10  HIS A ND1 1 
ATOM   92   N  ND1 B HIS A 1 10  ? 14.419  -11.060 10.338  0.50   13.74 ? 10  HIS A ND1 1 
ATOM   93   C  CD2 A HIS A 1 10  ? 13.581  -11.416 9.490   0.50   27.19 ? 10  HIS A CD2 1 
ATOM   94   C  CD2 B HIS A 1 10  ? 13.216  -11.158 8.513   0.50   15.26 ? 10  HIS A CD2 1 
ATOM   95   C  CE1 A HIS A 1 10  ? 15.313  -12.107 10.641  0.50   22.10 ? 10  HIS A CE1 1 
ATOM   96   C  CE1 B HIS A 1 10  ? 14.686  -12.224 9.728   0.50   12.37 ? 10  HIS A CE1 1 
ATOM   97   N  NE2 A HIS A 1 10  ? 14.410  -12.457 9.701   0.50   32.77 ? 10  HIS A NE2 1 
ATOM   98   N  NE2 B HIS A 1 10  ? 13.945  -12.285 8.611   0.50   14.69 ? 10  HIS A NE2 1 
ATOM   99   N  N   . ASN A 1 11  ? 10.407  -7.402  11.648  1.00   14.45 ? 11  ASN A N   1 
ATOM   100  C  CA  . ASN A 1 11  ? 9.985   -6.075  11.988  1.00   13.48 ? 11  ASN A CA  1 
ATOM   101  C  C   . ASN A 1 11  ? 8.673   -6.016  12.778  1.00   12.63 ? 11  ASN A C   1 
ATOM   102  O  O   . ASN A 1 11  ? 8.034   -4.965  12.856  1.00   13.27 ? 11  ASN A O   1 
ATOM   103  C  CB  . ASN A 1 11  ? 9.831   -5.269  10.766  1.00   13.23 ? 11  ASN A CB  1 
ATOM   104  C  CG  . ASN A 1 11  ? 8.776   -5.814  9.825   1.00   14.20 ? 11  ASN A CG  1 
ATOM   105  O  OD1 . ASN A 1 11  ? 8.148   -6.852  10.091  1.00   17.09 ? 11  ASN A OD1 1 
ATOM   106  N  ND2 . ASN A 1 11  ? 8.515   -5.111  8.738   1.00   16.82 ? 11  ASN A ND2 1 
ATOM   107  N  N   . GLY A 1 12  ? 8.373   -7.156  13.393  1.00   13.48 ? 12  GLY A N   1 
ATOM   108  C  CA  . GLY A 1 12  ? 7.072   -7.316  14.090  1.00   13.39 ? 12  GLY A CA  1 
ATOM   109  C  C   . GLY A 1 12  ? 7.038   -6.751  15.461  1.00   11.68 ? 12  GLY A C   1 
ATOM   110  O  O   . GLY A 1 12  ? 7.982   -6.062  15.928  1.00   12.52 ? 12  GLY A O   1 
ATOM   111  N  N   . PRO A 1 13  ? 5.949   -6.966  16.196  1.00   10.81 ? 13  PRO A N   1 
ATOM   112  C  CA  . PRO A 1 13  ? 5.694   -6.341  17.489  1.00   10.79 ? 13  PRO A CA  1 
ATOM   113  C  C   . PRO A 1 13  ? 6.819   -6.364  18.483  1.00   10.65 ? 13  PRO A C   1 
ATOM   114  O  O   . PRO A 1 13  ? 6.997   -5.392  19.248  1.00   11.29 ? 13  PRO A O   1 
ATOM   115  C  CB  . PRO A 1 13  ? 4.485   -7.106  17.996  1.00   11.76 ? 13  PRO A CB  1 
ATOM   116  C  CG  . PRO A 1 13  ? 3.695   -7.419  16.748  1.00   11.59 ? 13  PRO A CG  1 
ATOM   117  C  CD  . PRO A 1 13  ? 4.743   -7.691  15.713  1.00   12.32 ? 13  PRO A CD  1 
ATOM   118  N  N   . GLU A 1 14  ? 7.597   -7.441  18.519  1.00   11.83 ? 14  GLU A N   1 
ATOM   119  C  CA  . GLU A 1 14  ? 8.671   -7.490  19.465  1.00   13.63 ? 14  GLU A CA  1 
ATOM   120  C  C   . GLU A 1 14  ? 9.834   -6.527  19.173  1.00   12.49 ? 14  GLU A C   1 
ATOM   121  O  O   . GLU A 1 14  ? 10.718  -6.320  20.038  1.00   13.93 ? 14  GLU A O   1 
ATOM   122  C  CB  . GLU A 1 14  ? 9.200   -8.925  19.607  1.00   16.65 ? 14  GLU A CB  1 
ATOM   123  C  CG  . GLU A 1 14  ? 9.780   -9.564  18.338  1.00   17.01 ? 14  GLU A CG  1 
ATOM   124  C  CD  . GLU A 1 14  ? 8.956   -10.087 17.138  1.00   18.66 ? 14  GLU A CD  1 
ATOM   125  O  OE1 . GLU A 1 14  ? 7.788   -9.674  16.993  1.00   18.88 ? 14  GLU A OE1 1 
ATOM   126  O  OE2 . GLU A 1 14  ? 9.491   -10.903 16.360  1.00   24.91 ? 14  GLU A OE2 1 
ATOM   127  N  N   . HIS A 1 15  ? 9.844   -5.951  17.997  1.00   11.32 ? 15  HIS A N   1 
ATOM   128  C  CA  . HIS A 1 15  ? 10.855  -4.968  17.587  1.00   12.13 ? 15  HIS A CA  1 
ATOM   129  C  C   . HIS A 1 15  ? 10.434  -3.556  17.725  1.00   11.35 ? 15  HIS A C   1 
ATOM   130  O  O   . HIS A 1 15  ? 11.267  -2.647  17.657  1.00   11.88 ? 15  HIS A O   1 
ATOM   131  C  CB  . HIS A 1 15  ? 11.236  -5.190  16.138  1.00   12.93 ? 15  HIS A CB  1 
ATOM   132  C  CG  . HIS A 1 15  ? 11.934  -6.488  15.919  1.00   13.86 ? 15  HIS A CG  1 
ATOM   133  N  ND1 . HIS A 1 15  ? 13.279  -6.655  16.103  1.00   16.20 ? 15  HIS A ND1 1 
ATOM   134  C  CD2 . HIS A 1 15  ? 11.449  -7.701  15.477  1.00   15.56 ? 15  HIS A CD2 1 
ATOM   135  C  CE1 . HIS A 1 15  ? 13.547  -7.949  15.893  1.00   18.45 ? 15  HIS A CE1 1 
ATOM   136  N  NE2 . HIS A 1 15  ? 12.479  -8.579  15.470  1.00   18.92 ? 15  HIS A NE2 1 
ATOM   137  N  N   . TRP A 1 16  ? 9.120   -3.288  17.892  1.00   10.31 ? 16  TRP A N   1 
ATOM   138  C  CA  . TRP A 1 16  ? 8.615   -1.926  17.796  1.00   9.40  ? 16  TRP A CA  1 
ATOM   139  C  C   . TRP A 1 16  ? 9.202   -0.956  18.822  1.00   9.39  ? 16  TRP A C   1 
ATOM   140  O  O   . TRP A 1 16  ? 9.300   0.213   18.563  1.00   10.24 ? 16  TRP A O   1 
ATOM   141  C  CB  . TRP A 1 16  ? 7.092   -1.951  17.889  1.00   9.46  ? 16  TRP A CB  1 
ATOM   142  C  CG  . TRP A 1 16  ? 6.402   -2.655  16.748  1.00   8.81  ? 16  TRP A CG  1 
ATOM   143  C  CD1 . TRP A 1 16  ? 6.921   -3.115  15.590  1.00   10.04 ? 16  TRP A CD1 1 
ATOM   144  C  CD2 . TRP A 1 16  ? 4.984   -2.931  16.674  1.00   8.70  ? 16  TRP A CD2 1 
ATOM   145  N  NE1 . TRP A 1 16  ? 5.965   -3.690  14.795  1.00   9.70  ? 16  TRP A NE1 1 
ATOM   146  C  CE2 . TRP A 1 16  ? 4.745   -3.567  15.434  1.00   8.92  ? 16  TRP A CE2 1 
ATOM   147  C  CE3 . TRP A 1 16  ? 3.913   -2.712  17.572  1.00   8.93  ? 16  TRP A CE3 1 
ATOM   148  C  CZ2 . TRP A 1 16  ? 3.458   -4.002  15.059  1.00   8.98  ? 16  TRP A CZ2 1 
ATOM   149  C  CZ3 . TRP A 1 16  ? 2.659   -3.114  17.186  1.00   9.37  ? 16  TRP A CZ3 1 
ATOM   150  C  CH2 . TRP A 1 16  ? 2.439   -3.741  15.955  1.00   9.03  ? 16  TRP A CH2 1 
ATOM   151  N  N   . HIS A 1 17  ? 9.546   -1.495  19.995  1.00   9.55  ? 17  HIS A N   1 
ATOM   152  C  CA  . HIS A 1 17  ? 10.049  -0.631  21.024  1.00   10.25 ? 17  HIS A CA  1 
ATOM   153  C  C   . HIS A 1 17  ? 11.329  0.099   20.657  1.00   11.29 ? 17  HIS A C   1 
ATOM   154  O  O   . HIS A 1 17  ? 11.592  1.158   21.270  1.00   11.87 ? 17  HIS A O   1 
ATOM   155  C  CB  . HIS A 1 17  ? 10.329  -1.411  22.298  1.00   11.44 ? 17  HIS A CB  1 
ATOM   156  C  CG  . HIS A 1 17  ? 11.551  -2.289  22.198  1.00   13.19 ? 17  HIS A CG  1 
ATOM   157  N  ND1 . HIS A 1 17  ? 12.775  -1.920  22.677  1.00   16.38 ? 17  HIS A ND1 1 
ATOM   158  C  CD2 . HIS A 1 17  ? 11.689  -3.484  21.602  1.00   14.09 ? 17  HIS A CD2 1 
ATOM   159  C  CE1 . HIS A 1 17  ? 13.596  -2.884  22.431  1.00   15.87 ? 17  HIS A CE1 1 
ATOM   160  N  NE2 . HIS A 1 17  ? 13.016  -3.860  21.791  1.00   16.13 ? 17  HIS A NE2 1 
ATOM   161  N  N   . LYS A 1 18  ? 12.087  -0.339  19.661  1.00   11.62 ? 18  LYS A N   1 
ATOM   162  C  CA  . LYS A 1 18  ? 13.337  0.338   19.325  1.00   13.13 ? 18  LYS A CA  1 
ATOM   163  C  C   . LYS A 1 18  ? 13.038  1.670   18.668  1.00   13.63 ? 18  LYS A C   1 
ATOM   164  O  O   . LYS A 1 18  ? 13.717  2.664   18.969  1.00   20.06 ? 18  LYS A O   1 
ATOM   165  C  CB  . LYS A 1 18  ? 14.140  -0.550  18.412  1.00   13.78 ? 18  LYS A CB  1 
ATOM   166  C  CG  . LYS A 1 18  ? 14.723  -1.735  19.139  1.00   15.03 ? 18  LYS A CG  1 
ATOM   167  C  CD  . LYS A 1 18  ? 15.479  -2.706  18.215  1.00   14.77 ? 18  LYS A CD  1 
ATOM   168  C  CE  . LYS A 1 18  ? 14.484  -3.676  17.596  1.00   14.58 ? 18  LYS A CE  1 
ATOM   169  N  NZ  . LYS A 1 18  ? 15.157  -4.550  16.553  1.00   14.69 ? 18  LYS A NZ  1 
ATOM   170  N  N   . ASP A 1 19  ? 12.010  1.766   17.831  1.00   12.83 ? 19  ASP A N   1 
ATOM   171  C  CA  . ASP A 1 19  ? 11.613  3.035   17.280  1.00   14.34 ? 19  ASP A CA  1 
ATOM   172  C  C   . ASP A 1 19  ? 10.564  3.751   18.078  1.00   12.76 ? 19  ASP A C   1 
ATOM   173  O  O   . ASP A 1 19  ? 10.446  4.962   17.930  1.00   14.00 ? 19  ASP A O   1 
ATOM   174  C  CB  . ASP A 1 19  ? 11.088  2.835   15.857  1.00   16.25 ? 19  ASP A CB  1 
ATOM   175  C  CG  . ASP A 1 19  ? 12.185  2.904   14.797  1.00   23.36 ? 19  ASP A CG  1 
ATOM   176  O  OD1 . ASP A 1 19  ? 13.215  3.548   14.976  1.00   26.94 ? 19  ASP A OD1 1 
ATOM   177  O  OD2 . ASP A 1 19  ? 11.962  2.355   13.729  1.00   35.44 ? 19  ASP A OD2 1 
ATOM   178  N  N   . PHE A 1 20  ? 9.802   3.037   18.888  1.00   11.47 ? 20  PHE A N   1 
ATOM   179  C  CA  . PHE A 1 20  ? 8.684   3.576   19.630  1.00   10.74 ? 20  PHE A CA  1 
ATOM   180  C  C   . PHE A 1 20  ? 8.788   3.098   21.067  1.00   10.82 ? 20  PHE A C   1 
ATOM   181  O  O   . PHE A 1 20  ? 8.138   2.126   21.446  1.00   10.83 ? 20  PHE A O   1 
ATOM   182  C  CB  . PHE A 1 20  ? 7.362   3.123   19.006  1.00   11.13 ? 20  PHE A CB  1 
ATOM   183  C  CG  . PHE A 1 20  ? 7.254   3.482   17.556  1.00   11.50 ? 20  PHE A CG  1 
ATOM   184  C  CD1 . PHE A 1 20  ? 6.895   4.772   17.199  1.00   14.92 ? 20  PHE A CD1 1 
ATOM   185  C  CD2 . PHE A 1 20  ? 7.592   2.575   16.587  1.00   13.38 ? 20  PHE A CD2 1 
ATOM   186  C  CE1 . PHE A 1 20  ? 6.891   5.109   15.836  1.00   15.99 ? 20  PHE A CE1 1 
ATOM   187  C  CE2 . PHE A 1 20  ? 7.630   2.907   15.241  1.00   15.74 ? 20  PHE A CE2 1 
ATOM   188  C  CZ  . PHE A 1 20  ? 7.235   4.181   14.873  1.00   15.41 ? 20  PHE A CZ  1 
ATOM   189  N  N   A PRO A 1 21  ? 9.634   3.710   21.916  0.50   11.34 ? 21  PRO A N   1 
ATOM   190  N  N   B PRO A 1 21  ? 9.648   3.764   21.858  0.50   11.99 ? 21  PRO A N   1 
ATOM   191  C  CA  A PRO A 1 21  ? 9.859   3.039   23.211  0.50   12.22 ? 21  PRO A CA  1 
ATOM   192  C  CA  B PRO A 1 21  ? 9.893   3.349   23.225  0.50   11.94 ? 21  PRO A CA  1 
ATOM   193  C  C   A PRO A 1 21  ? 8.639   3.127   24.198  0.50   11.39 ? 21  PRO A C   1 
ATOM   194  C  C   B PRO A 1 21  ? 8.665   3.108   24.064  0.50   10.72 ? 21  PRO A C   1 
ATOM   195  O  O   A PRO A 1 21  ? 8.632   2.532   25.295  0.50   10.90 ? 21  PRO A O   1 
ATOM   196  O  O   B PRO A 1 21  ? 8.691   2.217   24.902  0.50   9.17  ? 21  PRO A O   1 
ATOM   197  C  CB  A PRO A 1 21  ? 11.076  3.819   23.765  0.50   12.09 ? 21  PRO A CB  1 
ATOM   198  C  CB  B PRO A 1 21  ? 10.831  4.465   23.793  0.50   11.71 ? 21  PRO A CB  1 
ATOM   199  C  CG  A PRO A 1 21  ? 10.883  5.240   23.150  0.50   13.00 ? 21  PRO A CG  1 
ATOM   200  C  CG  B PRO A 1 21  ? 11.674  4.730   22.547  0.50   17.98 ? 21  PRO A CG  1 
ATOM   201  C  CD  A PRO A 1 21  ? 10.477  4.928   21.737  0.50   11.25 ? 21  PRO A CD  1 
ATOM   202  C  CD  B PRO A 1 21  ? 10.723  4.655   21.351  0.50   13.12 ? 21  PRO A CD  1 
ATOM   203  N  N   . ILE A 1 22  ? 7.598   3.885   23.817  1.00   10.89 ? 22  ILE A N   1 
ATOM   204  C  CA  . ILE A 1 22  ? 6.295   3.802   24.568  1.00   10.23 ? 22  ILE A CA  1 
ATOM   205  C  C   . ILE A 1 22  ? 5.739   2.381   24.429  1.00   9.92  ? 22  ILE A C   1 
ATOM   206  O  O   . ILE A 1 22  ? 4.812   2.037   25.203  1.00   10.51 ? 22  ILE A O   1 
ATOM   207  C  CB  . ILE A 1 22  ? 5.325   4.875   24.070  1.00   10.59 ? 22  ILE A CB  1 
ATOM   208  C  CG1 . ILE A 1 22  ? 4.269   5.194   25.099  1.00   11.65 ? 22  ILE A CG1 1 
ATOM   209  C  CG2 . ILE A 1 22  ? 4.741   4.488   22.706  1.00   10.87 ? 22  ILE A CG2 1 
ATOM   210  C  CD1 . ILE A 1 22  ? 3.367   6.320   24.680  1.00   15.99 ? 22  ILE A CD1 1 
ATOM   211  N  N   . ALA A 1 23  ? 6.241   1.550   23.548  1.00   9.77  ? 23  ALA A N   1 
ATOM   212  C  CA  . ALA A 1 23  ? 5.807   0.176   23.432  1.00   10.09 ? 23  ALA A CA  1 
ATOM   213  C  C   . ALA A 1 23  ? 5.897   -0.554  24.738  1.00   10.99 ? 23  ALA A C   1 
ATOM   214  O  O   . ALA A 1 23  ? 5.191   -1.563  24.922  1.00   11.49 ? 23  ALA A O   1 
ATOM   215  C  CB  . ALA A 1 23  ? 6.615   -0.587  22.386  1.00   10.76 ? 23  ALA A CB  1 
ATOM   216  N  N   . LYS A 1 24  ? 6.843   -0.137  25.621  1.00   11.16 ? 24  LYS A N   1 
ATOM   217  C  CA  . LYS A 1 24  ? 7.020   -0.763  26.926  1.00   12.07 ? 24  LYS A CA  1 
ATOM   218  C  C   . LYS A 1 24  ? 6.402   0.124   27.995  1.00   13.34 ? 24  LYS A C   1 
ATOM   219  O  O   . LYS A 1 24  ? 6.792   0.017   29.178  1.00   14.74 ? 24  LYS A O   1 
ATOM   220  C  CB  . LYS A 1 24  ? 8.499   -1.016  27.243  1.00   14.86 ? 24  LYS A CB  1 
ATOM   221  C  CG  . LYS A 1 24  ? 9.104   -2.009  26.298  1.00   15.60 ? 24  LYS A CG  1 
ATOM   222  C  CD  . LYS A 1 24  ? 10.551  -2.297  26.691  1.00   20.01 ? 24  LYS A CD  1 
ATOM   223  C  CE  . LYS A 1 24  ? 11.278  -3.181  25.695  1.00   24.07 ? 24  LYS A CE  1 
ATOM   224  N  NZ  . LYS A 1 24  ? 10.926  -4.583  25.947  1.00   29.20 ? 24  LYS A NZ  1 
ATOM   225  N  N   . GLY A 1 25  ? 5.403   0.962   27.656  1.00   12.24 ? 25  GLY A N   1 
ATOM   226  C  CA  . GLY A 1 25  ? 4.780   1.895   28.607  1.00   13.68 ? 25  GLY A CA  1 
ATOM   227  C  C   . GLY A 1 25  ? 3.803   1.290   29.575  1.00   11.17 ? 25  GLY A C   1 
ATOM   228  O  O   . GLY A 1 25  ? 3.635   0.074   29.646  1.00   12.53 ? 25  GLY A O   1 
ATOM   229  N  N   . GLU A 1 26  ? 3.173   2.175   30.312  1.00   11.51 ? 26  GLU A N   1 
ATOM   230  C  CA  . GLU A 1 26  ? 2.296   1.807   31.405  1.00   12.27 ? 26  GLU A CA  1 
ATOM   231  C  C   . GLU A 1 26  ? 0.882   1.563   30.964  1.00   10.83 ? 26  GLU A C   1 
ATOM   232  O  O   . GLU A 1 26  ? 0.114   1.062   31.820  1.00   12.57 ? 26  GLU A O   1 
ATOM   233  C  CB  . GLU A 1 26  ? 2.323   2.904   32.476  1.00   15.09 ? 26  GLU A CB  1 
ATOM   234  C  CG  . GLU A 1 26  ? 3.716   3.132   33.035  1.00   17.08 ? 26  GLU A CG  1 
ATOM   235  C  CD  . GLU A 1 26  ? 4.317   1.861   33.647  1.00   23.78 ? 26  GLU A CD  1 
ATOM   236  O  OE1 . GLU A 1 26  ? 3.652   1.220   34.529  1.00   29.51 ? 26  GLU A OE1 1 
ATOM   237  O  OE2 . GLU A 1 26  ? 5.452   1.466   33.265  1.00   30.11 ? 26  GLU A OE2 1 
ATOM   238  N  N   . ARG A 1 27  ? 0.462   1.920   29.755  1.00   9.30  ? 27  ARG A N   1 
ATOM   239  C  CA  . ARG A 1 27  ? -0.936  1.711   29.363  1.00   8.84  ? 27  ARG A CA  1 
ATOM   240  C  C   . ARG A 1 27  ? -1.006  1.242   27.924  1.00   8.10  ? 27  ARG A C   1 
ATOM   241  O  O   . ARG A 1 27  ? -1.756  1.827   27.109  1.00   8.41  ? 27  ARG A O   1 
ATOM   242  C  CB  . ARG A 1 27  ? -1.851  2.913   29.671  1.00   12.51 ? 27  ARG A CB  1 
ATOM   243  C  CG  . ARG A 1 27  ? -1.495  4.236   29.159  1.00   14.93 ? 27  ARG A CG  1 
ATOM   244  C  CD  . ARG A 1 27  ? -2.587  5.313   29.401  1.00   17.45 ? 27  ARG A CD  1 
ATOM   245  N  NE  . ARG A 1 27  ? -3.738  5.270   28.432  1.00   12.35 ? 27  ARG A NE  1 
ATOM   246  C  CZ  . ARG A 1 27  ? -4.681  6.190   28.402  1.00   11.39 ? 27  ARG A CZ  1 
ATOM   247  N  NH1 . ARG A 1 27  ? -4.651  7.280   29.226  1.00   13.69 ? 27  ARG A NH1 1 
ATOM   248  N  NH2 . ARG A 1 27  ? -5.619  6.087   27.572  1.00   13.10 ? 27  ARG A NH2 1 
ATOM   249  N  N   . GLN A 1 28  ? -0.296  0.175   27.629  1.00   7.70  ? 28  GLN A N   1 
ATOM   250  C  CA  . GLN A 1 28  ? -0.278  -0.377  26.287  1.00   7.34  ? 28  GLN A CA  1 
ATOM   251  C  C   . GLN A 1 28  ? -1.464  -1.335  26.036  1.00   6.68  ? 28  GLN A C   1 
ATOM   252  O  O   . GLN A 1 28  ? -1.926  -2.036  26.936  1.00   7.70  ? 28  GLN A O   1 
ATOM   253  C  CB  . GLN A 1 28  ? 1.073   -1.044  26.012  1.00   8.03  ? 28  GLN A CB  1 
ATOM   254  C  CG  . GLN A 1 28  ? 2.200   0.011   25.906  1.00   8.82  ? 28  GLN A CG  1 
ATOM   255  C  CD  . GLN A 1 28  ? 2.078   0.805   24.651  1.00   7.37  ? 28  GLN A CD  1 
ATOM   256  O  OE1 . GLN A 1 28  ? 2.256   0.251   23.553  1.00   8.35  ? 28  GLN A OE1 1 
ATOM   257  N  NE2 . GLN A 1 28  ? 1.742   2.070   24.757  1.00   8.02  ? 28  GLN A NE2 1 
ATOM   258  N  N   . SER A 1 29  ? -1.800  -1.417  24.749  1.00   6.77  ? 29  SER A N   1 
ATOM   259  C  CA  . SER A 1 29  ? -2.874  -2.301  24.272  1.00   6.70  ? 29  SER A CA  1 
ATOM   260  C  C   . SER A 1 29  ? -2.349  -3.178  23.189  1.00   6.31  ? 29  SER A C   1 
ATOM   261  O  O   . SER A 1 29  ? -1.398  -2.829  22.475  1.00   7.28  ? 29  SER A O   1 
ATOM   262  C  CB  . SER A 1 29  ? -4.045  -1.468  23.761  1.00   6.94  ? 29  SER A CB  1 
ATOM   263  O  OG  . SER A 1 29  ? -4.632  -0.718  24.824  1.00   6.87  ? 29  SER A OG  1 
ATOM   264  N  N   . PRO A 1 30  ? -2.989  -4.335  22.908  1.00   6.32  ? 30  PRO A N   1 
ATOM   265  C  CA  . PRO A 1 30  ? -4.180  -4.851  23.630  1.00   6.58  ? 30  PRO A CA  1 
ATOM   266  C  C   . PRO A 1 30  ? -3.770  -5.533  24.928  1.00   6.48  ? 30  PRO A C   1 
ATOM   267  O  O   . PRO A 1 30  ? -2.560  -5.551  25.258  1.00   7.30  ? 30  PRO A O   1 
ATOM   268  C  CB  . PRO A 1 30  ? -4.698  -5.897  22.641  1.00   7.03  ? 30  PRO A CB  1 
ATOM   269  C  CG  . PRO A 1 30  ? -3.437  -6.459  22.017  1.00   7.09  ? 30  PRO A CG  1 
ATOM   270  C  CD  . PRO A 1 30  ? -2.530  -5.243  21.871  1.00   7.11  ? 30  PRO A CD  1 
ATOM   271  N  N   . VAL A 1 31  ? -4.729  -6.064  25.637  1.00   7.07  ? 31  VAL A N   1 
ATOM   272  C  CA  . VAL A 1 31  ? -4.545  -6.829  26.870  1.00   7.30  ? 31  VAL A CA  1 
ATOM   273  C  C   . VAL A 1 31  ? -5.425  -8.066  26.815  1.00   7.37  ? 31  VAL A C   1 
ATOM   274  O  O   . VAL A 1 31  ? -6.424  -8.116  26.069  1.00   8.26  ? 31  VAL A O   1 
ATOM   275  C  CB  . VAL A 1 31  ? -4.848  -5.963  28.117  1.00   8.00  ? 31  VAL A CB  1 
ATOM   276  C  CG1 . VAL A 1 31  ? -3.932  -4.793  28.196  1.00   9.25  ? 31  VAL A CG1 1 
ATOM   277  C  CG2 . VAL A 1 31  ? -6.348  -5.552  28.174  1.00   9.04  ? 31  VAL A CG2 1 
ATOM   278  N  N   . ASP A 1 32  ? -5.098  -9.013  27.682  1.00   7.47  ? 32  ASP A N   1 
ATOM   279  C  CA  . ASP A 1 32  ? -6.009  -10.103 27.987  1.00   8.18  ? 32  ASP A CA  1 
ATOM   280  C  C   . ASP A 1 32  ? -7.047  -9.604  28.977  1.00   7.66  ? 32  ASP A C   1 
ATOM   281  O  O   . ASP A 1 32  ? -6.727  -8.920  29.964  1.00   9.52  ? 32  ASP A O   1 
ATOM   282  C  CB  . ASP A 1 32  ? -5.293  -11.288 28.588  1.00   8.75  ? 32  ASP A CB  1 
ATOM   283  C  CG  . ASP A 1 32  ? -6.209  -12.425 28.880  1.00   9.36  ? 32  ASP A CG  1 
ATOM   284  O  OD1 . ASP A 1 32  ? -6.872  -12.918 27.937  1.00   9.52  ? 32  ASP A OD1 1 
ATOM   285  O  OD2 . ASP A 1 32  ? -6.263  -12.870 30.052  1.00   11.34 ? 32  ASP A OD2 1 
ATOM   286  N  N   . ILE A 1 33  ? -8.309  -9.902  28.701  1.00   7.74  ? 33  ILE A N   1 
ATOM   287  C  CA  . ILE A 1 33  ? -9.421  -9.560  29.581  1.00   7.81  ? 33  ILE A CA  1 
ATOM   288  C  C   . ILE A 1 33  ? -9.682  -10.780 30.420  1.00   8.46  ? 33  ILE A C   1 
ATOM   289  O  O   . ILE A 1 33  ? -10.213 -11.778 29.953  1.00   9.62  ? 33  ILE A O   1 
ATOM   290  C  CB  . ILE A 1 33  ? -10.625 -9.124  28.769  1.00   8.36  ? 33  ILE A CB  1 
ATOM   291  C  CG1 . ILE A 1 33  ? -10.293 -7.945  27.938  1.00   9.61  ? 33  ILE A CG1 1 
ATOM   292  C  CG2 . ILE A 1 33  ? -11.837 -8.880  29.707  1.00   10.16 ? 33  ILE A CG2 1 
ATOM   293  C  CD1 . ILE A 1 33  ? -11.315 -7.635  26.802  1.00   10.58 ? 33  ILE A CD1 1 
ATOM   294  N  N   A ASP A 1 34  ? -9.173  -10.773 31.649  0.50   10.14 ? 34  ASP A N   1 
ATOM   295  N  N   B ASP A 1 34  ? -9.458  -10.684 31.716  0.50   9.40  ? 34  ASP A N   1 
ATOM   296  C  CA  A ASP A 1 34  ? -9.513  -11.823 32.635  0.50   10.34 ? 34  ASP A CA  1 
ATOM   297  C  CA  B ASP A 1 34  ? -9.746  -11.751 32.668  0.50   9.72  ? 34  ASP A CA  1 
ATOM   298  C  C   A ASP A 1 34  ? -10.914 -11.520 33.161  0.50   11.03 ? 34  ASP A C   1 
ATOM   299  C  C   B ASP A 1 34  ? -11.143 -11.521 33.176  0.50   10.76 ? 34  ASP A C   1 
ATOM   300  O  O   A ASP A 1 34  ? -10.969 -10.489 33.980  0.50   11.30 ? 34  ASP A O   1 
ATOM   301  O  O   B ASP A 1 34  ? -11.545 -10.652 33.909  0.50   10.52 ? 34  ASP A O   1 
ATOM   302  C  CB  A ASP A 1 34  ? -8.495  -11.806 33.788  0.50   13.89 ? 34  ASP A CB  1 
ATOM   303  C  CB  B ASP A 1 34  ? -8.707  -11.786 33.790  0.50   13.31 ? 34  ASP A CB  1 
ATOM   304  C  CG  A ASP A 1 34  ? -8.845  -12.773 34.884  0.50   14.36 ? 34  ASP A CG  1 
ATOM   305  C  CG  B ASP A 1 34  ? -8.740  -13.072 34.575  0.50   14.80 ? 34  ASP A CG  1 
ATOM   306  O  OD1 A ASP A 1 34  ? -10.027 -13.179 35.084  0.50   13.67 ? 34  ASP A OD1 1 
ATOM   307  O  OD1 B ASP A 1 34  ? -8.298  -14.134 34.110  0.50   17.00 ? 34  ASP A OD1 1 
ATOM   308  O  OD2 A ASP A 1 34  ? -7.906  -13.113 35.556  0.50   18.12 ? 34  ASP A OD2 1 
ATOM   309  O  OD2 B ASP A 1 34  ? -9.318  -13.026 35.655  0.50   19.01 ? 34  ASP A OD2 1 
ATOM   310  N  N   . THR A 1 35  ? -11.978 -12.312 32.685  1.00   11.73 ? 35  THR A N   1 
ATOM   311  C  CA  . THR A 1 35  ? -13.366 -12.037 32.932  1.00   12.03 ? 35  THR A CA  1 
ATOM   312  C  C   . THR A 1 35  ? -13.801 -12.185 34.348  1.00   13.29 ? 35  THR A C   1 
ATOM   313  O  O   . THR A 1 35  ? -14.730 -11.509 34.793  1.00   15.56 ? 35  THR A O   1 
ATOM   314  C  CB  . THR A 1 35  ? -14.230 -12.917 32.118  1.00   13.23 ? 35  THR A CB  1 
ATOM   315  O  OG1 . THR A 1 35  ? -14.114 -14.275 32.598  1.00   14.89 ? 35  THR A OG1 1 
ATOM   316  C  CG2 . THR A 1 35  ? -13.994 -12.805 30.643  1.00   14.91 ? 35  THR A CG2 1 
ATOM   317  N  N   . HIS A 1 36  ? -13.083 -13.024 35.115  1.00   12.90 ? 36  HIS A N   1 
ATOM   318  C  CA  . HIS A 1 36  ? -13.348 -13.183 36.560  1.00   14.87 ? 36  HIS A CA  1 
ATOM   319  C  C   . HIS A 1 36  ? -12.849 -12.005 37.377  1.00   15.59 ? 36  HIS A C   1 
ATOM   320  O  O   . HIS A 1 36  ? -13.416 -11.798 38.485  1.00   18.14 ? 36  HIS A O   1 
ATOM   321  C  CB  . HIS A 1 36  ? -12.826 -14.536 37.008  1.00   17.87 ? 36  HIS A CB  1 
ATOM   322  C  CG  . HIS A 1 36  ? -13.754 -15.637 36.539  1.00   17.12 ? 36  HIS A CG  1 
ATOM   323  N  ND1 . HIS A 1 36  ? -15.039 -15.695 36.944  1.00   21.06 ? 36  HIS A ND1 1 
ATOM   324  C  CD2 . HIS A 1 36  ? -13.609 -16.627 35.567  1.00   18.45 ? 36  HIS A CD2 1 
ATOM   325  C  CE1 . HIS A 1 36  ? -15.663 -16.715 36.327  1.00   25.66 ? 36  HIS A CE1 1 
ATOM   326  N  NE2 . HIS A 1 36  ? -14.787 -17.290 35.486  1.00   24.02 ? 36  HIS A NE2 1 
ATOM   327  N  N   A THR A 1 37  ? -11.871 -11.244 36.901  0.50   15.52 ? 37  THR A N   1 
ATOM   328  N  N   B THR A 1 37  ? -11.750 -11.340 36.962  0.50   15.24 ? 37  THR A N   1 
ATOM   329  C  CA  A THR A 1 37  ? -11.372 -10.170 37.739  0.50   16.56 ? 37  THR A CA  1 
ATOM   330  C  CA  B THR A 1 37  ? -11.165 -10.169 37.653  0.50   14.73 ? 37  THR A CA  1 
ATOM   331  C  C   A THR A 1 37  ? -11.687 -8.758  37.219  0.50   15.70 ? 37  THR A C   1 
ATOM   332  C  C   B THR A 1 37  ? -11.882 -8.846  37.299  0.50   13.06 ? 37  THR A C   1 
ATOM   333  O  O   A THR A 1 37  ? -11.256 -7.702  37.830  0.50   16.17 ? 37  THR A O   1 
ATOM   334  O  O   B THR A 1 37  ? -11.963 -7.927  38.117  0.50   12.38 ? 37  THR A O   1 
ATOM   335  C  CB  A THR A 1 37  ? -9.876  -10.272 37.968  0.50   18.27 ? 37  THR A CB  1 
ATOM   336  C  CB  B THR A 1 37  ? -9.640  -10.086 37.406  0.50   15.68 ? 37  THR A CB  1 
ATOM   337  O  OG1 A THR A 1 37  ? -9.170  -10.092 36.717  0.50   21.55 ? 37  THR A OG1 1 
ATOM   338  O  OG1 B THR A 1 37  ? -9.074  -11.297 37.890  0.50   20.04 ? 37  THR A OG1 1 
ATOM   339  C  CG2 A THR A 1 37  ? -9.554  -11.604 38.600  0.50   19.55 ? 37  THR A CG2 1 
ATOM   340  C  CG2 B THR A 1 37  ? -8.900  -8.935  38.140  0.50   16.70 ? 37  THR A CG2 1 
ATOM   341  N  N   . ALA A 1 38  ? -12.392 -8.750  36.083  1.00   13.75 ? 38  ALA A N   1 
ATOM   342  C  CA  . ALA A 1 38  ? -13.022 -7.517  35.659  1.00   12.95 ? 38  ALA A CA  1 
ATOM   343  C  C   . ALA A 1 38  ? -14.187 -7.215  36.592  1.00   15.66 ? 38  ALA A C   1 
ATOM   344  O  O   . ALA A 1 38  ? -14.994 -8.052  36.871  1.00   22.49 ? 38  ALA A O   1 
ATOM   345  C  CB  . ALA A 1 38  ? -13.506 -7.639  34.215  1.00   13.37 ? 38  ALA A CB  1 
ATOM   346  N  N   . LYS A 1 39  ? -14.241 -6.014  37.093  1.00   15.70 ? 39  LYS A N   1 
ATOM   347  C  CA  . LYS A 1 39  ? -15.380 -5.767  38.030  1.00   17.75 ? 39  LYS A CA  1 
ATOM   348  C  C   . LYS A 1 39  ? -16.498 -5.071  37.399  1.00   13.89 ? 39  LYS A C   1 
ATOM   349  O  O   . LYS A 1 39  ? -16.343 -4.076  36.642  1.00   12.88 ? 39  LYS A O   1 
ATOM   350  C  CB  . LYS A 1 39  ? -14.982 -5.079  39.296  1.00   21.59 ? 39  LYS A CB  1 
ATOM   351  C  CG  . LYS A 1 39  ? -15.914 -5.187  40.474  1.00   22.06 ? 39  LYS A CG  1 
ATOM   352  C  CD  . LYS A 1 39  ? -15.217 -4.209  41.372  1.00   26.63 ? 39  LYS A CD  1 
ATOM   353  C  CE  . LYS A 1 39  ? -16.218 -3.541  42.300  1.00   33.97 ? 39  LYS A CE  1 
ATOM   354  N  NZ  . LYS A 1 39  ? -16.811 -4.548  43.222  1.00   24.08 ? 39  LYS A NZ  1 
ATOM   355  N  N   . TYR A 1 40  ? -17.693 -5.562  37.690  1.00   15.83 ? 40  TYR A N   1 
ATOM   356  C  CA  . TYR A 1 40  ? -18.831 -4.872  37.305  1.00   14.24 ? 40  TYR A CA  1 
ATOM   357  C  C   . TYR A 1 40  ? -18.876 -3.495  37.933  1.00   12.60 ? 40  TYR A C   1 
ATOM   358  O  O   . TYR A 1 40  ? -18.737 -3.332  39.186  1.00   15.45 ? 40  TYR A O   1 
ATOM   359  C  CB  . TYR A 1 40  ? -20.100 -5.645  37.734  1.00   17.82 ? 40  TYR A CB  1 
ATOM   360  C  CG  . TYR A 1 40  ? -21.361 -4.850  37.598  1.00   18.55 ? 40  TYR A CG  1 
ATOM   361  C  CD1 . TYR A 1 40  ? -21.769 -4.371  36.366  1.00   17.27 ? 40  TYR A CD1 1 
ATOM   362  C  CD2 . TYR A 1 40  ? -22.225 -4.658  38.671  1.00   21.68 ? 40  TYR A CD2 1 
ATOM   363  C  CE1 . TYR A 1 40  ? -22.930 -3.638  36.200  1.00   19.47 ? 40  TYR A CE1 1 
ATOM   364  C  CE2 . TYR A 1 40  ? -23.440 -3.969  38.499  1.00   20.46 ? 40  TYR A CE2 1 
ATOM   365  C  CZ  . TYR A 1 40  ? -23.784 -3.434  37.286  1.00   22.38 ? 40  TYR A CZ  1 
ATOM   366  O  OH  . TYR A 1 40  ? -24.961 -2.722  37.159  1.00   29.49 ? 40  TYR A OH  1 
ATOM   367  N  N   . ASP A 1 41  ? -19.106 -2.460  37.124  1.00   11.88 ? 41  ASP A N   1 
ATOM   368  C  CA  . ASP A 1 41  ? -19.170 -1.111  37.615  1.00   12.34 ? 41  ASP A CA  1 
ATOM   369  C  C   . ASP A 1 41  ? -20.569 -0.582  37.341  1.00   14.28 ? 41  ASP A C   1 
ATOM   370  O  O   . ASP A 1 41  ? -20.855 -0.189  36.193  1.00   14.27 ? 41  ASP A O   1 
ATOM   371  C  CB  . ASP A 1 41  ? -18.100 -0.261  36.909  1.00   14.55 ? 41  ASP A CB  1 
ATOM   372  C  CG  . ASP A 1 41  ? -18.070 1.162   37.399  1.00   15.92 ? 41  ASP A CG  1 
ATOM   373  O  OD1 . ASP A 1 41  ? -18.970 1.561   38.201  1.00   17.45 ? 41  ASP A OD1 1 
ATOM   374  O  OD2 . ASP A 1 41  ? -17.092 1.864   37.028  1.00   18.27 ? 41  ASP A OD2 1 
ATOM   375  N  N   . PRO A 1 42  ? -21.387 -0.451  38.411  1.00   16.84 ? 42  PRO A N   1 
ATOM   376  C  CA  . PRO A 1 42  ? -22.765 -0.007  38.165  1.00   18.87 ? 42  PRO A CA  1 
ATOM   377  C  C   . PRO A 1 42  ? -22.817 1.465   37.768  1.00   19.19 ? 42  PRO A C   1 
ATOM   378  O  O   . PRO A 1 42  ? -23.895 1.966   37.357  1.00   24.67 ? 42  PRO A O   1 
ATOM   379  C  CB  . PRO A 1 42  ? -23.448 -0.195  39.541  1.00   24.04 ? 42  PRO A CB  1 
ATOM   380  C  CG  . PRO A 1 42  ? -22.309 -0.214  40.522  1.00   24.91 ? 42  PRO A CG  1 
ATOM   381  C  CD  . PRO A 1 42  ? -21.141 -0.838  39.824  1.00   19.29 ? 42  PRO A CD  1 
ATOM   382  N  N   . SER A 1 43  ? -21.727 2.193   37.914  1.00   18.69 ? 43  SER A N   1 
ATOM   383  C  CA  . SER A 1 43  ? -21.681 3.593   37.458  1.00   18.92 ? 43  SER A CA  1 
ATOM   384  C  C   . SER A 1 43  ? -21.480 3.733   35.946  1.00   17.45 ? 43  SER A C   1 
ATOM   385  O  O   . SER A 1 43  ? -21.650 4.832   35.339  1.00   21.71 ? 43  SER A O   1 
ATOM   386  C  CB  . SER A 1 43  ? -20.580 4.371   38.168  1.00   20.45 ? 43  SER A CB  1 
ATOM   387  O  OG  . SER A 1 43  ? -19.265 4.106   37.712  1.00   19.96 ? 43  SER A OG  1 
ATOM   388  N  N   . LEU A 1 44  ? -21.075 2.668   35.242  1.00   17.16 ? 44  LEU A N   1 
ATOM   389  C  CA  . LEU A 1 44  ? -20.922 2.680   33.758  1.00   17.44 ? 44  LEU A CA  1 
ATOM   390  C  C   . LEU A 1 44  ? -22.301 2.846   33.141  1.00   17.82 ? 44  LEU A C   1 
ATOM   391  O  O   . LEU A 1 44  ? -23.291 2.479   33.705  1.00   22.78 ? 44  LEU A O   1 
ATOM   392  C  CB  . LEU A 1 44  ? -20.219 1.442   33.268  1.00   14.95 ? 44  LEU A CB  1 
ATOM   393  C  CG  . LEU A 1 44  ? -18.768 1.439   33.505  1.00   14.61 ? 44  LEU A CG  1 
ATOM   394  C  CD1 . LEU A 1 44  ? -18.276 0.028   33.161  1.00   15.54 ? 44  LEU A CD1 1 
ATOM   395  C  CD2 . LEU A 1 44  ? -18.037 2.552   32.753  1.00   15.50 ? 44  LEU A CD2 1 
ATOM   396  N  N   . LYS A 1 45  ? -22.361 3.608   32.046  1.00   16.45 ? 45  LYS A N   1 
ATOM   397  C  CA  . LYS A 1 45  ? -23.641 3.836   31.348  1.00   17.21 ? 45  LYS A CA  1 
ATOM   398  C  C   . LYS A 1 45  ? -23.700 2.946   30.130  1.00   16.72 ? 45  LYS A C   1 
ATOM   399  O  O   . LYS A 1 45  ? -22.687 2.435   29.613  1.00   16.93 ? 45  LYS A O   1 
ATOM   400  C  CB  . LYS A 1 45  ? -23.740 5.221   30.891  1.00   17.72 ? 45  LYS A CB  1 
ATOM   401  C  CG  . LYS A 1 45  ? -23.491 6.223   31.962  1.00   21.99 ? 45  LYS A CG  1 
ATOM   402  C  CD  . LYS A 1 45  ? -23.768 7.642   31.487  0.010  20.98 ? 45  LYS A CD  1 
ATOM   403  C  CE  . LYS A 1 45  ? -25.257 7.957   31.468  0.010  18.94 ? 45  LYS A CE  1 
ATOM   404  N  NZ  . LYS A 1 45  ? -25.533 9.308   30.904  0.010  15.90 ? 45  LYS A NZ  1 
ATOM   405  N  N   . PRO A 1 46  ? -24.960 2.763   29.603  1.00   17.28 ? 46  PRO A N   1 
ATOM   406  C  CA  . PRO A 1 46  ? -25.077 2.098   28.300  1.00   17.00 ? 46  PRO A CA  1 
ATOM   407  C  C   . PRO A 1 46  ? -24.251 2.848   27.261  1.00   12.41 ? 46  PRO A C   1 
ATOM   408  O  O   . PRO A 1 46  ? -24.247 4.064   27.323  1.00   14.23 ? 46  PRO A O   1 
ATOM   409  C  CB  . PRO A 1 46  ? -26.589 2.130   28.013  1.00   17.23 ? 46  PRO A CB  1 
ATOM   410  C  CG  . PRO A 1 46  ? -27.260 2.294   29.371  1.00   23.56 ? 46  PRO A CG  1 
ATOM   411  C  CD  . PRO A 1 46  ? -26.266 3.067   30.228  1.00   18.94 ? 46  PRO A CD  1 
ATOM   412  N  N   . LEU A 1 47  ? -23.727 2.061   26.331  1.00   15.15 ? 47  LEU A N   1 
ATOM   413  C  CA  . LEU A 1 47  ? -22.987 2.682   25.260  1.00   13.91 ? 47  LEU A CA  1 
ATOM   414  C  C   . LEU A 1 47  ? -24.017 3.349   24.292  1.00   14.36 ? 47  LEU A C   1 
ATOM   415  O  O   . LEU A 1 47  ? -25.067 2.704   24.045  1.00   18.48 ? 47  LEU A O   1 
ATOM   416  C  CB  . LEU A 1 47  ? -22.232 1.631   24.508  1.00   19.46 ? 47  LEU A CB  1 
ATOM   417  C  CG  . LEU A 1 47  ? -21.142 2.004   23.626  1.00   17.48 ? 47  LEU A CG  1 
ATOM   418  C  CD1 . LEU A 1 47  ? -20.128 2.964   24.350  1.00   19.69 ? 47  LEU A CD1 1 
ATOM   419  C  CD2 . LEU A 1 47  ? -20.501 0.734   23.045  1.00   19.04 ? 47  LEU A CD2 1 
ATOM   420  N  N   . SER A 1 48  ? -23.783 4.536   23.784  1.00   11.55 ? 48  SER A N   1 
ATOM   421  C  CA  . SER A 1 48  ? -24.626 5.156   22.777  1.00   12.96 ? 48  SER A CA  1 
ATOM   422  C  C   . SER A 1 48  ? -23.870 5.179   21.466  1.00   12.41 ? 48  SER A C   1 
ATOM   423  O  O   . SER A 1 48  ? -22.826 5.895   21.335  1.00   12.96 ? 48  SER A O   1 
ATOM   424  C  CB  . SER A 1 48  ? -24.984 6.548   23.221  1.00   14.50 ? 48  SER A CB  1 
ATOM   425  O  OG  . SER A 1 48  ? -25.595 7.299   22.202  1.00   16.20 ? 48  SER A OG  1 
ATOM   426  N  N   . VAL A 1 49  ? -24.280 4.404   20.518  1.00   12.70 ? 49  VAL A N   1 
ATOM   427  C  CA  . VAL A 1 49  ? -23.701 4.343   19.229  1.00   14.55 ? 49  VAL A CA  1 
ATOM   428  C  C   . VAL A 1 49  ? -24.659 4.933   18.215  1.00   15.26 ? 49  VAL A C   1 
ATOM   429  O  O   . VAL A 1 49  ? -25.730 4.388   18.028  1.00   18.98 ? 49  VAL A O   1 
ATOM   430  C  CB  . VAL A 1 49  ? -23.390 2.860   18.825  1.00   17.37 ? 49  VAL A CB  1 
ATOM   431  C  CG1 . VAL A 1 49  ? -22.646 2.810   17.499  1.00   20.71 ? 49  VAL A CG1 1 
ATOM   432  C  CG2 . VAL A 1 49  ? -22.581 2.116   19.883  1.00   19.37 ? 49  VAL A CG2 1 
ATOM   433  N  N   . SER A 1 50  ? -24.354 6.058   17.623  1.00   15.50 ? 50  SER A N   1 
ATOM   434  C  CA  . SER A 1 50  ? -25.293 6.740   16.714  1.00   15.95 ? 50  SER A CA  1 
ATOM   435  C  C   . SER A 1 50  ? -24.664 6.865   15.379  1.00   15.27 ? 50  SER A C   1 
ATOM   436  O  O   . SER A 1 50  ? -23.975 7.855   15.073  1.00   16.64 ? 50  SER A O   1 
ATOM   437  C  CB  . SER A 1 50  ? -25.700 8.082   17.286  1.00   20.04 ? 50  SER A CB  1 
ATOM   438  O  OG  . SER A 1 50  ? -26.306 7.891   18.558  1.00   25.21 ? 50  SER A OG  1 
ATOM   439  N  N   . TYR A 1 51  ? -24.890 5.860   14.549  1.00   15.03 ? 51  TYR A N   1 
ATOM   440  C  CA  . TYR A 1 51  ? -24.327 5.758   13.236  1.00   14.71 ? 51  TYR A CA  1 
ATOM   441  C  C   . TYR A 1 51  ? -25.300 6.036   12.091  1.00   16.15 ? 51  TYR A C   1 
ATOM   442  O  O   . TYR A 1 51  ? -24.928 5.845   10.962  1.00   17.17 ? 51  TYR A O   1 
ATOM   443  C  CB  . TYR A 1 51  ? -23.676 4.373   13.058  1.00   14.93 ? 51  TYR A CB  1 
ATOM   444  C  CG  . TYR A 1 51  ? -22.412 4.098   13.867  1.00   12.98 ? 51  TYR A CG  1 
ATOM   445  C  CD1 . TYR A 1 51  ? -21.659 5.105   14.499  1.00   12.80 ? 51  TYR A CD1 1 
ATOM   446  C  CD2 . TYR A 1 51  ? -21.924 2.796   13.953  1.00   12.71 ? 51  TYR A CD2 1 
ATOM   447  C  CE1 . TYR A 1 51  ? -20.443 4.820   15.196  1.00   11.78 ? 51  TYR A CE1 1 
ATOM   448  C  CE2 . TYR A 1 51  ? -20.734 2.500   14.587  1.00   11.75 ? 51  TYR A CE2 1 
ATOM   449  C  CZ  . TYR A 1 51  ? -20.013 3.523   15.261  1.00   11.12 ? 51  TYR A CZ  1 
ATOM   450  O  OH  . TYR A 1 51  ? -18.872 3.139   15.899  1.00   11.28 ? 51  TYR A OH  1 
ATOM   451  N  N   . ASP A 1 52  ? -26.524 6.435   12.353  1.00   16.96 ? 52  ASP A N   1 
ATOM   452  C  CA  . ASP A 1 52  ? -27.551 6.666   11.337  1.00   18.18 ? 52  ASP A CA  1 
ATOM   453  C  C   . ASP A 1 52  ? -27.116 7.645   10.244  1.00   19.00 ? 52  ASP A C   1 
ATOM   454  O  O   . ASP A 1 52  ? -27.523 7.469   9.073   1.00   23.21 ? 52  ASP A O   1 
ATOM   455  C  CB  . ASP A 1 52  ? -28.837 7.138   12.043  1.00   21.54 ? 52  ASP A CB  1 
ATOM   456  C  CG  . ASP A 1 52  ? -28.582 8.188   13.179  1.00   35.54 ? 52  ASP A CG  1 
ATOM   457  O  OD1 . ASP A 1 52  ? -27.963 7.849   14.289  1.00   34.88 ? 52  ASP A OD1 1 
ATOM   458  O  OD2 . ASP A 1 52  ? -29.046 9.343   12.968  1.00   52.71 ? 52  ASP A OD2 1 
ATOM   459  N  N   . GLN A 1 53  ? -26.287 8.640   10.573  1.00   19.39 ? 53  GLN A N   1 
ATOM   460  C  CA  . GLN A 1 53  ? -25.814 9.573   9.524   1.00   17.79 ? 53  GLN A CA  1 
ATOM   461  C  C   . GLN A 1 53  ? -24.380 9.333   9.077   1.00   16.97 ? 53  GLN A C   1 
ATOM   462  O  O   . GLN A 1 53  ? -23.806 10.172  8.398   1.00   18.60 ? 53  GLN A O   1 
ATOM   463  C  CB  . GLN A 1 53  ? -26.013 11.031  9.996   1.00   25.20 ? 53  GLN A CB  1 
ATOM   464  C  CG  . GLN A 1 53  ? -27.450 11.282  10.398  1.00   32.53 ? 53  GLN A CG  1 
ATOM   465  C  CD  . GLN A 1 53  ? -28.368 11.336  9.207   1.00   45.80 ? 53  GLN A CD  1 
ATOM   466  O  OE1 . GLN A 1 53  ? -27.956 11.755  8.108   0.0000 42.97 ? 53  GLN A OE1 1 
ATOM   467  N  NE2 . GLN A 1 53  ? -29.620 10.918  9.400   0.0000 55.79 ? 53  GLN A NE2 1 
ATOM   468  N  N   . ALA A 1 54  ? -23.842 8.170   9.393   1.00   15.74 ? 54  ALA A N   1 
ATOM   469  C  CA  . ALA A 1 54  ? -22.431 7.941   9.048   1.00   14.54 ? 54  ALA A CA  1 
ATOM   470  C  C   . ALA A 1 54  ? -22.301 7.994   7.556   1.00   15.52 ? 54  ALA A C   1 
ATOM   471  O  O   . ALA A 1 54  ? -23.164 7.462   6.805   1.00   20.09 ? 54  ALA A O   1 
ATOM   472  C  CB  . ALA A 1 54  ? -21.960 6.571   9.550   1.00   17.99 ? 54  ALA A CB  1 
ATOM   473  N  N   . THR A 1 55  ? -21.217 8.612   7.049   1.00   13.49 ? 55  THR A N   1 
ATOM   474  C  CA  . THR A 1 55  ? -20.879 8.803   5.621   1.00   15.52 ? 55  THR A CA  1 
ATOM   475  C  C   . THR A 1 55  ? -19.539 8.265   5.345   1.00   11.63 ? 55  THR A C   1 
ATOM   476  O  O   . THR A 1 55  ? -18.538 8.894   5.614   1.00   12.58 ? 55  THR A O   1 
ATOM   477  C  CB  . THR A 1 55  ? -20.873 10.355  5.203   1.00   22.39 ? 55  THR A CB  1 
ATOM   478  O  OG1 . THR A 1 55  ? -22.130 11.006  5.456   1.00   27.64 ? 55  THR A OG1 1 
ATOM   479  C  CG2 . THR A 1 55  ? -20.484 10.471  3.699   1.00   26.34 ? 55  THR A CG2 1 
ATOM   480  N  N   . SER A 1 56  ? -19.534 7.060   4.852   1.00   11.99 ? 56  SER A N   1 
ATOM   481  C  CA  . SER A 1 56  ? -18.255 6.489   4.413   1.00   12.52 ? 56  SER A CA  1 
ATOM   482  C  C   . SER A 1 56  ? -17.853 7.120   3.123   1.00   12.11 ? 56  SER A C   1 
ATOM   483  O  O   . SER A 1 56  ? -18.674 7.589   2.355   1.00   13.95 ? 56  SER A O   1 
ATOM   484  C  CB  . SER A 1 56  ? -18.345 4.947   4.279   1.00   13.12 ? 56  SER A CB  1 
ATOM   485  O  OG  . SER A 1 56  ? -19.194 4.587   3.185   1.00   14.06 ? 56  SER A OG  1 
ATOM   486  N  N   . LEU A 1 57  ? -16.547 7.174   2.944   1.00   11.50 ? 57  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 57  ? -16.014 7.764   1.722   1.00   13.37 ? 57  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 57  ? -15.160 6.816   0.883   1.00   11.80 ? 57  LEU A C   1 
ATOM   489  O  O   . LEU A 1 57  ? -15.196 6.854   -0.354  1.00   13.44 ? 57  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 57  ? -15.171 8.947   2.137   1.00   15.11 ? 57  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 57  ? -16.014 10.162  2.680   1.00   19.25 ? 57  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 57  ? -15.058 11.307  3.170   1.00   21.80 ? 57  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 57  ? -17.096 10.663  1.697   1.00   20.70 ? 57  LEU A CD2 1 
ATOM   494  N  N   . ARG A 1 58  ? -14.271 6.063   1.527   1.00   13.01 ? 58  ARG A N   1 
ATOM   495  C  CA  . ARG A 1 58  ? -13.192 5.418   0.792   1.00   12.22 ? 58  ARG A CA  1 
ATOM   496  C  C   . ARG A 1 58  ? -12.696 4.247   1.594   1.00   11.05 ? 58  ARG A C   1 
ATOM   497  O  O   . ARG A 1 58  ? -12.832 4.204   2.810   1.00   11.55 ? 58  ARG A O   1 
ATOM   498  C  CB  . ARG A 1 58  ? -12.003 6.424   0.613   1.00   14.38 ? 58  ARG A CB  1 
ATOM   499  C  CG  . ARG A 1 58  ? -10.945 6.029   -0.341  1.00   14.48 ? 58  ARG A CG  1 
ATOM   500  C  CD  . ARG A 1 58  ? -9.879  7.107   -0.567  1.00   16.59 ? 58  ARG A CD  1 
ATOM   501  N  NE  . ARG A 1 58  ? -9.053  7.150   0.616   1.00   15.53 ? 58  ARG A NE  1 
ATOM   502  C  CZ  . ARG A 1 58  ? -7.746  7.356   0.629   1.00   13.88 ? 58  ARG A CZ  1 
ATOM   503  N  NH1 . ARG A 1 58  ? -7.084  7.596   -0.497  1.00   16.08 ? 58  ARG A NH1 1 
ATOM   504  N  NH2 . ARG A 1 58  ? -7.107  7.337   1.790   1.00   13.93 ? 58  ARG A NH2 1 
ATOM   505  N  N   . ILE A 1 59  ? -12.058 3.277   0.920   1.00   11.22 ? 59  ILE A N   1 
ATOM   506  C  CA  . ILE A 1 59  ? -11.411 2.180   1.613   1.00   10.78 ? 59  ILE A CA  1 
ATOM   507  C  C   . ILE A 1 59  ? -9.959  2.177   1.068   1.00   9.97  ? 59  ILE A C   1 
ATOM   508  O  O   . ILE A 1 59  ? -9.691  2.339   -0.136  1.00   12.49 ? 59  ILE A O   1 
ATOM   509  C  CB  . ILE A 1 59  ? -12.118 0.862   1.339   1.00   10.67 ? 59  ILE A CB  1 
ATOM   510  C  CG1 . ILE A 1 59  ? -11.536 -0.267  2.245   1.00   11.13 ? 59  ILE A CG1 1 
ATOM   511  C  CG2 . ILE A 1 59  ? -12.136 0.445   -0.142  1.00   12.80 ? 59  ILE A CG2 1 
ATOM   512  C  CD1 . ILE A 1 59  ? -12.361 -1.518  2.145   1.00   12.33 ? 59  ILE A CD1 1 
ATOM   513  N  N   . LEU A 1 60  ? -8.985  1.995   1.973   1.00   10.03 ? 60  LEU A N   1 
ATOM   514  C  CA  . LEU A 1 60  ? -7.603  2.107   1.722   1.00   9.90  ? 60  LEU A CA  1 
ATOM   515  C  C   . LEU A 1 60  ? -6.784  0.923   2.252   1.00   9.50  ? 60  LEU A C   1 
ATOM   516  O  O   . LEU A 1 60  ? -6.945  0.602   3.431   1.00   10.03 ? 60  LEU A O   1 
ATOM   517  C  CB  . LEU A 1 60  ? -7.055  3.402   2.405   1.00   11.78 ? 60  LEU A CB  1 
ATOM   518  C  CG  . LEU A 1 60  ? -5.526  3.567   2.364   1.00   11.91 ? 60  LEU A CG  1 
ATOM   519  C  CD1 . LEU A 1 60  ? -4.964  3.807   0.937   1.00   13.62 ? 60  LEU A CD1 1 
ATOM   520  C  CD2 . LEU A 1 60  ? -5.044  4.671   3.371   1.00   13.91 ? 60  LEU A CD2 1 
ATOM   521  N  N   . ASN A 1 61  ? -5.950  0.301   1.447   1.00   9.35  ? 61  ASN A N   1 
ATOM   522  C  CA  . ASN A 1 61  ? -4.933  -0.645  1.941   1.00   10.00 ? 61  ASN A CA  1 
ATOM   523  C  C   . ASN A 1 61  ? -3.668  0.142   2.325   1.00   9.68  ? 61  ASN A C   1 
ATOM   524  O  O   . ASN A 1 61  ? -3.092  0.735   1.442   1.00   11.17 ? 61  ASN A O   1 
ATOM   525  C  CB  . ASN A 1 61  ? -4.634  -1.686  0.854   1.00   11.02 ? 61  ASN A CB  1 
ATOM   526  C  CG  . ASN A 1 61  ? -3.594  -2.675  1.263   1.00   10.01 ? 61  ASN A CG  1 
ATOM   527  O  OD1 . ASN A 1 61  ? -2.726  -2.401  2.125   1.00   11.46 ? 61  ASN A OD1 1 
ATOM   528  N  ND2 . ASN A 1 61  ? -3.639  -3.872  0.660   1.00   11.81 ? 61  ASN A ND2 1 
ATOM   529  N  N   . ASN A 1 62  ? -3.416  0.252   3.605   1.00   10.08 ? 62  ASN A N   1 
ATOM   530  C  CA  . ASN A 1 62  ? -2.348  1.065   4.067   1.00   11.48 ? 62  ASN A CA  1 
ATOM   531  C  C   . ASN A 1 62  ? -1.105  0.289   4.299   1.00   11.87 ? 62  ASN A C   1 
ATOM   532  O  O   . ASN A 1 62  ? -0.098  0.815   4.884   1.00   14.43 ? 62  ASN A O   1 
ATOM   533  C  CB  . ASN A 1 62  ? -2.756  1.904   5.300   1.00   13.25 ? 62  ASN A CB  1 
ATOM   534  C  CG  . ASN A 1 62  ? -3.075  1.053   6.477   1.00   12.28 ? 62  ASN A CG  1 
ATOM   535  O  OD1 . ASN A 1 62  ? -2.698  -0.148  6.552   1.00   12.37 ? 62  ASN A OD1 1 
ATOM   536  N  ND2 . ASN A 1 62  ? -3.834  1.619   7.383   1.00   16.84 ? 62  ASN A ND2 1 
ATOM   537  N  N   . GLY A 1 63  ? -1.045  -0.986  3.869   1.00   11.24 ? 63  GLY A N   1 
ATOM   538  C  CA  . GLY A 1 63  ? 0.085   -1.780  4.064   1.00   11.82 ? 63  GLY A CA  1 
ATOM   539  C  C   . GLY A 1 63  ? 0.154   -2.561  5.398   1.00   12.21 ? 63  GLY A C   1 
ATOM   540  O  O   . GLY A 1 63  ? 0.995   -3.429  5.559   1.00   13.57 ? 63  GLY A O   1 
ATOM   541  N  N   . HIS A 1 64  ? -0.750  -2.285  6.304   1.00   11.86 ? 64  HIS A N   1 
ATOM   542  C  CA  . HIS A 1 64  ? -0.879  -3.014  7.606   1.00   12.55 ? 64  HIS A CA  1 
ATOM   543  C  C   . HIS A 1 64  ? -2.281  -3.593  7.768   1.00   10.98 ? 64  HIS A C   1 
ATOM   544  O  O   . HIS A 1 64  ? -2.407  -4.643  8.391   1.00   15.94 ? 64  HIS A O   1 
ATOM   545  C  CB  . HIS A 1 64  ? -0.462  -2.236  8.849   1.00   14.17 ? 64  HIS A CB  1 
ATOM   546  C  CG  . HIS A 1 64  ? -0.836  -0.818  9.049   1.00   18.22 ? 64  HIS A CG  1 
ATOM   547  N  ND1 . HIS A 1 64  ? -1.879  -0.338  9.968   1.00   20.27 ? 64  HIS A ND1 1 
ATOM   548  C  CD2 . HIS A 1 64  ? -0.153  0.300   8.604   1.00   25.28 ? 64  HIS A CD2 1 
ATOM   549  C  CE1 . HIS A 1 64  ? -1.818  1.019   9.934   1.00   27.71 ? 64  HIS A CE1 1 
ATOM   550  N  NE2 . HIS A 1 64  ? -0.781  1.402   9.127   1.00   29.72 ? 64  HIS A NE2 1 
ATOM   551  N  N   . ALA A 1 65  ? -3.288  -2.949  7.238   1.00   10.18 ? 65  ALA A N   1 
ATOM   552  C  CA  . ALA A 1 65  ? -4.680  -3.384  7.265   1.00   9.71  ? 65  ALA A CA  1 
ATOM   553  C  C   . ALA A 1 65  ? -5.371  -2.644  6.142   1.00   9.31  ? 65  ALA A C   1 
ATOM   554  O  O   . ALA A 1 65  ? -4.705  -2.010  5.300   1.00   10.98 ? 65  ALA A O   1 
ATOM   555  C  CB  . ALA A 1 65  ? -5.284  -3.188  8.626   1.00   11.37 ? 65  ALA A CB  1 
ATOM   556  N  N   . PHE A 1 66  ? -6.657  -2.685  6.113   1.00   9.11  ? 66  PHE A N   1 
ATOM   557  C  CA  . PHE A 1 66  ? -7.444  -1.737  5.308   1.00   9.72  ? 66  PHE A CA  1 
ATOM   558  C  C   . PHE A 1 66  ? -8.272  -0.896  6.184   1.00   9.29  ? 66  PHE A C   1 
ATOM   559  O  O   . PHE A 1 66  ? -8.939  -1.379  7.143   1.00   10.06 ? 66  PHE A O   1 
ATOM   560  C  CB  . PHE A 1 66  ? -8.260  -2.454  4.196   1.00   10.91 ? 66  PHE A CB  1 
ATOM   561  C  CG  . PHE A 1 66  ? -9.311  -3.398  4.691   1.00   10.14 ? 66  PHE A CG  1 
ATOM   562  C  CD1 . PHE A 1 66  ? -10.533 -2.932  5.018   1.00   11.38 ? 66  PHE A CD1 1 
ATOM   563  C  CD2 . PHE A 1 66  ? -9.032  -4.761  4.842   1.00   10.74 ? 66  PHE A CD2 1 
ATOM   564  C  CE1 . PHE A 1 66  ? -11.515 -3.792  5.526   1.00   11.98 ? 66  PHE A CE1 1 
ATOM   565  C  CE2 . PHE A 1 66  ? -10.001 -5.644  5.352   1.00   12.23 ? 66  PHE A CE2 1 
ATOM   566  C  CZ  . PHE A 1 66  ? -11.254 -5.162  5.672   1.00   12.04 ? 66  PHE A CZ  1 
ATOM   567  N  N   . ASN A 1 67  ? -8.379  0.382   5.873   1.00   9.59  ? 67  ASN A N   1 
ATOM   568  C  CA  . ASN A 1 67  ? -9.235  1.325   6.595   1.00   9.31  ? 67  ASN A CA  1 
ATOM   569  C  C   . ASN A 1 67  ? -10.477 1.712   5.774   1.00   8.67  ? 67  ASN A C   1 
ATOM   570  O  O   . ASN A 1 67  ? -10.303 2.140   4.611   1.00   10.45 ? 67  ASN A O   1 
ATOM   571  C  CB  . ASN A 1 67  ? -8.532  2.607   6.981   1.00   11.00 ? 67  ASN A CB  1 
ATOM   572  C  CG  . ASN A 1 67  ? -7.524  2.415   8.014   1.00   11.45 ? 67  ASN A CG  1 
ATOM   573  O  OD1 . ASN A 1 67  ? -7.355  1.366   8.636   1.00   13.25 ? 67  ASN A OD1 1 
ATOM   574  N  ND2 . ASN A 1 67  ? -6.775  3.478   8.287   1.00   14.65 ? 67  ASN A ND2 1 
ATOM   575  N  N   . VAL A 1 68  ? -11.654 1.589   6.343   1.00   9.27  ? 68  VAL A N   1 
ATOM   576  C  CA  . VAL A 1 68  ? -12.878 2.218   5.799   1.00   9.31  ? 68  VAL A CA  1 
ATOM   577  C  C   . VAL A 1 68  ? -12.951 3.575   6.427   1.00   10.10 ? 68  VAL A C   1 
ATOM   578  O  O   . VAL A 1 68  ? -13.099 3.681   7.665   1.00   9.82  ? 68  VAL A O   1 
ATOM   579  C  CB  . VAL A 1 68  ? -14.113 1.364   5.947   1.00   10.70 ? 68  VAL A CB  1 
ATOM   580  C  CG1 . VAL A 1 68  ? -15.371 2.148   5.555   1.00   12.20 ? 68  VAL A CG1 1 
ATOM   581  C  CG2 . VAL A 1 68  ? -13.981 0.067   5.226   1.00   11.49 ? 68  VAL A CG2 1 
ATOM   582  N  N   . GLU A 1 69  ? -12.894 4.647   5.625   1.00   10.42 ? 69  GLU A N   1 
ATOM   583  C  CA  . GLU A 1 69  ? -12.777 6.024   6.102   1.00   10.53 ? 69  GLU A CA  1 
ATOM   584  C  C   . GLU A 1 69  ? -14.125 6.706   6.033   1.00   10.11 ? 69  GLU A C   1 
ATOM   585  O  O   . GLU A 1 69  ? -14.891 6.475   5.072   1.00   11.58 ? 69  GLU A O   1 
ATOM   586  C  CB  . GLU A 1 69  ? -11.839 6.753   5.216   1.00   12.44 ? 69  GLU A CB  1 
ATOM   587  C  CG  . GLU A 1 69  ? -10.432 6.156   5.261   1.00   12.58 ? 69  GLU A CG  1 
ATOM   588  C  CD  . GLU A 1 69  ? -9.555  6.626   4.151   1.00   13.78 ? 69  GLU A CD  1 
ATOM   589  O  OE1 . GLU A 1 69  ? -10.048 7.349   3.205   1.00   14.84 ? 69  GLU A OE1 1 
ATOM   590  O  OE2 . GLU A 1 69  ? -8.325  6.362   4.169   1.00   15.43 ? 69  GLU A OE2 1 
ATOM   591  N  N   . PHE A 1 70  ? -14.369 7.588   6.997   1.00   10.55 ? 70  PHE A N   1 
ATOM   592  C  CA  . PHE A 1 70  ? -15.579 8.306   7.092   1.00   10.32 ? 70  PHE A CA  1 
ATOM   593  C  C   . PHE A 1 70  ? -15.380 9.792   7.021   1.00   11.04 ? 70  PHE A C   1 
ATOM   594  O  O   . PHE A 1 70  ? -14.290 10.309  7.389   1.00   12.41 ? 70  PHE A O   1 
ATOM   595  C  CB  . PHE A 1 70  ? -16.327 7.995   8.394   1.00   10.72 ? 70  PHE A CB  1 
ATOM   596  C  CG  . PHE A 1 70  ? -16.865 6.595   8.368   1.00   10.60 ? 70  PHE A CG  1 
ATOM   597  C  CD1 . PHE A 1 70  ? -16.054 5.481   8.615   1.00   11.35 ? 70  PHE A CD1 1 
ATOM   598  C  CD2 . PHE A 1 70  ? -18.217 6.377   8.097   1.00   10.64 ? 70  PHE A CD2 1 
ATOM   599  C  CE1 . PHE A 1 70  ? -16.577 4.214   8.458   1.00   11.73 ? 70  PHE A CE1 1 
ATOM   600  C  CE2 . PHE A 1 70  ? -18.731 5.078   7.918   1.00   11.66 ? 70  PHE A CE2 1 
ATOM   601  C  CZ  . PHE A 1 70  ? -17.869 4.000   8.146   1.00   11.94 ? 70  PHE A CZ  1 
ATOM   602  N  N   . ASP A 1 71  ? -16.354 10.525  6.524   1.00   13.50 ? 71  ASP A N   1 
ATOM   603  C  CA  . ASP A 1 71  ? -16.293 11.982  6.558   1.00   14.57 ? 71  ASP A CA  1 
ATOM   604  C  C   . ASP A 1 71  ? -16.585 12.359  7.967   1.00   14.05 ? 71  ASP A C   1 
ATOM   605  O  O   . ASP A 1 71  ? -17.699 12.199  8.461   1.00   20.10 ? 71  ASP A O   1 
ATOM   606  C  CB  . ASP A 1 71  ? -17.392 12.530  5.684   1.00   19.62 ? 71  ASP A CB  1 
ATOM   607  C  CG  . ASP A 1 71  ? -17.551 14.054  5.847   1.00   24.12 ? 71  ASP A CG  1 
ATOM   608  O  OD1 . ASP A 1 71  ? -16.669 14.677  6.418   1.00   24.41 ? 71  ASP A OD1 1 
ATOM   609  O  OD2 . ASP A 1 71  ? -18.580 14.643  5.474   1.00   30.37 ? 71  ASP A OD2 1 
ATOM   610  N  N   . ASP A 1 72  ? -15.569 12.875  8.628   1.00   13.82 ? 72  ASP A N   1 
ATOM   611  C  CA  . ASP A 1 72  ? -15.684 13.277  10.029  1.00   14.10 ? 72  ASP A CA  1 
ATOM   612  C  C   . ASP A 1 72  ? -15.676 14.827  10.153  1.00   17.60 ? 72  ASP A C   1 
ATOM   613  O  O   . ASP A 1 72  ? -15.284 15.333  11.220  1.00   19.33 ? 72  ASP A O   1 
ATOM   614  C  CB  . ASP A 1 72  ? -14.632 12.658  10.934  1.00   14.55 ? 72  ASP A CB  1 
ATOM   615  C  CG  . ASP A 1 72  ? -13.266 13.167  10.616  1.00   15.84 ? 72  ASP A CG  1 
ATOM   616  O  OD1 . ASP A 1 72  ? -13.081 13.799  9.491   1.00   17.73 ? 72  ASP A OD1 1 
ATOM   617  O  OD2 . ASP A 1 72  ? -12.336 12.959  11.390  1.00   16.21 ? 72  ASP A OD2 1 
ATOM   618  N  N   . SER A 1 73  ? -16.073 15.536  9.113   1.00   16.85 ? 73  SER A N   1 
ATOM   619  C  CA  . SER A 1 73  ? -16.059 17.034  9.155   1.00   19.32 ? 73  SER A CA  1 
ATOM   620  C  C   . SER A 1 73  ? -17.429 17.609  9.708   1.00   20.14 ? 73  SER A C   1 
ATOM   621  O  O   . SER A 1 73  ? -17.551 18.818  9.880   1.00   18.43 ? 73  SER A O   1 
ATOM   622  C  CB  . SER A 1 73  ? -15.749 17.534  7.778   1.00   23.72 ? 73  SER A CB  1 
ATOM   623  O  OG  . SER A 1 73  ? -16.913 17.354  7.036   1.00   21.60 ? 73  SER A OG  1 
ATOM   624  N  N   . GLN A 1 74  ? -18.428 16.777  9.970   1.00   21.72 ? 74  GLN A N   1 
ATOM   625  C  CA  . GLN A 1 74  ? -19.704 17.182  10.567  1.00   20.53 ? 74  GLN A CA  1 
ATOM   626  C  C   . GLN A 1 74  ? -19.961 16.250  11.727  1.00   20.66 ? 74  GLN A C   1 
ATOM   627  O  O   . GLN A 1 74  ? -19.382 15.130  11.840  1.00   17.26 ? 74  GLN A O   1 
ATOM   628  C  CB  . GLN A 1 74  ? -20.893 17.180  9.550   1.00   22.83 ? 74  GLN A CB  1 
ATOM   629  C  CG  . GLN A 1 74  ? -20.862 18.341  8.639   1.00   28.10 ? 74  GLN A CG  1 
ATOM   630  C  CD  . GLN A 1 74  ? -21.975 18.231  7.635   1.00   28.40 ? 74  GLN A CD  1 
ATOM   631  O  OE1 . GLN A 1 74  ? -21.716 18.064  6.439   0.0000 51.27 ? 74  GLN A OE1 1 
ATOM   632  N  NE2 . GLN A 1 74  ? -23.199 18.358  8.094   0.0000 51.02 ? 74  GLN A NE2 1 
ATOM   633  N  N   . ASP A 1 75  ? -20.908 16.683  12.549  1.00   22.45 ? 75  ASP A N   1 
ATOM   634  C  CA  . ASP A 1 75  ? -21.282 15.962  13.696  1.00   19.94 ? 75  ASP A CA  1 
ATOM   635  C  C   . ASP A 1 75  ? -22.199 14.805  13.194  1.00   21.93 ? 75  ASP A C   1 
ATOM   636  O  O   . ASP A 1 75  ? -23.449 14.976  13.150  1.00   26.95 ? 75  ASP A O   1 
ATOM   637  C  CB  . ASP A 1 75  ? -22.046 16.984  14.618  1.00   26.19 ? 75  ASP A CB  1 
ATOM   638  C  CG  . ASP A 1 75  ? -22.737 16.342  15.796  1.00   28.42 ? 75  ASP A CG  1 
ATOM   639  O  OD1 . ASP A 1 75  ? -22.409 15.167  16.079  1.00   24.23 ? 75  ASP A OD1 1 
ATOM   640  O  OD2 . ASP A 1 75  ? -23.557 17.059  16.469  0.0000 50.91 ? 75  ASP A OD2 1 
ATOM   641  N  N   . LYS A 1 76  ? -21.672 13.630  12.862  1.00   18.84 ? 76  LYS A N   1 
ATOM   642  C  CA  . LYS A 1 76  ? -22.528 12.568  12.294  1.00   21.34 ? 76  LYS A CA  1 
ATOM   643  C  C   . LYS A 1 76  ? -22.665 11.276  13.130  1.00   32.54 ? 76  LYS A C   1 
ATOM   644  O  O   . LYS A 1 76  ? -23.585 11.126  13.933  1.00   47.18 ? 76  LYS A O   1 
ATOM   645  C  CB  . LYS A 1 76  ? -22.171 12.361  10.805  1.00   21.83 ? 76  LYS A CB  1 
ATOM   646  C  CG  . LYS A 1 76  ? -22.525 13.517  9.823   1.00   34.07 ? 76  LYS A CG  1 
ATOM   647  C  CD  . LYS A 1 76  ? -21.785 13.263  8.493   1.00   38.68 ? 76  LYS A CD  1 
ATOM   648  C  CE  . LYS A 1 76  ? -22.240 14.156  7.342   0.0000 40.94 ? 76  LYS A CE  1 
ATOM   649  N  NZ  . LYS A 1 76  ? -21.205 14.365  6.294   0.0000 47.06 ? 76  LYS A NZ  1 
ATOM   650  N  N   . ALA A 1 77  ? -21.714 10.427  12.938  1.00   23.48 ? 77  ALA A N   1 
ATOM   651  C  CA  . ALA A 1 77  ? -21.475 9.103   13.503  1.00   14.65 ? 77  ALA A CA  1 
ATOM   652  C  C   . ALA A 1 77  ? -20.714 9.229   14.866  1.00   12.88 ? 77  ALA A C   1 
ATOM   653  O  O   . ALA A 1 77  ? -19.480 9.395   14.900  1.00   19.62 ? 77  ALA A O   1 
ATOM   654  C  CB  . ALA A 1 77  ? -20.638 8.453   12.491  1.00   17.02 ? 77  ALA A CB  1 
ATOM   655  N  N   . VAL A 1 78  ? -21.432 9.172   15.943  1.00   13.39 ? 78  VAL A N   1 
ATOM   656  C  CA  . VAL A 1 78  ? -20.803 9.465   17.197  1.00   13.43 ? 78  VAL A CA  1 
ATOM   657  C  C   . VAL A 1 78  ? -21.012 8.360   18.212  1.00   12.13 ? 78  VAL A C   1 
ATOM   658  O  O   . VAL A 1 78  ? -22.041 7.655   18.229  1.00   14.03 ? 78  VAL A O   1 
ATOM   659  C  CB  . VAL A 1 78  ? -21.089 10.827  17.731  1.00   20.39 ? 78  VAL A CB  1 
ATOM   660  C  CG1 . VAL A 1 78  ? -20.878 11.902  16.719  1.00   21.84 ? 78  VAL A CG1 1 
ATOM   661  C  CG2 . VAL A 1 78  ? -22.450 10.811  18.131  1.00   21.63 ? 78  VAL A CG2 1 
ATOM   662  N  N   . LEU A 1 79  ? -19.999 8.216   19.032  1.00   10.77 ? 79  LEU A N   1 
ATOM   663  C  CA  . LEU A 1 79  ? -20.014 7.328   20.160  1.00   10.64 ? 79  LEU A CA  1 
ATOM   664  C  C   . LEU A 1 79  ? -19.994 8.165   21.419  1.00   11.13 ? 79  LEU A C   1 
ATOM   665  O  O   . LEU A 1 79  ? -19.172 9.130   21.529  1.00   12.21 ? 79  LEU A O   1 
ATOM   666  C  CB  . LEU A 1 79  ? -18.736 6.427   20.056  1.00   11.61 ? 79  LEU A CB  1 
ATOM   667  C  CG  . LEU A 1 79  ? -18.597 5.372   21.103  1.00   12.33 ? 79  LEU A CG  1 
ATOM   668  C  CD1 . LEU A 1 79  ? -19.668 4.293   20.848  1.00   16.28 ? 79  LEU A CD1 1 
ATOM   669  C  CD2 . LEU A 1 79  ? -17.239 4.713   21.045  1.00   13.08 ? 79  LEU A CD2 1 
ATOM   670  N  N   . LYS A 1 80  ? -20.863 7.841   22.345  1.00   11.41 ? 80  LYS A N   1 
ATOM   671  C  CA  . LYS A 1 80  ? -20.904 8.545   23.638  1.00   12.72 ? 80  LYS A CA  1 
ATOM   672  C  C   . LYS A 1 80  ? -21.432 7.613   24.683  1.00   11.66 ? 80  LYS A C   1 
ATOM   673  O  O   . LYS A 1 80  ? -21.698 6.461   24.385  1.00   12.35 ? 80  LYS A O   1 
ATOM   674  C  CB  . LYS A 1 80  ? -21.665 9.820   23.558  1.00   15.97 ? 80  LYS A CB  1 
ATOM   675  C  CG  . LYS A 1 80  ? -23.079 9.613   23.330  1.00   17.07 ? 80  LYS A CG  1 
ATOM   676  C  CD  . LYS A 1 80  ? -23.786 10.980  23.254  1.00   19.91 ? 80  LYS A CD  1 
ATOM   677  C  CE  . LYS A 1 80  ? -23.362 11.749  22.059  1.00   27.69 ? 80  LYS A CE  1 
ATOM   678  N  NZ  . LYS A 1 80  ? -22.040 11.219  21.660  1.00   39.11 ? 80  LYS A NZ  1 
ATOM   679  N  N   . GLY A 1 81  ? -21.539 8.106   25.901  1.00   13.53 ? 81  GLY A N   1 
ATOM   680  C  CA  . GLY A 1 81  ? -22.022 7.224   27.002  1.00   14.44 ? 81  GLY A CA  1 
ATOM   681  C  C   . GLY A 1 81  ? -21.013 6.215   27.306  1.00   12.85 ? 81  GLY A C   1 
ATOM   682  O  O   . GLY A 1 81  ? -19.801 6.433   27.134  1.00   12.40 ? 81  GLY A O   1 
ATOM   683  N  N   . GLY A 1 82  ? -21.442 5.049   27.756  1.00   15.47 ? 82  GLY A N   1 
ATOM   684  C  CA  . GLY A 1 82  ? -20.469 4.075   28.186  1.00   17.35 ? 82  GLY A CA  1 
ATOM   685  C  C   . GLY A 1 82  ? -19.636 4.694   29.308  1.00   15.82 ? 82  GLY A C   1 
ATOM   686  O  O   . GLY A 1 82  ? -20.146 5.312   30.214  1.00   19.17 ? 82  GLY A O   1 
ATOM   687  N  N   . PRO A 1 83  ? -18.257 4.520   29.261  1.00   13.06 ? 83  PRO A N   1 
ATOM   688  C  CA  . PRO A 1 83  ? -17.396 5.131   30.174  1.00   14.10 ? 83  PRO A CA  1 
ATOM   689  C  C   . PRO A 1 83  ? -16.989 6.564   29.762  1.00   13.78 ? 83  PRO A C   1 
ATOM   690  O  O   . PRO A 1 83  ? -16.217 7.172   30.469  1.00   16.35 ? 83  PRO A O   1 
ATOM   691  C  CB  . PRO A 1 83  ? -16.085 4.268   30.036  1.00   13.80 ? 83  PRO A CB  1 
ATOM   692  C  CG  . PRO A 1 83  ? -16.110 3.910   28.542  1.00   12.41 ? 83  PRO A CG  1 
ATOM   693  C  CD  . PRO A 1 83  ? -17.570 3.704   28.255  1.00   12.17 ? 83  PRO A CD  1 
ATOM   694  N  N   . LEU A 1 84  ? -17.445 7.079   28.651  1.00   12.03 ? 84  LEU A N   1 
ATOM   695  C  CA  . LEU A 1 84  ? -16.973 8.295   28.078  1.00   12.15 ? 84  LEU A CA  1 
ATOM   696  C  C   . LEU A 1 84  ? -17.589 9.531   28.646  1.00   13.38 ? 84  LEU A C   1 
ATOM   697  O  O   . LEU A 1 84  ? -18.806 9.557   28.905  1.00   14.85 ? 84  LEU A O   1 
ATOM   698  C  CB  . LEU A 1 84  ? -17.191 8.285   26.600  1.00   10.60 ? 84  LEU A CB  1 
ATOM   699  C  CG  . LEU A 1 84  ? -16.603 7.009   25.872  1.00   9.90  ? 84  LEU A CG  1 
ATOM   700  C  CD1 . LEU A 1 84  ? -17.110 6.988   24.431  1.00   12.35 ? 84  LEU A CD1 1 
ATOM   701  C  CD2 . LEU A 1 84  ? -15.072 7.016   25.945  1.00   9.99  ? 84  LEU A CD2 1 
ATOM   702  N  N   . ASP A 1 85  ? -16.848 10.592  28.710  1.00   13.73 ? 85  ASP A N   1 
ATOM   703  C  CA  . ASP A 1 85  ? -17.372 11.956  28.956  1.00   16.10 ? 85  ASP A CA  1 
ATOM   704  C  C   . ASP A 1 85  ? -17.333 12.622  27.563  1.00   15.28 ? 85  ASP A C   1 
ATOM   705  O  O   . ASP A 1 85  ? -16.314 12.574  26.803  1.00   19.74 ? 85  ASP A O   1 
ATOM   706  C  CB  . ASP A 1 85  ? -16.400 12.690  29.888  1.00   21.94 ? 85  ASP A CB  1 
ATOM   707  C  CG  . ASP A 1 85  ? -16.503 12.256  31.299  1.00   31.47 ? 85  ASP A CG  1 
ATOM   708  O  OD1 . ASP A 1 85  ? -17.620 11.853  31.780  1.00   34.91 ? 85  ASP A OD1 1 
ATOM   709  O  OD2 . ASP A 1 85  ? -15.451 12.369  31.988  0.0000 47.90 ? 85  ASP A OD2 1 
ATOM   710  N  N   . GLY A 1 86  ? -18.387 13.308  27.186  1.00   20.46 ? 86  GLY A N   1 
ATOM   711  C  CA  . GLY A 1 86  ? -18.360 13.938  25.962  1.00   19.88 ? 86  GLY A CA  1 
ATOM   712  C  C   . GLY A 1 86  ? -18.601 12.989  24.726  1.00   19.48 ? 86  GLY A C   1 
ATOM   713  O  O   . GLY A 1 86  ? -19.084 11.857  24.827  1.00   24.01 ? 86  GLY A O   1 
ATOM   714  N  N   A THR A 1 87  ? -18.253 13.468  23.567  0.50   12.05 ? 87  THR A N   1 
ATOM   715  N  N   B THR A 1 87  ? -18.287 13.555  23.536  0.50   15.23 ? 87  THR A N   1 
ATOM   716  C  CA  A THR A 1 87  ? -18.674 12.794  22.394  0.50   10.34 ? 87  THR A CA  1 
ATOM   717  C  CA  B THR A 1 87  ? -18.641 13.076  22.147  0.50   16.13 ? 87  THR A CA  1 
ATOM   718  C  C   A THR A 1 87  ? -17.474 12.578  21.528  0.50   9.49  ? 87  THR A C   1 
ATOM   719  C  C   B THR A 1 87  ? -17.466 12.715  21.255  0.50   13.09 ? 87  THR A C   1 
ATOM   720  O  O   A THR A 1 87  ? -16.567 13.422  21.502  0.50   10.06 ? 87  THR A O   1 
ATOM   721  O  O   B THR A 1 87  ? -16.559 13.534  20.988  0.50   12.78 ? 87  THR A O   1 
ATOM   722  C  CB  A THR A 1 87  ? -19.690 13.715  21.656  0.50   12.11 ? 87  THR A CB  1 
ATOM   723  C  CB  B THR A 1 87  ? -19.391 14.154  21.327  0.50   16.99 ? 87  THR A CB  1 
ATOM   724  O  OG1 A THR A 1 87  ? -19.115 15.024  21.478  0.50   12.26 ? 87  THR A OG1 1 
ATOM   725  O  OG1 B THR A 1 87  ? -20.569 14.565  22.017  0.50   23.73 ? 87  THR A OG1 1 
ATOM   726  C  CG2 A THR A 1 87  ? -20.950 13.891  22.469  0.50   13.06 ? 87  THR A CG2 1 
ATOM   727  C  CG2 B THR A 1 87  ? -19.788 13.636  19.955  0.50   21.26 ? 87  THR A CG2 1 
ATOM   728  N  N   . TYR A 1 88  ? -17.511 11.481  20.791  1.00   9.88  ? 88  TYR A N   1 
ATOM   729  C  CA  . TYR A 1 88  ? -16.399 10.996  19.977  1.00   9.45  ? 88  TYR A CA  1 
ATOM   730  C  C   . TYR A 1 88  ? -16.882 10.690  18.611  1.00   10.07 ? 88  TYR A C   1 
ATOM   731  O  O   . TYR A 1 88  ? -17.871 9.957   18.425  1.00   13.01 ? 88  TYR A O   1 
ATOM   732  C  CB  . TYR A 1 88  ? -15.790 9.753   20.574  1.00   9.32  ? 88  TYR A CB  1 
ATOM   733  C  CG  . TYR A 1 88  ? -15.039 9.971   21.901  1.00   8.95  ? 88  TYR A CG  1 
ATOM   734  C  CD1 . TYR A 1 88  ? -15.683 10.301  23.101  1.00   10.24 ? 88  TYR A CD1 1 
ATOM   735  C  CD2 . TYR A 1 88  ? -13.637 9.829   21.953  1.00   8.23  ? 88  TYR A CD2 1 
ATOM   736  C  CE1 . TYR A 1 88  ? -14.996 10.509  24.282  1.00   9.74  ? 88  TYR A CE1 1 
ATOM   737  C  CE2 . TYR A 1 88  ? -12.958 9.992   23.148  1.00   8.07  ? 88  TYR A CE2 1 
ATOM   738  C  CZ  . TYR A 1 88  ? -13.618 10.292  24.294  1.00   8.56  ? 88  TYR A CZ  1 
ATOM   739  O  OH  . TYR A 1 88  ? -12.915 10.389  25.487  1.00   9.81  ? 88  TYR A OH  1 
ATOM   740  N  N   . ARG A 1 89  ? -16.231 11.171  17.595  1.00   8.72  ? 89  ARG A N   1 
ATOM   741  C  CA  . ARG A 1 89  ? -16.650 11.060  16.204  1.00   9.94  ? 89  ARG A CA  1 
ATOM   742  C  C   . ARG A 1 89  ? -15.913 9.976   15.467  1.00   7.70  ? 89  ARG A C   1 
ATOM   743  O  O   . ARG A 1 89  ? -14.666 9.881   15.521  1.00   8.31  ? 89  ARG A O   1 
ATOM   744  C  CB  . ARG A 1 89  ? -16.356 12.393  15.545  1.00   12.21 ? 89  ARG A CB  1 
ATOM   745  C  CG  . ARG A 1 89  ? -17.167 12.509  14.223  1.00   14.28 ? 89  ARG A CG  1 
ATOM   746  C  CD  . ARG A 1 89  ? -17.016 13.910  13.634  1.00   14.72 ? 89  ARG A CD  1 
ATOM   747  N  NE  . ARG A 1 89  ? -17.648 14.925  14.479  1.00   15.86 ? 89  ARG A NE  1 
ATOM   748  C  CZ  . ARG A 1 89  ? -17.510 16.241  14.324  1.00   14.85 ? 89  ARG A CZ  1 
ATOM   749  N  NH1 . ARG A 1 89  ? -16.760 16.722  13.350  1.00   18.01 ? 89  ARG A NH1 1 
ATOM   750  N  NH2 . ARG A 1 89  ? -18.126 17.079  15.146  1.00   15.84 ? 89  ARG A NH2 1 
ATOM   751  N  N   . LEU A 1 90  ? -16.635 9.153   14.722  1.00   8.92  ? 90  LEU A N   1 
ATOM   752  C  CA  . LEU A 1 90  ? -16.058 8.055   13.929  1.00   8.51  ? 90  LEU A CA  1 
ATOM   753  C  C   . LEU A 1 90  ? -15.237 8.601   12.794  1.00   9.05  ? 90  LEU A C   1 
ATOM   754  O  O   . LEU A 1 90  ? -15.701 9.441   11.992  1.00   10.63 ? 90  LEU A O   1 
ATOM   755  C  CB  . LEU A 1 90  ? -17.173 7.204   13.372  1.00   9.11  ? 90  LEU A CB  1 
ATOM   756  C  CG  . LEU A 1 90  ? -16.734 6.020   12.479  1.00   10.17 ? 90  LEU A CG  1 
ATOM   757  C  CD1 . LEU A 1 90  ? -15.957 4.956   13.296  1.00   10.44 ? 90  LEU A CD1 1 
ATOM   758  C  CD2 . LEU A 1 90  ? -17.959 5.370   11.834  1.00   12.16 ? 90  LEU A CD2 1 
ATOM   759  N  N   . ILE A 1 91  ? -14.007 8.149   12.699  1.00   8.55  ? 91  ILE A N   1 
ATOM   760  C  CA  . ILE A 1 91  ? -13.098 8.507   11.608  1.00   8.32  ? 91  ILE A CA  1 
ATOM   761  C  C   . ILE A 1 91  ? -12.803 7.349   10.685  1.00   8.11  ? 91  ILE A C   1 
ATOM   762  O  O   . ILE A 1 91  ? -12.687 7.545   9.448   1.00   8.88  ? 91  ILE A O   1 
ATOM   763  C  CB  . ILE A 1 91  ? -11.817 9.204   12.120  1.00   9.61  ? 91  ILE A CB  1 
ATOM   764  C  CG1 . ILE A 1 91  ? -10.910 9.591   10.951  1.00   12.05 ? 91  ILE A CG1 1 
ATOM   765  C  CG2 . ILE A 1 91  ? -11.064 8.408   13.140  1.00   10.17 ? 91  ILE A CG2 1 
ATOM   766  C  CD1 . ILE A 1 91  ? -9.791  10.597  11.332  1.00   14.44 ? 91  ILE A CD1 1 
ATOM   767  N  N   . GLN A 1 92  ? -12.613 6.128   11.206  1.00   8.10  ? 92  GLN A N   1 
ATOM   768  C  CA  . GLN A 1 92  ? -12.284 4.967   10.347  1.00   7.82  ? 92  GLN A CA  1 
ATOM   769  C  C   . GLN A 1 92  ? -12.573 3.733   11.109  1.00   7.30  ? 92  GLN A C   1 
ATOM   770  O  O   . GLN A 1 92  ? -12.608 3.741   12.357  1.00   7.87  ? 92  GLN A O   1 
ATOM   771  C  CB  . GLN A 1 92  ? -10.834 4.992   9.845   1.00   9.41  ? 92  GLN A CB  1 
ATOM   772  C  CG  . GLN A 1 92  ? -9.770  5.124   10.977  1.00   9.68  ? 92  GLN A CG  1 
ATOM   773  C  CD  . GLN A 1 92  ? -9.074  3.845   11.318  1.00   8.79  ? 92  GLN A CD  1 
ATOM   774  O  OE1 . GLN A 1 92  ? -9.616  2.717   11.160  1.00   9.41  ? 92  GLN A OE1 1 
ATOM   775  N  NE2 . GLN A 1 92  ? -7.837  3.955   11.814  1.00   10.14 ? 92  GLN A NE2 1 
ATOM   776  N  N   . PHE A 1 93  ? -12.774 2.613   10.402  1.00   7.42  ? 93  PHE A N   1 
ATOM   777  C  CA  . PHE A 1 93  ? -12.664 1.308   11.009  1.00   7.79  ? 93  PHE A CA  1 
ATOM   778  C  C   . PHE A 1 93  ? -11.729 0.457   10.199  1.00   7.33  ? 93  PHE A C   1 
ATOM   779  O  O   . PHE A 1 93  ? -11.483 0.670   9.006   1.00   8.40  ? 93  PHE A O   1 
ATOM   780  C  CB  . PHE A 1 93  ? -14.011 0.625   11.263  1.00   8.53  ? 93  PHE A CB  1 
ATOM   781  C  CG  . PHE A 1 93  ? -14.760 0.128   10.049  1.00   8.16  ? 93  PHE A CG  1 
ATOM   782  C  CD1 . PHE A 1 93  ? -14.370 -1.007  9.366   1.00   9.34  ? 93  PHE A CD1 1 
ATOM   783  C  CD2 . PHE A 1 93  ? -15.907 0.809   9.609   1.00   9.31  ? 93  PHE A CD2 1 
ATOM   784  C  CE1 . PHE A 1 93  ? -15.082 -1.475  8.230   1.00   10.05 ? 93  PHE A CE1 1 
ATOM   785  C  CE2 . PHE A 1 93  ? -16.629 0.345   8.499   1.00   10.18 ? 93  PHE A CE2 1 
ATOM   786  C  CZ  . PHE A 1 93  ? -16.242 -0.774  7.824   1.00   10.31 ? 93  PHE A CZ  1 
ATOM   787  N  N   . HIS A 1 94  ? -11.181 -0.576  10.884  1.00   7.49  ? 94  HIS A N   1 
ATOM   788  C  CA  . HIS A 1 94  ? -10.312 -1.553  10.279  1.00   7.41  ? 94  HIS A CA  1 
ATOM   789  C  C   . HIS A 1 94  ? -10.386 -2.828  11.123  1.00   6.67  ? 94  HIS A C   1 
ATOM   790  O  O   . HIS A 1 94  ? -11.016 -2.860  12.168  1.00   7.16  ? 94  HIS A O   1 
ATOM   791  C  CB  . HIS A 1 94  ? -8.870  -1.056  10.206  1.00   7.72  ? 94  HIS A CB  1 
ATOM   792  C  CG  . HIS A 1 94  ? -8.344  -0.758  11.576  1.00   7.06  ? 94  HIS A CG  1 
ATOM   793  N  ND1 . HIS A 1 94  ? -8.508  0.427   12.215  1.00   7.49  ? 94  HIS A ND1 1 
ATOM   794  C  CD2 . HIS A 1 94  ? -7.709  -1.587  12.478  1.00   6.95  ? 94  HIS A CD2 1 
ATOM   795  C  CE1 . HIS A 1 94  ? -8.001  0.333   13.464  1.00   7.02  ? 94  HIS A CE1 1 
ATOM   796  N  NE2 . HIS A 1 94  ? -7.550  -0.917  13.643  1.00   6.72  ? 94  HIS A NE2 1 
ATOM   797  N  N   . PHE A 1 95  ? -9.711  -3.860  10.637  1.00   7.42  ? 95  PHE A N   1 
ATOM   798  C  CA  . PHE A 1 95  ? -9.673  -5.160  11.309  1.00   7.25  ? 95  PHE A CA  1 
ATOM   799  C  C   . PHE A 1 95  ? -8.223  -5.575  11.521  1.00   7.22  ? 95  PHE A C   1 
ATOM   800  O  O   . PHE A 1 95  ? -7.291  -5.113  10.840  1.00   7.96  ? 95  PHE A O   1 
ATOM   801  C  CB  . PHE A 1 95  ? -10.391 -6.241  10.479  1.00   7.94  ? 95  PHE A CB  1 
ATOM   802  C  CG  . PHE A 1 95  ? -11.822 -5.962  10.160  1.00   7.61  ? 95  PHE A CG  1 
ATOM   803  C  CD1 . PHE A 1 95  ? -12.160 -5.109  9.094   1.00   8.79  ? 95  PHE A CD1 1 
ATOM   804  C  CD2 . PHE A 1 95  ? -12.853 -6.579  10.828  1.00   8.49  ? 95  PHE A CD2 1 
ATOM   805  C  CE1 . PHE A 1 95  ? -13.477 -4.907  8.743   1.00   9.14  ? 95  PHE A CE1 1 
ATOM   806  C  CE2 . PHE A 1 95  ? -14.183 -6.382  10.498  1.00   9.46  ? 95  PHE A CE2 1 
ATOM   807  C  CZ  . PHE A 1 95  ? -14.475 -5.517  9.437   1.00   9.32  ? 95  PHE A CZ  1 
ATOM   808  N  N   . HIS A 1 96  ? -8.068  -6.563  12.410  1.00   6.70  ? 96  HIS A N   1 
ATOM   809  C  CA  . HIS A 1 96  ? -6.865  -7.348  12.593  1.00   6.89  ? 96  HIS A CA  1 
ATOM   810  C  C   . HIS A 1 96  ? -7.292  -8.817  12.469  1.00   7.00  ? 96  HIS A C   1 
ATOM   811  O  O   . HIS A 1 96  ? -8.368  -9.151  12.983  1.00   7.47  ? 96  HIS A O   1 
ATOM   812  C  CB  . HIS A 1 96  ? -6.215  -7.116  13.973  1.00   7.29  ? 96  HIS A CB  1 
ATOM   813  C  CG  . HIS A 1 96  ? -5.944  -5.678  14.239  1.00   6.90  ? 96  HIS A CG  1 
ATOM   814  N  ND1 . HIS A 1 96  ? -4.698  -5.136  14.072  1.00   8.08  ? 96  HIS A ND1 1 
ATOM   815  C  CD2 . HIS A 1 96  ? -6.731  -4.641  14.642  1.00   7.14  ? 96  HIS A CD2 1 
ATOM   816  C  CE1 . HIS A 1 96  ? -4.748  -3.825  14.347  1.00   8.52  ? 96  HIS A CE1 1 
ATOM   817  N  NE2 . HIS A 1 96  ? -5.988  -3.503  14.690  1.00   6.55  ? 96  HIS A NE2 1 
ATOM   818  N  N   . TRP A 1 97  ? -6.504  -9.644  11.817  1.00   7.00  ? 97  TRP A N   1 
ATOM   819  C  CA  . TRP A 1 97  ? -6.907  -11.038 11.616  1.00   7.66  ? 97  TRP A CA  1 
ATOM   820  C  C   . TRP A 1 97  ? -5.713  -11.924 11.484  1.00   7.37  ? 97  TRP A C   1 
ATOM   821  O  O   . TRP A 1 97  ? -4.555  -11.504 11.381  1.00   8.15  ? 97  TRP A O   1 
ATOM   822  C  CB  . TRP A 1 97  ? -7.811  -11.125 10.382  1.00   7.95  ? 97  TRP A CB  1 
ATOM   823  C  CG  . TRP A 1 97  ? -7.171  -10.733 9.089   1.00   7.66  ? 97  TRP A CG  1 
ATOM   824  C  CD1 . TRP A 1 97  ? -6.489  -11.564 8.254   1.00   8.45  ? 97  TRP A CD1 1 
ATOM   825  C  CD2 . TRP A 1 97  ? -7.151  -9.448  8.510   1.00   7.77  ? 97  TRP A CD2 1 
ATOM   826  N  NE1 . TRP A 1 97  ? -6.061  -10.843 7.139   1.00   8.89  ? 97  TRP A NE1 1 
ATOM   827  C  CE2 . TRP A 1 97  ? -6.371  -9.520  7.301   1.00   8.46  ? 97  TRP A CE2 1 
ATOM   828  C  CE3 . TRP A 1 97  ? -7.609  -8.172  8.907   1.00   7.50  ? 97  TRP A CE3 1 
ATOM   829  C  CZ2 . TRP A 1 97  ? -6.238  -8.434  6.442   1.00   8.67  ? 97  TRP A CZ2 1 
ATOM   830  C  CZ3 . TRP A 1 97  ? -7.386  -7.073  8.092   1.00   8.09  ? 97  TRP A CZ3 1 
ATOM   831  C  CH2 . TRP A 1 97  ? -6.743  -7.203  6.866   1.00   8.94  ? 97  TRP A CH2 1 
ATOM   832  N  N   . GLY A 1 98  ? -5.997  -13.232 11.492  1.00   7.71  ? 98  GLY A N   1 
ATOM   833  C  CA  . GLY A 1 98  ? -4.990  -14.246 11.533  1.00   8.52  ? 98  GLY A CA  1 
ATOM   834  C  C   . GLY A 1 98  ? -4.773  -14.935 10.197  1.00   8.95  ? 98  GLY A C   1 
ATOM   835  O  O   . GLY A 1 98  ? -5.510  -14.776 9.222   1.00   9.59  ? 98  GLY A O   1 
ATOM   836  N  N   . SER A 1 99  ? -3.736  -15.783 10.196  1.00   9.65  ? 99  SER A N   1 
ATOM   837  C  CA  . SER A 1 99  ? -3.540  -16.719 9.075   1.00   9.51  ? 99  SER A CA  1 
ATOM   838  C  C   . SER A 1 99  ? -4.409  -17.955 9.168   1.00   11.12 ? 99  SER A C   1 
ATOM   839  O  O   . SER A 1 99  ? -4.533  -18.642 8.161   1.00   13.21 ? 99  SER A O   1 
ATOM   840  C  CB  . SER A 1 99  ? -2.084  -17.103 9.043   1.00   12.02 ? 99  SER A CB  1 
ATOM   841  O  OG  . SER A 1 99  ? -1.633  -17.599 10.272  1.00   11.99 ? 99  SER A OG  1 
ATOM   842  N  N   . LEU A 1 100 ? -5.018  -18.199 10.329  1.00   10.86 ? 100 LEU A N   1 
ATOM   843  C  CA  . LEU A 1 100 ? -5.831  -19.390 10.667  1.00   12.39 ? 100 LEU A CA  1 
ATOM   844  C  C   . LEU A 1 100 ? -6.903  -18.890 11.544  1.00   11.12 ? 100 LEU A C   1 
ATOM   845  O  O   . LEU A 1 100 ? -6.708  -17.878 12.253  1.00   10.85 ? 100 LEU A O   1 
ATOM   846  C  CB  . LEU A 1 100 ? -4.963  -20.384 11.543  1.00   18.37 ? 100 LEU A CB  1 
ATOM   847  C  CG  . LEU A 1 100 ? -3.576  -20.696 10.959  1.00   20.18 ? 100 LEU A CG  1 
ATOM   848  C  CD1 . LEU A 1 100 ? -2.493  -21.130 11.959  1.00   25.20 ? 100 LEU A CD1 1 
ATOM   849  C  CD2 . LEU A 1 100 ? -3.913  -21.787 9.988   1.00   29.57 ? 100 LEU A CD2 1 
ATOM   850  N  N   . ASP A 1 101 ? -7.997  -19.632 11.590  1.00   11.55 ? 101 ASP A N   1 
ATOM   851  C  CA  . ASP A 1 101 ? -9.101  -19.200 12.404  1.00   11.35 ? 101 ASP A CA  1 
ATOM   852  C  C   . ASP A 1 101 ? -8.845  -19.112 13.893  1.00   10.91 ? 101 ASP A C   1 
ATOM   853  O  O   . ASP A 1 101 ? -9.496  -18.376 14.588  1.00   12.51 ? 101 ASP A O   1 
ATOM   854  C  CB  . ASP A 1 101 ? -10.354 -20.074 12.157  1.00   13.46 ? 101 ASP A CB  1 
ATOM   855  C  CG  . ASP A 1 101 ? -10.869 -20.114 10.779  1.00   16.18 ? 101 ASP A CG  1 
ATOM   856  O  OD1 . ASP A 1 101 ? -10.581 -19.243 9.924   1.00   14.39 ? 101 ASP A OD1 1 
ATOM   857  O  OD2 . ASP A 1 101 ? -11.739 -20.965 10.555  1.00   20.34 ? 101 ASP A OD2 1 
ATOM   858  N  N   . GLY A 1 102 ? -7.849  -19.865 14.360  1.00   10.47 ? 102 GLY A N   1 
ATOM   859  C  CA  . GLY A 1 102 ? -7.540  -19.878 15.784  1.00   11.12 ? 102 GLY A CA  1 
ATOM   860  C  C   . GLY A 1 102 ? -6.738  -18.711 16.347  1.00   9.91  ? 102 GLY A C   1 
ATOM   861  O  O   . GLY A 1 102 ? -6.399  -18.705 17.527  1.00   11.33 ? 102 GLY A O   1 
ATOM   862  N  N   A GLN A 1 103 ? -6.470  -17.690 15.530  0.50   9.02  ? 103 GLN A N   1 
ATOM   863  N  N   B GLN A 1 103 ? -6.415  -17.730 15.501  0.50   9.97  ? 103 GLN A N   1 
ATOM   864  C  CA  A GLN A 1 103 ? -5.734  -16.541 16.012  0.50   7.86  ? 103 GLN A CA  1 
ATOM   865  C  CA  B GLN A 1 103 ? -5.832  -16.512 15.991  0.50   9.58  ? 103 GLN A CA  1 
ATOM   866  C  C   A GLN A 1 103 ? -6.111  -15.360 15.155  0.50   7.39  ? 103 GLN A C   1 
ATOM   867  C  C   B GLN A 1 103 ? -6.264  -15.336 15.120  0.50   7.97  ? 103 GLN A C   1 
ATOM   868  O  O   A GLN A 1 103 ? -6.546  -15.566 14.053  0.50   7.71  ? 103 GLN A O   1 
ATOM   869  O  O   B GLN A 1 103 ? -6.907  -15.531 14.012  0.50   8.57  ? 103 GLN A O   1 
ATOM   870  C  CB  A GLN A 1 103 ? -4.248  -16.780 15.951  0.50   7.93  ? 103 GLN A CB  1 
ATOM   871  C  CB  B GLN A 1 103 ? -4.302  -16.582 16.196  0.50   12.06 ? 103 GLN A CB  1 
ATOM   872  C  CG  A GLN A 1 103 ? -3.698  -16.956 14.549  0.50   7.75  ? 103 GLN A CG  1 
ATOM   873  C  CG  B GLN A 1 103 ? -3.529  -16.873 14.956  0.50   15.03 ? 103 GLN A CG  1 
ATOM   874  C  CD  A GLN A 1 103 ? -2.259  -17.455 14.689  0.50   9.05  ? 103 GLN A CD  1 
ATOM   875  C  CD  B GLN A 1 103 ? -2.492  -17.913 15.262  0.50   25.24 ? 103 GLN A CD  1 
ATOM   876  O  OE1 A GLN A 1 103 ? -1.993  -18.458 15.452  0.50   12.80 ? 103 GLN A OE1 1 
ATOM   877  O  OE1 B GLN A 1 103 ? -1.641  -17.743 16.086  0.50   16.53 ? 103 GLN A OE1 1 
ATOM   878  N  NE2 A GLN A 1 103 ? -1.381  -17.026 13.879  0.50   8.35  ? 103 GLN A NE2 1 
ATOM   879  N  NE2 B GLN A 1 103 ? -2.674  -19.060 14.722  0.50   19.37 ? 103 GLN A NE2 1 
ATOM   880  N  N   . GLY A 1 104 ? -5.899  -14.147 15.599  1.00   7.61  ? 104 GLY A N   1 
ATOM   881  C  CA  . GLY A 1 104 ? -6.169  -12.944 14.823  1.00   7.86  ? 104 GLY A CA  1 
ATOM   882  C  C   . GLY A 1 104 ? -6.579  -11.782 15.647  1.00   7.25  ? 104 GLY A C   1 
ATOM   883  O  O   . GLY A 1 104 ? -6.348  -10.639 15.283  1.00   7.79  ? 104 GLY A O   1 
ATOM   884  N  N   . SER A 1 105 ? -7.319  -12.013 16.782  1.00   7.32  ? 105 SER A N   1 
ATOM   885  C  CA  . SER A 1 105 ? -7.701  -10.906 17.592  1.00   7.02  ? 105 SER A CA  1 
ATOM   886  C  C   . SER A 1 105 ? -6.504  -10.346 18.344  1.00   6.81  ? 105 SER A C   1 
ATOM   887  O  O   . SER A 1 105 ? -5.495  -11.008 18.588  1.00   8.12  ? 105 SER A O   1 
ATOM   888  C  CB  . SER A 1 105 ? -8.827  -11.248 18.549  1.00   7.01  ? 105 SER A CB  1 
ATOM   889  O  OG  . SER A 1 105 ? -8.493  -12.203 19.534  1.00   7.67  ? 105 SER A OG  1 
ATOM   890  N  N   . GLU A 1 106 ? -6.653  -9.093  18.764  1.00   7.24  ? 106 GLU A N   1 
ATOM   891  C  CA  . GLU A 1 106 ? -5.639  -8.370  19.567  1.00   7.00  ? 106 GLU A CA  1 
ATOM   892  C  C   . GLU A 1 106 ? -5.976  -8.547  21.042  1.00   6.90  ? 106 GLU A C   1 
ATOM   893  O  O   . GLU A 1 106 ? -5.182  -9.123  21.805  1.00   7.41  ? 106 GLU A O   1 
ATOM   894  C  CB  . GLU A 1 106 ? -5.587  -6.929  19.139  1.00   6.66  ? 106 GLU A CB  1 
ATOM   895  C  CG  . GLU A 1 106 ? -5.141  -6.772  17.695  1.00   8.91  ? 106 GLU A CG  1 
ATOM   896  C  CD  . GLU A 1 106 ? -4.462  -5.505  17.417  1.00   7.26  ? 106 GLU A CD  1 
ATOM   897  O  OE1 . GLU A 1 106 ? -5.014  -4.427  17.678  1.00   7.51  ? 106 GLU A OE1 1 
ATOM   898  O  OE2 . GLU A 1 106 ? -3.278  -5.575  16.933  1.00   8.66  ? 106 GLU A OE2 1 
ATOM   899  N  N   . HIS A 1 107 ? -7.151  -8.102  21.470  1.00   6.82  ? 107 HIS A N   1 
ATOM   900  C  CA  . HIS A 1 107 ? -7.604  -8.482  22.774  1.00   6.48  ? 107 HIS A CA  1 
ATOM   901  C  C   . HIS A 1 107 ? -7.898  -9.981  22.795  1.00   6.65  ? 107 HIS A C   1 
ATOM   902  O  O   . HIS A 1 107 ? -8.227  -10.603 21.789  1.00   7.31  ? 107 HIS A O   1 
ATOM   903  C  CB  . HIS A 1 107 ? -8.848  -7.687  23.168  1.00   7.16  ? 107 HIS A CB  1 
ATOM   904  C  CG  . HIS A 1 107 ? -8.541  -6.244  23.300  1.00   6.56  ? 107 HIS A CG  1 
ATOM   905  N  ND1 . HIS A 1 107 ? -8.601  -5.351  22.270  1.00   6.97  ? 107 HIS A ND1 1 
ATOM   906  C  CD2 . HIS A 1 107 ? -8.049  -5.522  24.385  1.00   7.02  ? 107 HIS A CD2 1 
ATOM   907  C  CE1 . HIS A 1 107 ? -8.151  -4.139  22.720  1.00   7.60  ? 107 HIS A CE1 1 
ATOM   908  N  NE2 . HIS A 1 107 ? -7.824  -4.219  24.001  1.00   7.11  ? 107 HIS A NE2 1 
ATOM   909  N  N   . THR A 1 108 ? -7.761  -10.552 23.993  1.00   7.07  ? 108 THR A N   1 
ATOM   910  C  CA  . THR A 1 108 ? -8.122  -11.941 24.254  1.00   7.34  ? 108 THR A CA  1 
ATOM   911  C  C   . THR A 1 108 ? -9.054  -11.931 25.469  1.00   6.90  ? 108 THR A C   1 
ATOM   912  O  O   . THR A 1 108 ? -9.053  -10.984 26.245  1.00   7.62  ? 108 THR A O   1 
ATOM   913  C  CB  . THR A 1 108 ? -6.901  -12.843 24.443  1.00   8.01  ? 108 THR A CB  1 
ATOM   914  O  OG1 . THR A 1 108 ? -6.058  -12.357 25.488  1.00   8.64  ? 108 THR A OG1 1 
ATOM   915  C  CG2 . THR A 1 108 ? -6.094  -12.903 23.149  1.00   9.44  ? 108 THR A CG2 1 
ATOM   916  N  N   . VAL A 1 109 ? -9.818  -13.026 25.611  1.00   7.43  ? 109 VAL A N   1 
ATOM   917  C  CA  . VAL A 1 109 ? -10.814 -13.119 26.699  1.00   7.94  ? 109 VAL A CA  1 
ATOM   918  C  C   . VAL A 1 109 ? -10.478 -14.418 27.444  1.00   7.98  ? 109 VAL A C   1 
ATOM   919  O  O   . VAL A 1 109 ? -10.638 -15.507 26.886  1.00   8.49  ? 109 VAL A O   1 
ATOM   920  C  CB  . VAL A 1 109 ? -12.246 -13.132 26.158  1.00   8.85  ? 109 VAL A CB  1 
ATOM   921  C  CG1 . VAL A 1 109 ? -13.262 -13.254 27.321  1.00   10.12 ? 109 VAL A CG1 1 
ATOM   922  C  CG2 . VAL A 1 109 ? -12.520 -11.861 25.349  1.00   9.62  ? 109 VAL A CG2 1 
ATOM   923  N  N   . ASP A 1 110 ? -9.949  -14.295 28.659  1.00   8.71  ? 110 ASP A N   1 
ATOM   924  C  CA  . ASP A 1 110 ? -9.461  -15.507 29.381  1.00   9.94  ? 110 ASP A CA  1 
ATOM   925  C  C   . ASP A 1 110 ? -8.532  -16.307 28.473  1.00   9.70  ? 110 ASP A C   1 
ATOM   926  O  O   . ASP A 1 110 ? -8.589  -17.543 28.424  1.00   10.32 ? 110 ASP A O   1 
ATOM   927  C  CB  . ASP A 1 110 ? -10.644 -16.346 29.894  1.00   11.64 ? 110 ASP A CB  1 
ATOM   928  C  CG  . ASP A 1 110 ? -11.449 -15.587 30.902  1.00   11.96 ? 110 ASP A CG  1 
ATOM   929  O  OD1 . ASP A 1 110 ? -10.920 -14.705 31.608  1.00   12.54 ? 110 ASP A OD1 1 
ATOM   930  O  OD2 . ASP A 1 110 ? -12.637 -15.907 31.032  1.00   14.43 ? 110 ASP A OD2 1 
ATOM   931  N  N   . LYS A 1 111 ? -7.660  -15.605 27.751  1.00   8.85  ? 111 LYS A N   1 
ATOM   932  C  CA  . LYS A 1 111 ? -6.660  -16.124 26.871  1.00   9.45  ? 111 LYS A CA  1 
ATOM   933  C  C   . LYS A 1 111 ? -7.251  -16.642 25.543  1.00   8.86  ? 111 LYS A C   1 
ATOM   934  O  O   . LYS A 1 111 ? -6.456  -17.033 24.649  1.00   10.92 ? 111 LYS A O   1 
ATOM   935  C  CB  . LYS A 1 111 ? -5.739  -17.168 27.499  1.00   11.12 ? 111 LYS A CB  1 
ATOM   936  C  CG  . LYS A 1 111 ? -4.986  -16.594 28.750  1.00   14.71 ? 111 LYS A CG  1 
ATOM   937  C  CD  . LYS A 1 111 ? -4.094  -15.332 28.411  1.00   15.97 ? 111 LYS A CD  1 
ATOM   938  C  CE  . LYS A 1 111 ? -3.254  -14.753 29.584  1.00   18.39 ? 111 LYS A CE  1 
ATOM   939  N  NZ  . LYS A 1 111 ? -2.152  -15.686 29.811  1.00   19.57 ? 111 LYS A NZ  1 
ATOM   940  N  N   . LYS A 1 112 ? -8.543  -16.620 25.352  1.00   8.65  ? 112 LYS A N   1 
ATOM   941  C  CA  . LYS A 1 112 ? -9.121  -17.023 24.074  1.00   9.44  ? 112 LYS A CA  1 
ATOM   942  C  C   . LYS A 1 112 ? -8.788  -15.986 23.003  1.00   8.51  ? 112 LYS A C   1 
ATOM   943  O  O   . LYS A 1 112 ? -9.042  -14.767 23.206  1.00   8.38  ? 112 LYS A O   1 
ATOM   944  C  CB  . LYS A 1 112 ? -10.645 -17.092 24.165  1.00   10.68 ? 112 LYS A CB  1 
ATOM   945  C  CG  . LYS A 1 112 ? -11.339 -17.472 22.849  1.00   11.54 ? 112 LYS A CG  1 
ATOM   946  C  CD  . LYS A 1 112 ? -12.849 -17.434 22.922  1.00   13.09 ? 112 LYS A CD  1 
ATOM   947  C  CE  . LYS A 1 112 ? -13.488 -17.660 21.606  1.00   14.41 ? 112 LYS A CE  1 
ATOM   948  N  NZ  . LYS A 1 112 ? -13.336 -18.988 21.160  1.00   14.33 ? 112 LYS A NZ  1 
ATOM   949  N  N   A LYS A 1 113 ? -8.173  -16.407 21.893  0.50   8.39  ? 113 LYS A N   1 
ATOM   950  N  N   B LYS A 1 113 ? -8.379  -16.502 21.845  0.50   8.32  ? 113 LYS A N   1 
ATOM   951  C  CA  A LYS A 1 113 ? -8.015  -15.589 20.680  0.50   8.85  ? 113 LYS A CA  1 
ATOM   952  C  CA  B LYS A 1 113 ? -8.145  -15.705 20.652  0.50   8.57  ? 113 LYS A CA  1 
ATOM   953  C  C   A LYS A 1 113 ? -9.134  -15.880 19.671  0.50   8.03  ? 113 LYS A C   1 
ATOM   954  C  C   B LYS A 1 113 ? -9.312  -15.910 19.750  0.50   8.50  ? 113 LYS A C   1 
ATOM   955  O  O   A LYS A 1 113 ? -9.375  -17.044 19.261  0.50   8.25  ? 113 LYS A O   1 
ATOM   956  O  O   B LYS A 1 113 ? -9.804  -17.034 19.567  0.50   8.94  ? 113 LYS A O   1 
ATOM   957  C  CB  A LYS A 1 113 ? -6.692  -15.935 20.021  0.50   9.50  ? 113 LYS A CB  1 
ATOM   958  C  CB  B LYS A 1 113 ? -6.880  -16.148 19.927  0.50   8.87  ? 113 LYS A CB  1 
ATOM   959  C  CG  A LYS A 1 113 ? -5.450  -15.522 20.771  0.50   9.12  ? 113 LYS A CG  1 
ATOM   960  C  CG  B LYS A 1 113 ? -5.551  -15.915 20.670  0.50   8.90  ? 113 LYS A CG  1 
ATOM   961  C  CD  A LYS A 1 113 ? -4.256  -16.302 20.259  0.50   11.04 ? 113 LYS A CD  1 
ATOM   962  C  CD  B LYS A 1 113 ? -4.365  -16.332 19.818  0.50   11.29 ? 113 LYS A CD  1 
ATOM   963  C  CE  A LYS A 1 113 ? -3.012  -15.714 20.941  0.50   13.21 ? 113 LYS A CE  1 
ATOM   964  C  CE  B LYS A 1 113 ? -2.986  -15.996 20.454  0.50   12.17 ? 113 LYS A CE  1 
ATOM   965  N  NZ  A LYS A 1 113 ? -1.735  -16.383 20.668  0.50   17.35 ? 113 LYS A NZ  1 
ATOM   966  N  NZ  B LYS A 1 113 ? -2.685  -16.525 21.796  0.50   11.33 ? 113 LYS A NZ  1 
ATOM   967  N  N   . TYR A 1 114 ? -9.806  -14.798 19.204  1.00   7.93  ? 114 TYR A N   1 
ATOM   968  C  CA  . TYR A 1 114 ? -10.798 -14.854 18.175  1.00   8.40  ? 114 TYR A CA  1 
ATOM   969  C  C   . TYR A 1 114 ? -10.123 -14.799 16.781  1.00   7.61  ? 114 TYR A C   1 
ATOM   970  O  O   . TYR A 1 114 ? -8.933  -14.500 16.659  1.00   8.40  ? 114 TYR A O   1 
ATOM   971  C  CB  . TYR A 1 114 ? -11.850 -13.743 18.308  1.00   8.17  ? 114 TYR A CB  1 
ATOM   972  C  CG  . TYR A 1 114 ? -12.809 -13.945 19.457  1.00   8.09  ? 114 TYR A CG  1 
ATOM   973  C  CD1 . TYR A 1 114 ? -12.494 -13.525 20.745  1.00   9.88  ? 114 TYR A CD1 1 
ATOM   974  C  CD2 . TYR A 1 114 ? -14.035 -14.551 19.248  1.00   9.73  ? 114 TYR A CD2 1 
ATOM   975  C  CE1 . TYR A 1 114 ? -13.380 -13.704 21.791  1.00   11.39 ? 114 TYR A CE1 1 
ATOM   976  C  CE2 . TYR A 1 114 ? -14.926 -14.736 20.287  1.00   11.20 ? 114 TYR A CE2 1 
ATOM   977  C  CZ  . TYR A 1 114 ? -14.592 -14.312 21.558  1.00   11.94 ? 114 TYR A CZ  1 
ATOM   978  O  OH  . TYR A 1 114 ? -15.465 -14.486 22.606  1.00   16.42 ? 114 TYR A OH  1 
ATOM   979  N  N   . ALA A 1 115 ? -10.886 -15.109 15.722  1.00   7.72  ? 115 ALA A N   1 
ATOM   980  C  CA  . ALA A 1 115 ? -10.342 -15.133 14.378  1.00   7.74  ? 115 ALA A CA  1 
ATOM   981  C  C   . ALA A 1 115 ? -9.989  -13.734 13.899  1.00   7.73  ? 115 ALA A C   1 
ATOM   982  O  O   . ALA A 1 115 ? -9.123  -13.595 13.014  1.00   8.07  ? 115 ALA A O   1 
ATOM   983  C  CB  . ALA A 1 115 ? -11.365 -15.761 13.428  1.00   9.78  ? 115 ALA A CB  1 
ATOM   984  N  N   . ALA A 1 116 ? -10.620 -12.697 14.424  1.00   7.70  ? 116 ALA A N   1 
ATOM   985  C  CA  . ALA A 1 116 ? -10.333 -11.350 13.964  1.00   7.42  ? 116 ALA A CA  1 
ATOM   986  C  C   . ALA A 1 116 ? -10.918 -10.392 14.978  1.00   6.83  ? 116 ALA A C   1 
ATOM   987  O  O   . ALA A 1 116 ? -11.662 -10.792 15.893  1.00   7.31  ? 116 ALA A O   1 
ATOM   988  C  CB  . ALA A 1 116 ? -10.858 -11.082 12.555  1.00   8.19  ? 116 ALA A CB  1 
ATOM   989  N  N   . GLU A 1 117 ? -10.607 -9.099  14.819  1.00   6.93  ? 117 GLU A N   1 
ATOM   990  C  CA  . GLU A 1 117 ? -11.135 -8.074  15.693  1.00   6.65  ? 117 GLU A CA  1 
ATOM   991  C  C   . GLU A 1 117 ? -11.322 -6.806  14.852  1.00   6.58  ? 117 GLU A C   1 
ATOM   992  O  O   . GLU A 1 117 ? -10.393 -6.416  14.139  1.00   8.28  ? 117 GLU A O   1 
ATOM   993  C  CB  . GLU A 1 117 ? -10.169 -7.805  16.870  1.00   7.49  ? 117 GLU A CB  1 
ATOM   994  C  CG  . GLU A 1 117 ? -10.674 -6.867  17.922  1.00   7.32  ? 117 GLU A CG  1 
ATOM   995  C  CD  . GLU A 1 117 ? -9.761  -6.797  19.145  1.00   6.94  ? 117 GLU A CD  1 
ATOM   996  O  OE1 . GLU A 1 117 ? -9.092  -7.820  19.441  1.00   8.29  ? 117 GLU A OE1 1 
ATOM   997  O  OE2 . GLU A 1 117 ? -9.707  -5.719  19.795  1.00   8.01  ? 117 GLU A OE2 1 
ATOM   998  N  N   . LEU A 1 118 ? -12.499 -6.215  14.968  1.00   6.73  ? 118 LEU A N   1 
ATOM   999  C  CA  . LEU A 1 118 ? -12.861 -4.964  14.326  1.00   6.88  ? 118 LEU A CA  1 
ATOM   1000 C  C   . LEU A 1 118 ? -12.631 -3.837  15.302  1.00   6.87  ? 118 LEU A C   1 
ATOM   1001 O  O   . LEU A 1 118 ? -13.055 -3.905  16.465  1.00   6.61  ? 118 LEU A O   1 
ATOM   1002 C  CB  . LEU A 1 118 ? -14.368 -5.067  13.990  1.00   7.59  ? 118 LEU A CB  1 
ATOM   1003 C  CG  . LEU A 1 118 ? -15.104 -3.759  13.597  1.00   7.81  ? 118 LEU A CG  1 
ATOM   1004 C  CD1 . LEU A 1 118 ? -14.539 -3.116  12.377  1.00   8.08  ? 118 LEU A CD1 1 
ATOM   1005 C  CD2 . LEU A 1 118 ? -16.567 -4.104  13.341  1.00   9.51  ? 118 LEU A CD2 1 
ATOM   1006 N  N   . HIS A 1 119 ? -12.027 -2.742  14.829  1.00   6.24  ? 119 HIS A N   1 
ATOM   1007 C  CA  . HIS A 1 119 ? -11.795 -1.538  15.575  1.00   6.13  ? 119 HIS A CA  1 
ATOM   1008 C  C   . HIS A 1 119 ? -12.470 -0.374  14.902  1.00   6.37  ? 119 HIS A C   1 
ATOM   1009 O  O   . HIS A 1 119 ? -12.084 -0.006  13.780  1.00   7.17  ? 119 HIS A O   1 
ATOM   1010 C  CB  . HIS A 1 119 ? -10.299 -1.253  15.691  1.00   7.06  ? 119 HIS A CB  1 
ATOM   1011 C  CG  . HIS A 1 119 ? -9.567  -2.224  16.557  1.00   6.43  ? 119 HIS A CG  1 
ATOM   1012 N  ND1 . HIS A 1 119 ? -8.222  -2.429  16.546  1.00   6.12  ? 119 HIS A ND1 1 
ATOM   1013 C  CD2 . HIS A 1 119 ? -10.121 -3.060  17.512  1.00   6.70  ? 119 HIS A CD2 1 
ATOM   1014 C  CE1 . HIS A 1 119 ? -7.953  -3.369  17.438  1.00   6.73  ? 119 HIS A CE1 1 
ATOM   1015 N  NE2 . HIS A 1 119 ? -9.063  -3.743  18.069  1.00   6.69  ? 119 HIS A NE2 1 
ATOM   1016 N  N   . LEU A 1 120 ? -13.463 0.207   15.571  1.00   6.63  ? 120 LEU A N   1 
ATOM   1017 C  CA  . LEU A 1 120 ? -14.164 1.426   15.129  1.00   6.99  ? 120 LEU A CA  1 
ATOM   1018 C  C   . LEU A 1 120 ? -13.489 2.570   15.926  1.00   6.32  ? 120 LEU A C   1 
ATOM   1019 O  O   . LEU A 1 120 ? -13.617 2.620   17.138  1.00   6.65  ? 120 LEU A O   1 
ATOM   1020 C  CB  . LEU A 1 120 ? -15.617 1.334   15.331  1.00   7.56  ? 120 LEU A CB  1 
ATOM   1021 C  CG  . LEU A 1 120 ? -16.333 0.249   14.463  1.00   8.82  ? 120 LEU A CG  1 
ATOM   1022 C  CD1 . LEU A 1 120 ? -17.204 -0.622  15.312  1.00   11.73 ? 120 LEU A CD1 1 
ATOM   1023 C  CD2 . LEU A 1 120 ? -17.144 0.922   13.372  1.00   11.23 ? 120 LEU A CD2 1 
ATOM   1024 N  N   . VAL A 1 121 ? -12.806 3.455   15.200  1.00   7.08  ? 121 VAL A N   1 
ATOM   1025 C  CA  . VAL A 1 121 ? -11.944 4.470   15.811  1.00   6.75  ? 121 VAL A CA  1 
ATOM   1026 C  C   . VAL A 1 121 ? -12.636 5.813   15.836  1.00   6.94  ? 121 VAL A C   1 
ATOM   1027 O  O   . VAL A 1 121 ? -13.065 6.309   14.780  1.00   7.81  ? 121 VAL A O   1 
ATOM   1028 C  CB  . VAL A 1 121 ? -10.640 4.574   15.017  1.00   7.48  ? 121 VAL A CB  1 
ATOM   1029 C  CG1 . VAL A 1 121 ? -9.688  5.612   15.637  1.00   8.61  ? 121 VAL A CG1 1 
ATOM   1030 C  CG2 . VAL A 1 121 ? -9.967  3.183   14.890  1.00   7.87  ? 121 VAL A CG2 1 
ATOM   1031 N  N   . HIS A 1 122 ? -12.703 6.416   17.019  1.00   6.74  ? 122 HIS A N   1 
ATOM   1032 C  CA  . HIS A 1 122 ? -13.416 7.679   17.205  1.00   7.11  ? 122 HIS A CA  1 
ATOM   1033 C  C   . HIS A 1 122 ? -12.521 8.682   17.961  1.00   7.69  ? 122 HIS A C   1 
ATOM   1034 O  O   . HIS A 1 122 ? -11.786 8.263   18.865  1.00   8.22  ? 122 HIS A O   1 
ATOM   1035 C  CB  . HIS A 1 122 ? -14.664 7.507   18.060  1.00   7.69  ? 122 HIS A CB  1 
ATOM   1036 C  CG  . HIS A 1 122 ? -15.544 6.372   17.625  1.00   7.27  ? 122 HIS A CG  1 
ATOM   1037 N  ND1 . HIS A 1 122 ? -15.252 5.074   17.895  1.00   7.80  ? 122 HIS A ND1 1 
ATOM   1038 C  CD2 . HIS A 1 122 ? -16.782 6.323   17.007  1.00   8.42  ? 122 HIS A CD2 1 
ATOM   1039 C  CE1 . HIS A 1 122 ? -16.250 4.301   17.424  1.00   7.96  ? 122 HIS A CE1 1 
ATOM   1040 N  NE2 . HIS A 1 122 ? -17.182 5.021   16.870  1.00   8.59  ? 122 HIS A NE2 1 
ATOM   1041 N  N   . TRP A 1 123 ? -12.630 9.960   17.637  1.00   7.80  ? 123 TRP A N   1 
ATOM   1042 C  CA  . TRP A 1 123 ? -11.847 11.005  18.336  1.00   8.09  ? 123 TRP A CA  1 
ATOM   1043 C  C   . TRP A 1 123 ? -12.693 11.962  19.084  1.00   7.50  ? 123 TRP A C   1 
ATOM   1044 O  O   . TRP A 1 123 ? -13.840 12.303  18.672  1.00   8.65  ? 123 TRP A O   1 
ATOM   1045 C  CB  . TRP A 1 123 ? -10.889 11.731  17.361  1.00   9.90  ? 123 TRP A CB  1 
ATOM   1046 C  CG  . TRP A 1 123 ? -11.561 12.365  16.176  1.00   10.05 ? 123 TRP A CG  1 
ATOM   1047 C  CD1 . TRP A 1 123 ? -11.786 11.774  14.963  1.00   10.14 ? 123 TRP A CD1 1 
ATOM   1048 C  CD2 . TRP A 1 123 ? -12.054 13.720  16.085  1.00   10.57 ? 123 TRP A CD2 1 
ATOM   1049 N  NE1 . TRP A 1 123 ? -12.388 12.612  14.122  1.00   11.20 ? 123 TRP A NE1 1 
ATOM   1050 C  CE2 . TRP A 1 123 ? -12.581 13.842  14.750  1.00   11.95 ? 123 TRP A CE2 1 
ATOM   1051 C  CE3 . TRP A 1 123 ? -12.086 14.824  16.930  1.00   11.53 ? 123 TRP A CE3 1 
ATOM   1052 C  CZ2 . TRP A 1 123 ? -13.174 15.016  14.284  1.00   13.21 ? 123 TRP A CZ2 1 
ATOM   1053 C  CZ3 . TRP A 1 123 ? -12.709 16.015  16.454  1.00   12.74 ? 123 TRP A CZ3 1 
ATOM   1054 C  CH2 . TRP A 1 123 ? -13.239 16.080  15.161  1.00   13.47 ? 123 TRP A CH2 1 
ATOM   1055 N  N   . ASN A 1 124 ? -12.202 12.412  20.219  1.00   7.94  ? 124 ASN A N   1 
ATOM   1056 C  CA  . ASN A 1 124 ? -12.942 13.303  21.110  1.00   8.70  ? 124 ASN A CA  1 
ATOM   1057 C  C   . ASN A 1 124 ? -13.076 14.681  20.534  1.00   8.86  ? 124 ASN A C   1 
ATOM   1058 O  O   . ASN A 1 124 ? -12.057 15.354  20.257  1.00   9.46  ? 124 ASN A O   1 
ATOM   1059 C  CB  . ASN A 1 124 ? -12.181 13.356  22.439  1.00   9.06  ? 124 ASN A CB  1 
ATOM   1060 C  CG  . ASN A 1 124 ? -12.916 13.971  23.542  1.00   9.43  ? 124 ASN A CG  1 
ATOM   1061 O  OD1 . ASN A 1 124 ? -13.774 14.851  23.322  1.00   10.58 ? 124 ASN A OD1 1 
ATOM   1062 N  ND2 . ASN A 1 124 ? -12.639 13.535  24.756  1.00   10.84 ? 124 ASN A ND2 1 
ATOM   1063 N  N   . THR A 1 125 ? -14.330 15.097  20.316  1.00   9.09  ? 125 THR A N   1 
ATOM   1064 C  CA  . THR A 1 125 ? -14.547 16.384  19.619  1.00   10.61 ? 125 THR A CA  1 
ATOM   1065 C  C   . THR A 1 125 ? -14.007 17.577  20.352  1.00   10.74 ? 125 THR A C   1 
ATOM   1066 O  O   . THR A 1 125 ? -13.828 18.616  19.756  1.00   12.65 ? 125 THR A O   1 
ATOM   1067 C  CB  . THR A 1 125 ? -16.051 16.536  19.261  1.00   12.50 ? 125 THR A CB  1 
ATOM   1068 O  OG1 . THR A 1 125 ? -16.831 16.534  20.434  1.00   17.04 ? 125 THR A OG1 1 
ATOM   1069 C  CG2 . THR A 1 125 ? -16.496 15.459  18.251  1.00   15.57 ? 125 THR A CG2 1 
ATOM   1070 N  N   A LYS A 1 126 ? -13.873 17.461  21.584  0.50   8.43  ? 127 LYS A N   1 
ATOM   1071 N  N   B LYS A 1 126 ? -13.522 17.440  21.881  0.50   9.14  ? 127 LYS A N   1 
ATOM   1072 C  CA  A LYS A 1 126 ? -13.365 18.582  22.314  0.50   9.57  ? 127 LYS A CA  1 
ATOM   1073 C  CA  B LYS A 1 126 ? -13.011 18.591  22.598  0.50   10.07 ? 127 LYS A CA  1 
ATOM   1074 C  C   A LYS A 1 126 ? -11.939 18.964  21.871  0.50   8.72  ? 127 LYS A C   1 
ATOM   1075 C  C   B LYS A 1 126 ? -11.633 18.934  22.073  0.50   9.41  ? 127 LYS A C   1 
ATOM   1076 O  O   A LYS A 1 126 ? -11.581 20.106  22.192  0.50   9.74  ? 127 LYS A O   1 
ATOM   1077 O  O   B LYS A 1 126 ? -11.047 19.974  22.465  0.50   9.75  ? 127 LYS A O   1 
ATOM   1078 C  CB  A LYS A 1 126 ? -13.502 18.341  23.823  0.50   10.35 ? 127 LYS A CB  1 
ATOM   1079 C  CB  B LYS A 1 126 ? -13.022 18.261  24.033  0.50   11.30 ? 127 LYS A CB  1 
ATOM   1080 C  CG  A LYS A 1 126 ? -12.410 17.531  24.477  0.50   11.04 ? 127 LYS A CG  1 
ATOM   1081 C  CG  B LYS A 1 126 ? -11.918 17.371  24.472  0.50   11.80 ? 127 LYS A CG  1 
ATOM   1082 C  CD  A LYS A 1 126 ? -12.795 17.107  25.884  0.50   14.41 ? 127 LYS A CD  1 
ATOM   1083 C  CD  B LYS A 1 126 ? -12.099 16.975  25.926  0.50   12.29 ? 127 LYS A CD  1 
ATOM   1084 C  CE  A LYS A 1 126 ? -11.687 16.378  26.597  0.50   15.92 ? 127 LYS A CE  1 
ATOM   1085 C  CE  B LYS A 1 126 ? -11.883 18.163  26.861  0.50   15.57 ? 127 LYS A CE  1 
ATOM   1086 N  NZ  A LYS A 1 126 ? -12.134 15.982  27.977  0.50   20.09 ? 127 LYS A NZ  1 
ATOM   1087 N  NZ  B LYS A 1 126 ? -12.294 17.709  28.220  0.50   15.25 ? 127 LYS A NZ  1 
ATOM   1088 N  N   . TYR A 1 127 ? -11.129 18.084  21.169  1.00   10.11 ? 128 TYR A N   1 
ATOM   1089 C  CA  . TYR A 1 127 ? -9.777  18.371  20.668  1.00   10.65 ? 128 TYR A CA  1 
ATOM   1090 C  C   . TYR A 1 127 ? -9.721  18.777  19.216  1.00   10.11 ? 128 TYR A C   1 
ATOM   1091 O  O   . TYR A 1 127 ? -8.658  19.008  18.662  1.00   10.93 ? 128 TYR A O   1 
ATOM   1092 C  CB  . TYR A 1 127 ? -8.822  17.211  20.975  1.00   10.88 ? 128 TYR A CB  1 
ATOM   1093 C  CG  . TYR A 1 127 ? -8.725  16.907  22.435  1.00   10.20 ? 128 TYR A CG  1 
ATOM   1094 C  CD1 . TYR A 1 127 ? -8.317  17.892  23.365  1.00   10.92 ? 128 TYR A CD1 1 
ATOM   1095 C  CD2 . TYR A 1 127 ? -9.003  15.645  22.938  1.00   9.77  ? 128 TYR A CD2 1 
ATOM   1096 C  CE1 . TYR A 1 127 ? -8.310  17.603  24.717  1.00   11.89 ? 128 TYR A CE1 1 
ATOM   1097 C  CE2 . TYR A 1 127 ? -8.969  15.329  24.255  1.00   10.52 ? 128 TYR A CE2 1 
ATOM   1098 C  CZ  . TYR A 1 127 ? -8.597  16.315  25.171  1.00   11.27 ? 128 TYR A CZ  1 
ATOM   1099 O  OH  . TYR A 1 127 ? -8.547  16.103  26.499  1.00   12.86 ? 128 TYR A OH  1 
ATOM   1100 N  N   . GLY A 1 128 ? -10.903 18.883  18.583  1.00   10.59 ? 129 GLY A N   1 
ATOM   1101 C  CA  . GLY A 1 128 ? -10.986 19.530  17.279  1.00   11.60 ? 129 GLY A CA  1 
ATOM   1102 C  C   . GLY A 1 128 ? -10.643 18.678  16.068  1.00   11.20 ? 129 GLY A C   1 
ATOM   1103 O  O   . GLY A 1 128 ? -11.268 18.830  15.013  1.00   12.79 ? 129 GLY A O   1 
ATOM   1104 N  N   . ASP A 1 129 ? -9.624  17.824  16.158  1.00   11.69 ? 130 ASP A N   1 
ATOM   1105 C  CA  . ASP A 1 129 ? -9.342  16.904  15.057  1.00   11.88 ? 130 ASP A CA  1 
ATOM   1106 C  C   . ASP A 1 129 ? -8.609  15.699  15.601  1.00   12.38 ? 130 ASP A C   1 
ATOM   1107 O  O   . ASP A 1 129 ? -8.155  15.690  16.762  1.00   12.38 ? 130 ASP A O   1 
ATOM   1108 C  CB  . ASP A 1 129 ? -8.739  17.497  13.863  1.00   15.46 ? 130 ASP A CB  1 
ATOM   1109 C  CG  . ASP A 1 129 ? -7.384  17.988  14.080  1.00   13.91 ? 130 ASP A CG  1 
ATOM   1110 O  OD1 . ASP A 1 129 ? -6.807  17.685  15.121  1.00   21.43 ? 130 ASP A OD1 1 
ATOM   1111 O  OD2 . ASP A 1 129 ? -6.894  18.684  13.172  1.00   19.51 ? 130 ASP A OD2 1 
ATOM   1112 N  N   . PHE A 1 130 ? -8.475  14.681  14.736  1.00   11.48 ? 131 PHE A N   1 
ATOM   1113 C  CA  . PHE A 1 130 ? -7.827  13.423  15.177  1.00   10.57 ? 131 PHE A CA  1 
ATOM   1114 C  C   . PHE A 1 130 ? -6.382  13.638  15.580  1.00   10.77 ? 131 PHE A C   1 
ATOM   1115 O  O   . PHE A 1 130 ? -5.906  13.057  16.551  1.00   10.45 ? 131 PHE A O   1 
ATOM   1116 C  CB  . PHE A 1 130 ? -7.935  12.454  14.013  1.00   11.14 ? 131 PHE A CB  1 
ATOM   1117 C  CG  . PHE A 1 130 ? -7.292  11.135  14.258  1.00   9.66  ? 131 PHE A CG  1 
ATOM   1118 C  CD1 . PHE A 1 130 ? -7.965  10.118  14.931  1.00   10.51 ? 131 PHE A CD1 1 
ATOM   1119 C  CD2 . PHE A 1 130 ? -6.005  10.890  13.861  1.00   12.83 ? 131 PHE A CD2 1 
ATOM   1120 C  CE1 . PHE A 1 130 ? -7.356  8.915   15.208  1.00   11.65 ? 131 PHE A CE1 1 
ATOM   1121 C  CE2 . PHE A 1 130 ? -5.408  9.660   14.111  1.00   14.64 ? 131 PHE A CE2 1 
ATOM   1122 C  CZ  . PHE A 1 130 ? -6.102  8.666   14.799  1.00   13.62 ? 131 PHE A CZ  1 
ATOM   1123 N  N   . GLY A 1 131 ? -5.638  14.430  14.785  1.00   12.16 ? 132 GLY A N   1 
ATOM   1124 C  CA  . GLY A 1 131 ? -4.272  14.562  15.062  1.00   12.41 ? 132 GLY A CA  1 
ATOM   1125 C  C   . GLY A 1 131 ? -3.949  15.249  16.422  1.00   12.08 ? 132 GLY A C   1 
ATOM   1126 O  O   . GLY A 1 131 ? -2.948  14.933  17.064  1.00   13.21 ? 132 GLY A O   1 
ATOM   1127 N  N   . LYS A 1 132 ? -4.801  16.172  16.859  1.00   11.60 ? 133 LYS A N   1 
ATOM   1128 C  CA  . LYS A 1 132 ? -4.621  16.705  18.186  1.00   10.98 ? 133 LYS A CA  1 
ATOM   1129 C  C   . LYS A 1 132 ? -5.145  15.722  19.244  1.00   10.28 ? 133 LYS A C   1 
ATOM   1130 O  O   . LYS A 1 132 ? -4.616  15.664  20.355  1.00   10.67 ? 133 LYS A O   1 
ATOM   1131 C  CB  . LYS A 1 132 ? -5.384  18.023  18.298  1.00   11.88 ? 133 LYS A CB  1 
ATOM   1132 C  CG  . LYS A 1 132 ? -4.682  19.190  17.546  1.00   14.43 ? 133 LYS A CG  1 
ATOM   1133 C  CD  . LYS A 1 132 ? -3.392  19.590  18.321  1.00   18.37 ? 133 LYS A CD  1 
ATOM   1134 C  CE  . LYS A 1 132 ? -2.850  20.979  17.886  1.00   19.84 ? 133 LYS A CE  1 
ATOM   1135 N  NZ  . LYS A 1 132 ? -1.868  21.451  18.921  1.00   30.51 ? 133 LYS A NZ  1 
ATOM   1136 N  N   . ALA A 1 133 ? -6.212  14.987  18.927  1.00   10.12 ? 134 ALA A N   1 
ATOM   1137 C  CA  . ALA A 1 133 ? -6.753  14.057  19.915  1.00   9.84  ? 134 ALA A CA  1 
ATOM   1138 C  C   . ALA A 1 133 ? -5.775  12.995  20.328  1.00   9.07  ? 134 ALA A C   1 
ATOM   1139 O  O   . ALA A 1 133 ? -5.761  12.608  21.477  1.00   9.10  ? 134 ALA A O   1 
ATOM   1140 C  CB  . ALA A 1 133 ? -8.042  13.455  19.338  1.00   9.49  ? 134 ALA A CB  1 
ATOM   1141 N  N   . VAL A 1 134 ? -4.964  12.494  19.407  1.00   9.50  ? 135 VAL A N   1 
ATOM   1142 C  CA  . VAL A 1 134 ? -4.049  11.394  19.756  1.00   10.07 ? 135 VAL A CA  1 
ATOM   1143 C  C   . VAL A 1 134 ? -2.960  11.833  20.712  1.00   9.77  ? 135 VAL A C   1 
ATOM   1144 O  O   . VAL A 1 134 ? -2.262  10.977  21.278  1.00   10.38 ? 135 VAL A O   1 
ATOM   1145 C  CB  . VAL A 1 134 ? -3.416  10.707  18.578  1.00   11.00 ? 135 VAL A CB  1 
ATOM   1146 C  CG1 . VAL A 1 134 ? -4.444  10.045  17.681  1.00   12.72 ? 135 VAL A CG1 1 
ATOM   1147 C  CG2 . VAL A 1 134 ? -2.509  11.624  17.751  1.00   11.93 ? 135 VAL A CG2 1 
ATOM   1148 N  N   . GLN A 1 135 ? -2.825  13.146  20.929  1.00   9.99  ? 136 GLN A N   1 
ATOM   1149 C  CA  . GLN A 1 135 ? -1.868  13.681  21.914  1.00   10.82 ? 136 GLN A CA  1 
ATOM   1150 C  C   . GLN A 1 135 ? -2.423  13.767  23.310  1.00   10.26 ? 136 GLN A C   1 
ATOM   1151 O  O   . GLN A 1 135 ? -1.751  14.343  24.193  1.00   12.23 ? 136 GLN A O   1 
ATOM   1152 C  CB  . GLN A 1 135 ? -1.369  15.053  21.413  1.00   12.21 ? 136 GLN A CB  1 
ATOM   1153 C  CG  . GLN A 1 135 ? -0.694  14.913  20.054  1.00   14.11 ? 136 GLN A CG  1 
ATOM   1154 C  CD  . GLN A 1 135 ? -0.225  16.245  19.537  1.00   18.37 ? 136 GLN A CD  1 
ATOM   1155 O  OE1 . GLN A 1 135 ? 0.629   16.901  20.184  1.00   24.67 ? 136 GLN A OE1 1 
ATOM   1156 N  NE2 . GLN A 1 135 ? -0.680  16.658  18.365  1.00   19.44 ? 136 GLN A NE2 1 
ATOM   1157 N  N   . GLN A 1 136 ? -3.638  13.264  23.522  1.00   9.82  ? 137 GLN A N   1 
ATOM   1158 C  CA  . GLN A 1 136 ? -4.334  13.442  24.794  1.00   9.17  ? 137 GLN A CA  1 
ATOM   1159 C  C   . GLN A 1 136 ? -4.667  12.111  25.380  1.00   9.17  ? 137 GLN A C   1 
ATOM   1160 O  O   . GLN A 1 136 ? -5.072  11.193  24.654  1.00   8.75  ? 137 GLN A O   1 
ATOM   1161 C  CB  . GLN A 1 136 ? -5.582  14.250  24.619  1.00   10.62 ? 137 GLN A CB  1 
ATOM   1162 C  CG  . GLN A 1 136 ? -5.304  15.634  23.950  1.00   13.36 ? 137 GLN A CG  1 
ATOM   1163 C  CD  . GLN A 1 136 ? -4.508  16.598  24.918  1.00   14.99 ? 137 GLN A CD  1 
ATOM   1164 O  OE1 . GLN A 1 136 ? -4.494  16.356  26.065  1.00   20.59 ? 137 GLN A OE1 1 
ATOM   1165 N  NE2 . GLN A 1 136 ? -3.962  17.661  24.440  1.00   22.04 ? 137 GLN A NE2 1 
ATOM   1166 N  N   . PRO A 1 137 ? -4.690  11.970  26.729  1.00   9.34  ? 138 PRO A N   1 
ATOM   1167 C  CA  . PRO A 1 137 ? -4.945  10.660  27.319  1.00   9.79  ? 138 PRO A CA  1 
ATOM   1168 C  C   . PRO A 1 137 ? -6.425  10.208  27.152  1.00   9.85  ? 138 PRO A C   1 
ATOM   1169 O  O   . PRO A 1 137 ? -6.647  9.005   27.210  1.00   12.98 ? 138 PRO A O   1 
ATOM   1170 C  CB  . PRO A 1 137 ? -4.700  10.860  28.822  1.00   11.65 ? 138 PRO A CB  1 
ATOM   1171 C  CG  . PRO A 1 137 ? -4.606  12.300  28.968  1.00   17.70 ? 138 PRO A CG  1 
ATOM   1172 C  CD  . PRO A 1 137 ? -4.188  12.941  27.711  1.00   11.87 ? 138 PRO A CD  1 
ATOM   1173 N  N   . ASP A 1 138 ? -7.344  11.143  26.889  1.00   9.00  ? 139 ASP A N   1 
ATOM   1174 C  CA  . ASP A 1 138 ? -8.715  10.842  26.604  1.00   9.16  ? 139 ASP A CA  1 
ATOM   1175 C  C   . ASP A 1 138 ? -9.050  11.272  25.179  1.00   8.33  ? 139 ASP A C   1 
ATOM   1176 O  O   . ASP A 1 138 ? -10.185 11.694  24.911  1.00   9.35  ? 139 ASP A O   1 
ATOM   1177 C  CB  . ASP A 1 138 ? -9.683  11.493  27.617  1.00   11.04 ? 139 ASP A CB  1 
ATOM   1178 C  CG  . ASP A 1 138 ? -9.544  12.963  27.680  1.00   11.50 ? 139 ASP A CG  1 
ATOM   1179 O  OD1 . ASP A 1 138 ? -8.611  13.544  27.077  1.00   11.81 ? 139 ASP A OD1 1 
ATOM   1180 O  OD2 . ASP A 1 138 ? -10.411 13.531  28.384  1.00   14.69 ? 139 ASP A OD2 1 
ATOM   1181 N  N   . GLY A 1 139 ? -8.124  11.158  24.260  1.00   7.96  ? 140 GLY A N   1 
ATOM   1182 C  CA  . GLY A 1 139 ? -8.332  11.625  22.914  1.00   8.11  ? 140 GLY A CA  1 
ATOM   1183 C  C   . GLY A 1 139 ? -9.168  10.718  22.030  1.00   7.49  ? 140 GLY A C   1 
ATOM   1184 O  O   . GLY A 1 139 ? -9.864  11.226  21.154  1.00   8.07  ? 140 GLY A O   1 
ATOM   1185 N  N   . LEU A 1 140 ? -9.055  9.392   22.202  1.00   7.52  ? 141 LEU A N   1 
ATOM   1186 C  CA  . LEU A 1 140 ? -9.741  8.450   21.330  1.00   7.56  ? 141 LEU A CA  1 
ATOM   1187 C  C   . LEU A 1 140 ? -10.566 7.523   22.112  1.00   7.12  ? 141 LEU A C   1 
ATOM   1188 O  O   . LEU A 1 140 ? -10.309 7.220   23.285  1.00   7.36  ? 141 LEU A O   1 
ATOM   1189 C  CB  . LEU A 1 140 ? -8.735  7.588   20.513  1.00   8.03  ? 141 LEU A CB  1 
ATOM   1190 C  CG  . LEU A 1 140 ? -7.809  8.263   19.489  1.00   10.10 ? 141 LEU A CG  1 
ATOM   1191 C  CD1 . LEU A 1 140 ? -7.155  7.204   18.609  1.00   9.47  ? 141 LEU A CD1 1 
ATOM   1192 C  CD2 . LEU A 1 140 ? -8.461  9.365   18.660  1.00   11.95 ? 141 LEU A CD2 1 
ATOM   1193 N  N   . ALA A 1 141 ? -11.608 6.996   21.442  1.00   7.16  ? 142 ALA A N   1 
ATOM   1194 C  CA  . ALA A 1 141 ? -12.396 5.846   21.925  1.00   7.45  ? 142 ALA A CA  1 
ATOM   1195 C  C   . ALA A 1 141 ? -12.422 4.861   20.809  1.00   7.10  ? 142 ALA A C   1 
ATOM   1196 O  O   . ALA A 1 141 ? -12.843 5.201   19.687  1.00   8.02  ? 142 ALA A O   1 
ATOM   1197 C  CB  . ALA A 1 141 ? -13.789 6.258   22.327  1.00   8.65  ? 142 ALA A CB  1 
ATOM   1198 N  N   . VAL A 1 142 ? -11.935 3.634   21.067  1.00   6.76  ? 143 VAL A N   1 
ATOM   1199 C  CA  . VAL A 1 142 ? -11.948 2.580   20.073  1.00   6.51  ? 143 VAL A CA  1 
ATOM   1200 C  C   . VAL A 1 142 ? -12.904 1.513   20.562  1.00   6.49  ? 143 VAL A C   1 
ATOM   1201 O  O   . VAL A 1 142 ? -12.773 1.008   21.675  1.00   6.89  ? 143 VAL A O   1 
ATOM   1202 C  CB  . VAL A 1 142 ? -10.555 2.037   19.708  1.00   7.07  ? 143 VAL A CB  1 
ATOM   1203 C  CG1 . VAL A 1 142 ? -10.696 1.026   18.599  1.00   7.78  ? 143 VAL A CG1 1 
ATOM   1204 C  CG2 . VAL A 1 142 ? -9.644  3.159   19.280  1.00   8.25  ? 143 VAL A CG2 1 
ATOM   1205 N  N   . LEU A 1 143 ? -13.890 1.249   19.722  1.00   7.05  ? 144 LEU A N   1 
ATOM   1206 C  CA  . LEU A 1 143 ? -14.870 0.182   19.938  1.00   6.87  ? 144 LEU A CA  1 
ATOM   1207 C  C   . LEU A 1 143 ? -14.340 -1.062  19.292  1.00   6.97  ? 144 LEU A C   1 
ATOM   1208 O  O   . LEU A 1 143 ? -14.179 -1.102  18.051  1.00   7.90  ? 144 LEU A O   1 
ATOM   1209 C  CB  . LEU A 1 143 ? -16.208 0.620   19.406  1.00   8.69  ? 144 LEU A CB  1 
ATOM   1210 C  CG  . LEU A 1 143 ? -17.385 -0.344  19.538  1.00   9.86  ? 144 LEU A CG  1 
ATOM   1211 C  CD1 . LEU A 1 143 ? -17.641 -0.666  20.991  1.00   11.68 ? 144 LEU A CD1 1 
ATOM   1212 C  CD2 . LEU A 1 143 ? -18.609 0.275   18.912  1.00   10.59 ? 144 LEU A CD2 1 
ATOM   1213 N  N   . GLY A 1 144 ? -14.062 -2.083  20.099  1.00   6.86  ? 145 GLY A N   1 
ATOM   1214 C  CA  . GLY A 1 144 ? -13.525 -3.332  19.591  1.00   7.24  ? 145 GLY A CA  1 
ATOM   1215 C  C   . GLY A 1 144 ? -14.576 -4.440  19.591  1.00   6.37  ? 145 GLY A C   1 
ATOM   1216 O  O   . GLY A 1 144 ? -15.312 -4.579  20.590  1.00   7.50  ? 145 GLY A O   1 
ATOM   1217 N  N   . ILE A 1 145 ? -14.635 -5.170  18.491  1.00   6.35  ? 146 ILE A N   1 
ATOM   1218 C  CA  . ILE A 1 145 ? -15.665 -6.200  18.306  1.00   6.51  ? 146 ILE A CA  1 
ATOM   1219 C  C   . ILE A 1 145 ? -14.979 -7.440  17.794  1.00   6.40  ? 146 ILE A C   1 
ATOM   1220 O  O   . ILE A 1 145 ? -14.261 -7.404  16.798  1.00   7.15  ? 146 ILE A O   1 
ATOM   1221 C  CB  . ILE A 1 145 ? -16.762 -5.714  17.348  1.00   7.87  ? 146 ILE A CB  1 
ATOM   1222 C  CG1 . ILE A 1 145 ? -17.389 -4.417  17.860  1.00   9.26  ? 146 ILE A CG1 1 
ATOM   1223 C  CG2 . ILE A 1 145 ? -17.789 -6.824  17.110  1.00   9.40  ? 146 ILE A CG2 1 
ATOM   1224 C  CD1 . ILE A 1 145 ? -18.446 -3.809  16.971  1.00   8.99  ? 146 ILE A CD1 1 
ATOM   1225 N  N   . PHE A 1 146 ? -15.137 -8.542  18.492  1.00   6.80  ? 147 PHE A N   1 
ATOM   1226 C  CA  . PHE A 1 146 ? -14.514 -9.809  18.070  1.00   7.07  ? 147 PHE A CA  1 
ATOM   1227 C  C   . PHE A 1 146 ? -15.288 -10.425 16.906  1.00   7.28  ? 147 PHE A C   1 
ATOM   1228 O  O   . PHE A 1 146 ? -16.525 -10.308 16.845  1.00   7.89  ? 147 PHE A O   1 
ATOM   1229 C  CB  . PHE A 1 146 ? -14.531 -10.772 19.232  1.00   7.36  ? 147 PHE A CB  1 
ATOM   1230 C  CG  . PHE A 1 146 ? -13.662 -10.321 20.407  1.00   6.76  ? 147 PHE A CG  1 
ATOM   1231 C  CD1 . PHE A 1 146 ? -12.317 -10.133 20.246  1.00   7.33  ? 147 PHE A CD1 1 
ATOM   1232 C  CD2 . PHE A 1 146 ? -14.212 -10.085 21.654  1.00   7.98  ? 147 PHE A CD2 1 
ATOM   1233 C  CE1 . PHE A 1 146 ? -11.501 -9.762  21.306  1.00   7.87  ? 147 PHE A CE1 1 
ATOM   1234 C  CE2 . PHE A 1 146 ? -13.407 -9.704  22.703  1.00   7.89  ? 147 PHE A CE2 1 
ATOM   1235 C  CZ  . PHE A 1 146 ? -12.042 -9.558  22.541  1.00   7.82  ? 147 PHE A CZ  1 
ATOM   1236 N  N   . LEU A 1 147 ? -14.562 -11.148 16.047  1.00   7.40  ? 148 LEU A N   1 
ATOM   1237 C  CA  . LEU A 1 147 ? -15.142 -11.921 14.953  1.00   7.75  ? 148 LEU A CA  1 
ATOM   1238 C  C   . LEU A 1 147 ? -14.796 -13.413 15.211  1.00   7.72  ? 148 LEU A C   1 
ATOM   1239 O  O   . LEU A 1 147 ? -13.645 -13.735 15.443  1.00   8.25  ? 148 LEU A O   1 
ATOM   1240 C  CB  . LEU A 1 147 ? -14.559 -11.533 13.613  1.00   8.27  ? 148 LEU A CB  1 
ATOM   1241 C  CG  . LEU A 1 147 ? -15.099 -10.276 12.930  1.00   8.60  ? 148 LEU A CG  1 
ATOM   1242 C  CD1 . LEU A 1 147 ? -14.882 -9.032  13.773  1.00   9.86  ? 148 LEU A CD1 1 
ATOM   1243 C  CD2 . LEU A 1 147 ? -14.499 -10.101 11.581  1.00   10.24 ? 148 LEU A CD2 1 
ATOM   1244 N  N   . LYS A 1 148 ? -15.836 -14.240 15.092  1.00   8.30  ? 149 LYS A N   1 
ATOM   1245 C  CA  . LYS A 1 148 ? -15.686 -15.699 15.061  1.00   9.02  ? 149 LYS A CA  1 
ATOM   1246 C  C   . LYS A 1 148 ? -16.159 -16.193 13.689  1.00   9.65  ? 149 LYS A C   1 
ATOM   1247 O  O   . LYS A 1 148 ? -16.983 -15.531 13.063  1.00   10.44 ? 149 LYS A O   1 
ATOM   1248 C  CB  . LYS A 1 148 ? -16.402 -16.357 16.207  1.00   10.76 ? 149 LYS A CB  1 
ATOM   1249 C  CG  . LYS A 1 148 ? -17.897 -16.247 16.151  1.00   12.59 ? 149 LYS A CG  1 
ATOM   1250 C  CD  . LYS A 1 148 ? -18.546 -16.959 17.345  1.00   17.65 ? 149 LYS A CD  1 
ATOM   1251 C  CE  . LYS A 1 148 ? -20.042 -16.997 17.245  1.00   28.05 ? 149 LYS A CE  1 
ATOM   1252 N  NZ  . LYS A 1 148 ? -20.588 -17.791 18.363  1.00   36.20 ? 149 LYS A NZ  1 
ATOM   1253 N  N   . VAL A 1 149 ? -15.672 -17.342 13.289  1.00   10.22 ? 150 VAL A N   1 
ATOM   1254 C  CA  . VAL A 1 149 ? -16.050 -17.932 11.995  1.00   10.50 ? 150 VAL A CA  1 
ATOM   1255 C  C   . VAL A 1 149 ? -17.272 -18.871 12.200  1.00   10.63 ? 150 VAL A C   1 
ATOM   1256 O  O   . VAL A 1 149 ? -17.210 -19.815 12.972  1.00   12.50 ? 150 VAL A O   1 
ATOM   1257 C  CB  . VAL A 1 149 ? -14.866 -18.699 11.430  1.00   11.10 ? 150 VAL A CB  1 
ATOM   1258 C  CG1 . VAL A 1 149 ? -15.240 -19.469 10.168  1.00   13.59 ? 150 VAL A CG1 1 
ATOM   1259 C  CG2 . VAL A 1 149 ? -13.756 -17.710 11.096  1.00   14.19 ? 150 VAL A CG2 1 
ATOM   1260 N  N   . GLY A 1 150 ? -18.319 -18.571 11.479  1.00   11.62 ? 151 GLY A N   1 
ATOM   1261 C  CA  . GLY A 1 150 ? -19.527 -19.407 11.491  1.00   12.55 ? 151 GLY A CA  1 
ATOM   1262 C  C   . GLY A 1 150 ? -20.414 -18.930 10.380  1.00   12.09 ? 151 GLY A C   1 
ATOM   1263 O  O   . GLY A 1 150 ? -20.049 -18.990 9.197   1.00   13.13 ? 151 GLY A O   1 
ATOM   1264 N  N   A SER A 1 151 ? -21.597 -18.415 10.696  0.50   12.92 ? 152 SER A N   1 
ATOM   1265 N  N   B SER A 1 151 ? -21.586 -18.422 10.737  0.50   12.99 ? 152 SER A N   1 
ATOM   1266 C  CA  A SER A 1 151 ? -22.493 -17.888 9.658   0.50   13.57 ? 152 SER A CA  1 
ATOM   1267 C  CA  B SER A 1 151 ? -22.488 -17.791 9.779   0.50   12.85 ? 152 SER A CA  1 
ATOM   1268 C  C   A SER A 1 151 ? -21.985 -16.563 9.161   0.50   11.52 ? 152 SER A C   1 
ATOM   1269 C  C   B SER A 1 151 ? -21.815 -16.581 9.118   0.50   12.49 ? 152 SER A C   1 
ATOM   1270 O  O   A SER A 1 151 ? -21.399 -15.795 9.925   0.50   10.43 ? 152 SER A O   1 
ATOM   1271 O  O   B SER A 1 151 ? -20.936 -15.921 9.715   0.50   11.25 ? 152 SER A O   1 
ATOM   1272 C  CB  A SER A 1 151 ? -23.885 -17.699 10.228  0.50   17.43 ? 152 SER A CB  1 
ATOM   1273 C  CB  B SER A 1 151 ? -23.809 -17.434 10.475  0.50   15.48 ? 152 SER A CB  1 
ATOM   1274 O  OG  A SER A 1 151 ? -23.843 -16.711 11.223  0.50   20.19 ? 152 SER A OG  1 
ATOM   1275 O  OG  B SER A 1 151 ? -24.457 -18.593 11.004  0.50   18.05 ? 152 SER A OG  1 
ATOM   1276 N  N   . ALA A 1 152 ? -22.195 -16.279 7.861   1.00   12.40 ? 153 ALA A N   1 
ATOM   1277 C  CA  . ALA A 1 152 ? -21.802 -15.067 7.254   1.00   12.40 ? 153 ALA A CA  1 
ATOM   1278 C  C   . ALA A 1 152 ? -22.439 -13.836 7.931   1.00   12.05 ? 153 ALA A C   1 
ATOM   1279 O  O   . ALA A 1 152 ? -23.545 -13.896 8.428   1.00   13.70 ? 153 ALA A O   1 
ATOM   1280 C  CB  . ALA A 1 152 ? -22.133 -15.064 5.740   1.00   15.59 ? 153 ALA A CB  1 
ATOM   1281 N  N   . LYS A 1 153 ? -21.698 -12.705 7.874   1.00   12.69 ? 154 LYS A N   1 
ATOM   1282 C  CA  . LYS A 1 153 ? -22.244 -11.426 8.318   1.00   14.02 ? 154 LYS A CA  1 
ATOM   1283 C  C   . LYS A 1 153 ? -22.681 -10.640 7.052   1.00   12.42 ? 154 LYS A C   1 
ATOM   1284 O  O   . LYS A 1 153 ? -21.832 -10.217 6.261   1.00   11.61 ? 154 LYS A O   1 
ATOM   1285 C  CB  . LYS A 1 153 ? -21.179 -10.639 9.075   1.00   13.23 ? 154 LYS A CB  1 
ATOM   1286 C  CG  . LYS A 1 153 ? -21.610 -9.433  9.835   1.00   15.74 ? 154 LYS A CG  1 
ATOM   1287 C  CD  . LYS A 1 153 ? -22.495 -9.782  11.064  1.00   17.60 ? 154 LYS A CD  1 
ATOM   1288 C  CE  . LYS A 1 153 ? -22.559 -8.601  11.900  1.00   16.73 ? 154 LYS A CE  1 
ATOM   1289 N  NZ  . LYS A 1 153 ? -23.471 -8.982  12.961  1.00   17.61 ? 154 LYS A NZ  1 
ATOM   1290 N  N   A PRO A 1 154 ? -23.975 -10.569 6.763   0.50   13.87 ? 155 PRO A N   1 
ATOM   1291 N  N   B PRO A 1 154 ? -23.979 -10.557 6.781   0.50   13.79 ? 155 PRO A N   1 
ATOM   1292 C  CA  A PRO A 1 154 ? -24.442 -9.907  5.529   0.50   14.44 ? 155 PRO A CA  1 
ATOM   1293 C  CA  B PRO A 1 154 ? -24.301 -9.986  5.481   0.50   13.18 ? 155 PRO A CA  1 
ATOM   1294 C  C   A PRO A 1 154 ? -23.951 -8.457  5.373   0.50   13.09 ? 155 PRO A C   1 
ATOM   1295 C  C   B PRO A 1 154 ? -23.790 -8.561  5.343   0.50   12.08 ? 155 PRO A C   1 
ATOM   1296 O  O   A PRO A 1 154 ? -23.648 -7.966  4.309   0.50   16.65 ? 155 PRO A O   1 
ATOM   1297 O  O   B PRO A 1 154 ? -23.304 -8.245  4.205   0.50   12.63 ? 155 PRO A O   1 
ATOM   1298 C  CB  A PRO A 1 154 ? -25.987 -10.002 5.684   0.50   16.32 ? 155 PRO A CB  1 
ATOM   1299 C  CB  B PRO A 1 154 ? -25.856 -10.088 5.430   0.50   16.25 ? 155 PRO A CB  1 
ATOM   1300 C  CG  A PRO A 1 154 ? -26.139 -11.283 6.448   0.50   16.22 ? 155 PRO A CG  1 
ATOM   1301 C  CG  B PRO A 1 154 ? -26.216 -10.016 6.900   0.50   18.54 ? 155 PRO A CG  1 
ATOM   1302 C  CD  A PRO A 1 154 ? -25.095 -11.230 7.503   0.50   16.91 ? 155 PRO A CD  1 
ATOM   1303 C  CD  B PRO A 1 154 ? -25.193 -10.857 7.595   0.50   17.35 ? 155 PRO A CD  1 
ATOM   1304 N  N   . GLY A 1 155 ? -23.827 -7.788  6.464   1.00   13.12 ? 156 GLY A N   1 
ATOM   1305 C  CA  . GLY A 1 155 ? -23.407 -6.408  6.447   1.00   13.84 ? 156 GLY A CA  1 
ATOM   1306 C  C   . GLY A 1 155 ? -21.927 -6.223  6.215   1.00   13.21 ? 156 GLY A C   1 
ATOM   1307 O  O   . GLY A 1 155 ? -21.457 -5.063  6.015   1.00   16.23 ? 156 GLY A O   1 
ATOM   1308 N  N   . LEU A 1 156 ? -21.161 -7.282  6.254   1.00   12.15 ? 157 LEU A N   1 
ATOM   1309 C  CA  . LEU A 1 156 ? -19.742 -7.250  5.908   1.00   11.16 ? 157 LEU A CA  1 
ATOM   1310 C  C   . LEU A 1 156 ? -19.450 -7.451  4.429   1.00   10.90 ? 157 LEU A C   1 
ATOM   1311 O  O   . LEU A 1 156 ? -18.362 -7.153  3.967   1.00   11.54 ? 157 LEU A O   1 
ATOM   1312 C  CB  . LEU A 1 156 ? -18.988 -8.283  6.722   1.00   11.76 ? 157 LEU A CB  1 
ATOM   1313 C  CG  . LEU A 1 156 ? -17.482 -8.386  6.602   1.00   12.01 ? 157 LEU A CG  1 
ATOM   1314 C  CD1 . LEU A 1 156 ? -16.749 -7.101  6.988   1.00   13.99 ? 157 LEU A CD1 1 
ATOM   1315 C  CD2 . LEU A 1 156 ? -16.918 -9.582  7.426   1.00   13.83 ? 157 LEU A CD2 1 
ATOM   1316 N  N   . GLN A 1 157 ? -20.393 -8.048  3.672   1.00   12.28 ? 158 GLN A N   1 
ATOM   1317 C  CA  . GLN A 1 157 ? -20.037 -8.532  2.326   1.00   12.36 ? 158 GLN A CA  1 
ATOM   1318 C  C   . GLN A 1 157 ? -19.621 -7.390  1.431   1.00   12.74 ? 158 GLN A C   1 
ATOM   1319 O  O   . GLN A 1 157 ? -18.779 -7.593  0.586   1.00   12.68 ? 158 GLN A O   1 
ATOM   1320 C  CB  . GLN A 1 157 ? -21.196 -9.350  1.766   1.00   14.27 ? 158 GLN A CB  1 
ATOM   1321 C  CG  . GLN A 1 157 ? -20.784 -10.072 0.491   1.00   14.88 ? 158 GLN A CG  1 
ATOM   1322 C  CD  . GLN A 1 157 ? -19.659 -11.085 0.718   1.00   13.33 ? 158 GLN A CD  1 
ATOM   1323 O  OE1 . GLN A 1 157 ? -19.516 -11.663 1.817   1.00   14.58 ? 158 GLN A OE1 1 
ATOM   1324 N  NE2 . GLN A 1 157 ? -18.860 -11.343 -0.330  1.00   15.69 ? 158 GLN A NE2 1 
ATOM   1325 N  N   . LYS A 1 158 ? -20.202 -6.178  1.560   1.00   13.03 ? 159 LYS A N   1 
ATOM   1326 C  CA  . LYS A 1 158 ? -19.804 -5.083  0.712   1.00   14.48 ? 159 LYS A CA  1 
ATOM   1327 C  C   . LYS A 1 158 ? -18.306 -4.745  0.855   1.00   12.25 ? 159 LYS A C   1 
ATOM   1328 O  O   . LYS A 1 158 ? -17.631 -4.393  -0.086  1.00   14.19 ? 159 LYS A O   1 
ATOM   1329 C  CB  . LYS A 1 158 ? -20.643 -3.841  0.925   1.00   17.23 ? 159 LYS A CB  1 
ATOM   1330 C  CG  . LYS A 1 158 ? -22.014 -3.967  0.260   1.00   26.78 ? 159 LYS A CG  1 
ATOM   1331 C  CD  . LYS A 1 158 ? -22.586 -2.566  0.004   0.0000 37.00 ? 159 LYS A CD  1 
ATOM   1332 C  CE  . LYS A 1 158 ? -21.663 -1.484  0.622   0.0000 43.07 ? 159 LYS A CE  1 
ATOM   1333 N  NZ  . LYS A 1 158 ? -21.886 -0.015  0.363   0.0000 58.90 ? 159 LYS A NZ  1 
ATOM   1334 N  N   . VAL A 1 159 ? -17.790 -4.865  2.091   1.00   12.69 ? 160 VAL A N   1 
ATOM   1335 C  CA  . VAL A 1 159 ? -16.369 -4.696  2.347   1.00   11.48 ? 160 VAL A CA  1 
ATOM   1336 C  C   . VAL A 1 159 ? -15.592 -5.792  1.680   1.00   11.62 ? 160 VAL A C   1 
ATOM   1337 O  O   . VAL A 1 159 ? -14.641 -5.547  0.948   1.00   12.98 ? 160 VAL A O   1 
ATOM   1338 C  CB  . VAL A 1 159 ? -16.119 -4.666  3.888   1.00   12.26 ? 160 VAL A CB  1 
ATOM   1339 C  CG1 . VAL A 1 159 ? -14.624 -4.715  4.206   1.00   14.36 ? 160 VAL A CG1 1 
ATOM   1340 C  CG2 . VAL A 1 159 ? -16.815 -3.485  4.540   1.00   14.07 ? 160 VAL A CG2 1 
ATOM   1341 N  N   . VAL A 1 160 ? -15.990 -7.033  1.917   1.00   11.79 ? 161 VAL A N   1 
ATOM   1342 C  CA  . VAL A 1 160 ? -15.323 -8.168  1.315   1.00   13.80 ? 161 VAL A CA  1 
ATOM   1343 C  C   . VAL A 1 160 ? -15.199 -8.051  -0.176  1.00   13.48 ? 161 VAL A C   1 
ATOM   1344 O  O   . VAL A 1 160 ? -14.148 -8.329  -0.752  1.00   15.37 ? 161 VAL A O   1 
ATOM   1345 C  CB  . VAL A 1 160 ? -16.066 -9.572  1.703   1.00   15.01 ? 161 VAL A CB  1 
ATOM   1346 C  CG1 . VAL A 1 160 ? -15.532 -10.725 0.935   1.00   17.62 ? 161 VAL A CG1 1 
ATOM   1347 C  CG2 . VAL A 1 160 ? -15.950 -9.789  3.242   1.00   15.04 ? 161 VAL A CG2 1 
ATOM   1348 N  N   . ASP A 1 161 ? -16.262 -7.623  -0.826  1.00   14.05 ? 162 ASP A N   1 
ATOM   1349 C  CA  . ASP A 1 161 ? -16.252 -7.689  -2.263  1.00   15.83 ? 162 ASP A CA  1 
ATOM   1350 C  C   . ASP A 1 161 ? -15.431 -6.574  -2.883  1.00   16.21 ? 162 ASP A C   1 
ATOM   1351 O  O   . ASP A 1 161 ? -15.048 -6.708  -4.044  1.00   21.80 ? 162 ASP A O   1 
ATOM   1352 C  CB  . ASP A 1 161 ? -17.645 -7.576  -2.685  1.00   19.79 ? 162 ASP A CB  1 
ATOM   1353 C  CG  . ASP A 1 161 ? -18.328 -8.954  -2.708  1.00   19.28 ? 162 ASP A CG  1 
ATOM   1354 O  OD1 . ASP A 1 161 ? -17.676 -10.044 -2.666  1.00   23.91 ? 162 ASP A OD1 1 
ATOM   1355 O  OD2 . ASP A 1 161 ? -19.532 -8.965  -2.537  1.00   23.34 ? 162 ASP A OD2 1 
ATOM   1356 N  N   . VAL A 1 162 ? -15.076 -5.516  -2.150  1.00   14.15 ? 163 VAL A N   1 
ATOM   1357 C  CA  . VAL A 1 162 ? -14.256 -4.451  -2.691  1.00   15.78 ? 163 VAL A CA  1 
ATOM   1358 C  C   . VAL A 1 162 ? -12.773 -4.760  -2.527  1.00   13.35 ? 163 VAL A C   1 
ATOM   1359 O  O   . VAL A 1 162 ? -11.885 -4.110  -3.094  1.00   14.99 ? 163 VAL A O   1 
ATOM   1360 C  CB  . VAL A 1 162 ? -14.612 -3.086  -2.074  1.00   16.38 ? 163 VAL A CB  1 
ATOM   1361 C  CG1 . VAL A 1 162 ? -14.060 -2.885  -0.721  1.00   15.51 ? 163 VAL A CG1 1 
ATOM   1362 C  CG2 . VAL A 1 162 ? -14.302 -1.868  -2.952  1.00   19.45 ? 163 VAL A CG2 1 
ATOM   1363 N  N   . LEU A 1 163 ? -12.446 -5.753  -1.709  1.00   13.19 ? 164 LEU A N   1 
ATOM   1364 C  CA  . LEU A 1 163 ? -11.061 -6.017  -1.403  1.00   12.78 ? 164 LEU A CA  1 
ATOM   1365 C  C   . LEU A 1 163 ? -10.173 -6.384  -2.573  1.00   13.75 ? 164 LEU A C   1 
ATOM   1366 O  O   . LEU A 1 163 ? -8.961  -6.042  -2.608  1.00   14.10 ? 164 LEU A O   1 
ATOM   1367 C  CB  . LEU A 1 163 ? -10.851 -7.067  -0.303  1.00   13.07 ? 164 LEU A CB  1 
ATOM   1368 C  CG  . LEU A 1 163 ? -11.487 -6.720  1.059   1.00   12.54 ? 164 LEU A CG  1 
ATOM   1369 C  CD1 . LEU A 1 163 ? -11.308 -7.857  2.091   1.00   13.74 ? 164 LEU A CD1 1 
ATOM   1370 C  CD2 . LEU A 1 163 ? -11.013 -5.385  1.604   1.00   12.66 ? 164 LEU A CD2 1 
ATOM   1371 N  N   . ASP A 1 164 ? -10.696 -7.063  -3.552  1.00   16.45 ? 165 ASP A N   1 
ATOM   1372 C  CA  . ASP A 1 164 ? -9.895  -7.385  -4.766  1.00   20.98 ? 165 ASP A CA  1 
ATOM   1373 C  C   . ASP A 1 164 ? -9.428  -6.106  -5.477  1.00   18.57 ? 165 ASP A C   1 
ATOM   1374 O  O   . ASP A 1 164 ? -8.424  -6.184  -6.212  1.00   22.92 ? 165 ASP A O   1 
ATOM   1375 C  CB  . ASP A 1 164 ? -10.690 -8.287  -5.755  1.00   25.93 ? 165 ASP A CB  1 
ATOM   1376 C  CG  . ASP A 1 164 ? -11.631 -7.470  -6.611  1.00   35.93 ? 165 ASP A CG  1 
ATOM   1377 O  OD1 . ASP A 1 164 ? -12.565 -6.837  -6.034  1.00   46.68 ? 165 ASP A OD1 1 
ATOM   1378 O  OD2 . ASP A 1 164 ? -11.451 -7.454  -7.870  0.0000 68.48 ? 165 ASP A OD2 1 
ATOM   1379 N  N   . SER A 1 165 ? -10.088 -4.948  -5.257  1.00   15.84 ? 166 SER A N   1 
ATOM   1380 C  CA  . SER A 1 165 ? -9.697  -3.701  -5.857  1.00   15.20 ? 166 SER A CA  1 
ATOM   1381 C  C   . SER A 1 165 ? -8.619  -2.953  -5.105  1.00   13.63 ? 166 SER A C   1 
ATOM   1382 O  O   . SER A 1 165 ? -8.121  -1.950  -5.601  1.00   15.51 ? 166 SER A O   1 
ATOM   1383 C  CB  . SER A 1 165 ? -10.851 -2.821  -6.208  1.00   18.42 ? 166 SER A CB  1 
ATOM   1384 O  OG  . SER A 1 165 ? -11.380 -2.236  -5.038  1.00   18.00 ? 166 SER A OG  1 
ATOM   1385 N  N   . ILE A 1 166 ? -8.304  -3.398  -3.872  1.00   12.87 ? 167 ILE A N   1 
ATOM   1386 C  CA  . ILE A 1 166 ? -7.277  -2.745  -3.070  1.00   12.60 ? 167 ILE A CA  1 
ATOM   1387 C  C   . ILE A 1 166 ? -6.271  -3.780  -2.547  1.00   10.98 ? 167 ILE A C   1 
ATOM   1388 O  O   . ILE A 1 166 ? -5.874  -3.764  -1.377  1.00   11.73 ? 167 ILE A O   1 
ATOM   1389 C  CB  . ILE A 1 166 ? -7.876  -1.913  -1.921  1.00   11.97 ? 167 ILE A CB  1 
ATOM   1390 C  CG1 . ILE A 1 166 ? -8.748  -2.751  -0.993  1.00   12.14 ? 167 ILE A CG1 1 
ATOM   1391 C  CG2 . ILE A 1 166 ? -8.647  -0.724  -2.478  1.00   14.02 ? 167 ILE A CG2 1 
ATOM   1392 C  CD1 . ILE A 1 166 ? -8.840  -2.143  0.376   1.00   12.85 ? 167 ILE A CD1 1 
ATOM   1393 N  N   . LYS A 1 167 ? -5.874  -4.680  -3.428  1.00   12.39 ? 168 LYS A N   1 
ATOM   1394 C  CA  . LYS A 1 167 ? -5.116  -5.820  -2.994  1.00   12.29 ? 168 LYS A CA  1 
ATOM   1395 C  C   . LYS A 1 167 ? -3.819  -5.424  -2.304  1.00   11.69 ? 168 LYS A C   1 
ATOM   1396 O  O   . LYS A 1 167 ? -3.345  -6.092  -1.365  1.00   11.94 ? 168 LYS A O   1 
ATOM   1397 C  CB  . LYS A 1 167 ? -4.799  -6.727  -4.220  1.00   14.09 ? 168 LYS A CB  1 
ATOM   1398 C  CG  . LYS A 1 167 ? -4.091  -8.011  -3.780  1.00   14.94 ? 168 LYS A CG  1 
ATOM   1399 C  CD  . LYS A 1 167 ? -3.841  -8.918  -4.978  1.00   21.03 ? 168 LYS A CD  1 
ATOM   1400 C  CE  . LYS A 1 167 ? -3.177  -10.258 -4.641  1.00   25.92 ? 168 LYS A CE  1 
ATOM   1401 N  NZ  . LYS A 1 167 ? -3.133  -11.126 -5.877  1.00   34.70 ? 168 LYS A NZ  1 
ATOM   1402 N  N   . THR A 1 168 ? -3.187  -4.402  -2.852  1.00   12.11 ? 169 THR A N   1 
ATOM   1403 C  CA  . THR A 1 168 ? -1.832  -4.106  -2.471  1.00   11.71 ? 169 THR A CA  1 
ATOM   1404 C  C   . THR A 1 168 ? -1.720  -2.681  -1.793  1.00   11.08 ? 169 THR A C   1 
ATOM   1405 O  O   . THR A 1 168 ? -2.607  -1.831  -1.924  1.00   12.56 ? 169 THR A O   1 
ATOM   1406 C  CB  . THR A 1 168 ? -0.849  -4.124  -3.678  1.00   13.71 ? 169 THR A CB  1 
ATOM   1407 O  OG1 . THR A 1 168 ? -1.430  -3.370  -4.767  1.00   14.56 ? 169 THR A OG1 1 
ATOM   1408 C  CG2 . THR A 1 168 ? -0.664  -5.573  -4.139  1.00   15.60 ? 169 THR A CG2 1 
ATOM   1409 N  N   A LYS A 1 169 ? -0.659  -2.556  -1.035  0.50   12.45 ? 170 LYS A N   1 
ATOM   1410 N  N   B LYS A 1 169 ? -0.648  -2.565  -1.037  0.50   13.39 ? 170 LYS A N   1 
ATOM   1411 C  CA  A LYS A 1 169 ? -0.439  -1.343  -0.287  0.50   11.05 ? 170 LYS A CA  1 
ATOM   1412 C  CA  B LYS A 1 169 ? -0.332  -1.387  -0.239  0.50   13.38 ? 170 LYS A CA  1 
ATOM   1413 C  C   A LYS A 1 169 ? -0.548  -0.112  -1.145  0.50   11.25 ? 170 LYS A C   1 
ATOM   1414 C  C   B LYS A 1 169 ? -0.320  -0.065  -1.000  0.50   13.73 ? 170 LYS A C   1 
ATOM   1415 O  O   A LYS A 1 169 ? 0.002   -0.058  -2.273  0.50   9.85  ? 170 LYS A O   1 
ATOM   1416 O  O   B LYS A 1 169 ? 0.504   0.049   -1.975  0.50   16.65 ? 170 LYS A O   1 
ATOM   1417 C  CB  A LYS A 1 169 ? 0.945   -1.364  0.363   0.50   11.67 ? 170 LYS A CB  1 
ATOM   1418 C  CB  B LYS A 1 169 ? 1.063   -1.577  0.312   0.50   13.81 ? 170 LYS A CB  1 
ATOM   1419 C  CG  A LYS A 1 169 ? 1.333   -0.155  1.248   0.50   13.98 ? 170 LYS A CG  1 
ATOM   1420 C  CG  B LYS A 1 169 ? 1.574   -0.358  1.054   0.50   14.31 ? 170 LYS A CG  1 
ATOM   1421 C  CD  A LYS A 1 169 ? 2.742   -0.214  1.787   0.50   17.35 ? 170 LYS A CD  1 
ATOM   1422 C  CD  B LYS A 1 169 ? 2.824   -0.683  1.788   0.50   15.61 ? 170 LYS A CD  1 
ATOM   1423 C  CE  A LYS A 1 169 ? 3.057   0.809   2.921   0.50   21.48 ? 170 LYS A CE  1 
ATOM   1424 C  CE  B LYS A 1 169 ? 3.878   -1.117  0.817   0.50   19.77 ? 170 LYS A CE  1 
ATOM   1425 N  NZ  A LYS A 1 169 ? 4.387   0.492   3.521   0.50   27.08 ? 170 LYS A NZ  1 
ATOM   1426 N  NZ  B LYS A 1 169 ? 5.119   -1.254  1.626   0.50   25.44 ? 170 LYS A NZ  1 
ATOM   1427 N  N   . GLY A 1 170 ? -1.206  0.867   -0.591  1.00   14.02 ? 171 GLY A N   1 
ATOM   1428 C  CA  . GLY A 1 170 ? -1.368  2.168   -1.252  1.00   14.36 ? 171 GLY A CA  1 
ATOM   1429 C  C   . GLY A 1 170 ? -2.551  2.239   -2.191  1.00   13.64 ? 171 GLY A C   1 
ATOM   1430 O  O   . GLY A 1 170 ? -2.829  3.330   -2.725  1.00   16.80 ? 171 GLY A O   1 
ATOM   1431 N  N   . LYS A 1 171 ? -3.227  1.137   -2.525  1.00   12.56 ? 172 LYS A N   1 
ATOM   1432 C  CA  . LYS A 1 171 ? -4.416  1.185   -3.285  1.00   13.53 ? 172 LYS A CA  1 
ATOM   1433 C  C   . LYS A 1 171 ? -5.611  1.643   -2.459  1.00   11.56 ? 172 LYS A C   1 
ATOM   1434 O  O   . LYS A 1 171 ? -5.812  1.213   -1.321  1.00   12.35 ? 172 LYS A O   1 
ATOM   1435 C  CB  . LYS A 1 171 ? -4.699  -0.152  -3.968  1.00   13.50 ? 172 LYS A CB  1 
ATOM   1436 C  CG  . LYS A 1 171 ? -3.681  -0.568  -4.988  1.00   15.44 ? 172 LYS A CG  1 
ATOM   1437 C  CD  . LYS A 1 171 ? -4.199  -1.666  -5.950  1.00   20.41 ? 172 LYS A CD  1 
ATOM   1438 C  CE  . LYS A 1 171 ? -5.371  -1.320  -6.873  1.00   26.88 ? 172 LYS A CE  1 
ATOM   1439 N  NZ  . LYS A 1 171 ? -5.732  -2.333  -7.955  1.00   29.22 ? 172 LYS A NZ  1 
ATOM   1440 N  N   . SER A 1 172 ? -6.464  2.446   -3.053  1.00   14.33 ? 173 SER A N   1 
ATOM   1441 C  CA  . SER A 1 172 ? -7.744  2.861   -2.449  1.00   14.31 ? 173 SER A CA  1 
ATOM   1442 C  C   . SER A 1 172 ? -8.879  2.737   -3.431  1.00   13.18 ? 173 SER A C   1 
ATOM   1443 O  O   . SER A 1 172 ? -8.662  2.611   -4.728  1.00   15.44 ? 173 SER A O   1 
ATOM   1444 C  CB  . SER A 1 172 ? -7.632  4.313   -1.940  1.00   15.48 ? 173 SER A CB  1 
ATOM   1445 O  OG  . SER A 1 172 ? -7.467  5.226   -3.004  1.00   19.02 ? 173 SER A OG  1 
ATOM   1446 N  N   . ALA A 1 173 ? -10.113 2.742   -2.952  1.00   14.35 ? 174 ALA A N   1 
ATOM   1447 C  CA  . ALA A 1 173 ? -11.310 2.692   -3.810  1.00   14.33 ? 174 ALA A CA  1 
ATOM   1448 C  C   . ALA A 1 173 ? -12.424 3.479   -3.209  1.00   13.62 ? 174 ALA A C   1 
ATOM   1449 O  O   . ALA A 1 173 ? -12.535 3.571   -1.936  1.00   12.56 ? 174 ALA A O   1 
ATOM   1450 C  CB  . ALA A 1 173 ? -11.749 1.242   -4.037  1.00   17.21 ? 174 ALA A CB  1 
ATOM   1451 N  N   . ASP A 1 174 ? -13.227 4.124   -4.006  1.00   15.82 ? 175 ASP A N   1 
ATOM   1452 C  CA  . ASP A 1 174 ? -14.410 4.774   -3.450  1.00   14.86 ? 175 ASP A CA  1 
ATOM   1453 C  C   . ASP A 1 174 ? -15.195 3.788   -2.713  1.00   14.88 ? 175 ASP A C   1 
ATOM   1454 O  O   . ASP A 1 174 ? -15.325 2.620   -3.136  1.00   17.20 ? 175 ASP A O   1 
ATOM   1455 C  CB  . ASP A 1 174 ? -15.232 5.327   -4.670  1.00   18.65 ? 175 ASP A CB  1 
ATOM   1456 C  CG  . ASP A 1 174 ? -14.463 6.470   -5.430  1.00   23.83 ? 175 ASP A CG  1 
ATOM   1457 O  OD1 . ASP A 1 174 ? -13.787 7.338   -4.781  1.00   34.98 ? 175 ASP A OD1 1 
ATOM   1458 O  OD2 . ASP A 1 174 ? -14.529 6.519   -6.720  1.00   24.11 ? 175 ASP A OD2 1 
ATOM   1459 N  N   . PHE A 1 175 ? -15.809 4.254   -1.591  1.00   13.82 ? 176 PHE A N   1 
ATOM   1460 C  CA  . PHE A 1 175 ? -16.558 3.341   -0.747  1.00   13.34 ? 176 PHE A CA  1 
ATOM   1461 C  C   . PHE A 1 175 ? -17.610 4.121   -0.016  1.00   12.58 ? 176 PHE A C   1 
ATOM   1462 O  O   . PHE A 1 175 ? -17.474 4.379   1.182   1.00   15.98 ? 176 PHE A O   1 
ATOM   1463 C  CB  . PHE A 1 175 ? -15.642 2.519   0.142   1.00   14.40 ? 176 PHE A CB  1 
ATOM   1464 C  CG  . PHE A 1 175 ? -16.253 1.285   0.661   1.00   13.23 ? 176 PHE A CG  1 
ATOM   1465 C  CD1 . PHE A 1 175 ? -16.532 0.235   -0.160  1.00   16.57 ? 176 PHE A CD1 1 
ATOM   1466 C  CD2 . PHE A 1 175 ? -16.567 1.156   2.022   1.00   13.18 ? 176 PHE A CD2 1 
ATOM   1467 C  CE1 . PHE A 1 175 ? -17.052 -0.926  0.332   1.00   18.56 ? 176 PHE A CE1 1 
ATOM   1468 C  CE2 . PHE A 1 175 ? -17.109 -0.017  2.550   1.00   15.00 ? 176 PHE A CE2 1 
ATOM   1469 C  CZ  . PHE A 1 175 ? -17.391 -1.062  1.687   1.00   15.90 ? 176 PHE A CZ  1 
ATOM   1470 N  N   . THR A 1 176 ? -18.652 4.545   -0.714  1.00   13.55 ? 177 THR A N   1 
ATOM   1471 C  CA  . THR A 1 176 ? -19.696 5.341   -0.144  1.00   12.63 ? 177 THR A CA  1 
ATOM   1472 C  C   . THR A 1 176 ? -20.852 4.570   0.299   1.00   11.99 ? 177 THR A C   1 
ATOM   1473 O  O   . THR A 1 176 ? -21.034 3.430   -0.174  1.00   13.01 ? 177 THR A O   1 
ATOM   1474 C  CB  . THR A 1 176 ? -20.107 6.427   -1.187  1.00   14.45 ? 177 THR A CB  1 
ATOM   1475 O  OG1 . THR A 1 176 ? -20.461 5.822   -2.447  1.00   21.19 ? 177 THR A OG1 1 
ATOM   1476 C  CG2 . THR A 1 176 ? -18.972 7.502   -1.403  1.00   21.67 ? 177 THR A CG2 1 
ATOM   1477 N  N   . ASN A 1 177 ? -21.660 5.145   1.170   1.00   12.59 ? 178 ASN A N   1 
ATOM   1478 C  CA  . ASN A 1 177 ? -22.918 4.588   1.605   1.00   13.69 ? 178 ASN A CA  1 
ATOM   1479 C  C   . ASN A 1 177 ? -22.797 3.262   2.344   1.00   12.68 ? 178 ASN A C   1 
ATOM   1480 O  O   . ASN A 1 177 ? -23.732 2.518   2.370   1.00   19.33 ? 178 ASN A O   1 
ATOM   1481 C  CB  . ASN A 1 177 ? -23.906 4.504   0.444   1.00   14.10 ? 178 ASN A CB  1 
ATOM   1482 C  CG  . ASN A 1 177 ? -24.121 5.870   -0.168  1.00   14.18 ? 178 ASN A CG  1 
ATOM   1483 O  OD1 . ASN A 1 177 ? -24.722 6.717   0.456   1.00   17.04 ? 178 ASN A OD1 1 
ATOM   1484 N  ND2 . ASN A 1 177 ? -23.485 6.130   -1.298  1.00   15.71 ? 178 ASN A ND2 1 
ATOM   1485 N  N   . PHE A 1 178 ? -21.633 3.011   2.951   1.00   12.00 ? 179 PHE A N   1 
ATOM   1486 C  CA  . PHE A 1 178 ? -21.504 1.807   3.777   1.00   12.35 ? 179 PHE A CA  1 
ATOM   1487 C  C   . PHE A 1 178 ? -21.997 2.058   5.167   1.00   11.75 ? 179 PHE A C   1 
ATOM   1488 O  O   . PHE A 1 178 ? -21.610 3.077   5.785   1.00   12.81 ? 179 PHE A O   1 
ATOM   1489 C  CB  . PHE A 1 178 ? -20.084 1.346   3.836   1.00   13.29 ? 179 PHE A CB  1 
ATOM   1490 C  CG  . PHE A 1 178 ? -19.937 0.099   4.659   1.00   12.41 ? 179 PHE A CG  1 
ATOM   1491 C  CD1 . PHE A 1 178 ? -20.314 -1.161  4.121   1.00   14.06 ? 179 PHE A CD1 1 
ATOM   1492 C  CD2 . PHE A 1 178 ? -19.573 0.155   6.012   1.00   11.52 ? 179 PHE A CD2 1 
ATOM   1493 C  CE1 . PHE A 1 178 ? -20.293 -2.294  4.879   1.00   14.53 ? 179 PHE A CE1 1 
ATOM   1494 C  CE2 . PHE A 1 178 ? -19.573 -1.002  6.785   1.00   11.29 ? 179 PHE A CE2 1 
ATOM   1495 C  CZ  . PHE A 1 178 ? -19.930 -2.232  6.267   1.00   12.44 ? 179 PHE A CZ  1 
ATOM   1496 N  N   . ASP A 1 179 ? -22.886 1.227   5.676   1.00   11.85 ? 180 ASP A N   1 
ATOM   1497 C  CA  . ASP A 1 179 ? -23.535 1.486   6.975   1.00   11.95 ? 180 ASP A CA  1 
ATOM   1498 C  C   . ASP A 1 179 ? -22.876 0.580   8.035   1.00   11.28 ? 180 ASP A C   1 
ATOM   1499 O  O   . ASP A 1 179 ? -23.089 -0.628  8.067   1.00   12.29 ? 180 ASP A O   1 
ATOM   1500 C  CB  . ASP A 1 179 ? -24.986 1.070   6.862   1.00   14.19 ? 180 ASP A CB  1 
ATOM   1501 C  CG  . ASP A 1 179 ? -25.772 1.430   8.106   1.00   15.02 ? 180 ASP A CG  1 
ATOM   1502 O  OD1 . ASP A 1 179 ? -25.190 1.705   9.178   1.00   14.28 ? 180 ASP A OD1 1 
ATOM   1503 O  OD2 . ASP A 1 179 ? -27.006 1.475   7.976   1.00   21.73 ? 180 ASP A OD2 1 
ATOM   1504 N  N   . PRO A 1 180 ? -22.054 1.178   8.937   1.00   10.21 ? 181 PRO A N   1 
ATOM   1505 C  CA  . PRO A 1 180 ? -21.341 0.326   9.938   1.00   11.25 ? 181 PRO A CA  1 
ATOM   1506 C  C   . PRO A 1 180 ? -22.260 -0.261  10.993  1.00   10.37 ? 181 PRO A C   1 
ATOM   1507 O  O   . PRO A 1 180 ? -21.799 -1.144  11.737  1.00   10.96 ? 181 PRO A O   1 
ATOM   1508 C  CB  . PRO A 1 180 ? -20.328 1.311   10.528  1.00   12.24 ? 181 PRO A CB  1 
ATOM   1509 C  CG  . PRO A 1 180 ? -20.993 2.690   10.400  1.00   12.96 ? 181 PRO A CG  1 
ATOM   1510 C  CD  . PRO A 1 180 ? -21.695 2.603   9.015   1.00   11.70 ? 181 PRO A CD  1 
ATOM   1511 N  N   . ARG A 1 181 ? -23.517 0.144   11.027  1.00   11.22 ? 182 ARG A N   1 
ATOM   1512 C  CA  . ARG A 1 181 ? -24.446 -0.551  11.941  1.00   11.45 ? 182 ARG A CA  1 
ATOM   1513 C  C   . ARG A 1 181 ? -24.552 -2.012  11.615  1.00   11.51 ? 182 ARG A C   1 
ATOM   1514 O  O   . ARG A 1 181 ? -24.906 -2.811  12.523  1.00   13.25 ? 182 ARG A O   1 
ATOM   1515 C  CB  . ARG A 1 181 ? -25.851 0.071   11.898  1.00   12.44 ? 182 ARG A CB  1 
ATOM   1516 C  CG  . ARG A 1 181 ? -25.812 1.502   12.422  1.00   13.76 ? 182 ARG A CG  1 
ATOM   1517 C  CD  . ARG A 1 181 ? -27.175 2.174   12.344  1.00   16.44 ? 182 ARG A CD  1 
ATOM   1518 N  NE  . ARG A 1 181 ? -27.495 2.433   10.940  1.00   16.57 ? 182 ARG A NE  1 
ATOM   1519 C  CZ  . ARG A 1 181 ? -28.532 3.187   10.604  1.00   17.75 ? 182 ARG A CZ  1 
ATOM   1520 N  NH1 . ARG A 1 181 ? -29.356 3.685   11.536  1.00   21.82 ? 182 ARG A NH1 1 
ATOM   1521 N  NH2 . ARG A 1 181 ? -28.797 3.354   9.320   1.00   23.38 ? 182 ARG A NH2 1 
ATOM   1522 N  N   . GLY A 1 182 ? -24.307 -2.396  10.361  1.00   11.83 ? 183 GLY A N   1 
ATOM   1523 C  CA  . GLY A 1 182 ? -24.406 -3.769  9.984   1.00   13.25 ? 183 GLY A CA  1 
ATOM   1524 C  C   . GLY A 1 182 ? -23.285 -4.628  10.541  1.00   12.79 ? 183 GLY A C   1 
ATOM   1525 O  O   . GLY A 1 182 ? -23.277 -5.827  10.264  1.00   16.27 ? 183 GLY A O   1 
ATOM   1526 N  N   . LEU A 1 183 ? -22.279 -4.049  11.261  1.00   11.66 ? 184 LEU A N   1 
ATOM   1527 C  CA  . LEU A 1 183 ? -21.167 -4.766  11.850  1.00   11.68 ? 184 LEU A CA  1 
ATOM   1528 C  C   . LEU A 1 183 ? -21.325 -4.953  13.341  1.00   11.12 ? 184 LEU A C   1 
ATOM   1529 O  O   . LEU A 1 183 ? -20.375 -5.542  13.966  1.00   12.94 ? 184 LEU A O   1 
ATOM   1530 C  CB  . LEU A 1 183 ? -19.840 -4.106  11.511  1.00   11.58 ? 184 LEU A CB  1 
ATOM   1531 C  CG  . LEU A 1 183 ? -19.587 -4.029  10.019  1.00   12.85 ? 184 LEU A CG  1 
ATOM   1532 C  CD1 . LEU A 1 183 ? -18.293 -3.258  9.836   1.00   14.51 ? 184 LEU A CD1 1 
ATOM   1533 C  CD2 . LEU A 1 183 ? -19.564 -5.358  9.301   1.00   15.82 ? 184 LEU A CD2 1 
ATOM   1534 N  N   A LEU A 1 184 ? -22.430 -4.463  13.968  0.50   12.31 ? 185 LEU A N   1 
ATOM   1535 N  N   B LEU A 1 184 ? -22.389 -4.536  13.922  0.50   11.59 ? 185 LEU A N   1 
ATOM   1536 C  CA  A LEU A 1 184 ? -22.690 -4.453  15.453  0.50   10.82 ? 185 LEU A CA  1 
ATOM   1537 C  CA  B LEU A 1 184 ? -22.408 -4.658  15.291  0.50   10.72 ? 185 LEU A CA  1 
ATOM   1538 C  C   A LEU A 1 184 ? -23.467 -5.657  16.025  0.50   9.89  ? 185 LEU A C   1 
ATOM   1539 C  C   B LEU A 1 184 ? -23.029 -6.030  15.620  0.50   9.73  ? 185 LEU A C   1 
ATOM   1540 O  O   A LEU A 1 184 ? -24.521 -6.028  15.448  0.50   9.65  ? 185 LEU A O   1 
ATOM   1541 O  O   B LEU A 1 184 ? -23.781 -6.555  14.803  0.50   10.91 ? 185 LEU A O   1 
ATOM   1542 C  CB  A LEU A 1 184 ? -23.478 -3.199  15.890  0.50   10.64 ? 185 LEU A CB  1 
ATOM   1543 C  CB  B LEU A 1 184 ? -23.314 -3.495  15.809  0.50   10.82 ? 185 LEU A CB  1 
ATOM   1544 C  CG  A LEU A 1 184 ? -22.789 -1.963  15.319  0.50   10.66 ? 185 LEU A CG  1 
ATOM   1545 C  CG  B LEU A 1 184 ? -22.833 -2.002  15.666  0.50   11.10 ? 185 LEU A CG  1 
ATOM   1546 C  CD1 A LEU A 1 184 ? -23.569 -0.765  15.788  0.50   12.01 ? 185 LEU A CD1 1 
ATOM   1547 C  CD1 B LEU A 1 184 ? -23.870 -0.972  16.073  0.50   12.04 ? 185 LEU A CD1 1 
ATOM   1548 C  CD2 A LEU A 1 184 ? -21.330 -1.939  15.824  0.50   9.90  ? 185 LEU A CD2 1 
ATOM   1549 C  CD2 B LEU A 1 184 ? -21.513 -1.681  16.396  0.50   11.33 ? 185 LEU A CD2 1 
ATOM   1550 N  N   A PRO A 1 185 ? -22.983 -6.228  17.132  0.50   9.54  ? 186 PRO A N   1 
ATOM   1551 N  N   B PRO A 1 185 ? -22.780 -6.578  16.799  0.50   9.27  ? 186 PRO A N   1 
ATOM   1552 C  CA  A PRO A 1 185 ? -23.674 -7.351  17.729  0.50   9.87  ? 186 PRO A CA  1 
ATOM   1553 C  CA  B PRO A 1 185 ? -23.589 -7.696  17.287  0.50   10.52 ? 186 PRO A CA  1 
ATOM   1554 C  C   A PRO A 1 185 ? -24.974 -6.890  18.332  0.50   9.44  ? 186 PRO A C   1 
ATOM   1555 C  C   B PRO A 1 185 ? -24.901 -7.108  17.908  0.50   10.07 ? 186 PRO A C   1 
ATOM   1556 O  O   A PRO A 1 185 ? -25.237 -5.709  18.531  0.50   8.10  ? 186 PRO A O   1 
ATOM   1557 O  O   B PRO A 1 185 ? -25.072 -5.900  17.806  0.50   10.58 ? 186 PRO A O   1 
ATOM   1558 C  CB  A PRO A 1 185 ? -22.661 -7.912  18.765  0.50   11.03 ? 186 PRO A CB  1 
ATOM   1559 C  CB  B PRO A 1 185 ? -22.703 -8.293  18.362  0.50   9.24  ? 186 PRO A CB  1 
ATOM   1560 C  CG  A PRO A 1 185 ? -21.914 -6.676  19.110  0.50   9.89  ? 186 PRO A CG  1 
ATOM   1561 C  CG  B PRO A 1 185 ? -22.086 -7.065  18.946  0.50   8.43  ? 186 PRO A CG  1 
ATOM   1562 C  CD  A PRO A 1 185 ? -21.741 -5.864  17.837  0.50   10.64 ? 186 PRO A CD  1 
ATOM   1563 C  CD  B PRO A 1 185 ? -21.823 -6.104  17.801  0.50   9.16  ? 186 PRO A CD  1 
ATOM   1564 N  N   . GLU A 1 186 ? -25.740 -7.908  18.624  1.00   12.65 ? 187 GLU A N   1 
ATOM   1565 C  CA  . GLU A 1 186 ? -27.004 -7.550  19.244  1.00   12.04 ? 187 GLU A CA  1 
ATOM   1566 C  C   . GLU A 1 186 ? -26.833 -6.790  20.549  1.00   11.62 ? 187 GLU A C   1 
ATOM   1567 O  O   . GLU A 1 186 ? -27.444 -5.757  20.774  1.00   14.74 ? 187 GLU A O   1 
ATOM   1568 C  CB  . GLU A 1 186 ? -27.705 -8.862  19.481  1.00   16.14 ? 187 GLU A CB  1 
ATOM   1569 C  CG  . GLU A 1 186 ? -28.981 -8.714  20.230  1.00   20.51 ? 187 GLU A CG  1 
ATOM   1570 C  CD  . GLU A 1 186 ? -29.629 -10.052 20.603  1.00   22.42 ? 187 GLU A CD  1 
ATOM   1571 O  OE1 . GLU A 1 186 ? -29.423 -10.973 19.877  1.00   21.50 ? 187 GLU A OE1 1 
ATOM   1572 O  OE2 . GLU A 1 186 ? -30.400 -10.047 21.596  1.00   26.60 ? 187 GLU A OE2 1 
ATOM   1573 N  N   . SER A 1 187 ? -25.933 -7.291  21.421  1.00   10.89 ? 188 SER A N   1 
ATOM   1574 C  CA  . SER A 1 187 ? -25.762 -6.660  22.710  1.00   11.24 ? 188 SER A CA  1 
ATOM   1575 C  C   . SER A 1 187 ? -24.597 -5.675  22.689  1.00   10.52 ? 188 SER A C   1 
ATOM   1576 O  O   . SER A 1 187 ? -23.546 -5.962  22.095  1.00   11.65 ? 188 SER A O   1 
ATOM   1577 C  CB  . SER A 1 187 ? -25.355 -7.752  23.695  1.00   12.90 ? 188 SER A CB  1 
ATOM   1578 O  OG  . SER A 1 187 ? -25.053 -7.182  24.992  1.00   13.24 ? 188 SER A OG  1 
ATOM   1579 N  N   . LEU A 1 188 ? -24.734 -4.592  23.381  1.00   10.26 ? 189 LEU A N   1 
ATOM   1580 C  CA  . LEU A 1 188 ? -23.661 -3.615  23.600  1.00   11.42 ? 189 LEU A CA  1 
ATOM   1581 C  C   . LEU A 1 188 ? -23.029 -3.779  24.984  1.00   10.69 ? 189 LEU A C   1 
ATOM   1582 O  O   . LEU A 1 188 ? -22.309 -2.831  25.406  1.00   11.82 ? 189 LEU A O   1 
ATOM   1583 C  CB  . LEU A 1 188 ? -24.130 -2.197  23.374  1.00   13.79 ? 189 LEU A CB  1 
ATOM   1584 C  CG  . LEU A 1 188 ? -24.624 -1.881  21.982  1.00   14.43 ? 189 LEU A CG  1 
ATOM   1585 C  CD1 . LEU A 1 188 ? -25.141 -0.461  21.841  1.00   19.11 ? 189 LEU A CD1 1 
ATOM   1586 C  CD2 . LEU A 1 188 ? -23.582 -2.222  20.900  1.00   16.68 ? 189 LEU A CD2 1 
ATOM   1587 N  N   . ASP A 1 189 ? -23.154 -4.902  25.670  1.00   9.79  ? 190 ASP A N   1 
ATOM   1588 C  CA  . ASP A 1 189 ? -22.380 -5.089  26.876  1.00   10.23 ? 190 ASP A CA  1 
ATOM   1589 C  C   . ASP A 1 189 ? -20.883 -5.061  26.559  1.00   8.96  ? 190 ASP A C   1 
ATOM   1590 O  O   . ASP A 1 189 ? -20.471 -5.604  25.541  1.00   8.71  ? 190 ASP A O   1 
ATOM   1591 C  CB  . ASP A 1 189 ? -22.731 -6.460  27.464  1.00   12.28 ? 190 ASP A CB  1 
ATOM   1592 C  CG  . ASP A 1 189 ? -24.137 -6.529  28.129  1.00   17.32 ? 190 ASP A CG  1 
ATOM   1593 O  OD1 . ASP A 1 189 ? -24.765 -5.467  28.293  1.00   20.78 ? 190 ASP A OD1 1 
ATOM   1594 O  OD2 . ASP A 1 189 ? -24.530 -7.682  28.437  1.00   24.02 ? 190 ASP A OD2 1 
ATOM   1595 N  N   . TYR A 1 190 ? -20.113 -4.463  27.487  1.00   8.65  ? 191 TYR A N   1 
ATOM   1596 C  CA  . TYR A 1 190 ? -18.693 -4.253  27.168  1.00   8.32  ? 191 TYR A CA  1 
ATOM   1597 C  C   . TYR A 1 190 ? -17.824 -4.316  28.402  1.00   7.64  ? 191 TYR A C   1 
ATOM   1598 O  O   . TYR A 1 190 ? -18.278 -4.161  29.560  1.00   8.75  ? 191 TYR A O   1 
ATOM   1599 C  CB  . TYR A 1 190 ? -18.561 -2.853  26.495  1.00   8.65  ? 191 TYR A CB  1 
ATOM   1600 C  CG  . TYR A 1 190 ? -18.961 -1.682  27.346  1.00   8.67  ? 191 TYR A CG  1 
ATOM   1601 C  CD1 . TYR A 1 190 ? -18.060 -1.065  28.208  1.00   9.46  ? 191 TYR A CD1 1 
ATOM   1602 C  CD2 . TYR A 1 190 ? -20.235 -1.171  27.284  1.00   8.86  ? 191 TYR A CD2 1 
ATOM   1603 C  CE1 . TYR A 1 190 ? -18.415 -0.022  29.046  1.00   9.42  ? 191 TYR A CE1 1 
ATOM   1604 C  CE2 . TYR A 1 190 ? -20.622 -0.100  28.074  1.00   10.31 ? 191 TYR A CE2 1 
ATOM   1605 C  CZ  . TYR A 1 190 ? -19.727 0.462   28.966  1.00   10.65 ? 191 TYR A CZ  1 
ATOM   1606 O  OH  . TYR A 1 190 ? -20.049 1.489   29.855  1.00   11.80 ? 191 TYR A OH  1 
ATOM   1607 N  N   . TRP A 1 191 ? -16.542 -4.416  28.112  1.00   7.47  ? 192 TRP A N   1 
ATOM   1608 C  CA  . TRP A 1 191 ? -15.458 -4.181  29.053  1.00   7.70  ? 192 TRP A CA  1 
ATOM   1609 C  C   . TRP A 1 191 ? -14.751 -2.892  28.640  1.00   7.19  ? 192 TRP A C   1 
ATOM   1610 O  O   . TRP A 1 191 ? -14.692 -2.556  27.444  1.00   8.15  ? 192 TRP A O   1 
ATOM   1611 C  CB  . TRP A 1 191 ? -14.410 -5.299  29.047  1.00   8.11  ? 192 TRP A CB  1 
ATOM   1612 C  CG  . TRP A 1 191 ? -14.939 -6.633  29.467  1.00   7.97  ? 192 TRP A CG  1 
ATOM   1613 C  CD1 . TRP A 1 191 ? -15.169 -7.037  30.759  1.00   9.44  ? 192 TRP A CD1 1 
ATOM   1614 C  CD2 . TRP A 1 191 ? -15.229 -7.746  28.636  1.00   7.72  ? 192 TRP A CD2 1 
ATOM   1615 N  NE1 . TRP A 1 191 ? -15.583 -8.366  30.751  1.00   10.34 ? 192 TRP A NE1 1 
ATOM   1616 C  CE2 . TRP A 1 191 ? -15.623 -8.801  29.470  1.00   9.96  ? 192 TRP A CE2 1 
ATOM   1617 C  CE3 . TRP A 1 191 ? -15.126 -7.962  27.232  1.00   8.64  ? 192 TRP A CE3 1 
ATOM   1618 C  CZ2 . TRP A 1 191 ? -15.948 -10.085 28.930  1.00   10.45 ? 192 TRP A CZ2 1 
ATOM   1619 C  CZ3 . TRP A 1 191 ? -15.402 -9.239  26.753  1.00   9.64  ? 192 TRP A CZ3 1 
ATOM   1620 C  CH2 . TRP A 1 191 ? -15.771 -10.249 27.606  1.00   10.65 ? 192 TRP A CH2 1 
ATOM   1621 N  N   . THR A 1 192 ? -14.168 -2.175  29.580  1.00   7.05  ? 193 THR A N   1 
ATOM   1622 C  CA  . THR A 1 192 ? -13.443 -0.951  29.262  1.00   7.28  ? 193 THR A CA  1 
ATOM   1623 C  C   . THR A 1 192 ? -12.212 -0.805  30.122  1.00   7.05  ? 193 THR A C   1 
ATOM   1624 O  O   . THR A 1 192 ? -12.197 -1.164  31.290  1.00   7.72  ? 193 THR A O   1 
ATOM   1625 C  CB  . THR A 1 192 ? -14.380 0.267   29.380  1.00   7.61  ? 193 THR A CB  1 
ATOM   1626 O  OG1 . THR A 1 192 ? -13.707 1.456   28.984  1.00   8.07  ? 193 THR A OG1 1 
ATOM   1627 C  CG2 . THR A 1 192 ? -14.938 0.464   30.766  1.00   8.81  ? 193 THR A CG2 1 
ATOM   1628 N  N   . TYR A 1 193 ? -11.171 -0.192  29.527  1.00   7.16  ? 194 TYR A N   1 
ATOM   1629 C  CA  . TYR A 1 193 ? -9.937  0.110   30.246  1.00   7.06  ? 194 TYR A CA  1 
ATOM   1630 C  C   . TYR A 1 193 ? -9.202  1.148   29.455  1.00   6.58  ? 194 TYR A C   1 
ATOM   1631 O  O   . TYR A 1 193 ? -9.402  1.343   28.273  1.00   7.11  ? 194 TYR A O   1 
ATOM   1632 C  CB  . TYR A 1 193 ? -9.109  -1.172  30.443  1.00   7.59  ? 194 TYR A CB  1 
ATOM   1633 C  CG  . TYR A 1 193 ? -8.426  -1.644  29.195  1.00   7.13  ? 194 TYR A CG  1 
ATOM   1634 C  CD1 . TYR A 1 193 ? -9.087  -2.376  28.176  1.00   7.05  ? 194 TYR A CD1 1 
ATOM   1635 C  CD2 . TYR A 1 193 ? -7.086  -1.298  28.935  1.00   7.49  ? 194 TYR A CD2 1 
ATOM   1636 C  CE1 . TYR A 1 193 ? -8.498  -2.694  26.972  1.00   6.90  ? 194 TYR A CE1 1 
ATOM   1637 C  CE2 . TYR A 1 193 ? -6.458  -1.641  27.733  1.00   7.78  ? 194 TYR A CE2 1 
ATOM   1638 C  CZ  . TYR A 1 193 ? -7.146  -2.346  26.743  1.00   6.69  ? 194 TYR A CZ  1 
ATOM   1639 O  OH  . TYR A 1 193 ? -6.504  -2.615  25.595  1.00   7.19  ? 194 TYR A OH  1 
ATOM   1640 N  N   . PRO A 1 194 ? -8.235  1.850   30.132  1.00   7.04  ? 195 PRO A N   1 
ATOM   1641 C  CA  . PRO A 1 194 ? -7.416  2.873   29.436  1.00   7.37  ? 195 PRO A CA  1 
ATOM   1642 C  C   . PRO A 1 194 ? -6.220  2.202   28.758  1.00   6.55  ? 195 PRO A C   1 
ATOM   1643 O  O   . PRO A 1 194 ? -5.473  1.423   29.401  1.00   7.46  ? 195 PRO A O   1 
ATOM   1644 C  CB  . PRO A 1 194 ? -6.945  3.780   30.577  1.00   8.58  ? 195 PRO A CB  1 
ATOM   1645 C  CG  . PRO A 1 194 ? -6.897  2.837   31.781  1.00   8.82  ? 195 PRO A CG  1 
ATOM   1646 C  CD  . PRO A 1 194 ? -8.032  1.892   31.593  1.00   7.96  ? 195 PRO A CD  1 
ATOM   1647 N  N   . GLY A 1 195 ? -5.993  2.515   27.495  1.00   6.57  ? 196 GLY A N   1 
ATOM   1648 C  CA  . GLY A 1 195 ? -4.870  1.901   26.783  1.00   7.30  ? 196 GLY A CA  1 
ATOM   1649 C  C   . GLY A 1 195 ? -4.365  2.758   25.674  1.00   6.24  ? 196 GLY A C   1 
ATOM   1650 O  O   . GLY A 1 195 ? -4.255  4.000   25.809  1.00   6.92  ? 196 GLY A O   1 
ATOM   1651 N  N   . SER A 1 196 ? -3.938  2.103   24.607  1.00   6.26  ? 197 SER A N   1 
ATOM   1652 C  CA  . SER A 1 196 ? -3.108  2.751   23.569  1.00   6.71  ? 197 SER A CA  1 
ATOM   1653 C  C   . SER A 1 196 ? -3.582  2.354   22.187  1.00   6.26  ? 197 SER A C   1 
ATOM   1654 O  O   . SER A 1 196 ? -4.328  1.390   21.994  1.00   6.57  ? 197 SER A O   1 
ATOM   1655 C  CB  . SER A 1 196 ? -1.626  2.362   23.730  1.00   7.05  ? 197 SER A CB  1 
ATOM   1656 O  OG  . SER A 1 196 ? -1.391  1.020   23.307  1.00   6.96  ? 197 SER A OG  1 
ATOM   1657 N  N   . LEU A 1 197 ? -3.035  3.034   21.172  1.00   6.37  ? 198 LEU A N   1 
ATOM   1658 C  CA  . LEU A 1 197 ? -3.056  2.508   19.824  1.00   6.61  ? 198 LEU A CA  1 
ATOM   1659 C  C   . LEU A 1 197 ? -2.319  1.183   19.833  1.00   6.41  ? 198 LEU A C   1 
ATOM   1660 O  O   . LEU A 1 197 ? -1.278  1.031   20.514  1.00   7.24  ? 198 LEU A O   1 
ATOM   1661 C  CB  . LEU A 1 197 ? -2.333  3.448   18.867  1.00   7.49  ? 198 LEU A CB  1 
ATOM   1662 C  CG  . LEU A 1 197 ? -2.833  4.890   18.830  1.00   7.94  ? 198 LEU A CG  1 
ATOM   1663 C  CD1 . LEU A 1 197 ? -2.011  5.700   17.803  1.00   8.99  ? 198 LEU A CD1 1 
ATOM   1664 C  CD2 . LEU A 1 197 ? -4.308  4.982   18.492  1.00   8.63  ? 198 LEU A CD2 1 
ATOM   1665 N  N   . THR A 1 198 ? -2.728  0.218   19.005  1.00   6.68  ? 199 THR A N   1 
ATOM   1666 C  CA  . THR A 1 198 ? -2.080  -1.073  18.954  1.00   7.13  ? 199 THR A CA  1 
ATOM   1667 C  C   . THR A 1 198 ? -1.067  -1.156  17.799  1.00   7.29  ? 199 THR A C   1 
ATOM   1668 O  O   . THR A 1 198 ? -0.481  -2.253  17.630  1.00   8.09  ? 199 THR A O   1 
ATOM   1669 C  CB  . THR A 1 198 ? -3.072  -2.231  18.867  1.00   6.96  ? 199 THR A CB  1 
ATOM   1670 O  OG1 . THR A 1 198 ? -3.662  -2.198  17.573  1.00   7.01  ? 199 THR A OG1 1 
ATOM   1671 C  CG2 . THR A 1 198 ? -4.079  -2.210  19.996  1.00   7.97  ? 199 THR A CG2 1 
ATOM   1672 N  N   . THR A 1 199 ? -0.909  -0.111  17.021  1.00   7.40  ? 200 THR A N   1 
ATOM   1673 C  CA  . THR A 1 199 ? 0.169   -0.026  16.042  1.00   7.99  ? 200 THR A CA  1 
ATOM   1674 C  C   . THR A 1 199 ? 0.931   1.232   16.332  1.00   7.96  ? 200 THR A C   1 
ATOM   1675 O  O   . THR A 1 199 ? 0.450   2.181   16.909  1.00   8.61  ? 200 THR A O   1 
ATOM   1676 C  CB  . THR A 1 199 ? -0.343  0.024   14.584  1.00   8.24  ? 200 THR A CB  1 
ATOM   1677 O  OG1 . THR A 1 199 ? -1.350  1.042   14.417  1.00   12.48 ? 200 THR A OG1 1 
ATOM   1678 C  CG2 . THR A 1 199 ? -1.007  -1.251  14.228  1.00   11.18 ? 200 THR A CG2 1 
ATOM   1679 N  N   . PRO A 1 200 ? 2.221   1.282   15.877  1.00   9.30  ? 201 PRO A N   1 
ATOM   1680 C  CA  . PRO A 1 200 ? 2.968   2.536   15.967  1.00   9.68  ? 201 PRO A CA  1 
ATOM   1681 C  C   . PRO A 1 200 ? 2.151   3.676   15.455  1.00   10.41 ? 201 PRO A C   1 
ATOM   1682 O  O   . PRO A 1 200 ? 1.491   3.553   14.389  1.00   12.63 ? 201 PRO A O   1 
ATOM   1683 C  CB  . PRO A 1 200 ? 4.188   2.232   15.096  1.00   11.44 ? 201 PRO A CB  1 
ATOM   1684 C  CG  . PRO A 1 200 ? 4.424   0.770   15.340  1.00   10.71 ? 201 PRO A CG  1 
ATOM   1685 C  CD  . PRO A 1 200 ? 3.027   0.198   15.270  1.00   10.16 ? 201 PRO A CD  1 
ATOM   1686 N  N   . PRO A 1 201 ? 2.171   4.823   16.106  1.00   9.80  ? 202 PRO A N   1 
ATOM   1687 C  CA  . PRO A 1 201 ? 3.095   5.236   17.194  1.00   9.29  ? 202 PRO A CA  1 
ATOM   1688 C  C   . PRO A 1 201 ? 2.728   4.776   18.616  1.00   8.94  ? 202 PRO A C   1 
ATOM   1689 O  O   . PRO A 1 201 ? 3.380   5.200   19.554  1.00   9.47  ? 202 PRO A O   1 
ATOM   1690 C  CB  . PRO A 1 201 ? 3.070   6.740   17.044  1.00   12.04 ? 202 PRO A CB  1 
ATOM   1691 C  CG  . PRO A 1 201 ? 1.697   7.061   16.578  1.00   12.50 ? 202 PRO A CG  1 
ATOM   1692 C  CD  . PRO A 1 201 ? 1.389   5.973   15.584  1.00   11.81 ? 202 PRO A CD  1 
ATOM   1693 N  N   . LEU A 1 202 ? 1.685   3.922   18.788  1.00   8.35  ? 203 LEU A N   1 
ATOM   1694 C  CA  . LEU A 1 202 ? 1.458   3.268   20.093  1.00   7.89  ? 203 LEU A CA  1 
ATOM   1695 C  C   . LEU A 1 202 ? 1.098   4.273   21.194  1.00   7.72  ? 203 LEU A C   1 
ATOM   1696 O  O   . LEU A 1 202 ? 1.269   4.035   22.370  1.00   7.88  ? 203 LEU A O   1 
ATOM   1697 C  CB  . LEU A 1 202 ? 2.643   2.371   20.544  1.00   8.45  ? 203 LEU A CB  1 
ATOM   1698 C  CG  . LEU A 1 202 ? 2.960   1.244   19.565  1.00   8.11  ? 203 LEU A CG  1 
ATOM   1699 C  CD1 . LEU A 1 202 ? 4.261   0.595   20.005  1.00   10.42 ? 203 LEU A CD1 1 
ATOM   1700 C  CD2 . LEU A 1 202 ? 1.848   0.193   19.464  1.00   9.19  ? 203 LEU A CD2 1 
ATOM   1701 N  N   . LEU A 1 203 ? 0.507   5.406   20.763  1.00   8.02  ? 204 LEU A N   1 
ATOM   1702 C  CA  . LEU A 1 203 ? 0.221   6.503   21.694  1.00   8.40  ? 204 LEU A CA  1 
ATOM   1703 C  C   . LEU A 1 203 ? -0.832  6.106   22.725  1.00   7.83  ? 204 LEU A C   1 
ATOM   1704 O  O   . LEU A 1 203 ? -1.809  5.357   22.411  1.00   8.10  ? 204 LEU A O   1 
ATOM   1705 C  CB  . LEU A 1 203 ? -0.289  7.738   20.919  1.00   9.23  ? 204 LEU A CB  1 
ATOM   1706 C  CG  . LEU A 1 203 ? 0.778   8.316   19.982  1.00   10.13 ? 204 LEU A CG  1 
ATOM   1707 C  CD1 . LEU A 1 203 ? 0.169   9.363   19.098  1.00   12.64 ? 204 LEU A CD1 1 
ATOM   1708 C  CD2 . LEU A 1 203 ? 1.954   8.920   20.794  1.00   14.67 ? 204 LEU A CD2 1 
ATOM   1709 N  N   . GLU A 1 204 ? -0.651  6.543   23.953  1.00   8.32  ? 205 GLU A N   1 
ATOM   1710 C  CA  . GLU A 1 204 ? -1.473  6.162   25.105  1.00   8.20  ? 205 GLU A CA  1 
ATOM   1711 C  C   . GLU A 1 204 ? -2.655  7.137   25.238  1.00   7.94  ? 205 GLU A C   1 
ATOM   1712 O  O   . GLU A 1 204 ? -2.743  7.912   26.184  1.00   10.48 ? 205 GLU A O   1 
ATOM   1713 C  CB  . GLU A 1 204 ? -0.599  6.039   26.326  1.00   9.65  ? 205 GLU A CB  1 
ATOM   1714 C  CG  . GLU A 1 204 ? 0.282   4.815   26.184  1.00   10.07 ? 205 GLU A CG  1 
ATOM   1715 C  CD  . GLU A 1 204 ? 1.253   4.517   27.348  1.00   10.31 ? 205 GLU A CD  1 
ATOM   1716 O  OE1 . GLU A 1 204 ? 1.571   5.475   28.118  1.00   11.73 ? 205 GLU A OE1 1 
ATOM   1717 O  OE2 . GLU A 1 204 ? 1.647   3.343   27.509  1.00   10.21 ? 205 GLU A OE2 1 
ATOM   1718 N  N   . CYS A 1 205 ? -3.549  7.046   24.288  1.00   7.83  ? 206 CYS A N   1 
ATOM   1719 C  CA  . CYS A 1 205 ? -4.593  8.035   24.082  1.00   8.02  ? 206 CYS A CA  1 
ATOM   1720 C  C   . CYS A 1 205 ? -5.982  7.400   23.982  1.00   6.99  ? 206 CYS A C   1 
ATOM   1721 O  O   . CYS A 1 205 ? -6.915  8.135   23.635  1.00   8.85  ? 206 CYS A O   1 
ATOM   1722 C  CB  . CYS A 1 205 ? -4.334  8.874   22.849  1.00   8.69  ? 206 CYS A CB  1 
ATOM   1723 S  SG  . CYS A 1 205 ? -4.270  7.892   21.302  1.00   9.29  ? 206 CYS A SG  1 
ATOM   1724 N  N   . VAL A 1 206 ? -6.114  6.124   24.260  1.00   6.97  ? 207 VAL A N   1 
ATOM   1725 C  CA  . VAL A 1 206 ? -7.360  5.411   23.920  1.00   6.72  ? 207 VAL A CA  1 
ATOM   1726 C  C   . VAL A 1 206 ? -8.110  5.000   25.169  1.00   6.93  ? 207 VAL A C   1 
ATOM   1727 O  O   . VAL A 1 206 ? -7.564  4.324   26.044  1.00   7.87  ? 207 VAL A O   1 
ATOM   1728 C  CB  . VAL A 1 206 ? -7.069  4.179   23.071  1.00   7.21  ? 207 VAL A CB  1 
ATOM   1729 C  CG1 . VAL A 1 206 ? -8.385  3.430   22.713  1.00   7.45  ? 207 VAL A CG1 1 
ATOM   1730 C  CG2 . VAL A 1 206 ? -6.322  4.492   21.764  1.00   7.91  ? 207 VAL A CG2 1 
ATOM   1731 N  N   . THR A 1 207 ? -9.425  5.263   25.201  1.00   6.70  ? 208 THR A N   1 
ATOM   1732 C  CA  . THR A 1 207 ? -10.366 4.536   26.055  1.00   7.36  ? 208 THR A CA  1 
ATOM   1733 C  C   . THR A 1 207 ? -10.871 3.377   25.224  1.00   6.47  ? 208 THR A C   1 
ATOM   1734 O  O   . THR A 1 207 ? -11.575 3.573   24.207  1.00   7.39  ? 208 THR A O   1 
ATOM   1735 C  CB  . THR A 1 207 ? -11.541 5.411   26.518  1.00   7.92  ? 208 THR A CB  1 
ATOM   1736 O  OG1 . THR A 1 207 ? -11.026 6.539   27.239  1.00   8.34  ? 208 THR A OG1 1 
ATOM   1737 C  CG2 . THR A 1 207 ? -12.465 4.612   27.410  1.00   9.10  ? 208 THR A CG2 1 
ATOM   1738 N  N   . TRP A 1 208 ? -10.501 2.164   25.623  1.00   6.41  ? 209 TRP A N   1 
ATOM   1739 C  CA  . TRP A 1 208 ? -10.918 0.962   24.914  1.00   6.29  ? 209 TRP A CA  1 
ATOM   1740 C  C   . TRP A 1 208 ? -12.314 0.547   25.443  1.00   6.21  ? 209 TRP A C   1 
ATOM   1741 O  O   . TRP A 1 208 ? -12.538 0.490   26.647  1.00   6.79  ? 209 TRP A O   1 
ATOM   1742 C  CB  . TRP A 1 208 ? -9.924  -0.200  25.121  1.00   6.37  ? 209 TRP A CB  1 
ATOM   1743 C  CG  . TRP A 1 208 ? -8.809  -0.090  24.143  1.00   5.85  ? 209 TRP A CG  1 
ATOM   1744 C  CD1 . TRP A 1 208 ? -7.559  0.491   24.321  1.00   6.78  ? 209 TRP A CD1 1 
ATOM   1745 C  CD2 . TRP A 1 208 ? -8.888  -0.490  22.796  1.00   6.28  ? 209 TRP A CD2 1 
ATOM   1746 N  NE1 . TRP A 1 208 ? -6.905  0.493   23.141  1.00   7.14  ? 209 TRP A NE1 1 
ATOM   1747 C  CE2 . TRP A 1 208 ? -7.660  -0.114  22.175  1.00   6.87  ? 209 TRP A CE2 1 
ATOM   1748 C  CE3 . TRP A 1 208 ? -9.844  -1.122  22.009  1.00   6.41  ? 209 TRP A CE3 1 
ATOM   1749 C  CZ2 . TRP A 1 208 ? -7.382  -0.339  20.829  1.00   7.81  ? 209 TRP A CZ2 1 
ATOM   1750 C  CZ3 . TRP A 1 208 ? -9.592  -1.379  20.707  1.00   7.75  ? 209 TRP A CZ3 1 
ATOM   1751 C  CH2 . TRP A 1 208 ? -8.372  -1.007  20.106  1.00   7.82  ? 209 TRP A CH2 1 
ATOM   1752 N  N   . ILE A 1 209 ? -13.184 0.164   24.504  1.00   6.45  ? 210 ILE A N   1 
ATOM   1753 C  CA  . ILE A 1 209 ? -14.508 -0.356  24.792  1.00   6.34  ? 210 ILE A CA  1 
ATOM   1754 C  C   . ILE A 1 209 ? -14.616 -1.618  23.998  1.00   6.05  ? 210 ILE A C   1 
ATOM   1755 O  O   . ILE A 1 209 ? -14.708 -1.546  22.747  1.00   7.47  ? 210 ILE A O   1 
ATOM   1756 C  CB  . ILE A 1 209 ? -15.607 0.662   24.460  1.00   7.36  ? 210 ILE A CB  1 
ATOM   1757 C  CG1 . ILE A 1 209 ? -15.388 1.957   25.246  1.00   8.76  ? 210 ILE A CG1 1 
ATOM   1758 C  CG2 . ILE A 1 209 ? -16.975 0.059   24.664  1.00   8.57  ? 210 ILE A CG2 1 
ATOM   1759 C  CD1 . ILE A 1 209 ? -16.226 3.117   24.788  1.00   10.45 ? 210 ILE A CD1 1 
ATOM   1760 N  N   . VAL A 1 210 ? -14.552 -2.787  24.614  1.00   6.47  ? 211 VAL A N   1 
ATOM   1761 C  CA  . VAL A 1 210 ? -14.508 -4.066  23.926  1.00   6.39  ? 211 VAL A CA  1 
ATOM   1762 C  C   . VAL A 1 210 ? -15.810 -4.775  24.180  1.00   6.53  ? 211 VAL A C   1 
ATOM   1763 O  O   . VAL A 1 210 ? -16.161 -5.061  25.320  1.00   7.37  ? 211 VAL A O   1 
ATOM   1764 C  CB  . VAL A 1 210 ? -13.307 -4.907  24.369  1.00   7.29  ? 211 VAL A CB  1 
ATOM   1765 C  CG1 . VAL A 1 210 ? -13.341 -6.274  23.688  1.00   8.25  ? 211 VAL A CG1 1 
ATOM   1766 C  CG2 . VAL A 1 210 ? -12.008 -4.157  24.098  1.00   8.79  ? 211 VAL A CG2 1 
ATOM   1767 N  N   . LEU A 1 211 ? -16.574 -5.037  23.127  1.00   7.52  ? 212 LEU A N   1 
ATOM   1768 C  CA  . LEU A 1 211 ? -17.886 -5.726  23.283  1.00   7.98  ? 212 LEU A CA  1 
ATOM   1769 C  C   . LEU A 1 211 ? -17.695 -7.172  23.637  1.00   7.67  ? 212 LEU A C   1 
ATOM   1770 O  O   . LEU A 1 211 ? -16.839 -7.864  23.102  1.00   8.27  ? 212 LEU A O   1 
ATOM   1771 C  CB  . LEU A 1 211 ? -18.714 -5.576  22.002  1.00   8.26  ? 212 LEU A CB  1 
ATOM   1772 C  CG  . LEU A 1 211 ? -19.077 -4.168  21.614  1.00   8.98  ? 212 LEU A CG  1 
ATOM   1773 C  CD1 . LEU A 1 211 ? -20.138 -4.214  20.483  1.00   11.18 ? 212 LEU A CD1 1 
ATOM   1774 C  CD2 . LEU A 1 211 ? -19.638 -3.348  22.760  1.00   10.46 ? 212 LEU A CD2 1 
ATOM   1775 N  N   . LYS A 1 212 ? -18.549 -7.642  24.556  1.00   8.42  ? 213 LYS A N   1 
ATOM   1776 C  CA  . LYS A 1 212 ? -18.480 -9.052  24.916  1.00   8.79  ? 213 LYS A CA  1 
ATOM   1777 C  C   . LYS A 1 212 ? -18.983 -9.976  23.837  1.00   8.13  ? 213 LYS A C   1 
ATOM   1778 O  O   . LYS A 1 212 ? -18.456 -11.084 23.685  1.00   10.31 ? 213 LYS A O   1 
ATOM   1779 C  CB  . LYS A 1 212 ? -19.270 -9.269  26.222  1.00   10.51 ? 213 LYS A CB  1 
ATOM   1780 C  CG  . LYS A 1 212 ? -19.365 -10.739 26.633  1.00   12.91 ? 213 LYS A CG  1 
ATOM   1781 C  CD  . LYS A 1 212 ? -19.945 -10.946 27.994  1.00   19.00 ? 213 LYS A CD  1 
ATOM   1782 C  CE  . LYS A 1 212 ? -20.499 -12.305 28.348  1.00   25.96 ? 213 LYS A CE  1 
ATOM   1783 N  NZ  . LYS A 1 212 ? -21.232 -12.198 29.650  1.00   36.85 ? 213 LYS A NZ  1 
ATOM   1784 N  N   . GLU A 1 213 ? -20.023 -9.600  23.101  1.00   7.98  ? 214 GLU A N   1 
ATOM   1785 C  CA  . GLU A 1 213 ? -20.616 -10.487 22.102  1.00   8.84  ? 214 GLU A CA  1 
ATOM   1786 C  C   . GLU A 1 213 ? -19.868 -10.381 20.814  1.00   7.89  ? 214 GLU A C   1 
ATOM   1787 O  O   . GLU A 1 213 ? -19.797 -9.290  20.242  1.00   8.33  ? 214 GLU A O   1 
ATOM   1788 C  CB  . GLU A 1 213 ? -22.077 -10.135 21.908  1.00   9.30  ? 214 GLU A CB  1 
ATOM   1789 C  CG  . GLU A 1 213 ? -22.732 -11.077 20.913  1.00   12.12 ? 214 GLU A CG  1 
ATOM   1790 C  CD  . GLU A 1 213 ? -24.233 -10.937 20.786  1.00   14.11 ? 214 GLU A CD  1 
ATOM   1791 O  OE1 . GLU A 1 213 ? -24.805 -9.963  21.315  1.00   13.98 ? 214 GLU A OE1 1 
ATOM   1792 O  OE2 . GLU A 1 213 ? -24.835 -11.817 20.134  1.00   24.90 ? 214 GLU A OE2 1 
ATOM   1793 N  N   . PRO A 1 214 ? -19.322 -11.497 20.306  1.00   8.49  ? 215 PRO A N   1 
ATOM   1794 C  CA  . PRO A 1 214 ? -18.654 -11.426 18.985  1.00   9.21  ? 215 PRO A CA  1 
ATOM   1795 C  C   . PRO A 1 214 ? -19.686 -11.399 17.878  1.00   8.81  ? 215 PRO A C   1 
ATOM   1796 O  O   . PRO A 1 214 ? -20.856 -11.791 18.067  1.00   10.88 ? 215 PRO A O   1 
ATOM   1797 C  CB  . PRO A 1 214 ? -17.925 -12.758 18.897  1.00   9.63  ? 215 PRO A CB  1 
ATOM   1798 C  CG  . PRO A 1 214 ? -18.762 -13.725 19.707  1.00   14.72 ? 215 PRO A CG  1 
ATOM   1799 C  CD  . PRO A 1 214 ? -19.270 -12.849 20.856  1.00   10.13 ? 215 PRO A CD  1 
ATOM   1800 N  N   . ILE A 1 215 ? -19.293 -10.958 16.696  1.00   9.13  ? 216 ILE A N   1 
ATOM   1801 C  CA  . ILE A 1 215 ? -20.075 -11.168 15.470  1.00   9.10  ? 216 ILE A CA  1 
ATOM   1802 C  C   . ILE A 1 215 ? -19.564 -12.399 14.781  1.00   8.61  ? 216 ILE A C   1 
ATOM   1803 O  O   . ILE A 1 215 ? -18.364 -12.768 14.915  1.00   10.22 ? 216 ILE A O   1 
ATOM   1804 C  CB  . ILE A 1 215 ? -20.074 -9.942  14.583  1.00   9.43  ? 216 ILE A CB  1 
ATOM   1805 C  CG1 . ILE A 1 215 ? -18.701 -9.593  14.066  1.00   10.70 ? 216 ILE A CG1 1 
ATOM   1806 C  CG2 . ILE A 1 215 ? -20.766 -8.751  15.246  1.00   11.23 ? 216 ILE A CG2 1 
ATOM   1807 C  CD1 . ILE A 1 215 ? -18.655 -8.554  12.919  1.00   12.48 ? 216 ILE A CD1 1 
ATOM   1808 N  N   A SER A 1 216 ? -20.435 -13.182 14.165  0.50   8.71  ? 217 SER A N   1 
ATOM   1809 N  N   B SER A 1 216 ? -20.442 -12.956 13.945  0.50   9.82  ? 217 SER A N   1 
ATOM   1810 C  CA  A SER A 1 216 ? -19.938 -14.262 13.290  0.50   9.14  ? 217 SER A CA  1 
ATOM   1811 C  CA  B SER A 1 216 ? -20.186 -14.142 13.148  0.50   10.54 ? 217 SER A CA  1 
ATOM   1812 C  C   A SER A 1 216 ? -19.852 -13.812 11.876  0.50   9.61  ? 217 SER A C   1 
ATOM   1813 C  C   B SER A 1 216 ? -19.848 -13.739 11.721  0.50   10.67 ? 217 SER A C   1 
ATOM   1814 O  O   A SER A 1 216 ? -20.821 -13.128 11.404  0.50   9.11  ? 217 SER A O   1 
ATOM   1815 O  O   B SER A 1 216 ? -20.535 -12.952 11.087  0.50   10.64 ? 217 SER A O   1 
ATOM   1816 C  CB  A SER A 1 216 ? -20.978 -15.379 13.234  0.50   11.28 ? 217 SER A CB  1 
ATOM   1817 C  CB  B SER A 1 216 ? -21.422 -15.127 13.170  0.50   12.46 ? 217 SER A CB  1 
ATOM   1818 O  OG  A SER A 1 216 ? -21.194 -15.925 14.468  0.50   11.69 ? 217 SER A OG  1 
ATOM   1819 O  OG  B SER A 1 216 ? -20.976 -16.366 12.640  0.50   17.70 ? 217 SER A OG  1 
ATOM   1820 N  N   . VAL A 1 217 ? -18.749 -14.225 11.213  1.00   9.92  ? 218 VAL A N   1 
ATOM   1821 C  CA  . VAL A 1 217 ? -18.493 -14.040 9.787   1.00   10.51 ? 218 VAL A CA  1 
ATOM   1822 C  C   . VAL A 1 217 ? -18.246 -15.388 9.181   1.00   9.84  ? 218 VAL A C   1 
ATOM   1823 O  O   . VAL A 1 217 ? -17.902 -16.336 9.900   1.00   10.66 ? 218 VAL A O   1 
ATOM   1824 C  CB  . VAL A 1 217 ? -17.269 -13.107 9.557   1.00   10.90 ? 218 VAL A CB  1 
ATOM   1825 C  CG1 . VAL A 1 217 ? -17.549 -11.765 10.205  1.00   12.09 ? 218 VAL A CG1 1 
ATOM   1826 C  CG2 . VAL A 1 217 ? -15.969 -13.718 10.016  1.00   12.54 ? 218 VAL A CG2 1 
ATOM   1827 N  N   . SER A 1 218 ? -18.360 -15.552 7.868   1.00   10.49 ? 219 SER A N   1 
ATOM   1828 C  CA  . SER A 1 218 ? -18.145 -16.888 7.326   1.00   10.84 ? 219 SER A CA  1 
ATOM   1829 C  C   . SER A 1 218 ? -16.684 -17.136 7.043   1.00   10.76 ? 219 SER A C   1 
ATOM   1830 O  O   . SER A 1 218 ? -15.871 -16.200 6.912   1.00   11.05 ? 219 SER A O   1 
ATOM   1831 C  CB  . SER A 1 218 ? -18.929 -17.067 6.037   1.00   11.30 ? 219 SER A CB  1 
ATOM   1832 O  OG  . SER A 1 218 ? -18.457 -16.210 5.047   1.00   12.34 ? 219 SER A OG  1 
ATOM   1833 N  N   A SER A 1 219 ? -16.314 -18.408 6.805   0.50   11.13 ? 220 SER A N   1 
ATOM   1834 N  N   B SER A 1 219 ? -16.412 -18.414 6.992   0.50   11.43 ? 220 SER A N   1 
ATOM   1835 C  CA  A SER A 1 219 ? -14.913 -18.760 6.449   0.50   12.72 ? 220 SER A CA  1 
ATOM   1836 C  CA  B SER A 1 219 ? -15.096 -18.763 6.645   0.50   11.55 ? 220 SER A CA  1 
ATOM   1837 C  C   A SER A 1 219 ? -14.566 -18.088 5.140   0.50   13.29 ? 220 SER A C   1 
ATOM   1838 C  C   B SER A 1 219 ? -14.662 -18.098 5.323   0.50   12.46 ? 220 SER A C   1 
ATOM   1839 O  O   A SER A 1 219 ? -13.449 -17.639 4.857   0.50   13.88 ? 220 SER A O   1 
ATOM   1840 O  O   B SER A 1 219 ? -13.494 -17.657 5.265   0.50   12.74 ? 220 SER A O   1 
ATOM   1841 C  CB  A SER A 1 219 ? -14.786 -20.290 6.314   0.50   14.07 ? 220 SER A CB  1 
ATOM   1842 C  CB  B SER A 1 219 ? -14.956 -20.276 6.634   0.50   13.74 ? 220 SER A CB  1 
ATOM   1843 O  OG  A SER A 1 219 ? -15.828 -20.922 5.566   0.50   17.53 ? 220 SER A OG  1 
ATOM   1844 O  OG  B SER A 1 219 ? -13.630 -20.625 6.257   0.50   13.43 ? 220 SER A OG  1 
ATOM   1845 N  N   . GLU A 1 220 ? -15.541 -18.017 4.289   1.00   12.05 ? 221 GLU A N   1 
ATOM   1846 C  CA  . GLU A 1 220 ? -15.262 -17.407 3.029   1.00   13.80 ? 221 GLU A CA  1 
ATOM   1847 C  C   . GLU A 1 220 ? -14.950 -15.910 3.142   1.00   12.68 ? 221 GLU A C   1 
ATOM   1848 O  O   . GLU A 1 220 ? -14.091 -15.361 2.403   1.00   13.86 ? 221 GLU A O   1 
ATOM   1849 C  CB  . GLU A 1 220 ? -16.372 -17.592 2.031   1.00   16.61 ? 221 GLU A CB  1 
ATOM   1850 C  CG  . GLU A 1 220 ? -16.598 -19.079 1.613   1.00   20.40 ? 221 GLU A CG  1 
ATOM   1851 C  CD  . GLU A 1 220 ? -17.483 -19.867 2.578   1.00   23.34 ? 221 GLU A CD  1 
ATOM   1852 O  OE1 . GLU A 1 220 ? -17.973 -19.378 3.595   1.00   22.14 ? 221 GLU A OE1 1 
ATOM   1853 O  OE2 . GLU A 1 220 ? -17.818 -21.031 2.286   1.00   34.67 ? 221 GLU A OE2 1 
ATOM   1854 N  N   . GLN A 1 221 ? -15.665 -15.236 4.038   1.00   11.10 ? 222 GLN A N   1 
ATOM   1855 C  CA  . GLN A 1 221 ? -15.414 -13.808 4.262   1.00   11.59 ? 222 GLN A CA  1 
ATOM   1856 C  C   . GLN A 1 221 ? -13.987 -13.586 4.800   1.00   11.37 ? 222 GLN A C   1 
ATOM   1857 O  O   . GLN A 1 221 ? -13.240 -12.757 4.275   1.00   12.28 ? 222 GLN A O   1 
ATOM   1858 C  CB  . GLN A 1 221 ? -16.479 -13.209 5.165   1.00   10.97 ? 222 GLN A CB  1 
ATOM   1859 C  CG  . GLN A 1 221 ? -17.812 -13.102 4.480   1.00   11.66 ? 222 GLN A CG  1 
ATOM   1860 C  CD  . GLN A 1 221 ? -18.945 -12.567 5.318   1.00   10.92 ? 222 GLN A CD  1 
ATOM   1861 O  OE1 . GLN A 1 221 ? -19.094 -12.932 6.524   1.00   10.72 ? 222 GLN A OE1 1 
ATOM   1862 N  NE2 . GLN A 1 221 ? -19.735 -11.683 4.731   1.00   11.66 ? 222 GLN A NE2 1 
ATOM   1863 N  N   A VAL A 1 222 ? -13.508 -14.393 5.763   0.50   11.58 ? 223 VAL A N   1 
ATOM   1864 N  N   B VAL A 1 222 ? -13.666 -14.306 5.870   0.50   11.58 ? 223 VAL A N   1 
ATOM   1865 C  CA  A VAL A 1 222 ? -12.154 -14.133 6.315   0.50   12.38 ? 223 VAL A CA  1 
ATOM   1866 C  CA  B VAL A 1 222 ? -12.358 -14.111 6.434   0.50   11.97 ? 223 VAL A CA  1 
ATOM   1867 C  C   A VAL A 1 222 ? -11.107 -14.581 5.349   0.50   12.25 ? 223 VAL A C   1 
ATOM   1868 C  C   B VAL A 1 222 ? -11.245 -14.563 5.448   0.50   11.93 ? 223 VAL A C   1 
ATOM   1869 O  O   A VAL A 1 222 ? -9.988  -14.029 5.266   0.50   11.39 ? 223 VAL A O   1 
ATOM   1870 O  O   B VAL A 1 222 ? -10.200 -13.903 5.441   0.50   12.24 ? 223 VAL A O   1 
ATOM   1871 C  CB  A VAL A 1 222 ? -11.875 -14.828 7.651   0.50   14.00 ? 223 VAL A CB  1 
ATOM   1872 C  CB  B VAL A 1 222 ? -12.256 -14.629 7.889   0.50   10.17 ? 223 VAL A CB  1 
ATOM   1873 C  CG1 A VAL A 1 222 ? -10.519 -14.360 8.206   0.50   14.00 ? 223 VAL A CG1 1 
ATOM   1874 C  CG1 B VAL A 1 222 ? -12.147 -16.124 7.865   0.50   11.08 ? 223 VAL A CG1 1 
ATOM   1875 C  CG2 A VAL A 1 222 ? -12.890 -14.407 8.657   0.50   16.06 ? 223 VAL A CG2 1 
ATOM   1876 C  CG2 B VAL A 1 222 ? -11.033 -14.030 8.638   0.50   12.03 ? 223 VAL A CG2 1 
ATOM   1877 N  N   . LEU A 1 223 ? -11.460 -15.610 4.613   1.00   12.90 ? 224 LEU A N   1 
ATOM   1878 C  CA  . LEU A 1 223 ? -10.525 -16.034 3.627   1.00   13.92 ? 224 LEU A CA  1 
ATOM   1879 C  C   . LEU A 1 223 ? -10.189 -14.890 2.650   1.00   13.20 ? 224 LEU A C   1 
ATOM   1880 O  O   . LEU A 1 223 ? -9.024  -14.780 2.222   1.00   14.58 ? 224 LEU A O   1 
ATOM   1881 C  CB  . LEU A 1 223 ? -10.991 -17.291 2.953   1.00   17.35 ? 224 LEU A CB  1 
ATOM   1882 C  CG  . LEU A 1 223 ? -10.772 -18.598 3.743   1.00   18.28 ? 224 LEU A CG  1 
ATOM   1883 C  CD1 . LEU A 1 223 ? -11.664 -19.716 3.250   1.00   23.71 ? 224 LEU A CD1 1 
ATOM   1884 C  CD2 . LEU A 1 223 ? -9.288  -18.998 3.739   1.00   22.72 ? 224 LEU A CD2 1 
ATOM   1885 N  N   . LYS A 1 224 ? -11.160 -14.046 2.348   1.00   13.04 ? 225 LYS A N   1 
ATOM   1886 C  CA  . LYS A 1 224 ? -10.898 -12.928 1.464   1.00   13.70 ? 225 LYS A CA  1 
ATOM   1887 C  C   . LYS A 1 224 ? -10.061 -11.864 2.129   1.00   11.96 ? 225 LYS A C   1 
ATOM   1888 O  O   . LYS A 1 224 ? -9.272  -11.252 1.442   1.00   12.60 ? 225 LYS A O   1 
ATOM   1889 C  CB  . LYS A 1 224 ? -12.207 -12.430 0.836   1.00   16.16 ? 225 LYS A CB  1 
ATOM   1890 C  CG  . LYS A 1 224 ? -12.684 -13.472 -0.244  1.00   20.77 ? 225 LYS A CG  1 
ATOM   1891 C  CD  . LYS A 1 224 ? -14.030 -13.178 -0.895  1.00   23.62 ? 225 LYS A CD  1 
ATOM   1892 C  CE  . LYS A 1 224 ? -14.513 -14.245 -1.936  1.00   28.02 ? 225 LYS A CE  1 
ATOM   1893 N  NZ  . LYS A 1 224 ? -15.847 -13.944 -2.636  1.00   27.02 ? 225 LYS A NZ  1 
ATOM   1894 N  N   . PHE A 1 225 ? -10.158 -11.653 3.440   1.00   11.39 ? 226 PHE A N   1 
ATOM   1895 C  CA  . PHE A 1 225 ? -9.259  -10.753 4.105   1.00   11.07 ? 226 PHE A CA  1 
ATOM   1896 C  C   . PHE A 1 225 ? -7.794  -11.245 3.899   1.00   10.39 ? 226 PHE A C   1 
ATOM   1897 O  O   . PHE A 1 225 ? -6.889  -10.484 3.699   1.00   11.03 ? 226 PHE A O   1 
ATOM   1898 C  CB  . PHE A 1 225 ? -9.438  -10.737 5.605   1.00   11.33 ? 226 PHE A CB  1 
ATOM   1899 C  CG  . PHE A 1 225 ? -10.644 -9.993  6.147   1.00   11.01 ? 226 PHE A CG  1 
ATOM   1900 C  CD1 . PHE A 1 225 ? -11.699 -9.538  5.357   1.00   14.50 ? 226 PHE A CD1 1 
ATOM   1901 C  CD2 . PHE A 1 225 ? -10.724 -9.773  7.522   1.00   14.15 ? 226 PHE A CD2 1 
ATOM   1902 C  CE1 . PHE A 1 225 ? -12.776 -8.875  5.948   1.00   15.52 ? 226 PHE A CE1 1 
ATOM   1903 C  CE2 . PHE A 1 225 ? -11.794 -9.115  8.101   1.00   15.48 ? 226 PHE A CE2 1 
ATOM   1904 C  CZ  . PHE A 1 225 ? -12.827 -8.672  7.312   1.00   14.55 ? 226 PHE A CZ  1 
ATOM   1905 N  N   . ARG A 1 226 ? -7.627  -12.583 3.953   1.00   10.71 ? 227 ARG A N   1 
ATOM   1906 C  CA  . ARG A 1 226 ? -6.338  -13.164 3.916   1.00   11.01 ? 227 ARG A CA  1 
ATOM   1907 C  C   . ARG A 1 226 ? -5.723  -13.198 2.500   1.00   11.46 ? 227 ARG A C   1 
ATOM   1908 O  O   . ARG A 1 226 ? -4.547  -13.612 2.375   1.00   12.60 ? 227 ARG A O   1 
ATOM   1909 C  CB  . ARG A 1 226 ? -6.353  -14.612 4.456   1.00   11.12 ? 227 ARG A CB  1 
ATOM   1910 C  CG  . ARG A 1 226 ? -6.852  -14.706 5.896   1.00   10.76 ? 227 ARG A CG  1 
ATOM   1911 C  CD  . ARG A 1 226 ? -6.778  -16.152 6.367   1.00   13.54 ? 227 ARG A CD  1 
ATOM   1912 N  NE  . ARG A 1 226 ? -7.342  -16.319 7.669   1.00   12.02 ? 227 ARG A NE  1 
ATOM   1913 C  CZ  . ARG A 1 226 ? -8.290  -17.173 8.030   1.00   11.90 ? 227 ARG A CZ  1 
ATOM   1914 N  NH1 . ARG A 1 226 ? -8.763  -18.075 7.180   1.00   15.33 ? 227 ARG A NH1 1 
ATOM   1915 N  NH2 . ARG A 1 226 ? -8.801  -17.162 9.245   1.00   12.86 ? 227 ARG A NH2 1 
ATOM   1916 N  N   . LYS A 1 227 ? -6.429  -12.746 1.473   1.00   10.59 ? 228 LYS A N   1 
ATOM   1917 C  CA  . LYS A 1 227 ? -5.889  -12.613 0.119   1.00   12.31 ? 228 LYS A CA  1 
ATOM   1918 C  C   . LYS A 1 227 ? -5.285  -11.245 -0.099  1.00   11.46 ? 228 LYS A C   1 
ATOM   1919 O  O   . LYS A 1 227 ? -4.656  -11.032 -1.135  1.00   13.49 ? 228 LYS A O   1 
ATOM   1920 C  CB  . LYS A 1 227 ? -7.001  -12.880 -0.898  1.00   14.03 ? 228 LYS A CB  1 
ATOM   1921 C  CG  . LYS A 1 227 ? -7.462  -14.297 -0.900  1.00   16.33 ? 228 LYS A CG  1 
ATOM   1922 C  CD  . LYS A 1 227 ? -8.529  -14.553 -1.964  1.00   27.39 ? 228 LYS A CD  1 
ATOM   1923 C  CE  . LYS A 1 227 ? -8.002  -15.439 -3.097  0.0000 43.96 ? 228 LYS A CE  1 
ATOM   1924 N  NZ  . LYS A 1 227 ? -8.368  -14.992 -4.467  0.0000 49.59 ? 228 LYS A NZ  1 
ATOM   1925 N  N   . LEU A 1 228 ? -5.514  -10.294 0.826   1.00   10.88 ? 229 LEU A N   1 
ATOM   1926 C  CA  . LEU A 1 228 ? -4.899  -8.992  0.713   1.00   10.91 ? 229 LEU A CA  1 
ATOM   1927 C  C   . LEU A 1 228 ? -3.418  -9.153  0.834   1.00   10.49 ? 229 LEU A C   1 
ATOM   1928 O  O   . LEU A 1 228 ? -2.869  -10.204 1.266   1.00   11.00 ? 229 LEU A O   1 
ATOM   1929 C  CB  . LEU A 1 228 ? -5.410  -8.051  1.813   1.00   11.00 ? 229 LEU A CB  1 
ATOM   1930 C  CG  . LEU A 1 228 ? -6.805  -7.589  1.599   1.00   11.23 ? 229 LEU A CG  1 
ATOM   1931 C  CD1 . LEU A 1 228 ? -7.366  -7.012  2.862   1.00   12.11 ? 229 LEU A CD1 1 
ATOM   1932 C  CD2 . LEU A 1 228 ? -6.889  -6.541  0.450   1.00   13.21 ? 229 LEU A CD2 1 
ATOM   1933 N  N   . ASN A 1 229 ? -2.660  -8.105  0.421   1.00   10.92 ? 230 ASN A N   1 
ATOM   1934 C  CA  . ASN A 1 229 ? -1.225  -8.139  0.483   1.00   10.72 ? 230 ASN A CA  1 
ATOM   1935 C  C   . ASN A 1 229 ? -0.660  -6.925  1.321   1.00   10.59 ? 230 ASN A C   1 
ATOM   1936 O  O   . ASN A 1 229 ? -1.147  -5.818  1.253   1.00   11.86 ? 230 ASN A O   1 
ATOM   1937 C  CB  . ASN A 1 229 ? -0.601  -7.946  -0.931  1.00   12.72 ? 230 ASN A CB  1 
ATOM   1938 C  CG  . ASN A 1 229 ? -0.686  -9.114  -1.849  1.00   13.86 ? 230 ASN A CG  1 
ATOM   1939 O  OD1 . ASN A 1 229 ? -0.190  -8.960  -3.004  1.00   16.06 ? 230 ASN A OD1 1 
ATOM   1940 N  ND2 . ASN A 1 229 ? -1.270  -10.265 -1.466  1.00   14.30 ? 230 ASN A ND2 1 
ATOM   1941 N  N   . PHE A 1 230 ? 0.384   -7.258  2.078   1.00   10.83 ? 231 PHE A N   1 
ATOM   1942 C  CA  . PHE A 1 230 ? 1.133   -6.184  2.768   1.00   11.36 ? 231 PHE A CA  1 
ATOM   1943 C  C   . PHE A 1 230 ? 1.989   -5.393  1.780   1.00   13.43 ? 231 PHE A C   1 
ATOM   1944 O  O   . PHE A 1 230 ? 2.244   -4.188  2.040   1.00   13.27 ? 231 PHE A O   1 
ATOM   1945 C  CB  . PHE A 1 230 ? 2.101   -6.781  3.752   1.00   11.69 ? 231 PHE A CB  1 
ATOM   1946 C  CG  . PHE A 1 230 ? 1.548   -7.389  5.015   1.00   10.70 ? 231 PHE A CG  1 
ATOM   1947 C  CD1 . PHE A 1 230 ? 0.746   -6.599  5.907   1.00   11.07 ? 231 PHE A CD1 1 
ATOM   1948 C  CD2 . PHE A 1 230 ? 1.931   -8.662  5.425   1.00   11.30 ? 231 PHE A CD2 1 
ATOM   1949 C  CE1 . PHE A 1 230 ? 0.306   -7.146  7.111   1.00   11.35 ? 231 PHE A CE1 1 
ATOM   1950 C  CE2 . PHE A 1 230 ? 1.471   -9.169  6.643   1.00   12.18 ? 231 PHE A CE2 1 
ATOM   1951 C  CZ  . PHE A 1 230 ? 0.691   -8.415  7.510   1.00   11.25 ? 231 PHE A CZ  1 
ATOM   1952 N  N   . ASN A 1 231 ? 2.466   -6.008  0.733   1.00   12.23 ? 232 ASN A N   1 
ATOM   1953 C  CA  . ASN A 1 231 ? 3.377   -5.391  -0.283  1.00   13.79 ? 232 ASN A CA  1 
ATOM   1954 C  C   . ASN A 1 231 ? 2.569   -4.523  -1.198  1.00   12.46 ? 232 ASN A C   1 
ATOM   1955 O  O   . ASN A 1 231 ? 1.358   -4.609  -1.390  1.00   13.36 ? 232 ASN A O   1 
ATOM   1956 C  CB  . ASN A 1 231 ? 4.033   -6.523  -1.074  1.00   15.38 ? 232 ASN A CB  1 
ATOM   1957 C  CG  . ASN A 1 231 ? 3.013   -7.393  -1.673  1.00   14.38 ? 232 ASN A CG  1 
ATOM   1958 O  OD1 . ASN A 1 231 ? 2.475   -8.285  -0.991  1.00   15.52 ? 232 ASN A OD1 1 
ATOM   1959 N  ND2 . ASN A 1 231 ? 2.772   -7.250  -2.987  1.00   17.07 ? 232 ASN A ND2 1 
ATOM   1960 N  N   . GLY A 1 232 ? 3.346   -3.672  -1.890  1.00   14.87 ? 233 GLY A N   1 
ATOM   1961 C  CA  . GLY A 1 232 ? 2.856   -2.860  -2.996  1.00   15.18 ? 233 GLY A CA  1 
ATOM   1962 C  C   . GLY A 1 232 ? 2.816   -3.649  -4.288  1.00   14.62 ? 233 GLY A C   1 
ATOM   1963 O  O   . GLY A 1 232 ? 3.447   -4.695  -4.400  1.00   17.80 ? 233 GLY A O   1 
ATOM   1964 N  N   . GLU A 1 233 ? 2.080   -3.118  -5.258  1.00   15.31 ? 234 GLU A N   1 
ATOM   1965 C  CA  . GLU A 1 233 ? 1.985   -3.723  -6.582  1.00   15.67 ? 234 GLU A CA  1 
ATOM   1966 C  C   . GLU A 1 233 ? 3.387   -3.873  -7.169  1.00   18.58 ? 234 GLU A C   1 
ATOM   1967 O  O   . GLU A 1 233 ? 4.203   -2.981  -7.024  1.00   18.74 ? 234 GLU A O   1 
ATOM   1968 C  CB  . GLU A 1 233 ? 1.165   -2.844  -7.493  1.00   16.85 ? 234 GLU A CB  1 
ATOM   1969 C  CG  . GLU A 1 233 ? 0.877   -3.419  -8.853  1.00   19.56 ? 234 GLU A CG  1 
ATOM   1970 C  CD  . GLU A 1 233 ? 0.119   -2.447  -9.731  1.00   24.07 ? 234 GLU A CD  1 
ATOM   1971 O  OE1 . GLU A 1 233 ? -0.179  -1.331  -9.258  1.00   24.15 ? 234 GLU A OE1 1 
ATOM   1972 O  OE2 . GLU A 1 233 ? -0.176  -2.795  -10.892 1.00   25.43 ? 234 GLU A OE2 1 
ATOM   1973 N  N   . GLY A 1 234 ? 3.648   -4.986  -7.849  1.00   19.63 ? 235 GLY A N   1 
ATOM   1974 C  CA  . GLY A 1 234 ? 4.965   -5.146  -8.469  1.00   25.08 ? 235 GLY A CA  1 
ATOM   1975 C  C   . GLY A 1 234 ? 6.058   -5.563  -7.490  1.00   26.46 ? 235 GLY A C   1 
ATOM   1976 O  O   . GLY A 1 234 ? 7.262   -5.695  -7.888  1.00   29.54 ? 235 GLY A O   1 
ATOM   1977 N  N   . GLU A 1 235 ? 5.664   -5.886  -6.243  1.00   19.93 ? 236 GLU A N   1 
ATOM   1978 C  CA  . GLU A 1 235 ? 6.650   -6.395  -5.281  1.00   18.59 ? 236 GLU A CA  1 
ATOM   1979 C  C   . GLU A 1 235 ? 6.256   -7.797  -4.912  1.00   21.00 ? 236 GLU A C   1 
ATOM   1980 O  O   . GLU A 1 235 ? 5.116   -8.294  -5.258  1.00   22.95 ? 236 GLU A O   1 
ATOM   1981 C  CB  . GLU A 1 235 ? 6.559   -5.556  -3.978  1.00   19.82 ? 236 GLU A CB  1 
ATOM   1982 C  CG  . GLU A 1 235 ? 7.015   -4.108  -4.133  1.00   21.71 ? 236 GLU A CG  1 
ATOM   1983 C  CD  . GLU A 1 235 ? 6.969   -3.324  -2.837  1.00   31.34 ? 236 GLU A CD  1 
ATOM   1984 O  OE1 . GLU A 1 235 ? 6.229   -3.732  -1.894  1.00   24.79 ? 236 GLU A OE1 1 
ATOM   1985 O  OE2 . GLU A 1 235 ? 7.698   -2.294  -2.791  1.00   36.58 ? 236 GLU A OE2 1 
ATOM   1986 N  N   . PRO A 1 236 ? 7.207   -8.546  -4.312  1.00   22.11 ? 237 PRO A N   1 
ATOM   1987 C  CA  . PRO A 1 236 ? 6.996   -9.949  -4.014  1.00   23.85 ? 237 PRO A CA  1 
ATOM   1988 C  C   . PRO A 1 236 ? 5.772   -10.080 -3.069  1.00   19.21 ? 237 PRO A C   1 
ATOM   1989 O  O   . PRO A 1 236 ? 5.634   -9.291  -2.151  1.00   20.50 ? 237 PRO A O   1 
ATOM   1990 C  CB  . PRO A 1 236 ? 8.289   -10.362 -3.306  1.00   26.52 ? 237 PRO A CB  1 
ATOM   1991 C  CG  . PRO A 1 236 ? 9.350   -9.477  -3.839  1.00   30.32 ? 237 PRO A CG  1 
ATOM   1992 C  CD  . PRO A 1 236 ? 8.619   -8.168  -4.010  1.00   27.54 ? 237 PRO A CD  1 
ATOM   1993 N  N   . GLU A 1 237 ? 4.927   -11.089 -3.313  1.00   19.58 ? 238 GLU A N   1 
ATOM   1994 C  CA  . GLU A 1 237 ? 3.654   -11.162 -2.573  1.00   17.50 ? 238 GLU A CA  1 
ATOM   1995 C  C   . GLU A 1 237 ? 3.886   -11.575 -1.139  1.00   15.78 ? 238 GLU A C   1 
ATOM   1996 O  O   . GLU A 1 237 ? 4.499   -12.612 -0.912  1.00   15.18 ? 238 GLU A O   1 
ATOM   1997 C  CB  . GLU A 1 237 ? 2.677   -12.141 -3.230  1.00   20.52 ? 238 GLU A CB  1 
ATOM   1998 C  CG  . GLU A 1 237 ? 1.316   -12.057 -2.574  1.00   21.46 ? 238 GLU A CG  1 
ATOM   1999 C  CD  . GLU A 1 237 ? 0.205   -12.904 -3.215  1.00   22.04 ? 238 GLU A CD  1 
ATOM   2000 O  OE1 . GLU A 1 237 ? 0.506   -14.030 -3.701  1.00   39.75 ? 238 GLU A OE1 1 
ATOM   2001 O  OE2 . GLU A 1 237 ? -0.980  -12.482 -3.273  1.00   19.54 ? 238 GLU A OE2 1 
ATOM   2002 N  N   . GLU A 1 238 ? 3.342   -10.809 -0.192  1.00   13.71 ? 239 GLU A N   1 
ATOM   2003 C  CA  . GLU A 1 238 ? 3.328   -11.124 1.191   1.00   13.71 ? 239 GLU A CA  1 
ATOM   2004 C  C   . GLU A 1 238 ? 1.904   -11.023 1.650   1.00   12.43 ? 239 GLU A C   1 
ATOM   2005 O  O   . GLU A 1 238 ? 1.337   -9.919  1.705   1.00   14.30 ? 239 GLU A O   1 
ATOM   2006 C  CB  . GLU A 1 238 ? 4.122   -10.072 1.961   1.00   16.65 ? 239 GLU A CB  1 
ATOM   2007 C  CG  . GLU A 1 238 ? 5.535   -9.831  1.596   1.00   20.73 ? 239 GLU A CG  1 
ATOM   2008 C  CD  . GLU A 1 238 ? 6.102   -8.525  2.190   1.00   29.70 ? 239 GLU A CD  1 
ATOM   2009 O  OE1 . GLU A 1 238 ? 5.618   -7.997  3.198   1.00   32.52 ? 239 GLU A OE1 1 
ATOM   2010 O  OE2 . GLU A 1 238 ? 7.068   -8.047  1.611   0.0000 49.56 ? 239 GLU A OE2 1 
ATOM   2011 N  N   . LEU A 1 239 ? 1.277   -12.182 1.968   1.00   11.29 ? 240 LEU A N   1 
ATOM   2012 C  CA  . LEU A 1 239 ? -0.102  -12.093 2.295   1.00   11.20 ? 240 LEU A CA  1 
ATOM   2013 C  C   . LEU A 1 239 ? -0.308  -11.271 3.579   1.00   10.63 ? 240 LEU A C   1 
ATOM   2014 O  O   . LEU A 1 239 ? 0.451   -11.455 4.542   1.00   11.33 ? 240 LEU A O   1 
ATOM   2015 C  CB  . LEU A 1 239 ? -0.649  -13.536 2.501   1.00   11.70 ? 240 LEU A CB  1 
ATOM   2016 C  CG  . LEU A 1 239 ? -0.695  -14.419 1.275   1.00   13.69 ? 240 LEU A CG  1 
ATOM   2017 C  CD1 . LEU A 1 239 ? -1.206  -15.785 1.750   1.00   18.34 ? 240 LEU A CD1 1 
ATOM   2018 C  CD2 . LEU A 1 239 ? -1.514  -13.799 0.178   1.00   15.24 ? 240 LEU A CD2 1 
ATOM   2019 N  N   . MET A 1 240 ? -1.369  -10.491 3.580   1.00   10.23 ? 241 MET A N   1 
ATOM   2020 C  CA  . MET A 1 240 ? -1.739  -9.681  4.768   1.00   10.56 ? 241 MET A CA  1 
ATOM   2021 C  C   . MET A 1 240 ? -2.528  -10.597 5.703   1.00   9.34  ? 241 MET A C   1 
ATOM   2022 O  O   . MET A 1 240 ? -3.697  -10.755 5.610   1.00   9.92  ? 241 MET A O   1 
ATOM   2023 C  CB  . MET A 1 240 ? -2.574  -8.516  4.331   1.00   10.29 ? 241 MET A CB  1 
ATOM   2024 C  CG  . MET A 1 240 ? -2.933  -7.537  5.477   1.00   11.02 ? 241 MET A CG  1 
ATOM   2025 S  SD  . MET A 1 240 ? -3.889  -6.139  4.973   1.00   11.39 ? 241 MET A SD  1 
ATOM   2026 C  CE  . MET A 1 240 ? -2.578  -5.075  4.315   1.00   11.95 ? 241 MET A CE  1 
ATOM   2027 N  N   . VAL A 1 241 ? -1.725  -11.219 6.606   1.00   9.49  ? 242 VAL A N   1 
ATOM   2028 C  CA  . VAL A 1 241 ? -2.262  -12.105 7.667   1.00   9.01  ? 242 VAL A CA  1 
ATOM   2029 C  C   . VAL A 1 241 ? -1.442  -11.876 8.939   1.00   8.65  ? 242 VAL A C   1 
ATOM   2030 O  O   . VAL A 1 241 ? -0.299  -11.435 8.891   1.00   9.32  ? 242 VAL A O   1 
ATOM   2031 C  CB  . VAL A 1 241 ? -2.145  -13.623 7.270   1.00   10.07 ? 242 VAL A CB  1 
ATOM   2032 C  CG1 . VAL A 1 241 ? -3.067  -13.932 6.103   1.00   12.13 ? 242 VAL A CG1 1 
ATOM   2033 C  CG2 . VAL A 1 241 ? -0.706  -14.034 7.044   1.00   11.60 ? 242 VAL A CG2 1 
ATOM   2034 N  N   . ASP A 1 242 ? -2.071  -12.199 10.099  1.00   8.20  ? 243 ASP A N   1 
ATOM   2035 C  CA  . ASP A 1 242 ? -1.414  -12.062 11.371  1.00   8.29  ? 243 ASP A CA  1 
ATOM   2036 C  C   . ASP A 1 242 ? -0.943  -10.623 11.631  1.00   8.25  ? 243 ASP A C   1 
ATOM   2037 O  O   . ASP A 1 242 ? 0.164   -10.377 12.113  1.00   9.75  ? 243 ASP A O   1 
ATOM   2038 C  CB  . ASP A 1 242 ? -0.329  -13.109 11.625  1.00   8.72  ? 243 ASP A CB  1 
ATOM   2039 C  CG  . ASP A 1 242 ? -0.876  -14.487 11.681  1.00   9.28  ? 243 ASP A CG  1 
ATOM   2040 O  OD1 . ASP A 1 242 ? -1.945  -14.668 12.332  1.00   9.21  ? 243 ASP A OD1 1 
ATOM   2041 O  OD2 . ASP A 1 242 ? -0.302  -15.424 11.065  1.00   11.09 ? 243 ASP A OD2 1 
ATOM   2042 N  N   . ASN A 1 243 ? -1.832  -9.695  11.315  1.00   7.65  ? 244 ASN A N   1 
ATOM   2043 C  CA  . ASN A 1 243 ? -1.568  -8.269  11.547  1.00   7.81  ? 244 ASN A CA  1 
ATOM   2044 C  C   . ASN A 1 243 ? -2.092  -7.824  12.906  1.00   7.33  ? 244 ASN A C   1 
ATOM   2045 O  O   . ASN A 1 243 ? -2.748  -6.769  12.987  1.00   8.95  ? 244 ASN A O   1 
ATOM   2046 C  CB  . ASN A 1 243 ? -2.100  -7.423  10.383  1.00   8.13  ? 244 ASN A CB  1 
ATOM   2047 C  CG  . ASN A 1 243 ? -3.574  -7.571  10.170  1.00   8.54  ? 244 ASN A CG  1 
ATOM   2048 O  OD1 . ASN A 1 243 ? -4.223  -8.450  10.756  1.00   9.03  ? 244 ASN A OD1 1 
ATOM   2049 N  ND2 . ASN A 1 243 ? -4.113  -6.742  9.322   1.00   12.42 ? 244 ASN A ND2 1 
ATOM   2050 N  N   . TRP A 1 244 ? -1.833  -8.596  13.934  1.00   7.29  ? 245 TRP A N   1 
ATOM   2051 C  CA  . TRP A 1 244 ? -2.273  -8.345  15.292  1.00   7.58  ? 245 TRP A CA  1 
ATOM   2052 C  C   . TRP A 1 244 ? -1.078  -8.256  16.217  1.00   7.64  ? 245 TRP A C   1 
ATOM   2053 O  O   . TRP A 1 244 ? -0.078  -8.967  16.085  1.00   8.73  ? 245 TRP A O   1 
ATOM   2054 C  CB  . TRP A 1 244 ? -3.231  -9.449  15.823  1.00   8.06  ? 245 TRP A CB  1 
ATOM   2055 C  CG  . TRP A 1 244 ? -2.765  -10.842 15.642  1.00   7.52  ? 245 TRP A CG  1 
ATOM   2056 C  CD1 . TRP A 1 244 ? -2.868  -11.607 14.482  1.00   7.85  ? 245 TRP A CD1 1 
ATOM   2057 C  CD2 . TRP A 1 244 ? -2.135  -11.684 16.571  1.00   7.71  ? 245 TRP A CD2 1 
ATOM   2058 N  NE1 . TRP A 1 244 ? -2.345  -12.849 14.689  1.00   8.49  ? 245 TRP A NE1 1 
ATOM   2059 C  CE2 . TRP A 1 244 ? -1.896  -12.927 15.959  1.00   8.49  ? 245 TRP A CE2 1 
ATOM   2060 C  CE3 . TRP A 1 244 ? -1.836  -11.526 17.950  1.00   8.78  ? 245 TRP A CE3 1 
ATOM   2061 C  CZ2 . TRP A 1 244 ? -1.313  -13.996 16.642  1.00   9.87  ? 245 TRP A CZ2 1 
ATOM   2062 C  CZ3 . TRP A 1 244 ? -1.298  -12.606 18.628  1.00   10.43 ? 245 TRP A CZ3 1 
ATOM   2063 C  CH2 . TRP A 1 244 ? -1.042  -13.825 17.968  1.00   10.29 ? 245 TRP A CH2 1 
ATOM   2064 N  N   . ARG A 1 245 ? -1.194  -7.370  17.189  1.00   7.70  ? 246 ARG A N   1 
ATOM   2065 C  CA  . ARG A 1 245 ? -0.229  -7.260  18.321  1.00   7.69  ? 246 ARG A CA  1 
ATOM   2066 C  C   . ARG A 1 245 ? -0.677  -8.177  19.427  1.00   7.32  ? 246 ARG A C   1 
ATOM   2067 O  O   . ARG A 1 245 ? -1.861  -8.157  19.757  1.00   8.44  ? 246 ARG A O   1 
ATOM   2068 C  CB  . ARG A 1 245 ? -0.142  -5.789  18.787  1.00   8.12  ? 246 ARG A CB  1 
ATOM   2069 C  CG  . ARG A 1 245 ? 0.965   -5.567  19.784  1.00   8.06  ? 246 ARG A CG  1 
ATOM   2070 C  CD  . ARG A 1 245 ? 0.883   -4.154  20.374  1.00   8.18  ? 246 ARG A CD  1 
ATOM   2071 N  NE  . ARG A 1 245 ? 2.119   -3.862  21.118  1.00   8.49  ? 246 ARG A NE  1 
ATOM   2072 C  CZ  . ARG A 1 245 ? 2.312   -2.822  21.907  1.00   8.13  ? 246 ARG A CZ  1 
ATOM   2073 N  NH1 . ARG A 1 245 ? 1.315   -2.075  22.271  1.00   8.91  ? 246 ARG A NH1 1 
ATOM   2074 N  NH2 . ARG A 1 245 ? 3.548   -2.600  22.375  1.00   10.14 ? 246 ARG A NH2 1 
ATOM   2075 N  N   A PRO A 1 246 ? 0.218   -8.949  20.050  0.50   8.16  ? 247 PRO A N   1 
ATOM   2076 N  N   B PRO A 1 246 ? 0.219   -8.932  20.056  0.50   8.24  ? 247 PRO A N   1 
ATOM   2077 C  CA  A PRO A 1 246 ? -0.099  -9.747  21.227  0.50   8.88  ? 247 PRO A CA  1 
ATOM   2078 C  CA  B PRO A 1 246 ? -0.299  -9.792  21.122  0.50   8.81  ? 247 PRO A CA  1 
ATOM   2079 C  C   A PRO A 1 246 ? -0.522  -8.927  22.450  0.50   8.64  ? 247 PRO A C   1 
ATOM   2080 C  C   B PRO A 1 246 ? -0.564  -8.964  22.388  0.50   8.36  ? 247 PRO A C   1 
ATOM   2081 O  O   A PRO A 1 246 ? -0.208  -7.719  22.602  0.50   7.98  ? 247 PRO A O   1 
ATOM   2082 O  O   B PRO A 1 246 ? -0.171  -7.776  22.496  0.50   8.61  ? 247 PRO A O   1 
ATOM   2083 C  CB  A PRO A 1 246 ? 1.216   -10.451 21.515  0.50   8.97  ? 247 PRO A CB  1 
ATOM   2084 C  CB  B PRO A 1 246 ? 0.840   -10.743 21.347  0.50   9.37  ? 247 PRO A CB  1 
ATOM   2085 C  CG  A PRO A 1 246 ? 1.857   -10.600 20.169  0.50   9.74  ? 247 PRO A CG  1 
ATOM   2086 C  CG  B PRO A 1 246 ? 2.083   -9.927  20.982  0.50   10.95 ? 247 PRO A CG  1 
ATOM   2087 C  CD  A PRO A 1 246 ? 1.565   -9.274  19.539  0.50   8.78  ? 247 PRO A CD  1 
ATOM   2088 C  CD  B PRO A 1 246 ? 1.693   -9.027  19.896  0.50   9.24  ? 247 PRO A CD  1 
ATOM   2089 N  N   . ALA A 1 247 ? -1.213  -9.595  23.377  1.00   9.41  ? 248 ALA A N   1 
ATOM   2090 C  CA  . ALA A 1 247 ? -1.540  -8.958  24.637  1.00   8.84  ? 248 ALA A CA  1 
ATOM   2091 C  C   . ALA A 1 247 ? -0.321  -8.435  25.364  1.00   8.76  ? 248 ALA A C   1 
ATOM   2092 O  O   . ALA A 1 247 ? 0.745   -9.103  25.412  1.00   10.15 ? 248 ALA A O   1 
ATOM   2093 C  CB  . ALA A 1 247 ? -2.291  -9.912  25.523  1.00   11.37 ? 248 ALA A CB  1 
ATOM   2094 N  N   . GLN A 1 248 ? -0.438  -7.264  25.964  1.00   8.24  ? 249 GLN A N   1 
ATOM   2095 C  CA  . GLN A 1 248 ? 0.614   -6.523  26.673  1.00   8.86  ? 249 GLN A CA  1 
ATOM   2096 C  C   . GLN A 1 248 ? 0.311   -6.540  28.139  1.00   8.82  ? 249 GLN A C   1 
ATOM   2097 O  O   . GLN A 1 248 ? -0.828  -6.739  28.600  1.00   10.20 ? 249 GLN A O   1 
ATOM   2098 C  CB  . GLN A 1 248 ? 0.640   -5.101  26.148  1.00   9.51  ? 249 GLN A CB  1 
ATOM   2099 C  CG  . GLN A 1 248 ? 0.949   -5.009  24.668  1.00   9.82  ? 249 GLN A CG  1 
ATOM   2100 C  CD  . GLN A 1 248 ? 2.257   -5.668  24.326  1.00   10.73 ? 249 GLN A CD  1 
ATOM   2101 O  OE1 . GLN A 1 248 ? 3.318   -5.347  24.923  1.00   13.07 ? 249 GLN A OE1 1 
ATOM   2102 N  NE2 . GLN A 1 248 ? 2.274   -6.582  23.361  1.00   11.60 ? 249 GLN A NE2 1 
ATOM   2103 N  N   . PRO A 1 249 ? 1.303   -6.244  28.984  1.00   10.54 ? 250 PRO A N   1 
ATOM   2104 C  CA  . PRO A 1 249 ? 1.104   -6.280  30.429  1.00   11.74 ? 250 PRO A CA  1 
ATOM   2105 C  C   . PRO A 1 249 ? 0.052   -5.286  30.866  1.00   9.55  ? 250 PRO A C   1 
ATOM   2106 O  O   . PRO A 1 249 ? 0.078   -4.112  30.538  1.00   10.13 ? 250 PRO A O   1 
ATOM   2107 C  CB  . PRO A 1 249 ? 2.515   -5.897  30.976  1.00   14.56 ? 250 PRO A CB  1 
ATOM   2108 C  CG  . PRO A 1 249 ? 3.518   -6.311  29.917  1.00   15.50 ? 250 PRO A CG  1 
ATOM   2109 C  CD  . PRO A 1 249 ? 2.734   -5.991  28.616  1.00   13.34 ? 250 PRO A CD  1 
ATOM   2110 N  N   . LEU A 1 250 ? -0.825  -5.739  31.761  1.00   11.08 ? 251 LEU A N   1 
ATOM   2111 C  CA  . LEU A 1 250 ? -1.878  -4.903  32.275  1.00   10.91 ? 251 LEU A CA  1 
ATOM   2112 C  C   . LEU A 1 250 ? -1.367  -3.826  33.218  1.00   9.77  ? 251 LEU A C   1 
ATOM   2113 O  O   . LEU A 1 250 ? -1.940  -2.718  33.276  1.00   10.66 ? 251 LEU A O   1 
ATOM   2114 C  CB  . LEU A 1 250 ? -2.930  -5.770  32.993  1.00   12.44 ? 251 LEU A CB  1 
ATOM   2115 C  CG  . LEU A 1 250 ? -4.209  -5.027  33.434  1.00   12.89 ? 251 LEU A CG  1 
ATOM   2116 C  CD1 . LEU A 1 250 ? -4.920  -4.485  32.183  1.00   13.21 ? 251 LEU A CD1 1 
ATOM   2117 C  CD2 . LEU A 1 250 ? -5.119  -6.006  34.222  1.00   16.00 ? 251 LEU A CD2 1 
ATOM   2118 N  N   A LYS A 1 251 ? -0.203  -3.996  33.863  0.50   9.70  ? 252 LYS A N   1 
ATOM   2119 N  N   B LYS A 1 251 ? -0.432  -4.215  34.051  0.50   11.20 ? 252 LYS A N   1 
ATOM   2120 C  CA  A LYS A 1 251 ? 0.381   -2.939  34.793  0.50   9.57  ? 252 LYS A CA  1 
ATOM   2121 C  CA  B LYS A 1 251 ? 0.197   -3.238  34.957  0.50   13.04 ? 252 LYS A CA  1 
ATOM   2122 C  C   A LYS A 1 251 ? -0.670  -2.500  35.796  0.50   12.03 ? 252 LYS A C   1 
ATOM   2123 C  C   B LYS A 1 251 ? -0.847  -2.520  35.851  0.50   13.01 ? 252 LYS A C   1 
ATOM   2124 O  O   A LYS A 1 251 ? -1.410  -3.395  36.277  0.50   13.79 ? 252 LYS A O   1 
ATOM   2125 O  O   B LYS A 1 251 ? -1.747  -3.232  36.338  0.50   16.51 ? 252 LYS A O   1 
ATOM   2126 C  CB  A LYS A 1 251 ? 1.010   -1.840  33.994  0.50   12.16 ? 252 LYS A CB  1 
ATOM   2127 C  CB  B LYS A 1 251 ? 1.077   -2.298  34.175  0.50   14.20 ? 252 LYS A CB  1 
ATOM   2128 C  CG  A LYS A 1 251 ? 2.086   -2.506  33.154  0.50   13.76 ? 252 LYS A CG  1 
ATOM   2129 C  CG  B LYS A 1 251 ? 2.359   -3.005  33.750  0.50   19.13 ? 252 LYS A CG  1 
ATOM   2130 C  CD  A LYS A 1 251 ? 3.158   -1.555  32.660  0.50   16.93 ? 252 LYS A CD  1 
ATOM   2131 C  CD  B LYS A 1 251 ? 3.202   -2.180  32.851  0.50   16.68 ? 252 LYS A CD  1 
ATOM   2132 C  CE  A LYS A 1 251 ? 4.471   -2.222  32.364  0.50   18.47 ? 252 LYS A CE  1 
ATOM   2133 C  CE  B LYS A 1 251 ? 4.342   -2.972  32.288  0.50   22.60 ? 252 LYS A CE  1 
ATOM   2134 N  NZ  A LYS A 1 251 ? 5.235   -1.608  31.237  0.50   19.50 ? 252 LYS A NZ  1 
ATOM   2135 N  NZ  B LYS A 1 251 ? 5.521   -3.108  33.194  0.50   24.50 ? 252 LYS A NZ  1 
ATOM   2136 N  N   . ASN A 1 252 ? -0.751  -1.222  36.066  1.00   12.11 ? 253 ASN A N   1 
ATOM   2137 C  CA  . ASN A 1 252 ? -1.560  -0.702  37.095  1.00   16.88 ? 253 ASN A CA  1 
ATOM   2138 C  C   . ASN A 1 252 ? -2.888  -0.284  36.485  1.00   17.21 ? 253 ASN A C   1 
ATOM   2139 O  O   . ASN A 1 252 ? -3.035  1.017   36.446  1.00   20.11 ? 253 ASN A O   1 
ATOM   2140 C  CB  . ASN A 1 252 ? -0.847  0.517   37.759  1.00   21.38 ? 253 ASN A CB  1 
ATOM   2141 C  CG  . ASN A 1 252 ? -1.534  0.976   38.998  1.00   25.16 ? 253 ASN A CG  1 
ATOM   2142 O  OD1 . ASN A 1 252 ? -1.916  0.168   39.852  1.00   38.73 ? 253 ASN A OD1 1 
ATOM   2143 N  ND2 . ASN A 1 252 ? -1.684  2.287   39.139  1.00   26.43 ? 253 ASN A ND2 1 
ATOM   2144 N  N   . ARG A 1 253 ? -3.684  -1.302  35.857  1.00   13.45 ? 254 ARG A N   1 
ATOM   2145 C  CA  . ARG A 1 253 ? -4.939  -0.952  35.297  1.00   9.92  ? 254 ARG A CA  1 
ATOM   2146 C  C   . ARG A 1 253 ? -6.037  -1.879  35.783  1.00   11.16 ? 254 ARG A C   1 
ATOM   2147 O  O   . ARG A 1 253 ? -5.791  -3.036  36.052  1.00   17.68 ? 254 ARG A O   1 
ATOM   2148 C  CB  . ARG A 1 253 ? -4.889  -0.933  33.803  1.00   10.02 ? 254 ARG A CB  1 
ATOM   2149 C  CG  . ARG A 1 253 ? -4.014  0.177   33.297  1.00   10.41 ? 254 ARG A CG  1 
ATOM   2150 C  CD  . ARG A 1 253 ? -3.846  0.163   31.781  1.00   9.32  ? 254 ARG A CD  1 
ATOM   2151 N  NE  . ARG A 1 253 ? -3.055  -0.994  31.331  1.00   8.72  ? 254 ARG A NE  1 
ATOM   2152 C  CZ  . ARG A 1 253 ? -2.799  -1.267  30.057  1.00   7.70  ? 254 ARG A CZ  1 
ATOM   2153 N  NH1 . ARG A 1 253 ? -3.409  -0.567  29.079  1.00   7.64  ? 254 ARG A NH1 1 
ATOM   2154 N  NH2 . ARG A 1 253 ? -1.961  -2.225  29.732  1.00   7.86  ? 254 ARG A NH2 1 
ATOM   2155 N  N   . GLN A 1 254 ? -7.241  -1.364  35.821  1.00   11.11 ? 255 GLN A N   1 
ATOM   2156 C  CA  . GLN A 1 254 ? -8.446  -2.127  36.096  1.00   12.20 ? 255 GLN A CA  1 
ATOM   2157 C  C   . GLN A 1 254 ? -9.279  -2.202  34.849  1.00   10.76 ? 255 GLN A C   1 
ATOM   2158 O  O   . GLN A 1 254 ? -9.531  -1.170  34.176  1.00   14.26 ? 255 GLN A O   1 
ATOM   2159 C  CB  . GLN A 1 254 ? -9.219  -1.582  37.255  1.00   17.14 ? 255 GLN A CB  1 
ATOM   2160 C  CG  . GLN A 1 254 ? -8.496  -1.904  38.621  1.00   21.29 ? 255 GLN A CG  1 
ATOM   2161 C  CD  . GLN A 1 254 ? -9.434  -1.822  39.771  1.00   27.16 ? 255 GLN A CD  1 
ATOM   2162 O  OE1 . GLN A 1 254 ? -10.311 -0.905  39.794  1.00   35.18 ? 255 GLN A OE1 1 
ATOM   2163 N  NE2 . GLN A 1 254 ? -9.314  -2.782  40.741  1.00   31.63 ? 255 GLN A NE2 1 
ATOM   2164 N  N   . ILE A 1 255 ? -9.749  -3.389  34.506  1.00   9.64  ? 256 ILE A N   1 
ATOM   2165 C  CA  . ILE A 1 255 ? -10.749 -3.562  33.439  1.00   9.04  ? 256 ILE A CA  1 
ATOM   2166 C  C   . ILE A 1 255 ? -12.135 -3.585  34.120  1.00   8.76  ? 256 ILE A C   1 
ATOM   2167 O  O   . ILE A 1 255 ? -12.327 -4.318  35.097  1.00   10.84 ? 256 ILE A O   1 
ATOM   2168 C  CB  . ILE A 1 255 ? -10.479 -4.787  32.634  1.00   9.12  ? 256 ILE A CB  1 
ATOM   2169 C  CG1 . ILE A 1 255 ? -9.068  -4.806  32.063  1.00   10.14 ? 256 ILE A CG1 1 
ATOM   2170 C  CG2 . ILE A 1 255 ? -11.528 -4.974  31.548  1.00   10.86 ? 256 ILE A CG2 1 
ATOM   2171 C  CD1 . ILE A 1 255 ? -8.724  -5.985  31.254  1.00   11.75 ? 256 ILE A CD1 1 
ATOM   2172 N  N   . LYS A 1 256 ? -13.064 -2.775  33.646  1.00   8.99  ? 257 LYS A N   1 
ATOM   2173 C  CA  . LYS A 1 256 ? -14.391 -2.688  34.224  1.00   8.77  ? 257 LYS A CA  1 
ATOM   2174 C  C   . LYS A 1 256 ? -15.391 -3.290  33.255  1.00   8.94  ? 257 LYS A C   1 
ATOM   2175 O  O   . LYS A 1 256 ? -15.230 -3.136  32.033  1.00   10.63 ? 257 LYS A O   1 
ATOM   2176 C  CB  . LYS A 1 256 ? -14.717 -1.246  34.507  1.00   10.70 ? 257 LYS A CB  1 
ATOM   2177 C  CG  . LYS A 1 256 ? -13.731 -0.714  35.534  1.00   14.32 ? 257 LYS A CG  1 
ATOM   2178 C  CD  . LYS A 1 256 ? -13.820 0.761   35.890  0.010  6.66  ? 257 LYS A CD  1 
ATOM   2179 C  CE  . LYS A 1 256 ? -12.717 1.094   36.928  0.010  7.19  ? 257 LYS A CE  1 
ATOM   2180 N  NZ  . LYS A 1 256 ? -12.748 2.512   37.407  0.010  6.12  ? 257 LYS A NZ  1 
ATOM   2181 N  N   . ALA A 1 257 ? -16.420 -3.929  33.787  1.00   9.48  ? 258 ALA A N   1 
ATOM   2182 C  CA  . ALA A 1 257 ? -17.475 -4.551  33.025  1.00   9.61  ? 258 ALA A CA  1 
ATOM   2183 C  C   . ALA A 1 257 ? -18.741 -3.707  33.180  1.00   10.24 ? 258 ALA A C   1 
ATOM   2184 O  O   . ALA A 1 257 ? -19.096 -3.264  34.300  1.00   10.92 ? 258 ALA A O   1 
ATOM   2185 C  CB  . ALA A 1 257 ? -17.731 -5.983  33.490  1.00   11.98 ? 258 ALA A CB  1 
ATOM   2186 N  N   . SER A 1 258 ? -19.475 -3.555  32.076  1.00   9.83  ? 259 SER A N   1 
ATOM   2187 C  CA  . SER A 1 258 ? -20.734 -2.843  32.066  1.00   11.33 ? 259 SER A CA  1 
ATOM   2188 C  C   . SER A 1 258 ? -21.917 -3.711  32.520  1.00   11.33 ? 259 SER A C   1 
ATOM   2189 O  O   . SER A 1 258 ? -23.016 -3.158  32.627  1.00   15.05 ? 259 SER A O   1 
ATOM   2190 C  CB  . SER A 1 258 ? -21.026 -2.304  30.684  1.00   11.38 ? 259 SER A CB  1 
ATOM   2191 O  OG  . SER A 1 258 ? -21.461 -3.325  29.818  1.00   10.37 ? 259 SER A OG  1 
ATOM   2192 N  N   . PHE A 1 259 ? -21.674 -4.963  32.744  1.00   11.93 ? 260 PHE A N   1 
ATOM   2193 C  CA  . PHE A 1 259 ? -22.742 -5.945  32.925  1.00   14.72 ? 260 PHE A CA  1 
ATOM   2194 C  C   . PHE A 1 259 ? -22.382 -6.848  34.071  1.00   17.91 ? 260 PHE A C   1 
ATOM   2195 O  O   . PHE A 1 259 ? -21.192 -7.025  34.395  1.00   18.27 ? 260 PHE A O   1 
ATOM   2196 C  CB  . PHE A 1 259 ? -22.879 -6.756  31.646  1.00   14.68 ? 260 PHE A CB  1 
ATOM   2197 C  CG  . PHE A 1 259 ? -21.596 -7.487  31.281  1.00   13.59 ? 260 PHE A CG  1 
ATOM   2198 C  CD1 . PHE A 1 259 ? -20.594 -6.845  30.509  1.00   12.00 ? 260 PHE A CD1 1 
ATOM   2199 C  CD2 . PHE A 1 259 ? -21.352 -8.791  31.736  1.00   17.76 ? 260 PHE A CD2 1 
ATOM   2200 C  CE1 . PHE A 1 259 ? -19.392 -7.510  30.259  1.00   14.41 ? 260 PHE A CE1 1 
ATOM   2201 C  CE2 . PHE A 1 259 ? -20.162 -9.426  31.449  1.00   18.65 ? 260 PHE A CE2 1 
ATOM   2202 C  CZ  . PHE A 1 259 ? -19.176 -8.809  30.732  1.00   16.27 ? 260 PHE A CZ  1 
ATOM   2203 N  N   . LYS A 1 260 ? -23.434 -7.413  34.680  1.00   28.55 ? 261 LYS A N   1 
ATOM   2204 C  CA  . LYS A 1 260 ? -23.377 -8.618  35.594  1.00   32.57 ? 261 LYS A CA  1 
ATOM   2205 C  C   . LYS A 1 260 ? -24.089 -9.775  34.885  1.00   44.52 ? 261 LYS A C   1 
ATOM   2206 O  O   . LYS A 1 260 ? -25.274 -10.038 35.118  0.0000 46.27 ? 261 LYS A O   1 
ATOM   2207 C  CB  . LYS A 1 260 ? -23.961 -8.388  37.027  1.00   52.13 ? 261 LYS A CB  1 
ATOM   2208 C  CG  . LYS A 1 260 ? -24.855 -7.150  37.218  0.0000 52.74 ? 261 LYS A CG  1 
ATOM   2209 C  CD  . LYS A 1 260 ? -26.333 -7.463  37.013  0.0000 72.21 ? 261 LYS A CD  1 
ATOM   2210 C  CE  . LYS A 1 260 ? -27.038 -7.640  38.356  0.0000 74.68 ? 261 LYS A CE  1 
ATOM   2211 N  NZ  . LYS A 1 260 ? -28.023 -8.756  38.310  0.0000 71.07 ? 261 LYS A NZ  1 
ATOM   2212 O  OXT . LYS A 1 260 ? -23.519 -10.495 34.044  1.00   54.22 ? 261 LYS A OXT 1 
HETATM 2213 ZN ZN  . ZN  B 2 .   ? -6.774  -1.713  15.332  1.00   6.43  ? 301 ZN  A ZN  1 
HETATM 2214 N  N1  . BCN C 3 .   ? -20.368 -14.314 23.169  1.00   32.61 ? 302 BCN A N1  1 
HETATM 2215 C  C1  . BCN C 3 .   ? -20.068 -15.639 22.554  1.00   18.35 ? 302 BCN A C1  1 
HETATM 2216 C  C2  . BCN C 3 .   ? -20.523 -16.084 21.179  1.00   38.16 ? 302 BCN A C2  1 
HETATM 2217 O  O21 . BCN C 3 .   ? -21.686 -15.902 20.687  1.00   50.45 ? 302 BCN A O21 1 
HETATM 2218 O  O22 . BCN C 3 .   ? -19.615 -16.672 20.556  1.00   45.18 ? 302 BCN A O22 1 
HETATM 2219 C  C3  . BCN C 3 .   ? -21.782 -14.000 23.091  1.00   21.26 ? 302 BCN A C3  1 
HETATM 2220 C  C4  . BCN C 3 .   ? -22.585 -12.814 23.672  1.00   34.63 ? 302 BCN A C4  1 
HETATM 2221 O  O4  . BCN C 3 .   ? -22.477 -12.417 25.053  1.00   26.35 ? 302 BCN A O4  1 
HETATM 2222 C  C5  . BCN C 3 .   ? -19.712 -14.088 24.478  1.00   29.26 ? 302 BCN A C5  1 
HETATM 2223 C  C6  . BCN C 3 .   ? -20.055 -15.274 25.408  1.00   34.47 ? 302 BCN A C6  1 
HETATM 2224 O  O6  . BCN C 3 .   ? -19.370 -15.014 26.593  1.00   26.09 ? 302 BCN A O6  1 
HETATM 2225 S  S   . DMS D 4 .   ? -5.805  7.508   11.114  1.00   33.65 ? 303 DMS A S   1 
HETATM 2226 O  O   . DMS D 4 .   ? -6.149  6.348   11.941  1.00   16.21 ? 303 DMS A O   1 
HETATM 2227 C  C1  . DMS D 4 .   ? -7.091  8.683   11.040  1.00   24.80 ? 303 DMS A C1  1 
HETATM 2228 C  C2  . DMS D 4 .   ? -4.191  8.075   11.003  1.00   44.08 ? 303 DMS A C2  1 
HETATM 2229 S  S   . DMS E 4 .   ? 1.266   -11.639 14.852  1.00   29.60 ? 304 DMS A S   1 
HETATM 2230 O  O   . DMS E 4 .   ? 2.296   -11.218 13.624  1.00   24.62 ? 304 DMS A O   1 
HETATM 2231 C  C1  . DMS E 4 .   ? 1.671   -13.345 14.755  1.00   33.03 ? 304 DMS A C1  1 
HETATM 2232 C  C2  . DMS E 4 .   ? 1.578   -11.244 16.441  1.00   20.42 ? 304 DMS A C2  1 
HETATM 2233 O  O25 . KR5 F 5 .   ? -1.463  7.629   14.813  1.00   19.17 ? 305 KR5 A O25 1 
HETATM 2234 C  C22 . KR5 F 5 .   ? -1.926  7.788   13.705  1.00   16.47 ? 305 KR5 A C22 1 
HETATM 2235 N  N27 . KR5 F 5 .   ? -1.900  9.155   13.327  1.00   18.18 ? 305 KR5 A N27 1 
HETATM 2236 C  C29 . KR5 F 5 .   ? -1.240  10.192  14.109  1.00   23.37 ? 305 KR5 A C29 1 
HETATM 2237 C  C33 . KR5 F 5 .   ? -0.369  9.822   15.270  1.00   31.33 ? 305 KR5 A C33 1 
HETATM 2238 C  C30 . KR5 F 5 .   ? -1.411  11.447  13.470  1.00   36.23 ? 305 KR5 A C30 1 
HETATM 2239 C  C31 . KR5 F 5 .   ? -2.264  11.165  12.359  1.00   46.06 ? 305 KR5 A C31 1 
HETATM 2240 C  C37 . KR5 F 5 .   ? -2.825  12.126  11.381  1.00   63.15 ? 305 KR5 A C37 1 
HETATM 2241 N  N28 . KR5 F 5 .   ? -2.555  9.819   12.302  1.00   40.48 ? 305 KR5 A N28 1 
HETATM 2242 C  C19 . KR5 F 5 .   ? -2.266  6.836   12.657  1.00   16.80 ? 305 KR5 A C19 1 
HETATM 2243 C  C18 . KR5 F 5 .   ? -2.607  5.522   13.277  1.00   14.05 ? 305 KR5 A C18 1 
HETATM 2244 N  N17 . KR5 F 5 .   ? -3.971  5.523   13.866  1.00   11.39 ? 305 KR5 A N17 1 
HETATM 2245 C  C8  . KR5 F 5 .   ? -4.415  4.396   14.574  1.00   9.19  ? 305 KR5 A C8  1 
HETATM 2246 C  C7  . KR5 F 5 .   ? -3.553  3.396   14.950  1.00   9.39  ? 305 KR5 A C7  1 
HETATM 2247 C  C6  . KR5 F 5 .   ? -4.039  2.274   15.661  1.00   8.74  ? 305 KR5 A C6  1 
HETATM 2248 C  C9  . KR5 F 5 .   ? -5.778  4.338   14.890  1.00   8.92  ? 305 KR5 A C9  1 
HETATM 2249 C  C10 . KR5 F 5 .   ? -6.251  3.234   15.585  1.00   8.74  ? 305 KR5 A C10 1 
HETATM 2250 C  C5  . KR5 F 5 .   ? -5.403  2.193   15.970  1.00   7.68  ? 305 KR5 A C5  1 
HETATM 2251 S  S2  . KR5 F 5 .   ? -6.016  0.794   16.833  1.00   7.01  ? 305 KR5 A S2  1 
HETATM 2252 O  O3  . KR5 F 5 .   ? -7.409  0.839   16.696  1.00   6.89  ? 305 KR5 A O3  1 
HETATM 2253 O  O4  . KR5 F 5 .   ? -5.458  0.876   18.176  1.00   7.27  ? 305 KR5 A O4  1 
HETATM 2254 N  N1  . KR5 F 5 .   ? -5.449  -0.526  16.091  1.00   6.63  ? 305 KR5 A N1  1 
HETATM 2255 O  O   . HOH G 6 .   ? -4.629  -13.565 18.099  1.00   9.00  ? 401 HOH A O   1 
HETATM 2256 O  O   . HOH G 6 .   ? -17.125 -8.481  20.443  1.00   9.01  ? 402 HOH A O   1 
HETATM 2257 O  O   . HOH G 6 .   ? -1.328  -4.199  15.769  1.00   9.07  ? 403 HOH A O   1 
HETATM 2258 O  O   . HOH G 6 .   ? -2.170  -12.341 22.892  1.00   9.81  ? 404 HOH A O   1 
HETATM 2259 O  O   . HOH G 6 .   ? -8.085  -15.512 11.405  1.00   10.27 ? 405 HOH A O   1 
HETATM 2260 O  O   . HOH G 6 .   ? -3.481  -13.310 25.192  1.00   10.54 ? 406 HOH A O   1 
HETATM 2261 O  O   . HOH G 6 .   ? -2.579  -8.776  29.129  1.00   10.30 ? 407 HOH A O   1 
HETATM 2262 O  O   . HOH G 6 .   ? -8.808  -3.898  7.940   1.00   8.74  ? 408 HOH A O   1 
HETATM 2263 O  O   . HOH G 6 .   ? -10.786 8.645   25.620  1.00   9.64  ? 409 HOH A O   1 
HETATM 2264 O  O   . HOH G 6 .   ? -21.685 -7.301  23.743  1.00   11.17 ? 410 HOH A O   1 
HETATM 2265 O  O   . HOH G 6 .   ? -3.591  -11.190 20.923  1.00   9.95  ? 411 HOH A O   1 
HETATM 2266 O  O   . HOH G 6 .   ? 1.188   -1.572  29.467  1.00   12.30 ? 412 HOH A O   1 
HETATM 2267 O  O   . HOH G 6 .   ? -12.975 -17.274 16.930  1.00   11.28 ? 413 HOH A O   1 
HETATM 2268 O  O   . HOH G 6 .   ? -3.873  -15.957 24.395  1.00   12.33 ? 414 HOH A O   1 
HETATM 2269 O  O   . HOH G 6 .   ? -4.025  0.070   13.592  1.00   11.77 ? 415 HOH A O   1 
HETATM 2270 O  O   . HOH G 6 .   ? -6.867  -20.344 19.632  1.00   11.17 ? 416 HOH A O   1 
HETATM 2271 O  O   . HOH G 6 .   ? 0.061   -1.119  -4.692  1.00   14.62 ? 417 HOH A O   1 
HETATM 2272 O  O   . HOH G 6 .   ? 4.799   -4.871  20.979  1.00   12.61 ? 418 HOH A O   1 
HETATM 2273 O  O   . HOH G 6 .   ? -13.087 -16.885 26.727  1.00   12.54 ? 419 HOH A O   1 
HETATM 2274 O  O   . HOH G 6 .   ? -16.142 -12.367 24.481  1.00   12.40 ? 420 HOH A O   1 
HETATM 2275 O  O   . HOH G 6 .   ? -22.029 5.688   4.781   1.00   14.78 ? 421 HOH A O   1 
HETATM 2276 O  O   . HOH G 6 .   ? -5.463  2.109   12.124  1.00   12.16 ? 422 HOH A O   1 
HETATM 2277 O  O   . HOH G 6 .   ? -10.481 -18.368 17.154  1.00   11.39 ? 423 HOH A O   1 
HETATM 2278 O  O   . HOH G 6 .   ? -18.040 -20.467 8.036   1.00   14.02 ? 424 HOH A O   1 
HETATM 2279 O  O   . HOH G 6 .   ? 7.541   5.982   21.651  1.00   14.25 ? 425 HOH A O   1 
HETATM 2280 O  O   . HOH G 6 .   ? 1.131   8.784   24.354  1.00   14.81 ? 426 HOH A O   1 
HETATM 2281 O  O   . HOH G 6 .   ? -19.399 9.991   8.889   1.00   13.52 ? 427 HOH A O   1 
HETATM 2282 O  O   . HOH G 6 .   ? -8.333  -19.443 21.739  1.00   12.86 ? 428 HOH A O   1 
HETATM 2283 O  O   . HOH G 6 .   ? -15.028 -21.175 17.688  1.00   15.39 ? 429 HOH A O   1 
HETATM 2284 O  O   . HOH G 6 .   ? 8.469   -3.903  21.080  1.00   13.01 ? 430 HOH A O   1 
HETATM 2285 O  O   . HOH G 6 .   ? 3.531   4.949   29.815  1.00   15.64 ? 431 HOH A O   1 
HETATM 2286 O  O   . HOH G 6 .   ? -13.978 10.223  28.006  1.00   14.68 ? 432 HOH A O   1 
HETATM 2287 O  O   . HOH G 6 .   ? -14.718 -18.647 18.748  1.00   13.69 ? 433 HOH A O   1 
HETATM 2288 O  O   . HOH G 6 .   ? 5.303   7.059   20.271  1.00   14.80 ? 434 HOH A O   1 
HETATM 2289 O  O   . HOH G 6 .   ? -10.774 -19.518 20.127  1.00   14.89 ? 435 HOH A O   1 
HETATM 2290 O  O   . HOH G 6 .   ? -13.508 -18.598 14.617  1.00   13.01 ? 436 HOH A O   1 
HETATM 2291 O  O   . HOH G 6 .   ? -14.380 -16.686 29.151  1.00   18.08 ? 437 HOH A O   1 
HETATM 2292 O  O   . HOH G 6 .   ? -23.957 -0.871  3.966   1.00   18.97 ? 438 HOH A O   1 
HETATM 2293 O  O   . HOH G 6 .   ? -12.138 2.621   31.136  1.00   15.19 ? 439 HOH A O   1 
HETATM 2294 O  O   . HOH G 6 .   ? -1.351  -11.208 29.090  1.00   14.73 ? 440 HOH A O   1 
HETATM 2295 O  O   . HOH G 6 .   ? -16.373 -10.008 33.075  1.00   16.82 ? 441 HOH A O   1 
HETATM 2296 O  O   . HOH G 6 .   ? -18.049 10.659  11.292  1.00   16.35 ? 442 HOH A O   1 
HETATM 2297 O  O   . HOH G 6 .   ? -4.758  4.189   10.440  1.00   18.69 ? 443 HOH A O   1 
HETATM 2298 O  O   . HOH G 6 .   ? -6.349  -4.709  -6.391  1.00   20.81 ? 444 HOH A O   1 
HETATM 2299 O  O   . HOH G 6 .   ? -17.485 -16.261 22.114  1.00   18.87 ? 445 HOH A O   1 
HETATM 2300 O  O   . HOH G 6 .   ? -21.255 7.790   1.902   1.00   15.82 ? 446 HOH A O   1 
HETATM 2301 O  O   . HOH G 6 .   ? -24.024 -0.788  26.563  1.00   17.12 ? 447 HOH A O   1 
HETATM 2302 O  O   . HOH G 6 .   ? -15.554 -21.961 13.154  1.00   14.54 ? 448 HOH A O   1 
HETATM 2303 O  O   . HOH G 6 .   ? 4.149   -6.608  7.750   1.00   19.18 ? 449 HOH A O   1 
HETATM 2304 O  O   . HOH G 6 .   ? -12.963 -19.609 26.217  1.00   19.04 ? 450 HOH A O   1 
HETATM 2305 O  O   . HOH G 6 .   ? -1.377  -13.062 27.008  1.00   19.64 ? 451 HOH A O   1 
HETATM 2306 O  O   . HOH G 6 .   ? -23.084 -11.789 14.195  1.00   20.49 ? 452 HOH A O   1 
HETATM 2307 O  O   . HOH G 6 .   ? -2.636  -3.751  11.526  1.00   15.03 ? 453 HOH A O   1 
HETATM 2308 O  O   . HOH G 6 .   ? -9.108  -5.801  36.042  1.00   17.10 ? 454 HOH A O   1 
HETATM 2309 O  O   . HOH G 6 .   ? -20.442 10.605  26.847  1.00   16.40 ? 455 HOH A O   1 
HETATM 2310 O  O   . HOH G 6 .   ? -4.873  -12.003 32.194  1.00   18.31 ? 456 HOH A O   1 
HETATM 2311 O  O   . HOH G 6 .   ? 2.579   -4.386  7.745   1.00   17.98 ? 457 HOH A O   1 
HETATM 2312 O  O   . HOH G 6 .   ? -16.316 15.789  23.788  1.00   15.71 ? 458 HOH A O   1 
HETATM 2313 O  O   . HOH G 6 .   ? -6.403  -19.834 23.854  1.00   18.64 ? 459 HOH A O   1 
HETATM 2314 O  O   . HOH G 6 .   ? -4.310  -8.449  31.202  1.00   16.99 ? 460 HOH A O   1 
HETATM 2315 O  O   . HOH G 6 .   ? -9.227  5.842   29.090  1.00   14.95 ? 461 HOH A O   1 
HETATM 2316 O  O   . HOH G 6 .   ? -0.620  10.771  23.470  1.00   15.38 ? 462 HOH A O   1 
HETATM 2317 O  O   . HOH G 6 .   ? -10.236 14.759  12.276  1.00   18.06 ? 463 HOH A O   1 
HETATM 2318 O  O   . HOH G 6 .   ? -24.260 8.512   20.193  1.00   17.40 ? 464 HOH A O   1 
HETATM 2319 O  O   . HOH G 6 .   ? -24.891 -7.768  9.105   1.00   18.28 ? 465 HOH A O   1 
HETATM 2320 O  O   . HOH G 6 .   ? -5.180  0.474   9.927   1.00   15.43 ? 466 HOH A O   1 
HETATM 2321 O  O   . HOH G 6 .   ? -13.834 -21.314 15.171  1.00   15.33 ? 467 HOH A O   1 
HETATM 2322 O  O   . HOH G 6 .   ? 8.226   -1.668  -10.545 1.00   22.77 ? 468 HOH A O   1 
HETATM 2323 O  O   . HOH G 6 .   ? -17.833 -21.331 17.529  1.00   20.89 ? 469 HOH A O   1 
HETATM 2324 O  O   . HOH G 6 .   ? -22.888 -5.947  2.736   1.00   19.75 ? 470 HOH A O   1 
HETATM 2325 O  O   . HOH G 6 .   ? 11.144  1.174   25.916  1.00   21.48 ? 471 HOH A O   1 
HETATM 2326 O  O   . HOH G 6 .   ? -7.082  5.949   6.503   1.00   18.04 ? 472 HOH A O   1 
HETATM 2327 O  O   . HOH G 6 .   ? -17.000 -18.010 20.191  1.00   21.15 ? 473 HOH A O   1 
HETATM 2328 O  O   . HOH G 6 .   ? -16.842 -14.002 26.447  1.00   16.65 ? 474 HOH A O   1 
HETATM 2329 O  O   . HOH G 6 .   ? -9.368  -10.143 -1.103  1.00   20.65 ? 475 HOH A O   1 
HETATM 2330 O  O   . HOH G 6 .   ? -3.771  -13.035 -2.774  1.00   22.80 ? 476 HOH A O   1 
HETATM 2331 O  O   . HOH G 6 .   ? -10.696 -20.465 25.036  1.00   16.89 ? 477 HOH A O   1 
HETATM 2332 O  O   . HOH G 6 .   ? -0.733  -8.598  32.587  1.00   23.90 ? 478 HOH A O   1 
HETATM 2333 O  O   . HOH G 6 .   ? -3.686  -23.226 21.575  1.00   16.78 ? 479 HOH A O   1 
HETATM 2334 O  O   . HOH G 6 .   ? -12.934 7.822   28.894  1.00   19.28 ? 480 HOH A O   1 
HETATM 2335 O  O   . HOH G 6 .   ? -7.019  -14.938 31.678  1.00   23.35 ? 481 HOH A O   1 
HETATM 2336 O  O   . HOH G 6 .   ? -9.563  -7.973  34.321  1.00   20.55 ? 482 HOH A O   1 
HETATM 2337 O  O   . HOH G 6 .   ? -7.276  -16.887 1.629   1.00   18.27 ? 483 HOH A O   1 
HETATM 2338 O  O   . HOH G 6 .   ? 4.464   -2.593  29.080  1.00   22.04 ? 484 HOH A O   1 
HETATM 2339 O  O   . HOH G 6 .   ? -18.756 3.565   -3.408  1.00   46.78 ? 485 HOH A O   1 
HETATM 2340 O  O   . HOH G 6 .   ? -23.366 -3.093  6.719   1.00   19.11 ? 486 HOH A O   1 
HETATM 2341 O  O   . HOH G 6 .   ? -2.133  -17.602 25.728  1.00   23.62 ? 487 HOH A O   1 
HETATM 2342 O  O   . HOH G 6 .   ? 2.427   -13.266 5.271   1.00   20.38 ? 488 HOH A O   1 
HETATM 2343 O  O   . HOH G 6 .   ? -7.462  -8.718  32.693  1.00   16.48 ? 489 HOH A O   1 
HETATM 2344 O  O   . HOH G 6 .   ? -9.483  2.982   34.904  1.00   19.70 ? 490 HOH A O   1 
HETATM 2345 O  O   . HOH G 6 .   ? -11.198 1.069   33.512  1.00   17.44 ? 491 HOH A O   1 
HETATM 2346 O  O   . HOH G 6 .   ? -11.182 -19.554 7.292   1.00   23.29 ? 492 HOH A O   1 
HETATM 2347 O  O   . HOH G 6 .   ? 1.766   -15.743 9.337   1.00   22.44 ? 493 HOH A O   1 
HETATM 2348 O  O   . HOH G 6 .   ? -8.726  -15.505 36.768  1.00   21.22 ? 494 HOH A O   1 
HETATM 2349 O  O   . HOH G 6 .   ? -7.184  -15.738 38.865  1.00   18.52 ? 495 HOH A O   1 
HETATM 2350 O  O   . HOH G 6 .   ? -26.940 -2.588  14.500  1.00   19.98 ? 496 HOH A O   1 
HETATM 2351 O  O   . HOH G 6 .   ? 2.448   -11.571 9.389   1.00   18.39 ? 497 HOH A O   1 
HETATM 2352 O  O   . HOH G 6 .   ? -11.146 15.382  32.420  1.00   17.78 ? 498 HOH A O   1 
HETATM 2353 O  O   . HOH G 6 .   ? -22.242 3.932   -2.975  1.00   23.67 ? 499 HOH A O   1 
HETATM 2354 O  O   . HOH G 6 .   ? -17.602 -19.535 35.406  1.00   23.13 ? 500 HOH A O   1 
HETATM 2355 O  O   . HOH G 6 .   ? 1.407   -6.346  34.467  1.00   22.47 ? 501 HOH A O   1 
HETATM 2356 O  O   . HOH G 6 .   ? -0.291  -14.335 22.157  1.00   21.70 ? 502 HOH A O   1 
HETATM 2357 O  O   . HOH G 6 .   ? 10.755  -12.090 -7.748  1.00   21.48 ? 503 HOH A O   1 
HETATM 2358 O  O   . HOH G 6 .   ? -14.209 14.228  27.266  1.00   19.44 ? 504 HOH A O   1 
HETATM 2359 O  O   . HOH G 6 .   ? 12.795  -17.132 6.859   1.00   21.78 ? 505 HOH A O   1 
HETATM 2360 O  O   . HOH G 6 .   ? -23.480 -13.313 11.198  1.00   18.79 ? 506 HOH A O   1 
HETATM 2361 O  O   . HOH G 6 .   ? 4.096   -3.409  26.567  1.00   19.23 ? 507 HOH A O   1 
HETATM 2362 O  O   . HOH G 6 .   ? -8.629  -19.921 26.797  1.00   20.15 ? 508 HOH A O   1 
HETATM 2363 O  O   . HOH G 6 .   ? -26.977 -4.036  25.018  1.00   20.04 ? 509 HOH A O   1 
HETATM 2364 O  O   . HOH G 6 .   ? -10.699 -19.135 34.764  1.00   20.07 ? 510 HOH A O   1 
HETATM 2365 O  O   . HOH G 6 .   ? -8.342  7.515   8.350   1.00   23.03 ? 511 HOH A O   1 
HETATM 2366 O  O   . HOH G 6 .   ? -22.225 -18.405 13.588  1.00   19.63 ? 512 HOH A O   1 
HETATM 2367 O  O   . HOH G 6 .   ? -0.287  -19.979 6.769   1.00   25.74 ? 513 HOH A O   1 
HETATM 2368 O  O   . HOH G 6 .   ? -2.774  -19.411 2.129   1.00   35.77 ? 514 HOH A O   1 
HETATM 2369 O  O   . HOH G 6 .   ? -18.430 -3.811  -2.622  1.00   24.43 ? 515 HOH A O   1 
HETATM 2370 O  O   . HOH G 6 .   ? 8.410   -4.695  23.799  1.00   25.92 ? 516 HOH A O   1 
HETATM 2371 O  O   . HOH G 6 .   ? -16.545 -11.399 41.938  1.00   20.76 ? 517 HOH A O   1 
HETATM 2372 O  O   . HOH G 6 .   ? -4.728  -15.972 0.856   1.00   23.73 ? 518 HOH A O   1 
HETATM 2373 O  O   . HOH G 6 .   ? -15.104 2.522   38.868  1.00   20.51 ? 519 HOH A O   1 
HETATM 2374 O  O   . HOH G 6 .   ? -0.523  13.882  16.260  1.00   22.77 ? 520 HOH A O   1 
HETATM 2375 O  O   . HOH G 6 .   ? 3.676   9.820   23.863  1.00   23.86 ? 521 HOH A O   1 
HETATM 2376 O  O   . HOH G 6 .   ? -11.152 -15.167 34.286  1.00   21.63 ? 522 HOH A O   1 
HETATM 2377 O  O   . HOH G 6 .   ? -3.765  -17.015 36.715  1.00   20.43 ? 523 HOH A O   1 
HETATM 2378 O  O   . HOH G 6 .   ? -1.672  11.402  25.949  1.00   24.12 ? 524 HOH A O   1 
HETATM 2379 O  O   . HOH G 6 .   ? -8.704  0.588   -6.488  1.00   22.81 ? 525 HOH A O   1 
HETATM 2380 O  O   . HOH G 6 .   ? 8.204   3.001   27.844  1.00   32.13 ? 526 HOH A O   1 
HETATM 2381 O  O   . HOH G 6 .   ? -7.491  -8.689  -2.317  1.00   25.59 ? 527 HOH A O   1 
HETATM 2382 O  O   . HOH G 6 .   ? -1.950  -4.776  -7.091  1.00   22.91 ? 528 HOH A O   1 
HETATM 2383 O  O   . HOH G 6 .   ? -30.974 -7.322  22.453  1.00   24.72 ? 529 HOH A O   1 
HETATM 2384 O  O   . HOH G 6 .   ? 5.481   -17.061 5.642   1.00   28.30 ? 530 HOH A O   1 
HETATM 2385 O  O   . HOH G 6 .   ? -16.924 -22.171 21.994  1.00   42.69 ? 531 HOH A O   1 
HETATM 2386 O  O   . HOH G 6 .   ? -24.706 -9.618  1.905   1.00   21.95 ? 532 HOH A O   1 
HETATM 2387 O  O   . HOH G 6 .   ? -17.674 6.234   38.576  1.00   24.01 ? 533 HOH A O   1 
HETATM 2388 O  O   . HOH G 6 .   ? 5.307   9.185   21.765  1.00   24.28 ? 534 HOH A O   1 
HETATM 2389 O  O   . HOH G 6 .   ? -26.302 3.380   15.481  1.00   21.95 ? 535 HOH A O   1 
HETATM 2390 O  O   . HOH G 6 .   ? -12.303 10.658  5.644   1.00   24.63 ? 536 HOH A O   1 
HETATM 2391 O  O   . HOH G 6 .   ? -25.619 -10.677 17.798  1.00   20.99 ? 537 HOH A O   1 
HETATM 2392 O  O   . HOH G 6 .   ? 4.926   -7.281  22.330  1.00   24.30 ? 538 HOH A O   1 
HETATM 2393 O  O   . HOH G 6 .   ? -4.093  -1.467  11.408  1.00   19.62 ? 539 HOH A O   1 
HETATM 2394 O  O   . HOH G 6 .   ? -23.293 -0.248  34.680  1.00   23.86 ? 540 HOH A O   1 
HETATM 2395 O  O   . HOH G 6 .   ? -22.763 -9.653  25.396  1.00   17.12 ? 541 HOH A O   1 
HETATM 2396 O  O   . HOH G 6 .   ? -26.415 -7.712  30.457  1.00   29.22 ? 542 HOH A O   1 
HETATM 2397 O  O   . HOH G 6 .   ? 1.070   -11.833 25.215  1.00   21.23 ? 543 HOH A O   1 
HETATM 2398 O  O   . HOH G 6 .   ? -15.367 -16.116 25.418  1.00   32.49 ? 544 HOH A O   1 
HETATM 2399 O  O   . HOH G 6 .   ? -24.770 4.673   8.234   1.00   36.47 ? 545 HOH A O   1 
HETATM 2400 O  O   . HOH G 6 .   ? -21.230 -19.756 6.644   1.00   22.93 ? 546 HOH A O   1 
HETATM 2401 O  O   . HOH G 6 .   ? 6.212   5.263   29.142  1.00   32.57 ? 547 HOH A O   1 
HETATM 2402 O  O   . HOH G 6 .   ? -12.663 12.505  29.147  1.00   23.93 ? 548 HOH A O   1 
HETATM 2403 O  O   . HOH G 6 .   ? -24.104 -7.203  0.332   1.00   30.12 ? 549 HOH A O   1 
HETATM 2404 O  O   . HOH G 6 .   ? -26.778 -1.355  26.035  1.00   22.96 ? 550 HOH A O   1 
HETATM 2405 O  O   . HOH G 6 .   ? -18.671 -21.281 14.774  1.00   18.91 ? 551 HOH A O   1 
HETATM 2406 O  O   . HOH G 6 .   ? -21.357 -20.655 14.647  1.00   26.00 ? 552 HOH A O   1 
HETATM 2407 O  O   . HOH G 6 .   ? -0.327  -15.535 27.188  1.00   34.57 ? 553 HOH A O   1 
HETATM 2408 O  O   . HOH G 6 .   ? -2.275  -11.683 31.700  1.00   24.88 ? 554 HOH A O   1 
HETATM 2409 O  O   . HOH G 6 .   ? -1.386  -13.271 33.301  1.00   18.77 ? 555 HOH A O   1 
HETATM 2410 O  O   . HOH G 6 .   ? -23.466 -11.096 17.121  1.00   25.05 ? 556 HOH A O   1 
HETATM 2411 O  O   . HOH G 6 .   ? -5.008  -20.804 21.603  1.00   17.15 ? 557 HOH A O   1 
HETATM 2412 O  O   . HOH G 6 .   ? -6.068  15.213  11.981  1.00   22.89 ? 558 HOH A O   1 
HETATM 2413 O  O   . HOH G 6 .   ? -13.108 -22.267 8.672   1.00   22.26 ? 559 HOH A O   1 
HETATM 2414 O  O   . HOH G 6 .   ? 1.602   12.431  22.787  1.00   23.29 ? 560 HOH A O   1 
HETATM 2415 O  O   . HOH G 6 .   ? -29.200 -5.974  24.379  1.00   23.28 ? 561 HOH A O   1 
HETATM 2416 O  O   . HOH G 6 .   ? -15.707 8.886   -2.152  1.00   22.89 ? 562 HOH A O   1 
HETATM 2417 O  O   . HOH G 6 .   ? -11.358 -23.680 12.346  1.00   20.85 ? 563 HOH A O   1 
HETATM 2418 O  O   . HOH G 6 .   ? 3.250   -1.393  8.594   1.00   25.73 ? 564 HOH A O   1 
HETATM 2419 O  O   . HOH G 6 .   ? -12.019 9.300   3.124   1.00   19.22 ? 565 HOH A O   1 
HETATM 2420 O  O   . HOH G 6 .   ? -11.720 -0.305  43.612  1.00   21.92 ? 566 HOH A O   1 
HETATM 2421 O  O   . HOH G 6 .   ? 10.194  -8.674  8.380   1.00   23.52 ? 567 HOH A O   1 
HETATM 2422 O  O   . HOH G 6 .   ? -25.231 9.525   12.932  1.00   29.24 ? 568 HOH A O   1 
HETATM 2423 O  O   . HOH G 6 .   ? -1.971  -17.043 34.528  1.00   23.43 ? 569 HOH A O   1 
HETATM 2424 O  O   . HOH G 6 .   ? -0.560  2.898   12.780  1.00   21.73 ? 570 HOH A O   1 
HETATM 2425 O  O   . HOH G 6 .   ? -13.052 -8.899  -3.199  1.00   27.53 ? 571 HOH A O   1 
HETATM 2426 O  O   . HOH G 6 .   ? -1.169  -17.350 -1.811  1.00   31.13 ? 572 HOH A O   1 
HETATM 2427 O  O   . HOH G 6 .   ? -7.539  -4.829  40.291  1.00   27.21 ? 573 HOH A O   1 
HETATM 2428 O  O   . HOH G 6 .   ? -5.309  2.200   37.437  1.00   21.95 ? 574 HOH A O   1 
HETATM 2429 O  O   . HOH G 6 .   ? 4.885   -13.164 -5.811  1.00   25.96 ? 575 HOH A O   1 
HETATM 2430 O  O   . HOH G 6 .   ? -25.664 -1.068  35.141  1.00   24.76 ? 576 HOH A O   1 
HETATM 2431 O  O   . HOH G 6 .   ? -30.635 -0.494  16.099  1.00   20.94 ? 577 HOH A O   1 
HETATM 2432 O  O   . HOH G 6 .   ? -11.741 10.717  0.721   1.00   24.27 ? 578 HOH A O   1 
HETATM 2433 O  O   . HOH G 6 .   ? -4.473  -1.561  38.005  1.00   25.16 ? 579 HOH A O   1 
HETATM 2434 O  O   . HOH G 6 .   ? 2.882   -13.733 8.145   1.00   23.79 ? 580 HOH A O   1 
HETATM 2435 O  O   . HOH G 6 .   ? -18.757 2.090   40.982  1.00   29.91 ? 581 HOH A O   1 
HETATM 2436 O  O   . HOH G 6 .   ? -15.210 9.535   31.566  1.00   39.94 ? 582 HOH A O   1 
HETATM 2437 O  O   . HOH G 6 .   ? -25.408 10.972  19.586  1.00   27.64 ? 583 HOH A O   1 
HETATM 2438 O  O   . HOH G 6 .   ? -21.745 -21.813 12.168  1.00   26.01 ? 584 HOH A O   1 
HETATM 2439 O  O   . HOH G 6 .   ? -26.039 6.075   27.191  1.00   21.50 ? 585 HOH A O   1 
HETATM 2440 O  O   . HOH G 6 .   ? 6.111   -11.309 15.620  1.00   25.66 ? 586 HOH A O   1 
HETATM 2441 O  O   . HOH G 6 .   ? 1.848   -14.243 20.562  1.00   27.69 ? 587 HOH A O   1 
HETATM 2442 O  O   . HOH G 6 .   ? -2.836  -14.518 37.214  1.00   22.47 ? 588 HOH A O   1 
HETATM 2443 O  O   . HOH G 6 .   ? -14.160 0.558   42.853  1.00   28.66 ? 589 HOH A O   1 
HETATM 2444 O  O   . HOH G 6 .   ? 3.750   -15.799 -6.811  1.00   31.11 ? 590 HOH A O   1 
HETATM 2445 O  O   . HOH G 6 .   ? -17.845 -22.107 5.978   1.00   20.72 ? 591 HOH A O   1 
HETATM 2446 O  O   . HOH G 6 .   ? -6.201  -23.554 27.773  1.00   28.42 ? 592 HOH A O   1 
HETATM 2447 O  O   . HOH G 6 .   ? -13.609 -0.874  -6.101  1.00   27.20 ? 593 HOH A O   1 
HETATM 2448 O  O   . HOH G 6 .   ? -16.333 16.559  26.648  1.00   28.20 ? 594 HOH A O   1 
HETATM 2449 O  O   . HOH G 6 .   ? 7.319   -3.865  -10.533 1.00   32.92 ? 595 HOH A O   1 
HETATM 2450 O  O   . HOH G 6 .   ? 11.932  -6.554  7.991   1.00   27.36 ? 596 HOH A O   1 
HETATM 2451 O  O   . HOH G 6 .   ? 2.853   -14.622 1.611   1.00   22.25 ? 597 HOH A O   1 
HETATM 2452 O  O   . HOH G 6 .   ? -16.675 -14.906 28.827  1.00   27.51 ? 598 HOH A O   1 
HETATM 2453 O  O   . HOH G 6 .   ? 5.861   -14.381 9.024   1.00   35.54 ? 599 HOH A O   1 
HETATM 2454 O  O   . HOH G 6 .   ? -23.641 8.178   3.610   1.00   24.54 ? 600 HOH A O   1 
HETATM 2455 O  O   . HOH G 6 .   ? -4.768  -7.291  38.089  1.00   27.97 ? 601 HOH A O   1 
HETATM 2456 O  O   . HOH G 6 .   ? 1.511   -17.814 7.240   1.00   31.33 ? 602 HOH A O   1 
HETATM 2457 O  O   . HOH G 6 .   ? -22.132 -14.165 18.738  1.00   28.86 ? 603 HOH A O   1 
HETATM 2458 O  O   . HOH G 6 .   ? -15.217 -20.088 23.170  1.00   29.04 ? 604 HOH A O   1 
HETATM 2459 O  O   . HOH G 6 .   ? 2.779   1.215   -6.253  1.00   24.30 ? 605 HOH A O   1 
HETATM 2460 O  O   . HOH G 6 .   ? -10.598 13.250  8.626   1.00   28.88 ? 606 HOH A O   1 
HETATM 2461 O  O   . HOH G 6 .   ? -5.889  -18.204 3.589   1.00   27.57 ? 607 HOH A O   1 
HETATM 2462 O  O   . HOH G 6 .   ? -1.909  -21.786 25.760  1.00   36.39 ? 608 HOH A O   1 
HETATM 2463 O  O   . HOH G 6 .   ? -27.940 6.223   21.742  1.00   24.63 ? 609 HOH A O   1 
HETATM 2464 O  O   . HOH G 6 .   ? -2.604  -19.371 21.466  1.00   22.94 ? 610 HOH A O   1 
HETATM 2465 O  O   . HOH G 6 .   ? 1.451   3.214   -4.928  1.00   30.02 ? 611 HOH A O   1 
HETATM 2466 O  O   . HOH G 6 .   ? -0.161  -2.596  39.611  1.00   42.46 ? 612 HOH A O   1 
HETATM 2467 O  O   . HOH G 6 .   ? -20.098 -25.376 18.989  1.00   26.86 ? 613 HOH A O   1 
HETATM 2468 O  O   . HOH G 6 .   ? -19.922 -4.392  41.456  1.00   31.65 ? 614 HOH A O   1 
HETATM 2469 O  O   . HOH G 6 .   ? 6.439   -5.877  6.693   1.00   31.16 ? 615 HOH A O   1 
HETATM 2470 O  O   . HOH G 6 .   ? 3.276   -13.927 12.787  1.00   31.90 ? 616 HOH A O   1 
HETATM 2471 O  O   . HOH G 6 .   ? -7.337  14.930  31.489  1.00   25.52 ? 617 HOH A O   1 
HETATM 2472 O  O   . HOH G 6 .   ? -28.191 5.475   19.125  1.00   26.53 ? 618 HOH A O   1 
HETATM 2473 O  O   . HOH G 6 .   ? -19.450 20.490  5.243   1.00   28.88 ? 619 HOH A O   1 
HETATM 2474 O  O   . HOH G 6 .   ? -18.065 -12.097 31.739  1.00   26.54 ? 620 HOH A O   1 
HETATM 2475 O  O   . HOH G 6 .   ? 5.585   -12.934 11.196  1.00   30.80 ? 621 HOH A O   1 
HETATM 2476 O  O   . HOH G 6 .   ? -14.807 5.615   37.100  1.00   24.18 ? 622 HOH A O   1 
HETATM 2477 O  O   . HOH G 6 .   ? 12.240  -7.310  -4.866  1.00   29.60 ? 623 HOH A O   1 
HETATM 2478 O  O   . HOH G 6 .   ? 1.777   -15.362 -5.133  1.00   38.55 ? 624 HOH A O   1 
HETATM 2479 O  O   . HOH G 6 .   ? -24.047 -2.907  29.173  1.00   29.41 ? 625 HOH A O   1 
HETATM 2480 O  O   . HOH G 6 .   ? 1.357   -16.219 4.875   1.00   27.45 ? 626 HOH A O   1 
HETATM 2481 O  O   . HOH G 6 .   ? -5.321  -13.756 38.525  1.00   25.73 ? 627 HOH A O   1 
HETATM 2482 O  O   . HOH G 6 .   ? -25.708 -9.020  11.253  1.00   24.78 ? 628 HOH A O   1 
HETATM 2483 O  O   . HOH G 6 .   ? -25.217 8.548   26.099  1.00   28.44 ? 629 HOH A O   1 
HETATM 2484 O  O   . HOH G 6 .   ? -6.319  -11.623 36.713  1.00   34.58 ? 630 HOH A O   1 
HETATM 2485 O  O   . HOH G 6 .   ? 6.634   -0.476  -1.173  1.00   37.09 ? 631 HOH A O   1 
HETATM 2486 O  O   . HOH G 6 .   ? 6.481   8.348   18.092  1.00   32.82 ? 632 HOH A O   1 
HETATM 2487 O  O   . HOH G 6 .   ? -16.721 -17.741 24.288  1.00   23.84 ? 633 HOH A O   1 
HETATM 2488 O  O   . HOH G 6 .   ? -3.993  -15.677 -2.005  1.00   34.51 ? 634 HOH A O   1 
HETATM 2489 O  O   . HOH G 6 .   ? 0.266   -21.904 17.522  1.00   33.34 ? 635 HOH A O   1 
HETATM 2490 O  O   . HOH G 6 .   ? -11.474 0.911   -7.740  1.00   34.67 ? 636 HOH A O   1 
HETATM 2491 O  O   . HOH G 6 .   ? -28.124 -1.515  28.440  1.00   32.38 ? 637 HOH A O   1 
HETATM 2492 O  O   . HOH G 6 .   ? 0.012   12.585  30.527  1.00   74.34 ? 638 HOH A O   1 
HETATM 2493 O  O   . HOH G 6 .   ? 4.016   -13.417 21.526  1.00   40.08 ? 639 HOH A O   1 
HETATM 2494 O  O   . HOH G 6 .   ? 8.873   -11.587 6.781   1.00   32.87 ? 640 HOH A O   1 
HETATM 2495 O  O   . HOH G 6 .   ? 5.430   -10.919 19.177  1.00   35.07 ? 641 HOH A O   1 
HETATM 2496 O  O   . HOH G 6 .   ? 9.995   -2.719  13.881  1.00   25.75 ? 642 HOH A O   1 
HETATM 2497 O  O   . HOH G 6 .   ? -16.999 -14.189 37.763  1.00   29.94 ? 643 HOH A O   1 
HETATM 2498 O  O   . HOH G 6 .   ? -19.984 -2.301  43.137  1.00   35.03 ? 644 HOH A O   1 
HETATM 2499 O  O   . HOH G 6 .   ? -17.028 -1.073  40.369  1.00   31.17 ? 645 HOH A O   1 
HETATM 2500 O  O   . HOH G 6 .   ? -20.721 8.080   30.142  1.00   23.43 ? 646 HOH A O   1 
HETATM 2501 O  O   . HOH G 6 .   ? -25.945 7.954   6.235   1.00   31.25 ? 647 HOH A O   1 
HETATM 2502 O  O   . HOH G 6 .   ? -25.662 4.365   3.981   1.00   39.48 ? 648 HOH A O   1 
HETATM 2503 O  O   . HOH G 6 .   ? -24.256 -0.103  1.221   1.00   33.42 ? 649 HOH A O   1 
HETATM 2504 O  O   . HOH G 6 .   ? -20.487 13.866  28.911  1.00   35.36 ? 650 HOH A O   1 
HETATM 2505 O  O   . HOH G 6 .   ? -7.738  -19.029 30.684  1.00   25.39 ? 651 HOH A O   1 
HETATM 2506 O  O   . HOH G 6 .   ? 0.894   14.828  24.355  1.00   30.21 ? 652 HOH A O   1 
HETATM 2507 O  O   . HOH G 6 .   ? 2.446   12.811  20.324  1.00   32.54 ? 653 HOH A O   1 
HETATM 2508 O  O   . HOH G 6 .   ? -25.862 -15.322 8.066   1.00   29.82 ? 654 HOH A O   1 
HETATM 2509 O  O   . HOH G 6 .   ? -21.002 -4.447  -3.365  1.00   41.50 ? 655 HOH A O   1 
HETATM 2510 O  O   . HOH G 6 .   ? -20.996 -6.987  -2.045  1.00   64.11 ? 656 HOH A O   1 
HETATM 2511 O  O   . HOH G 6 .   ? -10.116 6.024   -4.104  1.00   35.78 ? 657 HOH A O   1 
HETATM 2512 O  O   . HOH G 6 .   ? -27.266 -6.794  7.849   1.00   38.54 ? 658 HOH A O   1 
HETATM 2513 O  O   . HOH G 6 .   ? 1.389   4.981   12.100  1.00   28.14 ? 659 HOH A O   1 
HETATM 2514 O  O   . HOH G 6 .   ? 6.388   -5.521  3.620   1.00   29.19 ? 660 HOH A O   1 
HETATM 2515 O  O   . HOH G 6 .   ? 7.450   -7.907  -0.856  1.00   31.15 ? 661 HOH A O   1 
HETATM 2516 O  O   . HOH G 6 .   ? 9.659   -5.057  -8.078  1.00   33.37 ? 662 HOH A O   1 
HETATM 2517 O  O   . HOH G 6 .   ? 4.148   -11.590 23.328  1.00   37.60 ? 663 HOH A O   1 
HETATM 2518 O  O   . HOH G 6 .   ? 3.090   6.460   32.155  1.00   35.21 ? 664 HOH A O   1 
HETATM 2519 O  O   . HOH G 6 .   ? -10.170 15.174  5.654   1.00   33.36 ? 665 HOH A O   1 
HETATM 2520 O  O   . HOH G 6 .   ? -23.776 -3.589  3.924   1.00   31.73 ? 666 HOH A O   1 
HETATM 2521 O  O   . HOH G 6 .   ? -5.042  -9.723  33.550  1.00   26.49 ? 667 HOH A O   1 
HETATM 2522 O  O   . HOH G 6 .   ? -2.249  16.291  12.279  1.00   32.98 ? 668 HOH A O   1 
HETATM 2523 O  O   . HOH G 6 .   ? -25.667 -3.114  33.368  1.00   33.35 ? 669 HOH A O   1 
HETATM 2524 O  O   . HOH G 6 .   ? -23.005 -14.906 16.157  1.00   29.26 ? 670 HOH A O   1 
HETATM 2525 O  O   . HOH G 6 .   ? 3.917   4.384   10.644  1.00   39.05 ? 671 HOH A O   1 
HETATM 2526 O  O   . HOH G 6 .   ? -0.840  -17.520 18.175  1.00   27.09 ? 672 HOH A O   1 
HETATM 2527 O  O   . HOH G 6 .   ? -15.464 -10.342 37.498  1.00   33.49 ? 673 HOH A O   1 
HETATM 2528 O  O   . HOH G 6 .   ? -16.341 -15.698 32.947  1.00   32.80 ? 674 HOH A O   1 
HETATM 2529 O  O   . HOH G 6 .   ? -23.721 20.022  10.319  1.00   36.10 ? 675 HOH A O   1 
HETATM 2530 O  O   . HOH G 6 .   ? -1.217  -6.118  36.618  1.00   28.08 ? 676 HOH A O   1 
HETATM 2531 O  O   . HOH G 6 .   ? -1.013  18.479  22.161  1.00   42.47 ? 677 HOH A O   1 
HETATM 2532 O  O   . HOH G 6 .   ? -3.262  -17.904 -0.016  1.00   31.27 ? 678 HOH A O   1 
HETATM 2533 O  O   . HOH G 6 .   ? 10.165  6.730   15.364  1.00   37.57 ? 679 HOH A O   1 
HETATM 2534 O  O   . HOH G 6 .   ? 7.783   -1.143  -5.496  1.00   34.02 ? 680 HOH A O   1 
HETATM 2535 O  O   . HOH G 6 .   ? -24.662 13.479  20.216  1.00   35.55 ? 681 HOH A O   1 
HETATM 2536 O  O   . HOH G 6 .   ? -27.362 -5.491  27.488  1.00   34.69 ? 682 HOH A O   1 
HETATM 2537 O  O   . HOH G 6 .   ? -17.516 5.635   35.002  1.00   35.56 ? 683 HOH A O   1 
HETATM 2538 O  O   . HOH G 6 .   ? -29.934 3.862   27.506  1.00   32.30 ? 684 HOH A O   1 
HETATM 2539 O  O   . HOH G 6 .   ? 11.220  -3.913  7.746   1.00   35.54 ? 685 HOH A O   1 
HETATM 2540 O  O   . HOH G 6 .   ? 12.711  -4.418  4.423   1.00   39.99 ? 686 HOH A O   1 
HETATM 2541 O  O   . HOH G 6 .   ? 12.888  -3.882  13.465  1.00   29.19 ? 687 HOH A O   1 
HETATM 2542 O  O   . HOH G 6 .   ? 9.352   1.794   12.012  1.00   27.28 ? 688 HOH A O   1 
HETATM 2543 O  O   . HOH G 6 .   ? 10.150  5.713   13.022  1.00   37.85 ? 689 HOH A O   1 
HETATM 2544 O  O   . HOH G 6 .   ? -9.330  11.264  -0.626  1.00   35.87 ? 690 HOH A O   1 
HETATM 2545 O  O   . HOH G 6 .   ? 1.445   8.175   28.270  1.00   29.71 ? 691 HOH A O   1 
HETATM 2546 O  O   . HOH G 6 .   ? -23.765 -0.283  31.959  1.00   32.30 ? 692 HOH A O   1 
HETATM 2547 O  O   . HOH G 6 .   ? -12.312 4.256   35.147  1.00   24.37 ? 693 HOH A O   1 
HETATM 2548 O  O   . HOH G 6 .   ? -7.359  -10.256 -4.418  1.00   30.77 ? 694 HOH A O   1 
HETATM 2549 O  O   . HOH G 6 .   ? -5.648  -12.355 -5.070  1.00   30.31 ? 695 HOH A O   1 
HETATM 2550 O  O   . HOH G 6 .   ? 1.446   12.739  17.598  1.00   29.75 ? 696 HOH A O   1 
HETATM 2551 O  O   . HOH G 6 .   ? 9.385   7.331   18.015  1.00   33.45 ? 697 HOH A O   1 
HETATM 2552 O  O   . HOH G 6 .   ? -5.389  -13.467 34.484  1.00   30.10 ? 698 HOH A O   1 
HETATM 2553 O  O   . HOH G 6 .   ? -12.140 -4.286  37.746  1.00   30.95 ? 699 HOH A O   1 
HETATM 2554 O  O   . HOH G 6 .   ? -2.350  6.011   0.645   1.00   33.46 ? 700 HOH A O   1 
HETATM 2555 O  O   . HOH G 6 .   ? -1.259  4.267   2.184   1.00   35.94 ? 701 HOH A O   1 
HETATM 2556 O  O   . HOH G 6 .   ? 4.530   -0.991  -5.367  1.00   33.58 ? 702 HOH A O   1 
HETATM 2557 O  O   . HOH G 6 .   ? -22.945 15.339  19.041  1.00   31.83 ? 703 HOH A O   1 
HETATM 2558 O  O   . HOH G 6 .   ? -19.971 17.008  23.305  1.00   31.58 ? 704 HOH A O   1 
HETATM 2559 O  O   . HOH G 6 .   ? -3.608  17.767  14.128  1.00   31.61 ? 705 HOH A O   1 
HETATM 2560 O  O   . HOH G 6 .   ? -13.906 -9.086  -5.264  1.00   35.89 ? 706 HOH A O   1 
HETATM 2561 O  O   . HOH G 6 .   ? -7.067  -8.564  -6.991  1.00   35.59 ? 707 HOH A O   1 
HETATM 2562 O  O   . HOH G 6 .   ? 0.160   -6.991  -7.315  1.00   43.76 ? 708 HOH A O   1 
HETATM 2563 O  O   . HOH G 6 .   ? 5.284   -8.623  6.277   1.00   36.63 ? 709 HOH A O   1 
HETATM 2564 O  O   . HOH G 6 .   ? -13.957 -23.103 11.197  1.00   31.87 ? 710 HOH A O   1 
HETATM 2565 O  O   . HOH G 6 .   ? -0.411  -20.706 14.908  1.00   28.48 ? 711 HOH A O   1 
HETATM 2566 O  O   . HOH G 6 .   ? 1.325   -21.894 12.878  1.00   39.81 ? 712 HOH A O   1 
HETATM 2567 O  O   . HOH G 6 .   ? 4.157   -11.064 -7.380  1.00   39.03 ? 713 HOH A O   1 
HETATM 2568 O  O   . HOH G 6 .   ? -28.900 0.184   24.460  1.00   20.58 ? 714 HOH A O   1 
HETATM 2569 O  O   . HOH G 6 .   ? -28.440 1.881   22.745  1.00   23.14 ? 715 HOH A O   1 
HETATM 2570 O  O   . HOH G 6 .   ? -26.360 2.614   20.824  1.00   19.17 ? 716 HOH A O   1 
HETATM 2571 O  O   . HOH G 6 .   ? -27.828 4.032   24.013  1.00   51.44 ? 717 HOH A O   1 
HETATM 2572 O  O   . HOH G 6 .   ? -18.775 -9.046  34.538  1.00   28.18 ? 718 HOH A O   1 
HETATM 2573 O  O   . HOH G 6 .   ? 13.175  -0.583  9.714   1.00   42.57 ? 719 HOH A O   1 
HETATM 2574 O  O   . HOH G 6 .   ? -19.752 14.760  16.490  1.00   22.95 ? 720 HOH A O   1 
HETATM 2575 O  O   . HOH G 6 .   ? 5.759   0.841   8.368   1.00   29.03 ? 721 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   ? 0.2092 0.4110 0.3522 0.0068  0.0540  0.0798  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.2509 0.3242 0.3097 -0.0219 0.1303  0.0639  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.2500 0.2502 0.2578 -0.0438 0.0900  -0.0060 4   HIS A C   
4    O  O   . HIS A 4   ? 0.2360 0.2829 0.2473 -0.0020 0.0904  -0.0071 4   HIS A O   
5    C  CB  . HIS A 4   ? 0.2071 0.4760 0.2881 -0.0571 0.0542  0.0538  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.5989 0.4943 0.4485 -0.0108 0.1852  0.1331  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.5709 0.4535 0.5985 -0.1185 -0.0538 0.3219  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.2234 0.9729 1.0792 -0.2592 0.1189  -0.0465 4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.9110 0.6444 1.0995 -0.2824 -0.0167 0.0886  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.4659 0.8227 1.4313 -0.2635 0.3210  0.0610  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.1485 0.2365 0.2382 -0.0372 0.0553  0.0065  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1277 0.1796 0.1913 -0.0192 0.0381  0.0024  5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1257 0.1785 0.1597 -0.0030 0.0232  0.0043  5   TRP A C   
14   O  O   . TRP A 5   ? 0.1650 0.1966 0.1740 -0.0244 0.0331  0.0148  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1377 0.1546 0.1855 -0.0131 0.0141  -0.0142 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1255 0.1544 0.1481 -0.0258 0.0344  0.0038  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.1536 0.1641 0.1745 -0.0189 0.0366  0.0241  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1255 0.1666 0.1164 -0.0041 0.0208  -0.0020 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.1808 0.1711 0.1658 0.0012  0.0386  0.0219  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1376 0.1756 0.1375 0.0038  0.0054  0.0035  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1358 0.1606 0.1489 -0.0184 0.0322  -0.0196 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1537 0.1905 0.1343 0.0049  0.0126  -0.0104 5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1427 0.1832 0.1266 -0.0098 0.0210  -0.0344 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1586 0.1900 0.1375 -0.0080 0.0153  -0.0307 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1383 0.1532 0.1525 0.0068  0.0353  -0.0015 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1553 0.1497 0.1571 -0.0326 0.0227  -0.0131 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1220 0.1582 0.1537 0.0076  0.0340  -0.0059 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1200 0.1800 0.1571 -0.0006 0.0230  0.0006  6   GLY A O   
29   N  N   A TYR A 7   ? 0.1124 0.1445 0.1406 0.0124  0.0204  0.0076  7   TYR A N   
30   N  N   B TYR A 7   ? 0.1401 0.1648 0.2382 -0.0164 0.0953  -0.0049 7   TYR A N   
31   C  CA  A TYR A 7   ? 0.0987 0.1304 0.1403 -0.0013 -0.0335 0.0031  7   TYR A CA  
32   C  CA  B TYR A 7   ? 0.1465 0.1415 0.2279 0.0043  0.0405  -0.0027 7   TYR A CA  
33   C  C   A TYR A 7   ? 0.1268 0.1482 0.1528 -0.0092 0.0087  -0.0027 7   TYR A C   
34   C  C   B TYR A 7   ? 0.2982 0.1753 0.3084 0.0478  0.0952  -0.0281 7   TYR A C   
35   O  O   A TYR A 7   ? 0.1085 0.1427 0.1932 0.0164  -0.0115 -0.0115 7   TYR A O   
36   O  O   B TYR A 7   ? 0.2222 0.2754 0.3628 0.0322  -0.0320 0.0597  7   TYR A O   
37   C  CB  A TYR A 7   ? 0.0873 0.1132 0.1295 -0.0020 -0.0031 0.0125  7   TYR A CB  
38   C  CB  B TYR A 7   ? 0.1474 0.1779 0.1715 0.0425  0.0166  0.0119  7   TYR A CB  
39   C  CG  A TYR A 7   ? 0.0987 0.0997 0.0917 -0.0017 -0.0020 0.0241  7   TYR A CG  
40   C  CG  B TYR A 7   ? 0.1264 0.1349 0.1307 0.0017  -0.0131 -0.0261 7   TYR A CG  
41   C  CD1 A TYR A 7   ? 0.1081 0.1042 0.0972 -0.0156 0.0006  0.0104  7   TYR A CD1 
42   C  CD1 B TYR A 7   ? 0.0631 0.1436 0.1350 -0.0027 0.0151  -0.0027 7   TYR A CD1 
43   C  CD2 A TYR A 7   ? 0.0865 0.1030 0.0887 -0.0051 -0.0049 0.0170  7   TYR A CD2 
44   C  CD2 B TYR A 7   ? 0.1133 0.1431 0.1534 -0.0015 0.0071  -0.0057 7   TYR A CD2 
45   C  CE1 A TYR A 7   ? 0.0724 0.1042 0.0904 -0.0197 0.0059  0.0153  7   TYR A CE1 
46   C  CE1 B TYR A 7   ? 0.0996 0.1224 0.1295 0.0000  -0.0263 0.0000  7   TYR A CE1 
47   C  CE2 A TYR A 7   ? 0.0900 0.1260 0.0975 -0.0096 0.0164  0.0076  7   TYR A CE2 
48   C  CE2 B TYR A 7   ? 0.1542 0.1343 0.1058 0.0120  0.0051  0.0115  7   TYR A CE2 
49   C  CZ  A TYR A 7   ? 0.0923 0.0965 0.1026 -0.0109 0.0199  0.0020  7   TYR A CZ  
50   C  CZ  B TYR A 7   ? 0.1145 0.1155 0.1026 -0.0015 -0.0019 -0.0140 7   TYR A CZ  
51   O  OH  A TYR A 7   ? 0.1203 0.1008 0.0920 -0.0007 -0.0020 -0.0054 7   TYR A OH  
52   O  OH  B TYR A 7   ? 0.1298 0.1260 0.1255 -0.0020 0.0093  -0.0006 7   TYR A OH  
53   N  N   A GLY A 8   ? 0.1262 0.1961 0.3700 0.0060  0.0935  -0.0533 8   GLY A N   
54   N  N   B GLY A 8   ? 0.1247 0.2029 0.1735 0.0130  -0.0148 0.0052  8   GLY A N   
55   C  CA  A GLY A 8   ? 0.2736 0.2078 0.4248 0.0979  0.1045  -0.0170 8   GLY A CA  
56   C  CA  B GLY A 8   ? 0.1553 0.1650 0.1727 0.0087  -0.0351 -0.0192 8   GLY A CA  
57   C  C   A GLY A 8   ? 0.2260 0.3181 0.4311 0.0071  0.1519  0.0167  8   GLY A C   
58   C  C   B GLY A 8   ? 0.1343 0.1925 0.1381 0.0119  0.0085  -0.0035 8   GLY A C   
59   O  O   A GLY A 8   ? 0.1404 0.3515 0.3774 -0.0162 0.0498  0.1281  8   GLY A O   
60   O  O   B GLY A 8   ? 0.1108 0.1736 0.1463 0.0041  0.0125  -0.0388 8   GLY A O   
61   N  N   A LYS A 9   ? 0.1555 0.3499 0.6144 0.0917  0.1377  0.1101  9   LYS A N   
62   N  N   B LYS A 9   ? 0.1289 0.1781 0.1342 0.0252  -0.0264 -0.0392 9   LYS A N   
63   C  CA  A LYS A 9   ? 0.2171 0.4189 0.4447 0.0259  0.1343  0.1018  9   LYS A CA  
64   C  CA  B LYS A 9   ? 0.1537 0.1541 0.1190 0.0281  -0.0164 -0.0452 9   LYS A CA  
65   C  C   A LYS A 9   ? 0.2897 0.3619 0.3463 0.1111  0.0098  0.0218  9   LYS A C   
66   C  C   B LYS A 9   ? 0.1247 0.1703 0.1124 0.0092  0.0059  -0.0020 9   LYS A C   
67   O  O   A LYS A 9   ? 0.5641 0.6990 0.2275 0.1190  0.0041  0.0017  9   LYS A O   
68   O  O   B LYS A 9   ? 0.1352 0.1959 0.1437 0.0217  -0.0124 0.0121  9   LYS A O   
69   C  CB  A LYS A 9   ? 0.3727 0.5404 0.4828 0.1863  0.2452  0.0485  9   LYS A CB  
70   C  CB  B LYS A 9   ? 0.2461 0.1824 0.2128 0.0623  -0.0131 -0.0872 9   LYS A CB  
71   C  CG  A LYS A 9   ? 0.4377 0.5432 0.4909 0.0185  -0.1085 -0.0582 9   LYS A CG  
72   C  CG  B LYS A 9   ? 0.4097 0.1835 0.3488 0.0228  -0.0381 -0.1708 9   LYS A CG  
73   C  CD  A LYS A 9   ? 0.4029 0.6312 0.4860 -0.0581 0.0110  -0.1115 9   LYS A CD  
74   C  CD  B LYS A 9   ? 0.3508 0.2398 0.3287 0.0604  -0.0200 -0.0458 9   LYS A CD  
75   C  CE  A LYS A 9   ? 0.2933 0.3192 0.4861 -0.0520 -0.0816 -0.1580 9   LYS A CE  
76   C  CE  B LYS A 9   ? 0.3167 0.2126 0.3163 0.0381  -0.0148 -0.0164 9   LYS A CE  
77   N  NZ  A LYS A 9   ? 0.4799 0.8004 0.2845 -0.1344 -0.0604 -0.2711 9   LYS A NZ  
78   N  NZ  B LYS A 9   ? 0.3510 0.2754 0.3172 0.0081  -0.0329 0.1312  9   LYS A NZ  
79   N  N   A HIS A 10  ? 0.2466 0.2712 0.5580 0.0855  0.1656  0.0026  10  HIS A N   
80   N  N   B HIS A 10  ? 0.0939 0.1911 0.1647 0.0040  -0.0110 0.0010  10  HIS A N   
81   C  CA  A HIS A 10  ? 0.2578 0.3115 0.2881 0.0832  0.1525  0.0208  10  HIS A CA  
82   C  CA  B HIS A 10  ? 0.1343 0.1889 0.1553 -0.0104 -0.0303 -0.0500 10  HIS A CA  
83   C  C   A HIS A 10  ? 0.1421 0.2624 0.3007 -0.0092 0.0460  0.0658  10  HIS A C   
84   C  C   B HIS A 10  ? 0.1039 0.1970 0.1712 -0.0137 -0.0148 -0.0164 10  HIS A C   
85   O  O   A HIS A 10  ? 0.1367 0.1756 0.2745 0.0461  0.0781  0.0649  10  HIS A O   
86   O  O   B HIS A 10  ? 0.0702 0.1460 0.1485 0.0043  -0.0015 -0.0005 10  HIS A O   
87   C  CB  A HIS A 10  ? 0.1966 0.3014 0.2910 0.1128  0.1360  0.0063  10  HIS A CB  
88   C  CB  B HIS A 10  ? 0.0907 0.2240 0.2020 0.0331  -0.0140 -0.0221 10  HIS A CB  
89   C  CG  A HIS A 10  ? 0.2971 0.2529 0.3655 0.1066  0.1712  0.1415  10  HIS A CG  
90   C  CG  B HIS A 10  ? 0.1314 0.2137 0.1208 -0.0129 0.0129  -0.0102 10  HIS A CG  
91   N  ND1 A HIS A 10  ? 0.3373 0.2881 0.3662 0.0974  0.1203  0.0956  10  HIS A ND1 
92   N  ND1 B HIS A 10  ? 0.1543 0.1974 0.1702 0.0103  0.0012  -0.0098 10  HIS A ND1 
93   C  CD2 A HIS A 10  ? 0.3149 0.3727 0.3456 0.0843  0.1580  0.0131  10  HIS A CD2 
94   C  CD2 B HIS A 10  ? 0.1826 0.2483 0.1489 0.0015  -0.0194 -0.0436 10  HIS A CD2 
95   C  CE1 A HIS A 10  ? 0.2443 0.2680 0.3273 0.1492  0.1518  0.0912  10  HIS A CE1 
96   C  CE1 B HIS A 10  ? 0.1208 0.1858 0.1634 0.0568  0.0296  0.0010  10  HIS A CE1 
97   N  NE2 A HIS A 10  ? 0.3867 0.4253 0.4332 0.0843  0.0610  0.1316  10  HIS A NE2 
98   N  NE2 B HIS A 10  ? 0.2055 0.2152 0.1375 -0.0124 0.0163  -0.0789 10  HIS A NE2 
99   N  N   . ASN A 11  ? 0.1436 0.2031 0.2020 0.0280  0.0507  0.0013  11  ASN A N   
100  C  CA  . ASN A 11  ? 0.1358 0.1950 0.1812 0.0057  0.0487  -0.0092 11  ASN A CA  
101  C  C   . ASN A 11  ? 0.1412 0.1668 0.1719 0.0148  0.0306  0.0057  11  ASN A C   
102  O  O   . ASN A 11  ? 0.1273 0.2031 0.1736 0.0248  0.0467  -0.0005 11  ASN A O   
103  C  CB  . ASN A 11  ? 0.1225 0.1979 0.1819 0.0082  0.0674  -0.0129 11  ASN A CB  
104  C  CG  . ASN A 11  ? 0.1722 0.1905 0.1767 0.0070  0.0537  -0.0142 11  ASN A CG  
105  O  OD1 . ASN A 11  ? 0.1873 0.2398 0.2222 -0.0141 0.0434  0.0076  11  ASN A OD1 
106  N  ND2 . ASN A 11  ? 0.1976 0.2376 0.2038 -0.0194 0.0390  0.0172  11  ASN A ND2 
107  N  N   . GLY A 12  ? 0.1315 0.1982 0.1825 0.0219  0.0566  0.0057  12  GLY A N   
108  C  CA  . GLY A 12  ? 0.1172 0.2210 0.1704 0.0337  0.0467  0.0057  12  GLY A CA  
109  C  C   . GLY A 12  ? 0.1324 0.1509 0.1603 0.0124  0.0296  0.0296  12  GLY A C   
110  O  O   . GLY A 12  ? 0.1260 0.1812 0.1684 0.0231  0.0227  0.0146  12  GLY A O   
111  N  N   . PRO A 13  ? 0.1202 0.1492 0.1412 0.0082  0.0307  0.0097  13  PRO A N   
112  C  CA  . PRO A 13  ? 0.1108 0.1412 0.1578 -0.0108 0.0310  -0.0080 13  PRO A CA  
113  C  C   . PRO A 13  ? 0.1248 0.1367 0.1431 0.0063  0.0406  0.0031  13  PRO A C   
114  O  O   . PRO A 13  ? 0.1099 0.1611 0.1577 -0.0007 0.0222  -0.0062 13  PRO A O   
115  C  CB  . PRO A 13  ? 0.1342 0.1473 0.1652 -0.0171 0.0416  0.0005  13  PRO A CB  
116  C  CG  . PRO A 13  ? 0.1286 0.1458 0.1657 -0.0065 0.0381  -0.0065 13  PRO A CG  
117  C  CD  . PRO A 13  ? 0.1314 0.1749 0.1616 0.0141  0.0436  0.0006  13  PRO A CD  
118  N  N   . GLU A 14  ? 0.1501 0.1377 0.1615 0.0247  0.0137  0.0040  14  GLU A N   
119  C  CA  . GLU A 14  ? 0.2029 0.1352 0.1794 0.0178  0.0104  0.0296  14  GLU A CA  
120  C  C   . GLU A 14  ? 0.1403 0.1661 0.1679 0.0487  -0.0082 0.0006  14  GLU A C   
121  O  O   . GLU A 14  ? 0.1615 0.1791 0.1888 0.0406  0.0126  0.0159  14  GLU A O   
122  C  CB  . GLU A 14  ? 0.2831 0.1544 0.1949 0.0342  -0.0048 0.0322  14  GLU A CB  
123  C  CG  . GLU A 14  ? 0.1710 0.2404 0.2347 -0.0148 -0.0283 -0.0005 14  GLU A CG  
124  C  CD  . GLU A 14  ? 0.2193 0.2347 0.2549 0.0210  -0.0357 0.0231  14  GLU A CD  
125  O  OE1 . GLU A 14  ? 0.2222 0.2326 0.2624 0.0710  -0.0688 -0.0784 14  GLU A OE1 
126  O  OE2 . GLU A 14  ? 0.4986 0.2031 0.2444 0.0491  0.0238  -0.0219 14  GLU A OE2 
127  N  N   . HIS A 15  ? 0.1017 0.1700 0.1582 0.0198  0.0239  0.0057  15  HIS A N   
128  C  CA  . HIS A 15  ? 0.1236 0.1564 0.1805 0.0200  0.0217  -0.0074 15  HIS A CA  
129  C  C   . HIS A 15  ? 0.0926 0.1632 0.1756 0.0155  0.0324  -0.0062 15  HIS A C   
130  O  O   . HIS A 15  ? 0.0912 0.1724 0.1876 0.0131  0.0120  0.0126  15  HIS A O   
131  C  CB  . HIS A 15  ? 0.1001 0.1977 0.1932 0.0551  0.0222  0.0057  15  HIS A CB  
132  C  CG  . HIS A 15  ? 0.1333 0.2080 0.1852 0.0428  0.0003  0.0153  15  HIS A CG  
133  N  ND1 . HIS A 15  ? 0.1499 0.2540 0.2117 0.0780  -0.0059 -0.0088 15  HIS A ND1 
134  C  CD2 . HIS A 15  ? 0.1783 0.2000 0.2128 0.0571  0.0383  -0.0015 15  HIS A CD2 
135  C  CE1 . HIS A 15  ? 0.2261 0.2540 0.2207 0.1142  -0.0093 -0.0425 15  HIS A CE1 
136  N  NE2 . HIS A 15  ? 0.2542 0.2490 0.2157 0.1254  0.0307  -0.0164 15  HIS A NE2 
137  N  N   . TRP A 16  ? 0.0797 0.1435 0.1686 0.0041  0.0137  0.0031  16  TRP A N   
138  C  CA  . TRP A 16  ? 0.0627 0.1315 0.1627 0.0170  0.0120  0.0031  16  TRP A CA  
139  C  C   . TRP A 16  ? 0.0684 0.1391 0.1492 0.0177  0.0167  0.0196  16  TRP A C   
140  O  O   . TRP A 16  ? 0.0841 0.1370 0.1679 0.0043  -0.0065 0.0107  16  TRP A O   
141  C  CB  . TRP A 16  ? 0.0727 0.1409 0.1458 0.0208  0.0099  -0.0132 16  TRP A CB  
142  C  CG  . TRP A 16  ? 0.0838 0.1208 0.1300 0.0010  0.0107  -0.0093 16  TRP A CG  
143  C  CD1 . TRP A 16  ? 0.1098 0.1465 0.1248 0.0120  0.0165  -0.0003 16  TRP A CD1 
144  C  CD2 . TRP A 16  ? 0.0754 0.1142 0.1406 -0.0005 0.0178  0.0035  16  TRP A CD2 
145  N  NE1 . TRP A 16  ? 0.0865 0.1492 0.1327 0.0063  0.0198  -0.0031 16  TRP A NE1 
146  C  CE2 . TRP A 16  ? 0.0930 0.1181 0.1279 0.0098  0.0126  0.0110  16  TRP A CE2 
147  C  CE3 . TRP A 16  ? 0.0710 0.1208 0.1474 0.0068  0.0206  0.0038  16  TRP A CE3 
148  C  CZ2 . TRP A 16  ? 0.0935 0.1168 0.1307 -0.0092 0.0205  0.0093  16  TRP A CZ2 
149  C  CZ3 . TRP A 16  ? 0.0731 0.1298 0.1532 -0.0054 0.0217  -0.0040 16  TRP A CZ3 
150  C  CH2 . TRP A 16  ? 0.0851 0.1186 0.1394 0.0043  0.0182  0.0181  16  TRP A CH2 
151  N  N   . HIS A 17  ? 0.0758 0.1476 0.1393 0.0160  0.0046  -0.0006 17  HIS A N   
152  C  CA  . HIS A 17  ? 0.0754 0.1594 0.1544 0.0019  0.0049  0.0092  17  HIS A CA  
153  C  C   . HIS A 17  ? 0.0907 0.1676 0.1706 0.0148  0.0048  0.0026  17  HIS A C   
154  O  O   . HIS A 17  ? 0.0741 0.1855 0.1913 0.0065  -0.0052 -0.0085 17  HIS A O   
155  C  CB  . HIS A 17  ? 0.0772 0.1984 0.1591 0.0126  -0.0034 -0.0040 17  HIS A CB  
156  C  CG  . HIS A 17  ? 0.1084 0.2046 0.1880 0.0040  -0.0082 0.0280  17  HIS A CG  
157  N  ND1 . HIS A 17  ? 0.1347 0.2447 0.2429 0.0263  -0.0229 0.0331  17  HIS A ND1 
158  C  CD2 . HIS A 17  ? 0.1277 0.2056 0.2020 0.0395  0.0015  0.0416  17  HIS A CD2 
159  C  CE1 . HIS A 17  ? 0.1430 0.2509 0.2090 0.0671  0.0237  0.0221  17  HIS A CE1 
160  N  NE2 . HIS A 17  ? 0.1632 0.2286 0.2211 0.0617  0.0270  0.0379  17  HIS A NE2 
161  N  N   . LYS A 18  ? 0.0744 0.1800 0.1870 0.0038  0.0027  0.0057  18  LYS A N   
162  C  CA  . LYS A 18  ? 0.0718 0.2162 0.2108 -0.0175 0.0186  0.0013  18  LYS A CA  
163  C  C   . LYS A 18  ? 0.1067 0.2045 0.2065 -0.0204 -0.0076 0.0131  18  LYS A C   
164  O  O   . LYS A 18  ? 0.1498 0.2393 0.3729 -0.0322 -0.0675 0.0551  18  LYS A O   
165  C  CB  . LYS A 18  ? 0.0922 0.2246 0.2065 0.0219  0.0220  0.0331  18  LYS A CB  
166  C  CG  . LYS A 18  ? 0.1039 0.2415 0.2254 0.0310  0.0357  0.0335  18  LYS A CG  
167  C  CD  . LYS A 18  ? 0.0926 0.2461 0.2224 0.0450  0.0109  0.0478  18  LYS A CD  
168  C  CE  . LYS A 18  ? 0.1136 0.2347 0.2056 0.0322  0.0186  0.0513  18  LYS A CE  
169  N  NZ  . LYS A 18  ? 0.0945 0.2597 0.2038 0.0513  0.0165  0.0507  18  LYS A NZ  
170  N  N   . ASP A 19  ? 0.0881 0.2049 0.1941 -0.0020 0.0093  0.0197  19  ASP A N   
171  C  CA  . ASP A 19  ? 0.1347 0.2037 0.2065 -0.0020 0.0379  0.0303  19  ASP A CA  
172  C  C   . ASP A 19  ? 0.1049 0.1639 0.2161 -0.0153 0.0253  0.0261  19  ASP A C   
173  O  O   . ASP A 19  ? 0.1221 0.1713 0.2382 -0.0252 0.0342  0.0280  19  ASP A O   
174  C  CB  . ASP A 19  ? 0.1412 0.2689 0.2073 0.0252  0.0208  0.0414  19  ASP A CB  
175  C  CG  . ASP A 19  ? 0.1727 0.4090 0.3059 0.0135  0.0562  -0.0076 19  ASP A CG  
176  O  OD1 . ASP A 19  ? 0.1879 0.4733 0.3623 -0.0441 0.0851  0.0073  19  ASP A OD1 
177  O  OD2 . ASP A 19  ? 0.3260 0.5562 0.4645 -0.0399 0.0670  -0.1490 19  ASP A OD2 
178  N  N   . PHE A 20  ? 0.0890 0.1712 0.1756 -0.0115 0.0046  0.0177  20  PHE A N   
179  C  CA  . PHE A 20  ? 0.0697 0.1600 0.1782 -0.0110 0.0103  0.0052  20  PHE A CA  
180  C  C   . PHE A 20  ? 0.0882 0.1518 0.1710 -0.0046 0.0003  0.0130  20  PHE A C   
181  O  O   . PHE A 20  ? 0.1062 0.1440 0.1612 -0.0092 0.0040  0.0091  20  PHE A O   
182  C  CB  . PHE A 20  ? 0.0807 0.1632 0.1787 -0.0131 0.0131  0.0110  20  PHE A CB  
183  C  CG  . PHE A 20  ? 0.0820 0.1686 0.1861 -0.0381 0.0077  0.0086  20  PHE A CG  
184  C  CD1 . PHE A 20  ? 0.1279 0.2142 0.2249 -0.0520 0.0195  0.0531  20  PHE A CD1 
185  C  CD2 . PHE A 20  ? 0.1032 0.2108 0.1943 -0.0249 0.0108  0.0046  20  PHE A CD2 
186  C  CE1 . PHE A 20  ? 0.1351 0.2494 0.2231 -0.0344 -0.0152 0.0395  20  PHE A CE1 
187  C  CE2 . PHE A 20  ? 0.1075 0.2606 0.2297 -0.0254 -0.0003 0.0172  20  PHE A CE2 
188  C  CZ  . PHE A 20  ? 0.1036 0.2684 0.2134 -0.0675 0.0026  0.0288  20  PHE A CZ  
189  N  N   A PRO A 21  ? 0.0772 0.1718 0.1817 -0.0172 0.0015  0.0092  21  PRO A N   
190  N  N   B PRO A 21  ? 0.0798 0.1885 0.1873 -0.0153 -0.0088 0.0073  21  PRO A N   
191  C  CA  A PRO A 21  ? 0.0746 0.1999 0.1897 -0.0270 -0.0205 0.0093  21  PRO A CA  
192  C  CA  B PRO A 21  ? 0.0693 0.1887 0.1957 -0.0244 -0.0135 -0.0043 21  PRO A CA  
193  C  C   A PRO A 21  ? 0.0873 0.1552 0.1902 -0.0266 -0.0187 -0.0093 21  PRO A C   
194  C  C   B PRO A 21  ? 0.0833 0.1521 0.1720 -0.0263 -0.0164 -0.0093 21  PRO A C   
195  O  O   A PRO A 21  ? 0.0890 0.1756 0.1492 -0.0038 -0.0160 -0.0377 21  PRO A O   
196  O  O   B PRO A 21  ? 0.0794 0.1365 0.1323 -0.0060 -0.0197 -0.0208 21  PRO A O   
197  C  CB  A PRO A 21  ? 0.1066 0.1648 0.1879 -0.0296 -0.0240 0.0261  21  PRO A CB  
198  C  CB  B PRO A 21  ? 0.1080 0.1537 0.1832 -0.0189 -0.0286 0.0063  21  PRO A CB  
199  C  CG  A PRO A 21  ? 0.0942 0.1755 0.2242 -0.0414 -0.0263 -0.0076 21  PRO A CG  
200  C  CG  B PRO A 21  ? 0.1819 0.3145 0.1864 -0.0023 0.0048  -0.0189 21  PRO A CG  
201  C  CD  A PRO A 21  ? 0.1020 0.1445 0.1807 -0.0087 0.0152  0.0003  21  PRO A CD  
202  C  CD  B PRO A 21  ? 0.0920 0.2038 0.2025 -0.0315 0.0163  0.0000  21  PRO A CD  
203  N  N   . ILE A 22  ? 0.0932 0.1480 0.1722 -0.0214 -0.0131 -0.0109 22  ILE A N   
204  C  CA  . ILE A 22  ? 0.0916 0.1433 0.1537 -0.0098 0.0035  -0.0251 22  ILE A CA  
205  C  C   . ILE A 22  ? 0.1111 0.1316 0.1341 -0.0132 -0.0166 -0.0113 22  ILE A C   
206  O  O   . ILE A 22  ? 0.0944 0.1501 0.1548 -0.0063 0.0015  0.0006  22  ILE A O   
207  C  CB  . ILE A 22  ? 0.1085 0.1392 0.1544 -0.0109 -0.0040 -0.0194 22  ILE A CB  
208  C  CG1 . ILE A 22  ? 0.1164 0.1567 0.1694 -0.0024 -0.0081 -0.0350 22  ILE A CG1 
209  C  CG2 . ILE A 22  ? 0.1002 0.1544 0.1582 -0.0265 -0.0192 -0.0071 22  ILE A CG2 
210  C  CD1 . ILE A 22  ? 0.1826 0.1859 0.2390 0.0034  -0.0031 -0.0007 22  ILE A CD1 
211  N  N   . ALA A 23  ? 0.0881 0.1351 0.1479 -0.0098 -0.0110 -0.0048 23  ALA A N   
212  C  CA  . ALA A 23  ? 0.0917 0.1291 0.1624 -0.0065 0.0126  -0.0074 23  ALA A CA  
213  C  C   . ALA A 23  ? 0.0877 0.1500 0.1797 -0.0052 -0.0027 -0.0137 23  ALA A C   
214  O  O   . ALA A 23  ? 0.1112 0.1506 0.1747 -0.0166 0.0051  -0.0043 23  ALA A O   
215  C  CB  . ALA A 23  ? 0.0877 0.1483 0.1729 0.0007  0.0026  -0.0162 23  ALA A CB  
216  N  N   . LYS A 24  ? 0.1098 0.1641 0.1500 -0.0006 -0.0121 -0.0137 24  LYS A N   
217  C  CA  . LYS A 24  ? 0.0944 0.1891 0.1749 -0.0010 -0.0142 0.0035  24  LYS A CA  
218  C  C   . LYS A 24  ? 0.1430 0.1977 0.1659 -0.0156 -0.0351 0.0037  24  LYS A C   
219  O  O   . LYS A 24  ? 0.1445 0.2380 0.1776 -0.0110 -0.0377 0.0000  24  LYS A O   
220  C  CB  . LYS A 24  ? 0.1187 0.2242 0.2217 0.0218  -0.0252 0.0108  24  LYS A CB  
221  C  CG  . LYS A 24  ? 0.1453 0.2565 0.1911 0.0326  -0.0175 0.0273  24  LYS A CG  
222  C  CD  . LYS A 24  ? 0.1667 0.3352 0.2585 0.0579  0.0000  0.0315  24  LYS A CD  
223  C  CE  . LYS A 24  ? 0.2401 0.3384 0.3359 0.0344  0.0326  0.0087  24  LYS A CE  
224  N  NZ  . LYS A 24  ? 0.2170 0.3504 0.5422 0.0226  0.0322  -0.0538 24  LYS A NZ  
225  N  N   . GLY A 25  ? 0.1181 0.1765 0.1703 -0.0074 -0.0214 -0.0098 25  GLY A N   
226  C  CA  . GLY A 25  ? 0.1352 0.2101 0.1740 -0.0346 0.0219  -0.0125 25  GLY A CA  
227  C  C   . GLY A 25  ? 0.1048 0.1767 0.1427 -0.0142 -0.0208 -0.0165 25  GLY A C   
228  O  O   . GLY A 25  ? 0.1273 0.1896 0.1589 -0.0118 -0.0109 0.0000  25  GLY A O   
229  N  N   . GLU A 26  ? 0.1042 0.2011 0.1318 -0.0174 -0.0270 -0.0260 26  GLU A N   
230  C  CA  . GLU A 26  ? 0.1248 0.2108 0.1303 -0.0239 -0.0230 -0.0063 26  GLU A CA  
231  C  C   . GLU A 26  ? 0.1193 0.1738 0.1181 -0.0120 -0.0186 0.0031  26  GLU A C   
232  O  O   . GLU A 26  ? 0.1606 0.1974 0.1196 -0.0282 -0.0266 0.0085  26  GLU A O   
233  C  CB  . GLU A 26  ? 0.1500 0.2732 0.1501 -0.0478 -0.0425 -0.0631 26  GLU A CB  
234  C  CG  . GLU A 26  ? 0.1792 0.2870 0.1826 -0.0447 -0.0254 -0.0054 26  GLU A CG  
235  C  CD  . GLU A 26  ? 0.2863 0.3614 0.2560 -0.0074 -0.0863 -0.0366 26  GLU A CD  
236  O  OE1 . GLU A 26  ? 0.3433 0.4559 0.3221 -0.0458 -0.1412 0.0313  26  GLU A OE1 
237  O  OE2 . GLU A 26  ? 0.2820 0.4458 0.4162 0.0487  -0.0986 0.0188  26  GLU A OE2 
238  N  N   . ARG A 27  ? 0.1060 0.1370 0.1102 -0.0082 -0.0175 -0.0052 27  ARG A N   
239  C  CA  . ARG A 27  ? 0.0929 0.1173 0.1254 -0.0003 -0.0137 -0.0175 27  ARG A CA  
240  C  C   . ARG A 27  ? 0.0970 0.1094 0.1014 -0.0062 -0.0120 -0.0121 27  ARG A C   
241  O  O   . ARG A 27  ? 0.0923 0.1202 0.1069 -0.0023 -0.0197 -0.0043 27  ARG A O   
242  C  CB  . ARG A 27  ? 0.1914 0.1544 0.1295 0.0113  -0.0373 -0.0350 27  ARG A CB  
243  C  CG  . ARG A 27  ? 0.1710 0.2092 0.1869 -0.0298 -0.0124 -0.0038 27  ARG A CG  
244  C  CD  . ARG A 27  ? 0.2533 0.2279 0.1816 0.0832  -0.0593 0.0230  27  ARG A CD  
245  N  NE  . ARG A 27  ? 0.1733 0.1571 0.1386 -0.0137 0.0251  -0.0086 27  ARG A NE  
246  C  CZ  . ARG A 27  ? 0.1342 0.1658 0.1327 -0.0104 -0.0005 0.0154  27  ARG A CZ  
247  N  NH1 . ARG A 27  ? 0.1706 0.1923 0.1571 -0.0060 0.0153  -0.0546 27  ARG A NH1 
248  N  NH2 . ARG A 27  ? 0.1670 0.1819 0.1485 -0.0326 -0.0135 -0.0010 27  ARG A NH2 
249  N  N   . GLN A 28  ? 0.0834 0.1080 0.1010 -0.0052 -0.0035 -0.0183 28  GLN A N   
250  C  CA  . GLN A 28  ? 0.0710 0.1058 0.1017 -0.0153 -0.0020 -0.0120 28  GLN A CA  
251  C  C   . GLN A 28  ? 0.0683 0.0961 0.0895 0.0003  -0.0046 0.0027  28  GLN A C   
252  O  O   . GLN A 28  ? 0.0996 0.1085 0.0842 -0.0163 -0.0125 -0.0019 28  GLN A O   
253  C  CB  . GLN A 28  ? 0.0599 0.1236 0.1216 -0.0049 -0.0099 -0.0006 28  GLN A CB  
254  C  CG  . GLN A 28  ? 0.0785 0.1268 0.1298 -0.0104 -0.0006 0.0000  28  GLN A CG  
255  C  CD  . GLN A 28  ? 0.0631 0.1084 0.1085 -0.0097 -0.0074 -0.0132 28  GLN A CD  
256  O  OE1 . GLN A 28  ? 0.0876 0.1115 0.1182 -0.0115 -0.0012 -0.0109 28  GLN A OE1 
257  N  NE2 . GLN A 28  ? 0.0728 0.1114 0.1206 -0.0148 0.0006  -0.0060 28  GLN A NE2 
258  N  N   . SER A 29  ? 0.0732 0.0993 0.0847 -0.0013 -0.0104 -0.0110 29  SER A N   
259  C  CA  . SER A 29  ? 0.0746 0.0851 0.0948 -0.0010 -0.0057 -0.0152 29  SER A CA  
260  C  C   . SER A 29  ? 0.0675 0.0863 0.0859 -0.0003 -0.0006 0.0000  29  SER A C   
261  O  O   . SER A 29  ? 0.0768 0.0961 0.1036 -0.0082 0.0109  -0.0043 29  SER A O   
262  C  CB  . SER A 29  ? 0.0803 0.0965 0.0865 0.0043  -0.0006 -0.0148 29  SER A CB  
263  O  OG  . SER A 29  ? 0.0762 0.0900 0.0948 -0.0010 0.0024  -0.0082 29  SER A OG  
264  N  N   . PRO A 30  ? 0.0715 0.0856 0.0832 0.0003  0.0020  -0.0054 30  PRO A N   
265  C  CA  . PRO A 30  ? 0.0763 0.0894 0.0842 -0.0035 0.0057  0.0038  30  PRO A CA  
266  C  C   . PRO A 30  ? 0.0662 0.0860 0.0939 -0.0020 0.0070  -0.0040 30  PRO A C   
267  O  O   . PRO A 30  ? 0.0825 0.0979 0.0969 0.0023  -0.0052 -0.0006 30  PRO A O   
268  C  CB  . PRO A 30  ? 0.0832 0.0979 0.0860 0.0091  0.0023  -0.0115 30  PRO A CB  
269  C  CG  . PRO A 30  ? 0.0816 0.0929 0.0948 -0.0070 0.0035  0.0020  30  PRO A CG  
270  C  CD  . PRO A 30  ? 0.0856 0.0938 0.0908 -0.0046 0.0113  -0.0114 30  PRO A CD  
271  N  N   . VAL A 31  ? 0.0926 0.0900 0.0860 -0.0038 0.0077  0.0071  31  VAL A N   
272  C  CA  . VAL A 31  ? 0.0954 0.0873 0.0944 -0.0003 0.0007  0.0074  31  VAL A CA  
273  C  C   . VAL A 31  ? 0.0908 0.0930 0.0960 0.0062  0.0071  0.0107  31  VAL A C   
274  O  O   . VAL A 31  ? 0.0974 0.1069 0.1093 -0.0041 -0.0052 0.0167  31  VAL A O   
275  C  CB  . VAL A 31  ? 0.0997 0.1002 0.1036 -0.0038 -0.0093 0.0031  31  VAL A CB  
276  C  CG1 . VAL A 31  ? 0.1266 0.1105 0.1139 -0.0153 0.0054  -0.0076 31  VAL A CG1 
277  C  CG2 . VAL A 31  ? 0.0974 0.1262 0.1196 -0.0027 0.0087  -0.0003 31  VAL A CG2 
278  N  N   . ASP A 32  ? 0.0938 0.0913 0.0988 0.0043  -0.0041 0.0110  32  ASP A N   
279  C  CA  . ASP A 32  ? 0.1093 0.0900 0.1115 0.0076  0.0175  0.0087  32  ASP A CA  
280  C  C   . ASP A 32  ? 0.1036 0.0992 0.0882 0.0051  0.0046  -0.0012 32  ASP A C   
281  O  O   . ASP A 32  ? 0.1151 0.1360 0.1106 -0.0040 0.0027  -0.0120 32  ASP A O   
282  C  CB  . ASP A 32  ? 0.1309 0.0957 0.1057 0.0120  0.0020  0.0163  32  ASP A CB  
283  C  CG  . ASP A 32  ? 0.1352 0.1094 0.1108 0.0142  -0.0060 0.0244  32  ASP A CG  
284  O  OD1 . ASP A 32  ? 0.1327 0.1053 0.1236 0.0052  -0.0146 0.0164  32  ASP A OD1 
285  O  OD2 . ASP A 32  ? 0.1780 0.1315 0.1215 -0.0197 -0.0148 0.0286  32  ASP A OD2 
286  N  N   . ILE A 33  ? 0.0923 0.1030 0.0988 0.0054  0.0087  0.0110  33  ILE A N   
287  C  CA  . ILE A 33  ? 0.1023 0.0932 0.1011 0.0046  0.0062  0.0081  33  ILE A CA  
288  C  C   . ILE A 33  ? 0.1199 0.1076 0.0939 0.0197  0.0059  0.0020  33  ILE A C   
289  O  O   . ILE A 33  ? 0.1406 0.1208 0.1040 0.0013  0.0076  0.0125  33  ILE A O   
290  C  CB  . ILE A 33  ? 0.1044 0.0948 0.1184 0.0142  0.0093  0.0132  33  ILE A CB  
291  C  CG1 . ILE A 33  ? 0.1193 0.1177 0.1280 0.0142  -0.0175 0.0199  33  ILE A CG1 
292  C  CG2 . ILE A 33  ? 0.1137 0.1359 0.1366 0.0147  0.0216  0.0031  33  ILE A CG2 
293  C  CD1 . ILE A 33  ? 0.1063 0.1492 0.1465 0.0076  -0.0093 0.0280  33  ILE A CD1 
294  N  N   A ASP A 34  ? 0.1368 0.1395 0.1089 0.0283  0.0024  0.0146  34  ASP A N   
295  N  N   B ASP A 34  ? 0.1494 0.1252 0.0825 0.0313  0.0103  0.0171  34  ASP A N   
296  C  CA  A ASP A 34  ? 0.1483 0.1395 0.1049 0.0269  0.0135  0.0140  34  ASP A CA  
297  C  CA  B ASP A 34  ? 0.1579 0.1172 0.0942 0.0242  0.0141  0.0253  34  ASP A CA  
298  C  C   A ASP A 34  ? 0.1713 0.1465 0.1011 0.0388  0.0320  0.0207  34  ASP A C   
299  C  C   B ASP A 34  ? 0.1735 0.1424 0.0929 0.0219  0.0291  0.0281  34  ASP A C   
300  O  O   A ASP A 34  ? 0.1488 0.1733 0.1071 0.0012  0.0181  0.0005  34  ASP A O   
301  O  O   B ASP A 34  ? 0.1289 0.1598 0.1108 0.0136  0.0163  -0.0073 34  ASP A O   
302  C  CB  A ASP A 34  ? 0.2364 0.1564 0.1347 0.0260  -0.0315 0.0397  34  ASP A CB  
303  C  CB  B ASP A 34  ? 0.2002 0.1808 0.1245 0.0274  0.0003  0.0516  34  ASP A CB  
304  C  CG  A ASP A 34  ? 0.2134 0.1701 0.1621 -0.0073 -0.0219 0.0263  34  ASP A CG  
305  C  CG  B ASP A 34  ? 0.2806 0.1631 0.1186 0.0538  -0.0216 0.0231  34  ASP A CG  
306  O  OD1 A ASP A 34  ? 0.2081 0.2090 0.1020 0.0006  0.0035  0.0566  34  ASP A OD1 
307  O  OD1 B ASP A 34  ? 0.3088 0.1913 0.1458 0.0886  0.0197  0.0324  34  ASP A OD1 
308  O  OD2 A ASP A 34  ? 0.2847 0.2231 0.1806 0.0375  -0.0303 0.0988  34  ASP A OD2 
309  O  OD2 B ASP A 34  ? 0.2939 0.2342 0.1941 0.0597  0.0303  -0.0068 34  ASP A OD2 
310  N  N   . THR A 35  ? 0.1765 0.1503 0.1187 0.0240  0.0399  0.0403  35  THR A N   
311  C  CA  . THR A 35  ? 0.1697 0.1718 0.1155 0.0335  0.0309  0.0320  35  THR A CA  
312  C  C   . THR A 35  ? 0.2143 0.1674 0.1234 0.0469  0.0494  0.0362  35  THR A C   
313  O  O   . THR A 35  ? 0.2353 0.2140 0.1418 0.0741  0.0357  0.0502  35  THR A O   
314  C  CB  . THR A 35  ? 0.1603 0.1835 0.1588 0.0351  0.0292  0.0208  35  THR A CB  
315  O  OG1 . THR A 35  ? 0.2001 0.1984 0.1673 0.0199  0.0461  0.0353  35  THR A OG1 
316  C  CG2 . THR A 35  ? 0.2060 0.2159 0.1448 0.0588  0.0320  0.0500  35  THR A CG2 
317  N  N   . HIS A 36  ? 0.2062 0.1683 0.1155 0.0401  0.0392  0.0482  36  HIS A N   
318  C  CA  . HIS A 36  ? 0.2567 0.1819 0.1262 0.0185  0.0494  0.0597  36  HIS A CA  
319  C  C   . HIS A 36  ? 0.2619 0.2140 0.1163 0.0274  0.0351  0.0357  36  HIS A C   
320  O  O   . HIS A 36  ? 0.2458 0.2912 0.1523 0.0737  0.0120  0.0065  36  HIS A O   
321  C  CB  . HIS A 36  ? 0.3079 0.2378 0.1332 0.0310  0.0155  0.0841  36  HIS A CB  
322  C  CG  . HIS A 36  ? 0.2856 0.1749 0.1897 0.0482  0.0023  0.0504  36  HIS A CG  
323  N  ND1 . HIS A 36  ? 0.3300 0.2590 0.2110 -0.0335 -0.0296 0.0485  36  HIS A ND1 
324  C  CD2 . HIS A 36  ? 0.2998 0.2072 0.1939 0.0428  -0.0568 0.0789  36  HIS A CD2 
325  C  CE1 . HIS A 36  ? 0.4180 0.3134 0.2436 -0.0310 -0.0693 0.0178  36  HIS A CE1 
326  N  NE2 . HIS A 36  ? 0.3127 0.2784 0.3217 0.0687  -0.0054 0.0851  36  HIS A NE2 
327  N  N   A THR A 37  ? 0.2892 0.1402 0.1603 0.0478  0.0487  0.0313  37  THR A N   
328  N  N   B THR A 37  ? 0.2633 0.1728 0.1430 0.0603  0.0480  -0.0091 37  THR A N   
329  C  CA  A THR A 37  ? 0.2958 0.1738 0.1596 0.0652  0.0593  0.0048  37  THR A CA  
330  C  CA  B THR A 37  ? 0.2694 0.1791 0.1111 0.0693  0.0222  0.0566  37  THR A CA  
331  C  C   A THR A 37  ? 0.2497 0.1855 0.1614 0.0292  0.0120  0.0252  37  THR A C   
332  C  C   B THR A 37  ? 0.2089 0.1530 0.1343 0.0434  0.0091  0.0024  37  THR A C   
333  O  O   A THR A 37  ? 0.1900 0.2518 0.1724 -0.0098 -0.0126 0.0425  37  THR A O   
334  O  O   B THR A 37  ? 0.1841 0.1612 0.1251 0.0143  0.0167  -0.0027 37  THR A O   
335  C  CB  A THR A 37  ? 0.2761 0.2296 0.1886 0.0076  0.0239  -0.0309 37  THR A CB  
336  C  CB  B THR A 37  ? 0.2748 0.1535 0.1673 0.0601  0.0357  0.0617  37  THR A CB  
337  O  OG1 A THR A 37  ? 0.2666 0.3138 0.2382 0.0878  0.0722  0.0328  37  THR A OG1 
338  O  OG1 B THR A 37  ? 0.2766 0.1840 0.3009 0.0838  -0.0159 0.0821  37  THR A OG1 
339  C  CG2 A THR A 37  ? 0.2603 0.2339 0.2486 0.0261  0.0034  -0.0307 37  THR A CG2 
340  C  CG2 B THR A 37  ? 0.2628 0.2469 0.1248 0.0627  -0.0040 0.0494  37  THR A CG2 
341  N  N   . ALA A 38  ? 0.2461 0.1661 0.1102 0.0542  0.0221  0.0211  38  ALA A N   
342  C  CA  . ALA A 38  ? 0.2168 0.1562 0.1187 0.0524  0.0342  0.0291  38  ALA A CA  
343  C  C   . ALA A 38  ? 0.2011 0.1853 0.2083 0.0239  0.0285  -0.0071 38  ALA A C   
344  O  O   . ALA A 38  ? 0.3330 0.2300 0.2917 0.0109  0.1378  -0.0126 38  ALA A O   
345  C  CB  . ALA A 38  ? 0.1995 0.1585 0.1498 0.0261  -0.0013 0.0070  38  ALA A CB  
346  N  N   . LYS A 39  ? 0.2268 0.2083 0.1614 0.0758  0.0003  -0.0252 39  LYS A N   
347  C  CA  . LYS A 39  ? 0.2232 0.3027 0.1483 0.1230  0.0017  -0.0383 39  LYS A CA  
348  C  C   . LYS A 39  ? 0.1842 0.1961 0.1474 0.0364  -0.0054 -0.0285 39  LYS A C   
349  O  O   . LYS A 39  ? 0.1388 0.2108 0.1397 0.0170  0.0046  -0.0126 39  LYS A O   
350  C  CB  . LYS A 39  ? 0.2542 0.3860 0.1801 0.1014  -0.0370 -0.0542 39  LYS A CB  
351  C  CG  . LYS A 39  ? 0.3120 0.3601 0.1659 0.0731  -0.0328 -0.0099 39  LYS A CG  
352  C  CD  . LYS A 39  ? 0.3722 0.3745 0.2651 0.0776  -0.1083 -0.0172 39  LYS A CD  
353  C  CE  . LYS A 39  ? 0.4483 0.3671 0.4753 -0.0086 0.0337  -0.0273 39  LYS A CE  
354  N  NZ  . LYS A 39  ? 0.3628 0.3436 0.2087 0.0737  0.0526  0.0071  39  LYS A NZ  
355  N  N   . TYR A 40  ? 0.2432 0.2236 0.1343 0.0273  0.0182  0.0034  40  TYR A N   
356  C  CA  . TYR A 40  ? 0.1717 0.2167 0.1525 0.0063  0.0439  -0.0109 40  TYR A CA  
357  C  C   . TYR A 40  ? 0.1544 0.1959 0.1280 -0.0073 0.0388  0.0041  40  TYR A C   
358  O  O   . TYR A 40  ? 0.2153 0.2581 0.1136 0.0242  0.0251  -0.0242 40  TYR A O   
359  C  CB  . TYR A 40  ? 0.2480 0.2487 0.1800 -0.0570 0.0434  -0.0013 40  TYR A CB  
360  C  CG  . TYR A 40  ? 0.2727 0.2727 0.1596 -0.0601 0.0715  0.0103  40  TYR A CG  
361  C  CD1 . TYR A 40  ? 0.1882 0.2779 0.1900 -0.0373 0.0046  -0.0035 40  TYR A CD1 
362  C  CD2 . TYR A 40  ? 0.2421 0.3835 0.1982 0.0115  0.0776  0.0102  40  TYR A CD2 
363  C  CE1 . TYR A 40  ? 0.2186 0.3409 0.1800 -0.0456 0.0164  -0.0194 40  TYR A CE1 
364  C  CE2 . TYR A 40  ? 0.1880 0.4027 0.1864 -0.0303 0.0527  -0.0244 40  TYR A CE2 
365  C  CZ  . TYR A 40  ? 0.1905 0.4377 0.2221 -0.0241 0.0320  0.0313  40  TYR A CZ  
366  O  OH  . TYR A 40  ? 0.1879 0.5978 0.3346 0.0142  0.0277  -0.0483 40  TYR A OH  
367  N  N   . ASP A 41  ? 0.1422 0.1810 0.1280 0.0208  0.0326  -0.0076 41  ASP A N   
368  C  CA  . ASP A 41  ? 0.1404 0.1817 0.1465 -0.0060 0.0000  0.0035  41  ASP A CA  
369  C  C   . ASP A 41  ? 0.1598 0.2106 0.1719 0.0063  0.0173  -0.0141 41  ASP A C   
370  O  O   . ASP A 41  ? 0.1524 0.2304 0.1594 0.0120  0.0068  -0.0049 41  ASP A O   
371  C  CB  . ASP A 41  ? 0.1767 0.2099 0.1661 -0.0293 0.0000  -0.0227 41  ASP A CB  
372  C  CG  . ASP A 41  ? 0.1859 0.2350 0.1837 -0.0243 0.0082  -0.0294 41  ASP A CG  
373  O  OD1 . ASP A 41  ? 0.2062 0.2549 0.2020 0.0108  -0.0109 -0.0441 41  ASP A OD1 
374  O  OD2 . ASP A 41  ? 0.2211 0.2549 0.2181 -0.0436 -0.0226 -0.0315 41  ASP A OD2 
375  N  N   . PRO A 42  ? 0.1629 0.2876 0.1895 0.0307  0.0447  -0.0241 42  PRO A N   
376  C  CA  . PRO A 42  ? 0.1676 0.3095 0.2398 0.0096  0.0603  0.0167  42  PRO A CA  
377  C  C   . PRO A 42  ? 0.1844 0.2946 0.2498 0.0667  0.0612  -0.0030 42  PRO A C   
378  O  O   . PRO A 42  ? 0.2387 0.3819 0.3165 0.1005  0.0542  0.0132  42  PRO A O   
379  C  CB  . PRO A 42  ? 0.1870 0.4532 0.2730 0.0579  0.0890  -0.0248 42  PRO A CB  
380  C  CG  . PRO A 42  ? 0.2019 0.5012 0.2433 0.0403  0.0869  -0.0269 42  PRO A CG  
381  C  CD  . PRO A 42  ? 0.2486 0.3280 0.1564 0.0187  0.0794  -0.0174 42  PRO A CD  
382  N  N   . SER A 43  ? 0.2721 0.2608 0.1773 0.0344  0.0366  -0.0370 43  SER A N   
383  C  CA  . SER A 43  ? 0.2170 0.2448 0.2569 0.0263  0.0271  -0.0395 43  SER A CA  
384  C  C   . SER A 43  ? 0.2063 0.2290 0.2278 0.0502  -0.0048 -0.0043 43  SER A C   
385  O  O   . SER A 43  ? 0.3115 0.2549 0.2583 0.0925  -0.0019 -0.0019 43  SER A O   
386  C  CB  . SER A 43  ? 0.2347 0.2433 0.2987 -0.0003 0.0500  -0.0706 43  SER A CB  
387  O  OG  . SER A 43  ? 0.2545 0.2360 0.2678 0.0136  -0.0074 -0.0427 43  SER A OG  
388  N  N   . LEU A 44  ? 0.2238 0.2454 0.1826 0.0315  0.0054  -0.0172 44  LEU A N   
389  C  CA  . LEU A 44  ? 0.2020 0.2653 0.1950 0.0344  -0.0239 0.0104  44  LEU A CA  
390  C  C   . LEU A 44  ? 0.1420 0.2610 0.2741 0.0091  0.0220  -0.0023 44  LEU A C   
391  O  O   . LEU A 44  ? 0.1659 0.3944 0.3052 -0.0276 -0.0074 0.0582  44  LEU A O   
392  C  CB  . LEU A 44  ? 0.1614 0.2286 0.1779 -0.0074 0.0087  -0.0161 44  LEU A CB  
393  C  CG  . LEU A 44  ? 0.1861 0.2151 0.1537 -0.0259 -0.0147 0.0034  44  LEU A CG  
394  C  CD1 . LEU A 44  ? 0.2278 0.2101 0.1523 -0.0265 0.0194  -0.0274 44  LEU A CD1 
395  C  CD2 . LEU A 44  ? 0.1952 0.2304 0.1632 -0.0250 0.0017  0.0000  44  LEU A CD2 
396  N  N   . LYS A 45  ? 0.1670 0.2475 0.2105 0.0163  -0.0162 -0.0147 45  LYS A N   
397  C  CA  . LYS A 45  ? 0.1787 0.2407 0.2346 0.0357  0.0046  -0.0339 45  LYS A CA  
398  C  C   . LYS A 45  ? 0.1548 0.2527 0.2275 0.0441  0.0241  -0.0296 45  LYS A C   
399  O  O   . LYS A 45  ? 0.1700 0.2407 0.2325 0.0181  0.0208  -0.0357 45  LYS A O   
400  C  CB  . LYS A 45  ? 0.1661 0.2387 0.2685 0.0428  -0.0178 -0.0272 45  LYS A CB  
401  C  CG  . LYS A 45  ? 0.2617 0.3420 0.2317 0.0195  -0.0178 -0.0445 45  LYS A CG  
402  C  CD  . LYS A 45  ? 0.2301 0.3172 0.2497 0.0005  -0.0017 -0.0370 45  LYS A CD  
403  C  CE  . LYS A 45  ? 0.2307 0.2425 0.2466 -0.0052 -0.0048 -0.0013 45  LYS A CE  
404  N  NZ  . LYS A 45  ? 0.1102 0.2372 0.2569 -0.0252 -0.0031 0.0012  45  LYS A NZ  
405  N  N   . PRO A 46  ? 0.1485 0.2560 0.2518 -0.0135 0.0175  -0.0225 46  PRO A N   
406  C  CA  . PRO A 46  ? 0.1738 0.2594 0.2128 0.0189  0.0046  0.0195  46  PRO A CA  
407  C  C   . PRO A 46  ? 0.1023 0.1896 0.1794 0.0012  0.0041  -0.0093 46  PRO A C   
408  O  O   . PRO A 46  ? 0.1120 0.2074 0.2210 -0.0166 -0.0097 0.0132  46  PRO A O   
409  C  CB  . PRO A 46  ? 0.1440 0.2578 0.2527 -0.0307 0.0140  0.0230  46  PRO A CB  
410  C  CG  . PRO A 46  ? 0.1668 0.4332 0.2949 -0.0015 0.0040  -0.0535 46  PRO A CG  
411  C  CD  . PRO A 46  ? 0.1431 0.2924 0.2842 0.0368  0.0048  -0.0434 46  PRO A CD  
412  N  N   . LEU A 47  ? 0.1327 0.2332 0.2097 -0.0062 -0.0046 -0.0005 47  LEU A N   
413  C  CA  . LEU A 47  ? 0.0981 0.2211 0.2090 -0.0237 0.0057  -0.0049 47  LEU A CA  
414  C  C   . LEU A 47  ? 0.0860 0.2135 0.2459 -0.0174 -0.0166 0.0313  47  LEU A C   
415  O  O   . LEU A 47  ? 0.1166 0.2678 0.3176 -0.0581 -0.0658 0.0821  47  LEU A O   
416  C  CB  . LEU A 47  ? 0.1840 0.2894 0.2660 0.0797  0.0274  -0.0177 47  LEU A CB  
417  C  CG  . LEU A 47  ? 0.1391 0.2459 0.2790 -0.0102 -0.0199 -0.0359 47  LEU A CG  
418  C  CD1 . LEU A 47  ? 0.0920 0.2933 0.3630 -0.0535 -0.0019 -0.0142 47  LEU A CD1 
419  C  CD2 . LEU A 47  ? 0.1738 0.2283 0.3212 -0.0057 0.0208  -0.0546 47  LEU A CD2 
420  N  N   . SER A 48  ? 0.1036 0.1733 0.1616 -0.0092 -0.0082 0.0259  48  SER A N   
421  C  CA  . SER A 48  ? 0.1440 0.1869 0.1615 -0.0076 -0.0054 0.0175  48  SER A CA  
422  C  C   . SER A 48  ? 0.1298 0.1661 0.1753 -0.0295 -0.0027 0.0000  48  SER A C   
423  O  O   . SER A 48  ? 0.1225 0.1879 0.1819 -0.0368 0.0108  -0.0131 48  SER A O   
424  C  CB  . SER A 48  ? 0.1372 0.2153 0.1981 0.0087  -0.0007 0.0243  48  SER A CB  
425  O  OG  . SER A 48  ? 0.1640 0.2178 0.2337 0.0175  0.0164  0.0305  48  SER A OG  
426  N  N   . VAL A 49  ? 0.1440 0.1708 0.1676 -0.0136 0.0024  -0.0013 49  VAL A N   
427  C  CA  . VAL A 49  ? 0.1807 0.1911 0.1810 -0.0551 -0.0051 -0.0049 49  VAL A CA  
428  C  C   . VAL A 49  ? 0.1611 0.2265 0.1923 -0.0635 -0.0326 -0.0071 49  VAL A C   
429  O  O   . VAL A 49  ? 0.1722 0.3327 0.2161 -0.1098 -0.0434 0.0065  49  VAL A O   
430  C  CB  . VAL A 49  ? 0.2362 0.2328 0.1911 -0.0577 0.0287  -0.0194 49  VAL A CB  
431  C  CG1 . VAL A 49  ? 0.3255 0.2430 0.2181 -0.0526 0.0604  -0.0203 49  VAL A CG1 
432  C  CG2 . VAL A 49  ? 0.2152 0.2443 0.2766 -0.0636 0.0203  0.0003  49  VAL A CG2 
433  N  N   . SER A 50  ? 0.1615 0.2351 0.1923 -0.0604 -0.0293 0.0118  50  SER A N   
434  C  CA  . SER A 50  ? 0.1530 0.2448 0.2081 -0.0088 0.0026  0.0003  50  SER A CA  
435  C  C   . SER A 50  ? 0.1315 0.2397 0.2089 -0.0043 -0.0394 0.0000  50  SER A C   
436  O  O   . SER A 50  ? 0.1743 0.2344 0.2236 -0.0403 -0.0353 0.0164  50  SER A O   
437  C  CB  . SER A 50  ? 0.2500 0.2606 0.2508 -0.0141 -0.0320 -0.0003 50  SER A CB  
438  O  OG  . SER A 50  ? 0.2354 0.4226 0.2996 0.0074  -0.0392 -0.0188 50  SER A OG  
439  N  N   . TYR A 51  ? 0.1573 0.2090 0.2045 -0.0307 -0.0348 0.0119  51  TYR A N   
440  C  CA  . TYR A 51  ? 0.1330 0.2301 0.1959 -0.0263 -0.0471 0.0035  51  TYR A CA  
441  C  C   . TYR A 51  ? 0.1342 0.2597 0.2199 -0.0096 -0.0390 0.0322  51  TYR A C   
442  O  O   . TYR A 51  ? 0.1756 0.2750 0.2018 -0.0087 -0.0318 0.0194  51  TYR A O   
443  C  CB  . TYR A 51  ? 0.1458 0.2265 0.1947 -0.0228 -0.0452 -0.0171 51  TYR A CB  
444  C  CG  . TYR A 51  ? 0.1582 0.1867 0.1481 -0.0340 -0.0218 0.0071  51  TYR A CG  
445  C  CD1 . TYR A 51  ? 0.1352 0.1510 0.1999 -0.0192 -0.0331 0.0140  51  TYR A CD1 
446  C  CD2 . TYR A 51  ? 0.1348 0.1821 0.1659 -0.0194 -0.0060 -0.0043 51  TYR A CD2 
447  C  CE1 . TYR A 51  ? 0.1178 0.1729 0.1567 -0.0210 -0.0210 0.0065  51  TYR A CE1 
448  C  CE2 . TYR A 51  ? 0.1356 0.1641 0.1465 -0.0241 -0.0110 -0.0171 51  TYR A CE2 
449  C  CZ  . TYR A 51  ? 0.1187 0.1587 0.1449 -0.0276 -0.0126 0.0027  51  TYR A CZ  
450  O  OH  . TYR A 51  ? 0.1150 0.1483 0.1650 -0.0186 -0.0248 -0.0093 51  TYR A OH  
451  N  N   . ASP A 52  ? 0.1168 0.2908 0.2369 -0.0274 -0.0483 0.0439  52  ASP A N   
452  C  CA  . ASP A 52  ? 0.1368 0.2948 0.2592 -0.0164 -0.0568 0.0515  52  ASP A CA  
453  C  C   . ASP A 52  ? 0.1970 0.2734 0.2513 0.0104  -0.0516 0.0505  52  ASP A C   
454  O  O   . ASP A 52  ? 0.2899 0.3170 0.2748 -0.0346 -0.0982 0.0485  52  ASP A O   
455  C  CB  . ASP A 52  ? 0.1562 0.3476 0.3145 0.0504  -0.0577 0.0922  52  ASP A CB  
456  C  CG  . ASP A 52  ? 0.4372 0.5102 0.4029 0.1270  0.0189  -0.0483 52  ASP A CG  
457  O  OD1 . ASP A 52  ? 0.2696 0.5486 0.5070 0.0579  0.1080  0.1049  52  ASP A OD1 
458  O  OD2 . ASP A 52  ? 0.7638 0.6668 0.5722 0.1723  0.0250  0.2858  52  ASP A OD2 
459  N  N   . GLN A 53  ? 0.1713 0.2788 0.2865 0.0241  -0.0344 0.0586  53  GLN A N   
460  C  CA  . GLN A 53  ? 0.1761 0.2265 0.2734 0.0186  -0.0065 0.0419  53  GLN A CA  
461  C  C   . GLN A 53  ? 0.1798 0.2411 0.2238 0.0049  -0.0132 0.0152  53  GLN A C   
462  O  O   . GLN A 53  ? 0.2242 0.2260 0.2567 0.0143  -0.0082 0.0318  53  GLN A O   
463  C  CB  . GLN A 53  ? 0.2375 0.2883 0.4318 0.0533  -0.0197 -0.0049 53  GLN A CB  
464  C  CG  . GLN A 53  ? 0.3332 0.3300 0.5727 0.1092  0.0788  -0.0186 53  GLN A CG  
465  C  CD  . GLN A 53  ? 0.5867 0.5716 0.5817 0.1075  -0.0285 0.2106  53  GLN A CD  
466  O  OE1 . GLN A 53  ? 0.3291 0.6668 0.6365 0.0876  -0.1456 0.1342  53  GLN A OE1 
467  N  NE2 . GLN A 53  ? 0.7156 0.5618 0.8424 -0.0287 -0.2599 0.4390  53  GLN A NE2 
468  N  N   . ALA A 54  ? 0.1918 0.1923 0.2137 -0.0283 -0.0219 0.0020  54  ALA A N   
469  C  CA  . ALA A 54  ? 0.1579 0.1993 0.1950 -0.0263 -0.0093 -0.0171 54  ALA A CA  
470  C  C   . ALA A 54  ? 0.2020 0.1837 0.2037 -0.0299 -0.0263 -0.0155 54  ALA A C   
471  O  O   . ALA A 54  ? 0.2382 0.3194 0.2055 -0.0825 -0.0031 -0.0719 54  ALA A O   
472  C  CB  . ALA A 54  ? 0.2119 0.1986 0.2730 -0.0085 -0.0020 -0.0098 54  ALA A CB  
473  N  N   . THR A 55  ? 0.1503 0.1891 0.1729 0.0093  -0.0085 0.0041  55  THR A N   
474  C  CA  . THR A 55  ? 0.2043 0.2043 0.1808 0.0696  -0.0219 0.0170  55  THR A CA  
475  C  C   . THR A 55  ? 0.1670 0.1546 0.1200 -0.0035 -0.0324 0.0131  55  THR A C   
476  O  O   . THR A 55  ? 0.1712 0.1476 0.1591 0.0060  -0.0221 0.0298  55  THR A O   
477  C  CB  . THR A 55  ? 0.3125 0.2730 0.2651 0.0653  -0.0120 0.0785  55  THR A CB  
478  O  OG1 . THR A 55  ? 0.3131 0.2946 0.4426 0.0731  -0.1448 0.0357  55  THR A OG1 
479  C  CG2 . THR A 55  ? 0.4607 0.2845 0.2556 0.1370  -0.0260 0.0803  55  THR A CG2 
480  N  N   . SER A 56  ? 0.1693 0.1447 0.1415 0.0143  -0.0399 0.0124  56  SER A N   
481  C  CA  . SER A 56  ? 0.1921 0.1492 0.1342 0.0000  -0.0348 0.0156  56  SER A CA  
482  C  C   . SER A 56  ? 0.1763 0.1548 0.1289 0.0281  -0.0322 0.0263  56  SER A C   
483  O  O   . SER A 56  ? 0.2125 0.1632 0.1544 0.0399  -0.0483 0.0293  56  SER A O   
484  C  CB  . SER A 56  ? 0.2094 0.1433 0.1455 -0.0115 -0.0542 0.0046  56  SER A CB  
485  O  OG  . SER A 56  ? 0.2218 0.1598 0.1526 -0.0013 -0.0636 0.0236  56  SER A OG  
486  N  N   . LEU A 57  ? 0.1749 0.1295 0.1324 0.0208  -0.0227 0.0305  57  LEU A N   
487  C  CA  . LEU A 57  ? 0.2034 0.1530 0.1515 0.0109  -0.0098 0.0247  57  LEU A CA  
488  C  C   . LEU A 57  ? 0.1740 0.1542 0.1200 0.0031  -0.0092 0.0241  57  LEU A C   
489  O  O   . LEU A 57  ? 0.2140 0.1668 0.1296 0.0155  -0.0266 0.0452  57  LEU A O   
490  C  CB  . LEU A 57  ? 0.2253 0.1632 0.1853 -0.0241 0.0003  0.0390  57  LEU A CB  
491  C  CG  . LEU A 57  ? 0.3251 0.1585 0.2479 0.0186  -0.0406 -0.0027 57  LEU A CG  
492  C  CD1 . LEU A 57  ? 0.2996 0.2268 0.3018 -0.0471 -0.0489 0.0502  57  LEU A CD1 
493  C  CD2 . LEU A 57  ? 0.3235 0.2083 0.2545 0.0615  -0.0537 0.0120  57  LEU A CD2 
494  N  N   . ARG A 58  ? 0.1792 0.1553 0.1597 0.0285  -0.0248 0.0364  58  ARG A N   
495  C  CA  . ARG A 58  ? 0.1773 0.1597 0.1273 0.0003  -0.0244 0.0417  58  ARG A CA  
496  C  C   . ARG A 58  ? 0.1649 0.1571 0.0979 -0.0160 -0.0129 0.0230  58  ARG A C   
497  O  O   . ARG A 58  ? 0.1801 0.1517 0.1069 0.0104  -0.0046 0.0173  58  ARG A O   
498  C  CB  . ARG A 58  ? 0.1916 0.1819 0.1726 0.0027  -0.0074 0.0364  58  ARG A CB  
499  C  CG  . ARG A 58  ? 0.1632 0.1867 0.2002 -0.0318 0.0120  0.0474  58  ARG A CG  
500  C  CD  . ARG A 58  ? 0.2029 0.2364 0.1911 -0.0461 -0.0070 0.0443  58  ARG A CD  
501  N  NE  . ARG A 58  ? 0.1800 0.2195 0.1905 -0.0261 -0.0023 0.0342  58  ARG A NE  
502  C  CZ  . ARG A 58  ? 0.1659 0.2189 0.1424 -0.0148 0.0027  0.0394  58  ARG A CZ  
503  N  NH1 . ARG A 58  ? 0.2076 0.2257 0.1776 -0.0487 0.0137  0.0551  58  ARG A NH1 
504  N  NH2 . ARG A 58  ? 0.1967 0.1740 0.1582 -0.0214 0.0068  0.0299  58  ARG A NH2 
505  N  N   . ILE A 59  ? 0.1774 0.1395 0.1090 0.0109  -0.0148 0.0220  59  ILE A N   
506  C  CA  . ILE A 59  ? 0.1544 0.1500 0.1053 -0.0041 -0.0073 0.0377  59  ILE A CA  
507  C  C   . ILE A 59  ? 0.1553 0.1164 0.1071 0.0082  -0.0146 0.0252  59  ILE A C   
508  O  O   . ILE A 59  ? 0.1929 0.1803 0.1011 0.0159  -0.0003 0.0266  59  ILE A O   
509  C  CB  . ILE A 59  ? 0.1700 0.1322 0.1032 0.0082  -0.0177 0.0135  59  ILE A CB  
510  C  CG1 . ILE A 59  ? 0.1817 0.1386 0.1023 -0.0027 -0.0137 0.0155  59  ILE A CG1 
511  C  CG2 . ILE A 59  ? 0.2281 0.1548 0.1033 0.0137  -0.0467 0.0054  59  ILE A CG2 
512  C  CD1 . ILE A 59  ? 0.2010 0.1368 0.1307 -0.0098 -0.0097 -0.0020 59  ILE A CD1 
513  N  N   . LEU A 60  ? 0.1272 0.1230 0.1307 -0.0031 -0.0091 0.0091  60  LEU A N   
514  C  CA  . LEU A 60  ? 0.1548 0.1225 0.0984 0.0054  -0.0219 0.0252  60  LEU A CA  
515  C  C   . LEU A 60  ? 0.1388 0.1229 0.0990 -0.0073 0.0015  0.0125  60  LEU A C   
516  O  O   . LEU A 60  ? 0.1412 0.1377 0.1020 0.0057  0.0065  0.0239  60  LEU A O   
517  C  CB  . LEU A 60  ? 0.1613 0.1220 0.1641 -0.0087 -0.0088 0.0153  60  LEU A CB  
518  C  CG  . LEU A 60  ? 0.1747 0.1257 0.1519 -0.0121 -0.0057 0.0232  60  LEU A CG  
519  C  CD1 . LEU A 60  ? 0.2064 0.1509 0.1600 -0.0174 0.0076  0.0260  60  LEU A CD1 
520  C  CD2 . LEU A 60  ? 0.2010 0.1430 0.1846 -0.0217 -0.0148 -0.0137 60  LEU A CD2 
521  N  N   . ASN A 61  ? 0.1333 0.1160 0.1058 0.0010  0.0006  0.0142  61  ASN A N   
522  C  CA  . ASN A 61  ? 0.1415 0.1412 0.0972 -0.0043 0.0038  -0.0035 61  ASN A CA  
523  C  C   . ASN A 61  ? 0.1370 0.1341 0.0965 -0.0076 0.0043  0.0152  61  ASN A C   
524  O  O   . ASN A 61  ? 0.1691 0.1342 0.1211 -0.0077 0.0163  0.0218  61  ASN A O   
525  C  CB  . ASN A 61  ? 0.1731 0.1254 0.1202 0.0049  0.0165  0.0092  61  ASN A CB  
526  C  CG  . ASN A 61  ? 0.1526 0.1224 0.1054 -0.0209 0.0060  -0.0020 61  ASN A CG  
527  O  OD1 . ASN A 61  ? 0.1685 0.1406 0.1263 -0.0215 0.0015  0.0108  61  ASN A OD1 
528  N  ND2 . ASN A 61  ? 0.1940 0.1312 0.1234 -0.0159 0.0261  0.0000  61  ASN A ND2 
529  N  N   . ASN A 62  ? 0.1597 0.1282 0.0951 -0.0222 -0.0038 0.0115  62  ASN A N   
530  C  CA  . ASN A 62  ? 0.1747 0.1316 0.1298 -0.0229 -0.0070 -0.0006 62  ASN A CA  
531  C  C   . ASN A 62  ? 0.1679 0.1586 0.1243 -0.0465 0.0015  0.0059  62  ASN A C   
532  O  O   . ASN A 62  ? 0.1859 0.1882 0.1740 -0.0428 -0.0073 0.0241  62  ASN A O   
533  C  CB  . ASN A 62  ? 0.2203 0.1199 0.1632 -0.0222 -0.0142 0.0183  62  ASN A CB  
534  C  CG  . ASN A 62  ? 0.2017 0.1449 0.1196 -0.0274 -0.0030 -0.0166 62  ASN A CG  
535  O  OD1 . ASN A 62  ? 0.2019 0.1446 0.1234 -0.0270 -0.0080 0.0085  62  ASN A OD1 
536  N  ND2 . ASN A 62  ? 0.2939 0.1571 0.1887 0.0125  0.0277  -0.0035 62  ASN A ND2 
537  N  N   . GLY A 63  ? 0.1524 0.1448 0.1297 -0.0137 -0.0120 0.0146  63  GLY A N   
538  C  CA  . GLY A 63  ? 0.1664 0.1567 0.1261 -0.0148 0.0068  0.0167  63  GLY A CA  
539  C  C   . GLY A 63  ? 0.1661 0.1342 0.1634 -0.0195 -0.0109 0.0073  63  GLY A C   
540  O  O   . GLY A 63  ? 0.1810 0.1666 0.1679 -0.0065 0.0098  0.0135  63  GLY A O   
541  N  N   . HIS A 64  ? 0.1544 0.1551 0.1409 -0.0281 0.0020  0.0313  64  HIS A N   
542  C  CA  . HIS A 64  ? 0.1548 0.1704 0.1512 -0.0297 0.0068  0.0342  64  HIS A CA  
543  C  C   . HIS A 64  ? 0.1439 0.1273 0.1456 -0.0218 -0.0006 0.0281  64  HIS A C   
544  O  O   . HIS A 64  ? 0.1676 0.1888 0.2493 -0.0250 -0.0277 0.1049  64  HIS A O   
545  C  CB  . HIS A 64  ? 0.1456 0.2167 0.1758 -0.0776 0.0046  0.0087  64  HIS A CB  
546  C  CG  . HIS A 64  ? 0.2159 0.2854 0.1907 -0.0027 -0.0015 0.0035  64  HIS A CG  
547  N  ND1 . HIS A 64  ? 0.3350 0.2612 0.1738 0.0063  -0.0544 -0.0441 64  HIS A ND1 
548  C  CD2 . HIS A 64  ? 0.4257 0.2372 0.2976 -0.0577 -0.0644 -0.0046 64  HIS A CD2 
549  C  CE1 . HIS A 64  ? 0.3905 0.2879 0.3743 -0.1397 -0.0283 -0.0859 64  HIS A CE1 
550  N  NE2 . HIS A 64  ? 0.4259 0.2851 0.4180 -0.1124 -0.0104 -0.0939 64  HIS A NE2 
551  N  N   . ALA A 65  ? 0.1372 0.1336 0.1157 -0.0137 -0.0198 0.0189  65  ALA A N   
552  C  CA  . ALA A 65  ? 0.1255 0.1272 0.1163 -0.0167 -0.0093 0.0068  65  ALA A CA  
553  C  C   . ALA A 65  ? 0.1381 0.1123 0.1030 -0.0110 0.0020  0.0136  65  ALA A C   
554  O  O   . ALA A 65  ? 0.1580 0.1440 0.1150 -0.0226 0.0076  0.0186  65  ALA A O   
555  C  CB  . ALA A 65  ? 0.1625 0.1579 0.1115 -0.0162 -0.0077 0.0137  65  ALA A CB  
556  N  N   . PHE A 66  ? 0.1316 0.1154 0.0990 -0.0068 -0.0126 0.0093  66  PHE A N   
557  C  CA  . PHE A 66  ? 0.1564 0.1202 0.0923 0.0012  0.0020  0.0238  66  PHE A CA  
558  C  C   . PHE A 66  ? 0.1448 0.1194 0.0886 -0.0130 -0.0017 -0.0005 66  PHE A C   
559  O  O   . PHE A 66  ? 0.1744 0.1172 0.0908 -0.0054 0.0109  0.0071  66  PHE A O   
560  C  CB  . PHE A 66  ? 0.1700 0.1458 0.0987 0.0024  -0.0068 0.0164  66  PHE A CB  
561  C  CG  . PHE A 66  ? 0.1749 0.1295 0.0807 -0.0060 -0.0226 -0.0041 66  PHE A CG  
562  C  CD1 . PHE A 66  ? 0.1677 0.1618 0.1026 0.0040  -0.0175 -0.0035 66  PHE A CD1 
563  C  CD2 . PHE A 66  ? 0.1632 0.1512 0.0932 0.0023  -0.0024 -0.0258 66  PHE A CD2 
564  C  CE1 . PHE A 66  ? 0.1808 0.1605 0.1136 -0.0091 -0.0307 -0.0062 66  PHE A CE1 
565  C  CE2 . PHE A 66  ? 0.1897 0.1596 0.1151 -0.0269 -0.0241 -0.0242 66  PHE A CE2 
566  C  CZ  . PHE A 66  ? 0.1636 0.1746 0.1193 -0.0197 -0.0197 -0.0082 66  PHE A CZ  
567  N  N   . ASN A 67  ? 0.1377 0.1215 0.1049 -0.0010 -0.0026 0.0172  67  ASN A N   
568  C  CA  . ASN A 67  ? 0.1388 0.1187 0.0961 -0.0085 0.0065  0.0015  67  ASN A CA  
569  C  C   . ASN A 67  ? 0.1316 0.1020 0.0957 -0.0010 -0.0137 0.0136  67  ASN A C   
570  O  O   . ASN A 67  ? 0.1634 0.1347 0.0988 -0.0043 -0.0020 0.0308  67  ASN A O   
571  C  CB  . ASN A 67  ? 0.1614 0.1424 0.1141 -0.0283 -0.0142 0.0024  67  ASN A CB  
572  C  CG  . ASN A 67  ? 0.1411 0.1401 0.1537 -0.0286 -0.0183 -0.0031 67  ASN A CG  
573  O  OD1 . ASN A 67  ? 0.1763 0.1844 0.1427 -0.0351 -0.0348 0.0386  67  ASN A OD1 
574  N  ND2 . ASN A 67  ? 0.1803 0.1823 0.1941 -0.0340 -0.0427 -0.0091 67  ASN A ND2 
575  N  N   . VAL A 68  ? 0.1348 0.1085 0.1089 0.0006  -0.0051 0.0091  68  VAL A N   
576  C  CA  . VAL A 68  ? 0.1420 0.1236 0.0878 0.0303  -0.0113 0.0140  68  VAL A CA  
577  C  C   . VAL A 68  ? 0.1582 0.1234 0.1020 0.0115  -0.0186 0.0131  68  VAL A C   
578  O  O   . VAL A 68  ? 0.1582 0.1141 0.1006 0.0143  -0.0023 0.0118  68  VAL A O   
579  C  CB  . VAL A 68  ? 0.1465 0.1277 0.1324 0.0017  -0.0071 0.0000  68  VAL A CB  
580  C  CG1 . VAL A 68  ? 0.1629 0.1623 0.1383 0.0253  -0.0320 0.0010  68  VAL A CG1 
581  C  CG2 . VAL A 68  ? 0.1686 0.1377 0.1298 -0.0082 -0.0006 -0.0165 68  VAL A CG2 
582  N  N   . GLU A 69  ? 0.1657 0.1194 0.1106 0.0137  -0.0005 0.0189  69  GLU A N   
583  C  CA  . GLU A 69  ? 0.1649 0.1318 0.1032 0.0027  0.0125  0.0091  69  GLU A CA  
584  C  C   . GLU A 69  ? 0.1488 0.1112 0.1242 0.0140  -0.0262 0.0142  69  GLU A C   
585  O  O   . GLU A 69  ? 0.1655 0.1377 0.1366 0.0147  -0.0277 0.0137  69  GLU A O   
586  C  CB  . GLU A 69  ? 0.1492 0.1555 0.1677 -0.0006 0.0189  0.0242  69  GLU A CB  
587  C  CG  . GLU A 69  ? 0.1536 0.1691 0.1553 -0.0131 0.0244  0.0258  69  GLU A CG  
588  C  CD  . GLU A 69  ? 0.1609 0.1597 0.2027 0.0102  0.0162  0.0428  69  GLU A CD  
589  O  OE1 . GLU A 69  ? 0.1946 0.1905 0.1788 0.0093  0.0194  0.0432  69  GLU A OE1 
590  O  OE2 . GLU A 69  ? 0.1791 0.1977 0.2092 -0.0065 0.0210  0.0458  69  GLU A OE2 
591  N  N   . PHE A 70  ? 0.1499 0.1377 0.1132 0.0070  -0.0027 0.0126  70  PHE A N   
592  C  CA  . PHE A 70  ? 0.1455 0.1114 0.1351 0.0131  -0.0118 0.0136  70  PHE A CA  
593  C  C   . PHE A 70  ? 0.1546 0.1264 0.1384 0.0048  -0.0271 0.0173  70  PHE A C   
594  O  O   . PHE A 70  ? 0.1727 0.1264 0.1722 0.0088  -0.0181 0.0291  70  PHE A O   
595  C  CB  . PHE A 70  ? 0.1641 0.1221 0.1208 0.0027  -0.0131 0.0015  70  PHE A CB  
596  C  CG  . PHE A 70  ? 0.1546 0.1154 0.1327 0.0080  -0.0081 0.0248  70  PHE A CG  
597  C  CD1 . PHE A 70  ? 0.1729 0.1297 0.1287 0.0263  -0.0104 0.0293  70  PHE A CD1 
598  C  CD2 . PHE A 70  ? 0.1539 0.1254 0.1248 0.0124  -0.0170 0.0208  70  PHE A CD2 
599  C  CE1 . PHE A 70  ? 0.1720 0.1313 0.1422 0.0173  0.0151  0.0250  70  PHE A CE1 
600  C  CE2 . PHE A 70  ? 0.1753 0.1361 0.1314 0.0140  -0.0063 0.0140  70  PHE A CE2 
601  C  CZ  . PHE A 70  ? 0.1807 0.1280 0.1448 0.0043  -0.0017 0.0142  70  PHE A CZ  
602  N  N   . ASP A 71  ? 0.1952 0.1315 0.1860 0.0193  -0.0480 0.0375  71  ASP A N   
603  C  CA  . ASP A 71  ? 0.2081 0.1182 0.2272 0.0277  -0.0230 0.0542  71  ASP A CA  
604  C  C   . ASP A 71  ? 0.1652 0.1078 0.2608 0.0114  -0.0060 0.0421  71  ASP A C   
605  O  O   . ASP A 71  ? 0.1995 0.2029 0.3610 -0.0344 0.0364  0.0034  71  ASP A O   
606  C  CB  . ASP A 71  ? 0.2818 0.1562 0.3073 0.0342  -0.0834 0.0850  71  ASP A CB  
607  C  CG  . ASP A 71  ? 0.3449 0.1740 0.3975 0.0395  -0.1142 0.0900  71  ASP A CG  
608  O  OD1 . ASP A 71  ? 0.3393 0.1630 0.4250 0.0242  -0.0759 0.0909  71  ASP A OD1 
609  O  OD2 . ASP A 71  ? 0.3684 0.1861 0.5993 0.0000  -0.1509 0.0772  71  ASP A OD2 
610  N  N   . ASP A 72  ? 0.1792 0.1304 0.2153 0.0027  -0.0024 0.0110  72  ASP A N   
611  C  CA  . ASP A 72  ? 0.1880 0.1076 0.2400 -0.0017 0.0359  0.0146  72  ASP A CA  
612  C  C   . ASP A 72  ? 0.2517 0.1598 0.2569 -0.0303 0.0518  0.0427  72  ASP A C   
613  O  O   . ASP A 72  ? 0.3357 0.1365 0.2623 -0.0208 0.0546  -0.0167 72  ASP A O   
614  C  CB  . ASP A 72  ? 0.1973 0.1615 0.1941 -0.0085 0.0178  -0.0012 72  ASP A CB  
615  C  CG  . ASP A 72  ? 0.2229 0.2122 0.1666 0.0217  0.0163  0.0230  72  ASP A CG  
616  O  OD1 . ASP A 72  ? 0.2166 0.2671 0.1898 -0.0170 -0.0129 0.0518  72  ASP A OD1 
617  O  OD2 . ASP A 72  ? 0.2290 0.2055 0.1814 -0.0346 -0.0126 0.0000  72  ASP A OD2 
618  N  N   . SER A 73  ? 0.2408 0.1252 0.2743 -0.0087 0.0390  0.0264  73  SER A N   
619  C  CA  . SER A 73  ? 0.2666 0.1295 0.3379 -0.0255 0.0124  0.0253  73  SER A CA  
620  C  C   . SER A 73  ? 0.3048 0.1483 0.3122 -0.0240 0.0649  -0.0333 73  SER A C   
621  O  O   . SER A 73  ? 0.2926 0.1360 0.2716 0.0035  0.0074  0.0007  73  SER A O   
622  C  CB  . SER A 73  ? 0.3697 0.1676 0.3641 -0.0340 0.0082  0.0701  73  SER A CB  
623  O  OG  . SER A 73  ? 0.3278 0.1665 0.3264 0.0248  0.0658  0.0714  73  SER A OG  
624  N  N   . GLN A 74  ? 0.2718 0.1598 0.3934 0.0010  0.0847  0.0068  74  GLN A N   
625  C  CA  . GLN A 74  ? 0.2745 0.1972 0.3084 -0.0060 0.0373  0.0137  74  GLN A CA  
626  C  C   . GLN A 74  ? 0.2633 0.2469 0.2748 0.0432  0.0408  -0.0023 74  GLN A C   
627  O  O   . GLN A 74  ? 0.2372 0.1902 0.2285 -0.0219 -0.0390 0.0034  74  GLN A O   
628  C  CB  . GLN A 74  ? 0.2689 0.2574 0.3413 0.0239  -0.0142 0.0511  74  GLN A CB  
629  C  CG  . GLN A 74  ? 0.3646 0.2813 0.4217 -0.0087 0.0020  0.1004  74  GLN A CG  
630  C  CD  . GLN A 74  ? 0.3346 0.3185 0.4259 -0.0208 -0.0038 0.1393  74  GLN A CD  
631  O  OE1 . GLN A 74  ? 0.6696 0.6417 0.6366 0.0599  0.0546  -0.1729 74  GLN A OE1 
632  N  NE2 . GLN A 74  ? 0.5012 0.6697 0.7674 -0.0054 0.2205  -0.1237 74  GLN A NE2 
633  N  N   . ASP A 75  ? 0.3118 0.2727 0.2684 -0.0908 0.0516  -0.0284 75  ASP A N   
634  C  CA  . ASP A 75  ? 0.2874 0.2117 0.2583 -0.0465 -0.0148 0.0027  75  ASP A CA  
635  C  C   . ASP A 75  ? 0.2254 0.2906 0.3170 -0.0546 0.0604  -0.0807 75  ASP A C   
636  O  O   . ASP A 75  ? 0.2694 0.3400 0.4144 -0.0182 -0.0189 0.0035  75  ASP A O   
637  C  CB  . ASP A 75  ? 0.3515 0.4047 0.2389 -0.0886 0.0869  -0.0504 75  ASP A CB  
638  C  CG  . ASP A 75  ? 0.4365 0.2694 0.3740 -0.0799 0.0322  0.1259  75  ASP A CG  
639  O  OD1 . ASP A 75  ? 0.2254 0.3328 0.3623 -0.0031 -0.0463 0.1008  75  ASP A OD1 
640  O  OD2 . ASP A 75  ? 0.6581 0.6438 0.6323 0.2113  0.0522  -0.0170 75  ASP A OD2 
641  N  N   . LYS A 76  ? 0.2404 0.2231 0.2522 -0.0313 -0.0423 0.0524  76  LYS A N   
642  C  CA  . LYS A 76  ? 0.3212 0.1738 0.3158 -0.0241 -0.0060 0.0080  76  LYS A CA  
643  C  C   . LYS A 76  ? 0.5116 0.2137 0.5108 0.0649  -0.0648 0.1159  76  LYS A C   
644  O  O   . LYS A 76  ? 0.5360 0.7203 0.5364 -0.0970 -0.0987 0.0555  76  LYS A O   
645  C  CB  . LYS A 76  ? 0.3327 0.1905 0.3061 -0.0557 -0.0653 0.0405  76  LYS A CB  
646  C  CG  . LYS A 76  ? 0.5968 0.2161 0.4815 0.0208  -0.0408 0.0904  76  LYS A CG  
647  C  CD  . LYS A 76  ? 0.9139 0.2382 0.3174 -0.1516 -0.0627 0.0675  76  LYS A CD  
648  C  CE  . LYS A 76  ? 0.6412 0.5091 0.4050 -0.0207 0.1237  0.1719  76  LYS A CE  
649  N  NZ  . LYS A 76  ? 0.6154 0.5249 0.6474 0.2948  0.2267  0.3145  76  LYS A NZ  
650  N  N   . ALA A 77  ? 0.2533 0.3172 0.3215 0.0582  -0.1318 0.0379  77  ALA A N   
651  C  CA  . ALA A 77  ? 0.1765 0.2018 0.1781 -0.0003 -0.0494 0.0098  77  ALA A CA  
652  C  C   . ALA A 77  ? 0.1218 0.1819 0.1855 -0.0130 -0.0627 -0.0049 77  ALA A C   
653  O  O   . ALA A 77  ? 0.1268 0.3379 0.2806 -0.0006 -0.0340 -0.0797 77  ALA A O   
654  C  CB  . ALA A 77  ? 0.2292 0.2779 0.1395 -0.0307 -0.0392 0.0087  77  ALA A CB  
655  N  N   . VAL A 78  ? 0.1623 0.1770 0.1695 -0.0241 -0.0456 0.0104  78  VAL A N   
656  C  CA  . VAL A 78  ? 0.1861 0.1379 0.1861 -0.0076 -0.0671 0.0148  78  VAL A CA  
657  C  C   . VAL A 78  ? 0.1264 0.1412 0.1932 -0.0051 -0.0348 0.0060  78  VAL A C   
658  O  O   . VAL A 78  ? 0.1537 0.1718 0.2073 -0.0276 -0.0564 0.0230  78  VAL A O   
659  C  CB  . VAL A 78  ? 0.3203 0.1699 0.2845 0.0386  -0.0592 0.0065  78  VAL A CB  
660  C  CG1 . VAL A 78  ? 0.3212 0.1782 0.3303 -0.0305 -0.1023 0.0175  78  VAL A CG1 
661  C  CG2 . VAL A 78  ? 0.2842 0.2484 0.2890 -0.0207 -0.0463 0.0276  78  VAL A CG2 
662  N  N   . LEU A 79  ? 0.1333 0.1315 0.1445 0.0024  -0.0177 0.0017  79  LEU A N   
663  C  CA  . LEU A 79  ? 0.1181 0.1347 0.1516 -0.0010 -0.0176 0.0098  79  LEU A CA  
664  C  C   . LEU A 79  ? 0.1386 0.1341 0.1499 -0.0250 -0.0013 -0.0049 79  LEU A C   
665  O  O   . LEU A 79  ? 0.1492 0.1527 0.1618 -0.0329 0.0000  -0.0193 79  LEU A O   
666  C  CB  . LEU A 79  ? 0.1150 0.1503 0.1758 -0.0165 0.0031  0.0200  79  LEU A CB  
667  C  CG  . LEU A 79  ? 0.1151 0.1858 0.1675 0.0065  -0.0027 0.0076  79  LEU A CG  
668  C  CD1 . LEU A 79  ? 0.1177 0.1884 0.3125 -0.0194 0.0197  0.0570  79  LEU A CD1 
669  C  CD2 . LEU A 79  ? 0.1309 0.1738 0.1922 0.0173  -0.0098 -0.0013 79  LEU A CD2 
670  N  N   . LYS A 80  ? 0.1377 0.1532 0.1427 -0.0057 0.0132  -0.0054 80  LYS A N   
671  C  CA  . LYS A 80  ? 0.1544 0.1488 0.1801 -0.0148 0.0020  0.0060  80  LYS A CA  
672  C  C   . LYS A 80  ? 0.1173 0.1596 0.1659 0.0027  0.0125  0.0023  80  LYS A C   
673  O  O   . LYS A 80  ? 0.1178 0.1615 0.1898 -0.0120 -0.0043 0.0035  80  LYS A O   
674  C  CB  . LYS A 80  ? 0.2078 0.1869 0.2119 0.0320  0.0164  0.0087  80  LYS A CB  
675  C  CG  . LYS A 80  ? 0.1993 0.2020 0.2472 0.0120  0.0184  0.0472  80  LYS A CG  
676  C  CD  . LYS A 80  ? 0.2006 0.2411 0.3147 0.0173  -0.0324 0.0207  80  LYS A CD  
677  C  CE  . LYS A 80  ? 0.3273 0.3075 0.4171 0.0408  0.0065  0.0505  80  LYS A CE  
678  N  NZ  . LYS A 80  ? 0.3014 0.5906 0.5939 0.0612  -0.0350 -0.0759 80  LYS A NZ  
679  N  N   . GLY A 81  ? 0.1551 0.1837 0.1753 0.0167  0.0070  0.0017  81  GLY A N   
680  C  CA  . GLY A 81  ? 0.1643 0.1961 0.1879 0.0292  0.0509  0.0287  81  GLY A CA  
681  C  C   . GLY A 81  ? 0.1286 0.1636 0.1958 0.0113  0.0208  0.0255  81  GLY A C   
682  O  O   . GLY A 81  ? 0.1224 0.1668 0.1819 -0.0210 0.0233  -0.0126 81  GLY A O   
683  N  N   . GLY A 82  ? 0.1234 0.1826 0.2815 -0.0006 0.0195  0.0270  82  GLY A N   
684  C  CA  . GLY A 82  ? 0.1365 0.2016 0.3212 -0.0006 0.0057  0.0432  82  GLY A CA  
685  C  C   . GLY A 82  ? 0.1745 0.2010 0.2256 0.0399  0.0472  0.0242  82  GLY A C   
686  O  O   . GLY A 82  ? 0.1916 0.3179 0.2188 0.0615  0.0447  0.0252  82  GLY A O   
687  N  N   . PRO A 83  ? 0.1316 0.1643 0.2002 0.0193  0.0251  0.0203  83  PRO A N   
688  C  CA  . PRO A 83  ? 0.1810 0.1754 0.1792 0.0403  0.0372  0.0040  83  PRO A CA  
689  C  C   . PRO A 83  ? 0.1548 0.1923 0.1761 0.0395  0.0087  -0.0182 83  PRO A C   
690  O  O   . PRO A 83  ? 0.2020 0.2144 0.2045 0.0217  -0.0282 -0.0164 83  PRO A O   
691  C  CB  . PRO A 83  ? 0.1553 0.1900 0.1787 0.0406  0.0010  0.0165  83  PRO A CB  
692  C  CG  . PRO A 83  ? 0.1169 0.1736 0.1808 0.0364  -0.0017 0.0023  83  PRO A CG  
693  C  CD  . PRO A 83  ? 0.1350 0.1361 0.1913 0.0130  0.0320  0.0120  83  PRO A CD  
694  N  N   . LEU A 84  ? 0.1403 0.1560 0.1607 0.0313  0.0131  -0.0046 84  LEU A N   
695  C  CA  . LEU A 84  ? 0.1536 0.1367 0.1713 0.0165  -0.0130 -0.0310 84  LEU A CA  
696  C  C   . LEU A 84  ? 0.1422 0.1527 0.2134 0.0370  -0.0102 -0.0285 84  LEU A C   
697  O  O   . LEU A 84  ? 0.1535 0.1835 0.2272 0.0263  0.0308  -0.0427 84  LEU A O   
698  C  CB  . LEU A 84  ? 0.1154 0.1184 0.1688 0.0147  0.0192  -0.0093 84  LEU A CB  
699  C  CG  . LEU A 84  ? 0.1190 0.1224 0.1345 0.0068  0.0119  -0.0124 84  LEU A CG  
700  C  CD1 . LEU A 84  ? 0.1430 0.1467 0.1796 0.0136  0.0006  -0.0104 84  LEU A CD1 
701  C  CD2 . LEU A 84  ? 0.1072 0.1298 0.1424 0.0049  0.0195  -0.0142 84  LEU A CD2 
702  N  N   . ASP A 85  ? 0.1870 0.1476 0.1868 0.0017  -0.0049 -0.0491 85  ASP A N   
703  C  CA  . ASP A 85  ? 0.2301 0.1527 0.2290 -0.0024 0.0005  -0.0597 85  ASP A CA  
704  C  C   . ASP A 85  ? 0.1821 0.1413 0.2569 0.0164  0.0286  -0.0020 85  ASP A C   
705  O  O   . ASP A 85  ? 0.2483 0.2451 0.2565 0.0219  0.0291  -0.0275 85  ASP A O   
706  C  CB  . ASP A 85  ? 0.3517 0.1930 0.2888 -0.0254 0.0408  -0.1085 85  ASP A CB  
707  C  CG  . ASP A 85  ? 0.3864 0.4185 0.3910 -0.0784 0.1420  -0.0230 85  ASP A CG  
708  O  OD1 . ASP A 85  ? 0.3779 0.6057 0.3429 -0.1260 0.0610  -0.0195 85  ASP A OD1 
709  O  OD2 . ASP A 85  ? 0.4541 0.6140 0.7518 0.0231  0.0071  -0.1062 85  ASP A OD2 
710  N  N   . GLY A 86  ? 0.2804 0.2337 0.2632 -0.0194 -0.0777 0.0313  86  GLY A N   
711  C  CA  . GLY A 86  ? 0.2987 0.2531 0.2037 -0.0206 -0.0215 0.0165  86  GLY A CA  
712  C  C   . GLY A 86  ? 0.2903 0.2351 0.2148 -0.0568 -0.0104 -0.0197 86  GLY A C   
713  O  O   . GLY A 86  ? 0.3747 0.3045 0.2332 -0.1545 0.0097  0.0070  86  GLY A O   
714  N  N   A THR A 87  ? 0.1510 0.1409 0.1658 -0.0003 0.0038  -0.0355 87  THR A N   
715  N  N   B THR A 87  ? 0.1979 0.1746 0.2061 0.0120  0.0274  -0.0403 87  THR A N   
716  C  CA  A THR A 87  ? 0.1234 0.1094 0.1600 0.0082  0.0228  -0.0285 87  THR A CA  
717  C  CA  B THR A 87  ? 0.1667 0.2038 0.2421 0.0298  -0.0324 -0.0080 87  THR A CA  
718  C  C   A THR A 87  ? 0.1014 0.1173 0.1419 0.0098  -0.0024 -0.0120 87  THR A C   
719  C  C   B THR A 87  ? 0.1729 0.1173 0.2070 0.0121  -0.0428 -0.0241 87  THR A C   
720  O  O   A THR A 87  ? 0.1278 0.1206 0.1336 -0.0092 0.0204  -0.0060 87  THR A O   
721  O  O   B THR A 87  ? 0.1958 0.1203 0.1693 0.0076  -0.0307 -0.0185 87  THR A O   
722  C  CB  A THR A 87  ? 0.1384 0.1305 0.1911 0.0115  0.0173  -0.0135 87  THR A CB  
723  C  CB  B THR A 87  ? 0.1225 0.2236 0.2991 0.0741  -0.0412 -0.0210 87  THR A CB  
724  O  OG1 A THR A 87  ? 0.1381 0.1361 0.1913 0.0093  0.0054  0.0215  87  THR A OG1 
725  O  OG1 B THR A 87  ? 0.1934 0.3452 0.3630 0.1333  -0.0006 -0.0487 87  THR A OG1 
726  C  CG2 A THR A 87  ? 0.1428 0.1589 0.1946 0.0153  0.0227  0.0000  87  THR A CG2 
727  C  CG2 B THR A 87  ? 0.1898 0.3215 0.2962 0.0518  -0.0759 -0.0252 87  THR A CG2 
728  N  N   . TYR A 88  ? 0.0969 0.1229 0.1555 0.0110  -0.0070 -0.0120 88  TYR A N   
729  C  CA  . TYR A 88  ? 0.1060 0.1115 0.1413 -0.0054 -0.0132 -0.0153 88  TYR A CA  
730  C  C   . TYR A 88  ? 0.1178 0.1196 0.1449 -0.0049 -0.0164 -0.0143 88  TYR A C   
731  O  O   . TYR A 88  ? 0.1519 0.1763 0.1659 -0.0414 -0.0299 0.0152  88  TYR A O   
732  C  CB  . TYR A 88  ? 0.1238 0.1033 0.1272 0.0038  -0.0082 -0.0086 88  TYR A CB  
733  C  CG  . TYR A 88  ? 0.1118 0.0948 0.1334 -0.0027 0.0017  -0.0177 88  TYR A CG  
734  C  CD1 . TYR A 88  ? 0.1264 0.1266 0.1357 0.0040  -0.0052 -0.0098 88  TYR A CD1 
735  C  CD2 . TYR A 88  ? 0.1084 0.0772 0.1271 -0.0020 -0.0043 0.0005  88  TYR A CD2 
736  C  CE1 . TYR A 88  ? 0.1054 0.1215 0.1430 0.0017  0.0208  -0.0109 88  TYR A CE1 
737  C  CE2 . TYR A 88  ? 0.1033 0.0873 0.1160 0.0071  0.0034  -0.0017 88  TYR A CE2 
738  C  CZ  . TYR A 88  ? 0.1103 0.0922 0.1225 -0.0041 0.0035  -0.0109 88  TYR A CZ  
739  O  OH  . TYR A 88  ? 0.1271 0.1224 0.1233 -0.0034 -0.0006 -0.0208 88  TYR A OH  
740  N  N   . ARG A 89  ? 0.1080 0.0961 0.1273 0.0087  -0.0135 -0.0096 89  ARG A N   
741  C  CA  . ARG A 89  ? 0.1494 0.0900 0.1383 0.0177  -0.0143 0.0048  89  ARG A CA  
742  C  C   . ARG A 89  ? 0.1108 0.0834 0.0979 -0.0108 -0.0074 0.0110  89  ARG A C   
743  O  O   . ARG A 89  ? 0.1054 0.0859 0.1242 -0.0052 -0.0093 0.0074  89  ARG A O   
744  C  CB  . ARG A 89  ? 0.2006 0.0909 0.1720 0.0082  -0.0428 0.0222  89  ARG A CB  
745  C  CG  . ARG A 89  ? 0.2337 0.1449 0.1639 0.0023  -0.0206 0.0137  89  ARG A CG  
746  C  CD  . ARG A 89  ? 0.2480 0.1453 0.1658 0.0231  -0.0096 0.0140  89  ARG A CD  
747  N  NE  . ARG A 89  ? 0.2486 0.1616 0.1922 0.0020  -0.0049 0.0405  89  ARG A NE  
748  C  CZ  . ARG A 89  ? 0.2268 0.1571 0.1801 -0.0253 0.0054  0.0102  89  ARG A CZ  
749  N  NH1 . ARG A 89  ? 0.2682 0.1694 0.2468 0.0043  0.0577  0.0551  89  ARG A NH1 
750  N  NH2 . ARG A 89  ? 0.2506 0.1597 0.1914 0.0272  -0.0057 0.0281  89  ARG A NH2 
751  N  N   . LEU A 90  ? 0.1211 0.0960 0.1216 -0.0006 -0.0247 0.0104  90  LEU A N   
752  C  CA  . LEU A 90  ? 0.1316 0.0929 0.0987 -0.0082 -0.0159 0.0003  90  LEU A CA  
753  C  C   . LEU A 90  ? 0.1234 0.1121 0.1084 -0.0119 -0.0192 0.0207  90  LEU A C   
754  O  O   . LEU A 90  ? 0.1430 0.1312 0.1297 0.0137  -0.0125 0.0297  90  LEU A O   
755  C  CB  . LEU A 90  ? 0.1271 0.1090 0.1099 -0.0221 -0.0183 0.0038  90  LEU A CB  
756  C  CG  . LEU A 90  ? 0.1469 0.1187 0.1206 -0.0148 -0.0120 -0.0027 90  LEU A CG  
757  C  CD1 . LEU A 90  ? 0.1614 0.1115 0.1238 -0.0073 -0.0152 0.0003  90  LEU A CD1 
758  C  CD2 . LEU A 90  ? 0.1564 0.1568 0.1485 -0.0318 -0.0320 -0.0164 90  LEU A CD2 
759  N  N   . ILE A 91  ? 0.1273 0.0975 0.0999 -0.0102 0.0000  0.0041  91  ILE A N   
760  C  CA  . ILE A 91  ? 0.1280 0.0807 0.1072 -0.0046 -0.0013 0.0049  91  ILE A CA  
761  C  C   . ILE A 91  ? 0.1253 0.0860 0.0969 -0.0041 -0.0020 0.0159  91  ILE A C   
762  O  O   . ILE A 91  ? 0.1431 0.0930 0.1011 -0.0093 -0.0087 0.0153  91  ILE A O   
763  C  CB  . ILE A 91  ? 0.1518 0.1024 0.1111 -0.0244 0.0000  0.0203  91  ILE A CB  
764  C  CG1 . ILE A 91  ? 0.1801 0.1427 0.1351 -0.0485 -0.0005 0.0109  91  ILE A CG1 
765  C  CG2 . ILE A 91  ? 0.1473 0.1168 0.1221 -0.0151 0.0027  0.0035  91  ILE A CG2 
766  C  CD1 . ILE A 91  ? 0.2204 0.1682 0.1598 -0.0636 0.0013  -0.0065 91  ILE A CD1 
767  N  N   . GLN A 92  ? 0.1178 0.0772 0.1124 -0.0037 -0.0104 0.0172  92  GLN A N   
768  C  CA  . GLN A 92  ? 0.1278 0.0780 0.0912 0.0062  0.0020  0.0119  92  GLN A CA  
769  C  C   . GLN A 92  ? 0.1030 0.0904 0.0838 -0.0026 -0.0046 0.0137  92  GLN A C   
770  O  O   . GLN A 92  ? 0.1271 0.0832 0.0886 -0.0060 -0.0060 0.0019  92  GLN A O   
771  C  CB  . GLN A 92  ? 0.1442 0.1017 0.1114 0.0000  -0.0073 0.0164  92  GLN A CB  
772  C  CG  . GLN A 92  ? 0.1404 0.0916 0.1357 -0.0017 -0.0054 0.0219  92  GLN A CG  
773  C  CD  . GLN A 92  ? 0.1286 0.0983 0.1071 -0.0074 -0.0027 0.0115  92  GLN A CD  
774  O  OE1 . GLN A 92  ? 0.1419 0.1002 0.1154 -0.0013 -0.0125 0.0159  92  GLN A OE1 
775  N  NE2 . GLN A 92  ? 0.1333 0.1137 0.1383 -0.0063 -0.0077 0.0162  92  GLN A NE2 
776  N  N   . PHE A 93  ? 0.1112 0.0790 0.0917 -0.0006 -0.0146 0.0060  93  PHE A N   
777  C  CA  . PHE A 93  ? 0.1224 0.0877 0.0859 -0.0037 -0.0065 0.0074  93  PHE A CA  
778  C  C   . PHE A 93  ? 0.1187 0.0842 0.0754 -0.0082 -0.0113 0.0082  93  PHE A C   
779  O  O   . PHE A 93  ? 0.1327 0.1014 0.0850 0.0035  -0.0142 0.0159  93  PHE A O   
780  C  CB  . PHE A 93  ? 0.1336 0.1078 0.0825 -0.0076 -0.0207 0.0035  93  PHE A CB  
781  C  CG  . PHE A 93  ? 0.1168 0.0929 0.1005 -0.0098 -0.0143 0.0057  93  PHE A CG  
782  C  CD1 . PHE A 93  ? 0.1418 0.0929 0.1199 -0.0085 -0.0204 -0.0026 93  PHE A CD1 
783  C  CD2 . PHE A 93  ? 0.1307 0.1154 0.1075 -0.0027 -0.0281 0.0131  93  PHE A CD2 
784  C  CE1 . PHE A 93  ? 0.1418 0.1220 0.1181 -0.0065 -0.0351 -0.0175 93  PHE A CE1 
785  C  CE2 . PHE A 93  ? 0.1413 0.1233 0.1220 -0.0096 -0.0288 -0.0093 93  PHE A CE2 
786  C  CZ  . PHE A 93  ? 0.1515 0.1137 0.1264 -0.0076 -0.0329 -0.0087 93  PHE A CZ  
787  N  N   . HIS A 94  ? 0.1132 0.0803 0.0908 -0.0013 -0.0177 0.0020  94  HIS A N   
788  C  CA  . HIS A 94  ? 0.1099 0.0841 0.0876 -0.0049 -0.0038 0.0003  94  HIS A CA  
789  C  C   . HIS A 94  ? 0.0935 0.0860 0.0741 -0.0148 -0.0074 0.0003  94  HIS A C   
790  O  O   . HIS A 94  ? 0.1111 0.0793 0.0816 -0.0054 0.0038  0.0068  94  HIS A O   
791  C  CB  . HIS A 94  ? 0.1247 0.0895 0.0789 -0.0113 -0.0107 0.0030  94  HIS A CB  
792  C  CG  . HIS A 94  ? 0.1030 0.0759 0.0891 -0.0109 -0.0006 0.0035  94  HIS A CG  
793  N  ND1 . HIS A 94  ? 0.1142 0.0837 0.0865 -0.0126 -0.0107 0.0049  94  HIS A ND1 
794  C  CD2 . HIS A 94  ? 0.1044 0.0882 0.0711 -0.0115 -0.0003 -0.0017 94  HIS A CD2 
795  C  CE1 . HIS A 94  ? 0.0997 0.0812 0.0856 -0.0057 0.0006  0.0082  94  HIS A CE1 
796  N  NE2 . HIS A 94  ? 0.0909 0.0900 0.0745 -0.0034 -0.0146 0.0015  94  HIS A NE2 
797  N  N   . PHE A 95  ? 0.1115 0.0816 0.0887 -0.0104 -0.0041 0.0052  95  PHE A N   
798  C  CA  . PHE A 95  ? 0.1085 0.0816 0.0851 -0.0043 -0.0057 0.0115  95  PHE A CA  
799  C  C   . PHE A 95  ? 0.1078 0.0873 0.0790 -0.0115 -0.0027 -0.0082 95  PHE A C   
800  O  O   . PHE A 95  ? 0.1098 0.0992 0.0932 -0.0108 0.0030  0.0088  95  PHE A O   
801  C  CB  . PHE A 95  ? 0.1120 0.0927 0.0970 -0.0035 -0.0129 -0.0076 95  PHE A CB  
802  C  CG  . PHE A 95  ? 0.1118 0.0859 0.0913 -0.0068 -0.0104 -0.0115 95  PHE A CG  
803  C  CD1 . PHE A 95  ? 0.1343 0.1010 0.0984 -0.0017 -0.0186 -0.0082 95  PHE A CD1 
804  C  CD2 . PHE A 95  ? 0.1132 0.1008 0.1085 -0.0187 -0.0093 -0.0265 95  PHE A CD2 
805  C  CE1 . PHE A 95  ? 0.1400 0.1114 0.0957 -0.0017 -0.0260 -0.0148 95  PHE A CE1 
806  C  CE2 . PHE A 95  ? 0.1234 0.1090 0.1269 -0.0024 -0.0121 -0.0310 95  PHE A CE2 
807  C  CZ  . PHE A 95  ? 0.1272 0.1159 0.1111 0.0060  -0.0115 -0.0262 95  PHE A CZ  
808  N  N   . HIS A 96  ? 0.1067 0.0781 0.0697 -0.0038 -0.0085 -0.0023 96  HIS A N   
809  C  CA  . HIS A 96  ? 0.1014 0.0802 0.0799 -0.0062 0.0007  -0.0062 96  HIS A CA  
810  C  C   . HIS A 96  ? 0.0979 0.0938 0.0741 -0.0081 0.0063  0.0080  96  HIS A C   
811  O  O   . HIS A 96  ? 0.1026 0.0846 0.0963 -0.0109 0.0019  -0.0041 96  HIS A O   
812  C  CB  . HIS A 96  ? 0.1014 0.0812 0.0942 0.0000  -0.0049 -0.0082 96  HIS A CB  
813  C  CG  . HIS A 96  ? 0.0978 0.0856 0.0788 -0.0104 -0.0006 0.0006  96  HIS A CG  
814  N  ND1 . HIS A 96  ? 0.1006 0.0855 0.1208 -0.0065 0.0000  -0.0080 96  HIS A ND1 
815  C  CD2 . HIS A 96  ? 0.1081 0.0807 0.0825 -0.0104 -0.0015 -0.0126 96  HIS A CD2 
816  C  CE1 . HIS A 96  ? 0.0908 0.0891 0.1439 -0.0038 -0.0091 -0.0226 96  HIS A CE1 
817  N  NE2 . HIS A 96  ? 0.0966 0.0684 0.0838 0.0000  -0.0074 -0.0098 96  HIS A NE2 
818  N  N   . TRP A 97  ? 0.1048 0.0754 0.0856 -0.0091 0.0068  0.0000  97  TRP A N   
819  C  CA  . TRP A 97  ? 0.1080 0.0917 0.0912 -0.0068 0.0006  -0.0060 97  TRP A CA  
820  C  C   . TRP A 97  ? 0.1076 0.0824 0.0900 -0.0035 0.0054  -0.0027 97  TRP A C   
821  O  O   . TRP A 97  ? 0.1090 0.0930 0.1076 -0.0046 0.0059  0.0006  97  TRP A O   
822  C  CB  . TRP A 97  ? 0.1220 0.0916 0.0882 -0.0199 0.0024  0.0006  97  TRP A CB  
823  C  CG  . TRP A 97  ? 0.1227 0.0838 0.0843 -0.0102 -0.0121 -0.0114 97  TRP A CG  
824  C  CD1 . TRP A 97  ? 0.1175 0.1096 0.0938 -0.0137 0.0041  -0.0104 97  TRP A CD1 
825  C  CD2 . TRP A 97  ? 0.1203 0.0886 0.0860 -0.0142 -0.0006 -0.0041 97  TRP A CD2 
826  N  NE1 . TRP A 97  ? 0.1368 0.1001 0.1008 -0.0088 0.0074  -0.0068 97  TRP A NE1 
827  C  CE2 . TRP A 97  ? 0.1351 0.0932 0.0930 -0.0172 0.0109  -0.0126 97  TRP A CE2 
828  C  CE3 . TRP A 97  ? 0.1124 0.0926 0.0798 0.0031  -0.0108 -0.0035 97  TRP A CE3 
829  C  CZ2 . TRP A 97  ? 0.1272 0.1062 0.0960 -0.0170 0.0031  0.0076  97  TRP A CZ2 
830  C  CZ3 . TRP A 97  ? 0.1202 0.0938 0.0932 -0.0092 -0.0031 -0.0019 97  TRP A CZ3 
831  C  CH2 . TRP A 97  ? 0.1361 0.1039 0.0997 -0.0129 0.0003  0.0000  97  TRP A CH2 
832  N  N   . GLY A 98  ? 0.1177 0.0803 0.0948 -0.0043 0.0109  -0.0035 98  GLY A N   
833  C  CA  . GLY A 98  ? 0.1289 0.0956 0.0992 0.0057  0.0059  -0.0082 98  GLY A CA  
834  C  C   . GLY A 98  ? 0.1271 0.1011 0.1115 0.0038  0.0048  0.0082  98  GLY A C   
835  O  O   . GLY A 98  ? 0.1436 0.1017 0.1190 -0.0076 0.0017  -0.0137 98  GLY A O   
836  N  N   . SER A 99  ? 0.1474 0.0938 0.1254 0.0006  0.0107  -0.0153 99  SER A N   
837  C  CA  . SER A 99  ? 0.1456 0.0987 0.1169 -0.0030 0.0197  -0.0286 99  SER A CA  
838  C  C   . SER A 99  ? 0.1792 0.1018 0.1413 -0.0098 0.0015  -0.0414 99  SER A C   
839  O  O   . SER A 99  ? 0.2107 0.1331 0.1582 -0.0088 -0.0071 -0.0474 99  SER A O   
840  C  CB  . SER A 99  ? 0.1783 0.1196 0.1587 0.0153  0.0189  -0.0474 99  SER A CB  
841  O  OG  . SER A 99  ? 0.1519 0.1166 0.1869 0.0159  0.0151  -0.0121 99  SER A OG  
842  N  N   . LEU A 100 ? 0.1571 0.1057 0.1500 -0.0060 0.0164  -0.0137 100 LEU A N   
843  C  CA  . LEU A 100 ? 0.1959 0.0922 0.1824 0.0013  0.0414  -0.0051 100 LEU A CA  
844  C  C   . LEU A 100 ? 0.1392 0.1248 0.1582 -0.0147 0.0087  -0.0187 100 LEU A C   
845  O  O   . LEU A 100 ? 0.1576 0.1027 0.1517 -0.0120 0.0126  -0.0192 100 LEU A O   
846  C  CB  . LEU A 100 ? 0.2761 0.1817 0.2401 0.0753  0.0680  0.0177  100 LEU A CB  
847  C  CG  . LEU A 100 ? 0.3064 0.1894 0.2711 0.0627  0.0434  0.0232  100 LEU A CG  
848  C  CD1 . LEU A 100 ? 0.2606 0.3199 0.3768 0.1439  0.0639  0.0372  100 LEU A CD1 
849  C  CD2 . LEU A 100 ? 0.4449 0.2357 0.4429 -0.0142 0.2013  -0.1431 100 LEU A CD2 
850  N  N   . ASP A 101 ? 0.1379 0.1264 0.1743 -0.0038 0.0040  -0.0124 101 ASP A N   
851  C  CA  . ASP A 101 ? 0.1641 0.1093 0.1577 -0.0277 0.0093  0.0086  101 ASP A CA  
852  C  C   . ASP A 101 ? 0.1440 0.1103 0.1600 -0.0035 0.0187  0.0093  101 ASP A C   
853  O  O   . ASP A 101 ? 0.1667 0.1429 0.1657 0.0098  0.0167  0.0147  101 ASP A O   
854  C  CB  . ASP A 101 ? 0.1747 0.1483 0.1884 -0.0441 -0.0110 0.0359  101 ASP A CB  
855  C  CG  . ASP A 101 ? 0.2246 0.1528 0.2372 -0.0386 -0.0571 0.0206  101 ASP A CG  
856  O  OD1 . ASP A 101 ? 0.2011 0.1634 0.1819 -0.0307 -0.0087 0.0080  101 ASP A OD1 
857  O  OD2 . ASP A 101 ? 0.2976 0.2222 0.2531 -0.1071 -0.0621 0.0318  101 ASP A OD2 
858  N  N   . GLY A 102 ? 0.1351 0.1051 0.1573 -0.0103 0.0031  0.0093  102 GLY A N   
859  C  CA  . GLY A 102 ? 0.1524 0.1080 0.1622 -0.0034 -0.0041 0.0107  102 GLY A CA  
860  C  C   . GLY A 102 ? 0.1352 0.1024 0.1386 0.0082  0.0038  0.0093  102 GLY A C   
861  O  O   . GLY A 102 ? 0.1682 0.1157 0.1465 -0.0082 0.0174  0.0172  102 GLY A O   
862  N  N   A GLN A 103 ? 0.1215 0.0882 0.1331 -0.0151 0.0120  0.0068  103 GLN A N   
863  N  N   B GLN A 103 ? 0.1349 0.0904 0.1535 -0.0114 0.0177  0.0097  103 GLN A N   
864  C  CA  A GLN A 103 ? 0.1114 0.0869 0.1002 0.0003  0.0082  0.0003  103 GLN A CA  
865  C  CA  B GLN A 103 ? 0.1431 0.0997 0.1211 0.0043  0.0086  -0.0020 103 GLN A CA  
866  C  C   A GLN A 103 ? 0.0966 0.0798 0.1042 -0.0132 0.0120  0.0003  103 GLN A C   
867  C  C   B GLN A 103 ? 0.1005 0.0837 0.1184 -0.0074 0.0175  -0.0063 103 GLN A C   
868  O  O   A GLN A 103 ? 0.1069 0.0794 0.1066 0.0003  0.0010  -0.0013 103 GLN A O   
869  O  O   B GLN A 103 ? 0.1163 0.0939 0.1154 -0.0073 0.0161  -0.0142 103 GLN A O   
870  C  CB  A GLN A 103 ? 0.1169 0.0766 0.1076 0.0000  0.0130  -0.0252 103 GLN A CB  
871  C  CB  B GLN A 103 ? 0.1688 0.1386 0.1506 0.0599  0.0244  0.0164  103 GLN A CB  
872  C  CG  A GLN A 103 ? 0.1049 0.0972 0.0922 0.0228  0.0108  0.0119  103 GLN A CG  
873  C  CG  B GLN A 103 ? 0.1893 0.1801 0.2013 0.0142  0.0509  -0.0318 103 GLN A CG  
874  C  CD  A GLN A 103 ? 0.1106 0.0963 0.1368 0.0249  0.0491  0.0438  103 GLN A CD  
875  C  CD  B GLN A 103 ? 0.2777 0.3124 0.3688 0.0775  -0.0675 -0.0432 103 GLN A CD  
876  O  OE1 A GLN A 103 ? 0.1518 0.1553 0.1791 0.0709  0.0270  0.0483  103 GLN A OE1 
877  O  OE1 B GLN A 103 ? 0.1842 0.1719 0.2720 -0.0296 0.0154  -0.0200 103 GLN A OE1 
878  N  NE2 A GLN A 103 ? 0.0829 0.0975 0.1366 0.0282  0.0340  0.0392  103 GLN A NE2 
879  N  NE2 B GLN A 103 ? 0.2089 0.2786 0.2483 -0.0132 0.0098  -0.0377 103 GLN A NE2 
880  N  N   . GLY A 104 ? 0.1096 0.0794 0.1001 -0.0043 0.0137  -0.0019 104 GLY A N   
881  C  CA  . GLY A 104 ? 0.1224 0.0860 0.0904 -0.0057 0.0065  0.0048  104 GLY A CA  
882  C  C   . GLY A 104 ? 0.0942 0.0865 0.0947 -0.0035 -0.0041 0.0019  104 GLY A C   
883  O  O   . GLY A 104 ? 0.1036 0.0898 0.1023 -0.0030 0.0026  0.0054  104 GLY A O   
884  N  N   . SER A 105 ? 0.1030 0.0918 0.0834 -0.0118 0.0065  -0.0071 105 SER A N   
885  C  CA  . SER A 105 ? 0.0908 0.0890 0.0869 -0.0057 0.0074  -0.0082 105 SER A CA  
886  C  C   . SER A 105 ? 0.0856 0.0803 0.0929 -0.0109 0.0057  0.0038  105 SER A C   
887  O  O   . SER A 105 ? 0.1076 0.0939 0.1069 -0.0037 -0.0037 -0.0030 105 SER A O   
888  C  CB  . SER A 105 ? 0.0834 0.0886 0.0944 -0.0080 0.0068  0.0057  105 SER A CB  
889  O  OG  . SER A 105 ? 0.1048 0.0851 0.1014 -0.0013 0.0098  0.0015  105 SER A OG  
890  N  N   . GLU A 106 ? 0.0997 0.0882 0.0869 -0.0140 0.0063  -0.0031 106 GLU A N   
891  C  CA  . GLU A 106 ? 0.0965 0.0847 0.0847 -0.0143 -0.0048 0.0024  106 GLU A CA  
892  C  C   . GLU A 106 ? 0.0864 0.0829 0.0929 -0.0063 -0.0052 0.0082  106 GLU A C   
893  O  O   . GLU A 106 ? 0.0945 0.0904 0.0965 0.0027  0.0038  0.0024  106 GLU A O   
894  C  CB  . GLU A 106 ? 0.0912 0.0785 0.0832 -0.0038 0.0087  0.0024  106 GLU A CB  
895  C  CG  . GLU A 106 ? 0.1458 0.0907 0.1018 -0.0093 0.0186  0.0065  106 GLU A CG  
896  C  CD  . GLU A 106 ? 0.0927 0.0834 0.0997 -0.0088 -0.0019 -0.0070 106 GLU A CD  
897  O  OE1 . GLU A 106 ? 0.0904 0.0900 0.1048 -0.0082 -0.0006 -0.0046 106 GLU A OE1 
898  O  OE2 . GLU A 106 ? 0.1027 0.1032 0.1230 -0.0020 0.0114  -0.0059 106 GLU A OE2 
899  N  N   . HIS A 107 ? 0.0886 0.0833 0.0873 -0.0110 0.0000  0.0080  107 HIS A N   
900  C  CA  . HIS A 107 ? 0.0777 0.0834 0.0850 0.0082  0.0031  0.0006  107 HIS A CA  
901  C  C   . HIS A 107 ? 0.0803 0.0802 0.0920 0.0035  0.0097  0.0034  107 HIS A C   
902  O  O   . HIS A 107 ? 0.0917 0.0895 0.0966 -0.0086 -0.0007 0.0020  107 HIS A O   
903  C  CB  . HIS A 107 ? 0.1011 0.0793 0.0913 0.0006  0.0108  0.0027  107 HIS A CB  
904  C  CG  . HIS A 107 ? 0.0802 0.0816 0.0876 0.0070  0.0104  -0.0037 107 HIS A CG  
905  N  ND1 . HIS A 107 ? 0.0923 0.0775 0.0951 0.0026  -0.0071 -0.0046 107 HIS A ND1 
906  C  CD2 . HIS A 107 ? 0.0847 0.0832 0.0988 0.0131  -0.0006 -0.0130 107 HIS A CD2 
907  C  CE1 . HIS A 107 ? 0.1053 0.0926 0.0908 0.0006  -0.0065 -0.0120 107 HIS A CE1 
908  N  NE2 . HIS A 107 ? 0.0882 0.0890 0.0929 0.0110  -0.0034 -0.0120 107 HIS A NE2 
909  N  N   . THR A 108 ? 0.0932 0.0825 0.0929 -0.0076 0.0060  0.0054  108 THR A N   
910  C  CA  . THR A 108 ? 0.1118 0.0759 0.0912 0.0023  0.0109  0.0143  108 THR A CA  
911  C  C   . THR A 108 ? 0.0834 0.0829 0.0957 0.0020  -0.0082 0.0057  108 THR A C   
912  O  O   . THR A 108 ? 0.0981 0.0963 0.0951 0.0052  0.0015  0.0038  108 THR A O   
913  C  CB  . THR A 108 ? 0.1053 0.0922 0.1067 0.0051  -0.0070 -0.0017 108 THR A CB  
914  O  OG1 . THR A 108 ? 0.1187 0.0969 0.1124 0.0103  -0.0082 0.0007  108 THR A OG1 
915  C  CG2 . THR A 108 ? 0.1264 0.1166 0.1155 0.0087  0.0052  -0.0096 108 THR A CG2 
916  N  N   . VAL A 109 ? 0.1023 0.0856 0.0944 -0.0076 0.0034  0.0104  109 VAL A N   
917  C  CA  . VAL A 109 ? 0.1054 0.0944 0.1018 0.0000  0.0131  0.0159  109 VAL A CA  
918  C  C   . VAL A 109 ? 0.1024 0.1010 0.0997 -0.0071 0.0107  0.0006  109 VAL A C   
919  O  O   . VAL A 109 ? 0.1184 0.0944 0.1098 -0.0024 0.0087  0.0159  109 VAL A O   
920  C  CB  . VAL A 109 ? 0.1085 0.1017 0.1259 -0.0041 0.0080  0.0107  109 VAL A CB  
921  C  CG1 . VAL A 109 ? 0.1177 0.1261 0.1406 0.0020  0.0285  0.0230  109 VAL A CG1 
922  C  CG2 . VAL A 109 ? 0.1215 0.1137 0.1304 0.0017  -0.0006 0.0175  109 VAL A CG2 
923  N  N   . ASP A 110 ? 0.1186 0.1099 0.1023 0.0049  0.0087  0.0269  110 ASP A N   
924  C  CA  . ASP A 110 ? 0.1498 0.1071 0.1206 0.0137  0.0085  0.0304  110 ASP A CA  
925  C  C   . ASP A 110 ? 0.1611 0.0960 0.1114 0.0104  0.0233  0.0147  110 ASP A C   
926  O  O   . ASP A 110 ? 0.1562 0.1093 0.1264 0.0063  0.0054  0.0230  110 ASP A O   
927  C  CB  . ASP A 110 ? 0.1817 0.1193 0.1412 0.0043  0.0359  0.0392  110 ASP A CB  
928  C  CG  . ASP A 110 ? 0.1691 0.1562 0.1289 0.0037  0.0148  0.0381  110 ASP A CG  
929  O  OD1 . ASP A 110 ? 0.1797 0.1537 0.1430 0.0173  0.0307  0.0241  110 ASP A OD1 
930  O  OD2 . ASP A 110 ? 0.1810 0.2013 0.1659 0.0220  0.0153  0.0210  110 ASP A OD2 
931  N  N   . LYS A 111 ? 0.1212 0.1160 0.0988 0.0093  0.0027  0.0186  111 LYS A N   
932  C  CA  . LYS A 111 ? 0.1293 0.1159 0.1137 0.0161  -0.0060 0.0203  111 LYS A CA  
933  C  C   . LYS A 111 ? 0.1465 0.0842 0.1058 0.0081  0.0115  0.0059  111 LYS A C   
934  O  O   . LYS A 111 ? 0.1439 0.1463 0.1245 0.0225  0.0104  -0.0046 111 LYS A O   
935  C  CB  . LYS A 111 ? 0.1512 0.1430 0.1280 0.0193  0.0086  0.0226  111 LYS A CB  
936  C  CG  . LYS A 111 ? 0.1974 0.1774 0.1841 0.0692  -0.0199 0.0276  111 LYS A CG  
937  C  CD  . LYS A 111 ? 0.2020 0.2046 0.2002 0.0362  -0.0434 -0.0113 111 LYS A CD  
938  C  CE  . LYS A 111 ? 0.2531 0.2354 0.2101 0.0370  -0.0557 0.0017  111 LYS A CE  
939  N  NZ  . LYS A 111 ? 0.2361 0.2554 0.2522 -0.0049 -0.0524 0.0505  111 LYS A NZ  
940  N  N   . LYS A 112 ? 0.1314 0.0948 0.1024 0.0086  0.0104  0.0074  112 LYS A N   
941  C  CA  . LYS A 112 ? 0.1381 0.1145 0.1058 0.0087  0.0093  0.0048  112 LYS A CA  
942  C  C   . LYS A 112 ? 0.1218 0.0881 0.1133 0.0051  0.0000  0.0059  112 LYS A C   
943  O  O   . LYS A 112 ? 0.1257 0.0913 0.1011 -0.0003 0.0081  0.0017  112 LYS A O   
944  C  CB  . LYS A 112 ? 0.1435 0.1278 0.1343 -0.0136 0.0065  -0.0051 112 LYS A CB  
945  C  CG  . LYS A 112 ? 0.1535 0.1444 0.1404 -0.0171 0.0108  -0.0229 112 LYS A CG  
946  C  CD  . LYS A 112 ? 0.1573 0.1738 0.1659 -0.0102 -0.0091 0.0010  112 LYS A CD  
947  C  CE  . LYS A 112 ? 0.2228 0.1512 0.1735 -0.0255 -0.0324 -0.0023 112 LYS A CE  
948  N  NZ  . LYS A 112 ? 0.2026 0.1591 0.1826 -0.0035 -0.0362 0.0000  112 LYS A NZ  
949  N  N   A LYS A 113 ? 0.1160 0.0966 0.1058 0.0225  0.0006  0.0115  113 LYS A N   
950  N  N   B LYS A 113 ? 0.1208 0.0952 0.0999 0.0093  -0.0087 -0.0006 113 LYS A N   
951  C  CA  A LYS A 113 ? 0.1132 0.1154 0.1075 0.0159  -0.0164 0.0291  113 LYS A CA  
952  C  CA  B LYS A 113 ? 0.1229 0.0834 0.1194 0.0043  -0.0057 0.0146  113 LYS A CA  
953  C  C   A LYS A 113 ? 0.1096 0.0877 0.1076 0.0015  0.0153  0.0126  113 LYS A C   
954  C  C   B LYS A 113 ? 0.1181 0.0886 0.1160 -0.0043 0.0214  0.0181  113 LYS A C   
955  O  O   A LYS A 113 ? 0.1136 0.0948 0.1049 0.0031  0.0024  0.0046  113 LYS A O   
956  O  O   B LYS A 113 ? 0.1268 0.0776 0.1350 -0.0006 0.0141  0.0163  113 LYS A O   
957  C  CB  A LYS A 113 ? 0.1193 0.1099 0.1314 0.0051  -0.0015 0.0006  113 LYS A CB  
958  C  CB  B LYS A 113 ? 0.1172 0.1150 0.1049 -0.0013 0.0043  0.0073  113 LYS A CB  
959  C  CG  A LYS A 113 ? 0.0944 0.1445 0.1076 0.0031  0.0126  -0.0043 113 LYS A CG  
960  C  CG  B LYS A 113 ? 0.0988 0.1137 0.1254 -0.0057 0.0057  0.0049  113 LYS A CG  
961  C  CD  A LYS A 113 ? 0.1187 0.1720 0.1286 0.0274  0.0091  -0.0063 113 LYS A CD  
962  C  CD  B LYS A 113 ? 0.1208 0.1704 0.1377 0.0048  0.0126  -0.0309 113 LYS A CD  
963  C  CE  A LYS A 113 ? 0.1510 0.2360 0.1148 0.0073  -0.0244 -0.0174 113 LYS A CE  
964  C  CE  B LYS A 113 ? 0.1492 0.1519 0.1612 0.0051  -0.0115 -0.0162 113 LYS A CE  
965  N  NZ  A LYS A 113 ? 0.1929 0.2344 0.2319 0.0254  0.0161  0.0098  113 LYS A NZ  
966  N  NZ  B LYS A 113 ? 0.1142 0.1699 0.1464 -0.0013 -0.0261 -0.0041 113 LYS A NZ  
967  N  N   . TYR A 114 ? 0.1067 0.0909 0.1035 -0.0015 -0.0049 0.0024  114 TYR A N   
968  C  CA  . TYR A 114 ? 0.1127 0.0891 0.1172 -0.0081 -0.0065 0.0038  114 TYR A CA  
969  C  C   . TYR A 114 ? 0.1001 0.0737 0.1154 0.0031  0.0006  0.0019  114 TYR A C   
970  O  O   . TYR A 114 ? 0.0992 0.1005 0.1194 0.0006  0.0068  -0.0046 114 TYR A O   
971  C  CB  . TYR A 114 ? 0.1081 0.0882 0.1137 0.0015  0.0059  0.0104  114 TYR A CB  
972  C  CG  . TYR A 114 ? 0.1053 0.0856 0.1163 0.0031  0.0027  0.0109  114 TYR A CG  
973  C  CD1 . TYR A 114 ? 0.1391 0.0997 0.1366 0.0092  0.0098  0.0155  114 TYR A CD1 
974  C  CD2 . TYR A 114 ? 0.1081 0.1127 0.1489 0.0006  0.0107  0.0211  114 TYR A CD2 
975  C  CE1 . TYR A 114 ? 0.1833 0.1297 0.1199 0.0126  0.0103  0.0137  114 TYR A CE1 
976  C  CE2 . TYR A 114 ? 0.1367 0.1145 0.1744 -0.0031 0.0208  -0.0027 114 TYR A CE2 
977  C  CZ  . TYR A 114 ? 0.1598 0.1375 0.1561 0.0006  0.0432  0.0098  114 TYR A CZ  
978  O  OH  . TYR A 114 ? 0.2128 0.2142 0.1966 0.0119  0.0837  0.0087  114 TYR A OH  
979  N  N   . ALA A 115 ? 0.1108 0.0750 0.1072 -0.0086 -0.0063 0.0012  115 ALA A N   
980  C  CA  . ALA A 115 ? 0.1199 0.0711 0.1027 -0.0159 0.0043  -0.0020 115 ALA A CA  
981  C  C   . ALA A 115 ? 0.1157 0.0780 0.0997 -0.0114 -0.0027 0.0054  115 ALA A C   
982  O  O   . ALA A 115 ? 0.1142 0.0820 0.1105 -0.0136 0.0074  -0.0015 115 ALA A O   
983  C  CB  . ALA A 115 ? 0.1483 0.0907 0.1324 -0.0189 -0.0160 -0.0031 115 ALA A CB  
984  N  N   . ALA A 116 ? 0.1130 0.0737 0.1058 -0.0007 0.0054  0.0026  116 ALA A N   
985  C  CA  . ALA A 116 ? 0.1090 0.0843 0.0886 -0.0091 0.0076  0.0074  116 ALA A CA  
986  C  C   . ALA A 116 ? 0.0975 0.0794 0.0824 -0.0041 -0.0019 0.0065  116 ALA A C   
987  O  O   . ALA A 116 ? 0.0996 0.0825 0.0956 -0.0102 0.0049  0.0023  116 ALA A O   
988  C  CB  . ALA A 116 ? 0.1187 0.0954 0.0970 -0.0135 -0.0006 0.0006  116 ALA A CB  
989  N  N   . GLU A 117 ? 0.1093 0.0680 0.0859 -0.0063 0.0038  0.0031  117 GLU A N   
990  C  CA  . GLU A 117 ? 0.0979 0.0658 0.0887 -0.0041 -0.0031 -0.0027 117 GLU A CA  
991  C  C   . GLU A 117 ? 0.0886 0.0882 0.0731 -0.0062 0.0000  0.0037  117 GLU A C   
992  O  O   . GLU A 117 ? 0.1069 0.0984 0.1090 0.0031  0.0125  0.0137  117 GLU A O   
993  C  CB  . GLU A 117 ? 0.1145 0.0842 0.0859 -0.0005 -0.0172 -0.0041 117 GLU A CB  
994  C  CG  . GLU A 117 ? 0.0952 0.0954 0.0873 0.0007  -0.0131 -0.0057 117 GLU A CG  
995  C  CD  . GLU A 117 ? 0.0956 0.0807 0.0873 -0.0049 0.0049  0.0020  117 GLU A CD  
996  O  OE1 . GLU A 117 ? 0.1014 0.1058 0.1076 0.0020  -0.0027 0.0006  117 GLU A OE1 
997  O  OE2 . GLU A 117 ? 0.1163 0.0951 0.0929 -0.0081 -0.0097 0.0000  117 GLU A OE2 
998  N  N   . LEU A 118 ? 0.0917 0.0793 0.0846 -0.0043 -0.0087 -0.0020 118 LEU A N   
999  C  CA  . LEU A 118 ? 0.1006 0.0744 0.0864 -0.0076 -0.0087 0.0027  118 LEU A CA  
1000 C  C   . LEU A 118 ? 0.0966 0.0776 0.0868 0.0005  -0.0006 0.0043  118 LEU A C   
1001 O  O   . LEU A 118 ? 0.0960 0.0754 0.0798 -0.0068 -0.0013 0.0027  118 LEU A O   
1002 C  CB  . LEU A 118 ? 0.1026 0.0859 0.0996 -0.0057 -0.0113 0.0087  118 LEU A CB  
1003 C  CG  . LEU A 118 ? 0.0969 0.1023 0.0975 -0.0060 -0.0154 0.0131  118 LEU A CG  
1004 C  CD1 . LEU A 118 ? 0.1146 0.0895 0.1027 -0.0076 -0.0215 0.0160  118 LEU A CD1 
1005 C  CD2 . LEU A 118 ? 0.1075 0.1316 0.1224 0.0027  -0.0286 0.0118  118 LEU A CD2 
1006 N  N   . HIS A 119 ? 0.0869 0.0688 0.0815 -0.0017 -0.0057 0.0059  119 HIS A N   
1007 C  CA  . HIS A 119 ? 0.0856 0.0732 0.0741 0.0007  -0.0071 -0.0003 119 HIS A CA  
1008 C  C   . HIS A 119 ? 0.0904 0.0737 0.0776 -0.0120 -0.0027 0.0013  119 HIS A C   
1009 O  O   . HIS A 119 ? 0.1017 0.0833 0.0873 -0.0012 -0.0087 0.0076  119 HIS A O   
1010 C  CB  . HIS A 119 ? 0.1010 0.0798 0.0873 0.0068  -0.0038 0.0109  119 HIS A CB  
1011 C  CG  . HIS A 119 ? 0.0869 0.0803 0.0772 -0.0003 0.0038  -0.0076 119 HIS A CG  
1012 N  ND1 . HIS A 119 ? 0.0750 0.0891 0.0683 -0.0017 0.0041  0.0007  119 HIS A ND1 
1013 C  CD2 . HIS A 119 ? 0.0859 0.0825 0.0860 -0.0057 -0.0142 0.0041  119 HIS A CD2 
1014 C  CE1 . HIS A 119 ? 0.0895 0.0873 0.0789 -0.0065 -0.0081 -0.0087 119 HIS A CE1 
1015 N  NE2 . HIS A 119 ? 0.0812 0.0820 0.0909 -0.0038 -0.0054 0.0057  119 HIS A NE2 
1016 N  N   . LEU A 120 ? 0.0886 0.0750 0.0882 0.0003  -0.0038 0.0049  120 LEU A N   
1017 C  CA  . LEU A 120 ? 0.0996 0.0824 0.0834 0.0071  -0.0192 0.0098  120 LEU A CA  
1018 C  C   . LEU A 120 ? 0.0886 0.0719 0.0798 0.0131  -0.0035 0.0093  120 LEU A C   
1019 O  O   . LEU A 120 ? 0.0860 0.0821 0.0846 -0.0086 -0.0046 0.0043  120 LEU A O   
1020 C  CB  . LEU A 120 ? 0.0863 0.0881 0.1128 -0.0038 -0.0215 -0.0015 120 LEU A CB  
1021 C  CG  . LEU A 120 ? 0.1212 0.1057 0.1081 -0.0142 -0.0230 0.0092  120 LEU A CG  
1022 C  CD1 . LEU A 120 ? 0.1952 0.1368 0.1136 -0.0571 -0.0080 -0.0005 120 LEU A CD1 
1023 C  CD2 . LEU A 120 ? 0.1304 0.1611 0.1351 0.0068  -0.0483 -0.0119 120 LEU A CD2 
1024 N  N   . VAL A 121 ? 0.0983 0.0846 0.0860 -0.0062 -0.0068 0.0096  121 VAL A N   
1025 C  CA  . VAL A 121 ? 0.0975 0.0702 0.0886 -0.0003 -0.0081 0.0041  121 VAL A CA  
1026 C  C   . VAL A 121 ? 0.0891 0.0851 0.0895 -0.0062 0.0038  0.0068  121 VAL A C   
1027 O  O   . VAL A 121 ? 0.1099 0.0886 0.0981 0.0068  -0.0087 0.0081  121 VAL A O   
1028 C  CB  . VAL A 121 ? 0.1011 0.0790 0.1039 -0.0038 -0.0037 0.0031  121 VAL A CB  
1029 C  CG1 . VAL A 121 ? 0.1145 0.0975 0.1150 -0.0199 0.0077  0.0006  121 VAL A CG1 
1030 C  CG2 . VAL A 121 ? 0.1096 0.0832 0.1063 0.0024  0.0038  -0.0006 121 VAL A CG2 
1031 N  N   . HIS A 122 ? 0.0908 0.0715 0.0935 -0.0046 -0.0035 -0.0006 122 HIS A N   
1032 C  CA  . HIS A 122 ? 0.1023 0.0639 0.1040 -0.0035 -0.0093 0.0043  122 HIS A CA  
1033 C  C   . HIS A 122 ? 0.1062 0.0820 0.1036 0.0060  -0.0020 0.0126  122 HIS A C   
1034 O  O   . HIS A 122 ? 0.1259 0.0789 0.1076 -0.0102 -0.0197 0.0115  122 HIS A O   
1035 C  CB  . HIS A 122 ? 0.1072 0.0680 0.1169 0.0035  0.0031  -0.0054 122 HIS A CB  
1036 C  CG  . HIS A 122 ? 0.1008 0.0785 0.0969 0.0007  -0.0040 0.0024  122 HIS A CG  
1037 N  ND1 . HIS A 122 ? 0.0978 0.0821 0.1164 0.0010  0.0063  0.0038  122 HIS A ND1 
1038 C  CD2 . HIS A 122 ? 0.1062 0.1118 0.1020 -0.0020 -0.0020 0.0000  122 HIS A CD2 
1039 C  CE1 . HIS A 122 ? 0.0754 0.1017 0.1252 -0.0065 -0.0027 0.0046  122 HIS A CE1 
1040 N  NE2 . HIS A 122 ? 0.1053 0.1042 0.1166 0.0007  -0.0003 -0.0092 122 HIS A NE2 
1041 N  N   . TRP A 123 ? 0.1042 0.0772 0.1150 -0.0034 -0.0103 0.0019  123 TRP A N   
1042 C  CA  . TRP A 123 ? 0.1054 0.0873 0.1145 -0.0082 -0.0026 -0.0074 123 TRP A CA  
1043 C  C   . TRP A 123 ? 0.1036 0.0797 0.1015 0.0017  -0.0054 0.0020  123 TRP A C   
1044 O  O   . TRP A 123 ? 0.1103 0.0938 0.1243 0.0027  -0.0126 -0.0080 123 TRP A O   
1045 C  CB  . TRP A 123 ? 0.1251 0.1300 0.1209 -0.0207 0.0124  0.0013  123 TRP A CB  
1046 C  CG  . TRP A 123 ? 0.1420 0.1017 0.1379 -0.0259 0.0063  0.0071  123 TRP A CG  
1047 C  CD1 . TRP A 123 ? 0.1679 0.1072 0.1099 -0.0318 0.0046  0.0154  123 TRP A CD1 
1048 C  CD2 . TRP A 123 ? 0.1825 0.0856 0.1334 -0.0255 0.0109  -0.0027 123 TRP A CD2 
1049 N  NE1 . TRP A 123 ? 0.1979 0.0891 0.1386 -0.0171 -0.0176 0.0000  123 TRP A NE1 
1050 C  CE2 . TRP A 123 ? 0.2063 0.0834 0.1641 -0.0375 -0.0024 0.0228  123 TRP A CE2 
1051 C  CE3 . TRP A 123 ? 0.2040 0.0856 0.1482 -0.0320 0.0192  -0.0098 123 TRP A CE3 
1052 C  CZ2 . TRP A 123 ? 0.2265 0.0965 0.1787 -0.0207 0.0035  0.0132  123 TRP A CZ2 
1053 C  CZ3 . TRP A 123 ? 0.2509 0.0819 0.1510 -0.0326 0.0057  -0.0063 123 TRP A CZ3 
1054 C  CH2 . TRP A 123 ? 0.2326 0.1014 0.1779 -0.0170 0.0135  0.0110  123 TRP A CH2 
1055 N  N   . ASN A 124 ? 0.1063 0.0842 0.1111 0.0030  -0.0092 -0.0102 124 ASN A N   
1056 C  CA  . ASN A 124 ? 0.1215 0.0926 0.1164 0.0093  -0.0109 -0.0043 124 ASN A CA  
1057 C  C   . ASN A 124 ? 0.1063 0.0951 0.1350 0.0041  -0.0115 -0.0118 124 ASN A C   
1058 O  O   . ASN A 124 ? 0.1269 0.0948 0.1377 0.0013  -0.0043 0.0013  124 ASN A O   
1059 C  CB  . ASN A 124 ? 0.1272 0.1054 0.1115 -0.0006 0.0031  -0.0110 124 ASN A CB  
1060 C  CG  . ASN A 124 ? 0.1300 0.1039 0.1243 0.0015  -0.0073 -0.0031 124 ASN A CG  
1061 O  OD1 . ASN A 124 ? 0.1428 0.1054 0.1537 0.0136  -0.0015 -0.0175 124 ASN A OD1 
1062 N  ND2 . ASN A 124 ? 0.1782 0.1105 0.1233 0.0041  -0.0003 -0.0137 124 ASN A ND2 
1063 N  N   . THR A 125 ? 0.1163 0.0965 0.1324 0.0186  -0.0142 -0.0154 125 THR A N   
1064 C  CA  . THR A 125 ? 0.1386 0.0988 0.1659 0.0153  -0.0284 -0.0027 125 THR A CA  
1065 C  C   . THR A 125 ? 0.1533 0.0938 0.1607 0.0241  0.0020  0.0051  125 THR A C   
1066 O  O   . THR A 125 ? 0.1982 0.1099 0.1724 0.0148  -0.0142 0.0230  125 THR A O   
1067 C  CB  . THR A 125 ? 0.1429 0.1358 0.1961 0.0155  -0.0450 0.0165  125 THR A CB  
1068 O  OG1 . THR A 125 ? 0.1835 0.1704 0.2933 0.0443  0.0108  0.0142  125 THR A OG1 
1069 C  CG2 . THR A 125 ? 0.2175 0.1616 0.2123 -0.0043 -0.0636 -0.0080 125 THR A CG2 
1070 N  N   A LYS A 126 ? 0.1253 0.0834 0.1115 0.0104  -0.0333 -0.0242 127 LYS A N   
1071 N  N   B LYS A 126 ? 0.1190 0.0948 0.1334 0.0185  -0.0017 -0.0017 127 LYS A N   
1072 C  CA  A LYS A 126 ? 0.1334 0.1072 0.1229 0.0043  -0.0175 -0.0456 127 LYS A CA  
1073 C  CA  B LYS A 126 ? 0.1404 0.0935 0.1485 0.0063  -0.0027 0.0017  127 LYS A CA  
1074 C  C   A LYS A 126 ? 0.1548 0.0675 0.1087 0.0142  -0.0070 -0.0137 127 LYS A C   
1075 C  C   B LYS A 126 ? 0.1476 0.0930 0.1168 0.0063  -0.0129 -0.0107 127 LYS A C   
1076 O  O   A LYS A 126 ? 0.1429 0.0763 0.1507 0.0027  -0.0297 -0.0258 127 LYS A O   
1077 O  O   B LYS A 126 ? 0.1481 0.1008 0.1215 -0.0027 -0.0017 -0.0205 127 LYS A O   
1078 C  CB  A LYS A 126 ? 0.1588 0.1133 0.1211 -0.0076 -0.0265 -0.0096 127 LYS A CB  
1079 C  CB  B LYS A 126 ? 0.1404 0.1388 0.1500 -0.0131 -0.0322 -0.0109 127 LYS A CB  
1080 C  CG  A LYS A 126 ? 0.1341 0.1291 0.1561 -0.0087 -0.0287 -0.0131 127 LYS A CG  
1081 C  CG  B LYS A 126 ? 0.1430 0.1600 0.1453 0.0379  -0.0082 -0.0359 127 LYS A CG  
1082 C  CD  A LYS A 126 ? 0.2053 0.1958 0.1465 0.0253  0.0043  -0.0350 127 LYS A CD  
1083 C  CD  B LYS A 126 ? 0.1532 0.1711 0.1427 -0.0107 -0.0172 0.0040  127 LYS A CD  
1084 C  CE  A LYS A 126 ? 0.1683 0.2162 0.2200 -0.0186 -0.0082 0.0142  127 LYS A CE  
1085 C  CE  B LYS A 126 ? 0.3230 0.1150 0.1536 0.0165  0.0551  0.0109  127 LYS A CE  
1086 N  NZ  A LYS A 126 ? 0.2971 0.2874 0.1787 0.0562  0.0038  -0.0108 127 LYS A NZ  
1087 N  NZ  B LYS A 126 ? 0.2462 0.2090 0.1239 0.0137  0.0237  0.0035  127 LYS A NZ  
1088 N  N   . TYR A 127 ? 0.1553 0.0965 0.1321 0.0091  -0.0088 -0.0126 128 TYR A N   
1089 C  CA  . TYR A 127 ? 0.1780 0.0990 0.1273 -0.0020 -0.0241 0.0041  128 TYR A CA  
1090 C  C   . TYR A 127 ? 0.1494 0.0860 0.1483 -0.0059 -0.0046 -0.0126 128 TYR A C   
1091 O  O   . TYR A 127 ? 0.1679 0.0944 0.1528 -0.0034 0.0052  -0.0096 128 TYR A O   
1092 C  CB  . TYR A 127 ? 0.1503 0.1124 0.1506 0.0040  0.0091  0.0082  128 TYR A CB  
1093 C  CG  . TYR A 127 ? 0.1509 0.0974 0.1391 0.0013  -0.0162 -0.0024 128 TYR A CG  
1094 C  CD1 . TYR A 127 ? 0.1550 0.1072 0.1525 -0.0137 -0.0221 -0.0109 128 TYR A CD1 
1095 C  CD2 . TYR A 127 ? 0.1298 0.1084 0.1330 0.0023  -0.0076 -0.0027 128 TYR A CD2 
1096 C  CE1 . TYR A 127 ? 0.1867 0.1114 0.1534 0.0000  -0.0247 -0.0153 128 TYR A CE1 
1097 C  CE2 . TYR A 127 ? 0.1510 0.1128 0.1358 0.0120  -0.0038 -0.0175 128 TYR A CE2 
1098 C  CZ  . TYR A 127 ? 0.1738 0.1159 0.1385 0.0207  -0.0131 -0.0114 128 TYR A CZ  
1099 O  OH  . TYR A 127 ? 0.2152 0.1295 0.1440 0.0120  -0.0218 -0.0208 128 TYR A OH  
1100 N  N   . GLY A 128 ? 0.1729 0.0965 0.1325 -0.0054 -0.0155 0.0041  129 GLY A N   
1101 C  CA  . GLY A 128 ? 0.1810 0.1084 0.1510 -0.0057 -0.0038 0.0031  129 GLY A CA  
1102 C  C   . GLY A 128 ? 0.1710 0.1169 0.1375 -0.0148 -0.0188 0.0093  129 GLY A C   
1103 O  O   . GLY A 128 ? 0.2304 0.1067 0.1485 -0.0071 -0.0218 0.0110  129 GLY A O   
1104 N  N   . ASP A 129 ? 0.1964 0.1069 0.1409 0.0107  -0.0104 -0.0071 130 ASP A N   
1105 C  CA  . ASP A 129 ? 0.2105 0.1160 0.1248 0.0086  -0.0054 -0.0040 130 ASP A CA  
1106 C  C   . ASP A 129 ? 0.2314 0.1227 0.1163 0.0052  -0.0113 0.0076  130 ASP A C   
1107 O  O   . ASP A 129 ? 0.2325 0.1105 0.1272 0.0164  -0.0098 -0.0003 130 ASP A O   
1108 C  CB  . ASP A 129 ? 0.2479 0.1807 0.1588 0.0120  0.0211  0.0154  130 ASP A CB  
1109 C  CG  . ASP A 129 ? 0.2486 0.1291 0.1509 0.0215  0.0298  0.0153  130 ASP A CG  
1110 O  OD1 . ASP A 129 ? 0.3368 0.2010 0.2766 -0.0634 -0.0825 -0.0065 130 ASP A OD1 
1111 O  OD2 . ASP A 129 ? 0.2544 0.2148 0.2720 -0.0132 0.0951  0.0229  130 ASP A OD2 
1112 N  N   . PHE A 130 ? 0.2047 0.1054 0.1260 0.0092  -0.0020 -0.0041 131 PHE A N   
1113 C  CA  . PHE A 130 ? 0.1776 0.0918 0.1322 0.0049  -0.0015 -0.0205 131 PHE A CA  
1114 C  C   . PHE A 130 ? 0.1756 0.0966 0.1367 -0.0054 0.0166  0.0023  131 PHE A C   
1115 O  O   . PHE A 130 ? 0.1621 0.1096 0.1254 -0.0155 0.0017  0.0000  131 PHE A O   
1116 C  CB  . PHE A 130 ? 0.1869 0.1072 0.1289 0.0035  -0.0136 -0.0093 131 PHE A CB  
1117 C  CG  . PHE A 130 ? 0.1488 0.0920 0.1261 0.0006  0.0098  -0.0199 131 PHE A CG  
1118 C  CD1 . PHE A 130 ? 0.1555 0.1159 0.1278 -0.0108 0.0003  0.0046  131 PHE A CD1 
1119 C  CD2 . PHE A 130 ? 0.1981 0.1123 0.1770 -0.0068 0.0410  -0.0161 131 PHE A CD2 
1120 C  CE1 . PHE A 130 ? 0.1852 0.1164 0.1411 -0.0163 0.0041  -0.0081 131 PHE A CE1 
1121 C  CE2 . PHE A 130 ? 0.1964 0.1682 0.1916 0.0137  0.0131  -0.0076 131 PHE A CE2 
1122 C  CZ  . PHE A 130 ? 0.2143 0.1388 0.1641 -0.0063 -0.0109 -0.0428 131 PHE A CZ  
1123 N  N   . GLY A 131 ? 0.2040 0.1221 0.1359 -0.0274 0.0252  -0.0046 132 GLY A N   
1124 C  CA  . GLY A 131 ? 0.2004 0.1307 0.1402 -0.0206 0.0511  0.0000  132 GLY A CA  
1125 C  C   . GLY A 131 ? 0.1717 0.1433 0.1438 -0.0419 0.0293  0.0087  132 GLY A C   
1126 O  O   . GLY A 131 ? 0.1703 0.1307 0.2009 -0.0173 0.0292  -0.0197 132 GLY A O   
1127 N  N   . LYS A 132 ? 0.1738 0.1058 0.1607 -0.0285 0.0126  0.0060  133 LYS A N   
1128 C  CA  . LYS A 132 ? 0.1787 0.0974 0.1411 -0.0164 0.0115  0.0115  133 LYS A CA  
1129 C  C   . LYS A 132 ? 0.1447 0.1181 0.1279 -0.0208 -0.0017 0.0082  133 LYS A C   
1130 O  O   . LYS A 132 ? 0.1503 0.1137 0.1412 -0.0329 -0.0065 -0.0065 133 LYS A O   
1131 C  CB  . LYS A 132 ? 0.1576 0.1145 0.1792 -0.0163 0.0070  0.0046  133 LYS A CB  
1132 C  CG  . LYS A 132 ? 0.1922 0.1315 0.2245 -0.0054 0.0000  0.0339  133 LYS A CG  
1133 C  CD  . LYS A 132 ? 0.2022 0.1603 0.3352 -0.0339 -0.0152 0.0625  133 LYS A CD  
1134 C  CE  . LYS A 132 ? 0.2133 0.2161 0.3246 -0.0623 -0.0254 0.0640  133 LYS A CE  
1135 N  NZ  . LYS A 132 ? 0.3138 0.3424 0.5030 -0.0966 -0.1140 0.0339  133 LYS A NZ  
1136 N  N   . ALA A 133 ? 0.1557 0.1054 0.1234 -0.0379 0.0003  -0.0027 134 ALA A N   
1137 C  CA  . ALA A 133 ? 0.1377 0.1199 0.1164 -0.0253 -0.0031 0.0086  134 ALA A CA  
1138 C  C   . ALA A 133 ? 0.1193 0.1154 0.1098 -0.0280 0.0035  0.0054  134 ALA A C   
1139 O  O   . ALA A 133 ? 0.1011 0.1272 0.1173 -0.0184 0.0024  0.0046  134 ALA A O   
1140 C  CB  . ALA A 133 ? 0.1321 0.1069 0.1212 -0.0146 -0.0091 -0.0049 134 ALA A CB  
1141 N  N   . VAL A 134 ? 0.1307 0.1071 0.1229 -0.0199 0.0098  0.0051  135 VAL A N   
1142 C  CA  . VAL A 134 ? 0.1442 0.1066 0.1316 -0.0137 0.0062  0.0108  135 VAL A CA  
1143 C  C   . VAL A 134 ? 0.1351 0.1133 0.1229 -0.0159 0.0155  0.0077  135 VAL A C   
1144 O  O   . VAL A 134 ? 0.1247 0.1297 0.1401 -0.0170 0.0175  0.0076  135 VAL A O   
1145 C  CB  . VAL A 134 ? 0.1528 0.1332 0.1318 -0.0238 0.0306  -0.0121 135 VAL A CB  
1146 C  CG1 . VAL A 134 ? 0.1823 0.1400 0.1611 -0.0251 -0.0137 -0.0109 135 VAL A CG1 
1147 C  CG2 . VAL A 134 ? 0.1640 0.1336 0.1553 -0.0221 0.0408  -0.0093 135 VAL A CG2 
1148 N  N   . GLN A 135 ? 0.1273 0.1151 0.1370 -0.0306 0.0164  0.0007  136 GLN A N   
1149 C  CA  . GLN A 135 ? 0.1406 0.1196 0.1506 -0.0237 0.0023  -0.0137 136 GLN A CA  
1150 C  C   . GLN A 135 ? 0.1278 0.1289 0.1331 -0.0238 0.0027  -0.0102 136 GLN A C   
1151 O  O   . GLN A 135 ? 0.1191 0.1776 0.1679 -0.0353 -0.0051 -0.0211 136 GLN A O   
1152 C  CB  . GLN A 135 ? 0.1456 0.1580 0.1600 -0.0366 0.0154  0.0171  136 GLN A CB  
1153 C  CG  . GLN A 135 ? 0.1929 0.1665 0.1765 -0.0494 0.0253  0.0155  136 GLN A CG  
1154 C  CD  . GLN A 135 ? 0.2267 0.2369 0.2343 -0.0617 0.0205  0.0046  136 GLN A CD  
1155 O  OE1 . GLN A 135 ? 0.2897 0.3285 0.3190 -0.1168 -0.0115 0.0219  136 GLN A OE1 
1156 N  NE2 . GLN A 135 ? 0.2304 0.2390 0.2691 -0.0231 0.0216  0.0705  136 GLN A NE2 
1157 N  N   . GLN A 136 ? 0.1089 0.1333 0.1309 -0.0151 0.0099  0.0003  137 GLN A N   
1158 C  CA  . GLN A 136 ? 0.1227 0.1254 0.1001 -0.0085 -0.0081 -0.0035 137 GLN A CA  
1159 C  C   . GLN A 136 ? 0.1090 0.1280 0.1112 0.0057  0.0046  -0.0120 137 GLN A C   
1160 O  O   . GLN A 136 ? 0.1272 0.1018 0.1032 -0.0024 -0.0054 -0.0027 137 GLN A O   
1161 C  CB  . GLN A 136 ? 0.1424 0.1202 0.1410 -0.0052 -0.0219 0.0000  137 GLN A CB  
1162 C  CG  . GLN A 136 ? 0.2058 0.1518 0.1499 0.0540  0.0241  0.0063  137 GLN A CG  
1163 C  CD  . GLN A 136 ? 0.2020 0.1242 0.2433 0.0027  0.0284  0.0076  137 GLN A CD  
1164 O  OE1 . GLN A 136 ? 0.3318 0.1668 0.2838 -0.0161 -0.0548 -0.0776 137 GLN A OE1 
1165 N  NE2 . GLN A 136 ? 0.3982 0.1814 0.2578 -0.0767 -0.0606 -0.0505 137 GLN A NE2 
1166 N  N   . PRO A 137 ? 0.1069 0.1298 0.1178 -0.0065 0.0046  -0.0093 138 PRO A N   
1167 C  CA  . PRO A 137 ? 0.1251 0.1384 0.1084 0.0062  -0.0092 0.0143  138 PRO A CA  
1168 C  C   . PRO A 137 ? 0.1248 0.1325 0.1168 -0.0026 0.0082  0.0043  138 PRO A C   
1169 O  O   . PRO A 137 ? 0.1518 0.1377 0.2037 0.0000  -0.0096 0.0286  138 PRO A O   
1170 C  CB  . PRO A 137 ? 0.1585 0.1712 0.1130 -0.0088 -0.0215 0.0000  138 PRO A CB  
1171 C  CG  . PRO A 137 ? 0.3106 0.2296 0.1324 -0.0370 -0.0204 -0.0216 138 PRO A CG  
1172 C  CD  . PRO A 137 ? 0.1647 0.1744 0.1118 -0.0294 -0.0126 -0.0350 138 PRO A CD  
1173 N  N   . ASP A 138 ? 0.0992 0.1318 0.1108 0.0006  0.0000  -0.0013 139 ASP A N   
1174 C  CA  . ASP A 138 ? 0.1053 0.1352 0.1075 0.0000  0.0043  -0.0054 139 ASP A CA  
1175 C  C   . ASP A 138 ? 0.1035 0.0939 0.1187 -0.0155 0.0031  0.0017  139 ASP A C   
1176 O  O   . ASP A 138 ? 0.1155 0.1141 0.1255 -0.0038 0.0035  -0.0076 139 ASP A O   
1177 C  CB  . ASP A 138 ? 0.1280 0.1652 0.1260 -0.0110 0.0109  -0.0006 139 ASP A CB  
1178 C  CG  . ASP A 138 ? 0.1190 0.1831 0.1349 0.0010  0.0043  -0.0225 139 ASP A CG  
1179 O  OD1 . ASP A 138 ? 0.1675 0.1391 0.1421 -0.0031 -0.0035 -0.0232 139 ASP A OD1 
1180 O  OD2 . ASP A 138 ? 0.2037 0.1801 0.1743 0.0198  0.0208  -0.0322 139 ASP A OD2 
1181 N  N   . GLY A 139 ? 0.1005 0.0988 0.1030 -0.0071 0.0041  -0.0046 140 GLY A N   
1182 C  CA  . GLY A 139 ? 0.1168 0.0983 0.0929 -0.0146 -0.0098 -0.0104 140 GLY A CA  
1183 C  C   . GLY A 139 ? 0.0918 0.0851 0.1075 -0.0076 -0.0024 0.0000  140 GLY A C   
1184 O  O   . GLY A 139 ? 0.1090 0.0856 0.1120 -0.0020 -0.0108 -0.0052 140 GLY A O   
1185 N  N   . LEU A 140 ? 0.0908 0.0825 0.1124 0.0000  -0.0015 -0.0063 141 LEU A N   
1186 C  CA  . LEU A 140 ? 0.1035 0.0819 0.1018 -0.0070 0.0104  -0.0062 141 LEU A CA  
1187 C  C   . LEU A 140 ? 0.0972 0.0825 0.0908 0.0065  -0.0017 -0.0043 141 LEU A C   
1188 O  O   . LEU A 140 ? 0.0952 0.0842 0.1001 -0.0065 -0.0020 -0.0006 141 LEU A O   
1189 C  CB  . LEU A 140 ? 0.1014 0.1010 0.1026 -0.0024 0.0077  -0.0015 141 LEU A CB  
1190 C  CG  . LEU A 140 ? 0.1324 0.1173 0.1340 0.0230  0.0229  0.0024  141 LEU A CG  
1191 C  CD1 . LEU A 140 ? 0.1154 0.1145 0.1300 0.0148  0.0175  0.0059  141 LEU A CD1 
1192 C  CD2 . LEU A 140 ? 0.1815 0.1039 0.1686 0.0104  0.0346  0.0233  141 LEU A CD2 
1193 N  N   . ALA A 141 ? 0.1027 0.0741 0.0952 -0.0034 0.0000  0.0010  142 ALA A N   
1194 C  CA  . ALA A 141 ? 0.1018 0.0745 0.1067 -0.0107 0.0006  0.0003  142 ALA A CA  
1195 C  C   . ALA A 141 ? 0.0894 0.0825 0.0978 -0.0087 0.0006  0.0115  142 ALA A C   
1196 O  O   . ALA A 141 ? 0.1169 0.0856 0.1020 -0.0063 -0.0142 0.0049  142 ALA A O   
1197 C  CB  . ALA A 141 ? 0.1035 0.0979 0.1271 -0.0124 0.0040  -0.0049 142 ALA A CB  
1198 N  N   . VAL A 142 ? 0.0832 0.0790 0.0947 -0.0093 0.0000  0.0017  143 VAL A N   
1199 C  CA  . VAL A 142 ? 0.0913 0.0706 0.0856 -0.0068 -0.0020 -0.0010 143 VAL A CA  
1200 C  C   . VAL A 142 ? 0.0832 0.0776 0.0859 0.0003  0.0000  0.0037  143 VAL A C   
1201 O  O   . VAL A 142 ? 0.0878 0.0851 0.0887 -0.0088 -0.0027 0.0074  143 VAL A O   
1202 C  CB  . VAL A 142 ? 0.0784 0.0969 0.0932 -0.0073 0.0024  -0.0063 143 VAL A CB  
1203 C  CG1 . VAL A 142 ? 0.1014 0.1011 0.0929 0.0087  -0.0046 -0.0031 143 VAL A CG1 
1204 C  CG2 . VAL A 142 ? 0.0952 0.1114 0.1067 -0.0153 0.0049  0.0092  143 VAL A CG2 
1205 N  N   . LEU A 143 ? 0.0890 0.0820 0.0969 -0.0147 -0.0071 0.0027  144 LEU A N   
1206 C  CA  . LEU A 143 ? 0.0798 0.0887 0.0926 -0.0054 -0.0049 -0.0052 144 LEU A CA  
1207 C  C   . LEU A 143 ? 0.0891 0.0909 0.0847 -0.0183 -0.0054 0.0070  144 LEU A C   
1208 O  O   . LEU A 143 ? 0.1194 0.0868 0.0938 -0.0034 0.0005  0.0046  144 LEU A O   
1209 C  CB  . LEU A 143 ? 0.0936 0.1194 0.1169 -0.0087 -0.0131 0.0148  144 LEU A CB  
1210 C  CG  . LEU A 143 ? 0.1178 0.1181 0.1386 -0.0126 -0.0153 -0.0013 144 LEU A CG  
1211 C  CD1 . LEU A 143 ? 0.1103 0.1787 0.1546 -0.0196 -0.0086 0.0307  144 LEU A CD1 
1212 C  CD2 . LEU A 143 ? 0.0951 0.1501 0.1571 0.0000  -0.0080 0.0031  144 LEU A CD2 
1213 N  N   . GLY A 144 ? 0.0917 0.0807 0.0882 -0.0131 -0.0035 -0.0012 145 GLY A N   
1214 C  CA  . GLY A 144 ? 0.1020 0.0768 0.0960 -0.0148 0.0019  -0.0052 145 GLY A CA  
1215 C  C   . GLY A 144 ? 0.0763 0.0828 0.0829 -0.0007 -0.0030 0.0065  145 GLY A C   
1216 O  O   . GLY A 144 ? 0.0957 0.0961 0.0930 -0.0199 0.0027  -0.0057 145 GLY A O   
1217 N  N   . ILE A 145 ? 0.0793 0.0767 0.0851 -0.0065 -0.0092 -0.0010 146 ILE A N   
1218 C  CA  . ILE A 145 ? 0.0785 0.0794 0.0895 -0.0068 -0.0077 0.0023  146 ILE A CA  
1219 C  C   . ILE A 145 ? 0.0776 0.0750 0.0904 -0.0154 -0.0076 0.0000  146 ILE A C   
1220 O  O   . ILE A 145 ? 0.0983 0.0737 0.0996 -0.0074 0.0017  0.0013  146 ILE A O   
1221 C  CB  . ILE A 145 ? 0.0974 0.0882 0.1132 -0.0060 -0.0118 0.0005  146 ILE A CB  
1222 C  CG1 . ILE A 145 ? 0.1151 0.1093 0.1273 0.0155  -0.0303 -0.0038 146 ILE A CG1 
1223 C  CG2 . ILE A 145 ? 0.1014 0.1136 0.1421 -0.0136 -0.0329 0.0035  146 ILE A CG2 
1224 C  CD1 . ILE A 145 ? 0.0979 0.1164 0.1272 0.0037  -0.0225 0.0119  146 ILE A CD1 
1225 N  N   . PHE A 146 ? 0.0926 0.0781 0.0878 -0.0031 -0.0031 0.0010  147 PHE A N   
1226 C  CA  . PHE A 146 ? 0.1026 0.0731 0.0930 0.0024  -0.0148 0.0043  147 PHE A CA  
1227 C  C   . PHE A 146 ? 0.0938 0.0843 0.0983 -0.0020 -0.0087 -0.0065 147 PHE A C   
1228 O  O   . PHE A 146 ? 0.0929 0.0956 0.1108 -0.0030 -0.0109 -0.0052 147 PHE A O   
1229 C  CB  . PHE A 146 ? 0.1008 0.0854 0.0932 -0.0027 -0.0041 0.0102  147 PHE A CB  
1230 C  CG  . PHE A 146 ? 0.0975 0.0700 0.0891 -0.0027 -0.0046 0.0109  147 PHE A CG  
1231 C  CD1 . PHE A 146 ? 0.0957 0.0798 0.1027 -0.0005 -0.0037 0.0109  147 PHE A CD1 
1232 C  CD2 . PHE A 146 ? 0.1151 0.0856 0.1024 -0.0052 -0.0059 0.0131  147 PHE A CD2 
1233 C  CE1 . PHE A 146 ? 0.1002 0.0935 0.1053 -0.0065 -0.0103 0.0140  147 PHE A CE1 
1234 C  CE2 . PHE A 146 ? 0.1054 0.0895 0.1044 0.0000  -0.0010 0.0038  147 PHE A CE2 
1235 C  CZ  . PHE A 146 ? 0.0975 0.0899 0.1096 -0.0065 -0.0057 0.0195  147 PHE A CZ  
1236 N  N   . LEU A 147 ? 0.0997 0.0829 0.0984 -0.0065 -0.0006 -0.0052 148 LEU A N   
1237 C  CA  . LEU A 147 ? 0.1255 0.0763 0.0923 -0.0120 -0.0038 -0.0108 148 LEU A CA  
1238 C  C   . LEU A 147 ? 0.1018 0.1008 0.0904 -0.0143 0.0024  0.0006  148 LEU A C   
1239 O  O   . LEU A 147 ? 0.1072 0.0847 0.1212 -0.0063 0.0030  -0.0049 148 LEU A O   
1240 C  CB  . LEU A 147 ? 0.1315 0.0869 0.0957 -0.0104 -0.0091 -0.0057 148 LEU A CB  
1241 C  CG  . LEU A 147 ? 0.1342 0.0851 0.1075 -0.0109 -0.0108 -0.0043 148 LEU A CG  
1242 C  CD1 . LEU A 147 ? 0.1667 0.0900 0.1178 -0.0206 -0.0161 -0.0065 148 LEU A CD1 
1243 C  CD2 . LEU A 147 ? 0.1634 0.1151 0.1102 -0.0098 -0.0152 0.0043  148 LEU A CD2 
1244 N  N   . LYS A 148 ? 0.1169 0.0812 0.1169 -0.0159 -0.0124 -0.0026 149 LYS A N   
1245 C  CA  . LYS A 148 ? 0.1343 0.0824 0.1261 -0.0156 -0.0124 0.0012  149 LYS A CA  
1246 C  C   . LYS A 148 ? 0.1422 0.0997 0.1247 -0.0038 -0.0214 -0.0043 149 LYS A C   
1247 O  O   . LYS A 148 ? 0.1444 0.1278 0.1245 0.0027  -0.0233 -0.0065 149 LYS A O   
1248 C  CB  . LYS A 148 ? 0.1664 0.1202 0.1224 -0.0197 -0.0153 0.0108  149 LYS A CB  
1249 C  CG  . LYS A 148 ? 0.1747 0.1412 0.1624 -0.0229 0.0068  0.0230  149 LYS A CG  
1250 C  CD  . LYS A 148 ? 0.2376 0.2196 0.2134 -0.0187 0.0331  0.0205  149 LYS A CD  
1251 C  CE  . LYS A 148 ? 0.2669 0.4681 0.3309 -0.0803 0.0731  0.0944  149 LYS A CE  
1252 N  NZ  . LYS A 148 ? 0.4864 0.5235 0.3657 -0.2293 0.1032  0.0825  149 LYS A NZ  
1253 N  N   . VAL A 149 ? 0.1521 0.0930 0.1429 -0.0059 -0.0178 -0.0108 150 VAL A N   
1254 C  CA  . VAL A 149 ? 0.1525 0.1023 0.1440 -0.0108 -0.0091 -0.0272 150 VAL A CA  
1255 C  C   . VAL A 149 ? 0.1596 0.0983 0.1460 -0.0141 -0.0080 0.0037  150 VAL A C   
1256 O  O   . VAL A 149 ? 0.1824 0.1248 0.1675 -0.0200 -0.0211 0.0057  150 VAL A O   
1257 C  CB  . VAL A 149 ? 0.1463 0.1278 0.1476 -0.0063 -0.0229 -0.0109 150 VAL A CB  
1258 C  CG1 . VAL A 149 ? 0.1958 0.1655 0.1552 0.0054  -0.0125 -0.0439 150 VAL A CG1 
1259 C  CG2 . VAL A 149 ? 0.1753 0.1686 0.1952 -0.0297 -0.0137 0.0000  150 VAL A CG2 
1260 N  N   . GLY A 150 ? 0.1683 0.1190 0.1543 -0.0240 -0.0199 -0.0119 151 GLY A N   
1261 C  CA  . GLY A 150 ? 0.1613 0.1586 0.1568 -0.0427 -0.0344 0.0031  151 GLY A CA  
1262 C  C   . GLY A 150 ? 0.1774 0.1211 0.1607 -0.0372 -0.0253 -0.0126 151 GLY A C   
1263 O  O   . GLY A 150 ? 0.1780 0.1535 0.1674 -0.0331 -0.0280 -0.0249 151 GLY A O   
1264 N  N   A SER A 151 ? 0.1755 0.1467 0.1686 -0.0355 -0.0275 -0.0052 152 SER A N   
1265 N  N   B SER A 151 ? 0.1745 0.1467 0.1720 -0.0388 -0.0292 -0.0118 152 SER A N   
1266 C  CA  A SER A 151 ? 0.1940 0.1451 0.1763 -0.0368 -0.0364 -0.0006 152 SER A CA  
1267 C  CA  B SER A 151 ? 0.1782 0.1422 0.1676 -0.0153 -0.0219 -0.0263 152 SER A CA  
1268 C  C   A SER A 151 ? 0.1676 0.1221 0.1480 -0.0249 -0.0076 -0.0372 152 SER A C   
1269 C  C   B SER A 151 ? 0.1918 0.1238 0.1588 -0.0118 -0.0284 -0.0276 152 SER A C   
1270 O  O   A SER A 151 ? 0.1372 0.1388 0.1200 -0.0164 -0.0019 -0.0329 152 SER A O   
1271 O  O   B SER A 151 ? 0.1439 0.1458 0.1377 -0.0093 -0.0003 -0.0196 152 SER A O   
1272 C  CB  A SER A 151 ? 0.2002 0.2135 0.2484 -0.0758 -0.0115 -0.0177 152 SER A CB  
1273 C  CB  B SER A 151 ? 0.1643 0.1747 0.2490 -0.0280 0.0080  -0.0250 152 SER A CB  
1274 O  OG  A SER A 151 ? 0.2144 0.3300 0.2225 -0.0326 -0.0364 -0.0377 152 SER A OG  
1275 O  OG  B SER A 151 ? 0.1652 0.2524 0.2682 -0.0307 0.0194  0.0895  152 SER A OG  
1276 N  N   . ALA A 152 ? 0.1764 0.1360 0.1588 -0.0293 -0.0269 -0.0228 153 ALA A N   
1277 C  CA  . ALA A 152 ? 0.1799 0.1359 0.1553 -0.0017 -0.0228 -0.0214 153 ALA A CA  
1278 C  C   . ALA A 152 ? 0.1713 0.1499 0.1367 -0.0065 -0.0207 -0.0110 153 ALA A C   
1279 O  O   . ALA A 152 ? 0.1817 0.1557 0.1828 -0.0088 -0.0037 -0.0052 153 ALA A O   
1280 C  CB  . ALA A 152 ? 0.2509 0.1920 0.1494 0.0244  -0.0480 -0.0297 153 ALA A CB  
1281 N  N   . LYS A 153 ? 0.1767 0.1368 0.1684 -0.0054 -0.0395 0.0096  154 LYS A N   
1282 C  CA  . LYS A 153 ? 0.2332 0.1266 0.1727 0.0041  -0.0164 -0.0125 154 LYS A CA  
1283 C  C   . LYS A 153 ? 0.1791 0.1316 0.1609 -0.0109 -0.0041 -0.0255 154 LYS A C   
1284 O  O   . LYS A 153 ? 0.1588 0.1431 0.1391 -0.0015 -0.0239 -0.0074 154 LYS A O   
1285 C  CB  . LYS A 153 ? 0.2013 0.1330 0.1683 -0.0043 -0.0263 0.0070  154 LYS A CB  
1286 C  CG  . LYS A 153 ? 0.2531 0.1431 0.2016 0.0052  -0.0441 -0.0239 154 LYS A CG  
1287 C  CD  . LYS A 153 ? 0.2621 0.1596 0.2469 0.0126  -0.0553 -0.0564 154 LYS A CD  
1288 C  CE  . LYS A 153 ? 0.2669 0.1970 0.1715 -0.0010 -0.0368 -0.0313 154 LYS A CE  
1289 N  NZ  . LYS A 153 ? 0.2125 0.2517 0.2047 0.0229  -0.0120 -0.0194 154 LYS A NZ  
1290 N  N   A PRO A 154 ? 0.1849 0.1500 0.1921 -0.0146 -0.0110 -0.0040 155 PRO A N   
1291 N  N   B PRO A 154 ? 0.1871 0.1476 0.1891 -0.0170 -0.0206 -0.0081 155 PRO A N   
1292 C  CA  A PRO A 154 ? 0.1643 0.1823 0.2020 -0.0156 -0.0260 0.0038  155 PRO A CA  
1293 C  CA  B PRO A 154 ? 0.1603 0.1598 0.1803 -0.0114 -0.0342 -0.0131 155 PRO A CA  
1294 C  C   A PRO A 154 ? 0.1324 0.1958 0.1693 0.0125  -0.0390 -0.0087 155 PRO A C   
1295 C  C   B PRO A 154 ? 0.1394 0.1781 0.1413 0.0093  -0.0099 -0.0076 155 PRO A C   
1296 O  O   A PRO A 154 ? 0.1489 0.2610 0.2225 0.0399  -0.0474 0.0377  155 PRO A O   
1297 O  O   B PRO A 154 ? 0.1860 0.1731 0.1208 -0.0010 -0.0476 -0.0097 155 PRO A O   
1298 C  CB  A PRO A 154 ? 0.1541 0.2144 0.2515 -0.0419 -0.0121 0.0286  155 PRO A CB  
1299 C  CB  B PRO A 154 ? 0.1501 0.2155 0.2518 -0.0031 -0.0243 -0.0430 155 PRO A CB  
1300 C  CG  A PRO A 154 ? 0.1837 0.1367 0.2957 0.0109  0.0241  0.0057  155 PRO A CG  
1301 C  CG  B PRO A 154 ? 0.1853 0.2475 0.2716 -0.0164 0.0013  -0.0292 155 PRO A CG  
1302 C  CD  A PRO A 154 ? 0.2022 0.1781 0.2621 -0.0065 0.0331  0.0176  155 PRO A CD  
1303 C  CD  B PRO A 154 ? 0.2002 0.2308 0.2279 -0.0108 0.0142  -0.0403 155 PRO A CD  
1304 N  N   . GLY A 155 ? 0.1609 0.1571 0.1801 0.0237  -0.0153 -0.0035 156 GLY A N   
1305 C  CA  . GLY A 155 ? 0.1837 0.1465 0.1952 0.0057  -0.0154 -0.0013 156 GLY A CA  
1306 C  C   . GLY A 155 ? 0.2094 0.1464 0.1462 -0.0027 -0.0195 0.0130  156 GLY A C   
1307 O  O   . GLY A 155 ? 0.2263 0.1515 0.2389 0.0074  -0.0230 0.0320  156 GLY A O   
1308 N  N   . LEU A 156 ? 0.1624 0.1456 0.1535 -0.0062 -0.0153 -0.0065 157 LEU A N   
1309 C  CA  . LEU A 156 ? 0.1682 0.1202 0.1354 -0.0060 -0.0241 -0.0230 157 LEU A CA  
1310 C  C   . LEU A 156 ? 0.1553 0.1229 0.1356 -0.0125 -0.0271 -0.0071 157 LEU A C   
1311 O  O   . LEU A 156 ? 0.1694 0.1379 0.1312 -0.0249 -0.0264 -0.0200 157 LEU A O   
1312 C  CB  . LEU A 156 ? 0.1476 0.1419 0.1571 -0.0153 -0.0359 -0.0052 157 LEU A CB  
1313 C  CG  . LEU A 156 ? 0.1658 0.1456 0.1448 -0.0186 -0.0273 -0.0043 157 LEU A CG  
1314 C  CD1 . LEU A 156 ? 0.1986 0.1746 0.1580 -0.0410 -0.0370 -0.0115 157 LEU A CD1 
1315 C  CD2 . LEU A 156 ? 0.1977 0.1808 0.1467 -0.0126 -0.0205 0.0017  157 LEU A CD2 
1316 N  N   . GLN A 157 ? 0.1790 0.1577 0.1298 -0.0309 -0.0276 -0.0109 158 GLN A N   
1317 C  CA  . GLN A 157 ? 0.1803 0.1611 0.1280 -0.0304 -0.0148 -0.0252 158 GLN A CA  
1318 C  C   . GLN A 157 ? 0.1819 0.1544 0.1476 -0.0241 -0.0460 -0.0205 158 GLN A C   
1319 O  O   . GLN A 157 ? 0.1764 0.1632 0.1421 -0.0102 -0.0284 -0.0247 158 GLN A O   
1320 C  CB  . GLN A 157 ? 0.2076 0.1620 0.1724 -0.0443 -0.0285 -0.0308 158 GLN A CB  
1321 C  CG  . GLN A 157 ? 0.2292 0.1661 0.1701 -0.0211 -0.0417 -0.0335 158 GLN A CG  
1322 C  CD  . GLN A 157 ? 0.1977 0.1324 0.1764 -0.0335 -0.0241 -0.0192 158 GLN A CD  
1323 O  OE1 . GLN A 157 ? 0.2490 0.1582 0.1465 -0.0046 -0.0296 -0.0131 158 GLN A OE1 
1324 N  NE2 . GLN A 157 ? 0.2405 0.1903 0.1652 -0.0211 -0.0209 -0.0344 158 GLN A NE2 
1325 N  N   . LYS A 158 ? 0.1850 0.1754 0.1348 -0.0185 -0.0384 -0.0019 159 LYS A N   
1326 C  CA  . LYS A 158 ? 0.2055 0.1738 0.1706 0.0043  -0.0502 0.0189  159 LYS A CA  
1327 C  C   . LYS A 158 ? 0.1885 0.1525 0.1243 -0.0162 -0.0240 -0.0006 159 LYS A C   
1328 O  O   . LYS A 158 ? 0.2065 0.1986 0.1340 -0.0243 -0.0406 0.0020  159 LYS A O   
1329 C  CB  . LYS A 158 ? 0.2483 0.1920 0.2142 -0.0088 -0.0644 0.0612  159 LYS A CB  
1330 C  CG  . LYS A 158 ? 0.3546 0.3984 0.2644 0.0331  -0.0842 0.0812  159 LYS A CG  
1331 C  CD  . LYS A 158 ? 0.2770 0.4596 0.6693 0.0575  -0.1907 0.0899  159 LYS A CD  
1332 C  CE  . LYS A 158 ? 0.6848 0.6459 0.3057 -0.0948 -0.2365 0.0469  159 LYS A CE  
1333 N  NZ  . LYS A 158 ? 1.0289 0.6722 0.5367 -0.0049 0.0579  0.0478  159 LYS A NZ  
1334 N  N   . VAL A 159 ? 0.2011 0.1559 0.1252 -0.0068 -0.0388 -0.0170 160 VAL A N   
1335 C  CA  . VAL A 159 ? 0.1835 0.1306 0.1220 -0.0198 -0.0153 -0.0129 160 VAL A CA  
1336 C  C   . VAL A 159 ? 0.1788 0.1330 0.1298 -0.0231 -0.0209 -0.0146 160 VAL A C   
1337 O  O   . VAL A 159 ? 0.1887 0.1582 0.1463 -0.0142 -0.0175 -0.0164 160 VAL A O   
1338 C  CB  . VAL A 159 ? 0.1823 0.1518 0.1318 -0.0166 -0.0260 -0.0142 160 VAL A CB  
1339 C  CG1 . VAL A 159 ? 0.1943 0.1782 0.1729 -0.0328 -0.0208 0.0057  160 VAL A CG1 
1340 C  CG2 . VAL A 159 ? 0.2498 0.1506 0.1342 0.0000  -0.0264 -0.0252 160 VAL A CG2 
1341 N  N   . VAL A 160 ? 0.1861 0.1350 0.1266 -0.0124 -0.0197 -0.0247 161 VAL A N   
1342 C  CA  . VAL A 160 ? 0.2246 0.1537 0.1458 0.0052  0.0019  -0.0082 161 VAL A CA  
1343 C  C   . VAL A 160 ? 0.2074 0.1428 0.1620 -0.0266 0.0035  -0.0482 161 VAL A C   
1344 O  O   . VAL A 160 ? 0.2204 0.1823 0.1814 -0.0310 0.0077  -0.0281 161 VAL A O   
1345 C  CB  . VAL A 160 ? 0.2479 0.1542 0.1682 0.0065  0.0051  -0.0263 161 VAL A CB  
1346 C  CG1 . VAL A 160 ? 0.2637 0.1677 0.2380 -0.0340 -0.0436 -0.0357 161 VAL A CG1 
1347 C  CG2 . VAL A 160 ? 0.2322 0.1738 0.1652 0.0211  0.0206  -0.0155 161 VAL A CG2 
1348 N  N   . ASP A 161 ? 0.2314 0.1792 0.1233 -0.0381 -0.0219 -0.0131 162 ASP A N   
1349 C  CA  . ASP A 161 ? 0.2511 0.2249 0.1255 -0.0719 -0.0175 -0.0159 162 ASP A CA  
1350 C  C   . ASP A 161 ? 0.2773 0.2171 0.1212 -0.0498 -0.0024 -0.0215 162 ASP A C   
1351 O  O   . ASP A 161 ? 0.3847 0.2770 0.1667 -0.0966 0.0491  -0.0381 162 ASP A O   
1352 C  CB  . ASP A 161 ? 0.2982 0.2739 0.1797 -0.0425 -0.0524 -0.0582 162 ASP A CB  
1353 C  CG  . ASP A 161 ? 0.3161 0.2522 0.1643 -0.0156 -0.0178 -0.0309 162 ASP A CG  
1354 O  OD1 . ASP A 161 ? 0.3467 0.2601 0.3016 -0.0522 -0.0745 -0.0515 162 ASP A OD1 
1355 O  OD2 . ASP A 161 ? 0.3091 0.3452 0.2325 -0.0104 -0.0496 -0.0469 162 ASP A OD2 
1356 N  N   . VAL A 162 ? 0.2380 0.1779 0.1218 -0.0153 -0.0372 -0.0221 163 VAL A N   
1357 C  CA  . VAL A 162 ? 0.2326 0.1985 0.1685 -0.0132 -0.0511 0.0010  163 VAL A CA  
1358 C  C   . VAL A 162 ? 0.2217 0.1553 0.1300 -0.0219 -0.0063 0.0186  163 VAL A C   
1359 O  O   . VAL A 162 ? 0.2454 0.2006 0.1234 -0.0274 0.0060  -0.0013 163 VAL A O   
1360 C  CB  . VAL A 162 ? 0.2426 0.1922 0.1873 -0.0035 -0.0232 0.0024  163 VAL A CB  
1361 C  CG1 . VAL A 162 ? 0.2247 0.1867 0.1776 -0.0274 -0.0104 -0.0129 163 VAL A CG1 
1362 C  CG2 . VAL A 162 ? 0.3136 0.2056 0.2196 0.0092  0.0093  0.0370  163 VAL A CG2 
1363 N  N   . LEU A 163 ? 0.2092 0.1481 0.1439 -0.0307 -0.0324 0.0065  164 LEU A N   
1364 C  CA  . LEU A 163 ? 0.2178 0.1492 0.1186 0.0027  0.0142  0.0027  164 LEU A CA  
1365 C  C   . LEU A 163 ? 0.2099 0.1668 0.1454 -0.0093 -0.0027 -0.0147 164 LEU A C   
1366 O  O   . LEU A 163 ? 0.2387 0.1765 0.1202 -0.0034 0.0160  0.0192  164 LEU A O   
1367 C  CB  . LEU A 163 ? 0.2038 0.1494 0.1431 0.0060  0.0038  0.0060  164 LEU A CB  
1368 C  CG  . LEU A 163 ? 0.1988 0.1527 0.1248 -0.0097 0.0003  0.0151  164 LEU A CG  
1369 C  CD1 . LEU A 163 ? 0.2078 0.1476 0.1667 -0.0081 -0.0251 0.0263  164 LEU A CD1 
1370 C  CD2 . LEU A 163 ? 0.2019 0.1622 0.1168 0.0043  -0.0186 -0.0108 164 LEU A CD2 
1371 N  N   . ASP A 164 ? 0.3077 0.1855 0.1318 -0.0351 0.0103  -0.0335 165 ASP A N   
1372 C  CA  . ASP A 164 ? 0.3844 0.2200 0.1928 -0.0242 0.0513  -0.0606 165 ASP A CA  
1373 C  C   . ASP A 164 ? 0.3023 0.2691 0.1340 -0.0043 0.0115  -0.0013 165 ASP A C   
1374 O  O   . ASP A 164 ? 0.3630 0.2583 0.2497 0.0423  0.0837  -0.0098 165 ASP A O   
1375 C  CB  . ASP A 164 ? 0.4530 0.3066 0.2256 -0.0452 0.0228  -0.1330 165 ASP A CB  
1376 C  CG  . ASP A 164 ? 0.4804 0.4681 0.4167 -0.2495 -0.0515 -0.0535 165 ASP A CG  
1377 O  OD1 . ASP A 164 ? 0.7124 0.7821 0.2793 -0.2612 0.0775  0.0348  165 ASP A OD1 
1378 O  OD2 . ASP A 164 ? 0.8306 1.3516 0.4198 -0.3118 -0.0194 -0.5580 165 ASP A OD2 
1379 N  N   . SER A 165 ? 0.2333 0.2324 0.1359 -0.0348 -0.0254 0.0141  166 SER A N   
1380 C  CA  . SER A 165 ? 0.2315 0.2335 0.1124 -0.0104 -0.0043 -0.0068 166 SER A CA  
1381 C  C   . SER A 165 ? 0.1950 0.2011 0.1215 0.0043  0.0031  0.0186  166 SER A C   
1382 O  O   . SER A 165 ? 0.2606 0.2083 0.1202 -0.0041 -0.0146 0.0373  166 SER A O   
1383 C  CB  . SER A 165 ? 0.2560 0.3007 0.1430 -0.0027 -0.0087 -0.0041 166 SER A CB  
1384 O  OG  . SER A 165 ? 0.2518 0.2487 0.1832 0.0232  -0.0136 0.0401  166 SER A OG  
1385 N  N   . ILE A 166 ? 0.2079 0.1835 0.0975 0.0010  0.0007  0.0204  167 ILE A N   
1386 C  CA  . ILE A 166 ? 0.1764 0.1661 0.1360 -0.0076 0.0048  0.0035  167 ILE A CA  
1387 C  C   . ILE A 166 ? 0.1643 0.1571 0.0956 0.0074  0.0020  -0.0046 167 ILE A C   
1388 O  O   . ILE A 166 ? 0.1868 0.1562 0.1026 -0.0063 0.0027  0.0130  167 ILE A O   
1389 C  CB  . ILE A 166 ? 0.1914 0.1536 0.1096 -0.0091 -0.0060 0.0131  167 ILE A CB  
1390 C  CG1 . ILE A 166 ? 0.1880 0.1779 0.0954 -0.0210 -0.0063 0.0020  167 ILE A CG1 
1391 C  CG2 . ILE A 166 ? 0.2088 0.1808 0.1431 -0.0031 -0.0225 0.0233  167 ILE A CG2 
1392 C  CD1 . ILE A 166 ? 0.2004 0.1782 0.1094 -0.0104 0.0186  -0.0063 167 ILE A CD1 
1393 N  N   . LYS A 167 ? 0.1928 0.1553 0.1225 0.0027  0.0188  0.0148  168 LYS A N   
1394 C  CA  . LYS A 167 ? 0.1641 0.1738 0.1289 0.0096  -0.0046 -0.0126 168 LYS A CA  
1395 C  C   . LYS A 167 ? 0.1745 0.1528 0.1166 0.0060  0.0298  0.0216  168 LYS A C   
1396 O  O   . LYS A 167 ? 0.1918 0.1401 0.1215 -0.0104 0.0012  0.0035  168 LYS A O   
1397 C  CB  . LYS A 167 ? 0.2240 0.1782 0.1332 0.0038  -0.0207 -0.0474 168 LYS A CB  
1398 C  CG  . LYS A 167 ? 0.2275 0.1722 0.1677 -0.0115 0.0209  -0.0412 168 LYS A CG  
1399 C  CD  . LYS A 167 ? 0.3361 0.2257 0.2372 0.0077  -0.0333 -0.0825 168 LYS A CD  
1400 C  CE  . LYS A 167 ? 0.4210 0.2967 0.2673 0.0304  0.0052  -0.0588 168 LYS A CE  
1401 N  NZ  . LYS A 167 ? 0.5565 0.4025 0.3596 -0.0250 0.0577  -0.1659 168 LYS A NZ  
1402 N  N   . THR A 168 ? 0.1740 0.1589 0.1270 -0.0059 0.0000  0.0276  169 THR A N   
1403 C  CA  . THR A 168 ? 0.1704 0.1553 0.1190 0.0012  0.0308  0.0186  169 THR A CA  
1404 C  C   . THR A 168 ? 0.1523 0.1641 0.1045 -0.0027 0.0176  0.0152  169 THR A C   
1405 O  O   . THR A 168 ? 0.1832 0.1532 0.1410 -0.0043 0.0206  0.0296  169 THR A O   
1406 C  CB  . THR A 168 ? 0.1999 0.1703 0.1509 0.0164  0.0303  0.0177  169 THR A CB  
1407 O  OG1 . THR A 168 ? 0.2142 0.2200 0.1191 0.0027  0.0364  0.0142  169 THR A OG1 
1408 C  CG2 . THR A 168 ? 0.2340 0.1900 0.1684 0.0118  0.0645  0.0071  169 THR A CG2 
1409 N  N   A LYS A 169 ? 0.1835 0.1600 0.1293 -0.0281 0.0313  0.0119  170 LYS A N   
1410 N  N   B LYS A 169 ? 0.1991 0.1743 0.1352 -0.0366 0.0355  0.0142  170 LYS A N   
1411 C  CA  A LYS A 169 ? 0.1352 0.1370 0.1474 -0.0052 0.0252  0.0137  170 LYS A CA  
1412 C  CA  B LYS A 169 ? 0.1898 0.1616 0.1568 -0.0162 0.0299  0.0060  170 LYS A CA  
1413 C  C   A LYS A 169 ? 0.1588 0.1652 0.1033 -0.0227 0.0322  0.0275  170 LYS A C   
1414 C  C   B LYS A 169 ? 0.1676 0.2108 0.1431 -0.0285 0.0006  0.0533  170 LYS A C   
1415 O  O   A LYS A 169 ? 0.1271 0.1458 0.1014 -0.0208 0.0164  0.0333  170 LYS A O   
1416 O  O   B LYS A 169 ? 0.2361 0.2527 0.1438 -0.0615 0.0175  0.0063  170 LYS A O   
1417 C  CB  A LYS A 169 ? 0.1415 0.1585 0.1433 -0.0173 0.0406  0.0379  170 LYS A CB  
1418 C  CB  B LYS A 169 ? 0.2231 0.1372 0.1643 0.0276  0.0109  0.0142  170 LYS A CB  
1419 C  CG  A LYS A 169 ? 0.1779 0.1913 0.1618 0.0006  -0.0054 0.0375  170 LYS A CG  
1420 C  CG  B LYS A 169 ? 0.2096 0.1612 0.1729 -0.0273 0.0317  0.0384  170 LYS A CG  
1421 C  CD  A LYS A 169 ? 0.1932 0.2422 0.2239 0.0471  0.0017  0.0317  170 LYS A CD  
1422 C  CD  B LYS A 169 ? 0.2833 0.1385 0.1712 -0.0080 0.0286  0.0627  170 LYS A CD  
1423 C  CE  A LYS A 169 ? 0.2311 0.2808 0.3041 -0.1194 -0.0414 0.0697  170 LYS A CE  
1424 C  CE  B LYS A 169 ? 0.1905 0.2953 0.2655 -0.0288 0.0249  0.0584  170 LYS A CE  
1425 N  NZ  A LYS A 169 ? 0.2763 0.3980 0.3546 -0.0148 -0.0399 0.0593  170 LYS A NZ  
1426 N  NZ  B LYS A 169 ? 0.2854 0.3912 0.2899 0.0527  -0.0489 0.0395  170 LYS A NZ  
1427 N  N   . GLY A 170 ? 0.2144 0.1562 0.1621 -0.0309 0.0174  0.0249  171 GLY A N   
1428 C  CA  . GLY A 170 ? 0.2011 0.1512 0.1931 -0.0049 -0.0102 0.0478  171 GLY A CA  
1429 C  C   . GLY A 170 ? 0.2235 0.1501 0.1447 -0.0147 0.0041  0.0419  171 GLY A C   
1430 O  O   . GLY A 170 ? 0.2447 0.1627 0.2307 -0.0237 -0.0076 0.0608  171 GLY A O   
1431 N  N   . LYS A 171 ? 0.1668 0.1543 0.1562 -0.0125 0.0063  0.0386  172 LYS A N   
1432 C  CA  . LYS A 171 ? 0.1846 0.1659 0.1632 -0.0093 0.0221  0.0461  172 LYS A CA  
1433 C  C   . LYS A 171 ? 0.1625 0.1679 0.1085 0.0043  0.0109  0.0240  172 LYS A C   
1434 O  O   . LYS A 171 ? 0.1861 0.1780 0.1049 -0.0052 0.0170  0.0298  172 LYS A O   
1435 C  CB  . LYS A 171 ? 0.2004 0.1852 0.1272 0.0060  0.0163  0.0085  172 LYS A CB  
1436 C  CG  . LYS A 171 ? 0.1941 0.2285 0.1639 -0.0017 0.0130  -0.0097 172 LYS A CG  
1437 C  CD  . LYS A 171 ? 0.2935 0.2476 0.2343 0.0375  0.0085  -0.0381 172 LYS A CD  
1438 C  CE  . LYS A 171 ? 0.3528 0.3840 0.2845 0.0317  -0.0037 -0.0015 172 LYS A CE  
1439 N  NZ  . LYS A 171 ? 0.5342 0.3224 0.2538 -0.0353 0.0917  0.0040  172 LYS A NZ  
1440 N  N   . SER A 172 ? 0.2054 0.1916 0.1474 0.0031  -0.0043 0.0680  173 SER A N   
1441 C  CA  . SER A 172 ? 0.1803 0.1931 0.1703 0.0126  0.0082  0.0281  173 SER A CA  
1442 C  C   . SER A 172 ? 0.1706 0.1950 0.1348 0.0142  -0.0148 0.0443  173 SER A C   
1443 O  O   . SER A 172 ? 0.2236 0.2502 0.1127 0.0192  -0.0043 0.0322  173 SER A O   
1444 C  CB  . SER A 172 ? 0.2405 0.2087 0.1388 0.0071  0.0339  0.0206  173 SER A CB  
1445 O  OG  . SER A 172 ? 0.3179 0.2196 0.1850 0.0041  0.0023  0.0526  173 SER A OG  
1446 N  N   . ALA A 173 ? 0.1746 0.2178 0.1527 0.0272  -0.0087 0.0221  174 ALA A N   
1447 C  CA  . ALA A 173 ? 0.1670 0.2380 0.1391 0.0258  -0.0264 0.0403  174 ALA A CA  
1448 C  C   . ALA A 173 ? 0.1773 0.2049 0.1351 0.0159  -0.0306 0.0182  174 ALA A C   
1449 O  O   . ALA A 173 ? 0.1728 0.1918 0.1127 0.0046  -0.0186 0.0208  174 ALA A O   
1450 C  CB  . ALA A 173 ? 0.2459 0.2459 0.1620 0.0026  -0.0342 -0.0171 174 ALA A CB  
1451 N  N   . ASP A 174 ? 0.2131 0.2678 0.1202 0.0344  -0.0154 0.0555  175 ASP A N   
1452 C  CA  . ASP A 174 ? 0.2013 0.2304 0.1325 0.0346  -0.0119 0.0432  175 ASP A CA  
1453 C  C   . ASP A 174 ? 0.1833 0.2037 0.1782 0.0104  -0.0375 0.0320  175 ASP A C   
1454 O  O   . ASP A 174 ? 0.2390 0.2337 0.1808 0.0087  0.0060  -0.0087 175 ASP A O   
1455 C  CB  . ASP A 174 ? 0.2144 0.2691 0.2250 0.0326  -0.0388 0.0513  175 ASP A CB  
1456 C  CG  . ASP A 174 ? 0.3555 0.2971 0.2529 -0.0269 -0.0671 0.0820  175 ASP A CG  
1457 O  OD1 . ASP A 174 ? 0.5235 0.4914 0.3140 -0.1878 -0.0974 0.0434  175 ASP A OD1 
1458 O  OD2 . ASP A 174 ? 0.3233 0.3235 0.2691 -0.0195 -0.0447 0.0705  175 ASP A OD2 
1459 N  N   . PHE A 175 ? 0.1666 0.2122 0.1464 0.0026  -0.0017 0.0161  176 PHE A N   
1460 C  CA  . PHE A 175 ? 0.1632 0.1823 0.1611 0.0131  0.0031  0.0305  176 PHE A CA  
1461 C  C   . PHE A 175 ? 0.1860 0.1428 0.1491 -0.0049 -0.0243 0.0043  176 PHE A C   
1462 O  O   . PHE A 175 ? 0.2304 0.2242 0.1523 0.0461  -0.0439 -0.0233 176 PHE A O   
1463 C  CB  . PHE A 175 ? 0.1986 0.1772 0.1711 -0.0012 -0.0051 0.0203  176 PHE A CB  
1464 C  CG  . PHE A 175 ? 0.1884 0.1568 0.1573 0.0274  -0.0159 0.0119  176 PHE A CG  
1465 C  CD1 . PHE A 175 ? 0.2879 0.1713 0.1702 0.0076  0.0187  -0.0137 176 PHE A CD1 
1466 C  CD2 . PHE A 175 ? 0.1932 0.1577 0.1499 -0.0093 -0.0339 0.0276  176 PHE A CD2 
1467 C  CE1 . PHE A 175 ? 0.3088 0.1668 0.2293 0.0118  0.0485  0.0252  176 PHE A CE1 
1468 C  CE2 . PHE A 175 ? 0.2293 0.1611 0.1792 0.0034  -0.0357 0.0298  176 PHE A CE2 
1469 C  CZ  . PHE A 175 ? 0.2592 0.1546 0.1902 0.0043  -0.0340 0.0020  176 PHE A CZ  
1470 N  N   . THR A 176 ? 0.1898 0.1920 0.1330 0.0173  -0.0110 0.0340  177 THR A N   
1471 C  CA  . THR A 176 ? 0.1788 0.1597 0.1413 0.0271  -0.0170 0.0295  177 THR A CA  
1472 C  C   . THR A 176 ? 0.1859 0.1433 0.1261 0.0108  -0.0199 0.0370  177 THR A C   
1473 O  O   . THR A 176 ? 0.2175 0.1512 0.1255 -0.0038 -0.0281 0.0241  177 THR A O   
1474 C  CB  . THR A 176 ? 0.1943 0.2047 0.1500 -0.0030 -0.0386 0.0533  177 THR A CB  
1475 O  OG1 . THR A 176 ? 0.3928 0.2678 0.1446 0.0737  -0.0640 0.0645  177 THR A OG1 
1476 C  CG2 . THR A 176 ? 0.2612 0.2405 0.3217 0.0178  -0.0070 0.1254  177 THR A CG2 
1477 N  N   . ASN A 177 ? 0.1844 0.1729 0.1208 0.0140  -0.0221 0.0240  178 ASN A N   
1478 C  CA  . ASN A 177 ? 0.1898 0.1835 0.1465 -0.0125 -0.0491 0.0372  178 ASN A CA  
1479 C  C   . ASN A 177 ? 0.1715 0.1691 0.1411 -0.0080 -0.0272 0.0392  178 ASN A C   
1480 O  O   . ASN A 177 ? 0.2450 0.2222 0.2673 -0.0384 -0.0648 0.1023  178 ASN A O   
1481 C  CB  . ASN A 177 ? 0.1898 0.1773 0.1685 -0.0027 -0.0469 0.0509  178 ASN A CB  
1482 C  CG  . ASN A 177 ? 0.1948 0.1904 0.1536 0.0121  -0.0395 0.0285  178 ASN A CG  
1483 O  OD1 . ASN A 177 ? 0.2369 0.2022 0.2083 0.0296  0.0109  0.0527  178 ASN A OD1 
1484 N  ND2 . ASN A 177 ? 0.2364 0.1995 0.1607 0.0076  -0.0410 0.0577  178 ASN A ND2 
1485 N  N   . PHE A 178 ? 0.1799 0.1537 0.1221 0.0051  -0.0328 0.0187  179 PHE A N   
1486 C  CA  . PHE A 178 ? 0.2000 0.1483 0.1208 0.0027  -0.0272 0.0384  179 PHE A CA  
1487 C  C   . PHE A 178 ? 0.1639 0.1555 0.1268 -0.0076 -0.0417 0.0081  179 PHE A C   
1488 O  O   . PHE A 178 ? 0.2153 0.1534 0.1181 -0.0162 -0.0329 0.0271  179 PHE A O   
1489 C  CB  . PHE A 178 ? 0.2268 0.1546 0.1233 0.0007  -0.0082 0.0348  179 PHE A CB  
1490 C  CG  . PHE A 178 ? 0.1977 0.1492 0.1245 0.0003  -0.0197 0.0355  179 PHE A CG  
1491 C  CD1 . PHE A 178 ? 0.2232 0.1598 0.1509 0.0136  -0.0183 0.0216  179 PHE A CD1 
1492 C  CD2 . PHE A 178 ? 0.1606 0.1546 0.1224 -0.0027 -0.0171 0.0238  179 PHE A CD2 
1493 C  CE1 . PHE A 178 ? 0.2437 0.1555 0.1527 0.0154  -0.0238 0.0281  179 PHE A CE1 
1494 C  CE2 . PHE A 178 ? 0.1518 0.1437 0.1333 -0.0099 -0.0154 0.0320  179 PHE A CE2 
1495 C  CZ  . PHE A 178 ? 0.1782 0.1536 0.1409 -0.0026 -0.0152 0.0141  179 PHE A CZ  
1496 N  N   . ASP A 179 ? 0.1607 0.1571 0.1324 0.0103  -0.0263 0.0219  180 ASP A N   
1497 C  CA  . ASP A 179 ? 0.1668 0.1712 0.1159 0.0151  -0.0419 0.0241  180 ASP A CA  
1498 C  C   . ASP A 179 ? 0.1676 0.1284 0.1323 -0.0003 -0.0118 0.0020  180 ASP A C   
1499 O  O   . ASP A 179 ? 0.1887 0.1456 0.1325 0.0031  -0.0230 0.0060  180 ASP A O   
1500 C  CB  . ASP A 179 ? 0.1650 0.2002 0.1738 0.0153  -0.0439 0.0226  180 ASP A CB  
1501 C  CG  . ASP A 179 ? 0.1676 0.2181 0.1850 0.0227  -0.0339 0.0076  180 ASP A CG  
1502 O  OD1 . ASP A 179 ? 0.1835 0.1904 0.1685 0.0296  -0.0186 0.0252  180 ASP A OD1 
1503 O  OD2 . ASP A 179 ? 0.1928 0.3995 0.2332 0.0013  -0.0217 -0.0366 180 ASP A OD2 
1504 N  N   . PRO A 180 ? 0.1462 0.1321 0.1096 -0.0015 -0.0031 0.0197  181 PRO A N   
1505 C  CA  . PRO A 180 ? 0.1546 0.1386 0.1342 0.0003  -0.0166 0.0362  181 PRO A CA  
1506 C  C   . PRO A 180 ? 0.1449 0.1375 0.1115 -0.0031 -0.0153 0.0204  181 PRO A C   
1507 O  O   . PRO A 180 ? 0.1492 0.1411 0.1262 0.0003  -0.0216 0.0239  181 PRO A O   
1508 C  CB  . PRO A 180 ? 0.1469 0.1704 0.1474 -0.0082 -0.0220 0.0132  181 PRO A CB  
1509 C  CG  . PRO A 180 ? 0.1826 0.1630 0.1465 -0.0124 -0.0247 0.0118  181 PRO A CG  
1510 C  CD  . PRO A 180 ? 0.1625 0.1483 0.1334 -0.0087 -0.0344 0.0103  181 PRO A CD  
1511 N  N   . ARG A 181 ? 0.1431 0.1551 0.1280 0.0070  -0.0181 0.0222  182 ARG A N   
1512 C  CA  . ARG A 181 ? 0.1304 0.1573 0.1472 0.0003  -0.0219 0.0068  182 ARG A CA  
1513 C  C   . ARG A 181 ? 0.1327 0.1685 0.1360 -0.0104 -0.0282 0.0230  182 ARG A C   
1514 O  O   . ARG A 181 ? 0.1494 0.1747 0.1792 -0.0024 -0.0126 0.0399  182 ARG A O   
1515 C  CB  . ARG A 181 ? 0.1404 0.1717 0.1603 0.0010  -0.0046 0.0087  182 ARG A CB  
1516 C  CG  . ARG A 181 ? 0.1519 0.1805 0.1905 0.0010  -0.0057 -0.0108 182 ARG A CG  
1517 C  CD  . ARG A 181 ? 0.1950 0.2177 0.2119 0.0205  0.0239  0.0038  182 ARG A CD  
1518 N  NE  . ARG A 181 ? 0.1864 0.2184 0.2246 0.0244  0.0038  0.0538  182 ARG A NE  
1519 C  CZ  . ARG A 181 ? 0.1975 0.2371 0.2397 0.0250  0.0295  0.0480  182 ARG A CZ  
1520 N  NH1 . ARG A 181 ? 0.2268 0.2948 0.3075 0.0546  0.0452  0.0471  182 ARG A NH1 
1521 N  NH2 . ARG A 181 ? 0.2308 0.3598 0.2978 0.0469  -0.0038 0.1251  182 ARG A NH2 
1522 N  N   . GLY A 182 ? 0.1424 0.1686 0.1381 0.0110  -0.0318 0.0135  183 GLY A N   
1523 C  CA  . GLY A 182 ? 0.1720 0.1474 0.1837 -0.0177 -0.0449 0.0175  183 GLY A CA  
1524 C  C   . GLY A 182 ? 0.1668 0.1395 0.1792 -0.0020 -0.0474 0.0163  183 GLY A C   
1525 O  O   . GLY A 182 ? 0.2128 0.1553 0.2500 -0.0057 -0.0961 0.0041  183 GLY A O   
1526 N  N   . LEU A 183 ? 0.1494 0.1512 0.1422 -0.0010 -0.0375 0.0182  184 LEU A N   
1527 C  CA  . LEU A 183 ? 0.1479 0.1322 0.1634 0.0086  -0.0296 0.0015  184 LEU A CA  
1528 C  C   . LEU A 183 ? 0.1433 0.1406 0.1384 -0.0137 -0.0408 0.0034  184 LEU A C   
1529 O  O   . LEU A 183 ? 0.1621 0.1569 0.1727 0.0088  -0.0384 0.0296  184 LEU A O   
1530 C  CB  . LEU A 183 ? 0.1506 0.1661 0.1233 0.0163  -0.0243 0.0143  184 LEU A CB  
1531 C  CG  . LEU A 183 ? 0.1701 0.1805 0.1377 0.0185  -0.0263 0.0167  184 LEU A CG  
1532 C  CD1 . LEU A 183 ? 0.1747 0.2393 0.1372 0.0302  -0.0263 0.0383  184 LEU A CD1 
1533 C  CD2 . LEU A 183 ? 0.2484 0.2067 0.1456 0.0143  -0.0230 -0.0331 184 LEU A CD2 
1534 N  N   A LEU A 184 ? 0.1661 0.1507 0.1507 -0.0068 -0.0109 0.0274  185 LEU A N   
1535 N  N   B LEU A 184 ? 0.1625 0.1336 0.1439 -0.0049 -0.0270 0.0372  185 LEU A N   
1536 C  CA  A LEU A 184 ? 0.1444 0.1273 0.1392 -0.0214 -0.0388 0.0104  185 LEU A CA  
1537 C  CA  B LEU A 184 ? 0.1327 0.1321 0.1424 -0.0175 -0.0098 0.0417  185 LEU A CA  
1538 C  C   A LEU A 184 ? 0.1172 0.1330 0.1254 -0.0006 -0.0063 0.0057  185 LEU A C   
1539 C  C   B LEU A 184 ? 0.1527 0.0979 0.1190 0.0010  -0.0023 0.0027  185 LEU A C   
1540 O  O   A LEU A 184 ? 0.1212 0.1367 0.1087 -0.0098 -0.0093 0.0107  185 LEU A O   
1541 O  O   B LEU A 184 ? 0.1291 0.1442 0.1409 -0.0012 -0.0254 0.0063  185 LEU A O   
1542 C  CB  A LEU A 184 ? 0.1159 0.1316 0.1569 0.0003  -0.0218 -0.0026 185 LEU A CB  
1543 C  CB  B LEU A 184 ? 0.1145 0.1492 0.1473 -0.0054 -0.0346 0.0250  185 LEU A CB  
1544 C  CG  A LEU A 184 ? 0.0957 0.1645 0.1448 -0.0082 0.0031  0.0232  185 LEU A CG  
1545 C  CG  B LEU A 184 ? 0.1206 0.1598 0.1413 -0.0120 -0.0241 0.0104  185 LEU A CG  
1546 C  CD1 A LEU A 184 ? 0.1376 0.1810 0.1377 -0.0068 -0.0071 0.0114  185 LEU A CD1 
1547 C  CD1 B LEU A 184 ? 0.1402 0.1634 0.1537 0.0057  0.0137  0.0516  185 LEU A CD1 
1548 C  CD2 A LEU A 184 ? 0.0992 0.1455 0.1313 -0.0026 -0.0017 0.0000  185 LEU A CD2 
1549 C  CD2 B LEU A 184 ? 0.1150 0.1743 0.1412 0.0074  -0.0439 -0.0060 185 LEU A CD2 
1550 N  N   A PRO A 185 ? 0.1085 0.1254 0.1282 0.0054  0.0118  0.0130  186 PRO A N   
1551 N  N   B PRO A 185 ? 0.1142 0.1089 0.1289 0.0088  -0.0384 0.0031  186 PRO A N   
1552 C  CA  A PRO A 185 ? 0.1293 0.1121 0.1336 0.0030  -0.0043 0.0026  186 PRO A CA  
1553 C  CA  B PRO A 185 ? 0.1658 0.1236 0.1102 -0.0124 -0.0136 0.0052  186 PRO A CA  
1554 C  C   A PRO A 185 ? 0.1057 0.1279 0.1252 -0.0219 -0.0121 0.0000  186 PRO A C   
1555 C  C   B PRO A 185 ? 0.1339 0.1300 0.1187 -0.0181 -0.0483 0.0206  186 PRO A C   
1556 O  O   A PRO A 185 ? 0.0746 0.1212 0.1118 -0.0035 -0.0013 0.0085  186 PRO A O   
1557 O  O   B PRO A 185 ? 0.1111 0.1360 0.1550 0.0060  -0.0227 -0.0057 186 PRO A O   
1558 C  CB  A PRO A 185 ? 0.1386 0.1288 0.1517 0.0241  -0.0183 0.0026  186 PRO A CB  
1559 C  CB  B PRO A 185 ? 0.1279 0.1005 0.1225 -0.0071 -0.0043 -0.0147 186 PRO A CB  
1560 C  CG  A PRO A 185 ? 0.1084 0.1431 0.1242 -0.0046 -0.0098 -0.0071 186 PRO A CG  
1561 C  CG  B PRO A 185 ? 0.0957 0.1067 0.1177 0.0003  -0.0186 0.0000  186 PRO A CG  
1562 C  CD  A PRO A 185 ? 0.1128 0.1474 0.1439 0.0239  -0.0285 0.0271  186 PRO A CD  
1563 C  CD  B PRO A 185 ? 0.1111 0.1136 0.1234 0.0104  -0.0219 -0.0087 186 PRO A CD  
1564 N  N   . GLU A 186 ? 0.1650 0.1395 0.1761 -0.0310 -0.0221 0.0335  187 GLU A N   
1565 C  CA  . GLU A 186 ? 0.1141 0.1596 0.1837 -0.0331 -0.0287 0.0226  187 GLU A CA  
1566 C  C   . GLU A 186 ? 0.1020 0.1435 0.1959 -0.0142 -0.0153 0.0120  187 GLU A C   
1567 O  O   . GLU A 186 ? 0.1273 0.1965 0.2362 0.0109  -0.0092 0.0249  187 GLU A O   
1568 C  CB  . GLU A 186 ? 0.1573 0.2009 0.2551 -0.0610 -0.0759 0.0183  187 GLU A CB  
1569 C  CG  . GLU A 186 ? 0.2254 0.2253 0.3285 0.0148  -0.0340 0.0173  187 GLU A CG  
1570 C  CD  . GLU A 186 ? 0.2203 0.3240 0.3075 -0.0102 -0.0219 0.0131  187 GLU A CD  
1571 O  OE1 . GLU A 186 ? 0.1544 0.2761 0.3864 -0.0546 -0.0285 -0.0129 187 GLU A OE1 
1572 O  OE2 . GLU A 186 ? 0.2845 0.3012 0.4248 0.0359  0.0644  0.1093  187 GLU A OE2 
1573 N  N   . SER A 187 ? 0.0929 0.1454 0.1756 -0.0159 -0.0252 0.0197  188 SER A N   
1574 C  CA  . SER A 187 ? 0.0952 0.1499 0.1819 -0.0185 -0.0108 0.0046  188 SER A CA  
1575 C  C   . SER A 187 ? 0.0724 0.1546 0.1724 -0.0063 0.0017  0.0098  188 SER A C   
1576 O  O   . SER A 187 ? 0.1005 0.1711 0.1712 -0.0240 0.0007  -0.0098 188 SER A O   
1577 C  CB  . SER A 187 ? 0.1342 0.1803 0.1755 -0.0274 0.0037  0.0186  188 SER A CB  
1578 O  OG  . SER A 187 ? 0.1397 0.1821 0.1808 -0.0292 -0.0121 0.0170  188 SER A OG  
1579 N  N   . LEU A 188 ? 0.0832 0.1410 0.1657 -0.0147 -0.0108 0.0003  189 LEU A N   
1580 C  CA  . LEU A 188 ? 0.0997 0.1560 0.1781 -0.0030 -0.0361 0.0024  189 LEU A CA  
1581 C  C   . LEU A 188 ? 0.1049 0.1447 0.1564 -0.0086 -0.0153 -0.0104 189 LEU A C   
1582 O  O   . LEU A 188 ? 0.1212 0.1564 0.1712 -0.0148 -0.0175 -0.0088 189 LEU A O   
1583 C  CB  . LEU A 188 ? 0.1334 0.1808 0.2096 -0.0178 -0.0390 0.0296  189 LEU A CB  
1584 C  CG  . LEU A 188 ? 0.1036 0.2011 0.2433 0.0046  -0.0166 0.0513  189 LEU A CG  
1585 C  CD1 . LEU A 188 ? 0.2326 0.1897 0.3037 -0.0148 -0.0527 0.0746  189 LEU A CD1 
1586 C  CD2 . LEU A 188 ? 0.1415 0.2480 0.2440 -0.0068 -0.0491 0.0540  189 LEU A CD2 
1587 N  N   . ASP A 189 ? 0.0825 0.1481 0.1413 0.0010  0.0038  -0.0076 190 ASP A N   
1588 C  CA  . ASP A 189 ? 0.0799 0.1664 0.1422 -0.0154 0.0076  -0.0003 190 ASP A CA  
1589 C  C   . ASP A 189 ? 0.1018 0.1255 0.1130 -0.0142 0.0024  -0.0010 190 ASP A C   
1590 O  O   . ASP A 189 ? 0.0856 0.1291 0.1160 -0.0159 -0.0046 -0.0092 190 ASP A O   
1591 C  CB  . ASP A 189 ? 0.0992 0.2009 0.1665 -0.0432 0.0088  0.0131  190 ASP A CB  
1592 C  CG  . ASP A 189 ? 0.1843 0.2743 0.1995 -0.0443 -0.0306 -0.0076 190 ASP A CG  
1593 O  OD1 . ASP A 189 ? 0.1509 0.3860 0.2526 -0.0238 0.0546  0.0023  190 ASP A OD1 
1594 O  OD2 . ASP A 189 ? 0.1861 0.4334 0.2930 -0.1168 -0.0368 0.0868  190 ASP A OD2 
1595 N  N   . TYR A 190 ? 0.0825 0.1253 0.1206 -0.0081 0.0003  0.0020  191 TYR A N   
1596 C  CA  . TYR A 190 ? 0.0810 0.1279 0.1072 -0.0170 -0.0035 0.0040  191 TYR A CA  
1597 C  C   . TYR A 190 ? 0.0855 0.1084 0.0961 -0.0087 0.0006  0.0015  191 TYR A C   
1598 O  O   . TYR A 190 ? 0.0969 0.1386 0.0969 -0.0080 0.0082  0.0000  191 TYR A O   
1599 C  CB  . TYR A 190 ? 0.0935 0.1230 0.1120 -0.0065 -0.0031 0.0080  191 TYR A CB  
1600 C  CG  . TYR A 190 ? 0.0938 0.1229 0.1123 -0.0272 -0.0037 0.0104  191 TYR A CG  
1601 C  CD1 . TYR A 190 ? 0.1058 0.1264 0.1271 -0.0216 0.0031  0.0088  191 TYR A CD1 
1602 C  CD2 . TYR A 190 ? 0.1030 0.1202 0.1136 -0.0129 0.0046  0.0023  191 TYR A CD2 
1603 C  CE1 . TYR A 190 ? 0.1071 0.1130 0.1379 -0.0096 -0.0013 0.0085  191 TYR A CE1 
1604 C  CE2 . TYR A 190 ? 0.1063 0.1357 0.1494 -0.0076 -0.0082 0.0087  191 TYR A CE2 
1605 C  CZ  . TYR A 190 ? 0.1349 0.1309 0.1388 -0.0062 0.0070  -0.0017 191 TYR A CZ  
1606 O  OH  . TYR A 190 ? 0.1386 0.1523 0.1573 0.0088  -0.0118 -0.0178 191 TYR A OH  
1607 N  N   . TRP A 191 ? 0.0807 0.1048 0.0981 -0.0049 0.0027  0.0013  192 TRP A N   
1608 C  CA  . TRP A 191 ? 0.0812 0.1040 0.1072 -0.0076 0.0082  0.0082  192 TRP A CA  
1609 C  C   . TRP A 191 ? 0.0878 0.0992 0.0860 0.0049  0.0104  0.0015  192 TRP A C   
1610 O  O   . TRP A 191 ? 0.0992 0.1196 0.0908 -0.0155 0.0077  -0.0046 192 TRP A O   
1611 C  CB  . TRP A 191 ? 0.0979 0.1023 0.1078 -0.0087 0.0091  0.0043  192 TRP A CB  
1612 C  CG  . TRP A 191 ? 0.0878 0.1084 0.1066 0.0070  0.0119  0.0076  192 TRP A CG  
1613 C  CD1 . TRP A 191 ? 0.1206 0.1211 0.1169 0.0041  0.0052  0.0114  192 TRP A CD1 
1614 C  CD2 . TRP A 191 ? 0.0803 0.1027 0.1102 0.0093  -0.0031 0.0010  192 TRP A CD2 
1615 N  NE1 . TRP A 191 ? 0.1438 0.1145 0.1343 -0.0076 0.0037  0.0170  192 TRP A NE1 
1616 C  CE2 . TRP A 191 ? 0.1336 0.1089 0.1358 -0.0010 -0.0068 0.0091  192 TRP A CE2 
1617 C  CE3 . TRP A 191 ? 0.0776 0.1291 0.1216 0.0043  0.0000  -0.0164 192 TRP A CE3 
1618 C  CZ2 . TRP A 191 ? 0.1216 0.1141 0.1614 -0.0017 -0.0155 0.0060  192 TRP A CZ2 
1619 C  CZ3 . TRP A 191 ? 0.0846 0.1349 0.1467 -0.0041 -0.0088 -0.0120 192 TRP A CZ3 
1620 C  CH2 . TRP A 191 ? 0.1093 0.1216 0.1738 0.0027  -0.0232 -0.0217 192 TRP A CH2 
1621 N  N   . THR A 192 ? 0.0895 0.0957 0.0824 -0.0037 0.0012  -0.0041 193 THR A N   
1622 C  CA  . THR A 192 ? 0.0825 0.0972 0.0966 -0.0052 0.0024  -0.0043 193 THR A CA  
1623 C  C   . THR A 192 ? 0.0838 0.1026 0.0812 0.0019  0.0073  0.0043  193 THR A C   
1624 O  O   . THR A 192 ? 0.0881 0.1193 0.0860 -0.0054 0.0043  0.0049  193 THR A O   
1625 C  CB  . THR A 192 ? 0.0993 0.0935 0.0961 0.0000  0.0034  -0.0031 193 THR A CB  
1626 O  OG1 . THR A 192 ? 0.0957 0.1011 0.1098 0.0020  0.0068  -0.0065 193 THR A OG1 
1627 C  CG2 . THR A 192 ? 0.1141 0.1169 0.1036 0.0153  0.0196  -0.0020 193 THR A CG2 
1628 N  N   . TYR A 193 ? 0.0763 0.1023 0.0935 -0.0031 0.0010  -0.0060 194 TYR A N   
1629 C  CA  . TYR A 193 ? 0.0811 0.1045 0.0824 -0.0010 -0.0027 0.0052  194 TYR A CA  
1630 C  C   . TYR A 193 ? 0.0794 0.0930 0.0776 0.0074  0.0048  -0.0006 194 TYR A C   
1631 O  O   . TYR A 193 ? 0.0806 0.1039 0.0856 -0.0054 0.0013  0.0049  194 TYR A O   
1632 C  CB  . TYR A 193 ? 0.0975 0.1054 0.0851 0.0063  0.0043  0.0051  194 TYR A CB  
1633 C  CG  . TYR A 193 ? 0.0816 0.0965 0.0926 0.0068  -0.0109 0.0060  194 TYR A CG  
1634 C  CD1 . TYR A 193 ? 0.0850 0.0932 0.0895 0.0038  -0.0005 0.0017  194 TYR A CD1 
1635 C  CD2 . TYR A 193 ? 0.0890 0.1005 0.0952 0.0074  -0.0115 -0.0013 194 TYR A CD2 
1636 C  CE1 . TYR A 193 ? 0.0798 0.0851 0.0970 0.0031  -0.0012 0.0054  194 TYR A CE1 
1637 C  CE2 . TYR A 193 ? 0.0992 0.0932 0.1032 -0.0020 -0.0071 -0.0031 194 TYR A CE2 
1638 C  CZ  . TYR A 193 ? 0.0899 0.0829 0.0812 0.0097  0.0017  -0.0035 194 TYR A CZ  
1639 O  OH  . TYR A 193 ? 0.0930 0.0942 0.0856 0.0007  0.0065  -0.0043 194 TYR A OH  
1640 N  N   . PRO A 194 ? 0.0759 0.1078 0.0834 0.0006  0.0024  -0.0031 195 PRO A N   
1641 C  CA  . PRO A 194 ? 0.0923 0.0945 0.0929 0.0000  0.0070  -0.0093 195 PRO A CA  
1642 C  C   . PRO A 194 ? 0.0825 0.0816 0.0846 -0.0027 -0.0088 0.0000  195 PRO A C   
1643 O  O   . PRO A 194 ? 0.0882 0.1081 0.0869 0.0068  -0.0005 0.0019  195 PRO A O   
1644 C  CB  . PRO A 194 ? 0.1053 0.1173 0.1032 -0.0189 0.0074  -0.0126 195 PRO A CB  
1645 C  CG  . PRO A 194 ? 0.1005 0.1190 0.1155 -0.0136 0.0093  -0.0102 195 PRO A CG  
1646 C  CD  . PRO A 194 ? 0.0993 0.1248 0.0780 -0.0219 0.0057  -0.0126 195 PRO A CD  
1647 N  N   . GLY A 195 ? 0.0724 0.0869 0.0903 -0.0054 0.0015  -0.0023 196 GLY A N   
1648 C  CA  . GLY A 195 ? 0.0947 0.1049 0.0775 0.0027  0.0093  0.0060  196 GLY A CA  
1649 C  C   . GLY A 195 ? 0.0702 0.0837 0.0832 -0.0006 -0.0098 -0.0057 196 GLY A C   
1650 O  O   . GLY A 195 ? 0.0820 0.0891 0.0917 0.0019  0.0091  -0.0046 196 GLY A O   
1651 N  N   . SER A 196 ? 0.0684 0.0912 0.0781 0.0003  -0.0027 -0.0074 197 SER A N   
1652 C  CA  . SER A 196 ? 0.0675 0.0939 0.0932 -0.0006 0.0074  -0.0065 197 SER A CA  
1653 C  C   . SER A 196 ? 0.0772 0.0736 0.0872 -0.0010 0.0017  -0.0015 197 SER A C   
1654 O  O   . SER A 196 ? 0.0711 0.0869 0.0913 -0.0098 0.0010  -0.0012 197 SER A O   
1655 C  CB  . SER A 196 ? 0.0784 0.0894 0.1001 -0.0137 -0.0043 -0.0068 197 SER A CB  
1656 O  OG  . SER A 196 ? 0.0680 0.0969 0.0996 -0.0031 -0.0005 0.0010  197 SER A OG  
1657 N  N   . LEU A 197 ? 0.0709 0.0891 0.0820 -0.0073 0.0073  -0.0038 198 LEU A N   
1658 C  CA  . LEU A 197 ? 0.0819 0.0854 0.0837 -0.0074 0.0077  -0.0071 198 LEU A CA  
1659 C  C   . LEU A 197 ? 0.0746 0.0847 0.0842 -0.0023 0.0054  -0.0038 198 LEU A C   
1660 O  O   . LEU A 197 ? 0.0807 0.0936 0.1006 -0.0076 -0.0017 -0.0065 198 LEU A O   
1661 C  CB  . LEU A 197 ? 0.0917 0.1002 0.0923 -0.0082 0.0126  0.0038  198 LEU A CB  
1662 C  CG  . LEU A 197 ? 0.0993 0.0960 0.1062 -0.0140 0.0005  0.0031  198 LEU A CG  
1663 C  CD1 . LEU A 197 ? 0.1035 0.1136 0.1245 -0.0216 0.0109  0.0087  198 LEU A CD1 
1664 C  CD2 . LEU A 197 ? 0.0936 0.1175 0.1168 0.0043  0.0065  0.0151  198 LEU A CD2 
1665 N  N   . THR A 198 ? 0.0847 0.0815 0.0876 0.0035  0.0020  -0.0059 199 THR A N   
1666 C  CA  . THR A 198 ? 0.0855 0.0878 0.0975 -0.0024 0.0087  -0.0031 199 THR A CA  
1667 C  C   . THR A 198 ? 0.0763 0.0860 0.1145 0.0020  -0.0013 0.0017  199 THR A C   
1668 O  O   . THR A 198 ? 0.0869 0.0983 0.1220 -0.0024 0.0097  -0.0080 199 THR A O   
1669 C  CB  . THR A 198 ? 0.0838 0.0873 0.0930 -0.0153 0.0043  -0.0020 199 THR A CB  
1670 O  OG1 . THR A 198 ? 0.0863 0.0947 0.0854 -0.0082 -0.0024 0.0043  199 THR A OG1 
1671 C  CG2 . THR A 198 ? 0.0856 0.1093 0.1080 -0.0086 0.0142  0.0027  199 THR A CG2 
1672 N  N   . THR A 199 ? 0.0860 0.0972 0.0979 -0.0060 0.0148  -0.0023 200 THR A N   
1673 C  CA  . THR A 199 ? 0.0847 0.1027 0.1157 -0.0087 0.0187  -0.0176 200 THR A CA  
1674 C  C   . THR A 199 ? 0.0900 0.1057 0.1066 -0.0241 0.0216  -0.0126 200 THR A C   
1675 O  O   . THR A 199 ? 0.1006 0.1062 0.1203 -0.0217 0.0200  -0.0193 200 THR A O   
1676 C  CB  . THR A 199 ? 0.0923 0.1111 0.1096 -0.0010 0.0120  -0.0010 200 THR A CB  
1677 O  OG1 . THR A 199 ? 0.1891 0.1528 0.1318 0.0359  0.0071  0.0000  200 THR A OG1 
1678 C  CG2 . THR A 199 ? 0.1537 0.1449 0.1259 -0.0335 -0.0175 -0.0136 200 THR A CG2 
1679 N  N   . PRO A 200 ? 0.1069 0.1221 0.1242 -0.0241 0.0282  -0.0185 201 PRO A N   
1680 C  CA  . PRO A 200 ? 0.1023 0.1377 0.1275 -0.0384 0.0118  -0.0024 201 PRO A CA  
1681 C  C   . PRO A 200 ? 0.1315 0.1483 0.1159 -0.0339 0.0142  -0.0035 201 PRO A C   
1682 O  O   . PRO A 200 ? 0.1562 0.1843 0.1392 -0.0270 -0.0048 -0.0170 201 PRO A O   
1683 C  CB  . PRO A 200 ? 0.1127 0.1661 0.1559 -0.0386 0.0263  -0.0209 201 PRO A CB  
1684 C  CG  . PRO A 200 ? 0.0812 0.1704 0.1552 -0.0115 0.0218  -0.0239 201 PRO A CG  
1685 C  CD  . PRO A 200 ? 0.1044 0.1507 0.1309 -0.0137 0.0219  -0.0266 201 PRO A CD  
1686 N  N   . PRO A 201 ? 0.1169 0.1318 0.1234 -0.0296 0.0193  0.0049  202 PRO A N   
1687 C  CA  . PRO A 201 ? 0.1080 0.1254 0.1196 -0.0322 0.0115  -0.0137 202 PRO A CA  
1688 C  C   . PRO A 201 ? 0.0913 0.1238 0.1247 -0.0113 0.0093  -0.0110 202 PRO A C   
1689 O  O   . PRO A 201 ? 0.1084 0.1209 0.1304 -0.0263 0.0051  -0.0119 202 PRO A O   
1690 C  CB  . PRO A 201 ? 0.1476 0.1411 0.1686 -0.0458 0.0284  0.0193  202 PRO A CB  
1691 C  CG  . PRO A 201 ? 0.1632 0.1307 0.1808 -0.0243 0.0143  0.0013  202 PRO A CG  
1692 C  CD  . PRO A 201 ? 0.1624 0.1430 0.1431 -0.0172 0.0126  0.0041  202 PRO A CD  
1693 N  N   . LEU A 202 ? 0.0841 0.1132 0.1199 -0.0097 0.0162  0.0057  203 LEU A N   
1694 C  CA  . LEU A 202 ? 0.0838 0.1058 0.1099 -0.0118 0.0027  -0.0099 203 LEU A CA  
1695 C  C   . LEU A 202 ? 0.0784 0.1111 0.1039 -0.0264 0.0068  0.0013  203 LEU A C   
1696 O  O   . LEU A 202 ? 0.0820 0.1087 0.1084 -0.0126 -0.0013 -0.0027 203 LEU A O   
1697 C  CB  . LEU A 202 ? 0.0882 0.1106 0.1220 0.0000  -0.0024 -0.0096 203 LEU A CB  
1698 C  CG  . LEU A 202 ? 0.0772 0.1243 0.1067 -0.0164 0.0065  -0.0065 203 LEU A CG  
1699 C  CD1 . LEU A 202 ? 0.0798 0.1485 0.1676 0.0054  0.0010  -0.0154 203 LEU A CD1 
1700 C  CD2 . LEU A 202 ? 0.0895 0.1191 0.1404 -0.0088 -0.0015 -0.0076 203 LEU A CD2 
1701 N  N   . LEU A 203 ? 0.0812 0.1049 0.1184 -0.0098 0.0052  -0.0054 204 LEU A N   
1702 C  CA  . LEU A 203 ? 0.0990 0.0947 0.1254 -0.0159 0.0068  -0.0097 204 LEU A CA  
1703 C  C   . LEU A 203 ? 0.0843 0.0960 0.1169 0.0015  0.0041  -0.0023 204 LEU A C   
1704 O  O   . LEU A 203 ? 0.0947 0.1042 0.1087 -0.0200 -0.0054 -0.0054 204 LEU A O   
1705 C  CB  . LEU A 203 ? 0.1057 0.1081 0.1368 -0.0130 0.0155  0.0065  204 LEU A CB  
1706 C  CG  . LEU A 203 ? 0.1184 0.1278 0.1386 -0.0043 0.0263  0.0091  204 LEU A CG  
1707 C  CD1 . LEU A 203 ? 0.1640 0.1248 0.1914 -0.0049 0.0388  0.0337  204 LEU A CD1 
1708 C  CD2 . LEU A 203 ? 0.1365 0.1573 0.2635 -0.0582 0.0000  0.0282  204 LEU A CD2 
1709 N  N   . GLU A 204 ? 0.0868 0.1105 0.1190 -0.0178 -0.0041 -0.0197 205 GLU A N   
1710 C  CA  . GLU A 204 ? 0.0908 0.1175 0.1032 -0.0046 -0.0041 -0.0097 205 GLU A CA  
1711 C  C   . GLU A 204 ? 0.0930 0.1008 0.1076 -0.0153 -0.0088 -0.0247 205 GLU A C   
1712 O  O   . GLU A 204 ? 0.1181 0.1483 0.1316 0.0126  -0.0167 -0.0340 205 GLU A O   
1713 C  CB  . GLU A 204 ? 0.1080 0.1330 0.1257 0.0030  -0.0263 -0.0115 205 GLU A CB  
1714 C  CG  . GLU A 204 ? 0.1206 0.1160 0.1458 0.0046  -0.0230 -0.0115 205 GLU A CG  
1715 C  CD  . GLU A 204 ? 0.1345 0.1303 0.1268 -0.0093 -0.0074 -0.0115 205 GLU A CD  
1716 O  OE1 . GLU A 204 ? 0.1233 0.1559 0.1666 0.0081  -0.0261 -0.0388 205 GLU A OE1 
1717 O  OE2 . GLU A 204 ? 0.1115 0.1400 0.1361 -0.0125 -0.0194 -0.0098 205 GLU A OE2 
1718 N  N   . CYS A 205 ? 0.0821 0.0963 0.1190 -0.0109 -0.0052 -0.0043 206 CYS A N   
1719 C  CA  . CYS A 205 ? 0.0758 0.1093 0.1194 -0.0031 -0.0080 0.0104  206 CYS A CA  
1720 C  C   . CYS A 205 ? 0.0772 0.0890 0.0992 0.0076  -0.0024 -0.0057 206 CYS A C   
1721 O  O   . CYS A 205 ? 0.1053 0.0930 0.1377 0.0000  -0.0208 -0.0017 206 CYS A O   
1722 C  CB  . CYS A 205 ? 0.1096 0.0981 0.1224 -0.0233 0.0059  0.0012  206 CYS A CB  
1723 S  SG  . CYS A 205 ? 0.1263 0.1071 0.1194 -0.0038 0.0010  0.0019  206 CYS A SG  
1724 N  N   . VAL A 206 ? 0.0790 0.0776 0.1081 -0.0073 -0.0054 -0.0034 207 VAL A N   
1725 C  CA  . VAL A 206 ? 0.0772 0.0820 0.0961 -0.0130 -0.0093 0.0031  207 VAL A CA  
1726 C  C   . VAL A 206 ? 0.0798 0.0810 0.1024 0.0015  -0.0074 -0.0013 207 VAL A C   
1727 O  O   . VAL A 206 ? 0.0859 0.1099 0.1033 -0.0010 -0.0010 0.0115  207 VAL A O   
1728 C  CB  . VAL A 206 ? 0.0798 0.0916 0.1026 -0.0038 -0.0027 -0.0048 207 VAL A CB  
1729 C  CG1 . VAL A 206 ? 0.0798 0.0978 0.1054 -0.0034 -0.0076 -0.0063 207 VAL A CG1 
1730 C  CG2 . VAL A 206 ? 0.0864 0.1014 0.1128 0.0006  0.0132  0.0013  207 VAL A CG2 
1731 N  N   . THR A 207 ? 0.0741 0.0841 0.0965 -0.0035 0.0005  -0.0031 208 THR A N   
1732 C  CA  . THR A 207 ? 0.0834 0.1014 0.0947 -0.0038 0.0046  -0.0024 208 THR A CA  
1733 C  C   . THR A 207 ? 0.0820 0.0794 0.0846 -0.0074 0.0019  0.0074  208 THR A C   
1734 O  O   . THR A 207 ? 0.0929 0.0881 0.0996 -0.0071 -0.0136 0.0020  208 THR A O   
1735 C  CB  . THR A 207 ? 0.0954 0.0935 0.1120 -0.0035 0.0048  -0.0099 208 THR A CB  
1736 O  OG1 . THR A 207 ? 0.1026 0.0990 0.1150 0.0000  0.0046  -0.0175 208 THR A OG1 
1737 C  CG2 . THR A 207 ? 0.0983 0.1168 0.1307 -0.0120 0.0219  -0.0013 208 THR A CG2 
1738 N  N   . TRP A 208 ? 0.0740 0.0816 0.0878 0.0000  0.0049  -0.0015 209 TRP A N   
1739 C  CA  . TRP A 208 ? 0.0776 0.0785 0.0828 -0.0015 0.0027  -0.0013 209 TRP A CA  
1740 C  C   . TRP A 208 ? 0.0807 0.0794 0.0758 0.0124  0.0038  -0.0040 209 TRP A C   
1741 O  O   . TRP A 208 ? 0.0803 0.0920 0.0855 -0.0060 0.0052  -0.0005 209 TRP A O   
1742 C  CB  . TRP A 208 ? 0.0758 0.0837 0.0825 0.0063  -0.0003 0.0059  209 TRP A CB  
1743 C  CG  . TRP A 208 ? 0.0674 0.0697 0.0851 0.0091  0.0005  -0.0031 209 TRP A CG  
1744 C  CD1 . TRP A 208 ? 0.0771 0.0854 0.0951 -0.0006 -0.0027 0.0026  209 TRP A CD1 
1745 C  CD2 . TRP A 208 ? 0.0711 0.0759 0.0916 0.0048  0.0059  -0.0073 209 TRP A CD2 
1746 N  NE1 . TRP A 208 ? 0.0794 0.0891 0.1026 -0.0034 0.0109  0.0041  209 TRP A NE1 
1747 C  CE2 . TRP A 208 ? 0.0878 0.0768 0.0963 0.0068  -0.0017 -0.0005 209 TRP A CE2 
1748 C  CE3 . TRP A 208 ? 0.0834 0.0785 0.0815 0.0162  -0.0049 -0.0024 209 TRP A CE3 
1749 C  CZ2 . TRP A 208 ? 0.0956 0.0900 0.1108 0.0225  0.0132  0.0048  209 TRP A CZ2 
1750 C  CZ3 . TRP A 208 ? 0.1002 0.0926 0.1017 -0.0006 0.0013  0.0006  209 TRP A CZ3 
1751 C  CH2 . TRP A 208 ? 0.1105 0.0872 0.0993 0.0131  0.0048  -0.0043 209 TRP A CH2 
1752 N  N   . ILE A 209 ? 0.0696 0.0834 0.0920 -0.0027 0.0013  -0.0052 210 ILE A N   
1753 C  CA  . ILE A 209 ? 0.0649 0.0810 0.0948 -0.0038 -0.0041 0.0035  210 ILE A CA  
1754 C  C   . ILE A 209 ? 0.0652 0.0837 0.0810 -0.0054 0.0038  0.0031  210 ILE A C   
1755 O  O   . ILE A 209 ? 0.1089 0.0864 0.0882 -0.0019 0.0015  0.0024  210 ILE A O   
1756 C  CB  . ILE A 209 ? 0.0741 0.0960 0.1096 -0.0054 -0.0060 0.0030  210 ILE A CB  
1757 C  CG1 . ILE A 209 ? 0.0865 0.1067 0.1395 0.0024  -0.0137 -0.0142 210 ILE A CG1 
1758 C  CG2 . ILE A 209 ? 0.0570 0.1377 0.1306 0.0104  0.0070  0.0071  210 ILE A CG2 
1759 C  CD1 . ILE A 209 ? 0.1105 0.1142 0.1720 0.0137  -0.0003 0.0051  210 ILE A CD1 
1760 N  N   . VAL A 210 ? 0.0714 0.0815 0.0930 -0.0052 0.0000  0.0031  211 VAL A N   
1761 C  CA  . VAL A 210 ? 0.0678 0.0873 0.0878 -0.0070 0.0000  -0.0024 211 VAL A CA  
1762 C  C   . VAL A 210 ? 0.0794 0.0838 0.0847 0.0003  0.0020  0.0048  211 VAL A C   
1763 O  O   . VAL A 210 ? 0.0877 0.1010 0.0913 -0.0137 0.0054  -0.0005 211 VAL A O   
1764 C  CB  . VAL A 210 ? 0.0837 0.0969 0.0963 -0.0020 0.0035  -0.0048 211 VAL A CB  
1765 C  CG1 . VAL A 210 ? 0.0996 0.0938 0.1200 -0.0070 0.0017  -0.0027 211 VAL A CG1 
1766 C  CG2 . VAL A 210 ? 0.0799 0.1243 0.1297 -0.0027 0.0065  0.0000  211 VAL A CG2 
1767 N  N   . LEU A 211 ? 0.0803 0.1066 0.0987 -0.0119 -0.0027 0.0043  212 LEU A N   
1768 C  CA  . LEU A 211 ? 0.0838 0.1145 0.1048 -0.0219 -0.0057 -0.0012 212 LEU A CA  
1769 C  C   . LEU A 211 ? 0.0878 0.1108 0.0929 -0.0119 -0.0020 0.0057  212 LEU A C   
1770 O  O   . LEU A 211 ? 0.0978 0.1137 0.1026 -0.0087 0.0020  0.0010  212 LEU A O   
1771 C  CB  . LEU A 211 ? 0.0922 0.1133 0.1084 -0.0104 -0.0035 0.0038  212 LEU A CB  
1772 C  CG  . LEU A 211 ? 0.0926 0.1254 0.1230 -0.0065 -0.0164 0.0051  212 LEU A CG  
1773 C  CD1 . LEU A 211 ? 0.1076 0.1740 0.1431 -0.0103 -0.0282 0.0164  212 LEU A CD1 
1774 C  CD2 . LEU A 211 ? 0.1229 0.1542 0.1203 0.0057  -0.0031 -0.0035 212 LEU A CD2 
1775 N  N   . LYS A 212 ? 0.1010 0.1093 0.1098 -0.0237 -0.0020 0.0074  213 LYS A N   
1776 C  CA  . LYS A 212 ? 0.1130 0.1120 0.1089 -0.0126 0.0065  0.0109  213 LYS A CA  
1777 C  C   . LYS A 212 ? 0.0930 0.0961 0.1196 -0.0096 -0.0006 0.0186  213 LYS A C   
1778 O  O   . LYS A 212 ? 0.1136 0.1193 0.1588 -0.0065 -0.0238 0.0135  213 LYS A O   
1779 C  CB  . LYS A 212 ? 0.1381 0.1431 0.1178 -0.0370 0.0082  0.0194  213 LYS A CB  
1780 C  CG  . LYS A 212 ? 0.1776 0.1471 0.1656 -0.0085 0.0104  0.0274  213 LYS A CG  
1781 C  CD  . LYS A 212 ? 0.3334 0.2242 0.1643 -0.0483 0.0320  0.0522  213 LYS A CD  
1782 C  CE  . LYS A 212 ? 0.4300 0.3084 0.2479 -0.0666 0.0727  0.1115  213 LYS A CE  
1783 N  NZ  . LYS A 212 ? 0.5903 0.4976 0.3120 -0.1089 0.0966  0.0419  213 LYS A NZ  
1784 N  N   . GLU A 213 ? 0.0900 0.1075 0.1054 -0.0093 -0.0049 0.0077  214 GLU A N   
1785 C  CA  . GLU A 213 ? 0.1008 0.1155 0.1193 -0.0176 -0.0012 0.0034  214 GLU A CA  
1786 C  C   . GLU A 213 ? 0.0869 0.0952 0.1177 -0.0135 -0.0126 0.0102  214 GLU A C   
1787 O  O   . GLU A 213 ? 0.0935 0.1023 0.1208 -0.0063 -0.0076 0.0153  214 GLU A O   
1788 C  CB  . GLU A 213 ? 0.0917 0.1229 0.1386 -0.0315 -0.0153 0.0082  214 GLU A CB  
1789 C  CG  . GLU A 213 ? 0.1243 0.1591 0.1771 -0.0071 -0.0274 -0.0130 214 GLU A CG  
1790 C  CD  . GLU A 213 ? 0.1418 0.2125 0.1817 -0.0337 -0.0119 -0.0296 214 GLU A CD  
1791 O  OE1 . GLU A 213 ? 0.1220 0.1780 0.2310 -0.0115 -0.0487 0.0054  214 GLU A OE1 
1792 O  OE2 . GLU A 213 ? 0.2696 0.3188 0.3578 -0.0606 -0.0869 -0.0623 214 GLU A OE2 
1793 N  N   . PRO A 214 ? 0.1108 0.0987 0.1130 -0.0110 -0.0024 0.0109  215 PRO A N   
1794 C  CA  . PRO A 214 ? 0.1212 0.1098 0.1187 0.0065  -0.0104 -0.0060 215 PRO A CA  
1795 C  C   . PRO A 214 ? 0.1014 0.1098 0.1234 -0.0164 -0.0186 -0.0070 215 PRO A C   
1796 O  O   . PRO A 214 ? 0.1225 0.1618 0.1289 -0.0368 -0.0137 0.0093  215 PRO A O   
1797 C  CB  . PRO A 214 ? 0.1263 0.1011 0.1383 -0.0052 -0.0082 0.0085  215 PRO A CB  
1798 C  CG  . PRO A 214 ? 0.1862 0.1783 0.1947 -0.0238 0.0265  -0.0038 215 PRO A CG  
1799 C  CD  . PRO A 214 ? 0.1309 0.0988 0.1552 -0.0087 0.0208  0.0186  215 PRO A CD  
1800 N  N   . ILE A 215 ? 0.1196 0.1196 0.1076 -0.0060 -0.0155 -0.0046 216 ILE A N   
1801 C  CA  . ILE A 215 ? 0.1168 0.1085 0.1203 -0.0132 -0.0265 -0.0136 216 ILE A CA  
1802 C  C   . ILE A 215 ? 0.1132 0.1066 0.1071 -0.0098 -0.0161 -0.0137 216 ILE A C   
1803 O  O   . ILE A 215 ? 0.1257 0.1169 0.1454 -0.0098 -0.0146 -0.0183 216 ILE A O   
1804 C  CB  . ILE A 215 ? 0.1194 0.1199 0.1187 0.0037  -0.0208 -0.0164 216 ILE A CB  
1805 C  CG1 . ILE A 215 ? 0.1571 0.1221 0.1271 0.0093  -0.0172 0.0054  216 ILE A CG1 
1806 C  CG2 . ILE A 215 ? 0.1544 0.1296 0.1424 0.0098  -0.0142 -0.0206 216 ILE A CG2 
1807 C  CD1 . ILE A 215 ? 0.1764 0.1332 0.1647 -0.0063 -0.0148 0.0196  216 ILE A CD1 
1808 N  N   A SER A 216 ? 0.1093 0.1090 0.1124 -0.0108 -0.0242 -0.0037 217 SER A N   
1809 N  N   B SER A 216 ? 0.1333 0.1084 0.1315 -0.0161 -0.0271 -0.0186 217 SER A N   
1810 C  CA  A SER A 216 ? 0.1307 0.1020 0.1146 -0.0107 -0.0153 -0.0137 217 SER A CA  
1811 C  CA  B SER A 216 ? 0.1512 0.1209 0.1280 -0.0102 -0.0230 -0.0237 217 SER A CA  
1812 C  C   A SER A 216 ? 0.1456 0.0935 0.1262 -0.0178 -0.0186 0.0006  217 SER A C   
1813 C  C   B SER A 216 ? 0.1530 0.1120 0.1403 -0.0081 -0.0248 -0.0171 217 SER A C   
1814 O  O   A SER A 216 ? 0.1099 0.1261 0.1102 -0.0059 0.0043  -0.0080 217 SER A O   
1815 O  O   B SER A 216 ? 0.1625 0.1211 0.1203 -0.0146 -0.0219 0.0142  217 SER A O   
1816 C  CB  A SER A 216 ? 0.1819 0.0975 0.1491 -0.0269 -0.0071 -0.0193 217 SER A CB  
1817 C  CB  B SER A 216 ? 0.1791 0.1186 0.1756 -0.0121 0.0093  0.0081  217 SER A CB  
1818 O  OG  A SER A 216 ? 0.1731 0.1327 0.1379 -0.0425 0.0010  -0.0027 217 SER A OG  
1819 O  OG  B SER A 216 ? 0.3183 0.1764 0.1776 -0.0450 0.0228  -0.0608 217 SER A OG  
1820 N  N   . VAL A 217 ? 0.1361 0.1069 0.1336 -0.0183 -0.0181 -0.0178 218 VAL A N   
1821 C  CA  . VAL A 217 ? 0.1564 0.1017 0.1410 -0.0120 -0.0137 -0.0170 218 VAL A CA  
1822 C  C   . VAL A 217 ? 0.1523 0.1036 0.1178 -0.0171 -0.0230 -0.0108 218 VAL A C   
1823 O  O   . VAL A 217 ? 0.1627 0.1115 0.1306 -0.0166 -0.0217 -0.0125 218 VAL A O   
1824 C  CB  . VAL A 217 ? 0.1606 0.0951 0.1586 -0.0260 -0.0346 -0.0154 218 VAL A CB  
1825 C  CG1 . VAL A 217 ? 0.1931 0.1096 0.1567 -0.0109 -0.0175 -0.0164 218 VAL A CG1 
1826 C  CG2 . VAL A 217 ? 0.1533 0.1289 0.1941 -0.0186 -0.0115 -0.0184 218 VAL A CG2 
1827 N  N   . SER A 218 ? 0.1589 0.1096 0.1298 -0.0074 -0.0205 -0.0273 219 SER A N   
1828 C  CA  . SER A 218 ? 0.1645 0.0970 0.1501 -0.0200 -0.0186 -0.0276 219 SER A CA  
1829 C  C   . SER A 218 ? 0.1677 0.1026 0.1386 -0.0175 -0.0063 -0.0146 219 SER A C   
1830 O  O   . SER A 218 ? 0.1624 0.1105 0.1467 -0.0099 -0.0182 -0.0137 219 SER A O   
1831 C  CB  . SER A 218 ? 0.1761 0.1242 0.1291 -0.0248 -0.0071 -0.0218 219 SER A CB  
1832 O  OG  . SER A 218 ? 0.1831 0.1456 0.1402 -0.0088 -0.0239 -0.0176 219 SER A OG  
1833 N  N   A SER A 219 ? 0.1752 0.0834 0.1641 -0.0296 -0.0119 -0.0160 220 SER A N   
1834 N  N   B SER A 219 ? 0.1756 0.1040 0.1544 0.0012  0.0049  -0.0071 220 SER A N   
1835 C  CA  A SER A 219 ? 0.1885 0.1123 0.1824 -0.0447 0.0070  -0.0046 220 SER A CA  
1836 C  CA  B SER A 219 ? 0.1702 0.1115 0.1571 -0.0074 -0.0155 -0.0012 220 SER A CA  
1837 C  C   A SER A 219 ? 0.1755 0.1348 0.1948 0.0006  -0.0071 -0.0062 220 SER A C   
1838 C  C   B SER A 219 ? 0.1683 0.1289 0.1763 0.0035  -0.0010 -0.0153 220 SER A C   
1839 O  O   A SER A 219 ? 0.1916 0.1264 0.2092 -0.0115 0.0231  0.0070  220 SER A O   
1840 O  O   B SER A 219 ? 0.1711 0.1445 0.1685 -0.0034 0.0031  -0.0115 220 SER A O   
1841 C  CB  A SER A 219 ? 0.1967 0.1336 0.2040 -0.0043 0.0126  -0.0102 220 SER A CB  
1842 C  CB  B SER A 219 ? 0.1959 0.1314 0.1948 0.0060  0.0219  -0.0148 220 SER A CB  
1843 O  OG  A SER A 219 ? 0.2617 0.1332 0.2712 0.0177  -0.0230 -0.0785 220 SER A OG  
1844 O  OG  B SER A 219 ? 0.1871 0.1169 0.2058 -0.0166 -0.0015 -0.0065 220 SER A OG  
1845 N  N   . GLU A 220 ? 0.1764 0.1211 0.1600 -0.0115 0.0007  -0.0131 221 GLU A N   
1846 C  CA  . GLU A 220 ? 0.2196 0.1322 0.1726 -0.0023 -0.0170 -0.0386 221 GLU A CA  
1847 C  C   . GLU A 220 ? 0.1835 0.1483 0.1500 0.0019  0.0027  -0.0130 221 GLU A C   
1848 O  O   . GLU A 220 ? 0.1934 0.1695 0.1634 0.0077  0.0214  -0.0199 221 GLU A O   
1849 C  CB  . GLU A 220 ? 0.2824 0.1810 0.1675 0.0077  -0.0377 -0.0577 221 GLU A CB  
1850 C  CG  . GLU A 220 ? 0.3271 0.2311 0.2168 -0.0379 -0.0379 -0.0834 221 GLU A CG  
1851 C  CD  . GLU A 220 ? 0.3488 0.2354 0.3027 -0.0895 -0.0035 -0.1089 221 GLU A CD  
1852 O  OE1 . GLU A 220 ? 0.3009 0.2339 0.3064 -0.0991 0.0098  -0.0851 221 GLU A OE1 
1853 O  OE2 . GLU A 220 ? 0.5877 0.2509 0.4787 -0.1277 0.0425  -0.1444 221 GLU A OE2 
1854 N  N   . GLN A 221 ? 0.1605 0.1194 0.1418 -0.0085 -0.0071 -0.0174 222 GLN A N   
1855 C  CA  . GLN A 221 ? 0.1719 0.1168 0.1518 -0.0261 -0.0087 0.0000  222 GLN A CA  
1856 C  C   . GLN A 221 ? 0.1603 0.1264 0.1453 -0.0086 -0.0040 0.0115  222 GLN A C   
1857 O  O   . GLN A 221 ? 0.1726 0.1430 0.1509 -0.0115 -0.0006 0.0005  222 GLN A O   
1858 C  CB  . GLN A 221 ? 0.1483 0.1296 0.1386 -0.0114 -0.0167 -0.0126 222 GLN A CB  
1859 C  CG  . GLN A 221 ? 0.1564 0.1361 0.1503 -0.0258 -0.0204 -0.0063 222 GLN A CG  
1860 C  CD  . GLN A 221 ? 0.1523 0.1273 0.1352 -0.0184 -0.0086 -0.0114 222 GLN A CD  
1861 O  OE1 . GLN A 221 ? 0.1616 0.1196 0.1260 -0.0043 -0.0153 -0.0082 222 GLN A OE1 
1862 N  NE2 . GLN A 221 ? 0.1776 0.1236 0.1415 -0.0010 -0.0164 -0.0010 222 GLN A NE2 
1863 N  N   A VAL A 222 ? 0.1676 0.1163 0.1560 -0.0142 -0.0119 0.0093  223 VAL A N   
1864 N  N   B VAL A 222 ? 0.1670 0.1225 0.1501 -0.0082 -0.0192 0.0104  223 VAL A N   
1865 C  CA  A VAL A 222 ? 0.1711 0.1604 0.1388 -0.0098 -0.0059 0.0209  223 VAL A CA  
1866 C  CA  B VAL A 222 ? 0.1623 0.1427 0.1497 -0.0171 -0.0091 0.0260  223 VAL A CA  
1867 C  C   A VAL A 222 ? 0.1770 0.1368 0.1516 -0.0187 0.0052  0.0137  223 VAL A C   
1868 C  C   B VAL A 222 ? 0.1679 0.1264 0.1588 -0.0164 -0.0031 0.0166  223 VAL A C   
1869 O  O   A VAL A 222 ? 0.1605 0.1282 0.1439 -0.0085 0.0041  0.0137  223 VAL A O   
1870 O  O   B VAL A 222 ? 0.1501 0.1490 0.1659 -0.0148 -0.0054 0.0087  223 VAL A O   
1871 C  CB  A VAL A 222 ? 0.1957 0.1694 0.1668 0.0043  0.0115  0.0438  223 VAL A CB  
1872 C  CB  B VAL A 222 ? 0.1096 0.1412 0.1354 -0.0049 0.0113  -0.0015 223 VAL A CB  
1873 C  CG1 A VAL A 222 ? 0.1758 0.1870 0.1692 0.0031  0.0164  0.0178  223 VAL A CG1 
1874 C  CG1 B VAL A 222 ? 0.1242 0.1177 0.1791 -0.0458 -0.0283 0.0166  223 VAL A CG1 
1875 C  CG2 A VAL A 222 ? 0.1712 0.2601 0.1790 0.0414  -0.0080 -0.0142 223 VAL A CG2 
1876 C  CG2 B VAL A 222 ? 0.1668 0.1368 0.1534 -0.0031 -0.0143 -0.0403 223 VAL A CG2 
1877 N  N   . LEU A 223 ? 0.1738 0.1456 0.1706 -0.0003 -0.0026 0.0013  224 LEU A N   
1878 C  CA  . LEU A 223 ? 0.1949 0.1340 0.2001 -0.0155 0.0155  -0.0031 224 LEU A CA  
1879 C  C   . LEU A 223 ? 0.1771 0.1625 0.1618 -0.0076 0.0020  -0.0412 224 LEU A C   
1880 O  O   . LEU A 223 ? 0.1715 0.1853 0.1968 -0.0124 0.0172  -0.0236 224 LEU A O   
1881 C  CB  . LEU A 223 ? 0.2569 0.1677 0.2346 -0.0164 0.0296  -0.0208 224 LEU A CB  
1882 C  CG  . LEU A 223 ? 0.2779 0.1894 0.2272 -0.0119 0.0065  -0.0344 224 LEU A CG  
1883 C  CD1 . LEU A 223 ? 0.3752 0.2461 0.2795 -0.0584 0.0252  -0.0507 224 LEU A CD1 
1884 C  CD2 . LEU A 223 ? 0.2383 0.2910 0.3339 0.0030  0.0110  -0.0397 224 LEU A CD2 
1885 N  N   . LYS A 224 ? 0.1797 0.1562 0.1595 -0.0137 -0.0109 -0.0132 225 LYS A N   
1886 C  CA  . LYS A 224 ? 0.1737 0.1914 0.1553 -0.0175 0.0035  0.0000  225 LYS A CA  
1887 C  C   . LYS A 224 ? 0.1639 0.1605 0.1298 -0.0070 0.0024  0.0167  225 LYS A C   
1888 O  O   . LYS A 224 ? 0.1853 0.1648 0.1284 -0.0195 0.0080  -0.0082 225 LYS A O   
1889 C  CB  . LYS A 224 ? 0.1747 0.2430 0.1961 -0.0241 -0.0252 0.0240  225 LYS A CB  
1890 C  CG  . LYS A 224 ? 0.2283 0.3379 0.2229 -0.0280 -0.0750 -0.0137 225 LYS A CG  
1891 C  CD  . LYS A 224 ? 0.3262 0.2412 0.3300 -0.0087 -0.0768 -0.0548 225 LYS A CD  
1892 C  CE  . LYS A 224 ? 0.3722 0.3237 0.3688 0.0208  -0.0434 -0.1488 225 LYS A CE  
1893 N  NZ  . LYS A 224 ? 0.3212 0.3467 0.3589 0.0240  0.0872  -0.0381 225 LYS A NZ  
1894 N  N   . PHE A 225 ? 0.1600 0.1537 0.1187 -0.0054 0.0082  0.0088  226 PHE A N   
1895 C  CA  . PHE A 225 ? 0.1494 0.1412 0.1298 -0.0196 0.0194  0.0087  226 PHE A CA  
1896 C  C   . PHE A 225 ? 0.1562 0.1287 0.1098 -0.0306 0.0062  0.0063  226 PHE A C   
1897 O  O   . PHE A 225 ? 0.1605 0.1386 0.1196 -0.0205 0.0130  -0.0041 226 PHE A O   
1898 C  CB  . PHE A 225 ? 0.1656 0.1352 0.1297 -0.0073 0.0205  0.0125  226 PHE A CB  
1899 C  CG  . PHE A 225 ? 0.1564 0.1280 0.1340 -0.0220 0.0219  -0.0281 226 PHE A CG  
1900 C  CD1 . PHE A 225 ? 0.2034 0.1904 0.1570 0.0251  0.0242  0.0104  226 PHE A CD1 
1901 C  CD2 . PHE A 225 ? 0.1952 0.1925 0.1497 -0.0126 0.0318  -0.0401 226 PHE A CD2 
1902 C  CE1 . PHE A 225 ? 0.1859 0.1876 0.2161 0.0276  0.0346  0.0020  226 PHE A CE1 
1903 C  CE2 . PHE A 225 ? 0.1684 0.2152 0.2045 -0.0119 -0.0020 -0.0922 226 PHE A CE2 
1904 C  CZ  . PHE A 225 ? 0.1656 0.1761 0.2113 -0.0273 0.0012  -0.0653 226 PHE A CZ  
1905 N  N   . ARG A 226 ? 0.1406 0.1429 0.1234 -0.0082 0.0087  -0.0013 227 ARG A N   
1906 C  CA  . ARG A 226 ? 0.1571 0.1356 0.1255 -0.0109 0.0189  -0.0060 227 ARG A CA  
1907 C  C   . ARG A 226 ? 0.1569 0.1345 0.1440 -0.0113 0.0068  0.0007  227 ARG A C   
1908 O  O   . ARG A 226 ? 0.1736 0.1643 0.1406 0.0024  0.0141  0.0031  227 ARG A O   
1909 C  CB  . ARG A 226 ? 0.1606 0.1233 0.1385 0.0012  0.0109  0.0082  227 ARG A CB  
1910 C  CG  . ARG A 226 ? 0.1645 0.1268 0.1173 -0.0104 -0.0017 0.0118  227 ARG A CG  
1911 C  CD  . ARG A 226 ? 0.2382 0.1361 0.1401 -0.0194 0.0155  0.0214  227 ARG A CD  
1912 N  NE  . ARG A 226 ? 0.1938 0.1215 0.1413 -0.0299 -0.0060 0.0012  227 ARG A NE  
1913 C  CZ  . ARG A 226 ? 0.1925 0.1248 0.1348 -0.0357 -0.0087 -0.0177 227 ARG A CZ  
1914 N  NH1 . ARG A 226 ? 0.2107 0.1647 0.2069 -0.0439 -0.0170 -0.0487 227 ARG A NH1 
1915 N  NH2 . ARG A 226 ? 0.2177 0.1312 0.1397 -0.0449 0.0024  0.0035  227 ARG A NH2 
1916 N  N   . LYS A 227 ? 0.1597 0.1318 0.1106 -0.0074 0.0143  -0.0164 228 LYS A N   
1917 C  CA  . LYS A 227 ? 0.1896 0.1615 0.1164 -0.0252 0.0230  -0.0286 228 LYS A CA  
1918 C  C   . LYS A 227 ? 0.1887 0.1448 0.1018 -0.0186 0.0275  -0.0273 228 LYS A C   
1919 O  O   . LYS A 227 ? 0.2114 0.1702 0.1309 -0.0215 0.0296  -0.0211 228 LYS A O   
1920 C  CB  . LYS A 227 ? 0.2096 0.1982 0.1254 -0.0265 -0.0071 -0.0465 228 LYS A CB  
1921 C  CG  . LYS A 227 ? 0.2416 0.1909 0.1878 -0.0509 0.0082  -0.0419 228 LYS A CG  
1922 C  CD  . LYS A 227 ? 0.3903 0.3370 0.3133 -0.1533 -0.0571 -0.0908 228 LYS A CD  
1923 C  CE  . LYS A 227 ? 0.6194 0.6474 0.4034 -0.0335 -0.0425 -0.1644 228 LYS A CE  
1924 N  NZ  . LYS A 227 ? 0.4517 0.7433 0.6890 0.0288  -0.0781 0.1155  228 LYS A NZ  
1925 N  N   . LEU A 228 ? 0.1720 0.1277 0.1136 -0.0135 0.0121  -0.0126 229 LEU A N   
1926 C  CA  . LEU A 228 ? 0.1528 0.1386 0.1229 -0.0082 0.0102  -0.0135 229 LEU A CA  
1927 C  C   . LEU A 228 ? 0.1855 0.1181 0.0948 -0.0103 0.0119  -0.0126 229 LEU A C   
1928 O  O   . LEU A 228 ? 0.1664 0.1431 0.1084 -0.0017 0.0151  -0.0148 229 LEU A O   
1929 C  CB  . LEU A 228 ? 0.1634 0.1455 0.1090 -0.0052 0.0098  -0.0166 229 LEU A CB  
1930 C  CG  . LEU A 228 ? 0.1738 0.1588 0.0942 -0.0081 0.0020  0.0065  229 LEU A CG  
1931 C  CD1 . LEU A 228 ? 0.1864 0.1661 0.1076 -0.0081 0.0006  -0.0131 229 LEU A CD1 
1932 C  CD2 . LEU A 228 ? 0.2108 0.1616 0.1295 0.0034  0.0318  0.0271  229 LEU A CD2 
1933 N  N   . ASN A 229 ? 0.1636 0.1361 0.1150 -0.0131 0.0087  -0.0097 230 ASN A N   
1934 C  CA  . ASN A 229 ? 0.1596 0.1430 0.1048 -0.0118 0.0120  -0.0132 230 ASN A CA  
1935 C  C   . ASN A 229 ? 0.1413 0.1534 0.1076 0.0010  0.0331  0.0087  230 ASN A C   
1936 O  O   . ASN A 229 ? 0.1744 0.1438 0.1324 -0.0098 0.0186  -0.0015 230 ASN A O   
1937 C  CB  . ASN A 229 ? 0.2004 0.1736 0.1093 0.0013  0.0176  -0.0092 230 ASN A CB  
1938 C  CG  . ASN A 229 ? 0.2260 0.1905 0.1102 0.0049  0.0339  -0.0243 230 ASN A CG  
1939 O  OD1 . ASN A 229 ? 0.2743 0.1991 0.1368 0.0070  0.0381  -0.0252 230 ASN A OD1 
1940 N  ND2 . ASN A 229 ? 0.2231 0.1702 0.1499 -0.0197 0.0197  -0.0313 230 ASN A ND2 
1941 N  N   . PHE A 230 ? 0.1388 0.1379 0.1347 -0.0130 0.0274  0.0057  231 PHE A N   
1942 C  CA  . PHE A 230 ? 0.1494 0.1439 0.1384 -0.0196 0.0110  0.0170  231 PHE A CA  
1943 C  C   . PHE A 230 ? 0.2045 0.1709 0.1347 -0.0065 0.0219  0.0131  231 PHE A C   
1944 O  O   . PHE A 230 ? 0.1914 0.1641 0.1485 -0.0362 0.0093  0.0219  231 PHE A O   
1945 C  CB  . PHE A 230 ? 0.1729 0.1400 0.1313 -0.0120 0.0287  0.0093  231 PHE A CB  
1946 C  CG  . PHE A 230 ? 0.1436 0.1375 0.1255 -0.0161 0.0146  0.0015  231 PHE A CG  
1947 C  CD1 . PHE A 230 ? 0.1656 0.1386 0.1164 0.0005  0.0054  -0.0043 231 PHE A CD1 
1948 C  CD2 . PHE A 230 ? 0.1604 0.1591 0.1098 0.0131  0.0097  -0.0085 231 PHE A CD2 
1949 C  CE1 . PHE A 230 ? 0.1534 0.1507 0.1272 -0.0253 0.0171  0.0017  231 PHE A CE1 
1950 C  CE2 . PHE A 230 ? 0.1731 0.1552 0.1343 -0.0208 0.0048  0.0037  231 PHE A CE2 
1951 C  CZ  . PHE A 230 ? 0.1684 0.1571 0.1020 -0.0129 0.0107  -0.0017 231 PHE A CZ  
1952 N  N   . ASN A 231 ? 0.1624 0.1731 0.1291 -0.0005 0.0260  0.0118  232 ASN A N   
1953 C  CA  . ASN A 231 ? 0.1704 0.1871 0.1661 -0.0205 0.0259  0.0251  232 ASN A CA  
1954 C  C   . ASN A 231 ? 0.1503 0.1846 0.1384 0.0098  0.0219  0.0087  232 ASN A C   
1955 O  O   . ASN A 231 ? 0.1850 0.1773 0.1451 0.0082  0.0318  0.0097  232 ASN A O   
1956 C  CB  . ASN A 231 ? 0.1888 0.2040 0.1914 0.0017  0.0608  0.0432  232 ASN A CB  
1957 C  CG  . ASN A 231 ? 0.1941 0.1879 0.1641 0.0285  0.0425  0.0185  232 ASN A CG  
1958 O  OD1 . ASN A 231 ? 0.2175 0.2056 0.1664 0.0077  0.0658  0.0026  232 ASN A OD1 
1959 N  ND2 . ASN A 231 ? 0.2511 0.2369 0.1606 0.0346  0.0320  0.0031  232 ASN A ND2 
1960 N  N   . GLY A 232 ? 0.1983 0.1947 0.1720 0.0024  0.0331  0.0397  233 GLY A N   
1961 C  CA  . GLY A 232 ? 0.2278 0.1810 0.1677 0.0228  0.0582  0.0439  233 GLY A CA  
1962 C  C   . GLY A 232 ? 0.1659 0.1952 0.1943 0.0326  0.0027  0.0024  233 GLY A C   
1963 O  O   . GLY A 232 ? 0.2347 0.2644 0.1773 0.0537  0.0746  0.0579  233 GLY A O   
1964 N  N   . GLU A 233 ? 0.1999 0.2282 0.1536 0.0136  0.0445  0.0148  234 GLU A N   
1965 C  CA  . GLU A 233 ? 0.2070 0.2207 0.1676 0.0242  0.0375  0.0126  234 GLU A CA  
1966 C  C   . GLU A 233 ? 0.2339 0.2583 0.2135 0.0285  0.0043  0.0052  234 GLU A C   
1967 O  O   . GLU A 233 ? 0.2286 0.3199 0.1634 0.0197  0.0324  0.0252  234 GLU A O   
1968 C  CB  . GLU A 233 ? 0.2328 0.2231 0.1844 0.0166  0.0175  0.0474  234 GLU A CB  
1969 C  CG  . GLU A 233 ? 0.2685 0.2849 0.1897 -0.0286 0.0291  0.0410  234 GLU A CG  
1970 C  CD  . GLU A 233 ? 0.2924 0.3671 0.2551 0.0524  0.0331  -0.0333 234 GLU A CD  
1971 O  OE1 . GLU A 233 ? 0.3767 0.2921 0.2486 0.0049  0.0832  0.0662  234 GLU A OE1 
1972 O  OE2 . GLU A 233 ? 0.3668 0.3625 0.2371 0.0258  -0.0383 -0.0087 234 GLU A OE2 
1973 N  N   . GLY A 234 ? 0.2942 0.2730 0.1787 0.0705  0.0165  -0.0043 235 GLY A N   
1974 C  CA  . GLY A 234 ? 0.2944 0.4160 0.2423 0.1080  0.0204  -0.0353 235 GLY A CA  
1975 C  C   . GLY A 234 ? 0.3603 0.4489 0.1959 0.1732  0.0590  0.0298  235 GLY A C   
1976 O  O   . GLY A 234 ? 0.3806 0.4796 0.2621 0.1479  0.1211  0.0197  235 GLY A O   
1977 N  N   . GLU A 235 ? 0.2347 0.2933 0.2292 0.0711  0.0666  0.0285  236 GLU A N   
1978 C  CA  . GLU A 235 ? 0.1923 0.2506 0.2635 0.0575  0.0425  0.0288  236 GLU A CA  
1979 C  C   . GLU A 235 ? 0.3023 0.2946 0.2010 0.0617  0.0631  0.0315  236 GLU A C   
1980 O  O   . GLU A 235 ? 0.3228 0.2962 0.2529 0.0335  0.0851  0.0351  236 GLU A O   
1981 C  CB  . GLU A 235 ? 0.2725 0.2515 0.2290 0.0754  0.0636  0.0697  236 GLU A CB  
1982 C  CG  . GLU A 235 ? 0.2903 0.2784 0.2560 0.0207  0.0555  0.0093  236 GLU A CG  
1983 C  CD  . GLU A 235 ? 0.4149 0.4435 0.3323 -0.1211 0.1326  -0.0785 236 GLU A CD  
1984 O  OE1 . GLU A 235 ? 0.2585 0.3524 0.3310 -0.0230 0.0656  0.0097  236 GLU A OE1 
1985 O  OE2 . GLU A 235 ? 0.5299 0.4508 0.4090 -0.1474 0.1727  0.0608  236 GLU A OE2 
1986 N  N   . PRO A 236 ? 0.2217 0.3515 0.2669 0.0754  0.1133  0.1010  237 PRO A N   
1987 C  CA  . PRO A 236 ? 0.3014 0.3373 0.2675 0.1049  0.1296  0.1428  237 PRO A CA  
1988 C  C   . PRO A 236 ? 0.2472 0.2820 0.2008 0.0244  0.0750  0.0612  237 PRO A C   
1989 O  O   . PRO A 236 ? 0.2646 0.3003 0.2140 0.0163  0.0604  0.0397  237 PRO A O   
1990 C  CB  . PRO A 236 ? 0.2486 0.4140 0.3452 0.1098  0.1515  0.1765  237 PRO A CB  
1991 C  CG  . PRO A 236 ? 0.3122 0.3558 0.4842 0.0948  0.1327  0.2487  237 PRO A CG  
1992 C  CD  . PRO A 236 ? 0.2845 0.3643 0.3975 0.0908  0.0627  0.1507  237 PRO A CD  
1993 N  N   . GLU A 237 ? 0.2498 0.2960 0.1982 0.0505  0.0679  -0.0261 238 GLU A N   
1994 C  CA  . GLU A 237 ? 0.2214 0.2759 0.1675 0.0260  0.0684  -0.0038 238 GLU A CA  
1995 C  C   . GLU A 237 ? 0.1948 0.2092 0.1955 0.0013  0.0718  0.0041  238 GLU A C   
1996 O  O   . GLU A 237 ? 0.1852 0.2193 0.1722 0.0348  0.0399  -0.0136 238 GLU A O   
1997 C  CB  . GLU A 237 ? 0.2772 0.2874 0.2152 0.0562  0.0286  -0.0732 238 GLU A CB  
1998 C  CG  . GLU A 237 ? 0.2619 0.2975 0.2560 0.0195  -0.0006 -0.1040 238 GLU A CG  
1999 C  CD  . GLU A 237 ? 0.2831 0.2924 0.2621 0.0115  0.0193  -0.1324 238 GLU A CD  
2000 O  OE1 . GLU A 237 ? 0.4997 0.4248 0.5860 0.0666  -0.0665 -0.3181 238 GLU A OE1 
2001 O  OE2 . GLU A 237 ? 0.2892 0.2225 0.2308 0.0159  0.0171  -0.0627 238 GLU A OE2 
2002 N  N   . GLU A 238 ? 0.1772 0.1918 0.1518 -0.0131 0.0469  -0.0197 239 GLU A N   
2003 C  CA  . GLU A 238 ? 0.1573 0.2011 0.1625 -0.0195 0.0507  -0.0003 239 GLU A CA  
2004 C  C   . GLU A 238 ? 0.1615 0.1625 0.1481 0.0082  0.0425  -0.0003 239 GLU A C   
2005 O  O   . GLU A 238 ? 0.2142 0.1648 0.1643 -0.0057 0.0461  -0.0027 239 GLU A O   
2006 C  CB  . GLU A 238 ? 0.1867 0.2108 0.2351 -0.0263 0.0331  0.0010  239 GLU A CB  
2007 C  CG  . GLU A 238 ? 0.2318 0.2861 0.2696 -0.0151 0.0401  -0.0657 239 GLU A CG  
2008 C  CD  . GLU A 238 ? 0.3413 0.4374 0.3499 -0.1476 0.0627  -0.1297 239 GLU A CD  
2009 O  OE1 . GLU A 238 ? 0.3564 0.4444 0.4347 -0.0961 0.0238  -0.1553 239 GLU A OE1 
2010 O  OE2 . GLU A 238 ? 0.4842 0.7530 0.6456 -0.3652 0.1780  -0.2178 239 GLU A OE2 
2011 N  N   . LEU A 239 ? 0.1537 0.1539 0.1211 0.0020  0.0318  -0.0220 240 LEU A N   
2012 C  CA  . LEU A 239 ? 0.1448 0.1494 0.1314 -0.0034 0.0252  -0.0159 240 LEU A CA  
2013 C  C   . LEU A 239 ? 0.1526 0.1465 0.1045 -0.0099 0.0126  0.0052  240 LEU A C   
2014 O  O   . LEU A 239 ? 0.1444 0.1537 0.1323 0.0071  0.0266  -0.0059 240 LEU A O   
2015 C  CB  . LEU A 239 ? 0.1568 0.1339 0.1539 0.0060  0.0197  -0.0098 240 LEU A CB  
2016 C  CG  . LEU A 239 ? 0.1682 0.1555 0.1964 -0.0109 0.0136  -0.0414 240 LEU A CG  
2017 C  CD1 . LEU A 239 ? 0.2702 0.1318 0.2946 0.0217  -0.0346 -0.0366 240 LEU A CD1 
2018 C  CD2 . LEU A 239 ? 0.2222 0.1797 0.1773 0.0189  0.0035  -0.0430 240 LEU A CD2 
2019 N  N   . MET A 240 ? 0.1404 0.1356 0.1127 -0.0031 0.0258  -0.0051 241 MET A N   
2020 C  CA  . MET A 240 ? 0.1670 0.1334 0.1008 0.0068  0.0414  -0.0015 241 MET A CA  
2021 C  C   . MET A 240 ? 0.1342 0.1194 0.1011 -0.0146 0.0115  -0.0109 241 MET A C   
2022 O  O   . MET A 240 ? 0.1386 0.1350 0.1032 -0.0129 0.0114  0.0010  241 MET A O   
2023 C  CB  . MET A 240 ? 0.1503 0.1199 0.1206 -0.0020 0.0137  0.0142  241 MET A CB  
2024 C  CG  . MET A 240 ? 0.1607 0.1552 0.1027 -0.0208 0.0372  -0.0114 241 MET A CG  
2025 S  SD  . MET A 240 ? 0.1729 0.1261 0.1336 -0.0120 0.0222  -0.0017 241 MET A SD  
2026 C  CE  . MET A 240 ? 0.1879 0.1266 0.1394 -0.0199 0.0535  0.0270  241 MET A CE  
2027 N  N   . VAL A 241 ? 0.1386 0.1137 0.1078 -0.0153 0.0156  -0.0115 242 VAL A N   
2028 C  CA  . VAL A 241 ? 0.1341 0.1099 0.0981 -0.0231 0.0126  -0.0071 242 VAL A CA  
2029 C  C   . VAL A 241 ? 0.1229 0.0887 0.1169 -0.0099 0.0140  -0.0153 242 VAL A C   
2030 O  O   . VAL A 241 ? 0.1209 0.1327 0.1002 -0.0093 0.0177  -0.0121 242 VAL A O   
2031 C  CB  . VAL A 241 ? 0.1480 0.1155 0.1190 -0.0163 0.0186  -0.0131 242 VAL A CB  
2032 C  CG1 . VAL A 241 ? 0.2009 0.1333 0.1264 -0.0405 -0.0027 -0.0368 242 VAL A CG1 
2033 C  CG2 . VAL A 241 ? 0.1679 0.1289 0.1438 -0.0026 0.0317  -0.0253 242 VAL A CG2 
2034 N  N   . ASP A 242 ? 0.1215 0.0956 0.0944 -0.0060 0.0200  -0.0126 243 ASP A N   
2035 C  CA  . ASP A 242 ? 0.1173 0.0970 0.1002 0.0041  0.0115  -0.0052 243 ASP A CA  
2036 C  C   . ASP A 242 ? 0.1020 0.1121 0.0992 -0.0098 0.0146  -0.0120 243 ASP A C   
2037 O  O   . ASP A 242 ? 0.1139 0.1141 0.1421 -0.0070 0.0057  -0.0017 243 ASP A O   
2038 C  CB  . ASP A 242 ? 0.1146 0.0938 0.1227 0.0031  0.0131  -0.0068 243 ASP A CB  
2039 C  CG  . ASP A 242 ? 0.1253 0.1018 0.1254 -0.0019 0.0071  -0.0203 243 ASP A CG  
2040 O  OD1 . ASP A 242 ? 0.1215 0.0975 0.1309 0.0048  0.0131  -0.0077 243 ASP A OD1 
2041 O  OD2 . ASP A 242 ? 0.1483 0.1154 0.1573 0.0015  0.0240  -0.0200 243 ASP A OD2 
2042 N  N   . ASN A 243 ? 0.1048 0.0900 0.0960 -0.0017 0.0148  -0.0152 244 ASN A N   
2043 C  CA  . ASN A 243 ? 0.1036 0.0891 0.1036 0.0005  0.0120  -0.0087 244 ASN A CA  
2044 C  C   . ASN A 243 ? 0.0975 0.0909 0.0900 -0.0076 0.0125  0.0010  244 ASN A C   
2045 O  O   . ASN A 243 ? 0.1300 0.1060 0.1039 0.0104  0.0222  0.0017  244 ASN A O   
2046 C  CB  . ASN A 243 ? 0.1106 0.1026 0.0956 -0.0164 0.0131  0.0024  244 ASN A CB  
2047 C  CG  . ASN A 243 ? 0.1190 0.0978 0.1076 -0.0146 0.0071  -0.0012 244 ASN A CG  
2048 O  OD1 . ASN A 243 ? 0.1057 0.1120 0.1254 -0.0109 0.0080  0.0252  244 ASN A OD1 
2049 N  ND2 . ASN A 243 ? 0.1494 0.1580 0.1643 -0.0317 -0.0219 0.0548  244 ASN A ND2 
2050 N  N   . TRP A 244 ? 0.0965 0.0923 0.0881 -0.0065 0.0098  0.0006  245 TRP A N   
2051 C  CA  . TRP A 244 ? 0.0999 0.1005 0.0876 -0.0126 0.0076  -0.0071 245 TRP A CA  
2052 C  C   . TRP A 244 ? 0.0947 0.0876 0.1080 0.0003  0.0043  0.0003  245 TRP A C   
2053 O  O   . TRP A 244 ? 0.1051 0.1133 0.1130 0.0118  -0.0026 -0.0115 245 TRP A O   
2054 C  CB  . TRP A 244 ? 0.1075 0.0917 0.1071 -0.0038 0.0194  -0.0027 245 TRP A CB  
2055 C  CG  . TRP A 244 ? 0.0877 0.0904 0.1075 -0.0026 0.0030  -0.0043 245 TRP A CG  
2056 C  CD1 . TRP A 244 ? 0.0979 0.0904 0.1099 0.0000  0.0284  -0.0093 245 TRP A CD1 
2057 C  CD2 . TRP A 244 ? 0.0923 0.0993 0.1011 -0.0093 0.0121  -0.0031 245 TRP A CD2 
2058 N  NE1 . TRP A 244 ? 0.1145 0.1002 0.1076 -0.0048 0.0104  0.0027  245 TRP A NE1 
2059 C  CE2 . TRP A 244 ? 0.1124 0.0960 0.1141 -0.0074 0.0065  0.0043  245 TRP A CE2 
2060 C  CE3 . TRP A 244 ? 0.1203 0.0993 0.1137 -0.0074 0.0076  0.0060  245 TRP A CE3 
2061 C  CZ2 . TRP A 244 ? 0.1406 0.1044 0.1300 0.0000  0.0214  0.0041  245 TRP A CZ2 
2062 C  CZ3 . TRP A 244 ? 0.1343 0.1230 0.1386 0.0070  0.0027  -0.0046 245 TRP A CZ3 
2063 C  CH2 . TRP A 244 ? 0.1289 0.1259 0.1360 0.0049  0.0172  0.0098  245 TRP A CH2 
2064 N  N   . ARG A 245 ? 0.0917 0.1078 0.0930 -0.0098 0.0052  -0.0216 246 ARG A N   
2065 C  CA  . ARG A 245 ? 0.0952 0.0966 0.1002 0.0027  0.0082  -0.0020 246 ARG A CA  
2066 C  C   . ARG A 245 ? 0.0869 0.0961 0.0948 0.0054  0.0087  -0.0192 246 ARG A C   
2067 O  O   . ARG A 245 ? 0.0969 0.1121 0.1118 -0.0026 0.0087  -0.0113 246 ARG A O   
2068 C  CB  . ARG A 245 ? 0.0850 0.1078 0.1155 -0.0017 0.0013  -0.0131 246 ARG A CB  
2069 C  CG  . ARG A 245 ? 0.0746 0.1118 0.1196 -0.0118 0.0031  -0.0081 246 ARG A CG  
2070 C  CD  . ARG A 245 ? 0.0776 0.1177 0.1155 -0.0151 0.0071  -0.0108 246 ARG A CD  
2071 N  NE  . ARG A 245 ? 0.0829 0.1160 0.1234 -0.0125 0.0054  -0.0131 246 ARG A NE  
2072 C  CZ  . ARG A 245 ? 0.0754 0.1234 0.1102 -0.0091 0.0071  -0.0086 246 ARG A CZ  
2073 N  NH1 . ARG A 245 ? 0.0992 0.1212 0.1181 -0.0195 0.0167  -0.0093 246 ARG A NH1 
2074 N  NH2 . ARG A 245 ? 0.0936 0.1553 0.1361 -0.0274 0.0003  -0.0109 246 ARG A NH2 
2075 N  N   A PRO A 246 ? 0.0932 0.1014 0.1154 0.0010  0.0092  0.0041  247 PRO A N   
2076 N  N   B PRO A 246 ? 0.1005 0.0997 0.1128 0.0000  0.0060  0.0038  247 PRO A N   
2077 C  CA  A PRO A 246 ? 0.1190 0.1139 0.1044 0.0153  -0.0131 0.0000  247 PRO A CA  
2078 C  CA  B PRO A 246 ? 0.1305 0.1067 0.0974 0.0186  0.0070  0.0010  247 PRO A CA  
2079 C  C   A PRO A 246 ? 0.1078 0.1005 0.1196 0.0063  0.0000  -0.0060 247 PRO A C   
2080 C  C   B PRO A 246 ? 0.1106 0.1030 0.1040 0.0073  -0.0052 -0.0082 247 PRO A C   
2081 O  O   A PRO A 246 ? 0.0996 0.0997 0.1036 0.0005  0.0048  -0.0024 247 PRO A O   
2082 O  O   B PRO A 246 ? 0.1124 0.1072 0.1075 0.0017  0.0038  -0.0012 247 PRO A O   
2083 C  CB  A PRO A 246 ? 0.1238 0.1096 0.1072 0.0119  0.0136  -0.0005 247 PRO A CB  
2084 C  CB  B PRO A 246 ? 0.1036 0.1196 0.1327 -0.0006 -0.0164 -0.0071 247 PRO A CB  
2085 C  CG  A PRO A 246 ? 0.1136 0.1360 0.1203 0.0196  0.0261  0.0229  247 PRO A CG  
2086 C  CG  B PRO A 246 ? 0.1178 0.1239 0.1740 0.0153  0.0219  0.0068  247 PRO A CG  
2087 C  CD  A PRO A 246 ? 0.0878 0.1137 0.1321 0.0164  0.0026  -0.0093 247 PRO A CD  
2088 C  CD  B PRO A 246 ? 0.1098 0.1266 0.1145 0.0197  0.0062  -0.0251 247 PRO A CD  
2089 N  N   . ALA A 247 ? 0.1253 0.1190 0.1132 0.0065  0.0020  0.0041  248 ALA A N   
2090 C  CA  . ALA A 247 ? 0.1087 0.1208 0.1063 -0.0006 0.0000  0.0063  248 ALA A CA  
2091 C  C   . ALA A 247 ? 0.0900 0.1325 0.1102 0.0148  0.0062  0.0068  248 ALA A C   
2092 O  O   . ALA A 247 ? 0.1130 0.1415 0.1309 0.0265  -0.0063 0.0126  248 ALA A O   
2093 C  CB  . ALA A 247 ? 0.1603 0.1509 0.1208 -0.0148 0.0151  0.0046  248 ALA A CB  
2094 N  N   . GLN A 248 ? 0.0956 0.1142 0.1032 -0.0020 -0.0082 0.0054  249 GLN A N   
2095 C  CA  . GLN A 248 ? 0.0945 0.1247 0.1175 -0.0019 -0.0082 0.0137  249 GLN A CA  
2096 C  C   . GLN A 248 ? 0.1035 0.1157 0.1159 0.0148  -0.0135 0.0244  249 GLN A C   
2097 O  O   . GLN A 248 ? 0.1190 0.1336 0.1348 0.0003  0.0037  0.0098  249 GLN A O   
2098 C  CB  . GLN A 248 ? 0.1148 0.1242 0.1224 0.0077  -0.0115 0.0113  249 GLN A CB  
2099 C  CG  . GLN A 248 ? 0.1282 0.1239 0.1209 -0.0038 -0.0087 0.0129  249 GLN A CG  
2100 C  CD  . GLN A 248 ? 0.1036 0.1616 0.1422 -0.0219 -0.0065 0.0120  249 GLN A CD  
2101 O  OE1 . GLN A 248 ? 0.1145 0.2153 0.1667 -0.0324 -0.0027 -0.0110 249 GLN A OE1 
2102 N  NE2 . GLN A 248 ? 0.1471 0.1567 0.1368 -0.0137 0.0046  0.0000  249 GLN A NE2 
2103 N  N   . PRO A 249 ? 0.1155 0.1577 0.1270 0.0217  -0.0026 0.0098  250 PRO A N   
2104 C  CA  . PRO A 249 ? 0.1402 0.1814 0.1243 0.0315  -0.0024 0.0000  250 PRO A CA  
2105 C  C   . PRO A 249 ? 0.1243 0.1298 0.1085 0.0175  -0.0148 0.0120  250 PRO A C   
2106 O  O   . PRO A 249 ? 0.1123 0.1384 0.1340 0.0175  -0.0120 0.0129  250 PRO A O   
2107 C  CB  . PRO A 249 ? 0.1377 0.2447 0.1709 0.0564  -0.0434 -0.0219 250 PRO A CB  
2108 C  CG  . PRO A 249 ? 0.1447 0.2829 0.1613 0.0194  -0.0351 -0.0255 250 PRO A CG  
2109 C  CD  . PRO A 249 ? 0.1010 0.2339 0.1720 0.0353  -0.0337 -0.0164 250 PRO A CD  
2110 N  N   . LEU A 250 ? 0.1582 0.1464 0.1163 0.0296  -0.0031 0.0167  251 LEU A N   
2111 C  CA  . LEU A 250 ? 0.1449 0.1377 0.1318 0.0031  0.0052  0.0076  251 LEU A CA  
2112 C  C   . LEU A 250 ? 0.1282 0.1275 0.1151 0.0109  -0.0135 0.0243  251 LEU A C   
2113 O  O   . LEU A 250 ? 0.1361 0.1333 0.1357 0.0151  -0.0276 0.0060  251 LEU A O   
2114 C  CB  . LEU A 250 ? 0.1692 0.1544 0.1488 -0.0103 0.0097  0.0049  251 LEU A CB  
2115 C  CG  . LEU A 250 ? 0.1656 0.1674 0.1569 -0.0199 0.0329  0.0043  251 LEU A CG  
2116 C  CD1 . LEU A 250 ? 0.1537 0.1920 0.1562 -0.0107 -0.0141 -0.0281 251 LEU A CD1 
2117 C  CD2 . LEU A 250 ? 0.2017 0.2002 0.2061 -0.0335 0.0401  -0.0146 251 LEU A CD2 
2118 N  N   A LYS A 251 ? 0.1272 0.1406 0.1005 0.0152  -0.0227 0.0153  252 LYS A N   
2119 N  N   B LYS A 251 ? 0.1289 0.1726 0.1242 0.0205  -0.0143 0.0351  252 LYS A N   
2120 C  CA  A LYS A 251 ? 0.1123 0.1509 0.1006 0.0188  -0.0322 0.0185  252 LYS A CA  
2121 C  CA  B LYS A 251 ? 0.1747 0.1864 0.1342 0.0296  -0.0102 -0.0049 252 LYS A CA  
2122 C  C   A LYS A 251 ? 0.1412 0.1895 0.1263 0.0093  -0.0248 -0.0060 252 LYS A C   
2123 C  C   B LYS A 251 ? 0.1289 0.1932 0.1720 0.0252  -0.0091 0.0205  252 LYS A C   
2124 O  O   A LYS A 251 ? 0.1515 0.2152 0.1571 0.0054  -0.0060 -0.0251 252 LYS A O   
2125 O  O   B LYS A 251 ? 0.2016 0.2400 0.1855 -0.0020 0.0472  0.0154  252 LYS A O   
2126 C  CB  A LYS A 251 ? 0.1639 0.1334 0.1648 0.0035  -0.0126 0.0097  252 LYS A CB  
2127 C  CB  B LYS A 251 ? 0.1747 0.1803 0.1842 0.0080  -0.0619 0.0370  252 LYS A CB  
2128 C  CG  A LYS A 251 ? 0.1063 0.2448 0.1715 -0.0260 -0.0052 -0.0040 252 LYS A CG  
2129 C  CG  B LYS A 251 ? 0.2436 0.2131 0.2700 0.0195  -0.0026 -0.0074 252 LYS A CG  
2130 C  CD  A LYS A 251 ? 0.1844 0.2408 0.2178 0.0141  0.0359  0.0597  252 LYS A CD  
2131 C  CD  B LYS A 251 ? 0.1889 0.2011 0.2436 0.0024  -0.0476 -0.0693 252 LYS A CD  
2132 C  CE  A LYS A 251 ? 0.1562 0.2408 0.3046 -0.0220 0.0601  -0.0417 252 LYS A CE  
2133 C  CE  B LYS A 251 ? 0.1348 0.2454 0.4785 -0.0456 0.0359  -0.0439 252 LYS A CE  
2134 N  NZ  A LYS A 251 ? 0.1527 0.2887 0.2996 0.0000  0.0186  0.0560  252 LYS A NZ  
2135 N  NZ  B LYS A 251 ? 0.1582 0.3621 0.4104 0.0683  0.0529  -0.0098 252 LYS A NZ  
2136 N  N   . ASN A 252 ? 0.1455 0.1914 0.1230 0.0060  -0.0274 -0.0192 253 ASN A N   
2137 C  CA  . ASN A 252 ? 0.2143 0.2890 0.1381 0.0263  -0.0129 -0.0538 253 ASN A CA  
2138 C  C   . ASN A 252 ? 0.2221 0.2296 0.2022 0.0254  -0.0085 -0.0027 253 ASN A C   
2139 O  O   . ASN A 252 ? 0.2365 0.2544 0.2730 0.0181  -0.0065 -0.0147 253 ASN A O   
2140 C  CB  . ASN A 252 ? 0.2632 0.3716 0.1776 -0.0357 -0.0395 -0.0744 253 ASN A CB  
2141 C  CG  . ASN A 252 ? 0.3490 0.3379 0.2689 -0.0109 0.0125  -0.0794 253 ASN A CG  
2142 O  OD1 . ASN A 252 ? 0.6764 0.5120 0.2833 -0.1115 0.0948  -0.0155 253 ASN A OD1 
2143 N  ND2 . ASN A 252 ? 0.3018 0.3336 0.3686 -0.0077 -0.0012 -0.1247 253 ASN A ND2 
2144 N  N   . ARG A 253 ? 0.1501 0.2430 0.1178 0.0192  -0.0043 0.0208  254 ARG A N   
2145 C  CA  . ARG A 253 ? 0.1137 0.1580 0.1049 0.0125  -0.0098 0.0024  254 ARG A CA  
2146 C  C   . ARG A 253 ? 0.1634 0.1431 0.1173 0.0119  0.0027  -0.0108 254 ARG A C   
2147 O  O   . ARG A 253 ? 0.2170 0.1914 0.2633 0.0463  0.1008  0.0511  254 ARG A O   
2148 C  CB  . ARG A 253 ? 0.1374 0.1474 0.0960 -0.0035 0.0076  -0.0031 254 ARG A CB  
2149 C  CG  . ARG A 253 ? 0.1345 0.1410 0.1199 0.0054  0.0065  0.0007  254 ARG A CG  
2150 C  CD  . ARG A 253 ? 0.1402 0.1194 0.0945 0.0074  0.0142  -0.0118 254 ARG A CD  
2151 N  NE  . ARG A 253 ? 0.1051 0.1225 0.1035 0.0057  -0.0093 -0.0077 254 ARG A NE  
2152 C  CZ  . ARG A 253 ? 0.0969 0.1085 0.0873 -0.0065 0.0024  -0.0015 254 ARG A CZ  
2153 N  NH1 . ARG A 253 ? 0.0869 0.1036 0.0993 -0.0068 -0.0103 0.0024  254 ARG A NH1 
2154 N  NH2 . ARG A 253 ? 0.0922 0.1102 0.0961 0.0087  -0.0142 -0.0086 254 ARG A NH2 
2155 N  N   . GLN A 254 ? 0.1280 0.1733 0.1208 -0.0046 -0.0065 -0.0344 255 GLN A N   
2156 C  CA  . GLN A 254 ? 0.1597 0.1846 0.1190 -0.0043 -0.0027 -0.0310 255 GLN A CA  
2157 C  C   . GLN A 254 ? 0.1449 0.1359 0.1280 0.0097  -0.0073 -0.0076 255 GLN A C   
2158 O  O   . GLN A 254 ? 0.1995 0.1517 0.1905 -0.0086 -0.0370 -0.0109 255 GLN A O   
2159 C  CB  . GLN A 254 ? 0.1733 0.3262 0.1515 -0.0286 0.0182  -0.0860 255 GLN A CB  
2160 C  CG  . GLN A 254 ? 0.3005 0.3404 0.1682 -0.0175 0.0146  0.0020  255 GLN A CG  
2161 C  CD  . GLN A 254 ? 0.3903 0.4435 0.1983 0.0373  0.0746  0.0930  255 GLN A CD  
2162 O  OE1 . GLN A 254 ? 0.4472 0.4241 0.4654 0.0535  0.1132  -0.0406 255 GLN A OE1 
2163 N  NE2 . GLN A 254 ? 0.5888 0.4131 0.1999 -0.0189 0.0846  0.0434  255 GLN A NE2 
2164 N  N   . ILE A 255 ? 0.1186 0.1386 0.1089 0.0000  -0.0034 -0.0088 256 ILE A N   
2165 C  CA  . ILE A 255 ? 0.1123 0.1289 0.1020 0.0068  0.0020  0.0010  256 ILE A CA  
2166 C  C   . ILE A 255 ? 0.1184 0.1211 0.0930 -0.0071 0.0155  0.0085  256 ILE A C   
2167 O  O   . ILE A 255 ? 0.1422 0.1515 0.1178 0.0126  0.0151  0.0285  256 ILE A O   
2168 C  CB  . ILE A 255 ? 0.1221 0.1146 0.1096 0.0071  -0.0074 -0.0063 256 ILE A CB  
2169 C  CG1 . ILE A 255 ? 0.1186 0.1323 0.1343 0.0086  -0.0024 -0.0125 256 ILE A CG1 
2170 C  CG2 . ILE A 255 ? 0.1212 0.1641 0.1270 -0.0093 -0.0120 -0.0093 256 ILE A CG2 
2171 C  CD1 . ILE A 255 ? 0.1453 0.1587 0.1422 0.0000  0.0205  -0.0264 256 ILE A CD1 
2172 N  N   . LYS A 256 ? 0.1111 0.1332 0.0972 -0.0057 0.0027  0.0024  257 LYS A N   
2173 C  CA  . LYS A 256 ? 0.0993 0.1298 0.1040 -0.0118 0.0153  0.0015  257 LYS A CA  
2174 C  C   . LYS A 256 ? 0.1181 0.1248 0.0966 -0.0060 0.0077  0.0142  257 LYS A C   
2175 O  O   . LYS A 256 ? 0.1300 0.1754 0.0983 -0.0331 0.0035  0.0137  257 LYS A O   
2176 C  CB  . LYS A 256 ? 0.1257 0.1458 0.1350 -0.0160 0.0274  -0.0253 257 LYS A CB  
2177 C  CG  . LYS A 256 ? 0.2143 0.1377 0.1921 -0.0164 0.0313  -0.0403 257 LYS A CG  
2178 C  CD  . LYS A 256 ? 0.0597 0.1485 0.0445 0.0027  -0.0065 -0.0474 257 LYS A CD  
2179 C  CE  . LYS A 256 ? 0.0358 0.1719 0.0653 -0.0120 0.0012  -0.0548 257 LYS A CE  
2180 N  NZ  . LYS A 256 ? 0.0263 0.1680 0.0381 -0.0116 0.0034  -0.0426 257 LYS A NZ  
2181 N  N   . ALA A 257 ? 0.1027 0.1517 0.1057 -0.0091 0.0225  -0.0013 258 ALA A N   
2182 C  CA  . ALA A 257 ? 0.0957 0.1480 0.1215 -0.0119 0.0120  0.0020  258 ALA A CA  
2183 C  C   . ALA A 257 ? 0.1084 0.1557 0.1248 -0.0124 0.0088  -0.0124 258 ALA A C   
2184 O  O   . ALA A 257 ? 0.1248 0.1747 0.1151 -0.0087 0.0214  -0.0119 258 ALA A O   
2185 C  CB  . ALA A 257 ? 0.1291 0.1632 0.1625 -0.0151 0.0068  0.0063  258 ALA A CB  
2186 N  N   . SER A 258 ? 0.1120 0.1512 0.1103 -0.0024 0.0082  0.0043  259 SER A N   
2187 C  CA  . SER A 258 ? 0.1123 0.1736 0.1446 -0.0109 0.0182  0.0000  259 SER A CA  
2188 C  C   . SER A 258 ? 0.0956 0.1925 0.1422 -0.0164 0.0230  -0.0019 259 SER A C   
2189 O  O   . SER A 258 ? 0.1286 0.2494 0.1938 0.0099  0.0430  -0.0076 259 SER A O   
2190 C  CB  . SER A 258 ? 0.1312 0.1567 0.1444 0.0000  0.0189  -0.0006 259 SER A CB  
2191 O  OG  . SER A 258 ? 0.1053 0.1629 0.1259 -0.0027 0.0163  -0.0060 259 SER A OG  
2192 N  N   . PHE A 259 ? 0.1120 0.1844 0.1569 -0.0265 0.0307  0.0120  260 PHE A N   
2193 C  CA  . PHE A 259 ? 0.1564 0.2193 0.1835 -0.0472 0.0361  0.0160  260 PHE A CA  
2194 C  C   . PHE A 259 ? 0.2275 0.2614 0.1914 -0.0771 0.0573  0.0264  260 PHE A C   
2195 O  O   . PHE A 259 ? 0.2547 0.2372 0.2020 -0.0693 -0.0019 0.0623  260 PHE A O   
2196 C  CB  . PHE A 259 ? 0.1350 0.2161 0.2065 -0.0399 0.0130  -0.0164 260 PHE A CB  
2197 C  CG  . PHE A 259 ? 0.1535 0.1684 0.1943 -0.0263 -0.0013 0.0043  260 PHE A CG  
2198 C  CD1 . PHE A 259 ? 0.1510 0.1679 0.1367 -0.0344 -0.0142 -0.0041 260 PHE A CD1 
2199 C  CD2 . PHE A 259 ? 0.2250 0.1940 0.2556 -0.0164 0.0131  0.0271  260 PHE A CD2 
2200 C  CE1 . PHE A 259 ? 0.1518 0.1825 0.2131 -0.0303 -0.0065 -0.0052 260 PHE A CE1 
2201 C  CE2 . PHE A 259 ? 0.2025 0.2250 0.2811 -0.0143 -0.0060 0.0408  260 PHE A CE2 
2202 C  CZ  . PHE A 259 ? 0.2162 0.1898 0.2119 -0.0141 0.0034  -0.0266 260 PHE A CZ  
2203 N  N   . LYS A 260 ? 0.3555 0.4217 0.3075 -0.1635 0.1194  0.0929  261 LYS A N   
2204 C  CA  . LYS A 260 ? 0.3882 0.5264 0.3228 -0.1321 0.0750  0.1335  261 LYS A CA  
2205 C  C   . LYS A 260 ? 0.8399 0.3262 0.5253 -0.1666 0.1648  0.2117  261 LYS A C   
2206 O  O   . LYS A 260 ? 0.7128 0.5054 0.5400 -0.0373 0.0679  0.1272  261 LYS A O   
2207 C  CB  . LYS A 260 ? 0.9057 0.5188 0.5561 -0.0675 0.1254  -0.0710 261 LYS A CB  
2208 C  CG  . LYS A 260 ? 0.6470 0.7511 0.6057 -0.0071 0.6007  -0.0080 261 LYS A CG  
2209 C  CD  . LYS A 260 ? 0.9617 0.7171 1.0649 -0.4404 0.2689  0.2502  261 LYS A CD  
2210 C  CE  . LYS A 260 ? 0.8708 0.9269 1.0398 -0.1611 0.2275  -0.0046 261 LYS A CE  
2211 N  NZ  . LYS A 260 ? 0.3912 0.9203 1.3887 -0.0081 0.2246  -0.0648 261 LYS A NZ  
2212 O  OXT . LYS A 260 ? 0.8518 0.5723 0.6358 0.0802  0.1580  0.2533  261 LYS A OXT 
2213 ZN ZN  . ZN  B .   ? 0.0842 0.0785 0.0816 -0.0052 -0.0006 -0.0003 301 ZN  A ZN  
2214 N  N1  . BCN C .   ? 0.4952 0.3824 0.3616 0.0242  -0.0285 -0.1128 302 BCN A N1  
2215 C  C1  . BCN C .   ? 0.2321 0.1956 0.2696 -0.0313 0.0274  0.0445  302 BCN A C1  
2216 C  C2  . BCN C .   ? 0.5317 0.5156 0.4025 -0.0469 0.0164  -0.0592 302 BCN A C2  
2217 O  O21 . BCN C .   ? 0.5898 0.4970 0.8298 -0.3088 -0.1397 0.2397  302 BCN A O21 
2218 O  O22 . BCN C .   ? 0.6596 0.3413 0.7156 0.0307  0.0665  -0.0785 302 BCN A O22 
2219 C  C3  . BCN C .   ? 0.3082 0.2128 0.2867 -0.0706 0.0702  0.0211  302 BCN A C3  
2220 C  C4  . BCN C .   ? 0.4682 0.4584 0.3892 0.0838  0.0518  -0.0798 302 BCN A C4  
2221 O  O4  . BCN C .   ? 0.3506 0.2773 0.3731 -0.0724 0.0666  -0.0109 302 BCN A O4  
2222 C  C5  . BCN C .   ? 0.3158 0.5040 0.2919 -0.1459 -0.0185 -0.0126 302 BCN A C5  
2223 C  C6  . BCN C .   ? 0.5008 0.5594 0.2495 0.0303  -0.0164 0.0584  302 BCN A C6  
2224 O  O6  . BCN C .   ? 0.2982 0.3490 0.3440 -0.0749 0.0467  0.1001  302 BCN A O6  
2225 S  S   . DMS D .   ? 0.4832 0.3770 0.4185 0.0573  0.1098  0.1194  303 DMS A S   
2226 O  O   . DMS D .   ? 0.2221 0.1722 0.2214 -0.0487 -0.0419 0.0383  303 DMS A O   
2227 C  C1  . DMS D .   ? 0.2865 0.2680 0.3876 0.0060  -0.1453 0.0351  303 DMS A C1  
2228 C  C2  . DMS D .   ? 0.4365 0.5981 0.6402 -0.0353 0.0019  -0.0307 303 DMS A C2  
2229 S  S   . DMS E .   ? 0.2917 0.4372 0.3957 -0.0132 0.0331  -0.0518 304 DMS A S   
2230 O  O   . DMS E .   ? 0.2314 0.3217 0.3822 0.0564  -0.0220 0.0732  304 DMS A O   
2231 C  C1  . DMS E .   ? 0.3677 0.4314 0.4557 0.1783  0.0834  -0.1307 304 DMS A C1  
2232 C  C2  . DMS E .   ? 0.2527 0.2347 0.2883 0.0516  0.0427  -0.0842 304 DMS A C2  
2233 O  O25 . KR5 F .   ? 0.2376 0.2408 0.2497 -0.0121 0.0098  0.0186  305 KR5 A O25 
2234 C  C22 . KR5 F .   ? 0.2188 0.2150 0.1921 -0.0322 0.0636  -0.0071 305 KR5 A C22 
2235 N  N27 . KR5 F .   ? 0.2885 0.2256 0.1765 0.0054  0.0103  0.0197  305 KR5 A N27 
2236 C  C29 . KR5 F .   ? 0.3402 0.2506 0.2973 0.0188  0.0107  -0.0750 305 KR5 A C29 
2237 C  C33 . KR5 F .   ? 0.4323 0.3718 0.3864 0.1316  -0.0274 -0.0020 305 KR5 A C33 
2238 C  C30 . KR5 F .   ? 0.5619 0.2660 0.5486 0.1723  -0.1428 -0.0595 305 KR5 A C30 
2239 C  C31 . KR5 F .   ? 0.8252 0.4230 0.5019 0.0793  -0.1631 0.1280  305 KR5 A C31 
2240 C  C37 . KR5 F .   ? 1.0650 0.8245 0.5098 0.2105  -0.0285 0.3531  305 KR5 A C37 
2241 N  N28 . KR5 F .   ? 0.6233 0.4059 0.5088 0.1137  -0.0776 0.1591  305 KR5 A N28 
2242 C  C19 . KR5 F .   ? 0.2549 0.1841 0.1992 -0.0428 0.0388  0.0126  305 KR5 A C19 
2243 C  C18 . KR5 F .   ? 0.1794 0.1427 0.2117 -0.0331 0.0537  0.0041  305 KR5 A C18 
2244 N  N17 . KR5 F .   ? 0.1632 0.1132 0.1562 -0.0275 0.0182  0.0007  305 KR5 A N17 
2245 C  C8  . KR5 F .   ? 0.1472 0.0887 0.1130 -0.0198 0.0027  0.0082  305 KR5 A C8  
2246 C  C7  . KR5 F .   ? 0.1359 0.1071 0.1136 -0.0102 0.0051  0.0062  305 KR5 A C7  
2247 C  C6  . KR5 F .   ? 0.1242 0.1002 0.1076 -0.0103 0.0000  -0.0010 305 KR5 A C6  
2248 C  C9  . KR5 F .   ? 0.1233 0.0873 0.1280 -0.0010 -0.0164 0.0085  305 KR5 A C9  
2249 C  C10 . KR5 F .   ? 0.1163 0.1063 0.1093 -0.0097 -0.0176 0.0031  305 KR5 A C10 
2250 C  C5  . KR5 F .   ? 0.1066 0.0935 0.0916 0.0006  -0.0076 0.0031  305 KR5 A C5  
2251 S  S2  . KR5 F .   ? 0.0850 0.0904 0.0908 -0.0082 -0.0040 -0.0031 305 KR5 A S2  
2252 O  O3  . KR5 F .   ? 0.0797 0.0869 0.0952 -0.0063 0.0005  -0.0020 305 KR5 A O3  
2253 O  O4  . KR5 F .   ? 0.0856 0.0948 0.0957 -0.0074 0.0024  0.0012  305 KR5 A O4  
2254 N  N1  . KR5 F .   ? 0.0877 0.0728 0.0913 -0.0273 -0.0143 -0.0093 305 KR5 A N1  
2255 O  O   . HOH G .   ? 0.1238 0.1093 0.1089 0.0043  -0.0038 -0.0087 401 HOH A O   
2256 O  O   . HOH G .   ? 0.0983 0.1202 0.1239 -0.0098 0.0175  -0.0038 402 HOH A O   
2257 O  O   . HOH G .   ? 0.1215 0.1112 0.1120 -0.0015 0.0120  -0.0093 403 HOH A O   
2258 O  O   . HOH G .   ? 0.1230 0.1105 0.1388 0.0060  -0.0019 -0.0013 404 HOH A O   
2259 O  O   . HOH G .   ? 0.1360 0.1184 0.1357 -0.0063 0.0104  -0.0104 405 HOH A O   
2260 O  O   . HOH G .   ? 0.1190 0.1358 0.1456 0.0170  -0.0082 0.0063  406 HOH A O   
2261 O  O   . HOH G .   ? 0.1159 0.1500 0.1254 0.0030  -0.0159 0.0219  407 HOH A O   
2262 O  O   . HOH G .   ? 0.1411 0.1071 0.0838 -0.0098 -0.0035 0.0057  408 HOH A O   
2263 O  O   . HOH G .   ? 0.1273 0.1141 0.1247 -0.0068 0.0000  -0.0120 409 HOH A O   
2264 O  O   . HOH G .   ? 0.1001 0.1525 0.1718 -0.0088 -0.0035 -0.0304 410 HOH A O   
2265 O  O   . HOH G .   ? 0.1209 0.1339 0.1230 0.0164  0.0005  0.0049  411 HOH A O   
2266 O  O   . HOH G .   ? 0.1186 0.1887 0.1598 -0.0060 -0.0302 0.0322  412 HOH A O   
2267 O  O   . HOH G .   ? 0.1519 0.1164 0.1600 0.0020  -0.0148 -0.0087 413 HOH A O   
2268 O  O   . HOH G .   ? 0.1582 0.1406 0.1695 0.0233  0.0093  0.0076  414 HOH A O   
2269 O  O   . HOH G .   ? 0.1535 0.1550 0.1386 -0.0049 0.0230  -0.0114 415 HOH A O   
2270 O  O   . HOH G .   ? 0.1679 0.1164 0.1397 -0.0154 0.0126  0.0063  416 HOH A O   
2271 O  O   . HOH G .   ? 0.2081 0.1886 0.1587 0.0020  0.0375  0.0401  417 HOH A O   
2272 O  O   . HOH G .   ? 0.0876 0.2004 0.1909 0.0210  0.0274  -0.0192 418 HOH A O   
2273 O  O   . HOH G .   ? 0.1613 0.1360 0.1792 -0.0071 0.0185  0.0027  419 HOH A O   
2274 O  O   . HOH G .   ? 0.1409 0.1582 0.1720 0.0109  -0.0162 0.0076  420 HOH A O   
2275 O  O   . HOH G .   ? 0.2182 0.1688 0.1745 -0.0010 -0.0522 0.0160  421 HOH A O   
2276 O  O   . HOH G .   ? 0.1560 0.1494 0.1567 -0.0020 -0.0051 -0.0024 422 HOH A O   
2277 O  O   . HOH G .   ? 0.1537 0.1137 0.1650 -0.0155 -0.0005 0.0057  423 HOH A O   
2278 O  O   . HOH G .   ? 0.2028 0.1429 0.1870 -0.0265 -0.0114 -0.0210 424 HOH A O   
2279 O  O   . HOH G .   ? 0.1172 0.1792 0.2451 -0.0196 0.0082  0.0000  425 HOH A O   
2280 O  O   . HOH G .   ? 0.1923 0.1508 0.2196 -0.0621 -0.0443 -0.0184 426 HOH A O   
2281 O  O   . HOH G .   ? 0.1814 0.1604 0.1718 0.0085  -0.0302 0.0073  427 HOH A O   
2282 O  O   . HOH G .   ? 0.1871 0.1203 0.1810 0.0031  -0.0148 -0.0195 428 HOH A O   
2283 O  O   . HOH G .   ? 0.2310 0.1749 0.1788 0.0027  -0.0395 -0.0088 429 HOH A O   
2284 O  O   . HOH G .   ? 0.1343 0.1841 0.1756 0.0000  -0.0010 0.0170  430 HOH A O   
2285 O  O   . HOH G .   ? 0.1733 0.2029 0.2178 -0.0020 -0.0675 -0.0348 431 HOH A O   
2286 O  O   . HOH G .   ? 0.1776 0.1912 0.1889 0.0085  0.0342  -0.0098 432 HOH A O   
2287 O  O   . HOH G .   ? 0.1870 0.1605 0.1728 -0.0088 -0.0006 0.0038  433 HOH A O   
2288 O  O   . HOH G .   ? 0.1456 0.1580 0.2585 -0.0313 -0.0430 0.0130  434 HOH A O   
2289 O  O   . HOH G .   ? 0.2433 0.1316 0.1905 -0.0113 0.0065  0.0162  435 HOH A O   
2290 O  O   . HOH G .   ? 0.1977 0.1336 0.1629 0.0155  -0.0099 0.0124  436 HOH A O   
2291 O  O   . HOH G .   ? 0.2168 0.2675 0.2026 -0.0421 0.0529  0.0159  437 HOH A O   
2292 O  O   . HOH G .   ? 0.3219 0.2020 0.1967 -0.0516 -0.0388 -0.0104 438 HOH A O   
2293 O  O   . HOH G .   ? 0.1893 0.1753 0.2126 -0.0043 -0.0310 -0.0644 439 HOH A O   
2294 O  O   . HOH G .   ? 0.1819 0.1844 0.1932 0.0230  -0.0329 0.0265  440 HOH A O   
2295 O  O   . HOH G .   ? 0.2466 0.1941 0.1984 0.0269  0.0263  0.0754  441 HOH A O   
2296 O  O   . HOH G .   ? 0.1948 0.2382 0.1880 0.0077  -0.0416 0.0188  442 HOH A O   
2297 O  O   . HOH G .   ? 0.2278 0.2497 0.2326 -0.0544 -0.0460 0.0135  443 HOH A O   
2298 O  O   . HOH G .   ? 0.3391 0.3043 0.1474 -0.0023 0.0003  -0.0203 444 HOH A O   
2299 O  O   . HOH G .   ? 0.2114 0.2199 0.2858 0.0041  0.0538  0.0419  445 HOH A O   
2300 O  O   . HOH G .   ? 0.2468 0.1676 0.1864 0.0136  -0.0816 0.0226  446 HOH A O   
2301 O  O   . HOH G .   ? 0.2038 0.2134 0.2333 -0.0096 0.0000  -0.0324 447 HOH A O   
2302 O  O   . HOH G .   ? 0.2115 0.1580 0.1828 -0.0034 -0.0097 0.0093  448 HOH A O   
2303 O  O   . HOH G .   ? 0.2759 0.2576 0.1952 0.0210  0.0159  -0.0288 449 HOH A O   
2304 O  O   . HOH G .   ? 0.2761 0.1491 0.2982 -0.0126 0.0854  0.0013  450 HOH A O   
2305 O  O   . HOH G .   ? 0.2333 0.2495 0.2633 0.0254  -0.0986 -0.0007 451 HOH A O   
2306 O  O   . HOH G .   ? 0.1819 0.2698 0.3267 0.0680  -0.0693 -0.0665 452 HOH A O   
2307 O  O   . HOH G .   ? 0.1738 0.2311 0.1659 0.0307  0.0059  -0.0310 453 HOH A O   
2308 O  O   . HOH G .   ? 0.2565 0.1885 0.2047 0.0313  -0.0130 0.0273  454 HOH A O   
2309 O  O   . HOH G .   ? 0.1912 0.1925 0.2394 0.0115  0.0035  -0.0185 455 HOH A O   
2310 O  O   . HOH G .   ? 0.3045 0.2250 0.1659 -0.0208 -0.0243 0.0196  456 HOH A O   
2311 O  O   . HOH G .   ? 0.2213 0.2074 0.2544 -0.0153 -0.0175 0.0077  457 HOH A O   
2312 O  O   . HOH G .   ? 0.2099 0.1535 0.2333 0.0265  -0.0135 -0.0331 458 HOH A O   
2313 O  O   . HOH G .   ? 0.2653 0.1837 0.2592 0.0320  -0.0196 -0.0285 459 HOH A O   
2314 O  O   . HOH G .   ? 0.2040 0.2551 0.1864 -0.0209 0.0057  -0.0511 460 HOH A O   
2315 O  O   . HOH G .   ? 0.1764 0.1914 0.2002 0.0063  -0.0304 0.0031  461 HOH A O   
2316 O  O   . HOH G .   ? 0.2055 0.1753 0.2037 -0.0124 -0.0361 -0.0027 462 HOH A O   
2317 O  O   . HOH G .   ? 0.2842 0.2142 0.1879 0.0299  -0.0156 0.0331  463 HOH A O   
2318 O  O   . HOH G .   ? 0.1947 0.2242 0.2423 0.0130  -0.0031 0.0027  464 HOH A O   
2319 O  O   . HOH G .   ? 0.2644 0.2193 0.2108 0.0197  -0.0593 -0.0200 465 HOH A O   
2320 O  O   . HOH G .   ? 0.2271 0.2019 0.1573 0.0244  -0.0160 -0.0181 466 HOH A O   
2321 O  O   . HOH G .   ? 0.2479 0.1239 0.2107 0.0164  -0.0566 -0.0115 467 HOH A O   
2322 O  O   . HOH G .   ? 0.4564 0.1831 0.2257 0.0498  -0.0516 0.0410  468 HOH A O   
2323 O  O   . HOH G .   ? 0.2397 0.2876 0.2666 0.0186  -0.0093 0.0118  469 HOH A O   
2324 O  O   . HOH G .   ? 0.2569 0.2408 0.2526 0.0000  -0.0080 0.0472  470 HOH A O   
2325 O  O   . HOH G .   ? 0.1492 0.3452 0.3217 0.0329  -0.0007 0.0929  471 HOH A O   
2326 O  O   . HOH G .   ? 0.2265 0.1925 0.2662 -0.0255 -0.0333 0.0077  472 HOH A O   
2327 O  O   . HOH G .   ? 0.2322 0.3052 0.2662 -0.0384 0.0472  -0.0560 473 HOH A O   
2328 O  O   . HOH G .   ? 0.1867 0.2157 0.2303 0.0151  0.0114  0.0337  474 HOH A O   
2329 O  O   . HOH G .   ? 0.3594 0.2211 0.2040 0.0759  0.0187  0.0328  475 HOH A O   
2330 O  O   . HOH G .   ? 0.3535 0.2928 0.2199 -0.0142 0.0671  -0.1000 476 HOH A O   
2331 O  O   . HOH G .   ? 0.2585 0.1754 0.2078 -0.0027 -0.0136 -0.0297 477 HOH A O   
2332 O  O   . HOH G .   ? 0.4016 0.2231 0.2833 0.0847  0.0513  0.0882  478 HOH A O   
2333 O  O   . HOH G .   ? 0.2351 0.1555 0.2468 -0.0272 -0.0342 -0.0073 479 HOH A O   
2334 O  O   . HOH G .   ? 0.2518 0.2354 0.2451 0.0593  0.0342  -0.0063 480 HOH A O   
2335 O  O   . HOH G .   ? 0.4979 0.2046 0.1846 -0.0766 -0.0049 0.0599  481 HOH A O   
2336 O  O   . HOH G .   ? 0.2996 0.2108 0.2702 0.0450  0.0384  0.0200  482 HOH A O   
2337 O  O   . HOH G .   ? 0.2175 0.2236 0.2529 0.0166  0.0019  -0.0406 483 HOH A O   
2338 O  O   . HOH G .   ? 0.3050 0.2560 0.2763 -0.0342 0.0427  -0.0546 484 HOH A O   
2339 O  O   . HOH G .   ? 0.7350 0.6804 0.3619 0.2010  -0.2612 0.0507  485 HOH A O   
2340 O  O   . HOH G .   ? 0.2619 0.1961 0.2680 -0.0124 -0.0142 -0.0241 486 HOH A O   
2341 O  O   . HOH G .   ? 0.2901 0.3131 0.2944 0.1106  -0.0737 -0.0299 487 HOH A O   
2342 O  O   . HOH G .   ? 0.2761 0.2365 0.2615 0.0604  0.0153  -0.0307 488 HOH A O   
2343 O  O   . HOH G .   ? 0.2444 0.2078 0.1738 -0.0063 -0.0113 -0.0172 489 HOH A O   
2344 O  O   . HOH G .   ? 0.2815 0.2705 0.1966 0.0463  0.0114  -0.0515 490 HOH A O   
2345 O  O   . HOH G .   ? 0.2185 0.2407 0.2034 0.0255  0.0340  -0.0126 491 HOH A O   
2346 O  O   . HOH G .   ? 0.2730 0.3352 0.2766 -0.1272 0.0077  -0.0527 492 HOH A O   
2347 O  O   . HOH G .   ? 0.2354 0.3643 0.2529 0.0425  0.0555  -0.0003 493 HOH A O   
2348 O  O   . HOH G .   ? 0.2748 0.2416 0.2897 0.0006  -0.0441 0.0763  494 HOH A O   
2349 O  O   . HOH G .   ? 0.2423 0.2211 0.2401 0.0456  -0.0060 0.0263  495 HOH A O   
2350 O  O   . HOH G .   ? 0.1455 0.3853 0.2282 0.0186  0.0273  0.0904  496 HOH A O   
2351 O  O   . HOH G .   ? 0.1704 0.2393 0.2890 0.0077  -0.0153 -0.0082 497 HOH A O   
2352 O  O   . HOH G .   ? 0.2311 0.2425 0.2018 -0.0171 0.0115  -0.0359 498 HOH A O   
2353 O  O   . HOH G .   ? 0.2675 0.4695 0.1622 0.0877  -0.0644 -0.0383 499 HOH A O   
2354 O  O   . HOH G .   ? 0.4584 0.2558 0.1645 0.0590  0.0126  0.0288  500 HOH A O   
2355 O  O   . HOH G .   ? 0.3601 0.2881 0.2056 0.1330  -0.0540 0.0346  501 HOH A O   
2356 O  O   . HOH G .   ? 0.2380 0.2646 0.3219 0.1133  -0.0087 0.0057  502 HOH A O   
2357 O  O   . HOH G .   ? 0.2709 0.3282 0.2168 0.0794  0.0570  0.0452  503 HOH A O   
2358 O  O   . HOH G .   ? 0.3269 0.2153 0.1961 -0.0710 0.0693  -0.0472 504 HOH A O   
2359 O  O   . HOH G .   ? 0.3088 0.3700 0.1485 -0.0454 -0.0176 -0.0183 505 HOH A O   
2360 O  O   . HOH G .   ? 0.2225 0.2763 0.2148 -0.0104 -0.0370 0.0030  506 HOH A O   
2361 O  O   . HOH G .   ? 0.2994 0.2038 0.2272 -0.0899 -0.0298 -0.0195 507 HOH A O   
2362 O  O   . HOH G .   ? 0.2928 0.2070 0.2657 -0.0041 -0.0777 -0.0333 508 HOH A O   
2363 O  O   . HOH G .   ? 0.1553 0.2861 0.3201 0.0614  0.0239  -0.0162 509 HOH A O   
2364 O  O   . HOH G .   ? 0.2459 0.2081 0.3082 -0.0291 0.0509  -0.0489 510 HOH A O   
2365 O  O   . HOH G .   ? 0.2723 0.3131 0.2897 -0.0428 0.0575  -0.0414 511 HOH A O   
2366 O  O   . HOH G .   ? 0.3088 0.1934 0.2436 -0.0443 0.0097  -0.0113 512 HOH A O   
2367 O  O   . HOH G .   ? 0.4614 0.2572 0.2594 0.0412  0.0706  -0.1098 513 HOH A O   
2368 O  O   . HOH G .   ? 0.4262 0.5008 0.4320 0.0988  0.2046  0.0979  514 HOH A O   
2369 O  O   . HOH G .   ? 0.3100 0.4309 0.1871 -0.0031 -0.0869 0.0553  515 HOH A O   
2370 O  O   . HOH G .   ? 0.3524 0.3650 0.2675 0.0560  -0.0533 -0.0601 516 HOH A O   
2371 O  O   . HOH G .   ? 0.2376 0.2768 0.2743 0.0230  -0.0494 0.1177  517 HOH A O   
2372 O  O   . HOH G .   ? 0.2574 0.2144 0.4298 0.0092  0.0115  -0.0785 518 HOH A O   
2373 O  O   . HOH G .   ? 0.2383 0.2813 0.2597 -0.0057 0.0324  -0.0573 519 HOH A O   
2374 O  O   . HOH G .   ? 0.2372 0.3255 0.3025 -0.0082 0.0878  0.0617  520 HOH A O   
2375 O  O   . HOH G .   ? 0.2498 0.3206 0.3359 -0.1062 -0.0156 -0.0662 521 HOH A O   
2376 O  O   . HOH G .   ? 0.3420 0.2500 0.2297 0.0467  0.0196  0.0412  522 HOH A O   
2377 O  O   . HOH G .   ? 0.2874 0.2967 0.1921 -0.0292 0.0031  0.0586  523 HOH A O   
2378 O  O   . HOH G .   ? 0.1937 0.4562 0.2664 0.0529  0.0295  0.0621  524 HOH A O   
2379 O  O   . HOH G .   ? 0.4444 0.2628 0.1596 0.0286  0.0248  0.0125  525 HOH A O   
2380 O  O   . HOH G .   ? 0.3490 0.5414 0.3303 -0.1322 0.0688  -0.0010 526 HOH A O   
2381 O  O   . HOH G .   ? 0.3621 0.3458 0.2644 -0.0458 -0.0082 0.0233  527 HOH A O   
2382 O  O   . HOH G .   ? 0.3610 0.2912 0.2182 -0.0634 -0.0038 -0.0059 528 HOH A O   
2383 O  O   . HOH G .   ? 0.3407 0.3659 0.2328 0.0208  -0.0474 0.0627  529 HOH A O   
2384 O  O   . HOH G .   ? 0.3467 0.4726 0.2558 -0.0683 0.0359  -0.2159 530 HOH A O   
2385 O  O   . HOH G .   ? 0.2483 0.8442 0.5296 0.0992  0.0780  -0.2442 531 HOH A O   
2386 O  O   . HOH G .   ? 0.2851 0.3151 0.2337 -0.0590 -0.0296 -0.0221 532 HOH A O   
2387 O  O   . HOH G .   ? 0.2910 0.2739 0.3472 0.0005  -0.0838 -0.0076 533 HOH A O   
2388 O  O   . HOH G .   ? 0.2113 0.3143 0.3971 -0.0392 0.0355  -0.1151 534 HOH A O   
2389 O  O   . HOH G .   ? 0.2243 0.3680 0.2416 -0.0759 -0.0277 0.0037  535 HOH A O   
2390 O  O   . HOH G .   ? 0.3064 0.3273 0.3021 -0.0335 0.0579  -0.0200 536 HOH A O   
2391 O  O   . HOH G .   ? 0.2350 0.2637 0.2989 -0.0416 -0.0597 -0.0187 537 HOH A O   
2392 O  O   . HOH G .   ? 0.2750 0.3298 0.3185 0.0623  0.0711  0.0662  538 HOH A O   
2393 O  O   . HOH G .   ? 0.3486 0.2260 0.1708 0.0850  -0.0590 -0.0252 539 HOH A O   
2394 O  O   . HOH G .   ? 0.2134 0.4083 0.2847 -0.0293 -0.0386 0.0947  540 HOH A O   
2395 O  O   . HOH G .   ? 0.2002 0.2444 0.2056 -0.0193 0.0024  0.0091  541 HOH A O   
2396 O  O   . HOH G .   ? 0.2397 0.4519 0.4185 0.0154  0.1376  0.0922  542 HOH A O   
2397 O  O   . HOH G .   ? 0.3402 0.1844 0.2820 0.0715  -0.0263 0.0040  543 HOH A O   
2398 O  O   . HOH G .   ? 0.3036 0.4406 0.4902 0.1729  -0.1494 -0.1536 544 HOH A O   
2399 O  O   . HOH G .   ? 0.4490 0.2772 0.6596 -0.0115 -0.1040 -0.1747 545 HOH A O   
2400 O  O   . HOH G .   ? 0.3138 0.2711 0.2865 -0.0326 -0.0785 -0.0410 546 HOH A O   
2401 O  O   . HOH G .   ? 0.2207 0.4156 0.6013 -0.1035 -0.0766 0.0120  547 HOH A O   
2402 O  O   . HOH G .   ? 0.2845 0.3431 0.2818 -0.0465 0.0252  -0.1186 548 HOH A O   
2403 O  O   . HOH G .   ? 0.4584 0.3659 0.3203 -0.0970 -0.1413 0.0917  549 HOH A O   
2404 O  O   . HOH G .   ? 0.2538 0.3037 0.3149 -0.0266 -0.0254 -0.0015 550 HOH A O   
2405 O  O   . HOH G .   ? 0.2551 0.2224 0.2411 0.0146  -0.0153 0.0412  551 HOH A O   
2406 O  O   . HOH G .   ? 0.3233 0.2380 0.4266 0.0081  0.0480  0.0588  552 HOH A O   
2407 O  O   . HOH G .   ? 0.3819 0.3474 0.5841 0.0864  -0.1128 0.0684  553 HOH A O   
2408 O  O   . HOH G .   ? 0.3257 0.3763 0.2432 0.0678  -0.0110 0.0579  554 HOH A O   
2409 O  O   . HOH G .   ? 0.2563 0.2585 0.1982 -0.0071 -0.0308 0.0421  555 HOH A O   
2410 O  O   . HOH G .   ? 0.2560 0.3962 0.2994 -0.0640 -0.0969 0.0076  556 HOH A O   
2411 O  O   . HOH G .   ? 0.1916 0.2225 0.2375 -0.0020 -0.0392 -0.0221 557 HOH A O   
2412 O  O   . HOH G .   ? 0.4068 0.3018 0.1613 -0.0252 0.0417  0.0243  558 HOH A O   
2413 O  O   . HOH G .   ? 0.3203 0.2271 0.2982 -0.0141 -0.0715 0.0020  559 HOH A O   
2414 O  O   . HOH G .   ? 0.2524 0.2680 0.3646 -0.0564 0.0000  -0.0419 560 HOH A O   
2415 O  O   . HOH G .   ? 0.1946 0.3546 0.3352 0.0210  -0.0024 0.0684  561 HOH A O   
2416 O  O   . HOH G .   ? 0.3512 0.2709 0.2476 -0.0109 -0.0460 0.1342  562 HOH A O   
2417 O  O   . HOH G .   ? 0.3176 0.2211 0.2533 -0.0146 -0.0612 0.0115  563 HOH A O   
2418 O  O   . HOH G .   ? 0.2633 0.4835 0.2308 -0.1729 0.0445  -0.0807 564 HOH A O   
2419 O  O   . HOH G .   ? 0.2811 0.1819 0.2673 -0.0031 -0.0225 0.0423  565 HOH A O   
2420 O  O   . HOH G .   ? 0.3239 0.2242 0.2847 -0.0082 -0.0494 -0.0183 566 HOH A O   
2421 O  O   . HOH G .   ? 0.2741 0.3352 0.2842 0.0531  0.0172  -0.0348 567 HOH A O   
2422 O  O   . HOH G .   ? 0.3989 0.3434 0.3686 0.0671  -0.1128 0.0276  568 HOH A O   
2423 O  O   . HOH G .   ? 0.3398 0.3156 0.2347 0.0449  0.0167  -0.0098 569 HOH A O   
2424 O  O   . HOH G .   ? 0.2479 0.2472 0.3307 -0.0430 -0.0414 0.0706  570 HOH A O   
2425 O  O   . HOH G .   ? 0.4259 0.3481 0.2718 -0.0856 0.0662  -0.1224 571 HOH A O   
2426 O  O   . HOH G .   ? 0.5504 0.3109 0.3215 -0.0606 0.0557  -0.0060 572 HOH A O   
2427 O  O   . HOH G .   ? 0.4555 0.2964 0.2820 0.0564  0.0929  0.0916  573 HOH A O   
2428 O  O   . HOH G .   ? 0.2772 0.2376 0.3190 0.0170  -0.0335 -0.0731 574 HOH A O   
2429 O  O   . HOH G .   ? 0.3048 0.3722 0.3093 0.1281  0.0390  -0.0326 575 HOH A O   
2430 O  O   . HOH G .   ? 0.1887 0.4230 0.3291 0.0313  0.0252  0.0098  576 HOH A O   
2431 O  O   . HOH G .   ? 0.1869 0.2953 0.3134 0.0152  0.0120  0.0027  577 HOH A O   
2432 O  O   . HOH G .   ? 0.3336 0.3104 0.2782 -0.0126 -0.0362 0.1053  578 HOH A O   
2433 O  O   . HOH G .   ? 0.2712 0.4397 0.2450 0.0318  -0.0666 0.0299  579 HOH A O   
2434 O  O   . HOH G .   ? 0.2736 0.3607 0.2698 -0.0873 0.0153  -0.0013 580 HOH A O   
2435 O  O   . HOH G .   ? 0.4271 0.4767 0.2326 0.0450  -0.0522 -0.0947 581 HOH A O   
2436 O  O   . HOH G .   ? 0.6517 0.4045 0.4614 -0.0863 -0.0315 -0.0966 582 HOH A O   
2437 O  O   . HOH G .   ? 0.3896 0.3072 0.3533 0.0511  -0.0233 0.0366  583 HOH A O   
2438 O  O   . HOH G .   ? 0.3740 0.2045 0.4099 -0.0467 0.0640  0.0243  584 HOH A O   
2439 O  O   . HOH G .   ? 0.1789 0.2799 0.3582 0.0357  -0.0151 -0.0015 585 HOH A O   
2440 O  O   . HOH G .   ? 0.2545 0.3443 0.3761 -0.0060 -0.0832 -0.0063 586 HOH A O   
2441 O  O   . HOH G .   ? 0.2597 0.3359 0.4566 0.0759  0.0208  0.0087  587 HOH A O   
2442 O  O   . HOH G .   ? 0.3594 0.2480 0.2462 -0.0368 -0.0439 0.0467  588 HOH A O   
2443 O  O   . HOH G .   ? 0.4004 0.3583 0.3300 -0.0842 -0.1111 0.0326  589 HOH A O   
2444 O  O   . HOH G .   ? 0.6481 0.2754 0.2585 -0.1341 -0.0308 0.0206  590 HOH A O   
2445 O  O   . HOH G .   ? 0.3278 0.1808 0.2784 -0.0252 0.0153  -0.0381 591 HOH A O   
2446 O  O   . HOH G .   ? 0.3197 0.5008 0.2592 -0.0124 -0.0313 0.0313  592 HOH A O   
2447 O  O   . HOH G .   ? 0.3984 0.3456 0.2894 0.0719  -0.0741 -0.0215 593 HOH A O   
2448 O  O   . HOH G .   ? 0.3531 0.3892 0.3291 0.0076  -0.0136 -0.1344 594 HOH A O   
2449 O  O   . HOH G .   ? 0.4456 0.5109 0.2944 -0.0247 0.0636  -0.0467 595 HOH A O   
2450 O  O   . HOH G .   ? 0.3328 0.3650 0.3418 0.0935  0.1203  -0.0151 596 HOH A O   
2451 O  O   . HOH G .   ? 0.2351 0.2017 0.4083 0.0244  0.0137  -0.0531 597 HOH A O   
2452 O  O   . HOH G .   ? 0.3000 0.4456 0.2998 -0.0310 0.0215  0.1500  598 HOH A O   
2453 O  O   . HOH G .   ? 0.3684 0.4546 0.5274 0.0970  0.1272  0.0015  599 HOH A O   
2454 O  O   . HOH G .   ? 0.3515 0.2903 0.2906 0.0790  -0.0922 0.0452  600 HOH A O   
2455 O  O   . HOH G .   ? 0.3786 0.3637 0.3203 0.1418  0.1307  0.1343  601 HOH A O   
2456 O  O   . HOH G .   ? 0.5274 0.3810 0.2818 -0.0038 0.0476  -0.0798 602 HOH A O   
2457 O  O   . HOH G .   ? 0.4359 0.2646 0.3959 -0.1808 0.0269  0.0043  603 HOH A O   
2458 O  O   . HOH G .   ? 0.3176 0.2278 0.5580 0.0728  0.1216  0.1054  604 HOH A O   
2459 O  O   . HOH G .   ? 0.3479 0.3596 0.2157 -0.0562 0.0006  0.0719  605 HOH A O   
2460 O  O   . HOH G .   ? 0.3551 0.4298 0.3125 0.0671  0.0482  0.0636  606 HOH A O   
2461 O  O   . HOH G .   ? 0.4345 0.2856 0.3273 0.0675  -0.0196 0.0280  607 HOH A O   
2462 O  O   . HOH G .   ? 0.5467 0.3059 0.5299 -0.0952 -0.0701 -0.1168 608 HOH A O   
2463 O  O   . HOH G .   ? 0.1507 0.3580 0.4271 -0.0081 -0.0155 0.0680  609 HOH A O   
2464 O  O   . HOH G .   ? 0.2390 0.2292 0.4032 -0.0114 -0.0364 0.0114  610 HOH A O   
2465 O  O   . HOH G .   ? 0.4350 0.3370 0.3686 -0.0697 0.0727  0.0296  611 HOH A O   
2466 O  O   . HOH G .   ? 0.5116 0.8719 0.2296 0.2100  -0.0487 0.0472  612 HOH A O   
2467 O  O   . HOH G .   ? 0.2791 0.4097 0.3318 0.0054  -0.0068 -0.0604 613 HOH A O   
2468 O  O   . HOH G .   ? 0.5288 0.4918 0.1817 -0.0555 0.0675  0.0780  614 HOH A O   
2469 O  O   . HOH G .   ? 0.4122 0.5123 0.2594 0.0206  0.0630  -0.0148 615 HOH A O   
2470 O  O   . HOH G .   ? 0.2624 0.3991 0.5504 0.0351  0.0142  -0.1518 616 HOH A O   
2471 O  O   . HOH G .   ? 0.3932 0.3783 0.1981 -0.0068 -0.0153 -0.0114 617 HOH A O   
2472 O  O   . HOH G .   ? 0.2610 0.3009 0.4462 -0.0688 -0.0195 0.0505  618 HOH A O   
2473 O  O   . HOH G .   ? 0.4541 0.2592 0.3840 -0.1013 0.0414  -0.0662 619 HOH A O   
2474 O  O   . HOH G .   ? 0.2874 0.2651 0.4560 0.0297  -0.0087 -0.0026 620 HOH A O   
2475 O  O   . HOH G .   ? 0.2978 0.3174 0.5551 0.0302  0.0255  0.0015  621 HOH A O   
2476 O  O   . HOH G .   ? 0.3434 0.3231 0.2524 -0.0155 0.0068  -0.0271 622 HOH A O   
2477 O  O   . HOH G .   ? 0.4029 0.3619 0.3598 0.0487  -0.0346 0.0027  623 HOH A O   
2478 O  O   . HOH G .   ? 0.5655 0.3847 0.5145 0.1771  -0.0608 -0.1685 624 HOH A O   
2479 O  O   . HOH G .   ? 0.1066 0.6366 0.3740 0.1093  -0.0277 -0.2163 625 HOH A O   
2480 O  O   . HOH G .   ? 0.4442 0.3962 0.2025 0.1481  0.0097  -0.0929 626 HOH A O   
2481 O  O   . HOH G .   ? 0.3025 0.4079 0.2673 -0.0445 0.0597  -0.0623 627 HOH A O   
2482 O  O   . HOH G .   ? 0.2653 0.3876 0.2887 -0.0244 -0.0790 0.0126  628 HOH A O   
2483 O  O   . HOH G .   ? 0.2605 0.3521 0.4681 0.0151  -0.0012 0.0454  629 HOH A O   
2484 O  O   . HOH G .   ? 0.5296 0.3984 0.3860 0.0241  -0.0285 0.0445  630 HOH A O   
2485 O  O   . HOH G .   ? 0.6122 0.3754 0.4217 -0.1622 0.1036  0.0333  631 HOH A O   
2486 O  O   . HOH G .   ? 0.4519 0.2944 0.5008 -0.1582 0.0057  0.1239  632 HOH A O   
2487 O  O   . HOH G .   ? 0.3043 0.2454 0.3562 -0.0034 -0.0485 0.0575  633 HOH A O   
2488 O  O   . HOH G .   ? 0.4657 0.3176 0.5281 -0.1471 0.0020  -0.0916 634 HOH A O   
2489 O  O   . HOH G .   ? 0.4681 0.3287 0.4697 -0.0741 -0.0093 0.1588  635 HOH A O   
2490 O  O   . HOH G .   ? 0.5004 0.5435 0.2734 0.0592  -0.0772 0.0364  636 HOH A O   
2491 O  O   . HOH G .   ? 0.3199 0.4284 0.4818 -0.0416 0.0728  -0.0701 637 HOH A O   
2492 O  O   . HOH G .   ? 1.4722 0.6506 0.7019 -0.3282 -0.0126 -0.1326 638 HOH A O   
2493 O  O   . HOH G .   ? 0.4984 0.4038 0.6207 0.0511  0.1262  -0.0399 639 HOH A O   
2494 O  O   . HOH G .   ? 0.5202 0.4413 0.2876 -0.0115 -0.0281 -0.1439 640 HOH A O   
2495 O  O   . HOH G .   ? 0.3226 0.6194 0.3905 -0.0434 0.0474  -0.2100 641 HOH A O   
2496 O  O   . HOH G .   ? 0.2865 0.3355 0.3564 0.0054  0.0755  0.0403  642 HOH A O   
2497 O  O   . HOH G .   ? 0.3907 0.4264 0.3203 -0.0635 -0.0121 0.1271  643 HOH A O   
2498 O  O   . HOH G .   ? 0.4616 0.6133 0.2560 0.0068  0.0500  -0.0046 644 HOH A O   
2499 O  O   . HOH G .   ? 0.4038 0.4329 0.3474 -0.0135 -0.1567 -0.0057 645 HOH A O   
2500 O  O   . HOH G .   ? 0.2633 0.3589 0.2680 0.0885  0.0763  -0.0206 646 HOH A O   
2501 O  O   . HOH G .   ? 0.4185 0.3822 0.3865 0.0266  -0.1714 0.0615  647 HOH A O   
2502 O  O   . HOH G .   ? 0.5000 0.5410 0.4591 0.1942  0.1686  0.2298  648 HOH A O   
2503 O  O   . HOH G .   ? 0.4571 0.4332 0.3795 0.0237  -0.0843 0.1542  649 HOH A O   
2504 O  O   . HOH G .   ? 0.3486 0.5468 0.4481 0.1001  0.1579  0.0153  650 HOH A O   
2505 O  O   . HOH G .   ? 0.4948 0.2494 0.2204 0.0881  -0.0397 0.0511  651 HOH A O   
2506 O  O   . HOH G .   ? 0.2606 0.5594 0.3280 -0.0505 -0.0412 -0.0241 652 HOH A O   
2507 O  O   . HOH G .   ? 0.4201 0.3467 0.4696 -0.0124 -0.0944 0.0577  653 HOH A O   
2508 O  O   . HOH G .   ? 0.2784 0.3855 0.4690 -0.0816 -0.1669 0.0789  654 HOH A O   
2509 O  O   . HOH G .   ? 0.5641 0.5885 0.4241 -0.1860 -0.1934 0.1523  655 HOH A O   
2510 O  O   . HOH G .   ? 1.0183 0.5536 0.8639 0.1467  -0.1476 0.0019  656 HOH A O   
2511 O  O   . HOH G .   ? 0.6674 0.3774 0.3145 0.1508  0.0296  0.0693  657 HOH A O   
2512 O  O   . HOH G .   ? 0.3894 0.5576 0.5174 0.1500  0.0046  0.0432  658 HOH A O   
2513 O  O   . HOH G .   ? 0.4503 0.3427 0.2761 0.0656  -0.0427 0.0662  659 HOH A O   
2514 O  O   . HOH G .   ? 0.3510 0.2863 0.4715 -0.0346 -0.0505 -0.0097 660 HOH A O   
2515 O  O   . HOH G .   ? 0.2493 0.3522 0.5820 0.0460  0.0151  0.1773  661 HOH A O   
2516 O  O   . HOH G .   ? 0.4210 0.4386 0.4083 0.2108  0.1809  0.1044  662 HOH A O   
2517 O  O   . HOH G .   ? 0.3321 0.5457 0.5508 0.3528  -0.1010 -0.0160 663 HOH A O   
2518 O  O   . HOH G .   ? 0.6413 0.3973 0.2994 0.0825  -0.0766 -0.1691 664 HOH A O   
2519 O  O   . HOH G .   ? 0.3479 0.3650 0.5546 0.0293  0.0674  -0.0183 665 HOH A O   
2520 O  O   . HOH G .   ? 0.4305 0.2267 0.5485 0.0557  0.0093  0.0230  666 HOH A O   
2521 O  O   . HOH G .   ? 0.4174 0.2878 0.3012 -0.0082 -0.0006 -0.0077 667 HOH A O   
2522 O  O   . HOH G .   ? 0.6207 0.3086 0.3239 0.1032  0.1673  0.1413  668 HOH A O   
2523 O  O   . HOH G .   ? 0.2013 0.5116 0.5540 -0.0313 0.0759  0.0427  669 HOH A O   
2524 O  O   . HOH G .   ? 0.4023 0.3930 0.3165 -0.0878 0.0474  -0.0688 670 HOH A O   
2525 O  O   . HOH G .   ? 0.6402 0.3327 0.5109 0.1115  0.0419  0.1369  671 HOH A O   
2526 O  O   . HOH G .   ? 0.3824 0.2443 0.4025 0.0141  -0.0037 0.0348  672 HOH A O   
2527 O  O   . HOH G .   ? 0.4909 0.2939 0.4875 0.0051  0.0333  0.0825  673 HOH A O   
2528 O  O   . HOH G .   ? 0.3235 0.5968 0.3260 -0.0522 0.0474  0.1932  674 HOH A O   
2529 O  O   . HOH G .   ? 0.4984 0.3476 0.5256 0.0293  -0.0549 -0.0768 675 HOH A O   
2530 O  O   . HOH G .   ? 0.5515 0.2515 0.2639 0.0252  -0.0082 0.0746  676 HOH A O   
2531 O  O   . HOH G .   ? 0.3359 0.3860 0.8919 -0.1580 -0.0807 0.0926  677 HOH A O   
2532 O  O   . HOH G .   ? 0.3601 0.3217 0.5065 -0.0342 -0.0093 -0.1402 678 HOH A O   
2533 O  O   . HOH G .   ? 0.3661 0.4666 0.5949 -0.1597 -0.0208 0.0315  679 HOH A O   
2534 O  O   . HOH G .   ? 0.3718 0.3795 0.5414 -0.0037 0.0864  0.0860  680 HOH A O   
2535 O  O   . HOH G .   ? 0.3745 0.4068 0.5695 0.0340  0.0498  0.0071  681 HOH A O   
2536 O  O   . HOH G .   ? 0.2644 0.5310 0.5224 0.0285  -0.1142 0.0665  682 HOH A O   
2537 O  O   . HOH G .   ? 0.5388 0.3476 0.4648 0.1044  -0.1448 -0.1000 683 HOH A O   
2538 O  O   . HOH G .   ? 0.2666 0.5889 0.3718 -0.0728 -0.0746 0.0296  684 HOH A O   
2539 O  O   . HOH G .   ? 0.3201 0.4365 0.5939 -0.0428 -0.0027 0.1019  685 HOH A O   
2540 O  O   . HOH G .   ? 0.4645 0.5163 0.5385 0.1447  -0.1402 -0.1062 686 HOH A O   
2541 O  O   . HOH G .   ? 0.1817 0.5274 0.4000 -0.0315 0.0082  0.0463  687 HOH A O   
2542 O  O   . HOH G .   ? 0.2669 0.3894 0.3804 -0.0390 0.0674  -0.0019 688 HOH A O   
2543 O  O   . HOH G .   ? 0.4889 0.5034 0.4460 -0.0913 0.1194  0.1542  689 HOH A O   
2544 O  O   . HOH G .   ? 0.5120 0.3975 0.4532 0.0662  0.1298  0.0185  690 HOH A O   
2545 O  O   . HOH G .   ? 0.4559 0.1997 0.4731 -0.0233 -0.0653 -0.0683 691 HOH A O   
2546 O  O   . HOH G .   ? 0.4569 0.3817 0.3885 -0.0114 0.2158  -0.0403 692 HOH A O   
2547 O  O   . HOH G .   ? 0.2759 0.4124 0.2378 0.0441  -0.0333 -0.0619 693 HOH A O   
2548 O  O   . HOH G .   ? 0.4469 0.3052 0.4171 0.0489  -0.0373 -0.0434 694 HOH A O   
2549 O  O   . HOH G .   ? 0.3865 0.4419 0.3233 -0.0049 0.0487  -0.0496 695 HOH A O   
2550 O  O   . HOH G .   ? 0.3416 0.4124 0.3765 0.0568  0.0573  0.0723  696 HOH A O   
2551 O  O   . HOH G .   ? 0.3449 0.3440 0.5820 0.0259  0.0313  0.0264  697 HOH A O   
2552 O  O   . HOH G .   ? 0.3989 0.4548 0.2899 0.0153  -0.0487 0.1500  698 HOH A O   
2553 O  O   . HOH G .   ? 0.4749 0.5145 0.1862 -0.0683 0.0527  0.0310  699 HOH A O   
2554 O  O   . HOH G .   ? 0.3018 0.3657 0.6039 -0.0859 0.1450  0.0925  700 HOH A O   
2555 O  O   . HOH G .   ? 0.3134 0.4519 0.6003 -0.1208 -0.0147 -0.1562 701 HOH A O   
2556 O  O   . HOH G .   ? 0.4282 0.3968 0.4510 -0.1466 -0.0507 0.0237  702 HOH A O   
2557 O  O   . HOH G .   ? 0.3278 0.4022 0.4794 -0.0216 0.0687  -0.0141 703 HOH A O   
2558 O  O   . HOH G .   ? 0.4359 0.3224 0.4415 0.0406  0.0156  -0.1448 704 HOH A O   
2559 O  O   . HOH G .   ? 0.6129 0.2662 0.3217 -0.0608 0.1172  0.0723  705 HOH A O   
2560 O  O   . HOH G .   ? 0.5874 0.4736 0.3025 -0.0038 0.0498  0.0027  706 HOH A O   
2561 O  O   . HOH G .   ? 0.6794 0.3659 0.3068 -0.0379 0.0216  -0.0948 707 HOH A O   
2562 O  O   . HOH G .   ? 0.8234 0.5788 0.2603 0.0806  0.1216  -0.0248 708 HOH A O   
2563 O  O   . HOH G .   ? 0.3018 0.5274 0.5626 -0.0419 0.1233  -0.0904 709 HOH A O   
2564 O  O   . HOH G .   ? 0.4620 0.5070 0.2421 0.2260  -0.0450 -0.0318 710 HOH A O   
2565 O  O   . HOH G .   ? 0.3194 0.2978 0.4648 0.1076  0.0007  0.0210  711 HOH A O   
2566 O  O   . HOH G .   ? 0.7357 0.4212 0.3558 -0.0109 -0.1684 -0.0553 712 HOH A O   
2567 O  O   . HOH G .   ? 0.5418 0.3806 0.5604 0.0939  0.0768  -0.0269 713 HOH A O   
2568 O  O   . HOH G .   ? 0.1625 0.3438 0.2757 -0.0399 -0.0137 0.0027  714 HOH A O   
2569 O  O   . HOH G .   ? 0.1941 0.3303 0.3549 -0.0430 -0.0141 -0.0037 715 HOH A O   
2570 O  O   . HOH G .   ? 0.1835 0.2303 0.3145 -0.0623 -0.0331 0.0590  716 HOH A O   
2571 O  O   . HOH G .   ? 0.2213 0.9682 0.7649 -0.2858 -0.0634 0.4460  717 HOH A O   
2572 O  O   . HOH G .   ? 0.3984 0.3059 0.3666 0.0236  0.1124  0.0794  718 HOH A O   
2573 O  O   . HOH G .   ? 0.8234 0.4235 0.3704 0.0366  -0.2558 -0.1145 719 HOH A O   
2574 O  O   . HOH G .   ? 0.2646 0.3519 0.2554 -0.0504 0.0346  0.0627  720 HOH A O   
2575 O  O   . HOH G .   ? 0.3916 0.4156 0.2957 0.0026  0.0087  0.0059  721 HOH A O   
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 BCN 1   302 1   BCN BCN A . 
D 4 DMS 1   303 1   DMS DMS A . 
E 4 DMS 1   304 2   DMS DMS A . 
F 5 KR5 1   305 1   KR5 KR5 A . 
G 6 HOH 1   401 1   HOH HOH A . 
G 6 HOH 2   402 2   HOH HOH A . 
G 6 HOH 3   403 3   HOH HOH A . 
G 6 HOH 4   404 4   HOH HOH A . 
G 6 HOH 5   405 5   HOH HOH A . 
G 6 HOH 6   406 6   HOH HOH A . 
G 6 HOH 7   407 7   HOH HOH A . 
G 6 HOH 8   408 8   HOH HOH A . 
G 6 HOH 9   409 9   HOH HOH A . 
G 6 HOH 10  410 10  HOH HOH A . 
G 6 HOH 11  411 11  HOH HOH A . 
G 6 HOH 12  412 12  HOH HOH A . 
G 6 HOH 13  413 13  HOH HOH A . 
G 6 HOH 14  414 14  HOH HOH A . 
G 6 HOH 15  415 15  HOH HOH A . 
G 6 HOH 16  416 16  HOH HOH A . 
G 6 HOH 17  417 17  HOH HOH A . 
G 6 HOH 18  418 18  HOH HOH A . 
G 6 HOH 19  419 19  HOH HOH A . 
G 6 HOH 20  420 20  HOH HOH A . 
G 6 HOH 21  421 21  HOH HOH A . 
G 6 HOH 22  422 22  HOH HOH A . 
G 6 HOH 23  423 23  HOH HOH A . 
G 6 HOH 24  424 24  HOH HOH A . 
G 6 HOH 25  425 25  HOH HOH A . 
G 6 HOH 26  426 26  HOH HOH A . 
G 6 HOH 27  427 27  HOH HOH A . 
G 6 HOH 28  428 28  HOH HOH A . 
G 6 HOH 29  429 29  HOH HOH A . 
G 6 HOH 30  430 30  HOH HOH A . 
G 6 HOH 31  431 31  HOH HOH A . 
G 6 HOH 32  432 32  HOH HOH A . 
G 6 HOH 33  433 33  HOH HOH A . 
G 6 HOH 34  434 34  HOH HOH A . 
G 6 HOH 35  435 35  HOH HOH A . 
G 6 HOH 36  436 36  HOH HOH A . 
G 6 HOH 37  437 37  HOH HOH A . 
G 6 HOH 38  438 38  HOH HOH A . 
G 6 HOH 39  439 39  HOH HOH A . 
G 6 HOH 40  440 40  HOH HOH A . 
G 6 HOH 41  441 41  HOH HOH A . 
G 6 HOH 42  442 42  HOH HOH A . 
G 6 HOH 43  443 43  HOH HOH A . 
G 6 HOH 44  444 44  HOH HOH A . 
G 6 HOH 45  445 45  HOH HOH A . 
G 6 HOH 46  446 46  HOH HOH A . 
G 6 HOH 47  447 47  HOH HOH A . 
G 6 HOH 48  448 48  HOH HOH A . 
G 6 HOH 49  449 49  HOH HOH A . 
G 6 HOH 50  450 50  HOH HOH A . 
G 6 HOH 51  451 51  HOH HOH A . 
G 6 HOH 52  452 52  HOH HOH A . 
G 6 HOH 53  453 53  HOH HOH A . 
G 6 HOH 54  454 54  HOH HOH A . 
G 6 HOH 55  455 55  HOH HOH A . 
G 6 HOH 56  456 56  HOH HOH A . 
G 6 HOH 57  457 57  HOH HOH A . 
G 6 HOH 58  458 58  HOH HOH A . 
G 6 HOH 59  459 59  HOH HOH A . 
G 6 HOH 60  460 60  HOH HOH A . 
G 6 HOH 61  461 61  HOH HOH A . 
G 6 HOH 62  462 62  HOH HOH A . 
G 6 HOH 63  463 63  HOH HOH A . 
G 6 HOH 64  464 64  HOH HOH A . 
G 6 HOH 65  465 65  HOH HOH A . 
G 6 HOH 66  466 66  HOH HOH A . 
G 6 HOH 67  467 67  HOH HOH A . 
G 6 HOH 68  468 68  HOH HOH A . 
G 6 HOH 69  469 69  HOH HOH A . 
G 6 HOH 70  470 70  HOH HOH A . 
G 6 HOH 71  471 71  HOH HOH A . 
G 6 HOH 72  472 72  HOH HOH A . 
G 6 HOH 73  473 73  HOH HOH A . 
G 6 HOH 74  474 74  HOH HOH A . 
G 6 HOH 75  475 75  HOH HOH A . 
G 6 HOH 76  476 76  HOH HOH A . 
G 6 HOH 77  477 77  HOH HOH A . 
G 6 HOH 78  478 78  HOH HOH A . 
G 6 HOH 79  479 79  HOH HOH A . 
G 6 HOH 80  480 80  HOH HOH A . 
G 6 HOH 81  481 81  HOH HOH A . 
G 6 HOH 82  482 82  HOH HOH A . 
G 6 HOH 83  483 83  HOH HOH A . 
G 6 HOH 84  484 84  HOH HOH A . 
G 6 HOH 85  485 85  HOH HOH A . 
G 6 HOH 86  486 86  HOH HOH A . 
G 6 HOH 87  487 87  HOH HOH A . 
G 6 HOH 88  488 88  HOH HOH A . 
G 6 HOH 89  489 89  HOH HOH A . 
G 6 HOH 90  490 90  HOH HOH A . 
G 6 HOH 91  491 91  HOH HOH A . 
G 6 HOH 92  492 92  HOH HOH A . 
G 6 HOH 93  493 93  HOH HOH A . 
G 6 HOH 94  494 94  HOH HOH A . 
G 6 HOH 95  495 95  HOH HOH A . 
G 6 HOH 96  496 96  HOH HOH A . 
G 6 HOH 97  497 97  HOH HOH A . 
G 6 HOH 98  498 98  HOH HOH A . 
G 6 HOH 99  499 99  HOH HOH A . 
G 6 HOH 100 500 100 HOH HOH A . 
G 6 HOH 101 501 101 HOH HOH A . 
G 6 HOH 102 502 102 HOH HOH A . 
G 6 HOH 103 503 103 HOH HOH A . 
G 6 HOH 104 504 104 HOH HOH A . 
G 6 HOH 105 505 105 HOH HOH A . 
G 6 HOH 106 506 106 HOH HOH A . 
G 6 HOH 107 507 107 HOH HOH A . 
G 6 HOH 108 508 108 HOH HOH A . 
G 6 HOH 109 509 109 HOH HOH A . 
G 6 HOH 110 510 110 HOH HOH A . 
G 6 HOH 111 511 111 HOH HOH A . 
G 6 HOH 112 512 112 HOH HOH A . 
G 6 HOH 113 513 113 HOH HOH A . 
G 6 HOH 114 514 114 HOH HOH A . 
G 6 HOH 115 515 115 HOH HOH A . 
G 6 HOH 116 516 116 HOH HOH A . 
G 6 HOH 117 517 117 HOH HOH A . 
G 6 HOH 118 518 118 HOH HOH A . 
G 6 HOH 119 519 119 HOH HOH A . 
G 6 HOH 120 520 120 HOH HOH A . 
G 6 HOH 121 521 121 HOH HOH A . 
G 6 HOH 122 522 122 HOH HOH A . 
G 6 HOH 123 523 123 HOH HOH A . 
G 6 HOH 124 524 124 HOH HOH A . 
G 6 HOH 125 525 125 HOH HOH A . 
G 6 HOH 126 526 126 HOH HOH A . 
G 6 HOH 127 527 127 HOH HOH A . 
G 6 HOH 128 528 128 HOH HOH A . 
G 6 HOH 129 529 129 HOH HOH A . 
G 6 HOH 130 530 130 HOH HOH A . 
G 6 HOH 131 531 131 HOH HOH A . 
G 6 HOH 132 532 132 HOH HOH A . 
G 6 HOH 133 533 133 HOH HOH A . 
G 6 HOH 134 534 134 HOH HOH A . 
G 6 HOH 135 535 135 HOH HOH A . 
G 6 HOH 136 536 136 HOH HOH A . 
G 6 HOH 137 537 137 HOH HOH A . 
G 6 HOH 138 538 138 HOH HOH A . 
G 6 HOH 139 539 139 HOH HOH A . 
G 6 HOH 140 540 140 HOH HOH A . 
G 6 HOH 141 541 141 HOH HOH A . 
G 6 HOH 142 542 142 HOH HOH A . 
G 6 HOH 143 543 143 HOH HOH A . 
G 6 HOH 144 544 144 HOH HOH A . 
G 6 HOH 145 545 145 HOH HOH A . 
G 6 HOH 146 546 146 HOH HOH A . 
G 6 HOH 147 547 147 HOH HOH A . 
G 6 HOH 148 548 148 HOH HOH A . 
G 6 HOH 149 549 149 HOH HOH A . 
G 6 HOH 150 550 150 HOH HOH A . 
G 6 HOH 151 551 151 HOH HOH A . 
G 6 HOH 152 552 152 HOH HOH A . 
G 6 HOH 153 553 153 HOH HOH A . 
G 6 HOH 154 554 154 HOH HOH A . 
G 6 HOH 155 555 155 HOH HOH A . 
G 6 HOH 156 556 156 HOH HOH A . 
G 6 HOH 157 557 157 HOH HOH A . 
G 6 HOH 158 558 158 HOH HOH A . 
G 6 HOH 159 559 159 HOH HOH A . 
G 6 HOH 160 560 160 HOH HOH A . 
G 6 HOH 161 561 161 HOH HOH A . 
G 6 HOH 162 562 162 HOH HOH A . 
G 6 HOH 163 563 163 HOH HOH A . 
G 6 HOH 164 564 164 HOH HOH A . 
G 6 HOH 165 565 165 HOH HOH A . 
G 6 HOH 166 566 166 HOH HOH A . 
G 6 HOH 167 567 167 HOH HOH A . 
G 6 HOH 168 568 168 HOH HOH A . 
G 6 HOH 169 569 169 HOH HOH A . 
G 6 HOH 170 570 170 HOH HOH A . 
G 6 HOH 171 571 171 HOH HOH A . 
G 6 HOH 172 572 172 HOH HOH A . 
G 6 HOH 173 573 173 HOH HOH A . 
G 6 HOH 174 574 174 HOH HOH A . 
G 6 HOH 175 575 175 HOH HOH A . 
G 6 HOH 176 576 176 HOH HOH A . 
G 6 HOH 177 577 177 HOH HOH A . 
G 6 HOH 178 578 178 HOH HOH A . 
G 6 HOH 179 579 179 HOH HOH A . 
G 6 HOH 180 580 180 HOH HOH A . 
G 6 HOH 181 581 181 HOH HOH A . 
G 6 HOH 182 582 182 HOH HOH A . 
G 6 HOH 183 583 183 HOH HOH A . 
G 6 HOH 184 584 184 HOH HOH A . 
G 6 HOH 185 585 185 HOH HOH A . 
G 6 HOH 186 586 186 HOH HOH A . 
G 6 HOH 187 587 187 HOH HOH A . 
G 6 HOH 188 588 188 HOH HOH A . 
G 6 HOH 189 589 189 HOH HOH A . 
G 6 HOH 190 590 190 HOH HOH A . 
G 6 HOH 191 591 191 HOH HOH A . 
G 6 HOH 192 592 192 HOH HOH A . 
G 6 HOH 193 593 193 HOH HOH A . 
G 6 HOH 194 594 194 HOH HOH A . 
G 6 HOH 195 595 195 HOH HOH A . 
G 6 HOH 196 596 196 HOH HOH A . 
G 6 HOH 197 597 197 HOH HOH A . 
G 6 HOH 198 598 198 HOH HOH A . 
G 6 HOH 199 599 199 HOH HOH A . 
G 6 HOH 200 600 200 HOH HOH A . 
G 6 HOH 201 601 201 HOH HOH A . 
G 6 HOH 202 602 202 HOH HOH A . 
G 6 HOH 203 603 203 HOH HOH A . 
G 6 HOH 204 604 204 HOH HOH A . 
G 6 HOH 205 605 205 HOH HOH A . 
G 6 HOH 206 606 206 HOH HOH A . 
G 6 HOH 207 607 207 HOH HOH A . 
G 6 HOH 208 608 208 HOH HOH A . 
G 6 HOH 209 609 209 HOH HOH A . 
G 6 HOH 210 610 210 HOH HOH A . 
G 6 HOH 211 611 211 HOH HOH A . 
G 6 HOH 212 612 212 HOH HOH A . 
G 6 HOH 213 613 213 HOH HOH A . 
G 6 HOH 214 614 214 HOH HOH A . 
G 6 HOH 215 615 215 HOH HOH A . 
G 6 HOH 216 616 216 HOH HOH A . 
G 6 HOH 217 617 217 HOH HOH A . 
G 6 HOH 218 618 218 HOH HOH A . 
G 6 HOH 219 619 219 HOH HOH A . 
G 6 HOH 220 620 220 HOH HOH A . 
G 6 HOH 221 621 221 HOH HOH A . 
G 6 HOH 222 622 222 HOH HOH A . 
G 6 HOH 223 623 223 HOH HOH A . 
G 6 HOH 224 624 224 HOH HOH A . 
G 6 HOH 225 625 225 HOH HOH A . 
G 6 HOH 226 626 226 HOH HOH A . 
G 6 HOH 227 627 227 HOH HOH A . 
G 6 HOH 228 628 228 HOH HOH A . 
G 6 HOH 229 629 229 HOH HOH A . 
G 6 HOH 230 630 230 HOH HOH A . 
G 6 HOH 231 631 231 HOH HOH A . 
G 6 HOH 232 632 232 HOH HOH A . 
G 6 HOH 233 633 233 HOH HOH A . 
G 6 HOH 234 634 234 HOH HOH A . 
G 6 HOH 235 635 235 HOH HOH A . 
G 6 HOH 236 636 236 HOH HOH A . 
G 6 HOH 237 637 237 HOH HOH A . 
G 6 HOH 238 638 238 HOH HOH A . 
G 6 HOH 239 639 239 HOH HOH A . 
G 6 HOH 240 640 240 HOH HOH A . 
G 6 HOH 241 641 241 HOH HOH A . 
G 6 HOH 242 642 242 HOH HOH A . 
G 6 HOH 243 643 243 HOH HOH A . 
G 6 HOH 244 644 244 HOH HOH A . 
G 6 HOH 245 645 245 HOH HOH A . 
G 6 HOH 246 646 246 HOH HOH A . 
G 6 HOH 247 647 247 HOH HOH A . 
G 6 HOH 248 648 248 HOH HOH A . 
G 6 HOH 249 649 249 HOH HOH A . 
G 6 HOH 250 650 250 HOH HOH A . 
G 6 HOH 251 651 251 HOH HOH A . 
G 6 HOH 252 652 252 HOH HOH A . 
G 6 HOH 253 653 253 HOH HOH A . 
G 6 HOH 254 654 254 HOH HOH A . 
G 6 HOH 255 655 255 HOH HOH A . 
G 6 HOH 256 656 256 HOH HOH A . 
G 6 HOH 257 657 257 HOH HOH A . 
G 6 HOH 258 658 258 HOH HOH A . 
G 6 HOH 259 659 259 HOH HOH A . 
G 6 HOH 260 660 260 HOH HOH A . 
G 6 HOH 261 661 261 HOH HOH A . 
G 6 HOH 262 662 262 HOH HOH A . 
G 6 HOH 263 663 263 HOH HOH A . 
G 6 HOH 264 664 264 HOH HOH A . 
G 6 HOH 265 665 265 HOH HOH A . 
G 6 HOH 266 666 266 HOH HOH A . 
G 6 HOH 267 667 267 HOH HOH A . 
G 6 HOH 268 668 268 HOH HOH A . 
G 6 HOH 269 669 269 HOH HOH A . 
G 6 HOH 270 670 270 HOH HOH A . 
G 6 HOH 271 671 271 HOH HOH A . 
G 6 HOH 272 672 272 HOH HOH A . 
G 6 HOH 273 673 273 HOH HOH A . 
G 6 HOH 274 674 274 HOH HOH A . 
G 6 HOH 275 675 275 HOH HOH A . 
G 6 HOH 276 676 276 HOH HOH A . 
G 6 HOH 277 677 277 HOH HOH A . 
G 6 HOH 278 678 278 HOH HOH A . 
G 6 HOH 279 679 279 HOH HOH A . 
G 6 HOH 280 680 280 HOH HOH A . 
G 6 HOH 281 681 281 HOH HOH A . 
G 6 HOH 282 682 282 HOH HOH A . 
G 6 HOH 283 683 283 HOH HOH A . 
G 6 HOH 284 684 284 HOH HOH A . 
G 6 HOH 285 685 285 HOH HOH A . 
G 6 HOH 286 686 286 HOH HOH A . 
G 6 HOH 287 687 287 HOH HOH A . 
G 6 HOH 288 688 288 HOH HOH A . 
G 6 HOH 289 689 289 HOH HOH A . 
G 6 HOH 290 690 290 HOH HOH A . 
G 6 HOH 291 691 291 HOH HOH A . 
G 6 HOH 292 692 292 HOH HOH A . 
G 6 HOH 293 693 293 HOH HOH A . 
G 6 HOH 294 694 294 HOH HOH A . 
G 6 HOH 295 695 295 HOH HOH A . 
G 6 HOH 296 696 296 HOH HOH A . 
G 6 HOH 297 697 297 HOH HOH A . 
G 6 HOH 298 698 298 HOH HOH A . 
G 6 HOH 299 699 299 HOH HOH A . 
G 6 HOH 300 700 300 HOH HOH A . 
G 6 HOH 301 701 301 HOH HOH A . 
G 6 HOH 302 702 302 HOH HOH A . 
G 6 HOH 303 703 303 HOH HOH A . 
G 6 HOH 304 704 304 HOH HOH A . 
G 6 HOH 305 705 305 HOH HOH A . 
G 6 HOH 306 706 306 HOH HOH A . 
G 6 HOH 307 707 307 HOH HOH A . 
G 6 HOH 308 708 308 HOH HOH A . 
G 6 HOH 309 709 309 HOH HOH A . 
G 6 HOH 310 710 310 HOH HOH A . 
G 6 HOH 311 711 311 HOH HOH A . 
G 6 HOH 312 712 312 HOH HOH A . 
G 6 HOH 313 713 313 HOH HOH A . 
G 6 HOH 314 714 314 HOH HOH A . 
G 6 HOH 315 715 315 HOH HOH A . 
G 6 HOH 316 716 316 HOH HOH A . 
G 6 HOH 317 717 317 HOH HOH A . 
G 6 HOH 318 718 318 HOH HOH A . 
G 6 HOH 319 719 319 HOH HOH A . 
G 6 HOH 320 720 320 HOH HOH A . 
G 6 HOH 321 721 321 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.2 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.5 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.8  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? F KR5 .   ? A KR5 305 ? 1_555 110.4 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? F KR5 .   ? A KR5 305 ? 1_555 113.2 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? F KR5 .   ? A KR5 305 ? 1_555 118.2 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2014-11-26 
2 'Structure model' 1 1 2018-03-07 
3 'Structure model' 1 2 2023-09-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' Advisory                 
2 2 'Structure model' 'Data collection'        
3 3 'Structure model' Advisory                 
4 3 'Structure model' 'Data collection'        
5 3 'Structure model' 'Database references'    
6 3 'Structure model' 'Derived calculations'   
7 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  2 'Structure model' diffrn_source                 
2  2 'Structure model' pdbx_unobs_or_zero_occ_atoms  
3  3 'Structure model' chem_comp_atom                
4  3 'Structure model' chem_comp_bond                
5  3 'Structure model' database_2                    
6  3 'Structure model' pdbx_initial_refinement_model 
7  3 'Structure model' pdbx_struct_conn_angle        
8  3 'Structure model' pdbx_unobs_or_zero_occ_atoms  
9  3 'Structure model' struct_conn                   
10 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
2  3 'Structure model' '_database_2.pdbx_DOI'                        
3  3 'Structure model' '_database_2.pdbx_database_accession'         
4  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.value'               
17 3 'Structure model' '_struct_conn.pdbx_dist_value'                
18 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
19 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
20 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
21 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
22 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
23 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
24 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
25 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
26 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
27 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
28 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
29 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
30 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
31 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
SCALA       3.3.20 2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk 'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 2 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 3 
HKL-2000    .      ?               ?       ?                    ?                     'data collection' ? ?          ? 4 
XDS         .      ?               ?       ?                    ?                     'data reduction'  ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                     phasing           ? ?          ? 6 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            THR 
_pdbx_validate_rmsd_bond.auth_seq_id_1             125 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             127 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.610 
_pdbx_validate_rmsd_bond.bond_target_value         1.336 
_pdbx_validate_rmsd_bond.bond_deviation            0.274 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.023 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -140.19 54.59   
2 1 LYS A 76  ? ? -116.50 -84.63  
3 1 GLU A 106 ? ? -93.31  -60.23  
4 1 LYS A 111 ? ? 74.98   -2.57   
5 1 PHE A 176 ? ? -153.77 72.79   
6 1 ASN A 244 ? ? -92.41  45.61   
7 1 LYS A 252 ? A 50.75   -138.29 
8 1 LYS A 252 ? B 57.03   -137.98 
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   A 
_pdbx_validate_polymer_linkage.auth_comp_id_1   THR 
_pdbx_validate_polymer_linkage.auth_seq_id_1    125 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   A 
_pdbx_validate_polymer_linkage.auth_comp_id_2   LYS 
_pdbx_validate_polymer_linkage.auth_seq_id_2    127 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   B 
_pdbx_validate_polymer_linkage.dist             1.61 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A HIS 4   ? CD2 ? A HIS 4   CD2 
2  1 Y 0 A HIS 4   ? CE1 ? A HIS 4   CE1 
3  1 Y 0 A HIS 4   ? NE2 ? A HIS 4   NE2 
4  1 Y 0 A GLN 53  ? OE1 ? A GLN 53  OE1 
5  1 Y 0 A GLN 53  ? NE2 ? A GLN 53  NE2 
6  1 Y 0 A GLN 74  ? OE1 ? A GLN 74  OE1 
7  1 Y 0 A GLN 74  ? NE2 ? A GLN 74  NE2 
8  1 Y 0 A ASP 75  ? OD2 ? A ASP 75  OD2 
9  1 Y 0 A LYS 76  ? CE  ? A LYS 76  CE  
10 1 Y 0 A LYS 76  ? NZ  ? A LYS 76  NZ  
11 1 Y 0 A ASP 85  ? OD2 ? A ASP 85  OD2 
12 1 Y 0 A LYS 159 ? CD  ? A LYS 158 CD  
13 1 Y 0 A LYS 159 ? CE  ? A LYS 158 CE  
14 1 Y 0 A LYS 159 ? NZ  ? A LYS 158 NZ  
15 1 Y 0 A ASP 165 ? OD2 ? A ASP 164 OD2 
16 1 Y 0 A LYS 228 ? CE  ? A LYS 227 CE  
17 1 Y 0 A LYS 228 ? NZ  ? A LYS 227 NZ  
18 1 Y 0 A GLU 239 ? OE2 ? A GLU 238 OE2 
19 1 Y 0 A LYS 261 ? O   ? A LYS 260 O   
20 1 Y 0 A LYS 261 ? CG  ? A LYS 260 CG  
21 1 Y 0 A LYS 261 ? CD  ? A LYS 260 CD  
22 1 Y 0 A LYS 261 ? CE  ? A LYS 260 CE  
23 1 Y 0 A LYS 261 ? NZ  ? A LYS 260 NZ  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
KR5 O25  O  N N 217 
KR5 C22  C  N N 218 
KR5 N27  N  Y N 219 
KR5 C29  C  Y N 220 
KR5 C33  C  N N 221 
KR5 C30  C  Y N 222 
KR5 C31  C  Y N 223 
KR5 C37  C  N N 224 
KR5 N28  N  Y N 225 
KR5 C19  C  N N 226 
KR5 C18  C  N N 227 
KR5 N17  N  N N 228 
KR5 C8   C  Y N 229 
KR5 C7   C  Y N 230 
KR5 C6   C  Y N 231 
KR5 C9   C  Y N 232 
KR5 C10  C  Y N 233 
KR5 C5   C  Y N 234 
KR5 S2   S  N N 235 
KR5 O3   O  N N 236 
KR5 O4   O  N N 237 
KR5 N1   N  N N 238 
KR5 H1   H  N N 239 
KR5 H2   H  N N 240 
KR5 H3   H  N N 241 
KR5 H4   H  N N 242 
KR5 H5   H  N N 243 
KR5 H6   H  N N 244 
KR5 H7   H  N N 245 
KR5 H8   H  N N 246 
KR5 H9   H  N N 247 
KR5 H10  H  N N 248 
KR5 H11  H  N N 249 
KR5 H12  H  N N 250 
KR5 H13  H  N N 251 
KR5 H14  H  N N 252 
KR5 H15  H  N N 253 
KR5 H16  H  N N 254 
KR5 H17  H  N N 255 
KR5 H18  H  N N 256 
LEU N    N  N N 257 
LEU CA   C  N S 258 
LEU C    C  N N 259 
LEU O    O  N N 260 
LEU CB   C  N N 261 
LEU CG   C  N N 262 
LEU CD1  C  N N 263 
LEU CD2  C  N N 264 
LEU OXT  O  N N 265 
LEU H    H  N N 266 
LEU H2   H  N N 267 
LEU HA   H  N N 268 
LEU HB2  H  N N 269 
LEU HB3  H  N N 270 
LEU HG   H  N N 271 
LEU HD11 H  N N 272 
LEU HD12 H  N N 273 
LEU HD13 H  N N 274 
LEU HD21 H  N N 275 
LEU HD22 H  N N 276 
LEU HD23 H  N N 277 
LEU HXT  H  N N 278 
LYS N    N  N N 279 
LYS CA   C  N S 280 
LYS C    C  N N 281 
LYS O    O  N N 282 
LYS CB   C  N N 283 
LYS CG   C  N N 284 
LYS CD   C  N N 285 
LYS CE   C  N N 286 
LYS NZ   N  N N 287 
LYS OXT  O  N N 288 
LYS H    H  N N 289 
LYS H2   H  N N 290 
LYS HA   H  N N 291 
LYS HB2  H  N N 292 
LYS HB3  H  N N 293 
LYS HG2  H  N N 294 
LYS HG3  H  N N 295 
LYS HD2  H  N N 296 
LYS HD3  H  N N 297 
LYS HE2  H  N N 298 
LYS HE3  H  N N 299 
LYS HZ1  H  N N 300 
LYS HZ2  H  N N 301 
LYS HZ3  H  N N 302 
LYS HXT  H  N N 303 
MET N    N  N N 304 
MET CA   C  N S 305 
MET C    C  N N 306 
MET O    O  N N 307 
MET CB   C  N N 308 
MET CG   C  N N 309 
MET SD   S  N N 310 
MET CE   C  N N 311 
MET OXT  O  N N 312 
MET H    H  N N 313 
MET H2   H  N N 314 
MET HA   H  N N 315 
MET HB2  H  N N 316 
MET HB3  H  N N 317 
MET HG2  H  N N 318 
MET HG3  H  N N 319 
MET HE1  H  N N 320 
MET HE2  H  N N 321 
MET HE3  H  N N 322 
MET HXT  H  N N 323 
PHE N    N  N N 324 
PHE CA   C  N S 325 
PHE C    C  N N 326 
PHE O    O  N N 327 
PHE CB   C  N N 328 
PHE CG   C  Y N 329 
PHE CD1  C  Y N 330 
PHE CD2  C  Y N 331 
PHE CE1  C  Y N 332 
PHE CE2  C  Y N 333 
PHE CZ   C  Y N 334 
PHE OXT  O  N N 335 
PHE H    H  N N 336 
PHE H2   H  N N 337 
PHE HA   H  N N 338 
PHE HB2  H  N N 339 
PHE HB3  H  N N 340 
PHE HD1  H  N N 341 
PHE HD2  H  N N 342 
PHE HE1  H  N N 343 
PHE HE2  H  N N 344 
PHE HZ   H  N N 345 
PHE HXT  H  N N 346 
PRO N    N  N N 347 
PRO CA   C  N S 348 
PRO C    C  N N 349 
PRO O    O  N N 350 
PRO CB   C  N N 351 
PRO CG   C  N N 352 
PRO CD   C  N N 353 
PRO OXT  O  N N 354 
PRO H    H  N N 355 
PRO HA   H  N N 356 
PRO HB2  H  N N 357 
PRO HB3  H  N N 358 
PRO HG2  H  N N 359 
PRO HG3  H  N N 360 
PRO HD2  H  N N 361 
PRO HD3  H  N N 362 
PRO HXT  H  N N 363 
SER N    N  N N 364 
SER CA   C  N S 365 
SER C    C  N N 366 
SER O    O  N N 367 
SER CB   C  N N 368 
SER OG   O  N N 369 
SER OXT  O  N N 370 
SER H    H  N N 371 
SER H2   H  N N 372 
SER HA   H  N N 373 
SER HB2  H  N N 374 
SER HB3  H  N N 375 
SER HG   H  N N 376 
SER HXT  H  N N 377 
THR N    N  N N 378 
THR CA   C  N S 379 
THR C    C  N N 380 
THR O    O  N N 381 
THR CB   C  N R 382 
THR OG1  O  N N 383 
THR CG2  C  N N 384 
THR OXT  O  N N 385 
THR H    H  N N 386 
THR H2   H  N N 387 
THR HA   H  N N 388 
THR HB   H  N N 389 
THR HG1  H  N N 390 
THR HG21 H  N N 391 
THR HG22 H  N N 392 
THR HG23 H  N N 393 
THR HXT  H  N N 394 
TRP N    N  N N 395 
TRP CA   C  N S 396 
TRP C    C  N N 397 
TRP O    O  N N 398 
TRP CB   C  N N 399 
TRP CG   C  Y N 400 
TRP CD1  C  Y N 401 
TRP CD2  C  Y N 402 
TRP NE1  N  Y N 403 
TRP CE2  C  Y N 404 
TRP CE3  C  Y N 405 
TRP CZ2  C  Y N 406 
TRP CZ3  C  Y N 407 
TRP CH2  C  Y N 408 
TRP OXT  O  N N 409 
TRP H    H  N N 410 
TRP H2   H  N N 411 
TRP HA   H  N N 412 
TRP HB2  H  N N 413 
TRP HB3  H  N N 414 
TRP HD1  H  N N 415 
TRP HE1  H  N N 416 
TRP HE3  H  N N 417 
TRP HZ2  H  N N 418 
TRP HZ3  H  N N 419 
TRP HH2  H  N N 420 
TRP HXT  H  N N 421 
TYR N    N  N N 422 
TYR CA   C  N S 423 
TYR C    C  N N 424 
TYR O    O  N N 425 
TYR CB   C  N N 426 
TYR CG   C  Y N 427 
TYR CD1  C  Y N 428 
TYR CD2  C  Y N 429 
TYR CE1  C  Y N 430 
TYR CE2  C  Y N 431 
TYR CZ   C  Y N 432 
TYR OH   O  N N 433 
TYR OXT  O  N N 434 
TYR H    H  N N 435 
TYR H2   H  N N 436 
TYR HA   H  N N 437 
TYR HB2  H  N N 438 
TYR HB3  H  N N 439 
TYR HD1  H  N N 440 
TYR HD2  H  N N 441 
TYR HE1  H  N N 442 
TYR HE2  H  N N 443 
TYR HH   H  N N 444 
TYR HXT  H  N N 445 
VAL N    N  N N 446 
VAL CA   C  N S 447 
VAL C    C  N N 448 
VAL O    O  N N 449 
VAL CB   C  N N 450 
VAL CG1  C  N N 451 
VAL CG2  C  N N 452 
VAL OXT  O  N N 453 
VAL H    H  N N 454 
VAL H2   H  N N 455 
VAL HA   H  N N 456 
VAL HB   H  N N 457 
VAL HG11 H  N N 458 
VAL HG12 H  N N 459 
VAL HG13 H  N N 460 
VAL HG21 H  N N 461 
VAL HG22 H  N N 462 
VAL HG23 H  N N 463 
VAL HXT  H  N N 464 
ZN  ZN   ZN N N 465 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
KR5 C37 C31  sing N N 205 
KR5 N28 C31  doub Y N 206 
KR5 N28 N27  sing Y N 207 
KR5 C31 C30  sing Y N 208 
KR5 C19 C18  sing N N 209 
KR5 C19 C22  sing N N 210 
KR5 C18 N17  sing N N 211 
KR5 N27 C22  sing N N 212 
KR5 N27 C29  sing Y N 213 
KR5 C30 C29  doub Y N 214 
KR5 C22 O25  doub N N 215 
KR5 N17 C8   sing N N 216 
KR5 C29 C33  sing N N 217 
KR5 C8  C9   doub Y N 218 
KR5 C8  C7   sing Y N 219 
KR5 C9  C10  sing Y N 220 
KR5 C7  C6   doub Y N 221 
KR5 C10 C5   doub Y N 222 
KR5 C6  C5   sing Y N 223 
KR5 C5  S2   sing N N 224 
KR5 N1  S2   sing N N 225 
KR5 O3  S2   doub N N 226 
KR5 S2  O4   doub N N 227 
KR5 C33 H1   sing N N 228 
KR5 C33 H2   sing N N 229 
KR5 C33 H3   sing N N 230 
KR5 C30 H4   sing N N 231 
KR5 C37 H5   sing N N 232 
KR5 C37 H6   sing N N 233 
KR5 C37 H7   sing N N 234 
KR5 C19 H8   sing N N 235 
KR5 C19 H9   sing N N 236 
KR5 C18 H10  sing N N 237 
KR5 C18 H11  sing N N 238 
KR5 N17 H12  sing N N 239 
KR5 C7  H13  sing N N 240 
KR5 C6  H14  sing N N 241 
KR5 C9  H15  sing N N 242 
KR5 C10 H16  sing N N 243 
KR5 N1  H17  sing N N 244 
KR5 N1  H18  sing N N 245 
LEU N   CA   sing N N 246 
LEU N   H    sing N N 247 
LEU N   H2   sing N N 248 
LEU CA  C    sing N N 249 
LEU CA  CB   sing N N 250 
LEU CA  HA   sing N N 251 
LEU C   O    doub N N 252 
LEU C   OXT  sing N N 253 
LEU CB  CG   sing N N 254 
LEU CB  HB2  sing N N 255 
LEU CB  HB3  sing N N 256 
LEU CG  CD1  sing N N 257 
LEU CG  CD2  sing N N 258 
LEU CG  HG   sing N N 259 
LEU CD1 HD11 sing N N 260 
LEU CD1 HD12 sing N N 261 
LEU CD1 HD13 sing N N 262 
LEU CD2 HD21 sing N N 263 
LEU CD2 HD22 sing N N 264 
LEU CD2 HD23 sing N N 265 
LEU OXT HXT  sing N N 266 
LYS N   CA   sing N N 267 
LYS N   H    sing N N 268 
LYS N   H2   sing N N 269 
LYS CA  C    sing N N 270 
LYS CA  CB   sing N N 271 
LYS CA  HA   sing N N 272 
LYS C   O    doub N N 273 
LYS C   OXT  sing N N 274 
LYS CB  CG   sing N N 275 
LYS CB  HB2  sing N N 276 
LYS CB  HB3  sing N N 277 
LYS CG  CD   sing N N 278 
LYS CG  HG2  sing N N 279 
LYS CG  HG3  sing N N 280 
LYS CD  CE   sing N N 281 
LYS CD  HD2  sing N N 282 
LYS CD  HD3  sing N N 283 
LYS CE  NZ   sing N N 284 
LYS CE  HE2  sing N N 285 
LYS CE  HE3  sing N N 286 
LYS NZ  HZ1  sing N N 287 
LYS NZ  HZ2  sing N N 288 
LYS NZ  HZ3  sing N N 289 
LYS OXT HXT  sing N N 290 
MET N   CA   sing N N 291 
MET N   H    sing N N 292 
MET N   H2   sing N N 293 
MET CA  C    sing N N 294 
MET CA  CB   sing N N 295 
MET CA  HA   sing N N 296 
MET C   O    doub N N 297 
MET C   OXT  sing N N 298 
MET CB  CG   sing N N 299 
MET CB  HB2  sing N N 300 
MET CB  HB3  sing N N 301 
MET CG  SD   sing N N 302 
MET CG  HG2  sing N N 303 
MET CG  HG3  sing N N 304 
MET SD  CE   sing N N 305 
MET CE  HE1  sing N N 306 
MET CE  HE2  sing N N 307 
MET CE  HE3  sing N N 308 
MET OXT HXT  sing N N 309 
PHE N   CA   sing N N 310 
PHE N   H    sing N N 311 
PHE N   H2   sing N N 312 
PHE CA  C    sing N N 313 
PHE CA  CB   sing N N 314 
PHE CA  HA   sing N N 315 
PHE C   O    doub N N 316 
PHE C   OXT  sing N N 317 
PHE CB  CG   sing N N 318 
PHE CB  HB2  sing N N 319 
PHE CB  HB3  sing N N 320 
PHE CG  CD1  doub Y N 321 
PHE CG  CD2  sing Y N 322 
PHE CD1 CE1  sing Y N 323 
PHE CD1 HD1  sing N N 324 
PHE CD2 CE2  doub Y N 325 
PHE CD2 HD2  sing N N 326 
PHE CE1 CZ   doub Y N 327 
PHE CE1 HE1  sing N N 328 
PHE CE2 CZ   sing Y N 329 
PHE CE2 HE2  sing N N 330 
PHE CZ  HZ   sing N N 331 
PHE OXT HXT  sing N N 332 
PRO N   CA   sing N N 333 
PRO N   CD   sing N N 334 
PRO N   H    sing N N 335 
PRO CA  C    sing N N 336 
PRO CA  CB   sing N N 337 
PRO CA  HA   sing N N 338 
PRO C   O    doub N N 339 
PRO C   OXT  sing N N 340 
PRO CB  CG   sing N N 341 
PRO CB  HB2  sing N N 342 
PRO CB  HB3  sing N N 343 
PRO CG  CD   sing N N 344 
PRO CG  HG2  sing N N 345 
PRO CG  HG3  sing N N 346 
PRO CD  HD2  sing N N 347 
PRO CD  HD3  sing N N 348 
PRO OXT HXT  sing N N 349 
SER N   CA   sing N N 350 
SER N   H    sing N N 351 
SER N   H2   sing N N 352 
SER CA  C    sing N N 353 
SER CA  CB   sing N N 354 
SER CA  HA   sing N N 355 
SER C   O    doub N N 356 
SER C   OXT  sing N N 357 
SER CB  OG   sing N N 358 
SER CB  HB2  sing N N 359 
SER CB  HB3  sing N N 360 
SER OG  HG   sing N N 361 
SER OXT HXT  sing N N 362 
THR N   CA   sing N N 363 
THR N   H    sing N N 364 
THR N   H2   sing N N 365 
THR CA  C    sing N N 366 
THR CA  CB   sing N N 367 
THR CA  HA   sing N N 368 
THR C   O    doub N N 369 
THR C   OXT  sing N N 370 
THR CB  OG1  sing N N 371 
THR CB  CG2  sing N N 372 
THR CB  HB   sing N N 373 
THR OG1 HG1  sing N N 374 
THR CG2 HG21 sing N N 375 
THR CG2 HG22 sing N N 376 
THR CG2 HG23 sing N N 377 
THR OXT HXT  sing N N 378 
TRP N   CA   sing N N 379 
TRP N   H    sing N N 380 
TRP N   H2   sing N N 381 
TRP CA  C    sing N N 382 
TRP CA  CB   sing N N 383 
TRP CA  HA   sing N N 384 
TRP C   O    doub N N 385 
TRP C   OXT  sing N N 386 
TRP CB  CG   sing N N 387 
TRP CB  HB2  sing N N 388 
TRP CB  HB3  sing N N 389 
TRP CG  CD1  doub Y N 390 
TRP CG  CD2  sing Y N 391 
TRP CD1 NE1  sing Y N 392 
TRP CD1 HD1  sing N N 393 
TRP CD2 CE2  doub Y N 394 
TRP CD2 CE3  sing Y N 395 
TRP NE1 CE2  sing Y N 396 
TRP NE1 HE1  sing N N 397 
TRP CE2 CZ2  sing Y N 398 
TRP CE3 CZ3  doub Y N 399 
TRP CE3 HE3  sing N N 400 
TRP CZ2 CH2  doub Y N 401 
TRP CZ2 HZ2  sing N N 402 
TRP CZ3 CH2  sing Y N 403 
TRP CZ3 HZ3  sing N N 404 
TRP CH2 HH2  sing N N 405 
TRP OXT HXT  sing N N 406 
TYR N   CA   sing N N 407 
TYR N   H    sing N N 408 
TYR N   H2   sing N N 409 
TYR CA  C    sing N N 410 
TYR CA  CB   sing N N 411 
TYR CA  HA   sing N N 412 
TYR C   O    doub N N 413 
TYR C   OXT  sing N N 414 
TYR CB  CG   sing N N 415 
TYR CB  HB2  sing N N 416 
TYR CB  HB3  sing N N 417 
TYR CG  CD1  doub Y N 418 
TYR CG  CD2  sing Y N 419 
TYR CD1 CE1  sing Y N 420 
TYR CD1 HD1  sing N N 421 
TYR CD2 CE2  doub Y N 422 
TYR CD2 HD2  sing N N 423 
TYR CE1 CZ   doub Y N 424 
TYR CE1 HE1  sing N N 425 
TYR CE2 CZ   sing Y N 426 
TYR CE2 HE2  sing N N 427 
TYR CZ  OH   sing N N 428 
TYR OH  HH   sing N N 429 
TYR OXT HXT  sing N N 430 
VAL N   CA   sing N N 431 
VAL N   H    sing N N 432 
VAL N   H2   sing N N 433 
VAL CA  C    sing N N 434 
VAL CA  CB   sing N N 435 
VAL CA  HA   sing N N 436 
VAL C   O    doub N N 437 
VAL C   OXT  sing N N 438 
VAL CB  CG1  sing N N 439 
VAL CB  CG2  sing N N 440 
VAL CB  HB   sing N N 441 
VAL CG1 HG11 sing N N 442 
VAL CG1 HG12 sing N N 443 
VAL CG1 HG13 sing N N 444 
VAL CG2 HG21 sing N N 445 
VAL CG2 HG22 sing N N 446 
VAL CG2 HG23 sing N N 447 
VAL OXT HXT  sing N N 448 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                  ZN  
3 BICINE                                                                      BCN 
4 'DIMETHYL SULFOXIDE'                                                        DMS 
5 '4-{[3-(3,5-dimethyl-1H-pyrazol-1-yl)-3-oxopropyl]amino}benzenesulfonamide' KR5 
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' 
# 
