data_4Q09
# 
_entry.id   4Q09 
# 
_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   4Q09         pdb_00004q09 10.2210/pdb4q09/pdb 
RCSB  RCSB085441   ?            ?                   
WWPDB D_1000085441 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4PYX . unspecified 
PDB 4PYY . unspecified 
PDB 4PZH . unspecified 
PDB 4Q06 . unspecified 
PDB 4Q07 . unspecified 
PDB 4Q08 . unspecified 
PDB 4Q0L . unspecified 
# 
_pdbx_database_status.entry_id                        4Q09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2014-04-01 
_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                     'Discovery and characterization of novel selective inhibitors of carbonic anhydrase IX.' 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_volume            57 
_citation.page_first                9435 
_citation.page_last                 9446 
_citation.year                      2014 
_citation.journal_id_ASTM           JMCMAR 
_citation.country                   US 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_id_CSD            0151 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25358084 
_citation.pdbx_database_id_DOI      10.1021/jm501003k 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.'      1  ? 
primary 'Matuliene, J.'      2  ? 
primary 'Smirnov, A.'        3  ? 
primary 'Timm, D.D.'         4  ? 
primary 'Zubriene, A.'       5  ? 
primary 'Baranauskiene, L.'  6  ? 
primary 'Morkunaite, V.'     7  ? 
primary 'Smirnoviene, J.'    8  ? 
primary 'Michailoviene, V.'  9  ? 
primary 'Juozapaitiene, V.'  10 ? 
primary 'Mickeviciute, A.'   11 ? 
primary 'Kazokaite, J.'      12 ? 
primary 'Baksyte, S.'        13 ? 
primary 'Kasiliauskaite, A.' 14 ? 
primary 'Jachno, J.'         15 ? 
primary 'Revuckiene, J.'     16 ? 
primary 'Kisonaite, M.'      17 ? 
primary 'Pilipuityte, V.'    18 ? 
primary 'Ivanauskaite, E.'   19 ? 
primary 'Milinaviciute, G.'  20 ? 
primary 'Smirnovas, V.'      21 ? 
primary 'Petrikaite, V.'     22 ? 
primary 'Kairys, V.'         23 ? 
primary 'Petrauskas, V.'     24 ? 
primary 'Norvaisas, P.'      25 ? 
primary 'Linge, D.'          26 ? 
primary 'Gibieza, P.'        27 ? 
primary 'Capkauskaite, E.'   28 ? 
primary 'Zaksauskas, A.'     29 ? 
primary 'Kazlauskas, E.'     30 ? 
primary 'Manakova, E.'       31 ? 
primary 'Grazulis, S.'       32 ? 
primary 'Ladbury, J.E.'      33 ? 
primary 'Matulis, D.'        34 ? 
# 
_cell.entry_id           4Q09 
_cell.length_a           41.835 
_cell.length_b           41.011 
_cell.length_c           71.006 
_cell.angle_alpha        90.000 
_cell.angle_beta         103.560 
_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                         4Q09 
_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'                                                               29220.879 1   4.2.1.1 
'A65S, N67K, I91T, F130A, V134S, L203N' ? ? 
2 non-polymer syn 'ZINC ION'                                                                           65.409    1   ?       ? ? ? 
3 non-polymer syn '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 444.489   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                 78.133    1   ?       ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                                       62.068    5   ?       ? ? ? 
6 water       nat water                                                                                18.015    252 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
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  SER n 
1 66  PHE n 
1 67  LYS 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  THR 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 ALA n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 SER 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 ASN n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4Q09 
_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       260 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4Q09 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 4Q09 LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 4Q09 THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 4Q09 ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 4 
1 4Q09 SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 134 5 
1 4Q09 ASN A 203 ? UNP P00918 LEU 203 'engineered mutation' 203 6 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                              ?                 
'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                                                                             ?                 
'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                           ?                 
'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                      ?                 
'C4 H7 N O4'          133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                             ?                 
'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                 ?                 
'C2 H6 O S'           78.133  
EDO non-polymer         . 1,2-ETHANEDIOL                                                                       'ETHYLENE GLYCOL' 
'C2 H6 O2'            62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                                            ?                 
'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                      ?                 
'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                              ?                 
'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                            ?                 
'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                                ?                 
'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                           ?                 
'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                              ?                 
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                               ?                 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                           ?                 
'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                        ?                 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                              ?                 
'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                               ?                 
'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                            ?                 
'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                           ?                 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                             ?                 
'C9 H11 N O3'         181.189 
V14 non-polymer         . '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ?                 
'C16 H23 F3 N2 O5 S2' 444.489 
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          4Q09 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   37.2 
_exptl_crystal.density_Matthews      1.97 
_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   2012-12-02 
_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                     4Q09 
_reflns.d_resolution_high            1.200 
_reflns.d_resolution_low             69.03 
_reflns.number_all                   ? 
_reflns.number_obs                   72417 
_reflns.pdbx_Rmerge_I_obs            0.042 
_reflns.pdbx_netI_over_sigmaI        21.100 
_reflns.pdbx_Rsym_value              0.042 
_reflns.pdbx_redundancy              6.700 
_reflns.percent_possible_obs         98.800 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        10.985 
_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 
1.20 1.26  ? 66907 ? 0.346 2.2  0.346 ? 6.40 ? 10431 98.20 1  1 
1.26 1.34  ? 68642 ? 0.262 2.9  0.262 ? 6.90 ? 10001 99.10 2  1 
1.34 1.43  ? 62367 ? 0.184 4.2  0.184 ? 6.70 ? 9353  98.50 3  1 
1.43 1.55  ? 57724 ? 0.126 6.0  0.126 ? 6.70 ? 8680  98.50 4  1 
1.55 1.70  ? 55855 ? 0.087 8.6  0.087 ? 6.90 ? 8058  99.30 5  1 
1.70 1.90  ? 47812 ? 0.058 12.3 0.058 ? 6.60 ? 7274  98.60 6  1 
1.90 2.19  ? 46177 ? 0.040 17.1 0.040 ? 7.10 ? 6479  99.60 7  1 
2.19 2.68  ? 36236 ? 0.035 19.4 0.035 ? 6.60 ? 5463  98.80 8  1 
2.68 3.79  ? 30362 ? 0.028 21.5 0.028 ? 7.10 ? 4282  99.40 9  1 
3.79 69.03 ? 15862 ? 0.024 24.4 0.024 ? 6.60 ? 2396  98.90 10 1 
# 
_refine.entry_id                                 4Q09 
_refine.ls_d_res_high                            1.200 
_refine.ls_d_res_low                             69.030 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.690 
_refine.ls_number_reflns_obs                     72399 
_refine.ls_number_reflns_all                     72399 
_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                          0.143 
_refine.ls_R_factor_obs                          0.143 
_refine.ls_R_factor_R_work                       0.139 
_refine.ls_wR_factor_R_work                      0.139 
_refine.ls_R_factor_R_free                       0.178 
_refine.ls_wR_factor_R_free                      0.180 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  7246 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.485 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.510 
_refine.aniso_B[2][2]                            0.520 
_refine.aniso_B[3][3]                            -0.890 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.320 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.979 
_refine.correlation_coeff_Fo_to_Fc_free          0.969 
_refine.overall_SU_R_Cruickshank_DPI             0.042 
_refine.overall_SU_R_free                        0.043 
_refine.pdbx_overall_ESU_R                       0.042 
_refine.pdbx_overall_ESU_R_Free                  0.044 
_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                   0.885 
_refine.B_iso_max                                104.15 
_refine.B_iso_min                                6.59 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_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        2042 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.number_atoms_solvent             252 
_refine_hist.number_atoms_total               2347 
_refine_hist.d_res_high                       1.200 
_refine_hist.d_res_low                        69.030 
# 
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       2322 0.024  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3165 2.333  1.966  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 292  7.204  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 106  36.967 24.717 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 385  13.301 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 9    18.552 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         323  0.160  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1812 0.014  0.021  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr     2322 7.641  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free      253  28.909 5.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded    2249 17.759 5.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.200 
_refine_ls_shell.d_res_low                        1.231 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               98.000 
_refine_ls_shell.number_reflns_R_work             4763 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.213 
_refine_ls_shell.R_factor_R_free                  0.269 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             538 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                5301 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4Q09 
_struct.title                     'Crystal structure of chimeric carbonic anhydrase XII with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4Q09 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J 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 126 GLY A 128 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? SER A 134 ? ASP A 129 SER A 134 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 164 LYS A 167 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 218 ARG A 226 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 ? ? ? ? ? ? ? 2.049 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
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 C V14 . N10 ? ? A ZN  301 A V14 302 1_555 ? ? ? ? ? ? ? 1.943 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -1.91 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 13.19 
# 
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 256 ALA A 257 
B 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
B 4  VAL A 206 ? LEU A 211 ? VAL A 206 LEU A 211 
B 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
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 172 ASP A 174 
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 140 VAL A 149 
C 6  ILE A 215 ? VAL A 217 ? ILE A 215 VAL A 217 
# 
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 257 
B 2 3  O LYS A 256 ? O LYS A 256 N THR A 192 ? N THR A 192 
B 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
B 4 5  O LEU A 211 ? O LEU A 211 N GLY A 144 ? N GLY A 144 
B 5 6  O ILE A 145 ? O ILE A 145 N LEU A 118 ? N LEU A 118 
B 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
B 7 8  O THR A 91  ? O THR A 91  N PHE A 70  ? N PHE A 70  
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 173 
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 GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 145 
C 5 6  N PHE A 146 ? N PHE A 146 O ILE A 215 ? O ILE A 215 
# 
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 V14 302 ? 16 'BINDING SITE FOR RESIDUE V14 A 302' 
AC3 Software A DMS 303 ? 4  'BINDING SITE FOR RESIDUE DMS A 303' 
AC4 Software A EDO 304 ? 5  'BINDING SITE FOR RESIDUE EDO A 304' 
AC5 Software A EDO 305 ? 7  'BINDING SITE FOR RESIDUE EDO A 305' 
AC6 Software A EDO 306 ? 3  'BINDING SITE FOR RESIDUE EDO A 306' 
AC7 Software A EDO 307 ? 7  'BINDING SITE FOR RESIDUE EDO A 307' 
AC8 Software A EDO 308 ? 7  'BINDING SITE FOR RESIDUE EDO A 308' 
# 
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  V14 C .   ? V14 A 302 . ? 1_555 ? 
5  AC2 16 ASN A 62  ? ASN A 62  . ? 1_555 ? 
6  AC2 16 HIS A 64  ? HIS A 64  . ? 1_555 ? 
7  AC2 16 LYS A 67  ? LYS A 67  . ? 1_555 ? 
8  AC2 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
9  AC2 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
10 AC2 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
11 AC2 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
12 AC2 16 VAL A 121 ? VAL A 121 . ? 1_555 ? 
13 AC2 16 ALA A 130 ? ALA A 130 . ? 1_555 ? 
14 AC2 16 LEU A 197 ? LEU A 197 . ? 1_555 ? 
15 AC2 16 THR A 198 ? THR A 198 . ? 1_555 ? 
16 AC2 16 THR A 199 ? THR A 199 . ? 1_555 ? 
17 AC2 16 PRO A 200 ? PRO A 200 . ? 1_555 ? 
18 AC2 16 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
19 AC2 16 HOH J .   ? HOH A 520 . ? 1_555 ? 
20 AC2 16 HOH J .   ? HOH A 585 . ? 1_555 ? 
21 AC3 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
22 AC3 4  ASP A 242 ? ASP A 242 . ? 1_555 ? 
23 AC3 4  TRP A 244 ? TRP A 244 . ? 1_555 ? 
24 AC3 4  EDO I .   ? EDO A 308 . ? 1_555 ? 
25 AC4 5  LEU A 163 ? LEU A 163 . ? 1_555 ? 
26 AC4 5  ASP A 164 ? ASP A 164 . ? 1_555 ? 
27 AC4 5  LYS A 224 ? LYS A 224 . ? 1_555 ? 
28 AC4 5  LYS A 227 ? LYS A 227 . ? 1_555 ? 
29 AC4 5  HOH J .   ? HOH A 573 . ? 1_555 ? 
30 AC5 7  LYS A 18  ? LYS A 18  . ? 1_455 ? 
31 AC5 7  ASP A 19  ? ASP A 19  . ? 1_455 ? 
32 AC5 7  PRO A 21  ? PRO A 21  . ? 1_455 ? 
33 AC5 7  SER A 48  ? SER A 48  . ? 1_555 ? 
34 AC5 7  VAL A 49  ? VAL A 49  . ? 1_555 ? 
35 AC5 7  SER A 50  ? SER A 50  . ? 1_555 ? 
36 AC5 7  ASP A 52  ? ASP A 52  . ? 1_555 ? 
37 AC6 3  LYS A 111 ? LYS A 111 . ? 1_555 ? 
38 AC6 3  TYR A 127 ? TYR A 127 . ? 1_545 ? 
39 AC6 3  EDO H .   ? EDO A 307 . ? 1_555 ? 
40 AC7 7  GLY A 102 ? GLY A 102 . ? 1_555 ? 
41 AC7 7  LYS A 112 ? LYS A 112 . ? 1_555 ? 
42 AC7 7  LYS A 113 ? LYS A 113 . ? 1_555 ? 
43 AC7 7  LYS A 126 ? LYS A 126 . ? 1_545 ? 
44 AC7 7  TYR A 127 ? TYR A 127 . ? 1_545 ? 
45 AC7 7  LYS A 132 ? LYS A 132 . ? 1_545 ? 
46 AC7 7  EDO G .   ? EDO A 306 . ? 1_555 ? 
47 AC8 7  TYR A 7   ? TYR A 7   . ? 1_555 ? 
48 AC8 7  GLY A 8   ? GLY A 8   . ? 1_555 ? 
49 AC8 7  PRO A 13  ? PRO A 13  . ? 1_555 ? 
50 AC8 7  GLU A 14  ? GLU A 14  . ? 1_555 ? 
51 AC8 7  PRO A 246 ? PRO A 246 . ? 1_555 ? 
52 AC8 7  DMS D .   ? DMS A 303 . ? 1_555 ? 
53 AC8 7  HOH J .   ? HOH A 429 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4Q09 
_atom_sites.fract_transf_matrix[1][1]   0.023903 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005764 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024384 
_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]   0.014487 
_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  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 9.117   1.539   8.265   1.00 14.97  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 9.995   0.399   8.079   1.00 33.56  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.600   -0.745  8.967   1.00 35.88  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.929   -1.950  8.686   1.00 27.18  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 11.445  0.791   8.318   1.00 36.34  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 11.864  0.731   9.766   1.00 61.88  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 12.822  -0.103  10.206  1.00 81.59  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 11.421  1.443   10.876  1.00 80.36  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 12.986  0.065   11.532  1.00 98.70  ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 12.127  1.010   11.942  1.00 103.82 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.879   -0.458  10.017  1.00 32.04  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 8.310   -1.497  10.811  1.00 20.77  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 7.249   -2.331  10.084  1.00 18.62  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.663   -1.894  9.046   1.00 23.44  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.658   -0.856  12.019  1.00 21.22  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.457   -0.032  11.656  1.00 18.71  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 6.432   1.301   11.287  1.00 20.68  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 5.087   -0.464  11.671  1.00 15.82  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 5.148   1.722   11.072  1.00 20.43  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 4.287   0.690   11.294  1.00 16.72  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.449   -1.676  11.971  1.00 17.62  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.899   0.630   11.225  1.00 17.03  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 3.030   -1.730  11.886  1.00 16.48  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 2.293   -0.602  11.504  1.00 16.74  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.979   -3.521  10.637  1.00 17.42  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.921   -4.424  10.087  1.00 18.70  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.617   -5.494  11.112  1.00 14.79  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.650   -5.258  12.326  1.00 14.33  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 5.376   -6.726  10.625  1.00 15.77  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.945   -7.823  11.502  1.00 15.94  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.831   -9.024  11.359  1.00 18.00  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.501   -10.092 11.892  1.00 24.16  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.466   -8.200  11.175  1.00 15.27  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.550   -7.092  11.714  1.00 13.18  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 2.143   -7.065  13.066  1.00 12.11  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 2.061   -6.077  10.864  1.00 15.35  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 1.288   -6.068  13.516  1.00 12.45  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 1.178   -5.093  11.315  1.00 13.50  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.821   -5.092  12.640  1.00 11.82  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.013  -4.120  13.052  1.00 12.87  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.933   -8.861  10.618  1.00 20.58  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.801   -9.982  10.313  1.00 21.23  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.823   -10.236 11.419  1.00 21.89  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.888   -9.549  12.430  1.00 19.21  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.637   -11.235 11.211  1.00 19.37  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.671  -11.626 12.151  1.00 21.05  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.663  -10.507 12.481  1.00 17.47  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 12.119  -10.419 13.638  1.00 18.12  ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.510  -12.741 11.487  1.00 26.74  ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.560  -13.380 12.344  1.00 30.31  ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 13.145  -14.637 11.656  1.00 41.02  ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 14.414  -15.097 12.376  1.00 45.04  ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 15.318  -16.096 11.678  1.00 59.22  ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 12.088  -9.748  11.463  1.00 19.25  ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 13.111  -8.718  11.699  1.00 17.29  ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 12.596  -7.342  11.944  1.00 16.29  ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 13.446  -6.457  12.334  1.00 16.82  ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 14.142  -8.745  10.591  1.00 16.93  ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 14.774  -10.115 10.463  1.00 15.75  ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 15.823  -10.515 11.214  1.00 18.38  ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 14.438  -11.158 9.670   1.00 16.56  ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 16.132  -11.749 10.885  1.00 20.31  ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 15.268  -12.157 9.941   1.00 19.12  ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 11.267  -7.111  11.782  1.00 16.08  ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.764  -5.749  11.946  1.00 14.95  ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 9.436   -5.739  12.685  1.00 13.57  ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.767   -4.689  12.733  1.00 14.70  ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 10.581  -5.037  10.579  1.00 16.70  ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 9.532   -5.692  9.725   1.00 16.63  ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.932   -6.710  10.097  1.00 21.72  ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 9.243   -5.078  8.593   1.00 21.57  ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 9.059   -6.871  13.322  1.00 13.61  ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.725   -6.962  13.953  1.00 13.77  ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.725   -6.482  15.395  1.00 11.66  ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 8.657   -5.768  15.834  1.00 11.91  ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.647   -6.768  16.125  1.00 11.93  ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 6.402   -6.182  17.448  1.00 10.98  ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 7.545   -6.199  18.420  1.00 11.05  ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.673   -5.239  19.205  1.00 12.05  ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 5.239   -7.000  17.927  1.00 11.37  ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 4.422   -7.207  16.679  1.00 13.02  ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 5.467   -7.521  15.605  1.00 12.83  ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 8.435   -7.209  18.341  1.00 11.92  ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 9.526   -7.296  19.323  1.00 12.53  ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 10.626  -6.277  19.008  1.00 12.45  ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 11.521  -6.082  19.840  1.00 13.40  ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 10.154  -8.701  19.378  1.00 16.83  ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 9.124   -9.809  19.716  1.00 20.65  ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 8.404   -9.581  21.017  1.00 34.11  ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 9.075   -9.230  21.998  1.00 37.45  ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 7.164   -9.794  21.074  1.00 54.69  ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 10.593  -5.691  17.830  1.00 10.70  ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 11.565  -4.691  17.416  1.00 10.77  ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 11.090  -3.265  17.569  1.00 10.44  ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.890  -2.328  17.507  1.00 11.38  ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.899  -4.881  15.940  1.00 11.28  ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 12.631  -6.142  15.632  1.00 13.31  ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.998  -6.225  15.725  1.00 13.01  ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 12.194  -7.395  15.288  1.00 14.39  ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 14.392  -7.458  15.421  1.00 16.38  ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 13.306  -8.186  15.128  1.00 15.81  ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.773   -3.041  17.754  1.00 11.04  ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 9.196   -1.711  17.630  1.00 10.11  ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.754   -0.742  18.687  1.00 10.05  ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.857   0.478   18.350  1.00 11.38  ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.691   -1.780  17.753  1.00 10.21  ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 7.016   -2.415  16.615  1.00 9.47   ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 7.566   -2.842  15.383  1.00 10.30  ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 5.611   -2.774  16.560  1.00 9.17   ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 6.609   -3.451  14.604  1.00 10.59  ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 5.409   -3.406  15.272  1.00 10.59  ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 4.567   -2.640  17.452  1.00 9.56   ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 4.132   -3.838  14.870  1.00 10.10  ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 3.304   -3.078  17.044  1.00 10.86  ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 3.124   -3.665  15.793  1.00 10.64  ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 10.144  -1.227  19.876  1.00 10.25  ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.644  -0.342  20.927  1.00 12.20  ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.847  0.428   20.526  1.00 11.00  ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 12.136  1.491   21.096  1.00 11.86  ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.898  -1.115  22.219  1.00 12.18  ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 12.099  -1.964  22.140  1.00 11.79  ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 13.304  -1.575  22.684  1.00 13.90  ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 12.312  -3.185  21.549  1.00 12.47  ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 14.187  -2.512  22.442  1.00 13.97  ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 13.634  -3.482  21.754  1.00 13.95  ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 12.630  -0.025  19.530  1.00 10.76  ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 13.878  0.685   19.143  1.00 12.37  ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 13.495  1.991   18.487  1.00 12.41  ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 14.135  3.027   18.742  1.00 20.09  ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 14.731  -0.186  18.241  1.00 12.21  ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 15.355  -1.383  18.977  1.00 13.70  ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 16.074  -2.394  18.091  1.00 13.46  ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 15.112  -3.386  17.435  1.00 12.84  ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 15.747  -4.159  16.304  1.00 12.49  ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 12.500  2.031   17.635  1.00 13.08  ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 12.072  3.319   17.073  1.00 13.46  ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 11.060  4.035   17.948  1.00 13.46  ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 10.967  5.239   17.894  1.00 14.24  ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 11.488  3.108   15.696  1.00 16.59  ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 12.508  2.886   14.664  1.00 22.99  ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 13.502  3.664   14.546  1.00 23.63  ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 12.356  1.833   14.014  1.00 36.65  ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 10.307  3.309   18.781  1.00 11.88  ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 9.185   3.856   19.565  1.00 12.07  ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 9.294   3.367   20.988  1.00 11.05  ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 8.671   2.363   21.364  1.00 11.83  ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 7.842   3.483   18.929  1.00 14.06  ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 7.742   4.004   17.505  1.00 16.87  ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 7.489   5.335   17.235  1.00 20.65  ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 8.040   3.129   16.434  1.00 18.96  ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 7.456   5.775   15.908  1.00 27.09  ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 8.018   3.573   15.107  1.00 22.28  ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 7.718   4.900   14.860  1.00 23.77  ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 21  ? 10.174  3.981   21.806  1.00 12.46  ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 21  ? 10.459  3.422   23.121  1.00 13.02  ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 21  ? 9.232   3.310   24.038  1.00 11.74  ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 21  ? 9.283   2.525   25.010  1.00 13.54  ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 21  ? 11.532  4.345   23.702  1.00 17.00  ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 21  ? 12.123  5.057   22.523  1.00 21.08  ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 21  ? 11.102  5.104   21.453  1.00 14.72  ? 21  PRO A CD  1 
ATOM   161  N  N   A ILE A 1 22  ? 8.137   4.031   23.683  0.50 11.58  ? 22  ILE A N   1 
ATOM   162  N  N   B ILE A 1 22  ? 8.137   4.071   23.828  0.50 12.34  ? 22  ILE A N   1 
ATOM   163  C  CA  A ILE A 1 22  ? 6.853   3.955   24.369  0.50 10.17  ? 22  ILE A CA  1 
ATOM   164  C  CA  B ILE A 1 22  ? 6.941   3.867   24.654  0.50 11.18  ? 22  ILE A CA  1 
ATOM   165  C  C   A ILE A 1 22  ? 6.253   2.509   24.287  0.50 8.55   ? 22  ILE A C   1 
ATOM   166  C  C   B ILE A 1 22  ? 6.377   2.413   24.476  0.50 11.84  ? 22  ILE A C   1 
ATOM   167  O  O   A ILE A 1 22  ? 5.361   2.168   25.020  0.50 8.14   ? 22  ILE A O   1 
ATOM   168  O  O   B ILE A 1 22  ? 5.565   1.984   25.302  0.50 14.02  ? 22  ILE A O   1 
ATOM   169  C  CB  A ILE A 1 22  ? 5.884   5.058   23.833  0.50 10.98  ? 22  ILE A CB  1 
ATOM   170  C  CB  B ILE A 1 22  ? 5.848   4.903   24.330  0.50 10.33  ? 22  ILE A CB  1 
ATOM   171  C  CG1 A ILE A 1 22  ? 4.822   5.436   24.885  0.50 8.83   ? 22  ILE A CG1 1 
ATOM   172  C  CG1 B ILE A 1 22  ? 4.832   5.042   25.458  0.50 11.56  ? 22  ILE A CG1 1 
ATOM   173  C  CG2 A ILE A 1 22  ? 5.295   4.684   22.473  0.50 9.46   ? 22  ILE A CG2 1 
ATOM   174  C  CG2 B ILE A 1 22  ? 5.144   4.504   23.036  0.50 11.05  ? 22  ILE A CG2 1 
ATOM   175  C  CD1 A ILE A 1 22  ? 3.942   6.583   24.509  0.50 16.40  ? 22  ILE A CD1 1 
ATOM   176  C  CD1 B ILE A 1 22  ? 5.386   5.792   26.626  0.50 15.08  ? 22  ILE A CD1 1 
ATOM   177  N  N   . ALA A 1 23  ? 6.823   1.664   23.451  1.00 10.58  ? 23  ALA A N   1 
ATOM   178  C  CA  . ALA A 1 23  ? 6.415   0.265   23.295  1.00 11.05  ? 23  ALA A CA  1 
ATOM   179  C  C   . ALA A 1 23  ? 6.540   -0.454  24.624  1.00 11.06  ? 23  ALA A C   1 
ATOM   180  O  O   . ALA A 1 23  ? 5.821   -1.457  24.793  1.00 12.98  ? 23  ALA A O   1 
ATOM   181  C  CB  . ALA A 1 23  ? 7.226   -0.395  22.177  1.00 11.32  ? 23  ALA A CB  1 
ATOM   182  N  N   . LYS A 1 24  ? 7.487   -0.032  25.485  1.00 13.31  ? 24  LYS A N   1 
ATOM   183  C  CA  . LYS A 1 24  ? 7.709   -0.643  26.794  1.00 14.96  ? 24  LYS A CA  1 
ATOM   184  C  C   . LYS A 1 24  ? 7.065   0.234   27.905  1.00 15.40  ? 24  LYS A C   1 
ATOM   185  O  O   . LYS A 1 24  ? 7.476   0.086   29.050  1.00 17.48  ? 24  LYS A O   1 
ATOM   186  C  CB  . LYS A 1 24  ? 9.151   -0.888  27.074  1.00 17.45  ? 24  LYS A CB  1 
ATOM   187  C  CG  . LYS A 1 24  ? 9.746   -1.891  26.114  1.00 18.01  ? 24  LYS A CG  1 
ATOM   188  C  CD  . LYS A 1 24  ? 11.251  -2.006  26.503  1.00 22.04  ? 24  LYS A CD  1 
ATOM   189  C  CE  . LYS A 1 24  ? 11.962  -2.998  25.651  1.00 21.50  ? 24  LYS A CE  1 
ATOM   190  N  NZ  . LYS A 1 24  ? 11.318  -4.328  25.890  1.00 30.71  ? 24  LYS A NZ  1 
ATOM   191  N  N   . GLY A 1 25  ? 6.041   1.054   27.579  1.00 14.63  ? 25  GLY A N   1 
ATOM   192  C  CA  . GLY A 1 25  ? 5.423   1.973   28.533  1.00 16.39  ? 25  GLY A CA  1 
ATOM   193  C  C   . GLY A 1 25  ? 4.448   1.314   29.486  1.00 14.38  ? 25  GLY A C   1 
ATOM   194  O  O   . GLY A 1 25  ? 4.274   0.076   29.533  1.00 14.61  ? 25  GLY A O   1 
ATOM   195  N  N   . GLU A 1 26  ? 3.785   2.148   30.279  1.00 14.98  ? 26  GLU A N   1 
ATOM   196  C  CA  . GLU A 1 26  ? 2.933   1.665   31.320  1.00 16.28  ? 26  GLU A CA  1 
ATOM   197  C  C   . GLU A 1 26  ? 1.487   1.471   30.893  1.00 12.31  ? 26  GLU A C   1 
ATOM   198  O  O   . GLU A 1 26  ? 0.696   0.982   31.689  1.00 13.88  ? 26  GLU A O   1 
ATOM   199  C  CB  . GLU A 1 26  ? 2.983   2.623   32.546  1.00 21.64  ? 26  GLU A CB  1 
ATOM   200  C  CG  . GLU A 1 26  ? 4.409   2.860   33.092  1.00 26.14  ? 26  GLU A CG  1 
ATOM   201  C  CD  . GLU A 1 26  ? 5.047   1.589   33.622  1.00 42.36  ? 26  GLU A CD  1 
ATOM   202  O  OE1 . GLU A 1 26  ? 4.411   0.893   34.444  1.00 36.69  ? 26  GLU A OE1 1 
ATOM   203  O  OE2 . GLU A 1 26  ? 6.183   1.269   33.210  1.00 40.08  ? 26  GLU A OE2 1 
ATOM   204  N  N   A ARG A 1 27  ? 1.072   1.885   29.697  0.50 10.89  ? 27  ARG A N   1 
ATOM   205  N  N   B ARG A 1 27  ? 1.181   1.805   29.648  0.50 10.81  ? 27  ARG A N   1 
ATOM   206  C  CA  A ARG A 1 27  ? -0.334  1.658   29.279  0.50 9.85   ? 27  ARG A CA  1 
ATOM   207  C  CA  B ARG A 1 27  ? -0.220  1.733   29.206  0.50 11.80  ? 27  ARG A CA  1 
ATOM   208  C  C   A ARG A 1 27  ? -0.376  1.197   27.816  0.50 9.82   ? 27  ARG A C   1 
ATOM   209  C  C   B ARG A 1 27  ? -0.300  1.241   27.790  0.50 8.89   ? 27  ARG A C   1 
ATOM   210  O  O   A ARG A 1 27  ? -1.058  1.794   26.984  0.50 10.26  ? 27  ARG A O   1 
ATOM   211  O  O   B ARG A 1 27  ? -1.033  1.780   26.979  0.50 10.90  ? 27  ARG A O   1 
ATOM   212  C  CB  A ARG A 1 27  ? -1.258  2.859   29.599  0.50 11.99  ? 27  ARG A CB  1 
ATOM   213  C  CB  B ARG A 1 27  ? -0.856  3.126   29.303  0.50 12.86  ? 27  ARG A CB  1 
ATOM   214  C  CG  A ARG A 1 27  ? -0.848  4.254   29.006  0.50 11.43  ? 27  ARG A CG  1 
ATOM   215  C  CG  B ARG A 1 27  ? -0.646  3.880   30.606  0.50 15.51  ? 27  ARG A CG  1 
ATOM   216  C  CD  A ARG A 1 27  ? -1.773  5.489   29.223  0.50 14.71  ? 27  ARG A CD  1 
ATOM   217  C  CD  B ARG A 1 27  ? -1.305  5.245   30.565  0.50 18.30  ? 27  ARG A CD  1 
ATOM   218  N  NE  A ARG A 1 27  ? -2.978  5.332   28.402  0.50 14.47  ? 27  ARG A NE  1 
ATOM   219  N  NE  B ARG A 1 27  ? -0.882  6.037   31.717  0.50 16.25  ? 27  ARG A NE  1 
ATOM   220  C  CZ  A ARG A 1 27  ? -3.810  6.314   28.060  0.50 12.20  ? 27  ARG A CZ  1 
ATOM   221  C  CZ  B ARG A 1 27  ? 0.176   6.818   31.775  0.50 16.05  ? 27  ARG A CZ  1 
ATOM   222  N  NH1 A ARG A 1 27  ? -3.589  7.555   28.473  0.50 7.13   ? 27  ARG A NH1 1 
ATOM   223  N  NH1 B ARG A 1 27  ? 0.982   6.995   30.713  0.50 17.24  ? 27  ARG A NH1 1 
ATOM   224  N  NH2 A ARG A 1 27  ? -4.873  6.051   27.308  0.50 13.22  ? 27  ARG A NH2 1 
ATOM   225  N  NH2 B ARG A 1 27  ? 0.374   7.490   32.908  0.50 20.39  ? 27  ARG A NH2 1 
ATOM   226  N  N   . GLN A 1 28  ? 0.360   0.117   27.490  1.00 9.14   ? 28  GLN A N   1 
ATOM   227  C  CA  . GLN A 1 28  ? 0.401   -0.371  26.105  1.00 9.02   ? 28  GLN A CA  1 
ATOM   228  C  C   . GLN A 1 28  ? -0.758  -1.392  25.842  1.00 8.49   ? 28  GLN A C   1 
ATOM   229  O  O   . GLN A 1 28  ? -1.260  -2.035  26.762  1.00 9.94   ? 28  GLN A O   1 
ATOM   230  C  CB  . GLN A 1 28  ? 1.765   -1.058  25.816  1.00 10.05  ? 28  GLN A CB  1 
ATOM   231  C  CG  . GLN A 1 28  ? 2.871   -0.010  25.793  1.00 9.77   ? 28  GLN A CG  1 
ATOM   232  C  CD  . GLN A 1 28  ? 2.747   0.782   24.524  1.00 8.76   ? 28  GLN A CD  1 
ATOM   233  O  OE1 . GLN A 1 28  ? 2.912   0.258   23.436  1.00 9.40   ? 28  GLN A OE1 1 
ATOM   234  N  NE2 . GLN A 1 28  ? 2.365   2.078   24.626  1.00 10.12  ? 28  GLN A NE2 1 
ATOM   235  N  N   . SER A 1 29  ? -1.149  -1.454  24.581  1.00 7.96   ? 29  SER A N   1 
ATOM   236  C  CA  . SER A 1 29  ? -2.236  -2.324  24.147  1.00 7.81   ? 29  SER A CA  1 
ATOM   237  C  C   . SER A 1 29  ? -1.674  -3.141  22.984  1.00 8.49   ? 29  SER A C   1 
ATOM   238  O  O   . SER A 1 29  ? -0.739  -2.813  22.285  1.00 8.83   ? 29  SER A O   1 
ATOM   239  C  CB  . SER A 1 29  ? -3.366  -1.411  23.588  1.00 7.97   ? 29  SER A CB  1 
ATOM   240  O  OG  . SER A 1 29  ? -3.949  -0.704  24.646  1.00 8.63   ? 29  SER A OG  1 
ATOM   241  N  N   . PRO A 1 30  ? -2.363  -4.293  22.700  1.00 8.02   ? 30  PRO A N   1 
ATOM   242  C  CA  . PRO A 1 30  ? -3.525  -4.827  23.400  1.00 8.32   ? 30  PRO A CA  1 
ATOM   243  C  C   . PRO A 1 30  ? -3.107  -5.506  24.724  1.00 8.86   ? 30  PRO A C   1 
ATOM   244  O  O   . PRO A 1 30  ? -1.925  -5.574  25.071  1.00 9.15   ? 30  PRO A O   1 
ATOM   245  C  CB  . PRO A 1 30  ? -4.059  -5.898  22.401  1.00 8.37   ? 30  PRO A CB  1 
ATOM   246  C  CG  . PRO A 1 30  ? -2.787  -6.454  21.800  1.00 8.23   ? 30  PRO A CG  1 
ATOM   247  C  CD  . PRO A 1 30  ? -1.903  -5.226  21.624  1.00 8.50   ? 30  PRO A CD  1 
ATOM   248  N  N   . VAL A 1 31  ? -4.079  -6.103  25.401  1.00 8.20   ? 31  VAL A N   1 
ATOM   249  C  CA  . VAL A 1 31  ? -3.930  -6.832  26.620  1.00 9.67   ? 31  VAL A CA  1 
ATOM   250  C  C   . VAL A 1 31  ? -4.804  -8.063  26.601  1.00 8.73   ? 31  VAL A C   1 
ATOM   251  O  O   . VAL A 1 31  ? -5.755  -8.124  25.827  1.00 10.11  ? 31  VAL A O   1 
ATOM   252  C  CB  . VAL A 1 31  ? -4.241  -6.018  27.932  1.00 9.66   ? 31  VAL A CB  1 
ATOM   253  C  CG1 . VAL A 1 31  ? -3.265  -4.800  28.028  1.00 10.78  ? 31  VAL A CG1 1 
ATOM   254  C  CG2 . VAL A 1 31  ? -5.726  -5.558  27.933  1.00 11.15  ? 31  VAL A CG2 1 
ATOM   255  N  N   . ASP A 1 32  ? -4.446  -9.043  27.436  1.00 9.62   ? 32  ASP A N   1 
ATOM   256  C  CA  . ASP A 1 32  ? -5.369  -10.109 27.741  1.00 10.16  ? 32  ASP A CA  1 
ATOM   257  C  C   . ASP A 1 32  ? -6.441  -9.583  28.702  1.00 9.76   ? 32  ASP A C   1 
ATOM   258  O  O   . ASP A 1 32  ? -6.141  -8.983  29.729  1.00 11.64  ? 32  ASP A O   1 
ATOM   259  C  CB  . ASP A 1 32  ? -4.624  -11.302 28.387  1.00 12.20  ? 32  ASP A CB  1 
ATOM   260  C  CG  . ASP A 1 32  ? -5.569  -12.477 28.656  1.00 11.74  ? 32  ASP A CG  1 
ATOM   261  O  OD1 . ASP A 1 32  ? -6.292  -12.895 27.714  1.00 11.85  ? 32  ASP A OD1 1 
ATOM   262  O  OD2 . ASP A 1 32  ? -5.579  -12.908 29.835  1.00 16.30  ? 32  ASP A OD2 1 
ATOM   263  N  N   . ILE A 1 33  ? -7.697  -9.880  28.380  1.00 9.80   ? 33  ILE A N   1 
ATOM   264  C  CA  . ILE A 1 33  ? -8.814  -9.446  29.245  1.00 9.97   ? 33  ILE A CA  1 
ATOM   265  C  C   . ILE A 1 33  ? -9.126  -10.685 30.102  1.00 11.86  ? 33  ILE A C   1 
ATOM   266  O  O   . ILE A 1 33  ? -9.690  -11.680 29.612  1.00 13.62  ? 33  ILE A O   1 
ATOM   267  C  CB  . ILE A 1 33  ? -10.028 -9.073  28.389  1.00 11.58  ? 33  ILE A CB  1 
ATOM   268  C  CG1 . ILE A 1 33  ? -9.623  -7.833  27.530  1.00 11.68  ? 33  ILE A CG1 1 
ATOM   269  C  CG2 . ILE A 1 33  ? -11.198 -8.700  29.289  1.00 13.80  ? 33  ILE A CG2 1 
ATOM   270  C  CD1 . ILE A 1 33  ? -10.659 -7.586  26.451  1.00 12.05  ? 33  ILE A CD1 1 
ATOM   271  N  N   . ASP A 1 34  ? -8.723  -10.636 31.362  1.00 13.24  ? 34  ASP A N   1 
ATOM   272  C  CA  . ASP A 1 34  ? -9.052  -11.728 32.355  1.00 13.98  ? 34  ASP A CA  1 
ATOM   273  C  C   . ASP A 1 34  ? -10.444 -11.327 32.833  1.00 15.90  ? 34  ASP A C   1 
ATOM   274  O  O   . ASP A 1 34  ? -10.660 -10.340 33.610  1.00 17.69  ? 34  ASP A O   1 
ATOM   275  C  CB  . ASP A 1 34  ? -8.012  -11.711 33.472  1.00 17.00  ? 34  ASP A CB  1 
ATOM   276  C  CG  . ASP A 1 34  ? -8.312  -12.731 34.593  1.00 21.11  ? 34  ASP A CG  1 
ATOM   277  O  OD1 . ASP A 1 34  ? -7.364  -13.168 35.256  1.00 30.67  ? 34  ASP A OD1 1 
ATOM   278  O  OD2 . ASP A 1 34  ? -9.445  -13.054 34.851  1.00 23.21  ? 34  ASP A OD2 1 
ATOM   279  N  N   . THR A 1 35  ? -11.428 -12.132 32.427  1.00 14.94  ? 35  THR A N   1 
ATOM   280  C  CA  . THR A 1 35  ? -12.813 -11.772 32.650  1.00 16.44  ? 35  THR A CA  1 
ATOM   281  C  C   . THR A 1 35  ? -13.202 -11.906 34.097  1.00 18.11  ? 35  THR A C   1 
ATOM   282  O  O   . THR A 1 35  ? -14.180 -11.336 34.522  1.00 19.82  ? 35  THR A O   1 
ATOM   283  C  CB  . THR A 1 35  ? -13.736 -12.659 31.798  1.00 18.27  ? 35  THR A CB  1 
ATOM   284  O  OG1 . THR A 1 35  ? -13.663 -14.032 32.223  1.00 18.47  ? 35  THR A OG1 1 
ATOM   285  C  CG2 . THR A 1 35  ? -13.403 -12.534 30.284  1.00 21.01  ? 35  THR A CG2 1 
ATOM   286  N  N   . HIS A 1 36  ? -12.415 -12.685 34.859  1.00 21.60  ? 36  HIS A N   1 
ATOM   287  C  CA  . HIS A 1 36  ? -12.657 -12.931 36.291  1.00 24.02  ? 36  HIS A CA  1 
ATOM   288  C  C   . HIS A 1 36  ? -12.116 -11.906 37.194  1.00 28.52  ? 36  HIS A C   1 
ATOM   289  O  O   . HIS A 1 36  ? -12.588 -11.774 38.344  1.00 41.65  ? 36  HIS A O   1 
ATOM   290  C  CB  . HIS A 1 36  ? -12.119 -14.283 36.718  1.00 24.57  ? 36  HIS A CB  1 
ATOM   291  C  CG  . HIS A 1 36  ? -12.520 -15.402 35.786  1.00 22.47  ? 36  HIS A CG  1 
ATOM   292  N  ND1 . HIS A 1 36  ? -13.758 -15.930 35.781  1.00 21.72  ? 36  HIS A ND1 1 
ATOM   293  C  CD2 . HIS A 1 36  ? -11.807 -16.063 34.788  1.00 31.39  ? 36  HIS A CD2 1 
ATOM   294  C  CE1 . HIS A 1 36  ? -13.832 -16.891 34.842  1.00 26.56  ? 36  HIS A CE1 1 
ATOM   295  N  NE2 . HIS A 1 36  ? -12.637 -16.972 34.234  1.00 31.11  ? 36  HIS A NE2 1 
ATOM   296  N  N   . THR A 1 37  ? -11.136 -11.156 36.713  1.00 24.79  ? 37  THR A N   1 
ATOM   297  C  CA  . THR A 1 37  ? -10.625 -10.090 37.533  1.00 25.14  ? 37  THR A CA  1 
ATOM   298  C  C   . THR A 1 37  ? -11.160 -8.725  37.054  1.00 19.76  ? 37  THR A C   1 
ATOM   299  O  O   . THR A 1 37  ? -10.944 -7.751  37.730  1.00 25.19  ? 37  THR A O   1 
ATOM   300  C  CB  . THR A 1 37  ? -9.101  -10.140 37.672  1.00 31.30  ? 37  THR A CB  1 
ATOM   301  O  OG1 . THR A 1 37  ? -8.559  -10.096 36.381  1.00 30.41  ? 37  THR A OG1 1 
ATOM   302  C  CG2 . THR A 1 37  ? -8.705  -11.451 38.312  1.00 29.16  ? 37  THR A CG2 1 
ATOM   303  N  N   . ALA A 1 38  ? -11.807 -8.656  35.877  1.00 18.65  ? 38  ALA A N   1 
ATOM   304  C  CA  . ALA A 1 38  ? -12.409 -7.388  35.439  1.00 16.91  ? 38  ALA A CA  1 
ATOM   305  C  C   . ALA A 1 38  ? -13.458 -6.961  36.505  1.00 18.60  ? 38  ALA A C   1 
ATOM   306  O  O   . ALA A 1 38  ? -14.108 -7.784  37.157  1.00 19.69  ? 38  ALA A O   1 
ATOM   307  C  CB  . ALA A 1 38  ? -12.991 -7.512  34.020  1.00 17.39  ? 38  ALA A CB  1 
ATOM   308  N  N   . LYS A 1 39  ? -13.568 -5.667  36.736  1.00 17.10  ? 39  LYS A N   1 
ATOM   309  C  CA  . LYS A 1 39  ? -14.438 -5.115  37.795  1.00 16.96  ? 39  LYS A CA  1 
ATOM   310  C  C   . LYS A 1 39  ? -15.728 -4.645  37.116  1.00 15.60  ? 39  LYS A C   1 
ATOM   311  O  O   . LYS A 1 39  ? -15.671 -3.738  36.292  1.00 15.21  ? 39  LYS A O   1 
ATOM   312  C  CB  . LYS A 1 39  ? -13.680 -3.943  38.444  1.00 20.14  ? 39  LYS A CB  1 
ATOM   313  C  CG  . LYS A 1 39  ? -14.443 -3.093  39.425  1.00 22.32  ? 39  LYS A CG  1 
ATOM   314  C  CD  . LYS A 1 39  ? -14.818 -3.792  40.752  1.00 24.58  ? 39  LYS A CD  1 
ATOM   315  C  CE  . LYS A 1 39  ? -15.537 -2.861  41.710  1.00 27.43  ? 39  LYS A CE  1 
ATOM   316  N  NZ  . LYS A 1 39  ? -15.941 -3.633  42.928  1.00 25.40  ? 39  LYS A NZ  1 
ATOM   317  N  N   . TYR A 1 40  ? -16.858 -5.215  37.499  1.00 19.29  ? 40  TYR A N   1 
ATOM   318  C  CA  . TYR A 1 40  ? -18.138 -4.669  37.066  1.00 19.23  ? 40  TYR A CA  1 
ATOM   319  C  C   . TYR A 1 40  ? -18.326 -3.310  37.697  1.00 18.12  ? 40  TYR A C   1 
ATOM   320  O  O   . TYR A 1 40  ? -18.210 -3.162  38.929  1.00 23.23  ? 40  TYR A O   1 
ATOM   321  C  CB  . TYR A 1 40  ? -19.276 -5.553  37.536  1.00 23.27  ? 40  TYR A CB  1 
ATOM   322  C  CG  . TYR A 1 40  ? -20.621 -4.914  37.354  1.00 21.50  ? 40  TYR A CG  1 
ATOM   323  C  CD1 . TYR A 1 40  ? -21.113 -4.566  36.076  1.00 18.51  ? 40  TYR A CD1 1 
ATOM   324  C  CD2 . TYR A 1 40  ? -21.500 -4.716  38.452  1.00 29.31  ? 40  TYR A CD2 1 
ATOM   325  C  CE1 . TYR A 1 40  ? -22.369 -3.997  35.896  1.00 25.38  ? 40  TYR A CE1 1 
ATOM   326  C  CE2 . TYR A 1 40  ? -22.801 -4.154  38.265  1.00 32.89  ? 40  TYR A CE2 1 
ATOM   327  C  CZ  . TYR A 1 40  ? -23.220 -3.812  36.989  1.00 33.50  ? 40  TYR A CZ  1 
ATOM   328  O  OH  . TYR A 1 40  ? -24.483 -3.271  36.822  1.00 42.25  ? 40  TYR A OH  1 
ATOM   329  N  N   . ASP A 1 41  ? -18.576 -2.324  36.867  1.00 17.60  ? 41  ASP A N   1 
ATOM   330  C  CA  . ASP A 1 41  ? -18.767 -0.947  37.368  1.00 19.61  ? 41  ASP A CA  1 
ATOM   331  C  C   . ASP A 1 41  ? -20.189 -0.485  37.064  1.00 21.17  ? 41  ASP A C   1 
ATOM   332  O  O   . ASP A 1 41  ? -20.452 -0.071  35.948  1.00 22.34  ? 41  ASP A O   1 
ATOM   333  C  CB  . ASP A 1 41  ? -17.708 -0.022  36.801  1.00 23.06  ? 41  ASP A CB  1 
ATOM   334  C  CG  . ASP A 1 41  ? -17.789 1.349   37.350  1.00 27.15  ? 41  ASP A CG  1 
ATOM   335  O  OD1 . ASP A 1 41  ? -18.781 1.656   38.073  1.00 31.87  ? 41  ASP A OD1 1 
ATOM   336  O  OD2 . ASP A 1 41  ? -16.821 2.087   37.085  1.00 28.88  ? 41  ASP A OD2 1 
ATOM   337  N  N   . PRO A 1 42  ? -21.109 -0.604  38.055  1.00 28.64  ? 42  PRO A N   1 
ATOM   338  C  CA  . PRO A 1 42  ? -22.510 -0.191  37.781  1.00 25.06  ? 42  PRO A CA  1 
ATOM   339  C  C   . PRO A 1 42  ? -22.668 1.314   37.459  1.00 28.25  ? 42  PRO A C   1 
ATOM   340  O  O   . PRO A 1 42  ? -23.737 1.767   37.002  1.00 41.38  ? 42  PRO A O   1 
ATOM   341  C  CB  . PRO A 1 42  ? -23.240 -0.551  39.098  1.00 32.24  ? 42  PRO A CB  1 
ATOM   342  C  CG  . PRO A 1 42  ? -22.168 -0.560  40.159  1.00 37.21  ? 42  PRO A CG  1 
ATOM   343  C  CD  . PRO A 1 42  ? -20.907 -1.069  39.465  1.00 29.41  ? 42  PRO A CD  1 
ATOM   344  N  N   . SER A 1 43  ? -21.612 2.091   37.718  1.00 28.25  ? 43  SER A N   1 
ATOM   345  C  CA  . SER A 1 43  ? -21.632 3.520   37.397  1.00 33.46  ? 43  SER A CA  1 
ATOM   346  C  C   . SER A 1 43  ? -21.274 3.852   35.885  1.00 29.62  ? 43  SER A C   1 
ATOM   347  O  O   . SER A 1 43  ? -21.439 5.012   35.439  1.00 35.49  ? 43  SER A O   1 
ATOM   348  C  CB  . SER A 1 43  ? -20.702 4.256   38.351  1.00 36.10  ? 43  SER A CB  1 
ATOM   349  O  OG  . SER A 1 43  ? -19.415 4.332   37.803  1.00 34.25  ? 43  SER A OG  1 
ATOM   350  N  N   . LEU A 1 44  ? -20.798 2.860   35.112  1.00 26.89  ? 44  LEU A N   1 
ATOM   351  C  CA  . LEU A 1 44  ? -20.573 3.010   33.661  1.00 22.71  ? 44  LEU A CA  1 
ATOM   352  C  C   . LEU A 1 44  ? -21.883 3.151   32.920  1.00 29.08  ? 44  LEU A C   1 
ATOM   353  O  O   . LEU A 1 44  ? -22.874 2.441   33.186  1.00 30.26  ? 44  LEU A O   1 
ATOM   354  C  CB  . LEU A 1 44  ? -19.746 1.872   33.072  1.00 24.31  ? 44  LEU A CB  1 
ATOM   355  C  CG  . LEU A 1 44  ? -18.245 1.762   33.343  1.00 20.21  ? 44  LEU A CG  1 
ATOM   356  C  CD1 . LEU A 1 44  ? -17.793 0.363   32.919  1.00 20.36  ? 44  LEU A CD1 1 
ATOM   357  C  CD2 . LEU A 1 44  ? -17.496 2.834   32.595  1.00 18.43  ? 44  LEU A CD2 1 
ATOM   358  N  N   . LYS A 1 45  ? -21.820 3.999   31.919  1.00 31.08  ? 45  LYS A N   1 
ATOM   359  C  CA  . LYS A 1 45  ? -23.000 4.212   31.104  1.00 28.52  ? 45  LYS A CA  1 
ATOM   360  C  C   . LYS A 1 45  ? -23.108 3.248   29.949  1.00 25.85  ? 45  LYS A C   1 
ATOM   361  O  O   . LYS A 1 45  ? -22.095 2.552   29.567  1.00 30.83  ? 45  LYS A O   1 
ATOM   362  C  CB  . LYS A 1 45  ? -23.065 5.627   30.626  1.00 25.03  ? 45  LYS A CB  1 
ATOM   363  C  CG  . LYS A 1 45  ? -23.090 6.600   31.775  1.00 26.66  ? 45  LYS A CG  1 
ATOM   364  C  CD  . LYS A 1 45  ? -23.054 8.009   31.278  1.00 39.77  ? 45  LYS A CD  1 
ATOM   365  C  CE  . LYS A 1 45  ? -23.726 8.897   32.319  1.00 65.96  ? 45  LYS A CE  1 
ATOM   366  N  NZ  . LYS A 1 45  ? -23.487 8.430   33.724  1.00 66.68  ? 45  LYS A NZ  1 
ATOM   367  N  N   . PRO A 1 46  ? -24.357 3.151   29.406  1.00 21.56  ? 46  PRO A N   1 
ATOM   368  C  CA  . PRO A 1 46  ? -24.420 2.446   28.133  1.00 25.10  ? 46  PRO A CA  1 
ATOM   369  C  C   . PRO A 1 46  ? -23.619 3.300   27.166  1.00 17.25  ? 46  PRO A C   1 
ATOM   370  O  O   . PRO A 1 46  ? -23.500 4.558   27.299  1.00 21.93  ? 46  PRO A O   1 
ATOM   371  C  CB  . PRO A 1 46  ? -25.926 2.437   27.746  1.00 21.75  ? 46  PRO A CB  1 
ATOM   372  C  CG  . PRO A 1 46  ? -26.658 2.767   28.976  1.00 27.44  ? 46  PRO A CG  1 
ATOM   373  C  CD  . PRO A 1 46  ? -25.699 3.643   29.796  1.00 26.80  ? 46  PRO A CD  1 
ATOM   374  N  N   . LEU A 1 47  ? -22.937 2.571   26.290  1.00 18.42  ? 47  LEU A N   1 
ATOM   375  C  CA  . LEU A 1 47  ? -22.262 3.151   25.187  1.00 16.37  ? 47  LEU A CA  1 
ATOM   376  C  C   . LEU A 1 47  ? -23.315 3.707   24.225  1.00 17.34  ? 47  LEU A C   1 
ATOM   377  O  O   . LEU A 1 47  ? -24.246 2.994   23.899  1.00 22.51  ? 47  LEU A O   1 
ATOM   378  C  CB  . LEU A 1 47  ? -21.342 2.093   24.571  1.00 21.97  ? 47  LEU A CB  1 
ATOM   379  C  CG  . LEU A 1 47  ? -20.449 2.428   23.437  1.00 25.57  ? 47  LEU A CG  1 
ATOM   380  C  CD1 . LEU A 1 47  ? -19.760 1.185   22.952  1.00 32.36  ? 47  LEU A CD1 1 
ATOM   381  C  CD2 . LEU A 1 47  ? -21.260 3.013   22.288  1.00 46.99  ? 47  LEU A CD2 1 
ATOM   382  N  N   . SER A 1 48  ? -23.119 4.960   23.771  1.00 13.75  ? 48  SER A N   1 
ATOM   383  C  CA  . SER A 1 48  ? -23.941 5.503   22.684  1.00 14.06  ? 48  SER A CA  1 
ATOM   384  C  C   . SER A 1 48  ? -23.178 5.473   21.370  1.00 13.79  ? 48  SER A C   1 
ATOM   385  O  O   . SER A 1 48  ? -22.128 6.135   21.231  1.00 13.60  ? 48  SER A O   1 
ATOM   386  C  CB  . SER A 1 48  ? -24.312 6.959   23.064  1.00 17.95  ? 48  SER A CB  1 
ATOM   387  O  OG  . SER A 1 48  ? -24.932 7.633   21.974  1.00 20.31  ? 48  SER A OG  1 
ATOM   388  N  N   . VAL A 1 49  ? -23.692 4.705   20.418  1.00 16.24  ? 49  VAL A N   1 
ATOM   389  C  CA  . VAL A 1 49  ? -23.092 4.656   19.111  1.00 16.35  ? 49  VAL A CA  1 
ATOM   390  C  C   . VAL A 1 49  ? -24.049 5.249   18.134  1.00 17.93  ? 49  VAL A C   1 
ATOM   391  O  O   . VAL A 1 49  ? -25.134 4.669   17.936  1.00 25.94  ? 49  VAL A O   1 
ATOM   392  C  CB  . VAL A 1 49  ? -22.835 3.186   18.680  1.00 20.84  ? 49  VAL A CB  1 
ATOM   393  C  CG1 . VAL A 1 49  ? -22.264 3.172   17.278  1.00 22.60  ? 49  VAL A CG1 1 
ATOM   394  C  CG2 . VAL A 1 49  ? -21.988 2.431   19.691  1.00 22.31  ? 49  VAL A CG2 1 
ATOM   395  N  N   . SER A 1 50  ? -23.696 6.378   17.518  1.00 16.36  ? 50  SER A N   1 
ATOM   396  C  CA  . SER A 1 50  ? -24.641 7.123   16.639  1.00 17.96  ? 50  SER A CA  1 
ATOM   397  C  C   . SER A 1 50  ? -24.035 7.210   15.238  1.00 15.93  ? 50  SER A C   1 
ATOM   398  O  O   . SER A 1 50  ? -23.327 8.155   14.936  1.00 14.97  ? 50  SER A O   1 
ATOM   399  C  CB  . SER A 1 50  ? -24.984 8.536   17.156  1.00 21.17  ? 50  SER A CB  1 
ATOM   400  O  OG  . SER A 1 50  ? -25.595 8.454   18.424  1.00 27.48  ? 50  SER A OG  1 
ATOM   401  N  N   . TYR A 1 51  ? -24.272 6.188   14.437  1.00 15.32  ? 51  TYR A N   1 
ATOM   402  C  CA  . TYR A 1 51  ? -23.707 6.025   13.136  1.00 14.73  ? 51  TYR A CA  1 
ATOM   403  C  C   . TYR A 1 51  ? -24.675 6.240   11.953  1.00 13.55  ? 51  TYR A C   1 
ATOM   404  O  O   . TYR A 1 51  ? -24.323 5.945   10.819  1.00 14.02  ? 51  TYR A O   1 
ATOM   405  C  CB  . TYR A 1 51  ? -23.131 4.607   13.005  1.00 13.99  ? 51  TYR A CB  1 
ATOM   406  C  CG  . TYR A 1 51  ? -21.825 4.317   13.764  1.00 12.54  ? 51  TYR A CG  1 
ATOM   407  C  CD1 . TYR A 1 51  ? -21.106 5.307   14.431  1.00 12.79  ? 51  TYR A CD1 1 
ATOM   408  C  CD2 . TYR A 1 51  ? -21.299 3.034   13.748  1.00 11.82  ? 51  TYR A CD2 1 
ATOM   409  C  CE1 . TYR A 1 51  ? -19.918 5.003   15.086  1.00 11.78  ? 51  TYR A CE1 1 
ATOM   410  C  CE2 . TYR A 1 51  ? -20.116 2.726   14.398  1.00 11.58  ? 51  TYR A CE2 1 
ATOM   411  C  CZ  . TYR A 1 51  ? -19.416 3.721   15.049  1.00 12.46  ? 51  TYR A CZ  1 
ATOM   412  O  OH  . TYR A 1 51  ? -18.225 3.360   15.701  1.00 12.11  ? 51  TYR A OH  1 
ATOM   413  N  N   . ASP A 1 52  ? -25.853 6.747   12.262  1.00 16.48  ? 52  ASP A N   1 
ATOM   414  C  CA  . ASP A 1 52  ? -26.865 6.969   11.194  1.00 16.79  ? 52  ASP A CA  1 
ATOM   415  C  C   . ASP A 1 52  ? -26.423 7.872   10.016  1.00 17.52  ? 52  ASP A C   1 
ATOM   416  O  O   . ASP A 1 52  ? -26.792 7.619   8.858   1.00 19.15  ? 52  ASP A O   1 
ATOM   417  C  CB  . ASP A 1 52  ? -28.212 7.427   11.723  1.00 21.34  ? 52  ASP A CB  1 
ATOM   418  C  CG  . ASP A 1 52  ? -28.087 8.512   12.830  1.00 36.59  ? 52  ASP A CG  1 
ATOM   419  O  OD1 . ASP A 1 52  ? -27.384 8.223   13.857  1.00 46.48  ? 52  ASP A OD1 1 
ATOM   420  O  OD2 . ASP A 1 52  ? -28.695 9.623   12.689  1.00 48.01  ? 52  ASP A OD2 1 
ATOM   421  N  N   . GLN A 1 53  ? -25.617 8.874   10.292  1.00 16.95  ? 53  GLN A N   1 
ATOM   422  C  CA  . GLN A 1 53  ? -25.200 9.833   9.245   1.00 15.19  ? 53  GLN A CA  1 
ATOM   423  C  C   . GLN A 1 53  ? -23.761 9.594   8.804   1.00 12.78  ? 53  GLN A C   1 
ATOM   424  O  O   . GLN A 1 53  ? -23.148 10.453  8.146   1.00 14.13  ? 53  GLN A O   1 
ATOM   425  C  CB  . GLN A 1 53  ? -25.343 11.277  9.751   1.00 16.14  ? 53  GLN A CB  1 
ATOM   426  C  CG  . GLN A 1 53  ? -26.829 11.650  9.977   1.00 20.33  ? 53  GLN A CG  1 
ATOM   427  C  CD  . GLN A 1 53  ? -27.683 11.401  8.730   1.00 23.73  ? 53  GLN A CD  1 
ATOM   428  O  OE1 . GLN A 1 53  ? -28.688 10.656  8.782   1.00 36.72  ? 53  GLN A OE1 1 
ATOM   429  N  NE2 . GLN A 1 53  ? -27.251 11.945  7.561   1.00 21.09  ? 53  GLN A NE2 1 
ATOM   430  N  N   . ALA A 1 54  ? -23.236 8.415   9.078   1.00 12.97  ? 54  ALA A N   1 
ATOM   431  C  CA  . ALA A 1 54  ? -21.846 8.168   8.695   1.00 12.53  ? 54  ALA A CA  1 
ATOM   432  C  C   . ALA A 1 54  ? -21.663 8.314   7.181   1.00 11.43  ? 54  ALA A C   1 
ATOM   433  O  O   . ALA A 1 54  ? -22.525 7.875   6.333   1.00 14.00  ? 54  ALA A O   1 
ATOM   434  C  CB  . ALA A 1 54  ? -21.447 6.787   9.164   1.00 13.65  ? 54  ALA A CB  1 
ATOM   435  N  N   . THR A 1 55  ? -20.503 8.861   6.810   1.00 11.11  ? 55  THR A N   1 
ATOM   436  C  CA  . THR A 1 55  ? -20.134 9.017   5.424   1.00 11.04  ? 55  THR A CA  1 
ATOM   437  C  C   . THR A 1 55  ? -18.754 8.367   5.200   1.00 9.68   ? 55  THR A C   1 
ATOM   438  O  O   . THR A 1 55  ? -17.703 8.979   5.426   1.00 10.63  ? 55  THR A O   1 
ATOM   439  C  CB  . THR A 1 55  ? -20.039 10.532  5.018   1.00 11.72  ? 55  THR A CB  1 
ATOM   440  O  OG1 . THR A 1 55  ? -21.331 11.075  5.110   1.00 13.03  ? 55  THR A OG1 1 
ATOM   441  C  CG2 . THR A 1 55  ? -19.579 10.707  3.515   1.00 12.65  ? 55  THR A CG2 1 
ATOM   442  N  N   . SER A 1 56  ? -18.769 7.148   4.662   1.00 8.95   ? 56  SER A N   1 
ATOM   443  C  CA  . SER A 1 56  ? -17.527 6.526   4.249   1.00 9.48   ? 56  SER A CA  1 
ATOM   444  C  C   . SER A 1 56  ? -17.015 7.223   2.985   1.00 10.18  ? 56  SER A C   1 
ATOM   445  O  O   . SER A 1 56  ? -17.848 7.644   2.151   1.00 9.80   ? 56  SER A O   1 
ATOM   446  C  CB  . SER A 1 56  ? -17.668 5.012   4.063   1.00 9.49   ? 56  SER A CB  1 
ATOM   447  O  OG  . SER A 1 56  ? -18.472 4.713   2.946   1.00 9.84   ? 56  SER A OG  1 
ATOM   448  N  N   . LEU A 1 57  ? -15.694 7.246   2.786   1.00 9.96   ? 57  LEU A N   1 
ATOM   449  C  CA  . LEU A 1 57  ? -15.122 7.911   1.642   1.00 9.65   ? 57  LEU A CA  1 
ATOM   450  C  C   . LEU A 1 57  ? -14.289 6.985   0.753   1.00 9.35   ? 57  LEU A C   1 
ATOM   451  O  O   . LEU A 1 57  ? -14.479 6.968   -0.458  1.00 11.20  ? 57  LEU A O   1 
ATOM   452  C  CB  . LEU A 1 57  ? -14.273 9.136   2.022   1.00 12.52  ? 57  LEU A CB  1 
ATOM   453  C  CG  . LEU A 1 57  ? -15.093 10.308  2.581   1.00 13.29  ? 57  LEU A CG  1 
ATOM   454  C  CD1 . LEU A 1 57  ? -14.206 11.398  3.132   1.00 15.88  ? 57  LEU A CD1 1 
ATOM   455  C  CD2 . LEU A 1 57  ? -16.087 10.917  1.557   1.00 15.89  ? 57  LEU A CD2 1 
ATOM   456  N  N   . ARG A 1 58  ? -13.313 6.288   1.347   1.00 10.24  ? 58  ARG A N   1 
ATOM   457  C  CA  . ARG A 1 58  ? -12.320 5.582   0.563   1.00 10.17  ? 58  ARG A CA  1 
ATOM   458  C  C   . ARG A 1 58  ? -11.855 4.372   1.378   1.00 9.70   ? 58  ARG A C   1 
ATOM   459  O  O   . ARG A 1 58  ? -11.983 4.332   2.580   1.00 10.46  ? 58  ARG A O   1 
ATOM   460  C  CB  . ARG A 1 58  ? -11.092 6.455   0.243   1.00 12.90  ? 58  ARG A CB  1 
ATOM   461  C  CG  . ARG A 1 58  ? -11.391 7.676   -0.675  1.00 16.23  ? 58  ARG A CG  1 
ATOM   462  C  CD  . ARG A 1 58  ? -10.081 8.325   -1.169  1.00 17.70  ? 58  ARG A CD  1 
ATOM   463  N  NE  . ARG A 1 58  ? -9.331  7.421   -2.027  1.00 17.69  ? 58  ARG A NE  1 
ATOM   464  C  CZ  . ARG A 1 58  ? -9.669  7.180   -3.295  1.00 18.82  ? 58  ARG A CZ  1 
ATOM   465  N  NH1 . ARG A 1 58  ? -10.716 7.820   -3.845  1.00 26.52  ? 58  ARG A NH1 1 
ATOM   466  N  NH2 . ARG A 1 58  ? -8.913  6.404   -4.063  1.00 19.70  ? 58  ARG A NH2 1 
ATOM   467  N  N   . ILE A 1 59  ? -11.231 3.412   0.670   1.00 9.58   ? 59  ILE A N   1 
ATOM   468  C  CA  . ILE A 1 59  ? -10.599 2.227   1.305   1.00 9.65   ? 59  ILE A CA  1 
ATOM   469  C  C   . ILE A 1 59  ? -9.159  2.172   0.716   1.00 9.47   ? 59  ILE A C   1 
ATOM   470  O  O   . ILE A 1 59  ? -8.946  2.388   -0.445  1.00 10.27  ? 59  ILE A O   1 
ATOM   471  C  CB  . ILE A 1 59  ? -11.456 0.949   1.023   1.00 10.33  ? 59  ILE A CB  1 
ATOM   472  C  CG1 . ILE A 1 59  ? -10.947 -0.223  1.893   1.00 10.65  ? 59  ILE A CG1 1 
ATOM   473  C  CG2 . ILE A 1 59  ? -11.504 0.577   -0.474  1.00 11.42  ? 59  ILE A CG2 1 
ATOM   474  C  CD1 . ILE A 1 59  ? -11.843 -1.461  1.803   1.00 11.73  ? 59  ILE A CD1 1 
ATOM   475  N  N   . LEU A 1 60  ? -8.203  1.845   1.619   1.00 11.17  ? 60  LEU A N   1 
ATOM   476  C  CA  . LEU A 1 60  ? -6.784  1.934   1.238   1.00 12.87  ? 60  LEU A CA  1 
ATOM   477  C  C   . LEU A 1 60  ? -6.073  0.683   1.861   1.00 10.94  ? 60  LEU A C   1 
ATOM   478  O  O   . LEU A 1 60  ? -6.344  0.341   3.014   1.00 13.03  ? 60  LEU A O   1 
ATOM   479  C  CB  . LEU A 1 60  ? -6.154  3.275   1.862   1.00 18.52  ? 60  LEU A CB  1 
ATOM   480  C  CG  . LEU A 1 60  ? -4.616  3.349   2.019   1.00 22.80  ? 60  LEU A CG  1 
ATOM   481  C  CD1 . LEU A 1 60  ? -3.976  3.500   0.635   1.00 25.30  ? 60  LEU A CD1 1 
ATOM   482  C  CD2 . LEU A 1 60  ? -4.243  4.453   2.946   1.00 29.06  ? 60  LEU A CD2 1 
ATOM   483  N  N   . ASN A 1 61  ? -5.127  0.136   1.121   1.00 10.80  ? 61  ASN A N   1 
ATOM   484  C  CA  . ASN A 1 61  ? -4.131  -0.850  1.674   1.00 11.60  ? 61  ASN A CA  1 
ATOM   485  C  C   . ASN A 1 61  ? -2.878  0.015   2.004   1.00 10.38  ? 61  ASN A C   1 
ATOM   486  O  O   . ASN A 1 61  ? -2.270  0.566   1.109   1.00 12.20  ? 61  ASN A O   1 
ATOM   487  C  CB  . ASN A 1 61  ? -3.816  -1.878  0.579   1.00 12.14  ? 61  ASN A CB  1 
ATOM   488  C  CG  . ASN A 1 61  ? -2.766  -2.874  0.966   1.00 11.32  ? 61  ASN A CG  1 
ATOM   489  O  OD1 . ASN A 1 61  ? -1.905  -2.547  1.826   1.00 13.78  ? 61  ASN A OD1 1 
ATOM   490  N  ND2 . ASN A 1 61  ? -2.784  -4.084  0.389   1.00 12.33  ? 61  ASN A ND2 1 
ATOM   491  N  N   . ASN A 1 62  ? -2.560  0.093   3.292   1.00 11.36  ? 62  ASN A N   1 
ATOM   492  C  CA  . ASN A 1 62  ? -1.395  0.929   3.695   1.00 12.64  ? 62  ASN A CA  1 
ATOM   493  C  C   . ASN A 1 62  ? -0.134  0.058   3.956   1.00 13.58  ? 62  ASN A C   1 
ATOM   494  O  O   . ASN A 1 62  ? 0.841   0.551   4.557   1.00 18.02  ? 62  ASN A O   1 
ATOM   495  C  CB  . ASN A 1 62  ? -1.810  1.800   4.905   1.00 13.36  ? 62  ASN A CB  1 
ATOM   496  C  CG  . ASN A 1 62  ? -2.044  0.974   6.149   1.00 14.85  ? 62  ASN A CG  1 
ATOM   497  O  OD1 . ASN A 1 62  ? -1.844  -0.243  6.156   1.00 14.16  ? 62  ASN A OD1 1 
ATOM   498  N  ND2 . ASN A 1 62  ? -2.485  1.623   7.217   1.00 22.00  ? 62  ASN A ND2 1 
ATOM   499  N  N   . GLY A 1 63  ? -0.138  -1.193  3.550   1.00 13.32  ? 63  GLY A N   1 
ATOM   500  C  CA  . GLY A 1 63  ? 1.035   -2.027  3.741   1.00 16.57  ? 63  GLY A CA  1 
ATOM   501  C  C   . GLY A 1 63  ? 1.038   -2.803  5.061   1.00 13.58  ? 63  GLY A C   1 
ATOM   502  O  O   . GLY A 1 63  ? 1.887   -3.686  5.247   1.00 17.16  ? 63  GLY A O   1 
ATOM   503  N  N   A HIS A 1 64  ? 0.102   -2.455  5.958   0.50 13.27  ? 64  HIS A N   1 
ATOM   504  N  N   B HIS A 1 64  ? 0.087   -2.545  5.958   0.50 13.67  ? 64  HIS A N   1 
ATOM   505  C  CA  A HIS A 1 64  ? -0.046  -3.072  7.282   0.50 13.33  ? 64  HIS A CA  1 
ATOM   506  C  CA  B HIS A 1 64  ? 0.019   -3.331  7.195   0.50 13.91  ? 64  HIS A CA  1 
ATOM   507  C  C   A HIS A 1 64  ? -1.395  -3.726  7.444   0.50 12.87  ? 64  HIS A C   1 
ATOM   508  C  C   B HIS A 1 64  ? -1.402  -3.634  7.605   0.50 12.92  ? 64  HIS A C   1 
ATOM   509  O  O   A HIS A 1 64  ? -1.468  -4.900  7.832   0.50 12.99  ? 64  HIS A O   1 
ATOM   510  O  O   B HIS A 1 64  ? -1.620  -4.417  8.522   0.50 13.00  ? 64  HIS A O   1 
ATOM   511  C  CB  A HIS A 1 64  ? 0.182   -2.027  8.352   0.50 17.27  ? 64  HIS A CB  1 
ATOM   512  C  CB  B HIS A 1 64  ? 0.862   -2.677  8.305   0.50 17.65  ? 64  HIS A CB  1 
ATOM   513  C  CG  A HIS A 1 64  ? 1.490   -1.283  8.203   0.50 14.08  ? 64  HIS A CG  1 
ATOM   514  C  CG  B HIS A 1 64  ? 0.321   -1.344  8.759   0.50 16.34  ? 64  HIS A CG  1 
ATOM   515  N  ND1 A HIS A 1 64  ? 2.686   -1.884  8.394   0.50 17.35  ? 64  HIS A ND1 1 
ATOM   516  N  ND1 B HIS A 1 64  ? 0.731   -0.159  8.245   0.50 17.93  ? 64  HIS A ND1 1 
ATOM   517  C  CD2 A HIS A 1 64  ? 1.758   0.046   7.959   0.50 16.65  ? 64  HIS A CD2 1 
ATOM   518  C  CD2 B HIS A 1 64  ? -0.648  -1.057  9.700   0.50 16.60  ? 64  HIS A CD2 1 
ATOM   519  C  CE1 A HIS A 1 64  ? 3.678   -0.995  8.227   0.50 16.06  ? 64  HIS A CE1 1 
ATOM   520  C  CE1 B HIS A 1 64  ? 0.030   0.849   8.823   0.50 15.67  ? 64  HIS A CE1 1 
ATOM   521  N  NE2 A HIS A 1 64  ? 3.101   0.205   7.979   0.50 17.08  ? 64  HIS A NE2 1 
ATOM   522  N  NE2 B HIS A 1 64  ? -0.837  0.304   9.690   0.50 17.53  ? 64  HIS A NE2 1 
ATOM   523  N  N   A SER A 1 65  ? -2.458  -2.963  7.120   0.50 13.45  ? 65  SER A N   1 
ATOM   524  N  N   B SER A 1 65  ? -2.375  -3.062  6.875   0.50 11.21  ? 65  SER A N   1 
ATOM   525  C  CA  A SER A 1 65  ? -3.839  -3.389  7.175   0.50 12.34  ? 65  SER A CA  1 
ATOM   526  C  CA  B SER A 1 65  ? -3.762  -3.410  7.067   0.50 13.08  ? 65  SER A CA  1 
ATOM   527  C  C   A SER A 1 65  ? -4.520  -2.792  5.933   0.50 11.14  ? 65  SER A C   1 
ATOM   528  C  C   B SER A 1 65  ? -4.533  -2.739  5.915   0.50 11.26  ? 65  SER A C   1 
ATOM   529  O  O   A SER A 1 65  ? -3.869  -2.265  5.018   0.50 12.61  ? 65  SER A O   1 
ATOM   530  O  O   B SER A 1 65  ? -3.959  -2.154  4.997   0.50 11.96  ? 65  SER A O   1 
ATOM   531  C  CB  A SER A 1 65  ? -4.484  -2.826  8.436   0.50 13.27  ? 65  SER A CB  1 
ATOM   532  C  CB  B SER A 1 65  ? -4.251  -3.032  8.483   0.50 15.77  ? 65  SER A CB  1 
ATOM   533  O  OG  A SER A 1 65  ? -5.727  -3.407  8.713   0.50 12.36  ? 65  SER A OG  1 
ATOM   534  O  OG  B SER A 1 65  ? -4.702  -1.665  8.614   0.50 20.29  ? 65  SER A OG  1 
ATOM   535  N  N   . PHE A 1 66  ? -5.843  -2.850  5.927   1.00 12.01  ? 66  PHE A N   1 
ATOM   536  C  CA  . PHE A 1 66  ? -6.621  -1.991  5.084   1.00 11.77  ? 66  PHE A CA  1 
ATOM   537  C  C   . PHE A 1 66  ? -7.496  -1.143  5.951   1.00 10.73  ? 66  PHE A C   1 
ATOM   538  O  O   . PHE A 1 66  ? -7.937  -1.559  7.019   1.00 11.09  ? 66  PHE A O   1 
ATOM   539  C  CB  . PHE A 1 66  ? -7.422  -2.727  3.984   1.00 12.38  ? 66  PHE A CB  1 
ATOM   540  C  CG  . PHE A 1 66  ? -8.582  -3.570  4.484   1.00 12.42  ? 66  PHE A CG  1 
ATOM   541  C  CD1 . PHE A 1 66  ? -9.840  -2.972  4.703   1.00 11.53  ? 66  PHE A CD1 1 
ATOM   542  C  CD2 . PHE A 1 66  ? -8.399  -4.905  4.846   1.00 13.24  ? 66  PHE A CD2 1 
ATOM   543  C  CE1 . PHE A 1 66  ? -10.870 -3.736  5.180   1.00 12.62  ? 66  PHE A CE1 1 
ATOM   544  C  CE2 . PHE A 1 66  ? -9.476  -5.681  5.337   1.00 13.13  ? 66  PHE A CE2 1 
ATOM   545  C  CZ  . PHE A 1 66  ? -10.704 -5.079  5.500   1.00 12.87  ? 66  PHE A CZ  1 
ATOM   546  N  N   A LYS A 1 67  ? -7.872  0.051   5.465   0.50 11.13  ? 67  LYS A N   1 
ATOM   547  N  N   B LYS A 1 67  ? -7.712  0.126   5.535   0.50 10.72  ? 67  LYS A N   1 
ATOM   548  C  CA  A LYS A 1 67  ? -8.663  0.932   6.303   0.50 11.08  ? 67  LYS A CA  1 
ATOM   549  C  CA  B LYS A 1 67  ? -8.551  1.066   6.294   0.50 10.69  ? 67  LYS A CA  1 
ATOM   550  C  C   A LYS A 1 67  ? -9.655  1.727   5.461   0.50 10.69  ? 67  LYS A C   1 
ATOM   551  C  C   B LYS A 1 67  ? -9.694  1.552   5.402   0.50 8.03   ? 67  LYS A C   1 
ATOM   552  O  O   A LYS A 1 67  ? -9.356  2.298   4.389   0.50 9.66   ? 67  LYS A O   1 
ATOM   553  O  O   B LYS A 1 67  ? -9.531  1.707   4.209   0.50 8.56   ? 67  LYS A O   1 
ATOM   554  C  CB  A LYS A 1 67  ? -7.798  1.826   7.208   0.50 12.70  ? 67  LYS A CB  1 
ATOM   555  C  CB  B LYS A 1 67  ? -7.761  2.238   6.922   0.50 11.48  ? 67  LYS A CB  1 
ATOM   556  C  CG  A LYS A 1 67  ? -7.401  3.114   6.547   0.50 14.47  ? 67  LYS A CG  1 
ATOM   557  C  CG  B LYS A 1 67  ? -6.873  3.097   6.021   0.50 13.33  ? 67  LYS A CG  1 
ATOM   558  C  CD  A LYS A 1 67  ? -6.841  4.158   7.528   0.50 18.98  ? 67  LYS A CD  1 
ATOM   559  C  CD  B LYS A 1 67  ? -6.245  4.290   6.800   0.50 14.89  ? 67  LYS A CD  1 
ATOM   560  C  CE  A LYS A 1 67  ? -5.392  3.893   7.833   0.50 20.34  ? 67  LYS A CE  1 
ATOM   561  C  CE  B LYS A 1 67  ? -5.431  5.199   5.868   0.50 19.42  ? 67  LYS A CE  1 
ATOM   562  N  NZ  A LYS A 1 67  ? -4.595  5.180   7.925   0.50 20.18  ? 67  LYS A NZ  1 
ATOM   563  N  NZ  B LYS A 1 67  ? -4.812  6.502   6.295   0.50 20.11  ? 67  LYS A NZ  1 
ATOM   564  N  N   . VAL A 1 68  ? -10.857 1.780   6.039   1.00 8.48   ? 68  VAL A N   1 
ATOM   565  C  CA  . VAL A 1 68  ? -11.959 2.532   5.423   1.00 9.22   ? 68  VAL A CA  1 
ATOM   566  C  C   . VAL A 1 68  ? -12.008 3.895   6.182   1.00 8.93   ? 68  VAL A C   1 
ATOM   567  O  O   . VAL A 1 68  ? -12.154 3.908   7.386   1.00 9.21   ? 68  VAL A O   1 
ATOM   568  C  CB  . VAL A 1 68  ? -13.297 1.801   5.555   1.00 9.08   ? 68  VAL A CB  1 
ATOM   569  C  CG1 . VAL A 1 68  ? -14.425 2.744   5.065   1.00 10.04  ? 68  VAL A CG1 1 
ATOM   570  C  CG2 . VAL A 1 68  ? -13.289 0.509   4.706   1.00 10.70  ? 68  VAL A CG2 1 
ATOM   571  N  N   . GLU A 1 69  ? -11.801 4.963   5.419   1.00 9.51   ? 69  GLU A N   1 
ATOM   572  C  CA  . GLU A 1 69  ? -11.814 6.300   5.999   1.00 9.40   ? 69  GLU A CA  1 
ATOM   573  C  C   . GLU A 1 69  ? -13.125 6.983   5.787   1.00 8.58   ? 69  GLU A C   1 
ATOM   574  O  O   . GLU A 1 69  ? -13.738 6.814   4.727   1.00 10.33  ? 69  GLU A O   1 
ATOM   575  C  CB  . GLU A 1 69  ? -10.642 7.127   5.464   1.00 12.31  ? 69  GLU A CB  1 
ATOM   576  C  CG  . GLU A 1 69  ? -9.335  6.512   5.962   1.00 17.86  ? 69  GLU A CG  1 
ATOM   577  C  CD  . GLU A 1 69  ? -8.102  7.357   5.719   1.00 18.32  ? 69  GLU A CD  1 
ATOM   578  O  OE1 . GLU A 1 69  ? -7.523  7.202   4.637   1.00 20.28  ? 69  GLU A OE1 1 
ATOM   579  O  OE2 . GLU A 1 69  ? -7.661  8.191   6.560   1.00 21.82  ? 69  GLU A OE2 1 
ATOM   580  N  N   . PHE A 1 70  ? -13.494 7.799   6.761   1.00 8.74   ? 70  PHE A N   1 
ATOM   581  C  CA  . PHE A 1 70  ? -14.790 8.495   6.834   1.00 9.20   ? 70  PHE A CA  1 
ATOM   582  C  C   . PHE A 1 70  ? -14.617 10.006  6.743   1.00 9.51   ? 70  PHE A C   1 
ATOM   583  O  O   . PHE A 1 70  ? -13.541 10.550  7.096   1.00 11.16  ? 70  PHE A O   1 
ATOM   584  C  CB  . PHE A 1 70  ? -15.549 8.202   8.129   1.00 10.24  ? 70  PHE A CB  1 
ATOM   585  C  CG  . PHE A 1 70  ? -16.088 6.785   8.138   1.00 9.51   ? 70  PHE A CG  1 
ATOM   586  C  CD1 . PHE A 1 70  ? -15.257 5.668   8.350   1.00 10.73  ? 70  PHE A CD1 1 
ATOM   587  C  CD2 . PHE A 1 70  ? -17.447 6.516   7.855   1.00 10.34  ? 70  PHE A CD2 1 
ATOM   588  C  CE1 . PHE A 1 70  ? -15.757 4.355   8.236   1.00 11.35  ? 70  PHE A CE1 1 
ATOM   589  C  CE2 . PHE A 1 70  ? -17.961 5.228   7.772   1.00 10.46  ? 70  PHE A CE2 1 
ATOM   590  C  CZ  . PHE A 1 70  ? -17.088 4.143   7.971   1.00 11.21  ? 70  PHE A CZ  1 
ATOM   591  N  N   A ASP A 1 71  ? -15.681 10.698  6.320   0.50 10.26  ? 71  ASP A N   1 
ATOM   592  N  N   B ASP A 1 71  ? -15.687 10.714  6.378   0.50 10.77  ? 71  ASP A N   1 
ATOM   593  C  CA  A ASP A 1 71  ? -15.776 12.136  6.475   0.50 10.16  ? 71  ASP A CA  1 
ATOM   594  C  CA  B ASP A 1 71  ? -15.624 12.164  6.376   0.50 11.44  ? 71  ASP A CA  1 
ATOM   595  C  C   A ASP A 1 71  ? -15.933 12.393  7.983   0.50 10.67  ? 71  ASP A C   1 
ATOM   596  C  C   B ASP A 1 71  ? -15.936 12.637  7.807   0.50 11.69  ? 71  ASP A C   1 
ATOM   597  O  O   A ASP A 1 71  ? -16.983 12.072  8.592   0.50 10.07  ? 71  ASP A O   1 
ATOM   598  O  O   B ASP A 1 71  ? -17.109 12.674  8.203   0.50 16.40  ? 71  ASP A O   1 
ATOM   599  C  CB  A ASP A 1 71  ? -17.030 12.690  5.792   0.50 11.43  ? 71  ASP A CB  1 
ATOM   600  C  CB  B ASP A 1 71  ? -16.640 12.724  5.356   0.50 13.30  ? 71  ASP A CB  1 
ATOM   601  C  CG  A ASP A 1 71  ? -17.213 14.166  6.020   0.50 15.48  ? 71  ASP A CG  1 
ATOM   602  C  CG  B ASP A 1 71  ? -16.633 14.252  5.325   0.50 15.96  ? 71  ASP A CG  1 
ATOM   603  O  OD1 A ASP A 1 71  ? -16.279 14.851  6.512   0.50 14.31  ? 71  ASP A OD1 1 
ATOM   604  O  OD1 B ASP A 1 71  ? -17.378 14.792  4.477   0.50 16.79  ? 71  ASP A OD1 1 
ATOM   605  O  OD2 A ASP A 1 71  ? -18.320 14.644  5.703   0.50 18.70  ? 71  ASP A OD2 1 
ATOM   606  O  OD2 B ASP A 1 71  ? -15.942 14.884  6.184   0.50 17.56  ? 71  ASP A OD2 1 
ATOM   607  N  N   . ASP A 1 72  ? -14.897 12.958  8.592   1.00 10.67  ? 72  ASP A N   1 
ATOM   608  C  CA  . ASP A 1 72  ? -14.996 13.316  10.002  1.00 11.21  ? 72  ASP A CA  1 
ATOM   609  C  C   . ASP A 1 72  ? -14.902 14.873  10.201  1.00 11.15  ? 72  ASP A C   1 
ATOM   610  O  O   . ASP A 1 72  ? -14.471 15.313  11.266  1.00 13.55  ? 72  ASP A O   1 
ATOM   611  C  CB  . ASP A 1 72  ? -13.904 12.611  10.858  1.00 12.10  ? 72  ASP A CB  1 
ATOM   612  C  CG  . ASP A 1 72  ? -12.508 12.854  10.381  1.00 12.56  ? 72  ASP A CG  1 
ATOM   613  O  OD1 . ASP A 1 72  ? -12.297 13.601  9.392   1.00 13.66  ? 72  ASP A OD1 1 
ATOM   614  O  OD2 . ASP A 1 72  ? -11.598 12.377  11.117  1.00 14.32  ? 72  ASP A OD2 1 
ATOM   615  N  N   . SER A 1 73  ? -15.342 15.605  9.187   1.00 12.56  ? 73  SER A N   1 
ATOM   616  C  CA  . SER A 1 73  ? -15.329 17.076  9.264   1.00 13.86  ? 73  SER A CA  1 
ATOM   617  C  C   . SER A 1 73  ? -16.605 17.622  9.814   1.00 14.73  ? 73  SER A C   1 
ATOM   618  O  O   . SER A 1 73  ? -16.719 18.850  9.895   1.00 17.63  ? 73  SER A O   1 
ATOM   619  C  CB  . SER A 1 73  ? -15.050 17.575  7.887   1.00 16.01  ? 73  SER A CB  1 
ATOM   620  O  OG  . SER A 1 73  ? -16.204 17.503  6.992   1.00 16.54  ? 73  SER A OG  1 
ATOM   621  N  N   A GLN A 1 74  ? -17.571 16.757  10.101  0.50 15.83  ? 74  GLN A N   1 
ATOM   622  N  N   B GLN A 1 74  ? -17.558 16.852  10.281  0.50 15.04  ? 74  GLN A N   1 
ATOM   623  C  CA  A GLN A 1 74  ? -18.891 17.049  10.683  0.50 19.30  ? 74  GLN A CA  1 
ATOM   624  C  CA  B GLN A 1 74  ? -18.736 17.375  10.991  0.50 18.37  ? 74  GLN A CA  1 
ATOM   625  C  C   A GLN A 1 74  ? -19.181 15.987  11.761  0.50 14.81  ? 74  GLN A C   1 
ATOM   626  C  C   B GLN A 1 74  ? -19.150 16.328  11.982  0.50 18.48  ? 74  GLN A C   1 
ATOM   627  O  O   A GLN A 1 74  ? -18.544 14.927  11.715  0.50 14.71  ? 74  GLN A O   1 
ATOM   628  O  O   B GLN A 1 74  ? -18.722 15.188  11.864  0.50 16.71  ? 74  GLN A O   1 
ATOM   629  C  CB  A GLN A 1 74  ? -19.990 17.013  9.573   0.50 19.23  ? 74  GLN A CB  1 
ATOM   630  C  CB  B GLN A 1 74  ? -19.949 17.471  10.067  0.50 21.86  ? 74  GLN A CB  1 
ATOM   631  C  CG  A GLN A 1 74  ? -19.815 18.088  8.521   0.50 24.63  ? 74  GLN A CG  1 
ATOM   632  C  CG  B GLN A 1 74  ? -19.960 18.493  8.972   0.50 22.01  ? 74  GLN A CG  1 
ATOM   633  C  CD  A GLN A 1 74  ? -20.300 17.653  7.158   0.50 31.03  ? 74  GLN A CD  1 
ATOM   634  C  CD  B GLN A 1 74  ? -21.286 18.455  8.255   0.50 21.83  ? 74  GLN A CD  1 
ATOM   635  O  OE1 A GLN A 1 74  ? -21.500 17.408  6.973   0.50 27.27  ? 74  GLN A OE1 1 
ATOM   636  O  OE1 B GLN A 1 74  ? -22.296 18.666  8.888   0.50 28.72  ? 74  GLN A OE1 1 
ATOM   637  N  NE2 A GLN A 1 74  ? -19.371 17.530  6.188   0.50 22.57  ? 74  GLN A NE2 1 
ATOM   638  N  NE2 B GLN A 1 74  ? -21.292 18.153  6.939   0.50 25.99  ? 74  GLN A NE2 1 
ATOM   639  N  N   A ASP A 1 75  ? -20.145 16.279  12.671  0.50 20.43  ? 75  ASP A N   1 
ATOM   640  N  N   B ASP A 1 75  ? -20.058 16.643  12.903  0.50 21.80  ? 75  ASP A N   1 
ATOM   641  C  CA  A ASP A 1 75  ? -20.559 15.383  13.784  0.50 25.32  ? 75  ASP A CA  1 
ATOM   642  C  CA  B ASP A 1 75  ? -20.499 15.541  13.742  0.50 25.39  ? 75  ASP A CA  1 
ATOM   643  C  C   A ASP A 1 75  ? -21.455 14.223  13.366  0.50 17.28  ? 75  ASP A C   1 
ATOM   644  C  C   B ASP A 1 75  ? -21.440 14.658  12.881  0.50 18.83  ? 75  ASP A C   1 
ATOM   645  O  O   A ASP A 1 75  ? -22.513 13.949  13.939  0.50 23.97  ? 75  ASP A O   1 
ATOM   646  O  O   B ASP A 1 75  ? -22.571 15.048  12.633  0.50 20.20  ? 75  ASP A O   1 
ATOM   647  C  CB  A ASP A 1 75  ? -21.282 16.160  14.894  0.50 39.24  ? 75  ASP A CB  1 
ATOM   648  C  CB  B ASP A 1 75  ? -21.145 16.044  15.065  0.50 32.24  ? 75  ASP A CB  1 
ATOM   649  C  CG  A ASP A 1 75  ? -21.817 15.236  15.966  0.50 45.72  ? 75  ASP A CG  1 
ATOM   650  C  CG  B ASP A 1 75  ? -20.094 16.400  16.170  0.50 17.05  ? 75  ASP A CG  1 
ATOM   651  O  OD1 A ASP A 1 75  ? -21.731 14.021  15.739  0.50 56.72  ? 75  ASP A OD1 1 
ATOM   652  O  OD1 B ASP A 1 75  ? -18.910 16.053  16.025  0.50 27.14  ? 75  ASP A OD1 1 
ATOM   653  O  OD2 A ASP A 1 75  ? -22.329 15.709  17.007  0.50 53.23  ? 75  ASP A OD2 1 
ATOM   654  O  OD2 B ASP A 1 75  ? -20.522 16.968  17.191  0.50 26.63  ? 75  ASP A OD2 1 
ATOM   655  N  N   . LYS A 1 76  ? -20.999 13.487  12.389  1.00 17.55  ? 76  LYS A N   1 
ATOM   656  C  CA  . LYS A 1 76  ? -21.860 12.491  11.686  1.00 21.81  ? 76  LYS A CA  1 
ATOM   657  C  C   . LYS A 1 76  ? -21.961 10.994  12.139  1.00 21.59  ? 76  LYS A C   1 
ATOM   658  O  O   . LYS A 1 76  ? -22.818 10.274  11.710  1.00 24.75  ? 76  LYS A O   1 
ATOM   659  C  CB  . LYS A 1 76  ? -21.314 12.408  10.279  1.00 23.47  ? 76  LYS A CB  1 
ATOM   660  C  CG  . LYS A 1 76  ? -21.718 13.470  9.346   1.00 25.83  ? 76  LYS A CG  1 
ATOM   661  C  CD  . LYS A 1 76  ? -20.980 13.143  8.082   1.00 24.71  ? 76  LYS A CD  1 
ATOM   662  C  CE  . LYS A 1 76  ? -21.744 13.909  7.013   1.00 28.52  ? 76  LYS A CE  1 
ATOM   663  N  NZ  . LYS A 1 76  ? -21.120 13.833  5.680   1.00 34.92  ? 76  LYS A NZ  1 
ATOM   664  N  N   . ALA A 1 77  ? -21.026 10.514  12.907  1.00 17.43  ? 77  ALA A N   1 
ATOM   665  C  CA  . ALA A 1 77  ? -20.740 9.064   13.288  1.00 13.95  ? 77  ALA A CA  1 
ATOM   666  C  C   . ALA A 1 77  ? -19.978 9.209   14.576  1.00 13.50  ? 77  ALA A C   1 
ATOM   667  O  O   . ALA A 1 77  ? -18.742 9.389   14.582  1.00 19.23  ? 77  ALA A O   1 
ATOM   668  C  CB  . ALA A 1 77  ? -19.899 8.383   12.238  1.00 16.39  ? 77  ALA A CB  1 
ATOM   669  N  N   . VAL A 1 78  ? -20.686 9.258   15.704  1.00 12.73  ? 78  VAL A N   1 
ATOM   670  C  CA  . VAL A 1 78  ? -20.053 9.616   16.954  1.00 15.70  ? 78  VAL A CA  1 
ATOM   671  C  C   . VAL A 1 78  ? -20.287 8.554   18.036  1.00 14.16  ? 78  VAL A C   1 
ATOM   672  O  O   . VAL A 1 78  ? -21.332 7.877   18.113  1.00 14.72  ? 78  VAL A O   1 
ATOM   673  C  CB  . VAL A 1 78  ? -20.394 11.011  17.478  1.00 19.59  ? 78  VAL A CB  1 
ATOM   674  C  CG1 . VAL A 1 78  ? -20.019 12.148  16.524  1.00 19.82  ? 78  VAL A CG1 1 
ATOM   675  C  CG2 . VAL A 1 78  ? -21.792 11.056  17.865  1.00 20.18  ? 78  VAL A CG2 1 
ATOM   676  N  N   . LEU A 1 79  ? -19.301 8.449   18.927  1.00 12.13  ? 79  LEU A N   1 
ATOM   677  C  CA  . LEU A 1 79  ? -19.346 7.576   20.087  1.00 12.63  ? 79  LEU A CA  1 
ATOM   678  C  C   . LEU A 1 79  ? -19.310 8.490   21.289  1.00 14.36  ? 79  LEU A C   1 
ATOM   679  O  O   . LEU A 1 79  ? -18.481 9.427   21.380  1.00 16.30  ? 79  LEU A O   1 
ATOM   680  C  CB  . LEU A 1 79  ? -18.084 6.768   20.060  1.00 15.11  ? 79  LEU A CB  1 
ATOM   681  C  CG  . LEU A 1 79  ? -17.909 5.577   20.950  1.00 17.18  ? 79  LEU A CG  1 
ATOM   682  C  CD1 . LEU A 1 79  ? -18.939 4.503   20.694  1.00 20.76  ? 79  LEU A CD1 1 
ATOM   683  C  CD2 . LEU A 1 79  ? -16.573 4.969   20.730  1.00 15.13  ? 79  LEU A CD2 1 
ATOM   684  N  N   . LYS A 1 80  ? -20.174 8.167   22.232  1.00 14.25  ? 80  LYS A N   1 
ATOM   685  C  CA  . LYS A 1 80  ? -20.137 8.864   23.542  1.00 17.66  ? 80  LYS A CA  1 
ATOM   686  C  C   . LYS A 1 80  ? -20.707 7.972   24.628  1.00 15.20  ? 80  LYS A C   1 
ATOM   687  O  O   . LYS A 1 80  ? -21.000 6.792   24.339  1.00 16.08  ? 80  LYS A O   1 
ATOM   688  C  CB  . LYS A 1 80  ? -20.803 10.239  23.532  1.00 22.48  ? 80  LYS A CB  1 
ATOM   689  C  CG  . LYS A 1 80  ? -22.268 10.114  23.276  1.00 20.92  ? 80  LYS A CG  1 
ATOM   690  C  CD  . LYS A 1 80  ? -23.093 11.428  23.266  1.00 26.97  ? 80  LYS A CD  1 
ATOM   691  C  CE  . LYS A 1 80  ? -22.438 12.707  23.795  1.00 42.01  ? 80  LYS A CE  1 
ATOM   692  N  NZ  . LYS A 1 80  ? -22.255 12.858  25.277  1.00 59.76  ? 80  LYS A NZ  1 
ATOM   693  N  N   . GLY A 1 81  ? -20.786 8.471   25.861  1.00 17.67  ? 81  GLY A N   1 
ATOM   694  C  CA  . GLY A 1 81  ? -21.272 7.656   26.956  1.00 16.76  ? 81  GLY A CA  1 
ATOM   695  C  C   . GLY A 1 81  ? -20.234 6.597   27.336  1.00 17.07  ? 81  GLY A C   1 
ATOM   696  O  O   . GLY A 1 81  ? -19.049 6.747   27.038  1.00 16.86  ? 81  GLY A O   1 
ATOM   697  N  N   . GLY A 1 82  ? -20.703 5.481   27.920  1.00 20.45  ? 82  GLY A N   1 
ATOM   698  C  CA  . GLY A 1 82  ? -19.788 4.473   28.465  1.00 22.59  ? 82  GLY A CA  1 
ATOM   699  C  C   . GLY A 1 82  ? -18.803 5.168   29.390  1.00 19.78  ? 82  GLY A C   1 
ATOM   700  O  O   . GLY A 1 82  ? -19.193 5.948   30.270  1.00 24.88  ? 82  GLY A O   1 
ATOM   701  N  N   . PRO A 1 83  ? -17.522 4.803   29.250  1.00 20.72  ? 83  PRO A N   1 
ATOM   702  C  CA  . PRO A 1 83  ? -16.507 5.399   30.089  1.00 21.81  ? 83  PRO A CA  1 
ATOM   703  C  C   . PRO A 1 83  ? -16.107 6.812   29.650  1.00 17.62  ? 83  PRO A C   1 
ATOM   704  O  O   . PRO A 1 83  ? -15.223 7.392   30.268  1.00 23.13  ? 83  PRO A O   1 
ATOM   705  C  CB  . PRO A 1 83  ? -15.304 4.461   29.881  1.00 20.38  ? 83  PRO A CB  1 
ATOM   706  C  CG  . PRO A 1 83  ? -15.461 4.129   28.412  1.00 16.84  ? 83  PRO A CG  1 
ATOM   707  C  CD  . PRO A 1 83  ? -16.939 3.945   28.186  1.00 18.62  ? 83  PRO A CD  1 
ATOM   708  N  N   . LEU A 1 84  ? -16.673 7.293   28.527  1.00 16.93  ? 84  LEU A N   1 
ATOM   709  C  CA  . LEU A 1 84  ? -16.077 8.466   27.845  1.00 15.97  ? 84  LEU A CA  1 
ATOM   710  C  C   . LEU A 1 84  ? -16.710 9.762   28.416  1.00 17.22  ? 84  LEU A C   1 
ATOM   711  O  O   . LEU A 1 84  ? -17.893 9.790   28.751  1.00 19.24  ? 84  LEU A O   1 
ATOM   712  C  CB  . LEU A 1 84  ? -16.422 8.445   26.351  1.00 13.94  ? 84  LEU A CB  1 
ATOM   713  C  CG  . LEU A 1 84  ? -15.895 7.155   25.640  1.00 13.30  ? 84  LEU A CG  1 
ATOM   714  C  CD1 . LEU A 1 84  ? -16.446 7.187   24.239  1.00 16.42  ? 84  LEU A CD1 1 
ATOM   715  C  CD2 . LEU A 1 84  ? -14.351 7.187   25.671  1.00 13.85  ? 84  LEU A CD2 1 
ATOM   716  N  N   A ASP A 1 85  ? -15.899 10.820  28.431  0.50 19.18  ? 85  ASP A N   1 
ATOM   717  N  N   B ASP A 1 85  ? -15.880 10.780  28.640  0.50 20.61  ? 85  ASP A N   1 
ATOM   718  C  CA  A ASP A 1 85  ? -16.384 12.187  28.664  0.50 17.29  ? 85  ASP A CA  1 
ATOM   719  C  CA  B ASP A 1 85  ? -16.365 12.094  29.125  0.50 23.51  ? 85  ASP A CA  1 
ATOM   720  C  C   A ASP A 1 85  ? -16.324 12.916  27.343  0.50 14.54  ? 85  ASP A C   1 
ATOM   721  C  C   B ASP A 1 85  ? -16.744 13.008  27.976  0.50 26.44  ? 85  ASP A C   1 
ATOM   722  O  O   A ASP A 1 85  ? -15.322 12.768  26.605  0.50 15.12  ? 85  ASP A O   1 
ATOM   723  O  O   B ASP A 1 85  ? -17.272 14.099  28.174  0.50 30.12  ? 85  ASP A O   1 
ATOM   724  C  CB  A ASP A 1 85  ? -15.478 12.875  29.693  0.50 16.69  ? 85  ASP A CB  1 
ATOM   725  C  CB  B ASP A 1 85  ? -15.310 12.777  30.012  0.50 25.96  ? 85  ASP A CB  1 
ATOM   726  C  CG  A ASP A 1 85  ? -15.542 12.202  31.075  0.50 17.20  ? 85  ASP A CG  1 
ATOM   727  C  CG  B ASP A 1 85  ? -15.703 12.798  31.506  0.50 32.34  ? 85  ASP A CG  1 
ATOM   728  O  OD1 A ASP A 1 85  ? -16.659 11.864  31.526  0.50 25.08  ? 85  ASP A OD1 1 
ATOM   729  O  OD1 B ASP A 1 85  ? -16.877 13.109  31.819  0.50 46.78  ? 85  ASP A OD1 1 
ATOM   730  O  OD2 A ASP A 1 85  ? -14.464 11.964  31.677  0.50 24.78  ? 85  ASP A OD2 1 
ATOM   731  O  OD2 B ASP A 1 85  ? -14.838 12.545  32.385  0.50 29.29  ? 85  ASP A OD2 1 
ATOM   732  N  N   A GLY A 1 86  ? -17.370 13.685  27.021  0.50 16.47  ? 86  GLY A N   1 
ATOM   733  N  N   B GLY A 1 86  ? -16.484 12.591  26.752  0.50 26.43  ? 86  GLY A N   1 
ATOM   734  C  CA  A GLY A 1 86  ? -17.471 14.381  25.735  0.50 15.66  ? 86  GLY A CA  1 
ATOM   735  C  CA  B GLY A 1 86  ? -16.730 13.521  25.695  0.50 24.71  ? 86  GLY A CA  1 
ATOM   736  C  C   A GLY A 1 86  ? -17.758 13.492  24.493  0.50 14.07  ? 86  GLY A C   1 
ATOM   737  C  C   B GLY A 1 86  ? -17.638 13.022  24.622  0.50 22.69  ? 86  GLY A C   1 
ATOM   738  O  O   A GLY A 1 86  ? -18.218 12.349  24.635  0.50 30.72  ? 86  GLY A O   1 
ATOM   739  O  O   B GLY A 1 86  ? -18.512 12.178  24.859  0.50 21.75  ? 86  GLY A O   1 
ATOM   740  N  N   A THR A 1 87  ? -17.431 13.983  23.274  0.50 17.95  ? 87  THR A N   1 
ATOM   741  N  N   B THR A 1 87  ? -17.450 13.571  23.432  0.50 18.12  ? 87  THR A N   1 
ATOM   742  C  CA  A THR A 1 87  ? -17.854 13.370  21.963  0.50 16.34  ? 87  THR A CA  1 
ATOM   743  C  CA  B THR A 1 87  ? -17.941 12.952  22.247  0.50 16.16  ? 87  THR A CA  1 
ATOM   744  C  C   A THR A 1 87  ? -16.712 12.883  21.070  0.50 13.85  ? 87  THR A C   1 
ATOM   745  C  C   B THR A 1 87  ? -16.681 12.712  21.432  0.50 16.30  ? 87  THR A C   1 
ATOM   746  O  O   A THR A 1 87  ? -15.807 13.705  20.742  0.50 10.04  ? 87  THR A O   1 
ATOM   747  O  O   B THR A 1 87  ? -15.681 13.544  21.508  0.50 12.04  ? 87  THR A O   1 
ATOM   748  C  CB  A THR A 1 87  ? -18.681 14.404  21.133  0.50 16.87  ? 87  THR A CB  1 
ATOM   749  C  CB  B THR A 1 87  ? -18.877 13.900  21.486  0.50 17.47  ? 87  THR A CB  1 
ATOM   750  O  OG1 A THR A 1 87  ? -19.807 14.844  21.893  0.50 21.40  ? 87  THR A OG1 1 
ATOM   751  O  OG1 B THR A 1 87  ? -18.250 15.173  21.380  0.50 17.12  ? 87  THR A OG1 1 
ATOM   752  C  CG2 A THR A 1 87  ? -19.223 13.839  19.816  0.50 17.60  ? 87  THR A CG2 1 
ATOM   753  C  CG2 B THR A 1 87  ? -20.171 14.112  22.237  0.50 15.98  ? 87  THR A CG2 1 
ATOM   754  N  N   . TYR A 1 88  ? -16.736 11.602  20.689  1.00 13.81  ? 88  TYR A N   1 
ATOM   755  C  CA  . TYR A 1 88  ? -15.662 11.135  19.844  1.00 12.69  ? 88  TYR A CA  1 
ATOM   756  C  C   . TYR A 1 88  ? -16.175 10.838  18.426  1.00 12.03  ? 88  TYR A C   1 
ATOM   757  O  O   . TYR A 1 88  ? -17.175 10.163  18.261  1.00 17.12  ? 88  TYR A O   1 
ATOM   758  C  CB  . TYR A 1 88  ? -15.091 9.899   20.458  1.00 12.54  ? 88  TYR A CB  1 
ATOM   759  C  CG  . TYR A 1 88  ? -14.282 10.126  21.721  1.00 11.89  ? 88  TYR A CG  1 
ATOM   760  C  CD1 . TYR A 1 88  ? -14.864 10.500  22.946  1.00 11.52  ? 88  TYR A CD1 1 
ATOM   761  C  CD2 . TYR A 1 88  ? -12.868 9.875   21.722  1.00 11.16  ? 88  TYR A CD2 1 
ATOM   762  C  CE1 . TYR A 1 88  ? -14.095 10.687  24.103  1.00 13.16  ? 88  TYR A CE1 1 
ATOM   763  C  CE2 . TYR A 1 88  ? -12.123 10.033  22.872  1.00 10.29  ? 88  TYR A CE2 1 
ATOM   764  C  CZ  . TYR A 1 88  ? -12.734 10.415  24.044  1.00 11.17  ? 88  TYR A CZ  1 
ATOM   765  O  OH  . TYR A 1 88  ? -12.032 10.501  25.250  1.00 13.74  ? 88  TYR A OH  1 
ATOM   766  N  N   A ARG A 1 89  ? -15.524 11.345  17.364  0.50 12.53  ? 89  ARG A N   1 
ATOM   767  N  N   B ARG A 1 89  ? -15.417 11.270  17.437  0.50 11.42  ? 89  ARG A N   1 
ATOM   768  C  CA  A ARG A 1 89  ? -15.998 11.191  15.938  0.50 14.25  ? 89  ARG A CA  1 
ATOM   769  C  CA  B ARG A 1 89  ? -15.813 11.193  16.047  0.50 10.81  ? 89  ARG A CA  1 
ATOM   770  C  C   A ARG A 1 89  ? -15.212 10.077  15.284  0.50 10.04  ? 89  ARG A C   1 
ATOM   771  C  C   B ARG A 1 89  ? -15.145 10.084  15.254  0.50 10.70  ? 89  ARG A C   1 
ATOM   772  O  O   A ARG A 1 89  ? -13.982 9.984   15.399  0.50 9.47   ? 89  ARG A O   1 
ATOM   773  O  O   B ARG A 1 89  ? -13.934 9.946   15.341  0.50 9.16   ? 89  ARG A O   1 
ATOM   774  C  CB  A ARG A 1 89  ? -15.702 12.464  15.071  0.50 13.51  ? 89  ARG A CB  1 
ATOM   775  C  CB  B ARG A 1 89  ? -15.572 12.534  15.403  0.50 14.98  ? 89  ARG A CB  1 
ATOM   776  C  CG  A ARG A 1 89  ? -16.459 13.731  15.268  0.50 13.05  ? 89  ARG A CG  1 
ATOM   777  C  CG  B ARG A 1 89  ? -16.508 12.580  14.266  0.50 14.96  ? 89  ARG A CG  1 
ATOM   778  C  CD  A ARG A 1 89  ? -16.118 14.734  14.161  0.50 19.08  ? 89  ARG A CD  1 
ATOM   779  C  CD  B ARG A 1 89  ? -17.203 13.915  14.560  0.50 29.36  ? 89  ARG A CD  1 
ATOM   780  N  NE  A ARG A 1 89  ? -16.779 16.088  14.280  0.50 13.43  ? 89  ARG A NE  1 
ATOM   781  N  NE  B ARG A 1 89  ? -16.365 14.973  14.058  0.50 32.05  ? 89  ARG A NE  1 
ATOM   782  C  CZ  A ARG A 1 89  ? -16.341 17.288  13.837  0.50 18.12  ? 89  ARG A CZ  1 
ATOM   783  C  CZ  B ARG A 1 89  ? -16.464 16.306  14.174  0.50 20.72  ? 89  ARG A CZ  1 
ATOM   784  N  NH1 A ARG A 1 89  ? -15.255 17.340  13.058  0.50 16.55  ? 89  ARG A NH1 1 
ATOM   785  N  NH1 B ARG A 1 89  ? -17.356 16.979  14.960  0.50 15.13  ? 89  ARG A NH1 1 
ATOM   786  N  NH2 A ARG A 1 89  ? -17.042 18.432  14.098  0.50 21.60  ? 89  ARG A NH2 1 
ATOM   787  N  NH2 B ARG A 1 89  ? -15.534 17.010  13.545  0.50 27.31  ? 89  ARG A NH2 1 
ATOM   788  N  N   . LEU A 1 90  ? -15.957 9.238   14.554  1.00 10.01  ? 90  LEU A N   1 
ATOM   789  C  CA  . LEU A 1 90  ? -15.341 8.137   13.831  1.00 9.50   ? 90  LEU A CA  1 
ATOM   790  C  C   . LEU A 1 90  ? -14.479 8.683   12.675  1.00 9.36   ? 90  LEU A C   1 
ATOM   791  O  O   . LEU A 1 90  ? -14.993 9.463   11.840  1.00 12.12  ? 90  LEU A O   1 
ATOM   792  C  CB  . LEU A 1 90  ? -16.489 7.270   13.264  1.00 10.19  ? 90  LEU A CB  1 
ATOM   793  C  CG  . LEU A 1 90  ? -16.000 6.083   12.394  1.00 10.39  ? 90  LEU A CG  1 
ATOM   794  C  CD1 . LEU A 1 90  ? -15.268 5.035   13.181  1.00 11.21  ? 90  LEU A CD1 1 
ATOM   795  C  CD2 . LEU A 1 90  ? -17.228 5.468   11.717  1.00 11.87  ? 90  LEU A CD2 1 
ATOM   796  N  N   . THR A 1 91  ? -13.229 8.233   12.575  1.00 8.74   ? 91  THR A N   1 
ATOM   797  C  CA  . THR A 1 91  ? -12.388 8.611   11.455  1.00 9.81   ? 91  THR A CA  1 
ATOM   798  C  C   . THR A 1 91  ? -12.100 7.462   10.491  1.00 7.85   ? 91  THR A C   1 
ATOM   799  O  O   . THR A 1 91  ? -12.011 7.656   9.305   1.00 9.32   ? 91  THR A O   1 
ATOM   800  C  CB  . THR A 1 91  ? -11.082 9.287   11.941  1.00 10.86  ? 91  THR A CB  1 
ATOM   801  O  OG1 . THR A 1 91  ? -10.319 9.717   10.808  1.00 15.20  ? 91  THR A OG1 1 
ATOM   802  C  CG2 . THR A 1 91  ? -10.178 8.397   12.802  1.00 11.40  ? 91  THR A CG2 1 
ATOM   803  N  N   . GLN A 1 92  ? -11.949 6.202   11.005  1.00 8.94   ? 92  GLN A N   1 
ATOM   804  C  CA  . GLN A 1 92  ? -11.637 5.099   10.160  1.00 8.28   ? 92  GLN A CA  1 
ATOM   805  C  C   . GLN A 1 92  ? -11.934 3.799   10.905  1.00 8.19   ? 92  GLN A C   1 
ATOM   806  O  O   . GLN A 1 92  ? -12.008 3.795   12.129  1.00 8.41   ? 92  GLN A O   1 
ATOM   807  C  CB  . GLN A 1 92  ? -10.170 5.118   9.711   1.00 10.07  ? 92  GLN A CB  1 
ATOM   808  C  CG  . GLN A 1 92  ? -9.145  5.053   10.897  1.00 9.97   ? 92  GLN A CG  1 
ATOM   809  C  CD  . GLN A 1 92  ? -8.340  3.798   10.894  1.00 10.97  ? 92  GLN A CD  1 
ATOM   810  O  OE1 . GLN A 1 92  ? -7.112  3.800   10.856  1.00 17.28  ? 92  GLN A OE1 1 
ATOM   811  N  NE2 . GLN A 1 92  ? -9.011  2.704   11.060  1.00 9.32   ? 92  GLN A NE2 1 
ATOM   812  N  N   . PHE A 1 93  ? -12.086 2.694   10.134  1.00 7.90   ? 93  PHE A N   1 
ATOM   813  C  CA  . PHE A 1 93  ? -11.957 1.385   10.780  1.00 8.11   ? 93  PHE A CA  1 
ATOM   814  C  C   . PHE A 1 93  ? -10.966 0.564   9.956   1.00 7.43   ? 93  PHE A C   1 
ATOM   815  O  O   . PHE A 1 93  ? -10.729 0.797   8.776   1.00 7.90   ? 93  PHE A O   1 
ATOM   816  C  CB  . PHE A 1 93  ? -13.333 0.651   10.912  1.00 7.47   ? 93  PHE A CB  1 
ATOM   817  C  CG  . PHE A 1 93  ? -14.020 0.256   9.655   1.00 7.55   ? 93  PHE A CG  1 
ATOM   818  C  CD1 . PHE A 1 93  ? -13.634 -0.888  8.929   1.00 8.91   ? 93  PHE A CD1 1 
ATOM   819  C  CD2 . PHE A 1 93  ? -15.169 0.943   9.271   1.00 8.65   ? 93  PHE A CD2 1 
ATOM   820  C  CE1 . PHE A 1 93  ? -14.349 -1.234  7.799   1.00 9.23   ? 93  PHE A CE1 1 
ATOM   821  C  CE2 . PHE A 1 93  ? -15.867 0.567   8.096   1.00 8.92   ? 93  PHE A CE2 1 
ATOM   822  C  CZ  . PHE A 1 93  ? -15.456 -0.556  7.376   1.00 8.53   ? 93  PHE A CZ  1 
ATOM   823  N  N   . HIS A 1 94  ? -10.442 -0.465  10.622  1.00 7.29   ? 94  HIS A N   1 
ATOM   824  C  CA  . HIS A 1 94  ? -9.511  -1.427  10.025  1.00 8.36   ? 94  HIS A CA  1 
ATOM   825  C  C   . HIS A 1 94  ? -9.633  -2.712  10.812  1.00 7.70   ? 94  HIS A C   1 
ATOM   826  O  O   . HIS A 1 94  ? -10.287 -2.760  11.830  1.00 8.25   ? 94  HIS A O   1 
ATOM   827  C  CB  . HIS A 1 94  ? -8.077  -0.866  10.056  1.00 8.68   ? 94  HIS A CB  1 
ATOM   828  C  CG  . HIS A 1 94  ? -7.576  -0.643  11.449  1.00 8.19   ? 94  HIS A CG  1 
ATOM   829  N  ND1 . HIS A 1 94  ? -7.822  0.541   12.156  1.00 7.68   ? 94  HIS A ND1 1 
ATOM   830  C  CD2 . HIS A 1 94  ? -6.956  -1.463  12.328  1.00 7.76   ? 94  HIS A CD2 1 
ATOM   831  C  CE1 . HIS A 1 94  ? -7.386  0.393   13.406  1.00 8.12   ? 94  HIS A CE1 1 
ATOM   832  N  NE2 . HIS A 1 94  ? -6.818  -0.802  13.507  1.00 8.37   ? 94  HIS A NE2 1 
ATOM   833  N  N   . PHE A 1 95  ? -8.896  -3.706  10.364  1.00 8.45   ? 95  PHE A N   1 
ATOM   834  C  CA  . PHE A 1 95  ? -8.928  -5.027  11.003  1.00 8.69   ? 95  PHE A CA  1 
ATOM   835  C  C   . PHE A 1 95  ? -7.490  -5.520  11.247  1.00 8.56   ? 95  PHE A C   1 
ATOM   836  O  O   . PHE A 1 95  ? -6.530  -5.098  10.572  1.00 8.98   ? 95  PHE A O   1 
ATOM   837  C  CB  . PHE A 1 95  ? -9.601  -6.072  10.086  1.00 9.82   ? 95  PHE A CB  1 
ATOM   838  C  CG  . PHE A 1 95  ? -11.082 -5.803  9.790   1.00 9.60   ? 95  PHE A CG  1 
ATOM   839  C  CD1 . PHE A 1 95  ? -11.428 -4.855  8.777   1.00 10.64  ? 95  PHE A CD1 1 
ATOM   840  C  CD2 . PHE A 1 95  ? -12.080 -6.474  10.477  1.00 10.19  ? 95  PHE A CD2 1 
ATOM   841  C  CE1 . PHE A 1 95  ? -12.788 -4.675  8.486   1.00 11.18  ? 95  PHE A CE1 1 
ATOM   842  C  CE2 . PHE A 1 95  ? -13.423 -6.334  10.126  1.00 11.60  ? 95  PHE A CE2 1 
ATOM   843  C  CZ  . PHE A 1 95  ? -13.766 -5.403  9.178   1.00 11.19  ? 95  PHE A CZ  1 
ATOM   844  N  N   . HIS A 1 96  ? -7.390  -6.497  12.145  1.00 8.57   ? 96  HIS A N   1 
ATOM   845  C  CA  . HIS A 1 96  ? -6.178  -7.338  12.283  1.00 7.64   ? 96  HIS A CA  1 
ATOM   846  C  C   . HIS A 1 96  ? -6.646  -8.752  12.146  1.00 7.88   ? 96  HIS A C   1 
ATOM   847  O  O   . HIS A 1 96  ? -7.735  -9.094  12.642  1.00 8.91   ? 96  HIS A O   1 
ATOM   848  C  CB  . HIS A 1 96  ? -5.556  -7.131  13.683  1.00 9.06   ? 96  HIS A CB  1 
ATOM   849  C  CG  . HIS A 1 96  ? -5.260  -5.654  13.972  1.00 8.36   ? 96  HIS A CG  1 
ATOM   850  N  ND1 . HIS A 1 96  ? -4.057  -5.086  13.813  1.00 9.27   ? 96  HIS A ND1 1 
ATOM   851  C  CD2 . HIS A 1 96  ? -6.098  -4.623  14.392  1.00 8.62   ? 96  HIS A CD2 1 
ATOM   852  C  CE1 . HIS A 1 96  ? -4.126  -3.755  14.157  1.00 8.74   ? 96  HIS A CE1 1 
ATOM   853  N  NE2 . HIS A 1 96  ? -5.365  -3.440  14.463  1.00 8.75   ? 96  HIS A NE2 1 
ATOM   854  N  N   . TRP A 1 97  ? -5.854  -9.604  11.537  1.00 8.15   ? 97  TRP A N   1 
ATOM   855  C  CA  . TRP A 1 97  ? -6.282  -11.019 11.342  1.00 8.88   ? 97  TRP A CA  1 
ATOM   856  C  C   . TRP A 1 97  ? -5.085  -11.926 11.192  1.00 8.96   ? 97  TRP A C   1 
ATOM   857  O  O   . TRP A 1 97  ? -3.914  -11.504 11.149  1.00 9.49   ? 97  TRP A O   1 
ATOM   858  C  CB  . TRP A 1 97  ? -7.172  -11.122 10.057  1.00 9.67   ? 97  TRP A CB  1 
ATOM   859  C  CG  . TRP A 1 97  ? -6.501  -10.764 8.811   1.00 9.87   ? 97  TRP A CG  1 
ATOM   860  C  CD1 . TRP A 1 97  ? -5.811  -11.571 7.937   1.00 11.56  ? 97  TRP A CD1 1 
ATOM   861  C  CD2 . TRP A 1 97  ? -6.432  -9.440  8.219   1.00 9.33   ? 97  TRP A CD2 1 
ATOM   862  N  NE1 . TRP A 1 97  ? -5.344  -10.892 6.856   1.00 12.14  ? 97  TRP A NE1 1 
ATOM   863  C  CE2 . TRP A 1 97  ? -5.688  -9.560  6.993   1.00 10.49  ? 97  TRP A CE2 1 
ATOM   864  C  CE3 . TRP A 1 97  ? -6.948  -8.164  8.596   1.00 9.74   ? 97  TRP A CE3 1 
ATOM   865  C  CZ2 . TRP A 1 97  ? -5.432  -8.474  6.181   1.00 11.05  ? 97  TRP A CZ2 1 
ATOM   866  C  CZ3 . TRP A 1 97  ? -6.650  -7.065  7.748   1.00 10.47  ? 97  TRP A CZ3 1 
ATOM   867  C  CH2 . TRP A 1 97  ? -5.962  -7.207  6.555   1.00 10.64  ? 97  TRP A CH2 1 
ATOM   868  N  N   . GLY A 1 98  ? -5.354  -13.218 11.169  1.00 9.26   ? 98  GLY A N   1 
ATOM   869  C  CA  . GLY A 1 98  ? -4.370  -14.282 11.279  1.00 10.79  ? 98  GLY A CA  1 
ATOM   870  C  C   . GLY A 1 98  ? -4.119  -14.995 9.974   1.00 12.01  ? 98  GLY A C   1 
ATOM   871  O  O   . GLY A 1 98  ? -4.884  -14.821 8.963   1.00 13.29  ? 98  GLY A O   1 
ATOM   872  N  N   . SER A 1 99  ? -3.097  -15.869 9.981   1.00 13.77  ? 99  SER A N   1 
ATOM   873  C  CA  . SER A 1 99  ? -2.860  -16.771 8.884   1.00 15.58  ? 99  SER A CA  1 
ATOM   874  C  C   . SER A 1 99  ? -3.736  -17.985 8.945   1.00 17.95  ? 99  SER A C   1 
ATOM   875  O  O   . SER A 1 99  ? -3.785  -18.754 7.941   1.00 23.40  ? 99  SER A O   1 
ATOM   876  C  CB  . SER A 1 99  ? -1.402  -17.202 8.879   1.00 16.79  ? 99  SER A CB  1 
ATOM   877  O  OG  . SER A 1 99  ? -0.993  -17.618 10.165  1.00 17.12  ? 99  SER A OG  1 
ATOM   878  N  N   . LEU A 1 100 ? -4.350  -18.232 10.099  1.00 16.91  ? 100 LEU A N   1 
ATOM   879  C  CA  . LEU A 1 100 ? -5.261  -19.352 10.348  1.00 20.64  ? 100 LEU A CA  1 
ATOM   880  C  C   . LEU A 1 100 ? -6.289  -18.935 11.407  1.00 18.28  ? 100 LEU A C   1 
ATOM   881  O  O   . LEU A 1 100 ? -6.089  -17.894 12.044  1.00 18.90  ? 100 LEU A O   1 
ATOM   882  C  CB  . LEU A 1 100 ? -4.531  -20.639 10.713  1.00 29.86  ? 100 LEU A CB  1 
ATOM   883  C  CG  . LEU A 1 100 ? -3.336  -20.573 11.645  1.00 34.73  ? 100 LEU A CG  1 
ATOM   884  C  CD1 . LEU A 1 100 ? -2.132  -19.760 11.271  1.00 35.15  ? 100 LEU A CD1 1 
ATOM   885  C  CD2 . LEU A 1 100 ? -3.696  -20.267 13.086  1.00 48.05  ? 100 LEU A CD2 1 
ATOM   886  N  N   . ASP A 1 101 ? -7.423  -19.663 11.529  1.00 21.05  ? 101 ASP A N   1 
ATOM   887  C  CA  . ASP A 1 101 ? -8.571  -19.140 12.319  1.00 16.86  ? 101 ASP A CA  1 
ATOM   888  C  C   . ASP A 1 101 ? -8.314  -19.067 13.763  1.00 18.65  ? 101 ASP A C   1 
ATOM   889  O  O   . ASP A 1 101 ? -8.994  -18.323 14.471  1.00 22.48  ? 101 ASP A O   1 
ATOM   890  C  CB  . ASP A 1 101 ? -9.856  -19.912 12.095  1.00 18.15  ? 101 ASP A CB  1 
ATOM   891  C  CG  . ASP A 1 101 ? -10.337 -19.971 10.638  1.00 17.77  ? 101 ASP A CG  1 
ATOM   892  O  OD1 . ASP A 1 101 ? -9.854  -19.232 9.750   1.00 18.94  ? 101 ASP A OD1 1 
ATOM   893  O  OD2 . ASP A 1 101 ? -11.260 -20.781 10.386  1.00 23.80  ? 101 ASP A OD2 1 
ATOM   894  N  N   . GLY A 1 102 ? -7.287  -19.818 14.250  1.00 16.52  ? 102 GLY A N   1 
ATOM   895  C  CA  . GLY A 1 102 ? -6.998  -19.727 15.686  1.00 19.35  ? 102 GLY A CA  1 
ATOM   896  C  C   . GLY A 1 102 ? -6.144  -18.608 16.188  1.00 14.21  ? 102 GLY A C   1 
ATOM   897  O  O   . GLY A 1 102 ? -5.757  -18.584 17.374  1.00 18.03  ? 102 GLY A O   1 
ATOM   898  N  N   . GLN A 1 103 ? -5.878  -17.615 15.330  1.00 15.11  ? 103 GLN A N   1 
ATOM   899  C  CA  . GLN A 1 103 ? -5.192  -16.439 15.775  1.00 13.76  ? 103 GLN A CA  1 
ATOM   900  C  C   . GLN A 1 103 ? -5.543  -15.279 14.858  1.00 11.40  ? 103 GLN A C   1 
ATOM   901  O  O   . GLN A 1 103 ? -6.096  -15.512 13.770  1.00 11.81  ? 103 GLN A O   1 
ATOM   902  C  CB  . GLN A 1 103 ? -3.661  -16.672 15.754  1.00 12.20  ? 103 GLN A CB  1 
ATOM   903  C  CG  . GLN A 1 103 ? -3.080  -16.885 14.395  1.00 13.12  ? 103 GLN A CG  1 
ATOM   904  C  CD  . GLN A 1 103 ? -1.661  -17.423 14.478  1.00 15.05  ? 103 GLN A CD  1 
ATOM   905  O  OE1 . GLN A 1 103 ? -0.792  -17.016 13.726  1.00 16.30  ? 103 GLN A OE1 1 
ATOM   906  N  NE2 . GLN A 1 103 ? -1.414  -18.337 15.382  1.00 22.30  ? 103 GLN A NE2 1 
ATOM   907  N  N   . GLY A 1 104 ? -5.238  -14.045 15.312  1.00 10.75  ? 104 GLY A N   1 
ATOM   908  C  CA  . GLY A 1 104 ? -5.532  -12.876 14.510  1.00 10.11  ? 104 GLY A CA  1 
ATOM   909  C  C   . GLY A 1 104 ? -5.972  -11.715 15.350  1.00 8.76   ? 104 GLY A C   1 
ATOM   910  O  O   . GLY A 1 104 ? -5.719  -10.558 14.971  1.00 9.66   ? 104 GLY A O   1 
ATOM   911  N  N   . SER A 1 105 ? -6.681  -11.942 16.469  1.00 9.44   ? 105 SER A N   1 
ATOM   912  C  CA  . SER A 1 105 ? -7.072  -10.823 17.311  1.00 9.39   ? 105 SER A CA  1 
ATOM   913  C  C   . SER A 1 105 ? -5.864  -10.285 18.095  1.00 8.46   ? 105 SER A C   1 
ATOM   914  O  O   . SER A 1 105 ? -4.838  -10.958 18.291  1.00 10.40  ? 105 SER A O   1 
ATOM   915  C  CB  . SER A 1 105 ? -8.226  -11.207 18.249  1.00 10.45  ? 105 SER A CB  1 
ATOM   916  O  OG  . SER A 1 105 ? -7.836  -12.172 19.240  1.00 10.24  ? 105 SER A OG  1 
ATOM   917  N  N   . GLU A 1 106 ? -6.023  -9.036  18.494  1.00 8.27   ? 106 GLU A N   1 
ATOM   918  C  CA  . GLU A 1 106 ? -4.990  -8.359  19.331  1.00 8.50   ? 106 GLU A CA  1 
ATOM   919  C  C   . GLU A 1 106 ? -5.333  -8.528  20.795  1.00 8.67   ? 106 GLU A C   1 
ATOM   920  O  O   . GLU A 1 106 ? -4.526  -9.090  21.559  1.00 8.80   ? 106 GLU A O   1 
ATOM   921  C  CB  . GLU A 1 106 ? -4.928  -6.854  18.883  1.00 9.01   ? 106 GLU A CB  1 
ATOM   922  C  CG  . GLU A 1 106 ? -4.517  -6.744  17.469  1.00 9.95   ? 106 GLU A CG  1 
ATOM   923  C  CD  . GLU A 1 106 ? -3.819  -5.448  17.170  1.00 8.17   ? 106 GLU A CD  1 
ATOM   924  O  OE1 . GLU A 1 106 ? -4.410  -4.374  17.399  1.00 8.93   ? 106 GLU A OE1 1 
ATOM   925  O  OE2 . GLU A 1 106 ? -2.659  -5.478  16.693  1.00 9.91   ? 106 GLU A OE2 1 
ATOM   926  N  N   . HIS A 1 107 ? -6.520  -8.061  21.213  1.00 8.52   ? 107 HIS A N   1 
ATOM   927  C  CA  . HIS A 1 107 ? -6.988  -8.465  22.513  1.00 8.68   ? 107 HIS A CA  1 
ATOM   928  C  C   . HIS A 1 107 ? -7.246  -9.986  22.552  1.00 9.11   ? 107 HIS A C   1 
ATOM   929  O  O   . HIS A 1 107 ? -7.604  -10.563 21.505  1.00 9.24   ? 107 HIS A O   1 
ATOM   930  C  CB  . HIS A 1 107 ? -8.215  -7.671  22.937  1.00 9.25   ? 107 HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 107 ? -7.880  -6.220  23.066  1.00 8.47   ? 107 HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 107 ? -7.958  -5.329  22.017  1.00 9.22   ? 107 HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 107 ? -7.413  -5.511  24.115  1.00 9.32   ? 107 HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 107 ? -7.520  -4.118  22.446  1.00 8.76   ? 107 HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 107 ? -7.195  -4.213  23.734  1.00 7.96   ? 107 HIS A NE2 1 
ATOM   936  N  N   . THR A 1 108 ? -7.141  -10.533 23.741  1.00 9.86   ? 108 THR A N   1 
ATOM   937  C  CA  . THR A 1 108 ? -7.537  -11.918 23.969  1.00 9.84   ? 108 THR A CA  1 
ATOM   938  C  C   . THR A 1 108 ? -8.469  -11.908 25.166  1.00 9.45   ? 108 THR A C   1 
ATOM   939  O  O   . THR A 1 108 ? -8.515  -10.968 25.953  1.00 10.65  ? 108 THR A O   1 
ATOM   940  C  CB  . THR A 1 108 ? -6.301  -12.835 24.192  1.00 10.65  ? 108 THR A CB  1 
ATOM   941  O  OG1 . THR A 1 108 ? -5.454  -12.339 25.250  1.00 10.75  ? 108 THR A OG1 1 
ATOM   942  C  CG2 . THR A 1 108 ? -5.508  -12.892 22.880  1.00 11.36  ? 108 THR A CG2 1 
ATOM   943  N  N   . VAL A 1 109 ? -9.239  -12.978 25.297  1.00 10.60  ? 109 VAL A N   1 
ATOM   944  C  CA  . VAL A 1 109 ? -10.250 -13.052 26.373  1.00 11.56  ? 109 VAL A CA  1 
ATOM   945  C  C   . VAL A 1 109 ? -9.919  -14.341 27.131  1.00 11.46  ? 109 VAL A C   1 
ATOM   946  O  O   . VAL A 1 109 ? -10.134 -15.450 26.646  1.00 12.60  ? 109 VAL A O   1 
ATOM   947  C  CB  . VAL A 1 109 ? -11.690 -13.055 25.789  1.00 12.40  ? 109 VAL A CB  1 
ATOM   948  C  CG1 . VAL A 1 109 ? -12.696 -13.207 26.871  1.00 14.04  ? 109 VAL A CG1 1 
ATOM   949  C  CG2 . VAL A 1 109 ? -11.952 -11.805 24.973  1.00 13.56  ? 109 VAL A CG2 1 
ATOM   950  N  N   . ASP A 1 110 ? -9.411  -14.210 28.378  1.00 12.70  ? 110 ASP A N   1 
ATOM   951  C  CA  . ASP A 1 110 ? -8.995  -15.424 29.120  1.00 13.73  ? 110 ASP A CA  1 
ATOM   952  C  C   . ASP A 1 110 ? -8.047  -16.248 28.236  1.00 14.28  ? 110 ASP A C   1 
ATOM   953  O  O   . ASP A 1 110 ? -8.148  -17.498 28.183  1.00 15.53  ? 110 ASP A O   1 
ATOM   954  C  CB  . ASP A 1 110 ? -10.156 -16.239 29.634  1.00 16.83  ? 110 ASP A CB  1 
ATOM   955  C  CG  . ASP A 1 110 ? -10.986 -15.436 30.644  1.00 17.28  ? 110 ASP A CG  1 
ATOM   956  O  OD1 . ASP A 1 110 ? -10.437 -14.583 31.367  1.00 19.65  ? 110 ASP A OD1 1 
ATOM   957  O  OD2 . ASP A 1 110 ? -12.189 -15.660 30.725  1.00 20.92  ? 110 ASP A OD2 1 
ATOM   958  N  N   . LYS A 1 111 ? -7.141  -15.572 27.535  1.00 11.83  ? 111 LYS A N   1 
ATOM   959  C  CA  . LYS A 1 111 ? -6.154  -16.128 26.645  1.00 12.43  ? 111 LYS A CA  1 
ATOM   960  C  C   . LYS A 1 111 ? -6.676  -16.636 25.319  1.00 12.66  ? 111 LYS A C   1 
ATOM   961  O  O   . LYS A 1 111 ? -5.866  -16.946 24.433  1.00 13.82  ? 111 LYS A O   1 
ATOM   962  C  CB  . LYS A 1 111 ? -5.274  -17.176 27.331  1.00 16.18  ? 111 LYS A CB  1 
ATOM   963  C  CG  . LYS A 1 111 ? -4.517  -16.743 28.586  1.00 21.41  ? 111 LYS A CG  1 
ATOM   964  C  CD  . LYS A 1 111 ? -3.455  -15.673 28.321  1.00 22.73  ? 111 LYS A CD  1 
ATOM   965  C  CE  . LYS A 1 111 ? -2.723  -15.233 29.585  1.00 39.89  ? 111 LYS A CE  1 
ATOM   966  N  NZ  . LYS A 1 111 ? -1.265  -15.160 29.340  1.00 29.65  ? 111 LYS A NZ  1 
ATOM   967  N  N   . LYS A 1 112 ? -7.990  -16.580 25.093  1.00 12.72  ? 112 LYS A N   1 
ATOM   968  C  CA  . LYS A 1 112 ? -8.496  -16.990 23.820  1.00 13.69  ? 112 LYS A CA  1 
ATOM   969  C  C   . LYS A 1 112 ? -8.227  -15.928 22.731  1.00 12.19  ? 112 LYS A C   1 
ATOM   970  O  O   . LYS A 1 112 ? -8.478  -14.735 22.955  1.00 12.53  ? 112 LYS A O   1 
ATOM   971  C  CB  . LYS A 1 112 ? -9.999  -17.152 23.893  1.00 15.68  ? 112 LYS A CB  1 
ATOM   972  C  CG  . LYS A 1 112 ? -10.684 -17.456 22.548  1.00 17.56  ? 112 LYS A CG  1 
ATOM   973  C  CD  . LYS A 1 112 ? -12.213 -17.616 22.639  1.00 18.79  ? 112 LYS A CD  1 
ATOM   974  C  CE  . LYS A 1 112 ? -12.715 -17.722 21.219  1.00 23.42  ? 112 LYS A CE  1 
ATOM   975  N  NZ  . LYS A 1 112 ? -12.515 -19.038 20.594  1.00 30.23  ? 112 LYS A NZ  1 
ATOM   976  N  N   A LYS A 1 113 ? -7.649  -16.364 21.618  0.50 12.16  ? 113 LYS A N   1 
ATOM   977  N  N   B LYS A 1 113 ? -7.754  -16.402 21.574  0.50 12.65  ? 113 LYS A N   1 
ATOM   978  C  CA  A LYS A 1 113 ? -7.460  -15.558 20.423  0.50 13.23  ? 113 LYS A CA  1 
ATOM   979  C  CA  B LYS A 1 113 ? -7.478  -15.614 20.369  0.50 11.64  ? 113 LYS A CA  1 
ATOM   980  C  C   A LYS A 1 113 ? -8.685  -15.806 19.564  0.50 12.56  ? 113 LYS A C   1 
ATOM   981  C  C   B LYS A 1 113 ? -8.511  -15.825 19.288  0.50 11.50  ? 113 LYS A C   1 
ATOM   982  O  O   A LYS A 1 113 ? -9.194  -16.946 19.526  0.50 11.36  ? 113 LYS A O   1 
ATOM   983  O  O   B LYS A 1 113 ? -8.759  -16.982 18.856  0.50 11.94  ? 113 LYS A O   1 
ATOM   984  C  CB  A LYS A 1 113 ? -6.224  -16.011 19.630  0.50 11.16  ? 113 LYS A CB  1 
ATOM   985  C  CB  B LYS A 1 113 ? -6.114  -15.937 19.783  0.50 12.04  ? 113 LYS A CB  1 
ATOM   986  C  CG  A LYS A 1 113 ? -4.906  -15.855 20.450  0.50 11.34  ? 113 LYS A CG  1 
ATOM   987  C  CG  B LYS A 1 113 ? -4.960  -15.466 20.682  0.50 12.55  ? 113 LYS A CG  1 
ATOM   988  C  CD  A LYS A 1 113 ? -3.725  -16.442 19.676  0.50 12.68  ? 113 LYS A CD  1 
ATOM   989  C  CD  B LYS A 1 113 ? -3.687  -16.120 20.203  0.50 11.61  ? 113 LYS A CD  1 
ATOM   990  C  CE  A LYS A 1 113 ? -2.359  -16.028 20.219  0.50 13.63  ? 113 LYS A CE  1 
ATOM   991  C  CE  B LYS A 1 113 ? -2.474  -15.541 20.916  0.50 13.92  ? 113 LYS A CE  1 
ATOM   992  N  NZ  A LYS A 1 113 ? -2.004  -16.432 21.624  0.50 14.79  ? 113 LYS A NZ  1 
ATOM   993  N  NZ  B LYS A 1 113 ? -1.333  -16.396 20.461  0.50 18.40  ? 113 LYS A NZ  1 
ATOM   994  N  N   . TYR A 1 114 ? -9.168  -14.744 18.924  1.00 10.42  ? 114 TYR A N   1 
ATOM   995  C  CA  . TYR A 1 114 ? -10.161 -14.798 17.867  1.00 9.83   ? 114 TYR A CA  1 
ATOM   996  C  C   . TYR A 1 114 ? -9.490  -14.768 16.475  1.00 10.13  ? 114 TYR A C   1 
ATOM   997  O  O   . TYR A 1 114 ? -8.285  -14.451 16.347  1.00 10.65  ? 114 TYR A O   1 
ATOM   998  C  CB  . TYR A 1 114 ? -11.211 -13.708 17.995  1.00 10.49  ? 114 TYR A CB  1 
ATOM   999  C  CG  . TYR A 1 114 ? -12.148 -13.952 19.156  1.00 10.25  ? 114 TYR A CG  1 
ATOM   1000 C  CD1 . TYR A 1 114 ? -11.873 -13.545 20.428  1.00 12.25  ? 114 TYR A CD1 1 
ATOM   1001 C  CD2 . TYR A 1 114 ? -13.383 -14.604 18.949  1.00 12.49  ? 114 TYR A CD2 1 
ATOM   1002 C  CE1 . TYR A 1 114 ? -12.742 -13.734 21.450  1.00 16.02  ? 114 TYR A CE1 1 
ATOM   1003 C  CE2 . TYR A 1 114 ? -14.226 -14.793 19.987  1.00 14.31  ? 114 TYR A CE2 1 
ATOM   1004 C  CZ  . TYR A 1 114 ? -13.911 -14.384 21.229  1.00 18.05  ? 114 TYR A CZ  1 
ATOM   1005 O  OH  . TYR A 1 114 ? -14.809 -14.577 22.227  1.00 26.75  ? 114 TYR A OH  1 
ATOM   1006 N  N   . ALA A 1 115 ? -10.251 -15.068 15.403  1.00 10.21  ? 115 ALA A N   1 
ATOM   1007 C  CA  . ALA A 1 115 ? -9.706  -15.069 14.067  1.00 10.13  ? 115 ALA A CA  1 
ATOM   1008 C  C   . ALA A 1 115 ? -9.280  -13.704 13.599  1.00 10.33  ? 115 ALA A C   1 
ATOM   1009 O  O   . ALA A 1 115 ? -8.461  -13.535 12.677  1.00 10.71  ? 115 ALA A O   1 
ATOM   1010 C  CB  . ALA A 1 115 ? -10.720 -15.695 13.086  1.00 12.24  ? 115 ALA A CB  1 
ATOM   1011 N  N   . ALA A 1 116 ? -10.003 -12.674 14.083  1.00 9.25   ? 116 ALA A N   1 
ATOM   1012 C  CA  . ALA A 1 116 ? -9.707  -11.308 13.674  1.00 9.48   ? 116 ALA A CA  1 
ATOM   1013 C  C   . ALA A 1 116 ? -10.276 -10.351 14.692  1.00 7.74   ? 116 ALA A C   1 
ATOM   1014 O  O   . ALA A 1 116 ? -11.031 -10.730 15.592  1.00 8.79   ? 116 ALA A O   1 
ATOM   1015 C  CB  . ALA A 1 116 ? -10.243 -11.040 12.252  1.00 9.71   ? 116 ALA A CB  1 
ATOM   1016 N  N   . GLU A 1 117 ? -9.926  -9.058  14.527  1.00 8.74   ? 117 GLU A N   1 
ATOM   1017 C  CA  . GLU A 1 117 ? -10.471 -8.000  15.366  1.00 9.08   ? 117 GLU A CA  1 
ATOM   1018 C  C   . GLU A 1 117 ? -10.667 -6.737  14.545  1.00 8.24   ? 117 GLU A C   1 
ATOM   1019 O  O   . GLU A 1 117 ? -9.765  -6.357  13.823  1.00 9.01   ? 117 GLU A O   1 
ATOM   1020 C  CB  . GLU A 1 117 ? -9.497  -7.755  16.564  1.00 9.35   ? 117 GLU A CB  1 
ATOM   1021 C  CG  . GLU A 1 117 ? -10.073 -6.879  17.696  1.00 8.44   ? 117 GLU A CG  1 
ATOM   1022 C  CD  . GLU A 1 117 ? -9.166  -6.812  18.911  1.00 8.30   ? 117 GLU A CD  1 
ATOM   1023 O  OE1 . GLU A 1 117 ? -8.435  -7.786  19.142  1.00 9.14   ? 117 GLU A OE1 1 
ATOM   1024 O  OE2 . GLU A 1 117 ? -9.167  -5.735  19.607  1.00 9.49   ? 117 GLU A OE2 1 
ATOM   1025 N  N   . LEU A 1 118 ? -11.857 -6.172  14.674  1.00 8.04   ? 118 LEU A N   1 
ATOM   1026 C  CA  . LEU A 1 118 ? -12.249 -4.926  14.012  1.00 7.63   ? 118 LEU A CA  1 
ATOM   1027 C  C   . LEU A 1 118 ? -12.055 -3.777  15.011  1.00 6.96   ? 118 LEU A C   1 
ATOM   1028 O  O   . LEU A 1 118 ? -12.459 -3.860  16.151  1.00 7.27   ? 118 LEU A O   1 
ATOM   1029 C  CB  . LEU A 1 118 ? -13.749 -5.067  13.638  1.00 8.50   ? 118 LEU A CB  1 
ATOM   1030 C  CG  . LEU A 1 118 ? -14.513 -3.728  13.298  1.00 8.52   ? 118 LEU A CG  1 
ATOM   1031 C  CD1 . LEU A 1 118 ? -13.910 -3.040  12.053  1.00 8.67   ? 118 LEU A CD1 1 
ATOM   1032 C  CD2 . LEU A 1 118 ? -15.966 -4.075  13.080  1.00 10.34  ? 118 LEU A CD2 1 
ATOM   1033 N  N   . HIS A 1 119 ? -11.412 -2.721  14.502  1.00 7.13   ? 119 HIS A N   1 
ATOM   1034 C  CA  . HIS A 1 119 ? -11.180 -1.499  15.267  1.00 7.58   ? 119 HIS A CA  1 
ATOM   1035 C  C   . HIS A 1 119 ? -11.797 -0.281  14.595  1.00 6.88   ? 119 HIS A C   1 
ATOM   1036 O  O   . HIS A 1 119 ? -11.439 0.036   13.478  1.00 7.45   ? 119 HIS A O   1 
ATOM   1037 C  CB  . HIS A 1 119 ? -9.668  -1.258  15.430  1.00 8.55   ? 119 HIS A CB  1 
ATOM   1038 C  CG  . HIS A 1 119 ? -9.043  -2.245  16.330  1.00 7.52   ? 119 HIS A CG  1 
ATOM   1039 N  ND1 . HIS A 1 119 ? -7.680  -2.498  16.312  1.00 7.95   ? 119 HIS A ND1 1 
ATOM   1040 C  CD2 . HIS A 1 119 ? -9.607  -3.015  17.299  1.00 8.42   ? 119 HIS A CD2 1 
ATOM   1041 C  CE1 . HIS A 1 119 ? -7.426  -3.416  17.265  1.00 8.27   ? 119 HIS A CE1 1 
ATOM   1042 N  NE2 . HIS A 1 119 ? -8.572  -3.774  17.844  1.00 8.19   ? 119 HIS A NE2 1 
ATOM   1043 N  N   . LEU A 1 120 ? -12.779 0.308   15.301  1.00 7.13   ? 120 LEU A N   1 
ATOM   1044 C  CA  . LEU A 1 120 ? -13.415 1.540   14.836  1.00 7.84   ? 120 LEU A CA  1 
ATOM   1045 C  C   . LEU A 1 120 ? -12.794 2.705   15.670  1.00 6.92   ? 120 LEU A C   1 
ATOM   1046 O  O   . LEU A 1 120 ? -12.915 2.715   16.869  1.00 6.92   ? 120 LEU A O   1 
ATOM   1047 C  CB  . LEU A 1 120 ? -14.935 1.469   15.068  1.00 8.63   ? 120 LEU A CB  1 
ATOM   1048 C  CG  . LEU A 1 120 ? -15.648 0.452   14.195  1.00 9.21   ? 120 LEU A CG  1 
ATOM   1049 C  CD1 . LEU A 1 120 ? -16.517 -0.506  15.054  1.00 14.24  ? 120 LEU A CD1 1 
ATOM   1050 C  CD2 . LEU A 1 120 ? -16.489 1.115   13.084  1.00 10.75  ? 120 LEU A CD2 1 
ATOM   1051 N  N   . VAL A 1 121 ? -12.036 3.556   14.961  1.00 7.80   ? 121 VAL A N   1 
ATOM   1052 C  CA  . VAL A 1 121 ? -11.134 4.564   15.635  1.00 7.71   ? 121 VAL A CA  1 
ATOM   1053 C  C   . VAL A 1 121 ? -11.856 5.954   15.648  1.00 7.76   ? 121 VAL A C   1 
ATOM   1054 O  O   . VAL A 1 121 ? -12.266 6.395   14.582  1.00 8.25   ? 121 VAL A O   1 
ATOM   1055 C  CB  . VAL A 1 121 ? -9.830  4.691   14.853  1.00 8.21   ? 121 VAL A CB  1 
ATOM   1056 C  CG1 . VAL A 1 121 ? -8.903  5.710   15.534  1.00 9.41   ? 121 VAL A CG1 1 
ATOM   1057 C  CG2 . VAL A 1 121 ? -9.115  3.357   14.720  1.00 8.95   ? 121 VAL A CG2 1 
ATOM   1058 N  N   . HIS A 1 122 ? -11.962 6.477   16.849  1.00 7.86   ? 122 HIS A N   1 
ATOM   1059 C  CA  . HIS A 1 122 ? -12.655 7.725   17.014  1.00 8.66   ? 122 HIS A CA  1 
ATOM   1060 C  C   . HIS A 1 122 ? -11.778 8.708   17.734  1.00 8.15   ? 122 HIS A C   1 
ATOM   1061 O  O   . HIS A 1 122 ? -10.991 8.327   18.609  1.00 8.64   ? 122 HIS A O   1 
ATOM   1062 C  CB  . HIS A 1 122 ? -13.940 7.595   17.877  1.00 8.04   ? 122 HIS A CB  1 
ATOM   1063 C  CG  . HIS A 1 122 ? -14.857 6.444   17.487  1.00 8.29   ? 122 HIS A CG  1 
ATOM   1064 N  ND1 . HIS A 1 122 ? -14.552 5.141   17.679  1.00 8.42   ? 122 HIS A ND1 1 
ATOM   1065 C  CD2 . HIS A 1 122 ? -16.102 6.427   16.852  1.00 9.61   ? 122 HIS A CD2 1 
ATOM   1066 C  CE1 . HIS A 1 122 ? -15.560 4.379   17.257  1.00 9.64   ? 122 HIS A CE1 1 
ATOM   1067 N  NE2 . HIS A 1 122 ? -16.521 5.151   16.743  1.00 9.40   ? 122 HIS A NE2 1 
ATOM   1068 N  N   . TRP A 1 123 ? -11.918 10.035  17.476  1.00 8.78   ? 123 TRP A N   1 
ATOM   1069 C  CA  . TRP A 1 123 ? -11.089 11.024  18.172  1.00 8.95   ? 123 TRP A CA  1 
ATOM   1070 C  C   . TRP A 1 123 ? -11.956 12.022  18.919  1.00 8.43   ? 123 TRP A C   1 
ATOM   1071 O  O   . TRP A 1 123 ? -13.073 12.398  18.487  1.00 10.27  ? 123 TRP A O   1 
ATOM   1072 C  CB  . TRP A 1 123 ? -10.166 11.807  17.211  1.00 10.44  ? 123 TRP A CB  1 
ATOM   1073 C  CG  . TRP A 1 123 ? -10.803 12.370  15.992  1.00 11.25  ? 123 TRP A CG  1 
ATOM   1074 C  CD1 . TRP A 1 123 ? -11.010 11.743  14.780  1.00 13.71  ? 123 TRP A CD1 1 
ATOM   1075 C  CD2 . TRP A 1 123 ? -11.283 13.714  15.797  1.00 12.23  ? 123 TRP A CD2 1 
ATOM   1076 N  NE1 . TRP A 1 123 ? -11.599 12.562  13.859  1.00 13.67  ? 123 TRP A NE1 1 
ATOM   1077 C  CE2 . TRP A 1 123 ? -11.763 13.790  14.436  1.00 12.89  ? 123 TRP A CE2 1 
ATOM   1078 C  CE3 . TRP A 1 123 ? -11.364 14.847  16.603  1.00 13.63  ? 123 TRP A CE3 1 
ATOM   1079 C  CZ2 . TRP A 1 123 ? -12.314 14.960  13.923  1.00 15.46  ? 123 TRP A CZ2 1 
ATOM   1080 C  CZ3 . TRP A 1 123 ? -11.928 15.986  16.101  1.00 13.44  ? 123 TRP A CZ3 1 
ATOM   1081 C  CH2 . TRP A 1 123 ? -12.357 16.073  14.774  1.00 16.49  ? 123 TRP A CH2 1 
ATOM   1082 N  N   . ASN A 1 124 ? -11.438 12.460  20.021  1.00 9.51   ? 124 ASN A N   1 
ATOM   1083 C  CA  . ASN A 1 124 ? -12.189 13.381  20.932  1.00 10.96  ? 124 ASN A CA  1 
ATOM   1084 C  C   . ASN A 1 124 ? -12.304 14.762  20.333  1.00 11.04  ? 124 ASN A C   1 
ATOM   1085 O  O   . ASN A 1 124 ? -11.275 15.391  19.993  1.00 11.19  ? 124 ASN A O   1 
ATOM   1086 C  CB  . ASN A 1 124 ? -11.341 13.438  22.202  1.00 12.01  ? 124 ASN A CB  1 
ATOM   1087 C  CG  . ASN A 1 124 ? -12.072 14.043  23.394  1.00 11.39  ? 124 ASN A CG  1 
ATOM   1088 O  OD1 . ASN A 1 124 ? -12.904 14.981  23.189  1.00 15.01  ? 124 ASN A OD1 1 
ATOM   1089 N  ND2 . ASN A 1 124 ? -11.726 13.654  24.660  1.00 14.78  ? 124 ASN A ND2 1 
ATOM   1090 N  N   . THR A 1 125 ? -13.523 15.198  20.123  1.00 12.50  ? 125 THR A N   1 
ATOM   1091 C  CA  . THR A 1 125 ? -13.722 16.475  19.403  1.00 13.69  ? 125 THR A CA  1 
ATOM   1092 C  C   . THR A 1 125 ? -13.162 17.668  20.128  1.00 13.09  ? 125 THR A C   1 
ATOM   1093 O  O   . THR A 1 125 ? -12.964 18.718  19.507  1.00 17.28  ? 125 THR A O   1 
ATOM   1094 C  CB  . THR A 1 125 ? -15.239 16.685  19.112  1.00 17.79  ? 125 THR A CB  1 
ATOM   1095 O  OG1 . THR A 1 125 ? -15.978 16.712  20.351  1.00 20.12  ? 125 THR A OG1 1 
ATOM   1096 C  CG2 . THR A 1 125 ? -15.816 15.653  18.176  1.00 19.05  ? 125 THR A CG2 1 
ATOM   1097 N  N   . LYS A 1 126 ? -12.828 17.554  21.484  1.00 14.24  ? 126 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 126 ? -12.283 18.720  22.141  1.00 21.06  ? 126 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 126 ? -10.871 18.982  21.571  1.00 16.44  ? 126 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 126 ? -10.359 20.069  21.806  1.00 20.91  ? 126 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 126 ? -12.374 18.492  23.655  1.00 24.25  ? 126 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 126 ? -11.312 17.618  24.231  1.00 22.12  ? 126 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 126 ? -11.406 17.680  25.743  1.00 34.28  ? 126 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 126 ? -10.659 16.546  26.392  1.00 32.72  ? 126 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 126 ? -9.924  17.051  27.601  1.00 44.14  ? 126 LYS A NZ  1 
ATOM   1106 N  N   . TYR A 1 127 ? -10.262 18.077  20.778  1.00 12.72  ? 127 TYR A N   1 
ATOM   1107 C  CA  . TYR A 1 127 ? -8.912  18.314  20.229  1.00 12.42  ? 127 TYR A CA  1 
ATOM   1108 C  C   . TYR A 1 127 ? -8.930  18.651  18.744  1.00 11.20  ? 127 TYR A C   1 
ATOM   1109 O  O   . TYR A 1 127 ? -7.859  18.864  18.132  1.00 14.63  ? 127 TYR A O   1 
ATOM   1110 C  CB  . TYR A 1 127 ? -7.961  17.105  20.520  1.00 13.50  ? 127 TYR A CB  1 
ATOM   1111 C  CG  . TYR A 1 127 ? -7.863  16.831  22.004  1.00 13.67  ? 127 TYR A CG  1 
ATOM   1112 C  CD1 . TYR A 1 127 ? -7.438  17.866  22.883  1.00 15.57  ? 127 TYR A CD1 1 
ATOM   1113 C  CD2 . TYR A 1 127 ? -8.129  15.609  22.542  1.00 12.57  ? 127 TYR A CD2 1 
ATOM   1114 C  CE1 . TYR A 1 127 ? -7.398  17.664  24.235  1.00 17.72  ? 127 TYR A CE1 1 
ATOM   1115 C  CE2 . TYR A 1 127 ? -8.049  15.348  23.872  1.00 13.56  ? 127 TYR A CE2 1 
ATOM   1116 C  CZ  . TYR A 1 127 ? -7.624  16.396  24.743  1.00 15.84  ? 127 TYR A CZ  1 
ATOM   1117 O  OH  . TYR A 1 127 ? -7.564  16.201  26.100  1.00 17.22  ? 127 TYR A OH  1 
ATOM   1118 N  N   . GLY A 1 128 ? -10.121 18.703  18.116  1.00 13.26  ? 128 GLY A N   1 
ATOM   1119 C  CA  . GLY A 1 128 ? -10.182 19.299  16.815  1.00 14.80  ? 128 GLY A CA  1 
ATOM   1120 C  C   . GLY A 1 128 ? -9.822  18.458  15.577  1.00 13.43  ? 128 GLY A C   1 
ATOM   1121 O  O   . GLY A 1 128 ? -10.394 18.629  14.540  1.00 20.79  ? 128 GLY A O   1 
ATOM   1122 N  N   A ASP A 1 129 ? -8.854  17.554  15.766  0.50 15.27  ? 129 ASP A N   1 
ATOM   1123 N  N   B ASP A 1 129 ? -8.794  17.603  15.684  0.50 14.95  ? 129 ASP A N   1 
ATOM   1124 C  CA  A ASP A 1 129 ? -8.354  16.732  14.671  0.50 15.62  ? 129 ASP A CA  1 
ATOM   1125 C  CA  B ASP A 1 129 ? -8.260  16.802  14.539  0.50 15.72  ? 129 ASP A CA  1 
ATOM   1126 C  C   A ASP A 1 129 ? -7.688  15.470  15.172  0.50 13.22  ? 129 ASP A C   1 
ATOM   1127 C  C   B ASP A 1 129 ? -7.830  15.490  15.177  0.50 17.09  ? 129 ASP A C   1 
ATOM   1128 O  O   A ASP A 1 129 ? -7.122  15.424  16.278  0.50 13.19  ? 129 ASP A O   1 
ATOM   1129 O  O   B ASP A 1 129 ? -7.619  15.452  16.422  0.50 17.37  ? 129 ASP A O   1 
ATOM   1130 C  CB  A ASP A 1 129 ? -7.426  17.517  13.683  0.50 15.54  ? 129 ASP A CB  1 
ATOM   1131 C  CB  B ASP A 1 129 ? -7.096  17.580  13.830  0.50 16.57  ? 129 ASP A CB  1 
ATOM   1132 C  CG  A ASP A 1 129 ? -6.026  17.880  14.258  0.50 20.80  ? 129 ASP A CG  1 
ATOM   1133 C  CG  B ASP A 1 129 ? -6.167  16.700  12.900  0.50 21.08  ? 129 ASP A CG  1 
ATOM   1134 O  OD1 A ASP A 1 129 ? -5.103  17.021  14.359  0.50 15.98  ? 129 ASP A OD1 1 
ATOM   1135 O  OD1 B ASP A 1 129 ? -6.421  16.466  11.679  0.50 25.99  ? 129 ASP A OD1 1 
ATOM   1136 O  OD2 A ASP A 1 129 ? -5.753  19.110  14.447  0.50 19.05  ? 129 ASP A OD2 1 
ATOM   1137 O  OD2 B ASP A 1 129 ? -5.092  16.326  13.396  0.50 19.76  ? 129 ASP A OD2 1 
ATOM   1138 N  N   . ALA A 1 130 ? -7.775  14.421  14.374  1.00 14.73  ? 130 ALA A N   1 
ATOM   1139 C  CA  . ALA A 1 130 ? -7.276  13.127  14.823  1.00 14.32  ? 130 ALA A CA  1 
ATOM   1140 C  C   . ALA A 1 130 ? -5.777  13.130  15.211  1.00 14.89  ? 130 ALA A C   1 
ATOM   1141 O  O   . ALA A 1 130 ? -5.406  12.537  16.219  1.00 13.76  ? 130 ALA A O   1 
ATOM   1142 C  CB  . ALA A 1 130 ? -7.526  12.116  13.746  1.00 16.09  ? 130 ALA A CB  1 
ATOM   1143 N  N   . GLY A 1 131 ? -4.908  13.871  14.448  1.00 16.99  ? 131 GLY A N   1 
ATOM   1144 C  CA  . GLY A 1 131 ? -3.457  13.898  14.735  1.00 20.03  ? 131 GLY A CA  1 
ATOM   1145 C  C   . GLY A 1 131 ? -3.261  14.559  16.086  1.00 14.48  ? 131 GLY A C   1 
ATOM   1146 O  O   . GLY A 1 131 ? -2.482  14.030  16.926  1.00 16.93  ? 131 GLY A O   1 
ATOM   1147 N  N   . LYS A 1 132 ? -3.881  15.733  16.283  1.00 17.37  ? 132 LYS A N   1 
ATOM   1148 C  CA  . LYS A 1 132 ? -3.727  16.387  17.571  1.00 16.54  ? 132 LYS A CA  1 
ATOM   1149 C  C   . LYS A 1 132 ? -4.271  15.506  18.657  1.00 11.32  ? 132 LYS A C   1 
ATOM   1150 O  O   . LYS A 1 132 ? -3.694  15.413  19.720  1.00 13.99  ? 132 LYS A O   1 
ATOM   1151 C  CB  . LYS A 1 132 ? -4.383  17.813  17.636  1.00 22.11  ? 132 LYS A CB  1 
ATOM   1152 C  CG  . LYS A 1 132 ? -3.834  18.785  16.625  1.00 25.24  ? 132 LYS A CG  1 
ATOM   1153 C  CD  . LYS A 1 132 ? -2.318  18.812  16.612  1.00 36.87  ? 132 LYS A CD  1 
ATOM   1154 C  CE  . LYS A 1 132 ? -1.782  19.615  15.426  1.00 51.80  ? 132 LYS A CE  1 
ATOM   1155 N  NZ  . LYS A 1 132 ? -0.360  20.150  15.558  1.00 62.49  ? 132 LYS A NZ  1 
ATOM   1156 N  N   . ALA A 1 133 ? -5.414  14.875  18.424  1.00 12.25  ? 133 ALA A N   1 
ATOM   1157 C  CA  . ALA A 1 133 ? -6.012  14.025  19.490  1.00 12.30  ? 133 ALA A CA  1 
ATOM   1158 C  C   . ALA A 1 133 ? -5.061  12.876  19.891  1.00 10.32  ? 133 ALA A C   1 
ATOM   1159 O  O   . ALA A 1 133 ? -4.996  12.514  21.031  1.00 11.82  ? 133 ALA A O   1 
ATOM   1160 C  CB  . ALA A 1 133 ? -7.354  13.420  19.046  1.00 12.51  ? 133 ALA A CB  1 
ATOM   1161 N  N   . SER A 1 134 ? -4.304  12.394  18.914  1.00 11.22  ? 134 SER A N   1 
ATOM   1162 C  CA  . SER A 1 134 ? -3.390  11.233  19.124  1.00 11.03  ? 134 SER A CA  1 
ATOM   1163 C  C   . SER A 1 134 ? -2.260  11.632  20.038  1.00 11.44  ? 134 SER A C   1 
ATOM   1164 O  O   . SER A 1 134 ? -1.521  10.735  20.542  1.00 13.23  ? 134 SER A O   1 
ATOM   1165 C  CB  . SER A 1 134 ? -2.870  10.630  17.843  1.00 13.32  ? 134 SER A CB  1 
ATOM   1166 O  OG  . SER A 1 134 ? -1.863  11.423  17.315  1.00 15.00  ? 134 SER A OG  1 
ATOM   1167 N  N   . GLN A 1 135 ? -2.054  12.948  20.295  1.00 11.93  ? 135 GLN A N   1 
ATOM   1168 C  CA  . GLN A 1 135 ? -1.006  13.416  21.252  1.00 14.22  ? 135 GLN A CA  1 
ATOM   1169 C  C   . GLN A 1 135 ? -1.526  13.614  22.637  1.00 15.21  ? 135 GLN A C   1 
ATOM   1170 O  O   . GLN A 1 135 ? -0.768  14.137  23.477  1.00 19.59  ? 135 GLN A O   1 
ATOM   1171 C  CB  . GLN A 1 135 ? -0.403  14.749  20.754  1.00 18.94  ? 135 GLN A CB  1 
ATOM   1172 C  CG  . GLN A 1 135 ? -0.080  14.789  19.325  1.00 25.33  ? 135 GLN A CG  1 
ATOM   1173 C  CD  . GLN A 1 135 ? 0.910   13.796  18.832  1.00 31.96  ? 135 GLN A CD  1 
ATOM   1174 O  OE1 . GLN A 1 135 ? 1.924   13.529  19.468  1.00 41.64  ? 135 GLN A OE1 1 
ATOM   1175 N  NE2 . GLN A 1 135 ? 0.682   13.329  17.621  1.00 50.67  ? 135 GLN A NE2 1 
ATOM   1176 N  N   . GLN A 1 136 ? -2.765  13.225  22.949  1.00 13.86  ? 136 GLN A N   1 
ATOM   1177 C  CA  . GLN A 1 136 ? -3.393  13.492  24.215  1.00 13.73  ? 136 GLN A CA  1 
ATOM   1178 C  C   . GLN A 1 136 ? -3.746  12.216  24.935  1.00 12.84  ? 136 GLN A C   1 
ATOM   1179 O  O   . GLN A 1 136 ? -4.136  11.250  24.280  1.00 13.70  ? 136 GLN A O   1 
ATOM   1180 C  CB  . GLN A 1 136 ? -4.667  14.355  24.056  1.00 16.45  ? 136 GLN A CB  1 
ATOM   1181 C  CG  . GLN A 1 136 ? -4.416  15.615  23.233  1.00 18.08  ? 136 GLN A CG  1 
ATOM   1182 C  CD  . GLN A 1 136 ? -3.475  16.570  23.890  1.00 20.29  ? 136 GLN A CD  1 
ATOM   1183 O  OE1 . GLN A 1 136 ? -3.374  16.581  25.111  1.00 22.11  ? 136 GLN A OE1 1 
ATOM   1184 N  NE2 . GLN A 1 136 ? -2.769  17.395  23.092  1.00 30.72  ? 136 GLN A NE2 1 
ATOM   1185 N  N   . PRO A 1 137 ? -3.751  12.205  26.264  1.00 14.10  ? 137 PRO A N   1 
ATOM   1186 C  CA  . PRO A 1 137 ? -3.970  10.948  26.991  1.00 14.14  ? 137 PRO A CA  1 
ATOM   1187 C  C   . PRO A 1 137 ? -5.353  10.416  26.856  1.00 13.88  ? 137 PRO A C   1 
ATOM   1188 O  O   . PRO A 1 137 ? -5.514  9.229   27.013  1.00 16.40  ? 137 PRO A O   1 
ATOM   1189 C  CB  . PRO A 1 137 ? -3.622  11.353  28.467  1.00 19.74  ? 137 PRO A CB  1 
ATOM   1190 C  CG  . PRO A 1 137 ? -3.728  12.862  28.479  1.00 22.81  ? 137 PRO A CG  1 
ATOM   1191 C  CD  . PRO A 1 137 ? -3.261  13.289  27.148  1.00 17.15  ? 137 PRO A CD  1 
ATOM   1192 N  N   . ASP A 1 138 ? -6.359  11.267  26.570  1.00 13.26  ? 138 ASP A N   1 
ATOM   1193 C  CA  . ASP A 1 138 ? -7.771  10.908  26.320  1.00 13.67  ? 138 ASP A CA  1 
ATOM   1194 C  C   . ASP A 1 138 ? -8.158  11.296  24.918  1.00 10.28  ? 138 ASP A C   1 
ATOM   1195 O  O   . ASP A 1 138 ? -9.327  11.783  24.667  1.00 13.29  ? 138 ASP A O   1 
ATOM   1196 C  CB  . ASP A 1 138 ? -8.687  11.546  27.345  1.00 16.33  ? 138 ASP A CB  1 
ATOM   1197 C  CG  . ASP A 1 138 ? -8.602  13.088  27.310  1.00 18.21  ? 138 ASP A CG  1 
ATOM   1198 O  OD1 . ASP A 1 138 ? -7.602  13.657  26.700  1.00 16.82  ? 138 ASP A OD1 1 
ATOM   1199 O  OD2 . ASP A 1 138 ? -9.470  13.738  27.929  1.00 23.58  ? 138 ASP A OD2 1 
ATOM   1200 N  N   . GLY A 1 139 ? -7.237  11.196  23.949  1.00 10.19  ? 139 GLY A N   1 
ATOM   1201 C  CA  . GLY A 1 139 ? -7.468  11.633  22.609  1.00 10.37  ? 139 GLY A CA  1 
ATOM   1202 C  C   . GLY A 1 139 ? -8.356  10.788  21.757  1.00 8.54   ? 139 GLY A C   1 
ATOM   1203 O  O   . GLY A 1 139 ? -9.074  11.265  20.901  1.00 9.26   ? 139 GLY A O   1 
ATOM   1204 N  N   . LEU A 1 140 ? -8.218  9.442   21.898  1.00 8.83   ? 140 LEU A N   1 
ATOM   1205 C  CA  . LEU A 1 140 ? -8.899  8.511   21.021  1.00 7.88   ? 140 LEU A CA  1 
ATOM   1206 C  C   . LEU A 1 140 ? -9.737  7.521   21.794  1.00 7.51   ? 140 LEU A C   1 
ATOM   1207 O  O   . LEU A 1 140 ? -9.457  7.256   22.972  1.00 8.55   ? 140 LEU A O   1 
ATOM   1208 C  CB  . LEU A 1 140 ? -7.908  7.739   20.142  1.00 9.28   ? 140 LEU A CB  1 
ATOM   1209 C  CG  . LEU A 1 140 ? -6.917  8.468   19.258  1.00 11.27  ? 140 LEU A CG  1 
ATOM   1210 C  CD1 . LEU A 1 140 ? -6.103  7.458   18.466  1.00 11.95  ? 140 LEU A CD1 1 
ATOM   1211 C  CD2 . LEU A 1 140 ? -7.544  9.509   18.352  1.00 12.15  ? 140 LEU A CD2 1 
ATOM   1212 N  N   . ALA A 1 141 ? -10.817 7.041   21.162  1.00 8.73   ? 141 ALA A N   1 
ATOM   1213 C  CA  . ALA A 1 141 ? -11.561 5.932   21.690  1.00 8.42   ? 141 ALA A CA  1 
ATOM   1214 C  C   . ALA A 1 141 ? -11.643 4.941   20.568  1.00 7.68   ? 141 ALA A C   1 
ATOM   1215 O  O   . ALA A 1 141 ? -12.108 5.249   19.447  1.00 8.87   ? 141 ALA A O   1 
ATOM   1216 C  CB  . ALA A 1 141 ? -12.954 6.352   22.130  1.00 10.72  ? 141 ALA A CB  1 
ATOM   1217 N  N   . VAL A 1 142 ? -11.166 3.700   20.811  1.00 7.87   ? 142 VAL A N   1 
ATOM   1218 C  CA  . VAL A 1 142 ? -11.233 2.622   19.823  1.00 7.84   ? 142 VAL A CA  1 
ATOM   1219 C  C   . VAL A 1 142 ? -12.197 1.565   20.282  1.00 6.71   ? 142 VAL A C   1 
ATOM   1220 O  O   . VAL A 1 142 ? -12.064 1.088   21.414  1.00 7.82   ? 142 VAL A O   1 
ATOM   1221 C  CB  . VAL A 1 142 ? -9.841  2.052   19.471  1.00 7.64   ? 142 VAL A CB  1 
ATOM   1222 C  CG1 . VAL A 1 142 ? -10.016 1.005   18.345  1.00 9.08   ? 142 VAL A CG1 1 
ATOM   1223 C  CG2 . VAL A 1 142 ? -8.897  3.171   19.041  1.00 8.68   ? 142 VAL A CG2 1 
ATOM   1224 N  N   . LEU A 1 143 ? -13.220 1.342   19.453  1.00 7.20   ? 143 LEU A N   1 
ATOM   1225 C  CA  . LEU A 1 143 ? -14.212 0.295   19.709  1.00 8.22   ? 143 LEU A CA  1 
ATOM   1226 C  C   . LEU A 1 143 ? -13.727 -0.977  19.008  1.00 7.05   ? 143 LEU A C   1 
ATOM   1227 O  O   . LEU A 1 143 ? -13.556 -0.967  17.793  1.00 8.04   ? 143 LEU A O   1 
ATOM   1228 C  CB  . LEU A 1 143 ? -15.560 0.786   19.126  1.00 8.96   ? 143 LEU A CB  1 
ATOM   1229 C  CG  . LEU A 1 143 ? -16.757 -0.201  19.302  1.00 10.65  ? 143 LEU A CG  1 
ATOM   1230 C  CD1 . LEU A 1 143 ? -17.015 -0.428  20.779  1.00 13.71  ? 143 LEU A CD1 1 
ATOM   1231 C  CD2 . LEU A 1 143 ? -17.985 0.403   18.615  1.00 11.92  ? 143 LEU A CD2 1 
ATOM   1232 N  N   . GLY A 1 144 ? -13.449 -1.999  19.820  1.00 7.59   ? 144 GLY A N   1 
ATOM   1233 C  CA  . GLY A 1 144 ? -12.895 -3.268  19.301  1.00 8.30   ? 144 GLY A CA  1 
ATOM   1234 C  C   . GLY A 1 144 ? -13.980 -4.354  19.324  1.00 7.30   ? 144 GLY A C   1 
ATOM   1235 O  O   . GLY A 1 144 ? -14.712 -4.478  20.291  1.00 8.78   ? 144 GLY A O   1 
ATOM   1236 N  N   . ILE A 1 145 ? -14.048 -5.087  18.196  1.00 7.47   ? 145 ILE A N   1 
ATOM   1237 C  CA  . ILE A 1 145 ? -15.047 -6.160  18.036  1.00 8.05   ? 145 ILE A CA  1 
ATOM   1238 C  C   . ILE A 1 145 ? -14.311 -7.383  17.522  1.00 7.64   ? 145 ILE A C   1 
ATOM   1239 O  O   . ILE A 1 145 ? -13.599 -7.331  16.517  1.00 8.24   ? 145 ILE A O   1 
ATOM   1240 C  CB  . ILE A 1 145 ? -16.129 -5.700  17.058  1.00 8.29   ? 145 ILE A CB  1 
ATOM   1241 C  CG1 . ILE A 1 145 ? -16.799 -4.413  17.582  1.00 10.74  ? 145 ILE A CG1 1 
ATOM   1242 C  CG2 . ILE A 1 145 ? -17.148 -6.798  16.836  1.00 10.29  ? 145 ILE A CG2 1 
ATOM   1243 C  CD1 . ILE A 1 145 ? -17.824 -3.773  16.641  1.00 11.13  ? 145 ILE A CD1 1 
ATOM   1244 N  N   . PHE A 1 146 ? -14.518 -8.513  18.223  1.00 8.02   ? 146 PHE A N   1 
ATOM   1245 C  CA  . PHE A 1 146 ? -13.900 -9.803  17.794  1.00 8.24   ? 146 PHE A CA  1 
ATOM   1246 C  C   . PHE A 1 146 ? -14.676 -10.403 16.654  1.00 8.29   ? 146 PHE A C   1 
ATOM   1247 O  O   . PHE A 1 146 ? -15.899 -10.290 16.591  1.00 9.84   ? 146 PHE A O   1 
ATOM   1248 C  CB  . PHE A 1 146 ? -13.903 -10.745 19.026  1.00 9.34   ? 146 PHE A CB  1 
ATOM   1249 C  CG  . PHE A 1 146 ? -13.065 -10.261 20.135  1.00 8.19   ? 146 PHE A CG  1 
ATOM   1250 C  CD1 . PHE A 1 146 ? -11.660 -10.098 19.980  1.00 8.85   ? 146 PHE A CD1 1 
ATOM   1251 C  CD2 . PHE A 1 146 ? -13.615 -9.993  21.361  1.00 8.50   ? 146 PHE A CD2 1 
ATOM   1252 C  CE1 . PHE A 1 146 ? -10.884 -9.715  21.078  1.00 8.80   ? 146 PHE A CE1 1 
ATOM   1253 C  CE2 . PHE A 1 146 ? -12.844 -9.610  22.462  1.00 9.42   ? 146 PHE A CE2 1 
ATOM   1254 C  CZ  . PHE A 1 146 ? -11.451 -9.448  22.289  1.00 8.95   ? 146 PHE A CZ  1 
ATOM   1255 N  N   . LEU A 1 147 ? -13.937 -11.109 15.799  1.00 8.96   ? 147 LEU A N   1 
ATOM   1256 C  CA  . LEU A 1 147 ? -14.544 -11.884 14.729  1.00 9.48   ? 147 LEU A CA  1 
ATOM   1257 C  C   . LEU A 1 147 ? -14.195 -13.364 14.937  1.00 9.12   ? 147 LEU A C   1 
ATOM   1258 O  O   . LEU A 1 147 ? -13.020 -13.721 15.111  1.00 10.75  ? 147 LEU A O   1 
ATOM   1259 C  CB  . LEU A 1 147 ? -13.954 -11.489 13.369  1.00 10.25  ? 147 LEU A CB  1 
ATOM   1260 C  CG  . LEU A 1 147 ? -14.522 -10.214 12.708  1.00 9.76   ? 147 LEU A CG  1 
ATOM   1261 C  CD1 . LEU A 1 147 ? -14.339 -8.938  13.549  1.00 10.83  ? 147 LEU A CD1 1 
ATOM   1262 C  CD2 . LEU A 1 147 ? -13.907 -9.991  11.316  1.00 11.27  ? 147 LEU A CD2 1 
ATOM   1263 N  N   . LYS A 1 148 ? -15.239 -14.213 14.925  1.00 9.99   ? 148 LYS A N   1 
ATOM   1264 C  CA  . LYS A 1 148 ? -15.054 -15.672 14.900  1.00 10.59  ? 148 LYS A CA  1 
ATOM   1265 C  C   . LYS A 1 148 ? -15.558 -16.159 13.561  1.00 10.62  ? 148 LYS A C   1 
ATOM   1266 O  O   . LYS A 1 148 ? -16.378 -15.524 12.930  1.00 12.21  ? 148 LYS A O   1 
ATOM   1267 C  CB  . LYS A 1 148 ? -15.854 -16.325 16.045  1.00 13.00  ? 148 LYS A CB  1 
ATOM   1268 C  CG  . LYS A 1 148 ? -17.369 -16.171 16.001  1.00 15.47  ? 148 LYS A CG  1 
ATOM   1269 C  CD  . LYS A 1 148 ? -17.927 -16.958 17.173  1.00 22.74  ? 148 LYS A CD  1 
ATOM   1270 C  CE  . LYS A 1 148 ? -19.433 -16.993 17.038  1.00 32.76  ? 148 LYS A CE  1 
ATOM   1271 N  NZ  . LYS A 1 148 ? -20.013 -17.916 18.045  1.00 41.54  ? 148 LYS A NZ  1 
ATOM   1272 N  N   . VAL A 1 149 ? -15.096 -17.348 13.172  1.00 12.01  ? 149 VAL A N   1 
ATOM   1273 C  CA  . VAL A 1 149 ? -15.441 -17.869 11.879  1.00 12.63  ? 149 VAL A CA  1 
ATOM   1274 C  C   . VAL A 1 149 ? -16.623 -18.858 12.017  1.00 13.24  ? 149 VAL A C   1 
ATOM   1275 O  O   . VAL A 1 149 ? -16.612 -19.837 12.823  1.00 15.31  ? 149 VAL A O   1 
ATOM   1276 C  CB  . VAL A 1 149 ? -14.199 -18.558 11.227  1.00 12.54  ? 149 VAL A CB  1 
ATOM   1277 C  CG1 . VAL A 1 149 ? -14.611 -19.344 10.010  1.00 14.79  ? 149 VAL A CG1 1 
ATOM   1278 C  CG2 . VAL A 1 149 ? -13.177 -17.512 10.873  1.00 15.52  ? 149 VAL A CG2 1 
ATOM   1279 N  N   . GLY A 1 150 ? -17.656 -18.599 11.217  1.00 11.83  ? 150 GLY A N   1 
ATOM   1280 C  CA  . GLY A 1 150 ? -18.862 -19.430 11.301  1.00 13.78  ? 150 GLY A CA  1 
ATOM   1281 C  C   . GLY A 1 150 ? -19.805 -18.953 10.212  1.00 11.21  ? 150 GLY A C   1 
ATOM   1282 O  O   . GLY A 1 150 ? -19.487 -19.002 9.049   1.00 12.23  ? 150 GLY A O   1 
ATOM   1283 N  N   A SER A 1 151 ? -21.006 -18.495 10.582  0.50 13.20  ? 151 SER A N   1 
ATOM   1284 N  N   B SER A 1 151 ? -20.952 -18.435 10.627  0.50 13.47  ? 151 SER A N   1 
ATOM   1285 C  CA  A SER A 1 151 ? -21.931 -17.900 9.567   0.50 15.64  ? 151 SER A CA  1 
ATOM   1286 C  CA  B SER A 1 151 ? -21.892 -17.795 9.695   0.50 12.97  ? 151 SER A CA  1 
ATOM   1287 C  C   A SER A 1 151 ? -21.373 -16.534 9.108   0.50 12.07  ? 151 SER A C   1 
ATOM   1288 C  C   B SER A 1 151 ? -21.234 -16.535 9.054   0.50 11.31  ? 151 SER A C   1 
ATOM   1289 O  O   A SER A 1 151 ? -20.724 -15.820 9.896   0.50 11.09  ? 151 SER A O   1 
ATOM   1290 O  O   B SER A 1 151 ? -20.330 -15.917 9.624   0.50 11.95  ? 151 SER A O   1 
ATOM   1291 C  CB  A SER A 1 151 ? -23.348 -17.638 10.105  0.50 19.04  ? 151 SER A CB  1 
ATOM   1292 C  CB  B SER A 1 151 ? -23.169 -17.387 10.440  0.50 14.42  ? 151 SER A CB  1 
ATOM   1293 O  OG  A SER A 1 151 ? -23.336 -16.694 11.173  0.50 24.79  ? 151 SER A OG  1 
ATOM   1294 O  OG  B SER A 1 151 ? -23.840 -18.554 10.868  0.50 20.79  ? 151 SER A OG  1 
ATOM   1295 N  N   . ALA A 1 152 ? -21.675 -16.165 7.864   1.00 11.78  ? 152 ALA A N   1 
ATOM   1296 C  CA  . ALA A 1 152 ? -21.212 -14.911 7.250   1.00 12.29  ? 152 ALA A CA  1 
ATOM   1297 C  C   . ALA A 1 152 ? -21.886 -13.723 7.911   1.00 10.46  ? 152 ALA A C   1 
ATOM   1298 O  O   . ALA A 1 152 ? -22.976 -13.788 8.464   1.00 13.37  ? 152 ALA A O   1 
ATOM   1299 C  CB  . ALA A 1 152 ? -21.578 -14.909 5.747   1.00 13.81  ? 152 ALA A CB  1 
ATOM   1300 N  N   . LYS A 1 153 ? -21.184 -12.598 7.881   1.00 9.72   ? 153 LYS A N   1 
ATOM   1301 C  CA  . LYS A 1 153 ? -21.748 -11.328 8.301   1.00 9.97   ? 153 LYS A CA  1 
ATOM   1302 C  C   . LYS A 1 153 ? -22.168 -10.569 7.053   1.00 9.82   ? 153 LYS A C   1 
ATOM   1303 O  O   . LYS A 1 153 ? -21.321 -10.096 6.278   1.00 10.48  ? 153 LYS A O   1 
ATOM   1304 C  CB  . LYS A 1 153 ? -20.669 -10.520 9.071   1.00 10.16  ? 153 LYS A CB  1 
ATOM   1305 C  CG  . LYS A 1 153 ? -21.255 -9.307  9.775   1.00 11.47  ? 153 LYS A CG  1 
ATOM   1306 C  CD  . LYS A 1 153 ? -22.209 -9.642  10.937  1.00 12.74  ? 153 LYS A CD  1 
ATOM   1307 C  CE  . LYS A 1 153 ? -22.561 -8.440  11.873  1.00 16.11  ? 153 LYS A CE  1 
ATOM   1308 N  NZ  . LYS A 1 153 ? -23.695 -8.883  12.737  1.00 23.39  ? 153 LYS A NZ  1 
ATOM   1309 N  N   . PRO A 1 154 ? -23.460 -10.426 6.778   1.00 9.92   ? 154 PRO A N   1 
ATOM   1310 C  CA  . PRO A 1 154 ? -23.841 -9.857  5.470   1.00 11.36  ? 154 PRO A CA  1 
ATOM   1311 C  C   . PRO A 1 154 ? -23.304 -8.373  5.308   1.00 10.16  ? 154 PRO A C   1 
ATOM   1312 O  O   . PRO A 1 154 ? -22.949 -8.035  4.174   1.00 11.44  ? 154 PRO A O   1 
ATOM   1313 C  CB  . PRO A 1 154 ? -25.393 -9.896  5.486   1.00 13.43  ? 154 PRO A CB  1 
ATOM   1314 C  CG  . PRO A 1 154 ? -25.652 -11.085 6.338   1.00 14.19  ? 154 PRO A CG  1 
ATOM   1315 C  CD  . PRO A 1 154 ? -24.624 -11.020 7.473   1.00 11.11  ? 154 PRO A CD  1 
ATOM   1316 N  N   . GLY A 1 155 ? -23.251 -7.643  6.440   1.00 10.47  ? 155 GLY A N   1 
ATOM   1317 C  CA  . GLY A 1 155 ? -22.803 -6.238  6.390   1.00 12.24  ? 155 GLY A CA  1 
ATOM   1318 C  C   . GLY A 1 155 ? -21.330 -6.118  6.058   1.00 10.34  ? 155 GLY A C   1 
ATOM   1319 O  O   . GLY A 1 155 ? -20.865 -4.986  5.827   1.00 13.27  ? 155 GLY A O   1 
ATOM   1320 N  N   . LEU A 1 156 ? -20.527 -7.164  6.183   1.00 9.60   ? 156 LEU A N   1 
ATOM   1321 C  CA  . LEU A 1 156 ? -19.127 -7.133  5.803   1.00 10.02  ? 156 LEU A CA  1 
ATOM   1322 C  C   . LEU A 1 156 ? -18.885 -7.350  4.338   1.00 8.83   ? 156 LEU A C   1 
ATOM   1323 O  O   . LEU A 1 156 ? -17.793 -7.093  3.814   1.00 9.71   ? 156 LEU A O   1 
ATOM   1324 C  CB  . LEU A 1 156 ? -18.407 -8.192  6.648   1.00 11.14  ? 156 LEU A CB  1 
ATOM   1325 C  CG  . LEU A 1 156 ? -16.880 -8.334  6.434   1.00 10.77  ? 156 LEU A CG  1 
ATOM   1326 C  CD1 . LEU A 1 156 ? -16.116 -7.023  6.781   1.00 12.80  ? 156 LEU A CD1 1 
ATOM   1327 C  CD2 . LEU A 1 156 ? -16.366 -9.484  7.307   1.00 12.90  ? 156 LEU A CD2 1 
ATOM   1328 N  N   . GLN A 1 157 ? -19.884 -7.925  3.593   1.00 9.95   ? 157 GLN A N   1 
ATOM   1329 C  CA  . GLN A 1 157 ? -19.586 -8.382  2.262   1.00 9.87   ? 157 GLN A CA  1 
ATOM   1330 C  C   . GLN A 1 157 ? -19.146 -7.235  1.353   1.00 9.19   ? 157 GLN A C   1 
ATOM   1331 O  O   . GLN A 1 157 ? -18.297 -7.474  0.458   1.00 10.39  ? 157 GLN A O   1 
ATOM   1332 C  CB  . GLN A 1 157 ? -20.848 -9.135  1.716   1.00 11.19  ? 157 GLN A CB  1 
ATOM   1333 C  CG  . GLN A 1 157 ? -20.478 -9.908  0.455   1.00 11.51  ? 157 GLN A CG  1 
ATOM   1334 C  CD  . GLN A 1 157 ? -19.413 -10.997 0.676   1.00 10.71  ? 157 GLN A CD  1 
ATOM   1335 O  OE1 . GLN A 1 157 ? -19.280 -11.527 1.790   1.00 12.28  ? 157 GLN A OE1 1 
ATOM   1336 N  NE2 . GLN A 1 157 ? -18.653 -11.271 -0.359  1.00 13.39  ? 157 GLN A NE2 1 
ATOM   1337 N  N   . LYS A 1 158 ? -19.729 -6.021  1.451   1.00 9.94   ? 158 LYS A N   1 
ATOM   1338 C  CA  . LYS A 1 158 ? -19.330 -4.933  0.588   1.00 10.90  ? 158 LYS A CA  1 
ATOM   1339 C  C   . LYS A 1 158 ? -17.803 -4.647  0.731   1.00 9.87   ? 158 LYS A C   1 
ATOM   1340 O  O   . LYS A 1 158 ? -17.158 -4.280  -0.283  1.00 12.44  ? 158 LYS A O   1 
ATOM   1341 C  CB  . LYS A 1 158 ? -20.144 -3.698  0.901   1.00 12.46  ? 158 LYS A CB  1 
ATOM   1342 C  CG  . LYS A 1 158 ? -19.891 -2.480  -0.004  1.00 18.72  ? 158 LYS A CG  1 
ATOM   1343 C  CD  . LYS A 1 158 ? -20.768 -1.257  0.380   1.00 24.94  ? 158 LYS A CD  1 
ATOM   1344 C  CE  . LYS A 1 158 ? -20.417 0.086   -0.308  1.00 30.57  ? 158 LYS A CE  1 
ATOM   1345 N  NZ  . LYS A 1 158 ? -20.904 0.097   -1.722  1.00 27.39  ? 158 LYS A NZ  1 
ATOM   1346 N  N   . VAL A 1 159 ? -17.301 -4.779  1.953   1.00 9.59   ? 159 VAL A N   1 
ATOM   1347 C  CA  . VAL A 1 159 ? -15.859 -4.578  2.182   1.00 10.17  ? 159 VAL A CA  1 
ATOM   1348 C  C   . VAL A 1 159 ? -15.084 -5.729  1.494   1.00 9.35   ? 159 VAL A C   1 
ATOM   1349 O  O   . VAL A 1 159 ? -14.143 -5.470  0.697   1.00 11.07  ? 159 VAL A O   1 
ATOM   1350 C  CB  . VAL A 1 159 ? -15.541 -4.586  3.670   1.00 10.92  ? 159 VAL A CB  1 
ATOM   1351 C  CG1 . VAL A 1 159 ? -14.015 -4.610  3.899   1.00 13.66  ? 159 VAL A CG1 1 
ATOM   1352 C  CG2 . VAL A 1 159 ? -16.116 -3.345  4.360   1.00 16.04  ? 159 VAL A CG2 1 
ATOM   1353 N  N   . VAL A 1 160 ? -15.458 -6.980  1.751   1.00 9.40   ? 160 VAL A N   1 
ATOM   1354 C  CA  . VAL A 1 160 ? -14.629 -8.060  1.207   1.00 11.30  ? 160 VAL A CA  1 
ATOM   1355 C  C   . VAL A 1 160 ? -14.635 -8.050  -0.286  1.00 10.37  ? 160 VAL A C   1 
ATOM   1356 O  O   . VAL A 1 160 ? -13.601 -8.392  -0.903  1.00 11.54  ? 160 VAL A O   1 
ATOM   1357 C  CB  . VAL A 1 160 ? -14.776 -9.442  1.886   1.00 18.56  ? 160 VAL A CB  1 
ATOM   1358 C  CG1 . VAL A 1 160 ? -14.541 -9.395  3.363   1.00 24.30  ? 160 VAL A CG1 1 
ATOM   1359 C  CG2 . VAL A 1 160 ? -16.133 -9.855  1.636   1.00 16.43  ? 160 VAL A CG2 1 
ATOM   1360 N  N   . ASP A 1 161 ? -15.741 -7.659  -0.943  1.00 10.71  ? 161 ASP A N   1 
ATOM   1361 C  CA  . ASP A 1 161 ? -15.815 -7.717  -2.348  1.00 11.75  ? 161 ASP A CA  1 
ATOM   1362 C  C   . ASP A 1 161 ? -14.978 -6.707  -3.081  1.00 12.79  ? 161 ASP A C   1 
ATOM   1363 O  O   . ASP A 1 161 ? -14.738 -6.903  -4.272  1.00 15.75  ? 161 ASP A O   1 
ATOM   1364 C  CB  . ASP A 1 161 ? -17.245 -7.600  -2.837  1.00 13.47  ? 161 ASP A CB  1 
ATOM   1365 C  CG  . ASP A 1 161 ? -18.009 -8.934  -2.758  1.00 13.89  ? 161 ASP A CG  1 
ATOM   1366 O  OD1 . ASP A 1 161 ? -17.356 -10.015 -2.778  1.00 16.76  ? 161 ASP A OD1 1 
ATOM   1367 O  OD2 . ASP A 1 161 ? -19.255 -8.907  -2.694  1.00 15.94  ? 161 ASP A OD2 1 
ATOM   1368 N  N   . VAL A 1 162 ? -14.481 -5.629  -2.434  1.00 12.33  ? 162 VAL A N   1 
ATOM   1369 C  CA  . VAL A 1 162 ? -13.601 -4.737  -3.172  1.00 12.36  ? 162 VAL A CA  1 
ATOM   1370 C  C   . VAL A 1 162 ? -12.119 -4.924  -2.827  1.00 12.57  ? 162 VAL A C   1 
ATOM   1371 O  O   . VAL A 1 162 ? -11.251 -4.238  -3.404  1.00 11.84  ? 162 VAL A O   1 
ATOM   1372 C  CB  . VAL A 1 162 ? -13.958 -3.289  -2.890  1.00 14.46  ? 162 VAL A CB  1 
ATOM   1373 C  CG1 . VAL A 1 162 ? -15.364 -2.983  -3.360  1.00 18.07  ? 162 VAL A CG1 1 
ATOM   1374 C  CG2 . VAL A 1 162 ? -13.614 -2.912  -1.430  1.00 14.49  ? 162 VAL A CG2 1 
ATOM   1375 N  N   . LEU A 1 163 ? -11.791 -5.899  -1.961  1.00 11.27  ? 163 LEU A N   1 
ATOM   1376 C  CA  . LEU A 1 163 ? -10.405 -6.048  -1.577  1.00 10.66  ? 163 LEU A CA  1 
ATOM   1377 C  C   . LEU A 1 163 ? -9.493  -6.450  -2.793  1.00 10.64  ? 163 LEU A C   1 
ATOM   1378 O  O   . LEU A 1 163 ? -8.305  -6.104  -2.786  1.00 12.22  ? 163 LEU A O   1 
ATOM   1379 C  CB  . LEU A 1 163 ? -10.306 -7.088  -0.480  1.00 11.17  ? 163 LEU A CB  1 
ATOM   1380 C  CG  . LEU A 1 163 ? -10.900 -6.677  0.872   1.00 10.91  ? 163 LEU A CG  1 
ATOM   1381 C  CD1 . LEU A 1 163 ? -10.743 -7.762  1.906   1.00 12.89  ? 163 LEU A CD1 1 
ATOM   1382 C  CD2 . LEU A 1 163 ? -10.362 -5.297  1.343   1.00 12.02  ? 163 LEU A CD2 1 
ATOM   1383 N  N   . ASP A 1 164 ? -10.035 -7.144  -3.785  1.00 11.41  ? 164 ASP A N   1 
ATOM   1384 C  CA  . ASP A 1 164 ? -9.189  -7.489  -4.938  1.00 15.01  ? 164 ASP A CA  1 
ATOM   1385 C  C   . ASP A 1 164 ? -8.715  -6.231  -5.676  1.00 14.05  ? 164 ASP A C   1 
ATOM   1386 O  O   . ASP A 1 164 ? -7.692  -6.294  -6.364  1.00 17.03  ? 164 ASP A O   1 
ATOM   1387 C  CB  . ASP A 1 164 ? -9.964  -8.366  -5.926  1.00 18.22  ? 164 ASP A CB  1 
ATOM   1388 C  CG  . ASP A 1 164 ? -11.031 -7.549  -6.686  1.00 20.86  ? 164 ASP A CG  1 
ATOM   1389 O  OD1 . ASP A 1 164 ? -12.028 -7.087  -6.046  1.00 24.34  ? 164 ASP A OD1 1 
ATOM   1390 O  OD2 . ASP A 1 164 ? -10.868 -7.391  -7.937  1.00 32.03  ? 164 ASP A OD2 1 
ATOM   1391 N  N   . SER A 1 165 ? -9.402  -5.080  -5.464  1.00 13.44  ? 165 SER A N   1 
ATOM   1392 C  CA  . SER A 1 165 ? -8.951  -3.826  -6.110  1.00 14.00  ? 165 SER A CA  1 
ATOM   1393 C  C   . SER A 1 165 ? -7.846  -3.121  -5.336  1.00 13.21  ? 165 SER A C   1 
ATOM   1394 O  O   . SER A 1 165 ? -7.317  -2.095  -5.853  1.00 14.11  ? 165 SER A O   1 
ATOM   1395 C  CB  . SER A 1 165 ? -10.127 -2.877  -6.379  1.00 15.28  ? 165 SER A CB  1 
ATOM   1396 O  OG  . SER A 1 165 ? -10.608 -2.340  -5.153  1.00 15.84  ? 165 SER A OG  1 
ATOM   1397 N  N   . ILE A 1 166 ? -7.540  -3.546  -4.126  1.00 10.77  ? 166 ILE A N   1 
ATOM   1398 C  CA  . ILE A 1 166 ? -6.489  -2.877  -3.288  1.00 12.21  ? 166 ILE A CA  1 
ATOM   1399 C  C   . ILE A 1 166 ? -5.497  -3.915  -2.809  1.00 10.09  ? 166 ILE A C   1 
ATOM   1400 O  O   . ILE A 1 166 ? -5.091  -3.901  -1.628  1.00 12.26  ? 166 ILE A O   1 
ATOM   1401 C  CB  . ILE A 1 166 ? -7.106  -2.048  -2.145  1.00 10.98  ? 166 ILE A CB  1 
ATOM   1402 C  CG1 . ILE A 1 166 ? -7.981  -2.886  -1.221  1.00 11.25  ? 166 ILE A CG1 1 
ATOM   1403 C  CG2 . ILE A 1 166 ? -7.898  -0.858  -2.711  1.00 13.54  ? 166 ILE A CG2 1 
ATOM   1404 C  CD1 . ILE A 1 166 ? -8.142  -2.178  0.145   1.00 13.16  ? 166 ILE A CD1 1 
ATOM   1405 N  N   . LYS A 1 167 ? -5.053  -4.818  -3.720  1.00 12.25  ? 167 LYS A N   1 
ATOM   1406 C  CA  . LYS A 1 167 ? -4.287  -5.990  -3.268  1.00 13.75  ? 167 LYS A CA  1 
ATOM   1407 C  C   . LYS A 1 167 ? -2.979  -5.618  -2.617  1.00 14.13  ? 167 LYS A C   1 
ATOM   1408 O  O   . LYS A 1 167 ? -2.602  -6.216  -1.618  1.00 15.39  ? 167 LYS A O   1 
ATOM   1409 C  CB  . LYS A 1 167 ? -4.042  -6.940  -4.486  1.00 16.13  ? 167 LYS A CB  1 
ATOM   1410 C  CG  . LYS A 1 167 ? -3.300  -8.197  -4.069  1.00 20.04  ? 167 LYS A CG  1 
ATOM   1411 C  CD  . LYS A 1 167 ? -2.947  -8.996  -5.311  1.00 26.94  ? 167 LYS A CD  1 
ATOM   1412 C  CE  . LYS A 1 167 ? -2.192  -10.256 -4.971  1.00 32.44  ? 167 LYS A CE  1 
ATOM   1413 N  NZ  . LYS A 1 167 ? -1.708  -10.736 -6.293  1.00 41.40  ? 167 LYS A NZ  1 
ATOM   1414 N  N   . THR A 1 168 ? -2.307  -4.597  -3.168  1.00 15.15  ? 168 THR A N   1 
ATOM   1415 C  CA  . THR A 1 168 ? -0.929  -4.342  -2.719  1.00 18.02  ? 168 THR A CA  1 
ATOM   1416 C  C   . THR A 1 168 ? -0.793  -2.951  -2.084  1.00 17.21  ? 168 THR A C   1 
ATOM   1417 O  O   . THR A 1 168 ? -1.670  -2.079  -2.228  1.00 15.12  ? 168 THR A O   1 
ATOM   1418 C  CB  . THR A 1 168 ? 0.045   -4.436  -3.911  1.00 20.69  ? 168 THR A CB  1 
ATOM   1419 O  OG1 . THR A 1 168 ? -0.497  -3.693  -5.014  1.00 20.97  ? 168 THR A OG1 1 
ATOM   1420 C  CG2 . THR A 1 168 ? 0.270   -5.892  -4.336  1.00 20.87  ? 168 THR A CG2 1 
ATOM   1421 N  N   . LYS A 1 169 ? 0.268   -2.775  -1.322  1.00 15.85  ? 169 LYS A N   1 
ATOM   1422 C  CA  . LYS A 1 169 ? 0.499   -1.569  -0.541  1.00 16.12  ? 169 LYS A CA  1 
ATOM   1423 C  C   . LYS A 1 169 ? 0.429   -0.370  -1.425  1.00 15.86  ? 169 LYS A C   1 
ATOM   1424 O  O   . LYS A 1 169 ? 1.032   -0.271  -2.515  1.00 20.47  ? 169 LYS A O   1 
ATOM   1425 C  CB  . LYS A 1 169 ? 1.923   -1.648  0.019   1.00 17.84  ? 169 LYS A CB  1 
ATOM   1426 C  CG  . LYS A 1 169 ? 2.303   -0.407  0.815   1.00 18.65  ? 169 LYS A CG  1 
ATOM   1427 C  CD  . LYS A 1 169 ? 3.668   -0.580  1.468   1.00 22.45  ? 169 LYS A CD  1 
ATOM   1428 C  CE  . LYS A 1 169 ? 3.960   0.686   2.241   1.00 36.08  ? 169 LYS A CE  1 
ATOM   1429 N  NZ  . LYS A 1 169 ? 5.363   0.584   2.693   1.00 53.01  ? 169 LYS A NZ  1 
ATOM   1430 N  N   . GLY A 1 170 ? -0.351  0.590   -0.962  1.00 14.05  ? 170 GLY A N   1 
ATOM   1431 C  CA  . GLY A 1 170 ? -0.483  1.904   -1.624  1.00 16.97  ? 170 GLY A CA  1 
ATOM   1432 C  C   . GLY A 1 170 ? -1.728  1.996   -2.513  1.00 16.70  ? 170 GLY A C   1 
ATOM   1433 O  O   . GLY A 1 170 ? -2.047  3.068   -3.027  1.00 22.63  ? 170 GLY A O   1 
ATOM   1434 N  N   . LYS A 1 171 ? -2.420  0.895   -2.772  1.00 13.37  ? 171 LYS A N   1 
ATOM   1435 C  CA  . LYS A 1 171 ? -3.640  0.960   -3.642  1.00 13.43  ? 171 LYS A CA  1 
ATOM   1436 C  C   . LYS A 1 171 ? -4.811  1.464   -2.808  1.00 12.51  ? 171 LYS A C   1 
ATOM   1437 O  O   . LYS A 1 171 ? -4.960  1.107   -1.655  1.00 12.34  ? 171 LYS A O   1 
ATOM   1438 C  CB  . LYS A 1 171 ? -3.958  -0.396  -4.249  1.00 14.62  ? 171 LYS A CB  1 
ATOM   1439 C  CG  . LYS A 1 171 ? -2.920  -0.734  -5.312  1.00 17.90  ? 171 LYS A CG  1 
ATOM   1440 C  CD  . LYS A 1 171 ? -3.381  -1.901  -6.140  1.00 21.46  ? 171 LYS A CD  1 
ATOM   1441 C  CE  . LYS A 1 171 ? -4.033  -1.382  -7.408  1.00 31.36  ? 171 LYS A CE  1 
ATOM   1442 N  NZ  . LYS A 1 171 ? -4.554  -2.568  -8.118  1.00 34.68  ? 171 LYS A NZ  1 
ATOM   1443 N  N   . SER A 1 172 ? -5.681  2.277   -3.453  1.00 12.82  ? 172 SER A N   1 
ATOM   1444 C  CA  . SER A 1 172 ? -6.874  2.728   -2.770  1.00 12.16  ? 172 SER A CA  1 
ATOM   1445 C  C   . SER A 1 172 ? -8.035  2.799   -3.780  1.00 12.35  ? 172 SER A C   1 
ATOM   1446 O  O   . SER A 1 172 ? -7.820  2.726   -4.998  1.00 13.79  ? 172 SER A O   1 
ATOM   1447 C  CB  . SER A 1 172 ? -6.680  4.090   -2.107  1.00 14.28  ? 172 SER A CB  1 
ATOM   1448 O  OG  . SER A 1 172 ? -6.432  5.158   -3.019  1.00 17.02  ? 172 SER A OG  1 
ATOM   1449 N  N   . ALA A 1 173 ? -9.257  2.934   -3.254  1.00 12.33  ? 173 ALA A N   1 
ATOM   1450 C  CA  . ALA A 1 173 ? -10.438 3.061   -4.149  1.00 12.81  ? 173 ALA A CA  1 
ATOM   1451 C  C   . ALA A 1 173 ? -11.472 3.898   -3.407  1.00 12.88  ? 173 ALA A C   1 
ATOM   1452 O  O   . ALA A 1 173 ? -11.529 3.919   -2.162  1.00 12.41  ? 173 ALA A O   1 
ATOM   1453 C  CB  . ALA A 1 173 ? -11.043 1.665   -4.429  1.00 15.47  ? 173 ALA A CB  1 
ATOM   1454 N  N   . ASP A 1 174 ? -12.321 4.588   -4.204  1.00 16.17  ? 174 ASP A N   1 
ATOM   1455 C  CA  . ASP A 1 174 ? -13.503 5.230   -3.568  1.00 15.49  ? 174 ASP A CA  1 
ATOM   1456 C  C   . ASP A 1 174 ? -14.357 4.126   -2.891  1.00 12.57  ? 174 ASP A C   1 
ATOM   1457 O  O   . ASP A 1 174 ? -14.451 2.968   -3.349  1.00 15.58  ? 174 ASP A O   1 
ATOM   1458 C  CB  . ASP A 1 174 ? -14.299 5.959   -4.651  1.00 18.83  ? 174 ASP A CB  1 
ATOM   1459 C  CG  . ASP A 1 174 ? -13.557 7.090   -5.272  1.00 29.24  ? 174 ASP A CG  1 
ATOM   1460 O  OD1 . ASP A 1 174 ? -13.125 7.983   -4.526  1.00 40.20  ? 174 ASP A OD1 1 
ATOM   1461 O  OD2 . ASP A 1 174 ? -13.461 7.115   -6.530  1.00 53.21  ? 174 ASP A OD2 1 
ATOM   1462 N  N   . PHE A 1 175 ? -15.014 4.450   -1.790  1.00 10.86  ? 175 PHE A N   1 
ATOM   1463 C  CA  . PHE A 1 175 ? -15.790 3.462   -1.060  1.00 11.44  ? 175 PHE A CA  1 
ATOM   1464 C  C   . PHE A 1 175 ? -16.843 4.236   -0.239  1.00 10.50  ? 175 PHE A C   1 
ATOM   1465 O  O   . PHE A 1 175 ? -16.682 4.468   0.940   1.00 12.64  ? 175 PHE A O   1 
ATOM   1466 C  CB  . PHE A 1 175 ? -14.837 2.685   -0.109  1.00 11.20  ? 175 PHE A CB  1 
ATOM   1467 C  CG  . PHE A 1 175 ? -15.466 1.447   0.439   1.00 10.56  ? 175 PHE A CG  1 
ATOM   1468 C  CD1 . PHE A 1 175 ? -15.758 0.371   -0.426  1.00 12.90  ? 175 PHE A CD1 1 
ATOM   1469 C  CD2 . PHE A 1 175 ? -15.760 1.324   1.780   1.00 11.24  ? 175 PHE A CD2 1 
ATOM   1470 C  CE1 . PHE A 1 175 ? -16.375 -0.800  0.062   1.00 12.55  ? 175 PHE A CE1 1 
ATOM   1471 C  CE2 . PHE A 1 175 ? -16.344 0.152   2.285   1.00 12.81  ? 175 PHE A CE2 1 
ATOM   1472 C  CZ  . PHE A 1 175 ? -16.671 -0.921  1.416   1.00 12.81  ? 175 PHE A CZ  1 
ATOM   1473 N  N   . THR A 1 176 ? -17.937 4.626   -0.931  1.00 11.53  ? 176 THR A N   1 
ATOM   1474 C  CA  . THR A 1 176 ? -18.993 5.430   -0.357  1.00 12.23  ? 176 THR A CA  1 
ATOM   1475 C  C   . THR A 1 176 ? -20.165 4.621   0.063   1.00 9.78   ? 176 THR A C   1 
ATOM   1476 O  O   . THR A 1 176 ? -20.329 3.436   -0.369  1.00 12.31  ? 176 THR A O   1 
ATOM   1477 C  CB  . THR A 1 176 ? -19.484 6.533   -1.308  1.00 13.19  ? 176 THR A CB  1 
ATOM   1478 O  OG1 . THR A 1 176 ? -19.888 5.971   -2.559  1.00 15.88  ? 176 THR A OG1 1 
ATOM   1479 C  CG2 . THR A 1 176 ? -18.411 7.618   -1.530  1.00 19.13  ? 176 THR A CG2 1 
ATOM   1480 N  N   . ASN A 1 177 ? -20.980 5.136   0.956   1.00 10.15  ? 177 ASN A N   1 
ATOM   1481 C  CA  . ASN A 1 177 ? -22.202 4.523   1.366   1.00 11.50  ? 177 ASN A CA  1 
ATOM   1482 C  C   . ASN A 1 177 ? -22.029 3.198   2.078   1.00 12.42  ? 177 ASN A C   1 
ATOM   1483 O  O   . ASN A 1 177 ? -22.955 2.418   2.106   1.00 17.38  ? 177 ASN A O   1 
ATOM   1484 C  CB  . ASN A 1 177 ? -23.243 4.401   0.194   1.00 12.12  ? 177 ASN A CB  1 
ATOM   1485 C  CG  . ASN A 1 177 ? -23.569 5.775   -0.341  1.00 13.47  ? 177 ASN A CG  1 
ATOM   1486 O  OD1 . ASN A 1 177 ? -24.307 6.546   0.282   1.00 16.11  ? 177 ASN A OD1 1 
ATOM   1487 N  ND2 . ASN A 1 177 ? -23.018 6.106   -1.476  1.00 13.80  ? 177 ASN A ND2 1 
ATOM   1488 N  N   . PHE A 1 178 ? -20.892 2.992   2.728   1.00 10.50  ? 178 PHE A N   1 
ATOM   1489 C  CA  . PHE A 1 178 ? -20.746 1.843   3.567   1.00 10.07  ? 178 PHE A CA  1 
ATOM   1490 C  C   . PHE A 1 178 ? -21.284 2.124   4.946   1.00 10.27  ? 178 PHE A C   1 
ATOM   1491 O  O   . PHE A 1 178 ? -20.838 3.114   5.562   1.00 12.01  ? 178 PHE A O   1 
ATOM   1492 C  CB  . PHE A 1 178 ? -19.277 1.373   3.659   1.00 10.47  ? 178 PHE A CB  1 
ATOM   1493 C  CG  . PHE A 1 178 ? -19.195 0.184   4.511   1.00 10.02  ? 178 PHE A CG  1 
ATOM   1494 C  CD1 . PHE A 1 178 ? -19.573 -1.101  3.977   1.00 12.60  ? 178 PHE A CD1 1 
ATOM   1495 C  CD2 . PHE A 1 178 ? -18.806 0.251   5.839   1.00 9.95   ? 178 PHE A CD2 1 
ATOM   1496 C  CE1 . PHE A 1 178 ? -19.566 -2.228  4.791   1.00 11.19  ? 178 PHE A CE1 1 
ATOM   1497 C  CE2 . PHE A 1 178 ? -18.861 -0.913  6.645   1.00 9.88   ? 178 PHE A CE2 1 
ATOM   1498 C  CZ  . PHE A 1 178 ? -19.240 -2.130  6.127   1.00 10.41  ? 178 PHE A CZ  1 
ATOM   1499 N  N   . ASP A 1 179 ? -22.216 1.297   5.444   1.00 10.09  ? 179 ASP A N   1 
ATOM   1500 C  CA  . ASP A 1 179 ? -22.810 1.512   6.773   1.00 10.75  ? 179 ASP A CA  1 
ATOM   1501 C  C   . ASP A 1 179 ? -22.133 0.704   7.831   1.00 9.47   ? 179 ASP A C   1 
ATOM   1502 O  O   . ASP A 1 179 ? -22.312 -0.538  7.893   1.00 10.62  ? 179 ASP A O   1 
ATOM   1503 C  CB  . ASP A 1 179 ? -24.326 1.197   6.684   1.00 12.20  ? 179 ASP A CB  1 
ATOM   1504 C  CG  . ASP A 1 179 ? -25.093 1.565   7.924   1.00 12.59  ? 179 ASP A CG  1 
ATOM   1505 O  OD1 . ASP A 1 179 ? -24.471 1.873   8.960   1.00 12.30  ? 179 ASP A OD1 1 
ATOM   1506 O  OD2 . ASP A 1 179 ? -26.340 1.531   7.853   1.00 19.99  ? 179 ASP A OD2 1 
ATOM   1507 N  N   . PRO A 1 180 ? -21.331 1.301   8.702   1.00 9.85   ? 180 PRO A N   1 
ATOM   1508 C  CA  . PRO A 1 180 ? -20.633 0.490   9.715   1.00 11.31  ? 180 PRO A CA  1 
ATOM   1509 C  C   . PRO A 1 180 ? -21.573 -0.102  10.751  1.00 9.87   ? 180 PRO A C   1 
ATOM   1510 O  O   . PRO A 1 180 ? -21.128 -1.014  11.513  1.00 10.84  ? 180 PRO A O   1 
ATOM   1511 C  CB  . PRO A 1 180 ? -19.635 1.488   10.328  1.00 12.47  ? 180 PRO A CB  1 
ATOM   1512 C  CG  . PRO A 1 180 ? -20.310 2.840   10.144  1.00 12.13  ? 180 PRO A CG  1 
ATOM   1513 C  CD  . PRO A 1 180 ? -20.972 2.750   8.804   1.00 11.41  ? 180 PRO A CD  1 
ATOM   1514 N  N   . ARG A 1 181 ? -22.828 0.283   10.814  1.00 9.86   ? 181 ARG A N   1 
ATOM   1515 C  CA  . ARG A 1 181 ? -23.776 -0.386  11.695  1.00 10.82  ? 181 ARG A CA  1 
ATOM   1516 C  C   . ARG A 1 181 ? -23.912 -1.873  11.362  1.00 10.07  ? 181 ARG A C   1 
ATOM   1517 O  O   . ARG A 1 181 ? -24.269 -2.675  12.222  1.00 11.86  ? 181 ARG A O   1 
ATOM   1518 C  CB  . ARG A 1 181 ? -25.166 0.315   11.648  1.00 10.65  ? 181 ARG A CB  1 
ATOM   1519 C  CG  . ARG A 1 181 ? -25.122 1.710   12.233  1.00 12.88  ? 181 ARG A CG  1 
ATOM   1520 C  CD  . ARG A 1 181 ? -26.394 2.447   12.206  1.00 16.01  ? 181 ARG A CD  1 
ATOM   1521 N  NE  . ARG A 1 181 ? -26.727 2.621   10.784  1.00 14.90  ? 181 ARG A NE  1 
ATOM   1522 C  CZ  . ARG A 1 181 ? -27.753 3.343   10.419  1.00 15.81  ? 181 ARG A CZ  1 
ATOM   1523 N  NH1 . ARG A 1 181 ? -28.490 3.915   11.377  1.00 20.16  ? 181 ARG A NH1 1 
ATOM   1524 N  NH2 . ARG A 1 181 ? -27.976 3.506   9.116   1.00 19.89  ? 181 ARG A NH2 1 
ATOM   1525 N  N   . GLY A 1 182 ? -23.659 -2.211  10.104  1.00 10.81  ? 182 GLY A N   1 
ATOM   1526 C  CA  . GLY A 1 182 ? -23.750 -3.672  9.675   1.00 11.15  ? 182 GLY A CA  1 
ATOM   1527 C  C   . GLY A 1 182 ? -22.609 -4.524  10.164  1.00 10.79  ? 182 GLY A C   1 
ATOM   1528 O  O   . GLY A 1 182 ? -22.636 -5.705  9.877   1.00 12.18  ? 182 GLY A O   1 
ATOM   1529 N  N   . LEU A 1 183 ? -21.656 -3.964  10.936  1.00 10.42  ? 183 LEU A N   1 
ATOM   1530 C  CA  . LEU A 1 183 ? -20.559 -4.716  11.509  1.00 11.04  ? 183 LEU A CA  1 
ATOM   1531 C  C   . LEU A 1 183 ? -20.672 -4.937  12.997  1.00 10.40  ? 183 LEU A C   1 
ATOM   1532 O  O   . LEU A 1 183 ? -19.790 -5.542  13.617  1.00 12.58  ? 183 LEU A O   1 
ATOM   1533 C  CB  . LEU A 1 183 ? -19.239 -3.981  11.246  1.00 11.45  ? 183 LEU A CB  1 
ATOM   1534 C  CG  . LEU A 1 183 ? -18.858 -3.818  9.764   1.00 11.56  ? 183 LEU A CG  1 
ATOM   1535 C  CD1 . LEU A 1 183 ? -17.579 -3.004  9.608   1.00 13.28  ? 183 LEU A CD1 1 
ATOM   1536 C  CD2 . LEU A 1 183 ? -18.765 -5.156  8.991   1.00 14.12  ? 183 LEU A CD2 1 
ATOM   1537 N  N   . LEU A 1 184 ? -21.773 -4.478  13.612  1.00 10.45  ? 184 LEU A N   1 
ATOM   1538 C  CA  . LEU A 1 184 ? -21.872 -4.530  15.064  1.00 10.99  ? 184 LEU A CA  1 
ATOM   1539 C  C   . LEU A 1 184 ? -22.669 -5.759  15.536  1.00 10.42  ? 184 LEU A C   1 
ATOM   1540 O  O   . LEU A 1 184 ? -23.682 -6.129  14.946  1.00 14.70  ? 184 LEU A O   1 
ATOM   1541 C  CB  . LEU A 1 184 ? -22.619 -3.253  15.584  1.00 10.85  ? 184 LEU A CB  1 
ATOM   1542 C  CG  . LEU A 1 184 ? -21.993 -1.925  15.130  1.00 11.29  ? 184 LEU A CG  1 
ATOM   1543 C  CD1 . LEU A 1 184 ? -22.830 -0.762  15.690  1.00 12.81  ? 184 LEU A CD1 1 
ATOM   1544 C  CD2 . LEU A 1 184 ? -20.554 -1.827  15.599  1.00 14.43  ? 184 LEU A CD2 1 
ATOM   1545 N  N   . PRO A 1 185 ? -22.287 -6.329  16.653  1.00 10.08  ? 185 PRO A N   1 
ATOM   1546 C  CA  . PRO A 1 185 ? -23.056 -7.411  17.239  1.00 11.28  ? 185 PRO A CA  1 
ATOM   1547 C  C   . PRO A 1 185 ? -24.339 -6.848  17.943  1.00 9.70   ? 185 PRO A C   1 
ATOM   1548 O  O   . PRO A 1 185 ? -24.532 -5.647  18.017  1.00 11.71  ? 185 PRO A O   1 
ATOM   1549 C  CB  . PRO A 1 185 ? -22.051 -8.016  18.233  1.00 11.69  ? 185 PRO A CB  1 
ATOM   1550 C  CG  . PRO A 1 185 ? -21.298 -6.829  18.765  1.00 10.63  ? 185 PRO A CG  1 
ATOM   1551 C  CD  . PRO A 1 185 ? -21.141 -5.986  17.505  1.00 11.30  ? 185 PRO A CD  1 
ATOM   1552 N  N   . GLU A 1 186 ? -25.201 -7.750  18.418  1.00 12.25  ? 186 GLU A N   1 
ATOM   1553 C  CA  . GLU A 1 186 ? -26.416 -7.306  19.086  1.00 12.28  ? 186 GLU A CA  1 
ATOM   1554 C  C   . GLU A 1 186 ? -26.130 -6.515  20.325  1.00 11.88  ? 186 GLU A C   1 
ATOM   1555 O  O   . GLU A 1 186 ? -26.733 -5.434  20.516  1.00 14.53  ? 186 GLU A O   1 
ATOM   1556 C  CB  . GLU A 1 186 ? -27.261 -8.505  19.526  1.00 15.06  ? 186 GLU A CB  1 
ATOM   1557 C  CG  . GLU A 1 186 ? -27.901 -9.248  18.423  1.00 16.84  ? 186 GLU A CG  1 
ATOM   1558 C  CD  . GLU A 1 186 ? -28.660 -10.475 18.916  1.00 18.33  ? 186 GLU A CD  1 
ATOM   1559 O  OE1 . GLU A 1 186 ? -28.702 -10.810 20.123  1.00 22.52  ? 186 GLU A OE1 1 
ATOM   1560 O  OE2 . GLU A 1 186 ? -29.209 -11.160 18.068  1.00 22.87  ? 186 GLU A OE2 1 
ATOM   1561 N  N   . SER A 1 187 ? -25.291 -7.040  21.202  1.00 12.46  ? 187 SER A N   1 
ATOM   1562 C  CA  . SER A 1 187 ? -25.026 -6.414  22.486  1.00 12.71  ? 187 SER A CA  1 
ATOM   1563 C  C   . SER A 1 187 ? -23.914 -5.363  22.467  1.00 11.30  ? 187 SER A C   1 
ATOM   1564 O  O   . SER A 1 187 ? -22.913 -5.583  21.764  1.00 13.21  ? 187 SER A O   1 
ATOM   1565 C  CB  . SER A 1 187 ? -24.647 -7.467  23.544  1.00 14.89  ? 187 SER A CB  1 
ATOM   1566 O  OG  . SER A 1 187 ? -24.421 -6.914  24.796  1.00 14.62  ? 187 SER A OG  1 
ATOM   1567 N  N   . LEU A 1 188 ? -24.078 -4.264  23.224  1.00 12.76  ? 188 LEU A N   1 
ATOM   1568 C  CA  . LEU A 1 188 ? -22.989 -3.311  23.397  1.00 13.11  ? 188 LEU A CA  1 
ATOM   1569 C  C   . LEU A 1 188 ? -22.367 -3.472  24.774  1.00 12.49  ? 188 LEU A C   1 
ATOM   1570 O  O   . LEU A 1 188 ? -21.704 -2.561  25.226  1.00 17.36  ? 188 LEU A O   1 
ATOM   1571 C  CB  . LEU A 1 188 ? -23.529 -1.848  23.232  1.00 14.23  ? 188 LEU A CB  1 
ATOM   1572 C  CG  . LEU A 1 188 ? -23.907 -1.423  21.787  1.00 14.51  ? 188 LEU A CG  1 
ATOM   1573 C  CD1 . LEU A 1 188 ? -24.450 0.017   21.699  1.00 16.08  ? 188 LEU A CD1 1 
ATOM   1574 C  CD2 . LEU A 1 188 ? -22.747 -1.637  20.780  1.00 16.43  ? 188 LEU A CD2 1 
ATOM   1575 N  N   . ASP A 1 189 ? -22.559 -4.637  25.427  1.00 13.13  ? 189 ASP A N   1 
ATOM   1576 C  CA  . ASP A 1 189 ? -21.797 -4.919  26.668  1.00 13.70  ? 189 ASP A CA  1 
ATOM   1577 C  C   . ASP A 1 189 ? -20.299 -4.888  26.341  1.00 12.23  ? 189 ASP A C   1 
ATOM   1578 O  O   . ASP A 1 189 ? -19.871 -5.426  25.320  1.00 11.55  ? 189 ASP A O   1 
ATOM   1579 C  CB  . ASP A 1 189 ? -22.179 -6.281  27.215  1.00 19.22  ? 189 ASP A CB  1 
ATOM   1580 C  CG  . ASP A 1 189 ? -23.565 -6.300  27.870  1.00 23.83  ? 189 ASP A CG  1 
ATOM   1581 O  OD1 . ASP A 1 189 ? -24.236 -5.271  27.979  1.00 31.95  ? 189 ASP A OD1 1 
ATOM   1582 O  OD2 . ASP A 1 189 ? -23.970 -7.384  28.265  1.00 31.55  ? 189 ASP A OD2 1 
ATOM   1583 N  N   . TYR A 1 190 ? -19.510 -4.337  27.275  1.00 11.86  ? 190 TYR A N   1 
ATOM   1584 C  CA  . TYR A 1 190 ? -18.085 -4.099  26.918  1.00 10.50  ? 190 TYR A CA  1 
ATOM   1585 C  C   . TYR A 1 190 ? -17.204 -4.131  28.162  1.00 9.27   ? 190 TYR A C   1 
ATOM   1586 O  O   . TYR A 1 190 ? -17.624 -4.014  29.301  1.00 11.57  ? 190 TYR A O   1 
ATOM   1587 C  CB  . TYR A 1 190 ? -17.887 -2.725  26.241  1.00 12.51  ? 190 TYR A CB  1 
ATOM   1588 C  CG  . TYR A 1 190 ? -18.326 -1.532  27.133  1.00 10.94  ? 190 TYR A CG  1 
ATOM   1589 C  CD1 . TYR A 1 190 ? -17.435 -0.946  28.030  1.00 11.99  ? 190 TYR A CD1 1 
ATOM   1590 C  CD2 . TYR A 1 190 ? -19.612 -0.988  27.095  1.00 11.67  ? 190 TYR A CD2 1 
ATOM   1591 C  CE1 . TYR A 1 190 ? -17.819 0.116   28.840  1.00 12.26  ? 190 TYR A CE1 1 
ATOM   1592 C  CE2 . TYR A 1 190 ? -20.000 0.073   27.910  1.00 12.90  ? 190 TYR A CE2 1 
ATOM   1593 C  CZ  . TYR A 1 190 ? -19.096 0.637   28.759  1.00 13.62  ? 190 TYR A CZ  1 
ATOM   1594 O  OH  . TYR A 1 190 ? -19.378 1.661   29.627  1.00 14.55  ? 190 TYR A OH  1 
ATOM   1595 N  N   . TRP A 1 191 ? -15.925 -4.333  27.835  1.00 9.35   ? 191 TRP A N   1 
ATOM   1596 C  CA  . TRP A 1 191 ? -14.828 -4.079  28.796  1.00 8.55   ? 191 TRP A CA  1 
ATOM   1597 C  C   . TRP A 1 191 ? -14.136 -2.784  28.369  1.00 9.31   ? 191 TRP A C   1 
ATOM   1598 O  O   . TRP A 1 191 ? -14.073 -2.445  27.200  1.00 10.39  ? 191 TRP A O   1 
ATOM   1599 C  CB  . TRP A 1 191 ? -13.779 -5.197  28.725  1.00 10.73  ? 191 TRP A CB  1 
ATOM   1600 C  CG  . TRP A 1 191 ? -14.332 -6.543  29.160  1.00 10.92  ? 191 TRP A CG  1 
ATOM   1601 C  CD1 . TRP A 1 191 ? -14.581 -6.977  30.472  1.00 10.87  ? 191 TRP A CD1 1 
ATOM   1602 C  CD2 . TRP A 1 191 ? -14.635 -7.666  28.284  1.00 10.50  ? 191 TRP A CD2 1 
ATOM   1603 N  NE1 . TRP A 1 191 ? -15.035 -8.256  30.435  1.00 12.40  ? 191 TRP A NE1 1 
ATOM   1604 C  CE2 . TRP A 1 191 ? -15.086 -8.726  29.146  1.00 11.68  ? 191 TRP A CE2 1 
ATOM   1605 C  CE3 . TRP A 1 191 ? -14.552 -7.865  26.907  1.00 10.51  ? 191 TRP A CE3 1 
ATOM   1606 C  CZ2 . TRP A 1 191 ? -15.417 -9.974  28.635  1.00 12.53  ? 191 TRP A CZ2 1 
ATOM   1607 C  CZ3 . TRP A 1 191 ? -14.821 -9.164  26.408  1.00 12.11  ? 191 TRP A CZ3 1 
ATOM   1608 C  CH2 . TRP A 1 191 ? -15.292 -10.147 27.265  1.00 12.81  ? 191 TRP A CH2 1 
ATOM   1609 N  N   . THR A 1 192 ? -13.571 -2.071  29.339  1.00 9.71   ? 192 THR A N   1 
ATOM   1610 C  CA  . THR A 1 192 ? -12.838 -0.864  28.996  1.00 9.43   ? 192 THR A CA  1 
ATOM   1611 C  C   . THR A 1 192 ? -11.570 -0.701  29.880  1.00 8.76   ? 192 THR A C   1 
ATOM   1612 O  O   . THR A 1 192 ? -11.554 -1.084  31.052  1.00 10.08  ? 192 THR A O   1 
ATOM   1613 C  CB  . THR A 1 192 ? -13.738 0.371   29.118  1.00 9.27   ? 192 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 192 ? -13.063 1.539   28.660  1.00 10.14  ? 192 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 192 ? -14.286 0.592   30.517  1.00 11.21  ? 192 THR A CG2 1 
ATOM   1616 N  N   . TYR A 1 193 ? -10.537 -0.114  29.250  1.00 9.24   ? 193 TYR A N   1 
ATOM   1617 C  CA  . TYR A 1 193 ? -9.289  0.147   30.023  1.00 9.52   ? 193 TYR A CA  1 
ATOM   1618 C  C   . TYR A 1 193 ? -8.503  1.205   29.246  1.00 8.87   ? 193 TYR A C   1 
ATOM   1619 O  O   . TYR A 1 193 ? -8.733  1.395   28.045  1.00 9.26   ? 193 TYR A O   1 
ATOM   1620 C  CB  . TYR A 1 193 ? -8.479  -1.169  30.172  1.00 10.29  ? 193 TYR A CB  1 
ATOM   1621 C  CG  . TYR A 1 193 ? -7.811  -1.632  28.969  1.00 9.75   ? 193 TYR A CG  1 
ATOM   1622 C  CD1 . TYR A 1 193 ? -8.489  -2.355  27.957  1.00 9.06   ? 193 TYR A CD1 1 
ATOM   1623 C  CD2 . TYR A 1 193 ? -6.457  -1.307  28.729  1.00 9.84   ? 193 TYR A CD2 1 
ATOM   1624 C  CE1 . TYR A 1 193 ? -7.849  -2.685  26.761  1.00 8.57   ? 193 TYR A CE1 1 
ATOM   1625 C  CE2 . TYR A 1 193 ? -5.838  -1.617  27.560  1.00 9.01   ? 193 TYR A CE2 1 
ATOM   1626 C  CZ  . TYR A 1 193 ? -6.531  -2.329  26.566  1.00 7.84   ? 193 TYR A CZ  1 
ATOM   1627 O  OH  . TYR A 1 193 ? -5.877  -2.608  25.406  1.00 8.25   ? 193 TYR A OH  1 
ATOM   1628 N  N   . PRO A 1 194 ? -7.581  1.875   29.942  1.00 9.83   ? 194 PRO A N   1 
ATOM   1629 C  CA  . PRO A 1 194 ? -6.724  2.897   29.263  1.00 9.66   ? 194 PRO A CA  1 
ATOM   1630 C  C   . PRO A 1 194 ? -5.542  2.218   28.592  1.00 8.43   ? 194 PRO A C   1 
ATOM   1631 O  O   . PRO A 1 194 ? -4.827  1.415   29.260  1.00 9.99   ? 194 PRO A O   1 
ATOM   1632 C  CB  . PRO A 1 194 ? -6.249  3.770   30.417  1.00 12.31  ? 194 PRO A CB  1 
ATOM   1633 C  CG  . PRO A 1 194 ? -6.233  2.862   31.655  1.00 14.57  ? 194 PRO A CG  1 
ATOM   1634 C  CD  . PRO A 1 194 ? -7.374  1.840   31.393  1.00 12.98  ? 194 PRO A CD  1 
ATOM   1635 N  N   . GLY A 1 195 ? -5.289  2.543   27.351  1.00 8.12   ? 195 GLY A N   1 
ATOM   1636 C  CA  . GLY A 1 195 ? -4.196  1.922   26.647  1.00 9.22   ? 195 GLY A CA  1 
ATOM   1637 C  C   . GLY A 1 195 ? -3.631  2.777   25.529  1.00 8.42   ? 195 GLY A C   1 
ATOM   1638 O  O   . GLY A 1 195 ? -3.542  4.051   25.634  1.00 8.66   ? 195 GLY A O   1 
ATOM   1639 N  N   . SER A 1 196 ? -3.220  2.136   24.436  1.00 7.64   ? 196 SER A N   1 
ATOM   1640 C  CA  . SER A 1 196 ? -2.410  2.768   23.388  1.00 8.50   ? 196 SER A CA  1 
ATOM   1641 C  C   . SER A 1 196 ? -2.831  2.395   22.006  1.00 7.27   ? 196 SER A C   1 
ATOM   1642 O  O   . SER A 1 196 ? -3.624  1.412   21.821  1.00 8.22   ? 196 SER A O   1 
ATOM   1643 C  CB  . SER A 1 196 ? -0.929  2.388   23.538  1.00 8.26   ? 196 SER A CB  1 
ATOM   1644 O  OG  . SER A 1 196 ? -0.687  1.038   23.146  1.00 8.83   ? 196 SER A OG  1 
ATOM   1645 N  N   . LEU A 1 197 ? -2.308  3.049   21.003  1.00 7.61   ? 197 LEU A N   1 
ATOM   1646 C  CA  . LEU A 1 197 ? -2.314  2.522   19.655  1.00 7.79   ? 197 LEU A CA  1 
ATOM   1647 C  C   . LEU A 1 197 ? -1.604  1.164   19.684  1.00 8.76   ? 197 LEU A C   1 
ATOM   1648 O  O   . LEU A 1 197 ? -0.612  0.974   20.418  1.00 9.21   ? 197 LEU A O   1 
ATOM   1649 C  CB  . LEU A 1 197 ? -1.574  3.424   18.676  1.00 9.98   ? 197 LEU A CB  1 
ATOM   1650 C  CG  . LEU A 1 197 ? -2.096  4.869   18.624  1.00 10.21  ? 197 LEU A CG  1 
ATOM   1651 C  CD1 . LEU A 1 197 ? -1.225  5.598   17.637  1.00 12.65  ? 197 LEU A CD1 1 
ATOM   1652 C  CD2 . LEU A 1 197 ? -3.558  4.796   18.139  1.00 12.13  ? 197 LEU A CD2 1 
ATOM   1653 N  N   . THR A 1 198 ? -2.017  0.232   18.829  1.00 8.28   ? 198 THR A N   1 
ATOM   1654 C  CA  . THR A 1 198 ? -1.340  -1.087  18.752  1.00 8.33   ? 198 THR A CA  1 
ATOM   1655 C  C   . THR A 1 198 ? -0.362  -1.193  17.585  1.00 8.31   ? 198 THR A C   1 
ATOM   1656 O  O   . THR A 1 198 ? 0.259   -2.218  17.383  1.00 8.99   ? 198 THR A O   1 
ATOM   1657 C  CB  . THR A 1 198 ? -2.352  -2.218  18.620  1.00 7.97   ? 198 THR A CB  1 
ATOM   1658 O  OG1 . THR A 1 198 ? -2.945  -2.183  17.360  1.00 7.49   ? 198 THR A OG1 1 
ATOM   1659 C  CG2 . THR A 1 198 ? -3.355  -2.199  19.790  1.00 9.72   ? 198 THR A CG2 1 
ATOM   1660 N  N   . THR A 1 199 ? -0.182  -0.060  16.871  1.00 9.50   ? 199 THR A N   1 
ATOM   1661 C  CA  . THR A 1 199 ? 0.825   0.067   15.821  1.00 10.01  ? 199 THR A CA  1 
ATOM   1662 C  C   . THR A 1 199 ? 1.688   1.295   16.161  1.00 10.94  ? 199 THR A C   1 
ATOM   1663 O  O   . THR A 1 199 ? 1.177   2.232   16.807  1.00 10.69  ? 199 THR A O   1 
ATOM   1664 C  CB  . THR A 1 199 ? 0.195   0.279   14.423  1.00 11.29  ? 199 THR A CB  1 
ATOM   1665 O  OG1 . THR A 1 199 ? -0.756  1.355   14.520  1.00 14.57  ? 199 THR A OG1 1 
ATOM   1666 C  CG2 . THR A 1 199 ? -0.520  -0.947  13.961  1.00 10.69  ? 199 THR A CG2 1 
ATOM   1667 N  N   . PRO A 1 200 ? 2.952   1.326   15.680  1.00 10.67  ? 200 PRO A N   1 
ATOM   1668 C  CA  . PRO A 1 200 ? 3.720   2.566   15.739  1.00 12.44  ? 200 PRO A CA  1 
ATOM   1669 C  C   . PRO A 1 200 ? 2.805   3.735   15.264  1.00 12.26  ? 200 PRO A C   1 
ATOM   1670 O  O   . PRO A 1 200 ? 2.068   3.556   14.238  1.00 13.39  ? 200 PRO A O   1 
ATOM   1671 C  CB  . PRO A 1 200 ? 4.878   2.270   14.752  1.00 14.69  ? 200 PRO A CB  1 
ATOM   1672 C  CG  . PRO A 1 200 ? 5.110   0.805   14.984  1.00 12.33  ? 200 PRO A CG  1 
ATOM   1673 C  CD  . PRO A 1 200 ? 3.695   0.207   15.030  1.00 11.88  ? 200 PRO A CD  1 
ATOM   1674 N  N   . PRO A 1 201 ? 2.808   4.866   15.945  1.00 11.43  ? 201 PRO A N   1 
ATOM   1675 C  CA  . PRO A 1 201 ? 3.801   5.249   16.973  1.00 11.70  ? 201 PRO A CA  1 
ATOM   1676 C  C   . PRO A 1 201 ? 3.516   4.809   18.408  1.00 10.06  ? 201 PRO A C   1 
ATOM   1677 O  O   . PRO A 1 201 ? 4.266   5.178   19.310  1.00 11.50  ? 201 PRO A O   1 
ATOM   1678 C  CB  . PRO A 1 201 ? 3.835   6.766   16.892  1.00 13.59  ? 201 PRO A CB  1 
ATOM   1679 C  CG  . PRO A 1 201 ? 2.366   7.103   16.481  1.00 15.06  ? 201 PRO A CG  1 
ATOM   1680 C  CD  . PRO A 1 201 ? 2.023   6.018   15.479  1.00 14.59  ? 201 PRO A CD  1 
ATOM   1681 N  N   . LEU A 1 202 ? 2.474   3.971   18.618  1.00 9.94   ? 202 LEU A N   1 
ATOM   1682 C  CA  . LEU A 1 202 ? 2.192   3.355   19.925  1.00 9.30   ? 202 LEU A CA  1 
ATOM   1683 C  C   . LEU A 1 202 ? 1.792   4.312   21.015  1.00 9.21   ? 202 LEU A C   1 
ATOM   1684 O  O   . LEU A 1 202 ? 1.845   4.044   22.214  1.00 9.78   ? 202 LEU A O   1 
ATOM   1685 C  CB  . LEU A 1 202 ? 3.321   2.443   20.408  1.00 10.52  ? 202 LEU A CB  1 
ATOM   1686 C  CG  . LEU A 1 202 ? 3.655   1.339   19.378  1.00 9.64   ? 202 LEU A CG  1 
ATOM   1687 C  CD1 . LEU A 1 202 ? 4.970   0.674   19.815  1.00 11.65  ? 202 LEU A CD1 1 
ATOM   1688 C  CD2 . LEU A 1 202 ? 2.594   0.266   19.320  1.00 9.81   ? 202 LEU A CD2 1 
ATOM   1689 N  N   . ASN A 1 203 ? 1.338   5.539   20.594  1.00 10.80  ? 203 ASN A N   1 
ATOM   1690 C  CA  . ASN A 1 203 ? 0.967   6.592   21.587  1.00 10.62  ? 203 ASN A CA  1 
ATOM   1691 C  C   . ASN A 1 203 ? -0.011  6.098   22.602  1.00 9.57   ? 203 ASN A C   1 
ATOM   1692 O  O   . ASN A 1 203 ? -1.005  5.380   22.250  1.00 9.71   ? 203 ASN A O   1 
ATOM   1693 C  CB  . ASN A 1 203 ? 0.342   7.815   20.881  1.00 12.54  ? 203 ASN A CB  1 
ATOM   1694 C  CG  . ASN A 1 203 ? 1.286   8.493   19.912  1.00 14.97  ? 203 ASN A CG  1 
ATOM   1695 O  OD1 . ASN A 1 203 ? 2.396   8.056   19.645  1.00 18.81  ? 203 ASN A OD1 1 
ATOM   1696 N  ND2 . ASN A 1 203 ? 0.851   9.616   19.397  1.00 17.25  ? 203 ASN A ND2 1 
ATOM   1697 N  N   . GLU A 1 204 ? 0.132   6.499   23.841  1.00 10.59  ? 204 GLU A N   1 
ATOM   1698 C  CA  . GLU A 1 204 ? -0.747  6.132   24.936  1.00 10.82  ? 204 GLU A CA  1 
ATOM   1699 C  C   . GLU A 1 204 ? -1.933  7.062   25.036  1.00 9.67   ? 204 GLU A C   1 
ATOM   1700 O  O   . GLU A 1 204 ? -2.092  7.821   26.006  1.00 14.74  ? 204 GLU A O   1 
ATOM   1701 C  CB  . GLU A 1 204 ? 0.074   6.011   26.260  1.00 11.64  ? 204 GLU A CB  1 
ATOM   1702 C  CG  . GLU A 1 204 ? 1.058   4.808   26.095  1.00 11.97  ? 204 GLU A CG  1 
ATOM   1703 C  CD  . GLU A 1 204 ? 1.914   4.504   27.341  1.00 11.23  ? 204 GLU A CD  1 
ATOM   1704 O  OE1 . GLU A 1 204 ? 2.141   5.458   28.120  1.00 15.10  ? 204 GLU A OE1 1 
ATOM   1705 O  OE2 . GLU A 1 204 ? 2.326   3.310   27.448  1.00 11.13  ? 204 GLU A OE2 1 
ATOM   1706 N  N   . CYS A 1 205 ? -2.793  7.029   24.019  1.00 8.80   ? 205 CYS A N   1 
ATOM   1707 C  CA  . CYS A 1 205 ? -3.827  8.012   23.866  1.00 9.36   ? 205 CYS A CA  1 
ATOM   1708 C  C   . CYS A 1 205 ? -5.195  7.415   23.735  1.00 8.85   ? 205 CYS A C   1 
ATOM   1709 O  O   . CYS A 1 205 ? -6.127  8.133   23.324  1.00 11.01  ? 205 CYS A O   1 
ATOM   1710 C  CB  . CYS A 1 205 ? -3.539  8.849   22.592  1.00 10.75  ? 205 CYS A CB  1 
ATOM   1711 S  SG  . CYS A 1 205 ? -3.465  7.844   21.039  1.00 10.89  ? 205 CYS A SG  1 
ATOM   1712 N  N   . VAL A 1 206 ? -5.348  6.100   24.010  1.00 8.89   ? 206 VAL A N   1 
ATOM   1713 C  CA  . VAL A 1 206 ? -6.631  5.401   23.666  1.00 8.88   ? 206 VAL A CA  1 
ATOM   1714 C  C   . VAL A 1 206 ? -7.393  4.981   24.914  1.00 8.66   ? 206 VAL A C   1 
ATOM   1715 O  O   . VAL A 1 206 ? -6.849  4.341   25.800  1.00 10.24  ? 206 VAL A O   1 
ATOM   1716 C  CB  . VAL A 1 206 ? -6.332  4.164   22.818  1.00 8.62   ? 206 VAL A CB  1 
ATOM   1717 C  CG1 . VAL A 1 206 ? -7.655  3.426   22.491  1.00 9.36   ? 206 VAL A CG1 1 
ATOM   1718 C  CG2 . VAL A 1 206 ? -5.569  4.532   21.551  1.00 9.61   ? 206 VAL A CG2 1 
ATOM   1719 N  N   . THR A 1 207 ? -8.666  5.324   24.944  1.00 8.17   ? 207 THR A N   1 
ATOM   1720 C  CA  . THR A 1 207 ? -9.593  4.595   25.779  1.00 9.13   ? 207 THR A CA  1 
ATOM   1721 C  C   . THR A 1 207 ? -10.125 3.430   24.972  1.00 7.74   ? 207 THR A C   1 
ATOM   1722 O  O   . THR A 1 207 ? -10.800 3.617   23.932  1.00 8.45   ? 207 THR A O   1 
ATOM   1723 C  CB  . THR A 1 207 ? -10.797 5.489   26.239  1.00 10.46  ? 207 THR A CB  1 
ATOM   1724 O  OG1 . THR A 1 207 ? -10.258 6.601   26.985  1.00 11.67  ? 207 THR A OG1 1 
ATOM   1725 C  CG2 . THR A 1 207 ? -11.713 4.670   27.127  1.00 11.05  ? 207 THR A CG2 1 
ATOM   1726 N  N   . TRP A 1 208 ? -9.789  2.198   25.388  1.00 8.02   ? 208 TRP A N   1 
ATOM   1727 C  CA  . TRP A 1 208 ? -10.265 0.988   24.674  1.00 7.86   ? 208 TRP A CA  1 
ATOM   1728 C  C   . TRP A 1 208 ? -11.636 0.591   25.189  1.00 7.16   ? 208 TRP A C   1 
ATOM   1729 O  O   . TRP A 1 208 ? -11.863 0.558   26.381  1.00 8.77   ? 208 TRP A O   1 
ATOM   1730 C  CB  . TRP A 1 208 ? -9.249  -0.163  24.862  1.00 8.53   ? 208 TRP A CB  1 
ATOM   1731 C  CG  . TRP A 1 208 ? -8.120  -0.062  23.910  1.00 7.76   ? 208 TRP A CG  1 
ATOM   1732 C  CD1 . TRP A 1 208 ? -6.875  0.562   24.087  1.00 8.39   ? 208 TRP A CD1 1 
ATOM   1733 C  CD2 . TRP A 1 208 ? -8.148  -0.428  22.535  1.00 7.83   ? 208 TRP A CD2 1 
ATOM   1734 N  NE1 . TRP A 1 208 ? -6.177  0.510   22.930  1.00 8.28   ? 208 TRP A NE1 1 
ATOM   1735 C  CE2 . TRP A 1 208 ? -6.926  -0.070  21.935  1.00 7.93   ? 208 TRP A CE2 1 
ATOM   1736 C  CE3 . TRP A 1 208 ? -9.103  -1.057  21.738  1.00 7.95   ? 208 TRP A CE3 1 
ATOM   1737 C  CZ2 . TRP A 1 208 ? -6.635  -0.308  20.630  1.00 8.74   ? 208 TRP A CZ2 1 
ATOM   1738 C  CZ3 . TRP A 1 208 ? -8.818  -1.317  20.428  1.00 8.66   ? 208 TRP A CZ3 1 
ATOM   1739 C  CH2 . TRP A 1 208 ? -7.601  -0.986  19.857  1.00 9.38   ? 208 TRP A CH2 1 
ATOM   1740 N  N   . ILE A 1 209 ? -12.500 0.281   24.199  1.00 7.84   ? 209 ILE A N   1 
ATOM   1741 C  CA  . ILE A 1 209 ? -13.837 -0.249  24.545  1.00 8.10   ? 209 ILE A CA  1 
ATOM   1742 C  C   . ILE A 1 209 ? -13.980 -1.503  23.682  1.00 7.17   ? 209 ILE A C   1 
ATOM   1743 O  O   . ILE A 1 209 ? -14.072 -1.421  22.488  1.00 8.22   ? 209 ILE A O   1 
ATOM   1744 C  CB  . ILE A 1 209 ? -14.921 0.774   24.176  1.00 8.73   ? 209 ILE A CB  1 
ATOM   1745 C  CG1 . ILE A 1 209 ? -14.684 2.112   24.948  1.00 11.59  ? 209 ILE A CG1 1 
ATOM   1746 C  CG2 . ILE A 1 209 ? -16.302 0.216   24.511  1.00 9.85   ? 209 ILE A CG2 1 
ATOM   1747 C  CD1 . ILE A 1 209 ? -15.520 3.279   24.529  1.00 13.28  ? 209 ILE A CD1 1 
ATOM   1748 N  N   . VAL A 1 210 ? -13.936 -2.662  24.353  1.00 8.23   ? 210 VAL A N   1 
ATOM   1749 C  CA  . VAL A 1 210 ? -13.915 -3.939  23.639  1.00 8.12   ? 210 VAL A CA  1 
ATOM   1750 C  C   . VAL A 1 210 ? -15.224 -4.689  23.898  1.00 6.87   ? 210 VAL A C   1 
ATOM   1751 O  O   . VAL A 1 210 ? -15.571 -4.926  25.051  1.00 8.70   ? 210 VAL A O   1 
ATOM   1752 C  CB  . VAL A 1 210 ? -12.684 -4.806  24.090  1.00 8.77   ? 210 VAL A CB  1 
ATOM   1753 C  CG1 . VAL A 1 210 ? -12.719 -6.192  23.365  1.00 10.35  ? 210 VAL A CG1 1 
ATOM   1754 C  CG2 . VAL A 1 210 ? -11.382 -4.082  23.771  1.00 9.76   ? 210 VAL A CG2 1 
ATOM   1755 N  N   . LEU A 1 211 ? -15.987 -4.931  22.836  1.00 8.46   ? 211 LEU A N   1 
ATOM   1756 C  CA  . LEU A 1 211 ? -17.306 -5.574  23.027  1.00 8.20   ? 211 LEU A CA  1 
ATOM   1757 C  C   . LEU A 1 211 ? -17.149 -7.031  23.443  1.00 9.66   ? 211 LEU A C   1 
ATOM   1758 O  O   . LEU A 1 211 ? -16.289 -7.748  22.892  1.00 9.99   ? 211 LEU A O   1 
ATOM   1759 C  CB  . LEU A 1 211 ? -18.125 -5.468  21.744  1.00 9.65   ? 211 LEU A CB  1 
ATOM   1760 C  CG  . LEU A 1 211 ? -18.476 -4.034  21.342  1.00 9.05   ? 211 LEU A CG  1 
ATOM   1761 C  CD1 . LEU A 1 211 ? -19.522 -4.016  20.231  1.00 11.38  ? 211 LEU A CD1 1 
ATOM   1762 C  CD2 . LEU A 1 211 ? -19.007 -3.185  22.471  1.00 10.77  ? 211 LEU A CD2 1 
ATOM   1763 N  N   . LYS A 1 212 ? -18.019 -7.481  24.341  1.00 10.25  ? 212 LYS A N   1 
ATOM   1764 C  CA  . LYS A 1 212 ? -17.987 -8.887  24.768  1.00 13.30  ? 212 LYS A CA  1 
ATOM   1765 C  C   . LYS A 1 212 ? -18.450 -9.816  23.693  1.00 11.05  ? 212 LYS A C   1 
ATOM   1766 O  O   . LYS A 1 212 ? -17.956 -10.948 23.574  1.00 12.98  ? 212 LYS A O   1 
ATOM   1767 C  CB  . LYS A 1 212 ? -18.887 -9.026  26.007  1.00 16.56  ? 212 LYS A CB  1 
ATOM   1768 C  CG  . LYS A 1 212 ? -19.320 -10.422 26.438  1.00 30.32  ? 212 LYS A CG  1 
ATOM   1769 C  CD  . LYS A 1 212 ? -20.471 -10.240 27.460  1.00 40.39  ? 212 LYS A CD  1 
ATOM   1770 C  CE  . LYS A 1 212 ? -21.921 -10.368 26.917  1.00 44.17  ? 212 LYS A CE  1 
ATOM   1771 N  NZ  . LYS A 1 212 ? -22.460 -9.575  25.754  1.00 43.30  ? 212 LYS A NZ  1 
ATOM   1772 N  N   . GLU A 1 213 ? -19.413 -9.447  22.886  1.00 10.04  ? 213 GLU A N   1 
ATOM   1773 C  CA  . GLU A 1 213 ? -20.027 -10.365 21.905  1.00 10.86  ? 213 GLU A CA  1 
ATOM   1774 C  C   . GLU A 1 213 ? -19.256 -10.287 20.585  1.00 9.57   ? 213 GLU A C   1 
ATOM   1775 O  O   . GLU A 1 213 ? -19.184 -9.207  19.991  1.00 9.76   ? 213 GLU A O   1 
ATOM   1776 C  CB  . GLU A 1 213 ? -21.470 -10.011 21.663  1.00 11.57  ? 213 GLU A CB  1 
ATOM   1777 C  CG  . GLU A 1 213 ? -22.233 -10.946 20.756  1.00 14.30  ? 213 GLU A CG  1 
ATOM   1778 C  CD  . GLU A 1 213 ? -23.682 -10.449 20.502  1.00 17.94  ? 213 GLU A CD  1 
ATOM   1779 O  OE1 . GLU A 1 213 ? -24.289 -9.799  21.352  1.00 18.21  ? 213 GLU A OE1 1 
ATOM   1780 O  OE2 . GLU A 1 213 ? -24.223 -10.725 19.404  1.00 30.67  ? 213 GLU A OE2 1 
ATOM   1781 N  N   A PRO A 1 214 ? -18.735 -11.427 20.093  0.50 9.84   ? 214 PRO A N   1 
ATOM   1782 N  N   B PRO A 1 214 ? -18.626 -11.365 20.137  0.50 10.82  ? 214 PRO A N   1 
ATOM   1783 C  CA  A PRO A 1 214 ? -18.132 -11.424 18.768  0.50 8.91   ? 214 PRO A CA  1 
ATOM   1784 C  CA  B PRO A 1 214 ? -18.012 -11.316 18.801  0.50 11.08  ? 214 PRO A CA  1 
ATOM   1785 C  C   A PRO A 1 214 ? -19.142 -11.293 17.654  0.50 8.34   ? 214 PRO A C   1 
ATOM   1786 C  C   B PRO A 1 214 ? -19.056 -11.300 17.691  0.50 9.91   ? 214 PRO A C   1 
ATOM   1787 O  O   A PRO A 1 214 ? -20.329 -11.674 17.857  0.50 10.67  ? 214 PRO A O   1 
ATOM   1788 O  O   B PRO A 1 214 ? -20.198 -11.744 17.951  0.50 14.83  ? 214 PRO A O   1 
ATOM   1789 C  CB  A PRO A 1 214 ? -17.422 -12.815 18.678  0.50 11.51  ? 214 PRO A CB  1 
ATOM   1790 C  CB  B PRO A 1 214 ? -17.191 -12.644 18.740  0.50 9.92   ? 214 PRO A CB  1 
ATOM   1791 C  CG  A PRO A 1 214 ? -18.248 -13.686 19.571  0.50 13.48  ? 214 PRO A CG  1 
ATOM   1792 C  CG  B PRO A 1 214 ? -17.120 -13.081 20.178  0.50 12.45  ? 214 PRO A CG  1 
ATOM   1793 C  CD  A PRO A 1 214 ? -18.732 -12.796 20.703  0.50 11.74  ? 214 PRO A CD  1 
ATOM   1794 C  CD  B PRO A 1 214 ? -18.372 -12.654 20.837  0.50 11.86  ? 214 PRO A CD  1 
ATOM   1795 N  N   . ILE A 1 215 ? -18.677 -10.885 16.489  1.00 9.90   ? 215 ILE A N   1 
ATOM   1796 C  CA  . ILE A 1 215 ? -19.508 -11.155 15.271  1.00 10.17  ? 215 ILE A CA  1 
ATOM   1797 C  C   . ILE A 1 215 ? -18.953 -12.424 14.660  1.00 10.29  ? 215 ILE A C   1 
ATOM   1798 O  O   . ILE A 1 215 ? -17.792 -12.746 14.777  1.00 11.08  ? 215 ILE A O   1 
ATOM   1799 C  CB  . ILE A 1 215 ? -19.518 -9.926  14.326  1.00 11.08  ? 215 ILE A CB  1 
ATOM   1800 C  CG1 . ILE A 1 215 ? -18.109 -9.598  13.825  1.00 10.62  ? 215 ILE A CG1 1 
ATOM   1801 C  CG2 . ILE A 1 215 ? -20.177 -8.708  15.000  1.00 12.20  ? 215 ILE A CG2 1 
ATOM   1802 C  CD1 . ILE A 1 215 ? -18.128 -8.632  12.643  1.00 11.69  ? 215 ILE A CD1 1 
ATOM   1803 N  N   . SER A 1 216 ? -19.835 -13.079 13.904  0.50 7.01   ? 216 SER A N   1 
ATOM   1804 C  CA  A SER A 1 216 ? -19.402 -14.223 13.062  0.50 11.20  ? 216 SER A CA  1 
ATOM   1805 C  CA  B SER A 1 216 ? -19.452 -14.228 13.084  0.50 11.34  ? 216 SER A CA  1 
ATOM   1806 C  C   . SER A 1 216 ? -19.226 -13.741 11.679  0.50 6.68   ? 216 SER A C   1 
ATOM   1807 O  O   . SER A 1 216 ? -20.075 -12.975 11.163  0.50 6.59   ? 216 SER A O   1 
ATOM   1808 C  CB  A SER A 1 216 ? -20.420 -15.365 13.043  0.50 13.35  ? 216 SER A CB  1 
ATOM   1809 C  CB  B SER A 1 216 ? -20.585 -15.251 13.118  0.50 14.51  ? 216 SER A CB  1 
ATOM   1810 O  OG  A SER A 1 216 ? -20.602 -15.911 14.323  0.50 13.87  ? 216 SER A OG  1 
ATOM   1811 O  OG  B SER A 1 216 ? -20.190 -16.452 12.521  0.50 16.10  ? 216 SER A OG  1 
ATOM   1812 N  N   . VAL A 1 217 ? -18.160 -14.158 11.059  1.00 10.15  ? 217 VAL A N   1 
ATOM   1813 C  CA  . VAL A 1 217 ? -17.900 -13.996 9.688   1.00 9.54   ? 217 VAL A CA  1 
ATOM   1814 C  C   . VAL A 1 217 ? -17.665 -15.369 9.038   1.00 9.59   ? 217 VAL A C   1 
ATOM   1815 O  O   . VAL A 1 217 ? -17.227 -16.318 9.728   1.00 11.18  ? 217 VAL A O   1 
ATOM   1816 C  CB  . VAL A 1 217 ? -16.716 -13.056 9.447   1.00 11.56  ? 217 VAL A CB  1 
ATOM   1817 C  CG1 . VAL A 1 217 ? -16.977 -11.699 10.134  1.00 12.44  ? 217 VAL A CG1 1 
ATOM   1818 C  CG2 . VAL A 1 217 ? -15.379 -13.649 9.994   1.00 13.42  ? 217 VAL A CG2 1 
ATOM   1819 N  N   . SER A 1 218 ? -17.781 -15.507 7.733   1.00 9.95   ? 218 SER A N   1 
ATOM   1820 C  CA  . SER A 1 218 ? -17.575 -16.847 7.148   1.00 10.27  ? 218 SER A CA  1 
ATOM   1821 C  C   . SER A 1 218 ? -16.127 -17.050 6.804   1.00 10.64  ? 218 SER A C   1 
ATOM   1822 O  O   . SER A 1 218 ? -15.335 -16.098 6.648   1.00 11.11  ? 218 SER A O   1 
ATOM   1823 C  CB  . SER A 1 218 ? -18.440 -17.033 5.904   1.00 11.29  ? 218 SER A CB  1 
ATOM   1824 O  OG  . SER A 1 218 ? -18.051 -16.104 4.906   1.00 12.37  ? 218 SER A OG  1 
ATOM   1825 N  N   A SER A 1 219 ? -15.790 -18.335 6.631   0.50 11.49  ? 219 SER A N   1 
ATOM   1826 N  N   B SER A 1 219 ? -15.753 -18.316 6.655   0.50 12.40  ? 219 SER A N   1 
ATOM   1827 C  CA  A SER A 1 219 ? -14.458 -18.735 6.160   0.50 12.47  ? 219 SER A CA  1 
ATOM   1828 C  CA  B SER A 1 219 ? -14.401 -18.635 6.221   0.50 13.30  ? 219 SER A CA  1 
ATOM   1829 C  C   A SER A 1 219 ? -14.161 -18.003 4.851   0.50 11.55  ? 219 SER A C   1 
ATOM   1830 C  C   B SER A 1 219 ? -14.135 -17.989 4.837   0.50 12.20  ? 219 SER A C   1 
ATOM   1831 O  O   A SER A 1 219 ? -13.041 -17.519 4.693   0.50 13.44  ? 219 SER A O   1 
ATOM   1832 O  O   B SER A 1 219 ? -13.009 -17.529 4.619   0.50 15.25  ? 219 SER A O   1 
ATOM   1833 C  CB  A SER A 1 219 ? -14.380 -20.254 5.954   0.50 13.00  ? 219 SER A CB  1 
ATOM   1834 C  CB  B SER A 1 219 ? -14.202 -20.152 6.232   0.50 15.67  ? 219 SER A CB  1 
ATOM   1835 O  OG  A SER A 1 219 ? -15.375 -20.739 5.056   0.50 11.34  ? 219 SER A OG  1 
ATOM   1836 O  OG  B SER A 1 219 ? -12.945 -20.534 5.775   0.50 25.06  ? 219 SER A OG  1 
ATOM   1837 N  N   . GLU A 1 220 ? -15.117 -17.891 3.918   1.00 12.71  ? 220 GLU A N   1 
ATOM   1838 C  CA  . GLU A 1 220 ? -14.864 -17.205 2.654   1.00 13.85  ? 220 GLU A CA  1 
ATOM   1839 C  C   . GLU A 1 220 ? -14.525 -15.717 2.825   1.00 11.38  ? 220 GLU A C   1 
ATOM   1840 O  O   . GLU A 1 220 ? -13.707 -15.189 2.083   1.00 13.23  ? 220 GLU A O   1 
ATOM   1841 C  CB  . GLU A 1 220 ? -16.049 -17.311 1.669   1.00 14.96  ? 220 GLU A CB  1 
ATOM   1842 C  CG  . GLU A 1 220 ? -16.292 -18.768 1.207   1.00 19.85  ? 220 GLU A CG  1 
ATOM   1843 C  CD  . GLU A 1 220 ? -17.324 -19.514 2.048   1.00 22.79  ? 220 GLU A CD  1 
ATOM   1844 O  OE1 . GLU A 1 220 ? -17.666 -19.097 3.179   1.00 20.33  ? 220 GLU A OE1 1 
ATOM   1845 O  OE2 . GLU A 1 220 ? -17.803 -20.558 1.556   1.00 49.94  ? 220 GLU A OE2 1 
ATOM   1846 N  N   . GLN A 1 221 ? -15.211 -15.087 3.768   1.00 10.58  ? 221 GLN A N   1 
ATOM   1847 C  CA  . GLN A 1 221 ? -14.916 -13.679 4.016   1.00 10.14  ? 221 GLN A CA  1 
ATOM   1848 C  C   . GLN A 1 221 ? -13.496 -13.499 4.543   1.00 10.67  ? 221 GLN A C   1 
ATOM   1849 O  O   . GLN A 1 221 ? -12.727 -12.623 4.046   1.00 11.89  ? 221 GLN A O   1 
ATOM   1850 C  CB  . GLN A 1 221 ? -15.950 -13.134 5.014   1.00 10.36  ? 221 GLN A CB  1 
ATOM   1851 C  CG  . GLN A 1 221 ? -17.338 -12.980 4.331   1.00 10.31  ? 221 GLN A CG  1 
ATOM   1852 C  CD  . GLN A 1 221 ? -18.403 -12.460 5.230   1.00 9.39   ? 221 GLN A CD  1 
ATOM   1853 O  OE1 . GLN A 1 221 ? -18.513 -12.816 6.420   1.00 10.10  ? 221 GLN A OE1 1 
ATOM   1854 N  NE2 . GLN A 1 221 ? -19.237 -11.550 4.684   1.00 10.74  ? 221 GLN A NE2 1 
ATOM   1855 N  N   . VAL A 1 222 ? -13.083 -14.290 5.534   1.00 11.20  ? 222 VAL A N   1 
ATOM   1856 C  CA  . VAL A 1 222 ? -11.774 -14.101 6.072   1.00 14.03  ? 222 VAL A CA  1 
ATOM   1857 C  C   . VAL A 1 222 ? -10.670 -14.556 5.065   1.00 13.11  ? 222 VAL A C   1 
ATOM   1858 O  O   . VAL A 1 222 ? -9.586  -13.942 5.032   1.00 13.83  ? 222 VAL A O   1 
ATOM   1859 C  CB  . VAL A 1 222 ? -11.613 -14.808 7.434   1.00 17.25  ? 222 VAL A CB  1 
ATOM   1860 C  CG1 . VAL A 1 222 ? -12.592 -14.471 8.514   1.00 24.89  ? 222 VAL A CG1 1 
ATOM   1861 C  CG2 . VAL A 1 222 ? -11.588 -16.280 7.332   1.00 24.43  ? 222 VAL A CG2 1 
ATOM   1862 N  N   . LEU A 1 223 ? -10.977 -15.514 4.192   1.00 13.89  ? 223 LEU A N   1 
ATOM   1863 C  CA  . LEU A 1 223 ? -10.022 -15.895 3.149   1.00 15.17  ? 223 LEU A CA  1 
ATOM   1864 C  C   . LEU A 1 223 ? -9.687  -14.718 2.251   1.00 13.95  ? 223 LEU A C   1 
ATOM   1865 O  O   . LEU A 1 223 ? -8.536  -14.591 1.774   1.00 14.66  ? 223 LEU A O   1 
ATOM   1866 C  CB  . LEU A 1 223 ? -10.512 -17.151 2.378   1.00 19.97  ? 223 LEU A CB  1 
ATOM   1867 C  CG  . LEU A 1 223 ? -10.223 -18.503 3.125   1.00 24.06  ? 223 LEU A CG  1 
ATOM   1868 C  CD1 . LEU A 1 223 ? -11.061 -19.466 2.327   1.00 31.05  ? 223 LEU A CD1 1 
ATOM   1869 C  CD2 . LEU A 1 223 ? -8.771  -18.933 3.204   1.00 31.35  ? 223 LEU A CD2 1 
ATOM   1870 N  N   . LYS A 1 224 ? -10.678 -13.845 2.011   1.00 12.78  ? 224 LYS A N   1 
ATOM   1871 C  CA  . LYS A 1 224 ? -10.370 -12.668 1.157   1.00 14.19  ? 224 LYS A CA  1 
ATOM   1872 C  C   . LYS A 1 224 ? -9.452  -11.657 1.852   1.00 12.10  ? 224 LYS A C   1 
ATOM   1873 O  O   . LYS A 1 224 ? -8.633  -11.084 1.176   1.00 13.53  ? 224 LYS A O   1 
ATOM   1874 C  CB  . LYS A 1 224 ? -11.672 -11.987 0.657   1.00 16.96  ? 224 LYS A CB  1 
ATOM   1875 C  CG  . LYS A 1 224 ? -12.382 -12.842 -0.380  1.00 23.14  ? 224 LYS A CG  1 
ATOM   1876 C  CD  . LYS A 1 224 ? -13.771 -12.305 -0.657  1.00 38.75  ? 224 LYS A CD  1 
ATOM   1877 C  CE  . LYS A 1 224 ? -14.197 -12.623 -2.071  1.00 33.43  ? 224 LYS A CE  1 
ATOM   1878 N  NZ  . LYS A 1 224 ? -14.617 -14.039 -2.235  1.00 45.67  ? 224 LYS A NZ  1 
ATOM   1879 N  N   . PHE A 1 225 ? -9.569  -11.525 3.170   1.00 12.61  ? 225 PHE A N   1 
ATOM   1880 C  CA  . PHE A 1 225 ? -8.610  -10.696 3.895   1.00 12.00  ? 225 PHE A CA  1 
ATOM   1881 C  C   . PHE A 1 225 ? -7.164  -11.255 3.627   1.00 12.75  ? 225 PHE A C   1 
ATOM   1882 O  O   . PHE A 1 225 ? -6.209  -10.470 3.420   1.00 13.37  ? 225 PHE A O   1 
ATOM   1883 C  CB  . PHE A 1 225 ? -8.797  -10.761 5.394   1.00 11.98  ? 225 PHE A CB  1 
ATOM   1884 C  CG  . PHE A 1 225 ? -9.965  -9.977  5.971   1.00 12.00  ? 225 PHE A CG  1 
ATOM   1885 C  CD1 . PHE A 1 225 ? -10.997 -9.449  5.205   1.00 15.36  ? 225 PHE A CD1 1 
ATOM   1886 C  CD2 . PHE A 1 225 ? -10.021 -9.807  7.349   1.00 14.78  ? 225 PHE A CD2 1 
ATOM   1887 C  CE1 . PHE A 1 225 ? -12.043 -8.759  5.817   1.00 14.88  ? 225 PHE A CE1 1 
ATOM   1888 C  CE2 . PHE A 1 225 ? -11.056 -9.124  7.959   1.00 17.17  ? 225 PHE A CE2 1 
ATOM   1889 C  CZ  . PHE A 1 225 ? -12.069 -8.593  7.192   1.00 13.86  ? 225 PHE A CZ  1 
ATOM   1890 N  N   . ARG A 1 226 ? -7.015  -12.585 3.647   1.00 13.06  ? 226 ARG A N   1 
ATOM   1891 C  CA  . ARG A 1 226 ? -5.720  -13.224 3.566   1.00 13.68  ? 226 ARG A CA  1 
ATOM   1892 C  C   . ARG A 1 226 ? -5.119  -13.165 2.161   1.00 13.47  ? 226 ARG A C   1 
ATOM   1893 O  O   . ARG A 1 226 ? -3.976  -13.675 2.009   1.00 15.97  ? 226 ARG A O   1 
ATOM   1894 C  CB  . ARG A 1 226 ? -5.818  -14.690 4.082   1.00 14.13  ? 226 ARG A CB  1 
ATOM   1895 C  CG  . ARG A 1 226 ? -6.234  -14.778 5.487   1.00 12.77  ? 226 ARG A CG  1 
ATOM   1896 C  CD  . ARG A 1 226 ? -6.108  -16.231 5.951   1.00 15.79  ? 226 ARG A CD  1 
ATOM   1897 N  NE  . ARG A 1 226 ? -6.612  -16.383 7.316   1.00 13.64  ? 226 ARG A NE  1 
ATOM   1898 C  CZ  . ARG A 1 226 ? -7.518  -17.273 7.738   1.00 15.03  ? 226 ARG A CZ  1 
ATOM   1899 N  NH1 . ARG A 1 226 ? -8.004  -18.233 6.935   1.00 23.36  ? 226 ARG A NH1 1 
ATOM   1900 N  NH2 . ARG A 1 226 ? -7.894  -17.262 9.036   1.00 17.96  ? 226 ARG A NH2 1 
ATOM   1901 N  N   . LYS A 1 227 ? -5.848  -12.754 1.152   1.00 13.73  ? 227 LYS A N   1 
ATOM   1902 C  CA  . LYS A 1 227 ? -5.349  -12.555 -0.199  1.00 15.20  ? 227 LYS A CA  1 
ATOM   1903 C  C   . LYS A 1 227 ? -4.666  -11.225 -0.406  1.00 15.19  ? 227 LYS A C   1 
ATOM   1904 O  O   . LYS A 1 227 ? -3.950  -11.014 -1.392  1.00 18.29  ? 227 LYS A O   1 
ATOM   1905 C  CB  . LYS A 1 227 ? -6.456  -12.757 -1.280  1.00 17.49  ? 227 LYS A CB  1 
ATOM   1906 C  CG  . LYS A 1 227 ? -6.964  -14.185 -1.344  1.00 20.43  ? 227 LYS A CG  1 
ATOM   1907 C  CD  . LYS A 1 227 ? -7.952  -14.266 -2.512  1.00 23.76  ? 227 LYS A CD  1 
ATOM   1908 C  CE  . LYS A 1 227 ? -8.578  -15.648 -2.668  1.00 45.85  ? 227 LYS A CE  1 
ATOM   1909 N  NZ  . LYS A 1 227 ? -9.671  -15.952 -1.698  1.00 57.11  ? 227 LYS A NZ  1 
ATOM   1910 N  N   . LEU A 1 228 ? -4.842  -10.281 0.545   1.00 14.17  ? 228 LEU A N   1 
ATOM   1911 C  CA  . LEU A 1 228 ? -4.177  -9.028  0.472   1.00 13.94  ? 228 LEU A CA  1 
ATOM   1912 C  C   . LEU A 1 228 ? -2.671  -9.251  0.659   1.00 16.14  ? 228 LEU A C   1 
ATOM   1913 O  O   . LEU A 1 228 ? -2.207  -10.324 1.128   1.00 15.79  ? 228 LEU A O   1 
ATOM   1914 C  CB  . LEU A 1 228 ? -4.632  -8.094  1.606   1.00 12.96  ? 228 LEU A CB  1 
ATOM   1915 C  CG  . LEU A 1 228 ? -6.091  -7.617  1.429   1.00 12.21  ? 228 LEU A CG  1 
ATOM   1916 C  CD1 . LEU A 1 228 ? -6.560  -6.987  2.722   1.00 14.03  ? 228 LEU A CD1 1 
ATOM   1917 C  CD2 . LEU A 1 228 ? -6.187  -6.670  0.241   1.00 14.34  ? 228 LEU A CD2 1 
ATOM   1918 N  N   . ASN A 1 229 ? -1.872  -8.280  0.233   1.00 14.25  ? 229 ASN A N   1 
ATOM   1919 C  CA  . ASN A 1 229 ? -0.381  -8.376  0.264   1.00 14.72  ? 229 ASN A CA  1 
ATOM   1920 C  C   . ASN A 1 229 ? 0.189   -7.231  1.080   1.00 15.08  ? 229 ASN A C   1 
ATOM   1921 O  O   . ASN A 1 229 ? -0.305  -6.067  1.033   1.00 14.68  ? 229 ASN A O   1 
ATOM   1922 C  CB  . ASN A 1 229 ? 0.199   -8.144  -1.137  1.00 16.07  ? 229 ASN A CB  1 
ATOM   1923 C  CG  . ASN A 1 229 ? 0.157   -9.373  -2.059  1.00 19.01  ? 229 ASN A CG  1 
ATOM   1924 O  OD1 . ASN A 1 229 ? 0.699   -9.279  -3.140  1.00 30.58  ? 229 ASN A OD1 1 
ATOM   1925 N  ND2 . ASN A 1 229 ? -0.561  -10.405 -1.713  1.00 23.08  ? 229 ASN A ND2 1 
ATOM   1926 N  N   . PHE A 1 230 ? 1.188   -7.517  1.915   1.00 16.17  ? 230 PHE A N   1 
ATOM   1927 C  CA  . PHE A 1 230 ? 1.920   -6.479  2.599   1.00 15.05  ? 230 PHE A CA  1 
ATOM   1928 C  C   . PHE A 1 230 ? 2.730   -5.629  1.640   1.00 18.63  ? 230 PHE A C   1 
ATOM   1929 O  O   . PHE A 1 230 ? 2.979   -4.464  1.885   1.00 17.63  ? 230 PHE A O   1 
ATOM   1930 C  CB  . PHE A 1 230 ? 2.940   -7.071  3.623   1.00 17.97  ? 230 PHE A CB  1 
ATOM   1931 C  CG  . PHE A 1 230 ? 2.383   -7.637  4.906   1.00 15.46  ? 230 PHE A CG  1 
ATOM   1932 C  CD1 . PHE A 1 230 ? 1.571   -6.865  5.792   1.00 15.77  ? 230 PHE A CD1 1 
ATOM   1933 C  CD2 . PHE A 1 230 ? 2.678   -8.938  5.303   1.00 16.97  ? 230 PHE A CD2 1 
ATOM   1934 C  CE1 . PHE A 1 230 ? 1.183   -7.389  7.058   1.00 14.56  ? 230 PHE A CE1 1 
ATOM   1935 C  CE2 . PHE A 1 230 ? 2.215   -9.485  6.534   1.00 15.51  ? 230 PHE A CE2 1 
ATOM   1936 C  CZ  . PHE A 1 230 ? 1.471   -8.714  7.420   1.00 16.17  ? 230 PHE A CZ  1 
ATOM   1937 N  N   . ASN A 1 231 ? 3.267   -6.294  0.638   1.00 16.87  ? 231 ASN A N   1 
ATOM   1938 C  CA  . ASN A 1 231 ? 4.238   -5.683  -0.253  1.00 16.78  ? 231 ASN A CA  1 
ATOM   1939 C  C   . ASN A 1 231 ? 3.552   -4.813  -1.271  1.00 15.43  ? 231 ASN A C   1 
ATOM   1940 O  O   . ASN A 1 231 ? 2.319   -4.918  -1.597  1.00 20.78  ? 231 ASN A O   1 
ATOM   1941 C  CB  . ASN A 1 231 ? 4.998   -6.829  -1.016  1.00 18.82  ? 231 ASN A CB  1 
ATOM   1942 C  CG  . ASN A 1 231 ? 4.017   -7.752  -1.711  1.00 18.16  ? 231 ASN A CG  1 
ATOM   1943 O  OD1 . ASN A 1 231 ? 3.368   -8.604  -1.066  1.00 18.85  ? 231 ASN A OD1 1 
ATOM   1944 N  ND2 . ASN A 1 231 ? 3.852   -7.545  -3.021  1.00 22.33  ? 231 ASN A ND2 1 
ATOM   1945 N  N   . GLY A 1 232 ? 4.344   -3.888  -1.803  1.00 18.80  ? 232 GLY A N   1 
ATOM   1946 C  CA  . GLY A 1 232 ? 4.000   -3.123  -2.970  1.00 17.80  ? 232 GLY A CA  1 
ATOM   1947 C  C   . GLY A 1 232 ? 4.102   -4.022  -4.243  1.00 19.36  ? 232 GLY A C   1 
ATOM   1948 O  O   . GLY A 1 232 ? 4.817   -5.043  -4.263  1.00 22.63  ? 232 GLY A O   1 
ATOM   1949 N  N   . GLU A 1 233 ? 3.309   -3.643  -5.239  1.00 28.27  ? 233 GLU A N   1 
ATOM   1950 C  CA  . GLU A 1 233 ? 3.345   -4.319  -6.536  1.00 32.44  ? 233 GLU A CA  1 
ATOM   1951 C  C   . GLU A 1 233 ? 4.793   -4.322  -7.072  1.00 37.56  ? 233 GLU A C   1 
ATOM   1952 O  O   . GLU A 1 233 ? 5.402   -3.272  -7.134  1.00 42.72  ? 233 GLU A O   1 
ATOM   1953 C  CB  . GLU A 1 233 ? 2.430   -3.639  -7.540  1.00 33.05  ? 233 GLU A CB  1 
ATOM   1954 C  CG  . GLU A 1 233 ? 2.874   -3.924  -8.983  1.00 50.61  ? 233 GLU A CG  1 
ATOM   1955 C  CD  . GLU A 1 233 ? 1.776   -4.369  -9.969  1.00 72.46  ? 233 GLU A CD  1 
ATOM   1956 O  OE1 . GLU A 1 233 ? 0.561   -4.370  -9.596  1.00 46.53  ? 233 GLU A OE1 1 
ATOM   1957 O  OE2 . GLU A 1 233 ? 2.142   -4.768  -11.168 1.00 90.78  ? 233 GLU A OE2 1 
ATOM   1958 N  N   . GLY A 1 234 ? 5.346   -5.498  -7.379  1.00 40.74  ? 234 GLY A N   1 
ATOM   1959 C  CA  . GLY A 1 234 ? 6.723   -5.605  -7.877  1.00 48.72  ? 234 GLY A CA  1 
ATOM   1960 C  C   . GLY A 1 234 ? 7.853   -5.841  -6.871  1.00 55.11  ? 234 GLY A C   1 
ATOM   1961 O  O   . GLY A 1 234 ? 9.022   -5.628  -7.255  1.00 42.29  ? 234 GLY A O   1 
ATOM   1962 N  N   . GLU A 1 235 ? 7.503   -6.220  -5.616  1.00 26.35  ? 235 GLU A N   1 
ATOM   1963 C  CA  . GLU A 1 235 ? 8.354   -6.688  -4.541  1.00 21.10  ? 235 GLU A CA  1 
ATOM   1964 C  C   . GLU A 1 235 ? 7.898   -8.067  -4.361  1.00 20.47  ? 235 GLU A C   1 
ATOM   1965 O  O   . GLU A 1 235 ? 6.749   -8.356  -4.734  1.00 27.34  ? 235 GLU A O   1 
ATOM   1966 C  CB  . GLU A 1 235 ? 8.038   -5.872  -3.258  1.00 23.10  ? 235 GLU A CB  1 
ATOM   1967 C  CG  . GLU A 1 235 ? 8.197   -4.361  -3.441  1.00 31.13  ? 235 GLU A CG  1 
ATOM   1968 C  CD  . GLU A 1 235 ? 7.593   -3.526  -2.268  1.00 31.93  ? 235 GLU A CD  1 
ATOM   1969 O  OE1 . GLU A 1 235 ? 7.185   -4.006  -1.140  1.00 29.46  ? 235 GLU A OE1 1 
ATOM   1970 O  OE2 . GLU A 1 235 ? 7.481   -2.316  -2.500  1.00 46.47  ? 235 GLU A OE2 1 
ATOM   1971 N  N   . PRO A 1 236 ? 8.705   -8.909  -3.735  1.00 20.17  ? 236 PRO A N   1 
ATOM   1972 C  CA  . PRO A 1 236 ? 8.309   -10.304 -3.408  1.00 20.74  ? 236 PRO A CA  1 
ATOM   1973 C  C   . PRO A 1 236 ? 6.967   -10.339 -2.675  1.00 19.65  ? 236 PRO A C   1 
ATOM   1974 O  O   . PRO A 1 236 ? 6.696   -9.492  -1.780  1.00 23.49  ? 236 PRO A O   1 
ATOM   1975 C  CB  . PRO A 1 236 ? 9.472   -10.797 -2.527  1.00 23.82  ? 236 PRO A CB  1 
ATOM   1976 C  CG  . PRO A 1 236 ? 10.594  -10.050 -3.136  1.00 21.74  ? 236 PRO A CG  1 
ATOM   1977 C  CD  . PRO A 1 236 ? 10.117  -8.661  -3.328  1.00 21.38  ? 236 PRO A CD  1 
ATOM   1978 N  N   . GLU A 1 237 ? 6.141   -11.334 -3.031  1.00 18.81  ? 237 GLU A N   1 
ATOM   1979 C  CA  . GLU A 1 237 ? 4.795   -11.425 -2.532  1.00 19.02  ? 237 GLU A CA  1 
ATOM   1980 C  C   . GLU A 1 237 ? 4.790   -12.007 -1.086  1.00 18.71  ? 237 GLU A C   1 
ATOM   1981 O  O   . GLU A 1 237 ? 5.262   -13.141 -0.844  1.00 21.70  ? 237 GLU A O   1 
ATOM   1982 C  CB  . GLU A 1 237 ? 4.004   -12.284 -3.506  1.00 21.93  ? 237 GLU A CB  1 
ATOM   1983 C  CG  . GLU A 1 237 ? 2.598   -12.631 -3.075  1.00 26.05  ? 237 GLU A CG  1 
ATOM   1984 C  CD  . GLU A 1 237 ? 1.910   -13.446 -4.165  1.00 45.97  ? 237 GLU A CD  1 
ATOM   1985 O  OE1 . GLU A 1 237 ? 2.247   -13.231 -5.344  1.00 53.54  ? 237 GLU A OE1 1 
ATOM   1986 O  OE2 . GLU A 1 237 ? 1.058   -14.313 -3.863  1.00 49.53  ? 237 GLU A OE2 1 
ATOM   1987 N  N   . GLU A 1 238 ? 4.233   -11.244 -0.155  1.00 16.80  ? 238 GLU A N   1 
ATOM   1988 C  CA  . GLU A 1 238 ? 4.099   -11.641 1.223   1.00 17.32  ? 238 GLU A CA  1 
ATOM   1989 C  C   . GLU A 1 238 ? 2.693   -11.388 1.588   1.00 14.15  ? 238 GLU A C   1 
ATOM   1990 O  O   . GLU A 1 238 ? 2.229   -10.223 1.587   1.00 19.09  ? 238 GLU A O   1 
ATOM   1991 C  CB  . GLU A 1 238 ? 5.036   -10.878 2.180   1.00 19.00  ? 238 GLU A CB  1 
ATOM   1992 C  CG  . GLU A 1 238 ? 6.497   -11.072 1.873   1.00 21.51  ? 238 GLU A CG  1 
ATOM   1993 C  CD  . GLU A 1 238 ? 7.362   -10.429 2.924   1.00 25.17  ? 238 GLU A CD  1 
ATOM   1994 O  OE1 . GLU A 1 238 ? 7.280   -10.777 4.128   1.00 27.98  ? 238 GLU A OE1 1 
ATOM   1995 O  OE2 . GLU A 1 238 ? 8.168   -9.526  2.565   1.00 26.51  ? 238 GLU A OE2 1 
ATOM   1996 N  N   A LEU A 1 239 ? 1.925   -12.434 1.899   0.50 13.98  ? 239 LEU A N   1 
ATOM   1997 N  N   B LEU A 1 239 ? 1.953   -12.468 1.817   0.50 21.13  ? 239 LEU A N   1 
ATOM   1998 C  CA  A LEU A 1 239 ? 0.526   -12.250 2.198   0.50 15.86  ? 239 LEU A CA  1 
ATOM   1999 C  CA  B LEU A 1 239 ? 0.579   -12.328 2.203   0.50 18.24  ? 239 LEU A CA  1 
ATOM   2000 C  C   A LEU A 1 239 ? 0.314   -11.517 3.522   0.50 13.94  ? 239 LEU A C   1 
ATOM   2001 C  C   B LEU A 1 239 ? 0.509   -11.316 3.378   0.50 15.75  ? 239 LEU A C   1 
ATOM   2002 O  O   A LEU A 1 239 ? 0.968   -11.773 4.562   0.50 10.27  ? 239 LEU A O   1 
ATOM   2003 O  O   B LEU A 1 239 ? 1.470   -11.175 4.153   0.50 15.11  ? 239 LEU A O   1 
ATOM   2004 C  CB  A LEU A 1 239 ? -0.209  -13.572 2.160   0.50 17.27  ? 239 LEU A CB  1 
ATOM   2005 C  CB  B LEU A 1 239 ? 0.008   -13.699 2.539   0.50 20.70  ? 239 LEU A CB  1 
ATOM   2006 C  CG  A LEU A 1 239 ? -0.207  -14.349 0.850   0.50 20.87  ? 239 LEU A CG  1 
ATOM   2007 C  CG  B LEU A 1 239 ? -0.320  -14.656 1.354   0.50 15.50  ? 239 LEU A CG  1 
ATOM   2008 C  CD1 A LEU A 1 239 ? -0.863  -15.702 1.059   0.50 26.46  ? 239 LEU A CD1 1 
ATOM   2009 C  CD1 B LEU A 1 239 ? 0.880   -14.996 0.439   0.50 13.42  ? 239 LEU A CD1 1 
ATOM   2010 C  CD2 A LEU A 1 239 ? -0.971  -13.525 -0.146  0.50 16.31  ? 239 LEU A CD2 1 
ATOM   2011 C  CD2 B LEU A 1 239 ? -1.131  -15.811 1.927   0.50 20.30  ? 239 LEU A CD2 1 
ATOM   2012 N  N   . MET A 1 240 ? -0.590  -10.546 3.435   1.00 14.72  ? 240 MET A N   1 
ATOM   2013 C  CA  . MET A 1 240 ? -0.965  -9.708  4.579   1.00 14.93  ? 240 MET A CA  1 
ATOM   2014 C  C   . MET A 1 240 ? -1.760  -10.585 5.548   1.00 13.34  ? 240 MET A C   1 
ATOM   2015 O  O   . MET A 1 240 ? -2.992  -10.732 5.367   1.00 14.13  ? 240 MET A O   1 
ATOM   2016 C  CB  . MET A 1 240 ? -1.761  -8.484  4.170   1.00 14.88  ? 240 MET A CB  1 
ATOM   2017 C  CG  . MET A 1 240 ? -2.103  -7.528  5.325   1.00 12.53  ? 240 MET A CG  1 
ATOM   2018 S  SD  . MET A 1 240 ? -3.030  -6.115  4.837   1.00 13.78  ? 240 MET A SD  1 
ATOM   2019 C  CE  . MET A 1 240 ? -1.723  -5.202  4.032   1.00 14.65  ? 240 MET A CE  1 
ATOM   2020 N  N   . VAL A 1 241 ? -1.038  -11.259 6.459   1.00 13.27  ? 241 VAL A N   1 
ATOM   2021 C  CA  . VAL A 1 241 ? -1.615  -12.102 7.505   1.00 11.98  ? 241 VAL A CA  1 
ATOM   2022 C  C   . VAL A 1 241 ? -0.852  -11.931 8.774   1.00 10.51  ? 241 VAL A C   1 
ATOM   2023 O  O   . VAL A 1 241 ? 0.365   -11.554 8.722   1.00 12.15  ? 241 VAL A O   1 
ATOM   2024 C  CB  . VAL A 1 241 ? -1.624  -13.641 7.070   1.00 12.63  ? 241 VAL A CB  1 
ATOM   2025 C  CG1 . VAL A 1 241 ? -2.522  -13.841 5.829   1.00 15.18  ? 241 VAL A CG1 1 
ATOM   2026 C  CG2 . VAL A 1 241 ? -0.197  -14.065 6.738   1.00 13.87  ? 241 VAL A CG2 1 
ATOM   2027 N  N   . ASP A 1 242 ? -1.421  -12.188 9.913   1.00 11.21  ? 242 ASP A N   1 
ATOM   2028 C  CA  . ASP A 1 242 ? -0.730  -12.082 11.192  1.00 10.42  ? 242 ASP A CA  1 
ATOM   2029 C  C   . ASP A 1 242 ? -0.254  -10.677 11.405  1.00 10.31  ? 242 ASP A C   1 
ATOM   2030 O  O   . ASP A 1 242 ? 0.839   -10.401 11.955  1.00 11.50  ? 242 ASP A O   1 
ATOM   2031 C  CB  . ASP A 1 242 ? 0.362   -13.164 11.380  1.00 11.27  ? 242 ASP A CB  1 
ATOM   2032 C  CG  . ASP A 1 242 ? -0.242  -14.527 11.472  1.00 11.34  ? 242 ASP A CG  1 
ATOM   2033 O  OD1 . ASP A 1 242 ? -1.317  -14.710 12.159  1.00 11.93  ? 242 ASP A OD1 1 
ATOM   2034 O  OD2 . ASP A 1 242 ? 0.346   -15.457 10.938  1.00 14.43  ? 242 ASP A OD2 1 
ATOM   2035 N  N   . ASN A 1 243 ? -1.135  -9.736  11.143  1.00 9.44   ? 243 ASN A N   1 
ATOM   2036 C  CA  . ASN A 1 243 ? -0.897  -8.284  11.375  1.00 8.78   ? 243 ASN A CA  1 
ATOM   2037 C  C   . ASN A 1 243 ? -1.477  -7.845  12.696  1.00 8.48   ? 243 ASN A C   1 
ATOM   2038 O  O   . ASN A 1 243 ? -2.173  -6.796  12.784  1.00 10.04  ? 243 ASN A O   1 
ATOM   2039 C  CB  . ASN A 1 243 ? -1.384  -7.406  10.194  1.00 9.96   ? 243 ASN A CB  1 
ATOM   2040 C  CG  . ASN A 1 243 ? -2.848  -7.618  9.890   1.00 10.32  ? 243 ASN A CG  1 
ATOM   2041 O  OD1 . ASN A 1 243 ? -3.514  -8.445  10.453  1.00 10.70  ? 243 ASN A OD1 1 
ATOM   2042 N  ND2 . ASN A 1 243 ? -3.375  -6.712  9.038   1.00 13.37  ? 243 ASN A ND2 1 
ATOM   2043 N  N   . TRP A 1 244 ? -1.166  -8.573  13.756  1.00 9.29   ? 244 TRP A N   1 
ATOM   2044 C  CA  . TRP A 1 244 ? -1.603  -8.350  15.090  1.00 8.84   ? 244 TRP A CA  1 
ATOM   2045 C  C   . TRP A 1 244 ? -0.408  -8.218  16.027  1.00 8.57   ? 244 TRP A C   1 
ATOM   2046 O  O   . TRP A 1 244 ? 0.566   -8.922  15.900  1.00 10.25  ? 244 TRP A O   1 
ATOM   2047 C  CB  . TRP A 1 244 ? -2.597  -9.411  15.569  1.00 9.11   ? 244 TRP A CB  1 
ATOM   2048 C  CG  . TRP A 1 244 ? -2.127  -10.843 15.410  1.00 9.27   ? 244 TRP A CG  1 
ATOM   2049 C  CD1 . TRP A 1 244 ? -2.255  -11.620 14.256  1.00 9.41   ? 244 TRP A CD1 1 
ATOM   2050 C  CD2 . TRP A 1 244 ? -1.485  -11.685 16.406  1.00 8.86   ? 244 TRP A CD2 1 
ATOM   2051 N  NE1 . TRP A 1 244 ? -1.709  -12.859 14.450  1.00 9.33   ? 244 TRP A NE1 1 
ATOM   2052 C  CE2 . TRP A 1 244 ? -1.284  -12.966 15.764  1.00 10.50  ? 244 TRP A CE2 1 
ATOM   2053 C  CE3 . TRP A 1 244 ? -1.196  -11.559 17.737  1.00 10.08  ? 244 TRP A CE3 1 
ATOM   2054 C  CZ2 . TRP A 1 244 ? -0.675  -14.064 16.457  1.00 10.72  ? 244 TRP A CZ2 1 
ATOM   2055 C  CZ3 . TRP A 1 244 ? -0.634  -12.628 18.433  1.00 11.13  ? 244 TRP A CZ3 1 
ATOM   2056 C  CH2 . TRP A 1 244 ? -0.396  -13.868 17.802  1.00 11.65  ? 244 TRP A CH2 1 
ATOM   2057 N  N   . ARG A 1 245 ? -0.535  -7.317  16.993  1.00 9.17   ? 245 ARG A N   1 
ATOM   2058 C  CA  . ARG A 1 245 ? 0.443   -7.177  18.047  1.00 8.13   ? 245 ARG A CA  1 
ATOM   2059 C  C   . ARG A 1 245 ? -0.044  -8.097  19.177  1.00 8.94   ? 245 ARG A C   1 
ATOM   2060 O  O   . ARG A 1 245 ? -1.237  -8.104  19.507  1.00 10.10  ? 245 ARG A O   1 
ATOM   2061 C  CB  . ARG A 1 245 ? 0.482   -5.701  18.547  1.00 8.41   ? 245 ARG A CB  1 
ATOM   2062 C  CG  . ARG A 1 245 ? 1.586   -5.511  19.594  1.00 8.99   ? 245 ARG A CG  1 
ATOM   2063 C  CD  . ARG A 1 245 ? 1.505   -4.127  20.187  1.00 9.92   ? 245 ARG A CD  1 
ATOM   2064 N  NE  . ARG A 1 245 ? 2.770   -3.776  20.846  1.00 9.81   ? 245 ARG A NE  1 
ATOM   2065 C  CZ  . ARG A 1 245 ? 2.946   -2.779  21.713  1.00 9.60   ? 245 ARG A CZ  1 
ATOM   2066 N  NH1 . ARG A 1 245 ? 1.940   -1.982  22.049  1.00 10.30  ? 245 ARG A NH1 1 
ATOM   2067 N  NH2 . ARG A 1 245 ? 4.146   -2.573  22.244  1.00 11.43  ? 245 ARG A NH2 1 
ATOM   2068 N  N   . PRO A 1 246 ? 0.882   -8.889  19.795  1.00 9.72   ? 246 PRO A N   1 
ATOM   2069 C  CA  . PRO A 1 246 ? 0.418   -9.748  20.911  1.00 10.63  ? 246 PRO A CA  1 
ATOM   2070 C  C   . PRO A 1 246 ? 0.075   -8.941  22.196  1.00 10.09  ? 246 PRO A C   1 
ATOM   2071 O  O   . PRO A 1 246 ? 0.458   -7.739  22.330  1.00 10.22  ? 246 PRO A O   1 
ATOM   2072 C  CB  . PRO A 1 246 ? 1.640   -10.658 21.191  1.00 12.33  ? 246 PRO A CB  1 
ATOM   2073 C  CG  . PRO A 1 246 ? 2.541   -10.457 20.061  1.00 19.77  ? 246 PRO A CG  1 
ATOM   2074 C  CD  . PRO A 1 246 ? 2.274   -9.133  19.445  1.00 12.21  ? 246 PRO A CD  1 
ATOM   2075 N  N   . ALA A 1 247 ? -0.556  -9.578  23.168  1.00 10.55  ? 247 ALA A N   1 
ATOM   2076 C  CA  . ALA A 1 247 ? -0.924  -8.976  24.452  1.00 10.77  ? 247 ALA A CA  1 
ATOM   2077 C  C   . ALA A 1 247 ? 0.334   -8.449  25.152  1.00 9.74   ? 247 ALA A C   1 
ATOM   2078 O  O   . ALA A 1 247 ? 1.377   -9.124  25.173  1.00 12.18  ? 247 ALA A O   1 
ATOM   2079 C  CB  . ALA A 1 247 ? -1.592  -9.984  25.307  1.00 13.34  ? 247 ALA A CB  1 
ATOM   2080 N  N   . GLN A 1 248 ? 0.208   -7.253  25.708  1.00 9.34   ? 248 GLN A N   1 
ATOM   2081 C  CA  . GLN A 1 248 ? 1.252   -6.534  26.429  1.00 10.84  ? 248 GLN A CA  1 
ATOM   2082 C  C   . GLN A 1 248 ? 0.961   -6.533  27.925  1.00 11.81  ? 248 GLN A C   1 
ATOM   2083 O  O   . GLN A 1 248 ? -0.161  -6.787  28.374  1.00 12.23  ? 248 GLN A O   1 
ATOM   2084 C  CB  . GLN A 1 248 ? 1.315   -5.118  25.899  1.00 11.09  ? 248 GLN A CB  1 
ATOM   2085 C  CG  . GLN A 1 248 ? 1.625   -5.022  24.407  1.00 10.64  ? 248 GLN A CG  1 
ATOM   2086 C  CD  . GLN A 1 248 ? 2.939   -5.706  24.064  1.00 12.14  ? 248 GLN A CD  1 
ATOM   2087 O  OE1 . GLN A 1 248 ? 3.952   -5.381  24.680  1.00 15.36  ? 248 GLN A OE1 1 
ATOM   2088 N  NE2 . GLN A 1 248 ? 2.945   -6.636  23.118  1.00 12.43  ? 248 GLN A NE2 1 
ATOM   2089 N  N   . PRO A 1 249 ? 1.986   -6.247  28.763  1.00 12.77  ? 249 PRO A N   1 
ATOM   2090 C  CA  . PRO A 1 249 ? 1.761   -6.357  30.197  1.00 15.05  ? 249 PRO A CA  1 
ATOM   2091 C  C   . PRO A 1 249 ? 0.686   -5.351  30.684  1.00 12.57  ? 249 PRO A C   1 
ATOM   2092 O  O   . PRO A 1 249 ? 0.708   -4.171  30.335  1.00 13.40  ? 249 PRO A O   1 
ATOM   2093 C  CB  . PRO A 1 249 ? 3.154   -6.014  30.814  1.00 21.07  ? 249 PRO A CB  1 
ATOM   2094 C  CG  . PRO A 1 249 ? 4.126   -6.197  29.698  1.00 17.77  ? 249 PRO A CG  1 
ATOM   2095 C  CD  . PRO A 1 249 ? 3.397   -6.010  28.422  1.00 16.82  ? 249 PRO A CD  1 
ATOM   2096 N  N   . LEU A 1 250 ? -0.181  -5.808  31.568  1.00 13.26  ? 250 LEU A N   1 
ATOM   2097 C  CA  . LEU A 1 250 ? -1.265  -4.933  32.057  1.00 12.71  ? 250 LEU A CA  1 
ATOM   2098 C  C   . LEU A 1 250 ? -0.710  -3.890  33.011  1.00 12.98  ? 250 LEU A C   1 
ATOM   2099 O  O   . LEU A 1 250 ? -1.248  -2.753  33.123  1.00 12.47  ? 250 LEU A O   1 
ATOM   2100 C  CB  . LEU A 1 250 ? -2.296  -5.773  32.769  1.00 14.26  ? 250 LEU A CB  1 
ATOM   2101 C  CG  . LEU A 1 250 ? -3.605  -5.092  33.140  1.00 14.79  ? 250 LEU A CG  1 
ATOM   2102 C  CD1 . LEU A 1 250 ? -4.326  -4.502  31.953  1.00 15.62  ? 250 LEU A CD1 1 
ATOM   2103 C  CD2 . LEU A 1 250 ? -4.473  -6.102  33.922  1.00 18.55  ? 250 LEU A CD2 1 
ATOM   2104 N  N   . LYS A 1 251 ? 0.379   -4.175  33.710  1.00 15.05  ? 251 LYS A N   1 
ATOM   2105 C  CA  . LYS A 1 251 ? 1.004   -3.199  34.630  1.00 17.02  ? 251 LYS A CA  1 
ATOM   2106 C  C   . LYS A 1 251 ? -0.020  -2.731  35.658  1.00 19.11  ? 251 LYS A C   1 
ATOM   2107 O  O   . LYS A 1 251 ? -0.789  -3.575  36.181  1.00 27.97  ? 251 LYS A O   1 
ATOM   2108 C  CB  . LYS A 1 251 ? 1.774   -2.064  33.906  1.00 18.13  ? 251 LYS A CB  1 
ATOM   2109 C  CG  . LYS A 1 251 ? 2.817   -2.783  33.110  1.00 22.87  ? 251 LYS A CG  1 
ATOM   2110 C  CD  . LYS A 1 251 ? 3.791   -1.871  32.558  1.00 27.21  ? 251 LYS A CD  1 
ATOM   2111 C  CE  . LYS A 1 251 ? 5.036   -2.644  32.241  1.00 30.81  ? 251 LYS A CE  1 
ATOM   2112 N  NZ  . LYS A 1 251 ? 5.732   -1.845  31.189  1.00 33.83  ? 251 LYS A NZ  1 
ATOM   2113 N  N   . ASN A 1 252 ? -0.116  -1.464  35.974  1.00 20.91  ? 252 ASN A N   1 
ATOM   2114 C  CA  . ASN A 1 252 ? -1.025  -1.306  37.145  1.00 37.23  ? 252 ASN A CA  1 
ATOM   2115 C  C   . ASN A 1 252 ? -2.583  -1.291  36.834  1.00 26.12  ? 252 ASN A C   1 
ATOM   2116 O  O   . ASN A 1 252 ? -3.419  -1.099  37.743  1.00 28.54  ? 252 ASN A O   1 
ATOM   2117 C  CB  . ASN A 1 252 ? -0.519  -0.213  38.146  1.00 45.99  ? 252 ASN A CB  1 
ATOM   2118 C  CG  . ASN A 1 252 ? 0.628   0.588   37.578  1.00 60.08  ? 252 ASN A CG  1 
ATOM   2119 O  OD1 . ASN A 1 252 ? 0.422   1.600   36.910  1.00 95.21  ? 252 ASN A OD1 1 
ATOM   2120 N  ND2 . ASN A 1 252 ? 1.852   0.113   37.803  1.00 72.08  ? 252 ASN A ND2 1 
ATOM   2121 N  N   . ARG A 1 253 ? -2.975  -1.574  35.609  1.00 15.13  ? 253 ARG A N   1 
ATOM   2122 C  CA  . ARG A 1 253 ? -4.264  -1.109  35.127  1.00 13.69  ? 253 ARG A CA  1 
ATOM   2123 C  C   . ARG A 1 253 ? -5.356  -2.061  35.563  1.00 14.33  ? 253 ARG A C   1 
ATOM   2124 O  O   . ARG A 1 253 ? -5.147  -3.277  35.749  1.00 21.82  ? 253 ARG A O   1 
ATOM   2125 C  CB  . ARG A 1 253 ? -4.206  -1.050  33.644  1.00 12.40  ? 253 ARG A CB  1 
ATOM   2126 C  CG  . ARG A 1 253 ? -3.300  0.098   33.146  1.00 12.06  ? 253 ARG A CG  1 
ATOM   2127 C  CD  . ARG A 1 253 ? -3.179  0.112   31.664  1.00 11.09  ? 253 ARG A CD  1 
ATOM   2128 N  NE  . ARG A 1 253 ? -2.371  -1.015  31.170  1.00 9.89   ? 253 ARG A NE  1 
ATOM   2129 C  CZ  . ARG A 1 253 ? -2.131  -1.239  29.907  1.00 9.95   ? 253 ARG A CZ  1 
ATOM   2130 N  NH1 . ARG A 1 253 ? -2.765  -0.581  28.923  1.00 9.74   ? 253 ARG A NH1 1 
ATOM   2131 N  NH2 . ARG A 1 253 ? -1.327  -2.270  29.533  1.00 10.04  ? 253 ARG A NH2 1 
ATOM   2132 N  N   A GLN A 1 254 ? -6.545  -1.478  35.767  0.50 15.80  ? 254 GLN A N   1 
ATOM   2133 N  N   B GLN A 1 254 ? -6.572  -1.545  35.655  0.50 13.63  ? 254 GLN A N   1 
ATOM   2134 C  CA  A GLN A 1 254 ? -7.788  -2.198  35.956  0.50 15.42  ? 254 GLN A CA  1 
ATOM   2135 C  CA  B GLN A 1 254 ? -7.734  -2.323  35.939  0.50 17.41  ? 254 GLN A CA  1 
ATOM   2136 C  C   A GLN A 1 254 ? -8.621  -2.236  34.659  0.50 15.70  ? 254 GLN A C   1 
ATOM   2137 C  C   B GLN A 1 254 ? -8.588  -2.268  34.693  0.50 15.06  ? 254 GLN A C   1 
ATOM   2138 O  O   A GLN A 1 254 ? -8.792  -1.216  33.937  0.50 17.60  ? 254 GLN A O   1 
ATOM   2139 O  O   B GLN A 1 254 ? -8.730  -1.210  34.044  0.50 20.92  ? 254 GLN A O   1 
ATOM   2140 C  CB  A GLN A 1 254 ? -8.642  -1.578  37.072  0.50 17.10  ? 254 GLN A CB  1 
ATOM   2141 C  CB  B GLN A 1 254 ? -8.531  -1.691  37.068  0.50 21.68  ? 254 GLN A CB  1 
ATOM   2142 C  CG  A GLN A 1 254 ? -9.766  -2.516  37.506  0.50 19.13  ? 254 GLN A CG  1 
ATOM   2143 C  CG  B GLN A 1 254 ? -7.779  -1.646  38.385  0.50 24.10  ? 254 GLN A CG  1 
ATOM   2144 C  CD  A GLN A 1 254 ? -10.586 -1.948  38.647  0.50 21.36  ? 254 GLN A CD  1 
ATOM   2145 C  CD  B GLN A 1 254 ? -8.654  -1.208  39.558  0.50 30.88  ? 254 GLN A CD  1 
ATOM   2146 O  OE1 A GLN A 1 254 ? -11.088 -0.802  38.580  0.50 30.25  ? 254 GLN A OE1 1 
ATOM   2147 O  OE1 B GLN A 1 254 ? -9.846  -0.916  39.379  0.50 34.14  ? 254 GLN A OE1 1 
ATOM   2148 N  NE2 A GLN A 1 254 ? -10.767 -2.749  39.678  0.50 24.70  ? 254 GLN A NE2 1 
ATOM   2149 N  NE2 B GLN A 1 254 ? -8.078  -1.159  40.764  0.50 27.18  ? 254 GLN A NE2 1 
ATOM   2150 N  N   . ILE A 1 255 ? -9.156  -3.407  34.335  1.00 12.73  ? 255 ILE A N   1 
ATOM   2151 C  CA  . ILE A 1 255 ? -10.171 -3.497  33.274  1.00 11.51  ? 255 ILE A CA  1 
ATOM   2152 C  C   . ILE A 1 255 ? -11.519 -3.490  33.946  1.00 10.90  ? 255 ILE A C   1 
ATOM   2153 O  O   . ILE A 1 255 ? -11.745 -4.207  34.933  1.00 13.02  ? 255 ILE A O   1 
ATOM   2154 C  CB  . ILE A 1 255 ? -9.969  -4.746  32.445  1.00 11.47  ? 255 ILE A CB  1 
ATOM   2155 C  CG1 . ILE A 1 255 ? -8.529  -4.756  31.885  1.00 13.14  ? 255 ILE A CG1 1 
ATOM   2156 C  CG2 . ILE A 1 255 ? -11.006 -4.772  31.282  1.00 14.18  ? 255 ILE A CG2 1 
ATOM   2157 C  CD1 . ILE A 1 255 ? -8.228  -5.975  31.063  1.00 13.58  ? 255 ILE A CD1 1 
ATOM   2158 N  N   . LYS A 1 256 ? -12.398 -2.622  33.462  1.00 11.62  ? 256 LYS A N   1 
ATOM   2159 C  CA  . LYS A 1 256 ? -13.774 -2.474  33.966  1.00 11.74  ? 256 LYS A CA  1 
ATOM   2160 C  C   . LYS A 1 256 ? -14.743 -3.143  32.991  1.00 12.12  ? 256 LYS A C   1 
ATOM   2161 O  O   . LYS A 1 256 ? -14.486 -3.133  31.800  1.00 13.89  ? 256 LYS A O   1 
ATOM   2162 C  CB  . LYS A 1 256 ? -14.077 -0.970  34.129  1.00 14.40  ? 256 LYS A CB  1 
ATOM   2163 C  CG  . LYS A 1 256 ? -13.127 -0.243  35.128  1.00 18.22  ? 256 LYS A CG  1 
ATOM   2164 C  CD  . LYS A 1 256 ? -13.549 1.199   35.379  1.00 29.36  ? 256 LYS A CD  1 
ATOM   2165 C  CE  . LYS A 1 256 ? -12.594 1.785   36.443  1.00 45.98  ? 256 LYS A CE  1 
ATOM   2166 N  NZ  . LYS A 1 256 ? -12.491 3.277   36.527  1.00 41.88  ? 256 LYS A NZ  1 
ATOM   2167 N  N   . ALA A 1 257 ? -15.813 -3.777  33.524  1.00 11.80  ? 257 ALA A N   1 
ATOM   2168 C  CA  . ALA A 1 257 ? -16.890 -4.367  32.723  1.00 12.50  ? 257 ALA A CA  1 
ATOM   2169 C  C   . ALA A 1 257 ? -18.134 -3.502  32.895  1.00 12.26  ? 257 ALA A C   1 
ATOM   2170 O  O   . ALA A 1 257 ? -18.486 -3.105  34.001  1.00 14.45  ? 257 ALA A O   1 
ATOM   2171 C  CB  . ALA A 1 257 ? -17.141 -5.785  33.163  1.00 15.34  ? 257 ALA A CB  1 
ATOM   2172 N  N   . SER A 1 258 ? -18.867 -3.414  31.793  1.00 11.10  ? 258 SER A N   1 
ATOM   2173 C  CA  . SER A 1 258 ? -20.143 -2.677  31.857  1.00 12.93  ? 258 SER A CA  1 
ATOM   2174 C  C   . SER A 1 258 ? -21.308 -3.592  32.309  1.00 14.88  ? 258 SER A C   1 
ATOM   2175 O  O   . SER A 1 258 ? -22.459 -3.127  32.365  1.00 19.12  ? 258 SER A O   1 
ATOM   2176 C  CB  . SER A 1 258 ? -20.413 -2.130  30.494  1.00 15.08  ? 258 SER A CB  1 
ATOM   2177 O  OG  . SER A 1 258 ? -20.880 -3.119  29.577  1.00 13.91  ? 258 SER A OG  1 
ATOM   2178 N  N   . PHE A 1 259 ? -21.014 -4.888  32.565  1.00 15.73  ? 259 PHE A N   1 
ATOM   2179 C  CA  . PHE A 1 259 ? -22.023 -5.975  32.712  1.00 19.34  ? 259 PHE A CA  1 
ATOM   2180 C  C   . PHE A 1 259 ? -21.498 -6.957  33.783  1.00 19.74  ? 259 PHE A C   1 
ATOM   2181 O  O   . PHE A 1 259 ? -20.273 -7.033  34.065  1.00 20.81  ? 259 PHE A O   1 
ATOM   2182 C  CB  . PHE A 1 259 ? -22.262 -6.674  31.368  1.00 18.29  ? 259 PHE A CB  1 
ATOM   2183 C  CG  . PHE A 1 259 ? -21.045 -7.405  30.916  1.00 17.83  ? 259 PHE A CG  1 
ATOM   2184 C  CD1 . PHE A 1 259 ? -20.045 -6.714  30.220  1.00 13.88  ? 259 PHE A CD1 1 
ATOM   2185 C  CD2 . PHE A 1 259 ? -20.829 -8.750  31.285  1.00 21.87  ? 259 PHE A CD2 1 
ATOM   2186 C  CE1 . PHE A 1 259 ? -18.837 -7.397  29.876  1.00 15.57  ? 259 PHE A CE1 1 
ATOM   2187 C  CE2 . PHE A 1 259 ? -19.650 -9.393  30.961  1.00 19.70  ? 259 PHE A CE2 1 
ATOM   2188 C  CZ  . PHE A 1 259 ? -18.675 -8.745  30.231  1.00 19.42  ? 259 PHE A CZ  1 
ATOM   2189 N  N   . LYS A 1 260 ? -22.443 -7.699  34.381  1.00 29.49  ? 260 LYS A N   1 
ATOM   2190 C  CA  . LYS A 1 260 ? -22.141 -8.729  35.432  1.00 39.55  ? 260 LYS A CA  1 
ATOM   2191 C  C   . LYS A 1 260 ? -22.358 -10.149 34.917  1.00 52.15  ? 260 LYS A C   1 
ATOM   2192 C  CB  . LYS A 1 260 ? -22.970 -8.514  36.712  1.00 48.03  ? 260 LYS A CB  1 
ATOM   2193 C  CG  . LYS A 1 260 ? -22.345 -7.646  37.789  1.00 51.37  ? 260 LYS A CG  1 
ATOM   2194 C  CD  . LYS A 1 260 ? -23.042 -7.857  39.149  1.00 64.85  ? 260 LYS A CD  1 
ATOM   2195 C  CE  . LYS A 1 260 ? -22.324 -7.173  40.342  1.00 68.69  ? 260 LYS A CE  1 
ATOM   2196 N  NZ  . LYS A 1 260 ? -21.068 -7.781  40.932  1.00 63.53  ? 260 LYS A NZ  1 
ATOM   2197 O  OXT . LYS A 1 260 ? -22.846 -10.342 33.857  1.00 56.26  ? 260 LYS A OXT 1 
HETATM 2198 ZN ZN  . ZN  B 2 .   ? -6.165  -1.759  15.197  1.00 7.57   ? 301 ZN  A ZN  1 
HETATM 2199 F  F20 . V14 C 3 .   ? -5.595  3.661   15.608  1.00 11.33  ? 302 V14 A F20 1 
HETATM 2200 C  C5  . V14 C 3 .   ? -4.878  2.942   14.697  1.00 11.21  ? 302 V14 A C5  1 
HETATM 2201 C  C4  . V14 C 3 .   ? -4.605  1.595   14.936  1.00 10.14  ? 302 V14 A C4  1 
HETATM 2202 S  S7  . V14 C 3 .   ? -5.261  0.887   16.470  1.00 8.71   ? 302 V14 A S7  1 
HETATM 2203 O  O9  . V14 C 3 .   ? -6.654  1.251   16.452  1.00 8.87   ? 302 V14 A O9  1 
HETATM 2204 N  N10 . V14 C 3 .   ? -5.088  -0.599  16.324  1.00 10.43  ? 302 V14 A N10 1 
HETATM 2205 O  O8  . V14 C 3 .   ? -4.435  1.391   17.512  1.00 9.42   ? 302 V14 A O8  1 
HETATM 2206 C  C3  . V14 C 3 .   ? -3.938  0.923   13.982  1.00 10.65  ? 302 V14 A C3  1 
HETATM 2207 F  F12 . V14 C 3 .   ? -3.644  -0.412  14.056  1.00 12.44  ? 302 V14 A F12 1 
HETATM 2208 C  C2  . V14 C 3 .   ? -3.547  1.457   12.799  1.00 13.71  ? 302 V14 A C2  1 
HETATM 2209 F  F13 . V14 C 3 .   ? -2.864  0.759   11.899  1.00 16.19  ? 302 V14 A F13 1 
HETATM 2210 C  C6  . V14 C 3 .   ? -4.483  3.593   13.508  1.00 12.63  ? 302 V14 A C6  1 
HETATM 2211 C  C1  . V14 C 3 .   ? -3.777  2.825   12.584  1.00 13.98  ? 302 V14 A C1  1 
HETATM 2212 S  S11 . V14 C 3 .   ? -3.016  3.489   11.086  1.00 17.78  ? 302 V14 A S11 1 
HETATM 2213 O  O16 . V14 C 3 .   ? -3.565  4.810   10.868  1.00 26.05  ? 302 V14 A O16 1 
HETATM 2214 O  O17 . V14 C 3 .   ? -3.212  2.582   9.971   1.00 18.68  ? 302 V14 A O17 1 
HETATM 2215 C  C15 . V14 C 3 .   ? -1.200  3.464   11.098  1.00 29.58  ? 302 V14 A C15 1 
HETATM 2216 C  C18 . V14 C 3 .   ? -0.532  4.314   12.159  1.00 30.82  ? 302 V14 A C18 1 
HETATM 2217 O  O21 . V14 C 3 .   ? -0.571  3.817   13.494  1.00 28.83  ? 302 V14 A O21 1 
HETATM 2218 N  N19 . V14 C 3 .   ? -4.826  4.944   13.274  1.00 16.02  ? 302 V14 A N19 1 
HETATM 2219 C  C14 . V14 C 3 .   ? -4.952  6.064   14.222  1.00 14.82  ? 302 V14 A C14 1 
HETATM 2220 C  C28 . V14 C 3 .   ? -3.567  6.271   14.751  1.00 16.66  ? 302 V14 A C28 1 
HETATM 2221 C  C27 . V14 C 3 .   ? -2.629  7.058   13.873  1.00 18.36  ? 302 V14 A C27 1 
HETATM 2222 C  C26 . V14 C 3 .   ? -2.559  8.562   14.374  1.00 21.79  ? 302 V14 A C26 1 
HETATM 2223 C  C25 . V14 C 3 .   ? -3.784  9.541   14.120  1.00 20.37  ? 302 V14 A C25 1 
HETATM 2224 C  C24 . V14 C 3 .   ? -5.026  9.248   14.997  1.00 17.65  ? 302 V14 A C24 1 
HETATM 2225 C  C23 . V14 C 3 .   ? -6.161  8.368   14.384  1.00 16.54  ? 302 V14 A C23 1 
HETATM 2226 C  C22 . V14 C 3 .   ? -5.678  7.230   13.547  1.00 15.47  ? 302 V14 A C22 1 
HETATM 2227 S  S   . DMS D 4 .   ? 1.877   -11.573 14.747  1.00 26.94  ? 303 DMS A S   1 
HETATM 2228 O  O   . DMS D 4 .   ? 2.526   -12.814 14.197  1.00 61.16  ? 303 DMS A O   1 
HETATM 2229 C  C1  . DMS D 4 .   ? 2.185   -11.465 16.420  1.00 21.42  ? 303 DMS A C1  1 
HETATM 2230 C  C2  . DMS D 4 .   ? 3.153   -10.490 14.532  1.00 32.71  ? 303 DMS A C2  1 
HETATM 2231 C  C1  . EDO E 5 .   ? -7.534  -9.219  -2.094  1.00 27.23  ? 304 EDO A C1  1 
HETATM 2232 O  O1  . EDO E 5 .   ? -8.683  -10.062 -1.763  1.00 30.12  ? 304 EDO A O1  1 
HETATM 2233 C  C2  . EDO E 5 .   ? -6.710  -9.706  -3.304  1.00 29.45  ? 304 EDO A C2  1 
HETATM 2234 O  O2  . EDO E 5 .   ? -7.385  -10.388 -4.424  1.00 41.78  ? 304 EDO A O2  1 
HETATM 2235 C  C1  . EDO F 5 .   ? -27.595 6.151   19.031  1.00 46.70  ? 305 EDO A C1  1 
HETATM 2236 O  O1  . EDO F 5 .   ? -27.548 7.067   20.351  1.00 104.15 ? 305 EDO A O1  1 
HETATM 2237 C  C2  . EDO F 5 .   ? -28.691 6.857   17.974  1.00 97.05  ? 305 EDO A C2  1 
HETATM 2238 O  O2  . EDO F 5 .   ? -27.912 6.526   16.451  1.00 69.31  ? 305 EDO A O2  1 
HETATM 2239 C  C1  . EDO G 5 .   ? -4.743  -20.742 25.584  1.00 54.67  ? 306 EDO A C1  1 
HETATM 2240 O  O1  . EDO G 5 .   ? -5.104  -20.931 27.022  1.00 63.86  ? 306 EDO A O1  1 
HETATM 2241 C  C2  . EDO G 5 .   ? -5.992  -20.084 24.814  1.00 42.27  ? 306 EDO A C2  1 
HETATM 2242 O  O2  . EDO G 5 .   ? -5.539  -19.616 23.516  1.00 29.75  ? 306 EDO A O2  1 
HETATM 2243 C  C1  . EDO H 5 .   ? -7.464  -19.363 20.323  1.00 22.24  ? 307 EDO A C1  1 
HETATM 2244 O  O1  . EDO H 5 .   ? -7.471  -19.397 21.665  1.00 21.15  ? 307 EDO A O1  1 
HETATM 2245 C  C2  . EDO H 5 .   ? -6.112  -20.032 20.302  1.00 29.85  ? 307 EDO A C2  1 
HETATM 2246 O  O2  . EDO H 5 .   ? -5.992  -20.377 18.984  1.00 19.37  ? 307 EDO A O2  1 
HETATM 2247 C  C1  . EDO I 5 .   ? 5.622   -10.777 17.097  1.00 36.58  ? 308 EDO A C1  1 
HETATM 2248 O  O1  . EDO I 5 .   ? 5.763   -11.100 18.515  1.00 45.34  ? 308 EDO A O1  1 
HETATM 2249 C  C2  . EDO I 5 .   ? 6.618   -11.492 16.147  1.00 42.12  ? 308 EDO A C2  1 
HETATM 2250 O  O2  . EDO I 5 .   ? 6.812   -10.790 14.874  1.00 30.21  ? 308 EDO A O2  1 
HETATM 2251 O  O   . HOH J 6 .   ? -16.509 -8.380  20.206  1.00 10.18  ? 401 HOH A O   1 
HETATM 2252 O  O   . HOH J 6 .   ? -21.256 5.693   4.648   1.00 11.95  ? 402 HOH A O   1 
HETATM 2253 O  O   . HOH J 6 .   ? -20.606 7.793   1.764   1.00 11.15  ? 403 HOH A O   1 
HETATM 2254 O  O   . HOH J 6 .   ? -21.080 -7.025  23.386  1.00 12.94  ? 404 HOH A O   1 
HETATM 2255 O  O   . HOH J 6 .   ? -2.989  -11.197 20.697  1.00 11.02  ? 405 HOH A O   1 
HETATM 2256 O  O   . HOH J 6 .   ? 4.113   4.956   29.917  1.00 21.63  ? 406 HOH A O   1 
HETATM 2257 O  O   . HOH J 6 .   ? 1.842   -1.666  29.257  1.00 15.20  ? 407 HOH A O   1 
HETATM 2258 O  O   . HOH J 6 .   ? -4.009  -13.548 17.825  1.00 10.72  ? 408 HOH A O   1 
HETATM 2259 O  O   . HOH J 6 .   ? -0.735  -4.076  15.501  1.00 10.43  ? 409 HOH A O   1 
HETATM 2260 O  O   . HOH J 6 .   ? -18.666 10.062  8.704   1.00 12.51  ? 410 HOH A O   1 
HETATM 2261 O  O   . HOH J 6 .   ? -2.830  -13.309 24.982  1.00 12.81  ? 411 HOH A O   1 
HETATM 2262 O  O   . HOH J 6 .   ? -17.411 20.557  7.798   1.00 12.46  ? 412 HOH A O   1 
HETATM 2263 O  O   . HOH J 6 .   ? -24.315 11.981  6.123   1.00 17.92  ? 413 HOH A O   1 
HETATM 2264 O  O   . HOH J 6 .   ? -17.326 10.644  11.169  1.00 15.05  ? 414 HOH A O   1 
HETATM 2265 O  O   . HOH J 6 .   ? 5.439   -4.855  20.851  1.00 13.76  ? 415 HOH A O   1 
HETATM 2266 O  O   . HOH J 6 .   ? 9.088   -3.647  20.952  1.00 12.79  ? 416 HOH A O   1 
HETATM 2267 O  O   . HOH J 6 .   ? -8.870  14.682  11.610  1.00 30.49  ? 417 HOH A O   1 
HETATM 2268 O  O   . HOH J 6 .   ? -3.263  -15.944 24.225  1.00 14.66  ? 418 HOH A O   1 
HETATM 2269 O  O   . HOH J 6 .   ? -1.536  -12.343 22.678  1.00 11.46  ? 419 HOH A O   1 
HETATM 2270 O  O   . HOH J 6 .   ? 3.154   -11.520 9.447   1.00 22.76  ? 420 HOH A O   1 
HETATM 2271 O  O   . HOH J 6 .   ? -7.453  -15.517 11.198  1.00 14.58  ? 421 HOH A O   1 
HETATM 2272 O  O   . HOH J 6 .   ? -22.701 -2.908  6.426   1.00 16.69  ? 422 HOH A O   1 
HETATM 2273 O  O   . HOH J 6 .   ? 15.721  -2.353  14.239  1.00 15.98  ? 423 HOH A O   1 
HETATM 2274 O  O   . HOH J 6 .   ? -9.080  -8.016  33.910  1.00 28.01  ? 424 HOH A O   1 
HETATM 2275 O  O   . HOH J 6 .   ? -24.105 4.516   8.686   1.00 26.58  ? 425 HOH A O   1 
HETATM 2276 O  O   . HOH J 6 .   ? -12.552 -16.796 26.388  1.00 22.44  ? 426 HOH A O   1 
HETATM 2277 O  O   . HOH J 6 .   ? -26.192 3.564   20.806  1.00 41.41  ? 427 HOH A O   1 
HETATM 2278 O  O   . HOH J 6 .   ? -1.977  -8.748  28.996  1.00 13.71  ? 428 HOH A O   1 
HETATM 2279 O  O   . HOH J 6 .   ? 8.559   -9.248  16.330  1.00 20.43  ? 429 HOH A O   1 
HETATM 2280 O  O   . HOH J 6 .   ? -23.244 -0.807  3.810   1.00 20.84  ? 430 HOH A O   1 
HETATM 2281 O  O   . HOH J 6 .   ? 1.080   -1.550  -4.994  1.00 26.81  ? 431 HOH A O   1 
HETATM 2282 O  O   . HOH J 6 .   ? -24.472 -7.696  8.952   1.00 15.05  ? 432 HOH A O   1 
HETATM 2283 O  O   . HOH J 6 .   ? -15.920 -9.809  32.803  1.00 18.91  ? 433 HOH A O   1 
HETATM 2284 O  O   . HOH J 6 .   ? -4.801  3.153   -6.175  1.00 20.88  ? 434 HOH A O   1 
HETATM 2285 O  O   . HOH J 6 .   ? -19.607 10.922  26.752  1.00 20.22  ? 435 HOH A O   1 
HETATM 2286 O  O   . HOH J 6 .   ? 13.845  0.574   24.465  1.00 16.72  ? 436 HOH A O   1 
HETATM 2287 O  O   . HOH J 6 .   ? -13.809 -16.495 28.864  1.00 31.73  ? 437 HOH A O   1 
HETATM 2288 O  O   . HOH J 6 .   ? -0.613  -11.180 28.831  1.00 23.00  ? 438 HOH A O   1 
HETATM 2289 O  O   . HOH J 6 .   ? -15.399 16.013  23.472  1.00 20.99  ? 439 HOH A O   1 
HETATM 2290 O  O   . HOH J 6 .   ? -22.431 -5.881  2.554   1.00 17.72  ? 440 HOH A O   1 
HETATM 2291 O  O   . HOH J 6 .   ? -23.437 8.851   20.107  1.00 18.93  ? 441 HOH A O   1 
HETATM 2292 O  O   . HOH J 6 .   ? 3.578   -15.070 2.947   1.00 34.01  ? 442 HOH A O   1 
HETATM 2293 O  O   . HOH J 6 .   ? -13.037 10.448  27.773  1.00 21.03  ? 443 HOH A O   1 
HETATM 2294 O  O   . HOH J 6 .   ? -9.823  8.680   25.406  1.00 14.06  ? 444 HOH A O   1 
HETATM 2295 O  O   . HOH J 6 .   ? -13.111 14.265  27.202  1.00 26.12  ? 445 HOH A O   1 
HETATM 2296 O  O   . HOH J 6 .   ? -13.653 -8.891  -5.372  1.00 14.83  ? 446 HOH A O   1 
HETATM 2297 O  O   . HOH J 6 .   ? -10.924 10.226  7.993   1.00 20.51  ? 447 HOH A O   1 
HETATM 2298 O  O   . HOH J 6 .   ? -25.400 7.994   6.245   1.00 26.18  ? 448 HOH A O   1 
HETATM 2299 O  O   . HOH J 6 .   ? -22.875 -13.306 11.279  1.00 21.67  ? 449 HOH A O   1 
HETATM 2300 O  O   . HOH J 6 .   ? -18.880 -12.259 -3.478  1.00 16.42  ? 450 HOH A O   1 
HETATM 2301 O  O   . HOH J 6 .   ? -25.370 6.461   26.913  1.00 24.57  ? 451 HOH A O   1 
HETATM 2302 O  O   . HOH J 6 .   ? -0.033  -8.550  32.433  1.00 23.98  ? 452 HOH A O   1 
HETATM 2303 O  O   . HOH J 6 .   ? 0.262   -14.344 22.042  1.00 22.55  ? 453 HOH A O   1 
HETATM 2304 O  O   . HOH J 6 .   ? -21.540 -18.432 13.526  1.00 23.95  ? 454 HOH A O   1 
HETATM 2305 O  O   . HOH J 6 .   ? -1.491  -17.524 25.358  1.00 30.11  ? 455 HOH A O   1 
HETATM 2306 O  O   . HOH J 6 .   ? -12.426 -9.019  -3.365  1.00 15.62  ? 456 HOH A O   1 
HETATM 2307 O  O   . HOH J 6 .   ? -26.091 -3.770  25.245  1.00 19.68  ? 457 HOH A O   1 
HETATM 2308 O  O   . HOH J 6 .   ? -18.940 -20.717 4.773   1.00 19.92  ? 458 HOH A O   1 
HETATM 2309 O  O   . HOH J 6 .   ? -18.389 -4.249  -2.783  1.00 23.07  ? 459 HOH A O   1 
HETATM 2310 O  O   . HOH J 6 .   ? -8.591  -5.822  35.817  1.00 20.06  ? 460 HOH A O   1 
HETATM 2311 O  O   . HOH J 6 .   ? -11.418 2.907   30.571  1.00 25.43  ? 461 HOH A O   1 
HETATM 2312 O  O   . HOH J 6 .   ? -17.896 4.111   -3.836  1.00 29.45  ? 462 HOH A O   1 
HETATM 2313 O  O   . HOH J 6 .   ? -1.049  -4.964  -7.297  1.00 30.77  ? 463 HOH A O   1 
HETATM 2314 O  O   . HOH J 6 .   ? 4.896   -3.524  26.320  1.00 21.65  ? 464 HOH A O   1 
HETATM 2315 O  O   . HOH J 6 .   ? -24.502 -9.350  1.893   1.00 19.62  ? 465 HOH A O   1 
HETATM 2316 O  O   . HOH J 6 .   ? -7.907  0.486   -6.695  1.00 24.26  ? 466 HOH A O   1 
HETATM 2317 O  O   . HOH J 6 .   ? 8.000   6.261   21.719  1.00 15.78  ? 467 HOH A O   1 
HETATM 2318 O  O   . HOH J 6 .   ? -12.260 -17.277 16.611  1.00 18.66  ? 468 HOH A O   1 
HETATM 2319 O  O   . HOH J 6 .   ? 14.923  0.242   14.798  1.00 24.81  ? 469 HOH A O   1 
HETATM 2320 O  O   . HOH J 6 .   ? 15.633  -1.019  25.912  1.00 18.80  ? 470 HOH A O   1 
HETATM 2321 O  O   . HOH J 6 .   ? -0.946  -13.170 27.044  1.00 26.24  ? 471 HOH A O   1 
HETATM 2322 O  O   . HOH J 6 .   ? 3.202   -13.230 5.100   1.00 19.72  ? 472 HOH A O   1 
HETATM 2323 O  O   . HOH J 6 .   ? -25.399 -6.267  12.665  1.00 22.98  ? 473 HOH A O   1 
HETATM 2324 O  O   . HOH J 6 .   ? -7.909  -22.168 10.445  1.00 22.16  ? 474 HOH A O   1 
HETATM 2325 O  O   . HOH J 6 .   ? 2.494   -15.621 9.176   1.00 19.91  ? 475 HOH A O   1 
HETATM 2326 O  O   . HOH J 6 .   ? -6.810  -16.778 1.110   1.00 20.97  ? 476 HOH A O   1 
HETATM 2327 O  O   . HOH J 6 .   ? 10.848  -10.836 16.037  1.00 18.85  ? 477 HOH A O   1 
HETATM 2328 O  O   . HOH J 6 .   ? -6.427  -8.668  -7.439  1.00 28.54  ? 478 HOH A O   1 
HETATM 2329 O  O   . HOH J 6 .   ? -20.570 -6.613  -2.358  1.00 27.92  ? 479 HOH A O   1 
HETATM 2330 O  O   . HOH J 6 .   ? -13.353 -15.949 -0.605  1.00 27.51  ? 480 HOH A O   1 
HETATM 2331 O  O   . HOH J 6 .   ? 5.196   -2.659  28.884  1.00 28.92  ? 481 HOH A O   1 
HETATM 2332 O  O   . HOH J 6 .   ? -22.602 -12.034 13.781  1.00 28.11  ? 482 HOH A O   1 
HETATM 2333 O  O   . HOH J 6 .   ? -26.278 10.124  4.755   1.00 22.66  ? 483 HOH A O   1 
HETATM 2334 O  O   . HOH J 6 .   ? -0.666  -12.567 -3.601  1.00 40.43  ? 484 HOH A O   1 
HETATM 2335 O  O   . HOH J 6 .   ? -12.176 7.866   28.703  1.00 21.88  ? 485 HOH A O   1 
HETATM 2336 O  O   . HOH J 6 .   ? -20.822 -19.548 6.428   1.00 20.95  ? 486 HOH A O   1 
HETATM 2337 O  O   . HOH J 6 .   ? 13.515  -5.697  24.431  1.00 28.22  ? 487 HOH A O   1 
HETATM 2338 O  O   . HOH J 6 .   ? 11.120  -9.169  8.888   1.00 27.66  ? 488 HOH A O   1 
HETATM 2339 O  O   . HOH J 6 .   ? -6.391  -15.010 31.411  1.00 25.65  ? 489 HOH A O   1 
HETATM 2340 O  O   . HOH J 6 .   ? -6.901  -8.711  32.446  1.00 17.40  ? 490 HOH A O   1 
HETATM 2341 O  O   . HOH J 6 .   ? 5.723   7.256   20.420  1.00 18.07  ? 491 HOH A O   1 
HETATM 2342 O  O   . HOH J 6 .   ? -15.584 -12.338 24.238  1.00 19.15  ? 492 HOH A O   1 
HETATM 2343 O  O   . HOH J 6 .   ? -16.743 -7.259  39.474  1.00 31.38  ? 493 HOH A O   1 
HETATM 2344 O  O   . HOH J 6 .   ? -0.028  10.617  23.047  1.00 24.32  ? 494 HOH A O   1 
HETATM 2345 O  O   . HOH J 6 .   ? 9.946   0.389   30.156  1.00 47.06  ? 495 HOH A O   1 
HETATM 2346 O  O   . HOH J 6 .   ? 1.873   -11.826 24.784  1.00 25.92  ? 496 HOH A O   1 
HETATM 2347 O  O   . HOH J 6 .   ? -12.120 12.980  31.604  1.00 33.05  ? 497 HOH A O   1 
HETATM 2348 O  O   . HOH J 6 .   ? -12.786 -0.764  -6.062  1.00 22.16  ? 498 HOH A O   1 
HETATM 2349 O  O   . HOH J 6 .   ? 11.696  1.584   25.967  1.00 21.17  ? 499 HOH A O   1 
HETATM 2350 O  O   . HOH J 6 .   ? -23.435 -0.458  26.440  1.00 19.05  ? 500 HOH A O   1 
HETATM 2351 O  O   . HOH J 6 .   ? 10.791  -2.428  13.308  1.00 25.13  ? 501 HOH A O   1 
HETATM 2352 O  O   . HOH J 6 .   ? -23.640 -7.341  0.097   1.00 40.79  ? 502 HOH A O   1 
HETATM 2353 O  O   . HOH J 6 .   ? -4.767  -13.370 34.256  1.00 45.27  ? 503 HOH A O   1 
HETATM 2354 O  O   . HOH J 6 .   ? -26.811 -7.372  25.909  1.00 30.34  ? 504 HOH A O   1 
HETATM 2355 O  O   . HOH J 6 .   ? 14.995  3.028   23.571  1.00 21.95  ? 505 HOH A O   1 
HETATM 2356 O  O   . HOH J 6 .   ? -24.690 9.848   13.064  1.00 29.85  ? 506 HOH A O   1 
HETATM 2357 O  O   . HOH J 6 .   ? -17.334 -21.967 5.823   1.00 12.70  ? 507 HOH A O   1 
HETATM 2358 O  O   . HOH J 6 .   ? 2.562   -14.261 20.405  1.00 34.13  ? 508 HOH A O   1 
HETATM 2359 O  O   . HOH J 6 .   ? 3.387   -4.437  7.587   1.00 26.54  ? 509 HOH A O   1 
HETATM 2360 O  O   . HOH J 6 .   ? 4.908   -6.931  7.775   1.00 28.14  ? 510 HOH A O   1 
HETATM 2361 O  O   . HOH J 6 .   ? 14.491  5.264   25.230  1.00 27.93  ? 511 HOH A O   1 
HETATM 2362 O  O   . HOH J 6 .   ? 2.139   8.588   24.104  1.00 26.73  ? 512 HOH A O   1 
HETATM 2363 O  O   . HOH J 6 .   ? -3.643  -8.561  31.010  1.00 23.38  ? 513 HOH A O   1 
HETATM 2364 O  O   . HOH J 6 .   ? -4.207  -12.045 31.926  1.00 24.91  ? 514 HOH A O   1 
HETATM 2365 O  O   . HOH J 6 .   ? -8.068  -15.372 32.952  1.00 27.54  ? 515 HOH A O   1 
HETATM 2366 O  O   . HOH J 6 .   ? -14.990 -10.198 37.364  1.00 22.13  ? 516 HOH A O   1 
HETATM 2367 O  O   . HOH J 6 .   ? -25.824 3.503   15.405  1.00 45.02  ? 517 HOH A O   1 
HETATM 2368 O  O   . HOH J 6 .   ? -15.319 9.004   -2.225  1.00 24.37  ? 518 HOH A O   1 
HETATM 2369 O  O   . HOH J 6 .   ? -1.851  -3.211  11.178  1.00 19.54  ? 519 HOH A O   1 
HETATM 2370 O  O   . HOH J 6 .   ? -5.968  6.490   10.034  1.00 20.66  ? 520 HOH A O   1 
HETATM 2371 O  O   . HOH J 6 .   ? 10.577  5.944   13.069  1.00 44.71  ? 521 HOH A O   1 
HETATM 2372 O  O   . HOH J 6 .   ? -2.215  4.612   7.073   1.00 27.42  ? 522 HOH A O   1 
HETATM 2373 O  O   . HOH J 6 .   ? 14.505  -12.253 16.116  1.00 35.10  ? 523 HOH A O   1 
HETATM 2374 O  O   . HOH J 6 .   ? 15.291  -10.381 14.471  1.00 27.73  ? 524 HOH A O   1 
HETATM 2375 O  O   . HOH J 6 .   ? 18.907  -11.145 17.061  1.00 28.65  ? 525 HOH A O   1 
HETATM 2376 O  O   . HOH J 6 .   ? 11.813  -6.849  22.372  1.00 31.09  ? 526 HOH A O   1 
HETATM 2377 O  O   . HOH J 6 .   ? 9.190   -4.670  23.571  1.00 26.82  ? 527 HOH A O   1 
HETATM 2378 O  O   . HOH J 6 .   ? 12.121  -0.210  15.742  1.00 25.60  ? 528 HOH A O   1 
HETATM 2379 O  O   . HOH J 6 .   ? 4.517   8.734   22.598  1.00 30.37  ? 529 HOH A O   1 
HETATM 2380 O  O   . HOH J 6 .   ? 2.414   11.148  17.187  1.00 30.91  ? 530 HOH A O   1 
HETATM 2381 O  O   . HOH J 6 .   ? 8.770   3.412   27.841  1.00 37.54  ? 531 HOH A O   1 
HETATM 2382 O  O   . HOH J 6 .   ? 12.243  0.625   28.616  1.00 30.19  ? 532 HOH A O   1 
HETATM 2383 O  O   . HOH J 6 .   ? -0.168  9.498   27.403  1.00 29.13  ? 533 HOH A O   1 
HETATM 2384 O  O   . HOH J 6 .   ? 2.686   7.977   27.616  1.00 24.42  ? 534 HOH A O   1 
HETATM 2385 O  O   . HOH J 6 .   ? -5.015  -7.966  40.099  1.00 25.66  ? 535 HOH A O   1 
HETATM 2386 O  O   . HOH J 6 .   ? -18.097 -9.037  34.462  1.00 28.55  ? 536 HOH A O   1 
HETATM 2387 O  O   . HOH J 6 .   ? -16.193 -14.530 32.972  1.00 39.17  ? 537 HOH A O   1 
HETATM 2388 O  O   . HOH J 6 .   ? -19.188 -4.217  41.184  1.00 33.24  ? 538 HOH A O   1 
HETATM 2389 O  O   . HOH J 6 .   ? -22.718 -0.632  34.142  1.00 36.79  ? 539 HOH A O   1 
HETATM 2390 O  O   . HOH J 6 .   ? -23.553 -3.045  29.130  1.00 37.09  ? 540 HOH A O   1 
HETATM 2391 O  O   . HOH J 6 .   ? -27.448 -1.313  28.470  1.00 36.55  ? 541 HOH A O   1 
HETATM 2392 O  O   . HOH J 6 .   ? -25.281 12.266  13.575  1.00 35.44  ? 542 HOH A O   1 
HETATM 2393 O  O   . HOH J 6 .   ? -7.819  6.441   0.227   1.00 18.15  ? 543 HOH A O   1 
HETATM 2394 O  O   . HOH J 6 .   ? -8.268  12.076  -0.096  1.00 26.93  ? 544 HOH A O   1 
HETATM 2395 O  O   . HOH J 6 .   ? -17.064 17.652  3.892   1.00 29.49  ? 545 HOH A O   1 
HETATM 2396 O  O   . HOH J 6 .   ? -13.695 19.798  2.965   1.00 42.31  ? 546 HOH A O   1 
HETATM 2397 O  O   . HOH J 6 .   ? -10.318 12.977  8.068   1.00 24.19  ? 547 HOH A O   1 
HETATM 2398 O  O   . HOH J 6 .   ? -10.181 17.322  11.745  1.00 23.74  ? 548 HOH A O   1 
HETATM 2399 O  O   . HOH J 6 .   ? -18.724 11.987  12.953  1.00 40.74  ? 549 HOH A O   1 
HETATM 2400 O  O   . HOH J 6 .   ? -17.231 19.875  17.421  1.00 26.43  ? 550 HOH A O   1 
HETATM 2401 O  O   . HOH J 6 .   ? -14.492 20.121  17.557  1.00 27.87  ? 551 HOH A O   1 
HETATM 2402 O  O   . HOH J 6 .   ? -14.144 22.561  18.583  1.00 25.73  ? 552 HOH A O   1 
HETATM 2403 O  O   . HOH J 6 .   ? -24.472 11.395  19.684  1.00 34.99  ? 553 HOH A O   1 
HETATM 2404 O  O   . HOH J 6 .   ? -15.591 17.902  25.411  1.00 33.36  ? 554 HOH A O   1 
HETATM 2405 O  O   . HOH J 6 .   ? -8.108  8.136   9.385   1.00 24.37  ? 555 HOH A O   1 
HETATM 2406 O  O   . HOH J 6 .   ? -2.457  -17.524 5.229   1.00 24.91  ? 556 HOH A O   1 
HETATM 2407 O  O   . HOH J 6 .   ? 0.457   -17.663 5.552   1.00 29.39  ? 557 HOH A O   1 
HETATM 2408 O  O   . HOH J 6 .   ? 2.131   -17.659 7.339   1.00 26.80  ? 558 HOH A O   1 
HETATM 2409 O  O   . HOH J 6 .   ? -9.919  -18.332 16.832  1.00 20.20  ? 559 HOH A O   1 
HETATM 2410 O  O   . HOH J 6 .   ? -0.629  -17.657 17.909  1.00 30.28  ? 560 HOH A O   1 
HETATM 2411 O  O   . HOH J 6 .   ? -16.462 -14.084 26.193  1.00 32.45  ? 561 HOH A O   1 
HETATM 2412 O  O   . HOH J 6 .   ? -12.193 -19.582 26.209  1.00 30.33  ? 562 HOH A O   1 
HETATM 2413 O  O   . HOH J 6 .   ? -8.630  5.781   29.060  1.00 30.09  ? 563 HOH A O   1 
HETATM 2414 O  O   . HOH J 6 .   ? -16.689 -16.232 21.959  1.00 30.53  ? 564 HOH A O   1 
HETATM 2415 O  O   . HOH J 6 .   ? -16.307 -18.099 20.116  1.00 33.98  ? 565 HOH A O   1 
HETATM 2416 O  O   . HOH J 6 .   ? -12.909 -18.578 14.458  1.00 22.29  ? 566 HOH A O   1 
HETATM 2417 O  O   . HOH J 6 .   ? -19.788 -16.744 3.018   1.00 23.69  ? 567 HOH A O   1 
HETATM 2418 O  O   . HOH J 6 .   ? -15.878 -6.746  -6.621  1.00 20.60  ? 568 HOH A O   1 
HETATM 2419 O  O   . HOH J 6 .   ? -13.693 -5.391  -6.861  1.00 28.44  ? 569 HOH A O   1 
HETATM 2420 O  O   . HOH J 6 .   ? -5.486  -4.730  -6.633  1.00 18.82  ? 570 HOH A O   1 
HETATM 2421 O  O   . HOH J 6 .   ? -3.470  -5.842  -8.163  1.00 26.96  ? 571 HOH A O   1 
HETATM 2422 O  O   . HOH J 6 .   ? -12.229 -10.943 -6.208  1.00 32.36  ? 572 HOH A O   1 
HETATM 2423 O  O   . HOH J 6 .   ? -10.915 -11.393 -3.288  1.00 32.66  ? 573 HOH A O   1 
HETATM 2424 O  O   . HOH J 6 .   ? 1.990   -9.296  -5.134  1.00 33.31  ? 574 HOH A O   1 
HETATM 2425 O  O   . HOH J 6 .   ? -3.388  -12.945 -3.260  1.00 29.45  ? 575 HOH A O   1 
HETATM 2426 O  O   . HOH J 6 .   ? -3.433  -15.606 -2.274  1.00 30.43  ? 576 HOH A O   1 
HETATM 2427 O  O   . HOH J 6 .   ? -4.079  -15.913 0.584   1.00 31.93  ? 577 HOH A O   1 
HETATM 2428 O  O   . HOH J 6 .   ? -12.147 3.845   -7.084  1.00 38.42  ? 578 HOH A O   1 
HETATM 2429 O  O   . HOH J 6 .   ? -23.707 -0.087  1.109   1.00 36.37  ? 579 HOH A O   1 
HETATM 2430 O  O   . HOH J 6 .   ? -17.404 -12.131 31.462  1.00 42.84  ? 580 HOH A O   1 
HETATM 2431 O  O   . HOH J 6 .   ? -21.908 -12.618 24.508  1.00 43.61  ? 581 HOH A O   1 
HETATM 2432 O  O   . HOH J 6 .   ? -19.566 -15.537 22.305  1.00 30.37  ? 582 HOH A O   1 
HETATM 2433 O  O   . HOH J 6 .   ? -1.660  -11.811 31.305  1.00 37.10  ? 583 HOH A O   1 
HETATM 2434 O  O   . HOH J 6 .   ? -6.167  -5.555  37.124  1.00 24.75  ? 584 HOH A O   1 
HETATM 2435 O  O   . HOH J 6 .   ? -5.490  1.290   9.744   1.00 26.05  ? 585 HOH A O   1 
HETATM 2436 O  O   . HOH J 6 .   ? -3.960  8.298   10.165  1.00 33.61  ? 586 HOH A O   1 
HETATM 2437 O  O   . HOH J 6 .   ? -1.256  7.706   10.648  1.00 47.91  ? 587 HOH A O   1 
HETATM 2438 O  O   . HOH J 6 .   ? 15.019  -6.818  7.584   1.00 33.84  ? 588 HOH A O   1 
HETATM 2439 O  O   . HOH J 6 .   ? 4.379   -11.905 23.162  1.00 51.76  ? 589 HOH A O   1 
HETATM 2440 O  O   . HOH J 6 .   ? 5.974   -7.100  22.408  1.00 35.71  ? 590 HOH A O   1 
HETATM 2441 O  O   . HOH J 6 .   ? -1.457  8.692   29.189  1.00 27.05  ? 591 HOH A O   1 
HETATM 2442 O  O   . HOH J 6 .   ? -14.483 -19.232 32.875  1.00 37.79  ? 592 HOH A O   1 
HETATM 2443 O  O   . HOH J 6 .   ? -12.326 -18.570 31.614  1.00 38.10  ? 593 HOH A O   1 
HETATM 2444 O  O   . HOH J 6 .   ? -10.279 -19.086 33.515  1.00 37.07  ? 594 HOH A O   1 
HETATM 2445 O  O   . HOH J 6 .   ? -6.544  -19.339 35.313  1.00 36.43  ? 595 HOH A O   1 
HETATM 2446 O  O   . HOH J 6 .   ? -11.500 -3.258  42.102  1.00 35.64  ? 596 HOH A O   1 
HETATM 2447 O  O   . HOH J 6 .   ? -19.863 8.631   29.849  1.00 31.02  ? 597 HOH A O   1 
HETATM 2448 O  O   . HOH J 6 .   ? -19.460 13.970  29.063  1.00 43.21  ? 598 HOH A O   1 
HETATM 2449 O  O   . HOH J 6 .   ? -14.486 11.007  34.845  1.00 42.38  ? 599 HOH A O   1 
HETATM 2450 O  O   . HOH J 6 .   ? -8.801  5.541   2.737   1.00 23.91  ? 600 HOH A O   1 
HETATM 2451 O  O   . HOH J 6 .   ? 2.983   2.073   -2.917  1.00 29.84  ? 601 HOH A O   1 
HETATM 2452 O  O   . HOH J 6 .   ? 6.294   0.983   -4.752  1.00 33.20  ? 602 HOH A O   1 
HETATM 2453 O  O   . HOH J 6 .   ? -12.043 12.966  6.281   1.00 33.55  ? 603 HOH A O   1 
HETATM 2454 O  O   . HOH J 6 .   ? -12.677 18.616  11.647  1.00 34.66  ? 604 HOH A O   1 
HETATM 2455 O  O   . HOH J 6 .   ? -20.893 19.824  17.187  1.00 33.59  ? 605 HOH A O   1 
HETATM 2456 O  O   . HOH J 6 .   ? 3.314   -13.419 7.877   1.00 35.60  ? 606 HOH A O   1 
HETATM 2457 O  O   . HOH J 6 .   ? 5.308   -10.025 7.892   1.00 55.53  ? 607 HOH A O   1 
HETATM 2458 O  O   . HOH J 6 .   ? 6.528   -15.625 6.611   1.00 46.82  ? 608 HOH A O   1 
HETATM 2459 O  O   . HOH J 6 .   ? -2.425  17.733  20.493  1.00 25.91  ? 609 HOH A O   1 
HETATM 2460 O  O   . HOH J 6 .   ? -7.245  7.214   27.339  1.00 25.97  ? 610 HOH A O   1 
HETATM 2461 O  O   . HOH J 6 .   ? -25.449 -14.947 8.335   1.00 35.26  ? 611 HOH A O   1 
HETATM 2462 O  O   . HOH J 6 .   ? -25.093 -10.654 17.235  1.00 50.30  ? 612 HOH A O   1 
HETATM 2463 O  O   . HOH J 6 .   ? -23.872 -10.348 14.954  1.00 32.24  ? 613 HOH A O   1 
HETATM 2464 O  O   . HOH J 6 .   ? -27.025 -10.612 22.404  1.00 29.85  ? 614 HOH A O   1 
HETATM 2465 O  O   . HOH J 6 .   ? 6.652   9.374   24.172  1.00 46.05  ? 615 HOH A O   1 
HETATM 2466 O  O   . HOH J 6 .   ? 11.394  -8.907  0.009   1.00 44.22  ? 616 HOH A O   1 
HETATM 2467 O  O   . HOH J 6 .   ? 1.817   -6.623  34.188  1.00 47.10  ? 617 HOH A O   1 
HETATM 2468 O  O   . HOH J 6 .   ? -3.248  -4.692  37.515  1.00 34.20  ? 618 HOH A O   1 
HETATM 2469 O  O   . HOH J 6 .   ? -9.130  12.977  10.078  1.00 25.77  ? 619 HOH A O   1 
HETATM 2470 O  O   . HOH J 6 .   ? 9.308   -12.741 8.654   1.00 43.61  ? 620 HOH A O   1 
HETATM 2471 O  O   . HOH J 6 .   ? -17.991 14.054  2.200   1.00 41.30  ? 621 HOH A O   1 
HETATM 2472 O  O   . HOH J 6 .   ? -0.823  11.236  25.588  1.00 29.05  ? 622 HOH A O   1 
HETATM 2473 O  O   . HOH J 6 .   ? -18.320 -20.838 14.839  1.00 77.72  ? 623 HOH A O   1 
HETATM 2474 O  O   . HOH J 6 .   ? -26.065 -6.141  4.950   1.00 36.00  ? 624 HOH A O   1 
HETATM 2475 O  O   . HOH J 6 .   ? -9.559  1.573   38.548  1.00 37.49  ? 625 HOH A O   1 
HETATM 2476 O  O   . HOH J 6 .   ? -5.569  -18.799 2.557   1.00 33.25  ? 626 HOH A O   1 
HETATM 2477 O  O   . HOH J 6 .   ? -4.001  -8.425  -8.884  1.00 48.25  ? 627 HOH A O   1 
HETATM 2478 O  O   . HOH J 6 .   ? -19.734 17.971  3.777   1.00 44.19  ? 628 HOH A O   1 
HETATM 2479 O  O   . HOH J 6 .   ? 8.799   7.781   24.068  1.00 54.79  ? 629 HOH A O   1 
HETATM 2480 O  O   . HOH J 6 .   ? 1.840   2.986   5.220   1.00 33.99  ? 630 HOH A O   1 
HETATM 2481 O  O   . HOH J 6 .   ? -8.151  -3.984  7.733   1.00 21.11  ? 631 HOH A O   1 
HETATM 2482 O  O   . HOH J 6 .   ? -13.663 16.387  28.832  1.00 56.00  ? 632 HOH A O   1 
HETATM 2483 O  O   . HOH J 6 .   ? -12.976 19.728  14.467  1.00 66.81  ? 633 HOH A O   1 
HETATM 2484 O  O   . HOH J 6 .   ? 0.109   -1.458  -9.358  1.00 31.27  ? 634 HOH A O   1 
HETATM 2485 O  O   . HOH J 6 .   ? 0.422   0.326   -7.168  1.00 48.46  ? 635 HOH A O   1 
HETATM 2486 O  O   . HOH J 6 .   ? 6.395   -0.579  -0.977  1.00 39.32  ? 636 HOH A O   1 
HETATM 2487 O  O   . HOH J 6 .   ? 8.529   -6.062  0.025   1.00 35.60  ? 637 HOH A O   1 
HETATM 2488 O  O   . HOH J 6 .   ? 3.478   -9.074  26.850  1.00 72.31  ? 638 HOH A O   1 
HETATM 2489 O  O   . HOH J 6 .   ? 0.422   1.075   34.404  1.00 29.93  ? 639 HOH A O   1 
HETATM 2490 O  O   . HOH J 6 .   ? -19.165 17.308  23.381  1.00 47.19  ? 640 HOH A O   1 
HETATM 2491 O  O   . HOH J 6 .   ? 0.373   -3.116  39.356  1.00 46.77  ? 641 HOH A O   1 
HETATM 2492 O  O   . HOH J 6 .   ? -24.475 8.702   26.468  1.00 40.99  ? 642 HOH A O   1 
HETATM 2493 O  O   . HOH J 6 .   ? -21.536 -18.265 3.888   1.00 50.61  ? 643 HOH A O   1 
HETATM 2494 O  O   . HOH J 6 .   ? -20.299 -16.213 20.247  1.00 49.79  ? 644 HOH A O   1 
HETATM 2495 O  O   . HOH J 6 .   ? -7.812  -15.163 36.778  1.00 40.12  ? 645 HOH A O   1 
HETATM 2496 O  O   . HOH J 6 .   ? 9.677   2.350   12.043  1.00 44.52  ? 646 HOH A O   1 
HETATM 2497 O  O   . HOH J 6 .   ? -5.554  -0.394  39.620  1.00 42.25  ? 647 HOH A O   1 
HETATM 2498 O  O   . HOH J 6 .   ? -21.525 -13.990 18.633  1.00 36.86  ? 648 HOH A O   1 
HETATM 2499 O  O   . HOH J 6 .   ? 13.482  -3.577  13.099  1.00 24.03  ? 649 HOH A O   1 
HETATM 2500 O  O   . HOH J 6 .   ? -14.362 -2.893  -6.941  1.00 36.92  ? 650 HOH A O   1 
HETATM 2501 O  O   . HOH J 6 .   ? 8.696   -0.249  5.652   1.00 43.59  ? 651 HOH A O   1 
HETATM 2502 O  O   . HOH J 6 .   ? 2.349   12.261  22.484  1.00 39.71  ? 652 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   ? 0.0719 0.2245 0.2725 0.0359  0.0119  0.1448  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.2985 0.3625 0.6140 0.0666  0.2291  0.0965  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.3197 0.4404 0.6032 0.1808  -0.0524 0.1842  4   HIS A C   
4    O  O   . HIS A 4   ? 0.1800 0.4235 0.4293 -0.0560 0.0126  0.0480  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.3030 0.2470 0.8306 0.0926  0.0627  0.1111  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.8373 0.4851 1.0288 -0.0819 -0.0908 0.0324  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 1.0678 0.4519 1.5805 0.0375  -0.4690 -0.0961 4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.9940 0.7024 1.3567 -0.2872 0.3858  -0.0238 4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.7631 1.2992 1.6879 -0.5835 -0.1049 0.2105  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 1.1993 1.1977 1.5477 -0.6837 -0.1844 -0.0450 4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.1263 0.5188 0.5723 0.0392  0.0776  0.2344  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1168 0.2608 0.4117 -0.0625 -0.0220 0.0718  5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1398 0.2714 0.2962 -0.0027 -0.0098 0.0082  5   TRP A C   
14   O  O   . TRP A 5   ? 0.1392 0.4165 0.3350 0.0182  -0.0126 0.0988  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1441 0.2980 0.3643 -0.0414 -0.0485 0.0728  5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1509 0.2369 0.3230 -0.0636 -0.0384 0.0816  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.1703 0.2540 0.3616 -0.0592 -0.0346 0.1048  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1194 0.2127 0.2691 0.0082  0.0041  0.0071  5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.1920 0.2477 0.3366 -0.0346 -0.0425 0.1128  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1714 0.1940 0.2700 -0.0129 -0.0507 0.0333  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1039 0.2759 0.2894 -0.0469 -0.0091 0.0120  5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1712 0.2337 0.2423 0.0230  -0.0454 0.0295  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1125 0.2675 0.2463 0.0031  -0.0142 -0.0147 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1212 0.2594 0.2554 -0.0017 -0.0516 0.0054  5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1238 0.2296 0.3086 0.0120  0.0006  -0.0102 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1252 0.2574 0.3278 0.0120  -0.0335 -0.0120 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.0617 0.2434 0.2569 0.0010  -0.0494 -0.0540 6   GLY A C   
28   O  O   . GLY A 6   ? 0.0929 0.1897 0.2619 0.0092  -0.0366 -0.0573 6   GLY A O   
29   N  N   . TYR A 7   ? 0.0944 0.2398 0.2648 -0.0038 -0.0263 -0.0869 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.0916 0.1962 0.3179 -0.0164 -0.0091 -0.0841 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.0856 0.2452 0.3531 0.0041  -0.0264 -0.0662 7   TYR A C   
32   O  O   . TYR A 7   ? 0.1474 0.2281 0.5425 -0.0098 0.0249  -0.0793 7   TYR A O   
33   C  CB  . TYR A 7   ? 0.0913 0.1768 0.3122 -0.0087 -0.0140 -0.0776 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.0688 0.1870 0.2448 -0.0183 -0.0359 -0.0680 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.0680 0.1629 0.2294 -0.0340 -0.0192 -0.0706 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.0863 0.2387 0.2581 -0.0350 -0.0649 -0.0379 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.0837 0.1395 0.2497 -0.0147 -0.0408 -0.0309 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.0992 0.1649 0.2490 -0.0392 -0.0229 0.0048  7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.0882 0.1215 0.2393 -0.0417 -0.0285 -0.0355 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1498 0.0966 0.2425 0.0126  -0.0568 -0.0206 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.0851 0.3264 0.3704 0.0370  -0.0087 -0.1158 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.1444 0.2617 0.4007 0.0153  -0.0041 -0.1001 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.1360 0.3382 0.3576 0.0810  0.0520  -0.0829 8   GLY A C   
44   O  O   . GLY A 8   ? 0.1009 0.2698 0.3592 -0.0038 0.0272  -0.0749 8   GLY A O   
45   N  N   . LYS A 9   ? 0.1177 0.1965 0.4217 0.0043  0.0271  -0.0776 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.1437 0.1802 0.4758 -0.0131 0.0142  -0.0076 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.1061 0.1953 0.3625 0.0317  -0.0087 -0.0417 9   LYS A C   
48   O  O   . LYS A 9   ? 0.1351 0.1811 0.3722 -0.0019 0.0041  0.0017  9   LYS A O   
49   C  CB  . LYS A 9   ? 0.1680 0.2003 0.6478 0.0060  -0.0520 -0.0891 9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.2450 0.2587 0.6480 0.0627  -0.0542 -0.0294 9   LYS A CG  
51   C  CD  . LYS A 9   ? 0.3307 0.2409 0.9868 -0.0062 0.0900  -0.1203 9   LYS A CD  
52   C  CE  . LYS A 9   ? 0.4629 0.2757 0.9725 0.1323  0.2203  0.2360  9   LYS A CE  
53   N  NZ  . LYS A 9   ? 0.4862 0.4990 1.2647 0.3005  0.1930  0.1106  9   LYS A NZ  
54   N  N   . HIS A 10  ? 0.1392 0.2168 0.3754 0.0236  0.0214  -0.0136 10  HIS A N   
55   C  CA  . HIS A 10  ? 0.1651 0.1572 0.3345 0.0260  0.0631  -0.0049 10  HIS A CA  
56   C  C   . HIS A 10  ? 0.1159 0.1741 0.3291 0.0329  0.0102  -0.0472 10  HIS A C   
57   O  O   . HIS A 10  ? 0.1048 0.1685 0.3657 0.0329  -0.0115 -0.0054 10  HIS A O   
58   C  CB  . HIS A 10  ? 0.1414 0.2091 0.2928 0.0590  0.0320  -0.0063 10  HIS A CB  
59   C  CG  . HIS A 10  ? 0.1057 0.1694 0.3233 0.0136  -0.0054 0.0060  10  HIS A CG  
60   N  ND1 . HIS A 10  ? 0.1237 0.1865 0.3882 0.0333  0.0080  0.0375  10  HIS A ND1 
61   C  CD2 . HIS A 10  ? 0.1387 0.1800 0.3104 -0.0074 0.0340  0.0060  10  HIS A CD2 
62   C  CE1 . HIS A 10  ? 0.2836 0.1468 0.3413 0.0307  -0.0417 0.0537  10  HIS A CE1 
63   N  NE2 . HIS A 10  ? 0.1516 0.2030 0.3718 0.0416  0.0285  -0.0186 10  HIS A NE2 
64   N  N   . ASN A 11  ? 0.1199 0.1814 0.3097 0.0434  0.0186  -0.0286 11  ASN A N   
65   C  CA  . ASN A 11  ? 0.1111 0.1559 0.3009 0.0137  0.0152  -0.0197 11  ASN A CA  
66   C  C   . ASN A 11  ? 0.0895 0.1879 0.2382 0.0043  -0.0120 -0.0263 11  ASN A C   
67   O  O   . ASN A 11  ? 0.1001 0.1633 0.2953 -0.0087 -0.0049 -0.0104 11  ASN A O   
68   C  CB  . ASN A 11  ? 0.0926 0.2202 0.3219 0.0153  0.0043  0.0031  11  ASN A CB  
69   C  CG  . ASN A 11  ? 0.1489 0.2644 0.2184 0.0483  0.0048  -0.0174 11  ASN A CG  
70   O  OD1 . ASN A 11  ? 0.1917 0.2734 0.3601 0.0153  -0.0107 -0.0265 11  ASN A OD1 
71   N  ND2 . ASN A 11  ? 0.2524 0.2768 0.2903 0.0068  -0.0087 0.0559  11  ASN A ND2 
72   N  N   . GLY A 12  ? 0.0724 0.1870 0.2578 -0.0096 -0.0038 -0.0192 12  GLY A N   
73   C  CA  . GLY A 12  ? 0.0812 0.1710 0.2709 0.0068  -0.0074 -0.0428 12  GLY A CA  
74   C  C   . GLY A 12  ? 0.0781 0.0935 0.2714 0.0087  -0.0185 -0.0120 12  GLY A C   
75   O  O   . GLY A 12  ? 0.0842 0.0987 0.2694 -0.0114 -0.0281 -0.0063 12  GLY A O   
76   N  N   . PRO A 13  ? 0.0728 0.1358 0.2448 -0.0051 -0.0297 -0.0346 13  PRO A N   
77   C  CA  . PRO A 13  ? 0.0640 0.1000 0.2533 -0.0098 -0.0320 -0.0249 13  PRO A CA  
78   C  C   . PRO A 13  ? 0.0697 0.1152 0.2348 -0.0031 -0.0183 0.0013  13  PRO A C   
79   O  O   . PRO A 13  ? 0.0719 0.1523 0.2335 -0.0076 -0.0205 -0.0214 13  PRO A O   
80   C  CB  . PRO A 13  ? 0.0630 0.0877 0.2813 -0.0153 -0.0434 0.0054  13  PRO A CB  
81   C  CG  . PRO A 13  ? 0.0904 0.1527 0.2515 -0.0364 -0.0120 -0.0227 13  PRO A CG  
82   C  CD  . PRO A 13  ? 0.0441 0.1777 0.2657 -0.0221 -0.0115 -0.0412 13  PRO A CD  
83   N  N   . GLU A 14  ? 0.0790 0.1270 0.2469 0.0057  -0.0209 0.0126  14  GLU A N   
84   C  CA  . GLU A 14  ? 0.1057 0.1073 0.2628 -0.0071 -0.0631 0.0229  14  GLU A CA  
85   C  C   . GLU A 14  ? 0.1019 0.1057 0.2655 0.0226  -0.0353 0.0006  14  GLU A C   
86   O  O   . GLU A 14  ? 0.1161 0.1286 0.2644 0.0241  -0.0498 -0.0020 14  GLU A O   
87   C  CB  . GLU A 14  ? 0.1389 0.1120 0.3885 -0.0109 -0.0834 0.0494  14  GLU A CB  
88   C  CG  . GLU A 14  ? 0.2856 0.1045 0.3944 -0.0529 -0.0612 0.0294  14  GLU A CG  
89   C  CD  . GLU A 14  ? 0.6618 0.2529 0.3815 -0.1348 -0.0219 0.0502  14  GLU A CD  
90   O  OE1 . GLU A 14  ? 0.6452 0.4241 0.3537 -0.1597 0.0020  0.0166  14  GLU A OE1 
91   O  OE2 . GLU A 14  ? 0.7828 0.8057 0.4896 -0.4672 0.1580  -0.1186 14  GLU A OE2 
92   N  N   . HIS A 15  ? 0.0772 0.0825 0.2469 -0.0013 -0.0192 -0.0073 15  HIS A N   
93   C  CA  . HIS A 15  ? 0.0991 0.0825 0.2275 -0.0015 -0.0362 0.0104  15  HIS A CA  
94   C  C   . HIS A 15  ? 0.0538 0.1116 0.2312 0.0013  -0.0240 0.0207  15  HIS A C   
95   O  O   . HIS A 15  ? 0.0578 0.1071 0.2673 0.0019  -0.0208 -0.0048 15  HIS A O   
96   C  CB  . HIS A 15  ? 0.0834 0.1055 0.2398 0.0162  -0.0500 0.0159  15  HIS A CB  
97   C  CG  . HIS A 15  ? 0.0759 0.1396 0.2901 0.0359  -0.0109 -0.0041 15  HIS A CG  
98   N  ND1 . HIS A 15  ? 0.0820 0.1328 0.2795 0.0137  -0.0148 -0.0019 15  HIS A ND1 
99   C  CD2 . HIS A 15  ? 0.1565 0.1265 0.2637 0.0562  -0.0091 -0.0322 15  HIS A CD2 
100  C  CE1 . HIS A 15  ? 0.1396 0.1556 0.3271 0.0436  -0.0447 -0.0342 15  HIS A CE1 
101  N  NE2 . HIS A 15  ? 0.1212 0.1107 0.3689 0.0425  -0.0491 -0.0285 15  HIS A NE2 
102  N  N   . TRP A 16  ? 0.0517 0.1152 0.2527 0.0060  -0.0308 -0.0147 16  TRP A N   
103  C  CA  . TRP A 16  ? 0.0398 0.1177 0.2265 0.0119  -0.0520 -0.0087 16  TRP A CA  
104  C  C   . TRP A 16  ? 0.0344 0.1249 0.2226 -0.0225 -0.0164 -0.0006 16  TRP A C   
105  O  O   . TRP A 16  ? 0.0626 0.1120 0.2576 -0.0208 -0.0549 0.0120  16  TRP A O   
106  C  CB  . TRP A 16  ? 0.0402 0.1306 0.2172 -0.0210 -0.0397 0.0006  16  TRP A CB  
107  C  CG  . TRP A 16  ? 0.0577 0.0855 0.2168 0.0076  -0.0410 -0.0003 16  TRP A CG  
108  C  CD1 . TRP A 16  ? 0.0661 0.1010 0.2242 0.0082  -0.0313 -0.0124 16  TRP A CD1 
109  C  CD2 . TRP A 16  ? 0.0538 0.0908 0.2037 0.0155  -0.0307 0.0071  16  TRP A CD2 
110  N  NE1 . TRP A 16  ? 0.0568 0.1120 0.2337 0.0109  -0.0357 -0.0175 16  TRP A NE1 
111  C  CE2 . TRP A 16  ? 0.0705 0.1342 0.1976 0.0229  -0.0229 0.0098  16  TRP A CE2 
112  C  CE3 . TRP A 16  ? 0.0465 0.0948 0.2220 0.0192  -0.0208 0.0087  16  TRP A CE3 
113  C  CZ2 . TRP A 16  ? 0.0732 0.0829 0.2276 0.0087  -0.0305 0.0071  16  TRP A CZ2 
114  C  CZ3 . TRP A 16  ? 0.0737 0.1177 0.2213 0.0057  -0.0467 0.0207  16  TRP A CZ3 
115  C  CH2 . TRP A 16  ? 0.0724 0.1127 0.2190 0.0172  -0.0296 0.0080  16  TRP A CH2 
116  N  N   . HIS A 17  ? 0.0546 0.1055 0.2294 0.0076  -0.0346 0.0087  17  HIS A N   
117  C  CA  . HIS A 17  ? 0.0696 0.1412 0.2526 -0.0340 -0.0538 0.0124  17  HIS A CA  
118  C  C   . HIS A 17  ? 0.0414 0.1154 0.2608 0.0054  -0.0273 -0.0087 17  HIS A C   
119  O  O   . HIS A 17  ? 0.0741 0.1229 0.2538 -0.0142 -0.0329 -0.0197 17  HIS A O   
120  C  CB  . HIS A 17  ? 0.0458 0.1720 0.2448 0.0148  -0.0076 -0.0080 17  HIS A CB  
121  C  CG  . HIS A 17  ? 0.0553 0.1439 0.2486 0.0027  -0.0359 0.0035  17  HIS A CG  
122  N  ND1 . HIS A 17  ? 0.0534 0.2030 0.2718 -0.0098 -0.0381 0.0135  17  HIS A ND1 
123  C  CD2 . HIS A 17  ? 0.0732 0.1484 0.2520 0.0192  -0.0548 -0.0054 17  HIS A CD2 
124  C  CE1 . HIS A 17  ? 0.0379 0.2520 0.2409 0.0219  -0.0307 0.0263  17  HIS A CE1 
125  N  NE2 . HIS A 17  ? 0.0680 0.2012 0.2608 0.0186  -0.0408 0.0183  17  HIS A NE2 
126  N  N   . LYS A 18  ? 0.0553 0.1010 0.2527 0.0031  -0.0164 -0.0082 18  LYS A N   
127  C  CA  . LYS A 18  ? 0.0414 0.1475 0.2811 0.0070  -0.0218 0.0054  18  LYS A CA  
128  C  C   . LYS A 18  ? 0.0636 0.1161 0.2919 -0.0188 -0.0303 0.0205  18  LYS A C   
129  O  O   . LYS A 18  ? 0.1425 0.1805 0.4404 -0.0966 -0.0983 0.0834  18  LYS A O   
130  C  CB  . LYS A 18  ? 0.0754 0.1308 0.2578 0.0065  -0.0086 0.0140  18  LYS A CB  
131  C  CG  . LYS A 18  ? 0.0996 0.1326 0.2883 0.0449  -0.0357 0.0199  18  LYS A CG  
132  C  CD  . LYS A 18  ? 0.0766 0.1635 0.2712 0.0060  -0.0175 0.0098  18  LYS A CD  
133  C  CE  . LYS A 18  ? 0.0750 0.1231 0.2897 0.0164  -0.0186 0.0057  18  LYS A CE  
134  N  NZ  . LYS A 18  ? 0.0697 0.1349 0.2698 0.0258  -0.0135 0.0317  18  LYS A NZ  
135  N  N   . ASP A 19  ? 0.0648 0.1543 0.2777 0.0205  -0.0317 0.0074  19  ASP A N   
136  C  CA  . ASP A 19  ? 0.0969 0.1401 0.2743 0.0006  -0.0041 0.0065  19  ASP A CA  
137  C  C   . ASP A 19  ? 0.0767 0.1075 0.3271 -0.0003 -0.0131 -0.0074 19  ASP A C   
138  O  O   . ASP A 19  ? 0.1036 0.1206 0.3167 -0.0086 -0.0024 0.0131  19  ASP A O   
139  C  CB  . ASP A 19  ? 0.1818 0.2082 0.2402 0.0727  -0.0093 0.0226  19  ASP A CB  
140  C  CG  . ASP A 19  ? 0.1404 0.2648 0.4684 0.0197  0.0570  -0.1282 19  ASP A CG  
141  O  OD1 . ASP A 19  ? 0.2560 0.2836 0.3583 -0.0205 0.0617  0.0294  19  ASP A OD1 
142  O  OD2 . ASP A 19  ? 0.2944 0.5798 0.5184 -0.1004 0.0428  -0.3007 19  ASP A OD2 
143  N  N   . PHE A 20  ? 0.0741 0.1202 0.2569 -0.0141 -0.0054 -0.0015 20  PHE A N   
144  C  CA  . PHE A 20  ? 0.0722 0.1403 0.2461 -0.0006 -0.0102 -0.0271 20  PHE A CA  
145  C  C   . PHE A 20  ? 0.1003 0.0706 0.2488 0.0035  -0.0087 -0.0272 20  PHE A C   
146  O  O   . PHE A 20  ? 0.0983 0.0846 0.2664 -0.0109 -0.0153 -0.0102 20  PHE A O   
147  C  CB  . PHE A 20  ? 0.0873 0.1671 0.2797 -0.0364 -0.0346 0.0197  20  PHE A CB  
148  C  CG  . PHE A 20  ? 0.0907 0.2402 0.3102 -0.0375 -0.0383 0.0658  20  PHE A CG  
149  C  CD1 . PHE A 20  ? 0.0917 0.3072 0.3856 -0.0115 -0.0185 0.1237  20  PHE A CD1 
150  C  CD2 . PHE A 20  ? 0.0781 0.3731 0.2691 -0.0531 -0.0487 0.0588  20  PHE A CD2 
151  C  CE1 . PHE A 20  ? 0.1649 0.4650 0.3995 -0.1039 -0.0129 0.1728  20  PHE A CE1 
152  C  CE2 . PHE A 20  ? 0.1376 0.4289 0.2800 -0.0996 -0.0564 0.0996  20  PHE A CE2 
153  C  CZ  . PHE A 20  ? 0.1055 0.4697 0.3280 -0.0661 -0.0683 0.1957  20  PHE A CZ  
154  N  N   . PRO A 21  ? 0.1003 0.1204 0.2526 -0.0271 -0.0318 -0.0175 21  PRO A N   
155  C  CA  . PRO A 21  ? 0.0582 0.1583 0.2782 -0.0137 -0.0263 -0.0043 21  PRO A CA  
156  C  C   . PRO A 21  ? 0.0590 0.1559 0.2310 -0.0183 -0.0373 -0.0208 21  PRO A C   
157  O  O   . PRO A 21  ? 0.0706 0.1929 0.2508 -0.0320 -0.0461 -0.0093 21  PRO A O   
158  C  CB  . PRO A 21  ? 0.0913 0.2547 0.3000 -0.0636 -0.0745 0.0151  21  PRO A CB  
159  C  CG  . PRO A 21  ? 0.2187 0.2148 0.3673 -0.1322 -0.0930 0.0693  21  PRO A CG  
160  C  CD  . PRO A 21  ? 0.1073 0.1398 0.3122 -0.0511 -0.0220 0.0031  21  PRO A CD  
161  N  N   A ILE A 22  ? 0.0525 0.1233 0.2639 -0.0353 -0.0447 -0.0342 22  ILE A N   
162  N  N   B ILE A 22  ? 0.0740 0.1459 0.2490 0.0000  -0.0274 -0.0436 22  ILE A N   
163  C  CA  A ILE A 22  ? 0.0649 0.0920 0.2294 -0.0153 -0.0337 -0.0242 22  ILE A CA  
164  C  CA  B ILE A 22  ? 0.0904 0.1080 0.2263 0.0098  -0.0273 -0.0148 22  ILE A CA  
165  C  C   A ILE A 22  ? 0.0446 0.0873 0.1929 -0.0087 -0.0208 0.0097  22  ILE A C   
166  C  C   B ILE A 22  ? 0.1062 0.1071 0.2364 0.0174  -0.0315 -0.0161 22  ILE A C   
167  O  O   A ILE A 22  ? 0.0296 0.1013 0.1785 0.0050  -0.0237 0.0103  22  ILE A O   
168  O  O   B ILE A 22  ? 0.1265 0.1516 0.2545 -0.0068 -0.0274 -0.0163 22  ILE A O   
169  C  CB  A ILE A 22  ? 0.0965 0.1179 0.2026 -0.0120 -0.0291 0.0160  22  ILE A CB  
170  C  CB  B ILE A 22  ? 0.0582 0.1238 0.2105 -0.0052 -0.0214 0.0020  22  ILE A CB  
171  C  CG1 A ILE A 22  ? 0.0732 0.1064 0.1559 -0.0489 -0.0401 0.0458  22  ILE A CG1 
172  C  CG1 B ILE A 22  ? 0.1344 0.1073 0.1974 0.0535  0.0082  0.0296  22  ILE A CG1 
173  C  CG2 A ILE A 22  ? 0.0969 0.0824 0.1802 -0.0637 -0.0076 0.0114  22  ILE A CG2 
174  C  CG2 B ILE A 22  ? 0.1075 0.1215 0.1908 0.0051  -0.0248 -0.0131 22  ILE A CG2 
175  C  CD1 A ILE A 22  ? 0.1184 0.1852 0.3194 0.0610  -0.0381 -0.0175 22  ILE A CD1 
176  C  CD1 B ILE A 22  ? 0.1729 0.1331 0.2669 0.0092  0.0322  -0.0467 22  ILE A CD1 
177  N  N   . ALA A 23  ? 0.0615 0.1125 0.2281 -0.0071 -0.0250 -0.0284 23  ALA A N   
178  C  CA  . ALA A 23  ? 0.0684 0.1003 0.2511 -0.0031 -0.0368 -0.0166 23  ALA A CA  
179  C  C   . ALA A 23  ? 0.0439 0.1317 0.2445 0.0038  -0.0171 -0.0308 23  ALA A C   
180  O  O   . ALA A 23  ? 0.0878 0.1186 0.2869 -0.0142 -0.0153 -0.0118 23  ALA A O   
181  C  CB  . ALA A 23  ? 0.0551 0.0938 0.2813 -0.0041 -0.0320 -0.0359 23  ALA A CB  
182  N  N   . LYS A 24  ? 0.0847 0.1687 0.2524 0.0251  -0.0524 -0.0261 24  LYS A N   
183  C  CA  . LYS A 24  ? 0.0886 0.1931 0.2867 0.0460  -0.0126 0.0010  24  LYS A CA  
184  C  C   . LYS A 24  ? 0.1082 0.2055 0.2714 0.0087  -0.0057 -0.0059 24  LYS A C   
185  O  O   . LYS A 24  ? 0.1459 0.2416 0.2768 -0.0142 -0.0577 -0.0015 24  LYS A O   
186  C  CB  . LYS A 24  ? 0.0864 0.2906 0.2861 0.0555  -0.0500 -0.0142 24  LYS A CB  
187  C  CG  . LYS A 24  ? 0.1127 0.2560 0.3154 0.0869  0.0057  0.0296  24  LYS A CG  
188  C  CD  . LYS A 24  ? 0.1279 0.2998 0.4099 0.0458  -0.0076 -0.0141 24  LYS A CD  
189  C  CE  . LYS A 24  ? 0.1450 0.2375 0.4343 0.0467  0.0093  0.0250  24  LYS A CE  
190  N  NZ  . LYS A 24  ? 0.3738 0.2127 0.5802 0.0430  0.1067  -0.0175 24  LYS A NZ  
191  N  N   . GLY A 25  ? 0.0903 0.1624 0.3030 -0.0068 0.0024  -0.0208 25  GLY A N   
192  C  CA  . GLY A 25  ? 0.1229 0.2222 0.2777 0.0093  0.0027  -0.0188 25  GLY A CA  
193  C  C   . GLY A 25  ? 0.1088 0.2010 0.2364 -0.0315 -0.0428 -0.0175 25  GLY A C   
194  O  O   . GLY A 25  ? 0.1120 0.2123 0.2310 -0.0166 -0.0309 -0.0263 25  GLY A O   
195  N  N   . GLU A 26  ? 0.0803 0.2669 0.2220 -0.0193 -0.0450 -0.0496 26  GLU A N   
196  C  CA  . GLU A 26  ? 0.1190 0.2673 0.2321 -0.0331 -0.0483 -0.0261 26  GLU A CA  
197  C  C   . GLU A 26  ? 0.1256 0.1620 0.1800 -0.0054 -0.0540 -0.0229 26  GLU A C   
198  O  O   . GLU A 26  ? 0.1611 0.1816 0.1847 0.0049  -0.0410 0.0065  26  GLU A O   
199  C  CB  . GLU A 26  ? 0.1611 0.4266 0.2346 -0.0772 -0.0447 -0.0763 26  GLU A CB  
200  C  CG  . GLU A 26  ? 0.1570 0.5133 0.3230 -0.1172 -0.0390 -0.1290 26  GLU A CG  
201  C  CD  . GLU A 26  ? 0.3246 0.6556 0.6291 0.0608  -0.0394 -0.0175 26  GLU A CD  
202  O  OE1 . GLU A 26  ? 0.3562 0.5432 0.4948 0.0307  -0.2143 -0.1106 26  GLU A OE1 
203  O  OE2 . GLU A 26  ? 0.2380 0.7573 0.5277 -0.0031 -0.1102 0.0296  26  GLU A OE2 
204  N  N   A ARG A 27  ? 0.0819 0.1423 0.1897 -0.0171 -0.0476 -0.0205 27  ARG A N   
205  N  N   B ARG A 27  ? 0.1009 0.1254 0.1844 -0.0013 -0.0458 -0.0359 27  ARG A N   
206  C  CA  A ARG A 27  ? 0.0776 0.0715 0.2251 0.0049  -0.0551 -0.0253 27  ARG A CA  
207  C  CA  B ARG A 27  ? 0.1066 0.1344 0.2073 -0.0210 -0.0577 0.0000  27  ARG A CA  
208  C  C   A ARG A 27  ? 0.0750 0.0886 0.2096 0.0035  -0.0493 -0.0006 27  ARG A C   
209  C  C   B ARG A 27  ? 0.0450 0.0797 0.2132 -0.0175 -0.0491 -0.0054 27  ARG A C   
210  O  O   A ARG A 27  ? 0.0706 0.1116 0.2075 0.0114  -0.0463 -0.0015 27  ARG A O   
211  O  O   B ARG A 27  ? 0.1136 0.1084 0.1922 0.0057  -0.0544 -0.0035 27  ARG A O   
212  C  CB  A ARG A 27  ? 0.1660 0.0502 0.2393 0.0124  -0.0324 -0.0421 27  ARG A CB  
213  C  CB  B ARG A 27  ? 0.0768 0.1474 0.2644 -0.0263 -0.0922 -0.0421 27  ARG A CB  
214  C  CG  A ARG A 27  ? 0.1150 0.0820 0.2373 -0.0372 -0.0258 -0.0465 27  ARG A CG  
215  C  CG  B ARG A 27  ? 0.1791 0.1356 0.2745 -0.0164 -0.0452 -0.0675 27  ARG A CG  
216  C  CD  A ARG A 27  ? 0.2136 0.1301 0.2152 0.0052  -0.0153 -0.0771 27  ARG A CD  
217  C  CD  B ARG A 27  ? 0.3102 0.1172 0.2678 0.0027  0.0274  -0.0754 27  ARG A CD  
218  N  NE  A ARG A 27  ? 0.2224 0.0895 0.2378 0.0351  0.0031  -0.0013 27  ARG A NE  
219  N  NE  B ARG A 27  ? 0.1967 0.1787 0.2421 0.0342  0.0186  -0.0401 27  ARG A NE  
220  C  CZ  A ARG A 27  ? 0.2005 0.0662 0.1969 0.0500  0.0287  -0.0337 27  ARG A CZ  
221  C  CZ  B ARG A 27  ? 0.1383 0.1764 0.2953 0.0375  0.0320  -0.0688 27  ARG A CZ  
222  N  NH1 A ARG A 27  ? 0.0476 0.0908 0.1324 0.0285  -0.0353 -0.0754 27  ARG A NH1 
223  N  NH1 B ARG A 27  ? 0.1453 0.0967 0.4131 0.0258  0.0674  -0.0476 27  ARG A NH1 
224  N  NH2 A ARG A 27  ? 0.1143 0.0658 0.3222 -0.0375 0.0500  -0.0922 27  ARG A NH2 
225  N  NH2 B ARG A 27  ? 0.2193 0.3027 0.2527 0.0285  0.0052  -0.0010 27  ARG A NH2 
226  N  N   . GLN A 28  ? 0.0731 0.0750 0.1990 -0.0171 -0.0423 -0.0006 28  GLN A N   
227  C  CA  . GLN A 28  ? 0.0688 0.0825 0.1913 -0.0076 -0.0366 -0.0049 28  GLN A CA  
228  C  C   . GLN A 28  ? 0.0882 0.0561 0.1782 -0.0073 -0.0342 0.0216  28  GLN A C   
229  O  O   . GLN A 28  ? 0.0951 0.1052 0.1773 -0.0229 -0.0441 0.0093  28  GLN A O   
230  C  CB  . GLN A 28  ? 0.0529 0.0886 0.2402 -0.0063 -0.0375 -0.0020 28  GLN A CB  
231  C  CG  . GLN A 28  ? 0.0750 0.0987 0.1974 -0.0225 -0.0230 -0.0092 28  GLN A CG  
232  C  CD  . GLN A 28  ? 0.0564 0.0904 0.1861 -0.0208 -0.0228 -0.0228 28  GLN A CD  
233  O  OE1 . GLN A 28  ? 0.0851 0.0776 0.1944 -0.0153 -0.0274 -0.0177 28  GLN A OE1 
234  N  NE2 . GLN A 28  ? 0.0599 0.0784 0.2461 0.0040  -0.0303 -0.0173 28  GLN A NE2 
235  N  N   . SER A 29  ? 0.0759 0.0559 0.1705 -0.0035 -0.0326 0.0097  29  SER A N   
236  C  CA  . SER A 29  ? 0.0529 0.0599 0.1838 -0.0015 -0.0236 -0.0013 29  SER A CA  
237  C  C   . SER A 29  ? 0.0724 0.0714 0.1789 0.0024  -0.0384 0.0006  29  SER A C   
238  O  O   . SER A 29  ? 0.0631 0.0732 0.1992 0.0020  -0.0274 -0.0062 29  SER A O   
239  C  CB  . SER A 29  ? 0.0526 0.0502 0.2001 0.0109  -0.0219 -0.0197 29  SER A CB  
240  O  OG  . SER A 29  ? 0.0670 0.0627 0.1983 0.0043  -0.0285 -0.0186 29  SER A OG  
241  N  N   . PRO A 30  ? 0.0579 0.0546 0.1922 0.0076  -0.0251 0.0073  30  PRO A N   
242  C  CA  . PRO A 30  ? 0.0788 0.0582 0.1791 -0.0120 -0.0230 0.0040  30  PRO A CA  
243  C  C   . PRO A 30  ? 0.0772 0.0687 0.1906 0.0068  -0.0274 0.0115  30  PRO A C   
244  O  O   . PRO A 30  ? 0.0741 0.0656 0.2080 -0.0015 -0.0313 -0.0027 30  PRO A O   
245  C  CB  . PRO A 30  ? 0.0810 0.0515 0.1854 0.0187  -0.0421 -0.0098 30  PRO A CB  
246  C  CG  . PRO A 30  ? 0.0675 0.0450 0.2002 0.0065  -0.0344 -0.0093 30  PRO A CG  
247  C  CD  . PRO A 30  ? 0.0553 0.0631 0.2044 0.0109  -0.0160 -0.0093 30  PRO A CD  
248  N  N   . VAL A 31  ? 0.0750 0.0643 0.1723 0.0027  -0.0236 0.0065  31  VAL A N   
249  C  CA  . VAL A 31  ? 0.0960 0.0737 0.1976 -0.0043 -0.0423 0.0207  31  VAL A CA  
250  C  C   . VAL A 31  ? 0.0881 0.0415 0.2019 0.0113  -0.0197 0.0086  31  VAL A C   
251  O  O   . VAL A 31  ? 0.0816 0.0750 0.2275 0.0065  -0.0401 0.0098  31  VAL A O   
252  C  CB  . VAL A 31  ? 0.0885 0.0873 0.1911 0.0031  -0.0294 0.0065  31  VAL A CB  
253  C  CG1 . VAL A 31  ? 0.1168 0.0723 0.2204 0.0006  0.0006  0.0074  31  VAL A CG1 
254  C  CG2 . VAL A 31  ? 0.0921 0.0736 0.2578 0.0026  -0.0217 0.0120  31  VAL A CG2 
255  N  N   . ASP A 32  ? 0.0876 0.0555 0.2226 0.0163  -0.0252 0.0270  32  ASP A N   
256  C  CA  . ASP A 32  ? 0.1071 0.0653 0.2136 -0.0081 -0.0166 0.0250  32  ASP A CA  
257  C  C   . ASP A 32  ? 0.1066 0.0772 0.1870 0.0135  -0.0419 0.0115  32  ASP A C   
258  O  O   . ASP A 32  ? 0.1133 0.1306 0.1983 -0.0020 -0.0379 0.0057  32  ASP A O   
259  C  CB  . ASP A 32  ? 0.1416 0.0606 0.2614 -0.0013 -0.0192 0.0443  32  ASP A CB  
260  C  CG  . ASP A 32  ? 0.1403 0.0768 0.2290 0.0093  -0.0432 0.0483  32  ASP A CG  
261  O  OD1 . ASP A 32  ? 0.1204 0.0829 0.2470 0.0087  -0.0416 0.0305  32  ASP A OD1 
262  O  OD2 . ASP A 32  ? 0.2409 0.1102 0.2682 -0.0346 -0.0441 0.0489  32  ASP A OD2 
263  N  N   . ILE A 33  ? 0.0850 0.0700 0.2172 0.0070  -0.0197 0.0102  33  ILE A N   
264  C  CA  . ILE A 33  ? 0.0886 0.0744 0.2157 0.0031  -0.0185 0.0417  33  ILE A CA  
265  C  C   . ILE A 33  ? 0.1197 0.0942 0.2369 0.0148  0.0098  0.0401  33  ILE A C   
266  O  O   . ILE A 33  ? 0.1356 0.0829 0.2991 0.0017  -0.0071 0.0254  33  ILE A O   
267  C  CB  . ILE A 33  ? 0.0958 0.1057 0.2384 0.0076  -0.0203 0.0460  33  ILE A CB  
268  C  CG1 . ILE A 33  ? 0.1471 0.0636 0.2330 0.0087  -0.0504 0.0417  33  ILE A CG1 
269  C  CG2 . ILE A 33  ? 0.1097 0.1288 0.2858 0.0621  -0.0137 0.0258  33  ILE A CG2 
270  C  CD1 . ILE A 33  ? 0.1299 0.0974 0.2305 0.0082  -0.0320 0.0392  33  ILE A CD1 
271  N  N   . ASP A 34  ? 0.1805 0.0854 0.2373 0.0291  -0.0104 0.0381  34  ASP A N   
272  C  CA  . ASP A 34  ? 0.1394 0.1186 0.2732 0.0197  0.0037  0.0562  34  ASP A CA  
273  C  C   . ASP A 34  ? 0.1703 0.1222 0.3118 0.0412  0.0635  0.0768  34  ASP A C   
274  O  O   . ASP A 34  ? 0.1917 0.2046 0.2759 0.0586  0.0192  0.0388  34  ASP A O   
275  C  CB  . ASP A 34  ? 0.1908 0.1777 0.2773 0.0617  -0.0272 0.0776  34  ASP A CB  
276  C  CG  . ASP A 34  ? 0.2114 0.2258 0.3650 0.0597  -0.0302 0.0938  34  ASP A CG  
277  O  OD1 . ASP A 34  ? 0.2563 0.3402 0.5690 -0.0109 -0.1340 0.1889  34  ASP A OD1 
278  O  OD2 . ASP A 34  ? 0.3368 0.1631 0.3819 0.0524  0.0794  0.0983  34  ASP A OD2 
279  N  N   . THR A 35  ? 0.1547 0.1238 0.2892 0.0434  0.0176  0.1014  35  THR A N   
280  C  CA  . THR A 35  ? 0.1782 0.1360 0.3104 0.0608  0.0478  0.0551  35  THR A CA  
281  C  C   . THR A 35  ? 0.2030 0.1669 0.3181 0.0684  0.0864  0.1032  35  THR A C   
282  O  O   . THR A 35  ? 0.2032 0.1705 0.3792 0.0746  0.0612  0.0258  35  THR A O   
283  C  CB  . THR A 35  ? 0.1875 0.1631 0.3436 0.0759  0.0208  0.0551  35  THR A CB  
284  O  OG1 . THR A 35  ? 0.1574 0.1572 0.3871 0.0194  0.0137  0.0807  35  THR A OG1 
285  C  CG2 . THR A 35  ? 0.2021 0.2346 0.3616 0.0903  0.0227  0.0623  35  THR A CG2 
286  N  N   . HIS A 36  ? 0.2892 0.1856 0.3458 0.1027  0.1212  0.1190  36  HIS A N   
287  C  CA  . HIS A 36  ? 0.4320 0.1509 0.3298 0.1142  0.1277  0.1018  36  HIS A CA  
288  C  C   . HIS A 36  ? 0.5274 0.1782 0.3779 0.0939  0.1949  0.0113  36  HIS A C   
289  O  O   . HIS A 36  ? 0.8847 0.1938 0.5040 -0.0240 0.4043  0.0031  36  HIS A O   
290  C  CB  . HIS A 36  ? 0.4999 0.0859 0.3479 0.0546  0.0458  0.0581  36  HIS A CB  
291  C  CG  . HIS A 36  ? 0.3476 0.1280 0.3783 -0.0020 -0.0487 0.0648  36  HIS A CG  
292  N  ND1 . HIS A 36  ? 0.3102 0.1659 0.3490 -0.0812 -0.0856 0.0425  36  HIS A ND1 
293  C  CD2 . HIS A 36  ? 0.5281 0.2939 0.3707 0.2567  -0.1421 -0.0513 36  HIS A CD2 
294  C  CE1 . HIS A 36  ? 0.6049 0.1125 0.2917 0.1264  -0.0623 0.0082  36  HIS A CE1 
295  N  NE2 . HIS A 36  ? 0.6502 0.1432 0.3885 0.0759  0.0162  0.0434  36  HIS A NE2 
296  N  N   . THR A 37  ? 0.3280 0.2143 0.3995 0.1753  0.0863  0.1071  37  THR A N   
297  C  CA  . THR A 37  ? 0.3434 0.2508 0.3609 0.1912  0.1133  0.1142  37  THR A CA  
298  C  C   . THR A 37  ? 0.2175 0.1791 0.3540 0.0939  0.0259  0.0662  37  THR A C   
299  O  O   . THR A 37  ? 0.3892 0.2143 0.3535 0.1509  0.0087  0.0383  37  THR A O   
300  C  CB  . THR A 37  ? 0.3452 0.3874 0.4568 0.2016  0.0869  0.0856  37  THR A CB  
301  O  OG1 . THR A 37  ? 0.3370 0.4122 0.4061 0.1801  0.0394  0.1142  37  THR A OG1 
302  C  CG2 . THR A 37  ? 0.2784 0.3607 0.4690 0.1861  -0.0381 0.0263  37  THR A CG2 
303  N  N   . ALA A 38  ? 0.2301 0.1536 0.3249 0.0768  0.0741  0.0803  38  ALA A N   
304  C  CA  . ALA A 38  ? 0.2276 0.1190 0.2958 0.0588  0.0357  0.0337  38  ALA A CA  
305  C  C   . ALA A 38  ? 0.2439 0.1518 0.3109 0.0806  0.0529  0.0806  38  ALA A C   
306  O  O   . ALA A 38  ? 0.2398 0.1511 0.3574 0.0065  0.0395  0.0603  38  ALA A O   
307  C  CB  . ALA A 38  ? 0.2678 0.1010 0.2919 0.0432  0.0403  0.0295  38  ALA A CB  
308  N  N   . LYS A 39  ? 0.2129 0.1656 0.2712 0.0568  0.0129  0.0498  39  LYS A N   
309  C  CA  . LYS A 39  ? 0.1613 0.2188 0.2644 0.0680  -0.0125 0.0366  39  LYS A CA  
310  C  C   . LYS A 39  ? 0.1669 0.2274 0.1985 0.0661  0.0173  0.0476  39  LYS A C   
311  O  O   . LYS A 39  ? 0.1430 0.2319 0.2030 0.0636  -0.0230 0.0476  39  LYS A O   
312  C  CB  . LYS A 39  ? 0.2172 0.2382 0.3097 0.0710  -0.0535 0.0261  39  LYS A CB  
313  C  CG  . LYS A 39  ? 0.2317 0.3671 0.2493 0.0781  -0.0590 0.0318  39  LYS A CG  
314  C  CD  . LYS A 39  ? 0.2752 0.3750 0.2836 0.1254  0.0181  0.0564  39  LYS A CD  
315  C  CE  . LYS A 39  ? 0.2563 0.4514 0.3345 0.0250  0.0728  -0.0076 39  LYS A CE  
316  N  NZ  . LYS A 39  ? 0.1908 0.3993 0.3750 0.0776  0.0482  0.0399  39  LYS A NZ  
317  N  N   . TYR A 40  ? 0.1932 0.2727 0.2669 0.0537  0.0165  0.0315  40  TYR A N   
318  C  CA  . TYR A 40  ? 0.1766 0.2583 0.2958 0.0063  -0.0003 0.0136  40  TYR A CA  
319  C  C   . TYR A 40  ? 0.1608 0.2630 0.2648 0.0086  0.0010  0.0229  40  TYR A C   
320  O  O   . TYR A 40  ? 0.2500 0.3871 0.2457 0.1404  -0.0392 -0.0249 40  TYR A O   
321  C  CB  . TYR A 40  ? 0.1942 0.3424 0.3474 -0.0242 0.0489  0.0560  40  TYR A CB  
322  C  CG  . TYR A 40  ? 0.1775 0.3828 0.2565 -0.0375 -0.0129 -0.0054 40  TYR A CG  
323  C  CD1 . TYR A 40  ? 0.1816 0.2339 0.2879 -0.0076 -0.0485 -0.0030 40  TYR A CD1 
324  C  CD2 . TYR A 40  ? 0.2793 0.5457 0.2885 0.1001  0.0292  0.0579  40  TYR A CD2 
325  C  CE1 . TYR A 40  ? 0.1571 0.5224 0.2849 -0.0091 -0.0361 0.0489  40  TYR A CE1 
326  C  CE2 . TYR A 40  ? 0.3093 0.5701 0.3702 0.1133  -0.0557 0.0522  40  TYR A CE2 
327  C  CZ  . TYR A 40  ? 0.2445 0.7106 0.3179 0.0878  0.0125  0.0568  40  TYR A CZ  
328  O  OH  . TYR A 40  ? 0.1941 0.7864 0.6248 0.1198  0.1053  -0.0754 40  TYR A OH  
329  N  N   . ASP A 41  ? 0.1520 0.2026 0.3142 0.0238  0.0037  0.0076  41  ASP A N   
330  C  CA  . ASP A 41  ? 0.2328 0.2035 0.3088 0.0483  -0.0900 0.0031  41  ASP A CA  
331  C  C   . ASP A 41  ? 0.2752 0.2490 0.2802 0.1229  -0.0381 -0.0575 41  ASP A C   
332  O  O   . ASP A 41  ? 0.2120 0.3574 0.2793 0.0983  -0.0428 -0.0057 41  ASP A O   
333  C  CB  . ASP A 41  ? 0.2360 0.2725 0.3675 -0.0282 -0.1014 -0.0317 41  ASP A CB  
334  C  CG  . ASP A 41  ? 0.3386 0.2646 0.4282 -0.0296 -0.1263 -0.0340 41  ASP A CG  
335  O  OD1 . ASP A 41  ? 0.4648 0.2784 0.4677 0.0842  -0.1790 -0.1544 41  ASP A OD1 
336  O  OD2 . ASP A 41  ? 0.3657 0.3176 0.4140 -0.0860 -0.0649 0.0671  41  ASP A OD2 
337  N  N   . PRO A 42  ? 0.2736 0.5418 0.2727 0.1744  -0.0198 -0.0024 42  PRO A N   
338  C  CA  . PRO A 42  ? 0.2412 0.3585 0.3526 0.1305  -0.0071 0.0113  42  PRO A CA  
339  C  C   . PRO A 42  ? 0.2560 0.3794 0.4379 0.1430  0.0377  0.0129  42  PRO A C   
340  O  O   . PRO A 42  ? 0.3759 0.7260 0.4704 0.3429  0.0076  -0.0010 42  PRO A O   
341  C  CB  . PRO A 42  ? 0.3077 0.5428 0.3743 -0.0522 0.0020  0.0417  42  PRO A CB  
342  C  CG  . PRO A 42  ? 0.2917 0.7756 0.3467 0.0318  0.0715  -0.0210 42  PRO A CG  
343  C  CD  . PRO A 42  ? 0.4054 0.3790 0.3332 0.2345  0.0230  0.0895  42  PRO A CD  
344  N  N   . SER A 43  ? 0.4298 0.3849 0.2585 0.0243  0.0560  -0.0582 43  SER A N   
345  C  CA  . SER A 43  ? 0.5371 0.2894 0.4449 -0.2125 0.0337  -0.0737 43  SER A CA  
346  C  C   . SER A 43  ? 0.4661 0.2624 0.3970 0.1324  -0.0408 -0.0219 43  SER A C   
347  O  O   . SER A 43  ? 0.4226 0.3088 0.6172 0.1483  -0.1694 0.0197  43  SER A O   
348  C  CB  . SER A 43  ? 0.4668 0.4354 0.4693 -0.0118 -0.0806 -0.1194 43  SER A CB  
349  O  OG  . SER A 43  ? 0.5245 0.3867 0.3901 0.0533  -0.0560 -0.0518 43  SER A OG  
350  N  N   . LEU A 44  ? 0.3648 0.3788 0.2782 0.1712  -0.0414 0.0063  44  LEU A N   
351  C  CA  . LEU A 44  ? 0.2475 0.3131 0.3021 0.1048  -0.0807 0.0538  44  LEU A CA  
352  C  C   . LEU A 44  ? 0.1908 0.4797 0.4345 -0.0085 -0.0529 0.1668  44  LEU A C   
353  O  O   . LEU A 44  ? 0.2639 0.4841 0.4018 -0.1273 -0.0856 0.1120  44  LEU A O   
354  C  CB  . LEU A 44  ? 0.2098 0.4271 0.2867 0.0258  -0.0759 -0.0573 44  LEU A CB  
355  C  CG  . LEU A 44  ? 0.1805 0.2829 0.3043 0.0031  -0.0030 0.0107  44  LEU A CG  
356  C  CD1 . LEU A 44  ? 0.2028 0.2427 0.3280 -0.0161 -0.0480 -0.0103 44  LEU A CD1 
357  C  CD2 . LEU A 44  ? 0.2120 0.1773 0.3111 0.0054  -0.0337 0.0005  44  LEU A CD2 
358  N  N   . LYS A 45  ? 0.2328 0.5029 0.4453 0.0131  -0.1483 0.1479  45  LYS A N   
359  C  CA  . LYS A 45  ? 0.2890 0.3422 0.4523 0.0296  -0.1937 0.0219  45  LYS A CA  
360  C  C   . LYS A 45  ? 0.2202 0.5349 0.2269 0.0165  -0.0522 0.0584  45  LYS A C   
361  O  O   . LYS A 45  ? 0.1304 0.6283 0.4128 -0.0364 -0.0403 -0.0362 45  LYS A O   
362  C  CB  . LYS A 45  ? 0.2511 0.1683 0.5317 0.0320  -0.0162 -0.1084 45  LYS A CB  
363  C  CG  . LYS A 45  ? 0.3346 0.3072 0.3711 -0.0346 -0.0463 -0.0718 45  LYS A CG  
364  C  CD  . LYS A 45  ? 0.5626 0.3269 0.6215 0.0120  0.0825  -0.0082 45  LYS A CD  
365  C  CE  . LYS A 45  ? 1.0769 0.7569 0.6725 0.0571  0.2230  -0.1861 45  LYS A CE  
366  N  NZ  . LYS A 45  ? 0.7300 0.8675 0.9361 0.0414  0.3544  0.3465  45  LYS A NZ  
367  N  N   . PRO A 46  ? 0.1877 0.3433 0.2883 -0.0789 -0.0483 0.0454  46  PRO A N   
368  C  CA  . PRO A 46  ? 0.1579 0.5303 0.2653 -0.0850 -0.0269 0.0838  46  PRO A CA  
369  C  C   . PRO A 46  ? 0.1277 0.3068 0.2211 -0.0086 0.0031  0.0208  46  PRO A C   
370  O  O   . PRO A 46  ? 0.1414 0.3483 0.3436 -0.0340 -0.0419 0.0943  46  PRO A O   
371  C  CB  . PRO A 46  ? 0.1344 0.3650 0.3271 -0.0759 0.0035  0.0412  46  PRO A CB  
372  C  CG  . PRO A 46  ? 0.1861 0.4557 0.4007 -0.0662 0.0087  -0.0522 46  PRO A CG  
373  C  CD  . PRO A 46  ? 0.2531 0.4167 0.3485 0.0137  -0.0702 -0.0359 46  PRO A CD  
374  N  N   . LEU A 47  ? 0.1012 0.2373 0.3614 0.0142  -0.0147 0.0305  47  LEU A N   
375  C  CA  . LEU A 47  ? 0.0829 0.2448 0.2944 -0.0153 -0.0175 0.0269  47  LEU A CA  
376  C  C   . LEU A 47  ? 0.0588 0.1836 0.4165 0.0038  -0.0164 0.0456  47  LEU A C   
377  O  O   . LEU A 47  ? 0.1003 0.2012 0.5536 -0.0120 -0.0869 0.0229  47  LEU A O   
378  C  CB  . LEU A 47  ? 0.1601 0.2222 0.4526 -0.0040 -0.0384 0.0199  47  LEU A CB  
379  C  CG  . LEU A 47  ? 0.0886 0.3267 0.5561 -0.0812 -0.0593 -0.1270 47  LEU A CG  
380  C  CD1 . LEU A 47  ? 0.1924 0.3316 0.7056 0.0107  -0.1757 -0.2230 47  LEU A CD1 
381  C  CD2 . LEU A 47  ? 0.4862 0.5407 0.7584 -0.0177 -0.0759 0.0326  47  LEU A CD2 
382  N  N   . SER A 48  ? 0.0947 0.1773 0.2504 -0.0006 -0.0093 0.0388  48  SER A N   
383  C  CA  . SER A 48  ? 0.1317 0.1703 0.2321 0.0193  0.0068  0.0176  48  SER A CA  
384  C  C   . SER A 48  ? 0.1204 0.1856 0.2181 -0.0252 -0.0274 0.0151  48  SER A C   
385  O  O   . SER A 48  ? 0.1177 0.1247 0.2743 -0.0017 0.0052  -0.0137 48  SER A O   
386  C  CB  . SER A 48  ? 0.1773 0.1820 0.3226 0.0286  -0.0054 -0.0104 48  SER A CB  
387  O  OG  . SER A 48  ? 0.1832 0.2249 0.3637 0.0450  0.0098  0.0326  48  SER A OG  
388  N  N   . VAL A 49  ? 0.1782 0.2211 0.2179 -0.0197 -0.0046 -0.0344 49  VAL A N   
389  C  CA  . VAL A 49  ? 0.2468 0.1579 0.2166 -0.0639 -0.0182 -0.0208 49  VAL A CA  
390  C  C   . VAL A 49  ? 0.1863 0.2657 0.2294 -0.1111 -0.0092 -0.0020 49  VAL A C   
391  O  O   . VAL A 49  ? 0.2596 0.4449 0.2811 -0.2354 -0.0284 0.0126  49  VAL A O   
392  C  CB  . VAL A 49  ? 0.2515 0.2048 0.3355 -0.0745 0.0465  -0.0619 49  VAL A CB  
393  C  CG1 . VAL A 49  ? 0.3883 0.1509 0.3194 -0.0590 0.0505  -0.0176 49  VAL A CG1 
394  C  CG2 . VAL A 49  ? 0.2576 0.2240 0.3662 -0.0803 0.0357  -0.0678 49  VAL A CG2 
395  N  N   . SER A 50  ? 0.1297 0.2136 0.2782 -0.0509 -0.0017 -0.0216 50  SER A N   
396  C  CA  . SER A 50  ? 0.1304 0.2256 0.3264 -0.0296 -0.0049 -0.0164 50  SER A CA  
397  C  C   . SER A 50  ? 0.1133 0.2205 0.2714 -0.0505 -0.0109 -0.0196 50  SER A C   
398  O  O   . SER A 50  ? 0.1295 0.1721 0.2673 -0.0186 -0.0471 -0.0041 50  SER A O   
399  C  CB  . SER A 50  ? 0.2254 0.2587 0.3201 -0.0098 -0.0272 -0.0653 50  SER A CB  
400  O  OG  . SER A 50  ? 0.2023 0.4372 0.4045 0.0125  -0.0478 -0.0768 50  SER A OG  
401  N  N   . TYR A 51  ? 0.0768 0.2184 0.2870 -0.0405 -0.0324 -0.0230 51  TYR A N   
402  C  CA  . TYR A 51  ? 0.1213 0.1807 0.2578 -0.0183 -0.0390 -0.0182 51  TYR A CA  
403  C  C   . TYR A 51  ? 0.0658 0.1791 0.2698 -0.0043 -0.0241 0.0254  51  TYR A C   
404  O  O   . TYR A 51  ? 0.1416 0.1313 0.2597 -0.0215 -0.0164 0.0131  51  TYR A O   
405  C  CB  . TYR A 51  ? 0.1133 0.1405 0.2779 -0.0120 -0.0581 -0.0164 51  TYR A CB  
406  C  CG  . TYR A 51  ? 0.0965 0.1306 0.2493 -0.0357 -0.0186 0.0113  51  TYR A CG  
407  C  CD1 . TYR A 51  ? 0.0922 0.1261 0.2675 -0.0248 -0.0082 0.0003  51  TYR A CD1 
408  C  CD2 . TYR A 51  ? 0.1018 0.1172 0.2299 -0.0392 -0.0226 -0.0109 51  TYR A CD2 
409  C  CE1 . TYR A 51  ? 0.1254 0.1098 0.2123 -0.0109 -0.0229 0.0038  51  TYR A CE1 
410  C  CE2 . TYR A 51  ? 0.0917 0.1367 0.2116 -0.0296 -0.0259 -0.0130 51  TYR A CE2 
411  C  CZ  . TYR A 51  ? 0.0951 0.1023 0.2761 -0.0324 -0.0197 -0.0107 51  TYR A CZ  
412  O  OH  . TYR A 51  ? 0.1003 0.1071 0.2527 -0.0250 -0.0405 -0.0120 51  TYR A OH  
413  N  N   . ASP A 52  ? 0.0790 0.2260 0.3210 0.0208  -0.0242 -0.0098 52  ASP A N   
414  C  CA  . ASP A 52  ? 0.0987 0.2170 0.3222 -0.0115 -0.0197 0.0458  52  ASP A CA  
415  C  C   . ASP A 52  ? 0.1516 0.2075 0.3066 0.0494  -0.0265 0.0340  52  ASP A C   
416  O  O   . ASP A 52  ? 0.1933 0.2044 0.3298 -0.0324 -0.0480 0.0684  52  ASP A O   
417  C  CB  . ASP A 52  ? 0.1177 0.3082 0.3849 -0.0003 0.0304  0.0960  52  ASP A CB  
418  C  CG  . ASP A 52  ? 0.3853 0.3700 0.6348 0.1366  0.1110  -0.0759 52  ASP A CG  
419  O  OD1 . ASP A 52  ? 0.3055 0.7515 0.7092 0.0359  0.1005  -0.2073 52  ASP A OD1 
420  O  OD2 . ASP A 52  ? 0.5267 0.3555 0.9419 0.1096  0.0728  0.0851  52  ASP A OD2 
421  N  N   . GLN A 53  ? 0.0985 0.1974 0.3483 0.0230  0.0264  0.0274  53  GLN A N   
422  C  CA  . GLN A 53  ? 0.1199 0.1753 0.2820 0.0131  0.0153  0.0035  53  GLN A CA  
423  C  C   . GLN A 53  ? 0.1259 0.1498 0.2100 0.0359  -0.0315 0.0141  53  GLN A C   
424  O  O   . GLN A 53  ? 0.1509 0.1277 0.2583 0.0285  -0.0129 0.0252  53  GLN A O   
425  C  CB  . GLN A 53  ? 0.1667 0.1644 0.2822 0.0351  -0.0137 0.0010  53  GLN A CB  
426  C  CG  . GLN A 53  ? 0.1816 0.2371 0.3537 0.0535  -0.0148 0.0384  53  GLN A CG  
427  C  CD  . GLN A 53  ? 0.1190 0.3174 0.4652 0.0065  -0.0197 0.0102  53  GLN A CD  
428  O  OE1 . GLN A 53  ? 0.1750 0.2985 0.9218 -0.0031 0.0142  0.0675  53  GLN A OE1 
429  N  NE2 . GLN A 53  ? 0.1753 0.1757 0.4505 0.0603  -0.0582 0.0208  53  GLN A NE2 
430  N  N   . ALA A 54  ? 0.1259 0.1270 0.2398 0.0307  -0.0302 0.0086  54  ALA A N   
431  C  CA  . ALA A 54  ? 0.1292 0.1027 0.2441 0.0091  -0.0217 0.0136  54  ALA A CA  
432  C  C   . ALA A 54  ? 0.1057 0.0894 0.2391 -0.0031 -0.0184 -0.0041 54  ALA A C   
433  O  O   . ALA A 54  ? 0.1280 0.1491 0.2547 -0.0091 -0.0285 -0.0131 54  ALA A O   
434  C  CB  . ALA A 54  ? 0.1277 0.1203 0.2707 0.0452  -0.0346 0.0048  54  ALA A CB  
435  N  N   . THR A 55  ? 0.1132 0.0816 0.2275 0.0195  -0.0182 0.0208  55  THR A N   
436  C  CA  . THR A 55  ? 0.1032 0.0898 0.2265 0.0228  -0.0401 0.0065  55  THR A CA  
437  C  C   . THR A 55  ? 0.0948 0.0772 0.1958 0.0015  -0.0450 0.0017  55  THR A C   
438  O  O   . THR A 55  ? 0.1062 0.0684 0.2292 -0.0031 -0.0590 0.0218  55  THR A O   
439  C  CB  . THR A 55  ? 0.1027 0.1010 0.2416 0.0186  -0.0461 0.0283  55  THR A CB  
440  O  OG1 . THR A 55  ? 0.1026 0.1141 0.2784 0.0174  -0.0271 0.0165  55  THR A OG1 
441  C  CG2 . THR A 55  ? 0.1480 0.0882 0.2443 0.0109  -0.0498 0.0348  55  THR A CG2 
442  N  N   . SER A 56  ? 0.0838 0.0688 0.1875 0.0038  -0.0307 0.0057  56  SER A N   
443  C  CA  . SER A 56  ? 0.0790 0.0784 0.2028 0.0126  -0.0197 0.0131  56  SER A CA  
444  C  C   . SER A 56  ? 0.1102 0.0886 0.1881 0.0006  -0.0399 0.0322  56  SER A C   
445  O  O   . SER A 56  ? 0.1093 0.0674 0.1958 -0.0076 -0.0480 0.0274  56  SER A O   
446  C  CB  . SER A 56  ? 0.1143 0.0627 0.1834 -0.0006 -0.0463 0.0148  56  SER A CB  
447  O  OG  . SER A 56  ? 0.0956 0.0696 0.2087 -0.0015 -0.0522 0.0091  56  SER A OG  
448  N  N   . LEU A 57  ? 0.1000 0.0868 0.1915 -0.0186 -0.0219 0.0126  57  LEU A N   
449  C  CA  . LEU A 57  ? 0.0898 0.0750 0.2017 -0.0065 -0.0219 0.0197  57  LEU A CA  
450  C  C   . LEU A 57  ? 0.0987 0.0762 0.1802 0.0060  -0.0109 0.0335  57  LEU A C   
451  O  O   . LEU A 57  ? 0.1403 0.0939 0.1913 0.0000  -0.0372 0.0214  57  LEU A O   
452  C  CB  . LEU A 57  ? 0.1240 0.0895 0.2621 -0.0351 0.0006  0.0155  57  LEU A CB  
453  C  CG  . LEU A 57  ? 0.1793 0.1143 0.2114 -0.0272 -0.0015 -0.0020 57  LEU A CG  
454  C  CD1 . LEU A 57  ? 0.1699 0.1290 0.3046 -0.0560 0.0203  -0.0153 57  LEU A CD1 
455  C  CD2 . LEU A 57  ? 0.2284 0.0925 0.2827 0.0063  -0.0307 0.0328  57  LEU A CD2 
456  N  N   . ARG A 58  ? 0.0982 0.0680 0.2229 -0.0063 -0.0344 0.0247  58  ARG A N   
457  C  CA  . ARG A 58  ? 0.0930 0.0935 0.1999 -0.0120 -0.0197 0.0274  58  ARG A CA  
458  C  C   . ARG A 58  ? 0.1105 0.0864 0.1717 -0.0125 -0.0303 0.0115  58  ARG A C   
459  O  O   . ARG A 58  ? 0.1455 0.0829 0.1692 0.0054  -0.0186 0.0043  58  ARG A O   
460  C  CB  . ARG A 58  ? 0.1256 0.0982 0.2664 -0.0208 0.0080  0.0272  58  ARG A CB  
461  C  CG  . ARG A 58  ? 0.1777 0.1389 0.3000 -0.0307 0.0000  0.0485  58  ARG A CG  
462  C  CD  . ARG A 58  ? 0.1836 0.1188 0.3702 -0.0362 0.0390  0.0333  58  ARG A CD  
463  N  NE  . ARG A 58  ? 0.2091 0.1599 0.3030 -0.0175 0.0182  0.0416  58  ARG A NE  
464  C  CZ  . ARG A 58  ? 0.2497 0.1933 0.2720 -0.0348 0.0195  0.0608  58  ARG A CZ  
465  N  NH1 . ARG A 58  ? 0.2842 0.3210 0.4023 -0.0737 -0.0678 0.1562  58  ARG A NH1 
466  N  NH2 . ARG A 58  ? 0.2290 0.1906 0.3289 -0.0073 0.0436  0.0491  58  ARG A NH2 
467  N  N   . ILE A 59  ? 0.0776 0.0878 0.1987 0.0104  -0.0284 0.0010  59  ILE A N   
468  C  CA  . ILE A 59  ? 0.0987 0.0719 0.1960 0.0031  -0.0160 0.0219  59  ILE A CA  
469  C  C   . ILE A 59  ? 0.1238 0.0635 0.1726 0.0000  -0.0119 0.0186  59  ILE A C   
470  O  O   . ILE A 59  ? 0.1071 0.1021 0.1809 0.0135  -0.0286 0.0163  59  ILE A O   
471  C  CB  . ILE A 59  ? 0.1197 0.0841 0.1888 -0.0160 -0.0318 0.0242  59  ILE A CB  
472  C  CG1 . ILE A 59  ? 0.1140 0.0878 0.2030 0.0087  0.0006  0.0286  59  ILE A CG1 
473  C  CG2 . ILE A 59  ? 0.1484 0.1098 0.1756 -0.0373 -0.0450 0.0199  59  ILE A CG2 
474  C  CD1 . ILE A 59  ? 0.1351 0.0895 0.2211 0.0049  0.0000  0.0230  59  ILE A CD1 
475  N  N   . LEU A 60  ? 0.1246 0.0907 0.2091 0.0320  -0.0140 0.0155  60  LEU A N   
476  C  CA  . LEU A 60  ? 0.1037 0.1261 0.2592 0.0333  -0.0017 0.0193  60  LEU A CA  
477  C  C   . LEU A 60  ? 0.0976 0.1213 0.1967 0.0068  -0.0228 0.0012  60  LEU A C   
478  O  O   . LEU A 60  ? 0.1188 0.1586 0.2177 0.0362  -0.0087 0.0192  60  LEU A O   
479  C  CB  . LEU A 60  ? 0.1172 0.0781 0.5083 -0.0403 0.0175  0.0557  60  LEU A CB  
480  C  CG  . LEU A 60  ? 0.1671 0.2389 0.4602 -0.0460 -0.0657 -0.0500 60  LEU A CG  
481  C  CD1 . LEU A 60  ? 0.4210 0.1491 0.3910 -0.0373 -0.0425 -0.0313 60  LEU A CD1 
482  C  CD2 . LEU A 60  ? 0.3592 0.3630 0.3819 0.0895  -0.1536 -0.1133 60  LEU A CD2 
483  N  N   . ASN A 61  ? 0.0964 0.1064 0.2075 0.0010  -0.0041 -0.0208 61  ASN A N   
484  C  CA  . ASN A 61  ? 0.0895 0.1324 0.2190 -0.0070 -0.0307 -0.0052 61  ASN A CA  
485  C  C   . ASN A 61  ? 0.0907 0.1168 0.1870 -0.0003 -0.0146 0.0037  61  ASN A C   
486  O  O   . ASN A 61  ? 0.0904 0.1768 0.1965 -0.0195 -0.0214 -0.0130 61  ASN A O   
487  C  CB  . ASN A 61  ? 0.1066 0.1208 0.2339 0.0182  0.0059  -0.0219 61  ASN A CB  
488  C  CG  . ASN A 61  ? 0.1005 0.1392 0.1904 0.0080  -0.0154 -0.0142 61  ASN A CG  
489  O  OD1 . ASN A 61  ? 0.1005 0.2028 0.2204 -0.0020 -0.0181 -0.0254 61  ASN A OD1 
490  N  ND2 . ASN A 61  ? 0.1143 0.1428 0.2114 0.0355  -0.0241 -0.0263 61  ASN A ND2 
491  N  N   . ASN A 62  ? 0.1048 0.1365 0.1902 -0.0296 -0.0329 -0.0172 62  ASN A N   
492  C  CA  . ASN A 62  ? 0.1046 0.1719 0.2037 -0.0403 -0.0452 -0.0174 62  ASN A CA  
493  C  C   . ASN A 62  ? 0.1220 0.1739 0.2199 -0.0474 -0.0493 0.0020  62  ASN A C   
494  O  O   . ASN A 62  ? 0.1116 0.2727 0.3003 -0.0540 -0.0403 -0.0617 62  ASN A O   
495  C  CB  . ASN A 62  ? 0.1389 0.1502 0.2184 -0.0520 -0.0507 -0.0102 62  ASN A CB  
496  C  CG  . ASN A 62  ? 0.1714 0.1856 0.2073 -0.0115 -0.0639 -0.0126 62  ASN A CG  
497  O  OD1 . ASN A 62  ? 0.1525 0.1649 0.2205 0.0076  -0.0120 -0.0026 62  ASN A OD1 
498  N  ND2 . ASN A 62  ? 0.3000 0.2208 0.3152 -0.0109 -0.0065 -0.0687 62  ASN A ND2 
499  N  N   . GLY A 63  ? 0.0996 0.1766 0.2299 -0.0005 -0.0366 0.0172  63  GLY A N   
500  C  CA  . GLY A 63  ? 0.0842 0.3066 0.2389 0.0434  -0.0175 0.0000  63  GLY A CA  
501  C  C   . GLY A 63  ? 0.1286 0.1659 0.2213 0.0276  -0.0252 -0.0171 63  GLY A C   
502  O  O   . GLY A 63  ? 0.1421 0.2416 0.2684 0.0723  -0.0333 -0.0298 63  GLY A O   
503  N  N   A HIS A 64  ? 0.1080 0.2265 0.1696 -0.0252 -0.0445 -0.0194 64  HIS A N   
504  N  N   B HIS A 64  ? 0.0838 0.2196 0.2159 0.0068  -0.0414 -0.0142 64  HIS A N   
505  C  CA  A HIS A 64  ? 0.0806 0.2266 0.1992 -0.0115 -0.0513 -0.0038 64  HIS A CA  
506  C  CA  B HIS A 64  ? 0.1080 0.1974 0.2231 0.0688  -0.0286 -0.0217 64  HIS A CA  
507  C  C   A HIS A 64  ? 0.0917 0.1861 0.2111 0.0041  0.0126  0.0463  64  HIS A C   
508  C  C   B HIS A 64  ? 0.1019 0.2511 0.1378 0.0115  -0.0724 -0.0403 64  HIS A C   
509  O  O   A HIS A 64  ? 0.1181 0.1944 0.1809 0.0115  0.0214  0.0357  64  HIS A O   
510  O  O   B HIS A 64  ? 0.0696 0.2680 0.1565 0.0181  -0.0263 -0.0588 64  HIS A O   
511  C  CB  A HIS A 64  ? 0.1453 0.3165 0.1942 -0.0373 -0.0120 -0.0443 64  HIS A CB  
512  C  CB  B HIS A 64  ? 0.1550 0.2678 0.2479 0.0276  -0.0599 -0.0175 64  HIS A CB  
513  C  CG  A HIS A 64  ? 0.1071 0.2231 0.2046 -0.0031 -0.0662 -0.0263 64  HIS A CG  
514  C  CG  B HIS A 64  ? 0.0529 0.3050 0.2630 0.0176  -0.0688 -0.0485 64  HIS A CG  
515  N  ND1 A HIS A 64  ? 0.0648 0.3328 0.2617 -0.0252 -0.0702 0.0170  64  HIS A ND1 
516  N  ND1 B HIS A 64  ? 0.1843 0.2921 0.2048 0.0271  -0.0186 -0.0886 64  HIS A ND1 
517  C  CD2 A HIS A 64  ? 0.1737 0.2048 0.2540 -0.0041 -0.0151 -0.0318 64  HIS A CD2 
518  C  CD2 B HIS A 64  ? 0.0930 0.2576 0.2800 0.0961  -0.0593 -0.0265 64  HIS A CD2 
519  C  CE1 A HIS A 64  ? 0.1940 0.1911 0.2251 -0.0452 -0.0274 -0.0307 64  HIS A CE1 
520  C  CE1 B HIS A 64  ? 0.1500 0.2172 0.2283 0.0225  -0.0684 -0.0666 64  HIS A CE1 
521  N  NE2 A HIS A 64  ? 0.1859 0.1844 0.2786 -0.0397 0.0282  -0.0474 64  HIS A NE2 
522  N  NE2 B HIS A 64  ? 0.1753 0.2421 0.2486 0.0469  -0.0687 -0.0285 64  HIS A NE2 
523  N  N   A SER A 65  ? 0.0750 0.1534 0.2827 -0.0137 -0.0274 0.0074  65  SER A N   
524  N  N   B SER A 65  ? 0.1005 0.1430 0.1825 0.0261  -0.0516 -0.0351 65  SER A N   
525  C  CA  A SER A 65  ? 0.0636 0.1820 0.2231 -0.0020 -0.0297 0.0285  65  SER A CA  
526  C  CA  B SER A 65  ? 0.0938 0.1726 0.2305 0.0419  -0.0370 0.0034  65  SER A CA  
527  C  C   A SER A 65  ? 0.0864 0.1313 0.2055 0.0131  -0.0379 -0.0035 65  SER A C   
528  C  C   B SER A 65  ? 0.0850 0.1367 0.2062 0.0513  -0.0265 -0.0175 65  SER A C   
529  O  O   A SER A 65  ? 0.1206 0.1242 0.2344 0.0063  -0.0353 0.0226  65  SER A O   
530  O  O   B SER A 65  ? 0.0702 0.1428 0.2414 0.0392  -0.0087 -0.0199 65  SER A O   
531  C  CB  A SER A 65  ? 0.1674 0.1601 0.1768 -0.0467 -0.0447 0.0405  65  SER A CB  
532  C  CB  B SER A 65  ? 0.1212 0.1960 0.2818 0.0252  0.0120  -0.0337 65  SER A CB  
533  O  OG  A SER A 65  ? 0.0983 0.1492 0.2220 0.0250  -0.0544 0.0582  65  SER A OG  
534  O  OG  B SER A 65  ? 0.3628 0.1349 0.2734 0.0275  -0.1101 0.0086  65  SER A OG  
535  N  N   . PHE A 66  ? 0.0850 0.1421 0.2294 0.0496  -0.0388 0.0098  66  PHE A N   
536  C  CA  . PHE A 66  ? 0.0983 0.1683 0.1805 0.0406  -0.0285 0.0176  66  PHE A CA  
537  C  C   . PHE A 66  ? 0.0913 0.1150 0.2014 0.0293  -0.0346 -0.0109 66  PHE A C   
538  O  O   . PHE A 66  ? 0.1080 0.1097 0.2035 0.0207  -0.0395 -0.0129 66  PHE A O   
539  C  CB  . PHE A 66  ? 0.1396 0.1347 0.1960 0.0384  -0.0073 -0.0098 66  PHE A CB  
540  C  CG  . PHE A 66  ? 0.1297 0.1678 0.1744 0.0515  -0.0328 0.0076  66  PHE A CG  
541  C  CD1 . PHE A 66  ? 0.1028 0.1331 0.2020 0.0082  -0.0570 -0.0355 66  PHE A CD1 
542  C  CD2 . PHE A 66  ? 0.1475 0.1335 0.2222 0.0500  -0.0675 -0.0104 66  PHE A CD2 
543  C  CE1 . PHE A 66  ? 0.0985 0.1290 0.2520 0.0337  -0.0557 -0.0241 66  PHE A CE1 
544  C  CE2 . PHE A 66  ? 0.1498 0.1322 0.2170 0.0331  -0.0604 -0.0472 66  PHE A CE2 
545  C  CZ  . PHE A 66  ? 0.1410 0.1229 0.2251 0.0276  -0.0802 -0.0353 66  PHE A CZ  
546  N  N   A LYS A 67  ? 0.0789 0.1477 0.1962 0.0579  -0.0102 0.0195  67  LYS A N   
547  N  N   B LYS A 67  ? 0.1089 0.0926 0.2057 0.0140  -0.0485 -0.0172 67  LYS A N   
548  C  CA  A LYS A 67  ? 0.0913 0.1286 0.2010 0.0375  -0.0296 -0.0027 67  LYS A CA  
549  C  CA  B LYS A 67  ? 0.1071 0.1186 0.1805 0.0562  -0.0518 0.0221  67  LYS A CA  
550  C  C   A LYS A 67  ? 0.1172 0.1194 0.1694 0.0425  -0.0085 0.0068  67  LYS A C   
551  C  C   B LYS A 67  ? 0.0872 0.0727 0.1453 0.0228  -0.0445 -0.0030 67  LYS A C   
552  O  O   A LYS A 67  ? 0.0842 0.0982 0.1847 0.0287  -0.0231 0.0026  67  LYS A O   
553  O  O   B LYS A 67  ? 0.0794 0.0869 0.1590 0.0151  -0.0412 -0.0225 67  LYS A O   
554  C  CB  A LYS A 67  ? 0.1181 0.1301 0.2345 -0.0542 0.0006  0.0206  67  LYS A CB  
555  C  CB  B LYS A 67  ? 0.1289 0.1333 0.1741 0.0342  -0.0819 0.0627  67  LYS A CB  
556  C  CG  A LYS A 67  ? 0.1502 0.1193 0.2802 -0.0710 -0.0706 0.0302  67  LYS A CG  
557  C  CG  B LYS A 67  ? 0.1403 0.2267 0.1396 0.0324  -0.0068 0.0098  67  LYS A CG  
558  C  CD  A LYS A 67  ? 0.2186 0.1999 0.3027 -0.1588 -0.0209 -0.0141 67  LYS A CD  
559  C  CD  B LYS A 67  ? 0.1590 0.2626 0.1441 0.0381  -0.0322 -0.0063 67  LYS A CD  
560  C  CE  A LYS A 67  ? 0.2373 0.2793 0.2563 -0.0697 0.0183  -0.0003 67  LYS A CE  
561  C  CE  B LYS A 67  ? 0.1850 0.2037 0.3490 -0.0043 0.0046  -0.0247 67  LYS A CE  
562  N  NZ  A LYS A 67  ? 0.1123 0.3551 0.2994 -0.0575 -0.0041 -0.1286 67  LYS A NZ  
563  N  NZ  B LYS A 67  ? 0.2265 0.2046 0.3330 0.0049  -0.0174 -0.0557 67  LYS A NZ  
564  N  N   . VAL A 68  ? 0.0877 0.0722 0.1624 0.0027  -0.0280 0.0087  68  VAL A N   
565  C  CA  . VAL A 68  ? 0.0763 0.0525 0.2215 0.0080  -0.0355 0.0006  68  VAL A CA  
566  C  C   . VAL A 68  ? 0.0895 0.0838 0.1660 0.0141  -0.0274 0.0017  68  VAL A C   
567  O  O   . VAL A 68  ? 0.1224 0.0509 0.1764 0.0076  -0.0368 -0.0003 68  VAL A O   
568  C  CB  . VAL A 68  ? 0.0820 0.0643 0.1987 0.0071  -0.0148 -0.0098 68  VAL A CB  
569  C  CG1 . VAL A 68  ? 0.0913 0.0948 0.1953 0.0131  -0.0428 -0.0052 68  VAL A CG1 
570  C  CG2 . VAL A 68  ? 0.1249 0.0674 0.2143 0.0142  -0.0217 -0.0164 68  VAL A CG2 
571  N  N   . GLU A 69  ? 0.0842 0.0662 0.2111 0.0092  -0.0252 0.0125  69  GLU A N   
572  C  CA  . GLU A 69  ? 0.0746 0.0684 0.2143 -0.0052 -0.0452 0.0080  69  GLU A CA  
573  C  C   . GLU A 69  ? 0.0891 0.0617 0.1750 0.0109  -0.0302 0.0052  69  GLU A C   
574  O  O   . GLU A 69  ? 0.1331 0.0745 0.1850 0.0175  -0.0467 -0.0010 69  GLU A O   
575  C  CB  . GLU A 69  ? 0.0960 0.0987 0.2730 0.0015  0.0137  0.0355  69  GLU A CB  
576  C  CG  . GLU A 69  ? 0.0992 0.1536 0.4257 -0.0115 -0.0359 0.0285  69  GLU A CG  
577  C  CD  . GLU A 69  ? 0.2066 0.1879 0.3014 -0.0806 -0.0252 0.0582  69  GLU A CD  
578  O  OE1 . GLU A 69  ? 0.1827 0.2509 0.3368 -0.0208 -0.0225 0.0706  69  GLU A OE1 
579  O  OE2 . GLU A 69  ? 0.2039 0.2506 0.3745 -0.0869 -0.0828 0.0065  69  GLU A OE2 
580  N  N   . PHE A 70  ? 0.0885 0.0644 0.1789 -0.0131 -0.0263 0.0054  70  PHE A N   
581  C  CA  . PHE A 70  ? 0.0890 0.0436 0.2170 -0.0024 -0.0307 0.0148  70  PHE A CA  
582  C  C   . PHE A 70  ? 0.1044 0.0439 0.2132 -0.0098 -0.0406 -0.0071 70  PHE A C   
583  O  O   . PHE A 70  ? 0.1270 0.0499 0.2470 -0.0164 -0.0599 0.0027  70  PHE A O   
584  C  CB  . PHE A 70  ? 0.1190 0.0623 0.2078 -0.0010 -0.0401 0.0060  70  PHE A CB  
585  C  CG  . PHE A 70  ? 0.1039 0.0617 0.1956 -0.0060 -0.0318 0.0109  70  PHE A CG  
586  C  CD1 . PHE A 70  ? 0.1316 0.0715 0.2046 0.0218  -0.0098 0.0313  70  PHE A CD1 
587  C  CD2 . PHE A 70  ? 0.1071 0.0907 0.1949 -0.0175 -0.0408 0.0136  70  PHE A CD2 
588  C  CE1 . PHE A 70  ? 0.1152 0.0710 0.2450 0.0043  -0.0153 0.0458  70  PHE A CE1 
589  C  CE2 . PHE A 70  ? 0.1233 0.0727 0.2014 -0.0038 -0.0195 0.0142  70  PHE A CE2 
590  C  CZ  . PHE A 70  ? 0.1307 0.0768 0.2186 -0.0017 -0.0114 0.0107  70  PHE A CZ  
591  N  N   A ASP A 71  ? 0.1310 0.0456 0.2134 -0.0027 -0.0621 0.0017  71  ASP A N   
592  N  N   B ASP A 71  ? 0.1221 0.0342 0.2529 0.0151  -0.0230 0.0052  71  ASP A N   
593  C  CA  A ASP A 71  ? 0.1140 0.0456 0.2265 -0.0287 -0.0675 -0.0006 71  ASP A CA  
594  C  CA  B ASP A 71  ? 0.1392 0.0368 0.2585 0.0038  -0.0544 0.0236  71  ASP A CA  
595  C  C   A ASP A 71  ? 0.1459 0.0331 0.2265 -0.0186 -0.0165 0.0038  71  ASP A C   
596  C  C   B ASP A 71  ? 0.1610 0.0306 0.2524 0.0193  -0.0583 0.0141  71  ASP A C   
597  O  O   A ASP A 71  ? 0.1297 0.0395 0.2134 -0.0364 -0.0317 -0.0049 71  ASP A O   
598  O  O   B ASP A 71  ? 0.1969 0.1233 0.3027 -0.0513 0.0131  0.0397  71  ASP A O   
599  C  CB  A ASP A 71  ? 0.1199 0.0582 0.2563 -0.0085 -0.0670 0.0118  71  ASP A CB  
600  C  CB  B ASP A 71  ? 0.1184 0.0974 0.2897 0.0441  -0.0333 0.0531  71  ASP A CB  
601  C  CG  A ASP A 71  ? 0.1972 0.0705 0.3203 0.0109  -0.0974 -0.0164 71  ASP A CG  
602  C  CG  B ASP A 71  ? 0.1674 0.1036 0.3355 0.0452  -0.1307 0.0275  71  ASP A CG  
603  O  OD1 A ASP A 71  ? 0.1886 0.0555 0.2998 0.0248  -0.1202 0.0188  71  ASP A OD1 
604  O  OD1 B ASP A 71  ? 0.2547 0.0658 0.3176 0.0564  -0.1756 -0.0129 71  ASP A OD1 
605  O  OD2 A ASP A 71  ? 0.1958 0.1473 0.3675 0.0750  -0.0832 -0.0644 71  ASP A OD2 
606  O  OD2 B ASP A 71  ? 0.2585 0.0597 0.3490 0.0331  -0.1172 -0.0093 71  ASP A OD2 
607  N  N   . ASP A 72  ? 0.1624 0.0296 0.2134 0.0026  -0.0487 0.0027  72  ASP A N   
608  C  CA  . ASP A 72  ? 0.1687 0.0379 0.2193 -0.0010 -0.0258 0.0302  72  ASP A CA  
609  C  C   . ASP A 72  ? 0.1732 0.0445 0.2060 -0.0085 -0.0318 0.0153  72  ASP A C   
610  O  O   . ASP A 72  ? 0.2116 0.0724 0.2308 0.0238  -0.0644 -0.0113 72  ASP A O   
611  C  CB  . ASP A 72  ? 0.2011 0.0348 0.2240 0.0384  -0.0326 0.0041  72  ASP A CB  
612  C  CG  . ASP A 72  ? 0.2157 0.0656 0.1960 0.0339  -0.0331 0.0103  72  ASP A CG  
613  O  OD1 . ASP A 72  ? 0.1518 0.1416 0.2256 -0.0104 -0.0504 0.0247  72  ASP A OD1 
614  O  OD2 . ASP A 72  ? 0.2283 0.0978 0.2179 -0.0020 -0.0815 0.0238  72  ASP A OD2 
615  N  N   . SER A 73  ? 0.1897 0.0458 0.2416 0.0087  -0.0542 0.0241  73  SER A N   
616  C  CA  . SER A 73  ? 0.2372 0.0476 0.2418 0.0131  -0.0410 -0.0031 73  SER A CA  
617  C  C   . SER A 73  ? 0.2019 0.0450 0.3127 0.0131  -0.0832 -0.0228 73  SER A C   
618  O  O   . SER A 73  ? 0.2878 0.0464 0.3357 0.0458  -0.1114 -0.0137 73  SER A O   
619  C  CB  . SER A 73  ? 0.3048 0.0406 0.2628 -0.0027 -0.0768 0.0219  73  SER A CB  
620  O  OG  . SER A 73  ? 0.2996 0.0467 0.2822 0.0217  -0.0731 0.0109  73  SER A OG  
621  N  N   A GLN A 74  ? 0.1685 0.1177 0.3154 0.0049  -0.0551 -0.0148 74  GLN A N   
622  N  N   B GLN A 74  ? 0.2172 0.0403 0.3140 0.0535  -0.0273 -0.0102 74  GLN A N   
623  C  CA  A GLN A 74  ? 0.2240 0.0882 0.4212 0.0535  -0.0320 -0.0208 74  GLN A CA  
624  C  CA  B GLN A 74  ? 0.2423 0.1216 0.3341 0.0851  -0.0472 -0.0680 74  GLN A CA  
625  C  C   A GLN A 74  ? 0.1023 0.1159 0.3447 0.0715  -0.0829 -0.0588 74  GLN A C   
626  C  C   B GLN A 74  ? 0.2064 0.2082 0.2874 -0.0443 -0.0579 -0.1254 74  GLN A C   
627  O  O   A GLN A 74  ? 0.1197 0.0798 0.3596 0.0445  0.0432  0.0109  74  GLN A O   
628  O  O   B GLN A 74  ? 0.2303 0.1879 0.2168 -0.0175 -0.1358 -0.0496 74  GLN A O   
629  C  CB  A GLN A 74  ? 0.2277 0.0290 0.4739 -0.0270 -0.0578 0.0129  74  GLN A CB  
630  C  CB  B GLN A 74  ? 0.2281 0.2251 0.3772 0.1798  -0.0353 -0.0480 74  GLN A CB  
631  C  CG  A GLN A 74  ? 0.3190 0.0428 0.5741 -0.0308 -0.0274 0.0662  74  GLN A CG  
632  C  CG  B GLN A 74  ? 0.2705 0.1583 0.4074 -0.0414 -0.0926 -0.0697 74  GLN A CG  
633  C  CD  A GLN A 74  ? 0.2141 0.3664 0.5985 -0.0710 -0.1207 0.0421  74  GLN A CD  
634  C  CD  B GLN A 74  ? 0.2150 0.1932 0.4212 0.1023  -0.0700 -0.0062 74  GLN A CD  
635  O  OE1 A GLN A 74  ? 0.2231 0.3833 0.4298 -0.0353 -0.1694 0.0248  74  GLN A OE1 
636  O  OE1 B GLN A 74  ? 0.1455 0.4779 0.4677 -0.1150 -0.0071 -0.0159 74  GLN A OE1 
637  N  NE2 A GLN A 74  ? 0.2387 0.2003 0.4187 -0.1014 -0.2161 0.1984  74  GLN A NE2 
638  N  NE2 B GLN A 74  ? 0.1416 0.3079 0.5381 -0.0869 -0.0186 -0.1897 74  GLN A NE2 
639  N  N   A ASP A 75  ? 0.2163 0.1242 0.4359 -0.0608 0.0219  -0.0806 75  ASP A N   
640  N  N   B ASP A 75  ? 0.1771 0.2518 0.3995 -0.0603 -0.0295 -0.2248 75  ASP A N   
641  C  CA  A ASP A 75  ? 0.2495 0.2727 0.4397 -0.0812 -0.0375 -0.0412 75  ASP A CA  
642  C  CA  B ASP A 75  ? 0.1994 0.3659 0.3995 -0.0912 -0.0568 -0.1519 75  ASP A CA  
643  C  C   A ASP A 75  ? 0.2107 0.2405 0.2055 -0.0636 -0.0491 0.0441  75  ASP A C   
644  C  C   B ASP A 75  ? 0.1008 0.2100 0.4045 -0.0375 -0.0372 -0.0908 75  ASP A C   
645  O  O   A ASP A 75  ? 0.1820 0.3097 0.4192 -0.0803 0.0092  -0.0939 75  ASP A O   
646  O  O   B ASP A 75  ? 0.1807 0.1021 0.4848 0.0071  -0.1023 0.0362  75  ASP A O   
647  C  CB  A ASP A 75  ? 0.3914 0.5795 0.5199 -0.0478 -0.0383 -0.1791 75  ASP A CB  
648  C  CB  B ASP A 75  ? 0.3564 0.4634 0.4052 -0.1203 -0.0705 -0.2432 75  ASP A CB  
649  C  CG  A ASP A 75  ? 0.3260 0.6908 0.7202 0.3889  -0.0881 0.2152  75  ASP A CG  
650  C  CG  B ASP A 75  ? 0.2069 0.1265 0.3145 0.0390  -0.0564 -0.0081 75  ASP A CG  
651  O  OD1 A ASP A 75  ? 0.6661 0.7835 0.7056 0.0092  0.1497  -0.0579 75  ASP A OD1 
652  O  OD1 B ASP A 75  ? 0.1737 0.5597 0.2978 0.0719  -0.0869 -0.1869 75  ASP A OD1 
653  O  OD2 A ASP A 75  ? 0.1678 0.5734 1.2812 0.1150  -0.0834 -0.3271 75  ASP A OD2 
654  O  OD2 B ASP A 75  ? 0.3569 0.3650 0.2899 -0.0329 0.0093  -0.0504 75  ASP A OD2 
655  N  N   . LYS A 76  ? 0.1854 0.1466 0.3348 0.0135  -0.0553 0.0344  76  LYS A N   
656  C  CA  . LYS A 76  ? 0.2669 0.0798 0.4821 -0.0666 0.0063  -0.0307 76  LYS A CA  
657  C  C   . LYS A 76  ? 0.2269 0.1588 0.4347 -0.0206 -0.1366 0.0522  76  LYS A C   
658  O  O   . LYS A 76  ? 0.2646 0.2269 0.4490 -0.0938 -0.0657 0.0230  76  LYS A O   
659  C  CB  . LYS A 76  ? 0.3702 0.1816 0.3398 0.0041  -0.1800 -0.0357 76  LYS A CB  
660  C  CG  . LYS A 76  ? 0.3377 0.1703 0.4733 0.0666  -0.1137 -0.0006 76  LYS A CG  
661  C  CD  . LYS A 76  ? 0.3610 0.2064 0.3716 -0.1634 -0.1137 -0.0230 76  LYS A CD  
662  C  CE  . LYS A 76  ? 0.3454 0.1534 0.5849 0.1305  -0.0461 -0.0057 76  LYS A CE  
663  N  NZ  . LYS A 76  ? 0.5953 0.1563 0.5751 -0.0030 -0.1150 -0.0296 76  LYS A NZ  
664  N  N   . ALA A 77  ? 0.1807 0.1561 0.3253 0.0627  -0.1133 -0.0239 77  ALA A N   
665  C  CA  . ALA A 77  ? 0.1538 0.0966 0.2795 -0.0012 -0.0518 -0.0152 77  ALA A CA  
666  C  C   . ALA A 77  ? 0.1057 0.0842 0.3231 0.0131  -0.0489 -0.0263 77  ALA A C   
667  O  O   . ALA A 77  ? 0.1150 0.2381 0.3777 0.0241  -0.0714 -0.1023 77  ALA A O   
668  C  CB  . ALA A 77  ? 0.2003 0.1254 0.2971 0.0015  -0.0026 0.0164  77  ALA A CB  
669  N  N   . VAL A 78  ? 0.1263 0.1023 0.2549 0.0010  -0.0754 0.0284  78  VAL A N   
670  C  CA  . VAL A 78  ? 0.1660 0.1703 0.2603 0.0263  -0.0662 0.0322  78  VAL A CA  
671  C  C   . VAL A 78  ? 0.1342 0.1143 0.2896 -0.0219 -0.0768 0.0080  78  VAL A C   
672  O  O   . VAL A 78  ? 0.1252 0.1360 0.2982 -0.0210 -0.0688 0.0174  78  VAL A O   
673  C  CB  . VAL A 78  ? 0.2504 0.1477 0.3461 0.0241  -0.0859 0.0208  78  VAL A CB  
674  C  CG1 . VAL A 78  ? 0.2639 0.1392 0.3501 -0.0163 -0.1049 -0.0076 78  VAL A CG1 
675  C  CG2 . VAL A 78  ? 0.2382 0.1683 0.3601 -0.0313 -0.0715 -0.0529 78  VAL A CG2 
676  N  N   . LEU A 79  ? 0.1149 0.0930 0.2531 0.0006  -0.0406 -0.0015 79  LEU A N   
677  C  CA  . LEU A 79  ? 0.1005 0.1231 0.2563 -0.0104 -0.0186 -0.0038 79  LEU A CA  
678  C  C   . LEU A 79  ? 0.2041 0.0606 0.2811 -0.0219 0.0165  -0.0125 79  LEU A C   
679  O  O   . LEU A 79  ? 0.1856 0.1446 0.2892 -0.0710 0.0259  -0.0416 79  LEU A O   
680  C  CB  . LEU A 79  ? 0.1010 0.1439 0.3294 -0.0049 -0.0527 0.0204  79  LEU A CB  
681  C  CG  . LEU A 79  ? 0.1556 0.1473 0.3499 0.0239  -0.0399 0.0003  79  LEU A CG  
682  C  CD1 . LEU A 79  ? 0.1486 0.1230 0.5170 0.0081  0.0274  0.0185  79  LEU A CD1 
683  C  CD2 . LEU A 79  ? 0.1401 0.1333 0.3016 0.0248  -0.0135 0.0137  79  LEU A CD2 
684  N  N   . LYS A 80  ? 0.1570 0.1462 0.2381 -0.0342 -0.0249 -0.0087 80  LYS A N   
685  C  CA  . LYS A 80  ? 0.2378 0.1787 0.2545 -0.0024 0.0076  -0.0046 80  LYS A CA  
686  C  C   . LYS A 80  ? 0.1387 0.1624 0.2766 -0.0206 -0.0030 -0.0241 80  LYS A C   
687  O  O   . LYS A 80  ? 0.1545 0.1703 0.2863 -0.0432 0.0000  -0.0274 80  LYS A O   
688  C  CB  . LYS A 80  ? 0.2434 0.2143 0.3966 0.0582  -0.0147 -0.0608 80  LYS A CB  
689  C  CG  . LYS A 80  ? 0.2669 0.1791 0.3490 0.0252  0.0098  -0.0208 80  LYS A CG  
690  C  CD  . LYS A 80  ? 0.3041 0.2463 0.4742 0.0841  -0.0860 0.0219  80  LYS A CD  
691  C  CE  . LYS A 80  ? 0.4142 0.5615 0.6204 -0.0693 0.0225  -0.1650 80  LYS A CE  
692  N  NZ  . LYS A 80  ? 0.6711 0.9753 0.6241 0.0010  0.0124  -0.1040 80  LYS A NZ  
693  N  N   . GLY A 81  ? 0.2073 0.1870 0.2770 -0.0152 0.0350  -0.0285 81  GLY A N   
694  C  CA  . GLY A 81  ? 0.1638 0.1881 0.2849 0.0161  -0.0082 -0.0155 81  GLY A CA  
695  C  C   . GLY A 81  ? 0.1890 0.1956 0.2639 0.0535  0.0700  0.0333  81  GLY A C   
696  O  O   . GLY A 81  ? 0.1730 0.1507 0.3170 -0.0098 0.0261  -0.0208 81  GLY A O   
697  N  N   . GLY A 82  ? 0.1827 0.1541 0.4402 0.0297  0.0640  0.0458  82  GLY A N   
698  C  CA  . GLY A 82  ? 0.1793 0.1577 0.5212 0.0103  0.0626  0.0509  82  GLY A CA  
699  C  C   . GLY A 82  ? 0.2421 0.1279 0.3817 0.0885  0.0970  0.0243  82  GLY A C   
700  O  O   . GLY A 82  ? 0.3000 0.1999 0.4456 0.1140  0.1419  0.0142  82  GLY A O   
701  N  N   . PRO A 83  ? 0.2080 0.1221 0.4573 0.0687  0.0894  0.0013  83  PRO A N   
702  C  CA  . PRO A 83  ? 0.3120 0.1222 0.3944 0.0683  0.0675  -0.0102 83  PRO A CA  
703  C  C   . PRO A 83  ? 0.1629 0.1376 0.3689 0.0454  0.0263  -0.0217 83  PRO A C   
704  O  O   . PRO A 83  ? 0.2369 0.2265 0.4156 0.0040  -0.0381 -0.0003 83  PRO A O   
705  C  CB  . PRO A 83  ? 0.2730 0.1782 0.3231 0.0913  0.0131  0.0584  83  PRO A CB  
706  C  CG  . PRO A 83  ? 0.1622 0.1689 0.3088 0.0754  0.0074  0.0035  83  PRO A CG  
707  C  CD  . PRO A 83  ? 0.1500 0.0837 0.4736 0.0199  0.0557  -0.0087 83  PRO A CD  
708  N  N   . LEU A 84  ? 0.2125 0.1277 0.3032 0.0298  0.0575  -0.0054 84  LEU A N   
709  C  CA  . LEU A 84  ? 0.2224 0.0922 0.2921 0.0395  -0.0026 -0.0441 84  LEU A CA  
710  C  C   . LEU A 84  ? 0.2269 0.1290 0.2985 0.0357  0.0137  -0.0366 84  LEU A C   
711  O  O   . LEU A 84  ? 0.2416 0.1547 0.3346 0.0458  0.0449  -0.0478 84  LEU A O   
712  C  CB  . LEU A 84  ? 0.1405 0.1203 0.2687 0.0337  0.0126  -0.0436 84  LEU A CB  
713  C  CG  . LEU A 84  ? 0.1242 0.0807 0.3003 0.0219  -0.0153 -0.0373 84  LEU A CG  
714  C  CD1 . LEU A 84  ? 0.2005 0.1425 0.2809 0.0526  0.0119  -0.0656 84  LEU A CD1 
715  C  CD2 . LEU A 84  ? 0.1403 0.0785 0.3075 0.0254  0.0361  -0.0164 84  LEU A CD2 
716  N  N   A ASP A 85  ? 0.2639 0.1430 0.3217 -0.0192 0.0524  -0.0603 85  ASP A N   
717  N  N   B ASP A 85  ? 0.3339 0.1082 0.3411 0.0006  0.0137  -0.0956 85  ASP A N   
718  C  CA  A ASP A 85  ? 0.1953 0.1615 0.3000 0.0155  0.0063  -0.0427 85  ASP A CA  
719  C  CA  B ASP A 85  ? 0.3982 0.1933 0.3016 0.0935  0.0013  -0.1278 85  ASP A CA  
720  C  C   A ASP A 85  ? 0.1949 0.0951 0.2624 -0.0070 0.0155  -0.0952 85  ASP A C   
721  C  C   B ASP A 85  ? 0.4359 0.2840 0.2847 0.0195  0.0384  -0.0549 85  ASP A C   
722  O  O   A ASP A 85  ? 0.1863 0.0803 0.3079 0.0131  0.0428  -0.0390 85  ASP A O   
723  O  O   B ASP A 85  ? 0.3680 0.3172 0.4591 0.0540  0.0010  0.0186  85  ASP A O   
724  C  CB  A ASP A 85  ? 0.2102 0.0636 0.3603 0.0388  -0.0205 -0.0582 85  ASP A CB  
725  C  CB  B ASP A 85  ? 0.3731 0.3880 0.2254 0.0526  -0.0304 -0.0544 85  ASP A CB  
726  C  CG  A ASP A 85  ? 0.1771 0.1186 0.3580 -0.0258 0.0388  -0.0781 85  ASP A CG  
727  C  CG  B ASP A 85  ? 0.5432 0.4345 0.2511 0.0513  0.0282  -0.1611 85  ASP A CG  
728  O  OD1 A ASP A 85  ? 0.1674 0.3483 0.4372 -0.0640 0.0030  0.0549  85  ASP A OD1 
729  O  OD1 B ASP A 85  ? 0.5231 0.6646 0.5899 0.0417  0.2081  0.1956  85  ASP A OD1 
730  O  OD2 A ASP A 85  ? 0.2014 0.3016 0.4384 -0.1030 -0.0208 -0.0737 85  ASP A OD2 
731  O  OD2 B ASP A 85  ? 0.6233 0.1292 0.3605 -0.1207 -0.0183 0.0254  85  ASP A OD2 
732  N  N   A GLY A 86  ? 0.1911 0.1495 0.2851 0.0286  0.0500  -0.0886 86  GLY A N   
733  N  N   B GLY A 86  ? 0.4490 0.2443 0.3109 -0.0307 0.0960  -0.0225 86  GLY A N   
734  C  CA  A GLY A 86  ? 0.2017 0.0983 0.2951 0.0230  0.0680  -0.0590 86  GLY A CA  
735  C  CA  B GLY A 86  ? 0.3623 0.2177 0.3587 -0.1861 -0.0675 -0.0109 86  GLY A CA  
736  C  C   A GLY A 86  ? 0.1601 0.0812 0.2933 0.0847  0.0076  -0.0210 86  GLY A C   
737  C  C   B GLY A 86  ? 0.2624 0.2815 0.3183 -0.1544 -0.0318 0.0120  86  GLY A C   
738  O  O   A GLY A 86  ? 0.3490 0.2459 0.5723 -0.1212 0.1400  0.0763  86  GLY A O   
739  O  O   B GLY A 86  ? 0.2267 0.2452 0.3546 -0.1395 -0.1101 0.0419  86  GLY A O   
740  N  N   A THR A 87  ? 0.2260 0.1286 0.3273 0.1127  0.0456  -0.0087 87  THR A N   
741  N  N   B THR A 87  ? 0.2407 0.1611 0.2867 -0.0644 -0.0430 -0.0254 87  THR A N   
742  C  CA  A THR A 87  ? 0.0992 0.1486 0.3729 0.0601  0.0238  -0.0185 87  THR A CA  
743  C  CA  B THR A 87  ? 0.1976 0.1215 0.2949 0.0020  -0.0520 -0.0419 87  THR A CA  
744  C  C   A THR A 87  ? 0.0837 0.0573 0.3853 0.0272  0.0241  -0.0216 87  THR A C   
745  C  C   B THR A 87  ? 0.2486 0.0269 0.3438 0.0187  -0.0039 0.0013  87  THR A C   
746  O  O   A THR A 87  ? 0.0895 0.0450 0.2468 0.0164  -0.0182 -0.0175 87  THR A O   
747  O  O   B THR A 87  ? 0.2342 0.0333 0.1899 0.0324  -0.0258 -0.0159 87  THR A O   
748  C  CB  A THR A 87  ? 0.0658 0.1254 0.4499 0.0636  -0.0395 -0.0560 87  THR A CB  
749  C  CB  B THR A 87  ? 0.2292 0.1168 0.3176 -0.0003 0.0249  0.0522  87  THR A CB  
750  O  OG1 A THR A 87  ? 0.1480 0.1814 0.4837 0.0608  0.0214  -0.0922 87  THR A OG1 
751  O  OG1 B THR A 87  ? 0.1940 0.1326 0.3240 -0.0151 -0.0274 0.0229  87  THR A OG1 
752  C  CG2 A THR A 87  ? 0.1368 0.1281 0.4038 0.0723  -0.0825 -0.0318 87  THR A CG2 
753  C  CG2 B THR A 87  ? 0.1800 0.1096 0.3174 -0.0076 -0.0362 -0.0373 87  THR A CG2 
754  N  N   . TYR A 88  ? 0.1143 0.0662 0.3443 0.0326  -0.0153 -0.0263 88  TYR A N   
755  C  CA  . TYR A 88  ? 0.0886 0.0737 0.3197 0.0227  -0.0302 -0.0241 88  TYR A CA  
756  C  C   . TYR A 88  ? 0.0929 0.0806 0.2836 0.0130  -0.0531 -0.0059 88  TYR A C   
757  O  O   . TYR A 88  ? 0.1581 0.1632 0.3291 -0.0702 -0.0921 0.0364  88  TYR A O   
758  C  CB  . TYR A 88  ? 0.1622 0.0737 0.2407 0.0687  -0.0186 -0.0447 88  TYR A CB  
759  C  CG  . TYR A 88  ? 0.1538 0.0538 0.2441 0.0015  -0.0262 -0.0313 88  TYR A CG  
760  C  CD1 . TYR A 88  ? 0.1516 0.0573 0.2287 0.0049  -0.0126 -0.0135 88  TYR A CD1 
761  C  CD2 . TYR A 88  ? 0.1687 0.0412 0.2143 0.0170  -0.0185 0.0027  88  TYR A CD2 
762  C  CE1 . TYR A 88  ? 0.1798 0.0724 0.2479 0.0096  0.0263  -0.0221 88  TYR A CE1 
763  C  CE2 . TYR A 88  ? 0.1611 0.0315 0.1983 0.0026  0.0000  -0.0214 88  TYR A CE2 
764  C  CZ  . TYR A 88  ? 0.1640 0.0507 0.2096 0.0010  0.0060  -0.0287 88  TYR A CZ  
765  O  OH  . TYR A 88  ? 0.2071 0.0949 0.2199 0.0192  0.0013  -0.0518 88  TYR A OH  
766  N  N   A ARG A 89  ? 0.1337 0.0652 0.2773 0.0447  -0.0331 -0.0403 89  ARG A N   
767  N  N   B ARG A 89  ? 0.0965 0.0533 0.2840 0.0324  -0.0335 -0.0340 89  ARG A N   
768  C  CA  A ARG A 89  ? 0.2232 0.0477 0.2707 0.0663  -0.0595 -0.0151 89  ARG A CA  
769  C  CA  B ARG A 89  ? 0.0412 0.0812 0.2885 0.0153  -0.0573 -0.0102 89  ARG A CA  
770  C  C   A ARG A 89  ? 0.0855 0.0653 0.2308 0.0232  -0.0533 -0.0076 89  ARG A C   
771  C  C   B ARG A 89  ? 0.0749 0.0423 0.2894 -0.0126 -0.0315 0.0035  89  ARG A C   
772  O  O   A ARG A 89  ? 0.0847 0.0388 0.2363 0.0183  -0.0478 0.0010  89  ARG A O   
773  O  O   B ARG A 89  ? 0.0820 0.0430 0.2231 0.0015  -0.0386 0.0076  89  ARG A O   
774  C  CB  A ARG A 89  ? 0.1444 0.0315 0.3373 0.0229  -0.0982 0.0011  89  ARG A CB  
775  C  CB  B ARG A 89  ? 0.2438 0.0342 0.2910 0.0436  -0.1288 -0.0302 89  ARG A CB  
776  C  CG  A ARG A 89  ? 0.2069 0.0412 0.2477 0.0463  -0.0938 0.0026  89  ARG A CG  
777  C  CG  B ARG A 89  ? 0.2962 0.0643 0.2081 -0.0458 -0.1036 0.0842  89  ARG A CG  
778  C  CD  A ARG A 89  ? 0.2935 0.1386 0.2930 0.0557  -0.1172 0.1238  89  ARG A CD  
779  C  CD  B ARG A 89  ? 0.4591 0.2236 0.4329 0.0798  -0.2161 0.0034  89  ARG A CD  
780  N  NE  A ARG A 89  ? 0.2168 0.1136 0.1800 0.0071  -0.0331 -0.0370 89  ARG A NE  
781  N  NE  B ARG A 89  ? 0.6804 0.0467 0.4905 0.0216  -0.2433 0.0115  89  ARG A NE  
782  C  CZ  A ARG A 89  ? 0.2626 0.1012 0.3248 0.0636  -0.0527 0.0351  89  ARG A CZ  
783  C  CZ  B ARG A 89  ? 0.1163 0.1109 0.5600 0.0879  -0.1645 -0.1483 89  ARG A CZ  
784  N  NH1 A ARG A 89  ? 0.3203 0.1197 0.1888 0.0469  -0.0627 -0.0137 89  ARG A NH1 
785  N  NH1 B ARG A 89  ? 0.1897 0.1653 0.2199 -0.0631 -0.0603 0.0238  89  ARG A NH1 
786  N  NH2 A ARG A 89  ? 0.4083 0.0288 0.3836 0.0364  0.0107  0.0058  89  ARG A NH2 
787  N  NH2 B ARG A 89  ? 0.3707 0.2594 0.4077 0.0824  -0.0428 0.0098  89  ARG A NH2 
788  N  N   . LEU A 90  ? 0.1150 0.0454 0.2199 0.0136  -0.0465 -0.0104 90  LEU A N   
789  C  CA  . LEU A 90  ? 0.1021 0.0546 0.2041 0.0060  -0.0425 0.0010  90  LEU A CA  
790  C  C   . LEU A 90  ? 0.0992 0.0471 0.2093 0.0203  -0.0476 0.0093  90  LEU A C   
791  O  O   . LEU A 90  ? 0.1194 0.0894 0.2517 0.0013  -0.0568 0.0493  90  LEU A O   
792  C  CB  . LEU A 90  ? 0.1023 0.0577 0.2272 0.0153  -0.0573 -0.0081 90  LEU A CB  
793  C  CG  . LEU A 90  ? 0.1317 0.0702 0.1929 0.0071  -0.0577 -0.0153 90  LEU A CG  
794  C  CD1 . LEU A 90  ? 0.1545 0.0665 0.2050 -0.0046 -0.0636 0.0023  90  LEU A CD1 
795  C  CD2 . LEU A 90  ? 0.1310 0.0921 0.2278 -0.0273 -0.0465 -0.0120 90  LEU A CD2 
796  N  N   . THR A 91  ? 0.0920 0.0467 0.1935 0.0062  -0.0305 -0.0087 91  THR A N   
797  C  CA  . THR A 91  ? 0.1237 0.0529 0.1962 0.0048  -0.0452 -0.0046 91  THR A CA  
798  C  C   . THR A 91  ? 0.0913 0.0371 0.1696 0.0085  -0.0577 0.0000  91  THR A C   
799  O  O   . THR A 91  ? 0.1249 0.0627 0.1665 -0.0027 -0.0531 0.0160  91  THR A O   
800  C  CB  . THR A 91  ? 0.1206 0.0920 0.2002 -0.0126 -0.0553 -0.0013 91  THR A CB  
801  O  OG1 . THR A 91  ? 0.1608 0.1588 0.2578 -0.0864 -0.0675 0.0575  91  THR A OG1 
802  C  CG2 . THR A 91  ? 0.1430 0.0864 0.2037 -0.0254 -0.0763 -0.0054 91  THR A CG2 
803  N  N   . GLN A 92  ? 0.1097 0.0348 0.1951 0.0054  -0.0527 0.0019  92  GLN A N   
804  C  CA  . GLN A 92  ? 0.1014 0.0419 0.1714 -0.0054 -0.0260 0.0068  92  GLN A CA  
805  C  C   . GLN A 92  ? 0.0895 0.0415 0.1802 -0.0087 -0.0260 0.0060  92  GLN A C   
806  O  O   . GLN A 92  ? 0.1242 0.0302 0.1651 0.0080  -0.0217 0.0013  92  GLN A O   
807  C  CB  . GLN A 92  ? 0.0912 0.0885 0.2029 -0.0082 -0.0204 -0.0027 92  GLN A CB  
808  C  CG  . GLN A 92  ? 0.0949 0.0754 0.2084 -0.0035 -0.0417 -0.0074 92  GLN A CG  
809  C  CD  . GLN A 92  ? 0.1062 0.0994 0.2111 -0.0063 -0.0353 0.0019  92  GLN A CD  
810  O  OE1 . GLN A 92  ? 0.0985 0.2114 0.3467 0.0185  -0.0482 0.0141  92  GLN A OE1 
811  N  NE2 . GLN A 92  ? 0.1010 0.0653 0.1877 0.0153  -0.0364 0.0230  92  GLN A NE2 
812  N  N   . PHE A 93  ? 0.0728 0.0297 0.1976 0.0142  -0.0322 -0.0054 93  PHE A N   
813  C  CA  . PHE A 93  ? 0.0715 0.0375 0.1993 0.0109  -0.0253 0.0043  93  PHE A CA  
814  C  C   . PHE A 93  ? 0.0649 0.0535 0.1638 0.0041  -0.0454 0.0020  93  PHE A C   
815  O  O   . PHE A 93  ? 0.0794 0.0590 0.1617 0.0027  -0.0362 0.0013  93  PHE A O   
816  C  CB  . PHE A 93  ? 0.0658 0.0564 0.1617 0.0026  -0.0252 0.0020  93  PHE A CB  
817  C  CG  . PHE A 93  ? 0.0702 0.0421 0.1746 -0.0043 -0.0197 0.0086  93  PHE A CG  
818  C  CD1 . PHE A 93  ? 0.0882 0.0502 0.2003 -0.0068 -0.0357 -0.0115 93  PHE A CD1 
819  C  CD2 . PHE A 93  ? 0.0965 0.0482 0.1841 0.0065  -0.0207 0.0274  93  PHE A CD2 
820  C  CE1 . PHE A 93  ? 0.0860 0.0626 0.2021 -0.0073 -0.0432 -0.0031 93  PHE A CE1 
821  C  CE2 . PHE A 93  ? 0.0960 0.0631 0.1800 -0.0108 -0.0171 0.0227  93  PHE A CE2 
822  C  CZ  . PHE A 93  ? 0.0812 0.0406 0.2023 0.0006  -0.0240 0.0170  93  PHE A CZ  
823  N  N   . HIS A 94  ? 0.0688 0.0326 0.1755 0.0059  -0.0384 0.0013  94  HIS A N   
824  C  CA  . HIS A 94  ? 0.0697 0.0741 0.1737 0.0131  -0.0263 0.0065  94  HIS A CA  
825  C  C   . HIS A 94  ? 0.0816 0.0467 0.1642 0.0230  -0.0458 -0.0076 94  HIS A C   
826  O  O   . HIS A 94  ? 0.0983 0.0423 0.1728 0.0270  -0.0270 -0.0037 94  HIS A O   
827  C  CB  . HIS A 94  ? 0.0702 0.0648 0.1949 0.0125  -0.0419 -0.0229 94  HIS A CB  
828  C  CG  . HIS A 94  ? 0.0715 0.0559 0.1836 -0.0030 -0.0498 -0.0109 94  HIS A CG  
829  N  ND1 . HIS A 94  ? 0.0718 0.0529 0.1671 -0.0006 -0.0181 0.0020  94  HIS A ND1 
830  C  CD2 . HIS A 94  ? 0.0441 0.1010 0.1498 0.0085  -0.0322 -0.0043 94  HIS A CD2 
831  C  CE1 . HIS A 94  ? 0.0732 0.0509 0.1843 0.0068  -0.0472 0.0096  94  HIS A CE1 
832  N  NE2 . HIS A 94  ? 0.0697 0.0838 0.1644 0.0241  -0.0684 0.0015  94  HIS A NE2 
833  N  N   . PHE A 95  ? 0.0727 0.0509 0.1974 0.0186  -0.0439 -0.0274 95  PHE A N   
834  C  CA  . PHE A 95  ? 0.0640 0.0280 0.2381 0.0086  -0.0410 -0.0206 95  PHE A CA  
835  C  C   . PHE A 95  ? 0.0662 0.0719 0.1870 0.0131  -0.0373 -0.0197 95  PHE A C   
836  O  O   . PHE A 95  ? 0.0810 0.0666 0.1935 0.0162  -0.0281 -0.0026 95  PHE A O   
837  C  CB  . PHE A 95  ? 0.0687 0.0702 0.2342 0.0010  -0.0522 -0.0272 95  PHE A CB  
838  C  CG  . PHE A 95  ? 0.0701 0.0732 0.2213 0.0181  -0.0439 -0.0460 95  PHE A CG  
839  C  CD1 . PHE A 95  ? 0.0966 0.0812 0.2263 0.0259  -0.0662 -0.0322 95  PHE A CD1 
840  C  CD2 . PHE A 95  ? 0.0715 0.0706 0.2451 0.0130  -0.0274 -0.0375 95  PHE A CD2 
841  C  CE1 . PHE A 95  ? 0.0847 0.1062 0.2339 0.0252  -0.0496 -0.0428 95  PHE A CE1 
842  C  CE2 . PHE A 95  ? 0.0900 0.0929 0.2578 0.0399  -0.0439 -0.0366 95  PHE A CE2 
843  C  CZ  . PHE A 95  ? 0.0763 0.1003 0.2486 0.0421  -0.0500 -0.0559 95  PHE A CZ  
844  N  N   . HIS A 96  ? 0.0754 0.0309 0.2193 0.0147  -0.0281 -0.0181 96  HIS A N   
845  C  CA  . HIS A 96  ? 0.0671 0.0335 0.1896 0.0175  -0.0355 -0.0253 96  HIS A CA  
846  C  C   . HIS A 96  ? 0.0573 0.0403 0.2019 0.0142  -0.0296 -0.0221 96  HIS A C   
847  O  O   . HIS A 96  ? 0.0671 0.0384 0.2330 0.0131  -0.0259 -0.0164 96  HIS A O   
848  C  CB  . HIS A 96  ? 0.0992 0.0406 0.2046 0.0063  -0.0441 -0.0208 96  HIS A CB  
849  C  CG  . HIS A 96  ? 0.0656 0.0326 0.2195 0.0109  -0.0538 0.0082  96  HIS A CG  
850  N  ND1 . HIS A 96  ? 0.0640 0.0421 0.2463 -0.0027 -0.0296 -0.0253 96  HIS A ND1 
851  C  CD2 . HIS A 96  ? 0.0921 0.0254 0.2099 0.0013  -0.0502 0.0034  96  HIS A CD2 
852  C  CE1 . HIS A 96  ? 0.0714 0.0534 0.2071 0.0337  -0.0394 -0.0193 96  HIS A CE1 
853  N  NE2 . HIS A 96  ? 0.0754 0.0287 0.2283 0.0065  -0.0364 0.0031  96  HIS A NE2 
854  N  N   . TRP A 97  ? 0.0653 0.0397 0.2046 0.0230  -0.0430 -0.0370 97  TRP A N   
855  C  CA  . TRP A 97  ? 0.0688 0.0385 0.2300 0.0219  -0.0564 -0.0449 97  TRP A CA  
856  C  C   . TRP A 97  ? 0.0737 0.0474 0.2195 0.0252  -0.0386 -0.0471 97  TRP A C   
857  O  O   . TRP A 97  ? 0.0784 0.0458 0.2363 0.0259  -0.0326 -0.0292 97  TRP A O   
858  C  CB  . TRP A 97  ? 0.1044 0.0419 0.2213 0.0329  -0.0549 -0.0439 97  TRP A CB  
859  C  CG  . TRP A 97  ? 0.0838 0.0640 0.2272 0.0270  -0.0597 -0.0414 97  TRP A CG  
860  C  CD1 . TRP A 97  ? 0.1023 0.1039 0.2328 0.0454  -0.0557 -0.0548 97  TRP A CD1 
861  C  CD2 . TRP A 97  ? 0.0658 0.0860 0.2026 0.0296  -0.0465 -0.0307 97  TRP A CD2 
862  N  NE1 . TRP A 97  ? 0.1342 0.0944 0.2326 0.0643  -0.0679 -0.0456 97  TRP A NE1 
863  C  CE2 . TRP A 97  ? 0.0886 0.0987 0.2111 0.0414  -0.0586 -0.0342 97  TRP A CE2 
864  C  CE3 . TRP A 97  ? 0.0719 0.0680 0.2303 0.0208  -0.0381 -0.0283 97  TRP A CE3 
865  C  CZ2 . TRP A 97  ? 0.0816 0.1185 0.2199 0.0417  -0.0494 -0.0359 97  TRP A CZ2 
866  C  CZ3 . TRP A 97  ? 0.0886 0.0948 0.2143 0.0273  -0.0335 -0.0304 97  TRP A CZ3 
867  C  CH2 . TRP A 97  ? 0.0976 0.1014 0.2053 0.0295  -0.0476 -0.0236 97  TRP A CH2 
868  N  N   . GLY A 98  ? 0.0899 0.0363 0.2257 0.0247  -0.0496 -0.0345 98  GLY A N   
869  C  CA  . GLY A 98  ? 0.0926 0.0386 0.2788 0.0252  -0.0529 -0.0405 98  GLY A CA  
870  C  C   . GLY A 98  ? 0.1313 0.0569 0.2682 0.0397  -0.0604 -0.0719 98  GLY A C   
871  O  O   . GLY A 98  ? 0.1699 0.0599 0.2750 0.0353  -0.0684 -0.0388 98  GLY A O   
872  N  N   . SER A 99  ? 0.1605 0.0671 0.2955 0.0671  -0.0548 -0.0724 99  SER A N   
873  C  CA  . SER A 99  ? 0.1863 0.0891 0.3167 0.0881  -0.0666 -0.0957 99  SER A CA  
874  C  C   . SER A 99  ? 0.2296 0.0851 0.3673 0.0741  -0.1054 -0.0917 99  SER A C   
875  O  O   . SER A 99  ? 0.3680 0.1168 0.4043 0.0652  -0.1720 -0.1115 99  SER A O   
876  C  CB  . SER A 99  ? 0.1865 0.1405 0.3109 0.1155  -0.0913 -0.1054 99  SER A CB  
877  O  OG  . SER A 99  ? 0.1888 0.1093 0.3524 0.1171  -0.1032 -0.0775 99  SER A OG  
878  N  N   . LEU A 100 ? 0.1057 0.0781 0.4586 0.0208  -0.0737 -0.0864 100 LEU A N   
879  C  CA  . LEU A 100 ? 0.1660 0.0838 0.5343 0.0081  -0.0724 -0.0934 100 LEU A CA  
880  C  C   . LEU A 100 ? 0.1279 0.0838 0.4828 0.0131  -0.0524 -0.0806 100 LEU A C   
881  O  O   . LEU A 100 ? 0.1513 0.0684 0.4984 0.0252  -0.0719 -0.0864 100 LEU A O   
882  C  CB  . LEU A 100 ? 0.3346 0.0960 0.7038 0.0979  0.0006  -0.0551 100 LEU A CB  
883  C  CG  . LEU A 100 ? 0.4219 0.2348 0.6628 0.0522  -0.0154 0.1897  100 LEU A CG  
884  C  CD1 . LEU A 100 ? 0.4253 0.2477 0.6624 0.0606  0.0082  0.0087  100 LEU A CD1 
885  C  CD2 . LEU A 100 ? 0.6172 0.2872 0.9211 0.0328  0.1993  -0.0269 100 LEU A CD2 
886  N  N   . ASP A 101 ? 0.1353 0.0680 0.5964 0.0242  -0.0582 -0.0577 101 ASP A N   
887  C  CA  . ASP A 101 ? 0.1109 0.0768 0.4528 0.0215  -0.0728 -0.0209 101 ASP A CA  
888  C  C   . ASP A 101 ? 0.1753 0.0666 0.4668 -0.0274 -0.1023 0.0237  101 ASP A C   
889  O  O   . ASP A 101 ? 0.2226 0.0864 0.5449 0.0186  -0.0772 0.0059  101 ASP A O   
890  C  CB  . ASP A 101 ? 0.1960 0.0326 0.4609 -0.0254 -0.1096 0.0204  101 ASP A CB  
891  C  CG  . ASP A 101 ? 0.1032 0.1641 0.4077 0.0000  -0.0423 -0.0048 101 ASP A CG  
892  O  OD1 . ASP A 101 ? 0.1712 0.1579 0.3905 -0.0214 -0.0177 -0.0368 101 ASP A OD1 
893  O  OD2 . ASP A 101 ? 0.2014 0.1809 0.5220 -0.0614 -0.1412 0.0015  101 ASP A OD2 
894  N  N   . GLY A 102 ? 0.1403 0.0841 0.4034 -0.0006 -0.1049 -0.0390 102 GLY A N   
895  C  CA  . GLY A 102 ? 0.2087 0.0502 0.4765 -0.0428 -0.1098 0.0489  102 GLY A CA  
896  C  C   . GLY A 102 ? 0.1541 0.0471 0.3388 0.0012  -0.0846 0.0208  102 GLY A C   
897  O  O   . GLY A 102 ? 0.1829 0.0842 0.4180 -0.0087 -0.0926 0.0557  102 GLY A O   
898  N  N   . GLN A 103 ? 0.1070 0.0353 0.4318 0.0031  -0.0304 0.0287  103 GLN A N   
899  C  CA  . GLN A 103 ? 0.1240 0.0336 0.3650 0.0276  -0.0419 0.0020  103 GLN A CA  
900  C  C   . GLN A 103 ? 0.1075 0.0357 0.2897 0.0006  -0.0230 -0.0131 103 GLN A C   
901  O  O   . GLN A 103 ? 0.1084 0.0502 0.2901 0.0163  -0.0432 -0.0183 103 GLN A O   
902  C  CB  . GLN A 103 ? 0.1261 0.0544 0.2831 0.0296  -0.0309 -0.0060 103 GLN A CB  
903  C  CG  . GLN A 103 ? 0.1428 0.0790 0.2766 0.0524  -0.0049 -0.0059 103 GLN A CG  
904  C  CD  . GLN A 103 ? 0.1791 0.1088 0.2838 0.0606  -0.0141 -0.0096 103 GLN A CD  
905  O  OE1 . GLN A 103 ? 0.1738 0.1265 0.3190 0.0588  0.0126  -0.0020 103 GLN A OE1 
906  N  NE2 . GLN A 103 ? 0.1987 0.2357 0.4128 0.1720  0.0781  0.1238  103 GLN A NE2 
907  N  N   . GLY A 104 ? 0.0758 0.0296 0.3032 0.0146  -0.0269 -0.0052 104 GLY A N   
908  C  CA  . GLY A 104 ? 0.0938 0.0377 0.2527 0.0208  -0.0427 -0.0241 104 GLY A CA  
909  C  C   . GLY A 104 ? 0.0608 0.0397 0.2321 0.0129  -0.0500 -0.0109 104 GLY A C   
910  O  O   . GLY A 104 ? 0.0825 0.0450 0.2396 0.0024  -0.0423 0.0017  104 GLY A O   
911  N  N   . SER A 105 ? 0.0702 0.0520 0.2366 0.0098  -0.0315 -0.0130 105 SER A N   
912  C  CA  . SER A 105 ? 0.0797 0.0388 0.2382 0.0148  -0.0368 -0.0198 105 SER A CA  
913  C  C   . SER A 105 ? 0.0626 0.0375 0.2215 -0.0017 -0.0164 -0.0017 105 SER A C   
914  O  O   . SER A 105 ? 0.0816 0.0529 0.2606 0.0109  -0.0480 -0.0177 105 SER A O   
915  C  CB  . SER A 105 ? 0.0886 0.0678 0.2405 0.0041  -0.0469 0.0054  105 SER A CB  
916  O  OG  . SER A 105 ? 0.1027 0.0306 0.2558 -0.0010 -0.0357 0.0031  105 SER A OG  
917  N  N   . GLU A 106 ? 0.0806 0.0265 0.2069 -0.0080 -0.0346 0.0035  106 GLU A N   
918  C  CA  . GLU A 106 ? 0.0894 0.0432 0.1902 0.0104  -0.0509 -0.0118 106 GLU A CA  
919  C  C   . GLU A 106 ? 0.0803 0.0458 0.2035 0.0006  -0.0524 0.0043  106 GLU A C   
920  O  O   . GLU A 106 ? 0.0731 0.0671 0.1942 0.0152  -0.0403 0.0074  106 GLU A O   
921  C  CB  . GLU A 106 ? 0.1021 0.0414 0.1990 -0.0131 -0.0410 -0.0115 106 GLU A CB  
922  C  CG  . GLU A 106 ? 0.1208 0.0474 0.2098 0.0010  -0.0307 -0.0166 106 GLU A CG  
923  C  CD  . GLU A 106 ? 0.0644 0.0590 0.1868 0.0219  -0.0303 -0.0174 106 GLU A CD  
924  O  OE1 . GLU A 106 ? 0.0623 0.0546 0.2224 0.0098  -0.0405 -0.0163 106 GLU A OE1 
925  O  OE2 . GLU A 106 ? 0.0732 0.0627 0.2405 0.0196  -0.0260 -0.0153 106 GLU A OE2 
926  N  N   . HIS A 107 ? 0.0860 0.0270 0.2108 0.0096  -0.0333 -0.0098 107 HIS A N   
927  C  CA  . HIS A 107 ? 0.0832 0.0500 0.1967 0.0109  -0.0370 -0.0164 107 HIS A CA  
928  C  C   . HIS A 107 ? 0.0798 0.0644 0.2021 0.0010  -0.0292 -0.0027 107 HIS A C   
929  O  O   . HIS A 107 ? 0.0834 0.0446 0.2229 0.0125  -0.0414 -0.0012 107 HIS A O   
930  C  CB  . HIS A 107 ? 0.0882 0.0339 0.2294 0.0027  -0.0303 -0.0147 107 HIS A CB  
931  C  CG  . HIS A 107 ? 0.0577 0.0362 0.2278 0.0093  -0.0309 -0.0019 107 HIS A CG  
932  N  ND1 . HIS A 107 ? 0.0908 0.0370 0.2224 0.0054  -0.0410 0.0015  107 HIS A ND1 
933  C  CD2 . HIS A 107 ? 0.0869 0.0366 0.2305 0.0006  -0.0241 -0.0087 107 HIS A CD2 
934  C  CE1 . HIS A 107 ? 0.0925 0.0465 0.1938 0.0012  -0.0331 -0.0046 107 HIS A CE1 
935  N  NE2 . HIS A 107 ? 0.0838 0.0306 0.1881 -0.0003 -0.0366 -0.0136 107 HIS A NE2 
936  N  N   . THR A 108 ? 0.1030 0.0526 0.2190 0.0087  -0.0240 0.0153  108 THR A N   
937  C  CA  . THR A 108 ? 0.0942 0.0300 0.2495 0.0076  -0.0186 0.0010  108 THR A CA  
938  C  C   . THR A 108 ? 0.0982 0.0485 0.2123 -0.0005 -0.0518 0.0107  108 THR A C   
939  O  O   . THR A 108 ? 0.1046 0.0653 0.2346 0.0041  -0.0264 0.0074  108 THR A O   
940  C  CB  . THR A 108 ? 0.0869 0.0684 0.2493 0.0148  -0.0410 -0.0043 108 THR A CB  
941  O  OG1 . THR A 108 ? 0.0929 0.0573 0.2583 0.0020  -0.0430 0.0076  108 THR A OG1 
942  C  CG2 . THR A 108 ? 0.0942 0.0749 0.2626 0.0074  -0.0219 0.0035  108 THR A CG2 
943  N  N   . VAL A 109 ? 0.0921 0.0546 0.2560 0.0060  -0.0185 0.0263  109 VAL A N   
944  C  CA  . VAL A 109 ? 0.1054 0.0471 0.2867 -0.0104 -0.0130 0.0346  109 VAL A CA  
945  C  C   . VAL A 109 ? 0.1127 0.0377 0.2851 -0.0227 -0.0006 0.0250  109 VAL A C   
946  O  O   . VAL A 109 ? 0.1123 0.0386 0.3278 -0.0082 -0.0142 0.0285  109 VAL A O   
947  C  CB  . VAL A 109 ? 0.1012 0.0741 0.2960 0.0098  -0.0217 0.0062  109 VAL A CB  
948  C  CG1 . VAL A 109 ? 0.1365 0.0803 0.3167 0.0115  -0.0071 0.0537  109 VAL A CG1 
949  C  CG2 . VAL A 109 ? 0.1563 0.1005 0.2583 0.0276  -0.0467 0.0092  109 VAL A CG2 
950  N  N   . ASP A 110 ? 0.1595 0.0736 0.2495 0.0120  -0.0175 0.0405  110 ASP A N   
951  C  CA  . ASP A 110 ? 0.1608 0.0746 0.2863 0.0305  0.0019  0.0546  110 ASP A CA  
952  C  C   . ASP A 110 ? 0.1683 0.0590 0.3152 0.0328  0.0155  0.0553  110 ASP A C   
953  O  O   . ASP A 110 ? 0.1841 0.0666 0.3395 0.0151  -0.0276 0.0511  110 ASP A O   
954  C  CB  . ASP A 110 ? 0.1960 0.1054 0.3379 0.0353  0.0324  0.0741  110 ASP A CB  
955  C  CG  . ASP A 110 ? 0.2050 0.1208 0.3307 0.0531  0.0296  0.0860  110 ASP A CG  
956  O  OD1 . ASP A 110 ? 0.1865 0.1362 0.4239 0.0362  0.0405  0.0878  110 ASP A OD1 
957  O  OD2 . ASP A 110 ? 0.1967 0.2484 0.3497 0.0666  0.0287  0.0674  110 ASP A OD2 
958  N  N   . LYS A 111 ? 0.1193 0.0825 0.2477 0.0151  -0.0209 0.0220  111 LYS A N   
959  C  CA  . LYS A 111 ? 0.1181 0.0746 0.2795 0.0184  -0.0164 0.0098  111 LYS A CA  
960  C  C   . LYS A 111 ? 0.1299 0.0388 0.3125 0.0164  -0.0379 0.0142  111 LYS A C   
961  O  O   . LYS A 111 ? 0.1308 0.0921 0.3023 0.0230  -0.0241 0.0000  111 LYS A O   
962  C  CB  . LYS A 111 ? 0.1425 0.1527 0.3194 0.0579  -0.0296 0.0377  111 LYS A CB  
963  C  CG  . LYS A 111 ? 0.2441 0.2594 0.3100 0.0368  -0.0709 0.0395  111 LYS A CG  
964  C  CD  . LYS A 111 ? 0.2017 0.2378 0.4241 0.0784  -0.0688 -0.0505 111 LYS A CD  
965  C  CE  . LYS A 111 ? 0.2441 0.7116 0.5601 0.0196  -0.2231 -0.1084 111 LYS A CE  
966  N  NZ  . LYS A 111 ? 0.3091 0.3804 0.4370 -0.0623 -0.0913 0.0631  111 LYS A NZ  
967  N  N   . LYS A 112 ? 0.1335 0.0555 0.2942 0.0192  -0.0562 0.0248  112 LYS A N   
968  C  CA  . LYS A 112 ? 0.1057 0.0956 0.3190 0.0000  -0.0540 0.0275  112 LYS A CA  
969  C  C   . LYS A 112 ? 0.1039 0.0502 0.3091 0.0087  -0.0438 0.0076  112 LYS A C   
970  O  O   . LYS A 112 ? 0.1127 0.0458 0.3176 0.0035  -0.0353 -0.0074 112 LYS A O   
971  C  CB  . LYS A 112 ? 0.1237 0.0960 0.3761 -0.0307 -0.0296 0.0120  112 LYS A CB  
972  C  CG  . LYS A 112 ? 0.1491 0.1168 0.4013 0.0000  -0.1075 -0.0276 112 LYS A CG  
973  C  CD  . LYS A 112 ? 0.1658 0.1617 0.3864 0.0286  -0.0631 0.0335  112 LYS A CD  
974  C  CE  . LYS A 112 ? 0.3364 0.1450 0.4086 -0.0438 -0.1550 0.0436  112 LYS A CE  
975  N  NZ  . LYS A 112 ? 0.4388 0.1757 0.5342 -0.0237 -0.1888 0.0608  112 LYS A NZ  
976  N  N   A LYS A 113 ? 0.1012 0.0688 0.2921 0.0518  -0.0498 0.0086  113 LYS A N   
977  N  N   B LYS A 113 ? 0.1048 0.0754 0.3003 -0.0176 -0.0573 -0.0109 113 LYS A N   
978  C  CA  A LYS A 113 ? 0.1265 0.1315 0.2448 0.0362  -0.0483 0.0049  113 LYS A CA  
979  C  CA  B LYS A 113 ? 0.1190 0.0305 0.2926 0.0166  -0.0487 -0.0115 113 LYS A CA  
980  C  C   A LYS A 113 ? 0.1642 0.0447 0.2685 0.0137  -0.0700 0.0076  113 LYS A C   
981  C  C   B LYS A 113 ? 0.0904 0.0257 0.3207 0.0051  -0.0509 -0.0051 113 LYS A C   
982  O  O   A LYS A 113 ? 0.1405 0.0608 0.2303 0.0024  -0.0397 0.0203  113 LYS A O   
983  O  O   B LYS A 113 ? 0.1574 0.0258 0.2703 -0.0076 -0.0366 0.0038  113 LYS A O   
984  C  CB  A LYS A 113 ? 0.1193 0.0388 0.2657 0.0322  -0.0679 -0.0203 113 LYS A CB  
985  C  CB  B LYS A 113 ? 0.1023 0.0379 0.3174 -0.0215 -0.0408 0.0148  113 LYS A CB  
986  C  CG  A LYS A 113 ? 0.1353 0.0456 0.2500 0.0463  -0.0812 -0.0231 113 LYS A CG  
987  C  CG  B LYS A 113 ? 0.1019 0.1270 0.2481 -0.0065 -0.0370 -0.0197 113 LYS A CG  
988  C  CD  A LYS A 113 ? 0.1277 0.0940 0.2601 0.0458  -0.0926 -0.0872 113 LYS A CD  
989  C  CD  B LYS A 113 ? 0.1577 0.0489 0.2346 0.0177  -0.0423 -0.0344 113 LYS A CD  
990  C  CE  A LYS A 113 ? 0.1324 0.0983 0.2872 0.0634  -0.1089 -0.0702 113 LYS A CE  
991  C  CE  B LYS A 113 ? 0.2064 0.0603 0.2623 -0.0184 -0.0762 -0.0085 113 LYS A CE  
992  N  NZ  A LYS A 113 ? 0.1430 0.1001 0.3190 0.0397  -0.1168 -0.0386 113 LYS A NZ  
993  N  NZ  B LYS A 113 ? 0.1791 0.1723 0.3476 0.0375  -0.0768 0.0469  113 LYS A NZ  
994  N  N   . TYR A 114 ? 0.0964 0.0394 0.2603 0.0159  -0.0557 -0.0040 114 TYR A N   
995  C  CA  . TYR A 114 ? 0.1012 0.0467 0.2257 0.0059  -0.0507 -0.0130 114 TYR A CA  
996  C  C   . TYR A 114 ? 0.1039 0.0362 0.2448 0.0054  -0.0560 -0.0192 114 TYR A C   
997  O  O   . TYR A 114 ? 0.0741 0.0507 0.2799 0.0082  -0.0507 -0.0057 114 TYR A O   
998  C  CB  . TYR A 114 ? 0.0929 0.0483 0.2574 0.0020  -0.0524 -0.0068 114 TYR A CB  
999  C  CG  . TYR A 114 ? 0.1001 0.0456 0.2439 0.0307  -0.0383 0.0109  114 TYR A CG  
1000 C  CD1 . TYR A 114 ? 0.1484 0.0807 0.2364 0.0209  -0.0476 0.0322  114 TYR A CD1 
1001 C  CD2 . TYR A 114 ? 0.1317 0.0309 0.3118 0.0006  -0.0317 0.0115  114 TYR A CD2 
1002 C  CE1 . TYR A 114 ? 0.2335 0.1306 0.2445 0.0640  -0.0126 0.0063  114 TYR A CE1 
1003 C  CE2 . TYR A 114 ? 0.1316 0.1124 0.2998 -0.0003 -0.0210 0.0436  114 TYR A CE2 
1004 C  CZ  . TYR A 114 ? 0.2143 0.1759 0.2955 0.0586  -0.0214 0.0592  114 TYR A CZ  
1005 O  OH  . TYR A 114 ? 0.2944 0.3752 0.3467 0.0383  -0.0076 0.0983  114 TYR A OH  
1006 N  N   . ALA A 115 ? 0.1071 0.0344 0.2466 0.0183  -0.0658 -0.0292 115 ALA A N   
1007 C  CA  . ALA A 115 ? 0.1055 0.0291 0.2504 0.0006  -0.0535 -0.0204 115 ALA A CA  
1008 C  C   . ALA A 115 ? 0.0960 0.0348 0.2617 0.0164  -0.0423 -0.0249 115 ALA A C   
1009 O  O   . ALA A 115 ? 0.1012 0.0410 0.2648 0.0070  -0.0287 -0.0379 115 ALA A O   
1010 C  CB  . ALA A 115 ? 0.0966 0.0665 0.3018 0.0013  -0.0688 -0.0454 115 ALA A CB  
1011 N  N   . ALA A 116 ? 0.0926 0.0289 0.2299 0.0000  -0.0436 -0.0250 116 ALA A N   
1012 C  CA  . ALA A 116 ? 0.0994 0.0306 0.2301 0.0160  -0.0390 -0.0264 116 ALA A CA  
1013 C  C   . ALA A 116 ? 0.0577 0.0371 0.1993 0.0135  -0.0430 -0.0164 116 ALA A C   
1014 O  O   . ALA A 116 ? 0.0763 0.0446 0.2129 -0.0023 -0.0383 -0.0074 116 ALA A O   
1015 C  CB  . ALA A 116 ? 0.0969 0.0625 0.2096 0.0000  -0.0544 -0.0263 116 ALA A CB  
1016 N  N   . GLU A 117 ? 0.0900 0.0317 0.2102 0.0200  -0.0491 -0.0183 117 GLU A N   
1017 C  CA  . GLU A 117 ? 0.0994 0.0359 0.2096 0.0279  -0.0540 -0.0232 117 GLU A CA  
1018 C  C   . GLU A 117 ? 0.0657 0.0403 0.2069 0.0031  -0.0340 -0.0068 117 GLU A C   
1019 O  O   . GLU A 117 ? 0.0766 0.0423 0.2236 0.0294  -0.0119 -0.0046 117 GLU A O   
1020 C  CB  . GLU A 117 ? 0.1172 0.0439 0.1942 0.0087  -0.0489 -0.0307 117 GLU A CB  
1021 C  CG  . GLU A 117 ? 0.0754 0.0370 0.2082 0.0093  -0.0535 -0.0163 117 GLU A CG  
1022 C  CD  . GLU A 117 ? 0.0688 0.0414 0.2050 0.0049  -0.0357 -0.0054 117 GLU A CD  
1023 O  OE1 . GLU A 117 ? 0.0768 0.0623 0.2082 0.0164  -0.0388 -0.0041 117 GLU A OE1 
1024 O  OE2 . GLU A 117 ? 0.1102 0.0538 0.1965 0.0062  -0.0483 -0.0085 117 GLU A OE2 
1025 N  N   . LEU A 118 ? 0.0767 0.0306 0.1981 0.0150  -0.0423 -0.0017 118 LEU A N   
1026 C  CA  . LEU A 118 ? 0.0640 0.0269 0.1990 -0.0010 -0.0359 -0.0136 118 LEU A CA  
1027 C  C   . LEU A 118 ? 0.0728 0.0295 0.1620 0.0098  -0.0366 0.0071  118 LEU A C   
1028 O  O   . LEU A 118 ? 0.0737 0.0379 0.1644 -0.0006 -0.0185 0.0017  118 LEU A O   
1029 C  CB  . LEU A 118 ? 0.0671 0.0267 0.2291 0.0062  -0.0364 -0.0147 118 LEU A CB  
1030 C  CG  . LEU A 118 ? 0.0714 0.0617 0.1906 0.0270  -0.0403 -0.0065 118 LEU A CG  
1031 C  CD1 . LEU A 118 ? 0.0855 0.0564 0.1877 0.0006  -0.0461 -0.0024 118 LEU A CD1 
1032 C  CD2 . LEU A 118 ? 0.0666 0.1045 0.2217 0.0071  -0.0443 -0.0085 118 LEU A CD2 
1033 N  N   . HIS A 119 ? 0.0644 0.0261 0.1805 -0.0041 -0.0427 -0.0013 119 HIS A N   
1034 C  CA  . HIS A 119 ? 0.0652 0.0267 0.1960 0.0060  -0.0391 -0.0135 119 HIS A CA  
1035 C  C   . HIS A 119 ? 0.0767 0.0305 0.1541 0.0131  -0.0315 -0.0198 119 HIS A C   
1036 O  O   . HIS A 119 ? 0.0869 0.0432 0.1527 0.0218  -0.0313 -0.0031 119 HIS A O   
1037 C  CB  . HIS A 119 ? 0.0688 0.0313 0.2247 0.0049  -0.0526 -0.0027 119 HIS A CB  
1038 C  CG  . HIS A 119 ? 0.0627 0.0362 0.1870 0.0097  -0.0252 -0.0120 119 HIS A CG  
1039 N  ND1 . HIS A 119 ? 0.0582 0.0296 0.2141 -0.0102 -0.0274 -0.0017 119 HIS A ND1 
1040 C  CD2 . HIS A 119 ? 0.0692 0.0370 0.2138 -0.0010 -0.0502 0.0024  119 HIS A CD2 
1041 C  CE1 . HIS A 119 ? 0.0935 0.0405 0.1802 -0.0027 -0.0315 -0.0035 119 HIS A CE1 
1042 N  NE2 . HIS A 119 ? 0.0746 0.0520 0.1845 0.0137  -0.0373 0.0023  119 HIS A NE2 
1043 N  N   . LEU A 120 ? 0.0582 0.0331 0.1796 0.0153  -0.0346 -0.0076 120 LEU A N   
1044 C  CA  . LEU A 120 ? 0.0636 0.0353 0.1990 0.0194  -0.0394 -0.0148 120 LEU A CA  
1045 C  C   . LEU A 120 ? 0.0772 0.0357 0.1499 0.0219  -0.0335 -0.0041 120 LEU A C   
1046 O  O   . LEU A 120 ? 0.0765 0.0263 0.1599 0.0067  -0.0336 -0.0017 120 LEU A O   
1047 C  CB  . LEU A 120 ? 0.0612 0.0588 0.2078 0.0000  -0.0339 -0.0054 120 LEU A CB  
1048 C  CG  . LEU A 120 ? 0.0644 0.0926 0.1931 -0.0093 -0.0419 -0.0186 120 LEU A CG  
1049 C  CD1 . LEU A 120 ? 0.1992 0.0978 0.2439 -0.0908 -0.0306 -0.0031 120 LEU A CD1 
1050 C  CD2 . LEU A 120 ? 0.0895 0.1145 0.2046 0.0181  -0.0568 -0.0017 120 LEU A CD2 
1051 N  N   . VAL A 121 ? 0.0838 0.0333 0.1791 0.0120  -0.0251 0.0023  121 VAL A N   
1052 C  CA  . VAL A 121 ? 0.0907 0.0353 0.1668 0.0024  -0.0197 -0.0114 121 VAL A CA  
1053 C  C   . VAL A 121 ? 0.0819 0.0502 0.1629 -0.0031 -0.0182 0.0087  121 VAL A C   
1054 O  O   . VAL A 121 ? 0.1035 0.0370 0.1729 -0.0006 -0.0344 -0.0038 121 VAL A O   
1055 C  CB  . VAL A 121 ? 0.0819 0.0438 0.1861 -0.0010 -0.0252 0.0023  121 VAL A CB  
1056 C  CG1 . VAL A 121 ? 0.0706 0.0869 0.1999 -0.0205 -0.0322 0.0171  121 VAL A CG1 
1057 C  CG2 . VAL A 121 ? 0.0794 0.0590 0.2017 0.0086  -0.0164 0.0102  121 VAL A CG2 
1058 N  N   . HIS A 122 ? 0.0863 0.0414 0.1710 0.0102  -0.0308 -0.0093 122 HIS A N   
1059 C  CA  . HIS A 122 ? 0.0781 0.0423 0.2087 0.0109  -0.0217 -0.0253 122 HIS A CA  
1060 C  C   . HIS A 122 ? 0.1091 0.0423 0.1583 0.0040  -0.0340 0.0162  122 HIS A C   
1061 O  O   . HIS A 122 ? 0.0957 0.0395 0.1932 0.0038  -0.0421 0.0118  122 HIS A O   
1062 C  CB  . HIS A 122 ? 0.0869 0.0395 0.1791 0.0276  -0.0298 -0.0003 122 HIS A CB  
1063 C  CG  . HIS A 122 ? 0.0851 0.0287 0.2012 0.0120  -0.0163 -0.0060 122 HIS A CG  
1064 N  ND1 . HIS A 122 ? 0.0746 0.0328 0.2123 0.0186  -0.0154 -0.0152 122 HIS A ND1 
1065 C  CD2 . HIS A 122 ? 0.0851 0.0615 0.2184 0.0035  -0.0251 -0.0103 122 HIS A CD2 
1066 C  CE1 . HIS A 122 ? 0.0591 0.0785 0.2287 0.0131  -0.0086 -0.0142 122 HIS A CE1 
1067 N  NE2 . HIS A 122 ? 0.0715 0.0683 0.2175 -0.0175 -0.0328 -0.0104 122 HIS A NE2 
1068 N  N   . TRP A 123 ? 0.1102 0.0306 0.1929 0.0074  -0.0359 -0.0183 123 TRP A N   
1069 C  CA  . TRP A 123 ? 0.1140 0.0309 0.1951 -0.0006 -0.0275 -0.0219 123 TRP A CA  
1070 C  C   . TRP A 123 ? 0.1173 0.0332 0.1696 0.0243  -0.0401 0.0020  123 TRP A C   
1071 O  O   . TRP A 123 ? 0.1163 0.0441 0.2299 0.0232  -0.0469 -0.0048 123 TRP A O   
1072 C  CB  . TRP A 123 ? 0.1254 0.0657 0.2055 -0.0130 -0.0493 0.0074  123 TRP A CB  
1073 C  CG  . TRP A 123 ? 0.1586 0.0525 0.2163 -0.0361 -0.0820 0.0126  123 TRP A CG  
1074 C  CD1 . TRP A 123 ? 0.1841 0.1213 0.2154 -0.0187 -0.0957 0.0076  123 TRP A CD1 
1075 C  CD2 . TRP A 123 ? 0.2136 0.0373 0.2137 -0.0473 -0.0635 0.0132  123 TRP A CD2 
1076 N  NE1 . TRP A 123 ? 0.2260 0.0588 0.2345 -0.0176 -0.1186 -0.0074 123 TRP A NE1 
1077 C  CE2 . TRP A 123 ? 0.2222 0.0302 0.2372 -0.0296 -0.0797 0.0059  123 TRP A CE2 
1078 C  CE3 . TRP A 123 ? 0.2289 0.0317 0.2574 -0.0340 -0.0754 0.0012  123 TRP A CE3 
1079 C  CZ2 . TRP A 123 ? 0.2430 0.0361 0.3082 -0.0054 -0.1120 -0.0068 123 TRP A CZ2 
1080 C  CZ3 . TRP A 123 ? 0.2294 0.0421 0.2391 -0.0208 -0.0825 0.0082  123 TRP A CZ3 
1081 C  CH2 . TRP A 123 ? 0.3287 0.0542 0.2436 -0.0546 -0.0992 -0.0035 123 TRP A CH2 
1082 N  N   . ASN A 124 ? 0.1324 0.0359 0.1929 -0.0060 -0.0308 -0.0241 124 ASN A N   
1083 C  CA  . ASN A 124 ? 0.1561 0.0485 0.2118 0.0093  -0.0241 -0.0344 124 ASN A CA  
1084 C  C   . ASN A 124 ? 0.1324 0.0493 0.2378 0.0177  -0.0096 -0.0153 124 ASN A C   
1085 O  O   . ASN A 124 ? 0.1259 0.0520 0.2472 0.0135  -0.0207 -0.0219 124 ASN A O   
1086 C  CB  . ASN A 124 ? 0.2057 0.0520 0.1985 0.0054  -0.0353 -0.0252 124 ASN A CB  
1087 C  CG  . ASN A 124 ? 0.1520 0.0649 0.2157 -0.0137 -0.0247 -0.0320 124 ASN A CG  
1088 O  OD1 . ASN A 124 ? 0.2196 0.0653 0.2854 0.0249  0.0019  -0.0241 124 ASN A OD1 
1089 N  ND2 . ASN A 124 ? 0.2457 0.0949 0.2211 0.0197  -0.0175 -0.0450 124 ASN A ND2 
1090 N  N   . THR A 125 ? 0.1491 0.0432 0.2827 0.0335  -0.0298 -0.0432 125 THR A N   
1091 C  CA  . THR A 125 ? 0.1641 0.0437 0.3122 0.0164  -0.0368 -0.0353 125 THR A CA  
1092 C  C   . THR A 125 ? 0.1268 0.0456 0.3251 0.0322  -0.0006 -0.0458 125 THR A C   
1093 O  O   . THR A 125 ? 0.2120 0.0441 0.4004 0.0274  -0.0478 -0.0126 125 THR A O   
1094 C  CB  . THR A 125 ? 0.1568 0.1036 0.4156 0.0043  -0.0388 -0.0230 125 THR A CB  
1095 O  OG1 . THR A 125 ? 0.1683 0.1213 0.4747 0.0469  0.0040  -0.0516 125 THR A OG1 
1096 C  CG2 . THR A 125 ? 0.2014 0.1493 0.3731 0.0478  -0.1062 -0.0307 125 THR A CG2 
1097 N  N   . LYS A 126 ? 0.2062 0.0520 0.2827 0.0447  -0.0165 -0.0575 126 LYS A N   
1098 C  CA  . LYS A 126 ? 0.3424 0.1023 0.3553 -0.0430 0.0447  -0.1010 126 LYS A CA  
1099 C  C   . LYS A 126 ? 0.2249 0.0490 0.3508 0.0186  -0.0273 -0.0577 126 LYS A C   
1100 O  O   . LYS A 126 ? 0.2635 0.0538 0.4772 -0.0020 -0.0153 -0.0860 126 LYS A O   
1101 C  CB  . LYS A 126 ? 0.3752 0.1782 0.3679 0.0109  0.0107  -0.0882 126 LYS A CB  
1102 C  CG  . LYS A 126 ? 0.3016 0.1559 0.3831 -0.0719 -0.0612 -0.0807 126 LYS A CG  
1103 C  CD  . LYS A 126 ? 0.4648 0.4401 0.3977 -0.0452 0.2152  0.0197  126 LYS A CD  
1104 C  CE  . LYS A 126 ? 0.4799 0.2118 0.5515 -0.1101 0.0838  -0.1342 126 LYS A CE  
1105 N  NZ  . LYS A 126 ? 0.3977 0.5788 0.7005 -0.1467 0.0864  -0.3799 126 LYS A NZ  
1106 N  N   . TYR A 127 ? 0.1764 0.0636 0.2433 0.0142  -0.0379 -0.0076 127 TYR A N   
1107 C  CA  . TYR A 127 ? 0.1606 0.0377 0.2736 0.0175  -0.0737 -0.0270 127 TYR A CA  
1108 C  C   . TYR A 127 ? 0.1342 0.0289 0.2624 -0.0174 -0.0576 -0.0034 127 TYR A C   
1109 O  O   . TYR A 127 ? 0.1579 0.0658 0.3321 -0.0093 -0.0566 0.0019  127 TYR A O   
1110 C  CB  . TYR A 127 ? 0.1622 0.0362 0.3145 0.0017  -0.0908 0.0000  127 TYR A CB  
1111 C  CG  . TYR A 127 ? 0.1902 0.0397 0.2894 0.0012  -0.0838 -0.0038 127 TYR A CG  
1112 C  CD1 . TYR A 127 ? 0.2362 0.0491 0.3063 0.0148  -0.0996 -0.0263 127 TYR A CD1 
1113 C  CD2 . TYR A 127 ? 0.1826 0.0485 0.2463 0.0113  -0.0544 -0.0340 127 TYR A CD2 
1114 C  CE1 . TYR A 127 ? 0.3032 0.0825 0.2874 0.0794  -0.1027 -0.0715 127 TYR A CE1 
1115 C  CE2 . TYR A 127 ? 0.1917 0.0715 0.2520 0.0447  -0.0496 -0.0408 127 TYR A CE2 
1116 C  CZ  . TYR A 127 ? 0.2434 0.1057 0.2527 0.0584  -0.0864 -0.0678 127 TYR A CZ  
1117 O  OH  . TYR A 127 ? 0.2696 0.0929 0.2917 0.0219  -0.0781 -0.0658 127 TYR A OH  
1118 N  N   . GLY A 128 ? 0.1674 0.0688 0.2675 0.0027  -0.0746 -0.0005 128 GLY A N   
1119 C  CA  . GLY A 128 ? 0.1793 0.1005 0.2827 -0.0441 -0.0697 0.0113  128 GLY A CA  
1120 C  C   . GLY A 128 ? 0.1972 0.0728 0.2402 -0.0364 -0.0705 0.0502  128 GLY A C   
1121 O  O   . GLY A 128 ? 0.4187 0.0657 0.3054 -0.0242 -0.1738 0.0401  128 GLY A O   
1122 N  N   A ASP A 129 ? 0.2405 0.0869 0.2527 0.0254  -0.0348 0.0401  129 ASP A N   
1123 N  N   B ASP A 129 ? 0.2172 0.0851 0.2657 0.0098  -0.0754 -0.0038 129 ASP A N   
1124 C  CA  A ASP A 129 ? 0.3043 0.0428 0.2463 0.0304  -0.0731 0.0331  129 ASP A CA  
1125 C  CA  B ASP A 129 ? 0.1796 0.1075 0.3100 -0.0023 -0.0296 0.0114  129 ASP A CA  
1126 C  C   A ASP A 129 ? 0.2136 0.1096 0.1791 0.0666  -0.0461 0.0355  129 ASP A C   
1127 C  C   B ASP A 129 ? 0.2475 0.1045 0.2973 0.0074  -0.0337 0.0000  129 ASP A C   
1128 O  O   A ASP A 129 ? 0.1168 0.1814 0.2030 0.0342  -0.0568 0.0362  129 ASP A O   
1129 O  O   B ASP A 129 ? 0.3305 0.0333 0.2962 0.0164  -0.0401 0.0141  129 ASP A O   
1130 C  CB  A ASP A 129 ? 0.2459 0.1326 0.2118 0.0608  -0.0292 0.0102  129 ASP A CB  
1131 C  CB  B ASP A 129 ? 0.2002 0.0798 0.3495 -0.0635 -0.0275 -0.0142 129 ASP A CB  
1132 C  CG  A ASP A 129 ? 0.2339 0.1141 0.4422 0.0926  -0.0142 -0.1465 129 ASP A CG  
1133 C  CG  B ASP A 129 ? 0.2019 0.0921 0.5070 -0.0631 -0.0092 -0.0333 129 ASP A CG  
1134 O  OD1 A ASP A 129 ? 0.2256 0.1168 0.2646 0.0614  -0.0006 0.0416  129 ASP A OD1 
1135 O  OD1 B ASP A 129 ? 0.2750 0.1277 0.5849 0.1017  -0.0570 -0.0035 129 ASP A OD1 
1136 O  OD2 A ASP A 129 ? 0.1206 0.1172 0.4862 0.0274  -0.0192 -0.0043 129 ASP A OD2 
1137 O  OD2 B ASP A 129 ? 0.3743 0.1039 0.2723 0.0595  -0.0228 -0.0183 129 ASP A OD2 
1138 N  N   . ALA A 130 ? 0.2028 0.1054 0.2513 0.0298  -0.0658 0.0271  130 ALA A N   
1139 C  CA  . ALA A 130 ? 0.2148 0.0790 0.2502 0.0395  -0.0500 0.0017  130 ALA A CA  
1140 C  C   . ALA A 130 ? 0.1933 0.1572 0.2154 -0.0161 -0.0151 0.0241  130 ALA A C   
1141 O  O   . ALA A 130 ? 0.1978 0.0983 0.2269 0.0003  -0.0263 0.0000  130 ALA A O   
1142 C  CB  . ALA A 130 ? 0.2576 0.0788 0.2750 0.0515  -0.0581 -0.0170 130 ALA A CB  
1143 N  N   . GLY A 131 ? 0.2213 0.1741 0.2502 0.0085  -0.0120 0.0746  131 GLY A N   
1144 C  CA  . GLY A 131 ? 0.2078 0.2454 0.3077 0.0087  -0.0230 -0.0013 131 GLY A CA  
1145 C  C   . GLY A 131 ? 0.1577 0.1254 0.2671 -0.0307 0.0087  0.0274  131 GLY A C   
1146 O  O   . GLY A 131 ? 0.1687 0.1552 0.3192 -0.0125 -0.0309 0.0491  131 GLY A O   
1147 N  N   . LYS A 132 ? 0.2005 0.1115 0.3479 -0.0184 0.0131  0.0627  132 LYS A N   
1148 C  CA  . LYS A 132 ? 0.1915 0.1023 0.3348 -0.0447 -0.0732 0.0737  132 LYS A CA  
1149 C  C   . LYS A 132 ? 0.1432 0.0644 0.2224 -0.0228 -0.0573 -0.0108 132 LYS A C   
1150 O  O   . LYS A 132 ? 0.2005 0.0851 0.2461 -0.0588 -0.0834 0.0060  132 LYS A O   
1151 C  CB  . LYS A 132 ? 0.1956 0.0780 0.5666 -0.0702 -0.1133 0.1404  132 LYS A CB  
1152 C  CG  . LYS A 132 ? 0.2639 0.2293 0.4657 -0.0987 -0.1624 0.1532  132 LYS A CG  
1153 C  CD  . LYS A 132 ? 0.2583 0.4390 0.7037 -0.1809 -0.0662 0.2777  132 LYS A CD  
1154 C  CE  . LYS A 132 ? 0.8596 0.6667 0.4419 -0.3492 -0.0850 0.1641  132 LYS A CE  
1155 N  NZ  . LYS A 132 ? 0.7296 0.2019 1.4428 -0.0373 -0.1454 -0.1753 132 LYS A NZ  
1156 N  N   . ALA A 133 ? 0.1369 0.0710 0.2574 -0.0346 -0.0353 -0.0114 133 ALA A N   
1157 C  CA  . ALA A 133 ? 0.1280 0.0674 0.2718 -0.0183 -0.0504 0.0113  133 ALA A CA  
1158 C  C   . ALA A 133 ? 0.1064 0.0812 0.2046 -0.0159 -0.0454 -0.0071 133 ALA A C   
1159 O  O   . ALA A 133 ? 0.1380 0.0869 0.2242 -0.0085 -0.0584 -0.0187 133 ALA A O   
1160 C  CB  . ALA A 133 ? 0.1410 0.0597 0.2745 -0.0252 -0.0758 -0.0087 133 ALA A CB  
1161 N  N   . SER A 134 ? 0.1437 0.0772 0.2053 -0.0249 -0.0375 0.0114  134 SER A N   
1162 C  CA  . SER A 134 ? 0.1247 0.0825 0.2118 -0.0125 -0.0344 0.0070  134 SER A CA  
1163 C  C   . SER A 134 ? 0.1335 0.0890 0.2120 -0.0175 -0.0366 0.0217  134 SER A C   
1164 O  O   . SER A 134 ? 0.1179 0.1289 0.2558 -0.0096 -0.0275 0.0401  134 SER A O   
1165 C  CB  . SER A 134 ? 0.1486 0.1274 0.2301 -0.0230 -0.0186 -0.0076 134 SER A CB  
1166 O  OG  . SER A 134 ? 0.1635 0.1649 0.2414 0.0020  0.0027  -0.0046 134 SER A OG  
1167 N  N   . GLN A 135 ? 0.1221 0.0966 0.2346 -0.0370 -0.0450 -0.0054 135 GLN A N   
1168 C  CA  . GLN A 135 ? 0.1290 0.1233 0.2879 -0.0152 -0.0666 -0.0238 135 GLN A CA  
1169 C  C   . GLN A 135 ? 0.1504 0.1283 0.2991 -0.0068 -0.0750 -0.0710 135 GLN A C   
1170 O  O   . GLN A 135 ? 0.2134 0.2206 0.3104 -0.0768 -0.1067 -0.0103 135 GLN A O   
1171 C  CB  . GLN A 135 ? 0.2050 0.1310 0.3835 -0.0714 -0.1048 0.0176  135 GLN A CB  
1172 C  CG  . GLN A 135 ? 0.2777 0.2935 0.3914 -0.1280 -0.0768 0.0750  135 GLN A CG  
1173 C  CD  . GLN A 135 ? 0.2565 0.5288 0.4289 -0.0961 -0.0781 0.0263  135 GLN A CD  
1174 O  OE1 . GLN A 135 ? 0.3684 0.5267 0.6872 0.1062  -0.1155 -0.0275 135 GLN A OE1 
1175 N  NE2 . GLN A 135 ? 0.4812 0.8403 0.6039 0.4738  -0.1394 -0.2459 135 GLN A NE2 
1176 N  N   . GLN A 136 ? 0.1782 0.0824 0.2662 0.0104  -0.0465 -0.0049 136 GLN A N   
1177 C  CA  . GLN A 136 ? 0.1504 0.1106 0.2608 -0.0115 -0.0504 -0.0307 136 GLN A CA  
1178 C  C   . GLN A 136 ? 0.1773 0.1161 0.1944 -0.0034 -0.0491 -0.0538 136 GLN A C   
1179 O  O   . GLN A 136 ? 0.2193 0.0900 0.2111 0.0113  -0.0666 -0.0423 136 GLN A O   
1180 C  CB  . GLN A 136 ? 0.1992 0.0922 0.3337 0.0162  -0.0452 -0.0263 136 GLN A CB  
1181 C  CG  . GLN A 136 ? 0.2554 0.1464 0.2851 0.0366  -0.0205 -0.0065 136 GLN A CG  
1182 C  CD  . GLN A 136 ? 0.2351 0.1124 0.4235 0.0259  0.0048  0.0114  136 GLN A CD  
1183 O  OE1 . GLN A 136 ? 0.3276 0.1177 0.3948 -0.0582 -0.0697 -0.0566 136 GLN A OE1 
1184 N  NE2 . GLN A 136 ? 0.3314 0.2847 0.5511 -0.0627 0.0308  0.0974  136 GLN A NE2 
1185 N  N   . PRO A 137 ? 0.2069 0.1143 0.2145 0.0529  -0.0741 -0.0456 137 PRO A N   
1186 C  CA  . PRO A 137 ? 0.1820 0.1425 0.2127 0.0452  -0.0781 -0.0287 137 PRO A CA  
1187 C  C   . PRO A 137 ? 0.2263 0.1194 0.1816 0.0320  -0.0549 0.0197  137 PRO A C   
1188 O  O   . PRO A 137 ? 0.2310 0.1179 0.2743 0.0322  -0.0054 0.0432  137 PRO A O   
1189 C  CB  . PRO A 137 ? 0.2393 0.2928 0.2181 0.1102  -0.1102 -0.0549 137 PRO A CB  
1190 C  CG  . PRO A 137 ? 0.3382 0.2845 0.2441 -0.0307 -0.1194 -0.1096 137 PRO A CG  
1191 C  CD  . PRO A 137 ? 0.2294 0.2037 0.2186 0.0137  -0.0851 -0.0776 137 PRO A CD  
1192 N  N   . ASP A 138 ? 0.1852 0.0992 0.2195 0.0313  -0.0271 -0.0114 138 ASP A N   
1193 C  CA  . ASP A 138 ? 0.1854 0.1238 0.2102 0.0258  -0.0160 -0.0326 138 ASP A CA  
1194 C  C   . ASP A 138 ? 0.1683 0.0344 0.1879 -0.0093 -0.0035 -0.0221 138 ASP A C   
1195 O  O   . ASP A 138 ? 0.1635 0.1202 0.2211 0.0129  -0.0379 -0.0210 138 ASP A O   
1196 C  CB  . ASP A 138 ? 0.1983 0.2202 0.2021 0.0529  -0.0294 -0.0294 138 ASP A CB  
1197 C  CG  . ASP A 138 ? 0.1809 0.2565 0.2545 0.1089  -0.0443 -0.0241 138 ASP A CG  
1198 O  OD1 . ASP A 138 ? 0.2335 0.1149 0.2908 0.0469  -0.0648 -0.0643 138 ASP A OD1 
1199 O  OD2 . ASP A 138 ? 0.2903 0.3086 0.2969 0.1606  -0.0384 -0.0873 138 ASP A OD2 
1200 N  N   . GLY A 139 ? 0.1389 0.0741 0.1741 0.0173  -0.0251 -0.0148 139 GLY A N   
1201 C  CA  . GLY A 139 ? 0.1511 0.0776 0.1653 -0.0024 -0.0498 -0.0142 139 GLY A CA  
1202 C  C   . GLY A 139 ? 0.1215 0.0439 0.1590 0.0003  -0.0425 0.0031  139 GLY A C   
1203 O  O   . GLY A 139 ? 0.1261 0.0421 0.1835 0.0098  -0.0443 -0.0017 139 GLY A O   
1204 N  N   . LEU A 140 ? 0.0917 0.0377 0.2060 -0.0046 -0.0285 -0.0164 140 LEU A N   
1205 C  CA  . LEU A 140 ? 0.0910 0.0256 0.1825 0.0045  -0.0272 -0.0022 140 LEU A CA  
1206 C  C   . LEU A 140 ? 0.0684 0.0560 0.1608 0.0155  -0.0146 -0.0214 140 LEU A C   
1207 O  O   . LEU A 140 ? 0.1263 0.0284 0.1703 -0.0063 -0.0329 -0.0041 140 LEU A O   
1208 C  CB  . LEU A 140 ? 0.0803 0.0644 0.2080 0.0186  -0.0226 -0.0164 140 LEU A CB  
1209 C  CG  . LEU A 140 ? 0.1084 0.1106 0.2093 0.0351  -0.0019 0.0051  140 LEU A CG  
1210 C  CD1 . LEU A 140 ? 0.1254 0.1039 0.2247 0.0549  0.0027  0.0098  140 LEU A CD1 
1211 C  CD2 . LEU A 140 ? 0.1613 0.0806 0.2199 0.0031  -0.0231 -0.0065 140 LEU A CD2 
1212 N  N   . ALA A 141 ? 0.0750 0.0292 0.2275 -0.0031 -0.0214 -0.0251 141 ALA A N   
1213 C  CA  . ALA A 141 ? 0.0921 0.0473 0.1805 0.0131  -0.0253 -0.0183 141 ALA A CA  
1214 C  C   . ALA A 141 ? 0.0860 0.0406 0.1653 0.0098  -0.0291 -0.0166 141 ALA A C   
1215 O  O   . ALA A 141 ? 0.1254 0.0291 0.1825 0.0098  -0.0331 -0.0102 141 ALA A O   
1216 C  CB  . ALA A 141 ? 0.1030 0.0803 0.2242 0.0126  0.0013  -0.0285 141 ALA A CB  
1217 N  N   . VAL A 142 ? 0.0794 0.0295 0.1902 -0.0034 -0.0146 -0.0142 142 VAL A N   
1218 C  CA  . VAL A 142 ? 0.0812 0.0546 0.1622 0.0040  -0.0285 -0.0060 142 VAL A CA  
1219 C  C   . VAL A 142 ? 0.0829 0.0353 0.1368 0.0031  -0.0313 -0.0252 142 VAL A C   
1220 O  O   . VAL A 142 ? 0.0810 0.0573 0.1588 0.0000  -0.0326 -0.0085 142 VAL A O   
1221 C  CB  . VAL A 142 ? 0.0687 0.0494 0.1721 0.0076  -0.0401 -0.0082 142 VAL A CB  
1222 C  CG1 . VAL A 142 ? 0.1093 0.0524 0.1834 0.0214  -0.0274 -0.0197 142 VAL A CG1 
1223 C  CG2 . VAL A 142 ? 0.0877 0.0706 0.1714 0.0015  -0.0196 -0.0024 142 VAL A CG2 
1224 N  N   . LEU A 143 ? 0.0687 0.0293 0.1754 0.0082  -0.0372 -0.0240 143 LEU A N   
1225 C  CA  . LEU A 143 ? 0.0680 0.0305 0.2138 0.0143  -0.0210 -0.0010 143 LEU A CA  
1226 C  C   . LEU A 143 ? 0.0803 0.0377 0.1498 -0.0115 -0.0366 -0.0015 143 LEU A C   
1227 O  O   . LEU A 143 ? 0.0869 0.0403 0.1784 0.0074  -0.0264 0.0006  143 LEU A O   
1228 C  CB  . LEU A 143 ? 0.0917 0.0368 0.2120 0.0040  -0.0384 0.0023  143 LEU A CB  
1229 C  CG  . LEU A 143 ? 0.0790 0.0885 0.2373 -0.0115 -0.0252 0.0163  143 LEU A CG  
1230 C  CD1 . LEU A 143 ? 0.1017 0.1520 0.2671 -0.0003 -0.0379 0.0527  143 LEU A CD1 
1231 C  CD2 . LEU A 143 ? 0.0671 0.1484 0.2373 0.0230  -0.0263 -0.0073 143 LEU A CD2 
1232 N  N   . GLY A 144 ? 0.0727 0.0357 0.1800 0.0020  -0.0362 0.0038  144 GLY A N   
1233 C  CA  . GLY A 144 ? 0.0882 0.0261 0.2009 0.0057  -0.0401 0.0024  144 GLY A CA  
1234 C  C   . GLY A 144 ? 0.0763 0.0483 0.1527 0.0071  -0.0120 0.0038  144 GLY A C   
1235 O  O   . GLY A 144 ? 0.0958 0.0473 0.1905 -0.0052 -0.0109 -0.0086 144 GLY A O   
1236 N  N   . ILE A 145 ? 0.0476 0.0653 0.1710 0.0087  -0.0271 -0.0063 145 ILE A N   
1237 C  CA  . ILE A 145 ? 0.0573 0.0358 0.2125 0.0073  -0.0375 0.0037  145 ILE A CA  
1238 C  C   . ILE A 145 ? 0.0608 0.0458 0.1836 0.0027  -0.0375 -0.0030 145 ILE A C   
1239 O  O   . ILE A 145 ? 0.0803 0.0256 0.2073 0.0033  -0.0166 -0.0050 145 ILE A O   
1240 C  CB  . ILE A 145 ? 0.0627 0.0474 0.2050 0.0137  -0.0379 0.0024  145 ILE A CB  
1241 C  CG1 . ILE A 145 ? 0.1080 0.0710 0.2290 0.0427  -0.0269 0.0060  145 ILE A CG1 
1242 C  CG2 . ILE A 145 ? 0.0684 0.1014 0.2213 -0.0006 -0.0675 -0.0147 145 ILE A CG2 
1243 C  CD1 . ILE A 145 ? 0.0969 0.0834 0.2423 0.0148  -0.0496 0.0013  145 ILE A CD1 
1244 N  N   . PHE A 146 ? 0.0706 0.0438 0.1902 0.0026  -0.0339 0.0005  146 PHE A N   
1245 C  CA  . PHE A 146 ? 0.0842 0.0529 0.1757 0.0342  -0.0496 -0.0086 146 PHE A CA  
1246 C  C   . PHE A 146 ? 0.0590 0.0379 0.2178 0.0020  -0.0516 -0.0154 146 PHE A C   
1247 O  O   . PHE A 146 ? 0.0615 0.0666 0.2457 -0.0019 -0.0456 -0.0038 146 PHE A O   
1248 C  CB  . PHE A 146 ? 0.1005 0.0568 0.1976 -0.0109 -0.0502 0.0093  146 PHE A CB  
1249 C  CG  . PHE A 146 ? 0.0940 0.0481 0.1692 -0.0020 -0.0320 0.0006  146 PHE A CG  
1250 C  CD1 . PHE A 146 ? 0.0824 0.0379 0.2159 0.0241  -0.0417 0.0000  146 PHE A CD1 
1251 C  CD2 . PHE A 146 ? 0.0974 0.0379 0.1875 -0.0034 -0.0460 0.0113  146 PHE A CD2 
1252 C  CE1 . PHE A 146 ? 0.0944 0.0582 0.1816 -0.0027 -0.0439 0.0063  146 PHE A CE1 
1253 C  CE2 . PHE A 146 ? 0.1055 0.0582 0.1944 -0.0037 -0.0218 -0.0160 146 PHE A CE2 
1254 C  CZ  . PHE A 146 ? 0.0921 0.0406 0.2075 -0.0019 -0.0450 -0.0052 146 PHE A CZ  
1255 N  N   . LEU A 147 ? 0.0851 0.0362 0.2190 0.0087  -0.0361 -0.0160 147 LEU A N   
1256 C  CA  . LEU A 147 ? 0.0985 0.0392 0.2226 0.0231  -0.0524 -0.0296 147 LEU A CA  
1257 C  C   . LEU A 147 ? 0.0812 0.0432 0.2222 0.0152  -0.0445 -0.0126 147 LEU A C   
1258 O  O   . LEU A 147 ? 0.0829 0.0436 0.2818 0.0148  -0.0586 -0.0093 147 LEU A O   
1259 C  CB  . LEU A 147 ? 0.0996 0.0467 0.2430 0.0198  -0.0401 -0.0304 147 LEU A CB  
1260 C  CG  . LEU A 147 ? 0.1052 0.0441 0.2215 0.0103  -0.0546 -0.0120 147 LEU A CG  
1261 C  CD1 . LEU A 147 ? 0.1465 0.0405 0.2245 -0.0065 -0.0557 -0.0097 147 LEU A CD1 
1262 C  CD2 . LEU A 147 ? 0.1184 0.0860 0.2238 -0.0031 -0.0348 -0.0137 147 LEU A CD2 
1263 N  N   . LYS A 148 ? 0.1116 0.0370 0.2308 -0.0120 -0.0478 -0.0118 148 LYS A N   
1264 C  CA  . LYS A 148 ? 0.1080 0.0386 0.2558 -0.0093 -0.0640 -0.0159 148 LYS A CA  
1265 C  C   . LYS A 148 ? 0.1075 0.0544 0.2416 0.0203  -0.0566 0.0023  148 LYS A C   
1266 O  O   . LYS A 148 ? 0.1331 0.0636 0.2671 0.0476  -0.0636 -0.0080 148 LYS A O   
1267 C  CB  . LYS A 148 ? 0.1270 0.0985 0.2684 -0.0252 -0.0790 -0.0006 148 LYS A CB  
1268 C  CG  . LYS A 148 ? 0.1263 0.1425 0.3190 -0.0175 -0.0626 0.0241  148 LYS A CG  
1269 C  CD  . LYS A 148 ? 0.2703 0.1949 0.3989 -0.0630 -0.0353 0.0697  148 LYS A CD  
1270 C  CE  . LYS A 148 ? 0.2836 0.4514 0.5097 -0.0944 -0.0109 0.1369  148 LYS A CE  
1271 N  NZ  . LYS A 148 ? 0.4472 0.4778 0.6534 -0.1238 0.1502  0.1473  148 LYS A NZ  
1272 N  N   . VAL A 149 ? 0.1649 0.0296 0.2619 0.0229  -0.0908 -0.0074 149 VAL A N   
1273 C  CA  . VAL A 149 ? 0.1367 0.0724 0.2709 0.0274  -0.0978 -0.0384 149 VAL A CA  
1274 C  C   . VAL A 149 ? 0.1674 0.0351 0.3005 0.0183  -0.1058 -0.0057 149 VAL A C   
1275 O  O   . VAL A 149 ? 0.1852 0.0781 0.3183 0.0136  -0.1098 0.0020  149 VAL A O   
1276 C  CB  . VAL A 149 ? 0.1405 0.0702 0.2657 0.0248  -0.0820 -0.0292 149 VAL A CB  
1277 C  CG1 . VAL A 149 ? 0.1976 0.1107 0.2536 0.0148  -0.1084 -0.0241 149 VAL A CG1 
1278 C  CG2 . VAL A 149 ? 0.1344 0.1292 0.3262 -0.0126 -0.0274 -0.0242 149 VAL A CG2 
1279 N  N   . GLY A 150 ? 0.1286 0.0856 0.2353 0.0227  -0.0776 -0.0125 150 GLY A N   
1280 C  CA  . GLY A 150 ? 0.1491 0.1107 0.2637 -0.0103 -0.0974 0.0000  150 GLY A CA  
1281 C  C   . GLY A 150 ? 0.1617 0.0463 0.2179 -0.0010 -0.0640 -0.0203 150 GLY A C   
1282 O  O   . GLY A 150 ? 0.1423 0.0869 0.2354 0.0068  -0.0570 -0.0186 150 GLY A O   
1283 N  N   A SER A 151 ? 0.1310 0.0415 0.3287 -0.0328 -0.0575 -0.0227 151 SER A N   
1284 N  N   B SER A 151 ? 0.1297 0.0951 0.2870 0.0302  -0.0907 -0.0253 151 SER A N   
1285 C  CA  A SER A 151 ? 0.1547 0.1107 0.3289 -0.0555 -0.0891 -0.0076 151 SER A CA  
1286 C  CA  B SER A 151 ? 0.1014 0.0546 0.3368 0.0285  -0.0996 -0.0315 151 SER A CA  
1287 C  C   A SER A 151 ? 0.1421 0.0847 0.2317 -0.0102 -0.0555 -0.0361 151 SER A C   
1288 C  C   B SER A 151 ? 0.1064 0.0854 0.2378 0.0305  -0.0706 -0.0443 151 SER A C   
1289 O  O   A SER A 151 ? 0.1168 0.1008 0.2039 0.0023  -0.0766 -0.0174 151 SER A O   
1290 O  O   B SER A 151 ? 0.1152 0.0648 0.2739 -0.0059 -0.0469 -0.0471 151 SER A O   
1291 C  CB  A SER A 151 ? 0.1708 0.1850 0.3677 -0.1480 -0.0283 -0.0260 151 SER A CB  
1292 C  CB  B SER A 151 ? 0.0942 0.0815 0.3722 0.0520  -0.1273 -0.0533 151 SER A CB  
1293 O  OG  A SER A 151 ? 0.2152 0.3810 0.3458 -0.1870 0.0005  -0.0759 151 SER A OG  
1294 O  OG  B SER A 151 ? 0.0856 0.2430 0.4614 0.0098  -0.0702 0.0732  151 SER A OG  
1295 N  N   . ALA A 152 ? 0.1228 0.0772 0.2477 -0.0062 -0.0829 -0.0307 152 ALA A N   
1296 C  CA  . ALA A 152 ? 0.1595 0.0351 0.2725 0.0082  -0.0877 -0.0333 152 ALA A CA  
1297 C  C   . ALA A 152 ? 0.0991 0.0917 0.2066 0.0093  -0.0640 -0.0057 152 ALA A C   
1298 O  O   . ALA A 152 ? 0.1145 0.0746 0.3188 -0.0109 -0.0293 -0.0193 152 ALA A O   
1299 C  CB  . ALA A 152 ? 0.2062 0.0750 0.2434 0.0006  -0.0509 -0.0441 152 ALA A CB  
1300 N  N   . LYS A 153 ? 0.1145 0.0520 0.2030 0.0162  -0.0520 -0.0119 153 LYS A N   
1301 C  CA  . LYS A 153 ? 0.0917 0.0644 0.2229 0.0197  -0.0548 -0.0140 153 LYS A CA  
1302 C  C   . LYS A 153 ? 0.0759 0.0842 0.2132 0.0154  -0.0386 -0.0164 153 LYS A C   
1303 O  O   . LYS A 153 ? 0.0860 0.0900 0.2222 0.0208  -0.0373 -0.0076 153 LYS A O   
1304 C  CB  . LYS A 153 ? 0.0916 0.0606 0.2337 -0.0031 -0.0560 -0.0070 153 LYS A CB  
1305 C  CG  . LYS A 153 ? 0.1127 0.0920 0.2310 0.0250  -0.0505 -0.0109 153 LYS A CG  
1306 C  CD  . LYS A 153 ? 0.1676 0.0944 0.2220 0.0185  -0.0263 -0.0153 153 LYS A CD  
1307 C  CE  . LYS A 153 ? 0.2001 0.1136 0.2984 0.0423  0.0027  -0.0286 153 LYS A CE  
1308 N  NZ  . LYS A 153 ? 0.3562 0.2163 0.3161 0.0176  0.1066  -0.0307 153 LYS A NZ  
1309 N  N   . PRO A 154 ? 0.0807 0.0926 0.2035 0.0023  -0.0577 -0.0186 154 PRO A N   
1310 C  CA  . PRO A 154 ? 0.0930 0.1216 0.2169 -0.0147 -0.0625 0.0060  154 PRO A CA  
1311 C  C   . PRO A 154 ? 0.0608 0.1288 0.1962 0.0199  -0.0403 0.0082  154 PRO A C   
1312 O  O   . PRO A 154 ? 0.0974 0.1247 0.2125 0.0242  -0.0329 -0.0109 154 PRO A O   
1313 C  CB  . PRO A 154 ? 0.0833 0.1179 0.3091 -0.0131 -0.0560 0.0142  154 PRO A CB  
1314 C  CG  . PRO A 154 ? 0.1152 0.1620 0.2619 -0.0241 -0.0648 0.0346  154 PRO A CG  
1315 C  CD  . PRO A 154 ? 0.0803 0.1204 0.2213 -0.0232 -0.0355 0.0043  154 PRO A CD  
1316 N  N   . GLY A 155 ? 0.0736 0.0785 0.2457 0.0006  -0.0186 -0.0166 155 GLY A N   
1317 C  CA  . GLY A 155 ? 0.1032 0.0555 0.3064 0.0104  -0.0206 0.0012  155 GLY A CA  
1318 C  C   . GLY A 155 ? 0.1057 0.0494 0.2378 0.0216  -0.0283 -0.0207 155 GLY A C   
1319 O  O   . GLY A 155 ? 0.1167 0.0693 0.3181 0.0147  -0.0197 0.0142  155 GLY A O   
1320 N  N   . LEU A 156 ? 0.0763 0.0671 0.2215 0.0164  -0.0331 -0.0186 156 LEU A N   
1321 C  CA  . LEU A 156 ? 0.0854 0.0766 0.2188 0.0269  -0.0498 -0.0269 156 LEU A CA  
1322 C  C   . LEU A 156 ? 0.0753 0.0614 0.1987 0.0068  -0.0359 -0.0230 156 LEU A C   
1323 O  O   . LEU A 156 ? 0.0715 0.0806 0.2168 -0.0081 -0.0344 -0.0020 156 LEU A O   
1324 C  CB  . LEU A 156 ? 0.0767 0.1027 0.2439 0.0232  -0.0487 -0.0035 156 LEU A CB  
1325 C  CG  . LEU A 156 ? 0.0820 0.0960 0.2310 0.0146  -0.0610 -0.0217 156 LEU A CG  
1326 C  CD1 . LEU A 156 ? 0.1044 0.1344 0.2477 -0.0228 -0.0688 0.0051  156 LEU A CD1 
1327 C  CD2 . LEU A 156 ? 0.1054 0.0982 0.2867 0.0406  -0.0693 0.0017  156 LEU A CD2 
1328 N  N   . GLN A 157 ? 0.0789 0.0794 0.2199 -0.0046 -0.0531 -0.0414 157 GLN A N   
1329 C  CA  . GLN A 157 ? 0.0838 0.0724 0.2190 -0.0153 -0.0434 -0.0155 157 GLN A CA  
1330 C  C   . GLN A 157 ? 0.0732 0.0687 0.2071 0.0074  -0.0573 -0.0109 157 GLN A C   
1331 O  O   . GLN A 157 ? 0.0790 0.0948 0.2208 -0.0093 -0.0307 -0.0076 157 GLN A O   
1332 C  CB  . GLN A 157 ? 0.0935 0.0935 0.2381 -0.0170 -0.0483 -0.0377 157 GLN A CB  
1333 C  CG  . GLN A 157 ? 0.1039 0.1259 0.2075 -0.0017 -0.0551 -0.0148 157 GLN A CG  
1334 C  CD  . GLN A 157 ? 0.1075 0.0860 0.2136 -0.0209 -0.0428 -0.0206 157 GLN A CD  
1335 O  OE1 . GLN A 157 ? 0.1556 0.0882 0.2226 0.0183  -0.0463 -0.0155 157 GLN A OE1 
1336 N  NE2 . GLN A 157 ? 0.1313 0.1466 0.2310 -0.0357 -0.0204 -0.0254 157 GLN A NE2 
1337 N  N   . LYS A 158 ? 0.0922 0.0772 0.2084 0.0195  -0.0615 -0.0063 158 LYS A N   
1338 C  CA  . LYS A 158 ? 0.1001 0.0832 0.2308 0.0114  -0.0658 -0.0003 158 LYS A CA  
1339 C  C   . LYS A 158 ? 0.1106 0.0590 0.2055 -0.0031 -0.0401 0.0103  158 LYS A C   
1340 O  O   . LYS A 158 ? 0.1387 0.1158 0.2181 -0.0154 -0.0644 0.0068  158 LYS A O   
1341 C  CB  . LYS A 158 ? 0.1159 0.1190 0.2384 0.0381  -0.0687 -0.0034 158 LYS A CB  
1342 C  CG  . LYS A 158 ? 0.2624 0.1107 0.3382 0.0375  -0.1194 0.0142  158 LYS A CG  
1343 C  CD  . LYS A 158 ? 0.4433 0.1464 0.3578 0.1193  -0.1030 0.0273  158 LYS A CD  
1344 C  CE  . LYS A 158 ? 0.4282 0.2493 0.4841 0.0000  -0.2069 0.1303  158 LYS A CE  
1345 N  NZ  . LYS A 158 ? 0.2912 0.3055 0.4440 0.0060  -0.0988 0.1968  158 LYS A NZ  
1346 N  N   . VAL A 159 ? 0.0895 0.0666 0.2082 0.0129  -0.0555 0.0024  159 VAL A N   
1347 C  CA  . VAL A 159 ? 0.0895 0.0702 0.2269 -0.0114 -0.0370 -0.0197 159 VAL A CA  
1348 C  C   . VAL A 159 ? 0.0819 0.0636 0.2098 -0.0082 -0.0390 -0.0065 159 VAL A C   
1349 O  O   . VAL A 159 ? 0.1102 0.0793 0.2310 -0.0135 -0.0361 -0.0108 159 VAL A O   
1350 C  CB  . VAL A 159 ? 0.1084 0.0728 0.2337 0.0000  -0.0560 -0.0093 159 VAL A CB  
1351 C  CG1 . VAL A 159 ? 0.0920 0.1430 0.2842 -0.0460 -0.0680 0.0152  159 VAL A CG1 
1352 C  CG2 . VAL A 159 ? 0.2136 0.0966 0.2994 0.0670  -0.0908 -0.0498 159 VAL A CG2 
1353 N  N   . VAL A 160 ? 0.1054 0.0423 0.2096 0.0037  -0.0439 -0.0131 160 VAL A N   
1354 C  CA  . VAL A 160 ? 0.1231 0.0661 0.2402 0.0199  -0.0344 -0.0076 160 VAL A CA  
1355 C  C   . VAL A 160 ? 0.1066 0.0687 0.2188 -0.0013 -0.0186 -0.0197 160 VAL A C   
1356 O  O   . VAL A 160 ? 0.1387 0.0784 0.2213 0.0013  -0.0210 -0.0172 160 VAL A O   
1357 C  CB  . VAL A 160 ? 0.3208 0.0643 0.3201 0.0063  -0.0326 -0.0307 160 VAL A CB  
1358 C  CG1 . VAL A 160 ? 0.4706 0.1796 0.2730 0.1479  0.0882  0.0825  160 VAL A CG1 
1359 C  CG2 . VAL A 160 ? 0.1917 0.1556 0.2768 0.0714  -0.0377 -0.0326 160 VAL A CG2 
1360 N  N   . ASP A 161 ? 0.1036 0.0908 0.2127 -0.0230 -0.0434 -0.0159 161 ASP A N   
1361 C  CA  . ASP A 161 ? 0.0992 0.1053 0.2418 -0.0614 -0.0307 -0.0307 161 ASP A CA  
1362 C  C   . ASP A 161 ? 0.1159 0.1301 0.2398 -0.0658 -0.0225 -0.0165 161 ASP A C   
1363 O  O   . ASP A 161 ? 0.1660 0.1771 0.2554 -0.0373 -0.0020 -0.0073 161 ASP A O   
1364 C  CB  . ASP A 161 ? 0.0942 0.1667 0.2508 -0.0489 -0.0472 -0.0284 161 ASP A CB  
1365 C  CG  . ASP A 161 ? 0.1242 0.1583 0.2452 -0.0359 -0.0593 -0.0251 161 ASP A CG  
1366 O  OD1 . ASP A 161 ? 0.1800 0.1665 0.2903 -0.0417 -0.0728 -0.0209 161 ASP A OD1 
1367 O  OD2 . ASP A 161 ? 0.1288 0.2053 0.2714 -0.0370 -0.0644 -0.0324 161 ASP A OD2 
1368 N  N   . VAL A 162 ? 0.1215 0.0966 0.2504 -0.0476 -0.0724 0.0241  162 VAL A N   
1369 C  CA  . VAL A 162 ? 0.0969 0.0935 0.2793 -0.0275 -0.0461 0.0242  162 VAL A CA  
1370 C  C   . VAL A 162 ? 0.0886 0.1477 0.2414 -0.0164 -0.0104 0.0076  162 VAL A C   
1371 O  O   . VAL A 162 ? 0.1028 0.1378 0.2091 -0.0197 -0.0291 -0.0003 162 VAL A O   
1372 C  CB  . VAL A 162 ? 0.1185 0.1316 0.2994 0.0103  -0.0377 0.0238  162 VAL A CB  
1373 C  CG1 . VAL A 162 ? 0.1163 0.2269 0.3433 0.0225  -0.0335 -0.0010 162 VAL A CG1 
1374 C  CG2 . VAL A 162 ? 0.1599 0.0709 0.3199 -0.0043 0.0322  0.0141  162 VAL A CG2 
1375 N  N   . LEU A 163 ? 0.0882 0.1228 0.2172 -0.0251 -0.0399 -0.0155 163 LEU A N   
1376 C  CA  . LEU A 163 ? 0.0856 0.0951 0.2242 -0.0175 -0.0241 -0.0046 163 LEU A CA  
1377 C  C   . LEU A 163 ? 0.0834 0.1154 0.2053 -0.0074 -0.0491 -0.0203 163 LEU A C   
1378 O  O   . LEU A 163 ? 0.0951 0.1405 0.2287 -0.0181 -0.0208 -0.0120 163 LEU A O   
1379 C  CB  . LEU A 163 ? 0.0976 0.0825 0.2442 0.0031  -0.0272 0.0097  163 LEU A CB  
1380 C  CG  . LEU A 163 ? 0.1168 0.0856 0.2120 -0.0115 -0.0291 0.0027  163 LEU A CG  
1381 C  CD1 . LEU A 163 ? 0.1046 0.1009 0.2842 -0.0153 -0.0450 0.0284  163 LEU A CD1 
1382 C  CD2 . LEU A 163 ? 0.1385 0.0925 0.2258 -0.0265 -0.0276 -0.0023 163 LEU A CD2 
1383 N  N   . ASP A 164 ? 0.1238 0.1075 0.2021 -0.0217 -0.0252 -0.0264 164 ASP A N   
1384 C  CA  . ASP A 164 ? 0.1624 0.1520 0.2560 -0.0474 -0.0087 -0.0318 164 ASP A CA  
1385 C  C   . ASP A 164 ? 0.1453 0.1640 0.2245 -0.0524 -0.0054 -0.0308 164 ASP A C   
1386 O  O   . ASP A 164 ? 0.1741 0.1913 0.2815 -0.0057 0.0208  -0.0597 164 ASP A O   
1387 C  CB  . ASP A 164 ? 0.2222 0.1888 0.2813 -0.0438 0.0000  -0.0794 164 ASP A CB  
1388 C  CG  . ASP A 164 ? 0.2513 0.2594 0.2818 -0.1150 -0.0608 -0.0573 164 ASP A CG  
1389 O  OD1 . ASP A 164 ? 0.2442 0.3264 0.3542 -0.0627 -0.0166 -0.0298 164 ASP A OD1 
1390 O  OD2 . ASP A 164 ? 0.2281 0.6919 0.2969 -0.0148 0.0010  -0.1208 164 ASP A OD2 
1391 N  N   . SER A 165 ? 0.1520 0.1708 0.1879 -0.0197 -0.0359 -0.0120 165 SER A N   
1392 C  CA  . SER A 165 ? 0.1247 0.1796 0.2276 -0.0370 -0.0401 -0.0151 165 SER A CA  
1393 C  C   . SER A 165 ? 0.1116 0.2021 0.1884 -0.0491 -0.0054 -0.0098 165 SER A C   
1394 O  O   . SER A 165 ? 0.1159 0.2030 0.2172 -0.0342 -0.0282 0.0093  165 SER A O   
1395 C  CB  . SER A 165 ? 0.1394 0.2380 0.2032 -0.0348 -0.0522 0.0573  165 SER A CB  
1396 O  OG  . SER A 165 ? 0.1414 0.2109 0.2497 -0.0272 -0.0270 0.0175  165 SER A OG  
1397 N  N   . ILE A 166 ? 0.0895 0.1256 0.1941 -0.0005 -0.0291 -0.0173 166 ILE A N   
1398 C  CA  . ILE A 166 ? 0.0992 0.1493 0.2154 -0.0219 -0.0357 -0.0285 166 ILE A CA  
1399 C  C   . ILE A 166 ? 0.0860 0.1213 0.1762 -0.0210 -0.0176 -0.0313 166 ILE A C   
1400 O  O   . ILE A 166 ? 0.1195 0.1613 0.1850 0.0093  -0.0196 -0.0274 166 ILE A O   
1401 C  CB  . ILE A 166 ? 0.0842 0.1046 0.2285 -0.0131 -0.0296 -0.0249 166 ILE A CB  
1402 C  CG1 . ILE A 166 ? 0.0864 0.1298 0.2111 -0.0046 -0.0329 0.0060  166 ILE A CG1 
1403 C  CG2 . ILE A 166 ? 0.1084 0.1057 0.3003 -0.0197 -0.0263 0.0068  166 ILE A CG2 
1404 C  CD1 . ILE A 166 ? 0.1439 0.1462 0.2100 -0.0048 -0.0388 -0.0286 166 ILE A CD1 
1405 N  N   . LYS A 167 ? 0.1261 0.1642 0.1753 0.0137  -0.0217 -0.0258 167 LYS A N   
1406 C  CA  . LYS A 167 ? 0.1288 0.1721 0.2217 0.0410  -0.0381 -0.0417 167 LYS A CA  
1407 C  C   . LYS A 167 ? 0.1213 0.2442 0.1712 0.0242  -0.0023 -0.0226 167 LYS A C   
1408 O  O   . LYS A 167 ? 0.1466 0.2423 0.1958 0.0454  -0.0286 -0.0361 167 LYS A O   
1409 C  CB  . LYS A 167 ? 0.1789 0.1985 0.2353 0.0520  -0.0449 -0.0790 167 LYS A CB  
1410 C  CG  . LYS A 167 ? 0.2125 0.2481 0.3009 0.0856  -0.0208 -0.0493 167 LYS A CG  
1411 C  CD  . LYS A 167 ? 0.3634 0.2694 0.3907 0.1500  -0.1595 -0.1798 167 LYS A CD  
1412 C  CE  . LYS A 167 ? 0.5367 0.3201 0.3759 0.2029  -0.1456 -0.1018 167 LYS A CE  
1413 N  NZ  . LYS A 167 ? 0.6100 0.4523 0.5108 0.1921  0.0208  -0.2298 167 LYS A NZ  
1414 N  N   . THR A 168 ? 0.1179 0.2269 0.2310 0.0186  -0.0031 -0.0230 168 THR A N   
1415 C  CA  . THR A 168 ? 0.1163 0.3124 0.2558 -0.0346 0.0129  -0.0364 168 THR A CA  
1416 C  C   . THR A 168 ? 0.0960 0.3239 0.2339 0.0048  -0.0390 0.0109  168 THR A C   
1417 O  O   . THR A 168 ? 0.1115 0.2240 0.2391 -0.0241 -0.0153 0.0020  168 THR A O   
1418 C  CB  . THR A 168 ? 0.1694 0.3727 0.2439 -0.0414 0.0315  -0.0146 168 THR A CB  
1419 O  OG1 . THR A 168 ? 0.1631 0.4025 0.2310 0.0220  0.0126  -0.0092 168 THR A OG1 
1420 C  CG2 . THR A 168 ? 0.1710 0.3801 0.2418 0.0399  -0.0063 -0.0529 168 THR A CG2 
1421 N  N   . LYS A 169 ? 0.1071 0.2865 0.2087 -0.0454 -0.0284 0.0060  169 LYS A N   
1422 C  CA  . LYS A 169 ? 0.0816 0.2682 0.2628 -0.0294 -0.0136 0.0024  169 LYS A CA  
1423 C  C   . LYS A 169 ? 0.0740 0.2673 0.2612 -0.0412 0.0296  0.0031  169 LYS A C   
1424 O  O   . LYS A 169 ? 0.1247 0.4099 0.2433 -0.0441 0.0068  0.0302  169 LYS A O   
1425 C  CB  . LYS A 169 ? 0.0700 0.3526 0.2554 -0.0416 -0.0209 -0.0182 169 LYS A CB  
1426 C  CG  . LYS A 169 ? 0.1127 0.3330 0.2628 -0.0364 -0.0513 0.0060  169 LYS A CG  
1427 C  CD  . LYS A 169 ? 0.1048 0.4135 0.3348 -0.0068 -0.0513 -0.0214 169 LYS A CD  
1428 C  CE  . LYS A 169 ? 0.2141 0.4607 0.6959 -0.1066 -0.1506 -0.0724 169 LYS A CE  
1429 N  NZ  . LYS A 169 ? 0.3625 0.7261 0.9257 -0.0666 -0.3928 -0.1234 169 LYS A NZ  
1430 N  N   . GLY A 170 ? 0.0948 0.1597 0.2795 -0.0392 -0.0175 -0.0054 170 GLY A N   
1431 C  CA  . GLY A 170 ? 0.1120 0.1942 0.3386 -0.0758 -0.0331 0.0241  170 GLY A CA  
1432 C  C   . GLY A 170 ? 0.1446 0.2240 0.2660 -0.0878 -0.0104 0.0173  170 GLY A C   
1433 O  O   . GLY A 170 ? 0.2384 0.1996 0.4217 -0.1439 -0.1076 0.0361  170 GLY A O   
1434 N  N   . LYS A 171 ? 0.1109 0.1631 0.2339 -0.0361 -0.0142 0.0040  171 LYS A N   
1435 C  CA  . LYS A 171 ? 0.1070 0.1865 0.2169 -0.0348 -0.0196 0.0285  171 LYS A CA  
1436 C  C   . LYS A 171 ? 0.1392 0.1376 0.1985 -0.0593 -0.0230 0.0129  171 LYS A C   
1437 O  O   . LYS A 171 ? 0.1071 0.1545 0.2071 -0.0177 -0.0137 0.0148  171 LYS A O   
1438 C  CB  . LYS A 171 ? 0.0991 0.1899 0.2666 -0.0065 -0.0285 -0.0142 171 LYS A CB  
1439 C  CG  . LYS A 171 ? 0.1435 0.2181 0.3185 -0.0259 0.0208  -0.0392 171 LYS A CG  
1440 C  CD  . LYS A 171 ? 0.2486 0.2587 0.3079 -0.0658 0.0509  -0.0471 171 LYS A CD  
1441 C  CE  . LYS A 171 ? 0.4505 0.2372 0.5037 -0.0586 -0.0882 0.1035  171 LYS A CE  
1442 N  NZ  . LYS A 171 ? 0.4501 0.4381 0.4295 -0.2335 -0.0568 0.0789  171 LYS A NZ  
1443 N  N   . SER A 172 ? 0.1116 0.1532 0.2224 -0.0436 -0.0065 0.0048  172 SER A N   
1444 C  CA  . SER A 172 ? 0.1360 0.1039 0.2222 -0.0059 -0.0307 0.0142  172 SER A CA  
1445 C  C   . SER A 172 ? 0.1504 0.1351 0.1838 -0.0412 -0.0108 0.0307  172 SER A C   
1446 O  O   . SER A 172 ? 0.1367 0.1872 0.1999 -0.0241 -0.0229 0.0373  172 SER A O   
1447 C  CB  . SER A 172 ? 0.1685 0.0926 0.2815 -0.0447 0.0054  0.0192  172 SER A CB  
1448 O  OG  . SER A 172 ? 0.1536 0.1333 0.3598 -0.0093 0.0197  0.0626  172 SER A OG  
1449 N  N   . ALA A 173 ? 0.1145 0.1547 0.1994 -0.0175 -0.0175 0.0353  173 ALA A N   
1450 C  CA  . ALA A 173 ? 0.1403 0.1674 0.1789 0.0093  -0.0229 -0.0040 173 ALA A CA  
1451 C  C   . ALA A 173 ? 0.1590 0.1498 0.1805 -0.0082 -0.0119 0.0313  173 ALA A C   
1452 O  O   . ALA A 173 ? 0.1316 0.1353 0.2046 0.0043  -0.0141 0.0195  173 ALA A O   
1453 C  CB  . ALA A 173 ? 0.1592 0.1818 0.2466 -0.0153 -0.0197 -0.0219 173 ALA A CB  
1454 N  N   . ASP A 174 ? 0.1649 0.2578 0.1915 0.0535  -0.0186 0.0537  174 ASP A N   
1455 C  CA  . ASP A 174 ? 0.1450 0.2055 0.2380 0.0498  -0.0197 0.0715  174 ASP A CA  
1456 C  C   . ASP A 174 ? 0.1622 0.1380 0.1773 0.0274  -0.0469 0.0153  174 ASP A C   
1457 O  O   . ASP A 174 ? 0.1563 0.2075 0.2283 0.0006  -0.0263 -0.0242 174 ASP A O   
1458 C  CB  . ASP A 174 ? 0.1710 0.2741 0.2705 0.0882  -0.0240 0.0842  174 ASP A CB  
1459 C  CG  . ASP A 174 ? 0.4189 0.2901 0.4020 0.0054  -0.1238 0.1185  174 ASP A CG  
1460 O  OD1 . ASP A 174 ? 0.4675 0.5231 0.5368 -0.0328 0.0225  -0.0441 174 ASP A OD1 
1461 O  OD2 . ASP A 174 ? 0.7091 0.8906 0.4221 0.4314  -0.0838 -0.1110 174 ASP A OD2 
1462 N  N   . PHE A 175 ? 0.1347 0.1045 0.1735 0.0017  -0.0331 0.0104  175 PHE A N   
1463 C  CA  . PHE A 175 ? 0.1127 0.1080 0.2138 0.0093  -0.0164 0.0120  175 PHE A CA  
1464 C  C   . PHE A 175 ? 0.1118 0.0825 0.2048 -0.0320 -0.0443 -0.0015 175 PHE A C   
1465 O  O   . PHE A 175 ? 0.1353 0.1170 0.2281 0.0335  -0.0445 -0.0170 175 PHE A O   
1466 C  CB  . PHE A 175 ? 0.1124 0.1109 0.2021 -0.0159 -0.0441 0.0166  175 PHE A CB  
1467 C  CG  . PHE A 175 ? 0.0951 0.0978 0.2082 0.0113  -0.0284 0.0081  175 PHE A CG  
1468 C  CD1 . PHE A 175 ? 0.1396 0.1159 0.2348 0.0264  0.0000  -0.0194 175 PHE A CD1 
1469 C  CD2 . PHE A 175 ? 0.1134 0.1097 0.2041 0.0166  -0.0432 0.0461  175 PHE A CD2 
1470 C  CE1 . PHE A 175 ? 0.1525 0.1088 0.2157 -0.0068 -0.0219 -0.0293 175 PHE A CE1 
1471 C  CE2 . PHE A 175 ? 0.1328 0.1194 0.2346 -0.0063 -0.0219 0.0073  175 PHE A CE2 
1472 C  CZ  . PHE A 175 ? 0.1468 0.0973 0.2425 0.0370  -0.0239 -0.0013 175 PHE A CZ  
1473 N  N   . THR A 176 ? 0.1206 0.0942 0.2233 -0.0041 -0.0478 0.0118  176 THR A N   
1474 C  CA  . THR A 176 ? 0.1353 0.1054 0.2238 -0.0013 -0.0438 0.0392  176 THR A CA  
1475 C  C   . THR A 176 ? 0.1221 0.0450 0.2046 -0.0026 -0.0447 0.0344  176 THR A C   
1476 O  O   . THR A 176 ? 0.1507 0.0710 0.2459 -0.0093 -0.0644 0.0263  176 THR A O   
1477 C  CB  . THR A 176 ? 0.1798 0.0960 0.2254 -0.0337 -0.0834 0.0372  176 THR A CB  
1478 O  OG1 . THR A 176 ? 0.2026 0.1780 0.2229 0.0485  -0.0516 0.0115  176 THR A OG1 
1479 C  CG2 . THR A 176 ? 0.1562 0.1766 0.3939 -0.0658 -0.0737 0.1534  176 THR A CG2 
1480 N  N   . ASN A 177 ? 0.1184 0.0820 0.1854 -0.0140 -0.0505 0.0146  177 ASN A N   
1481 C  CA  . ASN A 177 ? 0.1324 0.0960 0.2087 -0.0307 -0.0623 0.0335  177 ASN A CA  
1482 C  C   . ASN A 177 ? 0.1498 0.0790 0.2430 -0.0324 -0.0728 0.0359  177 ASN A C   
1483 O  O   . ASN A 177 ? 0.1737 0.1489 0.3377 -0.0772 -0.1098 0.1054  177 ASN A O   
1484 C  CB  . ASN A 177 ? 0.1019 0.1240 0.2346 -0.0194 -0.0803 0.0491  177 ASN A CB  
1485 C  CG  . ASN A 177 ? 0.1216 0.1360 0.2542 0.0076  -0.0794 0.0242  177 ASN A CG  
1486 O  OD1 . ASN A 177 ? 0.1595 0.1238 0.3287 -0.0051 -0.0251 0.0604  177 ASN A OD1 
1487 N  ND2 . ASN A 177 ? 0.1644 0.1335 0.2265 -0.0068 -0.0957 0.0355  177 ASN A ND2 
1488 N  N   . PHE A 178 ? 0.1259 0.0842 0.1888 -0.0060 -0.0460 0.0199  178 PHE A N   
1489 C  CA  . PHE A 178 ? 0.1297 0.0473 0.2057 -0.0020 -0.0485 0.0104  178 PHE A CA  
1490 C  C   . PHE A 178 ? 0.1150 0.0759 0.1992 -0.0031 -0.0392 0.0164  178 PHE A C   
1491 O  O   . PHE A 178 ? 0.1611 0.0838 0.2116 -0.0242 -0.0399 0.0093  178 PHE A O   
1492 C  CB  . PHE A 178 ? 0.1128 0.0790 0.2060 0.0126  -0.0272 0.0284  178 PHE A CB  
1493 C  CG  . PHE A 178 ? 0.1134 0.0640 0.2035 -0.0006 -0.0027 0.0228  178 PHE A CG  
1494 C  CD1 . PHE A 178 ? 0.1933 0.0728 0.2125 -0.0170 -0.0013 0.0131  178 PHE A CD1 
1495 C  CD2 . PHE A 178 ? 0.1124 0.0546 0.2109 0.0160  -0.0515 0.0104  178 PHE A CD2 
1496 C  CE1 . PHE A 178 ? 0.1412 0.0697 0.2141 0.0065  -0.0377 -0.0026 178 PHE A CE1 
1497 C  CE2 . PHE A 178 ? 0.0886 0.0680 0.2188 0.0142  -0.0238 0.0175  178 PHE A CE2 
1498 C  CZ  . PHE A 178 ? 0.1037 0.1048 0.1870 0.0115  -0.0379 0.0161  178 PHE A CZ  
1499 N  N   . ASP A 179 ? 0.0846 0.1003 0.1985 0.0063  -0.0326 0.0173  179 ASP A N   
1500 C  CA  . ASP A 179 ? 0.0776 0.0938 0.2371 0.0059  -0.0252 0.0115  179 ASP A CA  
1501 C  C   . ASP A 179 ? 0.0856 0.0886 0.1856 0.0308  -0.0068 -0.0098 179 ASP A C   
1502 O  O   . ASP A 179 ? 0.1172 0.0727 0.2138 0.0120  -0.0331 0.0024  179 ASP A O   
1503 C  CB  . ASP A 179 ? 0.0788 0.1611 0.2236 0.0010  -0.0252 0.0261  179 ASP A CB  
1504 C  CG  . ASP A 179 ? 0.1124 0.1435 0.2226 0.0230  -0.0307 0.0184  179 ASP A CG  
1505 O  OD1 . ASP A 179 ? 0.1270 0.1125 0.2278 0.0379  -0.0208 0.0198  179 ASP A OD1 
1506 O  OD2 . ASP A 179 ? 0.1082 0.3314 0.3201 0.0333  -0.0135 -0.0394 179 ASP A OD2 
1507 N  N   . PRO A 180 ? 0.0873 0.0834 0.2037 0.0109  -0.0320 0.0160  180 PRO A N   
1508 C  CA  . PRO A 180 ? 0.0719 0.1477 0.2100 0.0027  -0.0375 0.0109  180 PRO A CA  
1509 C  C   . PRO A 180 ? 0.0784 0.1066 0.1899 0.0250  -0.0296 0.0000  180 PRO A C   
1510 O  O   . PRO A 180 ? 0.1091 0.0976 0.2053 0.0164  -0.0507 0.0093  180 PRO A O   
1511 C  CB  . PRO A 180 ? 0.0967 0.1088 0.2684 -0.0102 -0.0199 0.0038  180 PRO A CB  
1512 C  CG  . PRO A 180 ? 0.1586 0.0856 0.2168 -0.0225 -0.0375 0.0054  180 PRO A CG  
1513 C  CD  . PRO A 180 ? 0.1319 0.1014 0.2003 -0.0219 -0.0307 0.0015  180 PRO A CD  
1514 N  N   . ARG A 181 ? 0.0687 0.0750 0.2310 0.0065  -0.0068 -0.0068 181 ARG A N   
1515 C  CA  . ARG A 181 ? 0.0969 0.0710 0.2432 0.0324  -0.0026 0.0136  181 ARG A CA  
1516 C  C   . ARG A 181 ? 0.0697 0.0898 0.2231 0.0425  -0.0292 0.0307  181 ARG A C   
1517 O  O   . ARG A 181 ? 0.1159 0.1120 0.2229 0.0166  -0.0326 0.0093  181 ARG A O   
1518 C  CB  . ARG A 181 ? 0.0908 0.0657 0.2481 0.0292  -0.0357 -0.0046 181 ARG A CB  
1519 C  CG  . ARG A 181 ? 0.1536 0.0715 0.2644 0.0372  0.0048  -0.0216 181 ARG A CG  
1520 C  CD  . ARG A 181 ? 0.1563 0.1071 0.3449 0.0441  0.0643  -0.0104 181 ARG A CD  
1521 N  NE  . ARG A 181 ? 0.1204 0.0922 0.3535 0.0205  0.0465  0.0164  181 ARG A NE  
1522 C  CZ  . ARG A 181 ? 0.1249 0.1238 0.3519 -0.0003 0.0186  0.0219  181 ARG A CZ  
1523 N  NH1 . ARG A 181 ? 0.1762 0.1425 0.4474 0.0242  0.0719  0.0271  181 ARG A NH1 
1524 N  NH2 . ARG A 181 ? 0.1859 0.1845 0.3855 0.1062  -0.0087 0.0219  181 ARG A NH2 
1525 N  N   . GLY A 182 ? 0.1097 0.0781 0.2231 0.0183  -0.0315 0.0071  182 GLY A N   
1526 C  CA  . GLY A 182 ? 0.1333 0.0731 0.2172 0.0262  -0.0500 0.0082  182 GLY A CA  
1527 C  C   . GLY A 182 ? 0.1143 0.0891 0.2064 0.0294  -0.0342 -0.0115 182 GLY A C   
1528 O  O   . GLY A 182 ? 0.1310 0.0935 0.2381 0.0082  -0.0313 -0.0093 182 GLY A O   
1529 N  N   . LEU A 183 ? 0.0969 0.1023 0.1969 0.0342  -0.0313 -0.0082 183 LEU A N   
1530 C  CA  . LEU A 183 ? 0.0881 0.1197 0.2116 0.0307  -0.0353 0.0003  183 LEU A CA  
1531 C  C   . LEU A 183 ? 0.0900 0.1003 0.2050 0.0098  -0.0249 0.0142  183 LEU A C   
1532 O  O   . LEU A 183 ? 0.1154 0.0978 0.2648 0.0350  -0.0340 0.0318  183 LEU A O   
1533 C  CB  . LEU A 183 ? 0.1084 0.1132 0.2134 0.0368  -0.0516 0.0115  183 LEU A CB  
1534 C  CG  . LEU A 183 ? 0.1105 0.1319 0.1969 0.0595  -0.0386 0.0195  183 LEU A CG  
1535 C  CD1 . LEU A 183 ? 0.1229 0.1604 0.2211 0.0403  -0.0227 0.0209  183 LEU A CD1 
1536 C  CD2 . LEU A 183 ? 0.1543 0.1310 0.2511 0.0762  0.0000  0.0120  183 LEU A CD2 
1537 N  N   . LEU A 184 ? 0.1134 0.0886 0.1949 -0.0006 -0.0115 0.0060  184 LEU A N   
1538 C  CA  . LEU A 184 ? 0.1430 0.0627 0.2120 0.0142  -0.0065 0.0175  184 LEU A CA  
1539 C  C   . LEU A 184 ? 0.0985 0.1008 0.1965 -0.0120 -0.0417 0.0292  184 LEU A C   
1540 O  O   . LEU A 184 ? 0.1541 0.1179 0.2867 -0.0346 -0.0948 0.0219  184 LEU A O   
1541 C  CB  . LEU A 184 ? 0.1064 0.0627 0.2432 -0.0129 -0.0192 -0.0118 184 LEU A CB  
1542 C  CG  . LEU A 184 ? 0.0917 0.0947 0.2427 -0.0126 -0.0126 0.0063  184 LEU A CG  
1543 C  CD1 . LEU A 184 ? 0.1249 0.1150 0.2468 0.0204  -0.0197 -0.0012 184 LEU A CD1 
1544 C  CD2 . LEU A 184 ? 0.0985 0.1237 0.3260 0.0115  -0.0241 0.0031  184 LEU A CD2 
1545 N  N   . PRO A 185 ? 0.0976 0.0976 0.1877 0.0054  -0.0342 0.0175  185 PRO A N   
1546 C  CA  . PRO A 185 ? 0.0908 0.1247 0.2129 0.0024  -0.0275 0.0421  185 PRO A CA  
1547 C  C   . PRO A 185 ? 0.0834 0.0825 0.2028 0.0054  -0.0537 0.0208  185 PRO A C   
1548 O  O   . PRO A 185 ? 0.0886 0.0803 0.2761 0.0006  -0.0474 0.0254  185 PRO A O   
1549 C  CB  . PRO A 185 ? 0.0842 0.1039 0.2560 0.0041  -0.0430 0.0198  185 PRO A CB  
1550 C  CG  . PRO A 185 ? 0.0820 0.1062 0.2157 0.0265  -0.0364 -0.0057 185 PRO A CG  
1551 C  CD  . PRO A 185 ? 0.1089 0.1313 0.1893 0.0165  -0.0430 -0.0030 185 PRO A CD  
1552 N  N   . GLU A 186 ? 0.1124 0.0904 0.2626 -0.0035 -0.0410 0.0253  186 GLU A N   
1553 C  CA  . GLU A 186 ? 0.0634 0.1230 0.2802 -0.0160 -0.0469 -0.0020 186 GLU A CA  
1554 C  C   . GLU A 186 ? 0.0856 0.1208 0.2448 -0.0208 -0.0373 0.0339  186 GLU A C   
1555 O  O   . GLU A 186 ? 0.0816 0.1622 0.3082 0.0131  -0.0344 -0.0151 186 GLU A O   
1556 C  CB  . GLU A 186 ? 0.1154 0.1685 0.2883 -0.0577 -0.0653 0.0373  186 GLU A CB  
1557 C  CG  . GLU A 186 ? 0.1412 0.1240 0.3747 -0.0507 -0.0856 0.0076  186 GLU A CG  
1558 C  CD  . GLU A 186 ? 0.1349 0.1376 0.4241 -0.0214 -0.0816 0.0405  186 GLU A CD  
1559 O  OE1 . GLU A 186 ? 0.1914 0.1965 0.4679 -0.0746 -0.1089 0.1262  186 GLU A OE1 
1560 O  OE2 . GLU A 186 ? 0.2215 0.1242 0.5231 -0.0546 -0.0656 0.0196  186 GLU A OE2 
1561 N  N   . SER A 187 ? 0.0741 0.1768 0.2224 -0.0093 -0.0381 0.0357  187 SER A N   
1562 C  CA  . SER A 187 ? 0.0746 0.1791 0.2292 -0.0230 -0.0395 0.0373  187 SER A CA  
1563 C  C   . SER A 187 ? 0.0816 0.1324 0.2152 -0.0091 -0.0229 0.0175  187 SER A C   
1564 O  O   . SER A 187 ? 0.0649 0.1705 0.2664 -0.0120 -0.0071 -0.0082 187 SER A O   
1565 C  CB  . SER A 187 ? 0.1154 0.2502 0.2001 -0.0109 -0.0485 0.0544  187 SER A CB  
1566 O  OG  . SER A 187 ? 0.0966 0.2206 0.2382 -0.0263 -0.0412 0.0549  187 SER A OG  
1567 N  N   . LEU A 188 ? 0.0789 0.1240 0.2820 -0.0027 -0.0049 -0.0171 188 LEU A N   
1568 C  CA  . LEU A 188 ? 0.0754 0.1641 0.2587 -0.0153 -0.0370 -0.0153 188 LEU A CA  
1569 C  C   . LEU A 188 ? 0.0715 0.1633 0.2398 0.0115  -0.0219 0.0020  188 LEU A C   
1570 O  O   . LEU A 188 ? 0.0965 0.2666 0.2964 -0.0388 -0.0436 -0.0454 188 LEU A O   
1571 C  CB  . LEU A 188 ? 0.1163 0.1592 0.2653 0.0063  -0.0196 -0.0359 188 LEU A CB  
1572 C  CG  . LEU A 188 ? 0.1080 0.1529 0.2906 -0.0375 -0.0208 -0.0386 188 LEU A CG  
1573 C  CD1 . LEU A 188 ? 0.1317 0.1344 0.3449 -0.0043 -0.0450 -0.0359 188 LEU A CD1 
1574 C  CD2 . LEU A 188 ? 0.0958 0.1881 0.3402 0.0120  0.0013  -0.0024 188 LEU A CD2 
1575 N  N   . ASP A 189 ? 0.0766 0.1967 0.2256 0.0137  -0.0174 0.0024  189 ASP A N   
1576 C  CA  . ASP A 189 ? 0.0834 0.2132 0.2240 -0.0434 -0.0153 -0.0199 189 ASP A CA  
1577 C  C   . ASP A 189 ? 0.0891 0.1511 0.2245 -0.0141 -0.0164 -0.0107 189 ASP A C   
1578 O  O   . ASP A 189 ? 0.0812 0.1233 0.2342 -0.0151 -0.0186 -0.0098 189 ASP A O   
1579 C  CB  . ASP A 189 ? 0.1419 0.3219 0.2666 -0.1280 0.0035  0.0383  189 ASP A CB  
1580 C  CG  . ASP A 189 ? 0.1735 0.4541 0.2777 -0.0474 -0.0006 0.0097  189 ASP A CG  
1581 O  OD1 . ASP A 189 ? 0.2028 0.5935 0.4176 -0.1379 0.1058  -0.1001 189 ASP A OD1 
1582 O  OD2 . ASP A 189 ? 0.2217 0.6782 0.2989 -0.2082 -0.0776 0.1555  189 ASP A OD2 
1583 N  N   . TYR A 190 ? 0.0859 0.1668 0.1978 -0.0315 -0.0216 0.0120  190 TYR A N   
1584 C  CA  . TYR A 190 ? 0.0974 0.1340 0.1674 -0.0296 -0.0186 0.0108  190 TYR A CA  
1585 C  C   . TYR A 190 ? 0.0994 0.0864 0.1665 -0.0081 -0.0174 0.0034  190 TYR A C   
1586 O  O   . TYR A 190 ? 0.1014 0.1439 0.1942 -0.0006 -0.0193 0.0147  190 TYR A O   
1587 C  CB  . TYR A 190 ? 0.1152 0.1333 0.2269 -0.0065 -0.0206 0.0253  190 TYR A CB  
1588 C  CG  . TYR A 190 ? 0.0812 0.1132 0.2213 -0.0230 -0.0351 0.0217  190 TYR A CG  
1589 C  CD1 . TYR A 190 ? 0.0996 0.1571 0.1990 -0.0120 -0.0375 0.0015  190 TYR A CD1 
1590 C  CD2 . TYR A 190 ? 0.0940 0.1428 0.2066 0.0005  0.0027  0.0057  190 TYR A CD2 
1591 C  CE1 . TYR A 190 ? 0.1168 0.1238 0.2254 -0.0263 -0.0441 0.0161  190 TYR A CE1 
1592 C  CE2 . TYR A 190 ? 0.1240 0.1337 0.2324 -0.0154 -0.0231 -0.0108 190 TYR A CE2 
1593 C  CZ  . TYR A 190 ? 0.1577 0.1349 0.2249 0.0000  -0.0445 -0.0071 190 TYR A CZ  
1594 O  OH  . TYR A 190 ? 0.1554 0.1203 0.2773 0.0175  -0.0456 -0.0171 190 TYR A OH  
1595 N  N   . TRP A 191 ? 0.0938 0.0702 0.1911 -0.0164 -0.0318 -0.0076 191 TRP A N   
1596 C  CA  . TRP A 191 ? 0.0793 0.0737 0.1717 0.0019  -0.0340 0.0006  191 TRP A CA  
1597 C  C   . TRP A 191 ? 0.1111 0.0960 0.1466 0.0296  -0.0098 0.0020  191 TRP A C   
1598 O  O   . TRP A 191 ? 0.1298 0.0912 0.1737 -0.0284 -0.0197 -0.0031 191 TRP A O   
1599 C  CB  . TRP A 191 ? 0.0794 0.0895 0.2389 -0.0135 -0.0017 -0.0037 191 TRP A CB  
1600 C  CG  . TRP A 191 ? 0.0935 0.1125 0.2091 0.0000  -0.0388 0.0085  191 TRP A CG  
1601 C  CD1 . TRP A 191 ? 0.1021 0.0781 0.2328 0.0087  -0.0086 0.0197  191 TRP A CD1 
1602 C  CD2 . TRP A 191 ? 0.0803 0.0940 0.2247 0.0296  -0.0274 0.0218  191 TRP A CD2 
1603 N  NE1 . TRP A 191 ? 0.1188 0.0992 0.2533 -0.0137 -0.0071 0.0333  191 TRP A NE1 
1604 C  CE2 . TRP A 191 ? 0.1272 0.0635 0.2531 0.0397  -0.0109 0.0115  191 TRP A CE2 
1605 C  CE3 . TRP A 191 ? 0.0832 0.0886 0.2275 -0.0054 -0.0441 0.0131  191 TRP A CE3 
1606 C  CZ2 . TRP A 191 ? 0.1380 0.0649 0.2730 0.0227  -0.0285 0.0109  191 TRP A CZ2 
1607 C  CZ3 . TRP A 191 ? 0.0921 0.1039 0.2642 -0.0108 -0.0375 0.0109  191 TRP A CZ3 
1608 C  CH2 . TRP A 191 ? 0.1186 0.0922 0.2761 -0.0109 -0.0348 0.0034  191 TRP A CH2 
1609 N  N   . THR A 192 ? 0.1037 0.0864 0.1789 0.0020  -0.0274 0.0109  192 THR A N   
1610 C  CA  . THR A 192 ? 0.0952 0.0863 0.1768 0.0076  -0.0388 0.0019  192 THR A CA  
1611 C  C   . THR A 192 ? 0.0842 0.0958 0.1527 0.0137  -0.0226 -0.0113 192 THR A C   
1612 O  O   . THR A 192 ? 0.1037 0.1193 0.1601 0.0019  -0.0285 -0.0049 192 THR A O   
1613 C  CB  . THR A 192 ? 0.0869 0.0819 0.1834 0.0059  -0.0260 0.0137  192 THR A CB  
1614 O  OG1 . THR A 192 ? 0.1010 0.0838 0.2003 0.0020  -0.0322 0.0003  192 THR A OG1 
1615 C  CG2 . THR A 192 ? 0.1195 0.1430 0.1633 0.0419  -0.0294 0.0091  192 THR A CG2 
1616 N  N   . TYR A 193 ? 0.0732 0.0882 0.1897 0.0031  -0.0142 -0.0082 193 TYR A N   
1617 C  CA  . TYR A 193 ? 0.0763 0.0949 0.1906 0.0059  -0.0303 0.0031  193 TYR A CA  
1618 C  C   . TYR A 193 ? 0.0890 0.0701 0.1780 0.0258  -0.0285 -0.0131 193 TYR A C   
1619 O  O   . TYR A 193 ? 0.0873 0.0886 0.1759 -0.0030 -0.0401 0.0024  193 TYR A O   
1620 C  CB  . TYR A 193 ? 0.0922 0.1030 0.1956 0.0035  -0.0344 -0.0024 193 TYR A CB  
1621 C  CG  . TYR A 193 ? 0.0969 0.1084 0.1650 -0.0104 -0.0386 0.0125  193 TYR A CG  
1622 C  CD1 . TYR A 193 ? 0.0829 0.0794 0.1820 0.0071  -0.0210 -0.0104 193 TYR A CD1 
1623 C  CD2 . TYR A 193 ? 0.0965 0.0983 0.1791 0.0005  -0.0259 0.0046  193 TYR A CD2 
1624 C  CE1 . TYR A 193 ? 0.0662 0.0675 0.1920 0.0130  -0.0274 0.0076  193 TYR A CE1 
1625 C  CE2 . TYR A 193 ? 0.0684 0.0939 0.1800 0.0043  -0.0326 -0.0104 193 TYR A CE2 
1626 C  CZ  . TYR A 193 ? 0.0634 0.0599 0.1746 0.0142  -0.0309 -0.0020 193 TYR A CZ  
1627 O  OH  . TYR A 193 ? 0.0833 0.0467 0.1834 0.0015  -0.0280 -0.0063 193 TYR A OH  
1628 N  N   . PRO A 194 ? 0.0741 0.1221 0.1773 -0.0043 -0.0315 -0.0043 194 PRO A N   
1629 C  CA  . PRO A 194 ? 0.0969 0.0847 0.1852 -0.0131 -0.0154 -0.0286 194 PRO A CA  
1630 C  C   . PRO A 194 ? 0.0847 0.0719 0.1638 0.0017  -0.0274 -0.0176 194 PRO A C   
1631 O  O   . PRO A 194 ? 0.1000 0.0949 0.1845 0.0041  -0.0344 0.0102  194 PRO A O   
1632 C  CB  . PRO A 194 ? 0.1292 0.1212 0.2175 -0.0065 -0.0416 -0.0496 194 PRO A CB  
1633 C  CG  . PRO A 194 ? 0.1222 0.2012 0.2301 -0.0436 -0.0384 -0.0296 194 PRO A CG  
1634 C  CD  . PRO A 194 ? 0.1356 0.1843 0.1732 -0.0414 -0.0548 0.0000  194 PRO A CD  
1635 N  N   . GLY A 195 ? 0.0741 0.0661 0.1685 0.0035  -0.0177 -0.0113 195 GLY A N   
1636 C  CA  . GLY A 195 ? 0.0930 0.0824 0.1748 0.0241  -0.0057 0.0060  195 GLY A CA  
1637 C  C   . GLY A 195 ? 0.0728 0.0724 0.1748 0.0093  -0.0259 0.0086  195 GLY A C   
1638 O  O   . GLY A 195 ? 0.0895 0.0606 0.1791 0.0153  -0.0439 -0.0038 195 GLY A O   
1639 N  N   . SER A 196 ? 0.0662 0.0617 0.1624 0.0038  -0.0230 0.0027  196 SER A N   
1640 C  CA  . SER A 196 ? 0.0794 0.0675 0.1762 0.0081  -0.0296 0.0091  196 SER A CA  
1641 C  C   . SER A 196 ? 0.0511 0.0732 0.1518 0.0020  -0.0247 -0.0114 196 SER A C   
1642 O  O   . SER A 196 ? 0.0597 0.0500 0.2026 0.0031  -0.0348 -0.0108 196 SER A O   
1643 C  CB  . SER A 196 ? 0.0710 0.0450 0.1976 0.0000  -0.0362 -0.0041 196 SER A CB  
1644 O  OG  . SER A 196 ? 0.0657 0.0525 0.2172 -0.0065 -0.0452 -0.0081 196 SER A OG  
1645 N  N   . LEU A 197 ? 0.0538 0.0741 0.1613 0.0006  -0.0251 -0.0054 197 LEU A N   
1646 C  CA  . LEU A 197 ? 0.0688 0.0754 0.1516 -0.0071 -0.0381 0.0043  197 LEU A CA  
1647 C  C   . LEU A 197 ? 0.0702 0.0820 0.1805 -0.0080 -0.0291 -0.0023 197 LEU A C   
1648 O  O   . LEU A 197 ? 0.0722 0.0627 0.2150 -0.0087 -0.0315 -0.0006 197 LEU A O   
1649 C  CB  . LEU A 197 ? 0.1039 0.0671 0.2080 -0.0010 -0.0171 0.0030  197 LEU A CB  
1650 C  CG  . LEU A 197 ? 0.1035 0.0569 0.2274 -0.0092 -0.0441 0.0082  197 LEU A CG  
1651 C  CD1 . LEU A 197 ? 0.1319 0.1032 0.2454 -0.0249 -0.0436 0.0555  197 LEU A CD1 
1652 C  CD2 . LEU A 197 ? 0.0772 0.0666 0.3170 0.0141  -0.0322 0.0174  197 LEU A CD2 
1653 N  N   . THR A 198 ? 0.0697 0.0503 0.1944 -0.0012 -0.0252 -0.0140 198 THR A N   
1654 C  CA  . THR A 198 ? 0.0803 0.0450 0.1911 0.0024  -0.0307 -0.0054 198 THR A CA  
1655 C  C   . THR A 198 ? 0.0490 0.0564 0.2105 -0.0151 -0.0313 -0.0196 198 THR A C   
1656 O  O   . THR A 198 ? 0.0630 0.0812 0.1974 0.0126  -0.0282 -0.0065 198 THR A O   
1657 C  CB  . THR A 198 ? 0.0737 0.0430 0.1863 0.0000  -0.0406 -0.0027 198 THR A CB  
1658 O  OG1 . THR A 198 ? 0.0520 0.0502 0.1825 0.0063  -0.0381 -0.0005 198 THR A OG1 
1659 C  CG2 . THR A 198 ? 0.0812 0.0807 0.2075 -0.0005 -0.0231 0.0152  198 THR A CG2 
1660 N  N   . THR A 199 ? 0.0798 0.0728 0.2082 -0.0165 -0.0274 -0.0097 199 THR A N   
1661 C  CA  . THR A 199 ? 0.0781 0.1036 0.1985 -0.0148 -0.0303 -0.0148 199 THR A CA  
1662 C  C   . THR A 199 ? 0.0794 0.1168 0.2196 -0.0164 -0.0364 -0.0013 199 THR A C   
1663 O  O   . THR A 199 ? 0.0828 0.0922 0.2312 -0.0186 -0.0241 -0.0126 199 THR A O   
1664 C  CB  . THR A 199 ? 0.1230 0.0841 0.2217 0.0046  -0.0373 -0.0040 199 THR A CB  
1665 O  OG1 . THR A 199 ? 0.2134 0.0908 0.2493 0.0515  -0.0834 -0.0230 199 THR A OG1 
1666 C  CG2 . THR A 199 ? 0.1142 0.0731 0.2187 -0.0131 -0.0379 -0.0052 199 THR A CG2 
1667 N  N   . PRO A 200 ? 0.0798 0.0956 0.2299 -0.0247 -0.0294 0.0120  200 PRO A N   
1668 C  CA  . PRO A 200 ? 0.1010 0.1186 0.2531 -0.0505 -0.0298 0.0461  200 PRO A CA  
1669 C  C   . PRO A 200 ? 0.1277 0.0886 0.2495 -0.0375 -0.0320 -0.0142 200 PRO A C   
1670 O  O   . PRO A 200 ? 0.1376 0.1392 0.2319 -0.0098 -0.0342 -0.0034 200 PRO A O   
1671 C  CB  . PRO A 200 ? 0.1125 0.1342 0.3115 -0.0209 0.0000  0.0370  200 PRO A CB  
1672 C  CG  . PRO A 200 ? 0.1062 0.1215 0.2409 -0.0322 -0.0254 -0.0071 200 PRO A CG  
1673 C  CD  . PRO A 200 ? 0.0775 0.1145 0.2594 -0.0081 0.0006  0.0043  200 PRO A CD  
1674 N  N   . PRO A 201 ? 0.1120 0.1089 0.2132 -0.0284 -0.0230 0.0208  201 PRO A N   
1675 C  CA  . PRO A 201 ? 0.1053 0.1030 0.2362 -0.0340 -0.0165 0.0037  201 PRO A CA  
1676 C  C   . PRO A 201 ? 0.0680 0.0832 0.2310 -0.0013 -0.0241 -0.0098 201 PRO A C   
1677 O  O   . PRO A 201 ? 0.0741 0.0949 0.2678 -0.0315 -0.0430 -0.0019 201 PRO A O   
1678 C  CB  . PRO A 201 ? 0.1215 0.0838 0.3109 -0.0461 -0.0263 0.0283  201 PRO A CB  
1679 C  CG  . PRO A 201 ? 0.1520 0.1145 0.3059 -0.0136 -0.0597 0.0093  201 PRO A CG  
1680 C  CD  . PRO A 201 ? 0.1836 0.1249 0.2459 -0.0006 -0.0206 0.0153  201 PRO A CD  
1681 N  N   . LEU A 202 ? 0.0859 0.0745 0.2172 -0.0193 -0.0137 0.0097  202 LEU A N   
1682 C  CA  . LEU A 202 ? 0.0573 0.0976 0.1985 0.0000  -0.0318 -0.0175 202 LEU A CA  
1683 C  C   . LEU A 202 ? 0.0710 0.0653 0.2136 -0.0154 -0.0274 -0.0214 202 LEU A C   
1684 O  O   . LEU A 202 ? 0.0912 0.0749 0.2055 -0.0104 -0.0296 -0.0073 202 LEU A O   
1685 C  CB  . LEU A 202 ? 0.0617 0.0996 0.2384 0.0071  -0.0557 -0.0273 202 LEU A CB  
1686 C  CG  . LEU A 202 ? 0.0737 0.0838 0.2087 -0.0010 -0.0276 -0.0020 202 LEU A CG  
1687 C  CD1 . LEU A 202 ? 0.0595 0.0930 0.2903 -0.0068 -0.0333 -0.0049 202 LEU A CD1 
1688 C  CD2 . LEU A 202 ? 0.0790 0.0671 0.2266 0.0043  -0.0436 -0.0193 202 LEU A CD2 
1689 N  N   . ASN A 203 ? 0.0876 0.0573 0.2653 -0.0104 -0.0386 -0.0113 203 ASN A N   
1690 C  CA  . ASN A 203 ? 0.0904 0.0837 0.2296 -0.0031 -0.0247 -0.0041 203 ASN A CA  
1691 C  C   . ASN A 203 ? 0.0705 0.0807 0.2125 -0.0073 -0.0287 -0.0195 203 ASN A C   
1692 O  O   . ASN A 203 ? 0.0790 0.0615 0.2284 -0.0115 -0.0399 -0.0185 203 ASN A O   
1693 C  CB  . ASN A 203 ? 0.1154 0.0627 0.2982 0.0065  -0.0153 0.0003  203 ASN A CB  
1694 C  CG  . ASN A 203 ? 0.1272 0.0482 0.3935 -0.0287 0.0000  0.0081  203 ASN A CG  
1695 O  OD1 . ASN A 203 ? 0.1694 0.1082 0.4372 -0.0129 0.0296  0.0351  203 ASN A OD1 
1696 N  ND2 . ASN A 203 ? 0.2357 0.0573 0.3623 0.0182  0.0120  0.0000  203 ASN A ND2 
1697 N  N   . GLU A 204 ? 0.1005 0.0746 0.2272 -0.0307 -0.0359 -0.0262 204 GLU A N   
1698 C  CA  . GLU A 204 ? 0.1170 0.1109 0.1832 0.0109  -0.0474 -0.0291 204 GLU A CA  
1699 C  C   . GLU A 204 ? 0.0819 0.0702 0.2154 -0.0197 -0.0491 -0.0401 204 GLU A C   
1700 O  O   . GLU A 204 ? 0.1425 0.1471 0.2705 0.0610  -0.0947 -0.0815 204 GLU A O   
1701 C  CB  . GLU A 204 ? 0.1374 0.0886 0.2163 0.0208  -0.0706 -0.0410 204 GLU A CB  
1702 C  CG  . GLU A 204 ? 0.0978 0.1188 0.2382 0.0186  -0.0575 -0.0324 204 GLU A CG  
1703 C  CD  . GLU A 204 ? 0.1075 0.0982 0.2211 0.0054  -0.0447 -0.0436 204 GLU A CD  
1704 O  OE1 . GLU A 204 ? 0.1482 0.1385 0.2870 0.0092  -0.1032 -0.0586 204 GLU A OE1 
1705 O  OE2 . GLU A 204 ? 0.1111 0.1054 0.2064 -0.0023 -0.0581 -0.0286 204 GLU A OE2 
1706 N  N   . CYS A 205 ? 0.0732 0.0485 0.2125 -0.0068 -0.0538 -0.0026 205 CYS A N   
1707 C  CA  . CYS A 205 ? 0.0921 0.0406 0.2229 0.0013  -0.0518 -0.0131 205 CYS A CA  
1708 C  C   . CYS A 205 ? 0.0886 0.0383 0.2093 0.0046  -0.0351 -0.0085 205 CYS A C   
1709 O  O   . CYS A 205 ? 0.1161 0.0370 0.2653 -0.0051 -0.0683 0.0065  205 CYS A O   
1710 C  CB  . CYS A 205 ? 0.0930 0.0803 0.2353 0.0040  -0.0307 -0.0015 205 CYS A CB  
1711 S  SG  . CYS A 205 ? 0.1237 0.0675 0.2224 0.0000  -0.0522 -0.0085 205 CYS A SG  
1712 N  N   . VAL A 206 ? 0.0940 0.0485 0.1951 -0.0218 -0.0355 0.0038  206 VAL A N   
1713 C  CA  . VAL A 206 ? 0.0960 0.0465 0.1949 -0.0120 -0.0428 -0.0164 206 VAL A CA  
1714 C  C   . VAL A 206 ? 0.0710 0.0622 0.1956 -0.0142 -0.0478 0.0031  206 VAL A C   
1715 O  O   . VAL A 206 ? 0.0985 0.0806 0.2098 0.0054  -0.0540 0.0118  206 VAL A O   
1716 C  CB  . VAL A 206 ? 0.0790 0.0502 0.1985 0.0038  -0.0428 -0.0142 206 VAL A CB  
1717 C  CG1 . VAL A 206 ? 0.0745 0.0653 0.2159 -0.0043 -0.0441 -0.0252 206 VAL A CG1 
1718 C  CG2 . VAL A 206 ? 0.0974 0.0644 0.2032 0.0271  -0.0344 -0.0031 206 VAL A CG2 
1719 N  N   . THR A 207 ? 0.0696 0.0344 0.2064 -0.0074 -0.0184 -0.0120 207 THR A N   
1720 C  CA  . THR A 207 ? 0.0785 0.0710 0.1974 -0.0087 -0.0357 -0.0074 207 THR A CA  
1721 C  C   . THR A 207 ? 0.0856 0.0406 0.1680 -0.0038 -0.0230 -0.0015 207 THR A C   
1722 O  O   . THR A 207 ? 0.0983 0.0406 0.1820 0.0098  -0.0405 -0.0024 207 THR A O   
1723 C  CB  . THR A 207 ? 0.1040 0.0595 0.2337 -0.0049 -0.0103 -0.0026 207 THR A CB  
1724 O  OG1 . THR A 207 ? 0.1412 0.0564 0.2457 0.0000  -0.0194 -0.0285 207 THR A OG1 
1725 C  CG2 . THR A 207 ? 0.1071 0.0608 0.2518 -0.0035 -0.0043 -0.0153 207 THR A CG2 
1726 N  N   . TRP A 208 ? 0.0847 0.0456 0.1746 -0.0019 -0.0296 -0.0017 208 TRP A N   
1727 C  CA  . TRP A 208 ? 0.0790 0.0441 0.1755 0.0060  -0.0324 -0.0109 208 TRP A CA  
1728 C  C   . TRP A 208 ? 0.0798 0.0456 0.1466 0.0182  -0.0274 -0.0020 208 TRP A C   
1729 O  O   . TRP A 208 ? 0.0967 0.0723 0.1642 -0.0063 -0.0309 0.0046  208 TRP A O   
1730 C  CB  . TRP A 208 ? 0.0856 0.0441 0.1944 0.0162  -0.0254 -0.0093 208 TRP A CB  
1731 C  CG  . TRP A 208 ? 0.0759 0.0340 0.1850 0.0081  -0.0324 0.0010  208 TRP A CG  
1732 C  CD1 . TRP A 208 ? 0.0790 0.0520 0.1879 0.0098  -0.0344 0.0038  208 TRP A CD1 
1733 C  CD2 . TRP A 208 ? 0.0956 0.0275 0.1744 0.0115  -0.0386 0.0005  208 TRP A CD2 
1734 N  NE1 . TRP A 208 ? 0.0926 0.0454 0.1766 0.0107  -0.0331 -0.0164 208 TRP A NE1 
1735 C  CE2 . TRP A 208 ? 0.0949 0.0353 0.1710 0.0098  -0.0296 -0.0060 208 TRP A CE2 
1736 C  CE3 . TRP A 208 ? 0.0940 0.0300 0.1782 0.0046  -0.0395 -0.0104 208 TRP A CE3 
1737 C  CZ2 . TRP A 208 ? 0.0908 0.0573 0.1838 0.0252  -0.0329 -0.0120 208 TRP A CZ2 
1738 C  CZ3 . TRP A 208 ? 0.1116 0.0339 0.1834 0.0108  -0.0340 0.0027  208 TRP A CZ3 
1739 C  CH2 . TRP A 208 ? 0.1190 0.0571 0.1802 0.0228  -0.0392 -0.0131 208 TRP A CH2 
1740 N  N   . ILE A 209 ? 0.0658 0.0596 0.1726 0.0148  -0.0351 -0.0074 209 ILE A N   
1741 C  CA  . ILE A 209 ? 0.0715 0.0463 0.1899 0.0098  -0.0175 -0.0006 209 ILE A CA  
1742 C  C   . ILE A 209 ? 0.0559 0.0634 0.1532 0.0175  -0.0247 -0.0003 209 ILE A C   
1743 O  O   . ILE A 209 ? 0.1071 0.0454 0.1597 0.0051  -0.0239 0.0020  209 ILE A O   
1744 C  CB  . ILE A 209 ? 0.0615 0.0509 0.2193 0.0125  -0.0163 -0.0006 209 ILE A CB  
1745 C  CG1 . ILE A 209 ? 0.0976 0.0485 0.2942 0.0390  -0.0104 -0.0275 209 ILE A CG1 
1746 C  CG2 . ILE A 209 ? 0.0474 0.0957 0.2312 0.0209  -0.0108 0.0148  209 ILE A CG2 
1747 C  CD1 . ILE A 209 ? 0.1304 0.0688 0.3054 0.0436  -0.0564 -0.0208 209 ILE A CD1 
1748 N  N   . VAL A 210 ? 0.0860 0.0456 0.1811 0.0048  -0.0344 0.0015  210 VAL A N   
1749 C  CA  . VAL A 210 ? 0.0658 0.0335 0.2093 -0.0065 -0.0242 0.0040  210 VAL A CA  
1750 C  C   . VAL A 210 ? 0.0709 0.0362 0.1538 0.0024  -0.0176 -0.0126 210 VAL A C   
1751 O  O   . VAL A 210 ? 0.0824 0.0710 0.1771 -0.0063 -0.0243 -0.0006 210 VAL A O   
1752 C  CB  . VAL A 210 ? 0.0579 0.0731 0.2023 0.0081  -0.0229 -0.0076 210 VAL A CB  
1753 C  CG1 . VAL A 210 ? 0.1118 0.0379 0.2436 0.0160  -0.0076 -0.0074 210 VAL A CG1 
1754 C  CG2 . VAL A 210 ? 0.0688 0.0562 0.2459 -0.0003 -0.0342 -0.0063 210 VAL A CG2 
1755 N  N   . LEU A 211 ? 0.0732 0.0715 0.1766 -0.0054 -0.0272 -0.0148 211 LEU A N   
1756 C  CA  . LEU A 211 ? 0.0710 0.0570 0.1836 -0.0115 -0.0329 -0.0073 211 LEU A CA  
1757 C  C   . LEU A 211 ? 0.0912 0.0640 0.2117 -0.0183 -0.0263 -0.0108 211 LEU A C   
1758 O  O   . LEU A 211 ? 0.0965 0.0666 0.2163 -0.0137 -0.0384 -0.0019 211 LEU A O   
1759 C  CB  . LEU A 211 ? 0.1136 0.0634 0.1897 0.0043  -0.0280 0.0038  211 LEU A CB  
1760 C  CG  . LEU A 211 ? 0.0819 0.0714 0.1906 -0.0026 -0.0443 0.0024  211 LEU A CG  
1761 C  CD1 . LEU A 211 ? 0.1012 0.1263 0.2050 -0.0019 -0.0463 0.0031  211 LEU A CD1 
1762 C  CD2 . LEU A 211 ? 0.0969 0.0930 0.2193 0.0227  -0.0220 -0.0073 211 LEU A CD2 
1763 N  N   . LYS A 212 ? 0.0847 0.0886 0.2161 -0.0434 -0.0351 0.0214  212 LYS A N   
1764 C  CA  . LYS A 212 ? 0.1717 0.1010 0.2328 -0.0635 -0.0564 0.0242  212 LYS A CA  
1765 C  C   . LYS A 212 ? 0.1142 0.0582 0.2472 -0.0307 -0.0540 0.0326  212 LYS A C   
1766 O  O   . LYS A 212 ? 0.1283 0.0768 0.2879 -0.0151 -0.0784 0.0303  212 LYS A O   
1767 C  CB  . LYS A 212 ? 0.2578 0.1256 0.2459 -0.0688 -0.0428 0.0428  212 LYS A CB  
1768 C  CG  . LYS A 212 ? 0.5665 0.2391 0.3465 -0.2424 -0.0243 0.0702  212 LYS A CG  
1769 C  CD  . LYS A 212 ? 0.6351 0.5188 0.3808 -0.3267 0.0335  -0.0631 212 LYS A CD  
1770 C  CE  . LYS A 212 ? 0.5651 0.5623 0.5507 0.1119  0.0368  0.0471  212 LYS A CE  
1771 N  NZ  . LYS A 212 ? 0.4751 0.2466 0.9236 -0.0063 -0.3560 -0.0573 212 LYS A NZ  
1772 N  N   . GLU A 213 ? 0.0766 0.0992 0.2057 -0.0226 -0.0452 0.0186  213 GLU A N   
1773 C  CA  . GLU A 213 ? 0.1003 0.0828 0.2296 -0.0322 -0.0537 0.0432  213 GLU A CA  
1774 C  C   . GLU A 213 ? 0.0886 0.0582 0.2168 -0.0153 -0.0573 0.0214  213 GLU A C   
1775 O  O   . GLU A 213 ? 0.0768 0.0693 0.2249 -0.0074 -0.0295 0.0287  213 GLU A O   
1776 C  CB  . GLU A 213 ? 0.0926 0.1107 0.2362 -0.0263 -0.0524 0.0263  213 GLU A CB  
1777 C  CG  . GLU A 213 ? 0.1115 0.1333 0.2984 -0.0250 -0.0562 -0.0181 213 GLU A CG  
1778 C  CD  . GLU A 213 ? 0.1186 0.1949 0.3680 -0.0772 -0.0529 0.0153  213 GLU A CD  
1779 O  OE1 . GLU A 213 ? 0.1098 0.1820 0.4002 -0.0091 -0.0612 0.0081  213 GLU A OE1 
1780 O  OE2 . GLU A 213 ? 0.1565 0.6388 0.3700 -0.0939 -0.0555 -0.0992 213 GLU A OE2 
1781 N  N   A PRO A 214 ? 0.0908 0.0517 0.2314 0.0063  -0.0559 0.0315  214 PRO A N   
1782 N  N   B PRO A 214 ? 0.1075 0.0582 0.2454 -0.0214 -0.0399 -0.0038 214 PRO A N   
1783 C  CA  A PRO A 214 ? 0.0930 0.0454 0.2003 -0.0114 -0.0723 0.0248  214 PRO A CA  
1784 C  CA  B PRO A 214 ? 0.1398 0.0658 0.2152 0.0386  -0.0548 -0.0107 214 PRO A CA  
1785 C  C   A PRO A 214 ? 0.0623 0.0551 0.1994 0.0013  -0.0584 0.0013  214 PRO A C   
1786 C  C   B PRO A 214 ? 0.1195 0.0370 0.2199 -0.0006 -0.0452 0.0031  214 PRO A C   
1787 O  O   A PRO A 214 ? 0.0732 0.0781 0.2542 -0.0307 -0.0709 -0.0031 214 PRO A O   
1788 O  O   B PRO A 214 ? 0.1317 0.1750 0.2569 -0.0252 -0.0555 0.0571  214 PRO A O   
1789 C  CB  A PRO A 214 ? 0.1247 0.0715 0.2412 0.0221  -0.0665 0.0175  214 PRO A CB  
1790 C  CB  B PRO A 214 ? 0.0737 0.0368 0.2666 -0.0041 -0.0702 -0.0054 214 PRO A CB  
1791 C  CG  A PRO A 214 ? 0.1532 0.0802 0.2786 -0.0423 -0.0807 0.0115  214 PRO A CG  
1792 C  CG  B PRO A 214 ? 0.1544 0.0429 0.2759 0.0423  -0.0381 -0.0175 214 PRO A CG  
1793 C  CD  A PRO A 214 ? 0.1188 0.0456 0.2815 -0.0269 -0.0631 0.0430  214 PRO A CD  
1794 C  CD  B PRO A 214 ? 0.1181 0.0410 0.2915 -0.0109 -0.0460 -0.0013 214 PRO A CD  
1795 N  N   . ILE A 215 ? 0.1118 0.0693 0.1951 0.0076  -0.0500 0.0006  215 ILE A N   
1796 C  CA  . ILE A 215 ? 0.0949 0.0665 0.2249 0.0074  -0.0566 -0.0115 215 ILE A CA  
1797 C  C   . ILE A 215 ? 0.0926 0.0838 0.2145 0.0065  -0.0529 -0.0187 215 ILE A C   
1798 O  O   . ILE A 215 ? 0.1019 0.0538 0.2651 0.0052  -0.0518 -0.0221 215 ILE A O   
1799 C  CB  . ILE A 215 ? 0.1001 0.0588 0.2621 0.0186  -0.0562 0.0093  215 ILE A CB  
1800 C  CG1 . ILE A 215 ? 0.1003 0.0847 0.2186 0.0093  -0.0458 -0.0109 215 ILE A CG1 
1801 C  CG2 . ILE A 215 ? 0.1168 0.0803 0.2666 0.0344  -0.0344 -0.0043 215 ILE A CG2 
1802 C  CD1 . ILE A 215 ? 0.1222 0.0776 0.2443 0.0137  -0.0120 0.0172  215 ILE A CD1 
1803 N  N   . SER A 216 ? 0.0606 0.0270 0.1789 0.0065  -0.0504 -0.0031 216 SER A N   
1804 C  CA  A SER A 216 ? 0.1328 0.0648 0.2278 0.0103  -0.0623 -0.0483 216 SER A CA  
1805 C  CA  B SER A 216 ? 0.1349 0.0658 0.2303 0.0107  -0.0604 -0.0467 216 SER A CA  
1806 C  C   . SER A 216 ? 0.0608 0.0302 0.1626 0.0131  -0.0696 -0.0260 216 SER A C   
1807 O  O   . SER A 216 ? 0.0599 0.0253 0.1653 0.0005  -0.0693 -0.0011 216 SER A O   
1808 C  CB  A SER A 216 ? 0.2010 0.0768 0.2294 -0.0269 -0.0434 -0.0295 216 SER A CB  
1809 C  CB  B SER A 216 ? 0.1967 0.0922 0.2624 -0.0315 -0.0153 -0.0221 216 SER A CB  
1810 O  OG  A SER A 216 ? 0.1852 0.1265 0.2154 -0.0087 -0.0772 -0.0142 216 SER A OG  
1811 O  OG  B SER A 216 ? 0.1780 0.1435 0.2903 0.0236  -0.0842 -0.0661 216 SER A OG  
1812 N  N   . VAL A 217 ? 0.1277 0.0481 0.2098 -0.0081 -0.0535 -0.0130 217 VAL A N   
1813 C  CA  . VAL A 217 ? 0.1115 0.0304 0.2206 0.0030  -0.0750 -0.0062 217 VAL A CA  
1814 C  C   . VAL A 217 ? 0.1089 0.0467 0.2087 -0.0057 -0.0493 -0.0074 217 VAL A C   
1815 O  O   . VAL A 217 ? 0.1371 0.0485 0.2389 -0.0013 -0.0736 -0.0082 217 VAL A O   
1816 C  CB  . VAL A 217 ? 0.1003 0.0441 0.2949 0.0115  -0.0542 -0.0181 217 VAL A CB  
1817 C  CG1 . VAL A 217 ? 0.1216 0.0525 0.2985 -0.0102 -0.0724 -0.0340 217 VAL A CG1 
1818 C  CG2 . VAL A 217 ? 0.1093 0.0518 0.3488 0.0076  -0.0714 -0.0241 217 VAL A CG2 
1819 N  N   . SER A 218 ? 0.1143 0.0493 0.2145 -0.0080 -0.0623 -0.0082 218 SER A N   
1820 C  CA  . SER A 218 ? 0.1111 0.0361 0.2430 0.0126  -0.0617 -0.0115 218 SER A CA  
1821 C  C   . SER A 218 ? 0.1215 0.0465 0.2364 0.0183  -0.0573 0.0031  218 SER A C   
1822 O  O   . SER A 218 ? 0.1161 0.0579 0.2481 -0.0005 -0.0581 0.0006  218 SER A O   
1823 C  CB  . SER A 218 ? 0.1529 0.0454 0.2305 -0.0163 -0.0612 -0.0031 218 SER A CB  
1824 O  OG  . SER A 218 ? 0.1010 0.1019 0.2671 -0.0035 -0.0653 -0.0171 218 SER A OG  
1825 N  N   A SER A 219 ? 0.1233 0.0511 0.2621 0.0230  -0.0709 -0.0006 219 SER A N   
1826 N  N   B SER A 219 ? 0.1477 0.0464 0.2770 0.0137  -0.0666 -0.0164 219 SER A N   
1827 C  CA  A SER A 219 ? 0.1197 0.0562 0.2978 0.0297  -0.0683 0.0270  219 SER A CA  
1828 C  CA  B SER A 219 ? 0.1482 0.0529 0.3043 0.0093  -0.0570 0.0006  219 SER A CA  
1829 C  C   A SER A 219 ? 0.1096 0.0579 0.2712 0.0375  -0.0562 -0.0131 219 SER A C   
1830 C  C   B SER A 219 ? 0.1304 0.0553 0.2777 0.0403  -0.0658 -0.0175 219 SER A C   
1831 O  O   A SER A 219 ? 0.0922 0.0741 0.3445 0.0362  -0.0564 -0.0076 219 SER A O   
1832 O  O   B SER A 219 ? 0.1403 0.0948 0.3443 0.0027  -0.0588 0.0005  219 SER A O   
1833 C  CB  A SER A 219 ? 0.1179 0.0675 0.3086 0.0571  -0.0331 0.0229  219 SER A CB  
1834 C  CB  B SER A 219 ? 0.1723 0.0388 0.3842 -0.0432 -0.0544 0.0000  219 SER A CB  
1835 O  OG  A SER A 219 ? 0.1340 0.0346 0.2624 0.0316  -0.0152 -0.0082 219 SER A OG  
1836 O  OG  B SER A 219 ? 0.2373 0.1105 0.6042 0.0098  0.0017  0.0863  219 SER A OG  
1837 N  N   . GLU A 220 ? 0.1507 0.0815 0.2506 0.0296  -0.0706 -0.0247 220 GLU A N   
1838 C  CA  . GLU A 220 ? 0.2003 0.0781 0.2477 0.0487  -0.0710 -0.0472 220 GLU A CA  
1839 C  C   . GLU A 220 ? 0.1208 0.0820 0.2294 0.0249  -0.0261 -0.0087 220 GLU A C   
1840 O  O   . GLU A 220 ? 0.1504 0.0949 0.2574 0.0193  -0.0054 -0.0120 220 GLU A O   
1841 C  CB  . GLU A 220 ? 0.1836 0.1044 0.2806 0.0309  -0.0746 -0.0812 220 GLU A CB  
1842 C  CG  . GLU A 220 ? 0.2666 0.1039 0.3837 -0.0136 -0.0115 -0.0907 220 GLU A CG  
1843 C  CD  . GLU A 220 ? 0.3689 0.1380 0.3591 -0.0728 -0.0575 -0.0452 220 GLU A CD  
1844 O  OE1 . GLU A 220 ? 0.1924 0.1800 0.4000 -0.0944 -0.0405 -0.0829 220 GLU A OE1 
1845 O  OE2 . GLU A 220 ? 0.8427 0.1699 0.8848 -0.2107 -0.1324 -0.1010 220 GLU A OE2 
1846 N  N   . GLN A 221 ? 0.1124 0.0494 0.2400 0.0251  -0.0377 -0.0231 221 GLN A N   
1847 C  CA  . GLN A 221 ? 0.0728 0.0636 0.2488 -0.0010 -0.0414 -0.0381 221 GLN A CA  
1848 C  C   . GLN A 221 ? 0.0895 0.0670 0.2490 0.0031  -0.0553 -0.0153 221 GLN A C   
1849 O  O   . GLN A 221 ? 0.1111 0.0658 0.2750 -0.0065 -0.0394 -0.0098 221 GLN A O   
1850 C  CB  . GLN A 221 ? 0.0992 0.0675 0.2269 0.0049  -0.0511 -0.0253 221 GLN A CB  
1851 C  CG  . GLN A 221 ? 0.0828 0.0657 0.2434 0.0076  -0.0421 -0.0164 221 GLN A CG  
1852 C  CD  . GLN A 221 ? 0.0825 0.0564 0.2178 0.0010  -0.0443 -0.0285 221 GLN A CD  
1853 O  OE1 . GLN A 221 ? 0.1036 0.0671 0.2132 0.0087  -0.0412 -0.0060 221 GLN A OE1 
1854 N  NE2 . GLN A 221 ? 0.1194 0.0661 0.2226 0.0195  -0.0531 -0.0120 221 GLN A NE2 
1855 N  N   . VAL A 222 ? 0.0974 0.0833 0.2450 0.0104  -0.0693 -0.0155 222 VAL A N   
1856 C  CA  . VAL A 222 ? 0.0864 0.1856 0.2610 0.0126  -0.0666 -0.0142 222 VAL A CA  
1857 C  C   . VAL A 222 ? 0.1039 0.1351 0.2592 0.0060  -0.0582 0.0074  222 VAL A C   
1858 O  O   . VAL A 222 ? 0.1062 0.1342 0.2851 0.0015  -0.0533 0.0068  222 VAL A O   
1859 C  CB  . VAL A 222 ? 0.0922 0.2488 0.3143 0.0137  -0.1045 -0.0049 222 VAL A CB  
1860 C  CG1 . VAL A 222 ? 0.2500 0.3425 0.3531 0.0715  -0.0052 -0.0012 222 VAL A CG1 
1861 C  CG2 . VAL A 222 ? 0.2249 0.2267 0.4765 -0.0548 -0.0480 0.0344  222 VAL A CG2 
1862 N  N   . LEU A 223 ? 0.1109 0.1534 0.2635 0.0469  -0.0414 -0.0137 223 LEU A N   
1863 C  CA  . LEU A 223 ? 0.1298 0.1356 0.3109 0.0074  -0.0230 -0.0057 223 LEU A CA  
1864 C  C   . LEU A 223 ? 0.1281 0.1197 0.2824 0.0443  -0.0324 -0.0087 223 LEU A C   
1865 O  O   . LEU A 223 ? 0.0983 0.1665 0.2921 0.0082  -0.0399 -0.0274 223 LEU A O   
1866 C  CB  . LEU A 223 ? 0.2117 0.1064 0.4408 0.0074  -0.0938 -0.0366 223 LEU A CB  
1867 C  CG  . LEU A 223 ? 0.2089 0.1254 0.5799 -0.0219 -0.0680 -0.0263 223 LEU A CG  
1868 C  CD1 . LEU A 223 ? 0.4675 0.1599 0.5522 -0.0599 -0.0049 -0.1261 223 LEU A CD1 
1869 C  CD2 . LEU A 223 ? 0.2653 0.2319 0.6941 0.0776  0.0741  -0.0982 223 LEU A CD2 
1870 N  N   . LYS A 224 ? 0.1224 0.1252 0.2378 0.0471  -0.0544 -0.0230 224 LYS A N   
1871 C  CA  . LYS A 224 ? 0.1143 0.1651 0.2599 0.0384  -0.0697 -0.0160 224 LYS A CA  
1872 C  C   . LYS A 224 ? 0.1317 0.1010 0.2269 0.0522  -0.0480 0.0104  224 LYS A C   
1873 O  O   . LYS A 224 ? 0.1500 0.1412 0.2229 0.0298  -0.0328 -0.0098 224 LYS A O   
1874 C  CB  . LYS A 224 ? 0.1324 0.2046 0.3073 0.0425  -0.0881 0.0403  224 LYS A CB  
1875 C  CG  . LYS A 224 ? 0.1493 0.3285 0.4013 -0.0417 -0.1220 0.0250  224 LYS A CG  
1876 C  CD  . LYS A 224 ? 0.2903 0.6718 0.5102 0.1462  -0.2222 -0.0208 224 LYS A CD  
1877 C  CE  . LYS A 224 ? 0.3249 0.3555 0.5899 -0.0522 -0.2028 -0.0626 224 LYS A CE  
1878 N  NZ  . LYS A 224 ? 0.8356 0.3519 0.5479 -0.0876 -0.1207 -0.2205 224 LYS A NZ  
1879 N  N   . PHE A 225 ? 0.1398 0.1055 0.2339 0.0582  -0.0702 -0.0263 225 PHE A N   
1880 C  CA  . PHE A 225 ? 0.1298 0.0994 0.2267 0.0372  -0.0368 -0.0228 225 PHE A CA  
1881 C  C   . PHE A 225 ? 0.1428 0.1062 0.2353 0.0526  -0.0421 -0.0339 225 PHE A C   
1882 O  O   . PHE A 225 ? 0.1272 0.1349 0.2460 0.0505  -0.0406 -0.0401 225 PHE A O   
1883 C  CB  . PHE A 225 ? 0.1048 0.0994 0.2509 0.0305  -0.0307 -0.0098 225 PHE A CB  
1884 C  CG  . PHE A 225 ? 0.1109 0.0838 0.2614 0.0137  -0.0276 -0.0309 225 PHE A CG  
1885 C  CD1 . PHE A 225 ? 0.1450 0.1518 0.2867 0.0697  -0.0259 -0.0252 225 PHE A CD1 
1886 C  CD2 . PHE A 225 ? 0.0976 0.1728 0.2912 0.0353  -0.0658 -0.0776 225 PHE A CD2 
1887 C  CE1 . PHE A 225 ? 0.1872 0.1142 0.2639 0.0557  0.0126  -0.0114 225 PHE A CE1 
1888 C  CE2 . PHE A 225 ? 0.0957 0.2421 0.3145 0.0454  -0.0581 -0.0960 225 PHE A CE2 
1889 C  CZ  . PHE A 225 ? 0.1001 0.1158 0.3106 0.0236  -0.0610 -0.0595 225 PHE A CZ  
1890 N  N   . ARG A 226 ? 0.1395 0.1091 0.2475 0.0626  -0.0469 -0.0485 226 ARG A N   
1891 C  CA  . ARG A 226 ? 0.1550 0.1270 0.2378 0.0790  -0.0489 -0.0362 226 ARG A CA  
1892 C  C   . ARG A 226 ? 0.1261 0.1649 0.2208 0.0706  -0.0533 -0.0430 226 ARG A C   
1893 O  O   . ARG A 226 ? 0.1194 0.1895 0.2980 0.0662  -0.0390 -0.0498 226 ARG A O   
1894 C  CB  . ARG A 226 ? 0.1829 0.1014 0.2524 0.0489  -0.0934 -0.0474 226 ARG A CB  
1895 C  CG  . ARG A 226 ? 0.1347 0.0810 0.2694 0.0381  -0.0666 -0.0388 226 ARG A CG  
1896 C  CD  . ARG A 226 ? 0.2328 0.0904 0.2768 0.0419  -0.0732 -0.0264 226 ARG A CD  
1897 N  NE  . ARG A 226 ? 0.1689 0.0710 0.2781 0.0392  -0.0847 -0.0147 226 ARG A NE  
1898 C  CZ  . ARG A 226 ? 0.1480 0.1154 0.3077 -0.0068 -0.0639 -0.0719 226 ARG A CZ  
1899 N  NH1 . ARG A 226 ? 0.2127 0.2087 0.4663 -0.0350 -0.0930 -0.1659 226 ARG A NH1 
1900 N  NH2 . ARG A 226 ? 0.2326 0.1333 0.3165 -0.0381 -0.0273 -0.0790 226 ARG A NH2 
1901 N  N   . LYS A 227 ? 0.1383 0.1705 0.2129 0.0540  -0.0584 -0.0518 227 LYS A N   
1902 C  CA  . LYS A 227 ? 0.1735 0.1800 0.2240 0.0458  -0.0612 -0.0762 227 LYS A CA  
1903 C  C   . LYS A 227 ? 0.1832 0.1678 0.2260 0.0935  -0.0428 -0.0542 227 LYS A C   
1904 O  O   . LYS A 227 ? 0.1951 0.2705 0.2294 0.0688  -0.0231 -0.0553 227 LYS A O   
1905 C  CB  . LYS A 227 ? 0.2196 0.1834 0.2615 0.0564  -0.1040 -0.0798 227 LYS A CB  
1906 C  CG  . LYS A 227 ? 0.2314 0.2333 0.3115 0.0054  -0.0987 -0.1133 227 LYS A CG  
1907 C  CD  . LYS A 227 ? 0.1967 0.2836 0.4226 -0.0120 -0.1412 -0.0219 227 LYS A CD  
1908 C  CE  . LYS A 227 ? 0.4936 0.4557 0.7929 -0.2266 0.0274  -0.1404 227 LYS A CE  
1909 N  NZ  . LYS A 227 ? 0.7207 0.7218 0.7274 -0.3064 0.0593  0.0723  227 LYS A NZ  
1910 N  N   . LEU A 228 ? 0.1511 0.1536 0.2337 0.0599  -0.0592 -0.0674 228 LEU A N   
1911 C  CA  . LEU A 228 ? 0.1037 0.2055 0.2206 0.0483  -0.0274 -0.0785 228 LEU A CA  
1912 C  C   . LEU A 228 ? 0.1204 0.1993 0.2935 0.0820  -0.0285 -0.0377 228 LEU A C   
1913 O  O   . LEU A 228 ? 0.1448 0.2096 0.2457 0.0922  -0.0487 -0.0515 228 LEU A O   
1914 C  CB  . LEU A 228 ? 0.1238 0.1491 0.2195 0.0706  -0.0432 -0.0423 228 LEU A CB  
1915 C  CG  . LEU A 228 ? 0.1054 0.1347 0.2238 0.0375  -0.0460 -0.0186 228 LEU A CG  
1916 C  CD1 . LEU A 228 ? 0.0983 0.1746 0.2601 0.0551  -0.0406 -0.0661 228 LEU A CD1 
1917 C  CD2 . LEU A 228 ? 0.1237 0.1685 0.2527 0.0474  -0.0333 0.0065  228 LEU A CD2 
1918 N  N   . ASN A 229 ? 0.1089 0.1680 0.2646 0.0555  -0.0390 -0.0476 229 ASN A N   
1919 C  CA  . ASN A 229 ? 0.0930 0.2193 0.2470 0.0171  -0.0241 -0.0608 229 ASN A CA  
1920 C  C   . ASN A 229 ? 0.1028 0.1999 0.2703 0.0306  -0.0320 -0.0272 229 ASN A C   
1921 O  O   . ASN A 229 ? 0.1106 0.2136 0.2337 0.0423  -0.0247 -0.0392 229 ASN A O   
1922 C  CB  . ASN A 229 ? 0.1261 0.2233 0.2612 0.0333  -0.0197 -0.0516 229 ASN A CB  
1923 C  CG  . ASN A 229 ? 0.1852 0.2901 0.2470 0.1177  -0.0522 -0.0837 229 ASN A CG  
1924 O  OD1 . ASN A 229 ? 0.4390 0.3878 0.3350 0.1844  0.0540  -0.0744 229 ASN A OD1 
1925 N  ND2 . ASN A 229 ? 0.2335 0.3054 0.3382 0.1127  -0.0430 -0.1062 229 ASN A ND2 
1926 N  N   . PHE A 230 ? 0.1075 0.2601 0.2466 0.0588  -0.0373 -0.0732 230 PHE A N   
1927 C  CA  . PHE A 230 ? 0.1001 0.2461 0.2258 0.0593  -0.0062 -0.0538 230 PHE A CA  
1928 C  C   . PHE A 230 ? 0.1111 0.3226 0.2741 0.0964  -0.0368 -0.0432 230 PHE A C   
1929 O  O   . PHE A 230 ? 0.1272 0.2646 0.2782 0.0474  0.0013  -0.0164 230 PHE A O   
1930 C  CB  . PHE A 230 ? 0.1120 0.3310 0.2396 0.0631  -0.0489 -0.0458 230 PHE A CB  
1931 C  CG  . PHE A 230 ? 0.1254 0.2479 0.2141 0.0491  -0.0454 -0.0597 230 PHE A CG  
1932 C  CD1 . PHE A 230 ? 0.1028 0.2739 0.2226 0.0603  -0.0489 -0.0564 230 PHE A CD1 
1933 C  CD2 . PHE A 230 ? 0.0922 0.2242 0.3282 0.0086  -0.0494 -0.0175 230 PHE A CD2 
1934 C  CE1 . PHE A 230 ? 0.1635 0.1511 0.2387 0.0186  -0.0197 -0.0724 230 PHE A CE1 
1935 C  CE2 . PHE A 230 ? 0.1337 0.1608 0.2949 0.0560  -0.0656 -0.0562 230 PHE A CE2 
1936 C  CZ  . PHE A 230 ? 0.1642 0.1425 0.3077 0.0671  -0.0736 -0.0710 230 PHE A CZ  
1937 N  N   . ASN A 231 ? 0.0967 0.3084 0.2360 0.0737  -0.0250 -0.0303 231 ASN A N   
1938 C  CA  . ASN A 231 ? 0.1495 0.2213 0.2669 0.0386  -0.0461 -0.0533 231 ASN A CA  
1939 C  C   . ASN A 231 ? 0.1559 0.1448 0.2854 0.0728  0.0513  0.0285  231 ASN A C   
1940 O  O   . ASN A 231 ? 0.1242 0.3355 0.3298 0.0688  0.0241  -0.0434 231 ASN A O   
1941 C  CB  . ASN A 231 ? 0.1249 0.3174 0.2727 0.0469  -0.0104 -0.0860 231 ASN A CB  
1942 C  CG  . ASN A 231 ? 0.1186 0.3032 0.2682 0.0636  -0.0425 -0.0566 231 ASN A CG  
1943 O  OD1 . ASN A 231 ? 0.1315 0.2734 0.3115 0.0679  -0.0027 -0.0688 231 ASN A OD1 
1944 N  ND2 . ASN A 231 ? 0.1523 0.4174 0.2788 0.0392  -0.0575 -0.0421 231 ASN A ND2 
1945 N  N   . GLY A 232 ? 0.1949 0.2518 0.2675 -0.0118 0.0098  -0.0186 232 GLY A N   
1946 C  CA  . GLY A 232 ? 0.1581 0.2193 0.2989 0.0260  0.0465  -0.0175 232 GLY A CA  
1947 C  C   . GLY A 232 ? 0.2175 0.2278 0.2903 0.0610  0.0186  -0.0199 232 GLY A C   
1948 O  O   . GLY A 232 ? 0.2648 0.3109 0.2840 0.0610  0.0262  -0.0767 232 GLY A O   
1949 N  N   . GLU A 233 ? 0.2691 0.5414 0.2637 -0.0038 0.0342  0.0458  233 GLU A N   
1950 C  CA  . GLU A 233 ? 0.3075 0.6283 0.2969 -0.1084 0.0274  0.0087  233 GLU A CA  
1951 C  C   . GLU A 233 ? 0.2754 0.6093 0.5425 -0.0842 0.0619  -0.0186 233 GLU A C   
1952 O  O   . GLU A 233 ? 0.4390 0.7261 0.4582 -0.1712 0.1801  -0.2016 233 GLU A O   
1953 C  CB  . GLU A 233 ? 0.1904 0.7544 0.3109 -0.0428 0.0080  -0.0344 233 GLU A CB  
1954 C  CG  . GLU A 233 ? 0.5217 1.0145 0.3869 0.0978  0.0838  -0.0925 233 GLU A CG  
1955 C  CD  . GLU A 233 ? 0.0671 1.2280 1.4579 -0.1462 -0.1808 0.3212  233 GLU A CD  
1956 O  OE1 . GLU A 233 ? 0.2741 0.5698 0.9239 -0.1124 0.0070  -0.1386 233 GLU A OE1 
1957 O  OE2 . GLU A 233 ? 0.9423 0.2782 2.2286 -0.1555 0.3416  -0.3736 233 GLU A OE2 
1958 N  N   . GLY A 234 ? 0.3156 0.7950 0.4372 0.1404  -0.0873 0.0355  234 GLY A N   
1959 C  CA  . GLY A 234 ? 0.3544 0.8579 0.6388 0.1071  -0.0019 0.0162  234 GLY A CA  
1960 C  C   . GLY A 234 ? 0.4192 1.2206 0.4541 -0.0390 0.1199  0.2345  234 GLY A C   
1961 O  O   . GLY A 234 ? 0.5389 0.4474 0.6207 -0.2134 0.3143  -0.1259 234 GLY A O   
1962 N  N   . GLU A 235 ? 0.2840 0.4510 0.2662 0.1703  0.0322  0.0023  235 GLU A N   
1963 C  CA  . GLU A 235 ? 0.3118 0.2251 0.2648 0.0362  0.0252  0.0307  235 GLU A CA  
1964 C  C   . GLU A 235 ? 0.2346 0.2366 0.3064 0.0750  0.0381  -0.0308 235 GLU A C   
1965 O  O   . GLU A 235 ? 0.2168 0.4873 0.3348 0.0803  -0.0315 -0.1193 235 GLU A O   
1966 C  CB  . GLU A 235 ? 0.2919 0.2372 0.3485 0.0445  0.0768  0.0060  235 GLU A CB  
1967 C  CG  . GLU A 235 ? 0.5019 0.1847 0.4961 0.0054  0.2342  -0.0263 235 GLU A CG  
1968 C  CD  . GLU A 235 ? 0.5605 0.2418 0.4110 -0.0432 0.1140  -0.0771 235 GLU A CD  
1969 O  OE1 . GLU A 235 ? 0.2700 0.3558 0.4936 -0.0298 -0.0208 0.1457  235 GLU A OE1 
1970 O  OE2 . GLU A 235 ? 0.5841 0.2416 0.9401 0.0533  -0.1825 -0.0273 235 GLU A OE2 
1971 N  N   . PRO A 236 ? 0.1659 0.2522 0.3481 0.0172  0.0065  -0.0065 236 PRO A N   
1972 C  CA  . PRO A 236 ? 0.1466 0.2682 0.3734 0.0054  -0.0026 -0.0230 236 PRO A CA  
1973 C  C   . PRO A 236 ? 0.1111 0.3068 0.3287 0.0035  -0.0010 -0.1177 236 PRO A C   
1974 O  O   . PRO A 236 ? 0.1629 0.3623 0.3675 0.0780  -0.0487 -0.1492 236 PRO A O   
1975 C  CB  . PRO A 236 ? 0.0441 0.2536 0.6075 0.0259  -0.0458 -0.0820 236 PRO A CB  
1976 C  CG  . PRO A 236 ? 0.1142 0.2721 0.4397 0.0599  -0.0401 -0.0644 236 PRO A CG  
1977 C  CD  . PRO A 236 ? 0.1482 0.2425 0.4217 0.0798  -0.0051 -0.0579 236 PRO A CD  
1978 N  N   . GLU A 237 ? 0.1154 0.2527 0.3467 0.0634  -0.0285 -0.0917 237 GLU A N   
1979 C  CA  . GLU A 237 ? 0.1351 0.3032 0.2842 0.0992  -0.0135 -0.0785 237 GLU A CA  
1980 C  C   . GLU A 237 ? 0.1279 0.2833 0.2996 0.1071  -0.0533 -0.0768 237 GLU A C   
1981 O  O   . GLU A 237 ? 0.1852 0.3131 0.3262 0.1057  -0.0480 -0.0701 237 GLU A O   
1982 C  CB  . GLU A 237 ? 0.1523 0.3235 0.3574 0.0658  -0.0895 -0.0274 237 GLU A CB  
1983 C  CG  . GLU A 237 ? 0.1647 0.4199 0.4052 0.0397  -0.0948 0.1084  237 GLU A CG  
1984 C  CD  . GLU A 237 ? 0.5813 0.6492 0.5163 -0.1448 -0.3415 0.2011  237 GLU A CD  
1985 O  OE1 . GLU A 237 ? 0.5202 0.8881 0.6258 -0.3463 -0.0680 -0.0476 237 GLU A OE1 
1986 O  OE2 . GLU A 237 ? 0.3465 0.8435 0.6919 -0.0908 -0.2486 0.2087  237 GLU A OE2 
1987 N  N   . GLU A 238 ? 0.1204 0.2459 0.2720 0.0648  0.0000  -0.0494 238 GLU A N   
1988 C  CA  . GLU A 238 ? 0.1233 0.2488 0.2858 0.0666  -0.0065 -0.0417 238 GLU A CA  
1989 C  C   . GLU A 238 ? 0.1128 0.1967 0.2281 0.0634  0.0057  -0.0248 238 GLU A C   
1990 O  O   . GLU A 238 ? 0.1592 0.2398 0.3262 0.0891  -0.0307 -0.0625 238 GLU A O   
1991 C  CB  . GLU A 238 ? 0.1342 0.1922 0.3957 0.0285  -0.0071 -0.0856 238 GLU A CB  
1992 C  CG  . GLU A 238 ? 0.1471 0.3251 0.3452 0.0480  -0.0439 -0.0842 238 GLU A CG  
1993 C  CD  . GLU A 238 ? 0.2129 0.4115 0.3318 -0.0465 -0.0071 -0.0515 238 GLU A CD  
1994 O  OE1 . GLU A 238 ? 0.3118 0.3928 0.3585 -0.0370 -0.0529 0.0054  238 GLU A OE1 
1995 O  OE2 . GLU A 238 ? 0.2666 0.3273 0.4135 -0.0274 0.0197  -0.0803 238 GLU A OE2 
1996 N  N   A LEU A 239 ? 0.1298 0.1899 0.2113 0.1308  -0.0277 -0.0281 239 LEU A N   
1997 N  N   B LEU A 239 ? 0.2029 0.2745 0.3253 -0.0087 0.0450  0.0087  239 LEU A N   
1998 C  CA  A LEU A 239 ? 0.1091 0.2536 0.2400 0.1088  -0.0520 -0.0610 239 LEU A CA  
1999 C  CA  B LEU A 239 ? 0.1581 0.2572 0.2779 0.0148  -0.0443 -0.0714 239 LEU A CA  
2000 C  C   A LEU A 239 ? 0.1739 0.1484 0.2073 0.0899  -0.0368 -0.0153 239 LEU A C   
2001 C  C   B LEU A 239 ? 0.0960 0.2669 0.2354 0.0925  0.0012  -0.0568 239 LEU A C   
2002 O  O   A LEU A 239 ? 0.1021 0.1098 0.1782 0.0732  0.0098  0.0057  239 LEU A O   
2003 O  O   B LEU A 239 ? 0.1324 0.2290 0.2127 0.0197  -0.0137 0.0109  239 LEU A O   
2004 C  CB  A LEU A 239 ? 0.1288 0.2863 0.2409 0.0746  -0.1150 -0.0538 239 LEU A CB  
2005 C  CB  B LEU A 239 ? 0.1611 0.2486 0.3767 -0.0220 -0.0087 -0.1296 239 LEU A CB  
2006 C  CG  A LEU A 239 ? 0.2712 0.3075 0.2143 0.1699  -0.0197 -0.0460 239 LEU A CG  
2007 C  CG  B LEU A 239 ? 0.1150 0.0967 0.3772 0.0052  0.0037  -0.0812 239 LEU A CG  
2008 C  CD1 A LEU A 239 ? 0.4298 0.2912 0.2842 0.1713  -0.1230 0.0450  239 LEU A CD1 
2009 C  CD1 B LEU A 239 ? 0.1638 0.0623 0.2838 0.0450  -0.0176 0.0203  239 LEU A CD1 
2010 C  CD2 A LEU A 239 ? 0.1559 0.2265 0.2373 0.1438  -0.1106 -0.1524 239 LEU A CD2 
2011 C  CD2 B LEU A 239 ? 0.2041 0.1240 0.4433 -0.0195 0.0260  -0.0538 239 LEU A CD2 
2012 N  N   . MET A 240 ? 0.1369 0.1895 0.2330 0.1001  -0.0221 -0.0309 240 MET A N   
2013 C  CA  . MET A 240 ? 0.1579 0.1870 0.2222 0.1076  -0.0242 -0.0342 240 MET A CA  
2014 C  C   . MET A 240 ? 0.1120 0.1825 0.2125 0.0807  -0.0403 -0.0195 240 MET A C   
2015 O  O   . MET A 240 ? 0.1254 0.1486 0.2628 0.0612  -0.0582 -0.0410 240 MET A O   
2016 C  CB  . MET A 240 ? 0.1592 0.1629 0.2434 0.0900  -0.0263 -0.0259 240 MET A CB  
2017 C  CG  . MET A 240 ? 0.1168 0.1316 0.2275 0.0571  -0.0153 -0.0340 240 MET A CG  
2018 S  SD  . MET A 240 ? 0.1150 0.1412 0.2675 0.0357  -0.0120 -0.0260 240 MET A SD  
2019 C  CE  . MET A 240 ? 0.1088 0.2003 0.2477 0.0379  -0.0109 0.0193  240 MET A CE  
2020 N  N   . VAL A 241 ? 0.1680 0.1421 0.1941 0.1005  -0.0562 -0.0344 241 VAL A N   
2021 C  CA  . VAL A 241 ? 0.1435 0.1161 0.1956 0.0727  -0.0675 -0.0544 241 VAL A CA  
2022 C  C   . VAL A 241 ? 0.1116 0.0869 0.2008 0.0728  -0.0666 -0.0533 241 VAL A C   
2023 O  O   . VAL A 241 ? 0.0904 0.1383 0.2330 0.0579  -0.0498 -0.0476 241 VAL A O   
2024 C  CB  . VAL A 241 ? 0.1353 0.1116 0.2330 0.0568  -0.0719 -0.0649 241 VAL A CB  
2025 C  CG1 . VAL A 241 ? 0.2012 0.1075 0.2682 0.0366  -0.1141 -0.0794 241 VAL A CG1 
2026 C  CG2 . VAL A 241 ? 0.1367 0.1335 0.2569 0.0626  -0.0553 -0.0790 241 VAL A CG2 
2027 N  N   . ASP A 242 ? 0.1430 0.0846 0.1985 0.0509  -0.0414 -0.0588 242 ASP A N   
2028 C  CA  . ASP A 242 ? 0.1254 0.0627 0.2080 0.0551  -0.0496 -0.0428 242 ASP A CA  
2029 C  C   . ASP A 242 ? 0.0987 0.0727 0.2205 0.0509  -0.0511 -0.0476 242 ASP A C   
2030 O  O   . ASP A 242 ? 0.0873 0.0790 0.2707 0.0351  -0.0706 -0.0296 242 ASP A O   
2031 C  CB  . ASP A 242 ? 0.0985 0.0766 0.2531 0.0445  -0.0452 -0.0454 242 ASP A CB  
2032 C  CG  . ASP A 242 ? 0.1398 0.0606 0.2303 0.0571  -0.0467 -0.0293 242 ASP A CG  
2033 O  OD1 . ASP A 242 ? 0.1347 0.0626 0.2558 0.0421  -0.0511 -0.0276 242 ASP A OD1 
2034 O  OD2 . ASP A 242 ? 0.1644 0.0790 0.3050 0.0661  -0.0335 -0.0472 242 ASP A OD2 
2035 N  N   . ASN A 243 ? 0.0798 0.0661 0.2129 0.0315  -0.0292 -0.0275 243 ASN A N   
2036 C  CA  . ASN A 243 ? 0.0687 0.0653 0.1996 0.0074  -0.0276 0.0010  243 ASN A CA  
2037 C  C   . ASN A 243 ? 0.0631 0.0767 0.1823 0.0153  -0.0131 -0.0160 243 ASN A C   
2038 O  O   . ASN A 243 ? 0.0891 0.0798 0.2125 0.0362  -0.0197 -0.0164 243 ASN A O   
2039 C  CB  . ASN A 243 ? 0.0652 0.1365 0.1768 0.0153  -0.0296 -0.0065 243 ASN A CB  
2040 C  CG  . ASN A 243 ? 0.0639 0.1127 0.2154 0.0219  -0.0137 -0.0093 243 ASN A CG  
2041 O  OD1 . ASN A 243 ? 0.0789 0.0794 0.2484 0.0187  -0.0482 -0.0082 243 ASN A OD1 
2042 N  ND2 . ASN A 243 ? 0.0908 0.1784 0.2387 -0.0162 -0.0644 0.0498  243 ASN A ND2 
2043 N  N   . TRP A 244 ? 0.0825 0.0718 0.1985 -0.0049 -0.0322 -0.0098 244 TRP A N   
2044 C  CA  . TRP A 244 ? 0.0710 0.0784 0.1863 0.0019  -0.0340 0.0015  244 TRP A CA  
2045 C  C   . TRP A 244 ? 0.0500 0.0829 0.1926 0.0074  -0.0135 -0.0226 244 TRP A C   
2046 O  O   . TRP A 244 ? 0.0653 0.0974 0.2266 0.0284  -0.0281 -0.0249 244 TRP A O   
2047 C  CB  . TRP A 244 ? 0.0785 0.0491 0.2186 0.0194  -0.0264 -0.0080 244 TRP A CB  
2048 C  CG  . TRP A 244 ? 0.0529 0.0608 0.2384 0.0175  -0.0392 -0.0065 244 TRP A CG  
2049 C  CD1 . TRP A 244 ? 0.0715 0.0403 0.2459 0.0027  -0.0318 -0.0250 244 TRP A CD1 
2050 C  CD2 . TRP A 244 ? 0.0737 0.0617 0.2012 0.0164  -0.0373 -0.0249 244 TRP A CD2 
2051 N  NE1 . TRP A 244 ? 0.0847 0.0503 0.2195 0.0115  -0.0293 -0.0297 244 TRP A NE1 
2052 C  CE2 . TRP A 244 ? 0.1073 0.0596 0.2319 0.0417  -0.0425 -0.0197 244 TRP A CE2 
2053 C  CE3 . TRP A 244 ? 0.1073 0.0631 0.2125 0.0186  -0.0467 -0.0126 244 TRP A CE3 
2054 C  CZ2 . TRP A 244 ? 0.1057 0.0502 0.2513 0.0214  -0.0318 -0.0070 244 TRP A CZ2 
2055 C  CZ3 . TRP A 244 ? 0.1055 0.0741 0.2433 0.0192  -0.0456 0.0057  244 TRP A CZ3 
2056 C  CH2 . TRP A 244 ? 0.1123 0.0868 0.2434 0.0164  -0.0303 -0.0082 244 TRP A CH2 
2057 N  N   . ARG A 245 ? 0.0886 0.0834 0.1762 0.0120  -0.0326 -0.0216 245 ARG A N   
2058 C  CA  . ARG A 245 ? 0.0662 0.0606 0.1820 0.0003  -0.0326 -0.0236 245 ARG A CA  
2059 C  C   . ARG A 245 ? 0.0662 0.0697 0.2037 0.0013  -0.0419 -0.0241 245 ARG A C   
2060 O  O   . ARG A 245 ? 0.0776 0.0876 0.2184 0.0006  -0.0125 -0.0208 245 ARG A O   
2061 C  CB  . ARG A 245 ? 0.0740 0.0590 0.1865 0.0131  -0.0305 -0.0166 245 ARG A CB  
2062 C  CG  . ARG A 245 ? 0.0718 0.0555 0.2143 0.0035  -0.0401 -0.0074 245 ARG A CG  
2063 C  CD  . ARG A 245 ? 0.0810 0.0882 0.2078 -0.0162 -0.0373 -0.0308 245 ARG A CD  
2064 N  NE  . ARG A 245 ? 0.0759 0.0904 0.2064 -0.0219 -0.0357 -0.0208 245 ARG A NE  
2065 C  CZ  . ARG A 245 ? 0.0623 0.0829 0.2196 -0.0137 -0.0131 -0.0173 245 ARG A CZ  
2066 N  NH1 . ARG A 245 ? 0.0759 0.0956 0.2199 -0.0104 -0.0043 0.0035  245 ARG A NH1 
2067 N  NH2 . ARG A 245 ? 0.0797 0.1299 0.2245 -0.0254 -0.0401 -0.0175 245 ARG A NH2 
2068 N  N   . PRO A 246 ? 0.0767 0.0636 0.2290 0.0027  -0.0263 -0.0081 246 PRO A N   
2069 C  CA  . PRO A 246 ? 0.1014 0.0715 0.2310 0.0204  -0.0273 -0.0043 246 PRO A CA  
2070 C  C   . PRO A 246 ? 0.0810 0.0854 0.2168 0.0115  -0.0346 -0.0041 246 PRO A C   
2071 O  O   . PRO A 246 ? 0.0991 0.0665 0.2226 0.0098  -0.0395 -0.0093 246 PRO A O   
2072 C  CB  . PRO A 246 ? 0.1017 0.1039 0.2630 0.0195  -0.0331 0.0251  246 PRO A CB  
2073 C  CG  . PRO A 246 ? 0.1658 0.2001 0.3851 0.0577  0.0118  0.1142  246 PRO A CG  
2074 C  CD  . PRO A 246 ? 0.0702 0.0965 0.2973 0.0291  -0.0366 0.0114  246 PRO A CD  
2075 N  N   . ALA A 247 ? 0.0917 0.0877 0.2215 0.0164  -0.0115 0.0208  247 ALA A N   
2076 C  CA  . ALA A 247 ? 0.0942 0.1017 0.2134 -0.0041 -0.0305 0.0113  247 ALA A CA  
2077 C  C   . ALA A 247 ? 0.0803 0.0790 0.2109 0.0320  -0.0284 0.0060  247 ALA A C   
2078 O  O   . ALA A 247 ? 0.1136 0.0926 0.2565 0.0520  -0.0390 0.0175  247 ALA A O   
2079 C  CB  . ALA A 247 ? 0.1473 0.1123 0.2472 -0.0154 -0.0142 0.0087  247 ALA A CB  
2080 N  N   . GLN A 248 ? 0.0785 0.0706 0.2057 0.0196  -0.0399 0.0164  248 GLN A N   
2081 C  CA  . GLN A 248 ? 0.0737 0.0982 0.2400 0.0239  -0.0500 -0.0031 248 GLN A CA  
2082 C  C   . GLN A 248 ? 0.1125 0.0974 0.2387 0.0181  -0.0454 -0.0049 248 GLN A C   
2083 O  O   . GLN A 248 ? 0.1304 0.1115 0.2226 0.0163  -0.0275 0.0408  248 GLN A O   
2084 C  CB  . GLN A 248 ? 0.0940 0.0996 0.2278 0.0129  -0.0421 -0.0141 248 GLN A CB  
2085 C  CG  . GLN A 248 ? 0.1030 0.0842 0.2170 -0.0006 -0.0326 0.0043  248 GLN A CG  
2086 C  CD  . GLN A 248 ? 0.0732 0.1324 0.2558 -0.0148 -0.0239 0.0052  248 GLN A CD  
2087 O  OE1 . GLN A 248 ? 0.0983 0.2021 0.2831 -0.0198 -0.0553 -0.0109 248 GLN A OE1 
2088 N  NE2 . GLN A 248 ? 0.1091 0.1353 0.2278 0.0252  -0.0131 -0.0108 248 GLN A NE2 
2089 N  N   . PRO A 249 ? 0.1351 0.1369 0.2132 0.0447  -0.0546 -0.0229 249 PRO A N   
2090 C  CA  . PRO A 249 ? 0.1536 0.1739 0.2445 0.0873  -0.0542 -0.0198 249 PRO A CA  
2091 C  C   . PRO A 249 ? 0.1489 0.1421 0.1865 0.0697  -0.0570 0.0096  249 PRO A C   
2092 O  O   . PRO A 249 ? 0.1392 0.1502 0.2199 0.0522  -0.0608 0.0171  249 PRO A O   
2093 C  CB  . PRO A 249 ? 0.1444 0.3605 0.2955 0.1212  -0.1010 -0.0665 249 PRO A CB  
2094 C  CG  . PRO A 249 ? 0.2138 0.1947 0.2666 0.0098  -0.1040 -0.0226 249 PRO A CG  
2095 C  CD  . PRO A 249 ? 0.1172 0.2666 0.2551 0.0601  -0.0644 0.0076  249 PRO A CD  
2096 N  N   . LEU A 250 ? 0.1590 0.1425 0.2023 0.0640  -0.0292 0.0313  250 LEU A N   
2097 C  CA  . LEU A 250 ? 0.1389 0.1279 0.2163 0.0228  -0.0269 0.0086  250 LEU A CA  
2098 C  C   . LEU A 250 ? 0.1322 0.1326 0.2285 0.0397  -0.0441 0.0076  250 LEU A C   
2099 O  O   . LEU A 250 ? 0.1030 0.1254 0.2454 0.0331  -0.0597 -0.0119 250 LEU A O   
2100 C  CB  . LEU A 250 ? 0.1694 0.1195 0.2529 0.0120  -0.0219 0.0313  250 LEU A CB  
2101 C  CG  . LEU A 250 ? 0.1665 0.1692 0.2263 0.0071  0.0063  0.0054  250 LEU A CG  
2102 C  CD1 . LEU A 250 ? 0.1703 0.2197 0.2035 -0.0283 -0.0421 -0.0054 250 LEU A CD1 
2103 C  CD2 . LEU A 250 ? 0.2554 0.1613 0.2883 -0.0758 0.0054  -0.0164 250 LEU A CD2 
2104 N  N   . LYS A 251 ? 0.1538 0.1764 0.2418 0.0715  -0.0575 -0.0005 251 LYS A N   
2105 C  CA  . LYS A 251 ? 0.1337 0.2881 0.2247 0.0063  -0.0476 -0.0051 251 LYS A CA  
2106 C  C   . LYS A 251 ? 0.1559 0.3258 0.2445 0.0458  -0.0590 -0.0706 251 LYS A C   
2107 O  O   . LYS A 251 ? 0.1947 0.5648 0.3032 -0.0170 -0.0161 -0.0434 251 LYS A O   
2108 C  CB  . LYS A 251 ? 0.1615 0.2105 0.3170 0.0129  -0.0188 -0.0125 251 LYS A CB  
2109 C  CG  . LYS A 251 ? 0.2380 0.3120 0.3188 -0.0434 -0.0141 -0.1181 251 LYS A CG  
2110 C  CD  . LYS A 251 ? 0.2518 0.3930 0.3889 -0.0728 0.0460  -0.1212 251 LYS A CD  
2111 C  CE  . LYS A 251 ? 0.4047 0.4280 0.3379 0.1404  -0.0992 -0.1221 251 LYS A CE  
2112 N  NZ  . LYS A 251 ? 0.3867 0.5026 0.3961 0.2924  -0.0935 -0.1023 251 LYS A NZ  
2113 N  N   . ASN A 252 ? 0.1333 0.3625 0.2987 0.0568  -0.0790 -0.1079 252 ASN A N   
2114 C  CA  . ASN A 252 ? 0.2111 0.7357 0.4677 0.1643  0.0275  -0.1238 252 ASN A CA  
2115 C  C   . ASN A 252 ? 0.2353 0.4332 0.3239 0.1668  -0.0131 -0.1048 252 ASN A C   
2116 O  O   . ASN A 252 ? 0.2569 0.5501 0.2773 0.1040  -0.0254 0.0315  252 ASN A O   
2117 C  CB  . ASN A 252 ? 0.2389 0.9404 0.5683 0.0324  -0.1905 -0.1102 252 ASN A CB  
2118 C  CG  . ASN A 252 ? 0.5813 0.4952 1.2063 -0.0137 -0.1659 0.1508  252 ASN A CG  
2119 O  OD1 . ASN A 252 ? 1.4019 0.7425 1.4730 0.1510  -0.3079 0.2727  252 ASN A OD1 
2120 N  ND2 . ASN A 252 ? 0.6549 0.8478 1.2360 0.4092  -0.0917 -0.2034 252 ASN A ND2 
2121 N  N   . ARG A 253 ? 0.1597 0.1595 0.2558 0.0163  -0.0329 0.0041  253 ARG A N   
2122 C  CA  . ARG A 253 ? 0.1570 0.1272 0.2360 0.0274  -0.0243 -0.0019 253 ARG A CA  
2123 C  C   . ARG A 253 ? 0.1604 0.1644 0.2195 0.0463  -0.0229 0.0710  253 ARG A C   
2124 O  O   . ARG A 253 ? 0.2339 0.1967 0.3986 0.0557  0.0895  0.1054  253 ARG A O   
2125 C  CB  . ARG A 253 ? 0.1270 0.1281 0.2159 0.0173  -0.0324 0.0142  253 ARG A CB  
2126 C  CG  . ARG A 253 ? 0.1599 0.1158 0.1825 0.0063  -0.0142 -0.0006 253 ARG A CG  
2127 C  CD  . ARG A 253 ? 0.1475 0.0944 0.1796 -0.0013 -0.0324 -0.0093 253 ARG A CD  
2128 N  NE  . ARG A 253 ? 0.1127 0.0772 0.1856 0.0057  -0.0296 0.0065  253 ARG A NE  
2129 C  CZ  . ARG A 253 ? 0.0877 0.1272 0.1631 -0.0082 -0.0370 -0.0054 253 ARG A CZ  
2130 N  NH1 . ARG A 253 ? 0.0951 0.0878 0.1870 -0.0331 -0.0384 0.0006  253 ARG A NH1 
2131 N  NH2 . ARG A 253 ? 0.1010 0.0996 0.1807 -0.0035 -0.0342 -0.0063 253 ARG A NH2 
2132 N  N   A GLN A 254 ? 0.1220 0.2125 0.2657 0.0219  -0.0324 0.0062  254 GLN A N   
2133 N  N   B GLN A 254 ? 0.1525 0.0869 0.2784 0.0186  -0.0414 -0.0535 254 GLN A N   
2134 C  CA  A GLN A 254 ? 0.1340 0.2127 0.2393 0.0087  0.0063  -0.0237 254 GLN A CA  
2135 C  CA  B GLN A 254 ? 0.1556 0.2730 0.2330 -0.0458 -0.0601 -0.0020 254 GLN A CA  
2136 C  C   A GLN A 254 ? 0.1938 0.1556 0.2472 0.0109  -0.0208 -0.0208 254 GLN A C   
2137 C  C   B GLN A 254 ? 0.1999 0.1588 0.2136 0.0217  -0.0555 -0.0166 254 GLN A C   
2138 O  O   A GLN A 254 ? 0.2312 0.1419 0.2955 -0.0414 -0.1137 -0.0260 254 GLN A O   
2139 O  O   B GLN A 254 ? 0.3088 0.1547 0.3312 0.0195  -0.1272 -0.0010 254 GLN A O   
2140 C  CB  A GLN A 254 ? 0.1369 0.2508 0.2621 0.0136  0.0263  -0.0322 254 GLN A CB  
2141 C  CB  B GLN A 254 ? 0.2526 0.3359 0.2353 -0.0502 -0.0671 -0.0635 254 GLN A CB  
2142 C  CG  A GLN A 254 ? 0.1097 0.3377 0.2793 -0.0615 -0.0449 -0.0811 254 GLN A CG  
2143 C  CG  B GLN A 254 ? 0.2820 0.4356 0.1981 -0.0366 -0.0474 -0.0351 254 GLN A CG  
2144 C  CD  A GLN A 254 ? 0.2687 0.3479 0.1949 -0.0417 -0.0270 -0.0082 254 GLN A CD  
2145 C  CD  B GLN A 254 ? 0.3876 0.5048 0.2809 -0.0239 0.0109  -0.0520 254 GLN A CD  
2146 O  OE1 A GLN A 254 ? 0.4203 0.3707 0.3583 0.0000  0.1387  -0.0142 254 GLN A OE1 
2147 O  OE1 B GLN A 254 ? 0.3276 0.5198 0.4496 -0.1483 -0.0494 0.0303  254 GLN A OE1 
2148 N  NE2 A GLN A 254 ? 0.2714 0.4611 0.2060 -0.0983 -0.0445 0.0401  254 GLN A NE2 
2149 N  NE2 B GLN A 254 ? 0.5263 0.2427 0.2639 -0.0153 -0.0068 -0.0450 254 GLN A NE2 
2150 N  N   . ILE A 255 ? 0.1308 0.1456 0.2073 0.0228  -0.0397 0.0098  255 ILE A N   
2151 C  CA  . ILE A 255 ? 0.1259 0.1351 0.1762 0.0410  -0.0230 0.0026  255 ILE A CA  
2152 C  C   . ILE A 255 ? 0.0951 0.1054 0.2136 -0.0184 -0.0359 0.0344  255 ILE A C   
2153 O  O   . ILE A 255 ? 0.1337 0.1246 0.2364 0.0046  -0.0205 0.0560  255 ILE A O   
2154 C  CB  . ILE A 255 ? 0.1261 0.1073 0.2023 0.0107  -0.0296 -0.0093 255 ILE A CB  
2155 C  CG1 . ILE A 255 ? 0.1272 0.1238 0.2481 0.0359  -0.0335 -0.0087 255 ILE A CG1 
2156 C  CG2 . ILE A 255 ? 0.1197 0.1870 0.2321 -0.0104 -0.0313 -0.0205 255 ILE A CG2 
2157 C  CD1 . ILE A 255 ? 0.1553 0.1079 0.2529 0.0031  -0.0183 0.0020  255 ILE A CD1 
2158 N  N   . LYS A 256 ? 0.0996 0.1403 0.2014 0.0258  -0.0416 0.0109  256 LYS A N   
2159 C  CA  . LYS A 256 ? 0.0983 0.1475 0.2003 0.0172  -0.0346 0.0152  256 LYS A CA  
2160 C  C   . LYS A 256 ? 0.1149 0.1683 0.1773 -0.0107 -0.0335 0.0199  256 LYS A C   
2161 O  O   . LYS A 256 ? 0.1723 0.1719 0.1835 -0.0531 -0.0306 0.0199  256 LYS A O   
2162 C  CB  . LYS A 256 ? 0.1145 0.1816 0.2509 0.0432  -0.0293 -0.0216 256 LYS A CB  
2163 C  CG  . LYS A 256 ? 0.1471 0.2204 0.3248 0.0043  -0.0557 -0.0366 256 LYS A CG  
2164 C  CD  . LYS A 256 ? 0.2736 0.3021 0.5400 0.0505  0.0252  -0.1722 256 LYS A CD  
2165 C  CE  . LYS A 256 ? 0.5975 0.4955 0.6539 -0.1230 -0.0329 -0.2985 256 LYS A CE  
2166 N  NZ  . LYS A 256 ? 0.5587 0.4352 0.5975 -0.0590 0.1412  -0.1230 256 LYS A NZ  
2167 N  N   . ALA A 257 ? 0.0987 0.1421 0.2075 -0.0005 -0.0210 0.0253  257 ALA A N   
2168 C  CA  . ALA A 257 ? 0.0824 0.1764 0.2161 -0.0070 -0.0153 0.0258  257 ALA A CA  
2169 C  C   . ALA A 257 ? 0.1270 0.1717 0.1671 0.0059  -0.0175 -0.0020 257 ALA A C   
2170 O  O   . ALA A 257 ? 0.1407 0.2080 0.2002 0.0131  -0.0186 -0.0068 257 ALA A O   
2171 C  CB  . ALA A 257 ? 0.1632 0.1466 0.2730 -0.0065 0.0286  0.0595  257 ALA A CB  
2172 N  N   . SER A 258 ? 0.1080 0.1163 0.1974 0.0093  -0.0241 0.0065  258 SER A N   
2173 C  CA  . SER A 258 ? 0.1193 0.1523 0.2195 0.0297  -0.0065 0.0102  258 SER A CA  
2174 C  C   . SER A 258 ? 0.1048 0.2382 0.2222 0.0059  0.0098  0.0136  258 SER A C   
2175 O  O   . SER A 258 ? 0.1188 0.3136 0.2939 0.0412  0.0040  -0.0152 258 SER A O   
2176 C  CB  . SER A 258 ? 0.1719 0.1999 0.2011 0.0023  -0.0445 -0.0054 258 SER A CB  
2177 O  OG  . SER A 258 ? 0.1136 0.1996 0.2152 0.0096  -0.0265 0.0120  258 SER A OG  
2178 N  N   . PHE A 259 ? 0.1419 0.2132 0.2425 -0.0258 -0.0283 -0.0109 259 PHE A N   
2179 C  CA  . PHE A 259 ? 0.1902 0.2578 0.2870 -0.0741 0.0037  0.0027  259 PHE A CA  
2180 C  C   . PHE A 259 ? 0.2084 0.2247 0.3170 -0.0588 0.0427  0.0142  259 PHE A C   
2181 O  O   . PHE A 259 ? 0.2468 0.2515 0.2924 -0.0636 0.0096  0.0527  259 PHE A O   
2182 C  CB  . PHE A 259 ? 0.1177 0.2779 0.2994 -0.0434 -0.0340 -0.0476 259 PHE A CB  
2183 C  CG  . PHE A 259 ? 0.1080 0.2630 0.3063 0.0031  -0.0307 0.0540  259 PHE A CG  
2184 C  CD1 . PHE A 259 ? 0.0985 0.1836 0.2454 -0.0183 -0.0555 0.0208  259 PHE A CD1 
2185 C  CD2 . PHE A 259 ? 0.1500 0.2436 0.4372 -0.0524 0.0063  0.0496  259 PHE A CD2 
2186 C  CE1 . PHE A 259 ? 0.1249 0.2296 0.2371 -0.0219 -0.0307 -0.0109 259 PHE A CE1 
2187 C  CE2 . PHE A 259 ? 0.1527 0.2213 0.3747 -0.0443 -0.0228 0.0126  259 PHE A CE2 
2188 C  CZ  . PHE A 259 ? 0.1649 0.1721 0.4007 -0.0445 0.0065  -0.0060 259 PHE A CZ  
2189 N  N   . LYS A 260 ? 0.3273 0.4210 0.3722 -0.1976 0.0485  0.0631  260 LYS A N   
2190 C  CA  . LYS A 260 ? 0.5382 0.4920 0.4724 -0.1702 0.1097  0.1770  260 LYS A CA  
2191 C  C   . LYS A 260 ? 0.7544 0.5666 0.6603 -0.1508 0.1949  -0.0206 260 LYS A C   
2192 C  CB  . LYS A 260 ? 0.7656 0.6499 0.4095 -0.1976 0.0731  0.0346  260 LYS A CB  
2193 C  CG  . LYS A 260 ? 0.7910 0.6057 0.5551 -0.0860 -0.0675 0.0322  260 LYS A CG  
2194 C  CD  . LYS A 260 ? 0.9117 0.8568 0.6955 -0.1473 0.0041  0.1835  260 LYS A CD  
2195 C  CE  . LYS A 260 ? 0.6829 0.9204 1.0067 -0.0798 -0.2824 0.1923  260 LYS A CE  
2196 N  NZ  . LYS A 260 ? 0.7425 0.7184 0.9531 0.0054  -0.0557 0.4521  260 LYS A NZ  
2197 O  OXT . LYS A 260 ? 0.9017 0.5052 0.7307 -0.2960 -0.0221 0.2266  260 LYS A OXT 
2198 ZN ZN  . ZN  B .   ? 0.0599 0.0379 0.1897 0.0041  -0.0372 -0.0087 301 ZN  A ZN  
2199 F  F20 . V14 C .   ? 0.1389 0.0476 0.2441 0.0000  -0.0421 -0.0081 302 V14 A F20 
2200 C  C5  . V14 C .   ? 0.1106 0.0969 0.2184 0.0104  -0.0575 -0.0010 302 V14 A C5  
2201 C  C4  . V14 C .   ? 0.0860 0.0860 0.2132 -0.0068 -0.0538 -0.0185 302 V14 A C4  
2202 S  S7  . V14 C .   ? 0.0838 0.0423 0.2048 -0.0013 -0.0474 -0.0137 302 V14 A S7  
2203 O  O9  . V14 C .   ? 0.0666 0.0538 0.2168 0.0108  -0.0368 -0.0046 302 V14 A O9  
2204 N  N10 . V14 C .   ? 0.1008 0.0302 0.2653 -0.0171 -0.0623 0.0054  302 V14 A N10 
2205 O  O8  . V14 C .   ? 0.0992 0.0710 0.1879 0.0076  -0.0640 -0.0109 302 V14 A O8  
2206 C  C3  . V14 C .   ? 0.0900 0.0749 0.2398 -0.0108 -0.0194 -0.0219 302 V14 A C3  
2207 F  F12 . V14 C .   ? 0.1088 0.0860 0.2779 0.0104  0.0027  -0.0208 302 V14 A F12 
2208 C  C2  . V14 C .   ? 0.1356 0.1037 0.2815 -0.0115 0.0285  -0.0205 302 V14 A C2  
2209 F  F13 . V14 C .   ? 0.1976 0.1389 0.2786 0.0109  0.0406  -0.0098 302 V14 A F13 
2210 C  C6  . V14 C .   ? 0.1473 0.0881 0.2443 -0.0296 -0.0443 -0.0076 302 V14 A C6  
2211 C  C1  . V14 C .   ? 0.1694 0.1080 0.2536 -0.0104 -0.0208 -0.0175 302 V14 A C1  
2212 S  S11 . V14 C .   ? 0.2220 0.1703 0.2831 0.0057  -0.0010 0.0012  302 V14 A S11 
2213 O  O16 . V14 C .   ? 0.4841 0.1360 0.3695 0.0649  0.0916  0.0571  302 V14 A O16 
2214 O  O17 . V14 C .   ? 0.2623 0.1805 0.2671 -0.0091 -0.0315 -0.0062 302 V14 A O17 
2215 C  C15 . V14 C .   ? 0.2240 0.4286 0.4713 -0.1682 -0.0263 0.0652  302 V14 A C15 
2216 C  C18 . V14 C .   ? 0.3032 0.4555 0.4122 -0.0531 -0.1168 0.1279  302 V14 A C18 
2217 O  O21 . V14 C .   ? 0.2281 0.3535 0.5138 -0.0265 -0.0131 0.1463  302 V14 A O21 
2218 N  N19 . V14 C .   ? 0.2522 0.0737 0.2829 0.0059  -0.0443 -0.0230 302 V14 A N19 
2219 C  C14 . V14 C .   ? 0.1949 0.1035 0.2648 0.0274  -0.0649 -0.0080 302 V14 A C14 
2220 C  C28 . V14 C .   ? 0.1685 0.1249 0.3395 0.0054  -0.0372 0.0209  302 V14 A C28 
2221 C  C27 . V14 C .   ? 0.2391 0.1439 0.3145 -0.0829 -0.0126 -0.0035 302 V14 A C27 
2222 C  C26 . V14 C .   ? 0.2152 0.2357 0.3772 -0.0970 -0.0024 -0.0996 302 V14 A C26 
2223 C  C25 . V14 C .   ? 0.3194 0.0925 0.3621 -0.1083 0.0219  -0.0377 302 V14 A C25 
2224 C  C24 . V14 C .   ? 0.1962 0.1242 0.3501 -0.0270 -0.0522 -0.0397 302 V14 A C24 
2225 C  C23 . V14 C .   ? 0.1696 0.0994 0.3594 -0.0087 -0.0612 -0.0140 302 V14 A C23 
2226 C  C22 . V14 C .   ? 0.2008 0.0740 0.3129 -0.0076 -0.0219 0.0164  302 V14 A C22 
2227 S  S   . DMS D .   ? 0.2208 0.3686 0.4341 -0.0098 -0.0197 -0.0579 303 DMS A S   
2228 O  O   . DMS D .   ? 0.4354 1.1828 0.7055 0.3100  -0.2775 -0.4183 303 DMS A O   
2229 C  C1  . DMS D .   ? 0.2290 0.2657 0.3192 0.1000  -0.0564 -0.0097 303 DMS A C1  
2230 C  C2  . DMS D .   ? 0.4253 0.1759 0.6417 -0.1177 0.0232  -0.1220 303 DMS A C2  
2231 C  C1  . EDO E .   ? 0.4936 0.2599 0.2813 0.0359  -0.1585 -0.0697 304 EDO A C1  
2232 O  O1  . EDO E .   ? 0.4277 0.1965 0.5202 0.1454  0.0000  0.0443  304 EDO A O1  
2233 C  C2  . EDO E .   ? 0.3129 0.3731 0.4329 -0.0137 -0.0428 0.0537  304 EDO A C2  
2234 O  O2  . EDO E .   ? 0.8786 0.3192 0.3898 0.2433  -0.1950 -0.0922 304 EDO A O2  
2235 C  C1  . EDO F .   ? 0.3519 0.3429 1.0794 -0.2195 0.3652  0.0285  305 EDO A C1  
2236 O  O1  . EDO F .   ? 0.4927 1.7482 1.7165 -0.7688 0.6509  -0.9411 305 EDO A O1  
2237 C  C2  . EDO F .   ? 0.9107 0.7674 2.0092 -0.2469 -0.3400 0.2257  305 EDO A C2  
2238 O  O2  . EDO F .   ? 0.2727 0.6631 1.6978 -0.1254 -0.1395 0.3314  305 EDO A O2  
2239 C  C1  . EDO G .   ? 1.2200 0.1111 0.7462 0.0527  -0.3573 0.0675  306 EDO A C1  
2240 O  O1  . EDO G .   ? 1.2259 0.2621 0.9383 0.1375  -0.2161 -0.0060 306 EDO A O1  
2241 C  C2  . EDO G .   ? 0.8841 0.2308 0.4912 0.0702  -0.0417 0.0263  306 EDO A C2  
2242 O  O2  . EDO G .   ? 0.5177 0.2179 0.3946 0.1817  -0.1393 -0.0631 306 EDO A O2  
2243 C  C1  . EDO H .   ? 0.3201 0.1003 0.4246 0.0513  0.0665  0.0000  307 EDO A C1  
2244 O  O1  . EDO H .   ? 0.3693 0.0763 0.3580 0.0588  -0.0392 -0.0107 307 EDO A O1  
2245 C  C2  . EDO H .   ? 0.3698 0.2955 0.4688 0.0790  0.0304  0.1280  307 EDO A C2  
2246 O  O2  . EDO H .   ? 0.2373 0.1143 0.3844 0.0038  -0.0987 0.0043  307 EDO A O2  
2247 C  C1  . EDO I .   ? 0.5037 0.3747 0.5113 -0.0217 0.0087  0.0174  308 EDO A C1  
2248 O  O1  . EDO I .   ? 0.7659 0.5199 0.4370 -0.0873 0.1659  -0.0798 308 EDO A O1  
2249 C  C2  . EDO I .   ? 0.5381 0.5547 0.5076 -0.2282 0.1797  -0.0153 308 EDO A C2  
2250 O  O2  . EDO I .   ? 0.2991 0.2919 0.5569 -0.0878 -0.0087 0.0120  308 EDO A O2  
2251 O  O   . HOH J .   ? 0.0829 0.0737 0.2301 0.0087  -0.0228 0.0063  401 HOH A O   
2252 O  O   . HOH J .   ? 0.0974 0.1005 0.2563 -0.0153 -0.0317 0.0125  402 HOH A O   
2253 O  O   . HOH J .   ? 0.0969 0.0939 0.2328 0.0087  -0.0452 0.0092  403 HOH A O   
2254 O  O   . HOH J .   ? 0.0882 0.1233 0.2802 0.0229  -0.0296 -0.0417 404 HOH A O   
2255 O  O   . HOH J .   ? 0.0976 0.0859 0.2353 0.0193  -0.0460 0.0098  405 HOH A O   
2256 O  O   . HOH J .   ? 0.1899 0.1756 0.4562 0.0252  -0.1833 -0.0930 406 HOH A O   
2257 O  O   . HOH J .   ? 0.1216 0.1879 0.2678 -0.0076 -0.0588 0.0388  407 HOH A O   
2258 O  O   . HOH J .   ? 0.0974 0.0562 0.2536 0.0148  -0.0491 -0.0076 408 HOH A O   
2259 O  O   . HOH J .   ? 0.0983 0.0529 0.2452 0.0104  -0.0375 -0.0131 409 HOH A O   
2260 O  O   . HOH J .   ? 0.1308 0.1046 0.2400 0.0219  -0.0460 0.0076  410 HOH A O   
2261 O  O   . HOH J .   ? 0.1012 0.0864 0.2991 0.0184  -0.0419 0.0203  411 HOH A O   
2262 O  O   . HOH J .   ? 0.1414 0.0502 0.2818 0.0010  -0.0710 0.0031  412 HOH A O   
2263 O  O   . HOH J .   ? 0.2030 0.2154 0.2626 0.0027  -0.0221 0.0261  413 HOH A O   
2264 O  O   . HOH J .   ? 0.1620 0.1133 0.2966 0.0170  -0.0882 0.0230  414 HOH A O   
2265 O  O   . HOH J .   ? 0.0819 0.1775 0.2635 0.0119  -0.0485 -0.0410 415 HOH A O   
2266 O  O   . HOH J .   ? 0.0942 0.1263 0.2655 -0.0124 -0.0293 -0.0006 416 HOH A O   
2267 O  O   . HOH J .   ? 0.4823 0.3440 0.3321 0.2388  -0.0891 0.0062  417 HOH A O   
2268 O  O   . HOH J .   ? 0.1261 0.1118 0.3190 0.0177  -0.0570 0.0068  418 HOH A O   
2269 O  O   . HOH J .   ? 0.1102 0.0702 0.2549 0.0142  -0.0414 0.0109  419 HOH A O   
2270 O  O   . HOH J .   ? 0.1550 0.3398 0.3700 0.0529  -0.0666 -0.0250 420 HOH A O   
2271 O  O   . HOH J .   ? 0.0978 0.1039 0.3522 0.0205  -0.0527 -0.0860 421 HOH A O   
2272 O  O   . HOH J .   ? 0.1437 0.1281 0.3623 0.0000  -0.0109 -0.0546 422 HOH A O   
2273 O  O   . HOH J .   ? 0.1678 0.1692 0.2702 0.0296  0.0013  0.0368  423 HOH A O   
2274 O  O   . HOH J .   ? 0.3944 0.1726 0.4973 0.0899  0.1238  0.0491  424 HOH A O   
2275 O  O   . HOH J .   ? 0.3860 0.1599 0.4641 -0.0276 0.1185  -0.0416 425 HOH A O   
2276 O  O   . HOH J .   ? 0.2023 0.1186 0.5317 -0.0170 0.0221  0.0000  426 HOH A O   
2277 O  O   . HOH J .   ? 0.5442 0.7317 0.2975 -0.2249 -0.0013 0.0436  427 HOH A O   
2278 O  O   . HOH J .   ? 0.1249 0.1246 0.2714 0.0219  -0.0718 0.0137  428 HOH A O   
2279 O  O   . HOH J .   ? 0.1983 0.1771 0.4009 0.0856  -0.0838 -0.0679 429 HOH A O   
2280 O  O   . HOH J .   ? 0.2657 0.1516 0.3745 -0.0417 -0.0974 -0.0571 430 HOH A O   
2281 O  O   . HOH J .   ? 0.2213 0.4959 0.3016 -0.0693 0.0237  -0.0375 431 HOH A O   
2282 O  O   . HOH J .   ? 0.1462 0.1649 0.2608 0.0263  -0.0351 -0.0126 432 HOH A O   
2283 O  O   . HOH J .   ? 0.2093 0.1380 0.3711 0.0153  0.0478  0.0564  433 HOH A O   
2284 O  O   . HOH J .   ? 0.2023 0.2994 0.2915 -0.0608 0.0205  0.0992  434 HOH A O   
2285 O  O   . HOH J .   ? 0.2150 0.1665 0.3867 0.0285  0.0038  -0.0581 435 HOH A O   
2286 O  O   . HOH J .   ? 0.0908 0.2400 0.3043 -0.0344 -0.0377 -0.0034 436 HOH A O   
2287 O  O   . HOH J .   ? 0.3169 0.3165 0.5723 -0.0986 0.1181  0.0153  437 HOH A O   
2288 O  O   . HOH J .   ? 0.2675 0.1993 0.4070 0.1066  -0.0917 0.0006  438 HOH A O   
2289 O  O   . HOH J .   ? 0.2324 0.0864 0.4787 0.0020  0.0507  -0.0612 439 HOH A O   
2290 O  O   . HOH J .   ? 0.1541 0.2073 0.3118 0.0860  0.0060  0.0318  440 HOH A O   
2291 O  O   . HOH J .   ? 0.1787 0.1805 0.3601 0.0366  -0.0463 -0.0227 441 HOH A O   
2292 O  O   . HOH J .   ? 0.2520 0.2912 0.7491 -0.0728 -0.0155 -0.0930 442 HOH A O   
2293 O  O   . HOH J .   ? 0.2461 0.2425 0.3106 0.0060  0.0679  -0.0728 443 HOH A O   
2294 O  O   . HOH J .   ? 0.1974 0.0776 0.2592 -0.0209 -0.0023 -0.0197 444 HOH A O   
2295 O  O   . HOH J .   ? 0.3740 0.2606 0.3580 -0.0428 0.0898  -0.1303 445 HOH A O   
2296 O  O   . HOH J .   ? 0.1177 0.1726 0.2732 -0.0208 -0.0425 -0.0595 446 HOH A O   
2297 O  O   . HOH J .   ? 0.1532 0.2554 0.3707 -0.0675 -0.0789 0.1234  447 HOH A O   
2298 O  O   . HOH J .   ? 0.2231 0.3039 0.4677 0.0197  0.0104  0.1457  448 HOH A O   
2299 O  O   . HOH J .   ? 0.2308 0.2381 0.3544 0.0335  -0.1027 -0.0031 449 HOH A O   
2300 O  O   . HOH J .   ? 0.1929 0.1242 0.3068 -0.0405 -0.0856 -0.0046 450 HOH A O   
2301 O  O   . HOH J .   ? 0.2175 0.2596 0.4564 0.0586  -0.1124 -0.0207 451 HOH A O   
2302 O  O   . HOH J .   ? 0.3634 0.2062 0.3416 0.0768  -0.0414 0.0326  452 HOH A O   
2303 O  O   . HOH J .   ? 0.1987 0.2098 0.4483 0.1049  -0.0154 0.0237  453 HOH A O   
2304 O  O   . HOH J .   ? 0.3589 0.2029 0.3483 -0.0529 -0.0074 -0.0518 454 HOH A O   
2305 O  O   . HOH J .   ? 0.2734 0.2732 0.5975 0.0803  -0.1911 0.0355  455 HOH A O   
2306 O  O   . HOH J .   ? 0.1541 0.1633 0.2761 -0.0131 -0.0085 -0.0529 456 HOH A O   
2307 O  O   . HOH J .   ? 0.1474 0.2847 0.3156 0.0436  0.0051  0.0226  457 HOH A O   
2308 O  O   . HOH J .   ? 0.2842 0.1222 0.3503 -0.0186 -0.0344 -0.0171 458 HOH A O   
2309 O  O   . HOH J .   ? 0.2655 0.3271 0.2840 0.1190  -0.0841 0.0162  459 HOH A O   
2310 O  O   . HOH J .   ? 0.2339 0.1773 0.3508 0.0328  -0.0551 0.0553  460 HOH A O   
2311 O  O   . HOH J .   ? 0.3968 0.1511 0.4185 -0.0507 -0.1124 -0.0588 461 HOH A O   
2312 O  O   . HOH J .   ? 0.2711 0.5590 0.2890 0.1384  -0.1463 -0.1220 462 HOH A O   
2313 O  O   . HOH J .   ? 0.3424 0.5127 0.3140 -0.0370 -0.0851 -0.0187 463 HOH A O   
2314 O  O   . HOH J .   ? 0.3059 0.2100 0.3066 -0.1039 -0.0873 -0.0182 464 HOH A O   
2315 O  O   . HOH J .   ? 0.2014 0.2504 0.2937 0.0115  -0.0480 -0.0281 465 HOH A O   
2316 O  O   . HOH J .   ? 0.3330 0.2522 0.3364 -0.0252 0.0038  0.0443  466 HOH A O   
2317 O  O   . HOH J .   ? 0.0996 0.1604 0.3393 -0.0153 -0.0031 -0.0012 467 HOH A O   
2318 O  O   . HOH J .   ? 0.2402 0.1482 0.3206 -0.0732 -0.1040 0.0076  468 HOH A O   
2319 O  O   . HOH J .   ? 0.3420 0.2434 0.3574 0.0842  0.0798  0.0617  469 HOH A O   
2320 O  O   . HOH J .   ? 0.1595 0.2531 0.3018 0.0372  -0.0597 -0.0065 470 HOH A O   
2321 O  O   . HOH J .   ? 0.3228 0.2001 0.4740 0.0522  -0.2310 0.0041  471 HOH A O   
2322 O  O   . HOH J .   ? 0.1561 0.3140 0.2790 0.1569  -0.0098 -0.0057 472 HOH A O   
2323 O  O   . HOH J .   ? 0.2254 0.3221 0.3255 0.1014  -0.0406 -0.0054 473 HOH A O   
2324 O  O   . HOH J .   ? 0.3185 0.1298 0.3935 -0.0173 -0.0450 -0.0483 474 HOH A O   
2325 O  O   . HOH J .   ? 0.2213 0.2169 0.3183 0.0842  -0.0285 -0.0588 475 HOH A O   
2326 O  O   . HOH J .   ? 0.2089 0.1844 0.4034 0.0592  -0.0229 -0.0498 476 HOH A O   
2327 O  O   . HOH J .   ? 0.1448 0.1448 0.4268 0.0208  -0.0328 0.0000  477 HOH A O   
2328 O  O   . HOH J .   ? 0.3063 0.3770 0.4009 0.0108  0.0560  -0.0908 478 HOH A O   
2329 O  O   . HOH J .   ? 0.2581 0.2314 0.5715 0.0631  -0.2515 -0.1509 479 HOH A O   
2330 O  O   . HOH J .   ? 0.4079 0.2872 0.3501 0.0375  0.0496  -0.0443 480 HOH A O   
2331 O  O   . HOH J .   ? 0.4420 0.2887 0.3680 -0.1876 0.0496  -0.0944 481 HOH A O   
2332 O  O   . HOH J .   ? 0.1125 0.5687 0.3867 0.0841  -0.0873 0.0205  482 HOH A O   
2333 O  O   . HOH J .   ? 0.2154 0.3016 0.3440 0.0784  -0.0068 0.1172  483 HOH A O   
2334 O  O   . HOH J .   ? 0.6822 0.3610 0.4930 0.1010  0.1199  -0.1289 484 HOH A O   
2335 O  O   . HOH J .   ? 0.1949 0.2578 0.3788 0.0373  -0.0436 -0.0513 485 HOH A O   
2336 O  O   . HOH J .   ? 0.2125 0.1908 0.3928 0.0355  -0.0983 -0.0220 486 HOH A O   
2337 O  O   . HOH J .   ? 0.2425 0.4365 0.3932 0.0027  0.0427  0.0175  487 HOH A O   
2338 O  O   . HOH J .   ? 0.1863 0.4765 0.3882 0.0108  -0.0260 -0.0351 488 HOH A O   
2339 O  O   . HOH J .   ? 0.4370 0.1956 0.3418 -0.0929 0.0160  0.0454  489 HOH A O   
2340 O  O   . HOH J .   ? 0.1908 0.1796 0.2906 0.0086  -0.0035 0.0131  490 HOH A O   
2341 O  O   . HOH J .   ? 0.1694 0.1376 0.3795 -0.0619 -0.0728 0.0054  491 HOH A O   
2342 O  O   . HOH J .   ? 0.1757 0.1712 0.3806 0.0324  -0.0439 0.0076  492 HOH A O   
2343 O  O   . HOH J .   ? 0.3433 0.4212 0.4277 0.0328  -0.0197 0.1756  493 HOH A O   
2344 O  O   . HOH J .   ? 0.2770 0.2560 0.3912 0.0732  -0.0974 -0.0540 494 HOH A O   
2345 O  O   . HOH J .   ? 0.5187 0.7515 0.5177 -0.1360 -0.2533 -0.1168 495 HOH A O   
2346 O  O   . HOH J .   ? 0.3944 0.1574 0.4329 0.1402  -0.1084 -0.0153 496 HOH A O   
2347 O  O   . HOH J .   ? 0.3720 0.3352 0.5485 -0.1657 0.1361  -0.1993 497 HOH A O   
2348 O  O   . HOH J .   ? 0.1993 0.2093 0.4332 0.0232  -0.0197 -0.0315 498 HOH A O   
2349 O  O   . HOH J .   ? 0.1150 0.3413 0.3481 0.0186  -0.0505 0.0696  499 HOH A O   
2350 O  O   . HOH J .   ? 0.1328 0.2879 0.3032 0.0146  -0.0351 -0.0452 500 HOH A O   
2351 O  O   . HOH J .   ? 0.2314 0.1985 0.5249 0.0152  -0.0895 -0.0274 501 HOH A O   
2352 O  O   . HOH J .   ? 0.5709 0.4512 0.5278 -0.1650 -0.3003 0.0298  502 HOH A O   
2353 O  O   . HOH J .   ? 0.3655 0.9574 0.3973 0.0947  -0.0153 0.2921  503 HOH A O   
2354 O  O   . HOH J .   ? 0.2249 0.4128 0.5149 -0.0467 0.0732  0.0447  504 HOH A O   
2355 O  O   . HOH J .   ? 0.1398 0.2558 0.4384 -0.0037 -0.0458 0.0666  505 HOH A O   
2356 O  O   . HOH J .   ? 0.4948 0.1583 0.4812 0.0120  -0.1159 0.0165  506 HOH A O   
2357 O  O   . HOH J .   ? 0.1571 0.0517 0.2739 0.0135  -0.0737 -0.0115 507 HOH A O   
2358 O  O   . HOH J .   ? 0.2179 0.4855 0.5932 0.0296  0.0467  0.1358  508 HOH A O   
2359 O  O   . HOH J .   ? 0.2770 0.3494 0.3819 -0.0142 -0.1611 -0.0185 509 HOH A O   
2360 O  O   . HOH J .   ? 0.3077 0.4751 0.2863 0.1141  -0.1045 -0.0776 510 HOH A O   
2361 O  O   . HOH J .   ? 0.1756 0.3704 0.5152 -0.0772 -0.1374 0.0535  511 HOH A O   
2362 O  O   . HOH J .   ? 0.1834 0.2418 0.5903 -0.1010 0.0546  -0.2160 512 HOH A O   
2363 O  O   . HOH J .   ? 0.1931 0.4083 0.2869 -0.0046 -0.0207 -0.0129 513 HOH A O   
2364 O  O   . HOH J .   ? 0.3650 0.2703 0.3113 -0.0219 -0.0819 0.0175  514 HOH A O   
2365 O  O   . HOH J .   ? 0.3388 0.2980 0.4097 0.0104  0.0408  0.0882  515 HOH A O   
2366 O  O   . HOH J .   ? 0.2987 0.1498 0.3923 -0.0476 -0.0798 0.0680  516 HOH A O   
2367 O  O   . HOH J .   ? 0.3075 0.9297 0.4733 -0.0900 0.2739  -0.1272 517 HOH A O   
2368 O  O   . HOH J .   ? 0.3892 0.1850 0.3519 0.0241  -0.0571 0.0891  518 HOH A O   
2369 O  O   . HOH J .   ? 0.1523 0.3271 0.2630 0.0377  -0.0294 -0.0586 519 HOH A O   
2370 O  O   . HOH J .   ? 0.2763 0.1777 0.3309 -0.1400 0.0000  -0.0199 520 HOH A O   
2371 O  O   . HOH J .   ? 0.1844 0.7329 0.7814 -0.1518 0.0197  0.3655  521 HOH A O   
2372 O  O   . HOH J .   ? 0.3510 0.2195 0.4715 -0.0485 -0.0209 -0.0869 522 HOH A O   
2373 O  O   . HOH J .   ? 0.2578 0.3014 0.7746 0.0324  -0.0274 -0.1590 523 HOH A O   
2374 O  O   . HOH J .   ? 0.2041 0.3118 0.5378 0.1115  -0.1331 -0.1656 524 HOH A O   
2375 O  O   . HOH J .   ? 0.1705 0.4178 0.5004 -0.0317 -0.1481 -0.0020 525 HOH A O   
2376 O  O   . HOH J .   ? 0.5414 0.3079 0.3319 -0.0719 -0.0507 0.0227  526 HOH A O   
2377 O  O   . HOH J .   ? 0.3140 0.3792 0.3260 -0.1599 -0.0754 0.0355  527 HOH A O   
2378 O  O   . HOH J .   ? 0.1897 0.3589 0.4241 -0.0076 0.0229  0.0851  528 HOH A O   
2379 O  O   . HOH J .   ? 0.2099 0.1953 0.7486 -0.0093 0.0688  -0.0851 529 HOH A O   
2380 O  O   . HOH J .   ? 0.4688 0.2032 0.5026 -0.0131 0.1017  0.0329  530 HOH A O   
2381 O  O   . HOH J .   ? 0.3185 0.5842 0.5238 -0.0582 -0.1040 0.0405  531 HOH A O   
2382 O  O   . HOH J .   ? 0.2569 0.4449 0.4451 0.0131  -0.0274 -0.0546 532 HOH A O   
2383 O  O   . HOH J .   ? 0.3440 0.3310 0.4318 0.0952  -0.0693 -0.0996 533 HOH A O   
2384 O  O   . HOH J .   ? 0.3786 0.1421 0.4072 -0.0152 -0.0535 -0.0137 534 HOH A O   
2385 O  O   . HOH J .   ? 0.2443 0.3506 0.3801 0.0142  -0.0331 0.1796  535 HOH A O   
2386 O  O   . HOH J .   ? 0.3404 0.2800 0.4645 0.0916  0.0864  0.1005  536 HOH A O   
2387 O  O   . HOH J .   ? 0.2714 0.4198 0.7971 -0.0252 0.1668  0.2158  537 HOH A O   
2388 O  O   . HOH J .   ? 0.4361 0.4769 0.3501 -0.0904 -0.0115 0.0362  538 HOH A O   
2389 O  O   . HOH J .   ? 0.1992 0.6793 0.5194 -0.0619 -0.1268 0.2144  539 HOH A O   
2390 O  O   . HOH J .   ? 0.2145 0.7149 0.4799 0.0623  0.0197  -0.2425 540 HOH A O   
2391 O  O   . HOH J .   ? 0.2720 0.7497 0.3671 -0.1720 -0.0590 0.0658  541 HOH A O   
2392 O  O   . HOH J .   ? 0.4679 0.2888 0.5899 -0.0491 -0.0992 -0.0500 542 HOH A O   
2393 O  O   . HOH J .   ? 0.1917 0.1678 0.3303 -0.0329 -0.0320 0.0320  543 HOH A O   
2394 O  O   . HOH J .   ? 0.1967 0.3743 0.4523 0.0728  -0.0644 -0.0024 544 HOH A O   
2395 O  O   . HOH J .   ? 0.3819 0.3551 0.3833 0.1123  -0.0656 -0.0829 545 HOH A O   
2396 O  O   . HOH J .   ? 0.5224 0.4844 0.6006 0.1247  0.1650  0.0091  546 HOH A O   
2397 O  O   . HOH J .   ? 0.2450 0.3400 0.3341 -0.1164 -0.0359 0.0414  547 HOH A O   
2398 O  O   . HOH J .   ? 0.2734 0.1561 0.4724 0.0142  -0.1263 0.0759  548 HOH A O   
2399 O  O   . HOH J .   ? 0.8475 0.2254 0.4751 0.3224  -0.1771 -0.0636 549 HOH A O   
2400 O  O   . HOH J .   ? 0.3332 0.2671 0.4038 -0.0060 -0.0859 0.0368  550 HOH A O   
2401 O  O   . HOH J .   ? 0.2727 0.4106 0.3758 -0.0754 -0.1017 0.0043  551 HOH A O   
2402 O  O   . HOH J .   ? 0.3063 0.1450 0.5263 -0.0227 -0.1676 0.0275  552 HOH A O   
2403 O  O   . HOH J .   ? 0.3632 0.2143 0.7519 0.1162  0.0527  -0.0535 553 HOH A O   
2404 O  O   . HOH J .   ? 0.4133 0.2763 0.5781 0.0063  0.1145  -0.1718 554 HOH A O   
2405 O  O   . HOH J .   ? 0.2522 0.2601 0.4138 -0.0219 -0.0566 0.0590  555 HOH A O   
2406 O  O   . HOH J .   ? 0.2712 0.2211 0.4541 0.0230  -0.0164 -0.0922 556 HOH A O   
2407 O  O   . HOH J .   ? 0.3239 0.3364 0.4564 0.0294  0.0812  -0.1404 557 HOH A O   
2408 O  O   . HOH J .   ? 0.3000 0.2800 0.4384 -0.0010 0.0944  -0.1040 558 HOH A O   
2409 O  O   . HOH J .   ? 0.2046 0.0842 0.4787 0.0013  -0.0666 -0.0425 559 HOH A O   
2410 O  O   . HOH J .   ? 0.4368 0.2971 0.4165 0.1404  -0.0966 -0.0500 560 HOH A O   
2411 O  O   . HOH J .   ? 0.2980 0.3497 0.5853 0.0913  0.0439  0.1896  561 HOH A O   
2412 O  O   . HOH J .   ? 0.2639 0.1550 0.7336 -0.0472 -0.0130 0.0107  562 HOH A O   
2413 O  O   . HOH J .   ? 0.3783 0.2502 0.5149 0.1374  -0.2303 -0.1580 563 HOH A O   
2414 O  O   . HOH J .   ? 0.4550 0.2353 0.4697 -0.0271 0.0860  0.0684  564 HOH A O   
2415 O  O   . HOH J .   ? 0.3059 0.4217 0.5633 -0.0590 0.0979  0.0487  565 HOH A O   
2416 O  O   . HOH J .   ? 0.2583 0.1777 0.4110 0.1149  -0.1405 -0.0388 566 HOH A O   
2417 O  O   . HOH J .   ? 0.1994 0.4246 0.2763 -0.1190 -0.1128 0.0487  567 HOH A O   
2418 O  O   . HOH J .   ? 0.2240 0.1994 0.3594 -0.0509 -0.0030 -0.0262 568 HOH A O   
2419 O  O   . HOH J .   ? 0.4325 0.2497 0.3984 -0.0142 0.0296  0.0388  569 HOH A O   
2420 O  O   . HOH J .   ? 0.2190 0.2522 0.2439 -0.0015 -0.0195 -0.0322 570 HOH A O   
2421 O  O   . HOH J .   ? 0.2060 0.4503 0.3682 -0.0631 0.0326  -0.0425 571 HOH A O   
2422 O  O   . HOH J .   ? 0.4158 0.3271 0.4866 0.0617  -0.0829 0.0210  572 HOH A O   
2423 O  O   . HOH J .   ? 0.4765 0.2308 0.5335 0.0366  -0.1726 0.0302  573 HOH A O   
2424 O  O   . HOH J .   ? 0.3170 0.4700 0.4787 0.0859  0.1150  -0.0436 574 HOH A O   
2425 O  O   . HOH J .   ? 0.3959 0.3930 0.3300 0.1018  0.0197  -0.1506 575 HOH A O   
2426 O  O   . HOH J .   ? 0.3722 0.3000 0.4841 0.0351  0.0408  -0.1277 576 HOH A O   
2427 O  O   . HOH J .   ? 0.2741 0.3456 0.5934 0.0640  0.0151  -0.1694 577 HOH A O   
2428 O  O   . HOH J .   ? 0.5565 0.6327 0.2707 0.2451  0.0298  0.0298  578 HOH A O   
2429 O  O   . HOH J .   ? 0.6298 0.2468 0.5052 0.0560  -0.2867 0.0208  579 HOH A O   
2430 O  O   . HOH J .   ? 0.2100 0.3041 1.1138 -0.0074 -0.0441 0.1277  580 HOH A O   
2431 O  O   . HOH J .   ? 0.3170 0.4677 0.8723 -0.0254 -0.0013 0.3073  581 HOH A O   
2432 O  O   . HOH J .   ? 0.3185 0.2217 0.6136 -0.0537 0.0238  0.1018  582 HOH A O   
2433 O  O   . HOH J .   ? 0.4226 0.5781 0.4090 0.1067  0.0252  0.0098  583 HOH A O   
2434 O  O   . HOH J .   ? 0.3088 0.2369 0.3946 0.0630  -0.0073 0.0772  584 HOH A O   
2435 O  O   . HOH J .   ? 0.2964 0.3215 0.3718 -0.0283 0.0218  -0.0697 585 HOH A O   
2436 O  O   . HOH J .   ? 0.4695 0.2824 0.5253 -0.2283 0.0142  0.0175  586 HOH A O   
2437 O  O   . HOH J .   ? 0.3370 0.6571 0.8262 -0.0412 0.0816  0.3027  587 HOH A O   
2438 O  O   . HOH J .   ? 0.1651 0.4690 0.6517 0.0776  -0.0526 0.0935  588 HOH A O   
2439 O  O   . HOH J .   ? 0.6215 0.7279 0.6172 0.2196  0.0577  0.0606  589 HOH A O   
2440 O  O   . HOH J .   ? 0.4444 0.4514 0.4609 0.1876  0.0926  0.1676  590 HOH A O   
2441 O  O   . HOH J .   ? 0.3600 0.1624 0.5055 0.0104  -0.0877 -0.0353 591 HOH A O   
2442 O  O   . HOH J .   ? 0.4535 0.3395 0.6427 -0.0873 0.1341  -0.0125 592 HOH A O   
2443 O  O   . HOH J .   ? 0.4855 0.2513 0.7110 -0.1639 -0.2407 0.2240  593 HOH A O   
2444 O  O   . HOH J .   ? 0.3461 0.1735 0.8888 0.0966  0.0434  0.0366  594 HOH A O   
2445 O  O   . HOH J .   ? 0.5217 0.1580 0.7045 -0.0092 0.2485  -0.0273 595 HOH A O   
2446 O  O   . HOH J .   ? 0.2723 0.5870 0.4948 -0.0509 -0.0186 0.1393  596 HOH A O   
2447 O  O   . HOH J .   ? 0.4467 0.2531 0.4787 0.0869  0.1412  0.0315  597 HOH A O   
2448 O  O   . HOH J .   ? 0.3722 0.4844 0.7853 0.0974  0.1471  -0.2141 598 HOH A O   
2449 O  O   . HOH J .   ? 0.8215 0.2784 0.5102 0.0749  0.2186  -0.0204 599 HOH A O   
2450 O  O   . HOH J .   ? 0.1721 0.3212 0.4151 0.0017  -0.0027 0.0175  600 HOH A O   
2451 O  O   . HOH J .   ? 0.3373 0.2117 0.5849 -0.0220 0.0737  0.0472  601 HOH A O   
2452 O  O   . HOH J .   ? 0.3350 0.3486 0.5777 -0.0197 0.0759  0.2064  602 HOH A O   
2453 O  O   . HOH J .   ? 0.4722 0.3867 0.4160 -0.2757 0.0060  -0.0187 603 HOH A O   
2454 O  O   . HOH J .   ? 0.3555 0.1890 0.7724 -0.0164 0.0684  -0.1263 604 HOH A O   
2455 O  O   . HOH J .   ? 0.3921 0.3916 0.4925 0.0197  -0.0164 -0.0192 605 HOH A O   
2456 O  O   . HOH J .   ? 0.3179 0.5525 0.4821 -0.0973 -0.1721 0.0483  606 HOH A O   
2457 O  O   . HOH J .   ? 0.2199 1.3437 0.5461 0.2754  -0.1111 -0.0878 607 HOH A O   
2458 O  O   . HOH J .   ? 0.3154 0.9574 0.5062 -0.0895 -0.0447 -0.3639 608 HOH A O   
2459 O  O   . HOH J .   ? 0.3185 0.2236 0.4424 -0.0842 -0.1287 0.0353  609 HOH A O   
2460 O  O   . HOH J .   ? 0.3488 0.1940 0.4438 0.0662  -0.0482 -0.0318 610 HOH A O   
2461 O  O   . HOH J .   ? 0.2500 0.3479 0.7418 -0.1044 -0.2169 0.1532  611 HOH A O   
2462 O  O   . HOH J .   ? 0.5371 0.3165 1.0575 0.0165  -0.0505 0.0228  612 HOH A O   
2463 O  O   . HOH J .   ? 0.5454 0.2996 0.3799 -0.2197 -0.1511 0.0419  613 HOH A O   
2464 O  O   . HOH J .   ? 0.2958 0.2434 0.5950 -0.0856 -0.0571 0.1277  614 HOH A O   
2465 O  O   . HOH J .   ? 0.4772 0.4327 0.8399 -0.2485 0.1852  -0.3041 615 HOH A O   
2466 O  O   . HOH J .   ? 0.5083 0.5813 0.5906 -0.0706 0.2310  -0.2479 616 HOH A O   
2467 O  O   . HOH J .   ? 0.7505 0.4663 0.5726 0.4634  -0.2493 -0.0313 617 HOH A O   
2468 O  O   . HOH J .   ? 0.5095 0.2743 0.5156 0.0970  0.0109  0.0727  618 HOH A O   
2469 O  O   . HOH J .   ? 0.2948 0.1856 0.4986 0.0043  -0.0715 -0.0467 619 HOH A O   
2470 O  O   . HOH J .   ? 0.3488 0.6380 0.6703 -0.0176 -0.1040 -0.3621 620 HOH A O   
2471 O  O   . HOH J .   ? 0.9620 0.2030 0.4041 0.0275  -0.1861 -0.0125 621 HOH A O   
2472 O  O   . HOH J .   ? 0.2736 0.4226 0.4077 0.0921  0.0005  -0.0248 622 HOH A O   
2473 O  O   . HOH J .   ? 2.0520 0.3763 0.5246 -0.3813 0.0586  0.3616  623 HOH A O   
2474 O  O   . HOH J .   ? 0.3386 0.3720 0.6574 0.0073  -0.1324 0.0727  624 HOH A O   
2475 O  O   . HOH J .   ? 0.5490 0.5005 0.3750 -0.1746 0.0154  -0.2020 625 HOH A O   
2476 O  O   . HOH J .   ? 0.3373 0.3727 0.5533 0.0944  -0.0271 0.0142  626 HOH A O   
2477 O  O   . HOH J .   ? 0.5971 0.7228 0.5133 -0.0864 -0.0595 -0.3115 627 HOH A O   
2478 O  O   . HOH J .   ? 0.4526 0.3977 0.8288 -0.0315 0.1562  -0.1630 628 HOH A O   
2479 O  O   . HOH J .   ? 0.4844 0.5519 1.0453 0.0230  0.0214  -0.1632 629 HOH A O   
2480 O  O   . HOH J .   ? 0.3282 0.2387 0.7245 -0.0825 -0.1743 -0.0474 630 HOH A O   
2481 O  O   . HOH J .   ? 0.2892 0.1850 0.3278 0.0296  -0.0390 -0.0172 631 HOH A O   
2482 O  O   . HOH J .   ? 1.0276 0.2275 0.8726 0.1076  0.3129  -0.0147 632 HOH A O   
2483 O  O   . HOH J .   ? 0.5392 0.5162 1.4831 -0.1137 -0.0944 0.2167  633 HOH A O   
2484 O  O   . HOH J .   ? 0.3176 0.3057 0.5647 -0.0364 0.0023  0.0048  634 HOH A O   
2485 O  O   . HOH J .   ? 0.9854 0.3386 0.5174 -0.3161 0.2799  -0.0230 635 HOH A O   
2486 O  O   . HOH J .   ? 0.4223 0.2833 0.7882 -0.0988 0.0895  -0.0876 636 HOH A O   
2487 O  O   . HOH J .   ? 0.2599 0.4444 0.6485 0.0060  -0.1199 0.1010  637 HOH A O   
2488 O  O   . HOH J .   ? 0.8715 0.3747 1.5010 -0.0957 -0.5852 -0.2711 638 HOH A O   
2489 O  O   . HOH J .   ? 0.5343 0.3411 0.2619 -0.1625 0.0406  -0.0410 639 HOH A O   
2490 O  O   . HOH J .   ? 0.5417 0.4169 0.8345 0.2246  -0.2249 -0.2657 640 HOH A O   
2491 O  O   . HOH J .   ? 0.5338 0.8054 0.4379 0.2669  -0.0520 -0.1377 641 HOH A O   
2492 O  O   . HOH J .   ? 0.2958 0.5066 0.7551 0.0970  0.0441  0.0737  642 HOH A O   
2493 O  O   . HOH J .   ? 0.8087 0.3181 0.7961 -0.0577 -0.0104 -0.0137 643 HOH A O   
2494 O  O   . HOH J .   ? 0.6891 0.4539 0.7487 -0.2745 -0.0540 0.1660  644 HOH A O   
2495 O  O   . HOH J .   ? 0.4406 0.3907 0.6930 0.1321  0.1959  0.2399  645 HOH A O   
2496 O  O   . HOH J .   ? 0.5562 0.2138 0.9217 -0.0762 -0.0604 0.0259  646 HOH A O   
2497 O  O   . HOH J .   ? 0.6205 0.4679 0.5169 0.1841  -0.0687 0.0666  647 HOH A O   
2498 O  O   . HOH J .   ? 0.5030 0.3201 0.5774 -0.2178 0.0383  0.1053  648 HOH A O   
2499 O  O   . HOH J .   ? 0.1719 0.2240 0.5170 0.0362  -0.0776 -0.0296 649 HOH A O   
2500 O  O   . HOH J .   ? 0.4697 0.3842 0.5489 -0.0693 -0.2237 -0.1133 650 HOH A O   
2501 O  O   . HOH J .   ? 0.4097 0.4282 0.8184 0.1801  0.2556  0.3294  651 HOH A O   
2502 O  O   . HOH J .   ? 0.4277 0.3662 0.7149 -0.0438 0.0230  -0.0661 652 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  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS 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  THR 91  91  91  THR THR 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 126 126 126 LYS LYS A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 CYS 205 205 205 CYS CYS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 LYS 260 260 260 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 V14 1   302 1   V14 V14 A . 
D 4 DMS 1   303 5   DMS DMS A . 
E 5 EDO 1   304 1   EDO EDO A . 
F 5 EDO 1   305 2   EDO EDO A . 
G 5 EDO 1   306 3   EDO EDO A . 
H 5 EDO 1   307 4   EDO EDO A . 
I 5 EDO 1   308 5   EDO EDO A . 
J 6 HOH 1   401 1   HOH HOH A . 
J 6 HOH 2   402 2   HOH HOH A . 
J 6 HOH 3   403 3   HOH HOH A . 
J 6 HOH 4   404 4   HOH HOH A . 
J 6 HOH 5   405 5   HOH HOH A . 
J 6 HOH 6   406 6   HOH HOH A . 
J 6 HOH 7   407 7   HOH HOH A . 
J 6 HOH 8   408 8   HOH HOH A . 
J 6 HOH 9   409 9   HOH HOH A . 
J 6 HOH 10  410 10  HOH HOH A . 
J 6 HOH 11  411 11  HOH HOH A . 
J 6 HOH 12  412 12  HOH HOH A . 
J 6 HOH 13  413 13  HOH HOH A . 
J 6 HOH 14  414 14  HOH HOH A . 
J 6 HOH 15  415 15  HOH HOH A . 
J 6 HOH 16  416 16  HOH HOH A . 
J 6 HOH 17  417 17  HOH HOH A . 
J 6 HOH 18  418 18  HOH HOH A . 
J 6 HOH 19  419 19  HOH HOH A . 
J 6 HOH 20  420 20  HOH HOH A . 
J 6 HOH 21  421 21  HOH HOH A . 
J 6 HOH 22  422 22  HOH HOH A . 
J 6 HOH 23  423 23  HOH HOH A . 
J 6 HOH 24  424 24  HOH HOH A . 
J 6 HOH 25  425 25  HOH HOH A . 
J 6 HOH 26  426 26  HOH HOH A . 
J 6 HOH 27  427 27  HOH HOH A . 
J 6 HOH 28  428 28  HOH HOH A . 
J 6 HOH 29  429 29  HOH HOH A . 
J 6 HOH 30  430 30  HOH HOH A . 
J 6 HOH 31  431 31  HOH HOH A . 
J 6 HOH 32  432 32  HOH HOH A . 
J 6 HOH 33  433 33  HOH HOH A . 
J 6 HOH 34  434 34  HOH HOH A . 
J 6 HOH 35  435 35  HOH HOH A . 
J 6 HOH 36  436 36  HOH HOH A . 
J 6 HOH 37  437 37  HOH HOH A . 
J 6 HOH 38  438 38  HOH HOH A . 
J 6 HOH 39  439 39  HOH HOH A . 
J 6 HOH 40  440 40  HOH HOH A . 
J 6 HOH 41  441 41  HOH HOH A . 
J 6 HOH 42  442 42  HOH HOH A . 
J 6 HOH 43  443 43  HOH HOH A . 
J 6 HOH 44  444 44  HOH HOH A . 
J 6 HOH 45  445 45  HOH HOH A . 
J 6 HOH 46  446 46  HOH HOH A . 
J 6 HOH 47  447 47  HOH HOH A . 
J 6 HOH 48  448 48  HOH HOH A . 
J 6 HOH 49  449 49  HOH HOH A . 
J 6 HOH 50  450 50  HOH HOH A . 
J 6 HOH 51  451 51  HOH HOH A . 
J 6 HOH 52  452 52  HOH HOH A . 
J 6 HOH 53  453 53  HOH HOH A . 
J 6 HOH 54  454 54  HOH HOH A . 
J 6 HOH 55  455 55  HOH HOH A . 
J 6 HOH 56  456 56  HOH HOH A . 
J 6 HOH 57  457 57  HOH HOH A . 
J 6 HOH 58  458 58  HOH HOH A . 
J 6 HOH 59  459 59  HOH HOH A . 
J 6 HOH 60  460 60  HOH HOH A . 
J 6 HOH 61  461 61  HOH HOH A . 
J 6 HOH 62  462 62  HOH HOH A . 
J 6 HOH 63  463 63  HOH HOH A . 
J 6 HOH 64  464 64  HOH HOH A . 
J 6 HOH 65  465 65  HOH HOH A . 
J 6 HOH 66  466 66  HOH HOH A . 
J 6 HOH 67  467 67  HOH HOH A . 
J 6 HOH 68  468 68  HOH HOH A . 
J 6 HOH 69  469 69  HOH HOH A . 
J 6 HOH 70  470 70  HOH HOH A . 
J 6 HOH 71  471 71  HOH HOH A . 
J 6 HOH 72  472 72  HOH HOH A . 
J 6 HOH 73  473 73  HOH HOH A . 
J 6 HOH 74  474 74  HOH HOH A . 
J 6 HOH 75  475 75  HOH HOH A . 
J 6 HOH 76  476 76  HOH HOH A . 
J 6 HOH 77  477 77  HOH HOH A . 
J 6 HOH 78  478 78  HOH HOH A . 
J 6 HOH 79  479 79  HOH HOH A . 
J 6 HOH 80  480 80  HOH HOH A . 
J 6 HOH 81  481 81  HOH HOH A . 
J 6 HOH 82  482 82  HOH HOH A . 
J 6 HOH 83  483 83  HOH HOH A . 
J 6 HOH 84  484 84  HOH HOH A . 
J 6 HOH 85  485 85  HOH HOH A . 
J 6 HOH 86  486 86  HOH HOH A . 
J 6 HOH 87  487 87  HOH HOH A . 
J 6 HOH 88  488 88  HOH HOH A . 
J 6 HOH 89  489 89  HOH HOH A . 
J 6 HOH 90  490 90  HOH HOH A . 
J 6 HOH 91  491 91  HOH HOH A . 
J 6 HOH 92  492 92  HOH HOH A . 
J 6 HOH 93  493 93  HOH HOH A . 
J 6 HOH 94  494 94  HOH HOH A . 
J 6 HOH 95  495 95  HOH HOH A . 
J 6 HOH 96  496 96  HOH HOH A . 
J 6 HOH 97  497 97  HOH HOH A . 
J 6 HOH 98  498 98  HOH HOH A . 
J 6 HOH 99  499 99  HOH HOH A . 
J 6 HOH 100 500 100 HOH HOH A . 
J 6 HOH 101 501 101 HOH HOH A . 
J 6 HOH 102 502 102 HOH HOH A . 
J 6 HOH 103 503 103 HOH HOH A . 
J 6 HOH 104 504 104 HOH HOH A . 
J 6 HOH 105 505 105 HOH HOH A . 
J 6 HOH 106 506 106 HOH HOH A . 
J 6 HOH 107 507 107 HOH HOH A . 
J 6 HOH 108 508 108 HOH HOH A . 
J 6 HOH 109 509 109 HOH HOH A . 
J 6 HOH 110 510 110 HOH HOH A . 
J 6 HOH 111 511 111 HOH HOH A . 
J 6 HOH 112 512 112 HOH HOH A . 
J 6 HOH 113 513 113 HOH HOH A . 
J 6 HOH 114 514 114 HOH HOH A . 
J 6 HOH 115 515 115 HOH HOH A . 
J 6 HOH 116 516 116 HOH HOH A . 
J 6 HOH 117 517 117 HOH HOH A . 
J 6 HOH 118 518 118 HOH HOH A . 
J 6 HOH 119 519 119 HOH HOH A . 
J 6 HOH 120 520 120 HOH HOH A . 
J 6 HOH 121 521 121 HOH HOH A . 
J 6 HOH 122 522 122 HOH HOH A . 
J 6 HOH 123 523 123 HOH HOH A . 
J 6 HOH 124 524 124 HOH HOH A . 
J 6 HOH 125 525 125 HOH HOH A . 
J 6 HOH 126 526 126 HOH HOH A . 
J 6 HOH 127 527 127 HOH HOH A . 
J 6 HOH 128 528 128 HOH HOH A . 
J 6 HOH 129 529 129 HOH HOH A . 
J 6 HOH 130 530 130 HOH HOH A . 
J 6 HOH 131 531 131 HOH HOH A . 
J 6 HOH 132 532 132 HOH HOH A . 
J 6 HOH 133 533 133 HOH HOH A . 
J 6 HOH 134 534 134 HOH HOH A . 
J 6 HOH 135 535 135 HOH HOH A . 
J 6 HOH 136 536 136 HOH HOH A . 
J 6 HOH 137 537 137 HOH HOH A . 
J 6 HOH 138 538 138 HOH HOH A . 
J 6 HOH 139 539 139 HOH HOH A . 
J 6 HOH 140 540 140 HOH HOH A . 
J 6 HOH 141 541 141 HOH HOH A . 
J 6 HOH 142 542 142 HOH HOH A . 
J 6 HOH 143 543 143 HOH HOH A . 
J 6 HOH 144 544 144 HOH HOH A . 
J 6 HOH 145 545 145 HOH HOH A . 
J 6 HOH 146 546 146 HOH HOH A . 
J 6 HOH 147 547 147 HOH HOH A . 
J 6 HOH 148 548 148 HOH HOH A . 
J 6 HOH 149 549 149 HOH HOH A . 
J 6 HOH 150 550 150 HOH HOH A . 
J 6 HOH 151 551 151 HOH HOH A . 
J 6 HOH 152 552 152 HOH HOH A . 
J 6 HOH 153 553 153 HOH HOH A . 
J 6 HOH 154 554 154 HOH HOH A . 
J 6 HOH 155 555 155 HOH HOH A . 
J 6 HOH 156 556 156 HOH HOH A . 
J 6 HOH 157 557 157 HOH HOH A . 
J 6 HOH 158 558 158 HOH HOH A . 
J 6 HOH 159 559 159 HOH HOH A . 
J 6 HOH 160 560 160 HOH HOH A . 
J 6 HOH 161 561 161 HOH HOH A . 
J 6 HOH 162 562 162 HOH HOH A . 
J 6 HOH 163 563 163 HOH HOH A . 
J 6 HOH 164 564 164 HOH HOH A . 
J 6 HOH 165 565 165 HOH HOH A . 
J 6 HOH 166 566 166 HOH HOH A . 
J 6 HOH 167 567 167 HOH HOH A . 
J 6 HOH 168 568 168 HOH HOH A . 
J 6 HOH 169 569 169 HOH HOH A . 
J 6 HOH 170 570 170 HOH HOH A . 
J 6 HOH 171 571 171 HOH HOH A . 
J 6 HOH 172 572 172 HOH HOH A . 
J 6 HOH 173 573 173 HOH HOH A . 
J 6 HOH 174 574 174 HOH HOH A . 
J 6 HOH 175 575 175 HOH HOH A . 
J 6 HOH 176 576 176 HOH HOH A . 
J 6 HOH 177 577 177 HOH HOH A . 
J 6 HOH 178 578 178 HOH HOH A . 
J 6 HOH 179 579 179 HOH HOH A . 
J 6 HOH 180 580 180 HOH HOH A . 
J 6 HOH 181 581 181 HOH HOH A . 
J 6 HOH 182 582 182 HOH HOH A . 
J 6 HOH 183 583 183 HOH HOH A . 
J 6 HOH 184 584 184 HOH HOH A . 
J 6 HOH 185 585 185 HOH HOH A . 
J 6 HOH 186 586 186 HOH HOH A . 
J 6 HOH 187 587 187 HOH HOH A . 
J 6 HOH 188 588 188 HOH HOH A . 
J 6 HOH 189 589 189 HOH HOH A . 
J 6 HOH 190 590 190 HOH HOH A . 
J 6 HOH 191 591 191 HOH HOH A . 
J 6 HOH 192 592 192 HOH HOH A . 
J 6 HOH 193 593 193 HOH HOH A . 
J 6 HOH 194 594 194 HOH HOH A . 
J 6 HOH 195 595 195 HOH HOH A . 
J 6 HOH 196 596 196 HOH HOH A . 
J 6 HOH 197 597 197 HOH HOH A . 
J 6 HOH 198 598 198 HOH HOH A . 
J 6 HOH 199 599 199 HOH HOH A . 
J 6 HOH 200 600 200 HOH HOH A . 
J 6 HOH 201 601 201 HOH HOH A . 
J 6 HOH 202 602 202 HOH HOH A . 
J 6 HOH 203 603 203 HOH HOH A . 
J 6 HOH 204 604 204 HOH HOH A . 
J 6 HOH 205 605 205 HOH HOH A . 
J 6 HOH 206 606 206 HOH HOH A . 
J 6 HOH 207 607 207 HOH HOH A . 
J 6 HOH 208 608 208 HOH HOH A . 
J 6 HOH 209 609 209 HOH HOH A . 
J 6 HOH 210 610 210 HOH HOH A . 
J 6 HOH 211 611 211 HOH HOH A . 
J 6 HOH 212 612 212 HOH HOH A . 
J 6 HOH 213 613 213 HOH HOH A . 
J 6 HOH 214 614 214 HOH HOH A . 
J 6 HOH 215 615 215 HOH HOH A . 
J 6 HOH 216 616 216 HOH HOH A . 
J 6 HOH 217 617 217 HOH HOH A . 
J 6 HOH 218 618 218 HOH HOH A . 
J 6 HOH 219 619 219 HOH HOH A . 
J 6 HOH 220 620 220 HOH HOH A . 
J 6 HOH 221 621 221 HOH HOH A . 
J 6 HOH 222 622 222 HOH HOH A . 
J 6 HOH 223 623 223 HOH HOH A . 
J 6 HOH 224 624 224 HOH HOH A . 
J 6 HOH 225 625 225 HOH HOH A . 
J 6 HOH 226 626 226 HOH HOH A . 
J 6 HOH 227 627 227 HOH HOH A . 
J 6 HOH 228 628 228 HOH HOH A . 
J 6 HOH 229 629 229 HOH HOH A . 
J 6 HOH 230 630 230 HOH HOH A . 
J 6 HOH 231 631 231 HOH HOH A . 
J 6 HOH 232 632 232 HOH HOH A . 
J 6 HOH 233 633 233 HOH HOH A . 
J 6 HOH 234 634 234 HOH HOH A . 
J 6 HOH 235 635 235 HOH HOH A . 
J 6 HOH 236 636 236 HOH HOH A . 
J 6 HOH 237 637 237 HOH HOH A . 
J 6 HOH 238 638 238 HOH HOH A . 
J 6 HOH 239 639 239 HOH HOH A . 
J 6 HOH 240 640 240 HOH HOH A . 
J 6 HOH 241 641 241 HOH HOH A . 
J 6 HOH 242 642 242 HOH HOH A . 
J 6 HOH 243 643 243 HOH HOH A . 
J 6 HOH 244 644 244 HOH HOH A . 
J 6 HOH 245 645 245 HOH HOH A . 
J 6 HOH 246 646 246 HOH HOH A . 
J 6 HOH 247 647 247 HOH HOH A . 
J 6 HOH 248 648 248 HOH HOH A . 
J 6 HOH 249 649 249 HOH HOH A . 
J 6 HOH 250 650 250 HOH HOH A . 
J 6 HOH 251 651 251 HOH HOH A . 
J 6 HOH 252 652 252 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,H,I,J 
# 
_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_555 102.5 ? 
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_555 112.8 ? 
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_555 101.2 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V14 .   ? A V14 302 ? 1_555 112.1 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V14 .   ? A V14 302 ? 1_555 119.5 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V14 .   ? A V14 302 ? 1_555 108.3 ? 
# 
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 2015-01-28 
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' 'Data collection'        
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Derived calculations'   
5 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 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' database_2                    
5 3 'Structure model' pdbx_initial_refinement_model 
6 3 'Structure model' pdbx_struct_conn_angle        
7 3 'Structure model' struct_conn                   
8 3 'Structure model' struct_ref_seq_dif            
9 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_ref_seq_dif.details'                 
30 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
31 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
32 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       3.2.19 22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk 'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 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 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 27 ? B CZ A ARG 27 ? B NH2 A ARG 27 ? B 117.15 120.30 -3.15 0.50 N 
2 1 NE A ARG 89 ? B CZ A ARG 89 ? B NH1 A ARG 89 ? B 125.97 120.30 5.67  0.50 N 
3 1 NE A ARG 89 ? B CZ A ARG 89 ? B NH2 A ARG 89 ? B 115.78 120.30 -4.52 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? B -142.12 51.03   
2 1 LEU A 57  ? ? -121.34 -53.70  
3 1 HIS A 64  ? B -141.35 -5.60   
4 1 SER A 65  ? B -170.89 -175.94 
5 1 ALA A 77  ? ? -157.08 88.48   
6 1 LYS A 111 ? ? 73.71   -2.40   
7 1 PHE A 175 ? ? -157.10 80.40   
8 1 ASN A 243 ? ? -96.73  49.96   
9 1 LYS A 251 ? ? 56.23   -136.26 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     LYS 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      260 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     O 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    A 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    LYS 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     260 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    O 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
EDO C1   C  N N 98  
EDO O1   O  N N 99  
EDO C2   C  N N 100 
EDO O2   O  N N 101 
EDO H11  H  N N 102 
EDO H12  H  N N 103 
EDO HO1  H  N N 104 
EDO H21  H  N N 105 
EDO H22  H  N N 106 
EDO HO2  H  N N 107 
GLN N    N  N N 108 
GLN CA   C  N S 109 
GLN C    C  N N 110 
GLN O    O  N N 111 
GLN CB   C  N N 112 
GLN CG   C  N N 113 
GLN CD   C  N N 114 
GLN OE1  O  N N 115 
GLN NE2  N  N N 116 
GLN OXT  O  N N 117 
GLN H    H  N N 118 
GLN H2   H  N N 119 
GLN HA   H  N N 120 
GLN HB2  H  N N 121 
GLN HB3  H  N N 122 
GLN HG2  H  N N 123 
GLN HG3  H  N N 124 
GLN HE21 H  N N 125 
GLN HE22 H  N N 126 
GLN HXT  H  N N 127 
GLU N    N  N N 128 
GLU CA   C  N S 129 
GLU C    C  N N 130 
GLU O    O  N N 131 
GLU CB   C  N N 132 
GLU CG   C  N N 133 
GLU CD   C  N N 134 
GLU OE1  O  N N 135 
GLU OE2  O  N N 136 
GLU OXT  O  N N 137 
GLU H    H  N N 138 
GLU H2   H  N N 139 
GLU HA   H  N N 140 
GLU HB2  H  N N 141 
GLU HB3  H  N N 142 
GLU HG2  H  N N 143 
GLU HG3  H  N N 144 
GLU HE2  H  N N 145 
GLU HXT  H  N N 146 
GLY N    N  N N 147 
GLY CA   C  N N 148 
GLY C    C  N N 149 
GLY O    O  N N 150 
GLY OXT  O  N N 151 
GLY H    H  N N 152 
GLY H2   H  N N 153 
GLY HA2  H  N N 154 
GLY HA3  H  N N 155 
GLY HXT  H  N N 156 
HIS N    N  N N 157 
HIS CA   C  N S 158 
HIS C    C  N N 159 
HIS O    O  N N 160 
HIS CB   C  N N 161 
HIS CG   C  Y N 162 
HIS ND1  N  Y N 163 
HIS CD2  C  Y N 164 
HIS CE1  C  Y N 165 
HIS NE2  N  Y N 166 
HIS OXT  O  N N 167 
HIS H    H  N N 168 
HIS H2   H  N N 169 
HIS HA   H  N N 170 
HIS HB2  H  N N 171 
HIS HB3  H  N N 172 
HIS HD1  H  N N 173 
HIS HD2  H  N N 174 
HIS HE1  H  N N 175 
HIS HE2  H  N N 176 
HIS HXT  H  N N 177 
HOH O    O  N N 178 
HOH H1   H  N N 179 
HOH H2   H  N N 180 
ILE N    N  N N 181 
ILE CA   C  N S 182 
ILE C    C  N N 183 
ILE O    O  N N 184 
ILE CB   C  N S 185 
ILE CG1  C  N N 186 
ILE CG2  C  N N 187 
ILE CD1  C  N N 188 
ILE OXT  O  N N 189 
ILE H    H  N N 190 
ILE H2   H  N N 191 
ILE HA   H  N N 192 
ILE HB   H  N N 193 
ILE HG12 H  N N 194 
ILE HG13 H  N N 195 
ILE HG21 H  N N 196 
ILE HG22 H  N N 197 
ILE HG23 H  N N 198 
ILE HD11 H  N N 199 
ILE HD12 H  N N 200 
ILE HD13 H  N N 201 
ILE HXT  H  N N 202 
LEU N    N  N N 203 
LEU CA   C  N S 204 
LEU C    C  N N 205 
LEU O    O  N N 206 
LEU CB   C  N N 207 
LEU CG   C  N N 208 
LEU CD1  C  N N 209 
LEU CD2  C  N N 210 
LEU OXT  O  N N 211 
LEU H    H  N N 212 
LEU H2   H  N N 213 
LEU HA   H  N N 214 
LEU HB2  H  N N 215 
LEU HB3  H  N N 216 
LEU HG   H  N N 217 
LEU HD11 H  N N 218 
LEU HD12 H  N N 219 
LEU HD13 H  N N 220 
LEU HD21 H  N N 221 
LEU HD22 H  N N 222 
LEU HD23 H  N N 223 
LEU HXT  H  N N 224 
LYS N    N  N N 225 
LYS CA   C  N S 226 
LYS C    C  N N 227 
LYS O    O  N N 228 
LYS CB   C  N N 229 
LYS CG   C  N N 230 
LYS CD   C  N N 231 
LYS CE   C  N N 232 
LYS NZ   N  N N 233 
LYS OXT  O  N N 234 
LYS H    H  N N 235 
LYS H2   H  N N 236 
LYS HA   H  N N 237 
LYS HB2  H  N N 238 
LYS HB3  H  N N 239 
LYS HG2  H  N N 240 
LYS HG3  H  N N 241 
LYS HD2  H  N N 242 
LYS HD3  H  N N 243 
LYS HE2  H  N N 244 
LYS HE3  H  N N 245 
LYS HZ1  H  N N 246 
LYS HZ2  H  N N 247 
LYS HZ3  H  N N 248 
LYS HXT  H  N N 249 
MET N    N  N N 250 
MET CA   C  N S 251 
MET C    C  N N 252 
MET O    O  N N 253 
MET CB   C  N N 254 
MET CG   C  N N 255 
MET SD   S  N N 256 
MET CE   C  N N 257 
MET OXT  O  N N 258 
MET H    H  N N 259 
MET H2   H  N N 260 
MET HA   H  N N 261 
MET HB2  H  N N 262 
MET HB3  H  N N 263 
MET HG2  H  N N 264 
MET HG3  H  N N 265 
MET HE1  H  N N 266 
MET HE2  H  N N 267 
MET HE3  H  N N 268 
MET HXT  H  N N 269 
PHE N    N  N N 270 
PHE CA   C  N S 271 
PHE C    C  N N 272 
PHE O    O  N N 273 
PHE CB   C  N N 274 
PHE CG   C  Y N 275 
PHE CD1  C  Y N 276 
PHE CD2  C  Y N 277 
PHE CE1  C  Y N 278 
PHE CE2  C  Y N 279 
PHE CZ   C  Y N 280 
PHE OXT  O  N N 281 
PHE H    H  N N 282 
PHE H2   H  N N 283 
PHE HA   H  N N 284 
PHE HB2  H  N N 285 
PHE HB3  H  N N 286 
PHE HD1  H  N N 287 
PHE HD2  H  N N 288 
PHE HE1  H  N N 289 
PHE HE2  H  N N 290 
PHE HZ   H  N N 291 
PHE HXT  H  N N 292 
PRO N    N  N N 293 
PRO CA   C  N S 294 
PRO C    C  N N 295 
PRO O    O  N N 296 
PRO CB   C  N N 297 
PRO CG   C  N N 298 
PRO CD   C  N N 299 
PRO OXT  O  N N 300 
PRO H    H  N N 301 
PRO HA   H  N N 302 
PRO HB2  H  N N 303 
PRO HB3  H  N N 304 
PRO HG2  H  N N 305 
PRO HG3  H  N N 306 
PRO HD2  H  N N 307 
PRO HD3  H  N N 308 
PRO HXT  H  N N 309 
SER N    N  N N 310 
SER CA   C  N S 311 
SER C    C  N N 312 
SER O    O  N N 313 
SER CB   C  N N 314 
SER OG   O  N N 315 
SER OXT  O  N N 316 
SER H    H  N N 317 
SER H2   H  N N 318 
SER HA   H  N N 319 
SER HB2  H  N N 320 
SER HB3  H  N N 321 
SER HG   H  N N 322 
SER HXT  H  N N 323 
THR N    N  N N 324 
THR CA   C  N S 325 
THR C    C  N N 326 
THR O    O  N N 327 
THR CB   C  N R 328 
THR OG1  O  N N 329 
THR CG2  C  N N 330 
THR OXT  O  N N 331 
THR H    H  N N 332 
THR H2   H  N N 333 
THR HA   H  N N 334 
THR HB   H  N N 335 
THR HG1  H  N N 336 
THR HG21 H  N N 337 
THR HG22 H  N N 338 
THR HG23 H  N N 339 
THR HXT  H  N N 340 
TRP N    N  N N 341 
TRP CA   C  N S 342 
TRP C    C  N N 343 
TRP O    O  N N 344 
TRP CB   C  N N 345 
TRP CG   C  Y N 346 
TRP CD1  C  Y N 347 
TRP CD2  C  Y N 348 
TRP NE1  N  Y N 349 
TRP CE2  C  Y N 350 
TRP CE3  C  Y N 351 
TRP CZ2  C  Y N 352 
TRP CZ3  C  Y N 353 
TRP CH2  C  Y N 354 
TRP OXT  O  N N 355 
TRP H    H  N N 356 
TRP H2   H  N N 357 
TRP HA   H  N N 358 
TRP HB2  H  N N 359 
TRP HB3  H  N N 360 
TRP HD1  H  N N 361 
TRP HE1  H  N N 362 
TRP HE3  H  N N 363 
TRP HZ2  H  N N 364 
TRP HZ3  H  N N 365 
TRP HH2  H  N N 366 
TRP HXT  H  N N 367 
TYR N    N  N N 368 
TYR CA   C  N S 369 
TYR C    C  N N 370 
TYR O    O  N N 371 
TYR CB   C  N N 372 
TYR CG   C  Y N 373 
TYR CD1  C  Y N 374 
TYR CD2  C  Y N 375 
TYR CE1  C  Y N 376 
TYR CE2  C  Y N 377 
TYR CZ   C  Y N 378 
TYR OH   O  N N 379 
TYR OXT  O  N N 380 
TYR H    H  N N 381 
TYR H2   H  N N 382 
TYR HA   H  N N 383 
TYR HB2  H  N N 384 
TYR HB3  H  N N 385 
TYR HD1  H  N N 386 
TYR HD2  H  N N 387 
TYR HE1  H  N N 388 
TYR HE2  H  N N 389 
TYR HH   H  N N 390 
TYR HXT  H  N N 391 
V14 F20  F  N N 392 
V14 C5   C  Y N 393 
V14 C4   C  Y N 394 
V14 S7   S  N N 395 
V14 O9   O  N N 396 
V14 N10  N  N N 397 
V14 O8   O  N N 398 
V14 C3   C  Y N 399 
V14 F12  F  N N 400 
V14 C2   C  Y N 401 
V14 F13  F  N N 402 
V14 C6   C  Y N 403 
V14 C1   C  Y N 404 
V14 S11  S  N N 405 
V14 O16  O  N N 406 
V14 O17  O  N N 407 
V14 C15  C  N N 408 
V14 C18  C  N N 409 
V14 O21  O  N N 410 
V14 N19  N  N N 411 
V14 C14  C  N N 412 
V14 C28  C  N N 413 
V14 C27  C  N N 414 
V14 C26  C  N N 415 
V14 C25  C  N N 416 
V14 C24  C  N N 417 
V14 C23  C  N N 418 
V14 C22  C  N N 419 
V14 H1   H  N N 420 
V14 H2   H  N N 421 
V14 H3   H  N N 422 
V14 H4   H  N N 423 
V14 H5   H  N N 424 
V14 H6   H  N N 425 
V14 H7   H  N N 426 
V14 H8   H  N N 427 
V14 H9   H  N N 428 
V14 H10  H  N N 429 
V14 H11  H  N N 430 
V14 H12  H  N N 431 
V14 H13  H  N N 432 
V14 H14  H  N N 433 
V14 H15  H  N N 434 
V14 H16  H  N N 435 
V14 H17  H  N N 436 
V14 H18  H  N N 437 
V14 H19  H  N N 438 
V14 H20  H  N N 439 
V14 H21  H  N N 440 
V14 H22  H  N N 441 
V14 H23  H  N N 442 
VAL N    N  N N 443 
VAL CA   C  N S 444 
VAL C    C  N N 445 
VAL O    O  N N 446 
VAL CB   C  N N 447 
VAL CG1  C  N N 448 
VAL CG2  C  N N 449 
VAL OXT  O  N N 450 
VAL H    H  N N 451 
VAL H2   H  N N 452 
VAL HA   H  N N 453 
VAL HB   H  N N 454 
VAL HG11 H  N N 455 
VAL HG12 H  N N 456 
VAL HG13 H  N N 457 
VAL HG21 H  N N 458 
VAL HG22 H  N N 459 
VAL HG23 H  N N 460 
VAL HXT  H  N N 461 
ZN  ZN   ZN N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
EDO C1  O1   sing N N 92  
EDO C1  C2   sing N N 93  
EDO C1  H11  sing N N 94  
EDO C1  H12  sing N N 95  
EDO O1  HO1  sing N N 96  
EDO C2  O2   sing N N 97  
EDO C2  H21  sing N N 98  
EDO C2  H22  sing N N 99  
EDO O2  HO2  sing N N 100 
GLN N   CA   sing N N 101 
GLN N   H    sing N N 102 
GLN N   H2   sing N N 103 
GLN CA  C    sing N N 104 
GLN CA  CB   sing N N 105 
GLN CA  HA   sing N N 106 
GLN C   O    doub N N 107 
GLN C   OXT  sing N N 108 
GLN CB  CG   sing N N 109 
GLN CB  HB2  sing N N 110 
GLN CB  HB3  sing N N 111 
GLN CG  CD   sing N N 112 
GLN CG  HG2  sing N N 113 
GLN CG  HG3  sing N N 114 
GLN CD  OE1  doub N N 115 
GLN CD  NE2  sing N N 116 
GLN NE2 HE21 sing N N 117 
GLN NE2 HE22 sing N N 118 
GLN OXT HXT  sing N N 119 
GLU N   CA   sing N N 120 
GLU N   H    sing N N 121 
GLU N   H2   sing N N 122 
GLU CA  C    sing N N 123 
GLU CA  CB   sing N N 124 
GLU CA  HA   sing N N 125 
GLU C   O    doub N N 126 
GLU C   OXT  sing N N 127 
GLU CB  CG   sing N N 128 
GLU CB  HB2  sing N N 129 
GLU CB  HB3  sing N N 130 
GLU CG  CD   sing N N 131 
GLU CG  HG2  sing N N 132 
GLU CG  HG3  sing N N 133 
GLU CD  OE1  doub N N 134 
GLU CD  OE2  sing N N 135 
GLU OE2 HE2  sing N N 136 
GLU OXT HXT  sing N N 137 
GLY N   CA   sing N N 138 
GLY N   H    sing N N 139 
GLY N   H2   sing N N 140 
GLY CA  C    sing N N 141 
GLY CA  HA2  sing N N 142 
GLY CA  HA3  sing N N 143 
GLY C   O    doub N N 144 
GLY C   OXT  sing N N 145 
GLY OXT HXT  sing N N 146 
HIS N   CA   sing N N 147 
HIS N   H    sing N N 148 
HIS N   H2   sing N N 149 
HIS CA  C    sing N N 150 
HIS CA  CB   sing N N 151 
HIS CA  HA   sing N N 152 
HIS C   O    doub N N 153 
HIS C   OXT  sing N N 154 
HIS CB  CG   sing N N 155 
HIS CB  HB2  sing N N 156 
HIS CB  HB3  sing N N 157 
HIS CG  ND1  sing Y N 158 
HIS CG  CD2  doub Y N 159 
HIS ND1 CE1  doub Y N 160 
HIS ND1 HD1  sing N N 161 
HIS CD2 NE2  sing Y N 162 
HIS CD2 HD2  sing N N 163 
HIS CE1 NE2  sing Y N 164 
HIS CE1 HE1  sing N N 165 
HIS NE2 HE2  sing N N 166 
HIS OXT HXT  sing N N 167 
HOH O   H1   sing N N 168 
HOH O   H2   sing N N 169 
ILE N   CA   sing N N 170 
ILE N   H    sing N N 171 
ILE N   H2   sing N N 172 
ILE CA  C    sing N N 173 
ILE CA  CB   sing N N 174 
ILE CA  HA   sing N N 175 
ILE C   O    doub N N 176 
ILE C   OXT  sing N N 177 
ILE CB  CG1  sing N N 178 
ILE CB  CG2  sing N N 179 
ILE CB  HB   sing N N 180 
ILE CG1 CD1  sing N N 181 
ILE CG1 HG12 sing N N 182 
ILE CG1 HG13 sing N N 183 
ILE CG2 HG21 sing N N 184 
ILE CG2 HG22 sing N N 185 
ILE CG2 HG23 sing N N 186 
ILE CD1 HD11 sing N N 187 
ILE CD1 HD12 sing N N 188 
ILE CD1 HD13 sing N N 189 
ILE OXT HXT  sing N N 190 
LEU N   CA   sing N N 191 
LEU N   H    sing N N 192 
LEU N   H2   sing N N 193 
LEU CA  C    sing N N 194 
LEU CA  CB   sing N N 195 
LEU CA  HA   sing N N 196 
LEU C   O    doub N N 197 
LEU C   OXT  sing N N 198 
LEU CB  CG   sing N N 199 
LEU CB  HB2  sing N N 200 
LEU CB  HB3  sing N N 201 
LEU CG  CD1  sing N N 202 
LEU CG  CD2  sing N N 203 
LEU CG  HG   sing N N 204 
LEU CD1 HD11 sing N N 205 
LEU CD1 HD12 sing N N 206 
LEU CD1 HD13 sing N N 207 
LEU CD2 HD21 sing N N 208 
LEU CD2 HD22 sing N N 209 
LEU CD2 HD23 sing N N 210 
LEU OXT HXT  sing N N 211 
LYS N   CA   sing N N 212 
LYS N   H    sing N N 213 
LYS N   H2   sing N N 214 
LYS CA  C    sing N N 215 
LYS CA  CB   sing N N 216 
LYS CA  HA   sing N N 217 
LYS C   O    doub N N 218 
LYS C   OXT  sing N N 219 
LYS CB  CG   sing N N 220 
LYS CB  HB2  sing N N 221 
LYS CB  HB3  sing N N 222 
LYS CG  CD   sing N N 223 
LYS CG  HG2  sing N N 224 
LYS CG  HG3  sing N N 225 
LYS CD  CE   sing N N 226 
LYS CD  HD2  sing N N 227 
LYS CD  HD3  sing N N 228 
LYS CE  NZ   sing N N 229 
LYS CE  HE2  sing N N 230 
LYS CE  HE3  sing N N 231 
LYS NZ  HZ1  sing N N 232 
LYS NZ  HZ2  sing N N 233 
LYS NZ  HZ3  sing N N 234 
LYS OXT HXT  sing N N 235 
MET N   CA   sing N N 236 
MET N   H    sing N N 237 
MET N   H2   sing N N 238 
MET CA  C    sing N N 239 
MET CA  CB   sing N N 240 
MET CA  HA   sing N N 241 
MET C   O    doub N N 242 
MET C   OXT  sing N N 243 
MET CB  CG   sing N N 244 
MET CB  HB2  sing N N 245 
MET CB  HB3  sing N N 246 
MET CG  SD   sing N N 247 
MET CG  HG2  sing N N 248 
MET CG  HG3  sing N N 249 
MET SD  CE   sing N N 250 
MET CE  HE1  sing N N 251 
MET CE  HE2  sing N N 252 
MET CE  HE3  sing N N 253 
MET OXT HXT  sing N N 254 
PHE N   CA   sing N N 255 
PHE N   H    sing N N 256 
PHE N   H2   sing N N 257 
PHE CA  C    sing N N 258 
PHE CA  CB   sing N N 259 
PHE CA  HA   sing N N 260 
PHE C   O    doub N N 261 
PHE C   OXT  sing N N 262 
PHE CB  CG   sing N N 263 
PHE CB  HB2  sing N N 264 
PHE CB  HB3  sing N N 265 
PHE CG  CD1  doub Y N 266 
PHE CG  CD2  sing Y N 267 
PHE CD1 CE1  sing Y N 268 
PHE CD1 HD1  sing N N 269 
PHE CD2 CE2  doub Y N 270 
PHE CD2 HD2  sing N N 271 
PHE CE1 CZ   doub Y N 272 
PHE CE1 HE1  sing N N 273 
PHE CE2 CZ   sing Y N 274 
PHE CE2 HE2  sing N N 275 
PHE CZ  HZ   sing N N 276 
PHE OXT HXT  sing N N 277 
PRO N   CA   sing N N 278 
PRO N   CD   sing N N 279 
PRO N   H    sing N N 280 
PRO CA  C    sing N N 281 
PRO CA  CB   sing N N 282 
PRO CA  HA   sing N N 283 
PRO C   O    doub N N 284 
PRO C   OXT  sing N N 285 
PRO CB  CG   sing N N 286 
PRO CB  HB2  sing N N 287 
PRO CB  HB3  sing N N 288 
PRO CG  CD   sing N N 289 
PRO CG  HG2  sing N N 290 
PRO CG  HG3  sing N N 291 
PRO CD  HD2  sing N N 292 
PRO CD  HD3  sing N N 293 
PRO OXT HXT  sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
THR N   CA   sing N N 308 
THR N   H    sing N N 309 
THR N   H2   sing N N 310 
THR CA  C    sing N N 311 
THR CA  CB   sing N N 312 
THR CA  HA   sing N N 313 
THR C   O    doub N N 314 
THR C   OXT  sing N N 315 
THR CB  OG1  sing N N 316 
THR CB  CG2  sing N N 317 
THR CB  HB   sing N N 318 
THR OG1 HG1  sing N N 319 
THR CG2 HG21 sing N N 320 
THR CG2 HG22 sing N N 321 
THR CG2 HG23 sing N N 322 
THR OXT HXT  sing N N 323 
TRP N   CA   sing N N 324 
TRP N   H    sing N N 325 
TRP N   H2   sing N N 326 
TRP CA  C    sing N N 327 
TRP CA  CB   sing N N 328 
TRP CA  HA   sing N N 329 
TRP C   O    doub N N 330 
TRP C   OXT  sing N N 331 
TRP CB  CG   sing N N 332 
TRP CB  HB2  sing N N 333 
TRP CB  HB3  sing N N 334 
TRP CG  CD1  doub Y N 335 
TRP CG  CD2  sing Y N 336 
TRP CD1 NE1  sing Y N 337 
TRP CD1 HD1  sing N N 338 
TRP CD2 CE2  doub Y N 339 
TRP CD2 CE3  sing Y N 340 
TRP NE1 CE2  sing Y N 341 
TRP NE1 HE1  sing N N 342 
TRP CE2 CZ2  sing Y N 343 
TRP CE3 CZ3  doub Y N 344 
TRP CE3 HE3  sing N N 345 
TRP CZ2 CH2  doub Y N 346 
TRP CZ2 HZ2  sing N N 347 
TRP CZ3 CH2  sing Y N 348 
TRP CZ3 HZ3  sing N N 349 
TRP CH2 HH2  sing N N 350 
TRP OXT HXT  sing N N 351 
TYR N   CA   sing N N 352 
TYR N   H    sing N N 353 
TYR N   H2   sing N N 354 
TYR CA  C    sing N N 355 
TYR CA  CB   sing N N 356 
TYR CA  HA   sing N N 357 
TYR C   O    doub N N 358 
TYR C   OXT  sing N N 359 
TYR CB  CG   sing N N 360 
TYR CB  HB2  sing N N 361 
TYR CB  HB3  sing N N 362 
TYR CG  CD1  doub Y N 363 
TYR CG  CD2  sing Y N 364 
TYR CD1 CE1  sing Y N 365 
TYR CD1 HD1  sing N N 366 
TYR CD2 CE2  doub Y N 367 
TYR CD2 HD2  sing N N 368 
TYR CE1 CZ   doub Y N 369 
TYR CE1 HE1  sing N N 370 
TYR CE2 CZ   sing Y N 371 
TYR CE2 HE2  sing N N 372 
TYR CZ  OH   sing N N 373 
TYR OH  HH   sing N N 374 
TYR OXT HXT  sing N N 375 
V14 C18 O21  sing N N 376 
V14 C18 C15  sing N N 377 
V14 C15 S11  sing N N 378 
V14 O17 S11  doub N N 379 
V14 C22 C23  sing N N 380 
V14 C22 C14  sing N N 381 
V14 C23 C24  sing N N 382 
V14 N19 C14  sing N N 383 
V14 N19 C6   sing N N 384 
V14 C24 C25  sing N N 385 
V14 S11 C1   sing N N 386 
V14 S11 O16  doub N N 387 
V14 C14 C28  sing N N 388 
V14 C6  C1   doub Y N 389 
V14 C6  C5   sing Y N 390 
V14 C1  C2   sing Y N 391 
V14 F20 C5   sing N N 392 
V14 C25 C26  sing N N 393 
V14 C5  C4   doub Y N 394 
V14 C26 C27  sing N N 395 
V14 C28 C27  sing N N 396 
V14 C2  F13  sing N N 397 
V14 C2  C3   doub Y N 398 
V14 C4  C3   sing Y N 399 
V14 C4  S7   sing N N 400 
V14 C3  F12  sing N N 401 
V14 N10 S7   sing N N 402 
V14 S7  O9   doub N N 403 
V14 S7  O8   doub N N 404 
V14 N10 H1   sing N N 405 
V14 N10 H2   sing N N 406 
V14 C15 H3   sing N N 407 
V14 C15 H4   sing N N 408 
V14 C18 H5   sing N N 409 
V14 C18 H6   sing N N 410 
V14 O21 H7   sing N N 411 
V14 N19 H8   sing N N 412 
V14 C14 H9   sing N N 413 
V14 C28 H10  sing N N 414 
V14 C28 H11  sing N N 415 
V14 C27 H12  sing N N 416 
V14 C27 H13  sing N N 417 
V14 C26 H14  sing N N 418 
V14 C26 H15  sing N N 419 
V14 C25 H16  sing N N 420 
V14 C25 H17  sing N N 421 
V14 C24 H18  sing N N 422 
V14 C24 H19  sing N N 423 
V14 C23 H20  sing N N 424 
V14 C23 H21  sing N N 425 
V14 C22 H22  sing N N 426 
V14 C22 H23  sing N N 427 
VAL N   CA   sing N N 428 
VAL N   H    sing N N 429 
VAL N   H2   sing N N 430 
VAL CA  C    sing N N 431 
VAL CA  CB   sing N N 432 
VAL CA  HA   sing N N 433 
VAL C   O    doub N N 434 
VAL C   OXT  sing N N 435 
VAL CB  CG1  sing N N 436 
VAL CB  CG2  sing N N 437 
VAL CB  HB   sing N N 438 
VAL CG1 HG11 sing N N 439 
VAL CG1 HG12 sing N N 440 
VAL CG1 HG13 sing N N 441 
VAL CG2 HG21 sing N N 442 
VAL CG2 HG22 sing N N 443 
VAL CG2 HG23 sing N N 444 
VAL OXT HXT  sing N N 445 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                           ZN  
3 '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V14 
4 'DIMETHYL SULFOXIDE'                                                                 DMS 
5 1,2-ETHANEDIOL                                                                       EDO 
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' 
# 
