data_4Q08
# 
_entry.id   4Q08 
# 
_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   4Q08         pdb_00004q08 10.2210/pdb4q08/pdb 
RCSB  RCSB085440   ?            ?                   
WWPDB D_1000085440 ?            ?                   
# 
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 4Q09 . unspecified 
PDB 4Q0L . unspecified 
# 
_pdbx_database_status.entry_id                        4Q08 
_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           4Q08 
_cell.length_a           41.821 
_cell.length_b           41.058 
_cell.length_c           71.468 
_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                         4Q08 
_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 'DIMETHYL SULFOXIDE'                                                                 78.133    1   ?       ? ? ? 
4 non-polymer syn BICINE                                                                               163.172   1   ?       ? ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                               195.237   1   ?       ? ? ? 
6 non-polymer syn '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 412.491   1   ?       ? ? ? 
7 water       nat water                                                                                18.015    338 ?       ? ? ? 
# 
_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     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4Q08 
_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 4Q08 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 4Q08 LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 4Q08 THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 4Q08 ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 4 
1 4Q08 SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 134 5 
1 4Q08 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 
BCN non-polymer         . BICINE                                                                               ? 'C6 H13 N O4' 
163.172 
CYS 'L-peptide linking' y CYSTEINE                                                                             ? 'C3 H7 N O2 S' 
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                 ? 'C2 H6 O S' 
78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                            ? 'C5 H10 N2 O3' 
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                      ? 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                                              ? 'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                            ? 'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                                                ? 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                           ? 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                              ? 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                                               ? 'C6 H15 N2 O2 1' 
147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                               ? 'C6 H13 N O4 S' 
195.237 
MET 'L-peptide linking' y METHIONINE                                                                           ? 'C5 H11 N O2 S' 
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                        ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                              ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                               ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                            ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                           ? 'C11 H12 N2 O2' 
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                             ? 'C9 H11 N O3' 
181.189 
V90 non-polymer         . '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' ? 
'C16 H23 F3 N2 O3 S2' 412.491 
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          4Q08 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   37.7 
_exptl_crystal.density_Matthews      1.99 
_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   2013-05-23 
_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 P14 (MX2)' 
_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   'P14 (MX2)' 
# 
_reflns.entry_id                     4Q08 
_reflns.d_resolution_high            1.065 
_reflns.d_resolution_low             41.058 
_reflns.number_all                   ? 
_reflns.number_obs                   98666 
_reflns.pdbx_netI_over_sigmaI        14.000 
_reflns.pdbx_Rsym_value              0.032 
_reflns.pdbx_redundancy              3.100 
_reflns.percent_possible_obs         93.700 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        7.999 
_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 
1.06 1.12  ? 26510 ? 0.339 2.0  0.339 ? 2.30 ? 11417 75.00 1  1 
1.12 1.19  ? 32719 ? 0.231 3.2  0.231 ? 2.50 ? 12862 89.20 2  1 
1.19 1.27  ? 37666 ? 0.171 4.3  0.171 ? 2.90 ? 13001 95.50 3  1 
1.27 1.37  ? 41178 ? 0.125 5.9  0.125 ? 3.30 ? 12538 98.50 4  1 
1.37 1.51  ? 37637 ? 0.081 9.2  0.081 ? 3.30 ? 11551 98.80 5  1 
1.51 1.68  ? 35693 ? 0.050 14.6 0.050 ? 3.40 ? 10509 98.90 6  1 
1.68 1.94  ? 32124 ? 0.033 21.0 0.033 ? 3.50 ? 9285  99.30 7  1 
1.94 2.38  ? 26975 ? 0.025 26.3 0.025 ? 3.40 ? 7909  99.40 8  1 
2.38 3.37  ? 21108 ? 0.022 27.5 0.022 ? 3.40 ? 6144  99.40 9  1 
3.37 41.06 ? 11396 ? 0.024 19.8 0.024 ? 3.30 ? 3450  99.20 10 1 
# 
_refine.entry_id                                 4Q08 
_refine.ls_d_res_high                            1.070 
_refine.ls_d_res_low                             40.650 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    93.590 
_refine.ls_number_reflns_obs                     98646 
_refine.ls_number_reflns_all                     98646 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          0.131 
_refine.ls_R_factor_obs                          0.131 
_refine.ls_R_factor_R_work                       0.128 
_refine.ls_wR_factor_R_work                      0.128 
_refine.ls_R_factor_R_free                       0.156 
_refine.ls_wR_factor_R_free                      0.157 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  9883 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               14.485 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.220 
_refine.aniso_B[2][2]                            -0.120 
_refine.aniso_B[3][3]                            0.240 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.210 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.981 
_refine.correlation_coeff_Fo_to_Fc_free          0.974 
_refine.overall_SU_R_Cruickshank_DPI             0.029 
_refine.overall_SU_R_free                        0.031 
_refine.pdbx_overall_ESU_R                       0.029 
_refine.pdbx_overall_ESU_R_Free                  0.030 
_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                   0.932 
_refine.B_iso_max                                104.08 
_refine.B_iso_min                                4.01 
_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        2043 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             338 
_refine_hist.number_atoms_total               2432 
_refine_hist.d_res_high                       1.070 
_refine_hist.d_res_low                        40.650 
# 
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       2407 0.024  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3292 2.492  1.985  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 301  7.156  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 107  38.787 24.953 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 400  14.277 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 8    18.845 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         335  0.175  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1879 0.016  0.021  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr     2407 8.699  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free      339  22.141 5.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded    2324 10.488 5.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.065 
_refine_ls_shell.d_res_low                        1.093 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               65.180 
_refine_ls_shell.number_reflns_R_work             4525 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.211 
_refine_ls_shell.R_factor_R_free                  0.246 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             517 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                5042 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4Q08 
_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        4Q08 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
# 
_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 ? ? ? ? ? ? ? 1.991 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F V90 . N11 A ? A ZN  301 A V90 305 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F V90 . N11 B ? A ZN  301 A V90 305 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc6 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F V90 . S8  A ? A ZN  301 A V90 305 1_555 ? ? ? ? ? ? ? 2.992 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -3.15 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 15.97 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 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 DMS 302 ? 4  'BINDING SITE FOR RESIDUE DMS A 302' 
AC3 Software A BCN 303 ? 7  'BINDING SITE FOR RESIDUE BCN A 303' 
AC4 Software A MES 304 ? 5  'BINDING SITE FOR RESIDUE MES A 304' 
AC5 Software A V90 305 ? 20 'BINDING SITE FOR RESIDUE V90 A 305' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  V90 F .   ? V90 A 305 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 242 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 244 . ? 1_555 ? 
8  AC2 4  HOH G .   ? HOH A 669 . ? 1_555 ? 
9  AC3 7  LYS A 148 ? LYS A 148 . ? 1_555 ? 
10 AC3 7  LYS A 212 ? LYS A 212 . ? 1_555 ? 
11 AC3 7  GLU A 213 ? GLU A 213 . ? 1_555 ? 
12 AC3 7  PRO A 214 ? PRO A 214 . ? 1_555 ? 
13 AC3 7  HOH G .   ? HOH A 452 . ? 1_555 ? 
14 AC3 7  HOH G .   ? HOH A 509 . ? 1_555 ? 
15 AC3 7  HOH G .   ? HOH A 586 . ? 1_555 ? 
16 AC4 5  LEU A 163 ? LEU A 163 . ? 1_555 ? 
17 AC4 5  ASP A 164 ? ASP A 164 . ? 1_555 ? 
18 AC4 5  LYS A 224 ? LYS A 224 . ? 1_555 ? 
19 AC4 5  LYS A 227 ? LYS A 227 . ? 1_555 ? 
20 AC4 5  HOH G .   ? HOH A 450 . ? 1_555 ? 
21 AC5 20 TYR A 7   ? TYR A 7   . ? 1_555 ? 
22 AC5 20 ASN A 62  ? ASN A 62  . ? 1_555 ? 
23 AC5 20 HIS A 64  ? HIS A 64  . ? 1_555 ? 
24 AC5 20 SER A 65  ? SER A 65  . ? 1_555 ? 
25 AC5 20 LYS A 67  ? LYS A 67  . ? 1_555 ? 
26 AC5 20 GLN A 92  ? GLN A 92  . ? 1_555 ? 
27 AC5 20 HIS A 94  ? HIS A 94  . ? 1_555 ? 
28 AC5 20 HIS A 96  ? HIS A 96  . ? 1_555 ? 
29 AC5 20 HIS A 119 ? HIS A 119 . ? 1_555 ? 
30 AC5 20 VAL A 121 ? VAL A 121 . ? 1_555 ? 
31 AC5 20 LEU A 140 ? LEU A 140 . ? 1_555 ? 
32 AC5 20 VAL A 142 ? VAL A 142 . ? 1_555 ? 
33 AC5 20 LEU A 197 ? LEU A 197 . ? 1_555 ? 
34 AC5 20 THR A 198 ? THR A 198 . ? 1_555 ? 
35 AC5 20 THR A 199 ? THR A 199 . ? 1_555 ? 
36 AC5 20 TRP A 208 ? TRP A 208 . ? 1_555 ? 
37 AC5 20 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
38 AC5 20 HOH G .   ? HOH A 663 . ? 1_555 ? 
39 AC5 20 HOH G .   ? HOH A 680 . ? 1_555 ? 
40 AC5 20 HOH G .   ? HOH A 716 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4Q08 
_atom_sites.fract_transf_matrix[1][1]   0.023911 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005768 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024356 
_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]   0.014394 
_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   A HIS A 1 4   ? 11.811  -0.263  8.002   0.50 16.39  ? 4   HIS A N   1 
ATOM   2    N  N   B HIS A 1 4   ? 9.581   1.958   8.409   0.50 11.47  ? 4   HIS A N   1 
ATOM   3    C  CA  A HIS A 1 4   ? 10.592  0.151   8.676   0.50 20.56  ? 4   HIS A CA  1 
ATOM   4    C  CA  B HIS A 1 4   ? 10.240  0.551   8.426   0.50 22.69  ? 4   HIS A CA  1 
ATOM   5    C  C   A HIS A 1 4   ? 9.934   -0.916  9.491   0.50 15.38  ? 4   HIS A C   1 
ATOM   6    C  C   B HIS A 1 4   ? 9.714   -0.708  9.246   0.50 21.59  ? 4   HIS A C   1 
ATOM   7    O  O   A HIS A 1 4   ? 10.189  -2.123  9.293   0.50 18.33  ? 4   HIS A O   1 
ATOM   8    O  O   B HIS A 1 4   ? 9.940   -1.875  8.844   0.50 19.07  ? 4   HIS A O   1 
ATOM   9    C  CB  A HIS A 1 4   ? 9.591   0.747   7.705   0.50 18.10  ? 4   HIS A CB  1 
ATOM   10   C  CB  B HIS A 1 4   ? 11.769  0.698   8.554   0.50 27.75  ? 4   HIS A CB  1 
ATOM   11   C  CG  A HIS A 1 4   ? 9.091   2.018   8.197   0.50 14.85  ? 4   HIS A CG  1 
ATOM   12   C  CG  B HIS A 1 4   ? 12.320  0.220   9.836   0.50 27.08  ? 4   HIS A CG  1 
ATOM   13   N  ND1 A HIS A 1 4   ? 9.888   2.872   8.805   0.50 23.95  ? 4   HIS A ND1 1 
ATOM   14   N  ND1 B HIS A 1 4   ? 13.126  -0.843  9.885   0.50 23.04  ? 4   HIS A ND1 1 
ATOM   15   C  CD2 A HIS A 1 4   ? 7.801   2.502   8.289   0.50 12.74  ? 4   HIS A CD2 1 
ATOM   16   C  CD2 B HIS A 1 4   ? 12.132  0.660   11.158  0.50 27.73  ? 4   HIS A CD2 1 
ATOM   17   C  CE1 A HIS A 1 4   ? 9.146   3.949   9.213   0.50 25.58  ? 4   HIS A CE1 1 
ATOM   18   C  CE1 B HIS A 1 4   ? 13.433  -1.107  11.176  0.50 25.29  ? 4   HIS A CE1 1 
ATOM   19   N  NE2 A HIS A 1 4   ? 7.858   3.716   8.870   0.50 27.29  ? 4   HIS A NE2 1 
ATOM   20   N  NE2 B HIS A 1 4   ? 12.835  -0.169  11.959  0.50 23.49  ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 9.009   -0.497  10.362  1.00 20.82  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 8.335   -1.487  11.154  1.00 15.87  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 7.313   -2.235  10.350  1.00 14.50  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.828   -1.779  9.329   1.00 15.35  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.649   -0.748  12.340  1.00 16.28  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 6.470   0.125   11.971  1.00 14.74  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 6.493   1.471   11.677  1.00 16.68  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 5.121   -0.306  11.811  1.00 13.19  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 5.266   1.905   11.351  1.00 17.13  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 4.364   0.864   11.466  1.00 14.07  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 4.467   -1.540  12.093  1.00 12.37  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.978   0.813   11.279  1.00 15.29  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 3.068   -1.582  11.901  1.00 13.42  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 2.348   -0.395  11.546  1.00 13.57  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 7.002   -3.432  10.827  1.00 14.04  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.952   -4.257  10.294  1.00 13.60  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.555   -5.333  11.231  1.00 11.61  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.539   -5.131  12.472  1.00 11.25  ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 5.227   -6.508  10.698  1.00 13.80  ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.772   -7.642  11.497  1.00 13.34  ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.609   -8.867  11.365  1.00 16.64  ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 5.274   -9.933  11.840  1.00 23.48  ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 3.273   -7.972  11.157  1.00 13.67  ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 2.361   -6.850  11.641  1.00 11.34  ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.929   -6.864  13.008  1.00 10.77  ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.857   -5.926  10.781  1.00 11.83  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 1.042   -5.873  13.446  1.00 9.71   ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.980   -4.977  11.226  1.00 11.52  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.578   -4.960  12.585  1.00 10.33  ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.307  -3.990  12.924  1.00 12.21  ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.778   -8.735  10.705  1.00 15.81  ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.641   -9.914  10.418  1.00 18.54  ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.667   -10.170 11.532  1.00 17.52  ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.776   -9.501  12.556  1.00 16.51  ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.496   -11.187 11.295  1.00 20.11  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.474  -11.578 12.315  1.00 19.57  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.470  -10.492 12.613  1.00 17.49  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 11.924  -10.381 13.744  1.00 17.67  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 11.281  -12.772 11.783  1.00 26.13  ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 12.336  -13.274 12.739  1.00 28.92  ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 13.006  -14.538 12.217  1.00 44.15  ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 13.002  -14.674 10.686  1.00 62.87  ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 13.889  -15.750 10.130  1.00 87.89  ? 9   LYS A NZ  1 
ATOM   64   N  N   . HIS A 1 10  ? 11.841  -9.706  11.566  1.00 15.82  ? 10  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 10  ? 12.940  -8.711  11.796  1.00 15.54  ? 10  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 10  ? 12.461  -7.340  12.023  1.00 13.71  ? 10  HIS A C   1 
ATOM   67   O  O   . HIS A 1 10  ? 13.283  -6.459  12.377  1.00 15.43  ? 10  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 10  ? 13.960  -8.735  10.650  1.00 15.49  ? 10  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 10  ? 14.588  -10.090 10.545  1.00 14.91  ? 10  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 10  ? 15.611  -10.504 11.363  1.00 18.33  ? 10  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 10  ? 14.288  -11.087 9.730   1.00 14.52  ? 10  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 10  ? 15.925  -11.757 11.052  1.00 17.55  ? 10  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 10  ? 15.126  -12.131 9.991   1.00 16.74  ? 10  HIS A NE2 1 
ATOM   74   N  N   . ASN A 1 11  ? 11.120  -7.144  11.856  1.00 13.46  ? 11  ASN A N   1 
ATOM   75   C  CA  . ASN A 1 11  ? 10.593  -5.775  12.087  1.00 12.88  ? 11  ASN A CA  1 
ATOM   76   C  C   . ASN A 1 11  ? 9.276   -5.731  12.814  1.00 11.63  ? 11  ASN A C   1 
ATOM   77   O  O   . ASN A 1 11  ? 8.648   -4.685  12.886  1.00 11.38  ? 11  ASN A O   1 
ATOM   78   C  CB  . ASN A 1 11  ? 10.446  -4.992  10.771  1.00 13.79  ? 11  ASN A CB  1 
ATOM   79   C  CG  . ASN A 1 11  ? 9.433   -5.635  9.843   1.00 13.88  ? 11  ASN A CG  1 
ATOM   80   O  OD1 . ASN A 1 11  ? 8.779   -6.644  10.200  1.00 16.27  ? 11  ASN A OD1 1 
ATOM   81   N  ND2 . ASN A 1 11  ? 9.229   -5.026  8.705   1.00 17.49  ? 11  ASN A ND2 1 
ATOM   82   N  N   . GLY A 1 12  ? 8.895   -6.844  13.467  1.00 11.49  ? 12  GLY A N   1 
ATOM   83   C  CA  . GLY A 1 12  ? 7.594   -6.991  14.104  1.00 12.18  ? 12  GLY A CA  1 
ATOM   84   C  C   . GLY A 1 12  ? 7.592   -6.426  15.490  1.00 10.12  ? 12  GLY A C   1 
ATOM   85   O  O   . GLY A 1 12  ? 8.504   -5.745  15.953  1.00 10.13  ? 12  GLY A O   1 
ATOM   86   N  N   . PRO A 1 13  ? 6.489   -6.717  16.195  1.00 10.21  ? 13  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 13  ? 6.229   -6.158  17.523  1.00 9.64   ? 13  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 13  ? 7.394   -6.168  18.491  1.00 9.50   ? 13  PRO A C   1 
ATOM   89   O  O   . PRO A 1 13  ? 7.503   -5.195  19.246  1.00 10.79  ? 13  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 13  ? 5.016   -6.981  18.010  1.00 10.02  ? 13  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 13  ? 4.259   -7.200  16.726  1.00 10.95  ? 13  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 13  ? 5.311   -7.422  15.669  1.00 11.44  ? 13  PRO A CD  1 
ATOM   93   N  N   . GLU A 1 14  ? 8.214   -7.210  18.496  1.00 10.98  ? 14  GLU A N   1 
ATOM   94   C  CA  . GLU A 1 14  ? 9.339   -7.258  19.454  1.00 12.84  ? 14  GLU A CA  1 
ATOM   95   C  C   . GLU A 1 14  ? 10.444  -6.272  19.130  1.00 10.48  ? 14  GLU A C   1 
ATOM   96   O  O   . GLU A 1 14  ? 11.311  -6.055  19.977  1.00 12.35  ? 14  GLU A O   1 
ATOM   97   C  CB  . GLU A 1 14  ? 9.913   -8.667  19.531  1.00 16.31  ? 14  GLU A CB  1 
ATOM   98   C  CG  . GLU A 1 14  ? 8.889   -9.776  19.913  1.00 22.13  ? 14  GLU A CG  1 
ATOM   99   C  CD  . GLU A 1 14  ? 8.007   -9.350  21.071  1.00 26.62  ? 14  GLU A CD  1 
ATOM   100  O  OE1 . GLU A 1 14  ? 8.556   -8.875  22.085  1.00 39.09  ? 14  GLU A OE1 1 
ATOM   101  O  OE2 . GLU A 1 14  ? 6.774   -9.496  20.968  1.00 28.84  ? 14  GLU A OE2 1 
ATOM   102  N  N   . HIS A 1 15  ? 10.422  -5.682  17.930  1.00 9.62   ? 15  HIS A N   1 
ATOM   103  C  CA  . HIS A 1 15  ? 11.395  -4.699  17.527  1.00 9.59   ? 15  HIS A CA  1 
ATOM   104  C  C   . HIS A 1 15  ? 10.936  -3.286  17.699  1.00 9.38   ? 15  HIS A C   1 
ATOM   105  O  O   . HIS A 1 15  ? 11.773  -2.386  17.594  1.00 10.12  ? 15  HIS A O   1 
ATOM   106  C  CB  . HIS A 1 15  ? 11.725  -4.910  16.035  1.00 9.79   ? 15  HIS A CB  1 
ATOM   107  C  CG  . HIS A 1 15  ? 12.458  -6.154  15.739  1.00 10.76  ? 15  HIS A CG  1 
ATOM   108  N  ND1 . HIS A 1 15  ? 13.860  -6.230  15.833  1.00 12.68  ? 15  HIS A ND1 1 
ATOM   109  C  CD2 . HIS A 1 15  ? 11.971  -7.382  15.424  1.00 12.62  ? 15  HIS A CD2 1 
ATOM   110  C  CE1 . HIS A 1 15  ? 14.231  -7.457  15.553  1.00 15.63  ? 15  HIS A CE1 1 
ATOM   111  N  NE2 . HIS A 1 15  ? 13.122  -8.204  15.264  1.00 14.78  ? 15  HIS A NE2 1 
ATOM   112  N  N   . TRP A 1 16  ? 9.623   -3.042  17.817  1.00 8.64   ? 16  TRP A N   1 
ATOM   113  C  CA  . TRP A 1 16  ? 9.111   -1.690  17.717  1.00 8.91   ? 16  TRP A CA  1 
ATOM   114  C  C   . TRP A 1 16  ? 9.671   -0.733  18.755  1.00 8.50   ? 16  TRP A C   1 
ATOM   115  O  O   . TRP A 1 16  ? 9.780   0.446   18.428  1.00 9.33   ? 16  TRP A O   1 
ATOM   116  C  CB  . TRP A 1 16  ? 7.574   -1.721  17.822  1.00 8.56   ? 16  TRP A CB  1 
ATOM   117  C  CG  . TRP A 1 16  ? 6.909   -2.414  16.676  1.00 8.41   ? 16  TRP A CG  1 
ATOM   118  C  CD1 . TRP A 1 16  ? 7.422   -2.845  15.482  1.00 9.38   ? 16  TRP A CD1 1 
ATOM   119  C  CD2 . TRP A 1 16  ? 5.492   -2.738  16.634  1.00 7.95   ? 16  TRP A CD2 1 
ATOM   120  N  NE1 . TRP A 1 16  ? 6.458   -3.440  14.709  1.00 9.01   ? 16  TRP A NE1 1 
ATOM   121  C  CE2 . TRP A 1 16  ? 5.270   -3.385  15.353  1.00 8.58   ? 16  TRP A CE2 1 
ATOM   122  C  CE3 . TRP A 1 16  ? 4.445   -2.560  17.521  1.00 8.47   ? 16  TRP A CE3 1 
ATOM   123  C  CZ2 . TRP A 1 16  ? 3.993   -3.813  14.964  1.00 9.93   ? 16  TRP A CZ2 1 
ATOM   124  C  CZ3 . TRP A 1 16  ? 3.181   -3.013  17.144  1.00 8.74   ? 16  TRP A CZ3 1 
ATOM   125  C  CH2 . TRP A 1 16  ? 2.956   -3.589  15.892  1.00 8.92   ? 16  TRP A CH2 1 
ATOM   126  N  N   . HIS A 1 17  ? 10.039  -1.217  19.911  1.00 8.84   ? 17  HIS A N   1 
ATOM   127  C  CA  . HIS A 1 17  ? 10.536  -0.358  20.959  1.00 9.35   ? 17  HIS A CA  1 
ATOM   128  C  C   . HIS A 1 17  ? 11.819  0.388   20.580  1.00 9.34   ? 17  HIS A C   1 
ATOM   129  O  O   . HIS A 1 17  ? 12.054  1.444   21.138  1.00 10.85  ? 17  HIS A O   1 
ATOM   130  C  CB  . HIS A 1 17  ? 10.800  -1.147  22.261  1.00 10.11  ? 17  HIS A CB  1 
ATOM   131  C  CG  . HIS A 1 17  ? 12.010  -1.988  22.179  1.00 9.75   ? 17  HIS A CG  1 
ATOM   132  N  ND1 . HIS A 1 17  ? 13.222  -1.592  22.703  1.00 11.54  ? 17  HIS A ND1 1 
ATOM   133  C  CD2 . HIS A 1 17  ? 12.211  -3.173  21.578  1.00 11.49  ? 17  HIS A CD2 1 
ATOM   134  C  CE1 . HIS A 1 17  ? 14.103  -2.502  22.441  1.00 12.79  ? 17  HIS A CE1 1 
ATOM   135  N  NE2 . HIS A 1 17  ? 13.558  -3.495  21.770  1.00 12.30  ? 17  HIS A NE2 1 
ATOM   136  N  N   . LYS A 1 18  ? 12.556  -0.117  19.588  1.00 9.83   ? 18  LYS A N   1 
ATOM   137  C  CA  . LYS A 1 18  ? 13.785  0.596   19.144  1.00 10.76  ? 18  LYS A CA  1 
ATOM   138  C  C   . LYS A 1 18  ? 13.473  1.902   18.513  1.00 12.10  ? 18  LYS A C   1 
ATOM   139  O  O   . LYS A 1 18  ? 14.170  2.880   18.731  1.00 18.14  ? 18  LYS A O   1 
ATOM   140  C  CB  . LYS A 1 18  ? 14.612  -0.313  18.298  1.00 11.55  ? 18  LYS A CB  1 
ATOM   141  C  CG  . LYS A 1 18  ? 15.154  -1.508  18.990  1.00 11.99  ? 18  LYS A CG  1 
ATOM   142  C  CD  . LYS A 1 18  ? 15.909  -2.455  18.071  1.00 12.55  ? 18  LYS A CD  1 
ATOM   143  C  CE  . LYS A 1 18  ? 14.965  -3.423  17.473  1.00 12.06  ? 18  LYS A CE  1 
ATOM   144  N  NZ  . LYS A 1 18  ? 15.619  -4.188  16.386  1.00 11.90  ? 18  LYS A NZ  1 
ATOM   145  N  N   . ASP A 1 19  ? 12.428  1.979   17.753  1.00 11.79  ? 19  ASP A N   1 
ATOM   146  C  CA  . ASP A 1 19  ? 12.038  3.218   17.124  1.00 12.52  ? 19  ASP A CA  1 
ATOM   147  C  C   . ASP A 1 19  ? 11.008  3.996   17.950  1.00 11.55  ? 19  ASP A C   1 
ATOM   148  O  O   . ASP A 1 19  ? 10.934  5.189   17.826  1.00 13.41  ? 19  ASP A O   1 
ATOM   149  C  CB  . ASP A 1 19  ? 11.443  3.011   15.757  1.00 14.09  ? 19  ASP A CB  1 
ATOM   150  C  CG  . ASP A 1 19  ? 12.478  2.766   14.672  1.00 22.16  ? 19  ASP A CG  1 
ATOM   151  O  OD1 . ASP A 1 19  ? 13.451  3.589   14.543  1.00 22.34  ? 19  ASP A OD1 1 
ATOM   152  O  OD2 . ASP A 1 19  ? 12.401  1.587   14.128  1.00 32.04  ? 19  ASP A OD2 1 
ATOM   153  N  N   . PHE A 1 20  ? 10.242  3.272   18.795  1.00 9.62   ? 20  PHE A N   1 
ATOM   154  C  CA  . PHE A 1 20  ? 9.146   3.845   19.548  1.00 9.94   ? 20  PHE A CA  1 
ATOM   155  C  C   . PHE A 1 20  ? 9.260   3.339   20.961  1.00 9.66   ? 20  PHE A C   1 
ATOM   156  O  O   . PHE A 1 20  ? 8.594   2.371   21.355  1.00 10.02  ? 20  PHE A O   1 
ATOM   157  C  CB  . PHE A 1 20  ? 7.802   3.462   18.896  1.00 12.68  ? 20  PHE A CB  1 
ATOM   158  C  CG  . PHE A 1 20  ? 7.720   3.854   17.433  1.00 12.92  ? 20  PHE A CG  1 
ATOM   159  C  CD1 . PHE A 1 20  ? 7.461   5.157   17.069  1.00 16.94  ? 20  PHE A CD1 1 
ATOM   160  C  CD2 . PHE A 1 20  ? 8.107   2.899   16.489  1.00 15.33  ? 20  PHE A CD2 1 
ATOM   161  C  CE1 . PHE A 1 20  ? 7.472   5.467   15.653  1.00 16.72  ? 20  PHE A CE1 1 
ATOM   162  C  CE2 . PHE A 1 20  ? 8.152   3.148   15.102  1.00 16.33  ? 20  PHE A CE2 1 
ATOM   163  C  CZ  . PHE A 1 20  ? 7.838   4.446   14.734  1.00 17.96  ? 20  PHE A CZ  1 
ATOM   164  N  N   A PRO A 1 21  ? 10.134  3.940   21.780  0.50 11.26  ? 21  PRO A N   1 
ATOM   165  N  N   B PRO A 1 21  ? 10.067  3.936   21.829  0.50 9.89   ? 21  PRO A N   1 
ATOM   166  C  CA  A PRO A 1 21  ? 10.360  3.575   23.169  0.50 11.07  ? 21  PRO A CA  1 
ATOM   167  C  CA  B PRO A 1 21  ? 10.337  3.240   23.108  0.50 10.64  ? 21  PRO A CA  1 
ATOM   168  C  C   A PRO A 1 21  ? 9.119   3.487   23.941  0.50 9.42   ? 21  PRO A C   1 
ATOM   169  C  C   B PRO A 1 21  ? 9.132   3.152   24.083  0.50 9.10   ? 21  PRO A C   1 
ATOM   170  O  O   A PRO A 1 21  ? 9.123   2.812   24.970  0.50 9.91   ? 21  PRO A O   1 
ATOM   171  O  O   B PRO A 1 21  ? 9.190   2.315   24.997  0.50 8.89   ? 21  PRO A O   1 
ATOM   172  C  CB  A PRO A 1 21  ? 11.312  4.715   23.708  0.50 11.91  ? 21  PRO A CB  1 
ATOM   173  C  CB  B PRO A 1 21  ? 11.502  4.067   23.716  0.50 10.75  ? 21  PRO A CB  1 
ATOM   174  C  CG  A PRO A 1 21  ? 12.149  4.905   22.477  0.50 13.85  ? 21  PRO A CG  1 
ATOM   175  C  CG  B PRO A 1 21  ? 11.362  5.450   23.030  0.50 14.24  ? 21  PRO A CG  1 
ATOM   176  C  CD  A PRO A 1 21  ? 11.220  4.838   21.298  0.50 10.34  ? 21  PRO A CD  1 
ATOM   177  C  CD  B PRO A 1 21  ? 10.873  5.191   21.652  0.50 10.13  ? 21  PRO A CD  1 
ATOM   178  N  N   A ILE A 1 22  ? 8.061   4.179   23.502  0.50 8.10   ? 22  ILE A N   1 
ATOM   179  N  N   B ILE A 1 22  ? 8.085   4.000   23.931  0.50 9.14   ? 22  ILE A N   1 
ATOM   180  C  CA  A ILE A 1 22  ? 6.825   4.026   24.264  0.50 8.51   ? 22  ILE A CA  1 
ATOM   181  C  CA  B ILE A 1 22  ? 6.809   3.836   24.682  0.50 8.52   ? 22  ILE A CA  1 
ATOM   182  C  C   A ILE A 1 22  ? 6.211   2.612   24.260  0.50 8.42   ? 22  ILE A C   1 
ATOM   183  C  C   B ILE A 1 22  ? 6.243   2.434   24.444  0.50 8.89   ? 22  ILE A C   1 
ATOM   184  O  O   A ILE A 1 22  ? 5.300   2.346   25.039  0.50 9.48   ? 22  ILE A O   1 
ATOM   185  O  O   B ILE A 1 22  ? 5.335   2.017   25.181  0.50 8.58   ? 22  ILE A O   1 
ATOM   186  C  CB  A ILE A 1 22  ? 5.804   5.130   23.897  0.50 7.69   ? 22  ILE A CB  1 
ATOM   187  C  CB  B ILE A 1 22  ? 5.792   4.930   24.254  0.50 8.42   ? 22  ILE A CB  1 
ATOM   188  C  CG1 A ILE A 1 22  ? 4.809   5.324   24.984  0.50 9.22   ? 22  ILE A CG1 1 
ATOM   189  C  CG1 B ILE A 1 22  ? 4.717   5.223   25.321  0.50 11.76  ? 22  ILE A CG1 1 
ATOM   190  C  CG2 A ILE A 1 22  ? 5.167   4.794   22.549  0.50 9.11   ? 22  ILE A CG2 1 
ATOM   191  C  CG2 B ILE A 1 22  ? 5.130   4.553   22.918  0.50 9.44   ? 22  ILE A CG2 1 
ATOM   192  C  CD1 A ILE A 1 22  ? 3.874   6.443   24.732  0.50 11.18  ? 22  ILE A CD1 1 
ATOM   193  C  CD1 B ILE A 1 22  ? 5.275   5.744   26.603  0.50 14.93  ? 22  ILE A CD1 1 
ATOM   194  N  N   . ALA A 1 23  ? 6.722   1.698   23.421  1.00 8.89   ? 23  ALA A N   1 
ATOM   195  C  CA  . ALA A 1 23  ? 6.314   0.326   23.327  1.00 9.35   ? 23  ALA A CA  1 
ATOM   196  C  C   . ALA A 1 23  ? 6.433   -0.443  24.637  1.00 9.50   ? 23  ALA A C   1 
ATOM   197  O  O   . ALA A 1 23  ? 5.693   -1.435  24.810  1.00 10.83  ? 23  ALA A O   1 
ATOM   198  C  CB  . ALA A 1 23  ? 7.111   -0.383  22.279  1.00 9.26   ? 23  ALA A CB  1 
ATOM   199  N  N   . LYS A 1 24  ? 7.334   0.011   25.512  1.00 10.44  ? 24  LYS A N   1 
ATOM   200  C  CA  . LYS A 1 24  ? 7.541   -0.532  26.844  1.00 11.25  ? 24  LYS A CA  1 
ATOM   201  C  C   . LYS A 1 24  ? 6.886   0.313   27.897  1.00 11.96  ? 24  LYS A C   1 
ATOM   202  O  O   . LYS A 1 24  ? 7.262   0.178   29.093  1.00 13.32  ? 24  LYS A O   1 
ATOM   203  C  CB  . LYS A 1 24  ? 8.987   -0.791  27.125  1.00 12.18  ? 24  LYS A CB  1 
ATOM   204  C  CG  . LYS A 1 24  ? 9.610   -1.800  26.190  1.00 14.51  ? 24  LYS A CG  1 
ATOM   205  C  CD  . LYS A 1 24  ? 11.070  -1.978  26.556  1.00 18.14  ? 24  LYS A CD  1 
ATOM   206  C  CE  . LYS A 1 24  ? 11.715  -2.992  25.605  1.00 18.93  ? 24  LYS A CE  1 
ATOM   207  N  NZ  . LYS A 1 24  ? 11.358  -4.322  26.136  1.00 25.16  ? 24  LYS A NZ  1 
ATOM   208  N  N   . GLY A 1 25  ? 5.903   1.135   27.536  1.00 11.04  ? 25  GLY A N   1 
ATOM   209  C  CA  . GLY A 1 25  ? 5.292   2.066   28.473  1.00 13.26  ? 25  GLY A CA  1 
ATOM   210  C  C   . GLY A 1 25  ? 4.308   1.397   29.464  1.00 10.72  ? 25  GLY A C   1 
ATOM   211  O  O   . GLY A 1 25  ? 4.119   0.180   29.558  1.00 12.07  ? 25  GLY A O   1 
ATOM   212  N  N   . GLU A 1 26  ? 3.665   2.279   30.189  1.00 11.74  ? 26  GLU A N   1 
ATOM   213  C  CA  . GLU A 1 26  ? 2.784   1.920   31.274  1.00 12.37  ? 26  GLU A CA  1 
ATOM   214  C  C   . GLU A 1 26  ? 1.351   1.645   30.848  1.00 10.69  ? 26  GLU A C   1 
ATOM   215  O  O   . GLU A 1 26  ? 0.596   1.145   31.666  1.00 11.89  ? 26  GLU A O   1 
ATOM   216  C  CB  . GLU A 1 26  ? 2.823   3.043   32.324  1.00 16.21  ? 26  GLU A CB  1 
ATOM   217  C  CG  . GLU A 1 26  ? 4.220   3.249   32.892  1.00 18.07  ? 26  GLU A CG  1 
ATOM   218  C  CD  . GLU A 1 26  ? 4.747   1.989   33.603  1.00 24.04  ? 26  GLU A CD  1 
ATOM   219  O  OE1 . GLU A 1 26  ? 4.035   1.441   34.517  1.00 34.22  ? 26  GLU A OE1 1 
ATOM   220  O  OE2 . GLU A 1 26  ? 5.913   1.561   33.272  1.00 37.04  ? 26  GLU A OE2 1 
ATOM   221  N  N   . ARG A 1 27  ? 0.980   1.988   29.623  1.00 8.83   ? 27  ARG A N   1 
ATOM   222  C  CA  . ARG A 1 27  ? -0.431  1.752   29.259  1.00 8.11   ? 27  ARG A CA  1 
ATOM   223  C  C   . ARG A 1 27  ? -0.510  1.305   27.821  1.00 8.05   ? 27  ARG A C   1 
ATOM   224  O  O   . ARG A 1 27  ? -1.219  1.909   27.003  1.00 8.20   ? 27  ARG A O   1 
ATOM   225  C  CB  . ARG A 1 27  ? -1.328  2.977   29.572  1.00 10.28  ? 27  ARG A CB  1 
ATOM   226  C  CG  . ARG A 1 27  ? -0.938  4.279   29.016  1.00 12.55  ? 27  ARG A CG  1 
ATOM   227  C  CD  . ARG A 1 27  ? -1.954  5.434   29.170  1.00 14.50  ? 27  ARG A CD  1 
ATOM   228  N  NE  . ARG A 1 27  ? -3.090  5.349   28.255  1.00 11.91  ? 27  ARG A NE  1 
ATOM   229  C  CZ  . ARG A 1 27  ? -4.050  6.268   28.170  1.00 12.24  ? 27  ARG A CZ  1 
ATOM   230  N  NH1 . ARG A 1 27  ? -4.015  7.344   28.944  1.00 15.24  ? 27  ARG A NH1 1 
ATOM   231  N  NH2 . ARG A 1 27  ? -5.050  6.112   27.311  1.00 13.57  ? 27  ARG A NH2 1 
ATOM   232  N  N   . GLN A 1 28  ? 0.219   0.235   27.510  1.00 7.36   ? 28  GLN A N   1 
ATOM   233  C  CA  . GLN A 1 28  ? 0.230   -0.276  26.173  1.00 7.31   ? 28  GLN A CA  1 
ATOM   234  C  C   . GLN A 1 28  ? -0.922  -1.267  25.884  1.00 7.29   ? 28  GLN A C   1 
ATOM   235  O  O   . GLN A 1 28  ? -1.400  -1.939  26.795  1.00 7.93   ? 28  GLN A O   1 
ATOM   236  C  CB  . GLN A 1 28  ? 1.610   -0.937  25.890  1.00 7.91   ? 28  GLN A CB  1 
ATOM   237  C  CG  . GLN A 1 28  ? 2.734   0.070   25.818  1.00 8.55   ? 28  GLN A CG  1 
ATOM   238  C  CD  . GLN A 1 28  ? 2.599   0.895   24.539  1.00 7.81   ? 28  GLN A CD  1 
ATOM   239  O  OE1 . GLN A 1 28  ? 2.773   0.357   23.437  1.00 8.16   ? 28  GLN A OE1 1 
ATOM   240  N  NE2 . GLN A 1 28  ? 2.230   2.190   24.658  1.00 8.26   ? 28  GLN A NE2 1 
ATOM   241  N  N   . SER A 1 29  ? -1.287  -1.336  24.625  1.00 6.51   ? 29  SER A N   1 
ATOM   242  C  CA  . SER A 1 29  ? -2.346  -2.209  24.157  1.00 6.18   ? 29  SER A CA  1 
ATOM   243  C  C   . SER A 1 29  ? -1.830  -3.068  23.048  1.00 5.84   ? 29  SER A C   1 
ATOM   244  O  O   . SER A 1 29  ? -0.876  -2.726  22.353  1.00 7.05   ? 29  SER A O   1 
ATOM   245  C  CB  . SER A 1 29  ? -3.501  -1.331  23.608  1.00 7.09   ? 29  SER A CB  1 
ATOM   246  O  OG  . SER A 1 29  ? -4.089  -0.602  24.686  1.00 7.25   ? 29  SER A OG  1 
ATOM   247  N  N   . PRO A 1 30  ? -2.487  -4.195  22.775  1.00 6.38   ? 30  PRO A N   1 
ATOM   248  C  CA  . PRO A 1 30  ? -3.659  -4.746  23.495  1.00 6.86   ? 30  PRO A CA  1 
ATOM   249  C  C   . PRO A 1 30  ? -3.231  -5.397  24.811  1.00 6.60   ? 30  PRO A C   1 
ATOM   250  O  O   . PRO A 1 30  ? -2.054  -5.429  25.147  1.00 6.95   ? 30  PRO A O   1 
ATOM   251  C  CB  . PRO A 1 30  ? -4.188  -5.769  22.495  1.00 6.53   ? 30  PRO A CB  1 
ATOM   252  C  CG  . PRO A 1 30  ? -2.908  -6.344  21.906  1.00 6.78   ? 30  PRO A CG  1 
ATOM   253  C  CD  . PRO A 1 30  ? -2.025  -5.126  21.704  1.00 6.94   ? 30  PRO A CD  1 
ATOM   254  N  N   . VAL A 1 31  ? -4.222  -5.965  25.484  1.00 7.29   ? 31  VAL A N   1 
ATOM   255  C  CA  . VAL A 1 31  ? -4.016  -6.712  26.718  1.00 7.34   ? 31  VAL A CA  1 
ATOM   256  C  C   . VAL A 1 31  ? -4.886  -7.929  26.668  1.00 7.35   ? 31  VAL A C   1 
ATOM   257  O  O   . VAL A 1 31  ? -5.888  -7.997  25.926  1.00 7.69   ? 31  VAL A O   1 
ATOM   258  C  CB  . VAL A 1 31  ? -4.356  -5.869  27.968  1.00 7.74   ? 31  VAL A CB  1 
ATOM   259  C  CG1 . VAL A 1 31  ? -3.423  -4.663  28.058  1.00 8.91   ? 31  VAL A CG1 1 
ATOM   260  C  CG2 . VAL A 1 31  ? -5.842  -5.436  28.022  1.00 8.67   ? 31  VAL A CG2 1 
ATOM   261  N  N   . ASP A 1 32  ? -4.567  -8.899  27.527  1.00 7.53   ? 32  ASP A N   1 
ATOM   262  C  CA  . ASP A 1 32  ? -5.478  -9.984  27.831  1.00 8.04   ? 32  ASP A CA  1 
ATOM   263  C  C   . ASP A 1 32  ? -6.528  -9.475  28.813  1.00 7.79   ? 32  ASP A C   1 
ATOM   264  O  O   . ASP A 1 32  ? -6.212  -8.827  29.815  1.00 9.56   ? 32  ASP A O   1 
ATOM   265  C  CB  . ASP A 1 32  ? -4.747  -11.160 28.438  1.00 9.12   ? 32  ASP A CB  1 
ATOM   266  C  CG  . ASP A 1 32  ? -5.684  -12.328 28.742  1.00 9.27   ? 32  ASP A CG  1 
ATOM   267  O  OD1 . ASP A 1 32  ? -6.371  -12.786 27.817  1.00 9.44   ? 32  ASP A OD1 1 
ATOM   268  O  OD2 . ASP A 1 32  ? -5.711  -12.751 29.929  1.00 12.48  ? 32  ASP A OD2 1 
ATOM   269  N  N   . ILE A 1 33  ? -7.767  -9.780  28.525  1.00 7.78   ? 33  ILE A N   1 
ATOM   270  C  CA  . ILE A 1 33  ? -8.889  -9.406  29.387  1.00 8.22   ? 33  ILE A CA  1 
ATOM   271  C  C   . ILE A 1 33  ? -9.198  -10.648 30.211  1.00 8.43   ? 33  ILE A C   1 
ATOM   272  O  O   . ILE A 1 33  ? -9.767  -11.618 29.725  1.00 9.63   ? 33  ILE A O   1 
ATOM   273  C  CB  . ILE A 1 33  ? -10.105 -8.986  28.547  1.00 8.60   ? 33  ILE A CB  1 
ATOM   274  C  CG1 . ILE A 1 33  ? -9.729  -7.757  27.732  1.00 9.36   ? 33  ILE A CG1 1 
ATOM   275  C  CG2 . ILE A 1 33  ? -11.313 -8.722  29.432  1.00 10.66  ? 33  ILE A CG2 1 
ATOM   276  C  CD1 . ILE A 1 33  ? -10.760 -7.490  26.578  1.00 10.88  ? 33  ILE A CD1 1 
ATOM   277  N  N   A ASP A 1 34  ? -8.800  -10.569 31.481  0.50 10.15  ? 34  ASP A N   1 
ATOM   278  N  N   B ASP A 1 34  ? -8.908  -10.629 31.494  0.50 9.15   ? 34  ASP A N   1 
ATOM   279  C  CA  A ASP A 1 34  ? -9.123  -11.561 32.500  0.50 9.95   ? 34  ASP A CA  1 
ATOM   280  C  CA  B ASP A 1 34  ? -9.159  -11.781 32.349  0.50 10.35  ? 34  ASP A CA  1 
ATOM   281  C  C   A ASP A 1 34  ? -10.612 -11.349 32.955  0.50 12.75  ? 34  ASP A C   1 
ATOM   282  C  C   B ASP A 1 34  ? -10.492 -11.424 32.919  0.50 11.70  ? 34  ASP A C   1 
ATOM   283  O  O   A ASP A 1 34  ? -10.990 -10.424 33.716  0.50 13.45  ? 34  ASP A O   1 
ATOM   284  O  O   B ASP A 1 34  ? -10.591 -10.432 33.745  0.50 12.33  ? 34  ASP A O   1 
ATOM   285  C  CB  A ASP A 1 34  ? -8.100  -11.529 33.623  0.50 11.60  ? 34  ASP A CB  1 
ATOM   286  C  CB  B ASP A 1 34  ? -8.144  -11.809 33.439  0.50 12.54  ? 34  ASP A CB  1 
ATOM   287  C  CG  A ASP A 1 34  ? -8.406  -12.583 34.709  0.50 11.10  ? 34  ASP A CG  1 
ATOM   288  C  CG  B ASP A 1 34  ? -8.286  -13.058 34.310  0.50 15.05  ? 34  ASP A CG  1 
ATOM   289  O  OD1 A ASP A 1 34  ? -7.524  -12.884 35.502  0.50 19.18  ? 34  ASP A OD1 1 
ATOM   290  O  OD1 B ASP A 1 34  ? -7.843  -14.147 33.838  0.50 17.71  ? 34  ASP A OD1 1 
ATOM   291  O  OD2 A ASP A 1 34  ? -9.558  -13.051 34.805  0.50 15.11  ? 34  ASP A OD2 1 
ATOM   292  O  OD2 B ASP A 1 34  ? -8.879  -12.895 35.375  0.50 14.85  ? 34  ASP A OD2 1 
ATOM   293  N  N   . THR A 1 35  ? -11.499 -12.180 32.481  1.00 11.68  ? 35  THR A N   1 
ATOM   294  C  CA  . THR A 1 35  ? -12.922 -11.870 32.720  1.00 13.49  ? 35  THR A CA  1 
ATOM   295  C  C   . THR A 1 35  ? -13.289 -11.955 34.147  1.00 13.34  ? 35  THR A C   1 
ATOM   296  O  O   . THR A 1 35  ? -14.179 -11.277 34.556  1.00 15.01  ? 35  THR A O   1 
ATOM   297  C  CB  . THR A 1 35  ? -13.793 -12.777 31.916  1.00 14.49  ? 35  THR A CB  1 
ATOM   298  O  OG1 . THR A 1 35  ? -13.672 -14.113 32.379  1.00 14.83  ? 35  THR A OG1 1 
ATOM   299  C  CG2 . THR A 1 35  ? -13.544 -12.666 30.403  1.00 15.91  ? 35  THR A CG2 1 
ATOM   300  N  N   . HIS A 1 36  ? -12.596 -12.823 34.910  1.00 14.70  ? 36  HIS A N   1 
ATOM   301  C  CA  . HIS A 1 36  ? -12.877 -13.009 36.295  1.00 15.44  ? 36  HIS A CA  1 
ATOM   302  C  C   . HIS A 1 36  ? -12.378 -11.889 37.108  1.00 18.00  ? 36  HIS A C   1 
ATOM   303  O  O   . HIS A 1 36  ? -13.014 -11.626 38.160  1.00 21.10  ? 36  HIS A O   1 
ATOM   304  C  CB  . HIS A 1 36  ? -12.405 -14.419 36.714  1.00 18.01  ? 36  HIS A CB  1 
ATOM   305  C  CG  . HIS A 1 36  ? -13.310 -15.507 36.193  1.00 17.77  ? 36  HIS A CG  1 
ATOM   306  N  ND1 . HIS A 1 36  ? -14.584 -15.640 36.605  1.00 23.18  ? 36  HIS A ND1 1 
ATOM   307  C  CD2 . HIS A 1 36  ? -13.109 -16.480 35.217  1.00 20.32  ? 36  HIS A CD2 1 
ATOM   308  C  CE1 . HIS A 1 36  ? -15.161 -16.665 35.953  1.00 23.83  ? 36  HIS A CE1 1 
ATOM   309  N  NE2 . HIS A 1 36  ? -14.258 -17.179 35.104  1.00 25.55  ? 36  HIS A NE2 1 
ATOM   310  N  N   . THR A 1 37  ? -11.293 -11.211 36.699  1.00 17.73  ? 37  THR A N   1 
ATOM   311  C  CA  . THR A 1 37  ? -10.704 -10.095 37.410  1.00 18.84  ? 37  THR A CA  1 
ATOM   312  C  C   . THR A 1 37  ? -11.274 -8.726  37.012  1.00 16.20  ? 37  THR A C   1 
ATOM   313  O  O   . THR A 1 37  ? -11.070 -7.736  37.719  1.00 20.42  ? 37  THR A O   1 
ATOM   314  C  CB  . THR A 1 37  ? -9.172  -10.088 37.144  1.00 26.11  ? 37  THR A CB  1 
ATOM   315  O  OG1 . THR A 1 37  ? -8.680  -11.256 37.714  1.00 31.24  ? 37  THR A OG1 1 
ATOM   316  C  CG2 . THR A 1 37  ? -8.486  -8.972  37.952  1.00 28.41  ? 37  THR A CG2 1 
ATOM   317  N  N   . ALA A 1 38  ? -11.895 -8.607  35.838  1.00 13.82  ? 38  ALA A N   1 
ATOM   318  C  CA  . ALA A 1 38  ? -12.473 -7.337  35.440  1.00 13.73  ? 38  ALA A CA  1 
ATOM   319  C  C   . ALA A 1 38  ? -13.598 -6.980  36.432  1.00 17.11  ? 38  ALA A C   1 
ATOM   320  O  O   . ALA A 1 38  ? -14.283 -7.783  36.948  1.00 24.66  ? 38  ALA A O   1 
ATOM   321  C  CB  . ALA A 1 38  ? -12.947 -7.440  34.024  1.00 14.64  ? 38  ALA A CB  1 
ATOM   322  N  N   . LYS A 1 39  ? -13.575 -5.723  36.854  1.00 16.65  ? 39  LYS A N   1 
ATOM   323  C  CA  . LYS A 1 39  ? -14.482 -5.211  37.834  1.00 18.13  ? 39  LYS A CA  1 
ATOM   324  C  C   . LYS A 1 39  ? -15.759 -4.692  37.125  1.00 15.33  ? 39  LYS A C   1 
ATOM   325  O  O   . LYS A 1 39  ? -15.712 -3.752  36.399  1.00 13.49  ? 39  LYS A O   1 
ATOM   326  C  CB  . LYS A 1 39  ? -13.771 -4.087  38.612  1.00 22.97  ? 39  LYS A CB  1 
ATOM   327  C  CG  . LYS A 1 39  ? -14.550 -3.347  39.649  1.00 24.45  ? 39  LYS A CG  1 
ATOM   328  C  CD  . LYS A 1 39  ? -14.829 -4.181  40.921  1.00 23.58  ? 39  LYS A CD  1 
ATOM   329  C  CE  . LYS A 1 39  ? -15.347 -3.188  41.937  1.00 26.45  ? 39  LYS A CE  1 
ATOM   330  N  NZ  . LYS A 1 39  ? -15.878 -3.915  43.095  1.00 29.92  ? 39  LYS A NZ  1 
ATOM   331  N  N   . TYR A 1 40  ? -16.904 -5.277  37.489  1.00 16.24  ? 40  TYR A N   1 
ATOM   332  C  CA  . TYR A 1 40  ? -18.190 -4.669  37.120  1.00 14.51  ? 40  TYR A CA  1 
ATOM   333  C  C   . TYR A 1 40  ? -18.297 -3.285  37.722  1.00 12.95  ? 40  TYR A C   1 
ATOM   334  O  O   . TYR A 1 40  ? -18.174 -3.128  38.960  1.00 15.45  ? 40  TYR A O   1 
ATOM   335  C  CB  . TYR A 1 40  ? -19.408 -5.560  37.582  1.00 18.85  ? 40  TYR A CB  1 
ATOM   336  C  CG  . TYR A 1 40  ? -20.723 -4.843  37.433  1.00 17.17  ? 40  TYR A CG  1 
ATOM   337  C  CD1 . TYR A 1 40  ? -21.162 -4.436  36.152  1.00 18.20  ? 40  TYR A CD1 1 
ATOM   338  C  CD2 . TYR A 1 40  ? -21.571 -4.601  38.527  1.00 22.02  ? 40  TYR A CD2 1 
ATOM   339  C  CE1 . TYR A 1 40  ? -22.386 -3.708  36.017  1.00 20.37  ? 40  TYR A CE1 1 
ATOM   340  C  CE2 . TYR A 1 40  ? -22.798 -3.947  38.362  1.00 28.33  ? 40  TYR A CE2 1 
ATOM   341  C  CZ  . TYR A 1 40  ? -23.226 -3.513  37.134  1.00 28.44  ? 40  TYR A CZ  1 
ATOM   342  O  OH  . TYR A 1 40  ? -24.441 -2.878  36.942  1.00 30.81  ? 40  TYR A OH  1 
ATOM   343  N  N   . ASP A 1 41  ? -18.559 -2.275  36.919  1.00 13.09  ? 41  ASP A N   1 
ATOM   344  C  CA  . ASP A 1 41  ? -18.692 -0.922  37.357  1.00 15.03  ? 41  ASP A CA  1 
ATOM   345  C  C   . ASP A 1 41  ? -20.057 -0.395  37.100  1.00 14.92  ? 41  ASP A C   1 
ATOM   346  O  O   . ASP A 1 41  ? -20.343 -0.056  35.945  1.00 14.94  ? 41  ASP A O   1 
ATOM   347  C  CB  . ASP A 1 41  ? -17.607 -0.053  36.697  1.00 17.00  ? 41  ASP A CB  1 
ATOM   348  C  CG  . ASP A 1 41  ? -17.597 1.357   37.163  1.00 21.36  ? 41  ASP A CG  1 
ATOM   349  O  OD1 . ASP A 1 41  ? -18.525 1.771   37.917  1.00 21.57  ? 41  ASP A OD1 1 
ATOM   350  O  OD2 . ASP A 1 41  ? -16.644 2.073   36.760  1.00 22.45  ? 41  ASP A OD2 1 
ATOM   351  N  N   . PRO A 1 42  ? -20.934 -0.425  38.117  1.00 18.55  ? 42  PRO A N   1 
ATOM   352  C  CA  . PRO A 1 42  ? -22.297 0.053   37.857  1.00 22.13  ? 42  PRO A CA  1 
ATOM   353  C  C   . PRO A 1 42  ? -22.371 1.553   37.492  1.00 21.97  ? 42  PRO A C   1 
ATOM   354  O  O   . PRO A 1 42  ? -23.441 2.070   37.068  1.00 30.46  ? 42  PRO A O   1 
ATOM   355  C  CB  . PRO A 1 42  ? -23.065 -0.280  39.182  1.00 26.83  ? 42  PRO A CB  1 
ATOM   356  C  CG  . PRO A 1 42  ? -21.985 -0.375  40.241  1.00 32.76  ? 42  PRO A CG  1 
ATOM   357  C  CD  . PRO A 1 42  ? -20.699 -0.810  39.535  1.00 20.83  ? 42  PRO A CD  1 
ATOM   358  N  N   . SER A 1 43  ? -21.288 2.293   37.656  1.00 21.51  ? 43  SER A N   1 
ATOM   359  C  CA  . SER A 1 43  ? -21.267 3.699   37.174  1.00 24.77  ? 43  SER A CA  1 
ATOM   360  C  C   . SER A 1 43  ? -21.120 3.891   35.683  1.00 19.80  ? 43  SER A C   1 
ATOM   361  O  O   . SER A 1 43  ? -21.374 5.025   35.148  1.00 27.36  ? 43  SER A O   1 
ATOM   362  C  CB  . SER A 1 43  ? -20.195 4.524   37.909  1.00 22.32  ? 43  SER A CB  1 
ATOM   363  O  OG  . SER A 1 43  ? -18.874 4.229   37.589  1.00 27.19  ? 43  SER A OG  1 
ATOM   364  N  N   . LEU A 1 44  ? -20.678 2.837   35.025  1.00 18.55  ? 44  LEU A N   1 
ATOM   365  C  CA  . LEU A 1 44  ? -20.414 2.944   33.562  1.00 18.04  ? 44  LEU A CA  1 
ATOM   366  C  C   . LEU A 1 44  ? -21.768 3.047   32.851  1.00 18.82  ? 44  LEU A C   1 
ATOM   367  O  O   . LEU A 1 44  ? -22.747 2.396   33.210  1.00 24.23  ? 44  LEU A O   1 
ATOM   368  C  CB  . LEU A 1 44  ? -19.725 1.740   33.066  1.00 15.04  ? 44  LEU A CB  1 
ATOM   369  C  CG  . LEU A 1 44  ? -18.243 1.660   33.262  1.00 14.73  ? 44  LEU A CG  1 
ATOM   370  C  CD1 . LEU A 1 44  ? -17.717 0.306   32.905  1.00 14.87  ? 44  LEU A CD1 1 
ATOM   371  C  CD2 . LEU A 1 44  ? -17.524 2.753   32.558  1.00 15.35  ? 44  LEU A CD2 1 
ATOM   372  N  N   . LYS A 1 45  ? -21.812 3.883   31.826  1.00 18.36  ? 45  LYS A N   1 
ATOM   373  C  CA  . LYS A 1 45  ? -23.045 4.149   31.025  1.00 17.55  ? 45  LYS A CA  1 
ATOM   374  C  C   . LYS A 1 45  ? -23.102 3.280   29.865  1.00 15.16  ? 45  LYS A C   1 
ATOM   375  O  O   . LYS A 1 45  ? -22.081 2.722   29.440  1.00 15.39  ? 45  LYS A O   1 
ATOM   376  C  CB  . LYS A 1 45  ? -23.061 5.542   30.590  1.00 18.14  ? 45  LYS A CB  1 
ATOM   377  C  CG  . LYS A 1 45  ? -23.159 6.486   31.744  1.00 23.84  ? 45  LYS A CG  1 
ATOM   378  C  CD  . LYS A 1 45  ? -23.054 7.918   31.211  1.00 29.99  ? 45  LYS A CD  1 
ATOM   379  C  CE  . LYS A 1 45  ? -23.101 8.930   32.352  1.00 50.40  ? 45  LYS A CE  1 
ATOM   380  N  NZ  . LYS A 1 45  ? -22.938 10.324  31.835  1.00 65.56  ? 45  LYS A NZ  1 
ATOM   381  N  N   . PRO A 1 46  ? -24.330 3.020   29.351  1.00 14.67  ? 46  PRO A N   1 
ATOM   382  C  CA  . PRO A 1 46  ? -24.395 2.343   28.040  1.00 14.53  ? 46  PRO A CA  1 
ATOM   383  C  C   . PRO A 1 46  ? -23.571 3.119   27.010  1.00 12.04  ? 46  PRO A C   1 
ATOM   384  O  O   . PRO A 1 46  ? -23.544 4.319   27.075  1.00 14.11  ? 46  PRO A O   1 
ATOM   385  C  CB  . PRO A 1 46  ? -25.887 2.319   27.756  1.00 15.90  ? 46  PRO A CB  1 
ATOM   386  C  CG  . PRO A 1 46  ? -26.585 2.499   29.079  1.00 20.24  ? 46  PRO A CG  1 
ATOM   387  C  CD  . PRO A 1 46  ? -25.635 3.405   29.880  1.00 17.92  ? 46  PRO A CD  1 
ATOM   388  N  N   . LEU A 1 47  ? -22.971 2.407   26.076  1.00 13.59  ? 47  LEU A N   1 
ATOM   389  C  CA  . LEU A 1 47  ? -22.284 3.046   25.034  1.00 12.90  ? 47  LEU A CA  1 
ATOM   390  C  C   . LEU A 1 47  ? -23.348 3.638   24.048  1.00 14.12  ? 47  LEU A C   1 
ATOM   391  O  O   . LEU A 1 47  ? -24.305 2.910   23.731  1.00 17.05  ? 47  LEU A O   1 
ATOM   392  C  CB  . LEU A 1 47  ? -21.469 1.980   24.283  1.00 16.10  ? 47  LEU A CB  1 
ATOM   393  C  CG  . LEU A 1 47  ? -20.483 2.410   23.298  1.00 17.75  ? 47  LEU A CG  1 
ATOM   394  C  CD1 . LEU A 1 47  ? -19.458 3.296   24.037  1.00 21.47  ? 47  LEU A CD1 1 
ATOM   395  C  CD2 . LEU A 1 47  ? -19.793 1.216   22.679  1.00 21.04  ? 47  LEU A CD2 1 
ATOM   396  N  N   . SER A 1 48  ? -23.140 4.853   23.580  1.00 12.82  ? 48  SER A N   1 
ATOM   397  C  CA  . SER A 1 48  ? -23.977 5.394   22.540  1.00 12.11  ? 48  SER A CA  1 
ATOM   398  C  C   . SER A 1 48  ? -23.191 5.404   21.241  1.00 12.84  ? 48  SER A C   1 
ATOM   399  O  O   . SER A 1 48  ? -22.193 6.131   21.093  1.00 13.71  ? 48  SER A O   1 
ATOM   400  C  CB  . SER A 1 48  ? -24.346 6.810   22.984  1.00 15.70  ? 48  SER A CB  1 
ATOM   401  O  OG  . SER A 1 48  ? -24.946 7.519   21.928  1.00 19.48  ? 48  SER A OG  1 
ATOM   402  N  N   . VAL A 1 49  ? -23.627 4.611   20.296  1.00 14.13  ? 49  VAL A N   1 
ATOM   403  C  CA  . VAL A 1 49  ? -23.120 4.541   18.986  1.00 15.89  ? 49  VAL A CA  1 
ATOM   404  C  C   . VAL A 1 49  ? -24.089 5.241   18.022  1.00 17.52  ? 49  VAL A C   1 
ATOM   405  O  O   . VAL A 1 49  ? -25.236 4.757   17.876  1.00 20.67  ? 49  VAL A O   1 
ATOM   406  C  CB  . VAL A 1 49  ? -22.907 3.090   18.580  1.00 18.80  ? 49  VAL A CB  1 
ATOM   407  C  CG1 . VAL A 1 49  ? -22.263 3.020   17.199  1.00 23.97  ? 49  VAL A CG1 1 
ATOM   408  C  CG2 . VAL A 1 49  ? -22.079 2.370   19.591  1.00 20.02  ? 49  VAL A CG2 1 
ATOM   409  N  N   . SER A 1 50  ? -23.730 6.362   17.401  1.00 13.73  ? 50  SER A N   1 
ATOM   410  C  CA  . SER A 1 50  ? -24.659 7.098   16.516  1.00 15.53  ? 50  SER A CA  1 
ATOM   411  C  C   . SER A 1 50  ? -24.004 7.166   15.171  1.00 13.25  ? 50  SER A C   1 
ATOM   412  O  O   . SER A 1 50  ? -23.301 8.105   14.863  1.00 14.32  ? 50  SER A O   1 
ATOM   413  C  CB  . SER A 1 50  ? -24.937 8.516   16.979  1.00 21.65  ? 50  SER A CB  1 
ATOM   414  O  OG  . SER A 1 50  ? -25.629 8.413   18.188  1.00 28.09  ? 50  SER A OG  1 
ATOM   415  N  N   . TYR A 1 51  ? -24.241 6.104   14.388  1.00 14.23  ? 51  TYR A N   1 
ATOM   416  C  CA  . TYR A 1 51  ? -23.622 5.989   13.088  1.00 12.99  ? 51  TYR A CA  1 
ATOM   417  C  C   . TYR A 1 51  ? -24.559 6.261   11.874  1.00 13.62  ? 51  TYR A C   1 
ATOM   418  O  O   . TYR A 1 51  ? -24.132 6.115   10.733  1.00 13.53  ? 51  TYR A O   1 
ATOM   419  C  CB  . TYR A 1 51  ? -23.048 4.620   12.914  1.00 13.20  ? 51  TYR A CB  1 
ATOM   420  C  CG  . TYR A 1 51  ? -21.770 4.309   13.724  1.00 10.38  ? 51  TYR A CG  1 
ATOM   421  C  CD1 . TYR A 1 51  ? -21.056 5.276   14.429  1.00 11.70  ? 51  TYR A CD1 1 
ATOM   422  C  CD2 . TYR A 1 51  ? -21.287 2.993   13.764  1.00 10.88  ? 51  TYR A CD2 1 
ATOM   423  C  CE1 . TYR A 1 51  ? -19.839 4.927   15.109  1.00 11.48  ? 51  TYR A CE1 1 
ATOM   424  C  CE2 . TYR A 1 51  ? -20.116 2.657   14.375  1.00 10.79  ? 51  TYR A CE2 1 
ATOM   425  C  CZ  . TYR A 1 51  ? -19.366 3.637   15.064  1.00 10.41  ? 51  TYR A CZ  1 
ATOM   426  O  OH  . TYR A 1 51  ? -18.222 3.269   15.711  1.00 11.03  ? 51  TYR A OH  1 
ATOM   427  N  N   A ASP A 1 52  ? -25.754 6.804   12.221  0.50 16.10  ? 52  ASP A N   1 
ATOM   428  N  N   B ASP A 1 52  ? -25.837 6.641   12.052  0.50 14.40  ? 52  ASP A N   1 
ATOM   429  C  CA  A ASP A 1 52  ? -26.819 7.105   11.282  0.50 17.12  ? 52  ASP A CA  1 
ATOM   430  C  CA  B ASP A 1 52  ? -26.703 6.771   10.867  0.50 13.64  ? 52  ASP A CA  1 
ATOM   431  C  C   A ASP A 1 52  ? -26.462 7.907   10.004  0.50 17.56  ? 52  ASP A C   1 
ATOM   432  C  C   B ASP A 1 52  ? -26.245 7.770   9.751   0.50 12.93  ? 52  ASP A C   1 
ATOM   433  O  O   A ASP A 1 52  ? -26.956 7.577   8.929   0.50 22.12  ? 52  ASP A O   1 
ATOM   434  O  O   B ASP A 1 52  ? -26.565 7.531   8.596   0.50 13.49  ? 52  ASP A O   1 
ATOM   435  C  CB  A ASP A 1 52  ? -28.066 7.621   12.001  0.50 16.63  ? 52  ASP A CB  1 
ATOM   436  C  CB  B ASP A 1 52  ? -28.128 7.035   11.324  0.50 14.49  ? 52  ASP A CB  1 
ATOM   437  C  CG  A ASP A 1 52  ? -27.776 8.371   13.383  0.50 23.54  ? 52  ASP A CG  1 
ATOM   438  C  CG  B ASP A 1 52  ? -28.361 8.477   11.719  0.50 21.21  ? 52  ASP A CG  1 
ATOM   439  O  OD1 A ASP A 1 52  ? -27.103 7.862   14.324  0.50 23.89  ? 52  ASP A OD1 1 
ATOM   440  O  OD1 B ASP A 1 52  ? -29.210 9.129   11.053  0.50 28.07  ? 52  ASP A OD1 1 
ATOM   441  O  OD2 A ASP A 1 52  ? -28.287 9.524   13.541  0.50 36.50  ? 52  ASP A OD2 1 
ATOM   442  O  OD2 B ASP A 1 52  ? -27.738 8.923   12.722  0.50 27.93  ? 52  ASP A OD2 1 
ATOM   443  N  N   . GLN A 1 53  ? -25.525 8.844   10.120  1.00 14.98  ? 53  GLN A N   1 
ATOM   444  C  CA  . GLN A 1 53  ? -25.114 9.791   9.092   1.00 14.83  ? 53  GLN A CA  1 
ATOM   445  C  C   . GLN A 1 53  ? -23.651 9.536   8.667   1.00 11.86  ? 53  GLN A C   1 
ATOM   446  O  O   . GLN A 1 53  ? -23.026 10.402  8.059   1.00 13.31  ? 53  GLN A O   1 
ATOM   447  C  CB  . GLN A 1 53  ? -25.309 11.251  9.573   1.00 14.80  ? 53  GLN A CB  1 
ATOM   448  C  CG  . GLN A 1 53  ? -26.770 11.613  9.828   1.00 18.85  ? 53  GLN A CG  1 
ATOM   449  C  CD  . GLN A 1 53  ? -27.604 11.387  8.592   1.00 19.77  ? 53  GLN A CD  1 
ATOM   450  O  OE1 . GLN A 1 53  ? -28.647 10.703  8.658   1.00 31.65  ? 53  GLN A OE1 1 
ATOM   451  N  NE2 . GLN A 1 53  ? -27.132 11.911  7.427   1.00 16.42  ? 53  GLN A NE2 1 
ATOM   452  N  N   . ALA A 1 54  ? -23.132 8.348   8.952   1.00 11.71  ? 54  ALA A N   1 
ATOM   453  C  CA  . ALA A 1 54  ? -21.737 8.123   8.561   1.00 11.49  ? 54  ALA A CA  1 
ATOM   454  C  C   . ALA A 1 54  ? -21.571 8.295   7.058   1.00 10.89  ? 54  ALA A C   1 
ATOM   455  O  O   . ALA A 1 54  ? -22.418 7.861   6.259   1.00 12.30  ? 54  ALA A O   1 
ATOM   456  C  CB  . ALA A 1 54  ? -21.370 6.723   8.986   1.00 12.34  ? 54  ALA A CB  1 
ATOM   457  N  N   . THR A 1 55  ? -20.404 8.813   6.693   1.00 9.57   ? 55  THR A N   1 
ATOM   458  C  CA  . THR A 1 55  ? -20.044 8.954   5.310   1.00 9.02   ? 55  THR A CA  1 
ATOM   459  C  C   . THR A 1 55  ? -18.693 8.350   5.092   1.00 8.01   ? 55  THR A C   1 
ATOM   460  O  O   . THR A 1 55  ? -17.640 8.934   5.361   1.00 8.98   ? 55  THR A O   1 
ATOM   461  C  CB  . THR A 1 55  ? -19.957 10.500  4.909   1.00 10.49  ? 55  THR A CB  1 
ATOM   462  O  OG1 . THR A 1 55  ? -21.237 11.057  5.007   1.00 12.21  ? 55  THR A OG1 1 
ATOM   463  C  CG2 . THR A 1 55  ? -19.460 10.691  3.503   1.00 12.00  ? 55  THR A CG2 1 
ATOM   464  N  N   . SER A 1 56  ? -18.666 7.101   4.610   1.00 8.05   ? 56  SER A N   1 
ATOM   465  C  CA  . SER A 1 56  ? -17.412 6.469   4.216   1.00 8.11   ? 56  SER A CA  1 
ATOM   466  C  C   . SER A 1 56  ? -16.900 7.176   2.961   1.00 8.11   ? 56  SER A C   1 
ATOM   467  O  O   . SER A 1 56  ? -17.738 7.608   2.127   1.00 9.38   ? 56  SER A O   1 
ATOM   468  C  CB  . SER A 1 56  ? -17.599 4.997   4.058   1.00 8.30   ? 56  SER A CB  1 
ATOM   469  O  OG  . SER A 1 56  ? -18.378 4.645   2.949   1.00 9.26   ? 56  SER A OG  1 
ATOM   470  N  N   . LEU A 1 57  ? -15.590 7.227   2.792   1.00 7.93   ? 57  LEU A N   1 
ATOM   471  C  CA  . LEU A 1 57  ? -14.983 7.879   1.648   1.00 9.46   ? 57  LEU A CA  1 
ATOM   472  C  C   . LEU A 1 57  ? -14.135 6.940   0.827   1.00 8.94   ? 57  LEU A C   1 
ATOM   473  O  O   . LEU A 1 57  ? -14.338 6.895   -0.407  1.00 9.93   ? 57  LEU A O   1 
ATOM   474  C  CB  . LEU A 1 57  ? -14.134 9.093   2.063   1.00 9.44   ? 57  LEU A CB  1 
ATOM   475  C  CG  . LEU A 1 57  ? -14.955 10.262  2.583   1.00 11.20  ? 57  LEU A CG  1 
ATOM   476  C  CD1 . LEU A 1 57  ? -13.979 11.311  3.187   1.00 13.60  ? 57  LEU A CD1 1 
ATOM   477  C  CD2 . LEU A 1 57  ? -15.948 10.836  1.534   1.00 15.34  ? 57  LEU A CD2 1 
ATOM   478  N  N   . ARG A 1 58  ? -13.172 6.247   1.426   1.00 8.69   ? 58  ARG A N   1 
ATOM   479  C  CA  . ARG A 1 58  ? -12.174 5.527   0.678   1.00 8.87   ? 58  ARG A CA  1 
ATOM   480  C  C   . ARG A 1 58  ? -11.734 4.303   1.469   1.00 7.75   ? 58  ARG A C   1 
ATOM   481  O  O   . ARG A 1 58  ? -11.875 4.251   2.676   1.00 9.25   ? 58  ARG A O   1 
ATOM   482  C  CB  . ARG A 1 58  ? -10.961 6.396   0.334   1.00 10.44  ? 58  ARG A CB  1 
ATOM   483  C  CG  . ARG A 1 58  ? -11.296 7.627   -0.532  1.00 12.24  ? 58  ARG A CG  1 
ATOM   484  C  CD  . ARG A 1 58  ? -10.000 8.272   -1.064  1.00 14.71  ? 58  ARG A CD  1 
ATOM   485  N  NE  . ARG A 1 58  ? -9.211  7.351   -1.904  1.00 15.67  ? 58  ARG A NE  1 
ATOM   486  C  CZ  . ARG A 1 58  ? -9.498  7.112   -3.170  1.00 14.37  ? 58  ARG A CZ  1 
ATOM   487  N  NH1 . ARG A 1 58  ? -10.490 7.766   -3.752  1.00 18.55  ? 58  ARG A NH1 1 
ATOM   488  N  NH2 . ARG A 1 58  ? -8.731  6.302   -3.891  1.00 15.17  ? 58  ARG A NH2 1 
ATOM   489  N  N   . ILE A 1 59  ? -11.088 3.371   0.768   1.00 8.27   ? 59  ILE A N   1 
ATOM   490  C  CA  . ILE A 1 59  ? -10.439 2.223   1.365   1.00 7.86   ? 59  ILE A CA  1 
ATOM   491  C  C   . ILE A 1 59  ? -9.024  2.118   0.824   1.00 8.36   ? 59  ILE A C   1 
ATOM   492  O  O   . ILE A 1 59  ? -8.826  2.319   -0.371  1.00 8.96   ? 59  ILE A O   1 
ATOM   493  C  CB  . ILE A 1 59  ? -11.277 0.945   1.080   1.00 8.59   ? 59  ILE A CB  1 
ATOM   494  C  CG1 . ILE A 1 59  ? -10.809 -0.257  1.964   1.00 9.35   ? 59  ILE A CG1 1 
ATOM   495  C  CG2 . ILE A 1 59  ? -11.402 0.596   -0.411  1.00 9.30   ? 59  ILE A CG2 1 
ATOM   496  C  CD1 . ILE A 1 59  ? -11.689 -1.474  1.841   1.00 10.75  ? 59  ILE A CD1 1 
ATOM   497  N  N   A LEU A 1 60  ? -8.037  1.890   1.711   0.50 8.55   ? 60  LEU A N   1 
ATOM   498  N  N   B LEU A 1 60  ? -8.100  1.684   1.656   0.50 9.90   ? 60  LEU A N   1 
ATOM   499  C  CA  A LEU A 1 60  ? -6.590  1.867   1.362   0.50 7.32   ? 60  LEU A CA  1 
ATOM   500  C  CA  B LEU A 1 60  ? -6.746  1.620   1.172   0.50 11.45  ? 60  LEU A CA  1 
ATOM   501  C  C   A LEU A 1 60  ? -5.993  0.545   1.910   0.50 7.85   ? 60  LEU A C   1 
ATOM   502  C  C   B LEU A 1 60  ? -5.965  0.556   1.906   0.50 8.44   ? 60  LEU A C   1 
ATOM   503  O  O   A LEU A 1 60  ? -6.340  0.093   3.014   0.50 10.24  ? 60  LEU A O   1 
ATOM   504  O  O   B LEU A 1 60  ? -6.038  0.396   3.139   0.50 9.15   ? 60  LEU A O   1 
ATOM   505  C  CB  A LEU A 1 60  ? -5.827  3.091   1.920   0.50 7.05   ? 60  LEU A CB  1 
ATOM   506  C  CB  B LEU A 1 60  ? -6.060  2.954   1.402   0.50 11.77  ? 60  LEU A CB  1 
ATOM   507  C  CG  A LEU A 1 60  ? -4.300  3.086   1.769   0.50 7.88   ? 60  LEU A CG  1 
ATOM   508  C  CG  B LEU A 1 60  ? -5.956  3.259   2.879   0.50 12.81  ? 60  LEU A CG  1 
ATOM   509  C  CD1 A LEU A 1 60  ? -3.766  3.124   0.333   0.50 10.18  ? 60  LEU A CD1 1 
ATOM   510  C  CD1 B LEU A 1 60  ? -4.669  2.747   3.468   0.50 19.55  ? 60  LEU A CD1 1 
ATOM   511  C  CD2 A LEU A 1 60  ? -3.731  4.263   2.524   0.50 10.82  ? 60  LEU A CD2 1 
ATOM   512  C  CD2 B LEU A 1 60  ? -5.899  4.768   2.994   0.50 26.88  ? 60  LEU A CD2 1 
ATOM   513  N  N   . ASN A 1 61  ? -5.084  -0.084  1.173   1.00 7.97   ? 61  ASN A N   1 
ATOM   514  C  CA  . ASN A 1 61  ? -4.135  -1.063  1.657   1.00 7.69   ? 61  ASN A CA  1 
ATOM   515  C  C   . ASN A 1 61  ? -2.823  -0.291  1.923   1.00 8.02   ? 61  ASN A C   1 
ATOM   516  O  O   . ASN A 1 61  ? -2.239  0.199   0.961   1.00 9.29   ? 61  ASN A O   1 
ATOM   517  C  CB  . ASN A 1 61  ? -3.942  -2.160  0.677   1.00 8.71   ? 61  ASN A CB  1 
ATOM   518  C  CG  . ASN A 1 61  ? -2.864  -3.152  1.045   1.00 8.40   ? 61  ASN A CG  1 
ATOM   519  O  OD1 . ASN A 1 61  ? -1.994  -2.870  1.890   1.00 9.55   ? 61  ASN A OD1 1 
ATOM   520  N  ND2 . ASN A 1 61  ? -2.912  -4.363  0.449   1.00 9.03   ? 61  ASN A ND2 1 
ATOM   521  N  N   . ASN A 1 62  ? -2.430  -0.133  3.192   1.00 8.43   ? 62  ASN A N   1 
ATOM   522  C  CA  . ASN A 1 62  ? -1.240  0.648   3.507   1.00 9.20   ? 62  ASN A CA  1 
ATOM   523  C  C   . ASN A 1 62  ? -0.036  -0.277  3.759   1.00 9.95   ? 62  ASN A C   1 
ATOM   524  O  O   . ASN A 1 62  ? 1.013   0.230   4.245   1.00 11.82  ? 62  ASN A O   1 
ATOM   525  C  CB  . ASN A 1 62  ? -1.410  1.635   4.606   1.00 10.02  ? 62  ASN A CB  1 
ATOM   526  C  CG  . ASN A 1 62  ? -1.458  1.021   5.930   1.00 11.68  ? 62  ASN A CG  1 
ATOM   527  O  OD1 . ASN A 1 62  ? -1.549  -0.220  6.115   1.00 10.21  ? 62  ASN A OD1 1 
ATOM   528  N  ND2 . ASN A 1 62  ? -1.195  1.894   6.915   1.00 15.67  ? 62  ASN A ND2 1 
ATOM   529  N  N   . GLY A 1 63  ? -0.107  -1.550  3.420   1.00 9.53   ? 63  GLY A N   1 
ATOM   530  C  CA  . GLY A 1 63  ? 0.995   -2.466  3.652   1.00 10.54  ? 63  GLY A CA  1 
ATOM   531  C  C   . GLY A 1 63  ? 1.037   -3.079  5.005   1.00 9.59   ? 63  GLY A C   1 
ATOM   532  O  O   . GLY A 1 63  ? 1.818   -3.985  5.215   1.00 12.79  ? 63  GLY A O   1 
ATOM   533  N  N   . HIS A 1 64  ? 0.157   -2.638  5.902   1.00 9.75   ? 64  HIS A N   1 
ATOM   534  C  CA  . HIS A 1 64  ? 0.043   -3.190  7.243   1.00 10.15  ? 64  HIS A CA  1 
ATOM   535  C  C   . HIS A 1 64  ? -1.335  -3.814  7.426   1.00 9.35   ? 64  HIS A C   1 
ATOM   536  O  O   . HIS A 1 64  ? -1.451  -4.930  7.930   1.00 10.75  ? 64  HIS A O   1 
ATOM   537  C  CB  . HIS A 1 64  ? 0.279   -2.157  8.311   1.00 10.55  ? 64  HIS A CB  1 
ATOM   538  C  CG  . HIS A 1 64  ? 1.644   -1.507  8.213   1.00 11.45  ? 64  HIS A CG  1 
ATOM   539  N  ND1 . HIS A 1 64  ? 2.796   -2.180  8.372   1.00 14.49  ? 64  HIS A ND1 1 
ATOM   540  C  CD2 . HIS A 1 64  ? 1.939   -0.205  8.000   1.00 13.12  ? 64  HIS A CD2 1 
ATOM   541  C  CE1 . HIS A 1 64  ? 3.777   -1.318  8.328   1.00 14.78  ? 64  HIS A CE1 1 
ATOM   542  N  NE2 . HIS A 1 64  ? 3.259   -0.089  8.100   1.00 15.37  ? 64  HIS A NE2 1 
ATOM   543  N  N   . SER A 1 65  ? -2.398  -3.114  7.011   1.00 8.83   ? 65  SER A N   1 
ATOM   544  C  CA  . SER A 1 65  ? -3.754  -3.576  6.999   1.00 8.69   ? 65  SER A CA  1 
ATOM   545  C  C   . SER A 1 65  ? -4.465  -2.832  5.912   1.00 7.91   ? 65  SER A C   1 
ATOM   546  O  O   . SER A 1 65  ? -3.868  -2.155  5.106   1.00 9.30   ? 65  SER A O   1 
ATOM   547  C  CB  . SER A 1 65  ? -4.379  -3.418  8.325   1.00 11.14  ? 65  SER A CB  1 
ATOM   548  O  OG  . SER A 1 65  ? -5.573  -4.262  8.206   1.00 13.54  ? 65  SER A OG  1 
ATOM   549  N  N   . PHE A 1 66  ? -5.801  -2.939  5.890   1.00 8.05   ? 66  PHE A N   1 
ATOM   550  C  CA  . PHE A 1 66  ? -6.581  -1.997  5.097   1.00 8.45   ? 66  PHE A CA  1 
ATOM   551  C  C   . PHE A 1 66  ? -7.438  -1.165  6.001   1.00 8.33   ? 66  PHE A C   1 
ATOM   552  O  O   . PHE A 1 66  ? -7.824  -1.601  7.101   1.00 9.40   ? 66  PHE A O   1 
ATOM   553  C  CB  . PHE A 1 66  ? -7.432  -2.715  4.025   1.00 9.60   ? 66  PHE A CB  1 
ATOM   554  C  CG  . PHE A 1 66  ? -8.588  -3.537  4.519   1.00 8.52   ? 66  PHE A CG  1 
ATOM   555  C  CD1 . PHE A 1 66  ? -9.825  -2.953  4.747   1.00 9.03   ? 66  PHE A CD1 1 
ATOM   556  C  CD2 . PHE A 1 66  ? -8.413  -4.841  4.808   1.00 10.50  ? 66  PHE A CD2 1 
ATOM   557  C  CE1 . PHE A 1 66  ? -10.893 -3.721  5.229   1.00 9.87   ? 66  PHE A CE1 1 
ATOM   558  C  CE2 . PHE A 1 66  ? -9.479  -5.632  5.274   1.00 10.74  ? 66  PHE A CE2 1 
ATOM   559  C  CZ  . PHE A 1 66  ? -10.754 -5.069  5.469   1.00 10.54  ? 66  PHE A CZ  1 
ATOM   560  N  N   A LYS A 1 67  ? -7.570  0.110   5.626   0.50 7.61   ? 67  LYS A N   1 
ATOM   561  N  N   B LYS A 1 67  ? -7.864  -0.053  5.481   0.50 8.46   ? 67  LYS A N   1 
ATOM   562  C  CA  A LYS A 1 67  ? -8.470  1.010   6.378   0.50 8.94   ? 67  LYS A CA  1 
ATOM   563  C  CA  B LYS A 1 67  ? -8.517  0.902   6.305   0.50 9.83   ? 67  LYS A CA  1 
ATOM   564  C  C   A LYS A 1 67  ? -9.499  1.720   5.545   0.50 7.75   ? 67  LYS A C   1 
ATOM   565  C  C   B LYS A 1 67  ? -9.586  1.501   5.448   0.50 7.92   ? 67  LYS A C   1 
ATOM   566  O  O   A LYS A 1 67  ? -9.196  2.303   4.493   0.50 8.17   ? 67  LYS A O   1 
ATOM   567  O  O   B LYS A 1 67  ? -9.388  1.806   4.295   0.50 7.57   ? 67  LYS A O   1 
ATOM   568  C  CB  A LYS A 1 67  ? -7.694  2.100   7.125   0.50 9.63   ? 67  LYS A CB  1 
ATOM   569  C  CB  B LYS A 1 67  ? -7.518  1.980   6.751   0.50 12.05  ? 67  LYS A CB  1 
ATOM   570  C  CG  A LYS A 1 67  ? -6.829  2.934   6.182   0.50 10.18  ? 67  LYS A CG  1 
ATOM   571  C  CG  B LYS A 1 67  ? -8.098  3.017   7.617   0.50 11.70  ? 67  LYS A CG  1 
ATOM   572  C  CD  A LYS A 1 67  ? -6.007  4.022   6.874   0.50 11.66  ? 67  LYS A CD  1 
ATOM   573  C  CD  B LYS A 1 67  ? -7.072  4.149   7.799   0.50 13.93  ? 67  LYS A CD  1 
ATOM   574  C  CE  A LYS A 1 67  ? -4.966  4.735   5.986   0.50 13.94  ? 67  LYS A CE  1 
ATOM   575  C  CE  B LYS A 1 67  ? -5.686  3.887   8.433   0.50 19.53  ? 67  LYS A CE  1 
ATOM   576  N  NZ  A LYS A 1 67  ? -4.613  6.086   6.512   0.50 15.36  ? 67  LYS A NZ  1 
ATOM   577  N  NZ  B LYS A 1 67  ? -4.913  5.162   8.899   0.50 23.62  ? 67  LYS A NZ  1 
ATOM   578  N  N   . VAL A 1 68  ? -10.741 1.706   6.050   1.00 7.33   ? 68  VAL A N   1 
ATOM   579  C  CA  . VAL A 1 68  ? -11.862 2.460   5.478   1.00 7.38   ? 68  VAL A CA  1 
ATOM   580  C  C   . VAL A 1 68  ? -11.924 3.772   6.243   1.00 6.92   ? 68  VAL A C   1 
ATOM   581  O  O   . VAL A 1 68  ? -12.082 3.783   7.454   1.00 7.89   ? 68  VAL A O   1 
ATOM   582  C  CB  . VAL A 1 68  ? -13.182 1.699   5.608   1.00 8.43   ? 68  VAL A CB  1 
ATOM   583  C  CG1 . VAL A 1 68  ? -14.356 2.597   5.175   1.00 10.05  ? 68  VAL A CG1 1 
ATOM   584  C  CG2 . VAL A 1 68  ? -13.150 0.421   4.820   1.00 9.10   ? 68  VAL A CG2 1 
ATOM   585  N  N   . GLU A 1 69  ? -11.769 4.873   5.488   1.00 7.50   ? 69  GLU A N   1 
ATOM   586  C  CA  . GLU A 1 69  ? -11.743 6.195   6.088   1.00 8.06   ? 69  GLU A CA  1 
ATOM   587  C  C   . GLU A 1 69  ? -13.023 6.938   5.823   1.00 7.89   ? 69  GLU A C   1 
ATOM   588  O  O   . GLU A 1 69  ? -13.607 6.788   4.728   1.00 9.40   ? 69  GLU A O   1 
ATOM   589  C  CB  . GLU A 1 69  ? -10.508 6.963   5.650   1.00 10.22  ? 69  GLU A CB  1 
ATOM   590  C  CG  . GLU A 1 69  ? -9.227  6.259   6.092   1.00 11.83  ? 69  GLU A CG  1 
ATOM   591  C  CD  . GLU A 1 69  ? -7.970  7.038   5.847   1.00 13.12  ? 69  GLU A CD  1 
ATOM   592  O  OE1 . GLU A 1 69  ? -7.355  6.935   4.777   1.00 14.24  ? 69  GLU A OE1 1 
ATOM   593  O  OE2 . GLU A 1 69  ? -7.573  7.860   6.706   1.00 16.24  ? 69  GLU A OE2 1 
ATOM   594  N  N   . PHE A 1 70  ? -13.447 7.730   6.801   1.00 7.70   ? 70  PHE A N   1 
ATOM   595  C  CA  . PHE A 1 70  ? -14.707 8.442   6.795   1.00 7.87   ? 70  PHE A CA  1 
ATOM   596  C  C   . PHE A 1 70  ? -14.539 9.925   6.715   1.00 8.57   ? 70  PHE A C   1 
ATOM   597  O  O   . PHE A 1 70  ? -13.466 10.488  7.075   1.00 9.81   ? 70  PHE A O   1 
ATOM   598  C  CB  . PHE A 1 70  ? -15.499 8.132   8.083   1.00 8.09   ? 70  PHE A CB  1 
ATOM   599  C  CG  . PHE A 1 70  ? -16.045 6.725   8.106   1.00 8.04   ? 70  PHE A CG  1 
ATOM   600  C  CD1 . PHE A 1 70  ? -15.213 5.615   8.318   1.00 8.92   ? 70  PHE A CD1 1 
ATOM   601  C  CD2 . PHE A 1 70  ? -17.366 6.498   7.815   1.00 8.23   ? 70  PHE A CD2 1 
ATOM   602  C  CE1 . PHE A 1 70  ? -15.701 4.335   8.252   1.00 9.87   ? 70  PHE A CE1 1 
ATOM   603  C  CE2 . PHE A 1 70  ? -17.883 5.161   7.744   1.00 9.40   ? 70  PHE A CE2 1 
ATOM   604  C  CZ  . PHE A 1 70  ? -17.042 4.112   7.986   1.00 9.08   ? 70  PHE A CZ  1 
ATOM   605  N  N   A ASP A 1 71  ? -15.626 10.615  6.381   0.50 7.84   ? 71  ASP A N   1 
ATOM   606  N  N   B ASP A 1 71  ? -15.506 10.682  6.176   0.50 9.21   ? 71  ASP A N   1 
ATOM   607  C  CA  A ASP A 1 71  ? -15.647 12.048  6.511   0.50 7.37   ? 71  ASP A CA  1 
ATOM   608  C  CA  B ASP A 1 71  ? -15.647 12.181  6.343   0.50 10.78  ? 71  ASP A CA  1 
ATOM   609  C  C   A ASP A 1 71  ? -15.920 12.379  7.994   0.50 8.28   ? 71  ASP A C   1 
ATOM   610  C  C   B ASP A 1 71  ? -15.908 12.496  7.786   0.50 10.02  ? 71  ASP A C   1 
ATOM   611  O  O   A ASP A 1 71  ? -16.945 12.070  8.591   0.50 8.37   ? 71  ASP A O   1 
ATOM   612  O  O   B ASP A 1 71  ? -17.104 12.461  8.099   0.50 11.83  ? 71  ASP A O   1 
ATOM   613  C  CB  A ASP A 1 71  ? -16.607 12.696  5.445   0.50 7.88   ? 71  ASP A CB  1 
ATOM   614  C  CB  B ASP A 1 71  ? -17.043 12.526  5.712   0.50 11.58  ? 71  ASP A CB  1 
ATOM   615  C  CG  A ASP A 1 71  ? -16.821 14.185  5.677   0.50 9.01   ? 71  ASP A CG  1 
ATOM   616  C  CG  B ASP A 1 71  ? -17.386 14.041  5.477   0.50 20.51  ? 71  ASP A CG  1 
ATOM   617  O  OD1 A ASP A 1 71  ? -16.114 14.808  6.416   0.50 8.41   ? 71  ASP A OD1 1 
ATOM   618  O  OD1 B ASP A 1 71  ? -18.309 14.523  6.155   0.50 23.16  ? 71  ASP A OD1 1 
ATOM   619  O  OD2 A ASP A 1 71  ? -17.951 14.660  5.286   0.50 12.25  ? 71  ASP A OD2 1 
ATOM   620  O  OD2 B ASP A 1 71  ? -17.119 14.689  4.454   0.50 14.72  ? 71  ASP A OD2 1 
ATOM   621  N  N   . ASP A 1 72  ? -14.884 12.930  8.570   1.00 9.28   ? 72  ASP A N   1 
ATOM   622  C  CA  . ASP A 1 72  ? -14.974 13.313  9.968   1.00 9.04   ? 72  ASP A CA  1 
ATOM   623  C  C   . ASP A 1 72  ? -14.847 14.824  10.124  1.00 9.83   ? 72  ASP A C   1 
ATOM   624  O  O   . ASP A 1 72  ? -14.403 15.291  11.185  1.00 12.51  ? 72  ASP A O   1 
ATOM   625  C  CB  . ASP A 1 72  ? -13.907 12.609  10.827  1.00 10.19  ? 72  ASP A CB  1 
ATOM   626  C  CG  . ASP A 1 72  ? -12.498 12.814  10.384  1.00 11.11  ? 72  ASP A CG  1 
ATOM   627  O  OD1 . ASP A 1 72  ? -12.283 13.639  9.474   1.00 12.61  ? 72  ASP A OD1 1 
ATOM   628  O  OD2 . ASP A 1 72  ? -11.609 12.209  11.004  1.00 12.77  ? 72  ASP A OD2 1 
ATOM   629  N  N   . SER A 1 73  ? -15.275 15.557  9.115   1.00 12.11  ? 73  SER A N   1 
ATOM   630  C  CA  . SER A 1 73  ? -15.172 17.001  9.151   1.00 14.29  ? 73  SER A CA  1 
ATOM   631  C  C   . SER A 1 73  ? -16.394 17.644  9.783   1.00 16.03  ? 73  SER A C   1 
ATOM   632  O  O   . SER A 1 73  ? -16.463 18.892  9.901   1.00 17.99  ? 73  SER A O   1 
ATOM   633  C  CB  . SER A 1 73  ? -14.955 17.518  7.766   1.00 14.98  ? 73  SER A CB  1 
ATOM   634  O  OG  . SER A 1 73  ? -16.162 17.424  7.013   1.00 14.08  ? 73  SER A OG  1 
ATOM   635  N  N   . GLN A 1 74  ? -17.354 16.872  10.260  1.00 15.08  ? 74  GLN A N   1 
ATOM   636  C  CA  . GLN A 1 74  ? -18.450 17.301  11.042  1.00 18.20  ? 74  GLN A CA  1 
ATOM   637  C  C   . GLN A 1 74  ? -18.985 16.112  11.860  1.00 16.89  ? 74  GLN A C   1 
ATOM   638  O  O   . GLN A 1 74  ? -18.557 15.004  11.668  1.00 16.02  ? 74  GLN A O   1 
ATOM   639  C  CB  . GLN A 1 74  ? -19.463 17.962  10.134  1.00 23.35  ? 74  GLN A CB  1 
ATOM   640  C  CG  . GLN A 1 74  ? -20.177 17.040  9.245   1.00 23.02  ? 74  GLN A CG  1 
ATOM   641  C  CD  . GLN A 1 74  ? -21.255 17.876  8.498   1.00 31.84  ? 74  GLN A CD  1 
ATOM   642  O  OE1 . GLN A 1 74  ? -22.011 18.640  9.146   1.00 36.30  ? 74  GLN A OE1 1 
ATOM   643  N  NE2 . GLN A 1 74  ? -21.369 17.738  7.162   1.00 24.72  ? 74  GLN A NE2 1 
ATOM   644  N  N   A ASP A 1 75  ? -19.670 16.231  12.998  0.50 14.30  ? 75  ASP A N   1 
ATOM   645  N  N   B ASP A 1 75  ? -20.099 16.502  12.494  0.50 19.75  ? 75  ASP A N   1 
ATOM   646  C  CA  A ASP A 1 75  ? -20.233 15.083  13.692  0.50 14.19  ? 75  ASP A CA  1 
ATOM   647  C  CA  B ASP A 1 75  ? -20.723 15.856  13.630  0.50 22.16  ? 75  ASP A CA  1 
ATOM   648  C  C   A ASP A 1 75  ? -21.227 14.455  12.689  0.50 15.34  ? 75  ASP A C   1 
ATOM   649  C  C   B ASP A 1 75  ? -21.584 14.650  13.291  0.50 18.87  ? 75  ASP A C   1 
ATOM   650  O  O   A ASP A 1 75  ? -22.236 15.099  12.278  0.50 17.29  ? 75  ASP A O   1 
ATOM   651  O  O   B ASP A 1 75  ? -22.768 14.621  13.599  0.50 35.99  ? 75  ASP A O   1 
ATOM   652  C  CB  A ASP A 1 75  ? -20.928 15.678  14.909  0.50 15.68  ? 75  ASP A CB  1 
ATOM   653  C  CB  B ASP A 1 75  ? -21.592 16.862  14.342  0.50 21.55  ? 75  ASP A CB  1 
ATOM   654  C  CG  A ASP A 1 75  ? -19.970 16.333  15.920  0.50 14.48  ? 75  ASP A CG  1 
ATOM   655  C  CG  B ASP A 1 75  ? -22.318 16.236  15.463  0.50 23.52  ? 75  ASP A CG  1 
ATOM   656  O  OD1 A ASP A 1 75  ? -18.738 16.351  15.735  0.50 15.02  ? 75  ASP A OD1 1 
ATOM   657  O  OD1 B ASP A 1 75  ? -21.939 15.070  15.761  0.50 20.72  ? 75  ASP A OD1 1 
ATOM   658  O  OD2 A ASP A 1 75  ? -20.506 16.787  16.962  0.50 20.95  ? 75  ASP A OD2 1 
ATOM   659  O  OD2 B ASP A 1 75  ? -23.279 16.884  15.987  0.50 32.59  ? 75  ASP A OD2 1 
ATOM   660  N  N   A LYS A 1 76  ? -20.863 13.250  12.214  0.50 14.45  ? 76  LYS A N   1 
ATOM   661  N  N   B LYS A 1 76  ? -21.015 13.656  12.668  0.50 15.53  ? 76  LYS A N   1 
ATOM   662  C  CA  A LYS A 1 76  ? -21.704 12.400  11.373  0.50 13.29  ? 76  LYS A CA  1 
ATOM   663  C  CA  B LYS A 1 76  ? -21.870 12.636  12.056  0.50 18.84  ? 76  LYS A CA  1 
ATOM   664  C  C   A LYS A 1 76  ? -21.894 11.024  11.921  0.50 10.94  ? 76  LYS A C   1 
ATOM   665  C  C   B LYS A 1 76  ? -21.832 11.327  12.845  0.50 23.62  ? 76  LYS A C   1 
ATOM   666  O  O   A LYS A 1 76  ? -22.881 10.389  11.698  0.50 15.66  ? 76  LYS A O   1 
ATOM   667  O  O   B LYS A 1 76  ? -22.616 11.117  13.780  0.50 28.00  ? 76  LYS A O   1 
ATOM   668  C  CB  A LYS A 1 76  ? -21.072 12.193  10.001  0.50 13.00  ? 76  LYS A CB  1 
ATOM   669  C  CB  B LYS A 1 76  ? -21.773 12.631  10.474  0.50 18.64  ? 76  LYS A CB  1 
ATOM   670  C  CG  A LYS A 1 76  ? -21.339 13.319  9.036   0.50 14.10  ? 76  LYS A CG  1 
ATOM   671  C  CG  B LYS A 1 76  ? -20.421 12.842  9.779   0.50 16.37  ? 76  LYS A CG  1 
ATOM   672  C  CD  A LYS A 1 76  ? -20.746 13.060  7.689   0.50 13.41  ? 76  LYS A CD  1 
ATOM   673  C  CD  B LYS A 1 76  ? -20.489 12.937  8.255   0.50 16.89  ? 76  LYS A CD  1 
ATOM   674  C  CE  A LYS A 1 76  ? -20.970 14.286  6.828   0.50 17.11  ? 76  LYS A CE  1 
ATOM   675  C  CE  B LYS A 1 76  ? -21.664 13.753  7.775   0.50 16.03  ? 76  LYS A CE  1 
ATOM   676  N  NZ  A LYS A 1 76  ? -20.798 13.878  5.451   0.50 14.70  ? 76  LYS A NZ  1 
ATOM   677  N  NZ  B LYS A 1 76  ? -21.699 13.786  6.277   0.50 15.98  ? 76  LYS A NZ  1 
ATOM   678  N  N   . ALA A 1 77  ? -20.881 10.489  12.528  1.00 19.72  ? 77  ALA A N   1 
ATOM   679  C  CA  . ALA A 1 77  ? -20.770 9.088   13.102  1.00 13.41  ? 77  ALA A CA  1 
ATOM   680  C  C   . ALA A 1 77  ? -19.970 9.295   14.357  1.00 11.87  ? 77  ALA A C   1 
ATOM   681  O  O   . ALA A 1 77  ? -18.791 9.517   14.334  1.00 16.69  ? 77  ALA A O   1 
ATOM   682  C  CB  . ALA A 1 77  ? -19.991 8.298   12.087  1.00 16.41  ? 77  ALA A CB  1 
ATOM   683  N  N   . VAL A 1 78  ? -20.623 9.226   15.469  1.00 11.74  ? 78  VAL A N   1 
ATOM   684  C  CA  . VAL A 1 78  ? -20.019 9.555   16.789  1.00 13.71  ? 78  VAL A CA  1 
ATOM   685  C  C   . VAL A 1 78  ? -20.284 8.498   17.858  1.00 12.65  ? 78  VAL A C   1 
ATOM   686  O  O   . VAL A 1 78  ? -21.340 7.819   17.855  1.00 14.51  ? 78  VAL A O   1 
ATOM   687  C  CB  . VAL A 1 78  ? -20.335 10.960  17.284  1.00 15.62  ? 78  VAL A CB  1 
ATOM   688  C  CG1 . VAL A 1 78  ? -20.041 12.073  16.270  1.00 18.07  ? 78  VAL A CG1 1 
ATOM   689  C  CG2 . VAL A 1 78  ? -21.721 10.936  17.729  1.00 16.64  ? 78  VAL A CG2 1 
ATOM   690  N  N   . LEU A 1 79  ? -19.319 8.366   18.703  1.00 10.76  ? 79  LEU A N   1 
ATOM   691  C  CA  . LEU A 1 79  ? -19.384 7.572   19.898  1.00 11.68  ? 79  LEU A CA  1 
ATOM   692  C  C   . LEU A 1 79  ? -19.381 8.426   21.135  1.00 12.35  ? 79  LEU A C   1 
ATOM   693  O  O   . LEU A 1 79  ? -18.574 9.385   21.212  1.00 14.29  ? 79  LEU A O   1 
ATOM   694  C  CB  . LEU A 1 79  ? -18.135 6.608   19.917  1.00 13.27  ? 79  LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 79  ? -17.995 5.529   20.920  1.00 12.77  ? 79  LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 79  ? -19.016 4.442   20.673  1.00 17.26  ? 79  LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 79  ? -16.604 4.944   20.858  1.00 12.79  ? 79  LEU A CD2 1 
ATOM   698  N  N   . LYS A 1 80  ? -20.242 8.130   22.080  1.00 13.68  ? 80  LYS A N   1 
ATOM   699  C  CA  . LYS A 1 80  ? -20.259 8.796   23.335  1.00 16.20  ? 80  LYS A CA  1 
ATOM   700  C  C   . LYS A 1 80  ? -20.788 7.899   24.402  1.00 13.43  ? 80  LYS A C   1 
ATOM   701  O  O   . LYS A 1 80  ? -21.054 6.717   24.128  1.00 14.69  ? 80  LYS A O   1 
ATOM   702  C  CB  . LYS A 1 80  ? -20.971 10.086  23.300  1.00 18.94  ? 80  LYS A CB  1 
ATOM   703  C  CG  . LYS A 1 80  ? -22.403 9.981   23.135  1.00 22.81  ? 80  LYS A CG  1 
ATOM   704  C  CD  . LYS A 1 80  ? -23.024 11.351  22.821  1.00 34.67  ? 80  LYS A CD  1 
ATOM   705  C  CE  . LYS A 1 80  ? -24.453 11.281  23.349  1.00 45.92  ? 80  LYS A CE  1 
ATOM   706  N  NZ  . LYS A 1 80  ? -25.560 10.932  22.393  1.00 56.85  ? 80  LYS A NZ  1 
ATOM   707  N  N   . GLY A 1 81  ? -20.916 8.428   25.607  1.00 14.91  ? 81  GLY A N   1 
ATOM   708  C  CA  . GLY A 1 81  ? -21.322 7.602   26.701  1.00 14.87  ? 81  GLY A CA  1 
ATOM   709  C  C   . GLY A 1 81  ? -20.333 6.530   27.033  1.00 14.64  ? 81  GLY A C   1 
ATOM   710  O  O   . GLY A 1 81  ? -19.148 6.708   26.857  1.00 13.86  ? 81  GLY A O   1 
ATOM   711  N  N   . GLY A 1 82  ? -20.810 5.441   27.583  1.00 17.57  ? 82  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 82  ? -19.859 4.446   27.986  1.00 18.33  ? 82  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 82  ? -18.984 5.031   29.077  1.00 18.42  ? 82  GLY A C   1 
ATOM   714  O  O   . GLY A 1 82  ? -19.394 5.715   29.986  1.00 24.29  ? 82  GLY A O   1 
ATOM   715  N  N   . PRO A 1 83  ? -17.673 4.821   28.979  1.00 15.68  ? 83  PRO A N   1 
ATOM   716  C  CA  . PRO A 1 83  ? -16.744 5.349   29.944  1.00 16.68  ? 83  PRO A CA  1 
ATOM   717  C  C   . PRO A 1 83  ? -16.328 6.775   29.531  1.00 15.87  ? 83  PRO A C   1 
ATOM   718  O  O   . PRO A 1 83  ? -15.538 7.396   30.219  1.00 19.14  ? 83  PRO A O   1 
ATOM   719  C  CB  . PRO A 1 83  ? -15.461 4.442   29.765  1.00 16.31  ? 83  PRO A CB  1 
ATOM   720  C  CG  . PRO A 1 83  ? -15.502 4.103   28.318  1.00 14.43  ? 83  PRO A CG  1 
ATOM   721  C  CD  . PRO A 1 83  ? -17.005 3.939   28.023  1.00 15.06  ? 83  PRO A CD  1 
ATOM   722  N  N   . LEU A 1 84  ? -16.813 7.304   28.404  1.00 13.01  ? 84  LEU A N   1 
ATOM   723  C  CA  . LEU A 1 84  ? -16.290 8.496   27.769  1.00 12.34  ? 84  LEU A CA  1 
ATOM   724  C  C   . LEU A 1 84  ? -16.953 9.769   28.286  1.00 14.37  ? 84  LEU A C   1 
ATOM   725  O  O   . LEU A 1 84  ? -18.118 9.768   28.654  1.00 17.09  ? 84  LEU A O   1 
ATOM   726  C  CB  . LEU A 1 84  ? -16.545 8.471   26.258  1.00 12.68  ? 84  LEU A CB  1 
ATOM   727  C  CG  . LEU A 1 84  ? -15.995 7.215   25.573  1.00 10.96  ? 84  LEU A CG  1 
ATOM   728  C  CD1 . LEU A 1 84  ? -16.512 7.169   24.160  1.00 13.41  ? 84  LEU A CD1 1 
ATOM   729  C  CD2 . LEU A 1 84  ? -14.452 7.225   25.610  1.00 12.13  ? 84  LEU A CD2 1 
ATOM   730  N  N   . ASP A 1 85  ? -16.195 10.840  28.302  1.00 17.40  ? 85  ASP A N   1 
ATOM   731  C  CA  . ASP A 1 85  ? -16.755 12.217  28.578  1.00 21.83  ? 85  ASP A CA  1 
ATOM   732  C  C   . ASP A 1 85  ? -16.635 12.860  27.221  1.00 25.67  ? 85  ASP A C   1 
ATOM   733  O  O   . ASP A 1 85  ? -15.578 12.780  26.570  1.00 29.71  ? 85  ASP A O   1 
ATOM   734  C  CB  . ASP A 1 85  ? -15.816 12.955  29.523  1.00 34.79  ? 85  ASP A CB  1 
ATOM   735  C  CG  . ASP A 1 85  ? -15.882 12.447  30.958  1.00 60.70  ? 85  ASP A CG  1 
ATOM   736  O  OD1 . ASP A 1 85  ? -16.941 11.863  31.340  1.00 64.37  ? 85  ASP A OD1 1 
ATOM   737  O  OD2 . ASP A 1 85  ? -14.858 12.621  31.691  1.00 59.79  ? 85  ASP A OD2 1 
ATOM   738  N  N   . GLY A 1 86  ? -17.634 13.541  26.757  1.00 25.86  ? 86  GLY A N   1 
ATOM   739  C  CA  . GLY A 1 86  ? -17.514 14.090  25.447  1.00 30.84  ? 86  GLY A CA  1 
ATOM   740  C  C   . GLY A 1 86  ? -17.775 13.194  24.254  1.00 19.94  ? 86  GLY A C   1 
ATOM   741  O  O   . GLY A 1 86  ? -18.321 12.036  24.369  1.00 26.52  ? 86  GLY A O   1 
ATOM   742  N  N   . THR A 1 87  ? -17.622 13.751  23.080  1.00 15.58  ? 87  THR A N   1 
ATOM   743  C  CA  . THR A 1 87  ? -18.078 13.199  21.835  1.00 15.58  ? 87  THR A CA  1 
ATOM   744  C  C   . THR A 1 87  ? -16.851 12.822  20.989  1.00 13.59  ? 87  THR A C   1 
ATOM   745  O  O   . THR A 1 87  ? -15.909 13.634  20.870  1.00 14.29  ? 87  THR A O   1 
ATOM   746  C  CB  . THR A 1 87  ? -18.810 14.358  21.073  1.00 22.48  ? 87  THR A CB  1 
ATOM   747  O  OG1 . THR A 1 87  ? -19.970 14.708  21.785  1.00 33.17  ? 87  THR A OG1 1 
ATOM   748  C  CG2 . THR A 1 87  ? -19.228 13.935  19.617  1.00 23.73  ? 87  THR A CG2 1 
ATOM   749  N  N   . TYR A 1 88  ? -16.853 11.621  20.421  1.00 12.27  ? 88  TYR A N   1 
ATOM   750  C  CA  . TYR A 1 88  ? -15.737 11.146  19.618  1.00 11.03  ? 88  TYR A CA  1 
ATOM   751  C  C   . TYR A 1 88  ? -16.184 10.859  18.170  1.00 10.93  ? 88  TYR A C   1 
ATOM   752  O  O   . TYR A 1 88  ? -17.132 10.029  17.981  1.00 14.00  ? 88  TYR A O   1 
ATOM   753  C  CB  . TYR A 1 88  ? -15.138 9.893   20.267  1.00 11.43  ? 88  TYR A CB  1 
ATOM   754  C  CG  . TYR A 1 88  ? -14.402 10.136  21.586  1.00 10.22  ? 88  TYR A CG  1 
ATOM   755  C  CD1 . TYR A 1 88  ? -15.036 10.548  22.752  1.00 11.74  ? 88  TYR A CD1 1 
ATOM   756  C  CD2 . TYR A 1 88  ? -13.017 9.900   21.656  1.00 9.55   ? 88  TYR A CD2 1 
ATOM   757  C  CE1 . TYR A 1 88  ? -14.360 10.724  23.929  1.00 11.84  ? 88  TYR A CE1 1 
ATOM   758  C  CE2 . TYR A 1 88  ? -12.315 10.062  22.834  1.00 8.82   ? 88  TYR A CE2 1 
ATOM   759  C  CZ  . TYR A 1 88  ? -12.958 10.455  23.965  1.00 10.11  ? 88  TYR A CZ  1 
ATOM   760  O  OH  . TYR A 1 88  ? -12.276 10.561  25.149  1.00 11.28  ? 88  TYR A OH  1 
ATOM   761  N  N   A ARG A 1 89  ? -15.606 11.449  17.184  0.50 10.72  ? 89  ARG A N   1 
ATOM   762  N  N   B ARG A 1 89  ? -15.540 11.426  17.173  0.50 12.33  ? 89  ARG A N   1 
ATOM   763  C  CA  A ARG A 1 89  ? -16.000 11.175  15.866  0.50 10.66  ? 89  ARG A CA  1 
ATOM   764  C  CA  B ARG A 1 89  ? -15.858 11.264  15.764  0.50 11.73  ? 89  ARG A CA  1 
ATOM   765  C  C   A ARG A 1 89  ? -15.250 10.035  15.228  0.50 7.53   ? 89  ARG A C   1 
ATOM   766  C  C   B ARG A 1 89  ? -15.208 10.045  15.184  0.50 8.02   ? 89  ARG A C   1 
ATOM   767  O  O   A ARG A 1 89  ? -14.038 9.896   15.402  0.50 8.07   ? 89  ARG A O   1 
ATOM   768  O  O   B ARG A 1 89  ? -13.993 9.936   15.282  0.50 7.82   ? 89  ARG A O   1 
ATOM   769  C  CB  A ARG A 1 89  ? -15.616 12.388  14.975  0.50 12.58  ? 89  ARG A CB  1 
ATOM   770  C  CB  B ARG A 1 89  ? -15.186 12.433  15.031  0.50 16.93  ? 89  ARG A CB  1 
ATOM   771  C  CG  A ARG A 1 89  ? -16.486 13.647  15.024  0.50 9.40   ? 89  ARG A CG  1 
ATOM   772  C  CG  B ARG A 1 89  ? -15.898 13.667  15.028  0.50 12.16  ? 89  ARG A CG  1 
ATOM   773  C  CD  A ARG A 1 89  ? -15.948 14.753  14.093  0.50 8.61   ? 89  ARG A CD  1 
ATOM   774  C  CD  B ARG A 1 89  ? -16.374 13.942  13.670  0.50 11.02  ? 89  ARG A CD  1 
ATOM   775  N  NE  A ARG A 1 89  ? -16.497 16.083  14.383  0.50 8.69   ? 89  ARG A NE  1 
ATOM   776  N  NE  B ARG A 1 89  ? -17.078 14.916  14.413  0.50 11.01  ? 89  ARG A NE  1 
ATOM   777  C  CZ  A ARG A 1 89  ? -16.050 17.247  13.885  0.50 11.36  ? 89  ARG A CZ  1 
ATOM   778  C  CZ  B ARG A 1 89  ? -16.925 16.225  14.222  0.50 12.49  ? 89  ARG A CZ  1 
ATOM   779  N  NH1 A ARG A 1 89  ? -15.023 17.270  13.048  0.50 11.60  ? 89  ARG A NH1 1 
ATOM   780  N  NH1 B ARG A 1 89  ? -16.048 16.678  13.313  0.50 14.46  ? 89  ARG A NH1 1 
ATOM   781  N  NH2 A ARG A 1 89  ? -16.619 18.387  14.245  0.50 11.86  ? 89  ARG A NH2 1 
ATOM   782  N  NH2 B ARG A 1 89  ? -17.537 17.114  15.005  0.50 13.43  ? 89  ARG A NH2 1 
ATOM   783  N  N   . LEU A 1 90  ? -15.962 9.210   14.471  1.00 8.41   ? 90  LEU A N   1 
ATOM   784  C  CA  . LEU A 1 90  ? -15.388 8.118   13.731  1.00 8.68   ? 90  LEU A CA  1 
ATOM   785  C  C   . LEU A 1 90  ? -14.518 8.604   12.593  1.00 8.20   ? 90  LEU A C   1 
ATOM   786  O  O   . LEU A 1 90  ? -14.999 9.362   11.726  1.00 10.55  ? 90  LEU A O   1 
ATOM   787  C  CB  . LEU A 1 90  ? -16.506 7.230   13.177  1.00 8.71   ? 90  LEU A CB  1 
ATOM   788  C  CG  . LEU A 1 90  ? -16.051 6.024   12.326  1.00 8.50   ? 90  LEU A CG  1 
ATOM   789  C  CD1 . LEU A 1 90  ? -15.325 4.995   13.174  1.00 9.64   ? 90  LEU A CD1 1 
ATOM   790  C  CD2 . LEU A 1 90  ? -17.301 5.393   11.677  1.00 11.03  ? 90  LEU A CD2 1 
ATOM   791  N  N   . THR A 1 91  ? -13.269 8.203   12.517  1.00 8.00   ? 91  THR A N   1 
ATOM   792  C  CA  . THR A 1 91  ? -12.398 8.533   11.389  1.00 8.12   ? 91  THR A CA  1 
ATOM   793  C  C   . THR A 1 91  ? -12.116 7.353   10.489  1.00 7.87   ? 91  THR A C   1 
ATOM   794  O  O   . THR A 1 91  ? -11.978 7.564   9.289   1.00 8.08   ? 91  THR A O   1 
ATOM   795  C  CB  . THR A 1 91  ? -11.128 9.209   11.908  1.00 10.15  ? 91  THR A CB  1 
ATOM   796  O  OG1 . THR A 1 91  ? -10.285 9.544   10.754  1.00 12.56  ? 91  THR A OG1 1 
ATOM   797  C  CG2 . THR A 1 91  ? -10.297 8.366   12.834  1.00 10.07  ? 91  THR A CG2 1 
ATOM   798  N  N   A GLN A 1 92  ? -12.202 6.134   11.051  0.50 6.43   ? 92  GLN A N   1 
ATOM   799  N  N   B GLN A 1 92  ? -11.863 6.149   11.024  0.50 6.13   ? 92  GLN A N   1 
ATOM   800  C  CA  A GLN A 1 92  ? -11.802 5.018   10.208  0.50 6.99   ? 92  GLN A CA  1 
ATOM   801  C  CA  B GLN A 1 92  ? -11.602 4.968   10.213  0.50 6.43   ? 92  GLN A CA  1 
ATOM   802  C  C   A GLN A 1 92  ? -11.997 3.745   10.929  0.50 6.26   ? 92  GLN A C   1 
ATOM   803  C  C   B GLN A 1 92  ? -12.114 3.738   10.948  0.50 6.06   ? 92  GLN A C   1 
ATOM   804  O  O   A GLN A 1 92  ? -11.952 3.733   12.165  0.50 6.06   ? 92  GLN A O   1 
ATOM   805  O  O   B GLN A 1 92  ? -12.419 3.751   12.193  0.50 5.28   ? 92  GLN A O   1 
ATOM   806  C  CB  A GLN A 1 92  ? -10.285 5.087   9.826   0.50 7.49   ? 92  GLN A CB  1 
ATOM   807  C  CB  B GLN A 1 92  ? -10.107 4.775   9.821   0.50 7.82   ? 92  GLN A CB  1 
ATOM   808  C  CG  A GLN A 1 92  ? -9.315  5.224   11.017  0.50 8.29   ? 92  GLN A CG  1 
ATOM   809  C  CG  B GLN A 1 92  ? -9.288  4.508   11.073  0.50 8.88   ? 92  GLN A CG  1 
ATOM   810  C  CD  A GLN A 1 92  ? -8.513  3.961   11.297  0.50 7.71   ? 92  GLN A CD  1 
ATOM   811  C  CD  B GLN A 1 92  ? -7.912  4.060   10.702  0.50 8.71   ? 92  GLN A CD  1 
ATOM   812  O  OE1 A GLN A 1 92  ? -9.033  2.840   11.260  0.50 8.85   ? 92  GLN A OE1 1 
ATOM   813  O  OE1 B GLN A 1 92  ? -7.539  2.888   10.703  0.50 10.22  ? 92  GLN A OE1 1 
ATOM   814  N  NE2 A GLN A 1 92  ? -7.288  4.188   11.703  0.50 12.29  ? 92  GLN A NE2 1 
ATOM   815  N  NE2 B GLN A 1 92  ? -7.149  5.019   10.234  0.50 11.25  ? 92  GLN A NE2 1 
ATOM   816  N  N   . PHE A 1 93  ? -12.153 2.644   10.185  1.00 6.67   ? 93  PHE A N   1 
ATOM   817  C  CA  . PHE A 1 93  ? -12.052 1.320   10.777  1.00 6.94   ? 93  PHE A CA  1 
ATOM   818  C  C   . PHE A 1 93  ? -11.060 0.518   9.996   1.00 5.96   ? 93  PHE A C   1 
ATOM   819  O  O   . PHE A 1 93  ? -10.769 0.752   8.819   1.00 7.00   ? 93  PHE A O   1 
ATOM   820  C  CB  . PHE A 1 93  ? -13.419 0.608   10.959  1.00 7.29   ? 93  PHE A CB  1 
ATOM   821  C  CG  . PHE A 1 93  ? -14.084 0.187   9.692   1.00 7.02   ? 93  PHE A CG  1 
ATOM   822  C  CD1 . PHE A 1 93  ? -13.660 -0.940  8.988   1.00 7.81   ? 93  PHE A CD1 1 
ATOM   823  C  CD2 . PHE A 1 93  ? -15.198 0.889   9.215   1.00 8.02   ? 93  PHE A CD2 1 
ATOM   824  C  CE1 . PHE A 1 93  ? -14.322 -1.331  7.824   1.00 8.53   ? 93  PHE A CE1 1 
ATOM   825  C  CE2 . PHE A 1 93  ? -15.860 0.499   8.070   1.00 8.02   ? 93  PHE A CE2 1 
ATOM   826  C  CZ  . PHE A 1 93  ? -15.435 -0.604  7.353   1.00 8.52   ? 93  PHE A CZ  1 
ATOM   827  N  N   . HIS A 1 94  ? -10.529 -0.518  10.667  1.00 6.58   ? 94  HIS A N   1 
ATOM   828  C  CA  . HIS A 1 94  ? -9.623  -1.464  10.072  1.00 6.38   ? 94  HIS A CA  1 
ATOM   829  C  C   . HIS A 1 94  ? -9.741  -2.755  10.883  1.00 6.12   ? 94  HIS A C   1 
ATOM   830  O  O   . HIS A 1 94  ? -10.358 -2.793  11.940  1.00 6.71   ? 94  HIS A O   1 
ATOM   831  C  CB  . HIS A 1 94  ? -8.166  -0.932  10.072  1.00 6.64   ? 94  HIS A CB  1 
ATOM   832  C  CG  . HIS A 1 94  ? -7.688  -0.677  11.470  1.00 6.82   ? 94  HIS A CG  1 
ATOM   833  N  ND1 . HIS A 1 94  ? -7.863  0.487   12.136  1.00 7.11   ? 94  HIS A ND1 1 
ATOM   834  C  CD2 . HIS A 1 94  ? -7.132  -1.544  12.346  1.00 6.96   ? 94  HIS A CD2 1 
ATOM   835  C  CE1 . HIS A 1 94  ? -7.428  0.332   13.392  1.00 6.98   ? 94  HIS A CE1 1 
ATOM   836  N  NE2 . HIS A 1 94  ? -6.961  -0.900  13.567  1.00 5.95   ? 94  HIS A NE2 1 
ATOM   837  N  N   . PHE A 1 95  ? -9.055  -3.786  10.397  1.00 6.60   ? 95  PHE A N   1 
ATOM   838  C  CA  . PHE A 1 95  ? -9.040  -5.084  11.035  1.00 6.97   ? 95  PHE A CA  1 
ATOM   839  C  C   . PHE A 1 95  ? -7.628  -5.557  11.273  1.00 6.12   ? 95  PHE A C   1 
ATOM   840  O  O   . PHE A 1 95  ? -6.676  -5.116  10.607  1.00 7.30   ? 95  PHE A O   1 
ATOM   841  C  CB  . PHE A 1 95  ? -9.741  -6.142  10.178  1.00 7.21   ? 95  PHE A CB  1 
ATOM   842  C  CG  . PHE A 1 95  ? -11.231 -5.851  9.911   1.00 7.17   ? 95  PHE A CG  1 
ATOM   843  C  CD1 . PHE A 1 95  ? -11.603 -4.977  8.879   1.00 8.38   ? 95  PHE A CD1 1 
ATOM   844  C  CD2 . PHE A 1 95  ? -12.230 -6.531  10.601  1.00 7.97   ? 95  PHE A CD2 1 
ATOM   845  C  CE1 . PHE A 1 95  ? -12.931 -4.775  8.582   1.00 8.82   ? 95  PHE A CE1 1 
ATOM   846  C  CE2 . PHE A 1 95  ? -13.557 -6.327  10.296  1.00 8.21   ? 95  PHE A CE2 1 
ATOM   847  C  CZ  . PHE A 1 95  ? -13.897 -5.449  9.267   1.00 8.74   ? 95  PHE A CZ  1 
ATOM   848  N  N   . HIS A 1 96  ? -7.518  -6.516  12.166  1.00 6.55   ? 96  HIS A N   1 
ATOM   849  C  CA  . HIS A 1 96  ? -6.312  -7.336  12.358  1.00 6.60   ? 96  HIS A CA  1 
ATOM   850  C  C   . HIS A 1 96  ? -6.781  -8.778  12.266  1.00 6.62   ? 96  HIS A C   1 
ATOM   851  O  O   . HIS A 1 96  ? -7.882  -9.109  12.768  1.00 6.99   ? 96  HIS A O   1 
ATOM   852  C  CB  . HIS A 1 96  ? -5.739  -7.098  13.774  1.00 6.95   ? 96  HIS A CB  1 
ATOM   853  C  CG  . HIS A 1 96  ? -5.440  -5.655  14.060  1.00 6.40   ? 96  HIS A CG  1 
ATOM   854  N  ND1 . HIS A 1 96  ? -4.203  -5.129  13.871  1.00 7.04   ? 96  HIS A ND1 1 
ATOM   855  C  CD2 . HIS A 1 96  ? -6.230  -4.632  14.477  1.00 6.78   ? 96  HIS A CD2 1 
ATOM   856  C  CE1 . HIS A 1 96  ? -4.216  -3.821  14.202  1.00 6.86   ? 96  HIS A CE1 1 
ATOM   857  N  NE2 . HIS A 1 96  ? -5.468  -3.483  14.555  1.00 6.18   ? 96  HIS A NE2 1 
ATOM   858  N  N   . TRP A 1 97  ? -5.997  -9.645  11.623  1.00 6.32   ? 97  TRP A N   1 
ATOM   859  C  CA  . TRP A 1 97  ? -6.441  -11.026 11.440  1.00 7.07   ? 97  TRP A CA  1 
ATOM   860  C  C   . TRP A 1 97  ? -5.231  -11.948 11.364  1.00 6.65   ? 97  TRP A C   1 
ATOM   861  O  O   . TRP A 1 97  ? -4.050  -11.506 11.274  1.00 7.14   ? 97  TRP A O   1 
ATOM   862  C  CB  . TRP A 1 97  ? -7.339  -11.156 10.216  1.00 6.95   ? 97  TRP A CB  1 
ATOM   863  C  CG  . TRP A 1 97  ? -6.678  -10.827 8.937   1.00 6.89   ? 97  TRP A CG  1 
ATOM   864  C  CD1 . TRP A 1 97  ? -5.971  -11.688 8.120   1.00 7.99   ? 97  TRP A CD1 1 
ATOM   865  C  CD2 . TRP A 1 97  ? -6.593  -9.539  8.315   1.00 6.69   ? 97  TRP A CD2 1 
ATOM   866  N  NE1 . TRP A 1 97  ? -5.484  -10.993 7.016   1.00 7.97   ? 97  TRP A NE1 1 
ATOM   867  C  CE2 . TRP A 1 97  ? -5.863  -9.682  7.117   1.00 7.16   ? 97  TRP A CE2 1 
ATOM   868  C  CE3 . TRP A 1 97  ? -7.093  -8.282  8.652   1.00 7.08   ? 97  TRP A CE3 1 
ATOM   869  C  CZ2 . TRP A 1 97  ? -5.628  -8.616  6.272   1.00 7.95   ? 97  TRP A CZ2 1 
ATOM   870  C  CZ3 . TRP A 1 97  ? -6.878  -7.218  7.772   1.00 7.96   ? 97  TRP A CZ3 1 
ATOM   871  C  CH2 . TRP A 1 97  ? -6.134  -7.393  6.614   1.00 7.88   ? 97  TRP A CH2 1 
ATOM   872  N  N   . GLY A 1 98  ? -5.511  -13.235 11.390  1.00 7.06   ? 98  GLY A N   1 
ATOM   873  C  CA  . GLY A 1 98  ? -4.497  -14.243 11.446  1.00 7.61   ? 98  GLY A CA  1 
ATOM   874  C  C   . GLY A 1 98  ? -4.329  -15.006 10.160  1.00 7.86   ? 98  GLY A C   1 
ATOM   875  O  O   . GLY A 1 98  ? -5.065  -14.886 9.192   1.00 8.64   ? 98  GLY A O   1 
ATOM   876  N  N   . SER A 1 99  ? -3.314  -15.890 10.191  1.00 8.57   ? 99  SER A N   1 
ATOM   877  C  CA  . SER A 1 99  ? -3.104  -16.875 9.143   1.00 9.57   ? 99  SER A CA  1 
ATOM   878  C  C   . SER A 1 99  ? -4.080  -18.086 9.310   1.00 9.57   ? 99  SER A C   1 
ATOM   879  O  O   . SER A 1 99  ? -4.287  -18.776 8.317   1.00 14.08  ? 99  SER A O   1 
ATOM   880  C  CB  . SER A 1 99  ? -1.639  -17.272 9.122   1.00 10.75  ? 99  SER A CB  1 
ATOM   881  O  OG  . SER A 1 99  ? -1.217  -17.698 10.425  1.00 10.84  ? 99  SER A OG  1 
ATOM   882  N  N   . LEU A 1 100 ? -4.580  -18.298 10.481  1.00 10.05  ? 100 LEU A N   1 
ATOM   883  C  CA  . LEU A 1 100 ? -5.458  -19.401 10.808  1.00 12.09  ? 100 LEU A CA  1 
ATOM   884  C  C   . LEU A 1 100 ? -6.471  -18.899 11.758  1.00 11.54  ? 100 LEU A C   1 
ATOM   885  O  O   . LEU A 1 100 ? -6.257  -17.840 12.341  1.00 11.50  ? 100 LEU A O   1 
ATOM   886  C  CB  . LEU A 1 100 ? -4.672  -20.470 11.569  1.00 17.59  ? 100 LEU A CB  1 
ATOM   887  C  CG  . LEU A 1 100 ? -3.342  -20.977 11.025  1.00 19.78  ? 100 LEU A CG  1 
ATOM   888  C  CD1 . LEU A 1 100 ? -2.573  -21.711 12.117  1.00 24.95  ? 100 LEU A CD1 1 
ATOM   889  C  CD2 . LEU A 1 100 ? -3.647  -21.909 9.867   1.00 22.47  ? 100 LEU A CD2 1 
ATOM   890  N  N   . ASP A 1 101 ? -7.586  -19.632 11.898  1.00 11.07  ? 101 ASP A N   1 
ATOM   891  C  CA  . ASP A 1 101 ? -8.692  -19.073 12.630  1.00 11.05  ? 101 ASP A CA  1 
ATOM   892  C  C   . ASP A 1 101 ? -8.459  -18.947 14.096  1.00 11.46  ? 101 ASP A C   1 
ATOM   893  O  O   . ASP A 1 101 ? -9.142  -18.200 14.775  1.00 13.31  ? 101 ASP A O   1 
ATOM   894  C  CB  . ASP A 1 101 ? -9.984  -19.884 12.416  1.00 11.86  ? 101 ASP A CB  1 
ATOM   895  C  CG  . ASP A 1 101 ? -10.496 -19.893 10.977  1.00 13.60  ? 101 ASP A CG  1 
ATOM   896  O  OD1 . ASP A 1 101 ? -10.056 -19.169 10.107  1.00 14.26  ? 101 ASP A OD1 1 
ATOM   897  O  OD2 . ASP A 1 101 ? -11.428 -20.713 10.760  1.00 17.96  ? 101 ASP A OD2 1 
ATOM   898  N  N   . GLY A 1 102 ? -7.444  -19.685 14.644  1.00 12.04  ? 102 GLY A N   1 
ATOM   899  C  CA  . GLY A 1 102 ? -7.153  -19.616 16.034  1.00 12.95  ? 102 GLY A CA  1 
ATOM   900  C  C   . GLY A 1 102 ? -6.227  -18.506 16.483  1.00 10.90  ? 102 GLY A C   1 
ATOM   901  O  O   . GLY A 1 102 ? -5.851  -18.457 17.657  1.00 11.94  ? 102 GLY A O   1 
ATOM   902  N  N   . GLN A 1 103 ? -5.959  -17.528 15.598  1.00 10.30  ? 103 GLN A N   1 
ATOM   903  C  CA  . GLN A 1 103 ? -5.233  -16.347 16.022  1.00 8.95   ? 103 GLN A CA  1 
ATOM   904  C  C   . GLN A 1 103 ? -5.654  -15.208 15.113  1.00 7.51   ? 103 GLN A C   1 
ATOM   905  O  O   . GLN A 1 103 ? -6.182  -15.454 14.029  1.00 8.71   ? 103 GLN A O   1 
ATOM   906  C  CB  . GLN A 1 103 ? -3.710  -16.595 15.969  1.00 9.41   ? 103 GLN A CB  1 
ATOM   907  C  CG  . GLN A 1 103 ? -3.199  -16.904 14.600  1.00 10.27  ? 103 GLN A CG  1 
ATOM   908  C  CD  . GLN A 1 103 ? -1.833  -17.522 14.595  1.00 13.21  ? 103 GLN A CD  1 
ATOM   909  O  OE1 . GLN A 1 103 ? -0.891  -17.034 13.878  1.00 13.67  ? 103 GLN A OE1 1 
ATOM   910  N  NE2 . GLN A 1 103 ? -1.678  -18.553 15.306  1.00 19.13  ? 103 GLN A NE2 1 
ATOM   911  N  N   . GLY A 1 104 ? -5.339  -14.003 15.498  1.00 7.51   ? 104 GLY A N   1 
ATOM   912  C  CA  . GLY A 1 104 ? -5.642  -12.840 14.688  1.00 6.92   ? 104 GLY A CA  1 
ATOM   913  C  C   . GLY A 1 104 ? -6.104  -11.657 15.509  1.00 6.80   ? 104 GLY A C   1 
ATOM   914  O  O   . GLY A 1 104 ? -5.839  -10.517 15.109  1.00 7.67   ? 104 GLY A O   1 
ATOM   915  N  N   . SER A 1 105 ? -6.779  -11.886 16.638  1.00 6.62   ? 105 SER A N   1 
ATOM   916  C  CA  . SER A 1 105 ? -7.158  -10.791 17.454  1.00 6.54   ? 105 SER A CA  1 
ATOM   917  C  C   . SER A 1 105 ? -5.958  -10.201 18.215  1.00 6.77   ? 105 SER A C   1 
ATOM   918  O  O   . SER A 1 105 ? -4.938  -10.869 18.429  1.00 7.80   ? 105 SER A O   1 
ATOM   919  C  CB  . SER A 1 105 ? -8.299  -11.109 18.401  1.00 7.15   ? 105 SER A CB  1 
ATOM   920  O  OG  . SER A 1 105 ? -7.927  -12.091 19.380  1.00 7.17   ? 105 SER A OG  1 
ATOM   921  N  N   . GLU A 1 106 ? -6.123  -8.947  18.623  1.00 6.34   ? 106 GLU A N   1 
ATOM   922  C  CA  . GLU A 1 106 ? -5.132  -8.240  19.415  1.00 6.67   ? 106 GLU A CA  1 
ATOM   923  C  C   . GLU A 1 106 ? -5.430  -8.419  20.873  1.00 6.45   ? 106 GLU A C   1 
ATOM   924  O  O   . GLU A 1 106 ? -4.644  -9.002  21.645  1.00 7.24   ? 106 GLU A O   1 
ATOM   925  C  CB  . GLU A 1 106 ? -5.086  -6.779  18.982  1.00 6.80   ? 106 GLU A CB  1 
ATOM   926  C  CG  . GLU A 1 106 ? -4.589  -6.649  17.533  1.00 8.40   ? 106 GLU A CG  1 
ATOM   927  C  CD  . GLU A 1 106 ? -3.922  -5.371  17.278  1.00 6.84   ? 106 GLU A CD  1 
ATOM   928  O  OE1 . GLU A 1 106 ? -4.493  -4.287  17.551  1.00 6.96   ? 106 GLU A OE1 1 
ATOM   929  O  OE2 . GLU A 1 106 ? -2.758  -5.418  16.781  1.00 8.16   ? 106 GLU A OE2 1 
ATOM   930  N  N   . HIS A 1 107 ? -6.621  -7.997  21.305  1.00 6.39   ? 107 HIS A N   1 
ATOM   931  C  CA  . HIS A 1 107 ? -7.070  -8.383  22.632  1.00 6.34   ? 107 HIS A CA  1 
ATOM   932  C  C   . HIS A 1 107 ? -7.351  -9.878  22.657  1.00 6.56   ? 107 HIS A C   1 
ATOM   933  O  O   . HIS A 1 107 ? -7.683  -10.485 21.642  1.00 6.64   ? 107 HIS A O   1 
ATOM   934  C  CB  . HIS A 1 107 ? -8.316  -7.587  23.004  1.00 6.97   ? 107 HIS A CB  1 
ATOM   935  C  CG  . HIS A 1 107 ? -7.996  -6.129  23.163  1.00 6.22   ? 107 HIS A CG  1 
ATOM   936  N  ND1 . HIS A 1 107 ? -8.070  -5.261  22.117  1.00 6.74   ? 107 HIS A ND1 1 
ATOM   937  C  CD2 . HIS A 1 107 ? -7.537  -5.419  24.243  1.00 6.44   ? 107 HIS A CD2 1 
ATOM   938  C  CE1 . HIS A 1 107 ? -7.643  -4.065  22.591  1.00 6.63   ? 107 HIS A CE1 1 
ATOM   939  N  NE2 . HIS A 1 107 ? -7.316  -4.131  23.836  1.00 6.43   ? 107 HIS A NE2 1 
ATOM   940  N  N   . THR A 1 108 ? -7.239  -10.442 23.859  1.00 6.79   ? 108 THR A N   1 
ATOM   941  C  CA  . THR A 1 108 ? -7.615  -11.813 24.120  1.00 7.24   ? 108 THR A CA  1 
ATOM   942  C  C   . THR A 1 108 ? -8.544  -11.815 25.311  1.00 6.95   ? 108 THR A C   1 
ATOM   943  O  O   . THR A 1 108 ? -8.578  -10.866 26.085  1.00 7.49   ? 108 THR A O   1 
ATOM   944  C  CB  . THR A 1 108 ? -6.391  -12.712 24.329  1.00 8.16   ? 108 THR A CB  1 
ATOM   945  O  OG1 . THR A 1 108 ? -5.559  -12.213 25.372  1.00 8.30   ? 108 THR A OG1 1 
ATOM   946  C  CG2 . THR A 1 108 ? -5.577  -12.771 23.060  1.00 8.46   ? 108 THR A CG2 1 
ATOM   947  N  N   . VAL A 1 109 ? -9.301  -12.900 25.461  1.00 7.79   ? 109 VAL A N   1 
ATOM   948  C  CA  . VAL A 1 109 ? -10.298 -12.967 26.564  1.00 8.99   ? 109 VAL A CA  1 
ATOM   949  C  C   . VAL A 1 109 ? -9.971  -14.268 27.278  1.00 8.62   ? 109 VAL A C   1 
ATOM   950  O  O   . VAL A 1 109 ? -10.145 -15.373 26.729  1.00 9.31   ? 109 VAL A O   1 
ATOM   951  C  CB  . VAL A 1 109 ? -11.737 -12.999 25.989  1.00 9.44   ? 109 VAL A CB  1 
ATOM   952  C  CG1 . VAL A 1 109 ? -12.733 -13.124 27.148  1.00 11.40  ? 109 VAL A CG1 1 
ATOM   953  C  CG2 . VAL A 1 109 ? -11.974 -11.728 25.166  1.00 10.11  ? 109 VAL A CG2 1 
ATOM   954  N  N   . ASP A 1 110 ? -9.490  -14.147 28.500  1.00 9.03   ? 110 ASP A N   1 
ATOM   955  C  CA  . ASP A 1 110 ? -9.009  -15.358 29.240  1.00 10.90  ? 110 ASP A CA  1 
ATOM   956  C  C   . ASP A 1 110 ? -8.054  -16.176 28.342  1.00 10.30  ? 110 ASP A C   1 
ATOM   957  O  O   . ASP A 1 110 ? -8.072  -17.400 28.325  1.00 11.35  ? 110 ASP A O   1 
ATOM   958  C  CB  . ASP A 1 110 ? -10.170 -16.169 29.712  1.00 12.27  ? 110 ASP A CB  1 
ATOM   959  C  CG  . ASP A 1 110 ? -10.962 -15.434 30.732  1.00 12.16  ? 110 ASP A CG  1 
ATOM   960  O  OD1 . ASP A 1 110 ? -10.437 -14.556 31.407  1.00 13.29  ? 110 ASP A OD1 1 
ATOM   961  O  OD2 . ASP A 1 110 ? -12.171 -15.750 30.836  1.00 15.43  ? 110 ASP A OD2 1 
ATOM   962  N  N   . LYS A 1 111 ? -7.158  -15.446 27.661  1.00 9.59   ? 111 LYS A N   1 
ATOM   963  C  CA  . LYS A 1 111 ? -6.141  -15.970 26.780  1.00 9.74   ? 111 LYS A CA  1 
ATOM   964  C  C   . LYS A 1 111 ? -6.644  -16.450 25.452  1.00 9.32   ? 111 LYS A C   1 
ATOM   965  O  O   . LYS A 1 111 ? -5.885  -16.837 24.571  1.00 11.11  ? 111 LYS A O   1 
ATOM   966  C  CB  . LYS A 1 111 ? -5.210  -17.026 27.432  1.00 11.85  ? 111 LYS A CB  1 
ATOM   967  C  CG  . LYS A 1 111 ? -4.486  -16.418 28.679  1.00 15.19  ? 111 LYS A CG  1 
ATOM   968  C  CD  . LYS A 1 111 ? -3.527  -15.275 28.329  1.00 18.31  ? 111 LYS A CD  1 
ATOM   969  C  CE  . LYS A 1 111 ? -2.769  -14.546 29.446  1.00 21.00  ? 111 LYS A CE  1 
ATOM   970  N  NZ  . LYS A 1 111 ? -1.528  -15.240 29.792  1.00 25.61  ? 111 LYS A NZ  1 
ATOM   971  N  N   . LYS A 1 112 ? -7.970  -16.492 25.248  1.00 8.80   ? 112 LYS A N   1 
ATOM   972  C  CA  . LYS A 1 112 ? -8.526  -16.902 23.962  1.00 10.02  ? 112 LYS A CA  1 
ATOM   973  C  C   . LYS A 1 112 ? -8.259  -15.836 22.891  1.00 8.39   ? 112 LYS A C   1 
ATOM   974  O  O   . LYS A 1 112 ? -8.550  -14.671 23.095  1.00 8.51   ? 112 LYS A O   1 
ATOM   975  C  CB  . LYS A 1 112 ? -10.065 -17.039 24.063  1.00 11.92  ? 112 LYS A CB  1 
ATOM   976  C  CG  . LYS A 1 112 ? -10.748 -17.408 22.750  1.00 13.97  ? 112 LYS A CG  1 
ATOM   977  C  CD  . LYS A 1 112 ? -12.266 -17.358 22.808  1.00 15.55  ? 112 LYS A CD  1 
ATOM   978  C  CE  . LYS A 1 112 ? -12.796 -17.576 21.405  1.00 20.04  ? 112 LYS A CE  1 
ATOM   979  N  NZ  . LYS A 1 112 ? -12.756 -18.880 20.941  1.00 18.53  ? 112 LYS A NZ  1 
ATOM   980  N  N   A LYS A 1 113 ? -7.805  -16.318 21.749  0.50 8.51   ? 113 LYS A N   1 
ATOM   981  N  N   B LYS A 1 113 ? -7.655  -16.256 21.779  0.50 8.19   ? 113 LYS A N   1 
ATOM   982  C  CA  A LYS A 1 113 ? -7.626  -15.487 20.609  0.50 9.12   ? 113 LYS A CA  1 
ATOM   983  C  CA  B LYS A 1 113 ? -7.499  -15.440 20.565  0.50 9.22   ? 113 LYS A CA  1 
ATOM   984  C  C   A LYS A 1 113 ? -8.818  -15.730 19.720  0.50 7.97   ? 113 LYS A C   1 
ATOM   985  C  C   B LYS A 1 113 ? -8.610  -15.726 19.560  0.50 8.31   ? 113 LYS A C   1 
ATOM   986  O  O   A LYS A 1 113 ? -9.301  -16.851 19.583  0.50 8.51   ? 113 LYS A O   1 
ATOM   987  O  O   B LYS A 1 113 ? -8.861  -16.887 19.206  0.50 8.68   ? 113 LYS A O   1 
ATOM   988  C  CB  A LYS A 1 113 ? -6.333  -15.896 19.865  0.50 9.46   ? 113 LYS A CB  1 
ATOM   989  C  CB  B LYS A 1 113 ? -6.190  -15.794 19.853  0.50 10.00  ? 113 LYS A CB  1 
ATOM   990  C  CG  A LYS A 1 113 ? -5.035  -15.635 20.650  0.50 9.77   ? 113 LYS A CG  1 
ATOM   991  C  CG  B LYS A 1 113 ? -4.968  -15.393 20.659  0.50 10.39  ? 113 LYS A CG  1 
ATOM   992  C  CD  A LYS A 1 113 ? -3.830  -16.257 19.970  0.50 9.79   ? 113 LYS A CD  1 
ATOM   993  C  CD  B LYS A 1 113 ? -3.715  -15.969 20.086  0.50 9.40   ? 113 LYS A CD  1 
ATOM   994  C  CE  A LYS A 1 113 ? -2.479  -15.781 20.476  0.50 12.46  ? 113 LYS A CE  1 
ATOM   995  C  CE  B LYS A 1 113 ? -2.543  -15.398 20.859  0.50 13.54  ? 113 LYS A CE  1 
ATOM   996  N  NZ  A LYS A 1 113 ? -2.094  -16.338 21.790  0.50 12.51  ? 113 LYS A NZ  1 
ATOM   997  N  NZ  B LYS A 1 113 ? -1.417  -16.336 20.643  0.50 16.34  ? 113 LYS A NZ  1 
ATOM   998  N  N   . TYR A 1 114 ? -9.251  -14.663 19.076  1.00 7.51   ? 114 TYR A N   1 
ATOM   999  C  CA  . TYR A 1 114 ? -10.248 -14.723 18.036  1.00 7.68   ? 114 TYR A CA  1 
ATOM   1000 C  C   . TYR A 1 114 ? -9.571  -14.691 16.679  1.00 6.64   ? 114 TYR A C   1 
ATOM   1001 O  O   . TYR A 1 114 ? -8.379  -14.383 16.525  1.00 7.86   ? 114 TYR A O   1 
ATOM   1002 C  CB  . TYR A 1 114 ? -11.319 -13.624 18.202  1.00 7.92   ? 114 TYR A CB  1 
ATOM   1003 C  CG  . TYR A 1 114 ? -12.229 -13.859 19.351  1.00 7.71   ? 114 TYR A CG  1 
ATOM   1004 C  CD1 . TYR A 1 114 ? -11.979 -13.405 20.624  1.00 9.44   ? 114 TYR A CD1 1 
ATOM   1005 C  CD2 . TYR A 1 114 ? -13.441 -14.481 19.090  1.00 9.69   ? 114 TYR A CD2 1 
ATOM   1006 C  CE1 . TYR A 1 114 ? -12.893 -13.622 21.673  1.00 11.39  ? 114 TYR A CE1 1 
ATOM   1007 C  CE2 . TYR A 1 114 ? -14.371 -14.682 20.145  1.00 11.91  ? 114 TYR A CE2 1 
ATOM   1008 C  CZ  . TYR A 1 114 ? -14.051 -14.248 21.389  1.00 11.91  ? 114 TYR A CZ  1 
ATOM   1009 O  OH  . TYR A 1 114 ? -14.891 -14.348 22.497  1.00 17.91  ? 114 TYR A OH  1 
ATOM   1010 N  N   . ALA A 1 115 ? -10.324 -14.998 15.613  1.00 7.49   ? 115 ALA A N   1 
ATOM   1011 C  CA  . ALA A 1 115 ? -9.787  -15.049 14.266  1.00 7.57   ? 115 ALA A CA  1 
ATOM   1012 C  C   . ALA A 1 115 ? -9.422  -13.646 13.769  1.00 7.12   ? 115 ALA A C   1 
ATOM   1013 O  O   . ALA A 1 115 ? -8.569  -13.525 12.894  1.00 7.42   ? 115 ALA A O   1 
ATOM   1014 C  CB  . ALA A 1 115 ? -10.820 -15.678 13.332  1.00 8.55   ? 115 ALA A CB  1 
ATOM   1015 N  N   . ALA A 1 116 ? -10.087 -12.593 14.277  1.00 6.90   ? 116 ALA A N   1 
ATOM   1016 C  CA  . ALA A 1 116 ? -9.802  -11.260 13.822  1.00 6.67   ? 116 ALA A CA  1 
ATOM   1017 C  C   . ALA A 1 116 ? -10.368 -10.301 14.853  1.00 6.16   ? 116 ALA A C   1 
ATOM   1018 O  O   . ALA A 1 116 ? -11.116 -10.690 15.730  1.00 6.81   ? 116 ALA A O   1 
ATOM   1019 C  CB  . ALA A 1 116 ? -10.349 -11.002 12.432  1.00 7.15   ? 116 ALA A CB  1 
ATOM   1020 N  N   . GLU A 1 117 ? -10.027 -9.035  14.645  1.00 6.56   ? 117 GLU A N   1 
ATOM   1021 C  CA  . GLU A 1 117 ? -10.565 -7.976  15.494  1.00 6.43   ? 117 GLU A CA  1 
ATOM   1022 C  C   . GLU A 1 117 ? -10.732 -6.732  14.640  1.00 6.39   ? 117 GLU A C   1 
ATOM   1023 O  O   . GLU A 1 117 ? -9.834  -6.341  13.907  1.00 7.23   ? 117 GLU A O   1 
ATOM   1024 C  CB  . GLU A 1 117 ? -9.609  -7.724  16.685  1.00 7.40   ? 117 GLU A CB  1 
ATOM   1025 C  CG  . GLU A 1 117 ? -10.149 -6.793  17.772  1.00 7.37   ? 117 GLU A CG  1 
ATOM   1026 C  CD  . GLU A 1 117 ? -9.243  -6.728  19.008  1.00 6.89   ? 117 GLU A CD  1 
ATOM   1027 O  OE1 . GLU A 1 117 ? -8.555  -7.745  19.283  1.00 7.46   ? 117 GLU A OE1 1 
ATOM   1028 O  OE2 . GLU A 1 117 ? -9.201  -5.670  19.643  1.00 7.61   ? 117 GLU A OE2 1 
ATOM   1029 N  N   . LEU A 1 118 ? -11.919 -6.156  14.768  1.00 6.09   ? 118 LEU A N   1 
ATOM   1030 C  CA  . LEU A 1 118 ? -12.303 -4.907  14.093  1.00 5.39   ? 118 LEU A CA  1 
ATOM   1031 C  C   . LEU A 1 118 ? -12.093 -3.743  15.077  1.00 5.40   ? 118 LEU A C   1 
ATOM   1032 O  O   . LEU A 1 118 ? -12.507 -3.823  16.238  1.00 6.11   ? 118 LEU A O   1 
ATOM   1033 C  CB  . LEU A 1 118 ? -13.770 -5.013  13.748  1.00 6.60   ? 118 LEU A CB  1 
ATOM   1034 C  CG  . LEU A 1 118 ? -14.522 -3.737  13.384  1.00 6.84   ? 118 LEU A CG  1 
ATOM   1035 C  CD1 . LEU A 1 118 ? -13.908 -3.024  12.150  1.00 7.12   ? 118 LEU A CD1 1 
ATOM   1036 C  CD2 . LEU A 1 118 ? -15.998 -4.031  13.168  1.00 8.22   ? 118 LEU A CD2 1 
ATOM   1037 N  N   . HIS A 1 119 ? -11.443 -2.687  14.598  1.00 5.37   ? 119 HIS A N   1 
ATOM   1038 C  CA  . HIS A 1 119 ? -11.233 -1.470  15.370  1.00 5.71   ? 119 HIS A CA  1 
ATOM   1039 C  C   . HIS A 1 119 ? -11.859 -0.308  14.682  1.00 5.80   ? 119 HIS A C   1 
ATOM   1040 O  O   . HIS A 1 119 ? -11.493 0.023   13.544  1.00 6.34   ? 119 HIS A O   1 
ATOM   1041 C  CB  . HIS A 1 119 ? -9.719  -1.207  15.511  1.00 6.05   ? 119 HIS A CB  1 
ATOM   1042 C  CG  . HIS A 1 119 ? -9.050  -2.179  16.406  1.00 5.99   ? 119 HIS A CG  1 
ATOM   1043 N  ND1 . HIS A 1 119 ? -7.708  -2.413  16.409  1.00 5.78   ? 119 HIS A ND1 1 
ATOM   1044 C  CD2 . HIS A 1 119 ? -9.614  -2.963  17.362  1.00 6.22   ? 119 HIS A CD2 1 
ATOM   1045 C  CE1 . HIS A 1 119 ? -7.468  -3.347  17.341  1.00 6.71   ? 119 HIS A CE1 1 
ATOM   1046 N  NE2 . HIS A 1 119 ? -8.584  -3.709  17.921  1.00 6.51   ? 119 HIS A NE2 1 
ATOM   1047 N  N   . LEU A 1 120 ? -12.818 0.321   15.354  1.00 5.88   ? 120 LEU A N   1 
ATOM   1048 C  CA  . LEU A 1 120 ? -13.464 1.537   14.899  1.00 6.04   ? 120 LEU A CA  1 
ATOM   1049 C  C   . LEU A 1 120 ? -12.841 2.678   15.713  1.00 5.68   ? 120 LEU A C   1 
ATOM   1050 O  O   . LEU A 1 120 ? -12.964 2.711   16.936  1.00 6.18   ? 120 LEU A O   1 
ATOM   1051 C  CB  . LEU A 1 120 ? -14.967 1.474   15.099  1.00 7.01   ? 120 LEU A CB  1 
ATOM   1052 C  CG  . LEU A 1 120 ? -15.674 0.414   14.236  1.00 6.99   ? 120 LEU A CG  1 
ATOM   1053 C  CD1 . LEU A 1 120 ? -16.519 -0.496  15.093  1.00 12.03  ? 120 LEU A CD1 1 
ATOM   1054 C  CD2 . LEU A 1 120 ? -16.463 1.103   13.099  1.00 9.77   ? 120 LEU A CD2 1 
ATOM   1055 N  N   . VAL A 1 121 ? -12.119 3.549   15.035  1.00 6.35   ? 121 VAL A N   1 
ATOM   1056 C  CA  . VAL A 1 121 ? -11.249 4.557   15.653  1.00 6.67   ? 121 VAL A CA  1 
ATOM   1057 C  C   . VAL A 1 121 ? -11.940 5.888   15.630  1.00 6.43   ? 121 VAL A C   1 
ATOM   1058 O  O   . VAL A 1 121 ? -12.361 6.360   14.571  1.00 7.71   ? 121 VAL A O   1 
ATOM   1059 C  CB  . VAL A 1 121 ? -9.887  4.651   14.907  1.00 7.40   ? 121 VAL A CB  1 
ATOM   1060 C  CG1 . VAL A 1 121 ? -8.998  5.713   15.545  1.00 9.42   ? 121 VAL A CG1 1 
ATOM   1061 C  CG2 . VAL A 1 121 ? -9.191  3.302   14.843  1.00 7.67   ? 121 VAL A CG2 1 
ATOM   1062 N  N   . HIS A 1 122 ? -12.031 6.504   16.800  1.00 6.75   ? 122 HIS A N   1 
ATOM   1063 C  CA  . HIS A 1 122 ? -12.750 7.759   16.972  1.00 7.57   ? 122 HIS A CA  1 
ATOM   1064 C  C   . HIS A 1 122 ? -11.842 8.754   17.688  1.00 7.16   ? 122 HIS A C   1 
ATOM   1065 O  O   . HIS A 1 122 ? -11.068 8.340   18.579  1.00 8.43   ? 122 HIS A O   1 
ATOM   1066 C  CB  . HIS A 1 122 ? -13.981 7.607   17.778  1.00 7.77   ? 122 HIS A CB  1 
ATOM   1067 C  CG  . HIS A 1 122 ? -14.890 6.458   17.420  1.00 7.21   ? 122 HIS A CG  1 
ATOM   1068 N  ND1 . HIS A 1 122 ? -14.596 5.153   17.686  1.00 7.42   ? 122 HIS A ND1 1 
ATOM   1069 C  CD2 . HIS A 1 122 ? -16.121 6.423   16.822  1.00 7.95   ? 122 HIS A CD2 1 
ATOM   1070 C  CE1 . HIS A 1 122 ? -15.586 4.361   17.250  1.00 7.77   ? 122 HIS A CE1 1 
ATOM   1071 N  NE2 . HIS A 1 122 ? -16.536 5.129   16.713  1.00 8.15   ? 122 HIS A NE2 1 
ATOM   1072 N  N   . TRP A 1 123 ? -12.013 10.038  17.451  1.00 7.04   ? 123 TRP A N   1 
ATOM   1073 C  CA  . TRP A 1 123 ? -11.190 11.073  18.152  1.00 7.50   ? 123 TRP A CA  1 
ATOM   1074 C  C   . TRP A 1 123 ? -12.077 12.050  18.850  1.00 8.27   ? 123 TRP A C   1 
ATOM   1075 O  O   . TRP A 1 123 ? -13.190 12.384  18.393  1.00 9.40   ? 123 TRP A O   1 
ATOM   1076 C  CB  . TRP A 1 123 ? -10.224 11.750  17.170  1.00 9.74   ? 123 TRP A CB  1 
ATOM   1077 C  CG  . TRP A 1 123 ? -10.802 12.388  15.968  1.00 10.01  ? 123 TRP A CG  1 
ATOM   1078 C  CD1 . TRP A 1 123 ? -11.017 11.738  14.798  1.00 11.67  ? 123 TRP A CD1 1 
ATOM   1079 C  CD2 . TRP A 1 123 ? -11.262 13.721  15.809  1.00 11.30  ? 123 TRP A CD2 1 
ATOM   1080 N  NE1 . TRP A 1 123 ? -11.553 12.577  13.856  1.00 12.64  ? 123 TRP A NE1 1 
ATOM   1081 C  CE2 . TRP A 1 123 ? -11.703 13.808  14.443  1.00 11.93  ? 123 TRP A CE2 1 
ATOM   1082 C  CE3 . TRP A 1 123 ? -11.291 14.845  16.617  1.00 11.67  ? 123 TRP A CE3 1 
ATOM   1083 C  CZ2 . TRP A 1 123 ? -12.194 14.969  13.930  1.00 13.29  ? 123 TRP A CZ2 1 
ATOM   1084 C  CZ3 . TRP A 1 123 ? -11.818 15.987  16.125  1.00 13.29  ? 123 TRP A CZ3 1 
ATOM   1085 C  CH2 . TRP A 1 123 ? -12.223 16.072  14.803  1.00 14.59  ? 123 TRP A CH2 1 
ATOM   1086 N  N   . ASN A 1 124 ? -11.623 12.508  19.998  1.00 8.77   ? 124 ASN A N   1 
ATOM   1087 C  CA  . ASN A 1 124 ? -12.374 13.429  20.875  1.00 9.64   ? 124 ASN A CA  1 
ATOM   1088 C  C   . ASN A 1 124 ? -12.451 14.809  20.255  1.00 9.87   ? 124 ASN A C   1 
ATOM   1089 O  O   . ASN A 1 124 ? -11.415 15.442  20.000  1.00 9.50   ? 124 ASN A O   1 
ATOM   1090 C  CB  . ASN A 1 124 ? -11.608 13.457  22.210  1.00 10.46  ? 124 ASN A CB  1 
ATOM   1091 C  CG  . ASN A 1 124 ? -12.356 14.088  23.306  1.00 11.96  ? 124 ASN A CG  1 
ATOM   1092 O  OD1 . ASN A 1 124 ? -13.174 14.991  23.044  1.00 12.72  ? 124 ASN A OD1 1 
ATOM   1093 N  ND2 . ASN A 1 124 ? -12.046 13.683  24.537  1.00 12.88  ? 124 ASN A ND2 1 
ATOM   1094 N  N   . THR A 1 125 ? -13.662 15.260  19.997  1.00 11.08  ? 125 THR A N   1 
ATOM   1095 C  CA  . THR A 1 125 ? -13.854 16.514  19.262  1.00 11.87  ? 125 THR A CA  1 
ATOM   1096 C  C   . THR A 1 125 ? -13.333 17.692  20.031  1.00 11.37  ? 125 THR A C   1 
ATOM   1097 O  O   . THR A 1 125 ? -13.117 18.729  19.436  1.00 13.24  ? 125 THR A O   1 
ATOM   1098 C  CB  . THR A 1 125 ? -15.306 16.715  18.846  1.00 16.23  ? 125 THR A CB  1 
ATOM   1099 O  OG1 . THR A 1 125 ? -16.095 16.744  20.020  1.00 18.23  ? 125 THR A OG1 1 
ATOM   1100 C  CG2 . THR A 1 125 ? -15.744 15.607  17.876  1.00 17.93  ? 125 THR A CG2 1 
ATOM   1101 N  N   . LYS A 1 126 ? -13.100 17.589  21.382  1.00 11.73  ? 126 LYS A N   1 
ATOM   1102 C  CA  . LYS A 1 126 ? -12.565 18.701  22.094  1.00 13.14  ? 126 LYS A CA  1 
ATOM   1103 C  C   . LYS A 1 126 ? -11.150 19.064  21.636  1.00 12.59  ? 126 LYS A C   1 
ATOM   1104 O  O   . LYS A 1 126 ? -10.687 20.129  21.943  1.00 16.58  ? 126 LYS A O   1 
ATOM   1105 C  CB  . LYS A 1 126 ? -12.662 18.483  23.576  1.00 16.48  ? 126 LYS A CB  1 
ATOM   1106 C  CG  . LYS A 1 126 ? -11.618 17.662  24.166  1.00 17.07  ? 126 LYS A CG  1 
ATOM   1107 C  CD  . LYS A 1 126 ? -12.070 17.476  25.600  1.00 23.22  ? 126 LYS A CD  1 
ATOM   1108 C  CE  . LYS A 1 126 ? -11.092 16.620  26.288  1.00 23.71  ? 126 LYS A CE  1 
ATOM   1109 N  NZ  . LYS A 1 126 ? -10.491 17.579  27.284  1.00 47.00  ? 126 LYS A NZ  1 
ATOM   1110 N  N   . TYR A 1 127 ? -10.472 18.156  20.912  1.00 9.66   ? 127 TYR A N   1 
ATOM   1111 C  CA  . TYR A 1 127 ? -9.124  18.386  20.417  1.00 9.95   ? 127 TYR A CA  1 
ATOM   1112 C  C   . TYR A 1 127 ? -9.082  18.769  18.939  1.00 9.66   ? 127 TYR A C   1 
ATOM   1113 O  O   . TYR A 1 127 ? -8.006  18.973  18.394  1.00 10.92  ? 127 TYR A O   1 
ATOM   1114 C  CB  . TYR A 1 127 ? -8.204  17.227  20.694  1.00 10.93  ? 127 TYR A CB  1 
ATOM   1115 C  CG  . TYR A 1 127 ? -8.100  16.904  22.176  1.00 10.52  ? 127 TYR A CG  1 
ATOM   1116 C  CD1 . TYR A 1 127 ? -7.699  17.886  23.113  1.00 12.20  ? 127 TYR A CD1 1 
ATOM   1117 C  CD2 . TYR A 1 127 ? -8.442  15.638  22.673  1.00 10.37  ? 127 TYR A CD2 1 
ATOM   1118 C  CE1 . TYR A 1 127 ? -7.619  17.630  24.448  1.00 12.23  ? 127 TYR A CE1 1 
ATOM   1119 C  CE2 . TYR A 1 127 ? -8.376  15.371  24.021  1.00 11.03  ? 127 TYR A CE2 1 
ATOM   1120 C  CZ  . TYR A 1 127 ? -7.961  16.389  24.963  1.00 11.58  ? 127 TYR A CZ  1 
ATOM   1121 O  OH  . TYR A 1 127 ? -7.884  16.176  26.285  1.00 13.31  ? 127 TYR A OH  1 
ATOM   1122 N  N   . GLY A 1 128 ? -10.251 18.853  18.318  1.00 10.98  ? 128 GLY A N   1 
ATOM   1123 C  CA  . GLY A 1 128 ? -10.356 19.491  16.990  1.00 11.31  ? 128 GLY A CA  1 
ATOM   1124 C  C   . GLY A 1 128 ? -9.929  18.657  15.774  1.00 11.06  ? 128 GLY A C   1 
ATOM   1125 O  O   . GLY A 1 128 ? -10.541 18.760  14.729  1.00 12.81  ? 128 GLY A O   1 
ATOM   1126 N  N   . ASP A 1 129 ? -8.837  17.855  15.909  1.00 11.90  ? 129 ASP A N   1 
ATOM   1127 C  CA  . ASP A 1 129 ? -8.343  16.981  14.809  1.00 11.99  ? 129 ASP A CA  1 
ATOM   1128 C  C   . ASP A 1 129 ? -7.703  15.759  15.391  1.00 11.72  ? 129 ASP A C   1 
ATOM   1129 O  O   . ASP A 1 129 ? -7.311  15.753  16.568  1.00 12.10  ? 129 ASP A O   1 
ATOM   1130 C  CB  . ASP A 1 129 ? -7.375  17.718  13.833  1.00 11.63  ? 129 ASP A CB  1 
ATOM   1131 C  CG  . ASP A 1 129 ? -6.020  18.112  14.354  1.00 12.81  ? 129 ASP A CG  1 
ATOM   1132 O  OD1 . ASP A 1 129 ? -5.718  19.311  14.443  1.00 17.72  ? 129 ASP A OD1 1 
ATOM   1133 O  OD2 . ASP A 1 129 ? -5.158  17.222  14.541  1.00 14.48  ? 129 ASP A OD2 1 
ATOM   1134 N  N   . ALA A 1 130 ? -7.680  14.694  14.622  1.00 11.99  ? 130 ALA A N   1 
ATOM   1135 C  CA  . ALA A 1 130 ? -7.178  13.418  15.090  1.00 11.45  ? 130 ALA A CA  1 
ATOM   1136 C  C   . ALA A 1 130 ? -5.737  13.471  15.477  1.00 12.60  ? 130 ALA A C   1 
ATOM   1137 O  O   . ALA A 1 130 ? -5.358  12.715  16.353  1.00 12.03  ? 130 ALA A O   1 
ATOM   1138 C  CB  . ALA A 1 130 ? -7.430  12.401  14.005  1.00 14.08  ? 130 ALA A CB  1 
ATOM   1139 N  N   . GLY A 1 131 ? -4.854  14.242  14.775  1.00 12.75  ? 131 GLY A N   1 
ATOM   1140 C  CA  . GLY A 1 131 ? -3.429  14.350  15.113  1.00 13.72  ? 131 GLY A CA  1 
ATOM   1141 C  C   . GLY A 1 131 ? -3.335  14.934  16.541  1.00 13.07  ? 131 GLY A C   1 
ATOM   1142 O  O   . GLY A 1 131 ? -2.585  14.420  17.367  1.00 14.15  ? 131 GLY A O   1 
ATOM   1143 N  N   A LYS A 1 132 ? -4.051  16.018  16.829  0.50 12.38  ? 132 LYS A N   1 
ATOM   1144 N  N   B LYS A 1 132 ? -4.032  16.026  16.814  0.50 12.17  ? 132 LYS A N   1 
ATOM   1145 C  CA  A LYS A 1 132 ? -3.971  16.672  18.094  0.50 12.54  ? 132 LYS A CA  1 
ATOM   1146 C  CA  B LYS A 1 132 ? -3.904  16.655  18.074  0.50 12.10  ? 132 LYS A CA  1 
ATOM   1147 C  C   A LYS A 1 132 ? -4.467  15.668  19.102  0.50 10.69  ? 132 LYS A C   1 
ATOM   1148 C  C   B LYS A 1 132 ? -4.498  15.722  19.123  0.50 10.84  ? 132 LYS A C   1 
ATOM   1149 O  O   A LYS A 1 132 ? -3.829  15.477  20.151  0.50 12.66  ? 132 LYS A O   1 
ATOM   1150 O  O   B LYS A 1 132 ? -3.953  15.635  20.243  0.50 11.55  ? 132 LYS A O   1 
ATOM   1151 C  CB  A LYS A 1 132 ? -4.840  17.932  18.083  0.50 13.79  ? 132 LYS A CB  1 
ATOM   1152 C  CB  B LYS A 1 132 ? -4.562  18.075  18.007  0.50 10.12  ? 132 LYS A CB  1 
ATOM   1153 C  CG  A LYS A 1 132 ? -4.053  19.220  17.915  0.50 17.12  ? 132 LYS A CG  1 
ATOM   1154 C  CG  B LYS A 1 132 ? -3.677  19.146  17.406  0.50 15.69  ? 132 LYS A CG  1 
ATOM   1155 C  CD  A LYS A 1 132 ? -3.216  19.190  16.647  0.50 22.32  ? 132 LYS A CD  1 
ATOM   1156 C  CD  B LYS A 1 132 ? -2.724  19.669  18.461  0.50 17.32  ? 132 LYS A CD  1 
ATOM   1157 C  CE  A LYS A 1 132 ? -3.497  20.401  15.773  0.50 13.83  ? 132 LYS A CE  1 
ATOM   1158 C  CE  B LYS A 1 132 ? -3.409  20.711  19.325  0.50 24.85  ? 132 LYS A CE  1 
ATOM   1159 N  NZ  A LYS A 1 132 ? -2.919  20.238  14.410  0.50 22.19  ? 132 LYS A NZ  1 
ATOM   1160 N  NZ  B LYS A 1 132 ? -3.869  20.150  20.624  0.50 29.19  ? 132 LYS A NZ  1 
ATOM   1161 N  N   . ALA A 1 133 ? -5.612  15.019  18.794  1.00 9.52   ? 133 ALA A N   1 
ATOM   1162 C  CA  . ALA A 1 133 ? -6.194  14.119  19.736  1.00 9.42   ? 133 ALA A CA  1 
ATOM   1163 C  C   . ALA A 1 133 ? -5.196  13.028  20.136  1.00 9.23   ? 133 ALA A C   1 
ATOM   1164 O  O   . ALA A 1 133 ? -5.164  12.586  21.284  1.00 10.07  ? 133 ALA A O   1 
ATOM   1165 C  CB  . ALA A 1 133 ? -7.471  13.504  19.186  1.00 9.22   ? 133 ALA A CB  1 
ATOM   1166 N  N   . SER A 1 134 ? -4.373  12.563  19.175  1.00 10.32  ? 134 SER A N   1 
ATOM   1167 C  CA  . SER A 1 134 ? -3.413  11.442  19.455  1.00 11.00  ? 134 SER A CA  1 
ATOM   1168 C  C   . SER A 1 134 ? -2.355  11.850  20.422  1.00 11.23  ? 134 SER A C   1 
ATOM   1169 O  O   . SER A 1 134 ? -1.605  10.974  20.895  1.00 12.19  ? 134 SER A O   1 
ATOM   1170 C  CB  . SER A 1 134 ? -2.835  10.896  18.169  1.00 14.61  ? 134 SER A CB  1 
ATOM   1171 O  OG  . SER A 1 134 ? -1.859  11.798  17.651  1.00 17.03  ? 134 SER A OG  1 
ATOM   1172 N  N   . GLN A 1 135 ? -2.201  13.141  20.726  1.00 10.93  ? 135 GLN A N   1 
ATOM   1173 C  CA  . GLN A 1 135 ? -1.235  13.624  21.717  1.00 12.06  ? 135 GLN A CA  1 
ATOM   1174 C  C   . GLN A 1 135 ? -1.810  13.728  23.117  1.00 11.74  ? 135 GLN A C   1 
ATOM   1175 O  O   . GLN A 1 135 ? -1.110  14.236  24.033  1.00 15.36  ? 135 GLN A O   1 
ATOM   1176 C  CB  . GLN A 1 135 ? -0.647  14.987  21.238  1.00 17.54  ? 135 GLN A CB  1 
ATOM   1177 C  CG  . GLN A 1 135 ? -0.115  14.880  19.837  1.00 20.54  ? 135 GLN A CG  1 
ATOM   1178 C  CD  . GLN A 1 135 ? 1.118   14.023  19.773  1.00 34.49  ? 135 GLN A CD  1 
ATOM   1179 O  OE1 . GLN A 1 135 ? 2.081   14.246  20.520  1.00 51.17  ? 135 GLN A OE1 1 
ATOM   1180 N  NE2 . GLN A 1 135 ? 1.118   13.057  18.858  1.00 42.83  ? 135 GLN A NE2 1 
ATOM   1181 N  N   . GLN A 1 136 ? -3.053  13.275  23.312  1.00 10.25  ? 136 GLN A N   1 
ATOM   1182 C  CA  . GLN A 1 136 ? -3.721  13.488  24.570  1.00 9.56   ? 136 GLN A CA  1 
ATOM   1183 C  C   . GLN A 1 136 ? -4.065  12.172  25.180  1.00 9.69   ? 136 GLN A C   1 
ATOM   1184 O  O   . GLN A 1 136 ? -4.464  11.241  24.482  1.00 9.77   ? 136 GLN A O   1 
ATOM   1185 C  CB  . GLN A 1 136 ? -4.975  14.294  24.401  1.00 12.14  ? 136 GLN A CB  1 
ATOM   1186 C  CG  . GLN A 1 136 ? -4.849  15.532  23.511  1.00 13.94  ? 136 GLN A CG  1 
ATOM   1187 C  CD  . GLN A 1 136 ? -3.859  16.425  23.990  1.00 16.00  ? 136 GLN A CD  1 
ATOM   1188 O  OE1 . GLN A 1 136 ? -3.627  16.585  25.213  1.00 17.75  ? 136 GLN A OE1 1 
ATOM   1189 N  NE2 . GLN A 1 136 ? -3.194  17.064  23.026  1.00 25.25  ? 136 GLN A NE2 1 
ATOM   1190 N  N   . PRO A 1 137 ? -4.096  12.050  26.533  1.00 10.17  ? 137 PRO A N   1 
ATOM   1191 C  CA  . PRO A 1 137 ? -4.357  10.735  27.141  1.00 11.41  ? 137 PRO A CA  1 
ATOM   1192 C  C   . PRO A 1 137 ? -5.775  10.296  26.953  1.00 11.55  ? 137 PRO A C   1 
ATOM   1193 O  O   . PRO A 1 137 ? -6.014  9.098   27.055  1.00 15.05  ? 137 PRO A O   1 
ATOM   1194 C  CB  . PRO A 1 137 ? -4.097  10.895  28.626  1.00 14.94  ? 137 PRO A CB  1 
ATOM   1195 C  CG  . PRO A 1 137 ? -3.698  12.260  28.762  1.00 23.18  ? 137 PRO A CG  1 
ATOM   1196 C  CD  . PRO A 1 137 ? -3.575  13.025  27.487  1.00 12.72  ? 137 PRO A CD  1 
ATOM   1197 N  N   . ASP A 1 138 ? -6.713  11.228  26.689  1.00 10.02  ? 138 ASP A N   1 
ATOM   1198 C  CA  . ASP A 1 138 ? -8.135  10.920  26.441  1.00 10.75  ? 138 ASP A CA  1 
ATOM   1199 C  C   . ASP A 1 138 ? -8.458  11.374  24.984  1.00 9.84   ? 138 ASP A C   1 
ATOM   1200 O  O   . ASP A 1 138 ? -9.554  11.814  24.741  1.00 11.12  ? 138 ASP A O   1 
ATOM   1201 C  CB  . ASP A 1 138 ? -9.040  11.605  27.440  1.00 12.31  ? 138 ASP A CB  1 
ATOM   1202 C  CG  . ASP A 1 138 ? -8.909  13.103  27.455  1.00 13.42  ? 138 ASP A CG  1 
ATOM   1203 O  OD1 . ASP A 1 138 ? -7.958  13.657  26.866  1.00 13.34  ? 138 ASP A OD1 1 
ATOM   1204 O  OD2 . ASP A 1 138 ? -9.790  13.722  28.086  1.00 18.25  ? 138 ASP A OD2 1 
ATOM   1205 N  N   . GLY A 1 139 ? -7.508  11.224  24.079  1.00 7.63   ? 139 GLY A N   1 
ATOM   1206 C  CA  . GLY A 1 139 ? -7.738  11.733  22.750  1.00 8.59   ? 139 GLY A CA  1 
ATOM   1207 C  C   . GLY A 1 139 ? -8.586  10.840  21.861  1.00 7.45   ? 139 GLY A C   1 
ATOM   1208 O  O   . GLY A 1 139 ? -9.287  11.345  20.996  1.00 7.62   ? 139 GLY A O   1 
ATOM   1209 N  N   . LEU A 1 140 ? -8.386  9.529   21.943  1.00 7.01   ? 140 LEU A N   1 
ATOM   1210 C  CA  . LEU A 1 140 ? -9.030  8.574   21.008  1.00 6.94   ? 140 LEU A CA  1 
ATOM   1211 C  C   . LEU A 1 140 ? -9.848  7.617   21.813  1.00 6.94   ? 140 LEU A C   1 
ATOM   1212 O  O   . LEU A 1 140 ? -9.561  7.311   22.977  1.00 7.41   ? 140 LEU A O   1 
ATOM   1213 C  CB  . LEU A 1 140 ? -8.000  7.803   20.181  1.00 7.74   ? 140 LEU A CB  1 
ATOM   1214 C  CG  . LEU A 1 140 ? -7.119  8.580   19.258  1.00 10.69  ? 140 LEU A CG  1 
ATOM   1215 C  CD1 . LEU A 1 140 ? -6.271  7.605   18.422  1.00 11.32  ? 140 LEU A CD1 1 
ATOM   1216 C  CD2 . LEU A 1 140 ? -7.767  9.614   18.404  1.00 12.22  ? 140 LEU A CD2 1 
ATOM   1217 N  N   . ALA A 1 141 ? -10.889 7.068   21.159  1.00 7.12   ? 141 ALA A N   1 
ATOM   1218 C  CA  . ALA A 1 141 ? -11.644 5.926   21.685  1.00 7.34   ? 141 ALA A CA  1 
ATOM   1219 C  C   . ALA A 1 141 ? -11.737 4.936   20.560  1.00 6.89   ? 141 ALA A C   1 
ATOM   1220 O  O   . ALA A 1 141 ? -12.149 5.267   19.446  1.00 7.55   ? 141 ALA A O   1 
ATOM   1221 C  CB  . ALA A 1 141 ? -13.038 6.353   22.116  1.00 8.86   ? 141 ALA A CB  1 
ATOM   1222 N  N   . VAL A 1 142 ? -11.288 3.708   20.850  1.00 6.28   ? 142 VAL A N   1 
ATOM   1223 C  CA  . VAL A 1 142 ? -11.342 2.651   19.862  1.00 6.33   ? 142 VAL A CA  1 
ATOM   1224 C  C   . VAL A 1 142 ? -12.311 1.619   20.348  1.00 5.68   ? 142 VAL A C   1 
ATOM   1225 O  O   . VAL A 1 142 ? -12.189 1.129   21.474  1.00 6.90   ? 142 VAL A O   1 
ATOM   1226 C  CB  . VAL A 1 142 ? -9.948  2.065   19.506  1.00 6.75   ? 142 VAL A CB  1 
ATOM   1227 C  CG1 . VAL A 1 142 ? -10.114 1.037   18.431  1.00 7.76   ? 142 VAL A CG1 1 
ATOM   1228 C  CG2 . VAL A 1 142 ? -8.998  3.176   19.061  1.00 8.19   ? 142 VAL A CG2 1 
ATOM   1229 N  N   . LEU A 1 143 ? -13.328 1.350   19.498  1.00 6.42   ? 143 LEU A N   1 
ATOM   1230 C  CA  . LEU A 1 143 ? -14.279 0.323   19.742  1.00 6.35   ? 143 LEU A CA  1 
ATOM   1231 C  C   . LEU A 1 143 ? -13.762 -0.943  19.047  1.00 5.92   ? 143 LEU A C   1 
ATOM   1232 O  O   . LEU A 1 143 ? -13.589 -0.959  17.851  1.00 6.83   ? 143 LEU A O   1 
ATOM   1233 C  CB  . LEU A 1 143 ? -15.632 0.749   19.202  1.00 7.82   ? 143 LEU A CB  1 
ATOM   1234 C  CG  . LEU A 1 143 ? -16.778 -0.207  19.318  1.00 8.77   ? 143 LEU A CG  1 
ATOM   1235 C  CD1 . LEU A 1 143 ? -17.049 -0.485  20.764  1.00 11.14  ? 143 LEU A CD1 1 
ATOM   1236 C  CD2 . LEU A 1 143 ? -18.082 0.368   18.687  1.00 10.79  ? 143 LEU A CD2 1 
ATOM   1237 N  N   . GLY A 1 144 ? -13.502 -1.966  19.869  1.00 6.26   ? 144 GLY A N   1 
ATOM   1238 C  CA  . GLY A 1 144 ? -12.976 -3.220  19.373  1.00 6.59   ? 144 GLY A CA  1 
ATOM   1239 C  C   . GLY A 1 144 ? -14.046 -4.317  19.416  1.00 6.15   ? 144 GLY A C   1 
ATOM   1240 O  O   . GLY A 1 144 ? -14.749 -4.457  20.380  1.00 6.95   ? 144 GLY A O   1 
ATOM   1241 N  N   . ILE A 1 145 ? -14.079 -5.055  18.307  1.00 5.66   ? 145 ILE A N   1 
ATOM   1242 C  CA  . ILE A 1 145 ? -15.091 -6.107  18.123  1.00 6.39   ? 145 ILE A CA  1 
ATOM   1243 C  C   . ILE A 1 145 ? -14.372 -7.341  17.637  1.00 5.77   ? 145 ILE A C   1 
ATOM   1244 O  O   . ILE A 1 145 ? -13.671 -7.292  16.613  1.00 6.63   ? 145 ILE A O   1 
ATOM   1245 C  CB  . ILE A 1 145 ? -16.184 -5.621  17.137  1.00 7.03   ? 145 ILE A CB  1 
ATOM   1246 C  CG1 . ILE A 1 145 ? -16.817 -4.336  17.649  1.00 8.78   ? 145 ILE A CG1 1 
ATOM   1247 C  CG2 . ILE A 1 145 ? -17.189 -6.735  16.882  1.00 8.85   ? 145 ILE A CG2 1 
ATOM   1248 C  CD1 . ILE A 1 145 ? -17.856 -3.716  16.751  1.00 9.19   ? 145 ILE A CD1 1 
ATOM   1249 N  N   . PHE A 1 146 ? -14.556 -8.435  18.324  1.00 5.93   ? 146 PHE A N   1 
ATOM   1250 C  CA  . PHE A 1 146 ? -13.968 -9.707  17.916  1.00 6.29   ? 146 PHE A CA  1 
ATOM   1251 C  C   . PHE A 1 146 ? -14.720 -10.332 16.781  1.00 6.76   ? 146 PHE A C   1 
ATOM   1252 O  O   . PHE A 1 146 ? -15.963 -10.217 16.712  1.00 7.41   ? 146 PHE A O   1 
ATOM   1253 C  CB  . PHE A 1 146 ? -13.967 -10.671 19.097  1.00 6.81   ? 146 PHE A CB  1 
ATOM   1254 C  CG  . PHE A 1 146 ? -13.130 -10.196 20.236  1.00 6.09   ? 146 PHE A CG  1 
ATOM   1255 C  CD1 . PHE A 1 146 ? -11.777 -10.016 20.093  1.00 6.94   ? 146 PHE A CD1 1 
ATOM   1256 C  CD2 . PHE A 1 146 ? -13.683 -9.944  21.491  1.00 7.46   ? 146 PHE A CD2 1 
ATOM   1257 C  CE1 . PHE A 1 146 ? -10.968 -9.641  21.160  1.00 7.67   ? 146 PHE A CE1 1 
ATOM   1258 C  CE2 . PHE A 1 146 ? -12.891 -9.581  22.536  1.00 7.77   ? 146 PHE A CE2 1 
ATOM   1259 C  CZ  . PHE A 1 146 ? -11.519 -9.439  22.404  1.00 7.58   ? 146 PHE A CZ  1 
ATOM   1260 N  N   . LEU A 1 147 ? -14.024 -11.046 15.937  1.00 6.84   ? 147 LEU A N   1 
ATOM   1261 C  CA  . LEU A 1 147 ? -14.613 -11.863 14.863  1.00 6.93   ? 147 LEU A CA  1 
ATOM   1262 C  C   . LEU A 1 147 ? -14.284 -13.314 15.107  1.00 6.86   ? 147 LEU A C   1 
ATOM   1263 O  O   . LEU A 1 147 ? -13.099 -13.681 15.294  1.00 7.76   ? 147 LEU A O   1 
ATOM   1264 C  CB  . LEU A 1 147 ? -14.040 -11.487 13.489  1.00 7.14   ? 147 LEU A CB  1 
ATOM   1265 C  CG  . LEU A 1 147 ? -14.578 -10.218 12.824  1.00 8.10   ? 147 LEU A CG  1 
ATOM   1266 C  CD1 . LEU A 1 147 ? -14.386 -8.950  13.652  1.00 8.92   ? 147 LEU A CD1 1 
ATOM   1267 C  CD2 . LEU A 1 147 ? -13.954 -10.033 11.447  1.00 8.38   ? 147 LEU A CD2 1 
ATOM   1268 N  N   . LYS A 1 148 ? -15.313 -14.160 15.059  1.00 7.87   ? 148 LYS A N   1 
ATOM   1269 C  CA  . LYS A 1 148 ? -15.137 -15.587 15.047  1.00 8.50   ? 148 LYS A CA  1 
ATOM   1270 C  C   . LYS A 1 148 ? -15.658 -16.114 13.697  1.00 8.88   ? 148 LYS A C   1 
ATOM   1271 O  O   . LYS A 1 148 ? -16.426 -15.436 13.027  1.00 9.90   ? 148 LYS A O   1 
ATOM   1272 C  CB  . LYS A 1 148 ? -15.857 -16.268 16.186  1.00 10.51  ? 148 LYS A CB  1 
ATOM   1273 C  CG  . LYS A 1 148 ? -17.386 -16.139 16.189  1.00 11.89  ? 148 LYS A CG  1 
ATOM   1274 C  CD  . LYS A 1 148 ? -18.027 -16.847 17.392  1.00 16.93  ? 148 LYS A CD  1 
ATOM   1275 C  CE  . LYS A 1 148 ? -19.523 -16.944 17.269  1.00 27.98  ? 148 LYS A CE  1 
ATOM   1276 N  NZ  . LYS A 1 148 ? -20.004 -17.936 18.302  1.00 43.70  ? 148 LYS A NZ  1 
ATOM   1277 N  N   . VAL A 1 149 ? -15.218 -17.299 13.318  1.00 9.72   ? 149 VAL A N   1 
ATOM   1278 C  CA  . VAL A 1 149 ? -15.561 -17.850 12.032  1.00 9.78   ? 149 VAL A CA  1 
ATOM   1279 C  C   . VAL A 1 149 ? -16.746 -18.811 12.145  1.00 10.71  ? 149 VAL A C   1 
ATOM   1280 O  O   . VAL A 1 149 ? -16.685 -19.785 12.911  1.00 12.36  ? 149 VAL A O   1 
ATOM   1281 C  CB  . VAL A 1 149 ? -14.327 -18.507 11.362  1.00 10.36  ? 149 VAL A CB  1 
ATOM   1282 C  CG1 . VAL A 1 149 ? -14.720 -19.232 10.060  1.00 12.90  ? 149 VAL A CG1 1 
ATOM   1283 C  CG2 . VAL A 1 149 ? -13.255 -17.489 11.162  1.00 13.68  ? 149 VAL A CG2 1 
ATOM   1284 N  N   . GLY A 1 150 ? -17.792 -18.559 11.393  1.00 10.68  ? 150 GLY A N   1 
ATOM   1285 C  CA  . GLY A 1 150 ? -18.946 -19.439 11.399  1.00 12.63  ? 150 GLY A CA  1 
ATOM   1286 C  C   . GLY A 1 150 ? -19.858 -18.954 10.310  1.00 10.54  ? 150 GLY A C   1 
ATOM   1287 O  O   . GLY A 1 150 ? -19.522 -19.020 9.136   1.00 10.53  ? 150 GLY A O   1 
ATOM   1288 N  N   A SER A 1 151 ? -21.042 -18.454 10.703  0.50 11.37  ? 151 SER A N   1 
ATOM   1289 N  N   B SER A 1 151 ? -21.031 -18.420 10.640  0.50 11.66  ? 151 SER A N   1 
ATOM   1290 C  CA  A SER A 1 151 ? -22.003 -17.809 9.763   0.50 12.09  ? 151 SER A CA  1 
ATOM   1291 C  CA  B SER A 1 151 ? -21.842 -17.824 9.567   0.50 13.07  ? 151 SER A CA  1 
ATOM   1292 C  C   A SER A 1 151 ? -21.454 -16.494 9.200   0.50 9.86   ? 151 SER A C   1 
ATOM   1293 C  C   B SER A 1 151 ? -21.241 -16.539 9.043   0.50 10.07  ? 151 SER A C   1 
ATOM   1294 O  O   A SER A 1 151 ? -20.785 -15.787 9.973   0.50 9.12   ? 151 SER A O   1 
ATOM   1295 O  O   B SER A 1 151 ? -20.464 -15.836 9.668   0.50 8.93   ? 151 SER A O   1 
ATOM   1296 C  CB  A SER A 1 151 ? -23.294 -17.468 10.500  0.50 14.52  ? 151 SER A CB  1 
ATOM   1297 C  CB  B SER A 1 151 ? -23.282 -17.524 10.025  0.50 16.17  ? 151 SER A CB  1 
ATOM   1298 O  OG  A SER A 1 151 ? -23.894 -18.606 11.033  0.50 18.75  ? 151 SER A OG  1 
ATOM   1299 O  OG  B SER A 1 151 ? -23.333 -16.734 11.212  0.50 19.39  ? 151 SER A OG  1 
ATOM   1300 N  N   . ALA A 1 152 ? -21.746 -16.165 7.911   1.00 10.79  ? 152 ALA A N   1 
ATOM   1301 C  CA  . ALA A 1 152 ? -21.336 -14.921 7.300   1.00 10.84  ? 152 ALA A CA  1 
ATOM   1302 C  C   . ALA A 1 152 ? -21.970 -13.740 8.010   1.00 9.91   ? 152 ALA A C   1 
ATOM   1303 O  O   . ALA A 1 152 ? -23.089 -13.798 8.506   1.00 11.38  ? 152 ALA A O   1 
ATOM   1304 C  CB  . ALA A 1 152 ? -21.731 -14.894 5.835   1.00 12.37  ? 152 ALA A CB  1 
ATOM   1305 N  N   . LYS A 1 153 ? -21.241 -12.596 7.937   1.00 9.04   ? 153 LYS A N   1 
ATOM   1306 C  CA  . LYS A 1 153 ? -21.802 -11.313 8.377   1.00 8.99   ? 153 LYS A CA  1 
ATOM   1307 C  C   . LYS A 1 153 ? -22.234 -10.586 7.109   1.00 9.25   ? 153 LYS A C   1 
ATOM   1308 O  O   . LYS A 1 153 ? -21.367 -10.094 6.372   1.00 8.91   ? 153 LYS A O   1 
ATOM   1309 C  CB  . LYS A 1 153 ? -20.773 -10.537 9.181   1.00 9.64   ? 153 LYS A CB  1 
ATOM   1310 C  CG  . LYS A 1 153 ? -21.345 -9.326  9.897   1.00 11.53  ? 153 LYS A CG  1 
ATOM   1311 C  CD  . LYS A 1 153 ? -22.286 -9.652  11.070  1.00 11.80  ? 153 LYS A CD  1 
ATOM   1312 C  CE  . LYS A 1 153 ? -22.554 -8.499  12.002  1.00 16.74  ? 153 LYS A CE  1 
ATOM   1313 N  NZ  . LYS A 1 153 ? -23.778 -8.779  12.826  1.00 24.36  ? 153 LYS A NZ  1 
ATOM   1314 N  N   . PRO A 1 154 ? -23.514 -10.427 6.850   1.00 9.43   ? 154 PRO A N   1 
ATOM   1315 C  CA  . PRO A 1 154 ? -23.880 -9.798  5.559   1.00 10.36  ? 154 PRO A CA  1 
ATOM   1316 C  C   . PRO A 1 154 ? -23.359 -8.410  5.404   1.00 10.13  ? 154 PRO A C   1 
ATOM   1317 O  O   . PRO A 1 154 ? -22.990 -8.063  4.298   1.00 11.05  ? 154 PRO A O   1 
ATOM   1318 C  CB  . PRO A 1 154 ? -25.440 -9.869  5.589   1.00 12.23  ? 154 PRO A CB  1 
ATOM   1319 C  CG  . PRO A 1 154 ? -25.727 -11.159 6.412   1.00 14.70  ? 154 PRO A CG  1 
ATOM   1320 C  CD  . PRO A 1 154 ? -24.701 -11.002 7.570   1.00 11.33  ? 154 PRO A CD  1 
ATOM   1321 N  N   . GLY A 1 155 ? -23.303 -7.665  6.489   1.00 10.20  ? 155 GLY A N   1 
ATOM   1322 C  CA  . GLY A 1 155 ? -22.838 -6.269  6.444   1.00 11.75  ? 155 GLY A CA  1 
ATOM   1323 C  C   . GLY A 1 155 ? -21.356 -6.130  6.158   1.00 10.23  ? 155 GLY A C   1 
ATOM   1324 O  O   . GLY A 1 155 ? -20.920 -4.992  5.949   1.00 12.06  ? 155 GLY A O   1 
ATOM   1325 N  N   . LEU A 1 156 ? -20.572 -7.209  6.221   1.00 8.57   ? 156 LEU A N   1 
ATOM   1326 C  CA  . LEU A 1 156 ? -19.174 -7.156  5.901   1.00 9.06   ? 156 LEU A CA  1 
ATOM   1327 C  C   . LEU A 1 156 ? -18.972 -7.375  4.423   1.00 8.65   ? 156 LEU A C   1 
ATOM   1328 O  O   . LEU A 1 156 ? -17.861 -7.115  3.889   1.00 8.53   ? 156 LEU A O   1 
ATOM   1329 C  CB  . LEU A 1 156 ? -18.470 -8.231  6.746   1.00 9.50   ? 156 LEU A CB  1 
ATOM   1330 C  CG  . LEU A 1 156 ? -16.937 -8.350  6.530   1.00 9.59   ? 156 LEU A CG  1 
ATOM   1331 C  CD1 . LEU A 1 156 ? -16.168 -7.065  6.832   1.00 10.28  ? 156 LEU A CD1 1 
ATOM   1332 C  CD2 . LEU A 1 156 ? -16.423 -9.517  7.345   1.00 10.76  ? 156 LEU A CD2 1 
ATOM   1333 N  N   . GLN A 1 157 ? -19.958 -7.941  3.704   1.00 8.33   ? 157 GLN A N   1 
ATOM   1334 C  CA  . GLN A 1 157 ? -19.692 -8.365  2.349   1.00 8.79   ? 157 GLN A CA  1 
ATOM   1335 C  C   . GLN A 1 157 ? -19.252 -7.266  1.413   1.00 8.39   ? 157 GLN A C   1 
ATOM   1336 O  O   . GLN A 1 157 ? -18.388 -7.500  0.574   1.00 8.91   ? 157 GLN A O   1 
ATOM   1337 C  CB  . GLN A 1 157 ? -20.907 -9.139  1.773   1.00 9.97   ? 157 GLN A CB  1 
ATOM   1338 C  CG  . GLN A 1 157 ? -20.545 -9.919  0.505   1.00 10.26  ? 157 GLN A CG  1 
ATOM   1339 C  CD  . GLN A 1 157 ? -19.535 -10.986 0.770   1.00 9.82   ? 157 GLN A CD  1 
ATOM   1340 O  OE1 . GLN A 1 157 ? -19.397 -11.544 1.882   1.00 10.42  ? 157 GLN A OE1 1 
ATOM   1341 N  NE2 . GLN A 1 157 ? -18.779 -11.256 -0.285  1.00 12.39  ? 157 GLN A NE2 1 
ATOM   1342 N  N   . LYS A 1 158 ? -19.775 -6.044  1.580   1.00 8.79   ? 158 LYS A N   1 
ATOM   1343 C  CA  . LYS A 1 158 ? -19.392 -4.959  0.665   1.00 9.40   ? 158 LYS A CA  1 
ATOM   1344 C  C   . LYS A 1 158 ? -17.885 -4.676  0.823   1.00 9.74   ? 158 LYS A C   1 
ATOM   1345 O  O   . LYS A 1 158 ? -17.225 -4.304  -0.172  1.00 10.86  ? 158 LYS A O   1 
ATOM   1346 C  CB  . LYS A 1 158 ? -20.223 -3.745  0.945   1.00 11.71  ? 158 LYS A CB  1 
ATOM   1347 C  CG  . LYS A 1 158 ? -19.979 -2.508  0.113   1.00 16.11  ? 158 LYS A CG  1 
ATOM   1348 C  CD  . LYS A 1 158 ? -20.944 -1.313  0.415   1.00 20.21  ? 158 LYS A CD  1 
ATOM   1349 C  CE  . LYS A 1 158 ? -20.444 0.004   -0.220  1.00 27.33  ? 158 LYS A CE  1 
ATOM   1350 N  NZ  . LYS A 1 158 ? -20.858 -0.040  -1.689  1.00 20.55  ? 158 LYS A NZ  1 
ATOM   1351 N  N   . VAL A 1 159 ? -17.366 -4.804  2.046   1.00 8.64   ? 159 VAL A N   1 
ATOM   1352 C  CA  . VAL A 1 159 ? -15.907 -4.619  2.273   1.00 9.08   ? 159 VAL A CA  1 
ATOM   1353 C  C   . VAL A 1 159 ? -15.137 -5.731  1.575   1.00 7.70   ? 159 VAL A C   1 
ATOM   1354 O  O   . VAL A 1 159 ? -14.213 -5.485  0.809   1.00 9.04   ? 159 VAL A O   1 
ATOM   1355 C  CB  . VAL A 1 159 ? -15.603 -4.597  3.767   1.00 9.36   ? 159 VAL A CB  1 
ATOM   1356 C  CG1 . VAL A 1 159 ? -14.079 -4.598  3.985   1.00 10.79  ? 159 VAL A CG1 1 
ATOM   1357 C  CG2 . VAL A 1 159 ? -16.183 -3.384  4.383   1.00 12.95  ? 159 VAL A CG2 1 
ATOM   1358 N  N   . VAL A 1 160 ? -15.483 -6.981  1.863   1.00 7.88   ? 160 VAL A N   1 
ATOM   1359 C  CA  . VAL A 1 160 ? -14.689 -8.064  1.280   1.00 9.21   ? 160 VAL A CA  1 
ATOM   1360 C  C   . VAL A 1 160 ? -14.693 -8.076  -0.182  1.00 8.22   ? 160 VAL A C   1 
ATOM   1361 O  O   . VAL A 1 160 ? -13.665 -8.435  -0.818  1.00 9.46   ? 160 VAL A O   1 
ATOM   1362 C  CB  . VAL A 1 160 ? -14.849 -9.439  1.967   1.00 12.28  ? 160 VAL A CB  1 
ATOM   1363 C  CG1 . VAL A 1 160 ? -14.429 -9.341  3.432   1.00 15.87  ? 160 VAL A CG1 1 
ATOM   1364 C  CG2 . VAL A 1 160 ? -16.267 -9.942  1.817   1.00 13.62  ? 160 VAL A CG2 1 
ATOM   1365 N  N   . ASP A 1 161 ? -15.807 -7.690  -0.801  1.00 9.16   ? 161 ASP A N   1 
ATOM   1366 C  CA  . ASP A 1 161 ? -15.880 -7.773  -2.285  1.00 9.63   ? 161 ASP A CA  1 
ATOM   1367 C  C   . ASP A 1 161 ? -15.034 -6.732  -2.976  1.00 10.65  ? 161 ASP A C   1 
ATOM   1368 O  O   . ASP A 1 161 ? -14.827 -6.917  -4.182  1.00 13.24  ? 161 ASP A O   1 
ATOM   1369 C  CB  . ASP A 1 161 ? -17.314 -7.658  -2.696  1.00 11.23  ? 161 ASP A CB  1 
ATOM   1370 C  CG  . ASP A 1 161 ? -18.068 -8.989  -2.657  1.00 11.37  ? 161 ASP A CG  1 
ATOM   1371 O  OD1 . ASP A 1 161 ? -17.425 -10.093 -2.682  1.00 13.08  ? 161 ASP A OD1 1 
ATOM   1372 O  OD2 . ASP A 1 161 ? -19.327 -8.964  -2.564  1.00 13.45  ? 161 ASP A OD2 1 
ATOM   1373 N  N   A VAL A 1 162 ? -14.689 -5.617  -2.286  0.50 9.11   ? 162 VAL A N   1 
ATOM   1374 N  N   B VAL A 1 162 ? -14.393 -5.776  -2.342  0.50 8.91   ? 162 VAL A N   1 
ATOM   1375 C  CA  A VAL A 1 162 ? -13.774 -4.601  -2.803  0.50 9.02   ? 162 VAL A CA  1 
ATOM   1376 C  CA  B VAL A 1 162 ? -13.567 -4.876  -3.126  0.50 8.69   ? 162 VAL A CA  1 
ATOM   1377 C  C   A VAL A 1 162 ? -12.287 -4.911  -2.606  0.50 9.18   ? 162 VAL A C   1 
ATOM   1378 C  C   B VAL A 1 162 ? -12.115 -5.131  -2.833  0.50 9.07   ? 162 VAL A C   1 
ATOM   1379 O  O   A VAL A 1 162 ? -11.500 -4.197  -3.212  0.50 8.99   ? 162 VAL A O   1 
ATOM   1380 O  O   B VAL A 1 162 ? -11.198 -4.523  -3.373  0.50 8.97   ? 162 VAL A O   1 
ATOM   1381 C  CB  A VAL A 1 162 ? -14.072 -3.172  -2.253  0.50 10.48  ? 162 VAL A CB  1 
ATOM   1382 C  CB  B VAL A 1 162 ? -13.945 -3.403  -2.871  0.50 8.63   ? 162 VAL A CB  1 
ATOM   1383 C  CG1 A VAL A 1 162 ? -13.513 -2.972  -0.827  0.50 11.65  ? 162 VAL A CG1 1 
ATOM   1384 C  CG1 B VAL A 1 162 ? -15.355 -3.113  -3.281  0.50 11.98  ? 162 VAL A CG1 1 
ATOM   1385 C  CG2 A VAL A 1 162 ? -13.624 -2.063  -3.187  0.50 14.81  ? 162 VAL A CG2 1 
ATOM   1386 C  CG2 B VAL A 1 162 ? -13.599 -2.910  -1.486  0.50 9.19   ? 162 VAL A CG2 1 
ATOM   1387 N  N   . LEU A 1 163 ? -11.853 -5.988  -1.896  1.00 9.20   ? 163 LEU A N   1 
ATOM   1388 C  CA  . LEU A 1 163 ? -10.458 -6.172  -1.524  1.00 8.96   ? 163 LEU A CA  1 
ATOM   1389 C  C   . LEU A 1 163 ? -9.600  -6.568  -2.685  1.00 8.96   ? 163 LEU A C   1 
ATOM   1390 O  O   . LEU A 1 163 ? -8.418  -6.222  -2.717  1.00 9.87   ? 163 LEU A O   1 
ATOM   1391 C  CB  . LEU A 1 163 ? -10.337 -7.153  -0.372  1.00 9.03   ? 163 LEU A CB  1 
ATOM   1392 C  CG  . LEU A 1 163 ? -10.964 -6.729  0.949   1.00 8.70   ? 163 LEU A CG  1 
ATOM   1393 C  CD1 . LEU A 1 163 ? -10.762 -7.802  2.016   1.00 9.82   ? 163 LEU A CD1 1 
ATOM   1394 C  CD2 . LEU A 1 163 ? -10.421 -5.376  1.435   1.00 10.17  ? 163 LEU A CD2 1 
ATOM   1395 N  N   . ASP A 1 164 ? -10.126 -7.247  -3.675  1.00 10.37  ? 164 ASP A N   1 
ATOM   1396 C  CA  . ASP A 1 164 ? -9.317  -7.582  -4.868  1.00 12.48  ? 164 ASP A CA  1 
ATOM   1397 C  C   . ASP A 1 164 ? -8.827  -6.356  -5.561  1.00 11.54  ? 164 ASP A C   1 
ATOM   1398 O  O   . ASP A 1 164 ? -7.821  -6.486  -6.307  1.00 14.73  ? 164 ASP A O   1 
ATOM   1399 C  CB  . ASP A 1 164 ? -10.087 -8.454  -5.857  1.00 13.75  ? 164 ASP A CB  1 
ATOM   1400 C  CG  . ASP A 1 164 ? -11.123 -7.668  -6.606  1.00 17.88  ? 164 ASP A CG  1 
ATOM   1401 O  OD1 . ASP A 1 164 ? -12.115 -7.208  -5.972  1.00 18.84  ? 164 ASP A OD1 1 
ATOM   1402 O  OD2 . ASP A 1 164 ? -10.920 -7.389  -7.844  1.00 24.93  ? 164 ASP A OD2 1 
ATOM   1403 N  N   . SER A 1 165 ? -9.449  -5.209  -5.384  1.00 11.48  ? 165 SER A N   1 
ATOM   1404 C  CA  . SER A 1 165 ? -9.000  -4.002  -6.046  1.00 11.88  ? 165 SER A CA  1 
ATOM   1405 C  C   . SER A 1 165 ? -7.852  -3.279  -5.300  1.00 10.77  ? 165 SER A C   1 
ATOM   1406 O  O   . SER A 1 165 ? -7.341  -2.255  -5.817  1.00 11.78  ? 165 SER A O   1 
ATOM   1407 C  CB  . SER A 1 165 ? -10.173 -3.094  -6.284  1.00 12.86  ? 165 SER A CB  1 
ATOM   1408 O  OG  . SER A 1 165 ? -10.586 -2.461  -5.107  1.00 12.95  ? 165 SER A OG  1 
ATOM   1409 N  N   . ILE A 1 166 ? -7.582  -3.697  -4.067  1.00 9.76   ? 166 ILE A N   1 
ATOM   1410 C  CA  . ILE A 1 166 ? -6.532  -3.091  -3.250  1.00 10.14  ? 166 ILE A CA  1 
ATOM   1411 C  C   . ILE A 1 166 ? -5.587  -4.156  -2.762  1.00 8.42   ? 166 ILE A C   1 
ATOM   1412 O  O   . ILE A 1 166 ? -5.185  -4.165  -1.568  1.00 9.58   ? 166 ILE A O   1 
ATOM   1413 C  CB  . ILE A 1 166 ? -7.151  -2.231  -2.122  1.00 9.52   ? 166 ILE A CB  1 
ATOM   1414 C  CG1 . ILE A 1 166 ? -8.041  -3.003  -1.186  1.00 9.34   ? 166 ILE A CG1 1 
ATOM   1415 C  CG2 . ILE A 1 166 ? -7.851  -0.993  -2.709  1.00 11.19  ? 166 ILE A CG2 1 
ATOM   1416 C  CD1 . ILE A 1 166 ? -8.175  -2.336  0.147   1.00 10.83  ? 166 ILE A CD1 1 
ATOM   1417 N  N   . LYS A 1 167 ? -5.157  -5.061  -3.649  1.00 9.82   ? 167 LYS A N   1 
ATOM   1418 C  CA  . LYS A 1 167 ? -4.455  -6.264  -3.150  1.00 9.21   ? 167 LYS A CA  1 
ATOM   1419 C  C   . LYS A 1 167 ? -3.093  -5.919  -2.514  1.00 9.58   ? 167 LYS A C   1 
ATOM   1420 O  O   . LYS A 1 167 ? -2.699  -6.568  -1.556  1.00 10.40  ? 167 LYS A O   1 
ATOM   1421 C  CB  . LYS A 1 167 ? -4.238  -7.207  -4.331  1.00 12.87  ? 167 LYS A CB  1 
ATOM   1422 C  CG  . LYS A 1 167 ? -3.521  -8.496  -3.944  1.00 14.66  ? 167 LYS A CG  1 
ATOM   1423 C  CD  . LYS A 1 167 ? -3.420  -9.478  -5.079  1.00 19.95  ? 167 LYS A CD  1 
ATOM   1424 C  CE  . LYS A 1 167 ? -2.076  -9.501  -5.670  1.00 28.09  ? 167 LYS A CE  1 
ATOM   1425 N  NZ  . LYS A 1 167 ? -2.100  -10.561 -6.734  1.00 29.63  ? 167 LYS A NZ  1 
ATOM   1426 N  N   . THR A 1 168 ? -2.385  -4.952  -3.072  1.00 10.54  ? 168 THR A N   1 
ATOM   1427 C  CA  . THR A 1 168 ? -0.997  -4.680  -2.648  1.00 10.18  ? 168 THR A CA  1 
ATOM   1428 C  C   . THR A 1 168 ? -0.874  -3.311  -2.023  1.00 10.59  ? 168 THR A C   1 
ATOM   1429 O  O   . THR A 1 168 ? -1.749  -2.391  -2.187  1.00 9.97   ? 168 THR A O   1 
ATOM   1430 C  CB  . THR A 1 168 ? -0.037  -4.846  -3.883  1.00 11.78  ? 168 THR A CB  1 
ATOM   1431 O  OG1 . THR A 1 168 ? -0.602  -4.059  -4.963  1.00 12.16  ? 168 THR A OG1 1 
ATOM   1432 C  CG2 . THR A 1 168 ? 0.117   -6.282  -4.304  1.00 13.44  ? 168 THR A CG2 1 
ATOM   1433 N  N   . LYS A 1 169 ? 0.236   -3.110  -1.320  1.00 10.12  ? 169 LYS A N   1 
ATOM   1434 C  CA  . LYS A 1 169 ? 0.494   -1.909  -0.563  1.00 9.69   ? 169 LYS A CA  1 
ATOM   1435 C  C   . LYS A 1 169 ? 0.424   -0.705  -1.448  1.00 9.59   ? 169 LYS A C   1 
ATOM   1436 O  O   . LYS A 1 169 ? 1.040   -0.661  -2.559  1.00 11.28  ? 169 LYS A O   1 
ATOM   1437 C  CB  . LYS A 1 169 ? 1.901   -1.998  0.008   1.00 11.40  ? 169 LYS A CB  1 
ATOM   1438 C  CG  . LYS A 1 169 ? 2.347   -0.781  0.719   1.00 10.73  ? 169 LYS A CG  1 
ATOM   1439 C  CD  . LYS A 1 169 ? 3.743   -0.949  1.315   1.00 14.10  ? 169 LYS A CD  1 
ATOM   1440 C  CE  . LYS A 1 169 ? 4.348   0.334   1.738   1.00 19.34  ? 169 LYS A CE  1 
ATOM   1441 N  NZ  . LYS A 1 169 ? 3.591   0.907   2.859   1.00 21.96  ? 169 LYS A NZ  1 
ATOM   1442 N  N   . GLY A 1 170 ? -0.273  0.330   -1.026  1.00 9.09   ? 170 GLY A N   1 
ATOM   1443 C  CA  . GLY A 1 170 ? -0.393  1.570   -1.735  1.00 10.39  ? 170 GLY A CA  1 
ATOM   1444 C  C   . GLY A 1 170 ? -1.652  1.724   -2.545  1.00 10.21  ? 170 GLY A C   1 
ATOM   1445 O  O   . GLY A 1 170 ? -1.954  2.817   -3.022  1.00 12.44  ? 170 GLY A O   1 
ATOM   1446 N  N   A LYS A 1 171 ? -2.411  0.651   -2.781  0.50 9.77   ? 171 LYS A N   1 
ATOM   1447 N  N   B LYS A 1 171 ? -2.401  0.645   -2.775  0.50 10.03  ? 171 LYS A N   1 
ATOM   1448 C  CA  A LYS A 1 171 ? -3.614  0.697   -3.616  0.50 9.59   ? 171 LYS A CA  1 
ATOM   1449 C  CA  B LYS A 1 171 ? -3.629  0.737   -3.546  0.50 10.13  ? 171 LYS A CA  1 
ATOM   1450 C  C   A LYS A 1 171 ? -4.807  1.144   -2.802  0.50 9.20   ? 171 LYS A C   1 
ATOM   1451 C  C   B LYS A 1 171 ? -4.750  1.268   -2.697  0.50 9.83   ? 171 LYS A C   1 
ATOM   1452 O  O   A LYS A 1 171 ? -5.035  0.646   -1.718  0.50 8.75   ? 171 LYS A O   1 
ATOM   1453 O  O   B LYS A 1 171 ? -4.858  0.978   -1.498  0.50 11.38  ? 171 LYS A O   1 
ATOM   1454 C  CB  A LYS A 1 171 ? -3.866  -0.653  -4.255  0.50 10.68  ? 171 LYS A CB  1 
ATOM   1455 C  CB  B LYS A 1 171 ? -3.981  -0.571  -4.232  0.50 11.21  ? 171 LYS A CB  1 
ATOM   1456 C  CG  A LYS A 1 171 ? -2.764  -1.137  -5.205  0.50 11.30  ? 171 LYS A CG  1 
ATOM   1457 C  CG  B LYS A 1 171 ? -3.103  -0.826  -5.473  0.50 14.43  ? 171 LYS A CG  1 
ATOM   1458 C  CD  A LYS A 1 171 ? -3.313  -2.208  -6.110  0.50 13.91  ? 171 LYS A CD  1 
ATOM   1459 C  CD  B LYS A 1 171 ? -3.407  -2.150  -6.109  0.50 18.59  ? 171 LYS A CD  1 
ATOM   1460 C  CE  A LYS A 1 171 ? -2.639  -2.413  -7.423  0.50 15.54  ? 171 LYS A CE  1 
ATOM   1461 C  CE  B LYS A 1 171 ? -4.194  -1.880  -7.353  0.50 20.81  ? 171 LYS A CE  1 
ATOM   1462 N  NZ  A LYS A 1 171 ? -3.727  -2.957  -8.309  0.50 23.78  ? 171 LYS A NZ  1 
ATOM   1463 N  NZ  B LYS A 1 171 ? -3.207  -1.497  -8.384  0.50 18.64  ? 171 LYS A NZ  1 
ATOM   1464 N  N   . SER A 1 172 ? -5.568  2.086   -3.339  1.00 9.80   ? 172 SER A N   1 
ATOM   1465 C  CA  . SER A 1 172 ? -6.749  2.603   -2.694  1.00 9.12   ? 172 SER A CA  1 
ATOM   1466 C  C   . SER A 1 172 ? -7.898  2.659   -3.693  1.00 9.76   ? 172 SER A C   1 
ATOM   1467 O  O   . SER A 1 172 ? -7.724  2.603   -4.929  1.00 11.31  ? 172 SER A O   1 
ATOM   1468 C  CB  . SER A 1 172 ? -6.567  3.947   -2.013  1.00 10.47  ? 172 SER A CB  1 
ATOM   1469 O  OG  . SER A 1 172 ? -6.257  4.988   -2.933  1.00 12.71  ? 172 SER A OG  1 
ATOM   1470 N  N   . ALA A 1 173 ? -9.106  2.880   -3.204  1.00 9.31   ? 173 ALA A N   1 
ATOM   1471 C  CA  . ALA A 1 173 ? -10.273 3.024   -4.048  1.00 10.31  ? 173 ALA A CA  1 
ATOM   1472 C  C   . ALA A 1 173 ? -11.311 3.876   -3.288  1.00 9.39   ? 173 ALA A C   1 
ATOM   1473 O  O   . ALA A 1 173 ? -11.346 3.908   -2.070  1.00 9.32   ? 173 ALA A O   1 
ATOM   1474 C  CB  . ALA A 1 173 ? -10.930 1.690   -4.350  1.00 11.57  ? 173 ALA A CB  1 
ATOM   1475 N  N   A ASP A 1 174 ? -12.048 4.686   -4.015  0.50 9.27   ? 174 ASP A N   1 
ATOM   1476 N  N   B ASP A 1 174 ? -12.293 4.347   -4.082  0.50 11.24  ? 174 ASP A N   1 
ATOM   1477 C  CA  A ASP A 1 174 ? -13.272 5.242   -3.458  0.50 9.50   ? 174 ASP A CA  1 
ATOM   1478 C  CA  B ASP A 1 174 ? -13.418 5.065   -3.483  0.50 10.12  ? 174 ASP A CA  1 
ATOM   1479 C  C   A ASP A 1 174 ? -14.112 4.125   -2.836  0.50 8.65   ? 174 ASP A C   1 
ATOM   1480 C  C   B ASP A 1 174 ? -14.321 4.037   -2.865  0.50 10.96  ? 174 ASP A C   1 
ATOM   1481 O  O   A ASP A 1 174 ? -14.121 3.010   -3.348  0.50 9.90   ? 174 ASP A O   1 
ATOM   1482 O  O   B ASP A 1 174 ? -14.475 2.891   -3.297  0.50 12.09  ? 174 ASP A O   1 
ATOM   1483 C  CB  A ASP A 1 174 ? -14.008 5.863   -4.637  0.50 12.98  ? 174 ASP A CB  1 
ATOM   1484 C  CB  B ASP A 1 174 ? -14.194 6.090   -4.391  0.50 12.39  ? 174 ASP A CB  1 
ATOM   1485 C  CG  A ASP A 1 174 ? -13.319 7.059   -5.143  0.50 13.52  ? 174 ASP A CG  1 
ATOM   1486 C  CG  B ASP A 1 174 ? -14.910 5.427   -5.572  0.50 16.33  ? 174 ASP A CG  1 
ATOM   1487 O  OD1 A ASP A 1 174 ? -13.126 7.974   -4.366  0.50 19.99  ? 174 ASP A OD1 1 
ATOM   1488 O  OD1 B ASP A 1 174 ? -16.091 5.054   -5.459  0.50 18.92  ? 174 ASP A OD1 1 
ATOM   1489 O  OD2 A ASP A 1 174 ? -13.024 7.184   -6.364  0.50 21.14  ? 174 ASP A OD2 1 
ATOM   1490 O  OD2 B ASP A 1 174 ? -14.260 5.345   -6.617  0.50 26.06  ? 174 ASP A OD2 1 
ATOM   1491 N  N   . PHE A 1 175 ? -14.831 4.407   -1.727  1.00 9.51   ? 175 PHE A N   1 
ATOM   1492 C  CA  . PHE A 1 175 ? -15.633 3.420   -0.996  1.00 8.88   ? 175 PHE A CA  1 
ATOM   1493 C  C   . PHE A 1 175 ? -16.710 4.151   -0.244  1.00 8.90   ? 175 PHE A C   1 
ATOM   1494 O  O   . PHE A 1 175 ? -16.565 4.456   0.940   1.00 10.17  ? 175 PHE A O   1 
ATOM   1495 C  CB  . PHE A 1 175 ? -14.720 2.598   -0.075  1.00 9.64   ? 175 PHE A CB  1 
ATOM   1496 C  CG  . PHE A 1 175 ? -15.387 1.390   0.502   1.00 8.98   ? 175 PHE A CG  1 
ATOM   1497 C  CD1 . PHE A 1 175 ? -15.728 0.313   -0.331  1.00 11.61  ? 175 PHE A CD1 1 
ATOM   1498 C  CD2 . PHE A 1 175 ? -15.695 1.298   1.814   1.00 9.63   ? 175 PHE A CD2 1 
ATOM   1499 C  CE1 . PHE A 1 175 ? -16.325 -0.833  0.180   1.00 11.85  ? 175 PHE A CE1 1 
ATOM   1500 C  CE2 . PHE A 1 175 ? -16.309 0.137   2.345   1.00 10.47  ? 175 PHE A CE2 1 
ATOM   1501 C  CZ  . PHE A 1 175 ? -16.620 -0.910  1.503   1.00 10.76  ? 175 PHE A CZ  1 
ATOM   1502 N  N   . THR A 1 176 ? -17.787 4.505   -0.922  1.00 10.14  ? 176 THR A N   1 
ATOM   1503 C  CA  . THR A 1 176 ? -18.851 5.319   -0.395  1.00 9.90   ? 176 THR A CA  1 
ATOM   1504 C  C   . THR A 1 176 ? -20.051 4.489   0.049   1.00 9.18   ? 176 THR A C   1 
ATOM   1505 O  O   . THR A 1 176 ? -20.260 3.355   -0.385  1.00 10.05  ? 176 THR A O   1 
ATOM   1506 C  CB  . THR A 1 176 ? -19.347 6.437   -1.349  1.00 11.71  ? 176 THR A CB  1 
ATOM   1507 O  OG1 . THR A 1 176 ? -19.726 5.829   -2.573  1.00 14.04  ? 176 THR A OG1 1 
ATOM   1508 C  CG2 . THR A 1 176 ? -18.215 7.408   -1.636  1.00 19.17  ? 176 THR A CG2 1 
ATOM   1509 N  N   . ASN A 1 177 ? -20.853 5.104   0.899   1.00 8.96   ? 177 ASN A N   1 
ATOM   1510 C  CA  . ASN A 1 177 ? -22.124 4.570   1.359   1.00 9.18   ? 177 ASN A CA  1 
ATOM   1511 C  C   . ASN A 1 177 ? -21.953 3.224   2.081   1.00 10.15  ? 177 ASN A C   1 
ATOM   1512 O  O   . ASN A 1 177 ? -22.873 2.411   2.063   1.00 15.27  ? 177 ASN A O   1 
ATOM   1513 C  CB  . ASN A 1 177 ? -23.179 4.437   0.246   1.00 10.69  ? 177 ASN A CB  1 
ATOM   1514 C  CG  . ASN A 1 177 ? -23.492 5.825   -0.296  1.00 10.64  ? 177 ASN A CG  1 
ATOM   1515 O  OD1 . ASN A 1 177 ? -24.173 6.584   0.312   1.00 13.99  ? 177 ASN A OD1 1 
ATOM   1516 N  ND2 . ASN A 1 177 ? -22.951 6.133   -1.420  1.00 10.85  ? 177 ASN A ND2 1 
ATOM   1517 N  N   . PHE A 1 178 ? -20.838 2.993   2.761   1.00 8.68   ? 178 PHE A N   1 
ATOM   1518 C  CA  . PHE A 1 178 ? -20.709 1.794   3.601   1.00 9.11   ? 178 PHE A CA  1 
ATOM   1519 C  C   . PHE A 1 178 ? -21.228 2.136   4.966   1.00 8.45   ? 178 PHE A C   1 
ATOM   1520 O  O   . PHE A 1 178 ? -20.808 3.113   5.584   1.00 10.16  ? 178 PHE A O   1 
ATOM   1521 C  CB  . PHE A 1 178 ? -19.256 1.341   3.645   1.00 9.92   ? 178 PHE A CB  1 
ATOM   1522 C  CG  . PHE A 1 178 ? -19.213 0.131   4.523   1.00 8.73   ? 178 PHE A CG  1 
ATOM   1523 C  CD1 . PHE A 1 178 ? -19.601 -1.123  4.015   1.00 10.27  ? 178 PHE A CD1 1 
ATOM   1524 C  CD2 . PHE A 1 178 ? -18.819 0.220   5.839   1.00 8.47   ? 178 PHE A CD2 1 
ATOM   1525 C  CE1 . PHE A 1 178 ? -19.665 -2.209  4.840   1.00 10.27  ? 178 PHE A CE1 1 
ATOM   1526 C  CE2 . PHE A 1 178 ? -18.858 -0.954  6.664   1.00 8.71   ? 178 PHE A CE2 1 
ATOM   1527 C  CZ  . PHE A 1 178 ? -19.280 -2.124  6.187   1.00 9.62   ? 178 PHE A CZ  1 
ATOM   1528 N  N   . ASP A 1 179 ? -22.128 1.301   5.473   1.00 8.88   ? 179 ASP A N   1 
ATOM   1529 C  CA  . ASP A 1 179 ? -22.750 1.563   6.764   1.00 8.84   ? 179 ASP A CA  1 
ATOM   1530 C  C   . ASP A 1 179 ? -22.104 0.690   7.828   1.00 8.26   ? 179 ASP A C   1 
ATOM   1531 O  O   . ASP A 1 179 ? -22.333 -0.508  7.905   1.00 9.46   ? 179 ASP A O   1 
ATOM   1532 C  CB  . ASP A 1 179 ? -24.255 1.245   6.679   1.00 10.90  ? 179 ASP A CB  1 
ATOM   1533 C  CG  . ASP A 1 179 ? -25.003 1.615   7.909   1.00 12.32  ? 179 ASP A CG  1 
ATOM   1534 O  OD1 . ASP A 1 179 ? -24.437 1.870   8.989   1.00 11.50  ? 179 ASP A OD1 1 
ATOM   1535 O  OD2 . ASP A 1 179 ? -26.262 1.665   7.839   1.00 18.97  ? 179 ASP A OD2 1 
ATOM   1536 N  N   . PRO A 1 180 ? -21.327 1.286   8.755   1.00 8.06   ? 180 PRO A N   1 
ATOM   1537 C  CA  . PRO A 1 180 ? -20.630 0.455   9.767   1.00 8.95   ? 180 PRO A CA  1 
ATOM   1538 C  C   . PRO A 1 180 ? -21.558 -0.144  10.778  1.00 9.02   ? 180 PRO A C   1 
ATOM   1539 O  O   . PRO A 1 180 ? -21.122 -1.028  11.517  1.00 9.26   ? 180 PRO A O   1 
ATOM   1540 C  CB  . PRO A 1 180 ? -19.630 1.455   10.343  1.00 10.16  ? 180 PRO A CB  1 
ATOM   1541 C  CG  . PRO A 1 180 ? -20.260 2.792   10.161  1.00 11.11  ? 180 PRO A CG  1 
ATOM   1542 C  CD  . PRO A 1 180 ? -20.958 2.703   8.830   1.00 9.76   ? 180 PRO A CD  1 
ATOM   1543 N  N   . ARG A 1 181 ? -22.813 0.277   10.829  1.00 8.91   ? 181 ARG A N   1 
ATOM   1544 C  CA  . ARG A 1 181 ? -23.778 -0.404  11.741  1.00 9.10   ? 181 ARG A CA  1 
ATOM   1545 C  C   . ARG A 1 181 ? -23.891 -1.898  11.374  1.00 9.19   ? 181 ARG A C   1 
ATOM   1546 O  O   . ARG A 1 181 ? -24.244 -2.678  12.270  1.00 9.64   ? 181 ARG A O   1 
ATOM   1547 C  CB  . ARG A 1 181 ? -25.126 0.248   11.717  1.00 9.51   ? 181 ARG A CB  1 
ATOM   1548 C  CG  . ARG A 1 181 ? -25.083 1.657   12.251  1.00 12.08  ? 181 ARG A CG  1 
ATOM   1549 C  CD  . ARG A 1 181 ? -26.367 2.413   12.200  1.00 13.46  ? 181 ARG A CD  1 
ATOM   1550 N  NE  . ARG A 1 181 ? -26.709 2.607   10.838  1.00 12.71  ? 181 ARG A NE  1 
ATOM   1551 C  CZ  . ARG A 1 181 ? -27.754 3.318   10.460  1.00 15.92  ? 181 ARG A CZ  1 
ATOM   1552 N  NH1 . ARG A 1 181 ? -28.566 3.842   11.369  1.00 20.61  ? 181 ARG A NH1 1 
ATOM   1553 N  NH2 . ARG A 1 181 ? -27.979 3.545   9.162   1.00 17.09  ? 181 ARG A NH2 1 
ATOM   1554 N  N   . GLY A 1 182 ? -23.630 -2.254  10.127  1.00 8.80   ? 182 GLY A N   1 
ATOM   1555 C  CA  . GLY A 1 182 ? -23.740 -3.677  9.765   1.00 10.68  ? 182 GLY A CA  1 
ATOM   1556 C  C   . GLY A 1 182 ? -22.621 -4.567  10.286  1.00 10.08  ? 182 GLY A C   1 
ATOM   1557 O  O   . GLY A 1 182 ? -22.625 -5.732  10.006  1.00 11.26  ? 182 GLY A O   1 
ATOM   1558 N  N   . LEU A 1 183 ? -21.660 -3.973  11.003  1.00 9.45   ? 183 LEU A N   1 
ATOM   1559 C  CA  . LEU A 1 183 ? -20.526 -4.698  11.588  1.00 9.53   ? 183 LEU A CA  1 
ATOM   1560 C  C   . LEU A 1 183 ? -20.700 -4.901  13.066  1.00 9.35   ? 183 LEU A C   1 
ATOM   1561 O  O   . LEU A 1 183 ? -19.807 -5.515  13.684  1.00 10.44  ? 183 LEU A O   1 
ATOM   1562 C  CB  . LEU A 1 183 ? -19.226 -3.972  11.320  1.00 9.14   ? 183 LEU A CB  1 
ATOM   1563 C  CG  . LEU A 1 183 ? -18.897 -3.823  9.856   1.00 10.06  ? 183 LEU A CG  1 
ATOM   1564 C  CD1 . LEU A 1 183 ? -17.644 -3.004  9.744   1.00 12.49  ? 183 LEU A CD1 1 
ATOM   1565 C  CD2 . LEU A 1 183 ? -18.785 -5.112  9.074   1.00 13.29  ? 183 LEU A CD2 1 
ATOM   1566 N  N   . LEU A 1 184 ? -21.805 -4.460  13.672  1.00 9.32   ? 184 LEU A N   1 
ATOM   1567 C  CA  . LEU A 1 184 ? -21.928 -4.503  15.101  1.00 9.39   ? 184 LEU A CA  1 
ATOM   1568 C  C   . LEU A 1 184 ? -22.728 -5.722  15.612  1.00 10.72  ? 184 LEU A C   1 
ATOM   1569 O  O   . LEU A 1 184 ? -23.702 -6.120  14.997  1.00 14.95  ? 184 LEU A O   1 
ATOM   1570 C  CB  . LEU A 1 184 ? -22.666 -3.271  15.632  1.00 9.15   ? 184 LEU A CB  1 
ATOM   1571 C  CG  . LEU A 1 184 ? -22.089 -1.896  15.203  1.00 9.68   ? 184 LEU A CG  1 
ATOM   1572 C  CD1 . LEU A 1 184 ? -22.944 -0.735  15.683  1.00 12.18  ? 184 LEU A CD1 1 
ATOM   1573 C  CD2 . LEU A 1 184 ? -20.666 -1.776  15.695  1.00 13.21  ? 184 LEU A CD2 1 
ATOM   1574 N  N   . PRO A 1 185 ? -22.321 -6.317  16.729  1.00 9.49   ? 185 PRO A N   1 
ATOM   1575 C  CA  . PRO A 1 185 ? -23.094 -7.429  17.324  1.00 9.53   ? 185 PRO A CA  1 
ATOM   1576 C  C   . PRO A 1 185 ? -24.373 -6.862  17.974  1.00 9.04   ? 185 PRO A C   1 
ATOM   1577 O  O   . PRO A 1 185 ? -24.561 -5.643  18.077  1.00 10.76  ? 185 PRO A O   1 
ATOM   1578 C  CB  . PRO A 1 185 ? -22.108 -8.030  18.351  1.00 10.14  ? 185 PRO A CB  1 
ATOM   1579 C  CG  . PRO A 1 185 ? -21.382 -6.787  18.822  1.00 8.87   ? 185 PRO A CG  1 
ATOM   1580 C  CD  . PRO A 1 185 ? -21.179 -5.959  17.584  1.00 8.87   ? 185 PRO A CD  1 
ATOM   1581 N  N   . GLU A 1 186 ? -25.242 -7.751  18.455  1.00 10.80  ? 186 GLU A N   1 
ATOM   1582 C  CA  . GLU A 1 186 ? -26.472 -7.299  19.133  1.00 11.54  ? 186 GLU A CA  1 
ATOM   1583 C  C   . GLU A 1 186 ? -26.210 -6.507  20.363  1.00 10.99  ? 186 GLU A C   1 
ATOM   1584 O  O   . GLU A 1 186 ? -26.777 -5.447  20.588  1.00 11.94  ? 186 GLU A O   1 
ATOM   1585 C  CB  . GLU A 1 186 ? -27.278 -8.535  19.595  1.00 14.28  ? 186 GLU A CB  1 
ATOM   1586 C  CG  . GLU A 1 186 ? -28.002 -9.235  18.513  1.00 15.77  ? 186 GLU A CG  1 
ATOM   1587 C  CD  . GLU A 1 186 ? -28.752 -10.464 18.986  1.00 17.66  ? 186 GLU A CD  1 
ATOM   1588 O  OE1 . GLU A 1 186 ? -28.806 -10.730 20.179  1.00 20.46  ? 186 GLU A OE1 1 
ATOM   1589 O  OE2 . GLU A 1 186 ? -29.300 -11.127 18.088  1.00 23.37  ? 186 GLU A OE2 1 
ATOM   1590 N  N   . SER A 1 187 ? -25.328 -7.062  21.234  1.00 10.50  ? 187 SER A N   1 
ATOM   1591 C  CA  . SER A 1 187 ? -25.096 -6.439  22.523  1.00 10.54  ? 187 SER A CA  1 
ATOM   1592 C  C   . SER A 1 187 ? -23.945 -5.414  22.469  1.00 9.77   ? 187 SER A C   1 
ATOM   1593 O  O   . SER A 1 187 ? -22.931 -5.640  21.828  1.00 10.83  ? 187 SER A O   1 
ATOM   1594 C  CB  . SER A 1 187 ? -24.681 -7.518  23.534  1.00 12.15  ? 187 SER A CB  1 
ATOM   1595 O  OG  . SER A 1 187 ? -24.443 -6.954  24.807  1.00 13.11  ? 187 SER A OG  1 
ATOM   1596 N  N   . LEU A 1 188 ? -24.119 -4.332  23.196  1.00 10.89  ? 188 LEU A N   1 
ATOM   1597 C  CA  . LEU A 1 188 ? -23.072 -3.354  23.431  1.00 10.88  ? 188 LEU A CA  1 
ATOM   1598 C  C   . LEU A 1 188 ? -22.460 -3.522  24.838  1.00 10.73  ? 188 LEU A C   1 
ATOM   1599 O  O   . LEU A 1 188 ? -21.746 -2.572  25.289  1.00 12.96  ? 188 LEU A O   1 
ATOM   1600 C  CB  . LEU A 1 188 ? -23.569 -1.894  23.176  1.00 11.92  ? 188 LEU A CB  1 
ATOM   1601 C  CG  . LEU A 1 188 ? -23.930 -1.572  21.731  1.00 12.31  ? 188 LEU A CG  1 
ATOM   1602 C  CD1 . LEU A 1 188 ? -24.471 -0.116  21.707  1.00 16.10  ? 188 LEU A CD1 1 
ATOM   1603 C  CD2 . LEU A 1 188 ? -22.825 -1.819  20.752  1.00 15.32  ? 188 LEU A CD2 1 
ATOM   1604 N  N   . ASP A 1 189 ? -22.583 -4.677  25.469  1.00 10.30  ? 189 ASP A N   1 
ATOM   1605 C  CA  . ASP A 1 189 ? -21.829 -4.902  26.717  1.00 11.01  ? 189 ASP A CA  1 
ATOM   1606 C  C   . ASP A 1 189 ? -20.336 -4.855  26.416  1.00 9.25   ? 189 ASP A C   1 
ATOM   1607 O  O   . ASP A 1 189 ? -19.903 -5.395  25.398  1.00 9.10   ? 189 ASP A O   1 
ATOM   1608 C  CB  . ASP A 1 189 ? -22.201 -6.233  27.296  1.00 13.54  ? 189 ASP A CB  1 
ATOM   1609 C  CG  . ASP A 1 189 ? -23.616 -6.258  27.959  1.00 15.89  ? 189 ASP A CG  1 
ATOM   1610 O  OD1 . ASP A 1 189 ? -24.216 -5.206  28.049  1.00 23.93  ? 189 ASP A OD1 1 
ATOM   1611 O  OD2 . ASP A 1 189 ? -23.991 -7.329  28.303  1.00 24.06  ? 189 ASP A OD2 1 
ATOM   1612 N  N   . TYR A 1 190 ? -19.561 -4.270  27.311  1.00 8.95   ? 190 TYR A N   1 
ATOM   1613 C  CA  . TYR A 1 190 ? -18.168 -4.028  27.005  1.00 8.66   ? 190 TYR A CA  1 
ATOM   1614 C  C   . TYR A 1 190 ? -17.281 -4.098  28.249  1.00 7.68   ? 190 TYR A C   1 
ATOM   1615 O  O   . TYR A 1 190 ? -17.714 -3.932  29.379  1.00 9.02   ? 190 TYR A O   1 
ATOM   1616 C  CB  . TYR A 1 190 ? -17.984 -2.629  26.281  1.00 9.28   ? 190 TYR A CB  1 
ATOM   1617 C  CG  . TYR A 1 190 ? -18.375 -1.477  27.163  1.00 8.54   ? 190 TYR A CG  1 
ATOM   1618 C  CD1 . TYR A 1 190 ? -17.468 -0.850  28.031  1.00 9.59   ? 190 TYR A CD1 1 
ATOM   1619 C  CD2 . TYR A 1 190 ? -19.670 -0.942  27.118  1.00 9.81   ? 190 TYR A CD2 1 
ATOM   1620 C  CE1 . TYR A 1 190 ? -17.868 0.199   28.854  1.00 10.31  ? 190 TYR A CE1 1 
ATOM   1621 C  CE2 . TYR A 1 190 ? -20.063 0.099   27.922  1.00 10.62  ? 190 TYR A CE2 1 
ATOM   1622 C  CZ  . TYR A 1 190 ? -19.164 0.688   28.806  1.00 11.44  ? 190 TYR A CZ  1 
ATOM   1623 O  OH  . TYR A 1 190 ? -19.476 1.734   29.617  1.00 12.69  ? 190 TYR A OH  1 
ATOM   1624 N  N   . TRP A 1 191 ? -15.970 -4.239  27.904  1.00 7.52   ? 191 TRP A N   1 
ATOM   1625 C  CA  . TRP A 1 191 ? -14.875 -3.990  28.820  1.00 7.77   ? 191 TRP A CA  1 
ATOM   1626 C  C   . TRP A 1 191 ? -14.178 -2.711  28.419  1.00 7.03   ? 191 TRP A C   1 
ATOM   1627 O  O   . TRP A 1 191 ? -14.143 -2.378  27.224  1.00 8.27   ? 191 TRP A O   1 
ATOM   1628 C  CB  . TRP A 1 191 ? -13.850 -5.121  28.840  1.00 8.65   ? 191 TRP A CB  1 
ATOM   1629 C  CG  . TRP A 1 191 ? -14.386 -6.442  29.261  1.00 8.00   ? 191 TRP A CG  1 
ATOM   1630 C  CD1 . TRP A 1 191 ? -14.605 -6.864  30.536  1.00 9.77   ? 191 TRP A CD1 1 
ATOM   1631 C  CD2 . TRP A 1 191 ? -14.667 -7.564  28.377  1.00 8.33   ? 191 TRP A CD2 1 
ATOM   1632 N  NE1 . TRP A 1 191 ? -15.025 -8.168  30.531  1.00 10.12  ? 191 TRP A NE1 1 
ATOM   1633 C  CE2 . TRP A 1 191 ? -15.081 -8.642  29.262  1.00 9.57   ? 191 TRP A CE2 1 
ATOM   1634 C  CE3 . TRP A 1 191 ? -14.580 -7.771  27.013  1.00 8.89   ? 191 TRP A CE3 1 
ATOM   1635 C  CZ2 . TRP A 1 191 ? -15.407 -9.903  28.720  1.00 10.65  ? 191 TRP A CZ2 1 
ATOM   1636 C  CZ3 . TRP A 1 191 ? -14.860 -9.038  26.530  1.00 9.88   ? 191 TRP A CZ3 1 
ATOM   1637 C  CH2 . TRP A 1 191 ? -15.230 -10.061 27.334  1.00 10.39  ? 191 TRP A CH2 1 
ATOM   1638 N  N   . THR A 1 192 ? -13.609 -1.993  29.396  1.00 7.52   ? 192 THR A N   1 
ATOM   1639 C  CA  . THR A 1 192 ? -12.905 -0.791  29.037  1.00 7.82   ? 192 THR A CA  1 
ATOM   1640 C  C   . THR A 1 192 ? -11.653 -0.608  29.926  1.00 7.20   ? 192 THR A C   1 
ATOM   1641 O  O   . THR A 1 192 ? -11.632 -0.995  31.085  1.00 8.19   ? 192 THR A O   1 
ATOM   1642 C  CB  . THR A 1 192 ? -13.833 0.454   29.175  1.00 8.32   ? 192 THR A CB  1 
ATOM   1643 O  OG1 . THR A 1 192 ? -13.119 1.635   28.723  1.00 8.14   ? 192 THR A OG1 1 
ATOM   1644 C  CG2 . THR A 1 192 ? -14.365 0.693   30.532  1.00 9.40   ? 192 THR A CG2 1 
ATOM   1645 N  N   . TYR A 1 193 ? -10.614 -0.009  29.307  1.00 7.47   ? 193 TYR A N   1 
ATOM   1646 C  CA  . TYR A 1 193 ? -9.382  0.272   30.063  1.00 7.52   ? 193 TYR A CA  1 
ATOM   1647 C  C   . TYR A 1 193 ? -8.638  1.326   29.269  1.00 7.44   ? 193 TYR A C   1 
ATOM   1648 O  O   . TYR A 1 193 ? -8.834  1.495   28.057  1.00 7.26   ? 193 TYR A O   1 
ATOM   1649 C  CB  . TYR A 1 193 ? -8.551  -1.009  30.263  1.00 7.52   ? 193 TYR A CB  1 
ATOM   1650 C  CG  . TYR A 1 193 ? -7.869  -1.508  28.996  1.00 7.49   ? 193 TYR A CG  1 
ATOM   1651 C  CD1 . TYR A 1 193 ? -8.573  -2.233  28.017  1.00 7.14   ? 193 TYR A CD1 1 
ATOM   1652 C  CD2 . TYR A 1 193 ? -6.548  -1.161  28.723  1.00 7.81   ? 193 TYR A CD2 1 
ATOM   1653 C  CE1 . TYR A 1 193 ? -7.972  -2.594  26.849  1.00 6.97   ? 193 TYR A CE1 1 
ATOM   1654 C  CE2 . TYR A 1 193 ? -5.916  -1.525  27.559  1.00 7.52   ? 193 TYR A CE2 1 
ATOM   1655 C  CZ  . TYR A 1 193 ? -6.648  -2.217  26.575  1.00 6.74   ? 193 TYR A CZ  1 
ATOM   1656 O  OH  . TYR A 1 193 ? -5.993  -2.504  25.440  1.00 7.23   ? 193 TYR A OH  1 
ATOM   1657 N  N   . PRO A 1 194 ? -7.683  2.035   29.939  1.00 7.39   ? 194 PRO A N   1 
ATOM   1658 C  CA  . PRO A 1 194 ? -6.841  3.016   29.266  1.00 7.48   ? 194 PRO A CA  1 
ATOM   1659 C  C   . PRO A 1 194 ? -5.652  2.346   28.590  1.00 6.91   ? 194 PRO A C   1 
ATOM   1660 O  O   . PRO A 1 194 ? -4.915  1.567   29.229  1.00 7.69   ? 194 PRO A O   1 
ATOM   1661 C  CB  . PRO A 1 194 ? -6.354  3.927   30.382  1.00 8.83   ? 194 PRO A CB  1 
ATOM   1662 C  CG  . PRO A 1 194 ? -6.352  2.984   31.616  1.00 9.88   ? 194 PRO A CG  1 
ATOM   1663 C  CD  . PRO A 1 194 ? -7.510  2.077   31.401  1.00 8.67   ? 194 PRO A CD  1 
ATOM   1664 N  N   . GLY A 1 195 ? -5.435  2.643   27.330  1.00 6.69   ? 195 GLY A N   1 
ATOM   1665 C  CA  . GLY A 1 195 ? -4.344  2.016   26.598  1.00 7.44   ? 195 GLY A CA  1 
ATOM   1666 C  C   . GLY A 1 195 ? -3.783  2.892   25.507  1.00 6.32   ? 195 GLY A C   1 
ATOM   1667 O  O   . GLY A 1 195 ? -3.643  4.111   25.629  1.00 7.16   ? 195 GLY A O   1 
ATOM   1668 N  N   . SER A 1 196 ? -3.403  2.219   24.436  1.00 6.75   ? 196 SER A N   1 
ATOM   1669 C  CA  . SER A 1 196 ? -2.539  2.854   23.417  1.00 7.14   ? 196 SER A CA  1 
ATOM   1670 C  C   . SER A 1 196 ? -3.004  2.470   22.014  1.00 6.26   ? 196 SER A C   1 
ATOM   1671 O  O   . SER A 1 196 ? -3.767  1.488   21.832  1.00 6.80   ? 196 SER A O   1 
ATOM   1672 C  CB  . SER A 1 196 ? -1.080  2.466   23.600  1.00 7.46   ? 196 SER A CB  1 
ATOM   1673 O  OG  . SER A 1 196 ? -0.837  1.121   23.174  1.00 7.10   ? 196 SER A OG  1 
ATOM   1674 N  N   . LEU A 1 197 ? -2.450  3.136   21.023  1.00 6.77   ? 197 LEU A N   1 
ATOM   1675 C  CA  . LEU A 1 197 ? -2.425  2.579   19.666  1.00 6.88   ? 197 LEU A CA  1 
ATOM   1676 C  C   . LEU A 1 197 ? -1.727  1.254   19.681  1.00 7.11   ? 197 LEU A C   1 
ATOM   1677 O  O   . LEU A 1 197 ? -0.754  1.065   20.444  1.00 7.40   ? 197 LEU A O   1 
ATOM   1678 C  CB  . LEU A 1 197 ? -1.641  3.508   18.760  1.00 8.13   ? 197 LEU A CB  1 
ATOM   1679 C  CG  . LEU A 1 197 ? -2.125  4.976   18.739  1.00 11.26  ? 197 LEU A CG  1 
ATOM   1680 C  CD1 . LEU A 1 197 ? -1.247  5.761   17.733  1.00 12.50  ? 197 LEU A CD1 1 
ATOM   1681 C  CD2 . LEU A 1 197 ? -3.540  5.073   18.340  1.00 12.72  ? 197 LEU A CD2 1 
ATOM   1682 N  N   . THR A 1 198 ? -2.139  0.319   18.827  1.00 7.05   ? 198 THR A N   1 
ATOM   1683 C  CA  . THR A 1 198 ? -1.459  -0.951  18.730  1.00 7.44   ? 198 THR A CA  1 
ATOM   1684 C  C   . THR A 1 198 ? -0.466  -1.055  17.594  1.00 7.02   ? 198 THR A C   1 
ATOM   1685 O  O   . THR A 1 198 ? 0.105   -2.130  17.397  1.00 7.82   ? 198 THR A O   1 
ATOM   1686 C  CB  . THR A 1 198 ? -2.452  -2.123  18.693  1.00 6.71   ? 198 THR A CB  1 
ATOM   1687 O  OG1 . THR A 1 198 ? -3.076  -2.100  17.434  1.00 6.88   ? 198 THR A OG1 1 
ATOM   1688 C  CG2 . THR A 1 198 ? -3.431  -2.111  19.851  1.00 8.23   ? 198 THR A CG2 1 
ATOM   1689 N  N   . THR A 1 199 ? -0.264  0.037   16.862  1.00 8.05   ? 199 THR A N   1 
ATOM   1690 C  CA  . THR A 1 199 ? 0.844   0.139   15.921  1.00 8.27   ? 199 THR A CA  1 
ATOM   1691 C  C   . THR A 1 199 ? 1.616   1.392   16.243  1.00 8.26   ? 199 THR A C   1 
ATOM   1692 O  O   . THR A 1 199 ? 1.108   2.350   16.829  1.00 8.59   ? 199 THR A O   1 
ATOM   1693 C  CB  . THR A 1 199 ? 0.330   0.282   14.470  1.00 9.44   ? 199 THR A CB  1 
ATOM   1694 O  OG1 . THR A 1 199 ? -0.629  1.334   14.381  1.00 10.68  ? 199 THR A OG1 1 
ATOM   1695 C  CG2 . THR A 1 199 ? -0.231  -1.046  14.007  1.00 11.21  ? 199 THR A CG2 1 
ATOM   1696 N  N   . PRO A 1 200 ? 2.879   1.415   15.782  1.00 9.00   ? 200 PRO A N   1 
ATOM   1697 C  CA  . PRO A 1 200 ? 3.665   2.665   15.842  1.00 9.53   ? 200 PRO A CA  1 
ATOM   1698 C  C   . PRO A 1 200 ? 2.836   3.823   15.302  1.00 9.96   ? 200 PRO A C   1 
ATOM   1699 O  O   . PRO A 1 200 ? 2.174   3.701   14.271  1.00 11.42  ? 200 PRO A O   1 
ATOM   1700 C  CB  . PRO A 1 200 ? 4.864   2.322   14.938  1.00 11.83  ? 200 PRO A CB  1 
ATOM   1701 C  CG  . PRO A 1 200 ? 5.066   0.871   15.218  1.00 11.18  ? 200 PRO A CG  1 
ATOM   1702 C  CD  . PRO A 1 200 ? 3.636   0.314   15.161  1.00 9.99   ? 200 PRO A CD  1 
ATOM   1703 N  N   . PRO A 1 201 ? 2.827   4.962   16.018  1.00 10.15  ? 201 PRO A N   1 
ATOM   1704 C  CA  . PRO A 1 201 ? 3.796   5.324   17.098  1.00 10.25  ? 201 PRO A CA  1 
ATOM   1705 C  C   . PRO A 1 201 ? 3.435   4.869   18.484  1.00 8.70   ? 201 PRO A C   1 
ATOM   1706 O  O   . PRO A 1 201 ? 4.128   5.256   19.435  1.00 9.76   ? 201 PRO A O   1 
ATOM   1707 C  CB  . PRO A 1 201 ? 3.826   6.866   17.021  1.00 11.52  ? 201 PRO A CB  1 
ATOM   1708 C  CG  . PRO A 1 201 ? 2.359   7.177   16.527  1.00 16.22  ? 201 PRO A CG  1 
ATOM   1709 C  CD  . PRO A 1 201 ? 2.117   6.124   15.477  1.00 12.92  ? 201 PRO A CD  1 
ATOM   1710 N  N   . LEU A 1 202 ? 2.360   4.083   18.653  1.00 7.67   ? 202 LEU A N   1 
ATOM   1711 C  CA  . LEU A 1 202 ? 2.081   3.437   19.961  1.00 7.94   ? 202 LEU A CA  1 
ATOM   1712 C  C   . LEU A 1 202 ? 1.639   4.437   21.027  1.00 7.76   ? 202 LEU A C   1 
ATOM   1713 O  O   . LEU A 1 202 ? 1.717   4.150   22.202  1.00 7.72   ? 202 LEU A O   1 
ATOM   1714 C  CB  . LEU A 1 202 ? 3.203   2.533   20.434  1.00 8.22   ? 202 LEU A CB  1 
ATOM   1715 C  CG  . LEU A 1 202 ? 3.527   1.402   19.462  1.00 8.22   ? 202 LEU A CG  1 
ATOM   1716 C  CD1 . LEU A 1 202 ? 4.840   0.734   19.902  1.00 9.31   ? 202 LEU A CD1 1 
ATOM   1717 C  CD2 . LEU A 1 202 ? 2.429   0.342   19.359  1.00 8.45   ? 202 LEU A CD2 1 
ATOM   1718 N  N   . ASN A 1 203 ? 1.145   5.603   20.610  1.00 8.40   ? 203 ASN A N   1 
ATOM   1719 C  CA  . ASN A 1 203 ? 0.796   6.663   21.536  1.00 8.75   ? 203 ASN A CA  1 
ATOM   1720 C  C   . ASN A 1 203 ? -0.173  6.158   22.573  1.00 8.18   ? 203 ASN A C   1 
ATOM   1721 O  O   . ASN A 1 203 ? -1.169  5.438   22.271  1.00 8.20   ? 203 ASN A O   1 
ATOM   1722 C  CB  . ASN A 1 203 ? 0.128   7.797   20.780  1.00 10.16  ? 203 ASN A CB  1 
ATOM   1723 C  CG  . ASN A 1 203 ? 1.054   8.541   19.857  1.00 11.86  ? 203 ASN A CG  1 
ATOM   1724 O  OD1 . ASN A 1 203 ? 2.167   8.130   19.593  1.00 16.94  ? 203 ASN A OD1 1 
ATOM   1725 N  ND2 . ASN A 1 203 ? 0.633   9.709   19.405  1.00 15.76  ? 203 ASN A ND2 1 
ATOM   1726 N  N   . GLU A 1 204 ? -0.006  6.619   23.784  1.00 8.85   ? 204 GLU A N   1 
ATOM   1727 C  CA  . GLU A 1 204 ? -0.842  6.242   24.906  1.00 8.82   ? 204 GLU A CA  1 
ATOM   1728 C  C   . GLU A 1 204 ? -2.026  7.201   25.044  1.00 7.93   ? 204 GLU A C   1 
ATOM   1729 O  O   . GLU A 1 204 ? -2.141  7.967   26.003  1.00 9.72   ? 204 GLU A O   1 
ATOM   1730 C  CB  . GLU A 1 204 ? 0.011   6.136   26.161  1.00 9.09   ? 204 GLU A CB  1 
ATOM   1731 C  CG  . GLU A 1 204 ? 0.868   4.883   26.097  1.00 9.53   ? 204 GLU A CG  1 
ATOM   1732 C  CD  . GLU A 1 204 ? 1.806   4.600   27.260  1.00 9.58   ? 204 GLU A CD  1 
ATOM   1733 O  OE1 . GLU A 1 204 ? 2.114   5.545   28.019  1.00 12.37  ? 204 GLU A OE1 1 
ATOM   1734 O  OE2 . GLU A 1 204 ? 2.205   3.401   27.432  1.00 9.96   ? 204 GLU A OE2 1 
ATOM   1735 N  N   . CYS A 1 205 ? -2.909  7.137   24.067  1.00 8.02   ? 205 CYS A N   1 
ATOM   1736 C  CA  . CYS A 1 205 ? -3.944  8.158   23.864  1.00 7.76   ? 205 CYS A CA  1 
ATOM   1737 C  C   . CYS A 1 205 ? -5.298  7.505   23.714  1.00 7.67   ? 205 CYS A C   1 
ATOM   1738 O  O   . CYS A 1 205 ? -6.243  8.219   23.330  1.00 9.37   ? 205 CYS A O   1 
ATOM   1739 C  CB  . CYS A 1 205 ? -3.660  8.959   22.636  1.00 8.77   ? 205 CYS A CB  1 
ATOM   1740 S  SG  . CYS A 1 205 ? -3.571  8.006   21.102  1.00 9.43   ? 205 CYS A SG  1 
ATOM   1741 N  N   . VAL A 1 206 ? -5.460  6.203   24.029  1.00 7.09   ? 206 VAL A N   1 
ATOM   1742 C  CA  . VAL A 1 206 ? -6.730  5.507   23.683  1.00 7.05   ? 206 VAL A CA  1 
ATOM   1743 C  C   . VAL A 1 206 ? -7.474  5.090   24.886  1.00 7.21   ? 206 VAL A C   1 
ATOM   1744 O  O   . VAL A 1 206 ? -6.944  4.408   25.772  1.00 8.64   ? 206 VAL A O   1 
ATOM   1745 C  CB  . VAL A 1 206 ? -6.436  4.267   22.790  1.00 8.05   ? 206 VAL A CB  1 
ATOM   1746 C  CG1 . VAL A 1 206 ? -7.757  3.565   22.477  1.00 7.81   ? 206 VAL A CG1 1 
ATOM   1747 C  CG2 . VAL A 1 206 ? -5.703  4.633   21.518  1.00 8.14   ? 206 VAL A CG2 1 
ATOM   1748 N  N   . THR A 1 207 ? -8.802  5.373   24.949  1.00 7.02   ? 207 THR A N   1 
ATOM   1749 C  CA  . THR A 1 207 ? -9.726  4.677   25.789  1.00 7.70   ? 207 THR A CA  1 
ATOM   1750 C  C   . THR A 1 207 ? -10.257 3.494   24.984  1.00 6.49   ? 207 THR A C   1 
ATOM   1751 O  O   . THR A 1 207 ? -10.929 3.690   23.961  1.00 7.39   ? 207 THR A O   1 
ATOM   1752 C  CB  . THR A 1 207 ? -10.918 5.555   26.253  1.00 8.66   ? 207 THR A CB  1 
ATOM   1753 O  OG1 . THR A 1 207 ? -10.381 6.687   26.952  1.00 9.55   ? 207 THR A OG1 1 
ATOM   1754 C  CG2 . THR A 1 207 ? -11.815 4.789   27.142  1.00 9.50   ? 207 THR A CG2 1 
ATOM   1755 N  N   . TRP A 1 208 ? -9.895  2.299   25.392  1.00 6.29   ? 208 TRP A N   1 
ATOM   1756 C  CA  . TRP A 1 208 ? -10.375 1.082   24.704  1.00 6.12   ? 208 TRP A CA  1 
ATOM   1757 C  C   . TRP A 1 208 ? -11.733 0.684   25.216  1.00 6.05   ? 208 TRP A C   1 
ATOM   1758 O  O   . TRP A 1 208 ? -11.953 0.645   26.421  1.00 6.86   ? 208 TRP A O   1 
ATOM   1759 C  CB  . TRP A 1 208 ? -9.365  -0.055  24.919  1.00 6.64   ? 208 TRP A CB  1 
ATOM   1760 C  CG  . TRP A 1 208 ? -8.250  0.035   23.971  1.00 6.51   ? 208 TRP A CG  1 
ATOM   1761 C  CD1 . TRP A 1 208 ? -6.990  0.630   24.104  1.00 7.05   ? 208 TRP A CD1 1 
ATOM   1762 C  CD2 . TRP A 1 208 ? -8.312  -0.387  22.577  1.00 6.09   ? 208 TRP A CD2 1 
ATOM   1763 N  NE1 . TRP A 1 208 ? -6.304  0.583   22.938  1.00 7.35   ? 208 TRP A NE1 1 
ATOM   1764 C  CE2 . TRP A 1 208 ? -7.069  -0.028  21.975  1.00 6.45   ? 208 TRP A CE2 1 
ATOM   1765 C  CE3 . TRP A 1 208 ? -9.260  -1.028  21.822  1.00 6.86   ? 208 TRP A CE3 1 
ATOM   1766 C  CZ2 . TRP A 1 208 ? -6.809  -0.280  20.655  1.00 7.52   ? 208 TRP A CZ2 1 
ATOM   1767 C  CZ3 . TRP A 1 208 ? -9.005  -1.326  20.520  1.00 7.38   ? 208 TRP A CZ3 1 
ATOM   1768 C  CH2 . TRP A 1 208 ? -7.779  -0.978  19.947  1.00 8.12   ? 208 TRP A CH2 1 
ATOM   1769 N  N   . ILE A 1 209 ? -12.609 0.311   24.289  1.00 6.33   ? 209 ILE A N   1 
ATOM   1770 C  CA  . ILE A 1 209 ? -13.923 -0.197  24.593  1.00 6.69   ? 209 ILE A CA  1 
ATOM   1771 C  C   . ILE A 1 209 ? -14.038 -1.495  23.772  1.00 5.80   ? 209 ILE A C   1 
ATOM   1772 O  O   . ILE A 1 209 ? -14.123 -1.399  22.543  1.00 7.12   ? 209 ILE A O   1 
ATOM   1773 C  CB  . ILE A 1 209 ? -14.990 0.826   24.210  1.00 7.27   ? 209 ILE A CB  1 
ATOM   1774 C  CG1 . ILE A 1 209 ? -14.769 2.132   25.017  1.00 8.96   ? 209 ILE A CG1 1 
ATOM   1775 C  CG2 . ILE A 1 209 ? -16.399 0.227   24.460  1.00 8.88   ? 209 ILE A CG2 1 
ATOM   1776 C  CD1 . ILE A 1 209 ? -15.577 3.272   24.481  1.00 11.43  ? 209 ILE A CD1 1 
ATOM   1777 N  N   . VAL A 1 210 ? -13.996 -2.649  24.402  1.00 6.33   ? 210 VAL A N   1 
ATOM   1778 C  CA  . VAL A 1 210 ? -13.954 -3.911  23.718  1.00 6.09   ? 210 VAL A CA  1 
ATOM   1779 C  C   . VAL A 1 210 ? -15.277 -4.618  23.984  1.00 6.47   ? 210 VAL A C   1 
ATOM   1780 O  O   . VAL A 1 210 ? -15.629 -4.894  25.121  1.00 7.09   ? 210 VAL A O   1 
ATOM   1781 C  CB  . VAL A 1 210 ? -12.767 -4.769  24.185  1.00 6.60   ? 210 VAL A CB  1 
ATOM   1782 C  CG1 . VAL A 1 210 ? -12.793 -6.122  23.508  1.00 8.08   ? 210 VAL A CG1 1 
ATOM   1783 C  CG2 . VAL A 1 210 ? -11.468 -4.057  23.884  1.00 8.19   ? 210 VAL A CG2 1 
ATOM   1784 N  N   . LEU A 1 211 ? -16.010 -4.892  22.907  1.00 6.89   ? 211 LEU A N   1 
ATOM   1785 C  CA  . LEU A 1 211 ? -17.331 -5.550  23.111  1.00 7.14   ? 211 LEU A CA  1 
ATOM   1786 C  C   . LEU A 1 211 ? -17.166 -6.983  23.513  1.00 7.69   ? 211 LEU A C   1 
ATOM   1787 O  O   . LEU A 1 211 ? -16.313 -7.720  22.966  1.00 7.92   ? 211 LEU A O   1 
ATOM   1788 C  CB  . LEU A 1 211 ? -18.161 -5.429  21.816  1.00 7.81   ? 211 LEU A CB  1 
ATOM   1789 C  CG  . LEU A 1 211 ? -18.522 -4.035  21.400  1.00 8.07   ? 211 LEU A CG  1 
ATOM   1790 C  CD1 . LEU A 1 211 ? -19.549 -4.104  20.292  1.00 10.35  ? 211 LEU A CD1 1 
ATOM   1791 C  CD2 . LEU A 1 211 ? -19.043 -3.169  22.527  1.00 8.88   ? 211 LEU A CD2 1 
ATOM   1792 N  N   . LYS A 1 212 ? -18.016 -7.471  24.416  1.00 8.15   ? 212 LYS A N   1 
ATOM   1793 C  CA  . LYS A 1 212 ? -17.987 -8.851  24.816  1.00 9.18   ? 212 LYS A CA  1 
ATOM   1794 C  C   . LYS A 1 212 ? -18.454 -9.803  23.740  1.00 8.49   ? 212 LYS A C   1 
ATOM   1795 O  O   . LYS A 1 212 ? -17.943 -10.900 23.638  1.00 10.79  ? 212 LYS A O   1 
ATOM   1796 C  CB  . LYS A 1 212 ? -18.778 -9.061  26.073  1.00 12.37  ? 212 LYS A CB  1 
ATOM   1797 C  CG  . LYS A 1 212 ? -18.907 -10.523 26.464  1.00 17.76  ? 212 LYS A CG  1 
ATOM   1798 C  CD  . LYS A 1 212 ? -19.722 -10.725 27.711  1.00 24.72  ? 212 LYS A CD  1 
ATOM   1799 C  CE  . LYS A 1 212 ? -21.080 -9.956  27.572  1.00 39.94  ? 212 LYS A CE  1 
ATOM   1800 N  NZ  . LYS A 1 212 ? -22.362 -10.514 28.202  1.00 61.47  ? 212 LYS A NZ  1 
ATOM   1801 N  N   A GLU A 1 213 ? -19.454 -9.404  22.971  0.50 8.18   ? 213 GLU A N   1 
ATOM   1802 N  N   B GLU A 1 213 ? -19.442 -9.408  22.955  0.50 8.13   ? 213 GLU A N   1 
ATOM   1803 C  CA  A GLU A 1 213 ? -20.107 -10.281 22.002  0.50 8.19   ? 213 GLU A CA  1 
ATOM   1804 C  CA  B GLU A 1 213 ? -20.000 -10.311 21.964  0.50 8.52   ? 213 GLU A CA  1 
ATOM   1805 C  C   A GLU A 1 213 ? -19.359 -10.220 20.670  0.50 7.49   ? 213 GLU A C   1 
ATOM   1806 C  C   B GLU A 1 213 ? -19.237 -10.211 20.672  0.50 7.92   ? 213 GLU A C   1 
ATOM   1807 O  O   A GLU A 1 213 ? -19.310 -9.141  20.092  0.50 7.95   ? 213 GLU A O   1 
ATOM   1808 O  O   B GLU A 1 213 ? -19.152 -9.133  20.105  0.50 7.92   ? 213 GLU A O   1 
ATOM   1809 C  CB  A GLU A 1 213 ? -21.542 -9.823  21.772  0.50 9.30   ? 213 GLU A CB  1 
ATOM   1810 C  CB  B GLU A 1 213 ? -21.464 -10.042 21.690  0.50 8.95   ? 213 GLU A CB  1 
ATOM   1811 C  CG  A GLU A 1 213 ? -22.339 -10.785 20.935  0.50 9.50   ? 213 GLU A CG  1 
ATOM   1812 C  CG  B GLU A 1 213 ? -22.083 -11.019 20.734  0.50 11.39  ? 213 GLU A CG  1 
ATOM   1813 C  CD  A GLU A 1 213 ? -23.798 -10.314 20.630  0.50 11.21  ? 213 GLU A CD  1 
ATOM   1814 C  CD  B GLU A 1 213 ? -23.596 -10.845 20.560  0.50 12.22  ? 213 GLU A CD  1 
ATOM   1815 O  OE1 A GLU A 1 213 ? -24.399 -9.748  21.571  0.50 11.76  ? 213 GLU A OE1 1 
ATOM   1816 O  OE1 B GLU A 1 213 ? -24.194 -9.818  20.975  0.50 10.78  ? 213 GLU A OE1 1 
ATOM   1817 O  OE2 A GLU A 1 213 ? -24.289 -10.466 19.438  0.50 13.95  ? 213 GLU A OE2 1 
ATOM   1818 O  OE2 B GLU A 1 213 ? -24.207 -11.729 19.928  0.50 16.91  ? 213 GLU A OE2 1 
ATOM   1819 N  N   A PRO A 1 214 ? -18.807 -11.344 20.156  0.50 7.72   ? 214 PRO A N   1 
ATOM   1820 N  N   B PRO A 1 214 ? -18.672 -11.318 20.199  0.50 8.14   ? 214 PRO A N   1 
ATOM   1821 C  CA  A PRO A 1 214 ? -18.156 -11.269 18.867  0.50 7.61   ? 214 PRO A CA  1 
ATOM   1822 C  CA  B PRO A 1 214 ? -18.051 -11.331 18.882  0.50 8.79   ? 214 PRO A CA  1 
ATOM   1823 C  C   A PRO A 1 214 ? -19.193 -11.170 17.789  0.50 7.54   ? 214 PRO A C   1 
ATOM   1824 C  C   B PRO A 1 214 ? -19.095 -11.325 17.733  0.50 8.75   ? 214 PRO A C   1 
ATOM   1825 O  O   A PRO A 1 214 ? -20.385 -11.505 18.056  0.50 8.11   ? 214 PRO A O   1 
ATOM   1826 O  O   B PRO A 1 214 ? -20.203 -11.833 17.866  0.50 9.34   ? 214 PRO A O   1 
ATOM   1827 C  CB  A PRO A 1 214 ? -17.460 -12.624 18.749  0.50 8.19   ? 214 PRO A CB  1 
ATOM   1828 C  CB  B PRO A 1 214 ? -17.263 -12.650 18.901  0.50 9.91   ? 214 PRO A CB  1 
ATOM   1829 C  CG  A PRO A 1 214 ? -18.254 -13.533 19.625  0.50 8.51   ? 214 PRO A CG  1 
ATOM   1830 C  CG  B PRO A 1 214 ? -17.229 -13.087 20.325  0.50 11.80  ? 214 PRO A CG  1 
ATOM   1831 C  CD  A PRO A 1 214 ? -18.835 -12.720 20.712  0.50 8.12   ? 214 PRO A CD  1 
ATOM   1832 C  CD  B PRO A 1 214 ? -18.441 -12.562 20.987  0.50 9.21   ? 214 PRO A CD  1 
ATOM   1833 N  N   . ILE A 1 215 ? -18.754 -10.822 16.577  1.00 7.91   ? 215 ILE A N   1 
ATOM   1834 C  CA  . ILE A 1 215 ? -19.554 -11.085 15.382  1.00 7.96   ? 215 ILE A CA  1 
ATOM   1835 C  C   . ILE A 1 215 ? -19.021 -12.337 14.750  1.00 7.89   ? 215 ILE A C   1 
ATOM   1836 O  O   . ILE A 1 215 ? -17.832 -12.698 14.879  1.00 9.80   ? 215 ILE A O   1 
ATOM   1837 C  CB  . ILE A 1 215 ? -19.548 -9.889  14.407  1.00 8.71   ? 215 ILE A CB  1 
ATOM   1838 C  CG1 . ILE A 1 215 ? -18.140 -9.507  13.895  1.00 8.75   ? 215 ILE A CG1 1 
ATOM   1839 C  CG2 . ILE A 1 215 ? -20.209 -8.675  15.054  1.00 9.19   ? 215 ILE A CG2 1 
ATOM   1840 C  CD1 . ILE A 1 215 ? -18.190 -8.604  12.720  1.00 10.14  ? 215 ILE A CD1 1 
ATOM   1841 N  N   A SER A 1 216 ? -19.969 -13.068 14.150  0.50 8.92   ? 216 SER A N   1 
ATOM   1842 N  N   B SER A 1 216 ? -19.778 -12.995 13.879  0.50 8.20   ? 216 SER A N   1 
ATOM   1843 C  CA  A SER A 1 216 ? -19.670 -14.126 13.164  0.50 8.75   ? 216 SER A CA  1 
ATOM   1844 C  CA  B SER A 1 216 ? -19.340 -14.183 13.207  0.50 8.50   ? 216 SER A CA  1 
ATOM   1845 C  C   A SER A 1 216 ? -19.313 -13.669 11.725  0.50 8.14   ? 216 SER A C   1 
ATOM   1846 C  C   B SER A 1 216 ? -19.322 -13.774 11.803  0.50 8.30   ? 216 SER A C   1 
ATOM   1847 O  O   A SER A 1 216 ? -20.047 -12.885 11.096  0.50 8.60   ? 216 SER A O   1 
ATOM   1848 O  O   B SER A 1 216 ? -20.284 -13.076 11.344  0.50 8.71   ? 216 SER A O   1 
ATOM   1849 C  CB  A SER A 1 216 ? -20.830 -15.192 13.181  0.50 11.00  ? 216 SER A CB  1 
ATOM   1850 C  CB  B SER A 1 216 ? -20.408 -15.288 13.412  0.50 11.02  ? 216 SER A CB  1 
ATOM   1851 O  OG  A SER A 1 216 ? -20.691 -15.905 14.415  0.50 12.14  ? 216 SER A OG  1 
ATOM   1852 O  OG  B SER A 1 216 ? -20.224 -16.334 12.571  0.50 14.26  ? 216 SER A OG  1 
ATOM   1853 N  N   . VAL A 1 217 ? -18.213 -14.161 11.160  1.00 8.46   ? 217 VAL A N   1 
ATOM   1854 C  CA  . VAL A 1 217 ? -17.958 -14.007 9.745   1.00 8.04   ? 217 VAL A CA  1 
ATOM   1855 C  C   . VAL A 1 217 ? -17.732 -15.347 9.155   1.00 7.94   ? 217 VAL A C   1 
ATOM   1856 O  O   . VAL A 1 217 ? -17.357 -16.303 9.876   1.00 9.21   ? 217 VAL A O   1 
ATOM   1857 C  CB  . VAL A 1 217 ? -16.753 -13.066 9.495   1.00 9.00   ? 217 VAL A CB  1 
ATOM   1858 C  CG1 . VAL A 1 217 ? -17.021 -11.690 10.135  1.00 9.56   ? 217 VAL A CG1 1 
ATOM   1859 C  CG2 . VAL A 1 217 ? -15.463 -13.673 10.037  1.00 10.88  ? 217 VAL A CG2 1 
ATOM   1860 N  N   . SER A 1 218 ? -17.898 -15.487 7.860   1.00 8.26   ? 218 SER A N   1 
ATOM   1861 C  CA  . SER A 1 218 ? -17.666 -16.830 7.252   1.00 8.72   ? 218 SER A CA  1 
ATOM   1862 C  C   . SER A 1 218 ? -16.224 -17.067 6.931   1.00 8.09   ? 218 SER A C   1 
ATOM   1863 O  O   . SER A 1 218 ? -15.429 -16.133 6.744   1.00 8.90   ? 218 SER A O   1 
ATOM   1864 C  CB  . SER A 1 218 ? -18.546 -17.046 6.022   1.00 9.25   ? 218 SER A CB  1 
ATOM   1865 O  OG  . SER A 1 218 ? -18.155 -16.101 5.051   1.00 9.70   ? 218 SER A OG  1 
ATOM   1866 N  N   . SER A 1 219 ? -15.893 -18.319 6.715   1.00 9.48   ? 219 SER A N   1 
ATOM   1867 C  CA  . SER A 1 219 ? -14.596 -18.671 6.285   1.00 9.59   ? 219 SER A CA  1 
ATOM   1868 C  C   . SER A 1 219 ? -14.305 -18.010 4.939   1.00 9.95   ? 219 SER A C   1 
ATOM   1869 O  O   . SER A 1 219 ? -13.177 -17.577 4.699   1.00 10.74  ? 219 SER A O   1 
ATOM   1870 C  CB  . SER A 1 219 ? -14.488 -20.194 6.239   1.00 12.62  ? 219 SER A CB  1 
ATOM   1871 O  OG  . SER A 1 219 ? -15.442 -20.783 5.283   1.00 12.89  ? 219 SER A OG  1 
ATOM   1872 N  N   . GLU A 1 220 ? -15.290 -17.905 4.034   1.00 9.69   ? 220 GLU A N   1 
ATOM   1873 C  CA  . GLU A 1 220 ? -15.059 -17.238 2.763   1.00 10.47  ? 220 GLU A CA  1 
ATOM   1874 C  C   . GLU A 1 220 ? -14.688 -15.769 2.935   1.00 9.27   ? 220 GLU A C   1 
ATOM   1875 O  O   . GLU A 1 220 ? -13.874 -15.244 2.175   1.00 10.97  ? 220 GLU A O   1 
ATOM   1876 C  CB  . GLU A 1 220 ? -16.231 -17.347 1.767   1.00 11.41  ? 220 GLU A CB  1 
ATOM   1877 C  CG  . GLU A 1 220 ? -16.517 -18.748 1.231   1.00 13.20  ? 220 GLU A CG  1 
ATOM   1878 C  CD  . GLU A 1 220 ? -17.494 -19.458 2.148   1.00 15.49  ? 220 GLU A CD  1 
ATOM   1879 O  OE1 . GLU A 1 220 ? -17.836 -19.055 3.255   1.00 14.07  ? 220 GLU A OE1 1 
ATOM   1880 O  OE2 . GLU A 1 220 ? -18.009 -20.508 1.694   1.00 25.28  ? 220 GLU A OE2 1 
ATOM   1881 N  N   . GLN A 1 221 ? -15.332 -15.118 3.894   1.00 8.46   ? 221 GLN A N   1 
ATOM   1882 C  CA  . GLN A 1 221 ? -15.042 -13.710 4.146   1.00 8.52   ? 221 GLN A CA  1 
ATOM   1883 C  C   . GLN A 1 221 ? -13.586 -13.565 4.646   1.00 8.92   ? 221 GLN A C   1 
ATOM   1884 O  O   . GLN A 1 221 ? -12.837 -12.695 4.132   1.00 9.14   ? 221 GLN A O   1 
ATOM   1885 C  CB  . GLN A 1 221 ? -16.040 -13.132 5.096   1.00 8.07   ? 221 GLN A CB  1 
ATOM   1886 C  CG  . GLN A 1 221 ? -17.441 -13.003 4.455   1.00 8.44   ? 221 GLN A CG  1 
ATOM   1887 C  CD  . GLN A 1 221 ? -18.477 -12.486 5.355   1.00 7.98   ? 221 GLN A CD  1 
ATOM   1888 O  OE1 . GLN A 1 221 ? -18.577 -12.839 6.547   1.00 8.24   ? 221 GLN A OE1 1 
ATOM   1889 N  NE2 . GLN A 1 221 ? -19.336 -11.585 4.810   1.00 9.32   ? 221 GLN A NE2 1 
ATOM   1890 N  N   A VAL A 1 222 ? -13.231 -14.225 5.759   0.50 8.24   ? 222 VAL A N   1 
ATOM   1891 N  N   B VAL A 1 222 ? -13.145 -14.467 5.515   0.50 8.48   ? 222 VAL A N   1 
ATOM   1892 C  CA  A VAL A 1 222 ? -11.818 -14.147 6.201   0.50 9.99   ? 222 VAL A CA  1 
ATOM   1893 C  CA  B VAL A 1 222 ? -11.867 -14.275 6.159   0.50 9.69   ? 222 VAL A CA  1 
ATOM   1894 C  C   A VAL A 1 222 ? -10.837 -14.709 5.070   0.50 9.86   ? 222 VAL A C   1 
ATOM   1895 C  C   B VAL A 1 222 ? -10.781 -14.559 5.216   0.50 10.01  ? 222 VAL A C   1 
ATOM   1896 O  O   A VAL A 1 222 ? -9.721  -14.202 4.894   0.50 9.35   ? 222 VAL A O   1 
ATOM   1897 O  O   B VAL A 1 222 ? -9.731  -13.933 5.309   0.50 9.58   ? 222 VAL A O   1 
ATOM   1898 C  CB  A VAL A 1 222 ? -11.704 -14.644 7.676   0.50 11.56  ? 222 VAL A CB  1 
ATOM   1899 C  CB  B VAL A 1 222 ? -11.642 -15.125 7.395   0.50 10.22  ? 222 VAL A CB  1 
ATOM   1900 C  CG1 A VAL A 1 222 ? -11.716 -16.143 7.679   0.50 12.35  ? 222 VAL A CG1 1 
ATOM   1901 C  CG1 B VAL A 1 222 ? -12.586 -14.775 8.471   0.50 13.04  ? 222 VAL A CG1 1 
ATOM   1902 C  CG2 A VAL A 1 222 ? -10.431 -14.195 8.384   0.50 12.15  ? 222 VAL A CG2 1 
ATOM   1903 C  CG2 B VAL A 1 222 ? -11.746 -16.571 7.153   0.50 18.15  ? 222 VAL A CG2 1 
ATOM   1904 N  N   A LEU A 1 223 ? -11.216 -15.687 4.251   0.50 10.46  ? 223 LEU A N   1 
ATOM   1905 N  N   B LEU A 1 223 ? -11.052 -15.524 4.357   0.50 10.49  ? 223 LEU A N   1 
ATOM   1906 C  CA  A LEU A 1 223 ? -10.227 -16.025 3.224   0.50 11.84  ? 223 LEU A CA  1 
ATOM   1907 C  CA  B LEU A 1 223 ? -10.159 -15.944 3.346   0.50 12.76  ? 223 LEU A CA  1 
ATOM   1908 C  C   A LEU A 1 223 ? -9.879  -14.828 2.322   0.50 11.14  ? 223 LEU A C   1 
ATOM   1909 C  C   B LEU A 1 223 ? -9.862  -14.807 2.353   0.50 11.24  ? 223 LEU A C   1 
ATOM   1910 O  O   A LEU A 1 223 ? -8.688  -14.671 1.881   0.50 12.38  ? 223 LEU A O   1 
ATOM   1911 O  O   B LEU A 1 223 ? -8.686  -14.667 1.867   0.50 12.35  ? 223 LEU A O   1 
ATOM   1912 C  CB  A LEU A 1 223 ? -10.465 -17.334 2.461   0.50 18.20  ? 223 LEU A CB  1 
ATOM   1913 C  CB  B LEU A 1 223 ? -10.734 -17.174 2.692   0.50 13.98  ? 223 LEU A CB  1 
ATOM   1914 C  CG  A LEU A 1 223 ? -10.239 -18.512 3.489   0.50 18.14  ? 223 LEU A CG  1 
ATOM   1915 C  CG  B LEU A 1 223 ? -10.509 -18.562 3.514   0.50 21.66  ? 223 LEU A CG  1 
ATOM   1916 C  CD1 A LEU A 1 223 ? -11.157 -19.725 3.248   0.50 24.56  ? 223 LEU A CD1 1 
ATOM   1917 C  CD1 B LEU A 1 223 ? -10.741 -18.896 5.092   0.50 17.69  ? 223 LEU A CD1 1 
ATOM   1918 C  CD2 A LEU A 1 223 ? -8.791  -18.950 3.821   0.50 22.07  ? 223 LEU A CD2 1 
ATOM   1919 C  CD2 B LEU A 1 223 ? -11.215 -19.605 2.636   0.50 31.45  ? 223 LEU A CD2 1 
ATOM   1920 N  N   . LYS A 1 224 ? -10.822 -13.936 2.079   1.00 10.12  ? 224 LYS A N   1 
ATOM   1921 C  CA  . LYS A 1 224 ? -10.546 -12.747 1.270   1.00 11.90  ? 224 LYS A CA  1 
ATOM   1922 C  C   . LYS A 1 224 ? -9.619  -11.774 2.007   1.00 9.60   ? 224 LYS A C   1 
ATOM   1923 O  O   . LYS A 1 224 ? -8.760  -11.188 1.311   1.00 10.74  ? 224 LYS A O   1 
ATOM   1924 C  CB  . LYS A 1 224 ? -11.872 -12.084 0.856   1.00 13.83  ? 224 LYS A CB  1 
ATOM   1925 C  CG  . LYS A 1 224 ? -12.671 -12.956 -0.067  1.00 16.94  ? 224 LYS A CG  1 
ATOM   1926 C  CD  . LYS A 1 224 ? -13.898 -12.174 -0.667  1.00 25.87  ? 224 LYS A CD  1 
ATOM   1927 C  CE  . LYS A 1 224 ? -14.435 -12.584 -2.068  1.00 33.48  ? 224 LYS A CE  1 
ATOM   1928 N  NZ  . LYS A 1 224 ? -14.704 -14.064 -2.106  1.00 37.73  ? 224 LYS A NZ  1 
ATOM   1929 N  N   . PHE A 1 225 ? -9.715  -11.601 3.329   1.00 9.03   ? 225 PHE A N   1 
ATOM   1930 C  CA  . PHE A 1 225 ? -8.739  -10.815 4.054   1.00 8.43   ? 225 PHE A CA  1 
ATOM   1931 C  C   . PHE A 1 225 ? -7.346  -11.388 3.773   1.00 9.30   ? 225 PHE A C   1 
ATOM   1932 O  O   . PHE A 1 225 ? -6.382  -10.633 3.551   1.00 9.36   ? 225 PHE A O   1 
ATOM   1933 C  CB  . PHE A 1 225 ? -8.947  -10.840 5.514   1.00 9.12   ? 225 PHE A CB  1 
ATOM   1934 C  CG  . PHE A 1 225 ? -10.112 -10.079 6.114   1.00 8.72   ? 225 PHE A CG  1 
ATOM   1935 C  CD1 . PHE A 1 225 ? -11.044 -9.398  5.392   1.00 12.03  ? 225 PHE A CD1 1 
ATOM   1936 C  CD2 . PHE A 1 225 ? -10.206 -10.031 7.493   1.00 12.13  ? 225 PHE A CD2 1 
ATOM   1937 C  CE1 . PHE A 1 225 ? -12.066 -8.671  6.011   1.00 12.61  ? 225 PHE A CE1 1 
ATOM   1938 C  CE2 . PHE A 1 225 ? -11.195 -9.274  8.109   1.00 14.04  ? 225 PHE A CE2 1 
ATOM   1939 C  CZ  . PHE A 1 225 ? -12.133 -8.621  7.325   1.00 11.95  ? 225 PHE A CZ  1 
ATOM   1940 N  N   . ARG A 1 226 ? -7.215  -12.707 3.845   1.00 8.80   ? 226 ARG A N   1 
ATOM   1941 C  CA  . ARG A 1 226 ? -5.904  -13.354 3.756   1.00 9.86   ? 226 ARG A CA  1 
ATOM   1942 C  C   . ARG A 1 226 ? -5.340  -13.392 2.349   1.00 9.65   ? 226 ARG A C   1 
ATOM   1943 O  O   . ARG A 1 226 ? -4.187  -13.815 2.201   1.00 11.48  ? 226 ARG A O   1 
ATOM   1944 C  CB  . ARG A 1 226 ? -6.060  -14.810 4.304   1.00 9.59   ? 226 ARG A CB  1 
ATOM   1945 C  CG  . ARG A 1 226 ? -6.431  -14.886 5.757   1.00 9.36   ? 226 ARG A CG  1 
ATOM   1946 C  CD  . ARG A 1 226 ? -6.472  -16.319 6.218   1.00 11.78  ? 226 ARG A CD  1 
ATOM   1947 N  NE  . ARG A 1 226 ? -6.863  -16.455 7.616   1.00 9.19   ? 226 ARG A NE  1 
ATOM   1948 C  CZ  . ARG A 1 226 ? -7.675  -17.375 8.091   1.00 11.27  ? 226 ARG A CZ  1 
ATOM   1949 N  NH1 . ARG A 1 226 ? -8.056  -18.414 7.298   1.00 15.18  ? 226 ARG A NH1 1 
ATOM   1950 N  NH2 . ARG A 1 226 ? -8.033  -17.328 9.323   1.00 14.13  ? 226 ARG A NH2 1 
ATOM   1951 N  N   . LYS A 1 227 ? -6.075  -12.932 1.338   1.00 9.67   ? 227 LYS A N   1 
ATOM   1952 C  CA  . LYS A 1 227 ? -5.563  -12.793 0.008   1.00 10.37  ? 227 LYS A CA  1 
ATOM   1953 C  C   . LYS A 1 227 ? -4.886  -11.466 -0.224  1.00 10.02  ? 227 LYS A C   1 
ATOM   1954 O  O   . LYS A 1 227 ? -4.209  -11.266 -1.254  1.00 11.06  ? 227 LYS A O   1 
ATOM   1955 C  CB  . LYS A 1 227 ? -6.714  -12.976 -1.003  1.00 12.01  ? 227 LYS A CB  1 
ATOM   1956 C  CG  . LYS A 1 227 ? -7.177  -14.402 -1.174  1.00 17.58  ? 227 LYS A CG  1 
ATOM   1957 C  CD  . LYS A 1 227 ? -8.323  -14.516 -2.197  1.00 28.05  ? 227 LYS A CD  1 
ATOM   1958 C  CE  . LYS A 1 227 ? -9.114  -15.849 -2.001  1.00 38.42  ? 227 LYS A CE  1 
ATOM   1959 N  NZ  . LYS A 1 227 ? -10.584 -15.934 -2.305  1.00 52.80  ? 227 LYS A NZ  1 
ATOM   1960 N  N   . LEU A 1 228 ? -5.035  -10.499 0.692   1.00 9.60   ? 228 LEU A N   1 
ATOM   1961 C  CA  . LEU A 1 228 ? -4.322  -9.280  0.570   1.00 8.92   ? 228 LEU A CA  1 
ATOM   1962 C  C   . LEU A 1 228 ? -2.823  -9.546  0.722   1.00 9.00   ? 228 LEU A C   1 
ATOM   1963 O  O   . LEU A 1 228 ? -2.393  -10.589 1.198   1.00 9.39   ? 228 LEU A O   1 
ATOM   1964 C  CB  . LEU A 1 228 ? -4.792  -8.307  1.679   1.00 9.36   ? 228 LEU A CB  1 
ATOM   1965 C  CG  . LEU A 1 228 ? -6.181  -7.788  1.487   1.00 9.18   ? 228 LEU A CG  1 
ATOM   1966 C  CD1 . LEU A 1 228 ? -6.644  -7.113  2.751   1.00 9.85   ? 228 LEU A CD1 1 
ATOM   1967 C  CD2 . LEU A 1 228 ? -6.262  -6.826  0.275   1.00 11.37  ? 228 LEU A CD2 1 
ATOM   1968 N  N   . ASN A 1 229 ? -2.028  -8.593  0.242   1.00 9.10   ? 229 ASN A N   1 
ATOM   1969 C  CA  . ASN A 1 229 ? -0.540  -8.693  0.345   1.00 9.02   ? 229 ASN A CA  1 
ATOM   1970 C  C   . ASN A 1 229 ? -0.021  -7.536  1.186   1.00 8.95   ? 229 ASN A C   1 
ATOM   1971 O  O   . ASN A 1 229 ? -0.466  -6.384  1.084   1.00 9.50   ? 229 ASN A O   1 
ATOM   1972 C  CB  . ASN A 1 229 ? 0.055   -8.510  -1.049  1.00 10.54  ? 229 ASN A CB  1 
ATOM   1973 C  CG  . ASN A 1 229 ? -0.101  -9.668  -1.960  1.00 11.77  ? 229 ASN A CG  1 
ATOM   1974 O  OD1 . ASN A 1 229 ? 0.428   -9.557  -3.073  1.00 17.68  ? 229 ASN A OD1 1 
ATOM   1975 N  ND2 . ASN A 1 229 ? -0.806  -10.747 -1.622  1.00 14.60  ? 229 ASN A ND2 1 
ATOM   1976 N  N   . PHE A 1 230 ? 1.018   -7.837  1.980   1.00 9.55   ? 230 PHE A N   1 
ATOM   1977 C  CA  . PHE A 1 230 ? 1.802   -6.787  2.668   1.00 9.81   ? 230 PHE A CA  1 
ATOM   1978 C  C   . PHE A 1 230 ? 2.634   -5.971  1.666   1.00 9.56   ? 230 PHE A C   1 
ATOM   1979 O  O   . PHE A 1 230 ? 2.880   -4.804  1.865   1.00 10.28  ? 230 PHE A O   1 
ATOM   1980 C  CB  . PHE A 1 230 ? 2.803   -7.424  3.663   1.00 10.10  ? 230 PHE A CB  1 
ATOM   1981 C  CG  . PHE A 1 230 ? 2.223   -7.948  4.954   1.00 9.09   ? 230 PHE A CG  1 
ATOM   1982 C  CD1 . PHE A 1 230 ? 1.454   -7.123  5.790   1.00 9.90   ? 230 PHE A CD1 1 
ATOM   1983 C  CD2 . PHE A 1 230 ? 2.533   -9.225  5.370   1.00 10.43  ? 230 PHE A CD2 1 
ATOM   1984 C  CE1 . PHE A 1 230 ? 1.073   -7.589  7.040   1.00 10.09  ? 230 PHE A CE1 1 
ATOM   1985 C  CE2 . PHE A 1 230 ? 2.110   -9.701  6.597   1.00 10.48  ? 230 PHE A CE2 1 
ATOM   1986 C  CZ  . PHE A 1 230 ? 1.368   -8.869  7.459   1.00 9.92   ? 230 PHE A CZ  1 
ATOM   1987 N  N   . ASN A 1 231 ? 3.169   -6.649  0.649   1.00 10.19  ? 231 ASN A N   1 
ATOM   1988 C  CA  . ASN A 1 231 ? 4.078   -6.041  -0.287  1.00 9.77   ? 231 ASN A CA  1 
ATOM   1989 C  C   . ASN A 1 231 ? 3.442   -5.162  -1.242  1.00 10.47  ? 231 ASN A C   1 
ATOM   1990 O  O   . ASN A 1 231 ? 2.242   -5.253  -1.522  1.00 10.69  ? 231 ASN A O   1 
ATOM   1991 C  CB  . ASN A 1 231 ? 4.839   -7.180  -1.026  1.00 11.48  ? 231 ASN A CB  1 
ATOM   1992 C  CG  . ASN A 1 231 ? 3.852   -8.082  -1.735  1.00 10.79  ? 231 ASN A CG  1 
ATOM   1993 O  OD1 . ASN A 1 231 ? 3.242   -8.943  -1.069  1.00 11.24  ? 231 ASN A OD1 1 
ATOM   1994 N  ND2 . ASN A 1 231 ? 3.703   -7.920  -3.033  1.00 13.85  ? 231 ASN A ND2 1 
ATOM   1995 N  N   . GLY A 1 232 ? 4.250   -4.240  -1.803  1.00 11.28  ? 232 GLY A N   1 
ATOM   1996 C  CA  . GLY A 1 232 ? 3.847   -3.496  -2.966  1.00 11.62  ? 232 GLY A CA  1 
ATOM   1997 C  C   . GLY A 1 232 ? 3.950   -4.393  -4.218  1.00 12.29  ? 232 GLY A C   1 
ATOM   1998 O  O   . GLY A 1 232 ? 4.672   -5.415  -4.250  1.00 13.67  ? 232 GLY A O   1 
ATOM   1999 N  N   . GLU A 1 233 ? 3.184   -4.055  -5.241  1.00 13.76  ? 233 GLU A N   1 
ATOM   2000 C  CA  . GLU A 1 233 ? 3.288   -4.760  -6.489  1.00 14.26  ? 233 GLU A CA  1 
ATOM   2001 C  C   . GLU A 1 233 ? 4.688   -4.754  -7.038  1.00 14.62  ? 233 GLU A C   1 
ATOM   2002 O  O   . GLU A 1 233 ? 5.365   -3.764  -6.916  1.00 16.58  ? 233 GLU A O   1 
ATOM   2003 C  CB  . GLU A 1 233 ? 2.342   -4.122  -7.484  1.00 16.35  ? 233 GLU A CB  1 
ATOM   2004 C  CG  . GLU A 1 233 ? 2.357   -4.903  -8.818  1.00 20.93  ? 233 GLU A CG  1 
ATOM   2005 C  CD  . GLU A 1 233 ? 1.399   -4.335  -9.822  1.00 37.35  ? 233 GLU A CD  1 
ATOM   2006 O  OE1 . GLU A 1 233 ? 0.455   -3.598  -9.381  1.00 30.41  ? 233 GLU A OE1 1 
ATOM   2007 O  OE2 . GLU A 1 233 ? 1.565   -4.609  -11.069 1.00 41.21  ? 233 GLU A OE2 1 
ATOM   2008 N  N   . GLY A 1 234 ? 5.174   -5.927  -7.535  1.00 20.14  ? 234 GLY A N   1 
ATOM   2009 C  CA  . GLY A 1 234 ? 6.498   -6.010  -8.094  1.00 23.26  ? 234 GLY A CA  1 
ATOM   2010 C  C   . GLY A 1 234 ? 7.488   -6.537  -7.064  1.00 20.27  ? 234 GLY A C   1 
ATOM   2011 O  O   . GLY A 1 234 ? 8.553   -6.897  -7.445  1.00 34.70  ? 234 GLY A O   1 
ATOM   2012 N  N   . GLU A 1 235 ? 7.163   -6.551  -5.762  1.00 15.67  ? 235 GLU A N   1 
ATOM   2013 C  CA  . GLU A 1 235 ? 8.059   -7.023  -4.712  1.00 14.09  ? 235 GLU A CA  1 
ATOM   2014 C  C   . GLU A 1 235 ? 7.661   -8.455  -4.442  1.00 13.34  ? 235 GLU A C   1 
ATOM   2015 O  O   . GLU A 1 235 ? 6.538   -8.861  -4.802  1.00 13.76  ? 235 GLU A O   1 
ATOM   2016 C  CB  . GLU A 1 235 ? 7.930   -6.177  -3.467  1.00 14.17  ? 235 GLU A CB  1 
ATOM   2017 C  CG  . GLU A 1 235 ? 8.042   -4.686  -3.695  1.00 21.00  ? 235 GLU A CG  1 
ATOM   2018 C  CD  . GLU A 1 235 ? 7.635   -3.838  -2.503  1.00 26.39  ? 235 GLU A CD  1 
ATOM   2019 O  OE1 . GLU A 1 235 ? 7.171   -4.395  -1.489  1.00 20.07  ? 235 GLU A OE1 1 
ATOM   2020 O  OE2 . GLU A 1 235 ? 7.782   -2.597  -2.588  1.00 35.33  ? 235 GLU A OE2 1 
ATOM   2021 N  N   . PRO A 1 236 ? 8.510   -9.255  -3.783  1.00 12.86  ? 236 PRO A N   1 
ATOM   2022 C  CA  . PRO A 1 236 ? 8.131   -10.650 -3.498  1.00 12.17  ? 236 PRO A CA  1 
ATOM   2023 C  C   . PRO A 1 236 ? 6.787   -10.661 -2.751  1.00 11.47  ? 236 PRO A C   1 
ATOM   2024 O  O   . PRO A 1 236 ? 6.517   -9.813  -1.824  1.00 12.21  ? 236 PRO A O   1 
ATOM   2025 C  CB  . PRO A 1 236 ? 9.310   -11.177 -2.679  1.00 13.41  ? 236 PRO A CB  1 
ATOM   2026 C  CG  . PRO A 1 236 ? 10.489  -10.371 -3.201  1.00 14.85  ? 236 PRO A CG  1 
ATOM   2027 C  CD  . PRO A 1 236 ? 9.904   -8.953  -3.370  1.00 14.59  ? 236 PRO A CD  1 
ATOM   2028 N  N   . GLU A 1 237 ? 5.978   -11.648 -3.081  1.00 12.04  ? 237 GLU A N   1 
ATOM   2029 C  CA  . GLU A 1 237 ? 4.659   -11.758 -2.529  1.00 10.61  ? 237 GLU A CA  1 
ATOM   2030 C  C   . GLU A 1 237 ? 4.675   -12.261 -1.104  1.00 10.94  ? 237 GLU A C   1 
ATOM   2031 O  O   . GLU A 1 237 ? 5.149   -13.403 -0.837  1.00 11.50  ? 237 GLU A O   1 
ATOM   2032 C  CB  . GLU A 1 237 ? 3.861   -12.625 -3.478  1.00 11.25  ? 237 GLU A CB  1 
ATOM   2033 C  CG  . GLU A 1 237 ? 2.474   -12.812 -2.973  1.00 14.32  ? 237 GLU A CG  1 
ATOM   2034 C  CD  . GLU A 1 237 ? 1.705   -13.779 -3.886  1.00 20.45  ? 237 GLU A CD  1 
ATOM   2035 O  OE1 . GLU A 1 237 ? 2.206   -14.176 -4.960  1.00 25.44  ? 237 GLU A OE1 1 
ATOM   2036 O  OE2 . GLU A 1 237 ? 0.554   -14.040 -3.567  1.00 28.60  ? 237 GLU A OE2 1 
ATOM   2037 N  N   . GLU A 1 238 ? 4.085   -11.505 -0.171  1.00 10.55  ? 238 GLU A N   1 
ATOM   2038 C  CA  . GLU A 1 238 ? 3.922   -11.907 1.231   1.00 10.12  ? 238 GLU A CA  1 
ATOM   2039 C  C   . GLU A 1 238 ? 2.479   -11.654 1.561   1.00 8.98   ? 238 GLU A C   1 
ATOM   2040 O  O   . GLU A 1 238 ? 2.042   -10.499 1.561   1.00 10.98  ? 238 GLU A O   1 
ATOM   2041 C  CB  . GLU A 1 238 ? 4.822   -11.104 2.119   1.00 12.39  ? 238 GLU A CB  1 
ATOM   2042 C  CG  . GLU A 1 238 ? 6.306   -11.450 1.862   1.00 13.82  ? 238 GLU A CG  1 
ATOM   2043 C  CD  . GLU A 1 238 ? 7.163   -10.735 2.865   1.00 14.75  ? 238 GLU A CD  1 
ATOM   2044 O  OE1 . GLU A 1 238 ? 7.185   -11.052 4.095   1.00 19.26  ? 238 GLU A OE1 1 
ATOM   2045 O  OE2 . GLU A 1 238 ? 7.892   -9.793  2.427   1.00 15.83  ? 238 GLU A OE2 1 
ATOM   2046 N  N   A LEU A 1 239 ? 1.726   -12.726 1.855   0.50 9.21   ? 239 LEU A N   1 
ATOM   2047 N  N   B LEU A 1 239 ? 1.730   -12.699 1.827   0.50 10.06  ? 239 LEU A N   1 
ATOM   2048 C  CA  A LEU A 1 239 ? 0.305   -12.650 2.226   0.50 8.36   ? 239 LEU A CA  1 
ATOM   2049 C  CA  B LEU A 1 239 ? 0.363   -12.452 2.165   0.50 10.54  ? 239 LEU A CA  1 
ATOM   2050 C  C   A LEU A 1 239 ? 0.173   -11.805 3.507   0.50 8.44   ? 239 LEU A C   1 
ATOM   2051 C  C   B LEU A 1 239 ? 0.279   -11.631 3.461   0.50 10.44  ? 239 LEU A C   1 
ATOM   2052 O  O   A LEU A 1 239 ? 0.893   -11.981 4.488   0.50 7.86   ? 239 LEU A O   1 
ATOM   2053 O  O   B LEU A 1 239 ? 1.088   -11.664 4.391   0.50 10.87  ? 239 LEU A O   1 
ATOM   2054 C  CB  A LEU A 1 239 ? -0.230  -14.047 2.520   0.50 9.75   ? 239 LEU A CB  1 
ATOM   2055 C  CB  B LEU A 1 239 ? -0.402  -13.774 2.295   0.50 11.45  ? 239 LEU A CB  1 
ATOM   2056 C  CG  A LEU A 1 239 ? -0.563  -14.925 1.318   0.50 10.03  ? 239 LEU A CG  1 
ATOM   2057 C  CG  B LEU A 1 239 ? -0.569  -14.571 0.993   0.50 12.24  ? 239 LEU A CG  1 
ATOM   2058 C  CD1 A LEU A 1 239 ? -1.409  -16.106 1.767   0.50 16.15  ? 239 LEU A CD1 1 
ATOM   2059 C  CD1 B LEU A 1 239 ? 0.762   -15.073 0.450   0.50 9.30   ? 239 LEU A CD1 1 
ATOM   2060 C  CD2 A LEU A 1 239 ? -1.299  -14.097 0.282   0.50 9.27   ? 239 LEU A CD2 1 
ATOM   2061 C  CD2 B LEU A 1 239 ? -1.568  -15.712 1.129   0.50 20.47  ? 239 LEU A CD2 1 
ATOM   2062 N  N   . MET A 1 240 ? -0.792  -10.851 3.485   1.00 9.42   ? 240 MET A N   1 
ATOM   2063 C  CA  . MET A 1 240 ? -1.118  -10.016 4.669   1.00 9.37   ? 240 MET A CA  1 
ATOM   2064 C  C   . MET A 1 240 ? -1.948  -10.844 5.623   1.00 8.41   ? 240 MET A C   1 
ATOM   2065 O  O   . MET A 1 240 ? -3.161  -10.983 5.483   1.00 9.28   ? 240 MET A O   1 
ATOM   2066 C  CB  . MET A 1 240 ? -1.930  -8.806  4.182   1.00 9.05   ? 240 MET A CB  1 
ATOM   2067 C  CG  . MET A 1 240 ? -2.236  -7.807  5.348   1.00 9.62   ? 240 MET A CG  1 
ATOM   2068 S  SD  . MET A 1 240 ? -3.177  -6.400  4.806   1.00 10.13  ? 240 MET A SD  1 
ATOM   2069 C  CE  . MET A 1 240 ? -1.831  -5.394  4.167   1.00 10.84  ? 240 MET A CE  1 
ATOM   2070 N  N   . VAL A 1 241 ? -1.226  -11.454 6.576   1.00 8.27   ? 241 VAL A N   1 
ATOM   2071 C  CA  . VAL A 1 241 ? -1.785  -12.243 7.619   1.00 7.99   ? 241 VAL A CA  1 
ATOM   2072 C  C   . VAL A 1 241 ? -0.976  -12.007 8.871   1.00 7.29   ? 241 VAL A C   1 
ATOM   2073 O  O   . VAL A 1 241 ? 0.214   -11.630 8.788   1.00 8.40   ? 241 VAL A O   1 
ATOM   2074 C  CB  . VAL A 1 241 ? -1.780  -13.775 7.312   1.00 9.22   ? 241 VAL A CB  1 
ATOM   2075 C  CG1 . VAL A 1 241 ? -2.711  -14.057 6.101   1.00 10.71  ? 241 VAL A CG1 1 
ATOM   2076 C  CG2 . VAL A 1 241 ? -0.357  -14.287 7.050   1.00 10.65  ? 241 VAL A CG2 1 
ATOM   2077 N  N   . ASP A 1 242 ? -1.566  -12.255 10.016  1.00 7.10   ? 242 ASP A N   1 
ATOM   2078 C  CA  . ASP A 1 242 ? -0.905  -12.096 11.306  1.00 7.79   ? 242 ASP A CA  1 
ATOM   2079 C  C   . ASP A 1 242 ? -0.414  -10.696 11.525  1.00 7.35   ? 242 ASP A C   1 
ATOM   2080 O  O   . ASP A 1 242 ? 0.707   -10.442 11.983  1.00 9.04   ? 242 ASP A O   1 
ATOM   2081 C  CB  . ASP A 1 242 ? 0.177   -13.173 11.525  1.00 8.36   ? 242 ASP A CB  1 
ATOM   2082 C  CG  . ASP A 1 242 ? -0.423  -14.546 11.651  1.00 8.22   ? 242 ASP A CG  1 
ATOM   2083 O  OD1 . ASP A 1 242 ? -1.478  -14.699 12.306  1.00 8.27   ? 242 ASP A OD1 1 
ATOM   2084 O  OD2 . ASP A 1 242 ? 0.153   -15.481 11.047  1.00 10.26  ? 242 ASP A OD2 1 
ATOM   2085 N  N   . ASN A 1 243 ? -1.271  -9.733  11.209  1.00 6.88   ? 243 ASN A N   1 
ATOM   2086 C  CA  . ASN A 1 243 ? -0.998  -8.329  11.440  1.00 7.02   ? 243 ASN A CA  1 
ATOM   2087 C  C   . ASN A 1 243 ? -1.589  -7.857  12.767  1.00 6.74   ? 243 ASN A C   1 
ATOM   2088 O  O   . ASN A 1 243 ? -2.308  -6.833  12.828  1.00 8.52   ? 243 ASN A O   1 
ATOM   2089 C  CB  . ASN A 1 243 ? -1.499  -7.463  10.254  1.00 7.32   ? 243 ASN A CB  1 
ATOM   2090 C  CG  . ASN A 1 243 ? -2.958  -7.640  9.922   1.00 7.11   ? 243 ASN A CG  1 
ATOM   2091 O  OD1 . ASN A 1 243 ? -3.647  -8.488  10.496  1.00 8.30   ? 243 ASN A OD1 1 
ATOM   2092 N  ND2 . ASN A 1 243 ? -3.462  -6.876  8.988   1.00 9.12   ? 243 ASN A ND2 1 
ATOM   2093 N  N   . TRP A 1 244 ? -1.271  -8.550  13.839  1.00 6.77   ? 244 TRP A N   1 
ATOM   2094 C  CA  . TRP A 1 244 ? -1.712  -8.283  15.183  1.00 6.95   ? 244 TRP A CA  1 
ATOM   2095 C  C   . TRP A 1 244 ? -0.506  -8.136  16.109  1.00 6.92   ? 244 TRP A C   1 
ATOM   2096 O  O   . TRP A 1 244 ? 0.471   -8.879  15.994  1.00 8.47   ? 244 TRP A O   1 
ATOM   2097 C  CB  . TRP A 1 244 ? -2.659  -9.358  15.685  1.00 6.96   ? 244 TRP A CB  1 
ATOM   2098 C  CG  . TRP A 1 244 ? -2.214  -10.766 15.543  1.00 6.53   ? 244 TRP A CG  1 
ATOM   2099 C  CD1 . TRP A 1 244 ? -2.327  -11.530 14.419  1.00 7.38   ? 244 TRP A CD1 1 
ATOM   2100 C  CD2 . TRP A 1 244 ? -1.592  -11.592 16.511  1.00 6.80   ? 244 TRP A CD2 1 
ATOM   2101 N  NE1 . TRP A 1 244 ? -1.825  -12.791 14.605  1.00 7.66   ? 244 TRP A NE1 1 
ATOM   2102 C  CE2 . TRP A 1 244 ? -1.376  -12.864 15.894  1.00 7.65   ? 244 TRP A CE2 1 
ATOM   2103 C  CE3 . TRP A 1 244 ? -1.305  -11.455 17.845  1.00 7.97   ? 244 TRP A CE3 1 
ATOM   2104 C  CZ2 . TRP A 1 244 ? -0.807  -13.948 16.624  1.00 8.90   ? 244 TRP A CZ2 1 
ATOM   2105 C  CZ3 . TRP A 1 244 ? -0.788  -12.521 18.561  1.00 9.02   ? 244 TRP A CZ3 1 
ATOM   2106 C  CH2 . TRP A 1 244 ? -0.535  -13.739 17.946  1.00 9.46   ? 244 TRP A CH2 1 
ATOM   2107 N  N   . ARG A 1 245 ? -0.650  -7.225  17.029  1.00 7.48   ? 245 ARG A N   1 
ATOM   2108 C  CA  . ARG A 1 245 ? 0.289   -7.076  18.156  1.00 7.32   ? 245 ARG A CA  1 
ATOM   2109 C  C   . ARG A 1 245 ? -0.193  -8.004  19.281  1.00 7.21   ? 245 ARG A C   1 
ATOM   2110 O  O   . ARG A 1 245 ? -1.365  -7.989  19.589  1.00 7.74   ? 245 ARG A O   1 
ATOM   2111 C  CB  . ARG A 1 245 ? 0.304   -5.650  18.652  1.00 7.19   ? 245 ARG A CB  1 
ATOM   2112 C  CG  . ARG A 1 245 ? 1.447   -5.381  19.650  1.00 7.73   ? 245 ARG A CG  1 
ATOM   2113 C  CD  . ARG A 1 245 ? 1.336   -4.023  20.257  1.00 7.83   ? 245 ARG A CD  1 
ATOM   2114 N  NE  . ARG A 1 245 ? 2.604   -3.724  20.982  1.00 7.73   ? 245 ARG A NE  1 
ATOM   2115 C  CZ  . ARG A 1 245 ? 2.764   -2.687  21.794  1.00 7.72   ? 245 ARG A CZ  1 
ATOM   2116 N  NH1 . ARG A 1 245 ? 1.801   -1.908  22.139  1.00 8.58   ? 245 ARG A NH1 1 
ATOM   2117 N  NH2 . ARG A 1 245 ? 4.026   -2.432  22.248  1.00 9.40   ? 245 ARG A NH2 1 
ATOM   2118 N  N   . PRO A 1 246 ? 0.703   -8.781  19.904  1.00 7.73   ? 246 PRO A N   1 
ATOM   2119 C  CA  . PRO A 1 246 ? 0.279   -9.620  21.025  1.00 8.76   ? 246 PRO A CA  1 
ATOM   2120 C  C   . PRO A 1 246 ? -0.054  -8.785  22.266  1.00 7.98   ? 246 PRO A C   1 
ATOM   2121 O  O   . PRO A 1 246 ? 0.301   -7.596  22.391  1.00 8.28   ? 246 PRO A O   1 
ATOM   2122 C  CB  . PRO A 1 246 ? 1.475   -10.517 21.326  1.00 10.59  ? 246 PRO A CB  1 
ATOM   2123 C  CG  . PRO A 1 246 ? 2.336   -10.381 20.101  1.00 16.32  ? 246 PRO A CG  1 
ATOM   2124 C  CD  . PRO A 1 246 ? 2.121   -9.017  19.536  1.00 10.19  ? 246 PRO A CD  1 
ATOM   2125 N  N   . ALA A 1 247 ? -0.712  -9.449  23.223  1.00 8.62   ? 247 ALA A N   1 
ATOM   2126 C  CA  . ALA A 1 247 ? -1.052  -8.805  24.500  1.00 8.67   ? 247 ALA A CA  1 
ATOM   2127 C  C   . ALA A 1 247 ? 0.227   -8.291  25.202  1.00 7.99   ? 247 ALA A C   1 
ATOM   2128 O  O   . ALA A 1 247 ? 1.238   -8.976  25.236  1.00 9.67   ? 247 ALA A O   1 
ATOM   2129 C  CB  . ALA A 1 247 ? -1.770  -9.819  25.383  1.00 10.35  ? 247 ALA A CB  1 
ATOM   2130 N  N   . GLN A 1 248 ? 0.076   -7.122  25.789  1.00 7.79   ? 248 GLN A N   1 
ATOM   2131 C  CA  . GLN A 1 248 ? 1.110   -6.410  26.511  1.00 8.01   ? 248 GLN A CA  1 
ATOM   2132 C  C   . GLN A 1 248 ? 0.818   -6.417  27.989  1.00 8.62   ? 248 GLN A C   1 
ATOM   2133 O  O   . GLN A 1 248 ? -0.300  -6.633  28.429  1.00 9.37   ? 248 GLN A O   1 
ATOM   2134 C  CB  . GLN A 1 248 ? 1.190   -4.971  25.940  1.00 8.72   ? 248 GLN A CB  1 
ATOM   2135 C  CG  . GLN A 1 248 ? 1.460   -4.919  24.498  1.00 9.32   ? 248 GLN A CG  1 
ATOM   2136 C  CD  . GLN A 1 248 ? 2.788   -5.554  24.141  1.00 9.55   ? 248 GLN A CD  1 
ATOM   2137 O  OE1 . GLN A 1 248 ? 3.841   -5.253  24.738  1.00 11.86  ? 248 GLN A OE1 1 
ATOM   2138 N  NE2 . GLN A 1 248 ? 2.769   -6.506  23.202  1.00 10.46  ? 248 GLN A NE2 1 
ATOM   2139 N  N   . PRO A 1 249 ? 1.828   -6.092  28.809  1.00 9.73   ? 249 PRO A N   1 
ATOM   2140 C  CA  . PRO A 1 249 ? 1.628   -6.160  30.264  1.00 10.50  ? 249 PRO A CA  1 
ATOM   2141 C  C   . PRO A 1 249 ? 0.532   -5.185  30.717  1.00 9.56   ? 249 PRO A C   1 
ATOM   2142 O  O   . PRO A 1 249 ? 0.564   -3.996  30.381  1.00 9.74   ? 249 PRO A O   1 
ATOM   2143 C  CB  . PRO A 1 249 ? 3.039   -5.797  30.795  1.00 13.27  ? 249 PRO A CB  1 
ATOM   2144 C  CG  . PRO A 1 249 ? 3.963   -6.222  29.766  1.00 16.42  ? 249 PRO A CG  1 
ATOM   2145 C  CD  . PRO A 1 249 ? 3.262   -5.851  28.466  1.00 11.78  ? 249 PRO A CD  1 
ATOM   2146 N  N   . LEU A 1 250 ? -0.339  -5.661  31.607  1.00 9.95   ? 250 LEU A N   1 
ATOM   2147 C  CA  . LEU A 1 250 ? -1.375  -4.808  32.132  1.00 9.54   ? 250 LEU A CA  1 
ATOM   2148 C  C   . LEU A 1 250 ? -0.859  -3.718  33.063  1.00 9.11   ? 250 LEU A C   1 
ATOM   2149 O  O   . LEU A 1 250 ? -1.394  -2.623  33.126  1.00 10.21  ? 250 LEU A O   1 
ATOM   2150 C  CB  . LEU A 1 250 ? -2.375  -5.696  32.829  1.00 11.95  ? 250 LEU A CB  1 
ATOM   2151 C  CG  . LEU A 1 250 ? -3.708  -4.985  33.274  1.00 12.42  ? 250 LEU A CG  1 
ATOM   2152 C  CD1 . LEU A 1 250 ? -4.441  -4.384  32.060  1.00 12.58  ? 250 LEU A CD1 1 
ATOM   2153 C  CD2 . LEU A 1 250 ? -4.608  -5.952  34.005  1.00 16.32  ? 250 LEU A CD2 1 
ATOM   2154 N  N   . LYS A 1 251 ? 0.218   -4.005  33.778  1.00 10.39  ? 251 LYS A N   1 
ATOM   2155 C  CA  . LYS A 1 251 ? 0.830   -3.004  34.650  1.00 11.84  ? 251 LYS A CA  1 
ATOM   2156 C  C   . LYS A 1 251 ? -0.197  -2.436  35.634  1.00 12.09  ? 251 LYS A C   1 
ATOM   2157 O  O   . LYS A 1 251 ? -1.010  -3.252  36.127  1.00 14.54  ? 251 LYS A O   1 
ATOM   2158 C  CB  . LYS A 1 251 ? 1.646   -1.968  33.849  1.00 12.94  ? 251 LYS A CB  1 
ATOM   2159 C  CG  . LYS A 1 251 ? 2.778   -2.633  33.073  1.00 16.27  ? 251 LYS A CG  1 
ATOM   2160 C  CD  . LYS A 1 251 ? 3.709   -1.709  32.408  1.00 16.80  ? 251 LYS A CD  1 
ATOM   2161 C  CE  . LYS A 1 251 ? 5.000   -2.352  32.044  1.00 22.25  ? 251 LYS A CE  1 
ATOM   2162 N  NZ  . LYS A 1 251 ? 5.845   -1.444  31.210  1.00 25.30  ? 251 LYS A NZ  1 
ATOM   2163 N  N   . ASN A 1 252 ? -0.197  -1.138  35.847  1.00 11.70  ? 252 ASN A N   1 
ATOM   2164 C  CA  . ASN A 1 252 ? -1.020  -0.639  36.909  1.00 16.38  ? 252 ASN A CA  1 
ATOM   2165 C  C   . ASN A 1 252 ? -2.353  -0.219  36.310  1.00 18.25  ? 252 ASN A C   1 
ATOM   2166 O  O   . ASN A 1 252 ? -2.531  1.107   36.306  1.00 20.13  ? 252 ASN A O   1 
ATOM   2167 C  CB  . ASN A 1 252 ? -0.304  0.551   37.591  1.00 21.60  ? 252 ASN A CB  1 
ATOM   2168 C  CG  . ASN A 1 252 ? -1.009  1.044   38.785  1.00 25.90  ? 252 ASN A CG  1 
ATOM   2169 O  OD1 . ASN A 1 252 ? -1.523  0.243   39.544  1.00 38.07  ? 252 ASN A OD1 1 
ATOM   2170 N  ND2 . ASN A 1 252 ? -1.124  2.366   38.915  1.00 23.82  ? 252 ASN A ND2 1 
ATOM   2171 N  N   . ARG A 1 253 ? -3.134  -1.251  35.698  1.00 14.13  ? 253 ARG A N   1 
ATOM   2172 C  CA  . ARG A 1 253 ? -4.439  -0.914  35.159  1.00 10.54  ? 253 ARG A CA  1 
ATOM   2173 C  C   . ARG A 1 253 ? -5.491  -1.837  35.626  1.00 11.98  ? 253 ARG A C   1 
ATOM   2174 O  O   . ARG A 1 253 ? -5.223  -3.014  35.840  1.00 17.03  ? 253 ARG A O   1 
ATOM   2175 C  CB  . ARG A 1 253 ? -4.357  -0.857  33.662  1.00 9.39   ? 253 ARG A CB  1 
ATOM   2176 C  CG  . ARG A 1 253 ? -3.491  0.279   33.157  1.00 9.95   ? 253 ARG A CG  1 
ATOM   2177 C  CD  . ARG A 1 253 ? -3.381  0.264   31.661  1.00 9.21   ? 253 ARG A CD  1 
ATOM   2178 N  NE  . ARG A 1 253 ? -2.535  -0.888  31.187  1.00 8.52   ? 253 ARG A NE  1 
ATOM   2179 C  CZ  . ARG A 1 253 ? -2.292  -1.142  29.907  1.00 7.37   ? 253 ARG A CZ  1 
ATOM   2180 N  NH1 . ARG A 1 253 ? -2.904  -0.461  28.951  1.00 7.76   ? 253 ARG A NH1 1 
ATOM   2181 N  NH2 . ARG A 1 253 ? -1.474  -2.124  29.602  1.00 7.60   ? 253 ARG A NH2 1 
ATOM   2182 N  N   A GLN A 1 254 ? -6.718  -1.368  35.744  0.50 12.21  ? 254 GLN A N   1 
ATOM   2183 N  N   B GLN A 1 254 ? -6.706  -1.301  35.680  0.50 12.34  ? 254 GLN A N   1 
ATOM   2184 C  CA  A GLN A 1 254 ? -7.864  -2.252  35.989  0.50 13.01  ? 254 GLN A CA  1 
ATOM   2185 C  CA  B GLN A 1 254 ? -7.926  -2.057  36.022  0.50 12.69  ? 254 GLN A CA  1 
ATOM   2186 C  C   A GLN A 1 254 ? -8.667  -2.158  34.699  0.50 11.06  ? 254 GLN A C   1 
ATOM   2187 C  C   B GLN A 1 254 ? -8.865  -2.089  34.811  0.50 12.78  ? 254 GLN A C   1 
ATOM   2188 O  O   A GLN A 1 254 ? -8.788  -1.133  34.018  0.50 13.56  ? 254 GLN A O   1 
ATOM   2189 O  O   B GLN A 1 254 ? -9.223  -1.071  34.254  0.50 13.48  ? 254 GLN A O   1 
ATOM   2190 C  CB  A GLN A 1 254 ? -8.734  -1.710  37.121  0.50 16.81  ? 254 GLN A CB  1 
ATOM   2191 C  CB  B GLN A 1 254 ? -8.660  -1.414  37.178  0.50 15.72  ? 254 GLN A CB  1 
ATOM   2192 C  CG  A GLN A 1 254 ? -9.703  -2.648  37.866  0.50 20.92  ? 254 GLN A CG  1 
ATOM   2193 C  CG  B GLN A 1 254 ? -8.008  -1.774  38.526  0.50 14.97  ? 254 GLN A CG  1 
ATOM   2194 C  CD  A GLN A 1 254 ? -10.714 -1.933  38.752  0.50 25.55  ? 254 GLN A CD  1 
ATOM   2195 C  CD  B GLN A 1 254 ? -8.711  -1.266  39.769  0.50 23.27  ? 254 GLN A CD  1 
ATOM   2196 O  OE1 A GLN A 1 254 ? -10.906 -0.674  38.741  0.50 34.19  ? 254 GLN A OE1 1 
ATOM   2197 O  OE1 B GLN A 1 254 ? -9.888  -0.901  39.746  0.50 30.87  ? 254 GLN A OE1 1 
ATOM   2198 N  NE2 A GLN A 1 254 ? -11.366 -2.728  39.561  0.50 29.05  ? 254 GLN A NE2 1 
ATOM   2199 N  NE2 B GLN A 1 254 ? -7.960  -1.217  40.874  0.50 28.73  ? 254 GLN A NE2 1 
ATOM   2200 N  N   . ILE A 1 255 ? -9.208  -3.290  34.372  1.00 10.13  ? 255 ILE A N   1 
ATOM   2201 C  CA  . ILE A 1 255 ? -10.212 -3.430  33.272  1.00 9.66   ? 255 ILE A CA  1 
ATOM   2202 C  C   . ILE A 1 255 ? -11.581 -3.431  33.946  1.00 9.09   ? 255 ILE A C   1 
ATOM   2203 O  O   . ILE A 1 255 ? -11.797 -4.156  34.920  1.00 11.22  ? 255 ILE A O   1 
ATOM   2204 C  CB  . ILE A 1 255 ? -9.982  -4.651  32.455  1.00 9.91   ? 255 ILE A CB  1 
ATOM   2205 C  CG1 . ILE A 1 255 ? -8.521  -4.668  31.906  1.00 10.96  ? 255 ILE A CG1 1 
ATOM   2206 C  CG2 . ILE A 1 255 ? -11.081 -4.779  31.359  1.00 10.94  ? 255 ILE A CG2 1 
ATOM   2207 C  CD1 . ILE A 1 255 ? -8.249  -5.879  31.060  1.00 13.11  ? 255 ILE A CD1 1 
ATOM   2208 N  N   . LYS A 1 256 ? -12.458 -2.564  33.459  1.00 8.76   ? 256 LYS A N   1 
ATOM   2209 C  CA  . LYS A 1 256 ? -13.792 -2.460  33.990  1.00 9.55   ? 256 LYS A CA  1 
ATOM   2210 C  C   . LYS A 1 256 ? -14.780 -3.086  33.038  1.00 9.34   ? 256 LYS A C   1 
ATOM   2211 O  O   . LYS A 1 256 ? -14.618 -2.974  31.837  1.00 11.34  ? 256 LYS A O   1 
ATOM   2212 C  CB  . LYS A 1 256 ? -14.154 -0.989  34.240  1.00 11.34  ? 256 LYS A CB  1 
ATOM   2213 C  CG  . LYS A 1 256 ? -13.223 -0.366  35.268  1.00 17.06  ? 256 LYS A CG  1 
ATOM   2214 C  CD  . LYS A 1 256 ? -13.877 0.888   35.729  1.00 33.84  ? 256 LYS A CD  1 
ATOM   2215 C  CE  . LYS A 1 256 ? -12.972 2.133   35.786  1.00 40.51  ? 256 LYS A CE  1 
ATOM   2216 N  NZ  . LYS A 1 256 ? -12.055 2.115   36.942  1.00 54.88  ? 256 LYS A NZ  1 
ATOM   2217 N  N   . ALA A 1 257 ? -15.840 -3.683  33.572  1.00 10.02  ? 257 ALA A N   1 
ATOM   2218 C  CA  . ALA A 1 257 ? -16.913 -4.323  32.798  1.00 10.76  ? 257 ALA A CA  1 
ATOM   2219 C  C   . ALA A 1 257 ? -18.169 -3.487  32.954  1.00 10.84  ? 257 ALA A C   1 
ATOM   2220 O  O   . ALA A 1 257 ? -18.513 -3.060  34.063  1.00 11.07  ? 257 ALA A O   1 
ATOM   2221 C  CB  . ALA A 1 257 ? -17.147 -5.783  33.206  1.00 11.68  ? 257 ALA A CB  1 
ATOM   2222 N  N   . SER A 1 258 ? -18.906 -3.348  31.824  1.00 10.27  ? 258 SER A N   1 
ATOM   2223 C  CA  . SER A 1 258 ? -20.180 -2.636  31.875  1.00 11.63  ? 258 SER A CA  1 
ATOM   2224 C  C   . SER A 1 258 ? -21.304 -3.576  32.338  1.00 11.75  ? 258 SER A C   1 
ATOM   2225 O  O   . SER A 1 258 ? -22.450 -3.063  32.423  1.00 16.25  ? 258 SER A O   1 
ATOM   2226 C  CB  . SER A 1 258 ? -20.508 -2.081  30.527  1.00 12.39  ? 258 SER A CB  1 
ATOM   2227 O  OG  . SER A 1 258 ? -20.918 -3.065  29.635  1.00 11.06  ? 258 SER A OG  1 
ATOM   2228 N  N   . PHE A 1 259 ? -21.053 -4.840  32.575  1.00 12.54  ? 259 PHE A N   1 
ATOM   2229 C  CA  . PHE A 1 259 ? -22.084 -5.870  32.746  1.00 14.32  ? 259 PHE A CA  1 
ATOM   2230 C  C   . PHE A 1 259 ? -21.573 -6.808  33.864  1.00 17.51  ? 259 PHE A C   1 
ATOM   2231 O  O   . PHE A 1 259 ? -20.383 -6.956  34.110  1.00 17.81  ? 259 PHE A O   1 
ATOM   2232 C  CB  . PHE A 1 259 ? -22.291 -6.621  31.434  1.00 13.56  ? 259 PHE A CB  1 
ATOM   2233 C  CG  . PHE A 1 259 ? -21.022 -7.330  30.994  1.00 13.54  ? 259 PHE A CG  1 
ATOM   2234 C  CD1 . PHE A 1 259 ? -20.054 -6.624  30.282  1.00 11.24  ? 259 PHE A CD1 1 
ATOM   2235 C  CD2 . PHE A 1 259 ? -20.820 -8.667  31.333  1.00 17.25  ? 259 PHE A CD2 1 
ATOM   2236 C  CE1 . PHE A 1 259 ? -18.874 -7.267  29.938  1.00 13.79  ? 259 PHE A CE1 1 
ATOM   2237 C  CE2 . PHE A 1 259 ? -19.618 -9.310  30.994  1.00 19.01  ? 259 PHE A CE2 1 
ATOM   2238 C  CZ  . PHE A 1 259 ? -18.643 -8.601  30.263  1.00 16.69  ? 259 PHE A CZ  1 
ATOM   2239 N  N   . LYS A 1 260 ? -22.568 -7.527  34.371  1.00 25.79  ? 260 LYS A N   1 
ATOM   2240 C  CA  . LYS A 1 260 ? -22.573 -8.560  35.393  1.00 38.82  ? 260 LYS A CA  1 
ATOM   2241 C  C   . LYS A 1 260 ? -22.767 -8.206  36.888  1.00 51.20  ? 260 LYS A C   1 
ATOM   2242 O  O   . LYS A 1 260 ? -23.740 -7.484  37.209  1.00 57.04  ? 260 LYS A O   1 
ATOM   2243 C  CB  . LYS A 1 260 ? -21.603 -9.748  35.137  1.00 43.05  ? 260 LYS A CB  1 
ATOM   2244 C  CG  . LYS A 1 260 ? -22.175 -10.710 34.105  1.00 40.46  ? 260 LYS A CG  1 
ATOM   2245 C  CD  . LYS A 1 260 ? -23.556 -10.231 33.714  1.00 42.83  ? 260 LYS A CD  1 
ATOM   2246 C  CE  . LYS A 1 260 ? -23.959 -10.801 32.361  1.00 67.20  ? 260 LYS A CE  1 
ATOM   2247 N  NZ  . LYS A 1 260 ? -24.840 -9.843  31.639  1.00 57.34  ? 260 LYS A NZ  1 
ATOM   2248 O  OXT . LYS A 1 260 ? -21.976 -8.578  37.759  1.00 71.57  ? 260 LYS A OXT 1 
HETATM 2249 ZN ZN  . ZN  B 2 .   ? -6.221  -1.743  15.212  1.00 6.20   ? 301 ZN  A ZN  1 
HETATM 2250 S  S   . DMS C 3 .   ? 1.752   -11.602 14.852  1.00 16.02  ? 302 DMS A S   1 
HETATM 2251 O  O   . DMS C 3 .   ? 2.360   -12.854 14.373  1.00 22.09  ? 302 DMS A O   1 
HETATM 2252 C  C1  . DMS C 3 .   ? 2.038   -11.481 16.519  1.00 14.73  ? 302 DMS A C1  1 
HETATM 2253 C  C2  . DMS C 3 .   ? 2.817   -10.324 14.397  1.00 17.82  ? 302 DMS A C2  1 
HETATM 2254 N  N1  . BCN D 4 .   ? -20.130 -14.779 23.365  1.00 35.26  ? 303 BCN A N1  1 
HETATM 2255 C  C1  . BCN D 4 .   ? -19.489 -15.520 22.263  1.00 23.03  ? 303 BCN A C1  1 
HETATM 2256 C  C2  . BCN D 4 .   ? -20.394 -16.299 21.371  1.00 58.00  ? 303 BCN A C2  1 
HETATM 2257 O  O21 . BCN D 4 .   ? -21.494 -16.795 21.790  1.00 104.08 ? 303 BCN A O21 1 
HETATM 2258 O  O22 . BCN D 4 .   ? -19.922 -16.390 20.210  1.00 47.68  ? 303 BCN A O22 1 
HETATM 2259 C  C3  . BCN D 4 .   ? -19.154 -14.244 24.355  1.00 30.20  ? 303 BCN A C3  1 
HETATM 2260 C  C4  . BCN D 4 .   ? -19.405 -15.259 25.494  1.00 41.17  ? 303 BCN A C4  1 
HETATM 2261 O  O4  . BCN D 4 .   ? -18.844 -14.748 26.688  1.00 48.84  ? 303 BCN A O4  1 
HETATM 2262 C  C5  . BCN D 4 .   ? -21.233 -13.836 23.043  1.00 25.40  ? 303 BCN A C5  1 
HETATM 2263 C  C6  . BCN D 4 .   ? -21.070 -12.777 24.134  1.00 34.53  ? 303 BCN A C6  1 
HETATM 2264 O  O6  . BCN D 4 .   ? -22.288 -12.247 24.649  1.00 34.81  ? 303 BCN A O6  1 
HETATM 2265 O  O1  . MES E 5 .   ? -6.954  -9.375  -2.721  1.00 27.41  ? 304 MES A O1  1 
HETATM 2266 C  C2  . MES E 5 .   ? -7.940  -9.607  -1.671  1.00 21.80  ? 304 MES A C2  1 
HETATM 2267 C  C3  . MES E 5 .   ? -9.194  -10.315 -1.705  1.00 21.35  ? 304 MES A C3  1 
HETATM 2268 N  N4  . MES E 5 .   ? -9.532  -10.785 -3.132  1.00 38.00  ? 304 MES A N4  1 
HETATM 2269 C  C5  . MES E 5 .   ? -8.321  -11.129 -4.008  1.00 25.88  ? 304 MES A C5  1 
HETATM 2270 C  C6  . MES E 5 .   ? -7.007  -10.357 -3.863  1.00 27.55  ? 304 MES A C6  1 
HETATM 2271 C  C7  . MES E 5 .   ? -10.859 -11.590 -3.274  1.00 22.79  ? 304 MES A C7  1 
HETATM 2272 C  C8  . MES E 5 .   ? -10.891 -12.375 -4.596  1.00 68.56  ? 304 MES A C8  1 
HETATM 2273 S  S   . MES E 5 .   ? -9.583  -13.335 -5.039  1.00 91.00  ? 304 MES A S   1 
HETATM 2274 F  F18 A V90 F 6 .   ? -2.827  3.243   12.821  0.50 10.60  ? 305 V90 A F18 1 
HETATM 2275 F  F18 B V90 F 6 .   ? -4.149  3.281   11.164  0.50 17.87  ? 305 V90 A F18 1 
HETATM 2276 C  C5  A V90 F 6 .   ? -3.702  3.276   13.813  0.50 8.39   ? 305 V90 A C5  1 
HETATM 2277 C  C5  B V90 F 6 .   ? -4.004  2.198   11.972  0.50 12.47  ? 305 V90 A C5  1 
HETATM 2278 C  C6  A V90 F 6 .   ? -4.243  4.560   14.082  0.50 7.29   ? 305 V90 A C6  1 
HETATM 2279 C  C6  B V90 F 6 .   ? -3.444  1.029   11.439  0.50 14.81  ? 305 V90 A C6  1 
HETATM 2280 S  S12 A V90 F 6 .   ? -3.811  5.998   13.180  0.50 15.62  ? 305 V90 A S12 1 
HETATM 2281 S  S12 B V90 F 6 .   ? -2.933  0.982   9.717   0.50 21.49  ? 305 V90 A S12 1 
HETATM 2282 C  C13 A V90 F 6 .   ? -2.411  6.716   14.082  0.50 24.94  ? 305 V90 A C13 1 
HETATM 2283 C  C13 B V90 F 6 .   ? -1.189  0.684   10.129  0.50 18.86  ? 305 V90 A C13 1 
HETATM 2284 C  C14 A V90 F 6 .   ? -1.181  5.941   13.721  0.50 24.37  ? 305 V90 A C14 1 
HETATM 2285 C  C14 B V90 F 6 .   ? -0.615  1.910   10.809  0.50 20.94  ? 305 V90 A C14 1 
HETATM 2286 O  O15 A V90 F 6 .   ? -0.508  6.475   12.647  0.50 39.22  ? 305 V90 A O15 1 
HETATM 2287 O  O15 B V90 F 6 .   ? -0.183  2.820   9.844   0.50 14.97  ? 305 V90 A O15 1 
HETATM 2288 C  C1  A V90 F 6 .   ? -5.034  4.606   15.287  0.50 7.81   ? 305 V90 A C1  1 
HETATM 2289 C  C1  B V90 F 6 .   ? -3.284  -0.102  12.249  0.50 14.04  ? 305 V90 A C1  1 
HETATM 2290 F  F17 A V90 F 6 .   ? -5.599  5.741   15.684  0.50 9.95   ? 305 V90 A F17 1 
HETATM 2291 F  F17 B V90 F 6 .   ? -2.742  -1.236  11.737  0.50 28.61  ? 305 V90 A F17 1 
HETATM 2292 C  C4  A V90 F 6 .   ? -4.075  2.112   14.458  0.50 6.51   ? 305 V90 A C4  1 
HETATM 2293 C  C4  B V90 F 6 .   ? -4.407  2.240   13.326  0.50 11.38  ? 305 V90 A C4  1 
HETATM 2294 C  C3  A V90 F 6 .   ? -4.974  2.189   15.556  0.50 6.12   ? 305 V90 A C3  1 
HETATM 2295 C  C3  B V90 F 6 .   ? -4.241  1.095   14.132  0.50 9.17   ? 305 V90 A C3  1 
HETATM 2296 S  S8  A V90 F 6 .   ? -5.481  0.825   16.557  0.50 5.53   ? 305 V90 A S8  1 
HETATM 2297 S  S8  B V90 F 6 .   ? -4.751  1.134   15.863  0.50 9.40   ? 305 V90 A S8  1 
HETATM 2298 O  O10 A V90 F 6 .   ? -6.930  0.852   16.468  0.50 5.93   ? 305 V90 A O10 1 
HETATM 2299 O  O10 B V90 F 6 .   ? -5.948  2.053   16.148  0.50 10.65  ? 305 V90 A O10 1 
HETATM 2300 N  N11 A V90 F 6 .   ? -4.923  -0.532  15.975  0.50 4.01   ? 305 V90 A N11 1 
HETATM 2301 N  N11 B V90 F 6 .   ? -5.178  -0.408  16.607  0.50 8.96   ? 305 V90 A N11 1 
HETATM 2302 O  O9  A V90 F 6 .   ? -4.916  1.067   17.884  0.50 6.28   ? 305 V90 A O9  1 
HETATM 2303 O  O9  B V90 F 6 .   ? -3.670  1.726   16.781  0.50 10.07  ? 305 V90 A O9  1 
HETATM 2304 C  C2  A V90 F 6 .   ? -5.405  3.416   15.923  0.50 7.07   ? 305 V90 A C2  1 
HETATM 2305 C  C2  B V90 F 6 .   ? -3.679  -0.070  13.586  0.50 10.44  ? 305 V90 A C2  1 
HETATM 2306 F  F16 A V90 F 6 .   ? -6.232  3.587   16.973  0.50 7.59   ? 305 V90 A F16 1 
HETATM 2307 F  F16 B V90 F 6 .   ? -3.513  -1.178  14.351  0.50 14.26  ? 305 V90 A F16 1 
HETATM 2308 N  N7  A V90 F 6 .   ? -3.520  0.919   13.962  0.50 6.92   ? 305 V90 A N7  1 
HETATM 2309 N  N7  B V90 F 6 .   ? -4.981  3.409   13.909  0.50 12.18  ? 305 V90 A N7  1 
HETATM 2310 C  C19 A V90 F 6 .   ? -3.475  0.552   12.579  0.50 7.59   ? 305 V90 A C19 1 
HETATM 2311 C  C19 B V90 F 6 .   ? -5.359  4.598   13.184  0.50 21.20  ? 305 V90 A C19 1 
HETATM 2312 C  C26 A V90 F 6 .   ? -3.456  -0.996  12.554  0.50 8.79   ? 305 V90 A C26 1 
HETATM 2313 C  C26 B V90 F 6 .   ? -6.263  5.454   14.066  0.50 21.96  ? 305 V90 A C26 1 
HETATM 2314 C  C25 A V90 F 6 .   ? -2.164  -1.368  11.862  0.50 14.64  ? 305 V90 A C25 1 
HETATM 2315 C  C25 B V90 F 6 .   ? -5.508  6.027   15.253  0.50 17.81  ? 305 V90 A C25 1 
HETATM 2316 C  C24 A V90 F 6 .   ? -2.314  -1.357  10.304  0.50 10.36  ? 305 V90 A C24 1 
HETATM 2317 C  C24 B V90 F 6 .   ? -5.207  7.498   15.017  0.50 22.18  ? 305 V90 A C24 1 
HETATM 2318 C  C23 A V90 F 6 .   ? -2.380  0.062   9.702   0.50 10.47  ? 305 V90 A C23 1 
HETATM 2319 C  C23 B V90 F 6 .   ? -3.723  7.789   15.180  0.50 24.82  ? 305 V90 A C23 1 
HETATM 2320 C  C22 A V90 F 6 .   ? -3.856  0.462   9.376   0.50 11.52  ? 305 V90 A C22 1 
HETATM 2321 C  C22 B V90 F 6 .   ? -2.897  7.124   14.092  0.50 23.05  ? 305 V90 A C22 1 
HETATM 2322 C  C21 A V90 F 6 .   ? -4.227  1.604   10.322  0.50 10.59  ? 305 V90 A C21 1 
HETATM 2323 C  C21 B V90 F 6 .   ? -3.208  5.640   14.019  0.50 8.97   ? 305 V90 A C21 1 
HETATM 2324 C  C20 A V90 F 6 .   ? -4.621  1.155   11.755  0.50 7.78   ? 305 V90 A C20 1 
HETATM 2325 C  C20 B V90 F 6 .   ? -4.083  5.348   12.812  0.50 15.53  ? 305 V90 A C20 1 
HETATM 2326 O  O   . HOH G 7 .   ? -2.949  -13.158 25.090  1.00 10.44  ? 401 HOH A O   1 
HETATM 2327 O  O   . HOH G 7 .   ? -21.094 -7.020  23.485  1.00 10.93  ? 402 HOH A O   1 
HETATM 2328 O  O   . HOH G 7 .   ? -16.534 -8.340  20.277  1.00 7.91   ? 403 HOH A O   1 
HETATM 2329 O  O   . HOH G 7 .   ? -21.183 5.697   4.556   1.00 10.41  ? 404 HOH A O   1 
HETATM 2330 O  O   . HOH G 7 .   ? -20.472 7.762   1.717   1.00 10.39  ? 405 HOH A O   1 
HETATM 2331 O  O   . HOH G 7 .   ? -4.116  -13.437 17.985  1.00 8.39   ? 406 HOH A O   1 
HETATM 2332 O  O   . HOH G 7 .   ? 1.685   -1.508  29.327  1.00 12.31  ? 407 HOH A O   1 
HETATM 2333 O  O   . HOH G 7 .   ? -3.073  -11.105 20.810  1.00 8.64   ? 408 HOH A O   1 
HETATM 2334 O  O   . HOH G 7 .   ? 4.079   5.063   29.775  1.00 17.73  ? 409 HOH A O   1 
HETATM 2335 O  O   . HOH G 7 .   ? -18.613 9.972   8.622   1.00 10.97  ? 410 HOH A O   1 
HETATM 2336 O  O   . HOH G 7 .   ? 5.274   -4.758  20.945  1.00 11.81  ? 411 HOH A O   1 
HETATM 2337 O  O   . HOH G 7 .   ? -2.056  -8.629  28.981  1.00 10.60  ? 412 HOH A O   1 
HETATM 2338 O  O   . HOH G 7 .   ? -13.349 10.504  27.674  1.00 16.98  ? 413 HOH A O   1 
HETATM 2339 O  O   . HOH G 7 .   ? -7.539  -15.545 11.397  1.00 9.61   ? 414 HOH A O   1 
HETATM 2340 O  O   . HOH G 7 .   ? -1.649  -12.213 22.760  1.00 9.41   ? 415 HOH A O   1 
HETATM 2341 O  O   . HOH G 7 .   ? -0.919  -12.963 26.950  1.00 22.38  ? 416 HOH A O   1 
HETATM 2342 O  O   . HOH G 7 .   ? -17.475 20.568  7.905   1.00 10.98  ? 417 HOH A O   1 
HETATM 2343 O  O   . HOH G 7 .   ? -3.351  -15.784 24.335  1.00 12.15  ? 418 HOH A O   1 
HETATM 2344 O  O   . HOH G 7 .   ? 1.035   -1.986  -4.954  1.00 13.17  ? 419 HOH A O   1 
HETATM 2345 O  O   . HOH G 7 .   ? -22.524 -11.596 13.902  1.00 19.99  ? 420 HOH A O   1 
HETATM 2346 O  O   . HOH G 7 .   ? -4.286  -11.872 32.010  1.00 19.50  ? 421 HOH A O   1 
HETATM 2347 O  O   . HOH G 7 .   ? -22.739 -2.913  6.568   1.00 15.37  ? 422 HOH A O   1 
HETATM 2348 O  O   . HOH G 7 .   ? -22.470 -5.947  2.586   1.00 17.45  ? 423 HOH A O   1 
HETATM 2349 O  O   . HOH G 7 .   ? -0.929  -3.968  15.509  1.00 9.68   ? 424 HOH A O   1 
HETATM 2350 O  O   . HOH G 7 .   ? -13.873 -16.494 28.923  1.00 19.56  ? 425 HOH A O   1 
HETATM 2351 O  O   . HOH G 7 .   ? 5.603   7.310   20.477  1.00 15.57  ? 426 HOH A O   1 
HETATM 2352 O  O   . HOH G 7 .   ? -17.396 -22.039 5.906   1.00 8.43   ? 427 HOH A O   1 
HETATM 2353 O  O   . HOH G 7 .   ? -17.591 4.363   -3.973  1.00 30.02  ? 428 HOH A O   1 
HETATM 2354 O  O   . HOH G 7 .   ? 8.948   -3.661  21.010  1.00 11.23  ? 429 HOH A O   1 
HETATM 2355 O  O   . HOH G 7 .   ? -23.186 -0.770  3.833   1.00 17.85  ? 430 HOH A O   1 
HETATM 2356 O  O   . HOH G 7 .   ? -20.636 -6.673  -2.234  1.00 23.97  ? 431 HOH A O   1 
HETATM 2357 O  O   . HOH G 7 .   ? -12.584 -16.759 26.565  1.00 15.02  ? 432 HOH A O   1 
HETATM 2358 O  O   . HOH G 7 .   ? -17.429 10.541  11.133  1.00 14.93  ? 433 HOH A O   1 
HETATM 2359 O  O   . HOH G 7 .   ? -20.891 -19.612 6.577   1.00 16.22  ? 434 HOH A O   1 
HETATM 2360 O  O   . HOH G 7 .   ? 8.258   -8.765  -0.032  1.00 15.95  ? 435 HOH A O   1 
HETATM 2361 O  O   . HOH G 7 .   ? -24.503 -7.675  9.042   1.00 14.23  ? 436 HOH A O   1 
HETATM 2362 O  O   . HOH G 7 .   ? -12.497 -17.149 16.834  1.00 13.13  ? 437 HOH A O   1 
HETATM 2363 O  O   . HOH G 7 .   ? -11.509 2.844   30.746  1.00 18.77  ? 438 HOH A O   1 
HETATM 2364 O  O   . HOH G 7 .   ? -28.045 11.597  5.293   1.00 11.30  ? 439 HOH A O   1 
HETATM 2365 O  O   . HOH G 7 .   ? -8.601  15.149  11.933  1.00 15.87  ? 440 HOH A O   1 
HETATM 2366 O  O   . HOH G 7 .   ? -6.266  -20.234 19.479  1.00 14.29  ? 441 HOH A O   1 
HETATM 2367 O  O   . HOH G 7 .   ? -13.224 19.930  15.024  1.00 20.44  ? 442 HOH A O   1 
HETATM 2368 O  O   . HOH G 7 .   ? -4.681  3.048   -6.016  1.00 17.16  ? 443 HOH A O   1 
HETATM 2369 O  O   . HOH G 7 .   ? 13.772  0.515   24.440  1.00 15.59  ? 444 HOH A O   1 
HETATM 2370 O  O   . HOH G 7 .   ? -8.046  -22.096 10.531  1.00 15.39  ? 445 HOH A O   1 
HETATM 2371 O  O   . HOH G 7 .   ? -10.118 8.761   25.369  1.00 11.48  ? 446 HOH A O   1 
HETATM 2372 O  O   . HOH G 7 .   ? -0.155  -8.475  32.399  1.00 21.84  ? 447 HOH A O   1 
HETATM 2373 O  O   . HOH G 7 .   ? -7.730  -19.323 21.605  1.00 16.70  ? 448 HOH A O   1 
HETATM 2374 O  O   . HOH G 7 .   ? -14.551 20.202  17.551  1.00 18.49  ? 449 HOH A O   1 
HETATM 2375 O  O   . HOH G 7 .   ? -12.523 -9.091  -3.266  1.00 13.57  ? 450 HOH A O   1 
HETATM 2376 O  O   . HOH G 7 .   ? 3.044   -13.519 5.045   1.00 14.15  ? 451 HOH A O   1 
HETATM 2377 O  O   . HOH G 7 .   ? -16.919 -16.172 21.996  1.00 21.66  ? 452 HOH A O   1 
HETATM 2378 O  O   . HOH G 7 .   ? -5.544  -4.961  -6.568  1.00 15.31  ? 453 HOH A O   1 
HETATM 2379 O  O   . HOH G 7 .   ? -6.574  -14.723 31.543  1.00 19.35  ? 454 HOH A O   1 
HETATM 2380 O  O   . HOH G 7 .   ? 5.566   -7.178  22.228  1.00 24.98  ? 455 HOH A O   1 
HETATM 2381 O  O   . HOH G 7 .   ? -15.882 -9.786  32.826  1.00 16.02  ? 456 HOH A O   1 
HETATM 2382 O  O   . HOH G 7 .   ? 2.285   -15.673 9.320   1.00 18.21  ? 457 HOH A O   1 
HETATM 2383 O  O   . HOH G 7 .   ? -9.220  -7.920  33.970  1.00 19.67  ? 458 HOH A O   1 
HETATM 2384 O  O   . HOH G 7 .   ? 1.872   8.811   23.842  1.00 15.44  ? 459 HOH A O   1 
HETATM 2385 O  O   . HOH G 7 .   ? -3.428  5.272   -2.882  1.00 13.69  ? 460 HOH A O   1 
HETATM 2386 O  O   . HOH G 7 .   ? -25.347 6.400   26.905  1.00 21.66  ? 461 HOH A O   1 
HETATM 2387 O  O   . HOH G 7 .   ? 7.959   6.238   21.677  1.00 14.22  ? 462 HOH A O   1 
HETATM 2388 O  O   . HOH G 7 .   ? 0.603   -15.870 -6.328  1.00 29.44  ? 463 HOH A O   1 
HETATM 2389 O  O   . HOH G 7 .   ? -8.260  7.845   9.438   1.00 18.23  ? 464 HOH A O   1 
HETATM 2390 O  O   . HOH G 7 .   ? -26.225 -3.798  25.081  1.00 17.28  ? 465 HOH A O   1 
HETATM 2391 O  O   . HOH G 7 .   ? -8.696  -5.742  35.847  1.00 17.22  ? 466 HOH A O   1 
HETATM 2392 O  O   . HOH G 7 .   ? -6.965  -8.596  32.533  1.00 15.47  ? 467 HOH A O   1 
HETATM 2393 O  O   . HOH G 7 .   ? -12.295 7.991   28.544  1.00 23.76  ? 468 HOH A O   1 
HETATM 2394 O  O   . HOH G 7 .   ? 11.634  1.515   25.954  1.00 19.30  ? 469 HOH A O   1 
HETATM 2395 O  O   . HOH G 7 .   ? -10.976 10.464  8.289   1.00 18.60  ? 470 HOH A O   1 
HETATM 2396 O  O   . HOH G 7 .   ? -3.805  -13.127 -3.174  1.00 17.36  ? 471 HOH A O   1 
HETATM 2397 O  O   . HOH G 7 .   ? -24.713 9.750   13.012  1.00 28.93  ? 472 HOH A O   1 
HETATM 2398 O  O   . HOH G 7 .   ? 1.732   -11.671 24.967  1.00 20.51  ? 473 HOH A O   1 
HETATM 2399 O  O   . HOH G 7 .   ? -8.162  -15.271 36.619  1.00 22.29  ? 474 HOH A O   1 
HETATM 2400 O  O   . HOH G 7 .   ? -23.565 8.719   19.983  1.00 19.39  ? 475 HOH A O   1 
HETATM 2401 O  O   . HOH G 7 .   ? -0.659  9.210   27.888  1.00 21.43  ? 476 HOH A O   1 
HETATM 2402 O  O   . HOH G 7 .   ? -22.956 -13.261 11.352  1.00 17.20  ? 477 HOH A O   1 
HETATM 2403 O  O   . HOH G 7 .   ? -25.260 7.975   6.201   1.00 19.75  ? 478 HOH A O   1 
HETATM 2404 O  O   . HOH G 7 .   ? -15.631 -12.288 24.360  1.00 13.43  ? 479 HOH A O   1 
HETATM 2405 O  O   . HOH G 7 .   ? -24.214 12.005  6.102   1.00 15.94  ? 480 HOH A O   1 
HETATM 2406 O  O   . HOH G 7 .   ? 1.849   -6.295  34.288  1.00 25.26  ? 481 HOH A O   1 
HETATM 2407 O  O   . HOH G 7 .   ? -0.711  -11.042 28.904  1.00 16.04  ? 482 HOH A O   1 
HETATM 2408 O  O   . HOH G 7 .   ? 2.951   -11.617 9.512   1.00 19.91  ? 483 HOH A O   1 
HETATM 2409 O  O   . HOH G 7 .   ? -21.897 3.939   -3.116  1.00 18.90  ? 484 HOH A O   1 
HETATM 2410 O  O   . HOH G 7 .   ? -8.680  5.371   2.791   1.00 14.93  ? 485 HOH A O   1 
HETATM 2411 O  O   . HOH G 7 .   ? -1.107  11.241  25.624  1.00 24.94  ? 486 HOH A O   1 
HETATM 2412 O  O   . HOH G 7 .   ? 10.956  -9.207  8.991   1.00 24.08  ? 487 HOH A O   1 
HETATM 2413 O  O   . HOH G 7 .   ? -3.718  -15.647 -2.278  1.00 17.98  ? 488 HOH A O   1 
HETATM 2414 O  O   . HOH G 7 .   ? 8.391   -9.244  16.509  1.00 19.14  ? 489 HOH A O   1 
HETATM 2415 O  O   . HOH G 7 .   ? -19.068 -20.829 4.857   1.00 16.35  ? 490 HOH A O   1 
HETATM 2416 O  O   . HOH G 7 .   ? 11.192  -9.150  -0.171  1.00 24.01  ? 491 HOH A O   1 
HETATM 2417 O  O   . HOH G 7 .   ? 13.401  -5.731  24.481  1.00 23.48  ? 492 HOH A O   1 
HETATM 2418 O  O   . HOH G 7 .   ? 4.860   -2.487  28.879  1.00 22.78  ? 493 HOH A O   1 
HETATM 2419 O  O   . HOH G 7 .   ? -4.538  15.710  12.080  1.00 26.43  ? 494 HOH A O   1 
HETATM 2420 O  O   . HOH G 7 .   ? -15.223 8.943   -2.194  1.00 21.58  ? 495 HOH A O   1 
HETATM 2421 O  O   . HOH G 7 .   ? -14.238 -18.429 18.675  1.00 15.90  ? 496 HOH A O   1 
HETATM 2422 O  O   . HOH G 7 .   ? -10.570 13.075  8.197   1.00 18.57  ? 497 HOH A O   1 
HETATM 2423 O  O   . HOH G 7 .   ? 14.974  0.150   14.929  1.00 20.57  ? 498 HOH A O   1 
HETATM 2424 O  O   . HOH G 7 .   ? -8.596  5.993   28.774  1.00 18.09  ? 499 HOH A O   1 
HETATM 2425 O  O   . HOH G 7 .   ? -6.895  -16.823 1.232   1.00 17.99  ? 500 HOH A O   1 
HETATM 2426 O  O   . HOH G 7 .   ? -21.667 -18.383 13.546  1.00 24.80  ? 501 HOH A O   1 
HETATM 2427 O  O   . HOH G 7 .   ? -0.115  10.654  23.275  1.00 21.07  ? 502 HOH A O   1 
HETATM 2428 O  O   . HOH G 7 .   ? -9.284  1.538   38.945  1.00 28.23  ? 503 HOH A O   1 
HETATM 2429 O  O   . HOH G 7 .   ? -1.011  -5.456  -7.342  1.00 22.56  ? 504 HOH A O   1 
HETATM 2430 O  O   . HOH G 7 .   ? 15.652  -2.404  14.245  1.00 14.10  ? 505 HOH A O   1 
HETATM 2431 O  O   . HOH G 7 .   ? -18.977 -12.251 -3.382  1.00 13.56  ? 506 HOH A O   1 
HETATM 2432 O  O   . HOH G 7 .   ? -19.766 10.875  26.550  1.00 20.98  ? 507 HOH A O   1 
HETATM 2433 O  O   . HOH G 7 .   ? -23.425 -0.506  26.394  1.00 14.53  ? 508 HOH A O   1 
HETATM 2434 O  O   . HOH G 7 .   ? -16.396 -13.894 26.279  1.00 21.30  ? 509 HOH A O   1 
HETATM 2435 O  O   . HOH G 7 .   ? -9.131  13.026  10.311  1.00 16.03  ? 510 HOH A O   1 
HETATM 2436 O  O   . HOH G 7 .   ? -18.183 -4.109  -2.738  1.00 21.48  ? 511 HOH A O   1 
HETATM 2437 O  O   . HOH G 7 .   ? 4.706   -3.362  26.362  1.00 17.44  ? 512 HOH A O   1 
HETATM 2438 O  O   . HOH G 7 .   ? -4.361  -15.996 0.563   1.00 17.62  ? 513 HOH A O   1 
HETATM 2439 O  O   . HOH G 7 .   ? 0.170   -14.244 22.127  1.00 20.18  ? 514 HOH A O   1 
HETATM 2440 O  O   . HOH G 7 .   ? -1.204  -12.643 -3.876  1.00 24.21  ? 515 HOH A O   1 
HETATM 2441 O  O   . HOH G 7 .   ? 13.356  -3.678  13.262  1.00 22.74  ? 516 HOH A O   1 
HETATM 2442 O  O   . HOH G 7 .   ? -26.185 10.134  4.698   1.00 18.30  ? 517 HOH A O   1 
HETATM 2443 O  O   . HOH G 7 .   ? -23.521 -7.468  0.003   1.00 36.44  ? 518 HOH A O   1 
HETATM 2444 O  O   . HOH G 7 .   ? 0.288   1.155   34.404  1.00 22.21  ? 519 HOH A O   1 
HETATM 2445 O  O   . HOH G 7 .   ? -12.941 -18.441 14.509  1.00 15.30  ? 520 HOH A O   1 
HETATM 2446 O  O   . HOH G 7 .   ? -3.758  -8.428  31.066  1.00 17.45  ? 521 HOH A O   1 
HETATM 2447 O  O   . HOH G 7 .   ? -17.303 19.939  17.403  1.00 22.26  ? 522 HOH A O   1 
HETATM 2448 O  O   . HOH G 7 .   ? -7.664  6.279   0.257   1.00 14.16  ? 523 HOH A O   1 
HETATM 2449 O  O   . HOH G 7 .   ? 4.956   -6.837  7.883   1.00 22.75  ? 524 HOH A O   1 
HETATM 2450 O  O   . HOH G 7 .   ? -15.700 16.014  23.472  1.00 20.50  ? 525 HOH A O   1 
HETATM 2451 O  O   . HOH G 7 .   ? -19.216 -4.128  41.236  1.00 33.85  ? 526 HOH A O   1 
HETATM 2452 O  O   . HOH G 7 .   ? -7.904  -17.457 34.773  1.00 22.19  ? 527 HOH A O   1 
HETATM 2453 O  O   . HOH G 7 .   ? 4.834   -3.841  3.446   1.00 35.13  ? 528 HOH A O   1 
HETATM 2454 O  O   . HOH G 7 .   ? -14.559 2.672   38.482  1.00 27.60  ? 529 HOH A O   1 
HETATM 2455 O  O   . HOH G 7 .   ? -6.175  -5.260  37.251  1.00 18.94  ? 530 HOH A O   1 
HETATM 2456 O  O   . HOH G 7 .   ? 3.398   -4.641  7.475   1.00 18.06  ? 531 HOH A O   1 
HETATM 2457 O  O   . HOH G 7 .   ? 14.903  2.956   23.617  1.00 20.79  ? 532 HOH A O   1 
HETATM 2458 O  O   . HOH G 7 .   ? -0.327  2.949   -5.415  1.00 28.11  ? 533 HOH A O   1 
HETATM 2459 O  O   . HOH G 7 .   ? -6.579  -8.777  -7.308  1.00 23.60  ? 534 HOH A O   1 
HETATM 2460 O  O   . HOH G 7 .   ? -25.826 13.752  6.531   1.00 16.71  ? 535 HOH A O   1 
HETATM 2461 O  O   . HOH G 7 .   ? 5.626   -12.701 5.481   1.00 21.18  ? 536 HOH A O   1 
HETATM 2462 O  O   . HOH G 7 .   ? -13.584 14.495  26.996  1.00 25.87  ? 537 HOH A O   1 
HETATM 2463 O  O   . HOH G 7 .   ? 5.207   -11.128 7.944   1.00 28.75  ? 538 HOH A O   1 
HETATM 2464 O  O   . HOH G 7 .   ? -12.492 -19.436 26.077  1.00 23.60  ? 539 HOH A O   1 
HETATM 2465 O  O   . HOH G 7 .   ? -12.788 -0.826  -5.817  1.00 19.56  ? 540 HOH A O   1 
HETATM 2466 O  O   . HOH G 7 .   ? -14.104 -21.200 2.937   1.00 30.85  ? 541 HOH A O   1 
HETATM 2467 O  O   . HOH G 7 .   ? -12.124 -18.280 32.138  1.00 26.37  ? 542 HOH A O   1 
HETATM 2468 O  O   . HOH G 7 .   ? 8.693   -10.004 -7.083  1.00 31.11  ? 543 HOH A O   1 
HETATM 2469 O  O   . HOH G 7 .   ? -21.167 19.593  17.297  1.00 35.08  ? 544 HOH A O   1 
HETATM 2470 O  O   . HOH G 7 .   ? -26.185 -1.050  25.863  1.00 18.21  ? 545 HOH A O   1 
HETATM 2471 O  O   . HOH G 7 .   ? -26.304 3.588   20.820  1.00 30.79  ? 546 HOH A O   1 
HETATM 2472 O  O   . HOH G 7 .   ? 1.143   2.296   1.618   1.00 18.70  ? 547 HOH A O   1 
HETATM 2473 O  O   . HOH G 7 .   ? -10.054 5.099   30.640  1.00 22.98  ? 548 HOH A O   1 
HETATM 2474 O  O   . HOH G 7 .   ? -1.101  -16.108 -3.305  1.00 21.83  ? 549 HOH A O   1 
HETATM 2475 O  O   . HOH G 7 .   ? -24.156 4.622   8.549   1.00 27.53  ? 550 HOH A O   1 
HETATM 2476 O  O   . HOH G 7 .   ? -10.059 -5.768  38.322  1.00 24.39  ? 551 HOH A O   1 
HETATM 2477 O  O   . HOH G 7 .   ? 15.149  -10.313 14.497  1.00 24.62  ? 552 HOH A O   1 
HETATM 2478 O  O   . HOH G 7 .   ? 4.234   8.947   22.307  1.00 24.31  ? 553 HOH A O   1 
HETATM 2479 O  O   . HOH G 7 .   ? 8.260   -6.094  0.298   1.00 29.63  ? 554 HOH A O   1 
HETATM 2480 O  O   . HOH G 7 .   ? 16.038  -14.658 8.832   1.00 26.26  ? 555 HOH A O   1 
HETATM 2481 O  O   . HOH G 7 .   ? -2.758  -18.051 0.647   1.00 22.48  ? 556 HOH A O   1 
HETATM 2482 O  O   . HOH G 7 .   ? 5.369   3.043   3.444   1.00 26.82  ? 557 HOH A O   1 
HETATM 2483 O  O   . HOH G 7 .   ? -25.812 -7.209  30.532  1.00 38.76  ? 558 HOH A O   1 
HETATM 2484 O  O   . HOH G 7 .   ? -11.752 16.416  9.695   1.00 26.67  ? 559 HOH A O   1 
HETATM 2485 O  O   . HOH G 7 .   ? -3.201  -19.863 6.391   1.00 23.60  ? 560 HOH A O   1 
HETATM 2486 O  O   . HOH G 7 .   ? -8.922  -21.359 8.237   1.00 23.22  ? 561 HOH A O   1 
HETATM 2487 O  O   . HOH G 7 .   ? 11.902  -7.701  -6.266  1.00 24.30  ? 562 HOH A O   1 
HETATM 2488 O  O   . HOH G 7 .   ? -13.561 -16.257 -0.400  1.00 31.24  ? 563 HOH A O   1 
HETATM 2489 O  O   . HOH G 7 .   ? -1.473  -17.326 25.507  1.00 29.49  ? 564 HOH A O   1 
HETATM 2490 O  O   . HOH G 7 .   ? -6.474  5.272   -6.223  1.00 24.65  ? 565 HOH A O   1 
HETATM 2491 O  O   . HOH G 7 .   ? 2.046   2.634   5.224   1.00 24.69  ? 566 HOH A O   1 
HETATM 2492 O  O   . HOH G 7 .   ? -17.147 17.726  3.994   1.00 30.76  ? 567 HOH A O   1 
HETATM 2493 O  O   . HOH G 7 .   ? -7.846  0.324   -6.586  1.00 20.31  ? 568 HOH A O   1 
HETATM 2494 O  O   . HOH G 7 .   ? 1.981   -9.403  -5.036  1.00 25.36  ? 569 HOH A O   1 
HETATM 2495 O  O   . HOH G 7 .   ? -23.815 -17.765 6.482   1.00 58.60  ? 570 HOH A O   1 
HETATM 2496 O  O   . HOH G 7 .   ? -4.797  -13.416 34.115  1.00 44.42  ? 571 HOH A O   1 
HETATM 2497 O  O   . HOH G 7 .   ? -9.833  3.325   37.269  1.00 42.36  ? 572 HOH A O   1 
HETATM 2498 O  O   . HOH G 7 .   ? -6.551  1.598   35.045  1.00 23.43  ? 573 HOH A O   1 
HETATM 2499 O  O   . HOH G 7 .   ? 12.263  0.473   28.590  1.00 33.40  ? 574 HOH A O   1 
HETATM 2500 O  O   . HOH G 7 .   ? -8.494  -3.935  7.767   1.00 15.77  ? 575 HOH A O   1 
HETATM 2501 O  O   . HOH G 7 .   ? -21.550 -14.050 18.563  1.00 29.22  ? 576 HOH A O   1 
HETATM 2502 O  O   . HOH G 7 .   ? -9.183  10.095  -5.976  1.00 31.44  ? 577 HOH A O   1 
HETATM 2503 O  O   . HOH G 7 .   ? 10.664  -10.740 16.177  1.00 17.82  ? 578 HOH A O   1 
HETATM 2504 O  O   . HOH G 7 .   ? 12.003  -6.654  7.781   1.00 34.96  ? 579 HOH A O   1 
HETATM 2505 O  O   . HOH G 7 .   ? -10.048 -20.355 24.913  1.00 22.49  ? 580 HOH A O   1 
HETATM 2506 O  O   . HOH G 7 .   ? -22.944 -11.068 17.122  1.00 22.74  ? 581 HOH A O   1 
HETATM 2507 O  O   . HOH G 7 .   ? -2.628  4.788   -6.579  1.00 21.97  ? 582 HOH A O   1 
HETATM 2508 O  O   . HOH G 7 .   ? -1.638  -11.709 31.512  1.00 29.89  ? 583 HOH A O   1 
HETATM 2509 O  O   . HOH G 7 .   ? 9.148   -4.665  23.612  1.00 23.07  ? 584 HOH A O   1 
HETATM 2510 O  O   . HOH G 7 .   ? 10.779  -2.526  13.342  1.00 23.49  ? 585 HOH A O   1 
HETATM 2511 O  O   . HOH G 7 .   ? -22.186 -9.489  25.168  1.00 22.78  ? 586 HOH A O   1 
HETATM 2512 O  O   . HOH G 7 .   ? 3.846   -0.945  4.950   1.00 27.67  ? 587 HOH A O   1 
HETATM 2513 O  O   . HOH G 7 .   ? -2.673  -19.941 26.617  1.00 42.53  ? 588 HOH A O   1 
HETATM 2514 O  O   . HOH G 7 .   ? -5.686  -18.601 3.052   1.00 41.36  ? 589 HOH A O   1 
HETATM 2515 O  O   . HOH G 7 .   ? -12.400 -22.094 8.597   1.00 29.15  ? 590 HOH A O   1 
HETATM 2516 O  O   . HOH G 7 .   ? -14.972 19.610  13.114  1.00 21.87  ? 591 HOH A O   1 
HETATM 2517 O  O   . HOH G 7 .   ? -10.710 -15.112 34.104  1.00 24.55  ? 592 HOH A O   1 
HETATM 2518 O  O   . HOH G 7 .   ? 8.684   7.962   23.811  1.00 37.11  ? 593 HOH A O   1 
HETATM 2519 O  O   . HOH G 7 .   ? -25.700 3.400   15.414  1.00 26.79  ? 594 HOH A O   1 
HETATM 2520 O  O   . HOH G 7 .   ? -11.915 12.570  29.089  1.00 28.11  ? 595 HOH A O   1 
HETATM 2521 O  O   . HOH G 7 .   ? -7.245  -18.028 -1.451  1.00 43.87  ? 596 HOH A O   1 
HETATM 2522 O  O   . HOH G 7 .   ? 11.652  -6.852  22.468  1.00 28.11  ? 597 HOH A O   1 
HETATM 2523 O  O   . HOH G 7 .   ? 1.905   -17.864 13.932  1.00 36.09  ? 598 HOH A O   1 
HETATM 2524 O  O   . HOH G 7 .   ? 14.395  -12.005 15.977  1.00 38.20  ? 599 HOH A O   1 
HETATM 2525 O  O   . HOH G 7 .   ? -17.749 -8.856  34.627  1.00 30.19  ? 600 HOH A O   1 
HETATM 2526 O  O   . HOH G 7 .   ? -26.232 -6.275  5.007   1.00 27.96  ? 601 HOH A O   1 
HETATM 2527 O  O   . HOH G 7 .   ? -0.913  -17.656 18.165  1.00 29.25  ? 602 HOH A O   1 
HETATM 2528 O  O   . HOH G 7 .   ? -25.154 -10.515 17.400  1.00 25.82  ? 603 HOH A O   1 
HETATM 2529 O  O   . HOH G 7 .   ? -19.167 17.364  5.998   1.00 27.16  ? 604 HOH A O   1 
HETATM 2530 O  O   . HOH G 7 .   ? 6.868   -5.192  27.333  1.00 37.97  ? 605 HOH A O   1 
HETATM 2531 O  O   . HOH G 7 .   ? -5.655  -19.684 23.813  1.00 22.97  ? 606 HOH A O   1 
HETATM 2532 O  O   . HOH G 7 .   ? -17.382 -12.006 31.451  1.00 27.99  ? 607 HOH A O   1 
HETATM 2533 O  O   . HOH G 7 .   ? 9.885   -8.340  3.641   1.00 34.40  ? 608 HOH A O   1 
HETATM 2534 O  O   . HOH G 7 .   ? -16.028 -15.356 32.691  1.00 34.01  ? 609 HOH A O   1 
HETATM 2535 O  O   . HOH G 7 .   ? -17.597 14.005  2.096   1.00 44.03  ? 610 HOH A O   1 
HETATM 2536 O  O   . HOH G 7 .   ? 14.393  -1.378  28.455  1.00 30.84  ? 611 HOH A O   1 
HETATM 2537 O  O   . HOH G 7 .   ? -18.321 20.111  14.785  1.00 26.75  ? 612 HOH A O   1 
HETATM 2538 O  O   . HOH G 7 .   ? -7.970  -19.822 26.540  1.00 26.08  ? 613 HOH A O   1 
HETATM 2539 O  O   . HOH G 7 .   ? -13.573 3.773   32.978  1.00 26.08  ? 614 HOH A O   1 
HETATM 2540 O  O   . HOH G 7 .   ? 12.580  4.284   27.262  1.00 32.93  ? 615 HOH A O   1 
HETATM 2541 O  O   . HOH G 7 .   ? -24.578 8.804   26.053  1.00 29.48  ? 616 HOH A O   1 
HETATM 2542 O  O   . HOH G 7 .   ? -27.941 15.142  6.783   1.00 25.88  ? 617 HOH A O   1 
HETATM 2543 O  O   . HOH G 7 .   ? 6.368   -0.773  -1.178  1.00 29.21  ? 618 HOH A O   1 
HETATM 2544 O  O   . HOH G 7 .   ? 2.173   8.141   27.983  1.00 24.82  ? 619 HOH A O   1 
HETATM 2545 O  O   . HOH G 7 .   ? 0.869   -0.300  -7.015  1.00 29.89  ? 620 HOH A O   1 
HETATM 2546 O  O   . HOH G 7 .   ? 9.036   -12.971 16.190  1.00 31.60  ? 621 HOH A O   1 
HETATM 2547 O  O   . HOH G 7 .   ? -29.211 9.676   6.072   1.00 26.86  ? 622 HOH A O   1 
HETATM 2548 O  O   . HOH G 7 .   ? -16.112 -14.729 28.679  1.00 30.99  ? 623 HOH A O   1 
HETATM 2549 O  O   . HOH G 7 .   ? -4.247  -8.625  -8.674  1.00 36.75  ? 624 HOH A O   1 
HETATM 2550 O  O   . HOH G 7 .   ? -14.542 6.245   32.625  1.00 33.81  ? 625 HOH A O   1 
HETATM 2551 O  O   . HOH G 7 .   ? -14.992 -10.101 37.713  1.00 28.73  ? 626 HOH A O   1 
HETATM 2552 O  O   . HOH G 7 .   ? -22.392 -14.739 16.204  1.00 33.62  ? 627 HOH A O   1 
HETATM 2553 O  O   . HOH G 7 .   ? -10.709 -19.612 7.308   1.00 31.09  ? 628 HOH A O   1 
HETATM 2554 O  O   . HOH G 7 .   ? -9.482  15.814  29.637  1.00 33.41  ? 629 HOH A O   1 
HETATM 2555 O  O   . HOH G 7 .   ? 0.453   -19.805 10.951  1.00 30.87  ? 630 HOH A O   1 
HETATM 2556 O  O   . HOH G 7 .   ? 3.987   -8.906  25.416  1.00 37.41  ? 631 HOH A O   1 
HETATM 2557 O  O   . HOH G 7 .   ? -3.437  -6.131  -8.088  1.00 23.96  ? 632 HOH A O   1 
HETATM 2558 O  O   . HOH G 7 .   ? -12.389 13.221  31.804  1.00 30.30  ? 633 HOH A O   1 
HETATM 2559 O  O   . HOH G 7 .   ? -21.603 15.650  3.569   1.00 31.96  ? 634 HOH A O   1 
HETATM 2560 O  O   . HOH G 7 .   ? -22.617 15.463  18.291  1.00 38.57  ? 635 HOH A O   1 
HETATM 2561 O  O   . HOH G 7 .   ? -12.786 -22.420 11.786  1.00 32.36  ? 636 HOH A O   1 
HETATM 2562 O  O   . HOH G 7 .   ? -10.202 17.454  11.882  1.00 19.11  ? 637 HOH A O   1 
HETATM 2563 O  O   . HOH G 7 .   ? -6.371  -19.627 5.338   1.00 33.01  ? 638 HOH A O   1 
HETATM 2564 O  O   . HOH G 7 .   ? -25.582 -6.304  12.785  1.00 23.51  ? 639 HOH A O   1 
HETATM 2565 O  O   . HOH G 7 .   ? 2.448   -14.043 20.611  1.00 28.23  ? 640 HOH A O   1 
HETATM 2566 O  O   . HOH G 7 .   ? -2.378  -17.589 5.209   1.00 29.01  ? 641 HOH A O   1 
HETATM 2567 O  O   . HOH G 7 .   ? -17.227 11.089  -1.959  1.00 20.38  ? 642 HOH A O   1 
HETATM 2568 O  O   . HOH G 7 .   ? 14.449  5.254   25.290  1.00 24.76  ? 643 HOH A O   1 
HETATM 2569 O  O   . HOH G 7 .   ? 14.815  -6.972  7.654   1.00 32.15  ? 644 HOH A O   1 
HETATM 2570 O  O   . HOH G 7 .   ? -10.052 -18.240 17.233  1.00 14.00  ? 645 HOH A O   1 
HETATM 2571 O  O   . HOH G 7 .   ? 6.590   -3.935  -10.561 1.00 17.65  ? 646 HOH A O   1 
HETATM 2572 O  O   . HOH G 7 .   ? -22.654 -0.260  34.282  1.00 22.79  ? 647 HOH A O   1 
HETATM 2573 O  O   . HOH G 7 .   ? -19.776 17.796  3.912   1.00 20.86  ? 648 HOH A O   1 
HETATM 2574 O  O   . HOH G 7 .   ? -16.553 -13.938 37.555  1.00 24.37  ? 649 HOH A O   1 
HETATM 2575 O  O   . HOH G 7 .   ? -23.454 -2.442  28.955  1.00 29.35  ? 650 HOH A O   1 
HETATM 2576 O  O   . HOH G 7 .   ? -20.296 18.915  13.598  1.00 23.08  ? 651 HOH A O   1 
HETATM 2577 O  O   . HOH G 7 .   ? -31.157 5.360   12.764  1.00 35.35  ? 652 HOH A O   1 
HETATM 2578 O  O   . HOH G 7 .   ? -4.185  8.210   9.963   1.00 29.60  ? 653 HOH A O   1 
HETATM 2579 O  O   . HOH G 7 .   ? -24.735 11.179  19.477  1.00 29.29  ? 654 HOH A O   1 
HETATM 2580 O  O   . HOH G 7 .   ? -16.496 -18.106 20.225  1.00 27.72  ? 655 HOH A O   1 
HETATM 2581 O  O   . HOH G 7 .   ? -20.262 2.083   -3.712  1.00 34.70  ? 656 HOH A O   1 
HETATM 2582 O  O   . HOH G 7 .   ? 4.905   -1.418  -5.464  1.00 23.56  ? 657 HOH A O   1 
HETATM 2583 O  O   . HOH G 7 .   ? -17.037 0.273   -3.776  1.00 28.65  ? 658 HOH A O   1 
HETATM 2584 O  O   . HOH G 7 .   ? -14.479 0.299   -3.670  1.00 27.60  ? 659 HOH A O   1 
HETATM 2585 O  O   . HOH G 7 .   ? -5.376  17.391  27.236  1.00 29.50  ? 660 HOH A O   1 
HETATM 2586 O  O   . HOH G 7 .   ? -15.000 -20.205 22.738  1.00 40.32  ? 661 HOH A O   1 
HETATM 2587 O  O   . HOH G 7 .   ? 14.134  0.032   6.335   1.00 29.05  ? 662 HOH A O   1 
HETATM 2588 O  O   . HOH G 7 .   ? 0.231   3.181   12.465  1.00 22.48  ? 663 HOH A O   1 
HETATM 2589 O  O   . HOH G 7 .   ? -23.778 -0.123  1.187   1.00 31.47  ? 664 HOH A O   1 
HETATM 2590 O  O   . HOH G 7 .   ? -18.484 17.689  18.630  1.00 26.37  ? 665 HOH A O   1 
HETATM 2591 O  O   . HOH G 7 .   ? 11.871  -0.415  15.763  1.00 25.93  ? 666 HOH A O   1 
HETATM 2592 O  O   . HOH G 7 .   ? -6.978  8.151   29.527  1.00 24.05  ? 667 HOH A O   1 
HETATM 2593 O  O   . HOH G 7 .   ? -1.988  2.797   -7.392  1.00 26.68  ? 668 HOH A O   1 
HETATM 2594 O  O   . HOH G 7 .   ? 3.937   -13.178 12.099  1.00 41.08  ? 669 HOH A O   1 
HETATM 2595 O  O   . HOH G 7 .   ? -4.548  -9.602  33.480  1.00 31.60  ? 670 HOH A O   1 
HETATM 2596 O  O   . HOH G 7 .   ? 5.947   -9.015  6.995   1.00 29.96  ? 671 HOH A O   1 
HETATM 2597 O  O   . HOH G 7 .   ? -10.115 21.638  19.978  1.00 21.94  ? 672 HOH A O   1 
HETATM 2598 O  O   . HOH G 7 .   ? -17.327 6.390   38.448  1.00 37.27  ? 673 HOH A O   1 
HETATM 2599 O  O   . HOH G 7 .   ? -11.792 14.229  -2.605  1.00 53.89  ? 674 HOH A O   1 
HETATM 2600 O  O   . HOH G 7 .   ? 11.522  -3.424  7.448   1.00 40.34  ? 675 HOH A O   1 
HETATM 2601 O  O   . HOH G 7 .   ? -14.184 -2.876  -7.025  1.00 32.55  ? 676 HOH A O   1 
HETATM 2602 O  O   . HOH G 7 .   ? 4.277   -11.800 23.380  1.00 39.40  ? 677 HOH A O   1 
HETATM 2603 O  O   . HOH G 7 .   ? 9.212   -12.231 8.326   1.00 45.49  ? 678 HOH A O   1 
HETATM 2604 O  O   . HOH G 7 .   ? -26.844 -7.419  25.876  1.00 31.02  ? 679 HOH A O   1 
HETATM 2605 O  O   . HOH G 7 .   ? -4.744  10.224  15.135  1.00 26.96  ? 680 HOH A O   1 
HETATM 2606 O  O   . HOH G 7 .   ? -10.387 -22.734 1.086   1.00 38.65  ? 681 HOH A O   1 
HETATM 2607 O  O   . HOH G 7 .   ? 6.918   -2.816  1.340   1.00 36.25  ? 682 HOH A O   1 
HETATM 2608 O  O   . HOH G 7 .   ? 6.860   -9.105  -10.096 1.00 28.26  ? 683 HOH A O   1 
HETATM 2609 O  O   . HOH G 7 .   ? 8.557   3.338   27.754  1.00 29.94  ? 684 HOH A O   1 
HETATM 2610 O  O   . HOH G 7 .   ? 9.941   2.240   11.990  1.00 34.78  ? 685 HOH A O   1 
HETATM 2611 O  O   . HOH G 7 .   ? 6.602   -10.658 15.091  1.00 33.82  ? 686 HOH A O   1 
HETATM 2612 O  O   . HOH G 7 .   ? -25.199 -1.056  34.852  1.00 31.53  ? 687 HOH A O   1 
HETATM 2613 O  O   . HOH G 7 .   ? -11.973 14.030  1.406   1.00 31.15  ? 688 HOH A O   1 
HETATM 2614 O  O   . HOH G 7 .   ? 6.409   9.404   24.354  1.00 46.28  ? 689 HOH A O   1 
HETATM 2615 O  O   . HOH G 7 .   ? -18.215 12.288  12.604  1.00 21.94  ? 690 HOH A O   1 
HETATM 2616 O  O   . HOH G 7 .   ? 4.597   -7.728  -11.110 1.00 30.39  ? 691 HOH A O   1 
HETATM 2617 O  O   . HOH G 7 .   ? -19.991 8.457   29.915  1.00 28.14  ? 692 HOH A O   1 
HETATM 2618 O  O   . HOH G 7 .   ? -12.025 3.902   -6.982  1.00 28.55  ? 693 HOH A O   1 
HETATM 2619 O  O   . HOH G 7 .   ? -31.007 7.081   15.505  1.00 46.08  ? 694 HOH A O   1 
HETATM 2620 O  O   . HOH G 7 .   ? -26.775 -10.804 22.253  1.00 35.12  ? 695 HOH A O   1 
HETATM 2621 O  O   . HOH G 7 .   ? -24.601 18.103  6.473   1.00 39.28  ? 696 HOH A O   1 
HETATM 2622 O  O   . HOH G 7 .   ? -21.696 19.707  12.044  1.00 37.00  ? 697 HOH A O   1 
HETATM 2623 O  O   . HOH G 7 .   ? -25.432 -6.345  33.842  1.00 87.45  ? 698 HOH A O   1 
HETATM 2624 O  O   . HOH G 7 .   ? 6.208   0.976   8.340   1.00 24.78  ? 699 HOH A O   1 
HETATM 2625 O  O   . HOH G 7 .   ? 6.063   -3.656  6.567   1.00 39.07  ? 700 HOH A O   1 
HETATM 2626 O  O   . HOH G 7 .   ? 9.844   7.720   18.331  1.00 34.06  ? 701 HOH A O   1 
HETATM 2627 O  O   . HOH G 7 .   ? 3.789   10.270  18.570  1.00 35.41  ? 702 HOH A O   1 
HETATM 2628 O  O   . HOH G 7 .   ? 1.802   11.077  17.163  1.00 38.45  ? 703 HOH A O   1 
HETATM 2629 O  O   . HOH G 7 .   ? 2.121   12.552  23.028  1.00 38.84  ? 704 HOH A O   1 
HETATM 2630 O  O   . HOH G 7 .   ? 1.916   2.403   35.979  1.00 35.30  ? 705 HOH A O   1 
HETATM 2631 O  O   . HOH G 7 .   ? 0.665   -3.012  39.151  1.00 35.34  ? 706 HOH A O   1 
HETATM 2632 O  O   . HOH G 7 .   ? -3.927  -1.430  37.882  1.00 27.67  ? 707 HOH A O   1 
HETATM 2633 O  O   . HOH G 7 .   ? -15.347 3.841   35.177  1.00 32.24  ? 708 HOH A O   1 
HETATM 2634 O  O   . HOH G 7 .   ? -14.569 5.883   36.756  1.00 34.71  ? 709 HOH A O   1 
HETATM 2635 O  O   . HOH G 7 .   ? -28.894 7.320   6.677   1.00 34.30  ? 710 HOH A O   1 
HETATM 2636 O  O   . HOH G 7 .   ? -24.101 15.409  5.358   1.00 30.20  ? 711 HOH A O   1 
HETATM 2637 O  O   . HOH G 7 .   ? -12.702 9.746   -2.904  1.00 31.71  ? 712 HOH A O   1 
HETATM 2638 O  O   . HOH G 7 .   ? -12.319 10.076  -5.907  1.00 42.76  ? 713 HOH A O   1 
HETATM 2639 O  O   . HOH G 7 .   ? -10.000 6.134   -6.699  1.00 38.55  ? 714 HOH A O   1 
HETATM 2640 O  O   . HOH G 7 .   ? -6.383  -2.409  -8.550  1.00 34.23  ? 715 HOH A O   1 
HETATM 2641 O  O   . HOH G 7 .   ? -2.108  4.744   9.116   1.00 31.60  ? 716 HOH A O   1 
HETATM 2642 O  O   . HOH G 7 .   ? -6.250  6.964   11.066  1.00 28.33  ? 717 HOH A O   1 
HETATM 2643 O  O   . HOH G 7 .   ? -1.544  8.564   6.874   1.00 35.46  ? 718 HOH A O   1 
HETATM 2644 O  O   . HOH G 7 .   ? -12.136 6.959   30.986  1.00 30.49  ? 719 HOH A O   1 
HETATM 2645 O  O   . HOH G 7 .   ? -15.631 17.102  26.207  1.00 31.69  ? 720 HOH A O   1 
HETATM 2646 O  O   . HOH G 7 .   ? -14.794 -16.039 25.219  1.00 36.90  ? 721 HOH A O   1 
HETATM 2647 O  O   . HOH G 7 .   ? -2.244  17.658  14.385  1.00 36.38  ? 722 HOH A O   1 
HETATM 2648 O  O   . HOH G 7 .   ? -2.899  17.988  21.002  1.00 30.97  ? 723 HOH A O   1 
HETATM 2649 O  O   . HOH G 7 .   ? -5.326  -13.002 -5.512  1.00 32.95  ? 724 HOH A O   1 
HETATM 2650 O  O   . HOH G 7 .   ? -29.061 -9.540  22.373  1.00 47.93  ? 725 HOH A O   1 
HETATM 2651 O  O   . HOH G 7 .   ? -10.607 1.165   33.358  1.00 25.61  ? 726 HOH A O   1 
HETATM 2652 O  O   . HOH G 7 .   ? -23.849 -10.350 15.159  1.00 27.38  ? 727 HOH A O   1 
HETATM 2653 O  O   . HOH G 7 .   ? 0.335   -7.861  -7.569  1.00 35.34  ? 728 HOH A O   1 
HETATM 2654 O  O   . HOH G 7 .   ? 7.493   -1.343  -4.766  1.00 42.68  ? 729 HOH A O   1 
HETATM 2655 O  O   . HOH G 7 .   ? 2.157   -9.634  30.341  1.00 48.43  ? 730 HOH A O   1 
HETATM 2656 O  O   . HOH G 7 .   ? 5.674   -11.001 18.830  1.00 42.96  ? 731 HOH A O   1 
HETATM 2657 O  O   . HOH G 7 .   ? -24.766 6.286   3.080   1.00 30.68  ? 732 HOH A O   1 
HETATM 2658 O  O   . HOH G 7 .   ? -2.119  22.022  21.623  1.00 33.73  ? 733 HOH A O   1 
HETATM 2659 O  O   . HOH G 7 .   ? -24.036 -20.598 8.724   1.00 51.15  ? 734 HOH A O   1 
HETATM 2660 O  O   . HOH G 7 .   ? -23.411 -3.411  3.886   1.00 31.81  ? 735 HOH A O   1 
HETATM 2661 O  O   . HOH G 7 .   ? -27.302 6.306   20.934  1.00 42.84  ? 736 HOH A O   1 
HETATM 2662 O  O   . HOH G 7 .   ? 4.294   -9.869  -5.910  1.00 28.65  ? 737 HOH A O   1 
HETATM 2663 O  O   . HOH G 7 .   ? -14.324 9.684   31.197  1.00 36.15  ? 738 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   A HIS A 4   ? 0.2547 0.1756 0.1923 0.0261  0.0599  0.0153  4   HIS A N   
2    N  N   B HIS A 4   ? 0.1136 0.1732 0.1488 0.0283  0.0516  0.0781  4   HIS A N   
3    C  CA  A HIS A 4   ? 0.1771 0.2861 0.3179 0.0498  0.0882  0.1859  4   HIS A CA  
4    C  CA  B HIS A 4   ? 0.2232 0.2323 0.4063 0.0588  0.1070  0.1128  4   HIS A CA  
5    C  C   A HIS A 4   ? 0.1309 0.2160 0.2370 0.0003  -0.0068 0.1045  4   HIS A C   
6    C  C   B HIS A 4   ? 0.2802 0.2725 0.2675 0.0342  0.0166  0.0925  4   HIS A C   
7    O  O   A HIS A 4   ? 0.2431 0.2118 0.2411 -0.0329 -0.0151 0.0957  4   HIS A O   
8    O  O   B HIS A 4   ? 0.1685 0.2773 0.2786 -0.0507 -0.0049 0.0328  4   HIS A O   
9    C  CB  A HIS A 4   ? 0.1849 0.1682 0.3348 0.0377  0.0291  0.0847  4   HIS A CB  
10   C  CB  B HIS A 4   ? 0.1925 0.2664 0.5953 0.1594  0.0445  0.0364  4   HIS A CB  
11   C  CG  A HIS A 4   ? 0.1199 0.2651 0.1791 0.0124  -0.0869 -0.0031 4   HIS A CG  
12   C  CG  B HIS A 4   ? 0.3467 0.2063 0.4758 -0.1303 0.0054  0.0010  4   HIS A CG  
13   N  ND1 A HIS A 4   ? 0.2739 0.2949 0.3411 -0.0126 -0.0348 -0.1111 4   HIS A ND1 
14   N  ND1 B HIS A 4   ? 0.2144 0.3370 0.3239 -0.0631 -0.0328 -0.1018 4   HIS A ND1 
15   C  CD2 A HIS A 4   ? 0.1127 0.1947 0.1766 -0.0049 -0.0126 0.0351  4   HIS A CD2 
16   C  CD2 B HIS A 4   ? 0.2782 0.3289 0.4465 -0.1736 -0.0719 0.0566  4   HIS A CD2 
17   C  CE1 A HIS A 4   ? 0.3734 0.2240 0.3745 0.0392  0.0581  0.0794  4   HIS A CE1 
18   C  CE1 B HIS A 4   ? 0.2187 0.4988 0.2433 -0.0680 0.1237  -0.0456 4   HIS A CE1 
19   N  NE2 A HIS A 4   ? 0.4719 0.3323 0.2325 -0.0196 0.0307  -0.0599 4   HIS A NE2 
20   N  NE2 B HIS A 4   ? 0.3131 0.4187 0.1607 0.0178  0.0865  -0.0052 4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1586 0.2829 0.3497 0.0131  0.0520  0.0820  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1206 0.2079 0.2743 -0.0195 -0.0035 0.0670  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1455 0.2267 0.1784 0.0344  0.0273  0.0054  5   TRP A C   
24   O  O   . TRP A 5   ? 0.1368 0.2424 0.2040 0.0164  0.0252  0.0485  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1128 0.2086 0.2969 -0.0209 -0.0175 0.0182  5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1550 0.2090 0.1961 -0.0186 0.0204  0.0417  5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.1981 0.2185 0.2171 0.0082  0.0351  0.0627  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1430 0.1959 0.1623 0.0136  0.0164  0.0132  5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.2228 0.2027 0.2249 0.0232  0.0328  0.0631  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1783 0.2086 0.1474 0.0013  0.0208  0.0081  5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1229 0.2081 0.1387 -0.0302 0.0142  -0.0344 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1532 0.2603 0.1676 0.0230  0.0310  0.0012  5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1395 0.2346 0.1357 -0.0046 0.0351  -0.0208 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1315 0.2298 0.1542 0.0164  0.0076  -0.0102 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1332 0.2001 0.2001 0.0124  0.0178  0.0049  6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1349 0.2147 0.1669 0.0137  0.0141  -0.0063 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.0937 0.1966 0.1506 0.0003  0.0163  -0.0065 6   GLY A C   
38   O  O   . GLY A 6   ? 0.0987 0.1908 0.1379 -0.0020 0.0239  -0.0216 6   GLY A O   
39   N  N   . TYR A 7   ? 0.1404 0.2151 0.1685 -0.0291 0.0307  -0.0335 7   TYR A N   
40   C  CA  . TYR A 7   ? 0.1058 0.2022 0.1987 -0.0065 0.0085  -0.0524 7   TYR A CA  
41   C  C   . TYR A 7   ? 0.1563 0.2296 0.2461 0.0126  -0.0015 -0.0326 7   TYR A C   
42   O  O   . TYR A 7   ? 0.2041 0.2417 0.4460 -0.0020 0.0944  -0.0806 7   TYR A O   
43   C  CB  . TYR A 7   ? 0.1315 0.2036 0.1842 -0.0219 0.0425  -0.0675 7   TYR A CB  
44   C  CG  . TYR A 7   ? 0.1058 0.1758 0.1490 -0.0372 0.0238  -0.0252 7   TYR A CG  
45   C  CD1 . TYR A 7   ? 0.0955 0.1727 0.1411 -0.0230 0.0080  -0.0324 7   TYR A CD1 
46   C  CD2 . TYR A 7   ? 0.1298 0.1643 0.1553 -0.0335 0.0081  -0.0238 7   TYR A CD2 
47   C  CE1 . TYR A 7   ? 0.0970 0.1167 0.1553 -0.0288 0.0006  -0.0098 7   TYR A CE1 
48   C  CE2 . TYR A 7   ? 0.1498 0.1603 0.1274 -0.0458 0.0125  -0.0156 7   TYR A CE2 
49   C  CZ  . TYR A 7   ? 0.1448 0.1250 0.1225 -0.0337 0.0273  -0.0082 7   TYR A CZ  
50   O  OH  . TYR A 7   ? 0.2018 0.1401 0.1218 -0.0010 0.0076  -0.0052 7   TYR A OH  
51   N  N   . GLY A 8   ? 0.1536 0.2496 0.1975 0.0136  0.0197  -0.0702 8   GLY A N   
52   C  CA  . GLY A 8   ? 0.1650 0.2572 0.2822 0.0131  0.0575  -0.0781 8   GLY A CA  
53   C  C   . GLY A 8   ? 0.1729 0.2106 0.2820 -0.0222 0.0505  -0.0631 8   GLY A C   
54   O  O   . GLY A 8   ? 0.1342 0.2328 0.2601 0.0035  0.0535  -0.0292 8   GLY A O   
55   N  N   . LYS A 9   ? 0.1886 0.2680 0.3073 0.0218  0.0653  -0.0579 9   LYS A N   
56   C  CA  . LYS A 9   ? 0.1914 0.2021 0.3499 0.0175  0.0305  -0.0299 9   LYS A CA  
57   C  C   . LYS A 9   ? 0.1906 0.2350 0.2388 0.0027  0.0593  -0.0274 9   LYS A C   
58   O  O   . LYS A 9   ? 0.1867 0.2025 0.2820 -0.0012 0.0416  0.0227  9   LYS A O   
59   C  CB  . LYS A 9   ? 0.2065 0.2386 0.5475 0.0252  0.0313  -0.0285 9   LYS A CB  
60   C  CG  . LYS A 9   ? 0.3709 0.2314 0.4964 0.0516  -0.0471 -0.0087 9   LYS A CG  
61   C  CD  . LYS A 9   ? 0.7203 0.2119 0.7451 -0.0040 0.2011  -0.0172 9   LYS A CD  
62   C  CE  . LYS A 9   ? 0.9620 0.6290 0.7978 0.1588  0.0687  -0.3235 9   LYS A CE  
63   N  NZ  . LYS A 9   ? 1.0843 0.6614 1.5937 0.1369  0.2662  -0.4672 9   LYS A NZ  
64   N  N   . HIS A 10  ? 0.1650 0.2119 0.2240 0.0483  0.0755  -0.0099 10  HIS A N   
65   C  CA  . HIS A 10  ? 0.1579 0.2034 0.2291 0.0115  0.0873  0.0093  10  HIS A CA  
66   C  C   . HIS A 10  ? 0.1509 0.1793 0.1905 0.0531  0.0104  -0.0010 10  HIS A C   
67   O  O   . HIS A 10  ? 0.1480 0.2010 0.2372 0.0364  0.0375  0.0006  10  HIS A O   
68   C  CB  . HIS A 10  ? 0.1615 0.2215 0.2052 0.0324  0.0882  0.0304  10  HIS A CB  
69   C  CG  . HIS A 10  ? 0.1792 0.2137 0.1732 0.0046  0.0186  0.0159  10  HIS A CG  
70   N  ND1 . HIS A 10  ? 0.1914 0.2276 0.2775 0.0549  0.0132  0.0006  10  HIS A ND1 
71   C  CD2 . HIS A 10  ? 0.1756 0.1969 0.1791 -0.0068 0.0631  -0.0124 10  HIS A CD2 
72   C  CE1 . HIS A 10  ? 0.2391 0.2282 0.1993 0.0621  -0.0040 0.0109  10  HIS A CE1 
73   N  NE2 . HIS A 10  ? 0.1960 0.2170 0.2228 0.0034  0.0324  -0.0005 10  HIS A NE2 
74   N  N   . ASN A 11  ? 0.1211 0.1923 0.1978 0.0271  0.0595  0.0231  11  ASN A N   
75   C  CA  . ASN A 11  ? 0.1330 0.1635 0.1925 0.0186  0.0483  0.0006  11  ASN A CA  
76   C  C   . ASN A 11  ? 0.1164 0.1776 0.1474 0.0177  0.0305  -0.0060 11  ASN A C   
77   O  O   . ASN A 11  ? 0.1137 0.1660 0.1526 0.0154  0.0244  -0.0049 11  ASN A O   
78   C  CB  . ASN A 11  ? 0.1263 0.1805 0.2171 0.0051  0.0274  0.0183  11  ASN A CB  
79   C  CG  . ASN A 11  ? 0.1633 0.2284 0.1352 -0.0049 0.0648  0.0041  11  ASN A CG  
80   O  OD1 . ASN A 11  ? 0.1870 0.2420 0.1890 -0.0186 0.0087  -0.0071 11  ASN A OD1 
81   N  ND2 . ASN A 11  ? 0.2377 0.2757 0.1509 0.0115  0.0557  0.0184  11  ASN A ND2 
82   N  N   . GLY A 12  ? 0.1113 0.1701 0.1550 0.0041  0.0394  0.0026  12  GLY A N   
83   C  CA  . GLY A 12  ? 0.0929 0.1931 0.1766 0.0040  0.0362  -0.0294 12  GLY A CA  
84   C  C   . GLY A 12  ? 0.0988 0.1473 0.1383 0.0027  0.0251  -0.0019 12  GLY A C   
85   O  O   . GLY A 12  ? 0.0863 0.1463 0.1523 0.0063  0.0126  0.0017  12  GLY A O   
86   N  N   . PRO A 13  ? 0.0995 0.1456 0.1428 -0.0041 0.0222  -0.0046 13  PRO A N   
87   C  CA  . PRO A 13  ? 0.0891 0.1325 0.1445 -0.0041 0.0174  -0.0013 13  PRO A CA  
88   C  C   . PRO A 13  ? 0.1058 0.1137 0.1415 -0.0073 0.0397  0.0031  13  PRO A C   
89   O  O   . PRO A 13  ? 0.0971 0.1573 0.1553 0.0000  0.0142  -0.0252 13  PRO A O   
90   C  CB  . PRO A 13  ? 0.1053 0.1509 0.1244 -0.0197 0.0247  -0.0137 13  PRO A CB  
91   C  CG  . PRO A 13  ? 0.1317 0.1524 0.1318 -0.0148 0.0328  -0.0261 13  PRO A CG  
92   C  CD  . PRO A 13  ? 0.1023 0.1787 0.1535 -0.0167 0.0419  -0.0206 13  PRO A CD  
93   N  N   . GLU A 14  ? 0.1200 0.1255 0.1712 0.0027  0.0040  0.0113  14  GLU A N   
94   C  CA  . GLU A 14  ? 0.1606 0.1383 0.1888 0.0054  -0.0142 0.0259  14  GLU A CA  
95   C  C   . GLU A 14  ? 0.1208 0.1261 0.1511 0.0232  -0.0006 0.0031  14  GLU A C   
96   O  O   . GLU A 14  ? 0.1360 0.1676 0.1657 0.0299  -0.0159 0.0159  14  GLU A O   
97   C  CB  . GLU A 14  ? 0.1720 0.1535 0.2942 0.0043  -0.0403 0.0465  14  GLU A CB  
98   C  CG  . GLU A 14  ? 0.2908 0.1594 0.3907 -0.0306 0.0255  0.0353  14  GLU A CG  
99   C  CD  . GLU A 14  ? 0.2908 0.2653 0.4553 0.0843  -0.0383 0.0049  14  GLU A CD  
100  O  OE1 . GLU A 14  ? 0.6118 0.5770 0.2964 -0.2736 -0.0768 0.1773  14  GLU A OE1 
101  O  OE2 . GLU A 14  ? 0.3210 0.2842 0.4907 -0.0026 0.0533  -0.0711 14  GLU A OE2 
102  N  N   . HIS A 15  ? 0.1014 0.1289 0.1351 0.0108  0.0000  -0.0012 15  HIS A N   
103  C  CA  . HIS A 15  ? 0.0743 0.1403 0.1498 0.0054  0.0120  0.0141  15  HIS A CA  
104  C  C   . HIS A 15  ? 0.0769 0.1351 0.1444 0.0081  0.0020  0.0054  15  HIS A C   
105  O  O   . HIS A 15  ? 0.0627 0.1509 0.1710 0.0051  0.0155  -0.0020 15  HIS A O   
106  C  CB  . HIS A 15  ? 0.0901 0.1308 0.1507 0.0186  0.0076  -0.0057 15  HIS A CB  
107  C  CG  . HIS A 15  ? 0.1098 0.1475 0.1511 0.0219  0.0204  0.0147  15  HIS A CG  
108  N  ND1 . HIS A 15  ? 0.1146 0.1934 0.1738 0.0392  0.0098  -0.0126 15  HIS A ND1 
109  C  CD2 . HIS A 15  ? 0.1344 0.1694 0.1754 0.0273  0.0063  0.0152  15  HIS A CD2 
110  C  CE1 . HIS A 15  ? 0.1994 0.1791 0.2151 0.0564  0.0085  0.0063  15  HIS A CE1 
111  N  NE2 . HIS A 15  ? 0.1693 0.1704 0.2217 0.0306  0.0337  -0.0230 15  HIS A NE2 
112  N  N   . TRP A 16  ? 0.0662 0.1224 0.1395 0.0142  0.0087  0.0003  16  TRP A N   
113  C  CA  . TRP A 16  ? 0.0597 0.1190 0.1598 0.0160  -0.0054 -0.0146 16  TRP A CA  
114  C  C   . TRP A 16  ? 0.0693 0.1137 0.1397 0.0017  0.0026  -0.0088 16  TRP A C   
115  O  O   . TRP A 16  ? 0.0732 0.1243 0.1568 -0.0068 -0.0104 0.0000  16  TRP A O   
116  C  CB  . TRP A 16  ? 0.0601 0.1244 0.1405 -0.0048 0.0027  -0.0074 16  TRP A CB  
117  C  CG  . TRP A 16  ? 0.0706 0.1234 0.1254 0.0000  0.0126  -0.0019 16  TRP A CG  
118  C  CD1 . TRP A 16  ? 0.0843 0.1455 0.1263 0.0013  0.0125  -0.0017 16  TRP A CD1 
119  C  CD2 . TRP A 16  ? 0.0610 0.1177 0.1230 0.0076  0.0147  0.0000  16  TRP A CD2 
120  N  NE1 . TRP A 16  ? 0.0706 0.1324 0.1393 0.0074  0.0046  -0.0097 16  TRP A NE1 
121  C  CE2 . TRP A 16  ? 0.0744 0.1211 0.1304 0.0024  0.0003  -0.0041 16  TRP A CE2 
122  C  CE3 . TRP A 16  ? 0.0750 0.1071 0.1395 0.0000  0.0093  0.0034  16  TRP A CE3 
123  C  CZ2 . TRP A 16  ? 0.0805 0.1474 0.1492 -0.0035 -0.0024 0.0000  16  TRP A CZ2 
124  C  CZ3 . TRP A 16  ? 0.0866 0.1157 0.1295 -0.0020 -0.0015 0.0017  16  TRP A CZ3 
125  C  CH2 . TRP A 16  ? 0.0970 0.1263 0.1154 -0.0131 0.0065  0.0005  16  TRP A CH2 
126  N  N   . HIS A 17  ? 0.0688 0.1208 0.1463 0.0102  -0.0013 -0.0037 17  HIS A N   
127  C  CA  . HIS A 17  ? 0.0709 0.1414 0.1428 -0.0076 -0.0093 0.0027  17  HIS A CA  
128  C  C   . HIS A 17  ? 0.0620 0.1489 0.1439 -0.0043 -0.0006 -0.0140 17  HIS A C   
129  O  O   . HIS A 17  ? 0.0887 0.1507 0.1727 -0.0092 -0.0175 -0.0208 17  HIS A O   
130  C  CB  . HIS A 17  ? 0.0740 0.1576 0.1527 0.0092  0.0120  0.0142  17  HIS A CB  
131  C  CG  . HIS A 17  ? 0.0883 0.1571 0.1247 0.0109  -0.0003 0.0125  17  HIS A CG  
132  N  ND1 . HIS A 17  ? 0.0891 0.1756 0.1736 0.0038  -0.0041 0.0251  17  HIS A ND1 
133  C  CD2 . HIS A 17  ? 0.1150 0.1563 0.1649 0.0348  0.0051  0.0207  17  HIS A CD2 
134  C  CE1 . HIS A 17  ? 0.1173 0.2030 0.1652 0.0406  -0.0035 0.0344  17  HIS A CE1 
135  N  NE2 . HIS A 17  ? 0.1121 0.1767 0.1782 0.0460  0.0162  0.0188  17  HIS A NE2 
136  N  N   . LYS A 18  ? 0.0653 0.1607 0.1474 -0.0003 0.0038  -0.0060 18  LYS A N   
137  C  CA  . LYS A 18  ? 0.0491 0.1793 0.1802 -0.0115 0.0068  0.0038  18  LYS A CA  
138  C  C   . LYS A 18  ? 0.0771 0.1941 0.1885 -0.0181 -0.0071 0.0192  18  LYS A C   
139  O  O   . LYS A 18  ? 0.1579 0.2257 0.3055 -0.0948 -0.0498 0.0684  18  LYS A O   
140  C  CB  . LYS A 18  ? 0.0832 0.1841 0.1714 0.0156  0.0071  0.0182  18  LYS A CB  
141  C  CG  . LYS A 18  ? 0.1141 0.1985 0.1428 0.0524  0.0277  0.0121  18  LYS A CG  
142  C  CD  . LYS A 18  ? 0.1058 0.1958 0.1753 0.0251  -0.0046 0.0152  18  LYS A CD  
143  C  CE  . LYS A 18  ? 0.1141 0.1652 0.1789 0.0208  0.0154  0.0227  18  LYS A CE  
144  N  NZ  . LYS A 18  ? 0.0869 0.1966 0.1685 0.0266  0.0167  0.0320  18  LYS A NZ  
145  N  N   . ASP A 19  ? 0.0884 0.1861 0.1731 0.0071  -0.0023 0.0143  19  ASP A N   
146  C  CA  . ASP A 19  ? 0.1215 0.1826 0.1717 -0.0102 0.0184  0.0119  19  ASP A CA  
147  C  C   . ASP A 19  ? 0.1158 0.1261 0.1967 -0.0153 0.0160  0.0087  19  ASP A C   
148  O  O   . ASP A 19  ? 0.1242 0.1561 0.2293 -0.0342 0.0304  0.0219  19  ASP A O   
149  C  CB  . ASP A 19  ? 0.1527 0.2370 0.1455 0.0129  0.0076  0.0248  19  ASP A CB  
150  C  CG  . ASP A 19  ? 0.1630 0.2975 0.3813 0.0113  0.0803  -0.1032 19  ASP A CG  
151  O  OD1 . ASP A 19  ? 0.2225 0.3165 0.3097 0.0263  0.0812  0.0263  19  ASP A OD1 
152  O  OD2 . ASP A 19  ? 0.4167 0.3562 0.4444 0.0023  0.1509  -0.0961 19  ASP A OD2 
153  N  N   . PHE A 20  ? 0.0856 0.1287 0.1512 -0.0063 0.0054  0.0103  20  PHE A N   
154  C  CA  . PHE A 20  ? 0.0803 0.1375 0.1597 -0.0110 0.0015  0.0049  20  PHE A CA  
155  C  C   . PHE A 20  ? 0.0755 0.1412 0.1500 -0.0065 0.0171  -0.0092 20  PHE A C   
156  O  O   . PHE A 20  ? 0.0891 0.1211 0.1703 -0.0071 0.0080  -0.0003 20  PHE A O   
157  C  CB  . PHE A 20  ? 0.0881 0.1992 0.1942 -0.0195 -0.0164 0.0286  20  PHE A CB  
158  C  CG  . PHE A 20  ? 0.0643 0.2115 0.2149 -0.0137 -0.0080 0.0538  20  PHE A CG  
159  C  CD1 . PHE A 20  ? 0.1102 0.2496 0.2838 -0.0193 -0.0342 0.0859  20  PHE A CD1 
160  C  CD2 . PHE A 20  ? 0.0917 0.2989 0.1920 -0.0370 -0.0103 0.0228  20  PHE A CD2 
161  C  CE1 . PHE A 20  ? 0.1141 0.2662 0.2549 -0.0427 -0.0388 0.1005  20  PHE A CE1 
162  C  CE2 . PHE A 20  ? 0.1206 0.3079 0.1921 -0.0377 -0.0125 0.0283  20  PHE A CE2 
163  C  CZ  . PHE A 20  ? 0.1114 0.3242 0.2467 -0.0340 0.0115  0.0820  20  PHE A CZ  
164  N  N   A PRO A 21  ? 0.0931 0.1632 0.1712 -0.0155 -0.0031 -0.0057 21  PRO A N   
165  N  N   B PRO A 21  ? 0.0761 0.1414 0.1580 -0.0287 0.0110  0.0048  21  PRO A N   
166  C  CA  A PRO A 21  ? 0.0875 0.1476 0.1853 -0.0253 -0.0087 -0.0148 21  PRO A CA  
167  C  CA  B PRO A 21  ? 0.0735 0.1754 0.1553 -0.0452 -0.0107 -0.0006 21  PRO A CA  
168  C  C   A PRO A 21  ? 0.1019 0.1052 0.1508 -0.0140 -0.0219 0.0027  21  PRO A C   
169  C  C   B PRO A 21  ? 0.0840 0.1247 0.1367 -0.0087 -0.0228 -0.0038 21  PRO A C   
170  O  O   A PRO A 21  ? 0.0983 0.1313 0.1467 0.0054  -0.0164 0.0038  21  PRO A O   
171  O  O   B PRO A 21  ? 0.0706 0.1040 0.1631 -0.0030 -0.0275 -0.0020 21  PRO A O   
172  C  CB  A PRO A 21  ? 0.1215 0.1567 0.1745 -0.0480 -0.0196 0.0104  21  PRO A CB  
173  C  CB  B PRO A 21  ? 0.0983 0.1613 0.1485 -0.0277 -0.0177 0.0024  21  PRO A CB  
174  C  CG  A PRO A 21  ? 0.1718 0.2183 0.1361 -0.0333 0.0068  -0.0249 21  PRO A CG  
175  C  CG  B PRO A 21  ? 0.1603 0.1687 0.2120 -0.0803 -0.0340 0.0031  21  PRO A CG  
176  C  CD  A PRO A 21  ? 0.1163 0.1667 0.1098 -0.0173 0.0318  -0.0272 21  PRO A CD  
177  C  CD  B PRO A 21  ? 0.0708 0.1386 0.1753 -0.0326 0.0399  -0.0306 21  PRO A CD  
178  N  N   A ILE A 22  ? 0.0761 0.1239 0.1075 -0.0099 -0.0093 -0.0120 22  ILE A N   
179  N  N   B ILE A 22  ? 0.0790 0.1412 0.1269 -0.0141 -0.0185 0.0183  22  ILE A N   
180  C  CA  A ILE A 22  ? 0.0921 0.1151 0.1159 -0.0166 -0.0166 0.0057  22  ILE A CA  
181  C  CA  B ILE A 22  ? 0.0829 0.1155 0.1252 -0.0107 -0.0188 0.0275  22  ILE A CA  
182  C  C   A ILE A 22  ? 0.0750 0.1243 0.1203 -0.0198 -0.0113 -0.0052 22  ILE A C   
183  C  C   B ILE A 22  ? 0.0762 0.1308 0.1304 -0.0137 -0.0098 0.0027  22  ILE A C   
184  O  O   A ILE A 22  ? 0.0988 0.1131 0.1481 0.0012  0.0087  0.0163  22  ILE A O   
185  O  O   B ILE A 22  ? 0.0873 0.1142 0.1243 -0.0087 -0.0076 0.0034  22  ILE A O   
186  C  CB  A ILE A 22  ? 0.1104 0.1030 0.0785 0.0027  0.0121  -0.0027 22  ILE A CB  
187  C  CB  B ILE A 22  ? 0.0911 0.1139 0.1148 -0.0098 -0.0060 0.0104  22  ILE A CB  
188  C  CG1 A ILE A 22  ? 0.1339 0.1280 0.0883 0.0038  0.0222  -0.0093 22  ILE A CG1 
189  C  CG1 B ILE A 22  ? 0.1212 0.1536 0.1718 0.0220  0.0065  0.0076  22  ILE A CG1 
190  C  CG2 A ILE A 22  ? 0.1098 0.1297 0.1067 -0.0454 -0.0126 -0.0059 22  ILE A CG2 
191  C  CG2 B ILE A 22  ? 0.1215 0.1237 0.1132 0.0153  -0.0270 0.0324  22  ILE A CG2 
192  C  CD1 A ILE A 22  ? 0.1124 0.1448 0.1676 0.0077  0.0024  0.0063  22  ILE A CD1 
193  C  CD1 B ILE A 22  ? 0.1456 0.1975 0.2239 -0.0335 0.0129  -0.0584 22  ILE A CD1 
194  N  N   . ALA A 23  ? 0.0815 0.1191 0.1368 -0.0093 -0.0173 -0.0104 23  ALA A N   
195  C  CA  . ALA A 23  ? 0.0878 0.1339 0.1333 0.0003  -0.0147 -0.0114 23  ALA A CA  
196  C  C   . ALA A 23  ? 0.0833 0.1314 0.1463 0.0063  0.0010  -0.0162 23  ALA A C   
197  O  O   . ALA A 23  ? 0.1137 0.1307 0.1668 -0.0060 0.0043  -0.0057 23  ALA A O   
198  C  CB  . ALA A 23  ? 0.0768 0.1315 0.1432 -0.0060 -0.0015 -0.0102 23  ALA A CB  
199  N  N   . LYS A 24  ? 0.1074 0.1629 0.1262 -0.0006 -0.0092 0.0020  24  LYS A N   
200  C  CA  . LYS A 24  ? 0.1024 0.1634 0.1615 0.0097  0.0017  0.0054  24  LYS A CA  
201  C  C   . LYS A 24  ? 0.1199 0.1888 0.1456 -0.0038 -0.0037 -0.0076 24  LYS A C   
202  O  O   . LYS A 24  ? 0.1379 0.2181 0.1499 -0.0142 -0.0188 0.0103  24  LYS A O   
203  C  CB  . LYS A 24  ? 0.1019 0.1905 0.1703 0.0130  -0.0020 0.0071  24  LYS A CB  
204  C  CG  . LYS A 24  ? 0.1377 0.2185 0.1949 0.0469  -0.0164 0.0031  24  LYS A CG  
205  C  CD  . LYS A 24  ? 0.1562 0.2707 0.2621 0.0715  -0.0176 0.0186  24  LYS A CD  
206  C  CE  . LYS A 24  ? 0.1580 0.3012 0.2599 0.0649  0.0295  0.0540  24  LYS A CE  
207  N  NZ  . LYS A 24  ? 0.2286 0.2745 0.4526 -0.0152 0.0731  0.0005  24  LYS A NZ  
208  N  N   . GLY A 25  ? 0.1031 0.1745 0.1419 0.0057  -0.0034 -0.0125 25  GLY A N   
209  C  CA  . GLY A 25  ? 0.1439 0.2055 0.1544 -0.0065 0.0119  -0.0436 25  GLY A CA  
210  C  C   . GLY A 25  ? 0.1058 0.1843 0.1172 0.0087  -0.0175 -0.0326 25  GLY A C   
211  O  O   . GLY A 25  ? 0.1168 0.1871 0.1544 0.0006  -0.0120 -0.0162 25  GLY A O   
212  N  N   . GLU A 26  ? 0.0894 0.2162 0.1404 -0.0003 -0.0292 -0.0476 26  GLU A N   
213  C  CA  . GLU A 26  ? 0.1154 0.2370 0.1173 -0.0043 -0.0052 -0.0339 26  GLU A CA  
214  C  C   . GLU A 26  ? 0.1156 0.1659 0.1246 -0.0142 -0.0137 -0.0015 26  GLU A C   
215  O  O   . GLU A 26  ? 0.1546 0.2061 0.0907 -0.0137 -0.0219 0.0070  26  GLU A O   
216  C  CB  . GLU A 26  ? 0.1779 0.2924 0.1456 -0.0487 -0.0535 -0.0674 26  GLU A CB  
217  C  CG  . GLU A 26  ? 0.1723 0.3422 0.1720 0.0071  -0.0432 -0.0658 26  GLU A CG  
218  C  CD  . GLU A 26  ? 0.2651 0.4419 0.2063 -0.0373 -0.1045 -0.0419 26  GLU A CD  
219  O  OE1 . GLU A 26  ? 0.3977 0.6103 0.2921 -0.0172 -0.0520 0.0428  26  GLU A OE1 
220  O  OE2 . GLU A 26  ? 0.3003 0.5740 0.5328 0.0493  -0.1071 -0.0126 26  GLU A OE2 
221  N  N   . ARG A 27  ? 0.1066 0.1314 0.0974 0.0017  -0.0068 -0.0156 27  ARG A N   
222  C  CA  . ARG A 27  ? 0.0919 0.1136 0.1024 0.0109  -0.0153 -0.0026 27  ARG A CA  
223  C  C   . ARG A 27  ? 0.0962 0.1184 0.0909 -0.0197 -0.0183 -0.0027 27  ARG A C   
224  O  O   . ARG A 27  ? 0.0864 0.1215 0.1034 0.0015  -0.0035 -0.0012 27  ARG A O   
225  C  CB  . ARG A 27  ? 0.1517 0.1411 0.0979 0.0059  -0.0103 -0.0340 27  ARG A CB  
226  C  CG  . ARG A 27  ? 0.1604 0.1647 0.1517 -0.0087 -0.0115 -0.0114 27  ARG A CG  
227  C  CD  . ARG A 27  ? 0.2050 0.1931 0.1526 0.0048  -0.0231 -0.0129 27  ARG A CD  
228  N  NE  . ARG A 27  ? 0.1825 0.1503 0.1198 -0.0010 0.0219  -0.0087 27  ARG A NE  
229  C  CZ  . ARG A 27  ? 0.1739 0.1694 0.1216 0.0274  0.0063  -0.0102 27  ARG A CZ  
230  N  NH1 . ARG A 27  ? 0.1763 0.2147 0.1879 0.0052  0.0065  -0.1010 27  ARG A NH1 
231  N  NH2 . ARG A 27  ? 0.1805 0.1773 0.1578 -0.0076 -0.0135 -0.0194 27  ARG A NH2 
232  N  N   . GLN A 28  ? 0.0926 0.1019 0.0850 -0.0060 -0.0060 -0.0057 28  GLN A N   
233  C  CA  . GLN A 28  ? 0.0864 0.1066 0.0848 -0.0073 -0.0104 -0.0093 28  GLN A CA  
234  C  C   . GLN A 28  ? 0.0884 0.0987 0.0895 -0.0010 -0.0065 0.0082  28  GLN A C   
235  O  O   . GLN A 28  ? 0.0971 0.1233 0.0806 -0.0109 -0.0049 -0.0020 28  GLN A O   
236  C  CB  . GLN A 28  ? 0.0806 0.1155 0.1041 0.0052  -0.0071 0.0065  28  GLN A CB  
237  C  CG  . GLN A 28  ? 0.0951 0.1215 0.1084 -0.0126 -0.0126 0.0006  28  GLN A CG  
238  C  CD  . GLN A 28  ? 0.0778 0.1077 0.1111 -0.0173 -0.0141 -0.0142 28  GLN A CD  
239  O  OE1 . GLN A 28  ? 0.0900 0.1093 0.1105 -0.0161 -0.0091 -0.0007 28  GLN A OE1 
240  N  NE2 . GLN A 28  ? 0.0681 0.1192 0.1264 -0.0035 -0.0081 -0.0131 28  GLN A NE2 
241  N  N   . SER A 29  ? 0.0680 0.1000 0.0790 -0.0010 0.0005  -0.0088 29  SER A N   
242  C  CA  . SER A 29  ? 0.0803 0.0776 0.0767 -0.0023 -0.0057 -0.0119 29  SER A CA  
243  C  C   . SER A 29  ? 0.0615 0.0857 0.0744 0.0013  -0.0013 0.0035  29  SER A C   
244  O  O   . SER A 29  ? 0.0865 0.1005 0.0805 -0.0082 0.0108  -0.0031 29  SER A O   
245  C  CB  . SER A 29  ? 0.0858 0.0943 0.0891 0.0074  -0.0052 -0.0063 29  SER A CB  
246  O  OG  . SER A 29  ? 0.0864 0.0925 0.0963 -0.0019 -0.0007 -0.0098 29  SER A OG  
247  N  N   . PRO A 30  ? 0.0803 0.0794 0.0829 -0.0010 0.0000  0.0000  30  PRO A N   
248  C  CA  . PRO A 30  ? 0.0873 0.0855 0.0877 -0.0104 0.0010  0.0013  30  PRO A CA  
249  C  C   . PRO A 30  ? 0.0770 0.0864 0.0873 0.0041  -0.0060 -0.0043 30  PRO A C   
250  O  O   . PRO A 30  ? 0.0811 0.0953 0.0873 0.0082  -0.0080 -0.0003 30  PRO A O   
251  C  CB  . PRO A 30  ? 0.0838 0.0900 0.0741 0.0063  0.0012  -0.0074 30  PRO A CB  
252  C  CG  . PRO A 30  ? 0.0796 0.0903 0.0875 0.0038  0.0135  -0.0038 30  PRO A CG  
253  C  CD  . PRO A 30  ? 0.0891 0.0892 0.0851 0.0012  0.0054  -0.0082 30  PRO A CD  
254  N  N   . VAL A 31  ? 0.0882 0.0952 0.0936 0.0096  -0.0057 0.0051  31  VAL A N   
255  C  CA  . VAL A 31  ? 0.0988 0.0926 0.0873 -0.0041 -0.0065 0.0051  31  VAL A CA  
256  C  C   . VAL A 31  ? 0.0831 0.0969 0.0991 0.0171  0.0037  0.0096  31  VAL A C   
257  O  O   . VAL A 31  ? 0.0895 0.1059 0.0966 0.0031  -0.0037 0.0160  31  VAL A O   
258  C  CB  . VAL A 31  ? 0.0926 0.0965 0.1048 -0.0038 0.0000  -0.0043 31  VAL A CB  
259  C  CG1 . VAL A 31  ? 0.1280 0.1067 0.1040 -0.0098 0.0037  -0.0097 31  VAL A CG1 
260  C  CG2 . VAL A 31  ? 0.1032 0.1167 0.1093 0.0135  0.0153  -0.0086 31  VAL A CG2 
261  N  N   . ASP A 32  ? 0.1001 0.0957 0.0900 0.0063  -0.0054 0.0148  32  ASP A N   
262  C  CA  . ASP A 32  ? 0.1050 0.0908 0.1094 0.0131  0.0054  0.0173  32  ASP A CA  
263  C  C   . ASP A 32  ? 0.1040 0.1079 0.0839 0.0060  -0.0076 0.0115  32  ASP A C   
264  O  O   . ASP A 32  ? 0.1174 0.1412 0.1044 -0.0013 -0.0091 -0.0031 32  ASP A O   
265  C  CB  . ASP A 32  ? 0.1299 0.1049 0.1118 0.0031  0.0043  0.0219  32  ASP A CB  
266  C  CG  . ASP A 32  ? 0.1308 0.1084 0.1130 0.0172  -0.0052 0.0227  32  ASP A CG  
267  O  OD1 . ASP A 32  ? 0.1333 0.1057 0.1195 0.0020  -0.0088 0.0320  32  ASP A OD1 
268  O  OD2 . ASP A 32  ? 0.2072 0.1439 0.1226 -0.0220 -0.0081 0.0353  32  ASP A OD2 
269  N  N   . ILE A 33  ? 0.0975 0.1084 0.0894 0.0104  0.0031  0.0017  33  ILE A N   
270  C  CA  . ILE A 33  ? 0.1039 0.1128 0.0956 0.0104  0.0137  0.0051  33  ILE A CA  
271  C  C   . ILE A 33  ? 0.1190 0.1067 0.0944 0.0065  0.0155  0.0120  33  ILE A C   
272  O  O   . ILE A 33  ? 0.1357 0.1234 0.1067 0.0049  0.0115  0.0287  33  ILE A O   
273  C  CB  . ILE A 33  ? 0.1009 0.1145 0.1111 0.0086  0.0115  0.0271  33  ILE A CB  
274  C  CG1 . ILE A 33  ? 0.1113 0.1163 0.1280 0.0060  -0.0088 0.0276  33  ILE A CG1 
275  C  CG2 . ILE A 33  ? 0.1111 0.1421 0.1519 0.0244  0.0307  0.0184  33  ILE A CG2 
276  C  CD1 . ILE A 33  ? 0.1168 0.1483 0.1482 0.0052  -0.0170 0.0410  33  ILE A CD1 
277  N  N   A ASP A 34  ? 0.1537 0.1321 0.0996 0.0136  0.0131  0.0288  34  ASP A N   
278  N  N   B ASP A 34  ? 0.1387 0.1164 0.0926 0.0166  0.0302  0.0259  34  ASP A N   
279  C  CA  A ASP A 34  ? 0.1643 0.1280 0.0856 0.0074  0.0148  0.0027  34  ASP A CA  
280  C  CA  B ASP A 34  ? 0.1551 0.1324 0.1054 0.0388  0.0255  0.0390  34  ASP A CA  
281  C  C   A ASP A 34  ? 0.1864 0.1908 0.1071 0.0248  0.0370  0.0419  34  ASP A C   
282  C  C   B ASP A 34  ? 0.1635 0.1756 0.1052 0.0644  0.0124  0.0615  34  ASP A C   
283  O  O   A ASP A 34  ? 0.2144 0.1902 0.1063 0.0392  0.0229  0.0262  34  ASP A O   
284  O  O   B ASP A 34  ? 0.1699 0.2065 0.0919 0.0153  0.0428  0.0480  34  ASP A O   
285  C  CB  A ASP A 34  ? 0.2095 0.1468 0.0843 0.0220  0.0015  0.0200  34  ASP A CB  
286  C  CB  B ASP A 34  ? 0.2194 0.1595 0.0972 0.0524  0.0107  0.0163  34  ASP A CB  
287  C  CG  A ASP A 34  ? 0.1747 0.1515 0.0953 0.0564  0.0445  0.0118  34  ASP A CG  
288  C  CG  B ASP A 34  ? 0.2469 0.1692 0.1556 0.0258  0.0285  0.0082  34  ASP A CG  
289  O  OD1 A ASP A 34  ? 0.2933 0.2547 0.1806 -0.0450 -0.0714 0.1115  34  ASP A OD1 
290  O  OD1 B ASP A 34  ? 0.3343 0.2142 0.1243 0.0803  0.0135  0.0331  34  ASP A OD1 
291  O  OD2 A ASP A 34  ? 0.2061 0.2323 0.1356 0.0130  -0.0153 0.0775  34  ASP A OD2 
292  O  OD2 B ASP A 34  ? 0.2522 0.1626 0.1492 0.0465  0.0487  0.0156  34  ASP A OD2 
293  N  N   . THR A 35  ? 0.1676 0.1743 0.1018 0.0406  0.0328  0.0469  35  THR A N   
294  C  CA  . THR A 35  ? 0.1808 0.1588 0.1729 0.0401  0.0579  0.0666  35  THR A CA  
295  C  C   . THR A 35  ? 0.2059 0.1463 0.1544 0.0476  0.0680  0.0551  35  THR A C   
296  O  O   . THR A 35  ? 0.2219 0.1949 0.1536 0.0788  0.0375  0.0357  35  THR A O   
297  C  CB  . THR A 35  ? 0.1696 0.2011 0.1798 0.0274  0.0485  0.0559  35  THR A CB  
298  O  OG1 . THR A 35  ? 0.1735 0.1928 0.1973 0.0049  0.0388  0.0741  35  THR A OG1 
299  C  CG2 . THR A 35  ? 0.1834 0.2395 0.1816 0.0705  0.0229  0.0540  35  THR A CG2 
300  N  N   . HIS A 36  ? 0.2343 0.1825 0.1414 0.0731  0.0922  0.0687  36  HIS A N   
301  C  CA  . HIS A 36  ? 0.2567 0.1958 0.1341 0.0498  0.0711  0.0635  36  HIS A CA  
302  C  C   . HIS A 36  ? 0.3172 0.2469 0.1199 0.0275  0.0562  0.0505  36  HIS A C   
303  O  O   . HIS A 36  ? 0.3397 0.3411 0.1208 0.0776  0.0226  0.0269  36  HIS A O   
304  C  CB  . HIS A 36  ? 0.3165 0.2061 0.1616 0.0233  0.0458  0.1070  36  HIS A CB  
305  C  CG  . HIS A 36  ? 0.3461 0.1625 0.1664 0.0219  0.0035  0.0595  36  HIS A CG  
306  N  ND1 . HIS A 36  ? 0.4375 0.2341 0.2091 -0.0274 -0.0498 0.0551  36  HIS A ND1 
307  C  CD2 . HIS A 36  ? 0.3944 0.1737 0.2038 0.0540  -0.0904 0.0590  36  HIS A CD2 
308  C  CE1 . HIS A 36  ? 0.4318 0.2411 0.2323 -0.0274 -0.0275 0.0266  36  HIS A CE1 
309  N  NE2 . HIS A 36  ? 0.4079 0.2365 0.3262 0.0723  -0.0273 0.0474  36  HIS A NE2 
310  N  N   . THR A 37  ? 0.3131 0.1701 0.1905 0.0767  0.0640  0.0498  37  THR A N   
311  C  CA  . THR A 37  ? 0.3129 0.2621 0.1410 0.1145  0.0120  0.0925  37  THR A CA  
312  C  C   . THR A 37  ? 0.2766 0.1782 0.1608 0.0737  0.0390  0.0046  37  THR A C   
313  O  O   . THR A 37  ? 0.3727 0.2160 0.1869 0.0696  -0.0478 0.0320  37  THR A O   
314  C  CB  . THR A 37  ? 0.3465 0.2750 0.3707 0.0908  -0.1819 0.0483  37  THR A CB  
315  O  OG1 . THR A 37  ? 0.4246 0.3431 0.4194 0.1430  0.0610  0.1483  37  THR A OG1 
316  C  CG2 . THR A 37  ? 0.4210 0.4880 0.1705 0.0666  -0.1083 0.0229  37  THR A CG2 
317  N  N   . ALA A 38  ? 0.2240 0.1958 0.1051 0.0653  0.0333  0.0291  38  ALA A N   
318  C  CA  . ALA A 38  ? 0.2171 0.1782 0.1261 0.0639  0.0535  0.0395  38  ALA A CA  
319  C  C   . ALA A 38  ? 0.2469 0.1859 0.2172 0.0608  0.0931  0.0666  38  ALA A C   
320  O  O   . ALA A 38  ? 0.3257 0.2253 0.3860 0.0472  0.1844  0.0834  38  ALA A O   
321  C  CB  . ALA A 38  ? 0.1958 0.2049 0.1555 0.0496  0.0370  0.0350  38  ALA A CB  
322  N  N   . LYS A 39  ? 0.2653 0.2300 0.1371 0.0983  0.0010  -0.0140 39  LYS A N   
323  C  CA  . LYS A 39  ? 0.2693 0.2861 0.1333 0.1093  -0.0015 -0.0329 39  LYS A CA  
324  C  C   . LYS A 39  ? 0.2034 0.2429 0.1360 0.0733  0.0355  0.0049  39  LYS A C   
325  O  O   . LYS A 39  ? 0.1527 0.2363 0.1234 0.0577  -0.0070 0.0024  39  LYS A O   
326  C  CB  . LYS A 39  ? 0.3406 0.3118 0.2203 0.1694  -0.1084 -0.0929 39  LYS A CB  
327  C  CG  . LYS A 39  ? 0.3355 0.3560 0.2375 0.0810  -0.0177 -0.0324 39  LYS A CG  
328  C  CD  . LYS A 39  ? 0.2524 0.3815 0.2621 0.1379  0.0198  0.0467  39  LYS A CD  
329  C  CE  . LYS A 39  ? 0.2926 0.4025 0.3100 0.0750  0.0187  0.0478  39  LYS A CE  
330  N  NZ  . LYS A 39  ? 0.2264 0.4756 0.4347 0.1105  0.0348  0.1932  39  LYS A NZ  
331  N  N   . TYR A 40  ? 0.2944 0.2264 0.0961 0.0644  0.0057  0.0215  40  TYR A N   
332  C  CA  . TYR A 40  ? 0.2302 0.2196 0.1014 0.0126  0.0253  0.0177  40  TYR A CA  
333  C  C   . TYR A 40  ? 0.1729 0.2194 0.0996 0.0093  0.0496  0.0003  40  TYR A C   
334  O  O   . TYR A 40  ? 0.2178 0.2748 0.0944 0.0627  0.0140  -0.0219 40  TYR A O   
335  C  CB  . TYR A 40  ? 0.2939 0.2343 0.1880 -0.0252 0.0643  0.0537  40  TYR A CB  
336  C  CG  . TYR A 40  ? 0.2476 0.2578 0.1467 -0.0384 0.0372  0.0041  40  TYR A CG  
337  C  CD1 . TYR A 40  ? 0.2527 0.2757 0.1632 -0.0241 0.0054  -0.0326 40  TYR A CD1 
338  C  CD2 . TYR A 40  ? 0.2770 0.3517 0.2077 0.0040  0.1070  0.0227  40  TYR A CD2 
339  C  CE1 . TYR A 40  ? 0.2527 0.4140 0.1071 -0.0115 0.0052  -0.0285 40  TYR A CE1 
340  C  CE2 . TYR A 40  ? 0.3601 0.5957 0.1206 0.0854  0.0458  -0.0277 40  TYR A CE2 
341  C  CZ  . TYR A 40  ? 0.2711 0.6470 0.1625 0.0375  0.0474  0.0200  40  TYR A CZ  
342  O  OH  . TYR A 40  ? 0.2104 0.6718 0.2881 0.0593  0.0412  -0.0538 40  TYR A OH  
343  N  N   . ASP A 41  ? 0.1597 0.2117 0.1259 0.0364  0.0272  -0.0081 41  ASP A N   
344  C  CA  . ASP A 41  ? 0.1828 0.2038 0.1842 0.0131  -0.0188 -0.0199 41  ASP A CA  
345  C  C   . ASP A 41  ? 0.1987 0.2375 0.1306 0.0540  0.0266  -0.0148 41  ASP A C   
346  O  O   . ASP A 41  ? 0.1667 0.2347 0.1659 0.0329  -0.0104 -0.0015 41  ASP A O   
347  C  CB  . ASP A 41  ? 0.2275 0.2231 0.1952 -0.0148 -0.0737 -0.0020 41  ASP A CB  
348  C  CG  . ASP A 41  ? 0.2702 0.2476 0.2935 -0.0027 -0.0395 0.0129  41  ASP A CG  
349  O  OD1 . ASP A 41  ? 0.2723 0.2960 0.2511 0.0417  -0.0750 -0.0934 41  ASP A OD1 
350  O  OD2 . ASP A 41  ? 0.3271 0.2964 0.2294 -0.0916 -0.0750 0.0063  41  ASP A OD2 
351  N  N   . PRO A 42  ? 0.2074 0.3510 0.1464 0.0421  0.0274  -0.0252 42  PRO A N   
352  C  CA  . PRO A 42  ? 0.1984 0.3628 0.2795 0.0630  0.0667  -0.0010 42  PRO A CA  
353  C  C   . PRO A 42  ? 0.2603 0.3104 0.2642 0.1118  0.1022  -0.0148 42  PRO A C   
354  O  O   . PRO A 42  ? 0.3355 0.4934 0.3285 0.2125  0.0802  0.0428  42  PRO A O   
355  C  CB  . PRO A 42  ? 0.2662 0.4626 0.2906 0.0816  0.1278  0.0054  42  PRO A CB  
356  C  CG  . PRO A 42  ? 0.3605 0.6786 0.2054 0.1862  0.1342  0.0386  42  PRO A CG  
357  C  CD  . PRO A 42  ? 0.2524 0.4020 0.1370 0.0966  0.0436  -0.0026 42  PRO A CD  
358  N  N   . SER A 43  ? 0.2833 0.3217 0.2122 0.1023  0.0546  -0.0535 43  SER A N   
359  C  CA  . SER A 43  ? 0.4485 0.2987 0.1940 0.1194  0.0216  -0.0781 43  SER A CA  
360  C  C   . SER A 43  ? 0.2937 0.2942 0.1642 0.1019  -0.0087 -0.0463 43  SER A C   
361  O  O   . SER A 43  ? 0.4467 0.2802 0.3125 0.1439  -0.0666 -0.0353 43  SER A O   
362  C  CB  . SER A 43  ? 0.3461 0.2736 0.2282 0.0847  0.0186  -0.0790 43  SER A CB  
363  O  OG  . SER A 43  ? 0.3582 0.3203 0.3546 0.0206  -0.0526 -0.1159 43  SER A OG  
364  N  N   . LEU A 44  ? 0.2545 0.2675 0.1827 0.0833  0.0126  -0.0520 44  LEU A N   
365  C  CA  . LEU A 44  ? 0.2389 0.2754 0.1712 0.0666  -0.0636 -0.0161 44  LEU A CA  
366  C  C   . LEU A 44  ? 0.2093 0.2718 0.2336 0.0320  -0.0129 0.0154  44  LEU A C   
367  O  O   . LEU A 44  ? 0.1738 0.4460 0.3009 0.0153  -0.0188 0.1137  44  LEU A O   
368  C  CB  . LEU A 44  ? 0.1606 0.2714 0.1392 -0.0197 0.0333  -0.0467 44  LEU A CB  
369  C  CG  . LEU A 44  ? 0.1595 0.2289 0.1711 -0.0108 -0.0060 0.0006  44  LEU A CG  
370  C  CD1 . LEU A 44  ? 0.1893 0.2320 0.1437 -0.0051 0.0057  -0.0031 44  LEU A CD1 
371  C  CD2 . LEU A 44  ? 0.1766 0.2045 0.2018 -0.0136 -0.0178 -0.0082 44  LEU A CD2 
372  N  N   . LYS A 45  ? 0.2128 0.2492 0.2354 0.0258  -0.0535 0.0324  45  LYS A N   
373  C  CA  . LYS A 45  ? 0.2176 0.2363 0.2125 0.0272  -0.0505 -0.0320 45  LYS A CA  
374  C  C   . LYS A 45  ? 0.1717 0.2314 0.1728 0.0439  0.0057  -0.0087 45  LYS A C   
375  O  O   . LYS A 45  ? 0.1533 0.2013 0.2300 0.0153  0.0104  -0.0013 45  LYS A O   
376  C  CB  . LYS A 45  ? 0.2180 0.2176 0.2536 0.0824  -0.0164 -0.0308 45  LYS A CB  
377  C  CG  . LYS A 45  ? 0.3267 0.3454 0.2336 0.0087  -0.0359 -0.0644 45  LYS A CG  
378  C  CD  . LYS A 45  ? 0.3118 0.3840 0.4435 -0.0216 0.0790  -0.0697 45  LYS A CD  
379  C  CE  . LYS A 45  ? 0.9250 0.3643 0.6255 0.0362  0.0436  -0.1436 45  LYS A CE  
380  N  NZ  . LYS A 45  ? 0.7889 0.5554 1.1467 -0.0423 0.2596  0.1613  45  LYS A NZ  
381  N  N   . PRO A 46  ? 0.1344 0.2415 0.1814 -0.0003 0.0244  0.0197  46  PRO A N   
382  C  CA  . PRO A 46  ? 0.1324 0.2203 0.1991 0.0010  0.0107  0.0049  46  PRO A CA  
383  C  C   . PRO A 46  ? 0.1263 0.1666 0.1644 -0.0027 0.0227  -0.0031 46  PRO A C   
384  O  O   . PRO A 46  ? 0.1186 0.2169 0.2004 0.0000  -0.0203 -0.0093 46  PRO A O   
385  C  CB  . PRO A 46  ? 0.1468 0.2357 0.2213 -0.0309 0.0165  -0.0074 46  PRO A CB  
386  C  CG  . PRO A 46  ? 0.1626 0.3666 0.2397 0.0208  0.0199  -0.0900 46  PRO A CG  
387  C  CD  . PRO A 46  ? 0.1773 0.3023 0.2011 0.0375  0.0109  -0.0109 46  PRO A CD  
388  N  N   . LEU A 47  ? 0.1130 0.2147 0.1885 0.0109  0.0103  -0.0511 47  LEU A N   
389  C  CA  . LEU A 47  ? 0.1084 0.2022 0.1793 -0.0057 0.0208  -0.0156 47  LEU A CA  
390  C  C   . LEU A 47  ? 0.0812 0.2370 0.2179 -0.0110 -0.0140 -0.0019 47  LEU A C   
391  O  O   . LEU A 47  ? 0.1166 0.2398 0.2912 -0.0454 -0.0355 0.0482  47  LEU A O   
392  C  CB  . LEU A 47  ? 0.1614 0.2623 0.1880 0.0621  0.0348  -0.0284 47  LEU A CB  
393  C  CG  . LEU A 47  ? 0.1387 0.3138 0.2217 0.0006  0.0092  -0.0640 47  LEU A CG  
394  C  CD1 . LEU A 47  ? 0.1202 0.3486 0.3467 -0.0595 0.0309  -0.0926 47  LEU A CD1 
395  C  CD2 . LEU A 47  ? 0.1405 0.3542 0.3045 0.0399  0.0057  -0.1376 47  LEU A CD2 
396  N  N   . SER A 48  ? 0.1061 0.1903 0.1905 -0.0030 -0.0060 -0.0043 48  SER A N   
397  C  CA  . SER A 48  ? 0.1316 0.1673 0.1614 -0.0035 0.0000  -0.0043 48  SER A CA  
398  C  C   . SER A 48  ? 0.1351 0.1955 0.1571 -0.0206 -0.0093 -0.0006 48  SER A C   
399  O  O   . SER A 48  ? 0.1421 0.2064 0.1721 -0.0414 0.0043  -0.0410 48  SER A O   
400  C  CB  . SER A 48  ? 0.1850 0.2010 0.2104 0.0068  -0.0162 -0.0148 48  SER A CB  
401  O  OG  . SER A 48  ? 0.1999 0.2944 0.2458 0.0463  0.0236  0.0288  48  SER A OG  
402  N  N   . VAL A 49  ? 0.1648 0.2298 0.1421 -0.0649 0.0041  -0.0228 49  VAL A N   
403  C  CA  . VAL A 49  ? 0.2162 0.2285 0.1588 -0.0527 0.0362  -0.0379 49  VAL A CA  
404  C  C   . VAL A 49  ? 0.2183 0.2538 0.1932 -0.1071 -0.0328 -0.0034 49  VAL A C   
405  O  O   . VAL A 49  ? 0.2219 0.3522 0.2111 -0.1550 -0.0383 0.0368  49  VAL A O   
406  C  CB  . VAL A 49  ? 0.2700 0.2334 0.2106 -0.0793 0.0573  -0.0538 49  VAL A CB  
407  C  CG1 . VAL A 49  ? 0.4571 0.2646 0.1890 -0.0851 0.0900  -0.0626 49  VAL A CG1 
408  C  CG2 . VAL A 49  ? 0.2489 0.2063 0.3052 -0.0780 0.0711  -0.0428 49  VAL A CG2 
409  N  N   . SER A 50  ? 0.1607 0.2079 0.1528 -0.0606 0.0329  -0.0465 50  SER A N   
410  C  CA  . SER A 50  ? 0.1102 0.2549 0.2248 -0.0430 -0.0154 -0.0513 50  SER A CA  
411  C  C   . SER A 50  ? 0.1198 0.2030 0.1807 -0.0092 -0.0262 -0.0198 50  SER A C   
412  O  O   . SER A 50  ? 0.1533 0.1994 0.1914 -0.0131 -0.0186 -0.0185 50  SER A O   
413  C  CB  . SER A 50  ? 0.2727 0.2813 0.2687 -0.0137 0.0625  -0.0551 50  SER A CB  
414  O  OG  . SER A 50  ? 0.2253 0.4687 0.3731 -0.0399 0.0098  -0.1303 50  SER A OG  
415  N  N   . TYR A 51  ? 0.1186 0.2363 0.1855 -0.0274 0.0043  -0.0399 51  TYR A N   
416  C  CA  . TYR A 51  ? 0.1412 0.1800 0.1722 -0.0082 -0.0194 -0.0269 51  TYR A CA  
417  C  C   . TYR A 51  ? 0.1385 0.1884 0.1905 -0.0143 0.0062  0.0222  51  TYR A C   
418  O  O   . TYR A 51  ? 0.1429 0.1877 0.1835 -0.0073 -0.0110 0.0080  51  TYR A O   
419  C  CB  . TYR A 51  ? 0.1252 0.1934 0.1827 -0.0295 -0.0207 -0.0230 51  TYR A CB  
420  C  CG  . TYR A 51  ? 0.1155 0.1616 0.1172 -0.0292 0.0024  0.0109  51  TYR A CG  
421  C  CD1 . TYR A 51  ? 0.1111 0.1536 0.1797 -0.0287 0.0068  -0.0274 51  TYR A CD1 
422  C  CD2 . TYR A 51  ? 0.1052 0.1614 0.1466 -0.0292 0.0107  -0.0103 51  TYR A CD2 
423  C  CE1 . TYR A 51  ? 0.1453 0.1412 0.1493 -0.0337 -0.0148 -0.0159 51  TYR A CE1 
424  C  CE2 . TYR A 51  ? 0.1146 0.1498 0.1456 -0.0454 -0.0102 -0.0026 51  TYR A CE2 
425  C  CZ  . TYR A 51  ? 0.1140 0.1367 0.1448 -0.0346 -0.0156 0.0135  51  TYR A CZ  
426  O  OH  . TYR A 51  ? 0.1265 0.1353 0.1571 -0.0171 -0.0161 -0.0198 51  TYR A OH  
427  N  N   A ASP A 52  ? 0.1421 0.2128 0.2565 0.0167  -0.0076 -0.0153 52  ASP A N   
428  N  N   B ASP A 52  ? 0.0974 0.2599 0.1897 -0.0313 -0.0216 0.0109  52  ASP A N   
429  C  CA  A ASP A 52  ? 0.1480 0.2095 0.2930 0.0277  -0.0109 0.0137  52  ASP A CA  
430  C  CA  B ASP A 52  ? 0.0916 0.2438 0.1826 -0.0230 -0.0124 0.0542  52  ASP A CA  
431  C  C   A ASP A 52  ? 0.2068 0.1840 0.2763 -0.0023 -0.0983 -0.0010 52  ASP A C   
432  C  C   B ASP A 52  ? 0.1048 0.2201 0.1664 0.0259  0.0109  0.0305  52  ASP A C   
433  O  O   A ASP A 52  ? 0.2205 0.3819 0.2381 -0.0406 -0.0482 -0.0162 52  ASP A O   
434  O  O   B ASP A 52  ? 0.1506 0.1843 0.1774 -0.0114 -0.0096 0.0763  52  ASP A O   
435  C  CB  A ASP A 52  ? 0.1648 0.1897 0.2773 -0.0232 0.0487  0.0494  52  ASP A CB  
436  C  CB  B ASP A 52  ? 0.0955 0.2520 0.2030 0.0164  -0.0170 0.0432  52  ASP A CB  
437  C  CG  A ASP A 52  ? 0.2381 0.4092 0.2470 0.0666  0.0000  0.0240  52  ASP A CG  
438  C  CG  B ASP A 52  ? 0.2626 0.2154 0.3278 -0.0601 0.0082  0.0535  52  ASP A CG  
439  O  OD1 A ASP A 52  ? 0.1591 0.5238 0.2246 0.0864  0.0087  -0.0548 52  ASP A OD1 
440  O  OD1 B ASP A 52  ? 0.2892 0.3876 0.3898 0.0584  0.1004  0.1617  52  ASP A OD1 
441  O  OD2 A ASP A 52  ? 0.4809 0.3544 0.5515 -0.0447 0.1133  -0.1224 52  ASP A OD2 
442  O  OD2 B ASP A 52  ? 0.3366 0.5109 0.2135 0.0540  0.0344  0.0048  52  ASP A OD2 
443  N  N   . GLN A 53  ? 0.1071 0.2036 0.2583 0.0186  0.0046  0.0203  53  GLN A N   
444  C  CA  . GLN A 53  ? 0.1526 0.1884 0.2222 -0.0155 0.0046  0.0109  53  GLN A CA  
445  C  C   . GLN A 53  ? 0.1600 0.1538 0.1368 0.0142  0.0041  0.0065  53  GLN A C   
446  O  O   . GLN A 53  ? 0.1608 0.1668 0.1781 0.0155  0.0080  0.0154  53  GLN A O   
447  C  CB  . GLN A 53  ? 0.1761 0.2079 0.1782 0.0373  -0.0186 -0.0060 53  GLN A CB  
448  C  CG  . GLN A 53  ? 0.2228 0.3100 0.1832 0.0799  0.0283  0.0126  53  GLN A CG  
449  C  CD  . GLN A 53  ? 0.2061 0.2770 0.2680 0.0606  -0.0037 0.0535  53  GLN A CD  
450  O  OE1 . GLN A 53  ? 0.2849 0.3970 0.5205 -0.0274 0.0392  0.1350  53  GLN A OE1 
451  N  NE2 . GLN A 53  ? 0.1860 0.2147 0.2230 0.0299  -0.0274 0.0309  53  GLN A NE2 
452  N  N   . ALA A 54  ? 0.1606 0.1509 0.1333 0.0076  0.0043  0.0038  54  ALA A N   
453  C  CA  . ALA A 54  ? 0.1380 0.1342 0.1642 0.0204  -0.0026 0.0052  54  ALA A CA  
454  C  C   . ALA A 54  ? 0.1324 0.1431 0.1380 -0.0057 -0.0114 -0.0187 54  ALA A C   
455  O  O   . ALA A 54  ? 0.1409 0.1744 0.1518 -0.0221 -0.0017 -0.0160 54  ALA A O   
456  C  CB  . ALA A 54  ? 0.1479 0.1541 0.1667 0.0041  0.0020  0.0208  54  ALA A CB  
457  N  N   . THR A 55  ? 0.1321 0.1019 0.1296 0.0087  -0.0019 -0.0038 55  THR A N   
458  C  CA  . THR A 55  ? 0.1173 0.1136 0.1115 0.0142  -0.0120 0.0035  55  THR A CA  
459  C  C   . THR A 55  ? 0.1133 0.0952 0.0956 0.0060  -0.0230 0.0262  55  THR A C   
460  O  O   . THR A 55  ? 0.1280 0.1005 0.1128 0.0115  -0.0220 0.0086  55  THR A O   
461  C  CB  . THR A 55  ? 0.1229 0.1142 0.1614 0.0307  0.0043  0.0183  55  THR A CB  
462  O  OG1 . THR A 55  ? 0.1447 0.1341 0.1851 0.0263  -0.0024 0.0027  55  THR A OG1 
463  C  CG2 . THR A 55  ? 0.1562 0.1305 0.1691 0.0124  -0.0142 0.0588  55  THR A CG2 
464  N  N   . SER A 56  ? 0.1079 0.0975 0.1004 -0.0031 -0.0027 0.0154  56  SER A N   
465  C  CA  . SER A 56  ? 0.1013 0.0895 0.1173 0.0142  0.0006  0.0164  56  SER A CA  
466  C  C   . SER A 56  ? 0.1274 0.0883 0.0921 0.0049  -0.0115 0.0131  56  SER A C   
467  O  O   . SER A 56  ? 0.1351 0.1252 0.0961 0.0086  -0.0281 0.0274  56  SER A O   
468  C  CB  . SER A 56  ? 0.1225 0.0839 0.1089 0.0046  -0.0192 0.0154  56  SER A CB  
469  O  OG  . SER A 56  ? 0.1243 0.1058 0.1216 0.0000  -0.0318 0.0132  56  SER A OG  
470  N  N   . LEU A 57  ? 0.1122 0.0856 0.1033 0.0023  -0.0024 0.0092  57  LEU A N   
471  C  CA  . LEU A 57  ? 0.1518 0.0918 0.1155 0.0086  0.0046  0.0216  57  LEU A CA  
472  C  C   . LEU A 57  ? 0.1422 0.0934 0.1040 0.0010  0.0020  0.0192  57  LEU A C   
473  O  O   . LEU A 57  ? 0.1798 0.0986 0.0988 0.0006  -0.0051 0.0236  57  LEU A O   
474  C  CB  . LEU A 57  ? 0.1543 0.0921 0.1120 0.0043  0.0076  0.0086  57  LEU A CB  
475  C  CG  . LEU A 57  ? 0.1675 0.0992 0.1587 0.0065  0.0043  0.0020  57  LEU A CG  
476  C  CD1 . LEU A 57  ? 0.1973 0.1195 0.2000 -0.0080 0.0339  -0.0351 57  LEU A CD1 
477  C  CD2 . LEU A 57  ? 0.2478 0.0978 0.2372 0.0388  -0.0315 0.0284  57  LEU A CD2 
478  N  N   . ARG A 58  ? 0.1220 0.0899 0.1181 -0.0003 0.0082  0.0148  58  ARG A N   
479  C  CA  . ARG A 58  ? 0.1468 0.0939 0.0961 -0.0012 0.0121  0.0160  58  ARG A CA  
480  C  C   . ARG A 58  ? 0.1218 0.0944 0.0781 0.0057  -0.0057 0.0074  58  ARG A C   
481  O  O   . ARG A 58  ? 0.1589 0.1084 0.0840 0.0220  0.0038  0.0074  58  ARG A O   
482  C  CB  . ARG A 58  ? 0.1507 0.0925 0.1536 -0.0175 0.0377  0.0261  58  ARG A CB  
483  C  CG  . ARG A 58  ? 0.1791 0.1119 0.1738 -0.0232 0.0355  0.0263  58  ARG A CG  
484  C  CD  . ARG A 58  ? 0.2111 0.1167 0.2309 -0.0265 0.0608  0.0098  58  ARG A CD  
485  N  NE  . ARG A 58  ? 0.2440 0.1431 0.2081 -0.0309 0.0706  0.0120  58  ARG A NE  
486  C  CZ  . ARG A 58  ? 0.2370 0.1428 0.1659 -0.0003 0.0229  0.0450  58  ARG A CZ  
487  N  NH1 . ARG A 58  ? 0.2714 0.1896 0.2436 0.0283  0.0344  0.0744  58  ARG A NH1 
488  N  NH2 . ARG A 58  ? 0.2447 0.1639 0.1676 -0.0165 0.0351  0.0219  58  ARG A NH2 
489  N  N   . ILE A 59  ? 0.1281 0.0846 0.1013 0.0077  -0.0007 0.0068  59  ILE A N   
490  C  CA  . ILE A 59  ? 0.1162 0.0890 0.0935 0.0115  0.0065  0.0217  59  ILE A CA  
491  C  C   . ILE A 59  ? 0.1235 0.1016 0.0925 0.0043  -0.0013 0.0013  59  ILE A C   
492  O  O   . ILE A 59  ? 0.1292 0.1272 0.0838 0.0023  0.0097  0.0092  59  ILE A O   
493  C  CB  . ILE A 59  ? 0.1466 0.0902 0.0894 0.0000  -0.0113 0.0183  59  ILE A CB  
494  C  CG1 . ILE A 59  ? 0.1462 0.1039 0.1049 0.0027  -0.0026 0.0181  59  ILE A CG1 
495  C  CG2 . ILE A 59  ? 0.1430 0.1137 0.0965 0.0104  -0.0031 -0.0035 59  ILE A CG2 
496  C  CD1 . ILE A 59  ? 0.1952 0.1014 0.1119 0.0088  0.0074  0.0108  59  ILE A CD1 
497  N  N   A LEU A 60  ? 0.1141 0.1077 0.1026 0.0097  -0.0005 0.0097  60  LEU A N   
498  N  N   B LEU A 60  ? 0.1349 0.1272 0.1139 0.0307  -0.0020 0.0260  60  LEU A N   
499  C  CA  A LEU A 60  ? 0.0986 0.0970 0.0824 0.0051  -0.0017 0.0020  60  LEU A CA  
500  C  CA  B LEU A 60  ? 0.1208 0.1325 0.1817 0.0227  -0.0107 0.0165  60  LEU A CA  
501  C  C   A LEU A 60  ? 0.1084 0.0948 0.0948 0.0030  -0.0057 0.0136  60  LEU A C   
502  C  C   B LEU A 60  ? 0.1203 0.0987 0.1014 0.0000  0.0040  0.0131  60  LEU A C   
503  O  O   A LEU A 60  ? 0.1386 0.1491 0.1013 0.0410  0.0043  0.0428  60  LEU A O   
504  O  O   B LEU A 60  ? 0.1465 0.1001 0.1008 0.0142  0.0159  0.0148  60  LEU A O   
505  C  CB  A LEU A 60  ? 0.1039 0.0814 0.0822 0.0031  0.0017  0.0087  60  LEU A CB  
506  C  CB  B LEU A 60  ? 0.1570 0.1474 0.1428 -0.0046 0.0140  0.0186  60  LEU A CB  
507  C  CG  A LEU A 60  ? 0.1025 0.0944 0.1024 -0.0087 -0.0059 -0.0271 60  LEU A CG  
508  C  CG  B LEU A 60  ? 0.1872 0.1536 0.1458 -0.0185 0.0549  -0.0155 60  LEU A CG  
509  C  CD1 A LEU A 60  ? 0.1713 0.1190 0.0963 -0.0326 -0.0107 0.0031  60  LEU A CD1 
510  C  CD1 B LEU A 60  ? 0.2426 0.2447 0.2554 -0.0052 0.0049  0.0148  60  LEU A CD1 
511  C  CD2 A LEU A 60  ? 0.1739 0.0715 0.1655 -0.0131 -0.0373 -0.0230 60  LEU A CD2 
512  C  CD2 B LEU A 60  ? 0.4941 0.1694 0.3578 0.0040  0.0164  -0.0900 60  LEU A CD2 
513  N  N   . ASN A 61  ? 0.1086 0.0988 0.0952 -0.0070 0.0030  0.0020  61  ASN A N   
514  C  CA  . ASN A 61  ? 0.0989 0.0921 0.1009 -0.0092 -0.0052 0.0086  61  ASN A CA  
515  C  C   . ASN A 61  ? 0.1101 0.1015 0.0928 -0.0031 0.0109  0.0107  61  ASN A C   
516  O  O   . ASN A 61  ? 0.1255 0.1190 0.1083 -0.0143 0.0115  0.0160  61  ASN A O   
517  C  CB  . ASN A 61  ? 0.1066 0.1024 0.1218 -0.0031 0.0148  -0.0118 61  ASN A CB  
518  C  CG  . ASN A 61  ? 0.1097 0.1017 0.1076 -0.0015 0.0082  0.0076  61  ASN A CG  
519  O  OD1 . ASN A 61  ? 0.1235 0.1049 0.1343 0.0038  -0.0088 -0.0057 61  ASN A OD1 
520  N  ND2 . ASN A 61  ? 0.1244 0.1053 0.1131 -0.0006 0.0103  -0.0143 61  ASN A ND2 
521  N  N   . ASN A 62  ? 0.1094 0.1093 0.1014 -0.0131 0.0082  0.0035  62  ASN A N   
522  C  CA  . ASN A 62  ? 0.1137 0.1270 0.1087 -0.0353 0.0109  -0.0091 62  ASN A CA  
523  C  C   . ASN A 62  ? 0.1208 0.1307 0.1263 -0.0159 0.0250  -0.0020 62  ASN A C   
524  O  O   . ASN A 62  ? 0.1121 0.1591 0.1775 -0.0255 0.0136  -0.0162 62  ASN A O   
525  C  CB  . ASN A 62  ? 0.1342 0.1347 0.1120 -0.0194 -0.0048 -0.0063 62  ASN A CB  
526  C  CG  . ASN A 62  ? 0.1946 0.1516 0.0974 0.0241  0.0049  -0.0222 62  ASN A CG  
527  O  OD1 . ASN A 62  ? 0.1441 0.1380 0.1057 0.0010  0.0041  0.0060  62  ASN A OD1 
528  N  ND2 . ASN A 62  ? 0.2309 0.1958 0.1685 -0.0015 -0.0162 -0.0303 62  ASN A ND2 
529  N  N   . GLY A 63  ? 0.1226 0.1307 0.1087 -0.0070 0.0081  -0.0087 63  GLY A N   
530  C  CA  . GLY A 63  ? 0.1110 0.1438 0.1455 0.0040  0.0098  0.0097  63  GLY A CA  
531  C  C   . GLY A 63  ? 0.1137 0.1289 0.1217 0.0000  0.0049  0.0120  63  GLY A C   
532  O  O   . GLY A 63  ? 0.1571 0.1538 0.1749 0.0263  0.0140  0.0049  63  GLY A O   
533  N  N   . HIS A 64  ? 0.1035 0.1481 0.1189 -0.0164 -0.0059 0.0031  64  HIS A N   
534  C  CA  . HIS A 64  ? 0.1255 0.1412 0.1186 -0.0103 -0.0178 0.0109  64  HIS A CA  
535  C  C   . HIS A 64  ? 0.1083 0.1289 0.1180 -0.0026 -0.0098 0.0244  64  HIS A C   
536  O  O   . HIS A 64  ? 0.1098 0.1527 0.1456 0.0065  -0.0087 0.0337  64  HIS A O   
537  C  CB  . HIS A 64  ? 0.1225 0.1673 0.1111 -0.0274 -0.0175 0.0137  64  HIS A CB  
538  C  CG  . HIS A 64  ? 0.1479 0.1545 0.1325 -0.0003 -0.0219 -0.0041 64  HIS A CG  
539  N  ND1 . HIS A 64  ? 0.1392 0.2140 0.1973 -0.0166 -0.0423 0.0093  64  HIS A ND1 
540  C  CD2 . HIS A 64  ? 0.1542 0.1720 0.1723 -0.0421 0.0082  0.0046  64  HIS A CD2 
541  C  CE1 . HIS A 64  ? 0.1427 0.2122 0.2063 -0.0372 -0.0086 -0.0142 64  HIS A CE1 
542  N  NE2 . HIS A 64  ? 0.1535 0.2300 0.2004 -0.0631 0.0076  0.0104  64  HIS A NE2 
543  N  N   . SER A 65  ? 0.1127 0.1215 0.1014 -0.0093 -0.0046 0.0120  65  SER A N   
544  C  CA  . SER A 65  ? 0.1166 0.1067 0.1067 -0.0218 -0.0126 0.0214  65  SER A CA  
545  C  C   . SER A 65  ? 0.1181 0.0979 0.0842 -0.0082 0.0082  0.0086  65  SER A C   
546  O  O   . SER A 65  ? 0.1033 0.1414 0.1084 0.0131  0.0057  0.0175  65  SER A O   
547  C  CB  . SER A 65  ? 0.1076 0.1755 0.1400 -0.0324 -0.0076 0.0610  65  SER A CB  
548  O  OG  . SER A 65  ? 0.1362 0.2183 0.1597 -0.0405 -0.0206 0.0658  65  SER A OG  
549  N  N   . PHE A 66  ? 0.1093 0.1049 0.0916 0.0071  -0.0109 0.0049  66  PHE A N   
550  C  CA  . PHE A 66  ? 0.1133 0.1158 0.0917 0.0137  -0.0088 -0.0020 66  PHE A CA  
551  C  C   . PHE A 66  ? 0.1243 0.1016 0.0904 0.0160  0.0000  -0.0013 66  PHE A C   
552  O  O   . PHE A 66  ? 0.1485 0.1186 0.0898 0.0129  -0.0005 -0.0034 66  PHE A O   
553  C  CB  . PHE A 66  ? 0.1224 0.1553 0.0868 0.0131  0.0000  -0.0120 66  PHE A CB  
554  C  CG  . PHE A 66  ? 0.1190 0.1200 0.0847 0.0152  -0.0225 -0.0192 66  PHE A CG  
555  C  CD1 . PHE A 66  ? 0.1084 0.1326 0.1019 -0.0010 -0.0368 -0.0125 66  PHE A CD1 
556  C  CD2 . PHE A 66  ? 0.1324 0.1254 0.1411 0.0120  -0.0423 -0.0292 66  PHE A CD2 
557  C  CE1 . PHE A 66  ? 0.1279 0.1289 0.1183 0.0086  -0.0302 0.0034  66  PHE A CE1 
558  C  CE2 . PHE A 66  ? 0.1542 0.1251 0.1287 0.0046  -0.0350 -0.0388 66  PHE A CE2 
559  C  CZ  . PHE A 66  ? 0.1456 0.1264 0.1283 0.0137  -0.0421 -0.0269 66  PHE A CZ  
560  N  N   A LYS A 67  ? 0.0894 0.1023 0.0973 0.0146  -0.0102 -0.0003 67  LYS A N   
561  N  N   B LYS A 67  ? 0.1199 0.1158 0.0856 0.0285  -0.0199 0.0000  67  LYS A N   
562  C  CA  A LYS A 67  ? 0.1206 0.1316 0.0874 0.0335  -0.0230 -0.0023 67  LYS A CA  
563  C  CA  B LYS A 67  ? 0.1327 0.1378 0.1027 0.0370  -0.0298 -0.0109 67  LYS A CA  
564  C  C   A LYS A 67  ? 0.1084 0.0882 0.0979 0.0375  0.0182  0.0155  67  LYS A C   
565  C  C   B LYS A 67  ? 0.1140 0.1075 0.0794 0.0178  -0.0024 -0.0023 67  LYS A C   
566  O  O   A LYS A 67  ? 0.1190 0.1032 0.0882 -0.0031 -0.0013 0.0141  67  LYS A O   
567  O  O   B LYS A 67  ? 0.1048 0.1050 0.0776 0.0000  -0.0017 0.0030  67  LYS A O   
568  C  CB  A LYS A 67  ? 0.1492 0.1455 0.0710 0.0405  -0.0329 -0.0142 67  LYS A CB  
569  C  CB  B LYS A 67  ? 0.1631 0.1743 0.1202 0.0342  -0.0205 -0.0309 67  LYS A CB  
570  C  CG  A LYS A 67  ? 0.1483 0.1095 0.1289 0.0065  -0.0219 -0.0046 67  LYS A CG  
571  C  CG  B LYS A 67  ? 0.1559 0.1404 0.1483 0.0131  0.0135  -0.0164 67  LYS A CG  
572  C  CD  A LYS A 67  ? 0.2082 0.1518 0.0829 -0.0006 -0.0054 -0.0131 67  LYS A CD  
573  C  CD  B LYS A 67  ? 0.2311 0.1924 0.1053 -0.0410 0.0259  -0.0339 67  LYS A CD  
574  C  CE  A LYS A 67  ? 0.1958 0.1817 0.1520 -0.0346 -0.0208 -0.0109 67  LYS A CE  
575  C  CE  B LYS A 67  ? 0.2066 0.2694 0.2657 -0.0296 0.0531  0.1234  67  LYS A CE  
576  N  NZ  A LYS A 67  ? 0.2350 0.2061 0.1421 -0.1089 0.0076  -0.0012 67  LYS A NZ  
577  N  NZ  B LYS A 67  ? 0.3792 0.1770 0.3413 0.0688  0.1280  0.0939  67  LYS A NZ  
578  N  N   . VAL A 68  ? 0.1094 0.0900 0.0790 0.0131  0.0000  0.0159  68  VAL A N   
579  C  CA  . VAL A 68  ? 0.1067 0.0762 0.0971 0.0049  0.0065  0.0104  68  VAL A CA  
580  C  C   . VAL A 68  ? 0.1025 0.0814 0.0789 0.0099  -0.0027 0.0186  68  VAL A C   
581  O  O   . VAL A 68  ? 0.1216 0.0917 0.0863 0.0068  -0.0030 0.0172  68  VAL A O   
582  C  CB  . VAL A 68  ? 0.1234 0.0998 0.0969 -0.0017 -0.0115 0.0120  68  VAL A CB  
583  C  CG1 . VAL A 68  ? 0.1289 0.1265 0.1264 0.0054  -0.0274 0.0030  68  VAL A CG1 
584  C  CG2 . VAL A 68  ? 0.1297 0.1033 0.1128 -0.0148 -0.0024 -0.0020 68  VAL A CG2 
585  N  N   . GLU A 69  ? 0.1076 0.0840 0.0929 0.0040  -0.0065 0.0193  69  GLU A N   
586  C  CA  . GLU A 69  ? 0.1104 0.0855 0.1102 0.0026  -0.0031 0.0114  69  GLU A CA  
587  C  C   . GLU A 69  ? 0.1218 0.0840 0.0936 -0.0003 -0.0027 0.0196  69  GLU A C   
588  O  O   . GLU A 69  ? 0.1397 0.1097 0.1076 0.0247  -0.0177 -0.0003 69  GLU A O   
589  C  CB  . GLU A 69  ? 0.1195 0.1219 0.1468 -0.0076 0.0305  0.0170  69  GLU A CB  
590  C  CG  . GLU A 69  ? 0.1292 0.1554 0.1644 -0.0236 0.0244  0.0197  69  GLU A CG  
591  C  CD  . GLU A 69  ? 0.1650 0.1659 0.1673 -0.0355 0.0204  -0.0082 69  GLU A CD  
592  O  OE1 . GLU A 69  ? 0.1800 0.1958 0.1652 -0.0342 0.0414  0.0163  69  GLU A OE1 
593  O  OE2 . GLU A 69  ? 0.2120 0.2109 0.1938 -0.0612 0.0247  -0.0086 69  GLU A OE2 
594  N  N   . PHE A 70  ? 0.1034 0.0812 0.1076 0.0093  0.0017  0.0104  70  PHE A N   
595  C  CA  . PHE A 70  ? 0.1086 0.0856 0.1049 0.0049  -0.0057 0.0057  70  PHE A CA  
596  C  C   . PHE A 70  ? 0.1260 0.0983 0.1014 -0.0007 -0.0088 0.0132  70  PHE A C   
597  O  O   . PHE A 70  ? 0.1272 0.0909 0.1544 0.0107  -0.0076 0.0020  70  PHE A O   
598  C  CB  . PHE A 70  ? 0.1110 0.0983 0.0979 0.0087  -0.0031 -0.0031 70  PHE A CB  
599  C  CG  . PHE A 70  ? 0.1106 0.0922 0.1023 0.0052  -0.0087 0.0109  70  PHE A CG  
600  C  CD1 . PHE A 70  ? 0.1473 0.0930 0.0987 0.0196  0.0049  0.0260  70  PHE A CD1 
601  C  CD2 . PHE A 70  ? 0.1119 0.0956 0.1050 0.0017  -0.0006 0.0131  70  PHE A CD2 
602  C  CE1 . PHE A 70  ? 0.1431 0.1010 0.1307 0.0285  0.0335  0.0230  70  PHE A CE1 
603  C  CE2 . PHE A 70  ? 0.1352 0.1067 0.1150 -0.0024 -0.0031 0.0282  70  PHE A CE2 
604  C  CZ  . PHE A 70  ? 0.1441 0.0823 0.1184 0.0048  0.0288  0.0155  70  PHE A CZ  
605  N  N   A ASP A 71  ? 0.1356 0.0855 0.0767 0.0043  -0.0074 0.0099  71  ASP A N   
606  N  N   B ASP A 71  ? 0.1357 0.0864 0.1278 0.0147  -0.0230 0.0000  71  ASP A N   
607  C  CA  A ASP A 71  ? 0.0891 0.0821 0.1087 0.0142  -0.0057 0.0082  71  ASP A CA  
608  C  CA  B ASP A 71  ? 0.1817 0.0849 0.1429 0.0277  -0.0220 0.0229  71  ASP A CA  
609  C  C   A ASP A 71  ? 0.1299 0.0759 0.1085 -0.0065 0.0102  0.0065  71  ASP A C   
610  C  C   B ASP A 71  ? 0.1673 0.0538 0.1597 0.0031  -0.0108 0.0229  71  ASP A C   
611  O  O   A ASP A 71  ? 0.1190 0.0893 0.1097 -0.0199 0.0034  0.0109  71  ASP A O   
612  O  O   B ASP A 71  ? 0.1677 0.1437 0.1380 0.0164  0.0054  0.0082  71  ASP A O   
613  C  CB  A ASP A 71  ? 0.0893 0.0670 0.1429 0.0065  -0.0120 0.0151  71  ASP A CB  
614  C  CB  B ASP A 71  ? 0.1545 0.1202 0.1650 0.0017  -0.0175 0.0113  71  ASP A CB  
615  C  CG  A ASP A 71  ? 0.1435 0.0631 0.1358 0.0098  -0.0658 0.0326  71  ASP A CG  
616  C  CG  B ASP A 71  ? 0.3596 0.1436 0.2759 0.0425  0.0461  0.0819  71  ASP A CG  
617  O  OD1 A ASP A 71  ? 0.1606 0.0355 0.1234 0.0175  -0.0657 0.0082  71  ASP A OD1 
618  O  OD1 B ASP A 71  ? 0.2633 0.3993 0.2174 -0.0417 0.0485  -0.0306 71  ASP A OD1 
619  O  OD2 A ASP A 71  ? 0.1745 0.0696 0.2213 0.0302  -0.0697 -0.0120 71  ASP A OD2 
620  O  OD2 B ASP A 71  ? 0.2093 0.1640 0.1858 0.0110  0.0469  0.0031  71  ASP A OD2 
621  N  N   . ASP A 72  ? 0.1492 0.0715 0.1317 -0.0054 -0.0108 0.0164  72  ASP A N   
622  C  CA  . ASP A 72  ? 0.1479 0.0701 0.1254 -0.0076 -0.0054 0.0017  72  ASP A CA  
623  C  C   . ASP A 72  ? 0.1634 0.0749 0.1351 -0.0161 -0.0027 0.0156  72  ASP A C   
624  O  O   . ASP A 72  ? 0.2259 0.0922 0.1571 -0.0080 -0.0239 0.0073  72  ASP A O   
625  C  CB  . ASP A 72  ? 0.1731 0.0683 0.1455 0.0054  -0.0087 0.0115  72  ASP A CB  
626  C  CG  . ASP A 72  ? 0.1746 0.1057 0.1419 -0.0154 -0.0307 0.0205  72  ASP A CG  
627  O  OD1 . ASP A 72  ? 0.1820 0.1499 0.1471 -0.0335 -0.0240 0.0390  72  ASP A OD1 
628  O  OD2 . ASP A 72  ? 0.2117 0.1351 0.1383 -0.0063 -0.0526 0.0175  72  ASP A OD2 
629  N  N   . SER A 73  ? 0.2183 0.0767 0.1649 -0.0026 -0.0164 0.0307  73  SER A N   
630  C  CA  . SER A 73  ? 0.2578 0.0831 0.2018 -0.0252 -0.0456 0.0307  73  SER A CA  
631  C  C   . SER A 73  ? 0.2795 0.1093 0.2201 -0.0093 -0.0878 -0.0031 73  SER A C   
632  O  O   . SER A 73  ? 0.3882 0.0832 0.2119 0.0092  -0.0724 -0.0057 73  SER A O   
633  C  CB  . SER A 73  ? 0.2494 0.1101 0.2095 -0.0527 -0.0653 0.0436  73  SER A CB  
634  O  OG  . SER A 73  ? 0.2518 0.0908 0.1924 0.0155  -0.0337 0.0241  73  SER A OG  
635  N  N   . GLN A 74  ? 0.2565 0.1502 0.1659 0.0248  -0.0222 -0.0250 74  GLN A N   
636  C  CA  . GLN A 74  ? 0.2585 0.1969 0.2359 0.0623  0.0041  -0.0054 74  GLN A CA  
637  C  C   . GLN A 74  ? 0.2036 0.2206 0.2171 -0.0027 -0.0474 -0.0732 74  GLN A C   
638  O  O   . GLN A 74  ? 0.1986 0.1632 0.2467 -0.0109 -0.0417 -0.0515 74  GLN A O   
639  C  CB  . GLN A 74  ? 0.2678 0.3012 0.3183 0.0886  -0.0731 -0.0956 74  GLN A CB  
640  C  CG  . GLN A 74  ? 0.3030 0.1871 0.3844 -0.0403 -0.1158 0.0230  74  GLN A CG  
641  C  CD  . GLN A 74  ? 0.5327 0.3361 0.3411 0.1067  -0.1036 0.0527  74  GLN A CD  
642  O  OE1 . GLN A 74  ? 0.4763 0.4948 0.4083 0.0412  -0.0627 0.0449  74  GLN A OE1 
643  N  NE2 . GLN A 74  ? 0.2621 0.3880 0.2892 0.0615  0.0049  0.0326  74  GLN A NE2 
644  N  N   A ASP A 75  ? 0.2325 0.1660 0.1448 -0.0051 -0.0811 0.0006  75  ASP A N   
645  N  N   B ASP A 75  ? 0.2251 0.2958 0.2293 -0.0153 -0.0399 -0.1324 75  ASP A N   
646  C  CA  A ASP A 75  ? 0.1817 0.1410 0.2163 -0.0007 -0.0421 -0.0392 75  ASP A CA  
647  C  CA  B ASP A 75  ? 0.2212 0.3321 0.2885 -0.0131 -0.0093 -0.0688 75  ASP A CA  
648  C  C   A ASP A 75  ? 0.1103 0.2149 0.2576 0.0026  -0.0507 -0.0548 75  ASP A C   
649  C  C   B ASP A 75  ? 0.2307 0.2937 0.1925 0.0292  -0.0013 -0.0634 75  ASP A C   
650  O  O   A ASP A 75  ? 0.2806 0.1432 0.2329 0.0667  -0.0693 -0.0088 75  ASP A O   
651  O  O   B ASP A 75  ? 0.2698 0.7113 0.3865 -0.0961 0.0219  -0.1518 75  ASP A O   
652  C  CB  A ASP A 75  ? 0.2381 0.1216 0.2359 0.0439  -0.0328 -0.0230 75  ASP A CB  
653  C  CB  B ASP A 75  ? 0.2549 0.2917 0.2723 0.0161  0.0098  0.0307  75  ASP A CB  
654  C  CG  A ASP A 75  ? 0.1870 0.1647 0.1984 0.0555  0.0285  -0.0195 75  ASP A CG  
655  C  CG  B ASP A 75  ? 0.2872 0.2565 0.3501 0.0241  0.0076  0.1333  75  ASP A CG  
656  O  OD1 A ASP A 75  ? 0.1817 0.2556 0.1333 0.0068  0.0187  -0.0177 75  ASP A OD1 
657  O  OD1 B ASP A 75  ? 0.2311 0.2536 0.3025 0.0515  -0.0219 0.0882  75  ASP A OD1 
658  O  OD2 A ASP A 75  ? 0.2632 0.2646 0.2682 -0.0071 0.0790  -0.0794 75  ASP A OD2 
659  O  OD2 B ASP A 75  ? 0.4314 0.3488 0.4579 0.0088  0.1846  0.0610  75  ASP A OD2 
660  N  N   A LYS A 76  ? 0.1256 0.1993 0.2237 0.0227  -0.0307 0.0024  76  LYS A N   
661  N  N   B LYS A 76  ? 0.2323 0.1049 0.2529 -0.0026 -0.0579 0.0472  76  LYS A N   
662  C  CA  A LYS A 76  ? 0.1516 0.1590 0.1941 0.0322  -0.0219 -0.0141 76  LYS A CA  
663  C  CA  B LYS A 76  ? 0.3253 0.1018 0.2887 -0.0120 0.0160  -0.0259 76  LYS A CA  
664  C  C   A LYS A 76  ? 0.1111 0.1932 0.1113 0.0082  -0.0020 0.0007  76  LYS A C   
665  C  C   B LYS A 76  ? 0.4977 0.2158 0.1840 0.0935  -0.0697 0.0469  76  LYS A C   
666  O  O   A LYS A 76  ? 0.1744 0.2151 0.2052 -0.0520 -0.0456 0.0273  76  LYS A O   
667  O  O   B LYS A 76  ? 0.2736 0.3907 0.3993 -0.0540 -0.0815 0.1040  76  LYS A O   
668  C  CB  A LYS A 76  ? 0.1446 0.1694 0.1799 0.0386  -0.0276 0.0469  76  LYS A CB  
669  C  CB  B LYS A 76  ? 0.1975 0.2460 0.2648 -0.0877 0.0206  -0.0702 76  LYS A CB  
670  C  CG  A LYS A 76  ? 0.1967 0.1391 0.1999 0.0210  0.0261  0.0445  76  LYS A CG  
671  C  CG  B LYS A 76  ? 0.1412 0.2531 0.2273 0.0007  -0.0153 0.0046  76  LYS A CG  
672  C  CD  A LYS A 76  ? 0.1456 0.1666 0.1972 -0.0377 0.0159  -0.0107 76  LYS A CD  
673  C  CD  B LYS A 76  ? 0.2081 0.2084 0.2248 0.0241  -0.0798 -0.0120 76  LYS A CD  
674  C  CE  A LYS A 76  ? 0.2239 0.2469 0.1790 0.0350  -0.0156 0.0043  76  LYS A CE  
675  C  CE  B LYS A 76  ? 0.1996 0.1925 0.2169 0.0221  -0.0185 0.0208  76  LYS A CE  
676  N  NZ  A LYS A 76  ? 0.2513 0.1341 0.1732 -0.0255 0.0040  0.0000  76  LYS A NZ  
677  N  NZ  B LYS A 76  ? 0.2262 0.1782 0.2025 -0.0142 -0.0226 0.0657  76  LYS A NZ  
678  N  N   . ALA A 77  ? 0.1782 0.2768 0.2942 0.0410  -0.0850 0.0684  77  ALA A N   
679  C  CA  . ALA A 77  ? 0.1406 0.1731 0.1956 0.0126  -0.0284 0.0344  77  ALA A CA  
680  C  C   . ALA A 77  ? 0.1210 0.1377 0.1921 0.0152  -0.0148 0.0031  77  ALA A C   
681  O  O   . ALA A 77  ? 0.1148 0.2086 0.3104 -0.0091 -0.0087 -0.0500 77  ALA A O   
682  C  CB  . ALA A 77  ? 0.2151 0.2540 0.1543 0.0515  -0.0299 -0.0137 77  ALA A CB  
683  N  N   . VAL A 78  ? 0.1307 0.1494 0.1656 -0.0034 -0.0342 -0.0027 78  VAL A N   
684  C  CA  . VAL A 78  ? 0.1845 0.1511 0.1852 -0.0073 -0.0472 -0.0120 78  VAL A CA  
685  C  C   . VAL A 78  ? 0.1611 0.1069 0.2124 -0.0076 -0.0640 -0.0102 78  VAL A C   
686  O  O   . VAL A 78  ? 0.1532 0.1699 0.2282 -0.0366 -0.0658 0.0243  78  VAL A O   
687  C  CB  . VAL A 78  ? 0.2057 0.1659 0.2215 -0.0087 -0.0285 0.0115  78  VAL A CB  
688  C  CG1 . VAL A 78  ? 0.2467 0.1543 0.2854 0.0214  -0.0346 0.0390  78  VAL A CG1 
689  C  CG2 . VAL A 78  ? 0.2113 0.1932 0.2276 0.0000  0.0882  -0.0040 78  VAL A CG2 
690  N  N   . LEU A 79  ? 0.1176 0.1386 0.1525 0.0000  -0.0236 -0.0177 79  LEU A N   
691  C  CA  . LEU A 79  ? 0.1251 0.1492 0.1694 -0.0184 -0.0182 -0.0176 79  LEU A CA  
692  C  C   . LEU A 79  ? 0.1533 0.1402 0.1756 -0.0142 -0.0249 -0.0126 79  LEU A C   
693  O  O   . LEU A 79  ? 0.1743 0.1833 0.1852 -0.0474 -0.0046 -0.0401 79  LEU A O   
694  C  CB  . LEU A 79  ? 0.1146 0.1823 0.2072 -0.0054 -0.0291 0.0198  79  LEU A CB  
695  C  CG  . LEU A 79  ? 0.1473 0.1552 0.1826 0.0164  -0.0096 0.0203  79  LEU A CG  
696  C  CD1 . LEU A 79  ? 0.1439 0.1808 0.3309 -0.0010 0.0137  0.0006  79  LEU A CD1 
697  C  CD2 . LEU A 79  ? 0.1500 0.1586 0.1772 0.0181  0.0346  -0.0152 79  LEU A CD2 
698  N  N   . LYS A 80  ? 0.1870 0.1747 0.1580 -0.0285 0.0120  -0.0280 80  LYS A N   
699  C  CA  . LYS A 80  ? 0.2075 0.1902 0.2178 -0.0027 0.0337  -0.0230 80  LYS A CA  
700  C  C   . LYS A 80  ? 0.1344 0.1893 0.1862 -0.0080 0.0148  -0.0317 80  LYS A C   
701  O  O   . LYS A 80  ? 0.1559 0.1747 0.2273 -0.0276 -0.0222 -0.0155 80  LYS A O   
702  C  CB  . LYS A 80  ? 0.2583 0.2160 0.2452 0.0154  0.0266  -0.0074 80  LYS A CB  
703  C  CG  . LYS A 80  ? 0.2653 0.2872 0.3142 0.0582  0.0472  -0.0027 80  LYS A CG  
704  C  CD  . LYS A 80  ? 0.2203 0.3662 0.7307 0.1445  -0.1133 -0.1802 80  LYS A CD  
705  C  CE  . LYS A 80  ? 0.4020 0.4171 0.9258 0.2703  0.0733  0.1120  80  LYS A CE  
706  N  NZ  . LYS A 80  ? 0.7286 0.6028 0.8288 -0.0960 0.1190  -0.0285 80  LYS A NZ  
707  N  N   . GLY A 81  ? 0.1694 0.2079 0.1888 -0.0043 0.0142  -0.0255 81  GLY A N   
708  C  CA  . GLY A 81  ? 0.1745 0.2122 0.1782 0.0262  -0.0034 -0.0175 81  GLY A CA  
709  C  C   . GLY A 81  ? 0.1242 0.1852 0.2467 -0.0155 0.0489  -0.0172 81  GLY A C   
710  O  O   . GLY A 81  ? 0.1287 0.2011 0.1967 -0.0283 0.0153  -0.0456 81  GLY A O   
711  N  N   . GLY A 82  ? 0.1351 0.2377 0.2944 0.0041  0.0461  0.0250  82  GLY A N   
712  C  CA  . GLY A 82  ? 0.1438 0.2440 0.3086 0.0074  0.0559  0.0135  82  GLY A CA  
713  C  C   . GLY A 82  ? 0.1598 0.2569 0.2831 0.0522  0.0386  0.0081  82  GLY A C   
714  O  O   . GLY A 82  ? 0.2070 0.4271 0.2888 0.0838  0.0838  0.0175  82  GLY A O   
715  N  N   . PRO A 83  ? 0.1571 0.1974 0.2411 0.0322  0.0286  -0.0027 83  PRO A N   
716  C  CA  . PRO A 83  ? 0.1879 0.2201 0.2253 0.0658  0.0086  -0.0264 83  PRO A CA  
717  C  C   . PRO A 83  ? 0.1661 0.2205 0.2163 0.0270  -0.0098 -0.0577 83  PRO A C   
718  O  O   . PRO A 83  ? 0.2125 0.2682 0.2465 0.0186  -0.0566 -0.0296 83  PRO A O   
719  C  CB  . PRO A 83  ? 0.1718 0.2601 0.1878 0.0432  0.0197  0.0065  83  PRO A CB  
720  C  CG  . PRO A 83  ? 0.1562 0.2023 0.1895 0.0274  0.0060  -0.0065 83  PRO A CG  
721  C  CD  . PRO A 83  ? 0.1406 0.1559 0.2757 0.0129  0.0507  -0.0229 83  PRO A CD  
722  N  N   . LEU A 84  ? 0.1324 0.1720 0.1898 0.0054  0.0322  -0.0298 84  LEU A N   
723  C  CA  . LEU A 84  ? 0.1333 0.1588 0.1765 0.0329  0.0010  -0.0491 84  LEU A CA  
724  C  C   . LEU A 84  ? 0.1559 0.1754 0.2145 0.0252  0.0339  -0.0671 84  LEU A C   
725  O  O   . LEU A 84  ? 0.1615 0.2312 0.2567 0.0476  0.0414  -0.1005 84  LEU A O   
726  C  CB  . LEU A 84  ? 0.1430 0.1474 0.1914 0.0285  0.0013  -0.0608 84  LEU A CB  
727  C  CG  . LEU A 84  ? 0.1105 0.1412 0.1644 0.0296  0.0203  -0.0303 84  LEU A CG  
728  C  CD1 . LEU A 84  ? 0.1597 0.1791 0.1705 0.0406  -0.0203 -0.0353 84  LEU A CD1 
729  C  CD2 . LEU A 84  ? 0.1181 0.1568 0.1861 0.0048  0.0074  -0.0309 84  LEU A CD2 
730  N  N   . ASP A 85  ? 0.2101 0.1726 0.2784 0.0228  -0.0057 -0.1004 85  ASP A N   
731  C  CA  . ASP A 85  ? 0.3357 0.1729 0.3208 0.0379  -0.0210 -0.1396 85  ASP A CA  
732  C  C   . ASP A 85  ? 0.3070 0.1790 0.4895 0.0759  0.1164  -0.0076 85  ASP A C   
733  O  O   . ASP A 85  ? 0.3497 0.3034 0.4758 0.0421  0.1010  -0.1118 85  ASP A O   
734  C  CB  . ASP A 85  ? 0.5066 0.2741 0.5411 -0.0082 -0.0441 -0.2205 85  ASP A CB  
735  C  CG  . ASP A 85  ? 0.7426 0.9272 0.6363 0.0953  -0.0318 -0.1580 85  ASP A CG  
736  O  OD1 . ASP A 85  ? 0.7508 0.8409 0.8542 0.0087  -0.0878 -0.5167 85  ASP A OD1 
737  O  OD2 . ASP A 85  ? 0.5368 0.7687 0.9660 0.1884  -0.0432 -0.2926 85  ASP A OD2 
738  N  N   . GLY A 86  ? 0.2908 0.2225 0.4693 -0.0313 0.0119  -0.0829 86  GLY A N   
739  C  CA  . GLY A 86  ? 0.4120 0.3551 0.4047 -0.2019 0.0623  -0.1377 86  GLY A CA  
740  C  C   . GLY A 86  ? 0.2203 0.2434 0.2937 -0.1005 -0.0027 -0.0388 86  GLY A C   
741  O  O   . GLY A 86  ? 0.3551 0.2483 0.4041 -0.1336 0.0529  -0.0384 86  GLY A O   
742  N  N   . THR A 87  ? 0.1827 0.1534 0.2558 0.0199  0.0227  -0.0544 87  THR A N   
743  C  CA  . THR A 87  ? 0.1448 0.1924 0.2547 0.0219  0.0057  -0.0926 87  THR A CA  
744  C  C   . THR A 87  ? 0.1221 0.1182 0.2757 0.0174  0.0037  -0.0445 87  THR A C   
745  O  O   . THR A 87  ? 0.1410 0.1115 0.2903 -0.0049 0.0176  -0.0456 87  THR A O   
746  C  CB  . THR A 87  ? 0.1482 0.3591 0.3467 0.1441  -0.0333 -0.0513 87  THR A CB  
747  O  OG1 . THR A 87  ? 0.3009 0.4943 0.4650 0.2197  0.0252  -0.0812 87  THR A OG1 
748  C  CG2 . THR A 87  ? 0.1902 0.3063 0.4050 0.0662  -0.0693 0.0120  87  THR A CG2 
749  N  N   . TYR A 88  ? 0.1079 0.1192 0.2388 0.0068  0.0082  -0.0441 88  TYR A N   
750  C  CA  . TYR A 88  ? 0.1202 0.1085 0.1903 0.0252  0.0063  -0.0428 88  TYR A CA  
751  C  C   . TYR A 88  ? 0.1156 0.1061 0.1934 0.0274  -0.0397 -0.0287 88  TYR A C   
752  O  O   . TYR A 88  ? 0.1440 0.1683 0.2196 -0.0348 -0.0505 -0.0052 88  TYR A O   
753  C  CB  . TYR A 88  ? 0.1298 0.1095 0.1948 0.0104  -0.0303 -0.0425 88  TYR A CB  
754  C  CG  . TYR A 88  ? 0.1167 0.0908 0.1805 0.0142  0.0184  -0.0366 88  TYR A CG  
755  C  CD1 . TYR A 88  ? 0.1289 0.1356 0.1815 -0.0166 -0.0098 -0.0537 88  TYR A CD1 
756  C  CD2 . TYR A 88  ? 0.1172 0.0860 0.1597 0.0043  -0.0071 -0.0175 88  TYR A CD2 
757  C  CE1 . TYR A 88  ? 0.1209 0.1155 0.2134 0.0049  0.0188  -0.0467 88  TYR A CE1 
758  C  CE2 . TYR A 88  ? 0.1322 0.0780 0.1247 0.0068  0.0097  -0.0176 88  TYR A CE2 
759  C  CZ  . TYR A 88  ? 0.1220 0.1210 0.1410 -0.0264 0.0107  -0.0500 88  TYR A CZ  
760  O  OH  . TYR A 88  ? 0.1412 0.1458 0.1413 -0.0007 0.0271  -0.0493 88  TYR A OH  
761  N  N   A ARG A 89  ? 0.1191 0.0917 0.1965 0.0082  -0.0185 -0.0645 89  ARG A N   
762  N  N   B ARG A 89  ? 0.1298 0.1254 0.2131 0.0192  -0.0097 -0.0520 89  ARG A N   
763  C  CA  A ARG A 89  ? 0.1292 0.0794 0.1964 0.0285  -0.0439 -0.0423 89  ARG A CA  
764  C  CA  B ARG A 89  ? 0.1005 0.1254 0.2194 0.0270  -0.0461 -0.0472 89  ARG A CA  
765  C  C   A ARG A 89  ? 0.1008 0.0580 0.1272 0.0017  -0.0175 0.0049  89  ARG A C   
766  C  C   B ARG A 89  ? 0.1023 0.0665 0.1357 -0.0068 -0.0208 0.0113  89  ARG A C   
767  O  O   A ARG A 89  ? 0.1085 0.0865 0.1114 0.0017  -0.0219 0.0019  89  ARG A O   
768  O  O   B ARG A 89  ? 0.1083 0.0767 0.1120 0.0087  -0.0167 -0.0003 89  ARG A O   
769  C  CB  A ARG A 89  ? 0.1202 0.0342 0.3235 0.0038  -0.1155 0.0059  89  ARG A CB  
770  C  CB  B ARG A 89  ? 0.2608 0.0876 0.2949 0.0126  -0.0399 0.0037  89  ARG A CB  
771  C  CG  A ARG A 89  ? 0.1208 0.0762 0.1599 0.0294  0.0052  0.0126  89  ARG A CG  
772  C  CG  B ARG A 89  ? 0.1228 0.1430 0.1961 -0.0087 -0.0052 0.0226  89  ARG A CG  
773  C  CD  A ARG A 89  ? 0.1287 0.0505 0.1479 -0.0074 -0.0355 0.0153  89  ARG A CD  
774  C  CD  B ARG A 89  ? 0.2108 0.0285 0.1792 0.0125  -0.0308 0.0164  89  ARG A CD  
775  N  NE  A ARG A 89  ? 0.1383 0.0741 0.1175 0.0086  -0.0024 -0.0043 89  ARG A NE  
776  N  NE  B ARG A 89  ? 0.1611 0.0952 0.1620 0.0071  -0.0441 0.0081  89  ARG A NE  
777  C  CZ  A ARG A 89  ? 0.2244 0.0882 0.1190 -0.0186 -0.0082 -0.0091 89  ARG A CZ  
778  C  CZ  B ARG A 89  ? 0.2476 0.0970 0.1297 0.0035  -0.0549 0.0071  89  ARG A CZ  
779  N  NH1 A ARG A 89  ? 0.1809 0.1465 0.1132 -0.0175 -0.0262 0.0087  89  ARG A NH1 
780  N  NH1 B ARG A 89  ? 0.1896 0.1632 0.1967 0.0326  -0.0186 0.0188  89  ARG A NH1 
781  N  NH2 A ARG A 89  ? 0.2169 0.0996 0.1340 0.0076  0.0026  -0.0052 89  ARG A NH2 
782  N  NH2 B ARG A 89  ? 0.2745 0.1031 0.1326 -0.0046 -0.0331 0.0160  89  ARG A NH2 
783  N  N   . LEU A 90  ? 0.1168 0.0759 0.1264 0.0120  -0.0287 -0.0052 90  LEU A N   
784  C  CA  . LEU A 90  ? 0.1193 0.0829 0.1274 -0.0006 -0.0348 -0.0065 90  LEU A CA  
785  C  C   . LEU A 90  ? 0.1180 0.0760 0.1175 -0.0057 -0.0219 0.0195  90  LEU A C   
786  O  O   . LEU A 90  ? 0.1377 0.1193 0.1437 -0.0041 -0.0258 0.0362  90  LEU A O   
787  C  CB  . LEU A 90  ? 0.1290 0.1006 0.1009 -0.0119 -0.0161 -0.0035 90  LEU A CB  
788  C  CG  . LEU A 90  ? 0.1332 0.0961 0.0935 -0.0199 -0.0126 0.0020  90  LEU A CG  
789  C  CD1 . LEU A 90  ? 0.1555 0.0799 0.1307 0.0000  -0.0196 -0.0091 90  LEU A CD1 
790  C  CD2 . LEU A 90  ? 0.1635 0.1274 0.1280 -0.0463 -0.0063 -0.0198 90  LEU A CD2 
791  N  N   . THR A 91  ? 0.1274 0.0750 0.1014 0.0115  -0.0229 -0.0059 91  THR A N   
792  C  CA  . THR A 91  ? 0.1368 0.0806 0.0909 -0.0006 -0.0114 0.0104  91  THR A CA  
793  C  C   . THR A 91  ? 0.1221 0.0631 0.1137 -0.0037 -0.0109 0.0118  91  THR A C   
794  O  O   . THR A 91  ? 0.1220 0.0823 0.1024 -0.0109 -0.0140 0.0220  91  THR A O   
795  C  CB  . THR A 91  ? 0.1430 0.1120 0.1304 -0.0176 -0.0155 0.0073  91  THR A CB  
796  O  OG1 . THR A 91  ? 0.1818 0.1515 0.1439 -0.0645 -0.0115 0.0335  91  THR A OG1 
797  C  CG2 . THR A 91  ? 0.1485 0.0945 0.1395 -0.0184 -0.0250 0.0104  91  THR A CG2 
798  N  N   A GLN A 92  ? 0.0847 0.0582 0.1013 -0.0109 0.0059  0.0097  92  GLN A N   
799  N  N   B GLN A 92  ? 0.0678 0.0766 0.0883 0.0052  -0.0253 0.0024  92  GLN A N   
800  C  CA  A GLN A 92  ? 0.1138 0.0653 0.0864 0.0027  0.0093  0.0087  92  GLN A CA  
801  C  CA  B GLN A 92  ? 0.1058 0.0781 0.0601 -0.0020 0.0076  0.0087  92  GLN A CA  
802  C  C   A GLN A 92  ? 0.0895 0.0648 0.0833 0.0030  -0.0006 0.0060  92  GLN A C   
803  C  C   B GLN A 92  ? 0.0900 0.0627 0.0775 0.0129  0.0085  0.0120  92  GLN A C   
804  O  O   A GLN A 92  ? 0.0753 0.0775 0.0771 0.0063  -0.0007 0.0188  92  GLN A O   
805  O  O   B GLN A 92  ? 0.0636 0.0648 0.0719 0.0031  0.0031  -0.0015 92  GLN A O   
806  C  CB  A GLN A 92  ? 0.1032 0.0874 0.0937 0.0141  -0.0093 -0.0041 92  GLN A CB  
807  C  CB  B GLN A 92  ? 0.0934 0.1075 0.0961 -0.0023 0.0031  0.0247  92  GLN A CB  
808  C  CG  A GLN A 92  ? 0.1206 0.0864 0.1079 0.0038  -0.0166 0.0010  92  GLN A CG  
809  C  CG  B GLN A 92  ? 0.0983 0.1395 0.0996 0.0209  0.0093  0.0120  92  GLN A CG  
810  C  CD  A GLN A 92  ? 0.1199 0.0910 0.0820 0.0006  -0.0082 0.0249  92  GLN A CD  
811  C  CD  B GLN A 92  ? 0.1162 0.0964 0.1181 0.0026  0.0129  0.0071  92  GLN A CD  
812  O  OE1 A GLN A 92  ? 0.1448 0.0882 0.1031 -0.0017 -0.0368 0.0186  92  GLN A OE1 
813  O  OE1 B GLN A 92  ? 0.1251 0.1133 0.1499 0.0080  0.0148  0.0274  92  GLN A OE1 
814  N  NE2 A GLN A 92  ? 0.1334 0.1306 0.2029 -0.0291 -0.0452 0.0627  92  GLN A NE2 
815  N  NE2 B GLN A 92  ? 0.1554 0.1225 0.1492 -0.0294 0.0344  0.0093  92  GLN A NE2 
816  N  N   . PHE A 93  ? 0.1060 0.0635 0.0839 0.0027  -0.0017 0.0120  93  PHE A N   
817  C  CA  . PHE A 93  ? 0.1084 0.0688 0.0864 0.0006  -0.0038 0.0135  93  PHE A CA  
818  C  C   . PHE A 93  ? 0.0884 0.0683 0.0697 -0.0035 -0.0126 0.0046  93  PHE A C   
819  O  O   . PHE A 93  ? 0.1103 0.0771 0.0781 0.0082  -0.0038 0.0107  93  PHE A O   
820  C  CB  . PHE A 93  ? 0.1007 0.0953 0.0805 -0.0019 -0.0051 0.0120  93  PHE A CB  
821  C  CG  . PHE A 93  ? 0.0979 0.0892 0.0794 -0.0015 0.0046  0.0114  93  PHE A CG  
822  C  CD1 . PHE A 93  ? 0.1084 0.0740 0.1141 -0.0082 0.0040  0.0023  93  PHE A CD1 
823  C  CD2 . PHE A 93  ? 0.1107 0.0891 0.1049 -0.0049 -0.0057 0.0115  93  PHE A CD2 
824  C  CE1 . PHE A 93  ? 0.1208 0.0908 0.1124 0.0071  -0.0208 0.0017  93  PHE A CE1 
825  C  CE2 . PHE A 93  ? 0.1118 0.0955 0.0974 -0.0015 -0.0132 0.0024  93  PHE A CE2 
826  C  CZ  . PHE A 93  ? 0.1186 0.0760 0.1290 0.0003  -0.0019 -0.0043 93  PHE A CZ  
827  N  N   . HIS A 94  ? 0.0979 0.0723 0.0795 0.0043  -0.0087 0.0031  94  HIS A N   
828  C  CA  . HIS A 94  ? 0.0920 0.0771 0.0732 0.0052  0.0031  0.0015  94  HIS A CA  
829  C  C   . HIS A 94  ? 0.0890 0.0699 0.0733 -0.0006 -0.0148 0.0013  94  HIS A C   
830  O  O   . HIS A 94  ? 0.0990 0.0732 0.0824 0.0073  0.0097  0.0119  94  HIS A O   
831  C  CB  . HIS A 94  ? 0.0922 0.0820 0.0778 0.0024  0.0024  0.0003  94  HIS A CB  
832  C  CG  . HIS A 94  ? 0.0999 0.0743 0.0846 -0.0059 -0.0026 0.0074  94  HIS A CG  
833  N  ND1 . HIS A 94  ? 0.1026 0.0799 0.0873 0.0086  -0.0076 0.0076  94  HIS A ND1 
834  C  CD2 . HIS A 94  ? 0.0926 0.1102 0.0617 -0.0020 -0.0026 0.0087  94  HIS A CD2 
835  C  CE1 . HIS A 94  ? 0.0806 0.0847 0.0996 0.0020  -0.0109 0.0196  94  HIS A CE1 
836  N  NE2 . HIS A 94  ? 0.0780 0.0781 0.0697 0.0000  -0.0087 0.0115  94  HIS A NE2 
837  N  N   . PHE A 95  ? 0.0961 0.0717 0.0828 0.0015  -0.0074 0.0015  95  PHE A N   
838  C  CA  . PHE A 95  ? 0.0956 0.0710 0.0979 0.0037  -0.0174 0.0031  95  PHE A CA  
839  C  C   . PHE A 95  ? 0.0919 0.0734 0.0671 0.0020  0.0085  0.0006  95  PHE A C   
840  O  O   . PHE A 95  ? 0.0990 0.0916 0.0865 0.0019  0.0076  0.0104  95  PHE A O   
841  C  CB  . PHE A 95  ? 0.0884 0.0944 0.0910 0.0164  -0.0093 -0.0148 95  PHE A CB  
842  C  CG  . PHE A 95  ? 0.1032 0.0768 0.0926 0.0148  -0.0052 -0.0129 95  PHE A CG  
843  C  CD1 . PHE A 95  ? 0.1132 0.0901 0.1147 0.0024  -0.0221 0.0000  95  PHE A CD1 
844  C  CD2 . PHE A 95  ? 0.1013 0.1000 0.1015 -0.0059 -0.0071 -0.0185 95  PHE A CD2 
845  C  CE1 . PHE A 95  ? 0.1111 0.1102 0.1137 0.0154  -0.0205 -0.0142 95  PHE A CE1 
846  C  CE2 . PHE A 95  ? 0.1008 0.1031 0.1078 -0.0076 0.0003  -0.0207 95  PHE A CE2 
847  C  CZ  . PHE A 95  ? 0.0942 0.1186 0.1190 0.0118  -0.0103 -0.0502 95  PHE A CZ  
848  N  N   . HIS A 96  ? 0.0872 0.0715 0.0901 0.0003  0.0000  0.0010  96  HIS A N   
849  C  CA  . HIS A 96  ? 0.0886 0.0768 0.0850 0.0141  -0.0103 -0.0015 96  HIS A CA  
850  C  C   . HIS A 96  ? 0.0934 0.0714 0.0868 0.0120  0.0040  0.0038  96  HIS A C   
851  O  O   . HIS A 96  ? 0.0904 0.0781 0.0970 0.0051  0.0076  -0.0041 96  HIS A O   
852  C  CB  . HIS A 96  ? 0.0946 0.0787 0.0907 0.0107  -0.0057 -0.0026 96  HIS A CB  
853  C  CG  . HIS A 96  ? 0.0856 0.0769 0.0803 0.0031  -0.0070 0.0043  96  HIS A CG  
854  N  ND1 . HIS A 96  ? 0.0948 0.0776 0.0947 0.0062  -0.0115 -0.0052 96  HIS A ND1 
855  C  CD2 . HIS A 96  ? 0.1102 0.0627 0.0847 -0.0052 -0.0103 0.0024  96  HIS A CD2 
856  C  CE1 . HIS A 96  ? 0.0975 0.0759 0.0869 0.0244  0.0000  0.0110  96  HIS A CE1 
857  N  NE2 . HIS A 96  ? 0.0838 0.0830 0.0678 0.0063  -0.0054 0.0035  96  HIS A NE2 
858  N  N   . TRP A 97  ? 0.0901 0.0715 0.0784 0.0065  -0.0038 -0.0024 97  TRP A N   
859  C  CA  . TRP A 97  ? 0.0974 0.0762 0.0948 0.0065  0.0000  -0.0019 97  TRP A CA  
860  C  C   . TRP A 97  ? 0.0952 0.0813 0.0761 0.0027  -0.0035 -0.0046 97  TRP A C   
861  O  O   . TRP A 97  ? 0.0898 0.0875 0.0936 0.0051  0.0046  -0.0043 97  TRP A O   
862  C  CB  . TRP A 97  ? 0.0946 0.0887 0.0805 0.0065  0.0034  -0.0060 97  TRP A CB  
863  C  CG  . TRP A 97  ? 0.0935 0.0824 0.0856 0.0027  -0.0070 -0.0131 97  TRP A CG  
864  C  CD1 . TRP A 97  ? 0.1112 0.1106 0.0813 0.0027  -0.0038 -0.0153 97  TRP A CD1 
865  C  CD2 . TRP A 97  ? 0.0900 0.0937 0.0701 -0.0019 -0.0017 0.0007  97  TRP A CD2 
866  N  NE1 . TRP A 97  ? 0.1194 0.0966 0.0866 0.0131  0.0019  0.0015  97  TRP A NE1 
867  C  CE2 . TRP A 97  ? 0.0987 0.0869 0.0864 0.0017  0.0024  -0.0046 97  TRP A CE2 
868  C  CE3 . TRP A 97  ? 0.0935 0.0838 0.0916 0.0027  0.0006  0.0017  97  TRP A CE3 
869  C  CZ2 . TRP A 97  ? 0.1084 0.1079 0.0856 0.0071  -0.0054 -0.0015 97  TRP A CZ2 
870  C  CZ3 . TRP A 97  ? 0.1123 0.0990 0.0908 0.0038  0.0043  0.0049  97  TRP A CZ3 
871  C  CH2 . TRP A 97  ? 0.1158 0.0996 0.0838 -0.0015 -0.0034 -0.0006 97  TRP A CH2 
872  N  N   . GLY A 98  ? 0.1035 0.0693 0.0951 0.0113  -0.0006 -0.0013 98  GLY A N   
873  C  CA  . GLY A 98  ? 0.1120 0.0891 0.0881 0.0142  0.0043  -0.0109 98  GLY A CA  
874  C  C   . GLY A 98  ? 0.1057 0.0863 0.1067 0.0088  -0.0051 -0.0020 98  GLY A C   
875  O  O   . GLY A 98  ? 0.1211 0.0964 0.1105 0.0035  -0.0046 -0.0197 98  GLY A O   
876  N  N   . SER A 99  ? 0.1198 0.0839 0.1217 0.0155  0.0003  -0.0210 99  SER A N   
877  C  CA  . SER A 99  ? 0.1377 0.0981 0.1279 0.0167  0.0065  -0.0195 99  SER A CA  
878  C  C   . SER A 99  ? 0.1350 0.0939 0.1344 0.0215  -0.0154 -0.0252 99  SER A C   
879  O  O   . SER A 99  ? 0.2066 0.1527 0.1755 -0.0034 -0.0204 -0.0719 99  SER A O   
880  C  CB  . SER A 99  ? 0.1472 0.1368 0.1245 0.0142  0.0109  -0.0370 99  SER A CB  
881  O  OG  . SER A 99  ? 0.1435 0.1022 0.1659 0.0231  0.0065  -0.0153 99  SER A OG  
882  N  N   . LEU A 100 ? 0.1357 0.0917 0.1544 0.0115  0.0250  -0.0164 100 LEU A N   
883  C  CA  . LEU A 100 ? 0.1400 0.0767 0.2425 0.0006  0.0273  -0.0261 100 LEU A CA  
884  C  C   . LEU A 100 ? 0.1366 0.1096 0.1923 0.0200  -0.0034 -0.0248 100 LEU A C   
885  O  O   . LEU A 100 ? 0.1435 0.0930 0.2003 0.0113  0.0010  -0.0326 100 LEU A O   
886  C  CB  . LEU A 100 ? 0.1824 0.1253 0.3607 0.0315  0.0683  0.0324  100 LEU A CB  
887  C  CG  . LEU A 100 ? 0.2513 0.2099 0.2901 0.0472  0.0478  0.0471  100 LEU A CG  
888  C  CD1 . LEU A 100 ? 0.3280 0.3064 0.3136 0.1272  0.0540  0.0894  100 LEU A CD1 
889  C  CD2 . LEU A 100 ? 0.2506 0.3222 0.2811 0.0255  0.0758  -0.1356 100 LEU A CD2 
890  N  N   . ASP A 101 ? 0.1333 0.0944 0.1930 0.0031  -0.0098 -0.0071 101 ASP A N   
891  C  CA  . ASP A 101 ? 0.1387 0.0865 0.1946 0.0136  0.0024  0.0163  101 ASP A CA  
892  C  C   . ASP A 101 ? 0.1332 0.0948 0.2074 0.0006  -0.0038 0.0152  101 ASP A C   
893  O  O   . ASP A 101 ? 0.1894 0.1172 0.1990 0.0237  0.0012  0.0244  101 ASP A O   
894  C  CB  . ASP A 101 ? 0.1424 0.1077 0.2002 -0.0088 -0.0206 0.0335  101 ASP A CB  
895  C  CG  . ASP A 101 ? 0.1368 0.1360 0.2438 -0.0027 -0.0271 0.0461  101 ASP A CG  
896  O  OD1 . ASP A 101 ? 0.1853 0.1393 0.2172 -0.0054 -0.0142 0.0428  101 ASP A OD1 
897  O  OD2 . ASP A 101 ? 0.1817 0.1912 0.3095 -0.0555 -0.0627 0.0586  101 ASP A OD2 
898  N  N   . GLY A 102 ? 0.1421 0.1124 0.2025 -0.0102 -0.0353 0.0320  102 GLY A N   
899  C  CA  . GLY A 102 ? 0.1588 0.1212 0.2118 0.0097  -0.0164 0.0439  102 GLY A CA  
900  C  C   . GLY A 102 ? 0.1456 0.1156 0.1527 0.0060  0.0080  0.0240  102 GLY A C   
901  O  O   . GLY A 102 ? 0.1703 0.1203 0.1631 0.0006  0.0098  0.0366  102 GLY A O   
902  N  N   . GLN A 103 ? 0.1217 0.0936 0.1758 0.0038  0.0093  0.0233  103 GLN A N   
903  C  CA  . GLN A 103 ? 0.1186 0.0856 0.1357 0.0087  0.0076  -0.0027 103 GLN A CA  
904  C  C   . GLN A 103 ? 0.0996 0.0875 0.0981 0.0048  0.0126  -0.0024 103 GLN A C   
905  O  O   . GLN A 103 ? 0.1314 0.0875 0.1120 0.0031  0.0038  -0.0051 103 GLN A O   
906  C  CB  . GLN A 103 ? 0.1288 0.1043 0.1242 0.0164  0.0043  0.0086  103 GLN A CB  
907  C  CG  . GLN A 103 ? 0.1216 0.1263 0.1421 0.0275  0.0227  0.0041  103 GLN A CG  
908  C  CD  . GLN A 103 ? 0.1720 0.1569 0.1729 0.0722  0.0366  0.0449  103 GLN A CD  
909  O  OE1 . GLN A 103 ? 0.1674 0.1756 0.1763 0.0463  0.0313  0.0219  103 GLN A OE1 
910  N  NE2 . GLN A 103 ? 0.2147 0.2377 0.2741 0.1506  0.1052  0.1262  103 GLN A NE2 
911  N  N   . GLY A 104 ? 0.0903 0.0893 0.1053 0.0038  -0.0003 -0.0013 104 GLY A N   
912  C  CA  . GLY A 104 ? 0.0961 0.0777 0.0891 0.0077  0.0126  0.0013  104 GLY A CA  
913  C  C   . GLY A 104 ? 0.0900 0.0692 0.0988 -0.0023 -0.0065 -0.0015 104 GLY A C   
914  O  O   . GLY A 104 ? 0.1041 0.0872 0.1000 0.0007  0.0048  0.0017  104 GLY A O   
915  N  N   . SER A 105 ? 0.0891 0.0812 0.0812 0.0003  0.0027  -0.0007 105 SER A N   
916  C  CA  . SER A 105 ? 0.0815 0.0688 0.0980 0.0005  0.0027  -0.0013 105 SER A CA  
917  C  C   . SER A 105 ? 0.0995 0.0743 0.0832 -0.0030 0.0024  0.0185  105 SER A C   
918  O  O   . SER A 105 ? 0.1084 0.0816 0.1062 0.0132  -0.0194 -0.0093 105 SER A O   
919  C  CB  . SER A 105 ? 0.0864 0.0955 0.0894 -0.0059 0.0026  0.0109  105 SER A CB  
920  O  OG  . SER A 105 ? 0.0988 0.0828 0.0908 -0.0041 0.0027  0.0148  105 SER A OG  
921  N  N   . GLU A 106 ? 0.0838 0.0714 0.0855 0.0015  0.0076  0.0024  106 GLU A N   
922  C  CA  . GLU A 106 ? 0.0922 0.0749 0.0864 -0.0027 -0.0030 0.0017  106 GLU A CA  
923  C  C   . GLU A 106 ? 0.0866 0.0716 0.0866 -0.0057 -0.0109 0.0065  106 GLU A C   
924  O  O   . GLU A 106 ? 0.0935 0.0856 0.0960 0.0052  -0.0054 0.0082  106 GLU A O   
925  C  CB  . GLU A 106 ? 0.1054 0.0776 0.0750 -0.0082 0.0027  0.0081  106 GLU A CB  
926  C  CG  . GLU A 106 ? 0.1383 0.0946 0.0859 -0.0120 0.0142  0.0065  106 GLU A CG  
927  C  CD  . GLU A 106 ? 0.0854 0.0838 0.0904 -0.0010 -0.0065 0.0031  106 GLU A CD  
928  O  OE1 . GLU A 106 ? 0.0833 0.0830 0.0979 -0.0046 0.0038  -0.0027 106 GLU A OE1 
929  O  OE2 . GLU A 106 ? 0.0912 0.1032 0.1155 0.0098  0.0037  0.0017  106 GLU A OE2 
930  N  N   . HIS A 107 ? 0.0840 0.0758 0.0828 0.0020  -0.0051 0.0024  107 HIS A N   
931  C  CA  . HIS A 107 ? 0.0936 0.0701 0.0768 0.0000  -0.0026 -0.0012 107 HIS A CA  
932  C  C   . HIS A 107 ? 0.0918 0.0776 0.0797 0.0057  -0.0054 0.0035  107 HIS A C   
933  O  O   . HIS A 107 ? 0.0937 0.0753 0.0829 0.0057  -0.0076 0.0054  107 HIS A O   
934  C  CB  . HIS A 107 ? 0.0934 0.0890 0.0822 0.0040  0.0065  0.0065  107 HIS A CB  
935  C  CG  . HIS A 107 ? 0.0788 0.0778 0.0796 0.0087  0.0057  0.0031  107 HIS A CG  
936  N  ND1 . HIS A 107 ? 0.0961 0.0732 0.0867 0.0062  0.0054  0.0120  107 HIS A ND1 
937  C  CD2 . HIS A 107 ? 0.0722 0.0926 0.0799 0.0104  0.0049  -0.0093 107 HIS A CD2 
938  C  CE1 . HIS A 107 ? 0.0927 0.0864 0.0725 0.0024  0.0159  -0.0020 107 HIS A CE1 
939  N  NE2 . HIS A 107 ? 0.0893 0.0794 0.0754 0.0098  -0.0052 -0.0063 107 HIS A NE2 
940  N  N   . THR A 108 ? 0.0936 0.0718 0.0922 0.0024  -0.0027 0.0110  108 THR A N   
941  C  CA  . THR A 108 ? 0.1049 0.0752 0.0948 0.0088  0.0074  0.0142  108 THR A CA  
942  C  C   . THR A 108 ? 0.1014 0.0741 0.0886 0.0065  -0.0052 0.0098  108 THR A C   
943  O  O   . THR A 108 ? 0.1074 0.0848 0.0922 0.0015  0.0074  0.0099  108 THR A O   
944  C  CB  . THR A 108 ? 0.1136 0.0961 0.1004 0.0253  -0.0108 0.0049  108 THR A CB  
945  O  OG1 . THR A 108 ? 0.1089 0.0917 0.1146 0.0068  -0.0059 0.0162  108 THR A OG1 
946  C  CG2 . THR A 108 ? 0.1174 0.0926 0.1114 0.0113  0.0013  0.0071  108 THR A CG2 
947  N  N   . VAL A 109 ? 0.1095 0.0856 0.1007 -0.0006 0.0038  0.0177  109 VAL A N   
948  C  CA  . VAL A 109 ? 0.1149 0.1036 0.1229 0.0017  0.0120  0.0229  109 VAL A CA  
949  C  C   . VAL A 109 ? 0.1208 0.0928 0.1139 0.0010  0.0038  0.0258  109 VAL A C   
950  O  O   . VAL A 109 ? 0.1316 0.0935 0.1287 0.0019  0.0162  0.0248  109 VAL A O   
951  C  CB  . VAL A 109 ? 0.1247 0.1128 0.1210 0.0060  0.0063  0.0193  109 VAL A CB  
952  C  CG1 . VAL A 109 ? 0.1340 0.1263 0.1728 -0.0020 0.0232  0.0219  109 VAL A CG1 
953  C  CG2 . VAL A 109 ? 0.1300 0.1157 0.1380 0.0046  -0.0214 0.0366  109 VAL A CG2 
954  N  N   . ASP A 110 ? 0.1324 0.1005 0.1102 0.0020  0.0052  0.0342  110 ASP A N   
955  C  CA  . ASP A 110 ? 0.1703 0.1190 0.1247 0.0185  0.0318  0.0621  110 ASP A CA  
956  C  C   . ASP A 110 ? 0.1544 0.1084 0.1286 0.0148  -0.0035 0.0239  110 ASP A C   
957  O  O   . ASP A 110 ? 0.1852 0.1040 0.1420 0.0252  0.0208  0.0427  110 ASP A O   
958  C  CB  . ASP A 110 ? 0.2070 0.1342 0.1247 0.0017  0.0388  0.0482  110 ASP A CB  
959  C  CG  . ASP A 110 ? 0.1808 0.1588 0.1224 -0.0182 0.0285  0.0553  110 ASP A CG  
960  O  OD1 . ASP A 110 ? 0.2081 0.1421 0.1546 0.0270  0.0403  0.0399  110 ASP A OD1 
961  O  OD2 . ASP A 110 ? 0.2011 0.2088 0.1764 0.0148  0.0307  0.0555  110 ASP A OD2 
962  N  N   . LYS A 111 ? 0.1361 0.1157 0.1123 0.0198  0.0068  0.0308  111 LYS A N   
963  C  CA  . LYS A 111 ? 0.1410 0.1049 0.1239 0.0275  -0.0026 0.0221  111 LYS A CA  
964  C  C   . LYS A 111 ? 0.1483 0.0961 0.1095 0.0296  0.0121  0.0263  111 LYS A C   
965  O  O   . LYS A 111 ? 0.1655 0.1217 0.1349 0.0264  0.0164  0.0060  111 LYS A O   
966  C  CB  . LYS A 111 ? 0.1667 0.1421 0.1415 0.0498  -0.0199 0.0283  111 LYS A CB  
967  C  CG  . LYS A 111 ? 0.2192 0.1965 0.1615 0.0803  -0.0241 0.0348  111 LYS A CG  
968  C  CD  . LYS A 111 ? 0.1937 0.2585 0.2433 0.0423  -0.0678 -0.0408 111 LYS A CD  
969  C  CE  . LYS A 111 ? 0.2870 0.3023 0.2086 0.0454  -0.0428 0.0049  111 LYS A CE  
970  N  NZ  . LYS A 111 ? 0.2415 0.3591 0.3725 0.0177  -0.0538 0.1155  111 LYS A NZ  
971  N  N   . LYS A 112 ? 0.1396 0.0842 0.1102 0.0107  0.0010  0.0124  112 LYS A N   
972  C  CA  . LYS A 112 ? 0.1481 0.1066 0.1261 0.0024  0.0131  0.0205  112 LYS A CA  
973  C  C   . LYS A 112 ? 0.1155 0.0877 0.1155 0.0026  -0.0142 0.0153  112 LYS A C   
974  O  O   . LYS A 112 ? 0.1273 0.0838 0.1121 0.0041  -0.0037 0.0038  112 LYS A O   
975  C  CB  . LYS A 112 ? 0.1658 0.1343 0.1527 -0.0460 0.0108  0.0003  112 LYS A CB  
976  C  CG  . LYS A 112 ? 0.1555 0.1703 0.2047 -0.0410 0.0082  -0.0439 112 LYS A CG  
977  C  CD  . LYS A 112 ? 0.1674 0.2203 0.2031 -0.0097 0.0057  -0.0198 112 LYS A CD  
978  C  CE  . LYS A 112 ? 0.2804 0.2364 0.2444 0.0015  -0.0619 -0.0666 112 LYS A CE  
979  N  NZ  . LYS A 112 ? 0.2424 0.2125 0.2490 0.0012  -0.0087 0.0401  112 LYS A NZ  
980  N  N   A LYS A 113 ? 0.1132 0.1067 0.1032 0.0051  0.0040  0.0086  113 LYS A N   
981  N  N   B LYS A 113 ? 0.0917 0.1128 0.1067 0.0198  0.0082  0.0171  113 LYS A N   
982  C  CA  A LYS A 113 ? 0.1396 0.0917 0.1149 0.0219  -0.0020 0.0159  113 LYS A CA  
983  C  CA  B LYS A 113 ? 0.1199 0.1150 0.1155 0.0049  -0.0097 0.0295  113 LYS A CA  
984  C  C   A LYS A 113 ? 0.1101 0.0734 0.1192 0.0131  0.0263  0.0140  113 LYS A C   
985  C  C   B LYS A 113 ? 0.1199 0.0812 0.1146 0.0167  -0.0041 0.0130  113 LYS A C   
986  O  O   A LYS A 113 ? 0.1322 0.0776 0.1136 -0.0006 0.0060  0.0143  113 LYS A O   
987  O  O   B LYS A 113 ? 0.1252 0.0799 0.1246 0.0252  -0.0052 0.0098  113 LYS A O   
988  C  CB  A LYS A 113 ? 0.1151 0.1541 0.0900 0.0068  -0.0181 0.0177  113 LYS A CB  
989  C  CB  B LYS A 113 ? 0.1283 0.1356 0.1159 0.0197  -0.0137 -0.0023 113 LYS A CB  
990  C  CG  A LYS A 113 ? 0.1128 0.1278 0.1307 -0.0007 -0.0041 -0.0027 113 LYS A CG  
991  C  CG  B LYS A 113 ? 0.1103 0.1765 0.1076 0.0126  0.0054  0.0258  113 LYS A CG  
992  C  CD  A LYS A 113 ? 0.1066 0.1127 0.1525 0.0063  0.0065  0.0031  113 LYS A CD  
993  C  CD  B LYS A 113 ? 0.1027 0.1254 0.1289 -0.0007 0.0082  -0.0030 113 LYS A CD  
994  C  CE  A LYS A 113 ? 0.1484 0.1391 0.1858 0.0046  -0.0270 -0.0077 113 LYS A CE  
995  C  CE  B LYS A 113 ? 0.1392 0.2443 0.1307 -0.0115 -0.0273 0.0113  113 LYS A CE  
996  N  NZ  A LYS A 113 ? 0.1349 0.1585 0.1818 0.0399  -0.0305 -0.0259 113 LYS A NZ  
997  N  NZ  B LYS A 113 ? 0.1932 0.2307 0.1967 0.0266  -0.0366 0.0073  113 LYS A NZ  
998  N  N   . TYR A 114 ? 0.1014 0.0766 0.1075 0.0065  -0.0035 0.0031  114 TYR A N   
999  C  CA  . TYR A 114 ? 0.1114 0.0690 0.1111 -0.0054 -0.0163 0.0031  114 TYR A CA  
1000 C  C   . TYR A 114 ? 0.0957 0.0522 0.1041 -0.0006 -0.0065 -0.0026 114 TYR A C   
1001 O  O   . TYR A 114 ? 0.1032 0.0842 0.1111 -0.0024 0.0015  -0.0031 114 TYR A O   
1002 C  CB  . TYR A 114 ? 0.1084 0.0725 0.1199 0.0024  -0.0038 0.0017  114 TYR A CB  
1003 C  CG  . TYR A 114 ? 0.1111 0.0688 0.1128 0.0102  0.0006  0.0119  114 TYR A CG  
1004 C  CD1 . TYR A 114 ? 0.1289 0.0874 0.1421 0.0178  -0.0074 0.0038  114 TYR A CD1 
1005 C  CD2 . TYR A 114 ? 0.1098 0.0904 0.1676 -0.0013 0.0071  0.0175  114 TYR A CD2 
1006 C  CE1 . TYR A 114 ? 0.1932 0.1102 0.1292 0.0425  0.0087  0.0296  114 TYR A CE1 
1007 C  CE2 . TYR A 114 ? 0.1492 0.1203 0.1831 0.0071  0.0287  0.0068  114 TYR A CE2 
1008 C  CZ  . TYR A 114 ? 0.1559 0.1492 0.1474 0.0120  0.0359  0.0263  114 TYR A CZ  
1009 O  OH  . TYR A 114 ? 0.2502 0.2216 0.2086 0.0406  0.0961  0.0392  114 TYR A OH  
1010 N  N   . ALA A 115 ? 0.1068 0.0750 0.1027 0.0076  -0.0087 -0.0012 115 ALA A N   
1011 C  CA  . ALA A 115 ? 0.1119 0.0751 0.1005 -0.0074 -0.0027 -0.0113 115 ALA A CA  
1012 C  C   . ALA A 115 ? 0.0892 0.0750 0.1060 0.0041  0.0035  0.0027  115 ALA A C   
1013 O  O   . ALA A 115 ? 0.0979 0.0763 0.1076 0.0057  0.0013  -0.0065 115 ALA A O   
1014 C  CB  . ALA A 115 ? 0.1234 0.0847 0.1168 -0.0068 -0.0136 -0.0124 115 ALA A CB  
1015 N  N   . ALA A 116 ? 0.1023 0.0599 0.0999 0.0054  -0.0005 0.0031  116 ALA A N   
1016 C  CA  . ALA A 116 ? 0.0969 0.0610 0.0956 -0.0054 0.0049  -0.0005 116 ALA A CA  
1017 C  C   . ALA A 116 ? 0.0812 0.0644 0.0885 0.0110  -0.0049 0.0108  116 ALA A C   
1018 O  O   . ALA A 116 ? 0.0970 0.0715 0.0900 -0.0031 0.0041  0.0046  116 ALA A O   
1019 C  CB  . ALA A 116 ? 0.1058 0.0820 0.0838 0.0013  -0.0010 -0.0070 116 ALA A CB  
1020 N  N   . GLU A 117 ? 0.0917 0.0628 0.0944 0.0163  0.0041  0.0054  117 GLU A N   
1021 C  CA  . GLU A 117 ? 0.0992 0.0594 0.0856 0.0167  -0.0074 -0.0040 117 GLU A CA  
1022 C  C   . GLU A 117 ? 0.0859 0.0687 0.0881 0.0027  0.0046  -0.0065 117 GLU A C   
1023 O  O   . GLU A 117 ? 0.0883 0.0810 0.1053 0.0126  0.0198  0.0218  117 GLU A O   
1024 C  CB  . GLU A 117 ? 0.0975 0.0866 0.0970 0.0071  -0.0006 -0.0003 117 GLU A CB  
1025 C  CG  . GLU A 117 ? 0.1098 0.0869 0.0831 0.0063  -0.0093 0.0049  117 GLU A CG  
1026 C  CD  . GLU A 117 ? 0.0962 0.0750 0.0903 -0.0038 -0.0031 0.0012  117 GLU A CD  
1027 O  OE1 . GLU A 117 ? 0.0979 0.0962 0.0891 0.0080  -0.0049 0.0124  117 GLU A OE1 
1028 O  OE2 . GLU A 117 ? 0.1201 0.0833 0.0855 0.0000  -0.0129 0.0107  117 GLU A OE2 
1029 N  N   . LEU A 118 ? 0.0899 0.0636 0.0778 0.0093  -0.0019 -0.0059 118 LEU A N   
1030 C  CA  . LEU A 118 ? 0.0857 0.0555 0.0636 0.0057  0.0046  0.0010  118 LEU A CA  
1031 C  C   . LEU A 118 ? 0.0820 0.0656 0.0573 0.0051  -0.0142 0.0043  118 LEU A C   
1032 O  O   . LEU A 118 ? 0.0961 0.0648 0.0710 0.0030  0.0003  0.0031  118 LEU A O   
1033 C  CB  . LEU A 118 ? 0.0916 0.0675 0.0916 -0.0107 -0.0023 0.0057  118 LEU A CB  
1034 C  CG  . LEU A 118 ? 0.0840 0.0865 0.0890 0.0076  -0.0099 0.0020  118 LEU A CG  
1035 C  CD1 . LEU A 118 ? 0.1062 0.0724 0.0917 0.0027  -0.0104 0.0087  118 LEU A CD1 
1036 C  CD2 . LEU A 118 ? 0.0917 0.1182 0.1023 0.0057  -0.0216 0.0164  118 LEU A CD2 
1037 N  N   . HIS A 119 ? 0.0732 0.0617 0.0692 0.0040  -0.0049 0.0023  119 HIS A N   
1038 C  CA  . HIS A 119 ? 0.0793 0.0644 0.0731 -0.0024 -0.0054 0.0060  119 HIS A CA  
1039 C  C   . HIS A 119 ? 0.0849 0.0647 0.0706 -0.0052 0.0024  0.0017  119 HIS A C   
1040 O  O   . HIS A 119 ? 0.0928 0.0737 0.0741 0.0052  -0.0024 0.0065  119 HIS A O   
1041 C  CB  . HIS A 119 ? 0.0787 0.0619 0.0891 0.0000  -0.0012 0.0085  119 HIS A CB  
1042 C  CG  . HIS A 119 ? 0.0838 0.0763 0.0671 0.0048  -0.0038 -0.0054 119 HIS A CG  
1043 N  ND1 . HIS A 119 ? 0.0706 0.0715 0.0776 -0.0057 0.0046  0.0024  119 HIS A ND1 
1044 C  CD2 . HIS A 119 ? 0.0847 0.0856 0.0661 0.0126  -0.0046 -0.0013 119 HIS A CD2 
1045 C  CE1 . HIS A 119 ? 0.0981 0.0900 0.0667 -0.0076 -0.0093 -0.0041 119 HIS A CE1 
1046 N  NE2 . HIS A 119 ? 0.0812 0.0864 0.0797 0.0068  -0.0060 0.0060  119 HIS A NE2 
1047 N  N   . LEU A 120 ? 0.0860 0.0619 0.0755 0.0031  -0.0140 -0.0017 120 LEU A N   
1048 C  CA  . LEU A 120 ? 0.0847 0.0570 0.0877 0.0063  -0.0137 0.0012  120 LEU A CA  
1049 C  C   . LEU A 120 ? 0.0829 0.0580 0.0749 0.0037  -0.0177 0.0071  120 LEU A C   
1050 O  O   . LEU A 120 ? 0.0902 0.0702 0.0741 -0.0010 -0.0109 -0.0020 120 LEU A O   
1051 C  CB  . LEU A 120 ? 0.0935 0.0778 0.0947 0.0104  -0.0175 -0.0137 120 LEU A CB  
1052 C  CG  . LEU A 120 ? 0.0837 0.0900 0.0917 -0.0031 -0.0109 -0.0074 120 LEU A CG  
1053 C  CD1 . LEU A 120 ? 0.1987 0.1167 0.1412 -0.0697 -0.0024 -0.0007 120 LEU A CD1 
1054 C  CD2 . LEU A 120 ? 0.1255 0.1177 0.1277 0.0209  -0.0384 -0.0126 120 LEU A CD2 
1055 N  N   . VAL A 121 ? 0.0833 0.0653 0.0925 0.0003  0.0000  0.0010  121 VAL A N   
1056 C  CA  . VAL A 121 ? 0.0970 0.0610 0.0952 -0.0068 -0.0142 0.0031  121 VAL A CA  
1057 C  C   . VAL A 121 ? 0.0837 0.0663 0.0944 -0.0043 -0.0129 0.0041  121 VAL A C   
1058 O  O   . VAL A 121 ? 0.1256 0.0674 0.0998 0.0000  -0.0203 0.0046  121 VAL A O   
1059 C  CB  . VAL A 121 ? 0.0981 0.0709 0.1120 -0.0006 -0.0049 0.0046  121 VAL A CB  
1060 C  CG1 . VAL A 121 ? 0.1005 0.0918 0.1655 -0.0155 -0.0070 0.0015  121 VAL A CG1 
1061 C  CG2 . VAL A 121 ? 0.0953 0.0887 0.1070 0.0046  0.0060  0.0071  121 VAL A CG2 
1062 N  N   . HIS A 122 ? 0.0868 0.0644 0.1049 0.0015  -0.0109 0.0027  122 HIS A N   
1063 C  CA  . HIS A 122 ? 0.1163 0.0522 0.1190 -0.0040 -0.0043 -0.0092 122 HIS A CA  
1064 C  C   . HIS A 122 ? 0.0988 0.0631 0.1102 0.0027  -0.0208 -0.0054 122 HIS A C   
1065 O  O   . HIS A 122 ? 0.1264 0.0819 0.1119 -0.0104 -0.0280 -0.0010 122 HIS A O   
1066 C  CB  . HIS A 122 ? 0.1181 0.0675 0.1095 0.0165  -0.0126 -0.0137 122 HIS A CB  
1067 C  CG  . HIS A 122 ? 0.1110 0.0690 0.0937 0.0085  -0.0126 -0.0115 122 HIS A CG  
1068 N  ND1 . HIS A 122 ? 0.0965 0.0741 0.1112 0.0038  0.0005  -0.0010 122 HIS A ND1 
1069 C  CD2 . HIS A 122 ? 0.0970 0.0934 0.1115 -0.0091 -0.0099 -0.0068 122 HIS A CD2 
1070 C  CE1 . HIS A 122 ? 0.0944 0.0887 0.1120 0.0023  0.0035  -0.0065 122 HIS A CE1 
1071 N  NE2 . HIS A 122 ? 0.1030 0.0996 0.1069 -0.0074 -0.0098 -0.0082 122 HIS A NE2 
1072 N  N   . TRP A 123 ? 0.1067 0.0624 0.0981 0.0060  -0.0228 0.0003  123 TRP A N   
1073 C  CA  . TRP A 123 ? 0.1155 0.0652 0.1041 0.0060  -0.0238 -0.0118 123 TRP A CA  
1074 C  C   . TRP A 123 ? 0.1087 0.0840 0.1212 0.0017  -0.0200 -0.0155 123 TRP A C   
1075 O  O   . TRP A 123 ? 0.1114 0.0787 0.1668 0.0109  -0.0322 -0.0205 123 TRP A O   
1076 C  CB  . TRP A 123 ? 0.1409 0.1111 0.1181 -0.0291 -0.0344 0.0051  123 TRP A CB  
1077 C  CG  . TRP A 123 ? 0.1764 0.0823 0.1216 -0.0408 -0.0421 -0.0013 123 TRP A CG  
1078 C  CD1 . TRP A 123 ? 0.2276 0.0947 0.1208 -0.0388 -0.0436 0.0000  123 TRP A CD1 
1079 C  CD2 . TRP A 123 ? 0.2119 0.0715 0.1459 -0.0296 -0.0504 0.0207  123 TRP A CD2 
1080 N  NE1 . TRP A 123 ? 0.2451 0.0894 0.1456 -0.0306 -0.0573 0.0132  123 TRP A NE1 
1081 C  CE2 . TRP A 123 ? 0.2226 0.0882 0.1423 -0.0241 -0.0458 0.0041  123 TRP A CE2 
1082 C  CE3 . TRP A 123 ? 0.2194 0.0675 0.1562 -0.0436 -0.0485 -0.0049 123 TRP A CE3 
1083 C  CZ2 . TRP A 123 ? 0.2590 0.0909 0.1551 -0.0153 -0.0491 0.0174  123 TRP A CZ2 
1084 C  CZ3 . TRP A 123 ? 0.2707 0.0708 0.1632 -0.0274 -0.0535 0.0137  123 TRP A CZ3 
1085 C  CH2 . TRP A 123 ? 0.2980 0.0907 0.1658 -0.0247 -0.0520 0.0093  123 TRP A CH2 
1086 N  N   . ASN A 124 ? 0.1234 0.0755 0.1342 0.0040  -0.0227 -0.0269 124 ASN A N   
1087 C  CA  . ASN A 124 ? 0.1243 0.0943 0.1475 0.0103  -0.0181 -0.0516 124 ASN A CA  
1088 C  C   . ASN A 124 ? 0.1393 0.0846 0.1510 0.0192  -0.0148 -0.0527 124 ASN A C   
1089 O  O   . ASN A 124 ? 0.1202 0.0952 0.1455 0.0013  -0.0216 -0.0375 124 ASN A O   
1090 C  CB  . ASN A 124 ? 0.1538 0.1033 0.1402 0.0043  -0.0051 -0.0340 124 ASN A CB  
1091 C  CG  . ASN A 124 ? 0.1710 0.1254 0.1581 -0.0087 0.0153  -0.0273 124 ASN A CG  
1092 O  OD1 . ASN A 124 ? 0.1738 0.1263 0.1833 0.0034  0.0159  -0.0557 124 ASN A OD1 
1093 N  ND2 . ASN A 124 ? 0.2109 0.1296 0.1488 -0.0115 0.0140  -0.0469 124 ASN A ND2 
1094 N  N   . THR A 125 ? 0.1351 0.0935 0.1924 0.0308  -0.0238 -0.0586 125 THR A N   
1095 C  CA  . THR A 125 ? 0.1503 0.0982 0.2023 0.0285  -0.0406 -0.0333 125 THR A CA  
1096 C  C   . THR A 125 ? 0.1370 0.0832 0.2117 0.0225  -0.0131 -0.0147 125 THR A C   
1097 O  O   . THR A 125 ? 0.1732 0.1017 0.2280 0.0309  -0.0156 -0.0115 125 THR A O   
1098 C  CB  . THR A 125 ? 0.1702 0.1509 0.2953 0.0148  -0.0731 -0.0285 125 THR A CB  
1099 O  OG1 . THR A 125 ? 0.1547 0.1943 0.3436 0.0557  -0.0306 -0.0555 125 THR A OG1 
1100 C  CG2 . THR A 125 ? 0.1976 0.2045 0.2791 0.0012  -0.0829 -0.0679 125 THR A CG2 
1101 N  N   . LYS A 126 ? 0.1393 0.0946 0.2115 0.0147  0.0046  -0.0399 126 LYS A N   
1102 C  CA  . LYS A 126 ? 0.1913 0.0900 0.2179 0.0010  0.0170  -0.0472 126 LYS A CA  
1103 C  C   . LYS A 126 ? 0.1932 0.0847 0.2004 -0.0063 0.0005  -0.0595 126 LYS A C   
1104 O  O   . LYS A 126 ? 0.2070 0.1181 0.3046 -0.0264 0.0318  -0.1052 126 LYS A O   
1105 C  CB  . LYS A 126 ? 0.2447 0.1664 0.2149 -0.0348 -0.0130 -0.0623 126 LYS A CB  
1106 C  CG  . LYS A 126 ? 0.2578 0.1712 0.2196 -0.0209 -0.0198 -0.0680 126 LYS A CG  
1107 C  CD  . LYS A 126 ? 0.2048 0.3849 0.2926 -0.0262 0.0507  -0.0692 126 LYS A CD  
1108 C  CE  . LYS A 126 ? 0.1538 0.3260 0.4208 0.0102  0.0277  -0.0992 126 LYS A CE  
1109 N  NZ  . LYS A 126 ? 0.6427 0.4859 0.6570 -0.2044 0.1032  -0.3009 126 LYS A NZ  
1110 N  N   . TYR A 127 ? 0.1395 0.0847 0.1427 -0.0031 -0.0043 -0.0263 127 TYR A N   
1111 C  CA  . TYR A 127 ? 0.1335 0.0887 0.1554 -0.0038 -0.0087 -0.0230 127 TYR A CA  
1112 C  C   . TYR A 127 ? 0.1251 0.0825 0.1594 0.0024  -0.0062 -0.0137 127 TYR A C   
1113 O  O   . TYR A 127 ? 0.1468 0.1035 0.1644 -0.0065 -0.0059 -0.0017 127 TYR A O   
1114 C  CB  . TYR A 127 ? 0.1700 0.0830 0.1622 0.0096  -0.0081 -0.0262 127 TYR A CB  
1115 C  CG  . TYR A 127 ? 0.1347 0.1022 0.1626 -0.0024 -0.0185 -0.0197 127 TYR A CG  
1116 C  CD1 . TYR A 127 ? 0.1879 0.1053 0.1703 0.0010  -0.0329 -0.0142 127 TYR A CD1 
1117 C  CD2 . TYR A 127 ? 0.1480 0.0988 0.1472 0.0129  -0.0098 -0.0104 127 TYR A CD2 
1118 C  CE1 . TYR A 127 ? 0.1947 0.1180 0.1519 0.0135  -0.0335 -0.0207 127 TYR A CE1 
1119 C  CE2 . TYR A 127 ? 0.1493 0.1300 0.1396 0.0260  -0.0185 -0.0502 127 TYR A CE2 
1120 C  CZ  . TYR A 127 ? 0.1799 0.1315 0.1287 -0.0006 -0.0024 -0.0196 127 TYR A CZ  
1121 O  OH  . TYR A 127 ? 0.2196 0.1491 0.1368 0.0240  -0.0299 -0.0307 127 TYR A OH  
1122 N  N   . GLY A 128 ? 0.1462 0.0979 0.1729 0.0109  -0.0160 -0.0026 128 GLY A N   
1123 C  CA  . GLY A 128 ? 0.1591 0.1034 0.1669 0.0082  -0.0109 -0.0007 128 GLY A CA  
1124 C  C   . GLY A 128 ? 0.1673 0.1242 0.1288 0.0185  -0.0003 0.0337  128 GLY A C   
1125 O  O   . GLY A 128 ? 0.2154 0.1122 0.1588 0.0132  -0.0401 0.0357  128 GLY A O   
1126 N  N   . ASP A 129 ? 0.1844 0.1208 0.1466 0.0390  -0.0098 -0.0054 129 ASP A N   
1127 C  CA  . ASP A 129 ? 0.2104 0.1208 0.1243 0.0131  -0.0068 0.0115  129 ASP A CA  
1128 C  C   . ASP A 129 ? 0.1985 0.1224 0.1243 0.0326  -0.0208 0.0019  129 ASP A C   
1129 O  O   . ASP A 129 ? 0.2073 0.1216 0.1305 0.0421  -0.0152 -0.0054 129 ASP A O   
1130 C  CB  . ASP A 129 ? 0.1860 0.1202 0.1357 0.0091  -0.0038 0.0092  129 ASP A CB  
1131 C  CG  . ASP A 129 ? 0.1842 0.1376 0.1650 0.0375  -0.0104 -0.0108 129 ASP A CG  
1132 O  OD1 . ASP A 129 ? 0.1969 0.1500 0.3264 0.0241  -0.0425 -0.0132 129 ASP A OD1 
1133 O  OD2 . ASP A 129 ? 0.1999 0.1595 0.1907 0.0582  -0.0065 0.0326  129 ASP A OD2 
1134 N  N   . ALA A 130 ? 0.2109 0.1120 0.1324 0.0166  -0.0020 0.0041  130 ALA A N   
1135 C  CA  . ALA A 130 ? 0.2169 0.1023 0.1157 0.0197  0.0074  -0.0063 130 ALA A CA  
1136 C  C   . ALA A 130 ? 0.2171 0.1128 0.1484 0.0386  0.0057  0.0027  130 ALA A C   
1137 O  O   . ALA A 130 ? 0.2158 0.1075 0.1336 0.0364  -0.0046 -0.0005 130 ALA A O   
1138 C  CB  . ALA A 130 ? 0.2240 0.1220 0.1888 0.0071  -0.0121 -0.0379 130 ALA A CB  
1139 N  N   . GLY A 131 ? 0.2262 0.1259 0.1323 0.0108  0.0137  0.0148  131 GLY A N   
1140 C  CA  . GLY A 131 ? 0.1703 0.2018 0.1489 0.0166  -0.0051 0.0392  131 GLY A CA  
1141 C  C   . GLY A 131 ? 0.1587 0.1588 0.1789 0.0175  0.0274  0.0362  131 GLY A C   
1142 O  O   . GLY A 131 ? 0.1748 0.1730 0.1897 0.0208  0.0295  0.0308  131 GLY A O   
1143 N  N   A LYS A 132 ? 0.1721 0.1280 0.1702 -0.0003 0.0254  0.0296  132 LYS A N   
1144 N  N   B LYS A 132 ? 0.1703 0.1296 0.1624 -0.0019 0.0304  0.0315  132 LYS A N   
1145 C  CA  A LYS A 132 ? 0.1809 0.1206 0.1749 -0.0062 0.0162  0.0274  132 LYS A CA  
1146 C  CA  B LYS A 132 ? 0.1801 0.1173 0.1622 0.0010  0.0198  0.0244  132 LYS A CA  
1147 C  C   A LYS A 132 ? 0.1342 0.1014 0.1704 -0.0093 0.0231  0.0110  132 LYS A C   
1148 C  C   B LYS A 132 ? 0.1344 0.1092 0.1679 -0.0098 0.0162  0.0156  132 LYS A C   
1149 O  O   A LYS A 132 ? 0.1506 0.1415 0.1888 -0.0275 0.0023  0.0261  132 LYS A O   
1150 O  O   B LYS A 132 ? 0.1561 0.1127 0.1702 -0.0163 0.0027  0.0126  132 LYS A O   
1151 C  CB  A LYS A 132 ? 0.1831 0.1141 0.2266 0.0027  0.0551  0.0406  132 LYS A CB  
1152 C  CB  B LYS A 132 ? 0.1292 0.1079 0.1472 -0.0104 -0.0205 0.0026  132 LYS A CB  
1153 C  CG  A LYS A 132 ? 0.1087 0.1807 0.3609 -0.0294 0.0373  0.0560  132 LYS A CG  
1154 C  CG  B LYS A 132 ? 0.2043 0.2363 0.1552 -0.0195 0.0644  0.0318  132 LYS A CG  
1155 C  CD  A LYS A 132 ? 0.4280 0.2569 0.1632 0.0227  0.0680  0.0938  132 LYS A CD  
1156 C  CD  B LYS A 132 ? 0.1870 0.1729 0.2982 -0.0328 -0.0461 0.0847  132 LYS A CD  
1157 C  CE  A LYS A 132 ? 0.1702 0.1737 0.1814 -0.0537 -0.0395 0.0588  132 LYS A CE  
1158 C  CE  B LYS A 132 ? 0.4151 0.2449 0.2840 0.0240  -0.1491 -0.0617 132 LYS A CE  
1159 N  NZ  A LYS A 132 ? 0.2775 0.3555 0.2101 -0.1314 -0.0348 0.0469  132 LYS A NZ  
1160 N  NZ  B LYS A 132 ? 0.3046 0.2935 0.5108 -0.0662 -0.2621 0.1615  132 LYS A NZ  
1161 N  N   . ALA A 133 ? 0.1448 0.0971 0.1195 -0.0024 0.0104  0.0010  133 ALA A N   
1162 C  CA  . ALA A 133 ? 0.1419 0.0979 0.1181 -0.0115 -0.0208 0.0054  133 ALA A CA  
1163 C  C   . ALA A 133 ? 0.1455 0.0952 0.1097 -0.0031 0.0216  0.0043  133 ALA A C   
1164 O  O   . ALA A 133 ? 0.1360 0.1233 0.1233 -0.0043 0.0038  0.0153  133 ALA A O   
1165 C  CB  . ALA A 133 ? 0.1198 0.1217 0.1087 -0.0153 -0.0003 -0.0065 133 ALA A CB  
1166 N  N   . SER A 134 ? 0.1626 0.1155 0.1140 0.0137  0.0082  0.0076  134 SER A N   
1167 C  CA  . SER A 134 ? 0.1677 0.1225 0.1274 0.0368  0.0043  0.0254  134 SER A CA  
1168 C  C   . SER A 134 ? 0.1388 0.1360 0.1518 0.0052  0.0167  0.0502  134 SER A C   
1169 O  O   . SER A 134 ? 0.1562 0.1492 0.1579 0.0194  0.0209  0.0443  134 SER A O   
1170 C  CB  . SER A 134 ? 0.2522 0.1533 0.1498 0.0450  0.0366  0.0121  134 SER A CB  
1171 O  OG  . SER A 134 ? 0.2312 0.2174 0.1981 0.0777  0.0498  0.0370  134 SER A OG  
1172 N  N   . GLN A 135 ? 0.1483 0.1454 0.1216 0.0054  0.0195  0.0280  135 GLN A N   
1173 C  CA  . GLN A 135 ? 0.1419 0.1421 0.1743 -0.0207 -0.0170 0.0159  135 GLN A CA  
1174 C  C   . GLN A 135 ? 0.1268 0.1484 0.1709 0.0020  -0.0081 -0.0031 135 GLN A C   
1175 O  O   . GLN A 135 ? 0.1595 0.2102 0.2138 -0.0351 -0.0306 0.0092  135 GLN A O   
1176 C  CB  . GLN A 135 ? 0.1704 0.2239 0.2718 -0.0944 0.0043  0.0351  135 GLN A CB  
1177 C  CG  . GLN A 135 ? 0.2334 0.2666 0.2802 -0.0825 0.0829  0.0829  135 GLN A CG  
1178 C  CD  . GLN A 135 ? 0.2748 0.4673 0.5684 -0.0926 0.2178  0.0496  135 GLN A CD  
1179 O  OE1 . GLN A 135 ? 0.3914 0.7325 0.8202 0.1295  0.1075  -0.0891 135 GLN A OE1 
1180 N  NE2 . GLN A 135 ? 0.7293 0.2851 0.6128 -0.1712 0.0992  0.0806  135 GLN A NE2 
1181 N  N   . GLN A 136 ? 0.1202 0.1206 0.1483 -0.0020 0.0006  0.0073  136 GLN A N   
1182 C  CA  . GLN A 136 ? 0.1254 0.1052 0.1325 -0.0142 -0.0198 -0.0130 136 GLN A CA  
1183 C  C   . GLN A 136 ? 0.1421 0.1189 0.1070 0.0074  -0.0035 -0.0142 136 GLN A C   
1184 O  O   . GLN A 136 ? 0.1485 0.1137 0.1087 0.0026  -0.0020 -0.0088 136 GLN A O   
1185 C  CB  . GLN A 136 ? 0.1826 0.1277 0.1509 0.0081  -0.0362 -0.0206 136 GLN A CB  
1186 C  CG  . GLN A 136 ? 0.2049 0.1439 0.1806 0.0024  -0.0091 0.0198  136 GLN A CG  
1187 C  CD  . GLN A 136 ? 0.1985 0.1717 0.2375 0.0013  0.0292  0.0636  136 GLN A CD  
1188 O  OE1 . GLN A 136 ? 0.2556 0.1429 0.2761 -0.0038 -0.0142 -0.0610 136 GLN A OE1 
1189 N  NE2 . GLN A 136 ? 0.2967 0.2806 0.3819 -0.0377 0.0724  0.1439  136 GLN A NE2 
1190 N  N   . PRO A 137 ? 0.1224 0.1527 0.1111 -0.0015 -0.0104 -0.0178 137 PRO A N   
1191 C  CA  . PRO A 137 ? 0.1712 0.1641 0.0981 0.0049  -0.0068 0.0043  137 PRO A CA  
1192 C  C   . PRO A 137 ? 0.1685 0.1669 0.1032 0.0076  0.0017  -0.0006 137 PRO A C   
1193 O  O   . PRO A 137 ? 0.1797 0.1588 0.2332 0.0153  -0.0019 0.0549  137 PRO A O   
1194 C  CB  . PRO A 137 ? 0.2050 0.2411 0.1212 -0.0177 -0.0231 -0.0020 137 PRO A CB  
1195 C  CG  . PRO A 137 ? 0.4140 0.3682 0.0987 -0.1049 -0.0229 -0.0438 137 PRO A CG  
1196 C  CD  . PRO A 137 ? 0.1562 0.2169 0.1101 -0.0208 -0.0065 -0.0640 137 PRO A CD  
1197 N  N   . ASP A 138 ? 0.1476 0.1325 0.1005 -0.0013 0.0062  -0.0071 138 ASP A N   
1198 C  CA  . ASP A 138 ? 0.1412 0.1517 0.1155 0.0020  -0.0020 -0.0151 138 ASP A CA  
1199 C  C   . ASP A 138 ? 0.1093 0.1402 0.1243 -0.0088 0.0051  -0.0199 138 ASP A C   
1200 O  O   . ASP A 138 ? 0.1333 0.1437 0.1455 0.0063  -0.0046 -0.0166 138 ASP A O   
1201 C  CB  . ASP A 138 ? 0.1490 0.1915 0.1272 0.0037  0.0164  -0.0208 138 ASP A CB  
1202 C  CG  . ASP A 138 ? 0.1572 0.1789 0.1738 0.0031  -0.0120 -0.0194 138 ASP A CG  
1203 O  OD1 . ASP A 138 ? 0.2059 0.1445 0.1563 0.0125  -0.0120 -0.0383 138 ASP A OD1 
1204 O  OD2 . ASP A 138 ? 0.2145 0.2653 0.2133 0.0553  0.0057  -0.0710 138 ASP A OD2 
1205 N  N   . GLY A 139 ? 0.1102 0.0919 0.0875 -0.0065 -0.0027 -0.0217 139 GLY A N   
1206 C  CA  . GLY A 139 ? 0.1439 0.0935 0.0886 -0.0049 -0.0137 -0.0137 139 GLY A CA  
1207 C  C   . GLY A 139 ? 0.1014 0.0741 0.1074 0.0027  -0.0088 -0.0046 139 GLY A C   
1208 O  O   . GLY A 139 ? 0.1150 0.0746 0.0996 0.0082  -0.0126 -0.0104 139 GLY A O   
1209 N  N   . LEU A 140 ? 0.0974 0.0803 0.0883 0.0027  0.0000  -0.0026 140 LEU A N   
1210 C  CA  . LEU A 140 ? 0.0989 0.0728 0.0918 -0.0035 -0.0076 -0.0031 140 LEU A CA  
1211 C  C   . LEU A 140 ? 0.0974 0.0744 0.0917 0.0051  -0.0065 -0.0041 140 LEU A C   
1212 O  O   . LEU A 140 ? 0.0946 0.0834 0.1032 -0.0006 -0.0118 -0.0062 140 LEU A O   
1213 C  CB  . LEU A 140 ? 0.0952 0.0947 0.1040 0.0092  -0.0120 -0.0098 140 LEU A CB  
1214 C  CG  . LEU A 140 ? 0.1579 0.0965 0.1518 0.0148  0.0337  0.0143  140 LEU A CG  
1215 C  CD1 . LEU A 140 ? 0.1679 0.1095 0.1524 0.0395  0.0344  0.0063  140 LEU A CD1 
1216 C  CD2 . LEU A 140 ? 0.1932 0.1254 0.1456 0.0120  0.0104  0.0098  140 LEU A CD2 
1217 N  N   . ALA A 141 ? 0.0956 0.0697 0.1051 -0.0013 -0.0126 -0.0164 141 ALA A N   
1218 C  CA  . ALA A 141 ? 0.1007 0.0776 0.1001 -0.0073 -0.0015 -0.0088 141 ALA A CA  
1219 C  C   . ALA A 141 ? 0.0892 0.0691 0.1032 -0.0115 -0.0099 0.0000  141 ALA A C   
1220 O  O   . ALA A 141 ? 0.1155 0.0690 0.1022 -0.0026 -0.0238 0.0015  141 ALA A O   
1221 C  CB  . ALA A 141 ? 0.1097 0.1076 0.1192 -0.0186 0.0049  -0.0076 141 ALA A CB  
1222 N  N   . VAL A 142 ? 0.0935 0.0717 0.0732 -0.0027 -0.0054 -0.0068 142 VAL A N   
1223 C  CA  . VAL A 142 ? 0.0935 0.0731 0.0737 -0.0023 -0.0085 0.0020  142 VAL A CA  
1224 C  C   . VAL A 142 ? 0.0891 0.0546 0.0718 0.0027  0.0015  -0.0041 142 VAL A C   
1225 O  O   . VAL A 142 ? 0.0935 0.0847 0.0838 0.0006  -0.0046 0.0051  142 VAL A O   
1226 C  CB  . VAL A 142 ? 0.0838 0.0876 0.0850 0.0041  0.0020  -0.0070 142 VAL A CB  
1227 C  CG1 . VAL A 142 ? 0.1098 0.1062 0.0785 0.0189  -0.0052 -0.0071 142 VAL A CG1 
1228 C  CG2 . VAL A 142 ? 0.1128 0.1104 0.0878 -0.0065 -0.0038 0.0082  142 VAL A CG2 
1229 N  N   . LEU A 143 ? 0.0930 0.0653 0.0856 -0.0052 -0.0057 -0.0074 143 LEU A N   
1230 C  CA  . LEU A 143 ? 0.0820 0.0696 0.0893 -0.0010 -0.0104 -0.0091 143 LEU A CA  
1231 C  C   . LEU A 143 ? 0.0908 0.0653 0.0687 -0.0076 -0.0006 0.0027  143 LEU A C   
1232 O  O   . LEU A 143 ? 0.1084 0.0698 0.0810 0.0006  0.0038  0.0006  143 LEU A O   
1233 C  CB  . LEU A 143 ? 0.0979 0.0921 0.1069 -0.0068 -0.0087 0.0000  143 LEU A CB  
1234 C  CG  . LEU A 143 ? 0.0952 0.1142 0.1235 -0.0051 -0.0038 0.0027  143 LEU A CG  
1235 C  CD1 . LEU A 143 ? 0.1061 0.1808 0.1361 -0.0120 -0.0125 0.0458  143 LEU A CD1 
1236 C  CD2 . LEU A 143 ? 0.0961 0.1615 0.1524 0.0098  -0.0170 0.0000  143 LEU A CD2 
1237 N  N   . GLY A 144 ? 0.0838 0.0649 0.0891 -0.0068 0.0013  -0.0034 144 GLY A N   
1238 C  CA  . GLY A 144 ? 0.0884 0.0724 0.0893 -0.0057 -0.0051 -0.0020 144 GLY A CA  
1239 C  C   . GLY A 144 ? 0.0910 0.0768 0.0655 0.0006  0.0024  0.0060  144 GLY A C   
1240 O  O   . GLY A 144 ? 0.1041 0.0778 0.0819 -0.0110 0.0186  -0.0037 144 GLY A O   
1241 N  N   . ILE A 145 ? 0.0771 0.0698 0.0679 0.0068  0.0054  -0.0035 145 ILE A N   
1242 C  CA  . ILE A 145 ? 0.0916 0.0681 0.0829 0.0031  -0.0109 0.0006  145 ILE A CA  
1243 C  C   . ILE A 145 ? 0.0820 0.0626 0.0744 -0.0031 -0.0098 0.0000  145 ILE A C   
1244 O  O   . ILE A 145 ? 0.0891 0.0723 0.0903 -0.0040 0.0051  0.0000  145 ILE A O   
1245 C  CB  . ILE A 145 ? 0.0917 0.0797 0.0955 0.0057  -0.0124 0.0023  145 ILE A CB  
1246 C  CG1 . ILE A 145 ? 0.0979 0.0928 0.1428 0.0288  -0.0115 0.0013  145 ILE A CG1 
1247 C  CG2 . ILE A 145 ? 0.0873 0.0947 0.1542 -0.0035 -0.0093 -0.0003 145 ILE A CG2 
1248 C  CD1 . ILE A 145 ? 0.1102 0.1000 0.1387 0.0153  -0.0216 0.0161  145 ILE A CD1 
1249 N  N   . PHE A 146 ? 0.0776 0.0593 0.0882 -0.0027 -0.0115 0.0035  146 PHE A N   
1250 C  CA  . PHE A 146 ? 0.0812 0.0680 0.0898 0.0104  -0.0038 0.0071  146 PHE A CA  
1251 C  C   . PHE A 146 ? 0.0874 0.0657 0.1035 0.0020  -0.0010 -0.0071 146 PHE A C   
1252 O  O   . PHE A 146 ? 0.0917 0.0892 0.1005 0.0041  -0.0087 -0.0043 146 PHE A O   
1253 C  CB  . PHE A 146 ? 0.1086 0.0719 0.0780 -0.0013 0.0000  0.0038  146 PHE A CB  
1254 C  CG  . PHE A 146 ? 0.0798 0.0636 0.0878 0.0015  -0.0037 -0.0006 146 PHE A CG  
1255 C  CD1 . PHE A 146 ? 0.0979 0.0802 0.0856 0.0087  -0.0065 -0.0020 146 PHE A CD1 
1256 C  CD2 . PHE A 146 ? 0.1194 0.0652 0.0987 0.0012  -0.0118 0.0114  146 PHE A CD2 
1257 C  CE1 . PHE A 146 ? 0.1093 0.0832 0.0988 0.0098  -0.0229 0.0015  146 PHE A CE1 
1258 C  CE2 . PHE A 146 ? 0.1200 0.0788 0.0962 0.0035  0.0071  0.0115  146 PHE A CE2 
1259 C  CZ  . PHE A 146 ? 0.1061 0.0869 0.0946 0.0024  -0.0026 0.0087  146 PHE A CZ  
1260 N  N   . LEU A 147 ? 0.0947 0.0728 0.0920 0.0006  0.0006  -0.0024 147 LEU A N   
1261 C  CA  . LEU A 147 ? 0.1040 0.0634 0.0960 -0.0024 -0.0076 -0.0046 147 LEU A CA  
1262 C  C   . LEU A 147 ? 0.0975 0.0706 0.0925 0.0000  0.0049  -0.0076 147 LEU A C   
1263 O  O   . LEU A 147 ? 0.1015 0.0699 0.1230 0.0093  -0.0015 0.0000  147 LEU A O   
1264 C  CB  . LEU A 147 ? 0.1058 0.0777 0.0875 -0.0007 0.0006  -0.0060 147 LEU A CB  
1265 C  CG  . LEU A 147 ? 0.1316 0.0683 0.1076 -0.0193 -0.0186 -0.0030 147 LEU A CG  
1266 C  CD1 . LEU A 147 ? 0.1624 0.0766 0.0996 0.0024  -0.0298 0.0019  147 LEU A CD1 
1267 C  CD2 . LEU A 147 ? 0.1303 0.0872 0.1008 -0.0131 -0.0088 0.0076  147 LEU A CD2 
1268 N  N   . LYS A 148 ? 0.1167 0.0707 0.1113 -0.0164 0.0027  -0.0024 148 LYS A N   
1269 C  CA  . LYS A 148 ? 0.1206 0.0802 0.1219 -0.0020 -0.0115 0.0093  148 LYS A CA  
1270 C  C   . LYS A 148 ? 0.1281 0.0785 0.1307 0.0153  -0.0215 0.0035  148 LYS A C   
1271 O  O   . LYS A 148 ? 0.1453 0.0974 0.1333 0.0250  -0.0236 -0.0093 148 LYS A O   
1272 C  CB  . LYS A 148 ? 0.1394 0.1115 0.1483 -0.0215 -0.0077 0.0239  148 LYS A CB  
1273 C  CG  . LYS A 148 ? 0.1615 0.1366 0.1536 -0.0195 0.0015  0.0142  148 LYS A CG  
1274 C  CD  . LYS A 148 ? 0.2151 0.2170 0.2109 -0.0220 0.0175  0.0737  148 LYS A CD  
1275 C  CE  . LYS A 148 ? 0.2648 0.4553 0.3431 -0.0759 0.0850  0.1358  148 LYS A CE  
1276 N  NZ  . LYS A 148 ? 0.4447 0.6284 0.5873 -0.0401 0.2675  0.2890  148 LYS A NZ  
1277 N  N   . VAL A 149 ? 0.1465 0.0750 0.1476 0.0174  -0.0465 -0.0107 149 VAL A N   
1278 C  CA  . VAL A 149 ? 0.1405 0.0891 0.1418 0.0098  -0.0381 -0.0132 149 VAL A CA  
1279 C  C   . VAL A 149 ? 0.1694 0.0821 0.1552 -0.0017 -0.0406 -0.0074 149 VAL A C   
1280 O  O   . VAL A 149 ? 0.1826 0.0917 0.1950 -0.0019 -0.0441 0.0010  149 VAL A O   
1281 C  CB  . VAL A 149 ? 0.1448 0.1101 0.1387 0.0137  -0.0208 -0.0076 149 VAL A CB  
1282 C  CG1 . VAL A 149 ? 0.1808 0.1483 0.1608 0.0146  -0.0251 -0.0148 149 VAL A CG1 
1283 C  CG2 . VAL A 149 ? 0.1528 0.1483 0.2185 -0.0137 -0.0368 0.0060  149 VAL A CG2 
1284 N  N   . GLY A 150 ? 0.1445 0.0988 0.1625 -0.0124 -0.0346 -0.0087 150 GLY A N   
1285 C  CA  . GLY A 150 ? 0.1772 0.1411 0.1616 -0.0317 -0.0627 0.0132  150 GLY A CA  
1286 C  C   . GLY A 150 ? 0.1446 0.1138 0.1419 -0.0361 -0.0195 -0.0043 150 GLY A C   
1287 O  O   . GLY A 150 ? 0.1404 0.1093 0.1503 -0.0109 -0.0227 0.0038  150 GLY A O   
1288 N  N   A SER A 151 ? 0.1670 0.1122 0.1527 -0.0333 -0.0080 -0.0109 151 SER A N   
1289 N  N   B SER A 151 ? 0.1722 0.1288 0.1418 -0.0175 -0.0263 -0.0096 151 SER A N   
1290 C  CA  A SER A 151 ? 0.1571 0.1224 0.1799 -0.0370 -0.0258 -0.0068 151 SER A CA  
1291 C  CA  B SER A 151 ? 0.1536 0.1427 0.2002 -0.0076 -0.0397 0.0241  151 SER A CA  
1292 C  C   A SER A 151 ? 0.1252 0.0996 0.1498 -0.0184 -0.0114 -0.0228 151 SER A C   
1293 C  C   B SER A 151 ? 0.1456 0.0982 0.1387 -0.0041 -0.0194 -0.0320 151 SER A C   
1294 O  O   A SER A 151 ? 0.1085 0.1208 0.1171 -0.0109 -0.0171 -0.0120 151 SER A O   
1295 O  O   B SER A 151 ? 0.0962 0.1167 0.1261 -0.0153 0.0048  -0.0196 151 SER A O   
1296 C  CB  A SER A 151 ? 0.1753 0.1683 0.2081 -0.0456 0.0031  -0.0390 151 SER A CB  
1297 C  CB  B SER A 151 ? 0.1710 0.1780 0.2653 -0.0483 0.0027  -0.0644 151 SER A CB  
1298 O  OG  A SER A 151 ? 0.1272 0.2320 0.3531 -0.0494 -0.0054 0.0776  151 SER A OG  
1299 O  OG  B SER A 151 ? 0.2201 0.3041 0.2124 -0.0344 0.0186  -0.0612 151 SER A OG  
1300 N  N   . ALA A 152 ? 0.1547 0.0988 0.1561 -0.0031 -0.0403 -0.0269 152 ALA A N   
1301 C  CA  . ALA A 152 ? 0.1597 0.0979 0.1543 0.0013  -0.0313 -0.0129 152 ALA A CA  
1302 C  C   . ALA A 152 ? 0.1263 0.0939 0.1561 0.0000  -0.0272 -0.0017 152 ALA A C   
1303 O  O   . ALA A 152 ? 0.1404 0.1234 0.1685 -0.0054 -0.0070 -0.0151 152 ALA A O   
1304 C  CB  . ALA A 152 ? 0.1925 0.1422 0.1351 0.0086  -0.0386 -0.0242 152 ALA A CB  
1305 N  N   . LYS A 153 ? 0.1250 0.0891 0.1290 0.0068  -0.0299 -0.0027 153 LYS A N   
1306 C  CA  . LYS A 153 ? 0.1133 0.0942 0.1341 0.0013  -0.0098 0.0065  153 LYS A CA  
1307 C  C   . LYS A 153 ? 0.1177 0.0920 0.1414 0.0109  -0.0193 -0.0060 153 LYS A C   
1308 O  O   . LYS A 153 ? 0.1052 0.1068 0.1263 0.0164  -0.0189 -0.0049 153 LYS A O   
1309 C  CB  . LYS A 153 ? 0.1333 0.0925 0.1404 0.0023  -0.0333 -0.0049 153 LYS A CB  
1310 C  CG  . LYS A 153 ? 0.1675 0.1084 0.1620 0.0142  -0.0197 -0.0062 153 LYS A CG  
1311 C  CD  . LYS A 153 ? 0.1973 0.1277 0.1234 0.0038  0.0092  -0.0163 153 LYS A CD  
1312 C  CE  . LYS A 153 ? 0.2628 0.1482 0.2248 0.0498  0.0041  -0.0436 153 LYS A CE  
1313 N  NZ  . LYS A 153 ? 0.4936 0.1993 0.2323 0.0040  0.1835  -0.0241 153 LYS A NZ  
1314 N  N   . PRO A 154 ? 0.1084 0.1208 0.1291 0.0092  -0.0159 -0.0074 154 PRO A N   
1315 C  CA  . PRO A 154 ? 0.1076 0.1404 0.1456 0.0000  -0.0200 -0.0003 154 PRO A CA  
1316 C  C   . PRO A 154 ? 0.1049 0.1570 0.1229 0.0337  -0.0166 0.0296  154 PRO A C   
1317 O  O   . PRO A 154 ? 0.1234 0.1630 0.1334 0.0285  -0.0082 0.0210  154 PRO A O   
1318 C  CB  . PRO A 154 ? 0.1045 0.1827 0.1771 0.0126  -0.0076 0.0307  154 PRO A CB  
1319 C  CG  . PRO A 154 ? 0.1569 0.2018 0.1999 0.0115  -0.0366 0.0218  154 PRO A CG  
1320 C  CD  . PRO A 154 ? 0.1154 0.1543 0.1608 0.0175  0.0000  0.0193  154 PRO A CD  
1321 N  N   . GLY A 155 ? 0.1165 0.1168 0.1538 0.0156  -0.0082 0.0087  155 GLY A N   
1322 C  CA  . GLY A 155 ? 0.1307 0.1206 0.1949 0.0160  0.0043  0.0175  155 GLY A CA  
1323 C  C   . GLY A 155 ? 0.1400 0.1024 0.1463 0.0104  0.0071  0.0151  155 GLY A C   
1324 O  O   . GLY A 155 ? 0.1506 0.1049 0.2027 0.0274  0.0142  0.0233  155 GLY A O   
1325 N  N   . LEU A 156 ? 0.0997 0.0973 0.1283 0.0086  -0.0086 -0.0015 156 LEU A N   
1326 C  CA  . LEU A 156 ? 0.1059 0.1124 0.1256 -0.0049 -0.0098 0.0020  156 LEU A CA  
1327 C  C   . LEU A 156 ? 0.0988 0.0962 0.1336 0.0120  -0.0170 0.0063  156 LEU A C   
1328 O  O   . LEU A 156 ? 0.1016 0.1095 0.1128 -0.0019 -0.0126 -0.0046 156 LEU A O   
1329 C  CB  . LEU A 156 ? 0.1296 0.1151 0.1162 0.0172  -0.0161 0.0023  156 LEU A CB  
1330 C  CG  . LEU A 156 ? 0.1165 0.1245 0.1233 -0.0062 -0.0299 -0.0003 156 LEU A CG  
1331 C  CD1 . LEU A 156 ? 0.1342 0.1237 0.1324 -0.0251 -0.0209 0.0070  156 LEU A CD1 
1332 C  CD2 . LEU A 156 ? 0.1318 0.1454 0.1315 0.0153  -0.0228 0.0068  156 LEU A CD2 
1333 N  N   . GLN A 157 ? 0.1042 0.0961 0.1159 -0.0081 -0.0076 -0.0012 157 GLN A N   
1334 C  CA  . GLN A 157 ? 0.1128 0.1163 0.1049 -0.0153 -0.0136 -0.0003 157 GLN A CA  
1335 C  C   . GLN A 157 ? 0.1023 0.1146 0.1019 -0.0054 -0.0126 -0.0052 157 GLN A C   
1336 O  O   . GLN A 157 ? 0.1034 0.1159 0.1190 -0.0143 -0.0104 -0.0121 157 GLN A O   
1337 C  CB  . GLN A 157 ? 0.1101 0.1347 0.1342 -0.0131 -0.0283 -0.0086 157 GLN A CB  
1338 C  CG  . GLN A 157 ? 0.1404 0.1225 0.1271 -0.0110 -0.0320 -0.0263 157 GLN A CG  
1339 C  CD  . GLN A 157 ? 0.1347 0.1176 0.1208 -0.0010 -0.0273 -0.0043 157 GLN A CD  
1340 O  OE1 . GLN A 157 ? 0.1743 0.1156 0.1058 -0.0093 0.0048  -0.0119 157 GLN A OE1 
1341 N  NE2 . GLN A 157 ? 0.1817 0.1553 0.1334 -0.0351 0.0007  -0.0270 157 GLN A NE2 
1342 N  N   . LYS A 158 ? 0.1049 0.1149 0.1138 0.0131  -0.0185 0.0046  158 LYS A N   
1343 C  CA  . LYS A 158 ? 0.1156 0.1167 0.1245 0.0103  -0.0333 0.0065  158 LYS A CA  
1344 C  C   . LYS A 158 ? 0.1509 0.0874 0.1314 -0.0026 -0.0222 0.0026  158 LYS A C   
1345 O  O   . LYS A 158 ? 0.1524 0.1280 0.1324 -0.0184 -0.0351 0.0162  158 LYS A O   
1346 C  CB  . LYS A 158 ? 0.1591 0.1476 0.1380 0.0335  -0.0274 0.0195  158 LYS A CB  
1347 C  CG  . LYS A 158 ? 0.2102 0.1842 0.2174 0.0293  -0.0346 0.0035  158 LYS A CG  
1348 C  CD  . LYS A 158 ? 0.3217 0.2303 0.2156 0.1221  -0.0489 0.0093  158 LYS A CD  
1349 C  CE  . LYS A 158 ? 0.3941 0.2915 0.3528 0.0357  -0.1058 0.0947  158 LYS A CE  
1350 N  NZ  . LYS A 158 ? 0.2372 0.2531 0.2903 0.0706  0.0171  0.0838  158 LYS A NZ  
1351 N  N   . VAL A 159 ? 0.1120 0.0926 0.1234 0.0104  -0.0252 -0.0062 159 VAL A N   
1352 C  CA  . VAL A 159 ? 0.1206 0.0912 0.1330 -0.0162 -0.0154 -0.0096 159 VAL A CA  
1353 C  C   . VAL A 159 ? 0.0954 0.0882 0.1086 -0.0023 -0.0166 0.0000  159 VAL A C   
1354 O  O   . VAL A 159 ? 0.1228 0.0944 0.1262 -0.0124 -0.0137 0.0010  159 VAL A O   
1355 C  CB  . VAL A 159 ? 0.1336 0.0951 0.1269 0.0020  -0.0247 -0.0098 159 VAL A CB  
1356 C  CG1 . VAL A 159 ? 0.1224 0.1455 0.1421 -0.0233 -0.0318 -0.0013 159 VAL A CG1 
1357 C  CG2 . VAL A 159 ? 0.2221 0.1272 0.1424 0.0333  -0.0507 -0.0271 159 VAL A CG2 
1358 N  N   . VAL A 160 ? 0.1137 0.0796 0.1060 -0.0010 -0.0092 0.0019  160 VAL A N   
1359 C  CA  . VAL A 160 ? 0.1405 0.0820 0.1272 -0.0020 0.0000  0.0054  160 VAL A CA  
1360 C  C   . VAL A 160 ? 0.1195 0.0714 0.1215 -0.0052 0.0015  -0.0020 160 VAL A C   
1361 O  O   . VAL A 160 ? 0.1195 0.1124 0.1273 -0.0082 0.0065  -0.0017 160 VAL A O   
1362 C  CB  . VAL A 160 ? 0.1975 0.1111 0.1577 0.0082  0.0171  0.0020  160 VAL A CB  
1363 C  CG1 . VAL A 160 ? 0.2973 0.1612 0.1444 0.0441  0.0381  0.0392  160 VAL A CG1 
1364 C  CG2 . VAL A 160 ? 0.1509 0.1824 0.1843 0.0441  -0.0120 -0.0295 160 VAL A CG2 
1365 N  N   . ASP A 161 ? 0.1265 0.1023 0.1190 -0.0251 -0.0155 -0.0013 161 ASP A N   
1366 C  CA  . ASP A 161 ? 0.1084 0.1375 0.1199 -0.0248 -0.0102 -0.0076 161 ASP A CA  
1367 C  C   . ASP A 161 ? 0.1189 0.1439 0.1418 -0.0274 0.0109  -0.0059 161 ASP A C   
1368 O  O   . ASP A 161 ? 0.1739 0.1895 0.1394 -0.0538 0.0225  -0.0048 161 ASP A O   
1369 C  CB  . ASP A 161 ? 0.1242 0.1658 0.1368 -0.0397 -0.0186 0.0052  161 ASP A CB  
1370 C  CG  . ASP A 161 ? 0.1280 0.1512 0.1527 -0.0054 -0.0073 -0.0219 161 ASP A CG  
1371 O  OD1 . ASP A 161 ? 0.1606 0.1587 0.1775 -0.0353 -0.0010 -0.0104 161 ASP A OD1 
1372 O  OD2 . ASP A 161 ? 0.1536 0.1931 0.1643 -0.0326 -0.0107 -0.0197 161 ASP A OD2 
1373 N  N   A VAL A 162 ? 0.0960 0.1386 0.1115 -0.0252 -0.0242 0.0088  162 VAL A N   
1374 N  N   B VAL A 162 ? 0.0974 0.1238 0.1172 -0.0214 -0.0177 0.0043  162 VAL A N   
1375 C  CA  A VAL A 162 ? 0.1280 0.1263 0.0883 -0.0241 -0.0068 0.0038  162 VAL A CA  
1376 C  CA  B VAL A 162 ? 0.1088 0.0909 0.1300 0.0005  0.0119  -0.0015 162 VAL A CA  
1377 C  C   A VAL A 162 ? 0.1095 0.1200 0.1190 -0.0485 -0.0087 0.0147  162 VAL A C   
1378 C  C   B VAL A 162 ? 0.1137 0.1403 0.0908 -0.0227 -0.0038 0.0142  162 VAL A C   
1379 O  O   A VAL A 162 ? 0.1237 0.1067 0.1111 -0.0135 0.0186  0.0060  162 VAL A O   
1380 O  O   B VAL A 162 ? 0.1036 0.1199 0.1171 -0.0031 -0.0003 -0.0027 162 VAL A O   
1381 C  CB  A VAL A 162 ? 0.1332 0.1325 0.1324 -0.0068 -0.0027 -0.0162 162 VAL A CB  
1382 C  CB  B VAL A 162 ? 0.1105 0.1131 0.1040 0.0197  0.0080  0.0104  162 VAL A CB  
1383 C  CG1 A VAL A 162 ? 0.1870 0.1318 0.1238 -0.0174 -0.0199 -0.0087 162 VAL A CG1 
1384 C  CG1 B VAL A 162 ? 0.1121 0.1334 0.2092 -0.0071 -0.0020 0.0326  162 VAL A CG1 
1385 C  CG2 A VAL A 162 ? 0.2198 0.1450 0.1976 -0.0333 -0.0520 0.0219  162 VAL A CG2 
1386 C  CG2 B VAL A 162 ? 0.1348 0.0900 0.1243 -0.0098 0.0059  0.0076  162 VAL A CG2 
1387 N  N   . LEU A 163 ? 0.1150 0.1216 0.1129 -0.0219 -0.0017 0.0107  163 LEU A N   
1388 C  CA  . LEU A 163 ? 0.1233 0.1138 0.1031 -0.0148 -0.0015 -0.0038 163 LEU A CA  
1389 C  C   . LEU A 163 ? 0.1052 0.1221 0.1128 -0.0104 0.0010  0.0035  163 LEU A C   
1390 O  O   . LEU A 163 ? 0.1272 0.1344 0.1130 -0.0155 0.0109  0.0010  163 LEU A O   
1391 C  CB  . LEU A 163 ? 0.1180 0.1250 0.1001 -0.0113 -0.0051 0.0110  163 LEU A CB  
1392 C  CG  . LEU A 163 ? 0.1165 0.1177 0.0962 0.0017  0.0006  0.0074  163 LEU A CG  
1393 C  CD1 . LEU A 163 ? 0.1137 0.1186 0.1406 0.0038  0.0153  0.0331  163 LEU A CD1 
1394 C  CD2 . LEU A 163 ? 0.1280 0.1394 0.1190 -0.0082 -0.0175 0.0071  163 LEU A CD2 
1395 N  N   . ASP A 164 ? 0.1535 0.1327 0.1077 -0.0335 0.0046  -0.0098 164 ASP A N   
1396 C  CA  . ASP A 164 ? 0.1779 0.1612 0.1351 -0.0491 0.0120  -0.0285 164 ASP A CA  
1397 C  C   . ASP A 164 ? 0.1511 0.1723 0.1149 -0.0261 0.0076  0.0015  164 ASP A C   
1398 O  O   . ASP A 164 ? 0.1934 0.2118 0.1544 -0.0357 0.0533  -0.0107 164 ASP A O   
1399 C  CB  . ASP A 164 ? 0.2165 0.1537 0.1520 -0.0296 0.0164  -0.0331 164 ASP A CB  
1400 C  CG  . ASP A 164 ? 0.2043 0.2651 0.2097 -0.0608 0.0063  -0.0419 164 ASP A CG  
1401 O  OD1 . ASP A 164 ? 0.2156 0.2899 0.2101 -0.0566 -0.0052 -0.0195 164 ASP A OD1 
1402 O  OD2 . ASP A 164 ? 0.3251 0.4388 0.1835 -0.0754 0.0208  -0.0346 164 ASP A OD2 
1403 N  N   . SER A 165 ? 0.1631 0.1600 0.1130 -0.0252 -0.0174 0.0142  165 SER A N   
1404 C  CA  . SER A 165 ? 0.1393 0.1730 0.1387 -0.0351 0.0000  0.0243  165 SER A CA  
1405 C  C   . SER A 165 ? 0.1532 0.1368 0.1192 -0.0197 -0.0027 0.0000  165 SER A C   
1406 O  O   . SER A 165 ? 0.1606 0.1621 0.1246 -0.0303 -0.0017 0.0366  165 SER A O   
1407 C  CB  . SER A 165 ? 0.1544 0.2169 0.1173 0.0000  -0.0073 0.0077  165 SER A CB  
1408 O  OG  . SER A 165 ? 0.1536 0.1682 0.1700 -0.0120 0.0017  0.0287  165 SER A OG  
1409 N  N   . ILE A 166 ? 0.1272 0.1324 0.1112 -0.0227 -0.0113 0.0164  166 ILE A N   
1410 C  CA  . ILE A 166 ? 0.1353 0.1172 0.1324 -0.0229 -0.0006 -0.0093 166 ILE A CA  
1411 C  C   . ILE A 166 ? 0.1174 0.1067 0.0957 -0.0120 0.0241  -0.0012 166 ILE A C   
1412 O  O   . ILE A 166 ? 0.1362 0.1180 0.1097 -0.0049 0.0000  -0.0076 166 ILE A O   
1413 C  CB  . ILE A 166 ? 0.1225 0.1146 0.1245 -0.0241 -0.0129 0.0114  166 ILE A CB  
1414 C  CG1 . ILE A 166 ? 0.1271 0.1216 0.1061 -0.0247 0.0010  -0.0031 166 ILE A CG1 
1415 C  CG2 . ILE A 166 ? 0.1448 0.1299 0.1503 -0.0203 -0.0173 0.0060  166 ILE A CG2 
1416 C  CD1 . ILE A 166 ? 0.1297 0.1597 0.1221 -0.0161 0.0048  -0.0171 166 ILE A CD1 
1417 N  N   . LYS A 167 ? 0.1246 0.1243 0.1242 -0.0085 0.0173  -0.0109 167 LYS A N   
1418 C  CA  . LYS A 167 ? 0.1303 0.1128 0.1067 -0.0167 0.0121  -0.0023 167 LYS A CA  
1419 C  C   . LYS A 167 ? 0.1420 0.0951 0.1268 -0.0054 0.0131  -0.0024 167 LYS A C   
1420 O  O   . LYS A 167 ? 0.1397 0.1316 0.1237 -0.0068 0.0052  0.0104  167 LYS A O   
1421 C  CB  . LYS A 167 ? 0.2052 0.1604 0.1234 -0.0125 0.0181  -0.0401 167 LYS A CB  
1422 C  CG  . LYS A 167 ? 0.1993 0.1274 0.2302 0.0049  0.0159  -0.0531 167 LYS A CG  
1423 C  CD  . LYS A 167 ? 0.2924 0.1863 0.2793 0.0178  0.0196  -0.1001 167 LYS A CD  
1424 C  CE  . LYS A 167 ? 0.3921 0.4049 0.2703 -0.1039 0.0551  -0.1124 167 LYS A CE  
1425 N  NZ  . LYS A 167 ? 0.5281 0.3303 0.2673 0.0537  0.0310  -0.0939 167 LYS A NZ  
1426 N  N   . THR A 168 ? 0.1380 0.1361 0.1263 -0.0185 0.0013  0.0019  168 THR A N   
1427 C  CA  . THR A 168 ? 0.1291 0.1200 0.1376 -0.0155 0.0219  0.0115  168 THR A CA  
1428 C  C   . THR A 168 ? 0.1370 0.1291 0.1360 -0.0093 0.0187  0.0197  168 THR A C   
1429 O  O   . THR A 168 ? 0.1288 0.1181 0.1318 -0.0154 0.0193  0.0051  168 THR A O   
1430 C  CB  . THR A 168 ? 0.1782 0.1395 0.1297 -0.0076 0.0252  0.0173  168 THR A CB  
1431 O  OG1 . THR A 168 ? 0.1556 0.1780 0.1281 -0.0186 0.0296  0.0080  168 THR A OG1 
1432 C  CG2 . THR A 168 ? 0.2099 0.1649 0.1358 -0.0326 0.0329  -0.0299 168 THR A CG2 
1433 N  N   . LYS A 169 ? 0.1362 0.1163 0.1321 -0.0113 0.0210  -0.0163 169 LYS A N   
1434 C  CA  . LYS A 169 ? 0.1412 0.1115 0.1155 -0.0177 0.0141  0.0063  169 LYS A CA  
1435 C  C   . LYS A 169 ? 0.1253 0.1199 0.1191 -0.0115 0.0230  -0.0062 169 LYS A C   
1436 O  O   . LYS A 169 ? 0.1464 0.1468 0.1351 -0.0098 0.0445  0.0017  169 LYS A O   
1437 C  CB  . LYS A 169 ? 0.1215 0.1579 0.1536 -0.0054 -0.0048 -0.0114 169 LYS A CB  
1438 C  CG  . LYS A 169 ? 0.1366 0.1450 0.1261 -0.0147 0.0110  0.0054  169 LYS A CG  
1439 C  CD  . LYS A 169 ? 0.1032 0.2185 0.2140 -0.0307 0.0154  -0.0093 169 LYS A CD  
1440 C  CE  . LYS A 169 ? 0.1353 0.2748 0.3246 -0.0037 -0.0140 -0.0803 169 LYS A CE  
1441 N  NZ  . LYS A 169 ? 0.2036 0.3230 0.3075 -0.0093 0.0304  -0.0452 169 LYS A NZ  
1442 N  N   . GLY A 170 ? 0.1148 0.0995 0.1308 -0.0118 0.0219  0.0035  170 GLY A N   
1443 C  CA  . GLY A 170 ? 0.1280 0.1034 0.1631 -0.0197 0.0209  0.0063  170 GLY A CA  
1444 C  C   . GLY A 170 ? 0.1573 0.1112 0.1192 -0.0163 0.0247  0.0243  170 GLY A C   
1445 O  O   . GLY A 170 ? 0.1743 0.1206 0.1776 -0.0195 -0.0130 0.0251  170 GLY A O   
1446 N  N   A LYS A 171 ? 0.1199 0.1377 0.1137 -0.0214 0.0153  0.0195  171 LYS A N   
1447 N  N   B LYS A 171 ? 0.1236 0.1404 0.1171 -0.0241 0.0193  0.0162  171 LYS A N   
1448 C  CA  A LYS A 171 ? 0.1356 0.1270 0.1018 -0.0007 0.0126  0.0186  171 LYS A CA  
1449 C  CA  B LYS A 171 ? 0.1454 0.1286 0.1107 -0.0166 0.0153  0.0355  171 LYS A CA  
1450 C  C   A LYS A 171 ? 0.1342 0.0944 0.1209 -0.0091 0.0184  0.0071  171 LYS A C   
1451 C  C   B LYS A 171 ? 0.1368 0.1111 0.1255 -0.0162 0.0027  0.0230  171 LYS A C   
1452 O  O   A LYS A 171 ? 0.1217 0.1039 0.1067 -0.0082 0.0082  0.0081  171 LYS A O   
1453 O  O   B LYS A 171 ? 0.1468 0.1545 0.1308 -0.0088 0.0173  0.0370  171 LYS A O   
1454 C  CB  A LYS A 171 ? 0.1351 0.1435 0.1272 -0.0065 -0.0120 0.0196  171 LYS A CB  
1455 C  CB  B LYS A 171 ? 0.1455 0.1418 0.1385 -0.0137 0.0155  0.0228  171 LYS A CB  
1456 C  CG  A LYS A 171 ? 0.1788 0.1139 0.1365 0.0137  0.0098  -0.0073 171 LYS A CG  
1457 C  CG  B LYS A 171 ? 0.1511 0.1938 0.2030 0.0261  0.0489  -0.0608 171 LYS A CG  
1458 C  CD  A LYS A 171 ? 0.2275 0.1933 0.1076 -0.0107 0.0178  -0.0087 171 LYS A CD  
1459 C  CD  B LYS A 171 ? 0.2818 0.2178 0.2065 -0.0208 0.0136  -0.0293 171 LYS A CD  
1460 C  CE  A LYS A 171 ? 0.3165 0.2174 0.0564 -0.0427 0.0239  0.0154  171 LYS A CE  
1461 C  CE  B LYS A 171 ? 0.2863 0.3334 0.1711 0.0461  0.0648  0.0469  171 LYS A CE  
1462 N  NZ  A LYS A 171 ? 0.4579 0.2725 0.1730 0.0199  -0.1243 0.0430  171 LYS A NZ  
1463 N  NZ  B LYS A 171 ? 0.3005 0.3045 0.1032 -0.0181 0.0194  0.0286  171 LYS A NZ  
1464 N  N   . SER A 172 ? 0.1235 0.1315 0.1172 -0.0104 0.0175  0.0230  172 SER A N   
1465 C  CA  . SER A 172 ? 0.1201 0.1030 0.1234 -0.0010 -0.0093 0.0197  172 SER A CA  
1466 C  C   . SER A 172 ? 0.1412 0.1253 0.1044 -0.0015 0.0054  0.0189  172 SER A C   
1467 O  O   . SER A 172 ? 0.1594 0.1793 0.0908 0.0063  0.0115  0.0285  172 SER A O   
1468 C  CB  . SER A 172 ? 0.1660 0.1155 0.1164 -0.0297 0.0000  0.0294  172 SER A CB  
1469 O  OG  . SER A 172 ? 0.1808 0.1465 0.1553 -0.0221 0.0252  0.0306  172 SER A OG  
1470 N  N   . ALA A 173 ? 0.1194 0.1306 0.1036 0.0041  -0.0087 0.0221  173 ALA A N   
1471 C  CA  . ALA A 173 ? 0.1342 0.1559 0.1017 0.0048  0.0153  0.0051  173 ALA A CA  
1472 C  C   . ALA A 173 ? 0.1280 0.1484 0.0803 0.0109  0.0120  0.0348  173 ALA A C   
1473 O  O   . ALA A 173 ? 0.1476 0.1208 0.0857 0.0186  0.0076  0.0222  173 ALA A O   
1474 C  CB  . ALA A 173 ? 0.1509 0.1377 0.1509 0.0153  -0.0176 -0.0225 173 ALA A CB  
1475 N  N   A ASP A 174 ? 0.1111 0.1014 0.1395 -0.0104 -0.0024 0.0238  174 ASP A N   
1476 N  N   B ASP A 174 ? 0.1635 0.1694 0.0939 0.0291  -0.0027 0.0333  174 ASP A N   
1477 C  CA  A ASP A 174 ? 0.1084 0.1146 0.1377 0.0062  -0.0020 0.0439  174 ASP A CA  
1478 C  CA  B ASP A 174 ? 0.1286 0.1633 0.0926 0.0043  -0.0209 0.0269  174 ASP A CA  
1479 C  C   A ASP A 174 ? 0.1182 0.1093 0.1009 0.0059  -0.0065 0.0162  174 ASP A C   
1480 C  C   B ASP A 174 ? 0.1797 0.1465 0.0901 0.0031  -0.0070 -0.0024 174 ASP A C   
1481 O  O   A ASP A 174 ? 0.1307 0.1254 0.1201 -0.0026 -0.0010 0.0041  174 ASP A O   
1482 O  O   B ASP A 174 ? 0.1604 0.1774 0.1216 -0.0023 -0.0198 -0.0342 174 ASP A O   
1483 C  CB  A ASP A 174 ? 0.1554 0.1881 0.1494 0.0178  -0.0015 0.0308  174 ASP A CB  
1484 C  CB  B ASP A 174 ? 0.2260 0.1518 0.0928 -0.0231 0.0148  0.0571  174 ASP A CB  
1485 C  CG  A ASP A 174 ? 0.1576 0.1846 0.1714 0.0155  -0.0421 0.0597  174 ASP A CG  
1486 C  CG  B ASP A 174 ? 0.2675 0.2073 0.1456 -0.0197 0.0331  -0.0318 174 ASP A CG  
1487 O  OD1 A ASP A 174 ? 0.2856 0.2307 0.2429 -0.0568 0.0776  0.0408  174 ASP A OD1 
1488 O  OD1 B ASP A 174 ? 0.2452 0.2599 0.2135 -0.0209 0.0344  0.0542  174 ASP A OD1 
1489 O  OD2 A ASP A 174 ? 0.2597 0.3194 0.2242 -0.0438 0.0443  0.0031  174 ASP A OD2 
1490 O  OD2 B ASP A 174 ? 0.3747 0.4902 0.1251 -0.1168 0.0441  -0.0263 174 ASP A OD2 
1491 N  N   . PHE A 175 ? 0.1474 0.1292 0.0847 0.0041  -0.0037 0.0172  175 PHE A N   
1492 C  CA  . PHE A 175 ? 0.1414 0.1121 0.0838 -0.0082 -0.0081 0.0175  175 PHE A CA  
1493 C  C   . PHE A 175 ? 0.1139 0.1185 0.1053 -0.0164 -0.0115 0.0131  175 PHE A C   
1494 O  O   . PHE A 175 ? 0.1322 0.1378 0.1164 0.0186  -0.0159 -0.0006 175 PHE A O   
1495 C  CB  . PHE A 175 ? 0.1181 0.1272 0.1207 0.0031  -0.0098 0.0208  175 PHE A CB  
1496 C  CG  . PHE A 175 ? 0.1237 0.1079 0.1093 0.0000  0.0000  0.0093  175 PHE A CG  
1497 C  CD1 . PHE A 175 ? 0.1772 0.1332 0.1307 0.0103  0.0395  -0.0076 175 PHE A CD1 
1498 C  CD2 . PHE A 175 ? 0.1335 0.1221 0.1101 0.0217  -0.0080 0.0197  175 PHE A CD2 
1499 C  CE1 . PHE A 175 ? 0.1880 0.1128 0.1493 -0.0154 0.0137  -0.0063 175 PHE A CE1 
1500 C  CE2 . PHE A 175 ? 0.1431 0.1307 0.1237 0.0115  -0.0010 0.0193  175 PHE A CE2 
1501 C  CZ  . PHE A 175 ? 0.1640 0.1007 0.1440 0.0131  -0.0099 0.0076  175 PHE A CZ  
1502 N  N   . THR A 176 ? 0.1171 0.1510 0.1172 -0.0049 -0.0210 0.0148  176 THR A N   
1503 C  CA  . THR A 176 ? 0.1347 0.1280 0.1132 -0.0027 -0.0174 0.0361  176 THR A CA  
1504 C  C   . THR A 176 ? 0.1446 0.1123 0.0917 -0.0006 -0.0351 0.0136  176 THR A C   
1505 O  O   . THR A 176 ? 0.1518 0.1075 0.1225 -0.0035 -0.0241 0.0153  176 THR A O   
1506 C  CB  . THR A 176 ? 0.1726 0.1483 0.1238 -0.0342 -0.0357 0.0399  176 THR A CB  
1507 O  OG1 . THR A 176 ? 0.2145 0.1835 0.1351 0.0076  -0.0286 0.0494  176 THR A OG1 
1508 C  CG2 . THR A 176 ? 0.2022 0.2354 0.2903 -0.0785 -0.0324 0.1167  176 THR A CG2 
1509 N  N   . ASN A 177 ? 0.1289 0.0943 0.1172 0.0040  -0.0333 0.0265  177 ASN A N   
1510 C  CA  . ASN A 177 ? 0.1149 0.1164 0.1172 -0.0098 -0.0331 0.0241  177 ASN A CA  
1511 C  C   . ASN A 177 ? 0.1282 0.1220 0.1353 -0.0207 -0.0277 0.0310  177 ASN A C   
1512 O  O   . ASN A 177 ? 0.1711 0.1833 0.2257 -0.0472 -0.0656 0.1067  177 ASN A O   
1513 C  CB  . ASN A 177 ? 0.1391 0.1336 0.1334 -0.0099 -0.0379 0.0379  177 ASN A CB  
1514 C  CG  . ASN A 177 ? 0.1456 0.1347 0.1237 0.0074  -0.0184 0.0294  177 ASN A CG  
1515 O  OD1 . ASN A 177 ? 0.1571 0.1676 0.2066 0.0320  0.0093  0.0348  177 ASN A OD1 
1516 N  ND2 . ASN A 177 ? 0.1732 0.1254 0.1132 0.0093  -0.0296 0.0238  177 ASN A ND2 
1517 N  N   . PHE A 178 ? 0.1233 0.1032 0.1031 0.0065  -0.0110 0.0238  178 PHE A N   
1518 C  CA  . PHE A 178 ? 0.1360 0.1004 0.1095 -0.0132 -0.0038 0.0269  178 PHE A CA  
1519 C  C   . PHE A 178 ? 0.1313 0.0970 0.0926 -0.0041 -0.0176 0.0121  178 PHE A C   
1520 O  O   . PHE A 178 ? 0.1629 0.1049 0.1182 -0.0171 -0.0108 0.0109  178 PHE A O   
1521 C  CB  . PHE A 178 ? 0.1406 0.1225 0.1136 0.0076  0.0027  0.0388  178 PHE A CB  
1522 C  CG  . PHE A 178 ? 0.1375 0.1024 0.0917 0.0034  0.0035  0.0274  178 PHE A CG  
1523 C  CD1 . PHE A 178 ? 0.1465 0.1202 0.1234 0.0076  0.0027  0.0197  178 PHE A CD1 
1524 C  CD2 . PHE A 178 ? 0.1049 0.1086 0.1083 0.0038  -0.0020 0.0206  178 PHE A CD2 
1525 C  CE1 . PHE A 178 ? 0.1694 0.1077 0.1131 0.0040  0.0120  0.0153  178 PHE A CE1 
1526 C  CE2 . PHE A 178 ? 0.1103 0.1175 0.1030 0.0151  0.0046  0.0295  178 PHE A CE2 
1527 C  CZ  . PHE A 178 ? 0.1289 0.1146 0.1220 0.0087  0.0038  0.0265  178 PHE A CZ  
1528 N  N   . ASP A 179 ? 0.1058 0.1216 0.1101 -0.0010 -0.0087 0.0184  179 ASP A N   
1529 C  CA  . ASP A 179 ? 0.1078 0.1146 0.1133 0.0076  -0.0007 0.0163  179 ASP A CA  
1530 C  C   . ASP A 179 ? 0.1206 0.0908 0.1022 0.0136  0.0065  0.0030  179 ASP A C   
1531 O  O   . ASP A 179 ? 0.1369 0.0979 0.1244 0.0081  -0.0035 0.0082  179 ASP A O   
1532 C  CB  . ASP A 179 ? 0.1225 0.1485 0.1430 0.0000  -0.0115 0.0226  179 ASP A CB  
1533 C  CG  . ASP A 179 ? 0.1048 0.1729 0.1905 0.0082  0.0026  0.0154  179 ASP A CG  
1534 O  OD1 . ASP A 179 ? 0.1431 0.1404 0.1533 0.0275  -0.0093 0.0299  179 ASP A OD1 
1535 O  OD2 . ASP A 179 ? 0.1218 0.3424 0.2565 0.0026  0.0126  -0.0873 179 ASP A OD2 
1536 N  N   . PRO A 180 ? 0.1159 0.1007 0.0894 -0.0010 -0.0073 0.0129  180 PRO A N   
1537 C  CA  . PRO A 180 ? 0.1052 0.1292 0.1053 0.0023  -0.0137 0.0197  180 PRO A CA  
1538 C  C   . PRO A 180 ? 0.1075 0.1234 0.1118 0.0141  0.0024  0.0132  180 PRO A C   
1539 O  O   . PRO A 180 ? 0.1191 0.1221 0.1102 0.0156  -0.0080 0.0153  180 PRO A O   
1540 C  CB  . PRO A 180 ? 0.0938 0.1536 0.1385 -0.0098 -0.0131 0.0076  180 PRO A CB  
1541 C  CG  . PRO A 180 ? 0.1462 0.1409 0.1351 -0.0219 -0.0386 0.0093  180 PRO A CG  
1542 C  CD  . PRO A 180 ? 0.1467 0.1221 0.1018 -0.0131 -0.0068 0.0107  180 PRO A CD  
1543 N  N   . ARG A 181 ? 0.0944 0.1325 0.1114 0.0046  0.0031  0.0175  181 ARG A N   
1544 C  CA  . ARG A 181 ? 0.1069 0.1316 0.1071 -0.0006 0.0020  -0.0003 181 ARG A CA  
1545 C  C   . ARG A 181 ? 0.1084 0.1269 0.1139 0.0177  -0.0041 0.0375  181 ARG A C   
1546 O  O   . ARG A 181 ? 0.1180 0.1316 0.1164 0.0184  0.0076  0.0236  181 ARG A O   
1547 C  CB  . ARG A 181 ? 0.1032 0.1234 0.1344 0.0109  0.0049  0.0049  181 ARG A CB  
1548 C  CG  . ARG A 181 ? 0.1510 0.1401 0.1678 0.0049  0.0348  -0.0285 181 ARG A CG  
1549 C  CD  . ARG A 181 ? 0.1770 0.1655 0.1687 0.0252  0.0710  0.0286  181 ARG A CD  
1550 N  NE  . ARG A 181 ? 0.1552 0.1466 0.1808 0.0366  0.0417  0.0126  181 ARG A NE  
1551 C  CZ  . ARG A 181 ? 0.1834 0.2031 0.2183 0.0397  0.0653  0.0471  181 ARG A CZ  
1552 N  NH1 . ARG A 181 ? 0.2140 0.2477 0.3212 0.0834  0.0851  0.0693  181 ARG A NH1 
1553 N  NH2 . ARG A 181 ? 0.1888 0.2055 0.2549 0.0410  0.0309  0.0456  181 ARG A NH2 
1554 N  N   . GLY A 182 ? 0.1113 0.1151 0.1078 0.0175  -0.0131 0.0104  182 GLY A N   
1555 C  CA  . GLY A 182 ? 0.1701 0.1162 0.1193 0.0241  -0.0252 -0.0013 182 GLY A CA  
1556 C  C   . GLY A 182 ? 0.1485 0.1133 0.1209 0.0175  -0.0131 -0.0037 182 GLY A C   
1557 O  O   . GLY A 182 ? 0.1580 0.1107 0.1588 0.0093  -0.0196 0.0017  182 GLY A O   
1558 N  N   . LEU A 183 ? 0.1159 0.1313 0.1118 0.0324  -0.0020 0.0082  183 LEU A N   
1559 C  CA  . LEU A 183 ? 0.1336 0.1103 0.1180 0.0198  -0.0119 0.0098  183 LEU A CA  
1560 C  C   . LEU A 183 ? 0.1287 0.1026 0.1239 0.0124  -0.0098 0.0092  183 LEU A C   
1561 O  O   . LEU A 183 ? 0.1388 0.1216 0.1361 0.0296  0.0031  0.0317  183 LEU A O   
1562 C  CB  . LEU A 183 ? 0.1155 0.1295 0.1023 0.0132  -0.0086 0.0104  183 LEU A CB  
1563 C  CG  . LEU A 183 ? 0.1475 0.1454 0.0891 0.0307  0.0046  0.0197  183 LEU A CG  
1564 C  CD1 . LEU A 183 ? 0.1614 0.2016 0.1114 0.0154  -0.0063 0.0388  183 LEU A CD1 
1565 C  CD2 . LEU A 183 ? 0.2185 0.1718 0.1146 0.0593  0.0118  -0.0120 183 LEU A CD2 
1566 N  N   . LEU A 184 ? 0.1210 0.1280 0.1050 0.0136  0.0017  0.0035  184 LEU A N   
1567 C  CA  . LEU A 184 ? 0.1298 0.1103 0.1164 -0.0020 0.0046  0.0103  184 LEU A CA  
1568 C  C   . LEU A 184 ? 0.1471 0.1289 0.1312 -0.0313 -0.0315 0.0131  184 LEU A C   
1569 O  O   . LEU A 184 ? 0.2235 0.1720 0.1722 -0.0829 -0.0785 0.0487  184 LEU A O   
1570 C  CB  . LEU A 184 ? 0.0970 0.1243 0.1263 -0.0046 0.0059  0.0103  184 LEU A CB  
1571 C  CG  . LEU A 184 ? 0.0828 0.1250 0.1600 -0.0007 -0.0038 0.0074  184 LEU A CG  
1572 C  CD1 . LEU A 184 ? 0.1450 0.1547 0.1629 0.0003  0.0153  -0.0103 184 LEU A CD1 
1573 C  CD2 . LEU A 184 ? 0.1066 0.1395 0.2558 0.0000  -0.0313 0.0023  184 LEU A CD2 
1574 N  N   . PRO A 185 ? 0.1261 0.1150 0.1192 -0.0020 -0.0097 0.0109  185 PRO A N   
1575 C  CA  . PRO A 185 ? 0.1330 0.1058 0.1233 0.0000  -0.0020 0.0181  185 PRO A CA  
1576 C  C   . PRO A 185 ? 0.1122 0.1139 0.1172 -0.0071 -0.0175 0.0077  185 PRO A C   
1577 O  O   . PRO A 185 ? 0.1050 0.1159 0.1876 -0.0057 -0.0241 0.0142  185 PRO A O   
1578 C  CB  . PRO A 185 ? 0.1075 0.1374 0.1402 0.0031  0.0000  0.0236  185 PRO A CB  
1579 C  CG  . PRO A 185 ? 0.0966 0.1287 0.1115 0.0177  -0.0164 0.0118  185 PRO A CG  
1580 C  CD  . PRO A 185 ? 0.1124 0.1049 0.1194 0.0006  -0.0172 0.0000  185 PRO A CD  
1581 N  N   . GLU A 186 ? 0.1445 0.1307 0.1351 -0.0130 -0.0162 0.0263  186 GLU A N   
1582 C  CA  . GLU A 186 ? 0.0927 0.1498 0.1959 -0.0254 -0.0086 0.0164  186 GLU A CA  
1583 C  C   . GLU A 186 ? 0.0928 0.1386 0.1861 -0.0118 -0.0082 0.0214  186 GLU A C   
1584 O  O   . GLU A 186 ? 0.1040 0.1800 0.1693 0.0225  -0.0013 0.0063  186 GLU A O   
1585 C  CB  . GLU A 186 ? 0.1532 0.1863 0.2029 -0.0597 -0.0288 0.0328  186 GLU A CB  
1586 C  CG  . GLU A 186 ? 0.1792 0.1613 0.2587 -0.0463 -0.0461 -0.0020 186 GLU A CG  
1587 C  CD  . GLU A 186 ? 0.1664 0.2310 0.2736 -0.0361 -0.0551 0.0119  186 GLU A CD  
1588 O  OE1 . GLU A 186 ? 0.1888 0.2833 0.3052 -0.0719 -0.0291 0.0768  186 GLU A OE1 
1589 O  OE2 . GLU A 186 ? 0.2822 0.2075 0.3980 -0.0763 -0.0785 0.0370  186 GLU A OE2 
1590 N  N   . SER A 187 ? 0.0788 0.1643 0.1555 -0.0104 -0.0136 0.0207  187 SER A N   
1591 C  CA  . SER A 187 ? 0.0830 0.1753 0.1419 0.0088  0.0091  0.0142  187 SER A CA  
1592 C  C   . SER A 187 ? 0.0742 0.1644 0.1323 -0.0125 -0.0077 0.0130  187 SER A C   
1593 O  O   . SER A 187 ? 0.0786 0.1823 0.1506 -0.0186 0.0173  -0.0037 187 SER A O   
1594 C  CB  . SER A 187 ? 0.1245 0.1852 0.1519 -0.0027 -0.0153 0.0076  187 SER A CB  
1595 O  OG  . SER A 187 ? 0.1101 0.2249 0.1631 -0.0038 0.0020  0.0313  187 SER A OG  
1596 N  N   . LEU A 188 ? 0.0878 0.1723 0.1533 0.0007  -0.0063 -0.0137 188 LEU A N   
1597 C  CA  . LEU A 188 ? 0.1000 0.1508 0.1624 -0.0177 -0.0107 -0.0113 188 LEU A CA  
1598 C  C   . LEU A 188 ? 0.0956 0.1474 0.1644 0.0097  -0.0027 -0.0346 188 LEU A C   
1599 O  O   . LEU A 188 ? 0.1203 0.2012 0.1705 -0.0049 -0.0135 -0.0344 188 LEU A O   
1600 C  CB  . LEU A 188 ? 0.1280 0.1578 0.1669 -0.0232 -0.0137 0.0099  188 LEU A CB  
1601 C  CG  . LEU A 188 ? 0.1053 0.1784 0.1836 -0.0073 -0.0153 -0.0041 188 LEU A CG  
1602 C  CD1 . LEU A 188 ? 0.1326 0.1869 0.2921 0.0003  -0.0126 0.0313  188 LEU A CD1 
1603 C  CD2 . LEU A 188 ? 0.0996 0.2608 0.2214 -0.0068 0.0175  0.0355  188 LEU A CD2 
1604 N  N   . ASP A 189 ? 0.0878 0.1766 0.1269 0.0049  -0.0015 -0.0124 189 ASP A N   
1605 C  CA  . ASP A 189 ? 0.0854 0.2004 0.1324 -0.0315 -0.0006 -0.0183 189 ASP A CA  
1606 C  C   . ASP A 189 ? 0.0925 0.1597 0.0992 -0.0035 -0.0005 -0.0065 189 ASP A C   
1607 O  O   . ASP A 189 ? 0.0893 0.1456 0.1107 -0.0126 -0.0046 0.0026  189 ASP A O   
1608 C  CB  . ASP A 189 ? 0.1316 0.2578 0.1251 -0.0776 0.0307  0.0304  189 ASP A CB  
1609 C  CG  . ASP A 189 ? 0.1550 0.2714 0.1773 -0.0644 0.0057  0.0104  189 ASP A CG  
1610 O  OD1 . ASP A 189 ? 0.1870 0.4036 0.3185 -0.0680 0.1225  -0.0636 189 ASP A OD1 
1611 O  OD2 . ASP A 189 ? 0.1888 0.4551 0.2703 -0.1553 -0.0221 0.0891  189 ASP A OD2 
1612 N  N   . TYR A 190 ? 0.0829 0.1543 0.1026 -0.0114 0.0035  0.0130  190 TYR A N   
1613 C  CA  . TYR A 190 ? 0.0707 0.1546 0.1033 -0.0019 0.0035  0.0114  190 TYR A CA  
1614 C  C   . TYR A 190 ? 0.0900 0.1203 0.0812 -0.0006 0.0024  0.0062  190 TYR A C   
1615 O  O   . TYR A 190 ? 0.0926 0.1555 0.0944 0.0005  0.0225  -0.0065 190 TYR A O   
1616 C  CB  . TYR A 190 ? 0.1103 0.1457 0.0964 0.0077  -0.0054 0.0076  190 TYR A CB  
1617 C  CG  . TYR A 190 ? 0.0763 0.1413 0.1067 -0.0043 0.0026  0.0098  190 TYR A CG  
1618 C  CD1 . TYR A 190 ? 0.1025 0.1543 0.1076 -0.0087 -0.0038 0.0087  190 TYR A CD1 
1619 C  CD2 . TYR A 190 ? 0.0974 0.1438 0.1313 -0.0113 0.0074  0.0120  190 TYR A CD2 
1620 C  CE1 . TYR A 190 ? 0.1203 0.1457 0.1254 -0.0120 -0.0088 -0.0063 190 TYR A CE1 
1621 C  CE2 . TYR A 190 ? 0.1130 0.1537 0.1366 -0.0057 0.0020  -0.0006 190 TYR A CE2 
1622 C  CZ  . TYR A 190 ? 0.1194 0.1834 0.1316 0.0109  -0.0065 -0.0082 190 TYR A CZ  
1623 O  OH  . TYR A 190 ? 0.1397 0.1842 0.1582 0.0242  0.0020  -0.0205 190 TYR A OH  
1624 N  N   . TRP A 191 ? 0.0821 0.1203 0.0830 0.0017  -0.0041 0.0000  191 TRP A N   
1625 C  CA  . TRP A 191 ? 0.0848 0.1182 0.0919 -0.0007 -0.0007 -0.0043 191 TRP A CA  
1626 C  C   . TRP A 191 ? 0.0868 0.1155 0.0645 0.0035  0.0049  -0.0049 191 TRP A C   
1627 O  O   . TRP A 191 ? 0.1078 0.1277 0.0785 -0.0153 -0.0019 0.0054  191 TRP A O   
1628 C  CB  . TRP A 191 ? 0.1033 0.1033 0.1217 -0.0019 0.0031  -0.0071 191 TRP A CB  
1629 C  CG  . TRP A 191 ? 0.0908 0.1118 0.1014 0.0120  -0.0093 0.0057  191 TRP A CG  
1630 C  CD1 . TRP A 191 ? 0.1330 0.1250 0.1131 0.0098  0.0017  0.0265  191 TRP A CD1 
1631 C  CD2 . TRP A 191 ? 0.0854 0.1272 0.1039 0.0115  -0.0038 0.0164  191 TRP A CD2 
1632 N  NE1 . TRP A 191 ? 0.1356 0.1353 0.1137 0.0097  0.0076  0.0131  191 TRP A NE1 
1633 C  CE2 . TRP A 191 ? 0.1253 0.1272 0.1111 0.0098  -0.0013 0.0098  191 TRP A CE2 
1634 C  CE3 . TRP A 191 ? 0.0916 0.1348 0.1113 0.0070  -0.0074 -0.0052 191 TRP A CE3 
1635 C  CZ2 . TRP A 191 ? 0.1132 0.1305 0.1606 0.0076  -0.0098 0.0073  191 TRP A CZ2 
1636 C  CZ3 . TRP A 191 ? 0.0928 0.1465 0.1360 -0.0006 0.0099  -0.0026 191 TRP A CZ3 
1637 C  CH2 . TRP A 191 ? 0.1093 0.1290 0.1561 0.0073  -0.0233 -0.0161 191 TRP A CH2 
1638 N  N   . THR A 192 ? 0.0891 0.1129 0.0834 0.0003  0.0076  -0.0068 192 THR A N   
1639 C  CA  . THR A 192 ? 0.0939 0.1243 0.0789 0.0059  -0.0012 -0.0043 192 THR A CA  
1640 C  C   . THR A 192 ? 0.0858 0.1093 0.0785 0.0086  -0.0017 -0.0024 192 THR A C   
1641 O  O   . THR A 192 ? 0.0989 0.1366 0.0754 -0.0027 0.0031  0.0013  192 THR A O   
1642 C  CB  . THR A 192 ? 0.1023 0.1177 0.0961 0.0153  0.0125  -0.0125 192 THR A CB  
1643 O  OG1 . THR A 192 ? 0.0982 0.1119 0.0989 0.0115  -0.0027 -0.0130 192 THR A OG1 
1644 C  CG2 . THR A 192 ? 0.1200 0.1518 0.0851 0.0208  0.0193  -0.0110 192 THR A CG2 
1645 N  N   . TYR A 193 ? 0.0838 0.1080 0.0917 0.0030  0.0063  -0.0096 193 TYR A N   
1646 C  CA  . TYR A 193 ? 0.0877 0.1181 0.0797 0.0024  -0.0087 -0.0087 193 TYR A CA  
1647 C  C   . TYR A 193 ? 0.0865 0.1111 0.0847 0.0109  0.0019  -0.0164 193 TYR A C   
1648 O  O   . TYR A 193 ? 0.0867 0.1051 0.0839 0.0062  -0.0060 -0.0054 193 TYR A O   
1649 C  CB  . TYR A 193 ? 0.0982 0.1149 0.0724 0.0124  -0.0126 -0.0070 193 TYR A CB  
1650 C  CG  . TYR A 193 ? 0.0891 0.1023 0.0931 0.0017  -0.0208 0.0065  193 TYR A CG  
1651 C  CD1 . TYR A 193 ? 0.0957 0.0900 0.0854 0.0086  -0.0048 0.0038  193 TYR A CD1 
1652 C  CD2 . TYR A 193 ? 0.0908 0.1019 0.1040 0.0000  -0.0063 -0.0154 193 TYR A CD2 
1653 C  CE1 . TYR A 193 ? 0.0863 0.0925 0.0860 0.0074  -0.0087 0.0082  193 TYR A CE1 
1654 C  CE2 . TYR A 193 ? 0.0997 0.0892 0.0964 0.0057  -0.0115 -0.0103 193 TYR A CE2 
1655 C  CZ  . TYR A 193 ? 0.0934 0.0868 0.0755 0.0046  -0.0074 -0.0049 193 TYR A CZ  
1656 O  OH  . TYR A 193 ? 0.0891 0.0966 0.0887 0.0076  0.0005  -0.0093 193 TYR A OH  
1657 N  N   . PRO A 194 ? 0.0952 0.1068 0.0785 0.0046  -0.0060 -0.0113 194 PRO A N   
1658 C  CA  . PRO A 194 ? 0.0907 0.1032 0.0902 0.0031  0.0030  -0.0104 194 PRO A CA  
1659 C  C   . PRO A 194 ? 0.0873 0.0902 0.0847 0.0031  -0.0051 -0.0225 194 PRO A C   
1660 O  O   . PRO A 194 ? 0.0910 0.1139 0.0869 0.0057  0.0006  0.0000  194 PRO A O   
1661 C  CB  . PRO A 194 ? 0.1164 0.1176 0.1014 0.0065  -0.0024 -0.0259 194 PRO A CB  
1662 C  CG  . PRO A 194 ? 0.1198 0.1489 0.1067 -0.0170 0.0015  -0.0200 194 PRO A CG  
1663 C  CD  . PRO A 194 ? 0.1175 0.1510 0.0606 -0.0131 0.0043  -0.0164 194 PRO A CD  
1664 N  N   . GLY A 195 ? 0.0750 0.1014 0.0776 0.0043  -0.0026 -0.0136 195 GLY A N   
1665 C  CA  . GLY A 195 ? 0.0901 0.1049 0.0873 0.0102  -0.0007 -0.0048 195 GLY A CA  
1666 C  C   . GLY A 195 ? 0.0759 0.0828 0.0814 -0.0065 -0.0148 -0.0049 195 GLY A C   
1667 O  O   . GLY A 195 ? 0.0895 0.0887 0.0935 -0.0035 -0.0048 -0.0115 195 GLY A O   
1668 N  N   . SER A 196 ? 0.0819 0.0907 0.0838 -0.0035 0.0027  -0.0043 196 SER A N   
1669 C  CA  . SER A 196 ? 0.0873 0.0964 0.0873 -0.0035 -0.0013 -0.0163 196 SER A CA  
1670 C  C   . SER A 196 ? 0.0653 0.0893 0.0831 0.0073  0.0003  -0.0077 196 SER A C   
1671 O  O   . SER A 196 ? 0.0772 0.0908 0.0902 -0.0027 -0.0118 -0.0030 196 SER A O   
1672 C  CB  . SER A 196 ? 0.0838 0.0918 0.1076 -0.0065 -0.0182 -0.0076 196 SER A CB  
1673 O  OG  . SER A 196 ? 0.0717 0.0942 0.1035 -0.0043 -0.0085 -0.0005 196 SER A OG  
1674 N  N   . LEU A 197 ? 0.0781 0.0936 0.0851 -0.0035 0.0048  -0.0074 197 LEU A N   
1675 C  CA  . LEU A 197 ? 0.0873 0.0872 0.0867 -0.0015 -0.0023 0.0030  197 LEU A CA  
1676 C  C   . LEU A 197 ? 0.0746 0.0935 0.1016 -0.0130 0.0043  0.0000  197 LEU A C   
1677 O  O   . LEU A 197 ? 0.0766 0.1067 0.0978 0.0023  0.0023  -0.0071 197 LEU A O   
1678 C  CB  . LEU A 197 ? 0.1093 0.0965 0.1031 -0.0104 0.0054  0.0071  197 LEU A CB  
1679 C  CG  . LEU A 197 ? 0.1403 0.1296 0.1580 -0.0038 0.0082  0.0151  197 LEU A CG  
1680 C  CD1 . LEU A 197 ? 0.1432 0.1471 0.1844 -0.0241 0.0060  0.0436  197 LEU A CD1 
1681 C  CD2 . LEU A 197 ? 0.1409 0.1755 0.1669 0.0454  0.0307  0.0175  197 LEU A CD2 
1682 N  N   . THR A 198 ? 0.0919 0.0822 0.0935 0.0000  -0.0082 -0.0125 198 THR A N   
1683 C  CA  . THR A 198 ? 0.0885 0.0926 0.1014 -0.0052 -0.0062 -0.0074 198 THR A CA  
1684 C  C   . THR A 198 ? 0.0806 0.0987 0.0873 -0.0041 -0.0098 -0.0104 198 THR A C   
1685 O  O   . THR A 198 ? 0.0790 0.1084 0.1095 -0.0073 -0.0040 -0.0054 198 THR A O   
1686 C  CB  . THR A 198 ? 0.0797 0.0990 0.0759 -0.0114 -0.0113 0.0005  198 THR A CB  
1687 O  OG1 . THR A 198 ? 0.0803 0.0931 0.0876 -0.0051 -0.0060 0.0046  198 THR A OG1 
1688 C  CG2 . THR A 198 ? 0.1030 0.1013 0.1084 -0.0087 0.0200  0.0073  198 THR A CG2 
1689 N  N   . THR A 199 ? 0.0895 0.1077 0.1084 -0.0052 0.0051  0.0000  199 THR A N   
1690 C  CA  . THR A 199 ? 0.0931 0.1162 0.1049 -0.0143 0.0076  0.0000  199 THR A CA  
1691 C  C   . THR A 199 ? 0.0749 0.1282 0.1107 -0.0132 0.0073  0.0076  199 THR A C   
1692 O  O   . THR A 199 ? 0.0943 0.1148 0.1172 -0.0193 -0.0007 -0.0054 199 THR A O   
1693 C  CB  . THR A 199 ? 0.1076 0.1289 0.1220 -0.0125 -0.0060 -0.0048 199 THR A CB  
1694 O  OG1 . THR A 199 ? 0.1216 0.1534 0.1307 -0.0109 -0.0054 0.0093  199 THR A OG1 
1695 C  CG2 . THR A 199 ? 0.1374 0.1484 0.1402 -0.0315 0.0054  -0.0208 199 THR A CG2 
1696 N  N   . PRO A 200 ? 0.0935 0.1238 0.1243 -0.0182 0.0082  0.0059  200 PRO A N   
1697 C  CA  . PRO A 200 ? 0.1163 0.1247 0.1208 -0.0230 0.0137  0.0185  200 PRO A CA  
1698 C  C   . PRO A 200 ? 0.1142 0.1316 0.1324 -0.0388 -0.0046 0.0082  200 PRO A C   
1699 O  O   . PRO A 200 ? 0.1377 0.1703 0.1259 -0.0006 -0.0115 0.0098  200 PRO A O   
1700 C  CB  . PRO A 200 ? 0.0990 0.1796 0.1708 -0.0189 0.0331  0.0148  200 PRO A CB  
1701 C  CG  . PRO A 200 ? 0.0986 0.1694 0.1568 -0.0164 0.0051  -0.0092 200 PRO A CG  
1702 C  CD  . PRO A 200 ? 0.0918 0.1579 0.1298 -0.0142 0.0162  -0.0062 200 PRO A CD  
1703 N  N   . PRO A 201 ? 0.1118 0.1431 0.1307 -0.0177 0.0098  0.0165  201 PRO A N   
1704 C  CA  . PRO A 201 ? 0.1361 0.1243 0.1290 -0.0450 0.0006  0.0197  201 PRO A CA  
1705 C  C   . PRO A 201 ? 0.0869 0.1246 0.1186 -0.0052 -0.0012 -0.0027 201 PRO A C   
1706 O  O   . PRO A 201 ? 0.1016 0.1233 0.1458 -0.0244 -0.0108 0.0003  201 PRO A O   
1707 C  CB  . PRO A 201 ? 0.1369 0.1380 0.1624 -0.0295 0.0035  0.0469  201 PRO A CB  
1708 C  CG  . PRO A 201 ? 0.2109 0.1878 0.2174 0.0023  -0.0241 0.0399  201 PRO A CG  
1709 C  CD  . PRO A 201 ? 0.1776 0.1303 0.1827 -0.0093 -0.0208 0.0362  201 PRO A CD  
1710 N  N   . LEU A 202 ? 0.0805 0.0969 0.1139 -0.0080 0.0026  0.0065  202 LEU A N   
1711 C  CA  . LEU A 202 ? 0.0839 0.1093 0.1084 0.0005  -0.0062 -0.0068 202 LEU A CA  
1712 C  C   . LEU A 202 ? 0.0794 0.1102 0.1052 -0.0137 0.0068  0.0051  202 LEU A C   
1713 O  O   . LEU A 202 ? 0.0766 0.1059 0.1107 -0.0104 0.0041  -0.0093 202 LEU A O   
1714 C  CB  . LEU A 202 ? 0.0790 0.1014 0.1316 -0.0097 -0.0048 -0.0040 202 LEU A CB  
1715 C  CG  . LEU A 202 ? 0.0847 0.1076 0.1199 -0.0038 -0.0073 0.0024  202 LEU A CG  
1716 C  CD1 . LEU A 202 ? 0.0865 0.1215 0.1456 -0.0003 -0.0046 -0.0281 202 LEU A CD1 
1717 C  CD2 . LEU A 202 ? 0.0819 0.1118 0.1272 -0.0087 0.0068  -0.0120 202 LEU A CD2 
1718 N  N   . ASN A 203 ? 0.0999 0.0926 0.1263 -0.0085 0.0096  -0.0099 203 ASN A N   
1719 C  CA  . ASN A 203 ? 0.0952 0.0911 0.1458 -0.0037 0.0153  -0.0037 203 ASN A CA  
1720 C  C   . ASN A 203 ? 0.0930 0.0996 0.1181 -0.0043 0.0015  -0.0173 203 ASN A C   
1721 O  O   . ASN A 203 ? 0.0988 0.0916 0.1209 -0.0118 -0.0091 -0.0073 203 ASN A O   
1722 C  CB  . ASN A 203 ? 0.1060 0.1156 0.1641 -0.0041 0.0222  0.0171  203 ASN A CB  
1723 C  CG  . ASN A 203 ? 0.1529 0.1298 0.1676 0.0219  0.0493  0.0207  203 ASN A CG  
1724 O  OD1 . ASN A 203 ? 0.1860 0.1695 0.2879 0.0136  0.0790  0.0447  203 ASN A OD1 
1725 N  ND2 . ASN A 203 ? 0.2142 0.1585 0.2259 0.0065  0.0652  0.0683  203 ASN A ND2 
1726 N  N   . GLU A 204 ? 0.0971 0.1181 0.1208 -0.0104 0.0063  -0.0171 204 GLU A N   
1727 C  CA  . GLU A 204 ? 0.1050 0.1279 0.1023 0.0043  -0.0200 -0.0340 204 GLU A CA  
1728 C  C   . GLU A 204 ? 0.1111 0.0856 0.1043 -0.0049 -0.0082 -0.0115 204 GLU A C   
1729 O  O   . GLU A 204 ? 0.1206 0.1349 0.1137 0.0219  -0.0274 -0.0253 204 GLU A O   
1730 C  CB  . GLU A 204 ? 0.0988 0.1360 0.1105 0.0000  -0.0219 -0.0230 204 GLU A CB  
1731 C  CG  . GLU A 204 ? 0.1033 0.1395 0.1191 0.0059  -0.0220 -0.0049 204 GLU A CG  
1732 C  CD  . GLU A 204 ? 0.1120 0.1291 0.1227 -0.0115 -0.0175 -0.0185 204 GLU A CD  
1733 O  OE1 . GLU A 204 ? 0.1400 0.1459 0.1841 0.0087  -0.0568 -0.0324 204 GLU A OE1 
1734 O  OE2 . GLU A 204 ? 0.1084 0.1379 0.1322 0.0006  -0.0208 -0.0027 204 GLU A OE2 
1735 N  N   . CYS A 205 ? 0.0841 0.0936 0.1269 -0.0093 -0.0082 -0.0052 205 CYS A N   
1736 C  CA  . CYS A 205 ? 0.0982 0.0944 0.1019 0.0031  -0.0198 0.0017  205 CYS A CA  
1737 C  C   . CYS A 205 ? 0.1023 0.0864 0.1026 0.0107  -0.0153 -0.0129 205 CYS A C   
1738 O  O   . CYS A 205 ? 0.1106 0.0917 0.1535 0.0006  -0.0344 -0.0026 205 CYS A O   
1739 C  CB  . CYS A 205 ? 0.1096 0.1132 0.1102 -0.0071 -0.0074 0.0051  205 CYS A CB  
1740 S  SG  . CYS A 205 ? 0.1295 0.1114 0.1172 0.0051  -0.0120 -0.0049 205 CYS A SG  
1741 N  N   . VAL A 206 ? 0.0814 0.0833 0.1043 0.0017  -0.0109 -0.0098 206 VAL A N   
1742 C  CA  . VAL A 206 ? 0.0795 0.0864 0.1017 -0.0104 -0.0035 -0.0049 206 VAL A CA  
1743 C  C   . VAL A 206 ? 0.0832 0.0840 0.1067 0.0003  -0.0153 -0.0054 206 VAL A C   
1744 O  O   . VAL A 206 ? 0.0974 0.1146 0.1162 -0.0023 -0.0181 0.0131  206 VAL A O   
1745 C  CB  . VAL A 206 ? 0.0777 0.0991 0.1289 0.0043  -0.0063 -0.0087 206 VAL A CB  
1746 C  CG1 . VAL A 206 ? 0.0822 0.0989 0.1155 -0.0010 -0.0178 -0.0156 206 VAL A CG1 
1747 C  CG2 . VAL A 206 ? 0.0847 0.1093 0.1150 -0.0051 0.0052  -0.0093 206 VAL A CG2 
1748 N  N   . THR A 207 ? 0.0829 0.0770 0.1067 -0.0043 0.0003  -0.0087 207 THR A N   
1749 C  CA  . THR A 207 ? 0.0955 0.0987 0.0980 -0.0031 -0.0076 -0.0060 207 THR A CA  
1750 C  C   . THR A 207 ? 0.0833 0.0753 0.0878 -0.0031 -0.0098 -0.0035 207 THR A C   
1751 O  O   . THR A 207 ? 0.0913 0.0918 0.0975 0.0013  -0.0162 -0.0035 207 THR A O   
1752 C  CB  . THR A 207 ? 0.1075 0.0972 0.1243 -0.0041 0.0115  -0.0177 207 THR A CB  
1753 O  OG1 . THR A 207 ? 0.1243 0.0970 0.1413 0.0104  -0.0142 -0.0287 207 THR A OG1 
1754 C  CG2 . THR A 207 ? 0.1024 0.1216 0.1368 -0.0020 0.0052  -0.0183 207 THR A CG2 
1755 N  N   . TRP A 208 ? 0.0732 0.0776 0.0881 0.0024  -0.0037 -0.0068 208 TRP A N   
1756 C  CA  . TRP A 208 ? 0.0798 0.0692 0.0834 0.0041  -0.0020 -0.0031 208 TRP A CA  
1757 C  C   . TRP A 208 ? 0.0812 0.0771 0.0714 0.0104  0.0043  -0.0071 208 TRP A C   
1758 O  O   . TRP A 208 ? 0.0847 0.0991 0.0768 0.0024  0.0059  -0.0052 208 TRP A O   
1759 C  CB  . TRP A 208 ? 0.0812 0.0921 0.0788 0.0070  -0.0060 0.0037  208 TRP A CB  
1760 C  CG  . TRP A 208 ? 0.0807 0.0856 0.0807 0.0017  -0.0031 0.0074  208 TRP A CG  
1761 C  CD1 . TRP A 208 ? 0.0840 0.0828 0.1009 0.0035  -0.0080 0.0043  208 TRP A CD1 
1762 C  CD2 . TRP A 208 ? 0.0776 0.0549 0.0988 0.0098  0.0012  0.0035  208 TRP A CD2 
1763 N  NE1 . TRP A 208 ? 0.0816 0.0894 0.1079 0.0048  -0.0049 -0.0006 208 TRP A NE1 
1764 C  CE2 . TRP A 208 ? 0.0803 0.0816 0.0829 0.0152  0.0093  0.0062  208 TRP A CE2 
1765 C  CE3 . TRP A 208 ? 0.0988 0.0706 0.0913 0.0108  -0.0174 -0.0003 208 TRP A CE3 
1766 C  CZ2 . TRP A 208 ? 0.0847 0.0910 0.1096 0.0253  0.0142  0.0063  208 TRP A CZ2 
1767 C  CZ3 . TRP A 208 ? 0.1048 0.0863 0.0891 0.0159  -0.0015 -0.0092 208 TRP A CZ3 
1768 C  CH2 . TRP A 208 ? 0.1335 0.0867 0.0881 0.0307  0.0165  -0.0109 208 TRP A CH2 
1769 N  N   . ILE A 209 ? 0.0746 0.0794 0.0864 0.0035  -0.0074 -0.0020 209 ILE A N   
1770 C  CA  . ILE A 209 ? 0.0787 0.0856 0.0898 -0.0027 0.0020  -0.0164 209 ILE A CA  
1771 C  C   . ILE A 209 ? 0.0717 0.0775 0.0711 -0.0017 0.0120  0.0019  209 ILE A C   
1772 O  O   . ILE A 209 ? 0.1146 0.0781 0.0776 0.0041  0.0031  -0.0035 209 ILE A O   
1773 C  CB  . ILE A 209 ? 0.0697 0.0955 0.1111 0.0125  0.0054  -0.0070 209 ILE A CB  
1774 C  CG1 . ILE A 209 ? 0.1080 0.0891 0.1431 0.0172  -0.0163 -0.0140 209 ILE A CG1 
1775 C  CG2 . ILE A 209 ? 0.0843 0.1256 0.1272 0.0197  0.0126  -0.0015 209 ILE A CG2 
1776 C  CD1 . ILE A 209 ? 0.1084 0.1208 0.2048 0.0262  -0.0017 -0.0109 209 ILE A CD1 
1777 N  N   . VAL A 210 ? 0.0760 0.0790 0.0855 -0.0052 0.0010  0.0020  210 VAL A N   
1778 C  CA  . VAL A 210 ? 0.0716 0.0784 0.0812 0.0013  0.0057  -0.0051 210 VAL A CA  
1779 C  C   . VAL A 210 ? 0.0828 0.0858 0.0772 0.0054  0.0096  -0.0085 210 VAL A C   
1780 O  O   . VAL A 210 ? 0.0829 0.1083 0.0781 -0.0098 0.0012  0.0003  210 VAL A O   
1781 C  CB  . VAL A 210 ? 0.0780 0.0894 0.0829 -0.0010 0.0043  0.0052  210 VAL A CB  
1782 C  CG1 . VAL A 210 ? 0.1014 0.0938 0.1118 -0.0043 0.0049  0.0031  210 VAL A CG1 
1783 C  CG2 . VAL A 210 ? 0.0917 0.0846 0.1347 -0.0046 -0.0031 0.0102  210 VAL A CG2 
1784 N  N   . LEU A 211 ? 0.0851 0.0851 0.0912 -0.0098 -0.0031 -0.0087 211 LEU A N   
1785 C  CA  . LEU A 211 ? 0.0829 0.1035 0.0847 -0.0076 0.0026  -0.0054 211 LEU A CA  
1786 C  C   . LEU A 211 ? 0.0733 0.1166 0.1022 -0.0060 -0.0013 0.0052  211 LEU A C   
1787 O  O   . LEU A 211 ? 0.0952 0.1094 0.0962 -0.0125 -0.0068 0.0076  211 LEU A O   
1788 C  CB  . LEU A 211 ? 0.1040 0.1077 0.0847 0.0000  -0.0052 -0.0034 211 LEU A CB  
1789 C  CG  . LEU A 211 ? 0.0865 0.1280 0.0921 0.0035  -0.0086 0.0017  211 LEU A CG  
1790 C  CD1 . LEU A 211 ? 0.1039 0.1635 0.1259 0.0040  -0.0329 0.0051  211 LEU A CD1 
1791 C  CD2 . LEU A 211 ? 0.0942 0.1395 0.1035 0.0052  0.0215  0.0147  211 LEU A CD2 
1792 N  N   . LYS A 212 ? 0.0829 0.1211 0.1054 -0.0199 0.0003  0.0125  212 LYS A N   
1793 C  CA  . LYS A 212 ? 0.1185 0.1234 0.1067 -0.0165 0.0074  0.0196  212 LYS A CA  
1794 C  C   . LYS A 212 ? 0.0934 0.1078 0.1211 -0.0103 -0.0093 0.0195  212 LYS A C   
1795 O  O   . LYS A 212 ? 0.1238 0.1137 0.1723 -0.0015 -0.0384 0.0340  212 LYS A O   
1796 C  CB  . LYS A 212 ? 0.1934 0.1770 0.0995 -0.0599 0.0048  0.0297  212 LYS A CB  
1797 C  CG  . LYS A 212 ? 0.2804 0.2415 0.1528 -0.0753 -0.0148 0.0710  212 LYS A CG  
1798 C  CD  . LYS A 212 ? 0.4345 0.2761 0.2287 -0.0361 0.0988  0.0361  212 LYS A CD  
1799 C  CE  . LYS A 212 ? 0.5159 0.7098 0.2919 0.0188  0.2492  -0.1151 212 LYS A CE  
1800 N  NZ  . LYS A 212 ? 0.7092 0.7439 0.8823 -0.3797 0.1640  -0.3368 212 LYS A NZ  
1801 N  N   A GLU A 213 ? 0.0864 0.1130 0.1111 -0.0153 -0.0087 0.0153  213 GLU A N   
1802 N  N   B GLU A 213 ? 0.0894 0.1097 0.1094 -0.0163 -0.0107 0.0163  213 GLU A N   
1803 C  CA  A GLU A 213 ? 0.1058 0.0999 0.1052 -0.0043 0.0013  0.0104  213 GLU A CA  
1804 C  CA  B GLU A 213 ? 0.1164 0.0955 0.1115 0.0007  -0.0160 0.0142  213 GLU A CA  
1805 C  C   A GLU A 213 ? 0.0913 0.0856 0.1076 -0.0068 -0.0049 0.0065  213 GLU A C   
1806 C  C   B GLU A 213 ? 0.0872 0.0997 0.1139 -0.0060 -0.0204 0.0164  213 GLU A C   
1807 O  O   A GLU A 213 ? 0.1032 0.0893 0.1094 0.0023  -0.0020 0.0082  213 GLU A O   
1808 O  O   B GLU A 213 ? 0.0840 0.1014 0.1154 -0.0027 0.0013  0.0160  213 GLU A O   
1809 C  CB  A GLU A 213 ? 0.0881 0.1518 0.1132 -0.0171 -0.0085 -0.0027 213 GLU A CB  
1810 C  CB  B GLU A 213 ? 0.0900 0.1093 0.1406 -0.0294 0.0057  0.0165  213 GLU A CB  
1811 C  CG  A GLU A 213 ? 0.1148 0.1137 0.1324 -0.0186 -0.0035 0.0164  213 GLU A CG  
1812 C  CG  B GLU A 213 ? 0.1032 0.1536 0.1757 0.0113  -0.0239 -0.0161 213 GLU A CG  
1813 C  CD  A GLU A 213 ? 0.1201 0.1387 0.1668 -0.0241 -0.0136 -0.0419 213 GLU A CD  
1814 C  CD  B GLU A 213 ? 0.1186 0.1368 0.2086 -0.0003 -0.0285 0.0186  213 GLU A CD  
1815 O  OE1 A GLU A 213 ? 0.1243 0.1650 0.1573 -0.0254 0.0073  -0.0198 213 GLU A OE1 
1816 O  OE1 B GLU A 213 ? 0.0834 0.1675 0.1587 0.0003  -0.0015 0.0164  213 GLU A OE1 
1817 O  OE2 A GLU A 213 ? 0.1616 0.1950 0.1731 0.0120  -0.0219 0.0076  213 GLU A OE2 
1818 O  OE2 B GLU A 213 ? 0.1476 0.2222 0.2725 -0.0421 -0.0445 -0.0017 213 GLU A OE2 
1819 N  N   A PRO A 214 ? 0.1035 0.0961 0.0937 0.0007  -0.0030 0.0178  214 PRO A N   
1820 N  N   B PRO A 214 ? 0.1066 0.0970 0.1058 -0.0181 -0.0098 0.0241  214 PRO A N   
1821 C  CA  A PRO A 214 ? 0.1181 0.0785 0.0926 -0.0119 -0.0120 0.0046  214 PRO A CA  
1822 C  CA  B PRO A 214 ? 0.1298 0.1005 0.1035 0.0073  -0.0141 0.0065  214 PRO A CA  
1823 C  C   A PRO A 214 ? 0.0956 0.0735 0.1172 0.0026  -0.0186 0.0027  214 PRO A C   
1824 C  C   B PRO A 214 ? 0.0945 0.1093 0.1287 0.0015  -0.0131 0.0103  214 PRO A C   
1825 O  O   A PRO A 214 ? 0.0988 0.1110 0.0981 0.0054  0.0003  -0.0136 214 PRO A O   
1826 O  O   B PRO A 214 ? 0.1106 0.1087 0.1352 -0.0164 -0.0076 0.0109  214 PRO A O   
1827 C  CB  A PRO A 214 ? 0.0812 0.0918 0.1378 -0.0091 -0.0219 0.0124  214 PRO A CB  
1828 C  CB  B PRO A 214 ? 0.1377 0.0996 0.1392 0.0098  0.0059  -0.0054 214 PRO A CB  
1829 C  CG  A PRO A 214 ? 0.0920 0.0899 0.1414 0.0010  -0.0043 0.0131  214 PRO A CG  
1830 C  CG  B PRO A 214 ? 0.1630 0.1494 0.1359 0.0318  0.0231  0.0131  214 PRO A CG  
1831 C  CD  A PRO A 214 ? 0.1034 0.0724 0.1326 -0.0077 -0.0163 -0.0043 214 PRO A CD  
1832 C  CD  B PRO A 214 ? 0.1066 0.0869 0.1562 -0.0027 0.0030  0.0262  214 PRO A CD  
1833 N  N   . ILE A 215 ? 0.1050 0.0886 0.1067 0.0005  -0.0099 -0.0020 215 ILE A N   
1834 C  CA  . ILE A 215 ? 0.1035 0.1014 0.0975 0.0010  -0.0082 -0.0137 215 ILE A CA  
1835 C  C   . ILE A 215 ? 0.1024 0.1027 0.0945 -0.0034 -0.0005 -0.0062 215 ILE A C   
1836 O  O   . ILE A 215 ? 0.1076 0.1041 0.1606 0.0046  -0.0085 -0.0209 215 ILE A O   
1837 C  CB  . ILE A 215 ? 0.1140 0.0960 0.1208 0.0265  -0.0062 -0.0038 215 ILE A CB  
1838 C  CG1 . ILE A 215 ? 0.1122 0.1115 0.1084 0.0188  -0.0037 -0.0027 215 ILE A CG1 
1839 C  CG2 . ILE A 215 ? 0.1208 0.1049 0.1234 0.0214  -0.0126 -0.0107 215 ILE A CG2 
1840 C  CD1 . ILE A 215 ? 0.1368 0.1199 0.1281 0.0164  0.0082  0.0136  215 ILE A CD1 
1841 N  N   A SER A 216 ? 0.1147 0.1043 0.1199 -0.0141 -0.0003 0.0013  216 SER A N   
1842 N  N   B SER A 216 ? 0.1225 0.0876 0.1010 0.0048  -0.0152 -0.0074 216 SER A N   
1843 C  CA  A SER A 216 ? 0.1136 0.1018 0.1168 0.0027  -0.0258 0.0023  216 SER A CA  
1844 C  CA  B SER A 216 ? 0.1088 0.1005 0.1136 -0.0020 -0.0232 -0.0344 216 SER A CA  
1845 C  C   A SER A 216 ? 0.1216 0.0908 0.0966 0.0006  -0.0357 -0.0118 216 SER A C   
1846 C  C   B SER A 216 ? 0.1156 0.0860 0.1137 -0.0043 -0.0242 -0.0088 216 SER A C   
1847 O  O   A SER A 216 ? 0.1019 0.1042 0.1206 -0.0043 -0.0175 0.0136  216 SER A O   
1848 O  O   B SER A 216 ? 0.1243 0.1030 0.1035 0.0024  -0.0087 0.0038  216 SER A O   
1849 C  CB  A SER A 216 ? 0.1973 0.0522 0.1685 -0.0333 -0.0384 0.0048  216 SER A CB  
1850 C  CB  B SER A 216 ? 0.1357 0.1245 0.1585 -0.0233 -0.0120 -0.0194 216 SER A CB  
1851 O  OG  A SER A 216 ? 0.1678 0.1404 0.1529 -0.0132 0.0031  0.0142  216 SER A OG  
1852 O  OG  B SER A 216 ? 0.2476 0.1360 0.1580 -0.0549 -0.0153 -0.0062 216 SER A OG  
1853 N  N   . VAL A 217 ? 0.1154 0.0895 0.1165 -0.0076 -0.0259 -0.0082 217 VAL A N   
1854 C  CA  . VAL A 217 ? 0.1078 0.0746 0.1228 0.0020  -0.0189 -0.0098 217 VAL A CA  
1855 C  C   . VAL A 217 ? 0.1156 0.0758 0.1101 -0.0093 -0.0254 -0.0082 217 VAL A C   
1856 O  O   . VAL A 217 ? 0.1341 0.0847 0.1313 -0.0110 -0.0254 -0.0043 217 VAL A O   
1857 C  CB  . VAL A 217 ? 0.1201 0.0776 0.1439 0.0000  -0.0276 -0.0063 217 VAL A CB  
1858 C  CG1 . VAL A 217 ? 0.1410 0.0830 0.1391 -0.0142 -0.0243 -0.0005 217 VAL A CG1 
1859 C  CG2 . VAL A 217 ? 0.1263 0.1093 0.1776 -0.0046 -0.0359 -0.0065 217 VAL A CG2 
1860 N  N   . SER A 218 ? 0.1243 0.0769 0.1123 -0.0173 -0.0167 -0.0087 218 SER A N   
1861 C  CA  . SER A 218 ? 0.1217 0.0805 0.1289 -0.0027 -0.0196 -0.0164 218 SER A CA  
1862 C  C   . SER A 218 ? 0.1282 0.0667 0.1122 -0.0099 -0.0219 0.0024  218 SER A C   
1863 O  O   . SER A 218 ? 0.1236 0.0812 0.1331 -0.0038 -0.0302 0.0057  218 SER A O   
1864 C  CB  . SER A 218 ? 0.1402 0.0955 0.1155 -0.0160 -0.0230 0.0060  218 SER A CB  
1865 O  OG  . SER A 218 ? 0.1201 0.1114 0.1367 -0.0046 -0.0285 -0.0006 218 SER A OG  
1866 N  N   . SER A 219 ? 0.1391 0.0750 0.1462 -0.0030 -0.0280 0.0038  219 SER A N   
1867 C  CA  . SER A 219 ? 0.1289 0.0768 0.1585 -0.0049 0.0060  0.0131  219 SER A CA  
1868 C  C   . SER A 219 ? 0.1219 0.0812 0.1747 -0.0031 -0.0153 0.0026  219 SER A C   
1869 O  O   . SER A 219 ? 0.1206 0.1063 0.1808 0.0031  -0.0102 0.0142  219 SER A O   
1870 C  CB  . SER A 219 ? 0.1676 0.0850 0.2266 -0.0027 -0.0186 0.0119  219 SER A CB  
1871 O  OG  . SER A 219 ? 0.1828 0.1086 0.1981 0.0080  -0.0065 -0.0137 219 SER A OG  
1872 N  N   . GLU A 220 ? 0.1312 0.0821 0.1547 -0.0082 -0.0153 -0.0119 220 GLU A N   
1873 C  CA  . GLU A 220 ? 0.1411 0.0892 0.1674 -0.0038 -0.0137 -0.0164 220 GLU A CA  
1874 C  C   . GLU A 220 ? 0.1247 0.1066 0.1209 0.0088  -0.0140 -0.0051 220 GLU A C   
1875 O  O   . GLU A 220 ? 0.1500 0.1348 0.1317 0.0142  0.0197  -0.0059 220 GLU A O   
1876 C  CB  . GLU A 220 ? 0.1467 0.1362 0.1506 0.0071  -0.0126 -0.0417 220 GLU A CB  
1877 C  CG  . GLU A 220 ? 0.1598 0.1598 0.1817 -0.0242 -0.0013 -0.0597 220 GLU A CG  
1878 C  CD  . GLU A 220 ? 0.2416 0.1216 0.2250 -0.0186 -0.0174 -0.0502 220 GLU A CD  
1879 O  OE1 . GLU A 220 ? 0.1704 0.1550 0.2091 -0.0370 0.0040  -0.0255 220 GLU A OE1 
1880 O  OE2 . GLU A 220 ? 0.3567 0.2079 0.3959 -0.1127 0.0103  -0.0957 220 GLU A OE2 
1881 N  N   . GLN A 221 ? 0.1172 0.0824 0.1216 -0.0006 -0.0057 -0.0098 221 GLN A N   
1882 C  CA  . GLN A 221 ? 0.1181 0.0823 0.1229 -0.0031 -0.0126 -0.0024 221 GLN A CA  
1883 C  C   . GLN A 221 ? 0.1171 0.0921 0.1296 0.0070  -0.0183 0.0027  221 GLN A C   
1884 O  O   . GLN A 221 ? 0.1166 0.1051 0.1254 0.0000  -0.0068 0.0137  221 GLN A O   
1885 C  CB  . GLN A 221 ? 0.1114 0.1014 0.0935 0.0026  -0.0131 -0.0219 221 GLN A CB  
1886 C  CG  . GLN A 221 ? 0.1078 0.0926 0.1199 0.0041  -0.0107 -0.0184 221 GLN A CG  
1887 C  CD  . GLN A 221 ? 0.1120 0.0842 0.1068 -0.0074 -0.0153 -0.0153 221 GLN A CD  
1888 O  OE1 . GLN A 221 ? 0.1128 0.0952 0.1051 0.0052  -0.0093 -0.0125 221 GLN A OE1 
1889 N  NE2 . GLN A 221 ? 0.1198 0.1058 0.1283 0.0154  -0.0092 0.0017  221 GLN A NE2 
1890 N  N   A VAL A 222 ? 0.1000 0.0961 0.1168 0.0041  -0.0092 0.0027  222 VAL A N   
1891 N  N   B VAL A 222 ? 0.1155 0.0707 0.1360 0.0073  -0.0197 0.0049  222 VAL A N   
1892 C  CA  A VAL A 222 ? 0.1005 0.1484 0.1307 -0.0119 -0.0162 0.0297  222 VAL A CA  
1893 C  CA  B VAL A 222 ? 0.1189 0.1164 0.1326 -0.0275 -0.0115 0.0292  222 VAL A CA  
1894 C  C   A VAL A 222 ? 0.1238 0.1107 0.1400 0.0065  -0.0130 0.0478  222 VAL A C   
1895 C  C   B VAL A 222 ? 0.1181 0.0995 0.1626 -0.0186 -0.0227 0.0228  222 VAL A C   
1896 O  O   A VAL A 222 ? 0.1307 0.0963 0.1282 0.0015  -0.0041 0.0148  222 VAL A O   
1897 O  O   B VAL A 222 ? 0.0961 0.1386 0.1292 -0.0171 0.0057  0.0031  222 VAL A O   
1898 C  CB  A VAL A 222 ? 0.1471 0.1430 0.1489 -0.0024 -0.0054 0.0240  222 VAL A CB  
1899 C  CB  B VAL A 222 ? 0.0759 0.1687 0.1438 0.0010  -0.0035 0.0399  222 VAL A CB  
1900 C  CG1 A VAL A 222 ? 0.1207 0.1430 0.2055 -0.0372 0.0019  -0.0276 222 VAL A CG1 
1901 C  CG1 B VAL A 222 ? 0.1344 0.2386 0.1221 0.0153  -0.0049 0.0355  222 VAL A CG1 
1902 C  CG2 A VAL A 222 ? 0.1878 0.1517 0.1219 -0.0125 -0.0515 0.0269  222 VAL A CG2 
1903 C  CG2 B VAL A 222 ? 0.2775 0.1912 0.2210 -0.0522 -0.0220 0.0092  222 VAL A CG2 
1904 N  N   A LEU A 223 ? 0.1199 0.1024 0.1748 0.0226  0.0026  0.0340  223 LEU A N   
1905 N  N   B LEU A 223 ? 0.1162 0.1136 0.1685 -0.0228 0.0054  0.0098  223 LEU A N   
1906 C  CA  A LEU A 223 ? 0.1098 0.1141 0.2255 -0.0041 0.0136  -0.0142 223 LEU A CA  
1907 C  CA  B LEU A 223 ? 0.1414 0.1280 0.2153 0.0051  0.0137  -0.0125 223 LEU A CA  
1908 C  C   A LEU A 223 ? 0.1297 0.1250 0.1686 -0.0026 -0.0164 -0.0082 223 LEU A C   
1909 C  C   B LEU A 223 ? 0.1274 0.1308 0.1685 -0.0006 -0.0164 -0.0124 223 LEU A C   
1910 O  O   A LEU A 223 ? 0.1183 0.1720 0.1800 0.0103  -0.0010 -0.0031 223 LEU A O   
1911 O  O   B LEU A 223 ? 0.1189 0.1699 0.1802 0.0087  0.0000  -0.0023 223 LEU A O   
1912 C  CB  A LEU A 223 ? 0.2476 0.1562 0.2874 -0.0794 0.0436  -0.0595 223 LEU A CB  
1913 C  CB  B LEU A 223 ? 0.1260 0.1067 0.2985 0.0351  0.0746  -0.0719 223 LEU A CB  
1914 C  CG  A LEU A 223 ? 0.2343 0.1951 0.2597 -0.0097 0.0379  -0.0847 223 LEU A CG  
1915 C  CG  B LEU A 223 ? 0.2714 0.1832 0.3684 -0.0838 -0.0137 0.0307  223 LEU A CG  
1916 C  CD1 A LEU A 223 ? 0.1605 0.3625 0.4101 -0.0834 0.0230  -0.0579 223 LEU A CD1 
1917 C  CD1 B LEU A 223 ? 0.1085 0.2027 0.3607 0.0842  -0.0728 -0.0271 223 LEU A CD1 
1918 C  CD2 A LEU A 223 ? 0.2083 0.1327 0.4972 0.0342  0.1797  -0.0750 223 LEU A CD2 
1919 C  CD2 B LEU A 223 ? 0.4796 0.1263 0.5889 -0.0189 -0.0291 -0.1035 223 LEU A CD2 
1920 N  N   . LYS A 224 ? 0.1250 0.1251 0.1344 0.0131  0.0000  -0.0076 224 LYS A N   
1921 C  CA  . LYS A 224 ? 0.1448 0.1535 0.1536 -0.0020 -0.0299 0.0153  224 LYS A CA  
1922 C  C   . LYS A 224 ? 0.1259 0.1139 0.1247 0.0250  0.0065  -0.0006 224 LYS A C   
1923 O  O   . LYS A 224 ? 0.1412 0.1491 0.1175 0.0043  0.0023  0.0088  224 LYS A O   
1924 C  CB  . LYS A 224 ? 0.1617 0.1958 0.1677 0.0082  -0.0474 0.0305  224 LYS A CB  
1925 C  CG  . LYS A 224 ? 0.1429 0.2838 0.2167 -0.0253 -0.0252 0.0243  224 LYS A CG  
1926 C  CD  . LYS A 224 ? 0.1738 0.4787 0.3303 0.0210  -0.0335 -0.0476 224 LYS A CD  
1927 C  CE  . LYS A 224 ? 0.4356 0.2854 0.5511 0.0772  -0.3467 -0.1133 224 LYS A CE  
1928 N  NZ  . LYS A 224 ? 0.5655 0.3174 0.5504 0.0000  -0.0798 -0.2520 224 LYS A NZ  
1929 N  N   . PHE A 225 ? 0.1270 0.1146 0.1014 0.0186  0.0135  0.0046  225 PHE A N   
1930 C  CA  . PHE A 225 ? 0.1172 0.0952 0.1079 0.0178  0.0173  0.0000  225 PHE A CA  
1931 C  C   . PHE A 225 ? 0.1484 0.1023 0.1024 -0.0031 0.0043  -0.0043 225 PHE A C   
1932 O  O   . PHE A 225 ? 0.1287 0.1128 0.1142 -0.0037 0.0082  -0.0082 225 PHE A O   
1933 C  CB  . PHE A 225 ? 0.1254 0.1085 0.1123 0.0302  0.0240  -0.0006 225 PHE A CB  
1934 C  CG  . PHE A 225 ? 0.1044 0.0961 0.1307 0.0062  0.0120  -0.0040 225 PHE A CG  
1935 C  CD1 . PHE A 225 ? 0.1404 0.1546 0.1616 0.0445  0.0199  0.0052  225 PHE A CD1 
1936 C  CD2 . PHE A 225 ? 0.1422 0.1748 0.1436 0.0310  0.0049  -0.0225 225 PHE A CD2 
1937 C  CE1 . PHE A 225 ? 0.1529 0.1640 0.1622 0.0373  0.0417  0.0307  225 PHE A CE1 
1938 C  CE2 . PHE A 225 ? 0.1449 0.2068 0.1817 0.0306  -0.0120 -0.0456 225 PHE A CE2 
1939 C  CZ  . PHE A 225 ? 0.1291 0.1360 0.1888 -0.0065 -0.0038 -0.0551 225 PHE A CZ  
1940 N  N   . ARG A 226 ? 0.1136 0.1022 0.1183 0.0207  0.0019  0.0052  226 ARG A N   
1941 C  CA  . ARG A 226 ? 0.1208 0.1350 0.1186 0.0315  0.0170  0.0142  226 ARG A CA  
1942 C  C   . ARG A 226 ? 0.1215 0.1172 0.1280 0.0175  0.0126  0.0086  226 ARG A C   
1943 O  O   . ARG A 226 ? 0.1327 0.1607 0.1427 0.0308  0.0208  -0.0098 226 ARG A O   
1944 C  CB  . ARG A 226 ? 0.1308 0.1158 0.1174 0.0172  0.0043  -0.0049 226 ARG A CB  
1945 C  CG  . ARG A 226 ? 0.1225 0.1230 0.1101 0.0085  -0.0012 0.0013  226 ARG A CG  
1946 C  CD  . ARG A 226 ? 0.1872 0.1252 0.1351 0.0238  -0.0087 -0.0031 226 ARG A CD  
1947 N  NE  . ARG A 226 ? 0.1305 0.1140 0.1043 0.0136  -0.0103 0.0019  226 ARG A NE  
1948 C  CZ  . ARG A 226 ? 0.1656 0.1312 0.1313 -0.0164 -0.0091 -0.0309 226 ARG A CZ  
1949 N  NH1 . ARG A 226 ? 0.1879 0.1756 0.2131 -0.0645 0.0065  -0.0640 226 ARG A NH1 
1950 N  NH2 . ARG A 226 ? 0.2250 0.1650 0.1466 -0.0617 0.0373  -0.0412 226 ARG A NH2 
1951 N  N   . LYS A 227 ? 0.1448 0.1298 0.0926 0.0010  0.0071  -0.0162 227 LYS A N   
1952 C  CA  . LYS A 227 ? 0.1384 0.1468 0.1087 -0.0121 0.0081  -0.0182 227 LYS A CA  
1953 C  C   . LYS A 227 ? 0.1334 0.1590 0.0882 -0.0060 0.0098  -0.0156 227 LYS A C   
1954 O  O   . LYS A 227 ? 0.1580 0.1621 0.1001 -0.0043 0.0187  -0.0147 227 LYS A O   
1955 C  CB  . LYS A 227 ? 0.1527 0.1897 0.1137 -0.0197 0.0052  -0.0241 227 LYS A CB  
1956 C  CG  . LYS A 227 ? 0.2201 0.1991 0.2486 -0.0732 -0.0065 -0.0579 227 LYS A CG  
1957 C  CD  . LYS A 227 ? 0.3009 0.3463 0.4187 -0.0697 -0.1032 -0.1129 227 LYS A CD  
1958 C  CE  . LYS A 227 ? 0.4910 0.4604 0.5084 -0.1439 -0.1600 -0.1032 227 LYS A CE  
1959 N  NZ  . LYS A 227 ? 0.5792 0.8004 0.6265 -0.1298 -0.4124 -0.1262 227 LYS A NZ  
1960 N  N   . LEU A 228 ? 0.1335 0.1261 0.1050 -0.0063 -0.0006 -0.0162 228 LEU A N   
1961 C  CA  . LEU A 228 ? 0.1084 0.1254 0.1051 0.0020  0.0137  -0.0148 228 LEU A CA  
1962 C  C   . LEU A 228 ? 0.1180 0.1189 0.1051 -0.0006 0.0178  -0.0148 228 LEU A C   
1963 O  O   . LEU A 228 ? 0.1321 0.1185 0.1060 0.0020  0.0015  -0.0027 228 LEU A O   
1964 C  CB  . LEU A 228 ? 0.1155 0.1253 0.1146 0.0207  0.0063  -0.0219 228 LEU A CB  
1965 C  CG  . LEU A 228 ? 0.1067 0.1387 0.1033 0.0142  -0.0043 0.0019  228 LEU A CG  
1966 C  CD1 . LEU A 228 ? 0.1133 0.1500 0.1107 0.0140  0.0043  -0.0126 228 LEU A CD1 
1967 C  CD2 . LEU A 228 ? 0.1336 0.1703 0.1278 0.0225  0.0037  0.0232  228 LEU A CD2 
1968 N  N   . ASN A 229 ? 0.1180 0.1289 0.0986 0.0142  0.0120  -0.0071 229 ASN A N   
1969 C  CA  . ASN A 229 ? 0.1227 0.1316 0.0882 -0.0034 0.0104  -0.0182 229 ASN A CA  
1970 C  C   . ASN A 229 ? 0.1190 0.1183 0.1027 0.0126  0.0273  -0.0013 229 ASN A C   
1971 O  O   . ASN A 229 ? 0.1224 0.1247 0.1137 0.0031  0.0159  -0.0031 229 ASN A O   
1972 C  CB  . ASN A 229 ? 0.1189 0.1580 0.1234 0.0000  0.0351  -0.0210 229 ASN A CB  
1973 C  CG  . ASN A 229 ? 0.1553 0.1925 0.0991 0.0303  0.0080  -0.0178 229 ASN A CG  
1974 O  OD1 . ASN A 229 ? 0.3179 0.2167 0.1371 0.0485  0.0649  -0.0182 229 ASN A OD1 
1975 N  ND2 . ASN A 229 ? 0.1887 0.2050 0.1611 -0.0097 0.0368  -0.0644 229 ASN A ND2 
1976 N  N   . PHE A 230 ? 0.1253 0.1263 0.1112 0.0026  0.0137  -0.0093 230 PHE A N   
1977 C  CA  . PHE A 230 ? 0.1220 0.1341 0.1165 -0.0017 0.0182  0.0034  230 PHE A CA  
1978 C  C   . PHE A 230 ? 0.1326 0.1151 0.1154 -0.0163 0.0052  0.0000  230 PHE A C   
1979 O  O   . PHE A 230 ? 0.1410 0.1211 0.1282 -0.0017 0.0283  -0.0015 230 PHE A O   
1980 C  CB  . PHE A 230 ? 0.1199 0.1422 0.1216 -0.0006 0.0174  0.0086  230 PHE A CB  
1981 C  CG  . PHE A 230 ? 0.1119 0.1254 0.1078 -0.0109 0.0098  -0.0109 230 PHE A CG  
1982 C  CD1 . PHE A 230 ? 0.1386 0.1224 0.1151 -0.0104 0.0163  -0.0137 230 PHE A CD1 
1983 C  CD2 . PHE A 230 ? 0.1411 0.1415 0.1137 0.0030  -0.0012 0.0017  230 PHE A CD2 
1984 C  CE1 . PHE A 230 ? 0.1404 0.1376 0.1052 -0.0185 0.0102  -0.0065 230 PHE A CE1 
1985 C  CE2 . PHE A 230 ? 0.1243 0.1524 0.1215 0.0076  0.0185  -0.0041 230 PHE A CE2 
1986 C  CZ  . PHE A 230 ? 0.1283 0.1360 0.1127 -0.0182 0.0031  -0.0163 230 PHE A CZ  
1987 N  N   . ASN A 231 ? 0.1254 0.1406 0.1210 0.0057  0.0249  -0.0017 231 ASN A N   
1988 C  CA  . ASN A 231 ? 0.1280 0.1307 0.1127 -0.0062 0.0305  0.0137  231 ASN A CA  
1989 C  C   . ASN A 231 ? 0.1392 0.1289 0.1296 -0.0057 0.0172  -0.0038 231 ASN A C   
1990 O  O   . ASN A 231 ? 0.1439 0.1262 0.1360 0.0074  0.0215  0.0071  231 ASN A O   
1991 C  CB  . ASN A 231 ? 0.1483 0.1439 0.1437 -0.0013 0.0271  -0.0027 231 ASN A CB  
1992 C  CG  . ASN A 231 ? 0.1494 0.1375 0.1230 0.0226  0.0231  0.0057  231 ASN A CG  
1993 O  OD1 . ASN A 231 ? 0.1412 0.1242 0.1616 0.0188  0.0335  -0.0108 231 ASN A OD1 
1994 N  ND2 . ASN A 231 ? 0.2154 0.1552 0.1553 0.0328  -0.0086 -0.0178 231 ASN A ND2 
1995 N  N   . GLY A 232 ? 0.1579 0.1454 0.1251 0.0051  0.0480  0.0110  232 GLY A N   
1996 C  CA  . GLY A 232 ? 0.1573 0.1330 0.1509 0.0135  0.0379  -0.0057 232 GLY A CA  
1997 C  C   . GLY A 232 ? 0.1985 0.1379 0.1303 0.0310  0.0249  0.0406  232 GLY A C   
1998 O  O   . GLY A 232 ? 0.2117 0.1564 0.1512 0.0195  0.0399  0.0098  232 GLY A O   
1999 N  N   . GLU A 233 ? 0.2244 0.1612 0.1371 0.0015  0.0399  0.0120  233 GLU A N   
2000 C  CA  . GLU A 233 ? 0.2417 0.1641 0.1360 0.0037  0.0302  0.0104  233 GLU A CA  
2001 C  C   . GLU A 233 ? 0.2381 0.1835 0.1336 -0.0120 0.0542  -0.0049 233 GLU A C   
2002 O  O   . GLU A 233 ? 0.2597 0.1773 0.1929 -0.0010 0.0688  0.0148  233 GLU A O   
2003 C  CB  . GLU A 233 ? 0.1885 0.2368 0.1957 0.0063  0.0074  0.0160  233 GLU A CB  
2004 C  CG  . GLU A 233 ? 0.3445 0.2921 0.1586 0.0335  0.0736  0.0177  233 GLU A CG  
2005 C  CD  . GLU A 233 ? 0.4582 0.5102 0.4508 0.0549  -0.0724 0.0895  233 GLU A CD  
2006 O  OE1 . GLU A 233 ? 0.3079 0.5995 0.2480 -0.0174 0.0467  0.0851  233 GLU A OE1 
2007 O  OE2 . GLU A 233 ? 0.6473 0.3984 0.5202 -0.1968 -0.0531 0.0082  233 GLU A OE2 
2008 N  N   . GLY A 234 ? 0.3086 0.2718 0.1850 0.1093  0.0381  -0.0193 234 GLY A N   
2009 C  CA  . GLY A 234 ? 0.3400 0.3416 0.2022 0.1212  0.0310  -0.0205 234 GLY A CA  
2010 C  C   . GLY A 234 ? 0.2912 0.2827 0.1964 0.1088  0.0745  -0.0013 234 GLY A C   
2011 O  O   . GLY A 234 ? 0.3959 0.6927 0.2298 0.2623  0.1146  -0.0627 234 GLY A O   
2012 N  N   . GLU A 235 ? 0.2635 0.1835 0.1483 0.0516  0.0450  0.0098  235 GLU A N   
2013 C  CA  . GLU A 235 ? 0.2113 0.1545 0.1693 0.0303  0.0518  0.0226  235 GLU A CA  
2014 C  C   . GLU A 235 ? 0.1897 0.1729 0.1440 0.0240  0.0428  0.0038  235 GLU A C   
2015 O  O   . GLU A 235 ? 0.1923 0.1704 0.1598 0.0346  0.0152  0.0027  235 GLU A O   
2016 C  CB  . GLU A 235 ? 0.2183 0.1553 0.1647 -0.0054 0.0340  -0.0068 235 GLU A CB  
2017 C  CG  . GLU A 235 ? 0.3540 0.1744 0.2694 -0.0241 0.1298  -0.0137 235 GLU A CG  
2018 C  CD  . GLU A 235 ? 0.5048 0.1615 0.3364 -0.1133 0.1141  -0.0351 235 GLU A CD  
2019 O  OE1 . GLU A 235 ? 0.2119 0.2298 0.3208 0.0034  0.0273  0.0603  235 GLU A OE1 
2020 O  OE2 . GLU A 235 ? 0.6776 0.1712 0.4934 -0.0516 0.2451  -0.0293 235 GLU A OE2 
2021 N  N   . PRO A 236 ? 0.1737 0.1432 0.1714 0.0259  0.0320  0.0107  236 PRO A N   
2022 C  CA  . PRO A 236 ? 0.1500 0.1570 0.1553 0.0020  0.0386  0.0052  236 PRO A CA  
2023 C  C   . PRO A 236 ? 0.1446 0.1316 0.1595 0.0259  0.0375  0.0046  236 PRO A C   
2024 O  O   . PRO A 236 ? 0.1527 0.1614 0.1500 0.0000  0.0355  -0.0238 236 PRO A O   
2025 C  CB  . PRO A 236 ? 0.1333 0.1740 0.2022 0.0240  0.0379  0.0189  236 PRO A CB  
2026 C  CG  . PRO A 236 ? 0.1684 0.1817 0.2138 0.0188  0.0623  0.0227  236 PRO A CG  
2027 C  CD  . PRO A 236 ? 0.1490 0.1807 0.2246 0.0038  0.0348  0.0320  236 PRO A CD  
2028 N  N   . GLU A 237 ? 0.1525 0.1555 0.1494 0.0065  0.0480  -0.0153 237 GLU A N   
2029 C  CA  . GLU A 237 ? 0.1412 0.1283 0.1334 0.0156  0.0291  -0.0065 237 GLU A CA  
2030 C  C   . GLU A 237 ? 0.1553 0.1298 0.1306 0.0176  0.0214  -0.0082 237 GLU A C   
2031 O  O   . GLU A 237 ? 0.1624 0.1342 0.1402 0.0306  0.0174  -0.0118 237 GLU A O   
2032 C  CB  . GLU A 237 ? 0.1703 0.1324 0.1247 0.0237  0.0238  -0.0153 237 GLU A CB  
2033 C  CG  . GLU A 237 ? 0.1640 0.1782 0.2018 -0.0082 0.0076  -0.0082 237 GLU A CG  
2034 C  CD  . GLU A 237 ? 0.2399 0.3106 0.2264 -0.0253 -0.0377 0.0255  237 GLU A CD  
2035 O  OE1 . GLU A 237 ? 0.4622 0.2840 0.2205 -0.0766 -0.0965 -0.0198 237 GLU A OE1 
2036 O  OE2 . GLU A 237 ? 0.3115 0.4981 0.2770 -0.1682 -0.0802 0.1383  237 GLU A OE2 
2037 N  N   . GLU A 238 ? 0.1281 0.1288 0.1439 0.0148  0.0408  -0.0087 238 GLU A N   
2038 C  CA  . GLU A 238 ? 0.1277 0.1270 0.1298 0.0098  0.0237  -0.0110 238 GLU A CA  
2039 C  C   . GLU A 238 ? 0.1184 0.1210 0.1016 0.0209  0.0310  -0.0043 238 GLU A C   
2040 O  O   . GLU A 238 ? 0.1397 0.1199 0.1573 0.0188  0.0261  0.0020  238 GLU A O   
2041 C  CB  . GLU A 238 ? 0.1418 0.1754 0.1536 0.0041  0.0200  -0.0043 238 GLU A CB  
2042 C  CG  . GLU A 238 ? 0.1642 0.1964 0.1642 0.0046  0.0208  -0.0060 238 GLU A CG  
2043 C  CD  . GLU A 238 ? 0.1937 0.1773 0.1896 -0.0092 0.0214  -0.0187 238 GLU A CD  
2044 O  OE1 . GLU A 238 ? 0.2655 0.2635 0.2027 -0.0463 0.0073  -0.0573 238 GLU A OE1 
2045 O  OE2 . GLU A 238 ? 0.1985 0.2291 0.1738 -0.0086 0.0057  -0.0005 238 GLU A OE2 
2046 N  N   A LEU A 239 ? 0.1172 0.1226 0.1102 0.0126  0.0204  -0.0052 239 LEU A N   
2047 N  N   B LEU A 239 ? 0.1340 0.1281 0.1199 0.0076  0.0137  -0.0104 239 LEU A N   
2048 C  CA  A LEU A 239 ? 0.0988 0.1206 0.0980 -0.0013 0.0284  -0.0035 239 LEU A CA  
2049 C  CA  B LEU A 239 ? 0.1185 0.1533 0.1287 0.0304  0.0017  -0.0275 239 LEU A CA  
2050 C  C   A LEU A 239 ? 0.0979 0.1163 0.1066 -0.0126 0.0142  0.0034  239 LEU A C   
2051 C  C   B LEU A 239 ? 0.1104 0.1757 0.1102 0.0118  0.0031  -0.0077 239 LEU A C   
2052 O  O   A LEU A 239 ? 0.0900 0.1067 0.1018 0.0098  0.0326  0.0046  239 LEU A O   
2053 O  O   B LEU A 239 ? 0.1362 0.1597 0.1171 0.0203  0.0003  -0.0063 239 LEU A O   
2054 C  CB  A LEU A 239 ? 0.0876 0.1360 0.1465 -0.0135 0.0346  0.0082  239 LEU A CB  
2055 C  CB  B LEU A 239 ? 0.1462 0.1371 0.1516 0.0273  -0.0270 0.0034  239 LEU A CB  
2056 C  CG  A LEU A 239 ? 0.1138 0.1252 0.1419 0.0186  0.0160  -0.0129 239 LEU A CG  
2057 C  CG  B LEU A 239 ? 0.1217 0.1802 0.1629 0.0187  0.0087  -0.0331 239 LEU A CG  
2058 C  CD1 A LEU A 239 ? 0.2011 0.1562 0.2565 -0.0063 -0.0285 0.0307  239 LEU A CD1 
2059 C  CD1 B LEU A 239 ? 0.1254 0.1243 0.1034 0.0333  -0.0120 -0.0161 239 LEU A CD1 
2060 C  CD2 A LEU A 239 ? 0.1128 0.1459 0.0935 0.0274  -0.0172 -0.0753 239 LEU A CD2 
2061 C  CD2 B LEU A 239 ? 0.3476 0.1582 0.2716 -0.0406 -0.0176 0.0098  239 LEU A CD2 
2062 N  N   . MET A 240 ? 0.1131 0.1445 0.1000 0.0148  0.0183  -0.0121 240 MET A N   
2063 C  CA  . MET A 240 ? 0.1291 0.1367 0.0900 0.0211  0.0193  0.0060  240 MET A CA  
2064 C  C   . MET A 240 ? 0.1032 0.1139 0.1023 -0.0017 0.0196  -0.0118 240 MET A C   
2065 O  O   . MET A 240 ? 0.1062 0.1430 0.1031 0.0076  0.0098  -0.0046 240 MET A O   
2066 C  CB  . MET A 240 ? 0.1141 0.1192 0.1104 0.0151  0.0326  -0.0038 240 MET A CB  
2067 C  CG  . MET A 240 ? 0.1317 0.1351 0.0988 0.0082  0.0265  0.0065  240 MET A CG  
2068 S  SD  . MET A 240 ? 0.1254 0.1289 0.1307 0.0013  0.0222  -0.0024 240 MET A SD  
2069 C  CE  . MET A 240 ? 0.1588 0.1280 0.1252 -0.0099 0.0291  -0.0049 240 MET A CE  
2070 N  N   . VAL A 241 ? 0.1105 0.1066 0.0970 0.0060  -0.0006 0.0051  241 VAL A N   
2071 C  CA  . VAL A 241 ? 0.1150 0.1061 0.0821 0.0080  0.0104  -0.0082 241 VAL A CA  
2072 C  C   . VAL A 241 ? 0.1014 0.0856 0.0900 0.0208  0.0098  -0.0205 241 VAL A C   
2073 O  O   . VAL A 241 ? 0.0895 0.1162 0.1133 0.0017  0.0068  -0.0148 241 VAL A O   
2074 C  CB  . VAL A 241 ? 0.1050 0.1215 0.1238 0.0003  -0.0086 -0.0272 241 VAL A CB  
2075 C  CG1 . VAL A 241 ? 0.1362 0.1515 0.1191 -0.0015 -0.0156 -0.0434 241 VAL A CG1 
2076 C  CG2 . VAL A 241 ? 0.1290 0.1300 0.1456 0.0366  0.0163  -0.0135 241 VAL A CG2 
2077 N  N   . ASP A 242 ? 0.0961 0.1005 0.0731 0.0109  0.0108  -0.0126 242 ASP A N   
2078 C  CA  . ASP A 242 ? 0.1115 0.0948 0.0893 0.0186  -0.0049 -0.0175 242 ASP A CA  
2079 C  C   . ASP A 242 ? 0.0913 0.0957 0.0920 0.0087  0.0005  -0.0006 242 ASP A C   
2080 O  O   . ASP A 242 ? 0.1070 0.1014 0.1351 0.0104  -0.0197 -0.0093 242 ASP A O   
2081 C  CB  . ASP A 242 ? 0.1053 0.0855 0.1269 0.0209  0.0059  -0.0118 242 ASP A CB  
2082 C  CG  . ASP A 242 ? 0.1122 0.0952 0.1048 0.0248  -0.0010 -0.0187 242 ASP A CG  
2083 O  OD1 . ASP A 242 ? 0.1087 0.0908 0.1146 0.0131  0.0038  -0.0074 242 ASP A OD1 
2084 O  OD2 . ASP A 242 ? 0.1427 0.0998 0.1474 0.0206  0.0186  -0.0219 242 ASP A OD2 
2085 N  N   . ASN A 243 ? 0.0979 0.0812 0.0822 0.0132  0.0159  -0.0065 243 ASN A N   
2086 C  CA  . ASN A 243 ? 0.0974 0.0908 0.0781 0.0000  0.0003  -0.0038 243 ASN A CA  
2087 C  C   . ASN A 243 ? 0.0847 0.0857 0.0856 -0.0048 -0.0027 0.0005  243 ASN A C   
2088 O  O   . ASN A 243 ? 0.1146 0.1111 0.0978 0.0265  0.0126  0.0024  243 ASN A O   
2089 C  CB  . ASN A 243 ? 0.0917 0.0944 0.0917 -0.0098 0.0054  0.0043  243 ASN A CB  
2090 C  CG  . ASN A 243 ? 0.0806 0.1049 0.0846 -0.0147 0.0140  0.0041  243 ASN A CG  
2091 O  OD1 . ASN A 243 ? 0.0806 0.1032 0.1314 0.0030  0.0102  0.0092  243 ASN A OD1 
2092 N  ND2 . ASN A 243 ? 0.0961 0.1186 0.1318 0.0000  -0.0071 0.0271  243 ASN A ND2 
2093 N  N   . TRP A 244 ? 0.0831 0.0952 0.0789 -0.0024 0.0013  -0.0012 244 TRP A N   
2094 C  CA  . TRP A 244 ? 0.0864 0.1071 0.0705 0.0109  0.0037  -0.0010 244 TRP A CA  
2095 C  C   . TRP A 244 ? 0.0900 0.0910 0.0819 0.0048  0.0074  -0.0038 244 TRP A C   
2096 O  O   . TRP A 244 ? 0.0910 0.1192 0.1114 0.0218  -0.0052 -0.0221 244 TRP A O   
2097 C  CB  . TRP A 244 ? 0.0916 0.0807 0.0918 0.0087  0.0085  -0.0092 244 TRP A CB  
2098 C  CG  . TRP A 244 ? 0.0715 0.0856 0.0909 0.0013  0.0085  -0.0019 244 TRP A CG  
2099 C  CD1 . TRP A 244 ? 0.0806 0.0946 0.1049 -0.0005 0.0030  -0.0027 244 TRP A CD1 
2100 C  CD2 . TRP A 244 ? 0.0830 0.0952 0.0798 0.0074  0.0226  0.0126  244 TRP A CD2 
2101 N  NE1 . TRP A 244 ? 0.1009 0.0893 0.1005 0.0049  -0.0043 -0.0006 244 TRP A NE1 
2102 C  CE2 . TRP A 244 ? 0.0869 0.0991 0.1045 0.0054  0.0098  -0.0006 244 TRP A CE2 
2103 C  CE3 . TRP A 244 ? 0.0995 0.1165 0.0866 0.0051  0.0024  0.0120  244 TRP A CE3 
2104 C  CZ2 . TRP A 244 ? 0.1010 0.1094 0.1277 0.0146  0.0131  0.0000  244 TRP A CZ2 
2105 C  CZ3 . TRP A 244 ? 0.1120 0.1059 0.1246 0.0119  0.0038  0.0196  244 TRP A CZ3 
2106 C  CH2 . TRP A 244 ? 0.1202 0.1237 0.1151 0.0186  0.0026  0.0156  244 TRP A CH2 
2107 N  N   . ARG A 245 ? 0.0891 0.1005 0.0945 0.0000  -0.0020 -0.0151 245 ARG A N   
2108 C  CA  . ARG A 245 ? 0.0875 0.0970 0.0935 -0.0076 -0.0065 -0.0093 245 ARG A CA  
2109 C  C   . ARG A 245 ? 0.0865 0.0855 0.1018 0.0043  -0.0013 -0.0109 245 ARG A C   
2110 O  O   . ARG A 245 ? 0.0918 0.0996 0.1023 0.0015  0.0082  -0.0027 245 ARG A O   
2111 C  CB  . ARG A 245 ? 0.0902 0.0898 0.0930 -0.0017 -0.0057 -0.0046 245 ARG A CB  
2112 C  CG  . ARG A 245 ? 0.0825 0.1066 0.1044 -0.0110 -0.0054 -0.0012 245 ARG A CG  
2113 C  CD  . ARG A 245 ? 0.0807 0.1087 0.1079 -0.0020 -0.0024 -0.0148 245 ARG A CD  
2114 N  NE  . ARG A 245 ? 0.0779 0.1076 0.1080 -0.0208 0.0096  -0.0129 245 ARG A NE  
2115 C  CZ  . ARG A 245 ? 0.0864 0.1136 0.0935 -0.0176 0.0097  -0.0076 245 ARG A CZ  
2116 N  NH1 . ARG A 245 ? 0.0999 0.1162 0.1097 -0.0110 0.0148  -0.0085 245 ARG A NH1 
2117 N  NH2 . ARG A 245 ? 0.0858 0.1455 0.1256 -0.0322 0.0125  -0.0087 245 ARG A NH2 
2118 N  N   . PRO A 246 ? 0.0907 0.1060 0.0970 0.0027  0.0099  -0.0024 246 PRO A N   
2119 C  CA  . PRO A 246 ? 0.1217 0.1059 0.1050 0.0081  -0.0071 0.0019  246 PRO A CA  
2120 C  C   . PRO A 246 ? 0.0988 0.1146 0.0898 0.0152  -0.0174 0.0027  246 PRO A C   
2121 O  O   . PRO A 246 ? 0.1136 0.1025 0.0982 0.0019  -0.0074 -0.0026 246 PRO A O   
2122 C  CB  . PRO A 246 ? 0.1419 0.1303 0.1300 0.0350  0.0146  0.0037  246 PRO A CB  
2123 C  CG  . PRO A 246 ? 0.1816 0.2134 0.2250 0.0623  0.0405  0.0969  246 PRO A CG  
2124 C  CD  . PRO A 246 ? 0.0908 0.1506 0.1458 0.0414  0.0060  0.0209  246 PRO A CD  
2125 N  N   . ALA A 247 ? 0.1107 0.1145 0.1023 0.0082  0.0020  0.0092  247 ALA A N   
2126 C  CA  . ALA A 247 ? 0.1201 0.1260 0.0830 -0.0043 -0.0003 0.0000  247 ALA A CA  
2127 C  C   . ALA A 247 ? 0.0942 0.1049 0.1042 0.0126  0.0060  0.0153  247 ALA A C   
2128 O  O   . ALA A 247 ? 0.1195 0.1253 0.1224 0.0337  -0.0093 -0.0068 247 ALA A O   
2129 C  CB  . ALA A 247 ? 0.1352 0.1318 0.1259 0.0082  0.0186  0.0043  247 ALA A CB  
2130 N  N   . GLN A 248 ? 0.0962 0.0989 0.1005 0.0017  0.0041  0.0020  248 GLN A N   
2131 C  CA  . GLN A 248 ? 0.0908 0.1054 0.1077 0.0012  -0.0013 0.0031  248 GLN A CA  
2132 C  C   . GLN A 248 ? 0.1007 0.1177 0.1089 0.0320  -0.0104 -0.0006 248 GLN A C   
2133 O  O   . GLN A 248 ? 0.1067 0.1368 0.1124 0.0219  0.0109  0.0049  248 GLN A O   
2134 C  CB  . GLN A 248 ? 0.1059 0.1172 0.1078 -0.0024 0.0000  0.0082  248 GLN A CB  
2135 C  CG  . GLN A 248 ? 0.1159 0.1322 0.1058 -0.0152 0.0076  0.0024  248 GLN A CG  
2136 C  CD  . GLN A 248 ? 0.0987 0.1483 0.1158 -0.0071 0.0063  0.0093  248 GLN A CD  
2137 O  OE1 . GLN A 248 ? 0.0991 0.1982 0.1533 -0.0283 0.0148  -0.0204 248 GLN A OE1 
2138 N  NE2 . GLN A 248 ? 0.1312 0.1655 0.1007 0.0020  0.0113  0.0043  248 GLN A NE2 
2139 N  N   . PRO A 249 ? 0.1255 0.1343 0.1095 0.0335  -0.0062 0.0063  249 PRO A N   
2140 C  CA  . PRO A 249 ? 0.1243 0.1597 0.1149 0.0357  -0.0115 0.0215  249 PRO A CA  
2141 C  C   . PRO A 249 ? 0.1321 0.1352 0.0957 0.0260  -0.0209 -0.0006 249 PRO A C   
2142 O  O   . PRO A 249 ? 0.1058 0.1432 0.1207 0.0280  -0.0109 0.0120  249 PRO A O   
2143 C  CB  . PRO A 249 ? 0.1405 0.2347 0.1289 0.0689  -0.0375 -0.0147 249 PRO A CB  
2144 C  CG  . PRO A 249 ? 0.1626 0.3113 0.1499 0.0403  -0.0430 -0.0671 249 PRO A CG  
2145 C  CD  . PRO A 249 ? 0.0869 0.2180 0.1423 0.0326  -0.0092 -0.0151 249 PRO A CD  
2146 N  N   . LEU A 250 ? 0.1523 0.1368 0.0890 0.0296  0.0071  0.0060  250 LEU A N   
2147 C  CA  . LEU A 250 ? 0.1212 0.1271 0.1140 0.0109  0.0000  0.0000  250 LEU A CA  
2148 C  C   . LEU A 250 ? 0.1217 0.1280 0.0961 0.0260  0.0065  0.0087  250 LEU A C   
2149 O  O   . LEU A 250 ? 0.1312 0.1263 0.1305 0.0255  -0.0285 0.0020  250 LEU A O   
2150 C  CB  . LEU A 250 ? 0.1624 0.1466 0.1449 0.0068  0.0264  -0.0005 250 LEU A CB  
2151 C  CG  . LEU A 250 ? 0.1437 0.1868 0.1413 -0.0209 0.0275  -0.0294 250 LEU A CG  
2152 C  CD1 . LEU A 250 ? 0.1462 0.1949 0.1368 -0.0193 0.0065  -0.0274 250 LEU A CD1 
2153 C  CD2 . LEU A 250 ? 0.2124 0.2065 0.2011 -0.0489 0.0799  -0.0098 250 LEU A CD2 
2154 N  N   . LYS A 251 ? 0.1424 0.1480 0.1043 0.0308  -0.0188 0.0010  251 LYS A N   
2155 C  CA  . LYS A 251 ? 0.1541 0.1881 0.1076 0.0296  -0.0131 -0.0092 251 LYS A CA  
2156 C  C   . LYS A 251 ? 0.1409 0.1888 0.1295 0.0241  -0.0125 -0.0148 251 LYS A C   
2157 O  O   . LYS A 251 ? 0.1964 0.2323 0.1237 -0.0026 0.0126  -0.0255 251 LYS A O   
2158 C  CB  . LYS A 251 ? 0.1472 0.1846 0.1596 -0.0098 -0.0176 0.0057  251 LYS A CB  
2159 C  CG  . LYS A 251 ? 0.1746 0.2336 0.2099 -0.0024 0.0586  -0.0227 251 LYS A CG  
2160 C  CD  . LYS A 251 ? 0.1797 0.2334 0.2249 0.0142  -0.0148 -0.0156 251 LYS A CD  
2161 C  CE  . LYS A 251 ? 0.1668 0.2912 0.3871 0.0194  0.0386  -0.0034 251 LYS A CE  
2162 N  NZ  . LYS A 251 ? 0.1333 0.3393 0.4885 0.0329  0.0564  0.0623  251 LYS A NZ  
2163 N  N   . ASN A 252 ? 0.1567 0.1931 0.0948 0.0185  -0.0153 -0.0230 252 ASN A N   
2164 C  CA  . ASN A 252 ? 0.2228 0.2851 0.1142 0.0653  -0.0167 -0.0436 252 ASN A CA  
2165 C  C   . ASN A 252 ? 0.2280 0.2678 0.1974 0.0619  -0.0262 -0.0732 252 ASN A C   
2166 O  O   . ASN A 252 ? 0.2522 0.2372 0.2754 0.0533  0.0054  -0.0232 252 ASN A O   
2167 C  CB  . ASN A 252 ? 0.2275 0.3152 0.2781 0.0399  0.0007  -0.1347 252 ASN A CB  
2168 C  CG  . ASN A 252 ? 0.3691 0.3018 0.3131 0.0509  0.0825  -0.0649 252 ASN A CG  
2169 O  OD1 . ASN A 252 ? 0.7401 0.5264 0.1799 -0.0379 0.1378  -0.0631 252 ASN A OD1 
2170 N  ND2 . ASN A 252 ? 0.2939 0.2949 0.3163 -0.0252 -0.0013 -0.0860 252 ASN A ND2 
2171 N  N   . ARG A 253 ? 0.1423 0.2752 0.1193 0.0584  0.0020  0.0337  253 ARG A N   
2172 C  CA  . ARG A 253 ? 0.1361 0.1797 0.0847 0.0285  -0.0185 -0.0027 253 ARG A CA  
2173 C  C   . ARG A 253 ? 0.1835 0.1516 0.1200 0.0228  0.0054  -0.0153 253 ARG A C   
2174 O  O   . ARG A 253 ? 0.2435 0.2034 0.1999 0.0295  0.1062  0.0487  253 ARG A O   
2175 C  CB  . ARG A 253 ? 0.1124 0.1587 0.0856 0.0059  0.0010  -0.0024 253 ARG A CB  
2176 C  CG  . ARG A 253 ? 0.1234 0.1404 0.1141 -0.0131 -0.0020 -0.0060 253 ARG A CG  
2177 C  CD  . ARG A 253 ? 0.1278 0.1288 0.0934 0.0174  -0.0013 -0.0126 253 ARG A CD  
2178 N  NE  . ARG A 253 ? 0.1008 0.1189 0.1040 0.0034  -0.0121 0.0049  253 ARG A NE  
2179 C  CZ  . ARG A 253 ? 0.0910 0.1128 0.0759 -0.0052 -0.0087 -0.0006 253 ARG A CZ  
2180 N  NH1 . ARG A 253 ? 0.0864 0.1086 0.0996 -0.0046 -0.0178 0.0120  253 ARG A NH1 
2181 N  NH2 . ARG A 253 ? 0.0903 0.1041 0.0939 0.0087  -0.0088 -0.0017 253 ARG A NH2 
2182 N  N   A GLN A 254 ? 0.1326 0.1959 0.1351 0.0102  -0.0241 -0.0283 254 GLN A N   
2183 N  N   B GLN A 254 ? 0.1277 0.2149 0.1263 0.0017  -0.0197 -0.0467 254 GLN A N   
2184 C  CA  A GLN A 254 ? 0.1298 0.2472 0.1172 -0.0027 0.0182  -0.0148 254 GLN A CA  
2185 C  CA  B GLN A 254 ? 0.1554 0.1987 0.1280 -0.0263 -0.0230 -0.0526 254 GLN A CA  
2186 C  C   A GLN A 254 ? 0.1264 0.1825 0.1111 0.0043  0.0326  -0.0175 254 GLN A C   
2187 C  C   B GLN A 254 ? 0.1705 0.1720 0.1430 -0.0252 -0.0379 0.0136  254 GLN A C   
2188 O  O   A GLN A 254 ? 0.1600 0.1875 0.1676 -0.0175 0.0184  -0.0031 254 GLN A O   
2189 O  O   B GLN A 254 ? 0.1342 0.1669 0.2108 -0.0017 -0.0693 -0.0313 254 GLN A O   
2190 C  CB  A GLN A 254 ? 0.2336 0.3240 0.0811 -0.0115 0.0388  -0.0653 254 GLN A CB  
2191 C  CB  B GLN A 254 ? 0.1554 0.2921 0.1497 -0.0310 0.0203  -0.0661 254 GLN A CB  
2192 C  CG  A GLN A 254 ? 0.3095 0.4232 0.0619 -0.0966 -0.0153 -0.0494 254 GLN A CG  
2193 C  CG  B GLN A 254 ? 0.1958 0.2219 0.1509 -0.0049 0.0383  -0.0110 254 GLN A CG  
2194 C  CD  A GLN A 254 ? 0.4981 0.2824 0.1903 -0.1220 0.0728  -0.0900 254 GLN A CD  
2195 C  CD  B GLN A 254 ? 0.4216 0.3738 0.0887 0.0049  0.1387  0.0733  254 GLN A CD  
2196 O  OE1 A GLN A 254 ? 0.6541 0.3571 0.2878 0.0390  0.2002  -0.0753 254 GLN A OE1 
2197 O  OE1 B GLN A 254 ? 0.4293 0.3892 0.3544 -0.0644 0.0326  -0.0284 254 GLN A OE1 
2198 N  NE2 A GLN A 254 ? 0.5996 0.3666 0.1377 -0.1018 0.0482  0.0388  254 GLN A NE2 
2199 N  NE2 B GLN A 254 ? 0.3449 0.3815 0.3652 0.0604  -0.0520 -0.1817 254 GLN A NE2 
2200 N  N   . ILE A 255 ? 0.1367 0.1456 0.1026 0.0031  -0.0027 0.0046  255 ILE A N   
2201 C  CA  . ILE A 255 ? 0.1164 0.1527 0.0979 0.0206  0.0041  0.0024  255 ILE A CA  
2202 C  C   . ILE A 255 ? 0.1377 0.1111 0.0963 0.0010  0.0046  0.0096  255 ILE A C   
2203 O  O   . ILE A 255 ? 0.1358 0.1712 0.1193 0.0054  0.0193  0.0357  255 ILE A O   
2204 C  CB  . ILE A 255 ? 0.1333 0.1385 0.1048 0.0076  -0.0097 -0.0091 255 ILE A CB  
2205 C  CG1 . ILE A 255 ? 0.1318 0.1625 0.1217 0.0253  -0.0076 0.0005  255 ILE A CG1 
2206 C  CG2 . ILE A 255 ? 0.1444 0.1828 0.0882 0.0074  -0.0048 -0.0098 255 ILE A CG2 
2207 C  CD1 . ILE A 255 ? 0.1624 0.1799 0.1556 0.0154  0.0076  -0.0308 255 ILE A CD1 
2208 N  N   . LYS A 256 ? 0.1007 0.1422 0.0895 0.0065  0.0006  -0.0054 256 LYS A N   
2209 C  CA  . LYS A 256 ? 0.1088 0.1675 0.0864 -0.0013 0.0175  0.0162  256 LYS A CA  
2210 C  C   . LYS A 256 ? 0.1282 0.1459 0.0806 -0.0131 0.0023  0.0076  256 LYS A C   
2211 O  O   . LYS A 256 ? 0.1519 0.1985 0.0804 -0.0410 0.0131  -0.0049 256 LYS A O   
2212 C  CB  . LYS A 256 ? 0.1289 0.1807 0.1209 0.0030  0.0096  -0.0113 256 LYS A CB  
2213 C  CG  . LYS A 256 ? 0.2341 0.2511 0.1630 -0.0350 0.0063  -0.0467 256 LYS A CG  
2214 C  CD  . LYS A 256 ? 0.5569 0.3201 0.4088 0.0364  -0.0509 -0.2328 256 LYS A CD  
2215 C  CE  . LYS A 256 ? 0.4210 0.7752 0.3431 -0.0375 -0.0790 -0.0899 256 LYS A CE  
2216 N  NZ  . LYS A 256 ? 0.5483 1.2381 0.2987 -0.3711 -0.1450 0.2386  256 LYS A NZ  
2217 N  N   . ALA A 257 ? 0.1115 0.1710 0.0979 -0.0013 0.0151  0.0031  257 ALA A N   
2218 C  CA  . ALA A 257 ? 0.1316 0.1464 0.1307 0.0076  0.0131  -0.0041 257 ALA A CA  
2219 C  C   . ALA A 257 ? 0.1600 0.1556 0.0960 -0.0109 0.0131  -0.0167 257 ALA A C   
2220 O  O   . ALA A 257 ? 0.1404 0.1937 0.0864 0.0034  0.0148  -0.0130 257 ALA A O   
2221 C  CB  . ALA A 257 ? 0.1341 0.1668 0.1427 -0.0046 0.0057  -0.0006 257 ALA A CB  
2222 N  N   . SER A 258 ? 0.1166 0.1756 0.0980 -0.0043 0.0013  -0.0046 258 SER A N   
2223 C  CA  . SER A 258 ? 0.1195 0.1993 0.1228 0.0077  0.0241  -0.0020 258 SER A CA  
2224 C  C   . SER A 258 ? 0.1132 0.2100 0.1229 0.0013  0.0230  -0.0250 258 SER A C   
2225 O  O   . SER A 258 ? 0.1485 0.2888 0.1800 0.0368  0.0390  0.0003  258 SER A O   
2226 C  CB  . SER A 258 ? 0.1488 0.2032 0.1185 0.0027  -0.0082 -0.0232 258 SER A CB  
2227 O  OG  . SER A 258 ? 0.1092 0.2056 0.1052 0.0098  0.0131  -0.0031 258 SER A OG  
2228 N  N   . PHE A 259 ? 0.1238 0.2088 0.1435 -0.0167 0.0322  -0.0125 259 PHE A N   
2229 C  CA  . PHE A 259 ? 0.1525 0.2250 0.1664 -0.0593 0.0263  -0.0031 259 PHE A CA  
2230 C  C   . PHE A 259 ? 0.2124 0.2709 0.1817 -0.0507 0.0560  0.0154  259 PHE A C   
2231 O  O   . PHE A 259 ? 0.2662 0.2435 0.1669 -0.0619 0.0000  0.0483  259 PHE A O   
2232 C  CB  . PHE A 259 ? 0.1430 0.1923 0.1797 -0.0434 -0.0074 -0.0237 259 PHE A CB  
2233 C  CG  . PHE A 259 ? 0.1572 0.1888 0.1684 -0.0208 -0.0057 0.0024  259 PHE A CG  
2234 C  CD1 . PHE A 259 ? 0.0999 0.1932 0.1339 -0.0175 -0.0059 -0.0007 259 PHE A CD1 
2235 C  CD2 . PHE A 259 ? 0.2413 0.1739 0.2399 -0.0154 0.0211  -0.0249 259 PHE A CD2 
2236 C  CE1 . PHE A 259 ? 0.1422 0.1999 0.1818 -0.0154 0.0000  -0.0458 259 PHE A CE1 
2237 C  CE2 . PHE A 259 ? 0.2325 0.2675 0.2221 0.0328  0.0103  0.0339  259 PHE A CE2 
2238 C  CZ  . PHE A 259 ? 0.1676 0.2161 0.2504 0.0099  -0.0054 -0.0346 259 PHE A CZ  
2239 N  N   . LYS A 260 ? 0.3190 0.4167 0.2442 -0.1260 0.1019  0.0755  260 LYS A N   
2240 C  CA  . LYS A 260 ? 0.5856 0.5928 0.2962 0.0458  0.0496  0.2053  260 LYS A CA  
2241 C  C   . LYS A 260 ? 0.7705 0.7713 0.4036 0.0355  0.2240  0.1752  260 LYS A C   
2242 O  O   . LYS A 260 ? 0.4572 0.9915 0.7185 -0.0518 0.3249  -0.0249 260 LYS A O   
2243 C  CB  . LYS A 260 ? 0.5457 0.6862 0.4038 -0.0619 0.1233  -0.0010 260 LYS A CB  
2244 C  CG  . LYS A 260 ? 0.3998 0.5849 0.5526 -0.2407 0.0266  0.1118  260 LYS A CG  
2245 C  CD  . LYS A 260 ? 0.5677 0.4314 0.6280 -0.1985 -0.0634 0.2633  260 LYS A CD  
2246 C  CE  . LYS A 260 ? 0.8450 0.9953 0.7128 -0.2494 -0.1371 0.2374  260 LYS A CE  
2247 N  NZ  . LYS A 260 ? 0.6363 0.5396 1.0026 -0.0759 0.2772  0.3357  260 LYS A NZ  
2248 O  OXT . LYS A 260 ? 0.8783 0.8919 0.9491 0.0736  -0.0115 0.2442  260 LYS A OXT 
2249 ZN ZN  . ZN  B .   ? 0.0797 0.0752 0.0805 0.0012  -0.0035 0.0010  301 ZN  A ZN  
2250 S  S   . DMS C .   ? 0.1863 0.2158 0.2063 -0.0063 0.0080  -0.0221 302 DMS A S   
2251 O  O   . DMS C .   ? 0.3079 0.2739 0.2576 0.0351  0.0302  -0.1057 302 DMS A O   
2252 C  C1  . DMS C .   ? 0.1814 0.1958 0.1824 0.0436  0.0154  -0.0329 302 DMS A C1  
2253 C  C2  . DMS C .   ? 0.1995 0.2002 0.2770 -0.0259 -0.0449 -0.0390 302 DMS A C2  
2254 N  N1  . BCN D .   ? 0.4291 0.4390 0.4717 -0.0447 0.0586  0.0478  303 BCN A N1  
2255 C  C1  . BCN D .   ? 0.2621 0.2339 0.3790 -0.0715 0.0395  0.0913  303 BCN A C1  
2256 C  C2  . BCN D .   ? 0.7512 0.9174 0.5350 -0.3088 -0.0151 -0.1729 303 BCN A C2  
2257 O  O21 . BCN D .   ? 0.7947 1.8902 1.2697 -0.6352 0.0205  -0.0588 303 BCN A O21 
2258 O  O22 . BCN D .   ? 0.6984 0.4390 0.6743 -0.1615 0.2321  0.1600  303 BCN A O22 
2259 C  C3  . BCN D .   ? 0.2971 0.4841 0.3661 0.0242  0.0136  0.0891  303 BCN A C3  
2260 C  C4  . BCN D .   ? 0.7645 0.4747 0.3251 0.1863  -0.0120 0.1251  303 BCN A C4  
2261 O  O4  . BCN D .   ? 0.4910 0.9293 0.4354 -0.2969 0.0287  0.2569  303 BCN A O4  
2262 C  C5  . BCN D .   ? 0.3476 0.2763 0.3413 -0.0838 0.0502  0.0662  303 BCN A C5  
2263 C  C6  . BCN D .   ? 0.4977 0.3828 0.4314 0.0216  0.0450  -0.0399 303 BCN A C6  
2264 O  O6  . BCN D .   ? 0.4162 0.3138 0.5928 -0.0658 0.1221  0.0186  303 BCN A O6  
2265 O  O1  . MES E .   ? 0.3239 0.4137 0.3037 -0.0335 -0.0649 0.0153  304 MES A O1  
2266 C  C2  . MES E .   ? 0.3030 0.2781 0.2471 0.0606  -0.1030 -0.0502 304 MES A C2  
2267 C  C3  . MES E .   ? 0.3003 0.1595 0.3515 0.0621  0.0178  0.0399  304 MES A C3  
2268 N  N4  . MES E .   ? 0.4914 0.4611 0.4914 -0.1307 0.0785  -0.0286 304 MES A N4  
2269 C  C5  . MES E .   ? 0.4359 0.2216 0.3258 0.0170  -0.0715 -0.1014 304 MES A C5  
2270 C  C6  . MES E .   ? 0.3788 0.1607 0.5073 0.0727  0.0210  0.0535  304 MES A C6  
2271 C  C7  . MES E .   ? 0.3648 0.2095 0.2917 -0.0527 -0.1230 0.0702  304 MES A C7  
2272 C  C8  . MES E .   ? 1.6998 0.6294 0.2754 0.1049  -0.4280 0.0480  304 MES A C8  
2273 S  S   . MES E .   ? 1.0506 1.2666 1.1404 -0.6068 -0.3179 0.0394  304 MES A S   
2274 F  F18 A V90 F .   ? 0.1264 0.0919 0.1842 -0.0137 0.0560  0.0188  305 V90 A F18 
2275 F  F18 B V90 F .   ? 0.1897 0.3364 0.1528 -0.0093 0.0048  0.1017  305 V90 A F18 
2276 C  C5  A V90 F .   ? 0.1043 0.0768 0.1377 -0.0262 0.0233  0.0163  305 V90 A C5  
2277 C  C5  B V90 F .   ? 0.1546 0.1870 0.1318 -0.0104 0.0260  0.0322  305 V90 A C5  
2278 C  C6  A V90 F .   ? 0.0762 0.0691 0.1313 -0.0093 0.0175  0.0057  305 V90 A C6  
2279 C  C6  B V90 F .   ? 0.1888 0.2310 0.1429 0.0065  0.0362  -0.0189 305 V90 A C6  
2280 S  S12 A V90 F .   ? 0.2425 0.1215 0.2293 -0.0206 0.0421  0.0318  305 V90 A S12 
2281 S  S12 B V90 F .   ? 0.2761 0.3833 0.1570 -0.0399 0.0230  0.0118  305 V90 A S12 
2282 C  C13 A V90 F .   ? 0.2606 0.2502 0.4368 -0.0182 -0.0412 0.0353  305 V90 A C13 
2283 C  C13 B V90 F .   ? 0.2606 0.2908 0.1650 0.0612  0.1071  -0.0124 305 V90 A C13 
2284 C  C14 A V90 F .   ? 0.2392 0.2648 0.4217 0.0035  -0.0469 0.1483  305 V90 A C14 
2285 C  C14 B V90 F .   ? 0.1976 0.3145 0.2836 -0.0303 0.0388  0.0982  305 V90 A C14 
2286 O  O15 A V90 F .   ? 0.4086 0.6682 0.4131 -0.0991 -0.0772 0.3413  305 V90 A O15 
2287 O  O15 B V90 F .   ? 0.1573 0.2156 0.1956 -0.0465 -0.0564 0.0513  305 V90 A O15 
2288 C  C1  A V90 F .   ? 0.1102 0.0679 0.1183 -0.0046 0.0054  -0.0054 305 V90 A C1  
2289 C  C1  B V90 F .   ? 0.1432 0.2377 0.1525 -0.0322 0.0247  0.0048  305 V90 A C1  
2290 F  F17 A V90 F .   ? 0.1472 0.0751 0.1555 0.0024  0.0320  0.0000  305 V90 A F17 
2291 F  F17 B V90 F .   ? 0.4052 0.3079 0.3738 0.2476  0.2497  0.0925  305 V90 A F17 
2292 C  C4  A V90 F .   ? 0.1005 0.0617 0.0851 0.0026  -0.0073 0.0019  305 V90 A C4  
2293 C  C4  B V90 F .   ? 0.1456 0.1615 0.1254 -0.0120 0.0261  0.0366  305 V90 A C4  
2294 C  C3  A V90 F .   ? 0.0732 0.0590 0.1000 0.0013  -0.0115 -0.0049 305 V90 A C3  
2295 C  C3  B V90 F .   ? 0.0908 0.1202 0.1371 -0.0156 -0.0120 0.0006  305 V90 A C3  
2296 S  S8  A V90 F .   ? 0.0715 0.0665 0.0718 0.0015  -0.0049 -0.0074 305 V90 A S8  
2297 S  S8  B V90 F .   ? 0.1234 0.1198 0.1137 -0.0096 -0.0186 0.0043  305 V90 A S8  
2298 O  O10 A V90 F .   ? 0.0697 0.0717 0.0838 0.0000  0.0003  -0.0208 305 V90 A O10 
2299 O  O10 B V90 F .   ? 0.1394 0.1071 0.1580 0.0057  -0.0236 0.0087  305 V90 A O10 
2300 N  N11 A V90 F .   ? 0.0448 0.0540 0.0536 -0.0152 0.0076  -0.0060 305 V90 A N11 
2301 N  N11 B V90 F .   ? 0.1254 0.1139 0.1010 -0.0104 0.0104  0.0070  305 V90 A N11 
2302 O  O9  A V90 F .   ? 0.0841 0.0903 0.0640 0.0121  0.0024  -0.0065 305 V90 A O9  
2303 O  O9  B V90 F .   ? 0.1347 0.1181 0.1298 -0.0197 -0.0474 -0.0170 305 V90 A O9  
2304 C  C2  A V90 F .   ? 0.0957 0.0636 0.1093 -0.0051 -0.0062 -0.0147 305 V90 A C2  
2305 C  C2  B V90 F .   ? 0.1111 0.1518 0.1335 -0.0015 0.0038  -0.0046 305 V90 A C2  
2306 F  F16 A V90 F .   ? 0.0969 0.0785 0.1128 0.0057  0.0017  -0.0176 305 V90 A F16 
2307 F  F16 B V90 F .   ? 0.1397 0.1474 0.2545 0.0098  0.0675  0.0051  305 V90 A F16 
2308 N  N7  A V90 F .   ? 0.0839 0.0854 0.0936 0.0092  0.0010  0.0023  305 V90 A N7  
2309 N  N7  B V90 F .   ? 0.1391 0.1448 0.1787 -0.0408 0.0233  0.0203  305 V90 A N7  
2310 C  C19 A V90 F .   ? 0.1114 0.0944 0.0824 0.0007  -0.0019 0.0092  305 V90 A C19 
2311 C  C19 B V90 F .   ? 0.3646 0.1872 0.2536 -0.0247 0.1164  0.0452  305 V90 A C19 
2312 C  C26 A V90 F .   ? 0.1324 0.0953 0.1060 0.0173  -0.0082 -0.0199 305 V90 A C26 
2313 C  C26 B V90 F .   ? 0.2673 0.3698 0.1973 0.0000  0.0458  -0.0005 305 V90 A C26 
2314 C  C25 A V90 F .   ? 0.1668 0.2205 0.1686 -0.0199 0.0386  -0.0625 305 V90 A C25 
2315 C  C25 B V90 F .   ? 0.2090 0.2330 0.2345 -0.0306 -0.0723 0.1523  305 V90 A C25 
2316 C  C24 A V90 F .   ? 0.1268 0.1292 0.1377 -0.0082 0.0417  -0.0024 305 V90 A C24 
2317 C  C24 B V90 F .   ? 0.3670 0.2540 0.2215 -0.0746 0.0768  0.0438  305 V90 A C24 
2318 C  C23 A V90 F .   ? 0.1467 0.1605 0.0907 0.0010  0.0153  0.0480  305 V90 A C23 
2319 C  C23 B V90 F .   ? 0.3131 0.3449 0.2849 -0.0027 0.0544  0.0362  305 V90 A C23 
2320 C  C22 A V90 F .   ? 0.1641 0.1148 0.1585 0.0230  0.0000  0.0189  305 V90 A C22 
2321 C  C22 B V90 F .   ? 0.3957 0.1536 0.3264 -0.0630 0.0988  -0.0241 305 V90 A C22 
2322 C  C21 A V90 F .   ? 0.1264 0.1634 0.1123 0.0432  0.0249  0.0344  305 V90 A C21 
2323 C  C21 B V90 F .   ? 0.1312 0.1353 0.0742 -0.0063 -0.0051 0.0401  305 V90 A C21 
2324 C  C20 A V90 F .   ? 0.0891 0.1199 0.0864 0.0006  0.0272  0.0197  305 V90 A C20 
2325 C  C20 B V90 F .   ? 0.2097 0.2442 0.1360 -0.0329 -0.0405 -0.0200 305 V90 A C20 
2326 O  O   . HOH G .   ? 0.1221 0.1306 0.1439 0.0037  -0.0236 0.0219  401 HOH A O   
2327 O  O   . HOH G .   ? 0.0892 0.1639 0.1620 0.0054  -0.0017 -0.0368 402 HOH A O   
2328 O  O   . HOH G .   ? 0.0952 0.1067 0.0986 -0.0006 0.0153  0.0048  403 HOH A O   
2329 O  O   . HOH G .   ? 0.1278 0.1208 0.1467 -0.0057 -0.0003 0.0006  404 HOH A O   
2330 O  O   . HOH G .   ? 0.1459 0.1040 0.1447 0.0102  -0.0335 0.0126  405 HOH A O   
2331 O  O   . HOH G .   ? 0.1189 0.0986 0.1014 0.0175  -0.0054 -0.0006 406 HOH A O   
2332 O  O   . HOH G .   ? 0.1239 0.1937 0.1500 -0.0183 -0.0331 0.0412  407 HOH A O   
2333 O  O   . HOH G .   ? 0.1059 0.1234 0.0988 0.0237  -0.0054 0.0007  408 HOH A O   
2334 O  O   . HOH G .   ? 0.2079 0.1967 0.2687 0.0248  -0.1155 -0.0649 409 HOH A O   
2335 O  O   . HOH G .   ? 0.1508 0.1278 0.1383 0.0153  -0.0219 0.0121  410 HOH A O   
2336 O  O   . HOH G .   ? 0.0997 0.1844 0.1642 0.0093  0.0057  -0.0259 411 HOH A O   
2337 O  O   . HOH G .   ? 0.1217 0.1556 0.1251 0.0015  -0.0195 0.0208  412 HOH A O   
2338 O  O   . HOH G .   ? 0.1964 0.2379 0.2108 0.0131  0.0537  -0.0627 413 HOH A O   
2339 O  O   . HOH G .   ? 0.1272 0.1049 0.1330 -0.0015 0.0037  -0.0265 414 HOH A O   
2340 O  O   . HOH G .   ? 0.1216 0.1066 0.1292 0.0098  -0.0110 0.0020  415 HOH A O   
2341 O  O   . HOH G .   ? 0.3124 0.2029 0.3350 0.0683  -0.1616 -0.0355 416 HOH A O   
2342 O  O   . HOH G .   ? 0.1639 0.1057 0.1476 -0.0152 -0.0274 0.0119  417 HOH A O   
2343 O  O   . HOH G .   ? 0.1561 0.1454 0.1600 0.0281  0.0054  0.0103  418 HOH A O   
2344 O  O   . HOH G .   ? 0.1976 0.1545 0.1482 -0.0148 0.0277  0.0177  419 HOH A O   
2345 O  O   . HOH G .   ? 0.1784 0.3113 0.2696 0.0570  -0.0388 0.0494  420 HOH A O   
2346 O  O   . HOH G .   ? 0.3300 0.2416 0.1691 -0.0421 -0.0271 0.0386  421 HOH A O   
2347 O  O   . HOH G .   ? 0.1894 0.1456 0.2488 0.0006  0.0023  -0.0342 422 HOH A O   
2348 O  O   . HOH G .   ? 0.1527 0.2314 0.2790 0.0610  0.0096  0.0295  423 HOH A O   
2349 O  O   . HOH G .   ? 0.1166 0.1246 0.1263 -0.0020 0.0146  -0.0087 424 HOH A O   
2350 O  O   . HOH G .   ? 0.2462 0.2951 0.2018 -0.0608 0.0606  0.0231  425 HOH A O   
2351 O  O   . HOH G .   ? 0.1673 0.1629 0.2615 -0.0357 -0.0549 -0.0109 426 HOH A O   
2352 O  O   . HOH G .   ? 0.1253 0.0696 0.1254 0.0000  -0.0225 -0.0003 427 HOH A O   
2353 O  O   . HOH G .   ? 0.2707 0.5776 0.2921 0.0929  -0.1617 -0.1289 428 HOH A O   
2354 O  O   . HOH G .   ? 0.1239 0.1462 0.1564 -0.0030 0.0096  0.0054  429 HOH A O   
2355 O  O   . HOH G .   ? 0.3192 0.1533 0.2055 -0.0535 -0.0322 -0.0252 430 HOH A O   
2356 O  O   . HOH G .   ? 0.2531 0.2187 0.4388 0.0326  -0.1483 -0.1164 431 HOH A O   
2357 O  O   . HOH G .   ? 0.1802 0.1748 0.2153 -0.0209 0.0355  -0.0129 432 HOH A O   
2358 O  O   . HOH G .   ? 0.1791 0.2210 0.1670 0.0381  -0.0520 -0.0012 433 HOH A O   
2359 O  O   . HOH G .   ? 0.2052 0.1956 0.2151 -0.0189 -0.0241 0.0126  434 HOH A O   
2360 O  O   . HOH G .   ? 0.1888 0.2002 0.2169 -0.0185 0.0175  0.0068  435 HOH A O   
2361 O  O   . HOH G .   ? 0.1917 0.1949 0.1536 0.0410  0.0329  0.0085  436 HOH A O   
2362 O  O   . HOH G .   ? 0.1756 0.1307 0.1924 -0.0096 -0.0405 0.0097  437 HOH A O   
2363 O  O   . HOH G .   ? 0.2800 0.2009 0.2320 0.0219  -0.0829 -0.0776 438 HOH A O   
2364 O  O   . HOH G .   ? 0.1272 0.1740 0.1279 0.0225  0.0057  0.0370  439 HOH A O   
2365 O  O   . HOH G .   ? 0.2648 0.1520 0.1861 -0.0043 -0.0342 0.0071  440 HOH A O   
2366 O  O   . HOH G .   ? 0.1840 0.1623 0.1967 -0.0017 0.0003  0.0274  441 HOH A O   
2367 O  O   . HOH G .   ? 0.3104 0.1351 0.3310 0.0209  -0.1181 0.0148  442 HOH A O   
2368 O  O   . HOH G .   ? 0.2057 0.2795 0.1668 -0.0203 0.0474  0.0746  443 HOH A O   
2369 O  O   . HOH G .   ? 0.1114 0.2632 0.2176 -0.0163 -0.0082 0.0006  444 HOH A O   
2370 O  O   . HOH G .   ? 0.2427 0.1357 0.2063 -0.0125 -0.0260 -0.0333 445 HOH A O   
2371 O  O   . HOH G .   ? 0.1536 0.1342 0.1483 -0.0126 0.0160  -0.0306 446 HOH A O   
2372 O  O   . HOH G .   ? 0.3639 0.1731 0.2926 0.0617  0.0375  0.0834  447 HOH A O   
2373 O  O   . HOH G .   ? 0.2619 0.1333 0.2391 0.0295  -0.0077 -0.0082 448 HOH A O   
2374 O  O   . HOH G .   ? 0.2205 0.2725 0.2093 -0.0216 -0.0274 -0.0379 449 HOH A O   
2375 O  O   . HOH G .   ? 0.1752 0.1861 0.1544 -0.0244 0.0049  -0.0252 450 HOH A O   
2376 O  O   . HOH G .   ? 0.1621 0.2088 0.1665 0.0584  0.0175  0.0120  451 HOH A O   
2377 O  O   . HOH G .   ? 0.2406 0.2411 0.3411 -0.0307 0.0359  0.0452  452 HOH A O   
2378 O  O   . HOH G .   ? 0.2224 0.2329 0.1263 -0.0146 0.0110  -0.0068 453 HOH A O   
2379 O  O   . HOH G .   ? 0.3693 0.2095 0.1563 -0.0452 0.0185  0.0546  454 HOH A O   
2380 O  O   . HOH G .   ? 0.3280 0.3106 0.3106 0.1092  0.0722  0.0790  455 HOH A O   
2381 O  O   . HOH G .   ? 0.2214 0.1950 0.1921 0.0211  0.0229  0.0802  456 HOH A O   
2382 O  O   . HOH G .   ? 0.1897 0.2781 0.2240 0.0562  0.0296  -0.0132 457 HOH A O   
2383 O  O   . HOH G .   ? 0.2666 0.2255 0.2551 0.0612  0.0702  0.0401  458 HOH A O   
2384 O  O   . HOH G .   ? 0.1659 0.1685 0.2524 -0.0575 0.0107  -0.0357 459 HOH A O   
2385 O  O   . HOH G .   ? 0.1844 0.1316 0.2039 -0.0103 0.0419  0.0252  460 HOH A O   
2386 O  O   . HOH G .   ? 0.1897 0.2777 0.3555 0.0006  -0.0425 -0.0368 461 HOH A O   
2387 O  O   . HOH G .   ? 0.1164 0.1833 0.2406 -0.0060 0.0054  -0.0031 462 HOH A O   
2388 O  O   . HOH G .   ? 0.5741 0.1731 0.3713 0.0216  -0.1884 -0.0467 463 HOH A O   
2389 O  O   . HOH G .   ? 0.2502 0.2030 0.2392 0.0052  0.0480  0.0322  464 HOH A O   
2390 O  O   . HOH G .   ? 0.1533 0.2766 0.2266 0.0443  0.0373  0.0320  465 HOH A O   
2391 O  O   . HOH G .   ? 0.2377 0.2097 0.2064 0.0515  -0.0390 0.0197  466 HOH A O   
2392 O  O   . HOH G .   ? 0.2307 0.2016 0.1553 0.0000  -0.0107 -0.0131 467 HOH A O   
2393 O  O   . HOH G .   ? 0.1969 0.2700 0.4356 0.0329  0.0068  -0.0573 468 HOH A O   
2394 O  O   . HOH G .   ? 0.1386 0.3258 0.2687 0.0230  -0.0046 0.0913  469 HOH A O   
2395 O  O   . HOH G .   ? 0.1835 0.3226 0.2005 -0.0296 -0.0109 0.1115  470 HOH A O   
2396 O  O   . HOH G .   ? 0.2413 0.2321 0.1861 -0.0043 0.0619  -0.0653 471 HOH A O   
2397 O  O   . HOH G .   ? 0.3129 0.2479 0.5382 0.0118  -0.0593 0.0636  472 HOH A O   
2398 O  O   . HOH G .   ? 0.3012 0.1782 0.3000 0.0697  -0.0754 0.0065  473 HOH A O   
2399 O  O   . HOH G .   ? 0.3147 0.2556 0.2766 0.0216  0.0086  0.0878  474 HOH A O   
2400 O  O   . HOH G .   ? 0.2328 0.2635 0.2402 0.0227  -0.0408 -0.0239 475 HOH A O   
2401 O  O   . HOH G .   ? 0.2897 0.2506 0.2741 0.0357  -0.0921 -0.1054 476 HOH A O   
2402 O  O   . HOH G .   ? 0.1959 0.2660 0.1914 -0.0023 -0.0244 0.0074  477 HOH A O   
2403 O  O   . HOH G .   ? 0.1895 0.2721 0.2888 0.0046  0.0041  0.0649  478 HOH A O   
2404 O  O   . HOH G .   ? 0.1492 0.1852 0.1756 0.0335  -0.0186 0.0119  479 HOH A O   
2405 O  O   . HOH G .   ? 0.2359 0.1929 0.1767 0.0242  -0.0017 0.0115  480 HOH A O   
2406 O  O   . HOH G .   ? 0.4550 0.3267 0.1782 0.2280  -0.0310 0.0161  481 HOH A O   
2407 O  O   . HOH G .   ? 0.2095 0.1852 0.2145 0.0434  -0.0291 0.0019  482 HOH A O   
2408 O  O   . HOH G .   ? 0.1371 0.3474 0.2718 0.0175  0.0271  0.0625  483 HOH A O   
2409 O  O   . HOH G .   ? 0.2128 0.3862 0.1190 0.1045  -0.0498 -0.0175 484 HOH A O   
2410 O  O   . HOH G .   ? 0.1958 0.1930 0.1782 -0.0074 0.0304  0.0000  485 HOH A O   
2411 O  O   . HOH G .   ? 0.2569 0.3970 0.2937 0.1045  0.0763  0.0736  486 HOH A O   
2412 O  O   . HOH G .   ? 0.1897 0.4697 0.2554 -0.0060 -0.0113 -0.0211 487 HOH A O   
2413 O  O   . HOH G .   ? 0.2264 0.2474 0.2091 0.0031  0.0241  -0.0353 488 HOH A O   
2414 O  O   . HOH G .   ? 0.2278 0.2108 0.2883 0.0675  -0.0688 -0.0754 489 HOH A O   
2415 O  O   . HOH G .   ? 0.1952 0.1509 0.2750 -0.0161 -0.0274 0.0010  490 HOH A O   
2416 O  O   . HOH G .   ? 0.2711 0.3048 0.3361 -0.0181 0.0333  -0.0241 491 HOH A O   
2417 O  O   . HOH G .   ? 0.2442 0.2964 0.3513 0.0005  0.0355  0.0438  492 HOH A O   
2418 O  O   . HOH G .   ? 0.3343 0.2587 0.2723 -0.0566 0.0619  -0.0557 493 HOH A O   
2419 O  O   . HOH G .   ? 0.4122 0.4025 0.1897 0.1394  0.0688  0.0702  494 HOH A O   
2420 O  O   . HOH G .   ? 0.3971 0.2113 0.2113 0.0386  -0.0197 0.0947  495 HOH A O   
2421 O  O   . HOH G .   ? 0.2208 0.1820 0.2011 0.0205  -0.0266 0.0109  496 HOH A O   
2422 O  O   . HOH G .   ? 0.2169 0.2820 0.2063 -0.0460 0.0394  0.0230  497 HOH A O   
2423 O  O   . HOH G .   ? 0.2930 0.2743 0.2140 0.0538  0.0240  0.0337  498 HOH A O   
2424 O  O   . HOH G .   ? 0.2558 0.2187 0.2126 0.0403  -0.0619 -0.0381 499 HOH A O   
2425 O  O   . HOH G .   ? 0.2180 0.1879 0.2777 0.0178  0.0272  -0.0299 500 HOH A O   
2426 O  O   . HOH G .   ? 0.4241 0.2420 0.2759 -0.0939 0.0772  -0.0520 501 HOH A O   
2427 O  O   . HOH G .   ? 0.3183 0.2300 0.2522 0.0277  -0.0614 -0.0305 502 HOH A O   
2428 O  O   . HOH G .   ? 0.6108 0.2908 0.1711 -0.0806 -0.0104 -0.0381 503 HOH A O   
2429 O  O   . HOH G .   ? 0.3345 0.3328 0.1897 -0.0115 -0.0060 -0.0392 504 HOH A O   
2430 O  O   . HOH G .   ? 0.1405 0.2212 0.1739 0.0255  0.0120  0.0577  505 HOH A O   
2431 O  O   . HOH G .   ? 0.1851 0.1665 0.1634 -0.0288 -0.0146 -0.0132 506 HOH A O   
2432 O  O   . HOH G .   ? 0.2023 0.2255 0.3691 -0.0287 -0.0226 -0.0811 507 HOH A O   
2433 O  O   . HOH G .   ? 0.1295 0.2235 0.1987 0.0126  -0.0060 -0.0173 508 HOH A O   
2434 O  O   . HOH G .   ? 0.2045 0.2456 0.3589 -0.0027 0.0074  0.1084  509 HOH A O   
2435 O  O   . HOH G .   ? 0.2567 0.1661 0.1861 -0.0057 0.0000  -0.0243 510 HOH A O   
2436 O  O   . HOH G .   ? 0.2879 0.3510 0.1773 0.1331  -0.0308 0.0384  511 HOH A O   
2437 O  O   . HOH G .   ? 0.2833 0.2090 0.1701 -0.0648 -0.0091 0.0000  512 HOH A O   
2438 O  O   . HOH G .   ? 0.2365 0.2034 0.2291 0.0496  0.0125  -0.0260 513 HOH A O   
2439 O  O   . HOH G .   ? 0.2196 0.2048 0.3420 0.0864  0.0093  0.0000  514 HOH A O   
2440 O  O   . HOH G .   ? 0.3594 0.2524 0.3082 0.0137  0.0812  -0.1102 515 HOH A O   
2441 O  O   . HOH G .   ? 0.2054 0.3025 0.3560 -0.0171 -0.0181 -0.0071 516 HOH A O   
2442 O  O   . HOH G .   ? 0.2264 0.2504 0.2185 0.0661  0.0474  0.0860  517 HOH A O   
2443 O  O   . HOH G .   ? 0.5087 0.4144 0.4614 -0.1684 -0.2624 0.2030  518 HOH A O   
2444 O  O   . HOH G .   ? 0.4748 0.2190 0.1500 -0.0010 -0.0333 -0.0226 519 HOH A O   
2445 O  O   . HOH G .   ? 0.2077 0.1676 0.2059 0.0230  -0.0126 0.0292  520 HOH A O   
2446 O  O   . HOH G .   ? 0.1941 0.2951 0.1738 0.0119  -0.0051 -0.0373 521 HOH A O   
2447 O  O   . HOH G .   ? 0.2479 0.2818 0.3161 -0.0068 -0.0059 0.0430  522 HOH A O   
2448 O  O   . HOH G .   ? 0.1820 0.1924 0.1635 -0.0153 0.0406  0.0052  523 HOH A O   
2449 O  O   . HOH G .   ? 0.2440 0.4156 0.2045 0.1005  0.0000  -0.0498 524 HOH A O   
2450 O  O   . HOH G .   ? 0.2237 0.1483 0.4068 -0.0154 0.0680  -0.0577 525 HOH A O   
2451 O  O   . HOH G .   ? 0.5587 0.5579 0.1694 -0.0379 0.0781  0.0626  526 HOH A O   
2452 O  O   . HOH G .   ? 0.3384 0.3258 0.1791 -0.0697 0.0087  0.0551  527 HOH A O   
2453 O  O   . HOH G .   ? 0.3858 0.2379 0.7110 -0.0964 -0.3673 0.0326  528 HOH A O   
2454 O  O   . HOH G .   ? 0.3596 0.3393 0.3499 -0.0452 -0.0423 -0.1171 529 HOH A O   
2455 O  O   . HOH G .   ? 0.2626 0.2671 0.1899 0.0377  0.0115  0.0443  530 HOH A O   
2456 O  O   . HOH G .   ? 0.2169 0.1940 0.2754 0.0142  -0.0610 -0.0104 531 HOH A O   
2457 O  O   . HOH G .   ? 0.2043 0.2449 0.3404 -0.0136 -0.0074 0.0439  532 HOH A O   
2458 O  O   . HOH G .   ? 0.3677 0.3980 0.3025 -0.0593 0.0843  0.1868  533 HOH A O   
2459 O  O   . HOH G .   ? 0.2436 0.3267 0.3262 -0.0027 0.0562  -0.0872 534 HOH A O   
2460 O  O   . HOH G .   ? 0.2048 0.2005 0.2293 0.0357  -0.0200 0.0120  535 HOH A O   
2461 O  O   . HOH G .   ? 0.2305 0.3555 0.2185 -0.0878 0.0074  0.0206  536 HOH A O   
2462 O  O   . HOH G .   ? 0.3673 0.3456 0.2700 -0.1455 0.1298  -0.1621 537 HOH A O   
2463 O  O   . HOH G .   ? 0.2542 0.5274 0.3106 -0.0868 0.0361  -0.0296 538 HOH A O   
2464 O  O   . HOH G .   ? 0.3429 0.1439 0.4097 -0.0165 0.0952  0.0068  539 HOH A O   
2465 O  O   . HOH G .   ? 0.2334 0.1912 0.3185 0.0194  -0.0324 -0.0394 540 HOH A O   
2466 O  O   . HOH G .   ? 0.3677 0.4952 0.3093 0.1019  0.1299  -0.0115 541 HOH A O   
2467 O  O   . HOH G .   ? 0.3366 0.2424 0.4228 -0.0151 -0.0351 0.1194  542 HOH A O   
2468 O  O   . HOH G .   ? 0.3943 0.3959 0.3916 -0.0983 0.2506  -0.1184 543 HOH A O   
2469 O  O   . HOH G .   ? 0.5443 0.3242 0.4644 0.0410  0.0199  0.0421  544 HOH A O   
2470 O  O   . HOH G .   ? 0.1684 0.2836 0.2399 -0.0137 -0.0291 -0.0077 545 HOH A O   
2471 O  O   . HOH G .   ? 0.3865 0.5296 0.2538 -0.3057 0.0137  -0.0432 546 HOH A O   
2472 O  O   . HOH G .   ? 0.2374 0.2246 0.2481 -0.0333 0.0186  0.0096  547 HOH A O   
2473 O  O   . HOH G .   ? 0.3154 0.2527 0.3050 -0.0586 -0.0847 -0.0603 548 HOH A O   
2474 O  O   . HOH G .   ? 0.2685 0.2624 0.2984 0.0153  0.0474  0.0472  549 HOH A O   
2475 O  O   . HOH G .   ? 0.4377 0.1932 0.4149 -0.0449 0.0621  -0.0549 550 HOH A O   
2476 O  O   . HOH G .   ? 0.3073 0.3467 0.2727 -0.0535 -0.0359 0.0454  551 HOH A O   
2477 O  O   . HOH G .   ? 0.2694 0.3027 0.3632 0.1128  -0.0777 -0.0732 552 HOH A O   
2478 O  O   . HOH G .   ? 0.2212 0.2802 0.4221 -0.0579 0.0825  -0.1274 553 HOH A O   
2479 O  O   . HOH G .   ? 0.4632 0.1905 0.4722 0.0344  -0.1622 -0.0513 554 HOH A O   
2480 O  O   . HOH G .   ? 0.4151 0.2596 0.3231 -0.0366 0.0428  -0.0662 555 HOH A O   
2481 O  O   . HOH G .   ? 0.2458 0.2312 0.3768 0.0164  0.0741  -0.0166 556 HOH A O   
2482 O  O   . HOH G .   ? 0.3474 0.2698 0.4018 -0.0263 -0.1510 0.0171  557 HOH A O   
2483 O  O   . HOH G .   ? 0.2435 0.8610 0.3680 -0.1032 0.0615  0.1004  558 HOH A O   
2484 O  O   . HOH G .   ? 0.3100 0.1937 0.5098 -0.0780 -0.0317 0.0921  559 HOH A O   
2485 O  O   . HOH G .   ? 0.3616 0.2892 0.2458 -0.0060 0.1322  -0.0438 560 HOH A O   
2486 O  O   . HOH G .   ? 0.3634 0.2151 0.3034 -0.0054 0.0192  0.0043  561 HOH A O   
2487 O  O   . HOH G .   ? 0.3673 0.2944 0.2614 0.1792  0.0247  -0.0121 562 HOH A O   
2488 O  O   . HOH G .   ? 0.3919 0.4806 0.3145 -0.0575 0.0970  -0.1893 563 HOH A O   
2489 O  O   . HOH G .   ? 0.3294 0.3736 0.4176 0.1634  -0.0895 0.0208  564 HOH A O   
2490 O  O   . HOH G .   ? 0.2865 0.2978 0.3524 -0.0182 -0.0494 -0.0006 565 HOH A O   
2491 O  O   . HOH G .   ? 0.2750 0.2250 0.4381 -0.0785 -0.0153 -0.0559 566 HOH A O   
2492 O  O   . HOH G .   ? 0.2872 0.4734 0.4081 0.0665  -0.0487 -0.2093 567 HOH A O   
2493 O  O   . HOH G .   ? 0.3754 0.2143 0.1817 0.0013  0.0244  0.0238  568 HOH A O   
2494 O  O   . HOH G .   ? 0.2694 0.4171 0.2770 0.0930  0.0876  -0.0097 569 HOH A O   
2495 O  O   . HOH G .   ? 1.0095 0.6126 0.6043 -0.6776 -0.2827 0.3447  570 HOH A O   
2496 O  O   . HOH G .   ? 0.4469 0.8029 0.4379 0.1243  0.0052  0.2621  571 HOH A O   
2497 O  O   . HOH G .   ? 0.9715 0.3691 0.2687 -0.0925 0.1471  0.0063  572 HOH A O   
2498 O  O   . HOH G .   ? 0.3072 0.2567 0.3262 0.0639  0.0582  -0.0140 573 HOH A O   
2499 O  O   . HOH G .   ? 0.2998 0.5418 0.4275 -0.1005 0.0017  -0.0285 574 HOH A O   
2500 O  O   . HOH G .   ? 0.2309 0.2050 0.1632 -0.0070 -0.0049 -0.0115 575 HOH A O   
2501 O  O   . HOH G .   ? 0.4077 0.2736 0.4291 -0.1658 0.0487  0.0386  576 HOH A O   
2502 O  O   . HOH G .   ? 0.2912 0.4867 0.4165 0.0219  -0.0819 0.1995  577 HOH A O   
2503 O  O   . HOH G .   ? 0.2010 0.1912 0.2847 -0.0098 0.0445  -0.0162 578 HOH A O   
2504 O  O   . HOH G .   ? 0.4914 0.3037 0.5332 -0.0741 0.2169  -0.1208 579 HOH A O   
2505 O  O   . HOH G .   ? 0.3544 0.2029 0.2971 -0.0135 0.0076  -0.0124 580 HOH A O   
2506 O  O   . HOH G .   ? 0.2183 0.3479 0.2978 -0.0384 -0.0606 0.0041  581 HOH A O   
2507 O  O   . HOH G .   ? 0.3156 0.2662 0.2529 -0.0719 0.0920  -0.0091 582 HOH A O   
2508 O  O   . HOH G .   ? 0.3526 0.5508 0.2320 0.0630  0.0264  0.0789  583 HOH A O   
2509 O  O   . HOH G .   ? 0.3133 0.3524 0.2106 -0.0284 -0.0296 0.0126  584 HOH A O   
2510 O  O   . HOH G .   ? 0.2284 0.2406 0.4232 -0.0152 -0.0926 0.0038  585 HOH A O   
2511 O  O   . HOH G .   ? 0.2942 0.3111 0.2601 -0.0386 -0.0054 0.0219  586 HOH A O   
2512 O  O   . HOH G .   ? 0.3384 0.4309 0.2822 -0.0377 -0.0661 0.0065  587 HOH A O   
2513 O  O   . HOH G .   ? 0.4935 0.4514 0.6711 0.0737  -0.0683 -0.0093 588 HOH A O   
2514 O  O   . HOH G .   ? 0.5792 0.5417 0.4505 0.1221  0.1230  0.2829  589 HOH A O   
2515 O  O   . HOH G .   ? 0.4214 0.2431 0.4431 -0.0098 -0.1743 0.0432  590 HOH A O   
2516 O  O   . HOH G .   ? 0.3197 0.1932 0.3181 0.0087  -0.1067 0.0091  591 HOH A O   
2517 O  O   . HOH G .   ? 0.4013 0.2793 0.2522 0.0236  -0.0082 0.0165  592 HOH A O   
2518 O  O   . HOH G .   ? 0.3652 0.3970 0.6480 -0.0895 -0.1659 -0.1386 593 HOH A O   
2519 O  O   . HOH G .   ? 0.1842 0.5806 0.2529 -0.0445 -0.0156 -0.1039 594 HOH A O   
2520 O  O   . HOH G .   ? 0.2496 0.4648 0.3537 -0.0913 0.0675  -0.2240 595 HOH A O   
2521 O  O   . HOH G .   ? 0.6302 0.5328 0.5036 -0.2207 0.0165  -0.1323 596 HOH A O   
2522 O  O   . HOH G .   ? 0.4830 0.3675 0.2174 -0.0724 -0.0674 0.0749  597 HOH A O   
2523 O  O   . HOH G .   ? 0.2379 0.4813 0.6521 0.1351  0.1140  0.0953  598 HOH A O   
2524 O  O   . HOH G .   ? 0.4253 0.5004 0.5256 0.0274  0.0527  -0.0767 599 HOH A O   
2525 O  O   . HOH G .   ? 0.5393 0.2861 0.3217 0.1098  0.1624  0.0623  600 HOH A O   
2526 O  O   . HOH G .   ? 0.3012 0.4226 0.3386 0.0564  0.0384  0.0666  601 HOH A O   
2527 O  O   . HOH G .   ? 0.4291 0.3316 0.3508 0.1907  -0.0026 -0.0302 602 HOH A O   
2528 O  O   . HOH G .   ? 0.3240 0.2601 0.3968 -0.0342 -0.0559 -0.0392 603 HOH A O   
2529 O  O   . HOH G .   ? 0.2917 0.3100 0.4304 -0.0781 -0.1230 0.1852  604 HOH A O   
2530 O  O   . HOH G .   ? 0.3287 0.7024 0.4115 0.1402  0.1439  0.2379  605 HOH A O   
2531 O  O   . HOH G .   ? 0.3465 0.1985 0.3278 0.0895  -0.0504 -0.0346 606 HOH A O   
2532 O  O   . HOH G .   ? 0.2624 0.3436 0.4576 0.0248  0.0143  0.0737  607 HOH A O   
2533 O  O   . HOH G .   ? 0.3709 0.5605 0.3756 -0.1384 -0.0151 -0.1722 608 HOH A O   
2534 O  O   . HOH G .   ? 0.2838 0.6250 0.3833 -0.0241 0.0247  0.2752  609 HOH A O   
2535 O  O   . HOH G .   ? 1.0858 0.2045 0.3826 0.1888  -0.1079 -0.0031 610 HOH A O   
2536 O  O   . HOH G .   ? 0.2739 0.4995 0.3984 0.0318  -0.0093 -0.0155 611 HOH A O   
2537 O  O   . HOH G .   ? 0.3878 0.3039 0.3246 -0.1297 -0.0921 0.1221  612 HOH A O   
2538 O  O   . HOH G .   ? 0.4383 0.1976 0.3549 -0.0414 -0.0768 0.0232  613 HOH A O   
2539 O  O   . HOH G .   ? 0.4088 0.3176 0.2646 0.0362  -0.0229 -0.0790 614 HOH A O   
2540 O  O   . HOH G .   ? 0.2698 0.5533 0.4282 -0.0991 -0.0472 -0.1071 615 HOH A O   
2541 O  O   . HOH G .   ? 0.2887 0.3652 0.4661 0.0097  -0.0238 -0.0216 616 HOH A O   
2542 O  O   . HOH G .   ? 0.3197 0.3659 0.2978 -0.0154 0.0115  -0.0575 617 HOH A O   
2543 O  O   . HOH G .   ? 0.3862 0.3973 0.3264 -0.0010 0.1023  0.0298  618 HOH A O   
2544 O  O   . HOH G .   ? 0.3479 0.2169 0.3783 -0.0013 -0.1102 -0.0296 619 HOH A O   
2545 O  O   . HOH G .   ? 0.3666 0.4607 0.3082 0.0456  0.1159  0.2108  620 HOH A O   
2546 O  O   . HOH G .   ? 0.3932 0.3097 0.4975 -0.1018 -0.0120 -0.0087 621 HOH A O   
2547 O  O   . HOH G .   ? 0.3544 0.3734 0.2928 -0.0263 0.0419  0.0653  622 HOH A O   
2548 O  O   . HOH G .   ? 0.3431 0.4981 0.3361 -0.0553 0.0243  0.2109  623 HOH A O   
2549 O  O   . HOH G .   ? 0.3759 0.6406 0.3797 -0.0027 0.1164  -0.1607 624 HOH A O   
2550 O  O   . HOH G .   ? 0.6729 0.2910 0.3208 0.1342  -0.0863 -0.0445 625 HOH A O   
2551 O  O   . HOH G .   ? 0.3856 0.2113 0.4945 -0.0340 -0.1168 0.0399  626 HOH A O   
2552 O  O   . HOH G .   ? 0.4943 0.4217 0.3614 0.0335  0.2417  -0.0560 627 HOH A O   
2553 O  O   . HOH G .   ? 0.4578 0.4045 0.3188 -0.1295 -0.1194 0.0688  628 HOH A O   
2554 O  O   . HOH G .   ? 0.5695 0.3537 0.3463 -0.0983 0.1642  -0.1186 629 HOH A O   
2555 O  O   . HOH G .   ? 0.4501 0.2637 0.4591 0.1923  -0.1545 -0.0551 630 HOH A O   
2556 O  O   . HOH G .   ? 0.1958 0.4472 0.7785 0.0359  -0.0644 0.1509  631 HOH A O   
2557 O  O   . HOH G .   ? 0.2379 0.4068 0.2655 -0.0313 0.0322  -0.0895 632 HOH A O   
2558 O  O   . HOH G .   ? 0.4754 0.3560 0.3199 -0.1878 0.1263  -0.1439 633 HOH A O   
2559 O  O   . HOH G .   ? 0.5659 0.3366 0.3120 -0.0529 -0.1764 0.0441  634 HOH A O   
2560 O  O   . HOH G .   ? 0.3842 0.5881 0.4930 -0.0538 0.1385  -0.1057 635 HOH A O   
2561 O  O   . HOH G .   ? 0.4402 0.2262 0.5630 -0.0463 0.1448  -0.0820 636 HOH A O   
2562 O  O   . HOH G .   ? 0.2763 0.1562 0.2933 0.0188  -0.0458 0.0326  637 HOH A O   
2563 O  O   . HOH G .   ? 0.4863 0.2829 0.4849 0.1667  0.1743  0.0922  638 HOH A O   
2564 O  O   . HOH G .   ? 0.2711 0.3754 0.2465 0.1114  -0.0125 -0.0275 639 HOH A O   
2565 O  O   . HOH G .   ? 0.2603 0.3355 0.4767 0.0683  0.0485  0.0408  640 HOH A O   
2566 O  O   . HOH G .   ? 0.4607 0.2456 0.3959 0.0489  -0.1035 -0.0733 641 HOH A O   
2567 O  O   . HOH G .   ? 0.2504 0.3285 0.1955 0.0260  -0.0564 0.0120  642 HOH A O   
2568 O  O   . HOH G .   ? 0.1615 0.4126 0.3664 -0.0522 -0.0560 0.0423  643 HOH A O   
2569 O  O   . HOH G .   ? 0.2563 0.5935 0.3716 0.0810  0.0239  0.1867  644 HOH A O   
2570 O  O   . HOH G .   ? 0.1588 0.1445 0.2287 -0.0031 -0.0233 0.0126  645 HOH A O   
2571 O  O   . HOH G .   ? 0.2870 0.2140 0.1696 -0.0370 0.0152  -0.0013 646 HOH A O   
2572 O  O   . HOH G .   ? 0.2174 0.4208 0.2275 -0.0456 -0.0196 0.0834  647 HOH A O   
2573 O  O   . HOH G .   ? 0.2840 0.2235 0.2849 -0.0706 -0.0043 -0.0339 648 HOH A O   
2574 O  O   . HOH G .   ? 0.3285 0.3797 0.2176 -0.0206 -0.0070 0.0410  649 HOH A O   
2575 O  O   . HOH G .   ? 0.1344 0.6516 0.3289 0.0759  -0.0309 -0.1552 650 HOH A O   
2576 O  O   . HOH G .   ? 0.3285 0.1773 0.3713 0.0588  -0.0093 -0.0269 651 HOH A O   
2577 O  O   . HOH G .   ? 0.2594 0.5626 0.5210 0.0353  0.0988  0.2624  652 HOH A O   
2578 O  O   . HOH G .   ? 0.2678 0.3763 0.4805 -0.0439 0.0675  0.0074  653 HOH A O   
2579 O  O   . HOH G .   ? 0.3655 0.2388 0.5083 0.0073  0.0522  -0.0222 654 HOH A O   
2580 O  O   . HOH G .   ? 0.3111 0.4023 0.3397 -0.0043 0.0417  -0.0603 655 HOH A O   
2581 O  O   . HOH G .   ? 0.4866 0.2275 0.6043 0.0675  0.0516  0.0480  656 HOH A O   
2582 O  O   . HOH G .   ? 0.3619 0.3016 0.2316 -0.0340 0.0983  -0.0054 657 HOH A O   
2583 O  O   . HOH G .   ? 0.3005 0.3490 0.4390 0.1164  -0.0403 0.1018  658 HOH A O   
2584 O  O   . HOH G .   ? 0.3012 0.3014 0.4460 0.0147  0.0498  -0.0952 659 HOH A O   
2585 O  O   . HOH G .   ? 0.3167 0.4751 0.3289 -0.0469 -0.0419 -0.0658 660 HOH A O   
2586 O  O   . HOH G .   ? 0.5388 0.3366 0.6564 0.2368  0.2675  0.1256  661 HOH A O   
2587 O  O   . HOH G .   ? 0.1701 0.4898 0.4440 0.0357  -0.0432 -0.1167 662 HOH A O   
2588 O  O   . HOH G .   ? 0.1832 0.2991 0.3718 -0.0333 -0.0054 0.1225  663 HOH A O   
2589 O  O   . HOH G .   ? 0.4963 0.3409 0.3585 0.0785  -0.0815 0.0750  664 HOH A O   
2590 O  O   . HOH G .   ? 0.2431 0.3481 0.4108 0.0005  -0.0049 0.0162  665 HOH A O   
2591 O  O   . HOH G .   ? 0.3501 0.3118 0.3235 0.1438  0.1379  0.1155  666 HOH A O   
2592 O  O   . HOH G .   ? 0.3531 0.2269 0.3337 0.0000  0.0186  0.0006  667 HOH A O   
2593 O  O   . HOH G .   ? 0.3289 0.3650 0.3197 -0.0626 0.0403  0.0768  668 HOH A O   
2594 O  O   . HOH G .   ? 0.2544 0.7821 0.5241 0.1368  -0.0052 -0.1708 669 HOH A O   
2595 O  O   . HOH G .   ? 0.4435 0.2415 0.5155 0.0432  -0.0878 0.0390  670 HOH A O   
2596 O  O   . HOH G .   ? 0.2998 0.3738 0.4647 0.0370  0.0031  -0.0886 671 HOH A O   
2597 O  O   . HOH G .   ? 0.3738 0.1787 0.2811 -0.0003 0.0266  0.0109  672 HOH A O   
2598 O  O   . HOH G .   ? 0.4884 0.3377 0.5899 0.0130  -0.2098 -0.0991 673 HOH A O   
2599 O  O   . HOH G .   ? 0.7109 0.8669 0.4698 -0.3224 0.0878  0.2267  674 HOH A O   
2600 O  O   . HOH G .   ? 0.4341 0.6973 0.4013 -0.2660 0.0590  0.0337  675 HOH A O   
2601 O  O   . HOH G .   ? 0.4673 0.3291 0.4402 -0.0296 -0.1518 -0.1352 676 HOH A O   
2602 O  O   . HOH G .   ? 0.3928 0.5059 0.5985 0.2563  -0.0137 -0.0485 677 HOH A O   
2603 O  O   . HOH G .   ? 0.9039 0.3535 0.4712 0.1597  -0.1841 -0.1688 678 HOH A O   
2604 O  O   . HOH G .   ? 0.2849 0.5309 0.3630 -0.1448 0.0935  0.0109  679 HOH A O   
2605 O  O   . HOH G .   ? 0.3880 0.3134 0.3231 0.0491  -0.1074 -0.0715 680 HOH A O   
2606 O  O   . HOH G .   ? 0.4219 0.4429 0.6036 0.1102  -0.0621 -0.0155 681 HOH A O   
2607 O  O   . HOH G .   ? 0.3208 0.3127 0.7437 0.0065  -0.0147 0.0449  682 HOH A O   
2608 O  O   . HOH G .   ? 0.3348 0.3127 0.4264 -0.1030 0.1136  -0.0606 683 HOH A O   
2609 O  O   . HOH G .   ? 0.2906 0.5490 0.2978 -0.0785 -0.0623 0.0281  684 HOH A O   
2610 O  O   . HOH G .   ? 0.2919 0.4018 0.6276 -0.0966 0.0432  -0.1307 685 HOH A O   
2611 O  O   . HOH G .   ? 0.3070 0.2775 0.7005 -0.0383 -0.0908 -0.0119 686 HOH A O   
2612 O  O   . HOH G .   ? 0.1893 0.6818 0.3269 0.0529  0.0210  0.0621  687 HOH A O   
2613 O  O   . HOH G .   ? 0.5256 0.3014 0.3567 0.0597  -0.0019 0.1032  688 HOH A O   
2614 O  O   . HOH G .   ? 0.3422 0.5605 0.8557 -0.1964 -0.0146 -0.2675 689 HOH A O   
2615 O  O   . HOH G .   ? 0.2529 0.2494 0.3314 0.0724  -0.0680 -0.0878 690 HOH A O   
2616 O  O   . HOH G .   ? 0.3621 0.3786 0.4138 -0.0864 0.1123  -0.1316 691 HOH A O   
2617 O  O   . HOH G .   ? 0.3185 0.3427 0.4081 -0.0135 0.1164  -0.0920 692 HOH A O   
2618 O  O   . HOH G .   ? 0.4831 0.4476 0.1541 0.1827  0.0153  0.0401  693 HOH A O   
2619 O  O   . HOH G .   ? 0.5393 0.4386 0.7730 -0.2249 -0.1221 0.2436  694 HOH A O   
2620 O  O   . HOH G .   ? 0.3488 0.4693 0.5163 -0.0353 0.1344  0.2338  695 HOH A O   
2621 O  O   . HOH G .   ? 0.4065 0.7088 0.3770 -0.0474 -0.0491 -0.2976 696 HOH A O   
2622 O  O   . HOH G .   ? 0.4406 0.2102 0.7548 -0.0068 0.1764  0.1062  697 HOH A O   
2623 O  O   . HOH G .   ? 0.3871 1.4344 1.5010 -0.2495 -0.0702 -0.1899 698 HOH A O   
2624 O  O   . HOH G .   ? 0.2849 0.4032 0.2536 -0.0351 -0.0491 -0.0020 699 HOH A O   
2625 O  O   . HOH G .   ? 0.5048 0.6362 0.3434 -0.0640 0.1569  -0.0152 700 HOH A O   
2626 O  O   . HOH G .   ? 0.3370 0.2046 0.7523 -0.0070 -0.0692 0.0017  701 HOH A O   
2627 O  O   . HOH G .   ? 0.3569 0.3684 0.6201 -0.0520 0.1076  0.0920  702 HOH A O   
2628 O  O   . HOH G .   ? 0.7742 0.2815 0.4050 0.0217  0.3228  0.1070  703 HOH A O   
2629 O  O   . HOH G .   ? 0.3474 0.4176 0.7106 -0.0847 -0.0020 0.2712  704 HOH A O   
2630 O  O   . HOH G .   ? 0.4860 0.5349 0.3203 -0.1518 -0.0553 -0.0196 705 HOH A O   
2631 O  O   . HOH G .   ? 0.5371 0.4397 0.3659 -0.0658 -0.0931 0.0142  706 HOH A O   
2632 O  O   . HOH G .   ? 0.3783 0.4783 0.1949 0.0454  -0.0522 0.0693  707 HOH A O   
2633 O  O   . HOH G .   ? 0.5827 0.3528 0.2894 -0.1448 -0.1234 0.0544  708 HOH A O   
2634 O  O   . HOH G .   ? 0.4681 0.4632 0.3874 -0.0644 -0.0759 -0.0243 709 HOH A O   
2635 O  O   . HOH G .   ? 0.3973 0.4259 0.4801 -0.0966 0.0733  -0.0603 710 HOH A O   
2636 O  O   . HOH G .   ? 0.5044 0.3447 0.2984 0.0104  -0.0612 -0.0969 711 HOH A O   
2637 O  O   . HOH G .   ? 0.3086 0.4113 0.4849 0.0828  0.1401  0.1617  712 HOH A O   
2638 O  O   . HOH G .   ? 0.3314 0.5794 0.7139 -0.1533 -0.0071 0.2707  713 HOH A O   
2639 O  O   . HOH G .   ? 0.4963 0.7415 0.2269 -0.1299 0.1005  0.0588  714 HOH A O   
2640 O  O   . HOH G .   ? 0.5903 0.4165 0.2939 -0.0357 0.1321  0.0505  715 HOH A O   
2641 O  O   . HOH G .   ? 0.3321 0.4171 0.4514 0.0454  0.0000  0.1356  716 HOH A O   
2642 O  O   . HOH G .   ? 0.3583 0.3030 0.4153 -0.1243 0.0065  0.0710  717 HOH A O   
2643 O  O   . HOH G .   ? 0.5806 0.3801 0.3867 -0.1049 0.1298  -0.0333 718 HOH A O   
2644 O  O   . HOH G .   ? 0.3000 0.5388 0.3194 0.0781  0.0359  0.0255  719 HOH A O   
2645 O  O   . HOH G .   ? 0.3203 0.6036 0.2802 0.0930  0.0219  -0.1238 720 HOH A O   
2646 O  O   . HOH G .   ? 0.4796 0.4336 0.4889 0.2804  -0.1692 -0.1146 721 HOH A O   
2647 O  O   . HOH G .   ? 0.4354 0.3321 0.6147 0.0943  0.2284  0.1929  722 HOH A O   
2648 O  O   . HOH G .   ? 0.4011 0.2626 0.5131 -0.0697 -0.1474 0.0529  723 HOH A O   
2649 O  O   . HOH G .   ? 0.4535 0.4711 0.3273 0.1456  -0.0410 0.0063  724 HOH A O   
2650 O  O   . HOH G .   ? 0.6054 0.3404 0.8751 0.1250  0.2291  0.2171  725 HOH A O   
2651 O  O   . HOH G .   ? 0.3806 0.3118 0.2806 -0.0368 0.1579  -0.0043 726 HOH A O   
2652 O  O   . HOH G .   ? 0.3370 0.2660 0.4372 -0.0644 -0.0610 -0.0507 727 HOH A O   
2653 O  O   . HOH G .   ? 0.5895 0.4438 0.3095 0.0697  0.1026  -0.0322 728 HOH A O   
2654 O  O   . HOH G .   ? 0.7286 0.2608 0.6320 -0.0590 0.1005  0.0965  729 HOH A O   
2655 O  O   . HOH G .   ? 0.4153 0.2899 1.1348 0.0886  -0.1172 0.0406  730 HOH A O   
2656 O  O   . HOH G .   ? 0.3666 0.5590 0.7067 -0.1995 0.2162  -0.2118 731 HOH A O   
2657 O  O   . HOH G .   ? 0.3578 0.3106 0.4972 -0.0482 0.0093  -0.0856 732 HOH A O   
2658 O  O   . HOH G .   ? 0.3736 0.2536 0.6542 0.0237  -0.1475 0.1102  733 HOH A O   
2659 O  O   . HOH G .   ? 0.6984 0.4248 0.8202 -0.1005 -0.1535 -0.2206 734 HOH A O   
2660 O  O   . HOH G .   ? 0.4514 0.2599 0.4974 0.0337  0.1221  0.1092  735 HOH A O   
2661 O  O   . HOH G .   ? 0.2612 0.4541 0.9125 0.0081  0.0170  0.2849  736 HOH A O   
2662 O  O   . HOH G .   ? 0.3763 0.3878 0.3246 0.0449  0.0562  -0.0423 737 HOH A O   
2663 O  O   . HOH G .   ? 0.4974 0.3596 0.5163 -0.0740 0.0229  -0.1297 738 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 DMS 1   302 1   DMS DMS A . 
D 4 BCN 1   303 2   BCN BCN A . 
E 5 MES 1   304 3   MES MES A . 
F 6 V90 1   305 1   V90 V90 A . 
G 7 HOH 1   401 1   HOH HOH A . 
G 7 HOH 2   402 2   HOH HOH A . 
G 7 HOH 3   403 3   HOH HOH A . 
G 7 HOH 4   404 4   HOH HOH A . 
G 7 HOH 5   405 5   HOH HOH A . 
G 7 HOH 6   406 6   HOH HOH A . 
G 7 HOH 7   407 7   HOH HOH A . 
G 7 HOH 8   408 8   HOH HOH A . 
G 7 HOH 9   409 9   HOH HOH A . 
G 7 HOH 10  410 10  HOH HOH A . 
G 7 HOH 11  411 11  HOH HOH A . 
G 7 HOH 12  412 12  HOH HOH A . 
G 7 HOH 13  413 13  HOH HOH A . 
G 7 HOH 14  414 14  HOH HOH A . 
G 7 HOH 15  415 15  HOH HOH A . 
G 7 HOH 16  416 16  HOH HOH A . 
G 7 HOH 17  417 17  HOH HOH A . 
G 7 HOH 18  418 18  HOH HOH A . 
G 7 HOH 19  419 19  HOH HOH A . 
G 7 HOH 20  420 20  HOH HOH A . 
G 7 HOH 21  421 21  HOH HOH A . 
G 7 HOH 22  422 22  HOH HOH A . 
G 7 HOH 23  423 23  HOH HOH A . 
G 7 HOH 24  424 24  HOH HOH A . 
G 7 HOH 25  425 25  HOH HOH A . 
G 7 HOH 26  426 26  HOH HOH A . 
G 7 HOH 27  427 27  HOH HOH A . 
G 7 HOH 28  428 28  HOH HOH A . 
G 7 HOH 29  429 29  HOH HOH A . 
G 7 HOH 30  430 30  HOH HOH A . 
G 7 HOH 31  431 31  HOH HOH A . 
G 7 HOH 32  432 32  HOH HOH A . 
G 7 HOH 33  433 33  HOH HOH A . 
G 7 HOH 34  434 34  HOH HOH A . 
G 7 HOH 35  435 35  HOH HOH A . 
G 7 HOH 36  436 36  HOH HOH A . 
G 7 HOH 37  437 37  HOH HOH A . 
G 7 HOH 38  438 38  HOH HOH A . 
G 7 HOH 39  439 39  HOH HOH A . 
G 7 HOH 40  440 40  HOH HOH A . 
G 7 HOH 41  441 41  HOH HOH A . 
G 7 HOH 42  442 42  HOH HOH A . 
G 7 HOH 43  443 43  HOH HOH A . 
G 7 HOH 44  444 44  HOH HOH A . 
G 7 HOH 45  445 45  HOH HOH A . 
G 7 HOH 46  446 46  HOH HOH A . 
G 7 HOH 47  447 47  HOH HOH A . 
G 7 HOH 48  448 48  HOH HOH A . 
G 7 HOH 49  449 49  HOH HOH A . 
G 7 HOH 50  450 50  HOH HOH A . 
G 7 HOH 51  451 51  HOH HOH A . 
G 7 HOH 52  452 52  HOH HOH A . 
G 7 HOH 53  453 53  HOH HOH A . 
G 7 HOH 54  454 54  HOH HOH A . 
G 7 HOH 55  455 55  HOH HOH A . 
G 7 HOH 56  456 56  HOH HOH A . 
G 7 HOH 57  457 57  HOH HOH A . 
G 7 HOH 58  458 58  HOH HOH A . 
G 7 HOH 59  459 59  HOH HOH A . 
G 7 HOH 60  460 60  HOH HOH A . 
G 7 HOH 61  461 61  HOH HOH A . 
G 7 HOH 62  462 62  HOH HOH A . 
G 7 HOH 63  463 63  HOH HOH A . 
G 7 HOH 64  464 64  HOH HOH A . 
G 7 HOH 65  465 65  HOH HOH A . 
G 7 HOH 66  466 66  HOH HOH A . 
G 7 HOH 67  467 67  HOH HOH A . 
G 7 HOH 68  468 68  HOH HOH A . 
G 7 HOH 69  469 69  HOH HOH A . 
G 7 HOH 70  470 70  HOH HOH A . 
G 7 HOH 71  471 71  HOH HOH A . 
G 7 HOH 72  472 72  HOH HOH A . 
G 7 HOH 73  473 73  HOH HOH A . 
G 7 HOH 74  474 74  HOH HOH A . 
G 7 HOH 75  475 75  HOH HOH A . 
G 7 HOH 76  476 76  HOH HOH A . 
G 7 HOH 77  477 77  HOH HOH A . 
G 7 HOH 78  478 78  HOH HOH A . 
G 7 HOH 79  479 79  HOH HOH A . 
G 7 HOH 80  480 80  HOH HOH A . 
G 7 HOH 81  481 81  HOH HOH A . 
G 7 HOH 82  482 82  HOH HOH A . 
G 7 HOH 83  483 83  HOH HOH A . 
G 7 HOH 84  484 84  HOH HOH A . 
G 7 HOH 85  485 85  HOH HOH A . 
G 7 HOH 86  486 86  HOH HOH A . 
G 7 HOH 87  487 87  HOH HOH A . 
G 7 HOH 88  488 88  HOH HOH A . 
G 7 HOH 89  489 89  HOH HOH A . 
G 7 HOH 90  490 90  HOH HOH A . 
G 7 HOH 91  491 91  HOH HOH A . 
G 7 HOH 92  492 92  HOH HOH A . 
G 7 HOH 93  493 93  HOH HOH A . 
G 7 HOH 94  494 94  HOH HOH A . 
G 7 HOH 95  495 95  HOH HOH A . 
G 7 HOH 96  496 96  HOH HOH A . 
G 7 HOH 97  497 97  HOH HOH A . 
G 7 HOH 98  498 98  HOH HOH A . 
G 7 HOH 99  499 99  HOH HOH A . 
G 7 HOH 100 500 100 HOH HOH A . 
G 7 HOH 101 501 101 HOH HOH A . 
G 7 HOH 102 502 102 HOH HOH A . 
G 7 HOH 103 503 103 HOH HOH A . 
G 7 HOH 104 504 104 HOH HOH A . 
G 7 HOH 105 505 105 HOH HOH A . 
G 7 HOH 106 506 106 HOH HOH A . 
G 7 HOH 107 507 107 HOH HOH A . 
G 7 HOH 108 508 108 HOH HOH A . 
G 7 HOH 109 509 109 HOH HOH A . 
G 7 HOH 110 510 110 HOH HOH A . 
G 7 HOH 111 511 111 HOH HOH A . 
G 7 HOH 112 512 112 HOH HOH A . 
G 7 HOH 113 513 113 HOH HOH A . 
G 7 HOH 114 514 114 HOH HOH A . 
G 7 HOH 115 515 115 HOH HOH A . 
G 7 HOH 116 516 116 HOH HOH A . 
G 7 HOH 117 517 117 HOH HOH A . 
G 7 HOH 118 518 118 HOH HOH A . 
G 7 HOH 119 519 119 HOH HOH A . 
G 7 HOH 120 520 120 HOH HOH A . 
G 7 HOH 121 521 121 HOH HOH A . 
G 7 HOH 122 522 122 HOH HOH A . 
G 7 HOH 123 523 123 HOH HOH A . 
G 7 HOH 124 524 125 HOH HOH A . 
G 7 HOH 125 525 126 HOH HOH A . 
G 7 HOH 126 526 127 HOH HOH A . 
G 7 HOH 127 527 128 HOH HOH A . 
G 7 HOH 128 528 129 HOH HOH A . 
G 7 HOH 129 529 130 HOH HOH A . 
G 7 HOH 130 530 131 HOH HOH A . 
G 7 HOH 131 531 132 HOH HOH A . 
G 7 HOH 132 532 133 HOH HOH A . 
G 7 HOH 133 533 134 HOH HOH A . 
G 7 HOH 134 534 135 HOH HOH A . 
G 7 HOH 135 535 137 HOH HOH A . 
G 7 HOH 136 536 138 HOH HOH A . 
G 7 HOH 137 537 139 HOH HOH A . 
G 7 HOH 138 538 140 HOH HOH A . 
G 7 HOH 139 539 141 HOH HOH A . 
G 7 HOH 140 540 142 HOH HOH A . 
G 7 HOH 141 541 143 HOH HOH A . 
G 7 HOH 142 542 144 HOH HOH A . 
G 7 HOH 143 543 145 HOH HOH A . 
G 7 HOH 144 544 146 HOH HOH A . 
G 7 HOH 145 545 147 HOH HOH A . 
G 7 HOH 146 546 148 HOH HOH A . 
G 7 HOH 147 547 149 HOH HOH A . 
G 7 HOH 148 548 150 HOH HOH A . 
G 7 HOH 149 549 151 HOH HOH A . 
G 7 HOH 150 550 152 HOH HOH A . 
G 7 HOH 151 551 153 HOH HOH A . 
G 7 HOH 152 552 154 HOH HOH A . 
G 7 HOH 153 553 155 HOH HOH A . 
G 7 HOH 154 554 156 HOH HOH A . 
G 7 HOH 155 555 157 HOH HOH A . 
G 7 HOH 156 556 158 HOH HOH A . 
G 7 HOH 157 557 159 HOH HOH A . 
G 7 HOH 158 558 160 HOH HOH A . 
G 7 HOH 159 559 161 HOH HOH A . 
G 7 HOH 160 560 162 HOH HOH A . 
G 7 HOH 161 561 163 HOH HOH A . 
G 7 HOH 162 562 164 HOH HOH A . 
G 7 HOH 163 563 165 HOH HOH A . 
G 7 HOH 164 564 166 HOH HOH A . 
G 7 HOH 165 565 167 HOH HOH A . 
G 7 HOH 166 566 168 HOH HOH A . 
G 7 HOH 167 567 169 HOH HOH A . 
G 7 HOH 168 568 170 HOH HOH A . 
G 7 HOH 169 569 171 HOH HOH A . 
G 7 HOH 170 570 172 HOH HOH A . 
G 7 HOH 171 571 173 HOH HOH A . 
G 7 HOH 172 572 174 HOH HOH A . 
G 7 HOH 173 573 175 HOH HOH A . 
G 7 HOH 174 574 176 HOH HOH A . 
G 7 HOH 175 575 177 HOH HOH A . 
G 7 HOH 176 576 178 HOH HOH A . 
G 7 HOH 177 577 179 HOH HOH A . 
G 7 HOH 178 578 180 HOH HOH A . 
G 7 HOH 179 579 181 HOH HOH A . 
G 7 HOH 180 580 182 HOH HOH A . 
G 7 HOH 181 581 183 HOH HOH A . 
G 7 HOH 182 582 184 HOH HOH A . 
G 7 HOH 183 583 185 HOH HOH A . 
G 7 HOH 184 584 186 HOH HOH A . 
G 7 HOH 185 585 187 HOH HOH A . 
G 7 HOH 186 586 188 HOH HOH A . 
G 7 HOH 187 587 189 HOH HOH A . 
G 7 HOH 188 588 190 HOH HOH A . 
G 7 HOH 189 589 191 HOH HOH A . 
G 7 HOH 190 590 192 HOH HOH A . 
G 7 HOH 191 591 193 HOH HOH A . 
G 7 HOH 192 592 194 HOH HOH A . 
G 7 HOH 193 593 195 HOH HOH A . 
G 7 HOH 194 594 196 HOH HOH A . 
G 7 HOH 195 595 197 HOH HOH A . 
G 7 HOH 196 596 198 HOH HOH A . 
G 7 HOH 197 597 199 HOH HOH A . 
G 7 HOH 198 598 200 HOH HOH A . 
G 7 HOH 199 599 201 HOH HOH A . 
G 7 HOH 200 600 202 HOH HOH A . 
G 7 HOH 201 601 203 HOH HOH A . 
G 7 HOH 202 602 204 HOH HOH A . 
G 7 HOH 203 603 205 HOH HOH A . 
G 7 HOH 204 604 206 HOH HOH A . 
G 7 HOH 205 605 207 HOH HOH A . 
G 7 HOH 206 606 208 HOH HOH A . 
G 7 HOH 207 607 209 HOH HOH A . 
G 7 HOH 208 608 210 HOH HOH A . 
G 7 HOH 209 609 211 HOH HOH A . 
G 7 HOH 210 610 212 HOH HOH A . 
G 7 HOH 211 611 213 HOH HOH A . 
G 7 HOH 212 612 214 HOH HOH A . 
G 7 HOH 213 613 215 HOH HOH A . 
G 7 HOH 214 614 216 HOH HOH A . 
G 7 HOH 215 615 217 HOH HOH A . 
G 7 HOH 216 616 218 HOH HOH A . 
G 7 HOH 217 617 219 HOH HOH A . 
G 7 HOH 218 618 220 HOH HOH A . 
G 7 HOH 219 619 221 HOH HOH A . 
G 7 HOH 220 620 222 HOH HOH A . 
G 7 HOH 221 621 223 HOH HOH A . 
G 7 HOH 222 622 224 HOH HOH A . 
G 7 HOH 223 623 225 HOH HOH A . 
G 7 HOH 224 624 226 HOH HOH A . 
G 7 HOH 225 625 227 HOH HOH A . 
G 7 HOH 226 626 228 HOH HOH A . 
G 7 HOH 227 627 229 HOH HOH A . 
G 7 HOH 228 628 230 HOH HOH A . 
G 7 HOH 229 629 231 HOH HOH A . 
G 7 HOH 230 630 232 HOH HOH A . 
G 7 HOH 231 631 233 HOH HOH A . 
G 7 HOH 232 632 234 HOH HOH A . 
G 7 HOH 233 633 235 HOH HOH A . 
G 7 HOH 234 634 236 HOH HOH A . 
G 7 HOH 235 635 237 HOH HOH A . 
G 7 HOH 236 636 238 HOH HOH A . 
G 7 HOH 237 637 239 HOH HOH A . 
G 7 HOH 238 638 240 HOH HOH A . 
G 7 HOH 239 639 241 HOH HOH A . 
G 7 HOH 240 640 242 HOH HOH A . 
G 7 HOH 241 641 243 HOH HOH A . 
G 7 HOH 242 642 244 HOH HOH A . 
G 7 HOH 243 643 245 HOH HOH A . 
G 7 HOH 244 644 246 HOH HOH A . 
G 7 HOH 245 645 247 HOH HOH A . 
G 7 HOH 246 646 248 HOH HOH A . 
G 7 HOH 247 647 249 HOH HOH A . 
G 7 HOH 248 648 250 HOH HOH A . 
G 7 HOH 249 649 251 HOH HOH A . 
G 7 HOH 250 650 252 HOH HOH A . 
G 7 HOH 251 651 253 HOH HOH A . 
G 7 HOH 252 652 254 HOH HOH A . 
G 7 HOH 253 653 255 HOH HOH A . 
G 7 HOH 254 654 256 HOH HOH A . 
G 7 HOH 255 655 257 HOH HOH A . 
G 7 HOH 256 656 258 HOH HOH A . 
G 7 HOH 257 657 259 HOH HOH A . 
G 7 HOH 258 658 260 HOH HOH A . 
G 7 HOH 259 659 261 HOH HOH A . 
G 7 HOH 260 660 262 HOH HOH A . 
G 7 HOH 261 661 263 HOH HOH A . 
G 7 HOH 262 662 264 HOH HOH A . 
G 7 HOH 263 663 265 HOH HOH A . 
G 7 HOH 264 664 266 HOH HOH A . 
G 7 HOH 265 665 267 HOH HOH A . 
G 7 HOH 266 666 268 HOH HOH A . 
G 7 HOH 267 667 269 HOH HOH A . 
G 7 HOH 268 668 270 HOH HOH A . 
G 7 HOH 269 669 271 HOH HOH A . 
G 7 HOH 270 670 272 HOH HOH A . 
G 7 HOH 271 671 273 HOH HOH A . 
G 7 HOH 272 672 274 HOH HOH A . 
G 7 HOH 273 673 275 HOH HOH A . 
G 7 HOH 274 674 276 HOH HOH A . 
G 7 HOH 275 675 277 HOH HOH A . 
G 7 HOH 276 676 278 HOH HOH A . 
G 7 HOH 277 677 279 HOH HOH A . 
G 7 HOH 278 678 280 HOH HOH A . 
G 7 HOH 279 679 281 HOH HOH A . 
G 7 HOH 280 680 282 HOH HOH A . 
G 7 HOH 281 681 283 HOH HOH A . 
G 7 HOH 282 682 284 HOH HOH A . 
G 7 HOH 283 683 285 HOH HOH A . 
G 7 HOH 284 684 286 HOH HOH A . 
G 7 HOH 285 685 287 HOH HOH A . 
G 7 HOH 286 686 288 HOH HOH A . 
G 7 HOH 287 687 289 HOH HOH A . 
G 7 HOH 288 688 290 HOH HOH A . 
G 7 HOH 289 689 291 HOH HOH A . 
G 7 HOH 290 690 292 HOH HOH A . 
G 7 HOH 291 691 293 HOH HOH A . 
G 7 HOH 292 692 294 HOH HOH A . 
G 7 HOH 293 693 295 HOH HOH A . 
G 7 HOH 294 694 296 HOH HOH A . 
G 7 HOH 295 695 297 HOH HOH A . 
G 7 HOH 296 696 298 HOH HOH A . 
G 7 HOH 297 697 299 HOH HOH A . 
G 7 HOH 298 698 300 HOH HOH A . 
G 7 HOH 299 699 301 HOH HOH A . 
G 7 HOH 300 700 302 HOH HOH A . 
G 7 HOH 301 701 303 HOH HOH A . 
G 7 HOH 302 702 304 HOH HOH A . 
G 7 HOH 303 703 305 HOH HOH A . 
G 7 HOH 304 704 306 HOH HOH A . 
G 7 HOH 305 705 307 HOH HOH A . 
G 7 HOH 306 706 308 HOH HOH A . 
G 7 HOH 307 707 309 HOH HOH A . 
G 7 HOH 308 708 310 HOH HOH A . 
G 7 HOH 309 709 311 HOH HOH A . 
G 7 HOH 310 710 312 HOH HOH A . 
G 7 HOH 311 711 313 HOH HOH A . 
G 7 HOH 312 712 314 HOH HOH A . 
G 7 HOH 313 713 315 HOH HOH A . 
G 7 HOH 314 714 316 HOH HOH A . 
G 7 HOH 315 715 317 HOH HOH A . 
G 7 HOH 316 716 318 HOH HOH A . 
G 7 HOH 317 717 319 HOH HOH A . 
G 7 HOH 318 718 320 HOH HOH A . 
G 7 HOH 319 719 321 HOH HOH A . 
G 7 HOH 320 720 322 HOH HOH A . 
G 7 HOH 321 721 323 HOH HOH A . 
G 7 HOH 322 722 324 HOH HOH A . 
G 7 HOH 323 723 325 HOH HOH A . 
G 7 HOH 324 724 326 HOH HOH A . 
G 7 HOH 325 725 327 HOH HOH A . 
G 7 HOH 326 726 328 HOH HOH A . 
G 7 HOH 327 727 329 HOH HOH A . 
G 7 HOH 328 728 330 HOH HOH A . 
G 7 HOH 329 729 331 HOH HOH A . 
G 7 HOH 330 730 332 HOH HOH A . 
G 7 HOH 331 731 333 HOH HOH A . 
G 7 HOH 332 732 334 HOH HOH A . 
G 7 HOH 333 733 335 HOH HOH A . 
G 7 HOH 334 734 336 HOH HOH A . 
G 7 HOH 335 735 337 HOH HOH A . 
G 7 HOH 336 736 338 HOH HOH A . 
G 7 HOH 337 737 339 HOH HOH A . 
G 7 HOH 338 738 340 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.7 ? 
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_555 110.8 ? 
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_555 100.5 ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 A F V90 .   ? A V90 305 ? 1_555 108.1 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 A F V90 .   ? A V90 305 ? 1_555 114.9 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 A F V90 .   ? A V90 305 ? 1_555 117.9 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 B F V90 .   ? A V90 305 ? 1_555 116.4 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 B F V90 .   ? A V90 305 ? 1_555 123.9 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 B F V90 .   ? A V90 305 ? 1_555 100.1 ? 
10 N11 A F V90 .   ? A V90 305 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 B F V90 .   ? A V90 305 ? 1_555 17.9  ? 
11 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S8  A F V90 .   ? A V90 305 ? 1_555 95.7  ? 
12 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S8  A F V90 .   ? A V90 305 ? 1_555 143.0 ? 
13 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S8  A F V90 .   ? A V90 305 ? 1_555 101.5 ? 
14 N11 A F V90 .   ? A V90 305 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S8  A F V90 .   ? A V90 305 ? 1_555 28.2  ? 
15 N11 B F V90 .   ? A V90 305 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S8  A F V90 .   ? A V90 305 ? 1_555 22.3  ? 
# 
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_alt_id'  
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
18 3 'Structure model' '_pdbx_struct_conn_angle.value'               
19 3 'Structure model' '_struct_conn.pdbx_dist_value'                
20 3 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
21 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
22 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
23 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
24 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
25 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
26 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
27 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
28 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
29 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
30 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
31 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
32 3 'Structure model' '_struct_ref_seq_dif.details'                 
33 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
34 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
35 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
SCALA       3.3.20 2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk 'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 2 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 3 
HKL-2000    .      ?               ?       ?                    ?                     'data collection' ? ?          ? 4 
XDS         .      ?               ?       ?                    ?                     'data reduction'  ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                     phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 71  ? B CG A ASP 71  ? B OD2 A ASP 71  ? B 125.47 118.30 7.17   0.90 N 
2 1 CG A ARG 89  ? B CD A ARG 89  ? B NE  A ARG 89  ? B 78.69  111.80 -33.11 2.10 N 
3 1 CB A LEU 223 ? B CG A LEU 223 ? B CD1 A LEU 223 ? B 130.07 111.00 19.07  1.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -142.71 55.55   
2 1 LEU A 57  ? ? -120.61 -53.99  
3 1 LYS A 76  ? B -107.26 -87.34  
4 1 LYS A 111 ? ? 74.78   -7.04   
5 1 PHE A 175 ? ? -155.75 80.87   
6 1 ASN A 243 ? ? -95.05  53.00   
7 1 LYS A 251 ? ? 54.78   -137.17 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 A MES 304 ? O1S ? E MES 1 O1S 
2 1 N 1 A MES 304 ? O2S ? E MES 1 O2S 
3 1 N 1 A MES 304 ? O3S ? E MES 1 O3S 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MES O1   O  N N 264 
MES C2   C  N N 265 
MES C3   C  N N 266 
MES N4   N  N N 267 
MES C5   C  N N 268 
MES C6   C  N N 269 
MES C7   C  N N 270 
MES C8   C  N N 271 
MES S    S  N N 272 
MES O1S  O  N N 273 
MES O2S  O  N N 274 
MES O3S  O  N N 275 
MES H21  H  N N 276 
MES H22  H  N N 277 
MES H31  H  N N 278 
MES H32  H  N N 279 
MES HN4  H  N N 280 
MES H51  H  N N 281 
MES H52  H  N N 282 
MES H61  H  N N 283 
MES H62  H  N N 284 
MES H71  H  N N 285 
MES H72  H  N N 286 
MES H81  H  N N 287 
MES H82  H  N N 288 
MET N    N  N N 289 
MET CA   C  N S 290 
MET C    C  N N 291 
MET O    O  N N 292 
MET CB   C  N N 293 
MET CG   C  N N 294 
MET SD   S  N N 295 
MET CE   C  N N 296 
MET OXT  O  N N 297 
MET H    H  N N 298 
MET H2   H  N N 299 
MET HA   H  N N 300 
MET HB2  H  N N 301 
MET HB3  H  N N 302 
MET HG2  H  N N 303 
MET HG3  H  N N 304 
MET HE1  H  N N 305 
MET HE2  H  N N 306 
MET HE3  H  N N 307 
MET HXT  H  N N 308 
PHE N    N  N N 309 
PHE CA   C  N S 310 
PHE C    C  N N 311 
PHE O    O  N N 312 
PHE CB   C  N N 313 
PHE CG   C  Y N 314 
PHE CD1  C  Y N 315 
PHE CD2  C  Y N 316 
PHE CE1  C  Y N 317 
PHE CE2  C  Y N 318 
PHE CZ   C  Y N 319 
PHE OXT  O  N N 320 
PHE H    H  N N 321 
PHE H2   H  N N 322 
PHE HA   H  N N 323 
PHE HB2  H  N N 324 
PHE HB3  H  N N 325 
PHE HD1  H  N N 326 
PHE HD2  H  N N 327 
PHE HE1  H  N N 328 
PHE HE2  H  N N 329 
PHE HZ   H  N N 330 
PHE HXT  H  N N 331 
PRO N    N  N N 332 
PRO CA   C  N S 333 
PRO C    C  N N 334 
PRO O    O  N N 335 
PRO CB   C  N N 336 
PRO CG   C  N N 337 
PRO CD   C  N N 338 
PRO OXT  O  N N 339 
PRO H    H  N N 340 
PRO HA   H  N N 341 
PRO HB2  H  N N 342 
PRO HB3  H  N N 343 
PRO HG2  H  N N 344 
PRO HG3  H  N N 345 
PRO HD2  H  N N 346 
PRO HD3  H  N N 347 
PRO HXT  H  N N 348 
SER N    N  N N 349 
SER CA   C  N S 350 
SER C    C  N N 351 
SER O    O  N N 352 
SER CB   C  N N 353 
SER OG   O  N N 354 
SER OXT  O  N N 355 
SER H    H  N N 356 
SER H2   H  N N 357 
SER HA   H  N N 358 
SER HB2  H  N N 359 
SER HB3  H  N N 360 
SER HG   H  N N 361 
SER HXT  H  N N 362 
THR N    N  N N 363 
THR CA   C  N S 364 
THR C    C  N N 365 
THR O    O  N N 366 
THR CB   C  N R 367 
THR OG1  O  N N 368 
THR CG2  C  N N 369 
THR OXT  O  N N 370 
THR H    H  N N 371 
THR H2   H  N N 372 
THR HA   H  N N 373 
THR HB   H  N N 374 
THR HG1  H  N N 375 
THR HG21 H  N N 376 
THR HG22 H  N N 377 
THR HG23 H  N N 378 
THR HXT  H  N N 379 
TRP N    N  N N 380 
TRP CA   C  N S 381 
TRP C    C  N N 382 
TRP O    O  N N 383 
TRP CB   C  N N 384 
TRP CG   C  Y N 385 
TRP CD1  C  Y N 386 
TRP CD2  C  Y N 387 
TRP NE1  N  Y N 388 
TRP CE2  C  Y N 389 
TRP CE3  C  Y N 390 
TRP CZ2  C  Y N 391 
TRP CZ3  C  Y N 392 
TRP CH2  C  Y N 393 
TRP OXT  O  N N 394 
TRP H    H  N N 395 
TRP H2   H  N N 396 
TRP HA   H  N N 397 
TRP HB2  H  N N 398 
TRP HB3  H  N N 399 
TRP HD1  H  N N 400 
TRP HE1  H  N N 401 
TRP HE3  H  N N 402 
TRP HZ2  H  N N 403 
TRP HZ3  H  N N 404 
TRP HH2  H  N N 405 
TRP HXT  H  N N 406 
TYR N    N  N N 407 
TYR CA   C  N S 408 
TYR C    C  N N 409 
TYR O    O  N N 410 
TYR CB   C  N N 411 
TYR CG   C  Y N 412 
TYR CD1  C  Y N 413 
TYR CD2  C  Y N 414 
TYR CE1  C  Y N 415 
TYR CE2  C  Y N 416 
TYR CZ   C  Y N 417 
TYR OH   O  N N 418 
TYR OXT  O  N N 419 
TYR H    H  N N 420 
TYR H2   H  N N 421 
TYR HA   H  N N 422 
TYR HB2  H  N N 423 
TYR HB3  H  N N 424 
TYR HD1  H  N N 425 
TYR HD2  H  N N 426 
TYR HE1  H  N N 427 
TYR HE2  H  N N 428 
TYR HH   H  N N 429 
TYR HXT  H  N N 430 
V90 F18  F  N N 431 
V90 C5   C  Y N 432 
V90 C6   C  Y N 433 
V90 S12  S  N N 434 
V90 C13  C  N N 435 
V90 C14  C  N N 436 
V90 O15  O  N N 437 
V90 C1   C  Y N 438 
V90 F17  F  N N 439 
V90 C4   C  Y N 440 
V90 C3   C  Y N 441 
V90 S8   S  N N 442 
V90 O10  O  N N 443 
V90 N11  N  N N 444 
V90 O9   O  N N 445 
V90 C2   C  Y N 446 
V90 F16  F  N N 447 
V90 N7   N  N N 448 
V90 C19  C  N N 449 
V90 C26  C  N N 450 
V90 C25  C  N N 451 
V90 C24  C  N N 452 
V90 C23  C  N N 453 
V90 C22  C  N N 454 
V90 C21  C  N N 455 
V90 C20  C  N N 456 
V90 H1   H  N N 457 
V90 H2   H  N N 458 
V90 H3   H  N N 459 
V90 H4   H  N N 460 
V90 H5   H  N N 461 
V90 H6   H  N N 462 
V90 H7   H  N N 463 
V90 H8   H  N N 464 
V90 H9   H  N N 465 
V90 H10  H  N N 466 
V90 H11  H  N N 467 
V90 H12  H  N N 468 
V90 H13  H  N N 469 
V90 H14  H  N N 470 
V90 H15  H  N N 471 
V90 H16  H  N N 472 
V90 H17  H  N N 473 
V90 H18  H  N N 474 
V90 H19  H  N N 475 
V90 H20  H  N N 476 
V90 H21  H  N N 477 
V90 H22  H  N N 478 
V90 H23  H  N N 479 
VAL N    N  N N 480 
VAL CA   C  N S 481 
VAL C    C  N N 482 
VAL O    O  N N 483 
VAL CB   C  N N 484 
VAL CG1  C  N N 485 
VAL CG2  C  N N 486 
VAL OXT  O  N N 487 
VAL H    H  N N 488 
VAL H2   H  N N 489 
VAL HA   H  N N 490 
VAL HB   H  N N 491 
VAL HG11 H  N N 492 
VAL HG12 H  N N 493 
VAL HG13 H  N N 494 
VAL HG21 H  N N 495 
VAL HG22 H  N N 496 
VAL HG23 H  N N 497 
VAL HXT  H  N N 498 
ZN  ZN   ZN N N 499 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MES O1  C2   sing N N 250 
MES O1  C6   sing N N 251 
MES C2  C3   sing N N 252 
MES C2  H21  sing N N 253 
MES C2  H22  sing N N 254 
MES C3  N4   sing N N 255 
MES C3  H31  sing N N 256 
MES C3  H32  sing N N 257 
MES N4  C5   sing N N 258 
MES N4  C7   sing N N 259 
MES N4  HN4  sing N N 260 
MES C5  C6   sing N N 261 
MES C5  H51  sing N N 262 
MES C5  H52  sing N N 263 
MES C6  H61  sing N N 264 
MES C6  H62  sing N N 265 
MES C7  C8   sing N N 266 
MES C7  H71  sing N N 267 
MES C7  H72  sing N N 268 
MES C8  S    sing N N 269 
MES C8  H81  sing N N 270 
MES C8  H82  sing N N 271 
MES S   O1S  doub N N 272 
MES S   O2S  doub N N 273 
MES S   O3S  sing N N 274 
MET N   CA   sing N N 275 
MET N   H    sing N N 276 
MET N   H2   sing N N 277 
MET CA  C    sing N N 278 
MET CA  CB   sing N N 279 
MET CA  HA   sing N N 280 
MET C   O    doub N N 281 
MET C   OXT  sing N N 282 
MET CB  CG   sing N N 283 
MET CB  HB2  sing N N 284 
MET CB  HB3  sing N N 285 
MET CG  SD   sing N N 286 
MET CG  HG2  sing N N 287 
MET CG  HG3  sing N N 288 
MET SD  CE   sing N N 289 
MET CE  HE1  sing N N 290 
MET CE  HE2  sing N N 291 
MET CE  HE3  sing N N 292 
MET OXT HXT  sing N N 293 
PHE N   CA   sing N N 294 
PHE N   H    sing N N 295 
PHE N   H2   sing N N 296 
PHE CA  C    sing N N 297 
PHE CA  CB   sing N N 298 
PHE CA  HA   sing N N 299 
PHE C   O    doub N N 300 
PHE C   OXT  sing N N 301 
PHE CB  CG   sing N N 302 
PHE CB  HB2  sing N N 303 
PHE CB  HB3  sing N N 304 
PHE CG  CD1  doub Y N 305 
PHE CG  CD2  sing Y N 306 
PHE CD1 CE1  sing Y N 307 
PHE CD1 HD1  sing N N 308 
PHE CD2 CE2  doub Y N 309 
PHE CD2 HD2  sing N N 310 
PHE CE1 CZ   doub Y N 311 
PHE CE1 HE1  sing N N 312 
PHE CE2 CZ   sing Y N 313 
PHE CE2 HE2  sing N N 314 
PHE CZ  HZ   sing N N 315 
PHE OXT HXT  sing N N 316 
PRO N   CA   sing N N 317 
PRO N   CD   sing N N 318 
PRO N   H    sing N N 319 
PRO CA  C    sing N N 320 
PRO CA  CB   sing N N 321 
PRO CA  HA   sing N N 322 
PRO C   O    doub N N 323 
PRO C   OXT  sing N N 324 
PRO CB  CG   sing N N 325 
PRO CB  HB2  sing N N 326 
PRO CB  HB3  sing N N 327 
PRO CG  CD   sing N N 328 
PRO CG  HG2  sing N N 329 
PRO CG  HG3  sing N N 330 
PRO CD  HD2  sing N N 331 
PRO CD  HD3  sing N N 332 
PRO OXT HXT  sing N N 333 
SER N   CA   sing N N 334 
SER N   H    sing N N 335 
SER N   H2   sing N N 336 
SER CA  C    sing N N 337 
SER CA  CB   sing N N 338 
SER CA  HA   sing N N 339 
SER C   O    doub N N 340 
SER C   OXT  sing N N 341 
SER CB  OG   sing N N 342 
SER CB  HB2  sing N N 343 
SER CB  HB3  sing N N 344 
SER OG  HG   sing N N 345 
SER OXT HXT  sing N N 346 
THR N   CA   sing N N 347 
THR N   H    sing N N 348 
THR N   H2   sing N N 349 
THR CA  C    sing N N 350 
THR CA  CB   sing N N 351 
THR CA  HA   sing N N 352 
THR C   O    doub N N 353 
THR C   OXT  sing N N 354 
THR CB  OG1  sing N N 355 
THR CB  CG2  sing N N 356 
THR CB  HB   sing N N 357 
THR OG1 HG1  sing N N 358 
THR CG2 HG21 sing N N 359 
THR CG2 HG22 sing N N 360 
THR CG2 HG23 sing N N 361 
THR OXT HXT  sing N N 362 
TRP N   CA   sing N N 363 
TRP N   H    sing N N 364 
TRP N   H2   sing N N 365 
TRP CA  C    sing N N 366 
TRP CA  CB   sing N N 367 
TRP CA  HA   sing N N 368 
TRP C   O    doub N N 369 
TRP C   OXT  sing N N 370 
TRP CB  CG   sing N N 371 
TRP CB  HB2  sing N N 372 
TRP CB  HB3  sing N N 373 
TRP CG  CD1  doub Y N 374 
TRP CG  CD2  sing Y N 375 
TRP CD1 NE1  sing Y N 376 
TRP CD1 HD1  sing N N 377 
TRP CD2 CE2  doub Y N 378 
TRP CD2 CE3  sing Y N 379 
TRP NE1 CE2  sing Y N 380 
TRP NE1 HE1  sing N N 381 
TRP CE2 CZ2  sing Y N 382 
TRP CE3 CZ3  doub Y N 383 
TRP CE3 HE3  sing N N 384 
TRP CZ2 CH2  doub Y N 385 
TRP CZ2 HZ2  sing N N 386 
TRP CZ3 CH2  sing Y N 387 
TRP CZ3 HZ3  sing N N 388 
TRP CH2 HH2  sing N N 389 
TRP OXT HXT  sing N N 390 
TYR N   CA   sing N N 391 
TYR N   H    sing N N 392 
TYR N   H2   sing N N 393 
TYR CA  C    sing N N 394 
TYR CA  CB   sing N N 395 
TYR CA  HA   sing N N 396 
TYR C   O    doub N N 397 
TYR C   OXT  sing N N 398 
TYR CB  CG   sing N N 399 
TYR CB  HB2  sing N N 400 
TYR CB  HB3  sing N N 401 
TYR CG  CD1  doub Y N 402 
TYR CG  CD2  sing Y N 403 
TYR CD1 CE1  sing Y N 404 
TYR CD1 HD1  sing N N 405 
TYR CD2 CE2  doub Y N 406 
TYR CD2 HD2  sing N N 407 
TYR CE1 CZ   doub Y N 408 
TYR CE1 HE1  sing N N 409 
TYR CE2 CZ   sing Y N 410 
TYR CE2 HE2  sing N N 411 
TYR CZ  OH   sing N N 412 
TYR OH  HH   sing N N 413 
TYR OXT HXT  sing N N 414 
V90 C22 C23  sing N N 415 
V90 C22 C21  sing N N 416 
V90 C23 C24  sing N N 417 
V90 C24 C25  sing N N 418 
V90 O15 C14  sing N N 419 
V90 C21 C20  sing N N 420 
V90 C14 C13  sing N N 421 
V90 C25 C26  sing N N 422 
V90 C20 C19  sing N N 423 
V90 C13 S12  sing N N 424 
V90 C26 C19  sing N N 425 
V90 C19 N7   sing N N 426 
V90 F18 C5   sing N N 427 
V90 S12 C6   sing N N 428 
V90 C5  C6   doub Y N 429 
V90 C5  C4   sing Y N 430 
V90 N7  C4   sing N N 431 
V90 C6  C1   sing Y N 432 
V90 C4  C3   doub Y N 433 
V90 C1  F17  sing N N 434 
V90 C1  C2   doub Y N 435 
V90 C3  C2   sing Y N 436 
V90 C3  S8   sing N N 437 
V90 N11 S8   sing N N 438 
V90 C2  F16  sing N N 439 
V90 O10 S8   doub N N 440 
V90 S8  O9   doub N N 441 
V90 C13 H1   sing N N 442 
V90 C13 H2   sing N N 443 
V90 C14 H3   sing N N 444 
V90 C14 H4   sing N N 445 
V90 O15 H5   sing N N 446 
V90 N11 H6   sing N N 447 
V90 N11 H7   sing N N 448 
V90 N7  H8   sing N N 449 
V90 C19 H9   sing N N 450 
V90 C26 H10  sing N N 451 
V90 C26 H11  sing N N 452 
V90 C25 H12  sing N N 453 
V90 C25 H13  sing N N 454 
V90 C24 H14  sing N N 455 
V90 C24 H15  sing N N 456 
V90 C23 H16  sing N N 457 
V90 C23 H17  sing N N 458 
V90 C22 H18  sing N N 459 
V90 C22 H19  sing N N 460 
V90 C21 H20  sing N N 461 
V90 C21 H21  sing N N 462 
V90 C20 H22  sing N N 463 
V90 C20 H23  sing N N 464 
VAL N   CA   sing N N 465 
VAL N   H    sing N N 466 
VAL N   H2   sing N N 467 
VAL CA  C    sing N N 468 
VAL CA  CB   sing N N 469 
VAL CA  HA   sing N N 470 
VAL C   O    doub N N 471 
VAL C   OXT  sing N N 472 
VAL CB  CG1  sing N N 473 
VAL CB  CG2  sing N N 474 
VAL CB  HB   sing N N 475 
VAL CG1 HG11 sing N N 476 
VAL CG1 HG12 sing N N 477 
VAL CG1 HG13 sing N N 478 
VAL CG2 HG21 sing N N 479 
VAL CG2 HG22 sing N N 480 
VAL CG2 HG23 sing N N 481 
VAL OXT HXT  sing N N 482 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                           ZN  
3 'DIMETHYL SULFOXIDE'                                                                 DMS 
4 BICINE                                                                               BCN 
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                               MES 
6 '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' V90 
7 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' 
# 
