data_4Q07
# 
_entry.id   4Q07 
# 
_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   4Q07         pdb_00004q07 10.2210/pdb4q07/pdb 
RCSB  RCSB085439   ?            ?                   
WWPDB D_1000085439 ?            ?                   
# 
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 4Q08 . unspecified 
PDB 4Q09 . unspecified 
PDB 4Q0L . unspecified 
# 
_pdbx_database_status.entry_id                        4Q07 
_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           4Q07 
_cell.length_a           41.931 
_cell.length_b           41.214 
_cell.length_c           72.066 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.210 
_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                         4Q07 
_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'                                                               29242.992 1   4.2.1.1 
'A65S, N67Q, I91L, F130V, V134L, L203A' ? ? 
2 non-polymer syn 'ZINC ION'                                                                           65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                 78.133    1   ?       ? ? ? 
4 non-polymer syn '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 444.489   1   ?       ? ? ? 
5 non-polymer syn BICINE                                                                               163.172   1   ?       ? ? ? 
6 water       nat water                                                                                18.015    306 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFQVEFDDSQDKAVLK
GGPLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDVGKALQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLAECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFQVEFDDSQDKAVLK
GGPLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDVGKALQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLAECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
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  GLN 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  LEU 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 VAL n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 LEU 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 ALA 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              4Q07 
_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 4Q07 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 4Q07 GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 4Q07 LEU A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 4Q07 VAL A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 4 
1 4Q07 LEU A 134 ? UNP P00918 VAL 134 'engineered mutation' 134 5 
1 4Q07 ALA 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 
MET 'L-peptide linking' y METHIONINE                                                                           ? 'C5 H11 N O2 S' 
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                        ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                              ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                               ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                            ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                           ? 'C11 H12 N2 O2' 
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                             ? 'C9 H11 N O3' 
181.189 
V14 non-polymer         . '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
'C16 H23 F3 N2 O5 S2' 444.489 
VAL 'L-peptide linking' y VALINE                                                                               ? 'C5 H11 N O2' 
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                           ? 'Zn 2' 65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4Q07 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   38.4 
_exptl_crystal.density_Matthews      2.01 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate, VAPOR DIFFUSION, SITTING DROP, temperature 291K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'PSI PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2013-05-21 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    
;High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM) 
: Si 311, Si 511
;
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
# 
_reflns.entry_id                     4Q07 
_reflns.d_resolution_high            1.149 
_reflns.d_resolution_low             69.862 
_reflns.number_all                   ? 
_reflns.number_obs                   77927 
_reflns.pdbx_netI_over_sigmaI        8.600 
_reflns.pdbx_Rsym_value              0.065 
_reflns.pdbx_redundancy              3.500 
_reflns.percent_possible_obs         92.000 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        8.729 
_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 
1.15 1.21  ? 30096 ? 0.204 3.3  0.204 ? 3.30 ? 9036  73.60 1  1 
1.21 1.29  ? 37218 ? 0.170 3.7  0.170 ? 3.50 ? 10683 91.50 2  1 
1.29 1.37  ? 35656 ? 0.134 4.5  0.134 ? 3.50 ? 10226 93.50 3  1 
1.37 1.48  ? 33851 ? 0.101 6.1  0.101 ? 3.50 ? 9680  95.00 4  1 
1.48 1.63  ? 31137 ? 0.079 8.0  0.079 ? 3.50 ? 8924  95.00 5  1 
1.63 1.82  ? 28993 ? 0.065 10.1 0.065 ? 3.50 ? 8205  96.50 6  1 
1.82 2.10  ? 25427 ? 0.060 10.9 0.060 ? 3.50 ? 7296  96.60 7  1 
2.10 2.57  ? 21895 ? 0.056 11.8 0.056 ? 3.50 ? 6263  98.30 8  1 
2.57 3.63  ? 16963 ? 0.058 10.3 0.058 ? 3.50 ? 4859  98.10 9  1 
3.63 69.86 ? 9360  ? 0.061 8.7  0.061 ? 3.40 ? 2755  98.10 10 1 
# 
_refine.entry_id                                 4Q07 
_refine.ls_d_res_high                            1.150 
_refine.ls_d_res_low                             69.860 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    91.560 
_refine.ls_number_reflns_obs                     77857 
_refine.ls_number_reflns_all                     77857 
_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                      0.135 
_refine.ls_R_factor_R_free                       0.158 
_refine.ls_wR_factor_R_free                      0.173 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  7772 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               14.353 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.290 
_refine.aniso_B[2][2]                            -0.040 
_refine.aniso_B[3][3]                            0.240 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.170 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.978 
_refine.correlation_coeff_Fo_to_Fc_free          0.972 
_refine.overall_SU_R_Cruickshank_DPI             0.043 
_refine.overall_SU_R_free                        0.041 
_refine.pdbx_overall_ESU_R                       0.042 
_refine.pdbx_overall_ESU_R_Free                  0.041 
_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                   0.930 
_refine.B_iso_max                                73.25 
_refine.B_iso_min                                5.23 
_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        2045 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             306 
_refine_hist.number_atoms_total               2395 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        69.860 
# 
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       2901 0.023  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3982 2.450  1.979  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 367  7.189  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 130  37.031 25.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 475  14.477 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 8    23.529 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         407  0.138  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   2291 0.017  0.021  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr     2901 6.764  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free      308  19.620 5.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded    2795 11.140 5.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.149 
_refine_ls_shell.d_res_low                        1.179 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               59.130 
_refine_ls_shell.number_reflns_R_work             3321 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.186 
_refine_ls_shell.R_factor_R_free                  0.230 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             375 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                3696 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4Q07 
_struct.title                     'Crystal structure of chimeric carbonic anhydrase IX with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4Q07 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   'biological unit is the same as asym.' 
# 
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 ? LEU A 134 ? ASP A 129 LEU A 134 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? ASP A 161 ? LYS A 153 ASP A 161 1 ? 9 
HELX_P HELX_P6 6 VAL A 162 ? LYS A 167 ? VAL A 162 LYS A 167 5 ? 6 
HELX_P HELX_P7 7 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P8 8 SER A 219 ? ARG A 226 ? SER A 219 ARG A 226 1 ? 8 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D V14 . N10 A ? A ZN  301 A V14 303 1_555 ? ? ? ? ? ? ? 1.928 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D V14 . N10 B ? A ZN  301 A V14 303 1_555 ? ? ? ? ? ? ? 1.929 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.23 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 9.26  
# 
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 ? GLY A 150 ? LEU A 140 GLY A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 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 ? GLY A 150 ? LEU A 140 GLY A 150 
C 6  ILE A 215 ? SER A 218 ? ILE A 215 SER A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 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 LEU A 91  ? N LEU A 91  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLN A 67  ? O GLN A 67  N LEU A 60  ? N LEU A 60  
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 LEU A 91  ? N LEU A 91  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 GLY A 150 ? N GLY A 150 O VAL A 217 ? O VAL A 217 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A DMS 302 ? 5  'BINDING SITE FOR RESIDUE DMS A 302' 
AC3 Software A V14 303 ? 17 'BINDING SITE FOR RESIDUE V14 A 303' 
AC4 Software A BCN 304 ? 8  'BINDING SITE FOR RESIDUE BCN A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  V14 D .   ? V14 A 303 . ? 1_555 ? 
5  AC2 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 5  ASP A 242 ? ASP A 242 . ? 1_555 ? 
7  AC2 5  TRP A 244 ? TRP A 244 . ? 1_555 ? 
8  AC2 5  PRO A 246 ? PRO A 246 . ? 1_555 ? 
9  AC2 5  HOH F .   ? HOH A 691 . ? 1_555 ? 
10 AC3 17 TRP A 5   ? TRP A 5   . ? 1_555 ? 
11 AC3 17 ASN A 62  ? ASN A 62  . ? 1_555 ? 
12 AC3 17 HIS A 64  ? HIS A 64  . ? 1_555 ? 
13 AC3 17 SER A 65  ? SER A 65  . ? 1_555 ? 
14 AC3 17 GLN A 67  ? GLN A 67  . ? 1_555 ? 
15 AC3 17 GLN A 92  ? GLN A 92  . ? 1_555 ? 
16 AC3 17 HIS A 94  ? HIS A 94  . ? 1_555 ? 
17 AC3 17 HIS A 96  ? HIS A 96  . ? 1_555 ? 
18 AC3 17 HIS A 119 ? HIS A 119 . ? 1_555 ? 
19 AC3 17 VAL A 121 ? VAL A 121 . ? 1_555 ? 
20 AC3 17 LEU A 197 ? LEU A 197 . ? 1_555 ? 
21 AC3 17 THR A 198 ? THR A 198 . ? 1_555 ? 
22 AC3 17 THR A 199 ? THR A 199 . ? 1_555 ? 
23 AC3 17 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
24 AC3 17 HOH F .   ? HOH A 591 . ? 1_555 ? 
25 AC3 17 HOH F .   ? HOH A 601 . ? 1_555 ? 
26 AC3 17 HOH F .   ? HOH A 638 . ? 1_555 ? 
27 AC4 8  TYR A 114 ? TYR A 114 . ? 1_555 ? 
28 AC4 8  LYS A 148 ? LYS A 148 . ? 1_555 ? 
29 AC4 8  LYS A 212 ? LYS A 212 . ? 1_555 ? 
30 AC4 8  GLU A 213 ? GLU A 213 . ? 1_555 ? 
31 AC4 8  PRO A 214 ? PRO A 214 . ? 1_555 ? 
32 AC4 8  HOH F .   ? HOH A 496 . ? 1_555 ? 
33 AC4 8  HOH F .   ? HOH A 590 . ? 1_555 ? 
34 AC4 8  HOH F .   ? HOH A 687 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4Q07 
_atom_sites.fract_transf_matrix[1][1]   0.023849 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006038 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024264 
_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]   0.014314 
_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   ? 11.317  -0.553  7.998   0.50 29.24 ? 4   HIS A N   1 
ATOM   2    N  N   B HIS A 1 4   ? 9.144   1.842   8.654   0.50 24.00 ? 4   HIS A N   1 
ATOM   3    C  CA  A HIS A 1 4   ? 10.188  0.051   8.751   0.50 28.75 ? 4   HIS A CA  1 
ATOM   4    C  CA  B HIS A 1 4   ? 9.651   0.372   8.374   0.50 27.21 ? 4   HIS A CA  1 
ATOM   5    C  C   A HIS A 1 4   ? 9.401   -1.020  9.443   0.50 25.27 ? 4   HIS A C   1 
ATOM   6    C  C   B HIS A 1 4   ? 9.247   -0.855  9.253   0.50 26.77 ? 4   HIS A C   1 
ATOM   7    O  O   A HIS A 1 4   ? 9.607   -2.231  9.235   0.50 23.19 ? 4   HIS A O   1 
ATOM   8    O  O   B HIS A 1 4   ? 9.646   -2.016  9.029   0.50 26.18 ? 4   HIS A O   1 
ATOM   9    C  CB  A HIS A 1 4   ? 9.313   0.946   7.863   0.50 34.49 ? 4   HIS A CB  1 
ATOM   10   C  CB  B HIS A 1 4   ? 11.179  0.368   8.297   0.50 36.24 ? 4   HIS A CB  1 
ATOM   11   C  CG  A HIS A 1 4   ? 8.868   2.224   8.552   0.50 33.90 ? 4   HIS A CG  1 
ATOM   12   C  CG  B HIS A 1 4   ? 11.830  0.144   9.639   0.50 40.57 ? 4   HIS A CG  1 
ATOM   13   N  ND1 A HIS A 1 4   ? 7.642   2.758   8.369   0.50 30.62 ? 4   HIS A ND1 1 
ATOM   14   N  ND1 B HIS A 1 4   ? 12.677  -0.878  9.886   0.50 43.06 ? 4   HIS A ND1 1 
ATOM   15   C  CD2 A HIS A 1 4   ? 9.515   3.029   9.496   0.50 42.35 ? 4   HIS A CD2 1 
ATOM   16   C  CD2 B HIS A 1 4   ? 11.665  0.816   10.844  0.50 31.28 ? 4   HIS A CD2 1 
ATOM   17   C  CE1 A HIS A 1 4   ? 7.528   3.881   9.119   0.50 40.22 ? 4   HIS A CE1 1 
ATOM   18   C  CE1 B HIS A 1 4   ? 13.039  -0.843  11.176  0.50 45.04 ? 4   HIS A CE1 1 
ATOM   19   N  NE2 A HIS A 1 4   ? 8.673   4.039   9.814   0.50 43.49 ? 4   HIS A NE2 1 
ATOM   20   N  NE2 B HIS A 1 4   ? 12.423  0.201   11.755  0.50 45.32 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.456   -0.610  10.271  1.00 19.94 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.846   -1.608  11.104  1.00 15.23 ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.813   -2.378  10.382  1.00 14.83 ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.234   -1.940  9.368   1.00 16.50 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.211   -0.900  12.290  1.00 15.59 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 6.009   -0.052  11.949  1.00 13.67 ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 5.989   1.289   11.618  1.00 17.35 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.652   -0.499  11.937  1.00 12.55 ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.744   1.708   11.437  1.00 15.90 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.863   0.662   11.610  1.00 14.40 ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 4.026   -1.712  12.238  1.00 11.90 ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.501   0.600   11.526  1.00 14.98 ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.626   -1.747  12.126  1.00 12.65 ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.900   -0.595  11.773  1.00 14.34 ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.555   -3.580  10.884  1.00 14.56 ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.500   -4.432  10.329  1.00 15.85 ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.181   -5.517  11.326  1.00 13.63 ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.229   -5.306  12.544  1.00 14.06 ? 6   GLY A O   1 
ATOM   39   N  N   A TYR A 1 7   ? 4.668   -6.577  10.716  0.50 14.89 ? 7   TYR A N   1 
ATOM   40   N  N   B TYR A 1 7   ? 5.055   -6.764  10.889  0.50 15.09 ? 7   TYR A N   1 
ATOM   41   C  CA  A TYR A 1 7   ? 4.242   -7.798  11.385  0.50 13.72 ? 7   TYR A CA  1 
ATOM   42   C  CA  B TYR A 1 7   ? 4.694   -7.891  11.816  0.50 12.61 ? 7   TYR A CA  1 
ATOM   43   C  C   A TYR A 1 7   ? 5.073   -8.984  11.020  0.50 14.73 ? 7   TYR A C   1 
ATOM   44   C  C   B TYR A 1 7   ? 5.599   -9.183  11.886  0.50 14.12 ? 7   TYR A C   1 
ATOM   45   O  O   A TYR A 1 7   ? 4.642   -10.125 11.282  0.50 20.74 ? 7   TYR A O   1 
ATOM   46   O  O   B TYR A 1 7   ? 5.288   -10.193 12.609  0.50 14.17 ? 7   TYR A O   1 
ATOM   47   C  CB  A TYR A 1 7   ? 2.763   -8.085  11.094  0.50 12.39 ? 7   TYR A CB  1 
ATOM   48   C  CB  B TYR A 1 7   ? 3.209   -8.255  11.576  0.50 14.36 ? 7   TYR A CB  1 
ATOM   49   C  CG  A TYR A 1 7   ? 1.884   -7.015  11.704  0.50 10.51 ? 7   TYR A CG  1 
ATOM   50   C  CG  B TYR A 1 7   ? 2.247   -7.104  11.941  0.50 11.71 ? 7   TYR A CG  1 
ATOM   51   C  CD1 A TYR A 1 7   ? 1.565   -7.073  13.061  0.50 12.05 ? 7   TYR A CD1 1 
ATOM   52   C  CD1 B TYR A 1 7   ? 1.770   -7.007  13.232  0.50 10.62 ? 7   TYR A CD1 1 
ATOM   53   C  CD2 A TYR A 1 7   ? 1.385   -5.991  10.946  0.50 11.19 ? 7   TYR A CD2 1 
ATOM   54   C  CD2 B TYR A 1 7   ? 1.838   -6.141  11.010  0.50 14.41 ? 7   TYR A CD2 1 
ATOM   55   C  CE1 A TYR A 1 7   ? 0.743   -6.091  13.662  0.50 9.75  ? 7   TYR A CE1 1 
ATOM   56   C  CE1 B TYR A 1 7   ? 0.901   -5.960  13.617  0.50 10.46 ? 7   TYR A CE1 1 
ATOM   57   C  CE2 A TYR A 1 7   ? 0.560   -5.000  11.483  0.50 10.19 ? 7   TYR A CE2 1 
ATOM   58   C  CE2 B TYR A 1 7   ? 0.941   -5.079  11.364  0.50 10.88 ? 7   TYR A CE2 1 
ATOM   59   C  CZ  A TYR A 1 7   ? 0.229   -5.079  12.857  0.50 9.97  ? 7   TYR A CZ  1 
ATOM   60   C  CZ  B TYR A 1 7   ? 0.463   -5.034  12.681  0.50 10.31 ? 7   TYR A CZ  1 
ATOM   61   O  OH  A TYR A 1 7   ? -0.582  -4.117  13.353  0.50 10.86 ? 7   TYR A OH  1 
ATOM   62   O  OH  B TYR A 1 7   ? -0.394  -4.044  13.072  0.50 10.25 ? 7   TYR A OH  1 
ATOM   63   N  N   A GLY A 1 8   ? 6.282   -8.724  10.506  0.50 16.11 ? 8   GLY A N   1 
ATOM   64   N  N   B GLY A 1 8   ? 6.682   -9.165  11.128  0.50 14.48 ? 8   GLY A N   1 
ATOM   65   C  CA  A GLY A 1 8   ? 7.230   -9.854  10.254  0.50 20.61 ? 8   GLY A CA  1 
ATOM   66   C  CA  B GLY A 1 8   ? 7.523   -10.365 11.068  0.50 13.81 ? 8   GLY A CA  1 
ATOM   67   C  C   A GLY A 1 8   ? 8.155   -10.147 11.435  0.50 17.35 ? 8   GLY A C   1 
ATOM   68   C  C   B GLY A 1 8   ? 8.692   -10.452 12.033  0.50 14.74 ? 8   GLY A C   1 
ATOM   69   O  O   A GLY A 1 8   ? 8.260   -9.385  12.430  0.50 19.34 ? 8   GLY A O   1 
ATOM   70   O  O   B GLY A 1 8   ? 8.820   -9.696  13.016  0.50 15.96 ? 8   GLY A O   1 
ATOM   71   N  N   A LYS A 1 9   ? 8.925   -11.223 11.292  0.50 20.58 ? 9   LYS A N   1 
ATOM   72   N  N   B LYS A 1 9   ? 9.610   -11.368 11.732  0.50 14.09 ? 9   LYS A N   1 
ATOM   73   C  CA  A LYS A 1 9   ? 9.827   -11.600 12.371  0.50 18.01 ? 9   LYS A CA  1 
ATOM   74   C  CA  B LYS A 1 9   ? 10.646  -11.755 12.679  0.50 17.17 ? 9   LYS A CA  1 
ATOM   75   C  C   A LYS A 1 9   ? 10.880  -10.518 12.362  0.50 15.01 ? 9   LYS A C   1 
ATOM   76   C  C   B LYS A 1 9   ? 11.530  -10.603 13.077  0.50 15.01 ? 9   LYS A C   1 
ATOM   77   O  O   A LYS A 1 9   ? 11.465  -10.238 13.403  0.50 15.78 ? 9   LYS A O   1 
ATOM   78   O  O   B LYS A 1 9   ? 11.900  -10.458 14.254  0.50 14.00 ? 9   LYS A O   1 
ATOM   79   C  CB  A LYS A 1 9   ? 10.504  -12.936 12.082  0.50 21.99 ? 9   LYS A CB  1 
ATOM   80   C  CB  B LYS A 1 9   ? 11.498  -12.851 12.072  0.50 19.22 ? 9   LYS A CB  1 
ATOM   81   C  CG  A LYS A 1 9   ? 11.598  -13.332 13.065  0.50 22.42 ? 9   LYS A CG  1 
ATOM   82   C  CG  B LYS A 1 9   ? 12.619  -13.277 12.976  0.50 23.34 ? 9   LYS A CG  1 
ATOM   83   C  CD  A LYS A 1 9   ? 12.356  -14.593 12.643  0.50 28.88 ? 9   LYS A CD  1 
ATOM   84   C  CD  B LYS A 1 9   ? 13.351  -14.477 12.398  0.50 34.05 ? 9   LYS A CD  1 
ATOM   85   C  CE  A LYS A 1 9   ? 13.089  -15.186 13.844  0.50 35.31 ? 9   LYS A CE  1 
ATOM   86   C  CE  B LYS A 1 9   ? 14.438  -14.928 13.355  0.50 33.94 ? 9   LYS A CE  1 
ATOM   87   N  NZ  A LYS A 1 9   ? 13.740  -16.496 13.559  0.50 42.73 ? 9   LYS A NZ  1 
ATOM   88   N  NZ  B LYS A 1 9   ? 15.478  -15.714 12.635  0.50 42.26 ? 9   LYS A NZ  1 
ATOM   89   N  N   A HIS A 1 10  ? 11.183  -9.955  11.175  0.50 15.77 ? 10  HIS A N   1 
ATOM   90   N  N   B HIS A 1 10  ? 11.857  -9.763  12.103  0.50 12.04 ? 10  HIS A N   1 
ATOM   91   C  CA  A HIS A 1 10  ? 12.198  -8.936  11.157  0.50 14.30 ? 10  HIS A CA  1 
ATOM   92   C  CA  B HIS A 1 10  ? 12.927  -8.787  12.261  0.50 11.08 ? 10  HIS A CA  1 
ATOM   93   C  C   A HIS A 1 10  ? 11.750  -7.547  11.537  0.50 13.13 ? 10  HIS A C   1 
ATOM   94   C  C   B HIS A 1 10  ? 12.371  -7.408  12.487  0.50 12.05 ? 10  HIS A C   1 
ATOM   95   O  O   A HIS A 1 10  ? 12.568  -6.751  11.982  0.50 18.54 ? 10  HIS A O   1 
ATOM   96   O  O   B HIS A 1 10  ? 13.144  -6.482  12.794  0.50 13.18 ? 10  HIS A O   1 
ATOM   97   C  CB  A HIS A 1 10  ? 12.988  -8.998  9.871   0.50 13.64 ? 10  HIS A CB  1 
ATOM   98   C  CB  B HIS A 1 10  ? 13.780  -8.840  11.011  0.50 12.20 ? 10  HIS A CB  1 
ATOM   99   C  CG  A HIS A 1 10  ? 13.596  -10.364 9.633   0.50 12.93 ? 10  HIS A CG  1 
ATOM   100  C  CG  B HIS A 1 10  ? 14.377  -10.176 10.808  0.50 12.01 ? 10  HIS A CG  1 
ATOM   101  N  ND1 A HIS A 1 10  ? 14.641  -10.839 10.385  0.50 14.75 ? 10  HIS A ND1 1 
ATOM   102  N  ND1 B HIS A 1 10  ? 15.392  -10.627 11.535  0.50 12.28 ? 10  HIS A ND1 1 
ATOM   103  C  CD2 A HIS A 1 10  ? 13.217  -11.397 8.784   0.50 14.64 ? 10  HIS A CD2 1 
ATOM   104  C  CD2 B HIS A 1 10  ? 13.998  -11.212 9.938   0.50 11.11 ? 10  HIS A CD2 1 
ATOM   105  C  CE1 A HIS A 1 10  ? 14.919  -12.099 9.994   0.50 17.74 ? 10  HIS A CE1 1 
ATOM   106  C  CE1 B HIS A 1 10  ? 15.704  -11.878 11.114  0.50 11.27 ? 10  HIS A CE1 1 
ATOM   107  N  NE2 A HIS A 1 10  ? 14.060  -12.439 9.010   0.50 18.50 ? 10  HIS A NE2 1 
ATOM   108  N  NE2 B HIS A 1 10  ? 14.826  -12.241 10.168  0.50 12.83 ? 10  HIS A NE2 1 
ATOM   109  N  N   A ASN A 1 11  ? 10.450  -7.245  11.422  0.50 11.84 ? 11  ASN A N   1 
ATOM   110  N  N   B ASN A 1 11  ? 11.048  -7.214  12.353  0.50 12.50 ? 11  ASN A N   1 
ATOM   111  C  CA  A ASN A 1 11  ? 9.970   -5.917  11.742  0.50 14.32 ? 11  ASN A CA  1 
ATOM   112  C  CA  B ASN A 1 11  ? 10.465  -5.842  12.437  0.50 14.15 ? 11  ASN A CA  1 
ATOM   113  C  C   A ASN A 1 11  ? 8.796   -5.890  12.740  0.50 15.12 ? 11  ASN A C   1 
ATOM   114  C  C   B ASN A 1 11  ? 9.069   -5.797  13.057  0.50 16.02 ? 11  ASN A C   1 
ATOM   115  O  O   A ASN A 1 11  ? 8.111   -4.885  12.804  0.50 16.74 ? 11  ASN A O   1 
ATOM   116  O  O   B ASN A 1 11  ? 8.401   -4.762  13.015  0.50 15.31 ? 11  ASN A O   1 
ATOM   117  C  CB  A ASN A 1 11  ? 9.692   -5.138  10.450  0.50 13.05 ? 11  ASN A CB  1 
ATOM   118  C  CB  B ASN A 1 11  ? 10.339  -5.212  11.044  0.50 13.10 ? 11  ASN A CB  1 
ATOM   119  C  CG  A ASN A 1 11  ? 8.626   -5.804  9.551   0.50 14.54 ? 11  ASN A CG  1 
ATOM   120  C  CG  B ASN A 1 11  ? 9.258   -5.808  10.199  0.50 14.87 ? 11  ASN A CG  1 
ATOM   121  O  OD1 A ASN A 1 11  ? 7.974   -6.752  9.934   0.50 18.20 ? 11  ASN A OD1 1 
ATOM   122  O  OD1 B ASN A 1 11  ? 8.702   -6.857  10.495  0.50 17.85 ? 11  ASN A OD1 1 
ATOM   123  N  ND2 A ASN A 1 11  ? 8.446   -5.277  8.357   0.50 16.09 ? 11  ASN A ND2 1 
ATOM   124  N  ND2 B ASN A 1 11  ? 8.896   -5.086  9.144   0.50 20.58 ? 11  ASN A ND2 1 
ATOM   125  N  N   . GLY A 1 12  ? 8.599   -6.939  13.563  1.00 15.19 ? 12  GLY A N   1 
ATOM   126  C  CA  . GLY A 1 12  ? 7.308   -7.049  14.234  1.00 13.83 ? 12  GLY A CA  1 
ATOM   127  C  C   . GLY A 1 12  ? 7.324   -6.500  15.620  1.00 12.00 ? 12  GLY A C   1 
ATOM   128  O  O   . GLY A 1 12  ? 8.236   -5.828  16.075  1.00 13.78 ? 12  GLY A O   1 
ATOM   129  N  N   . PRO A 1 13  ? 6.242   -6.813  16.352  1.00 11.45 ? 13  PRO A N   1 
ATOM   130  C  CA  . PRO A 1 13  ? 6.014   -6.250  17.669  1.00 11.50 ? 13  PRO A CA  1 
ATOM   131  C  C   . PRO A 1 13  ? 7.174   -6.286  18.629  1.00 11.77 ? 13  PRO A C   1 
ATOM   132  O  O   . PRO A 1 13  ? 7.246   -5.358  19.422  1.00 12.98 ? 13  PRO A O   1 
ATOM   133  C  CB  . PRO A 1 13  ? 4.822   -7.085  18.188  1.00 11.99 ? 13  PRO A CB  1 
ATOM   134  C  CG  . PRO A 1 13  ? 3.977   -7.289  16.923  1.00 11.90 ? 13  PRO A CG  1 
ATOM   135  C  CD  . PRO A 1 13  ? 5.047   -7.536  15.830  1.00 13.09 ? 13  PRO A CD  1 
ATOM   136  N  N   . GLU A 1 14  ? 8.004   -7.319  18.650  1.00 13.35 ? 14  GLU A N   1 
ATOM   137  C  CA  . GLU A 1 14  ? 9.132   -7.335  19.554  1.00 14.82 ? 14  GLU A CA  1 
ATOM   138  C  C   . GLU A 1 14  ? 10.206  -6.346  19.208  1.00 13.86 ? 14  GLU A C   1 
ATOM   139  O  O   . GLU A 1 14  ? 11.094  -6.143  20.016  1.00 16.42 ? 14  GLU A O   1 
ATOM   140  C  CB  . GLU A 1 14  ? 9.747   -8.720  19.570  1.00 17.70 ? 14  GLU A CB  1 
ATOM   141  C  CG  . GLU A 1 14  ? 8.752   -9.801  20.008  1.00 25.16 ? 14  GLU A CG  1 
ATOM   142  C  CD  . GLU A 1 14  ? 7.878   -9.457  21.251  1.00 32.65 ? 14  GLU A CD  1 
ATOM   143  O  OE1 . GLU A 1 14  ? 6.566   -9.536  21.229  1.00 34.40 ? 14  GLU A OE1 1 
ATOM   144  O  OE2 . GLU A 1 14  ? 8.495   -9.191  22.300  1.00 35.63 ? 14  GLU A OE2 1 
ATOM   145  N  N   . HIS A 1 15  ? 10.140  -5.772  17.984  1.00 12.20 ? 15  HIS A N   1 
ATOM   146  C  CA  . HIS A 1 15  ? 11.138  -4.779  17.613  1.00 13.48 ? 15  HIS A CA  1 
ATOM   147  C  C   . HIS A 1 15  ? 10.668  -3.354  17.780  1.00 13.63 ? 15  HIS A C   1 
ATOM   148  O  O   . HIS A 1 15  ? 11.493  -2.405  17.688  1.00 14.01 ? 15  HIS A O   1 
ATOM   149  C  CB  . HIS A 1 15  ? 11.473  -4.943  16.166  1.00 14.48 ? 15  HIS A CB  1 
ATOM   150  C  CG  . HIS A 1 15  ? 12.226  -6.193  15.872  1.00 16.26 ? 15  HIS A CG  1 
ATOM   151  N  ND1 . HIS A 1 15  ? 13.607  -6.243  15.901  1.00 18.33 ? 15  HIS A ND1 1 
ATOM   152  C  CD2 . HIS A 1 15  ? 11.776  -7.448  15.580  1.00 18.28 ? 15  HIS A CD2 1 
ATOM   153  C  CE1 . HIS A 1 15  ? 14.018  -7.481  15.628  1.00 20.11 ? 15  HIS A CE1 1 
ATOM   154  N  NE2 . HIS A 1 15  ? 12.910  -8.264  15.445  1.00 17.79 ? 15  HIS A NE2 1 
ATOM   155  N  N   . TRP A 1 16  ? 9.345   -3.120  17.941  1.00 11.53 ? 16  TRP A N   1 
ATOM   156  C  CA  . TRP A 1 16  ? 8.825   -1.783  17.818  1.00 10.88 ? 16  TRP A CA  1 
ATOM   157  C  C   . TRP A 1 16  ? 9.388   -0.811  18.825  1.00 10.44 ? 16  TRP A C   1 
ATOM   158  O  O   . TRP A 1 16  ? 9.481   0.393   18.548  1.00 11.41 ? 16  TRP A O   1 
ATOM   159  C  CB  . TRP A 1 16  ? 7.291   -1.805  17.956  1.00 10.99 ? 16  TRP A CB  1 
ATOM   160  C  CG  . TRP A 1 16  ? 6.636   -2.507  16.791  1.00 9.24  ? 16  TRP A CG  1 
ATOM   161  C  CD1 . TRP A 1 16  ? 7.145   -2.973  15.608  1.00 10.43 ? 16  TRP A CD1 1 
ATOM   162  C  CD2 . TRP A 1 16  ? 5.227   -2.857  16.752  1.00 9.36  ? 16  TRP A CD2 1 
ATOM   163  N  NE1 . TRP A 1 16  ? 6.180   -3.564  14.873  1.00 10.95 ? 16  TRP A NE1 1 
ATOM   164  C  CE2 . TRP A 1 16  ? 4.987   -3.492  15.500  1.00 9.71  ? 16  TRP A CE2 1 
ATOM   165  C  CE3 . TRP A 1 16  ? 4.168   -2.678  17.638  1.00 9.46  ? 16  TRP A CE3 1 
ATOM   166  C  CZ2 . TRP A 1 16  ? 3.700   -3.932  15.129  1.00 9.91  ? 16  TRP A CZ2 1 
ATOM   167  C  CZ3 . TRP A 1 16  ? 2.933   -3.127  17.267  1.00 8.85  ? 16  TRP A CZ3 1 
ATOM   168  C  CH2 . TRP A 1 16  ? 2.692   -3.742  16.038  1.00 9.30  ? 16  TRP A CH2 1 
ATOM   169  N  N   . HIS A 1 17  ? 9.721   -1.325  20.021  1.00 11.10 ? 17  HIS A N   1 
ATOM   170  C  CA  . HIS A 1 17  ? 10.219  -0.447  21.069  1.00 12.70 ? 17  HIS A CA  1 
ATOM   171  C  C   . HIS A 1 17  ? 11.464  0.333   20.652  1.00 13.61 ? 17  HIS A C   1 
ATOM   172  O  O   . HIS A 1 17  ? 11.762  1.377   21.266  1.00 14.34 ? 17  HIS A O   1 
ATOM   173  C  CB  . HIS A 1 17  ? 10.510  -1.169  22.371  1.00 14.68 ? 17  HIS A CB  1 
ATOM   174  C  CG  . HIS A 1 17  ? 11.725  -2.053  22.274  1.00 15.06 ? 17  HIS A CG  1 
ATOM   175  N  ND1 . HIS A 1 17  ? 12.941  -1.667  22.787  1.00 15.82 ? 17  HIS A ND1 1 
ATOM   176  C  CD2 . HIS A 1 17  ? 11.926  -3.239  21.647  1.00 14.85 ? 17  HIS A CD2 1 
ATOM   177  C  CE1 . HIS A 1 17  ? 13.859  -2.584  22.528  1.00 17.07 ? 17  HIS A CE1 1 
ATOM   178  N  NE2 . HIS A 1 17  ? 13.282  -3.570  21.845  1.00 15.85 ? 17  HIS A NE2 1 
ATOM   179  N  N   . LYS A 1 18  ? 12.254  -0.199  19.688  1.00 13.65 ? 18  LYS A N   1 
ATOM   180  C  CA  . LYS A 1 18  ? 13.480  0.524   19.270  1.00 15.65 ? 18  LYS A CA  1 
ATOM   181  C  C   . LYS A 1 18  ? 13.131  1.873   18.596  1.00 15.32 ? 18  LYS A C   1 
ATOM   182  O  O   . LYS A 1 18  ? 13.836  2.855   18.807  1.00 20.76 ? 18  LYS A O   1 
ATOM   183  C  CB  . LYS A 1 18  ? 14.336  -0.360  18.374  1.00 14.20 ? 18  LYS A CB  1 
ATOM   184  C  CG  . LYS A 1 18  ? 14.963  -1.499  19.119  1.00 17.24 ? 18  LYS A CG  1 
ATOM   185  C  CD  . LYS A 1 18  ? 15.683  -2.467  18.221  1.00 15.40 ? 18  LYS A CD  1 
ATOM   186  C  CE  . LYS A 1 18  ? 14.713  -3.450  17.617  1.00 15.21 ? 18  LYS A CE  1 
ATOM   187  N  NZ  . LYS A 1 18  ? 15.334  -4.258  16.532  1.00 16.08 ? 18  LYS A NZ  1 
ATOM   188  N  N   . ASP A 1 19  ? 12.069  1.922   17.811  1.00 15.06 ? 19  ASP A N   1 
ATOM   189  C  CA  . ASP A 1 19  ? 11.681  3.205   17.200  1.00 16.04 ? 19  ASP A CA  1 
ATOM   190  C  C   . ASP A 1 19  ? 10.637  3.934   18.046  1.00 15.46 ? 19  ASP A C   1 
ATOM   191  O  O   . ASP A 1 19  ? 10.519  5.169   17.947  1.00 15.93 ? 19  ASP A O   1 
ATOM   192  C  CB  . ASP A 1 19  ? 11.162  3.070   15.768  1.00 19.91 ? 19  ASP A CB  1 
ATOM   193  C  CG  . ASP A 1 19  ? 12.233  2.791   14.796  1.00 23.33 ? 19  ASP A CG  1 
ATOM   194  O  OD1 . ASP A 1 19  ? 13.276  3.478   14.800  1.00 25.25 ? 19  ASP A OD1 1 
ATOM   195  O  OD2 . ASP A 1 19  ? 12.118  1.705   14.164  1.00 36.93 ? 19  ASP A OD2 1 
ATOM   196  N  N   A PHE A 1 20  ? 9.880   3.175   18.829  0.50 12.58 ? 20  PHE A N   1 
ATOM   197  N  N   B PHE A 1 20  ? 9.926   3.227   18.921  0.50 12.66 ? 20  PHE A N   1 
ATOM   198  C  CA  A PHE A 1 20  ? 8.727   3.673   19.556  0.50 10.69 ? 20  PHE A CA  1 
ATOM   199  C  CA  B PHE A 1 20  ? 8.912   3.837   19.789  0.50 14.30 ? 20  PHE A CA  1 
ATOM   200  C  C   A PHE A 1 20  ? 8.822   3.217   21.011  0.50 11.25 ? 20  PHE A C   1 
ATOM   201  C  C   B PHE A 1 20  ? 9.049   3.281   21.192  0.50 13.48 ? 20  PHE A C   1 
ATOM   202  O  O   A PHE A 1 20  ? 8.185   2.229   21.408  0.50 12.21 ? 20  PHE A O   1 
ATOM   203  O  O   B PHE A 1 20  ? 8.388   2.272   21.545  0.50 12.41 ? 20  PHE A O   1 
ATOM   204  C  CB  A PHE A 1 20  ? 7.402   3.232   18.869  0.50 10.64 ? 20  PHE A CB  1 
ATOM   205  C  CB  B PHE A 1 20  ? 7.486   3.559   19.239  0.50 12.30 ? 20  PHE A CB  1 
ATOM   206  C  CG  A PHE A 1 20  ? 7.376   3.574   17.418  0.50 11.32 ? 20  PHE A CG  1 
ATOM   207  C  CG  B PHE A 1 20  ? 7.314   4.087   17.861  0.50 12.12 ? 20  PHE A CG  1 
ATOM   208  C  CD1 A PHE A 1 20  ? 7.057   4.863   17.009  0.50 11.67 ? 20  PHE A CD1 1 
ATOM   209  C  CD1 B PHE A 1 20  ? 6.967   5.397   17.660  0.50 13.28 ? 20  PHE A CD1 1 
ATOM   210  C  CD2 A PHE A 1 20  ? 7.732   2.618   16.466  0.50 12.11 ? 20  PHE A CD2 1 
ATOM   211  C  CD2 B PHE A 1 20  ? 7.579   3.281   16.767  0.50 14.74 ? 20  PHE A CD2 1 
ATOM   212  C  CE1 A PHE A 1 20  ? 7.111   5.189   15.662  0.50 13.19 ? 20  PHE A CE1 1 
ATOM   213  C  CE1 B PHE A 1 20  ? 6.908   5.904   16.380  0.50 15.29 ? 20  PHE A CE1 1 
ATOM   214  C  CE2 A PHE A 1 20  ? 7.772   2.952   15.120  0.50 13.58 ? 20  PHE A CE2 1 
ATOM   215  C  CE2 B PHE A 1 20  ? 7.507   3.775   15.477  0.50 16.71 ? 20  PHE A CE2 1 
ATOM   216  C  CZ  A PHE A 1 20  ? 7.461   4.231   14.700  0.50 12.12 ? 20  PHE A CZ  1 
ATOM   217  C  CZ  B PHE A 1 20  ? 7.167   5.091   15.282  0.50 16.82 ? 20  PHE A CZ  1 
ATOM   218  N  N   A PRO A 1 21  ? 9.649   3.879   21.804  0.50 13.28 ? 21  PRO A N   1 
ATOM   219  N  N   B PRO A 1 21  ? 9.914   3.888   22.006  0.50 14.29 ? 21  PRO A N   1 
ATOM   220  C  CA  A PRO A 1 21  ? 9.975   3.390   23.153  0.50 13.80 ? 21  PRO A CA  1 
ATOM   221  C  CA  B PRO A 1 21  ? 10.157  3.298   23.296  0.50 14.44 ? 21  PRO A CA  1 
ATOM   222  C  C   A PRO A 1 21  ? 8.816   3.245   24.156  0.50 13.68 ? 21  PRO A C   1 
ATOM   223  C  C   B PRO A 1 21  ? 8.880   3.266   24.060  0.50 13.70 ? 21  PRO A C   1 
ATOM   224  O  O   A PRO A 1 21  ? 8.906   2.411   25.060  0.50 13.45 ? 21  PRO A O   1 
ATOM   225  O  O   B PRO A 1 21  ? 8.818   2.539   25.036  0.50 13.54 ? 21  PRO A O   1 
ATOM   226  C  CB  A PRO A 1 21  ? 10.992  4.428   23.659  0.50 17.46 ? 21  PRO A CB  1 
ATOM   227  C  CB  B PRO A 1 21  ? 11.130  4.295   23.981  0.50 17.30 ? 21  PRO A CB  1 
ATOM   228  C  CG  A PRO A 1 21  ? 11.614  4.943   22.401  0.50 18.86 ? 21  PRO A CG  1 
ATOM   229  C  CG  B PRO A 1 21  ? 10.930  5.532   23.201  0.50 17.15 ? 21  PRO A CG  1 
ATOM   230  C  CD  A PRO A 1 21  ? 10.581  4.924   21.343  0.50 15.96 ? 21  PRO A CD  1 
ATOM   231  C  CD  B PRO A 1 21  ? 10.762  5.065   21.807  0.50 14.40 ? 21  PRO A CD  1 
ATOM   232  N  N   A ILE A 1 22  ? 7.724   4.009   24.005  0.50 10.66 ? 22  ILE A N   1 
ATOM   233  N  N   B ILE A 1 22  ? 7.841   4.007   23.646  0.50 11.55 ? 22  ILE A N   1 
ATOM   234  C  CA  A ILE A 1 22  ? 6.525   3.808   24.810  0.50 10.84 ? 22  ILE A CA  1 
ATOM   235  C  CA  B ILE A 1 22  ? 6.573   3.928   24.359  0.50 10.67 ? 22  ILE A CA  1 
ATOM   236  C  C   A ILE A 1 22  ? 5.969   2.392   24.585  0.50 10.53 ? 22  ILE A C   1 
ATOM   237  C  C   B ILE A 1 22  ? 5.901   2.542   24.312  0.50 9.74  ? 22  ILE A C   1 
ATOM   238  O  O   A ILE A 1 22  ? 5.065   2.022   25.382  0.50 9.32  ? 22  ILE A O   1 
ATOM   239  O  O   B ILE A 1 22  ? 4.933   2.288   25.019  0.50 9.48  ? 22  ILE A O   1 
ATOM   240  C  CB  A ILE A 1 22  ? 5.460   4.874   24.428  0.50 9.27  ? 22  ILE A CB  1 
ATOM   241  C  CB  B ILE A 1 22  ? 5.580   5.040   23.929  0.50 9.41  ? 22  ILE A CB  1 
ATOM   242  C  CG1 A ILE A 1 22  ? 4.462   5.083   25.582  0.50 12.41 ? 22  ILE A CG1 1 
ATOM   243  C  CG1 B ILE A 1 22  ? 4.606   5.298   25.075  0.50 8.13  ? 22  ILE A CG1 1 
ATOM   244  C  CG2 A ILE A 1 22  ? 4.831   4.506   23.092  0.50 10.17 ? 22  ILE A CG2 1 
ATOM   245  C  CG2 B ILE A 1 22  ? 4.892   4.680   22.621  0.50 11.29 ? 22  ILE A CG2 1 
ATOM   246  C  CD1 A ILE A 1 22  ? 4.933   5.963   26.695  0.50 17.02 ? 22  ILE A CD1 1 
ATOM   247  C  CD1 B ILE A 1 22  ? 3.594   6.387   24.921  0.50 11.52 ? 22  ILE A CD1 1 
ATOM   248  N  N   . ALA A 1 23  ? 6.441   1.629   23.542  1.00 10.46 ? 23  ALA A N   1 
ATOM   249  C  CA  . ALA A 1 23  ? 6.005   0.252   23.434  1.00 10.09 ? 23  ALA A CA  1 
ATOM   250  C  C   . ALA A 1 23  ? 6.123   -0.468  24.766  1.00 10.40 ? 23  ALA A C   1 
ATOM   251  O  O   . ALA A 1 23  ? 5.392   -1.469  24.933  1.00 11.20 ? 23  ALA A O   1 
ATOM   252  C  CB  . ALA A 1 23  ? 6.818   -0.508  22.386  1.00 10.54 ? 23  ALA A CB  1 
ATOM   253  N  N   . LYS A 1 24  ? 7.008   -0.022  25.646  1.00 11.00 ? 24  LYS A N   1 
ATOM   254  C  CA  . LYS A 1 24  ? 7.194   -0.627  26.930  1.00 11.91 ? 24  LYS A CA  1 
ATOM   255  C  C   . LYS A 1 24  ? 6.582   0.233   28.071  1.00 11.83 ? 24  LYS A C   1 
ATOM   256  O  O   . LYS A 1 24  ? 6.952   0.123   29.232  1.00 15.49 ? 24  LYS A O   1 
ATOM   257  C  CB  . LYS A 1 24  ? 8.642   -0.898  27.254  1.00 14.95 ? 24  LYS A CB  1 
ATOM   258  C  CG  . LYS A 1 24  ? 9.266   -1.895  26.309  1.00 16.08 ? 24  LYS A CG  1 
ATOM   259  C  CD  . LYS A 1 24  ? 10.743  -2.119  26.680  1.00 20.95 ? 24  LYS A CD  1 
ATOM   260  C  CE  . LYS A 1 24  ? 11.473  -3.029  25.732  1.00 24.06 ? 24  LYS A CE  1 
ATOM   261  N  NZ  . LYS A 1 24  ? 10.946  -4.390  25.834  1.00 26.32 ? 24  LYS A NZ  1 
ATOM   262  N  N   . GLY A 1 25  ? 5.549   1.008   27.708  1.00 11.93 ? 25  GLY A N   1 
ATOM   263  C  CA  . GLY A 1 25  ? 4.969   1.972   28.603  1.00 13.04 ? 25  GLY A CA  1 
ATOM   264  C  C   . GLY A 1 25  ? 3.986   1.368   29.594  1.00 11.90 ? 25  GLY A C   1 
ATOM   265  O  O   . GLY A 1 25  ? 3.788   0.159   29.672  1.00 12.33 ? 25  GLY A O   1 
ATOM   266  N  N   . GLU A 1 26  ? 3.346   2.257   30.314  1.00 12.43 ? 26  GLU A N   1 
ATOM   267  C  CA  . GLU A 1 26  ? 2.475   1.875   31.414  1.00 13.31 ? 26  GLU A CA  1 
ATOM   268  C  C   . GLU A 1 26  ? 1.034   1.599   31.021  1.00 10.73 ? 26  GLU A C   1 
ATOM   269  O  O   . GLU A 1 26  ? 0.264   1.127   31.853  1.00 11.90 ? 26  GLU A O   1 
ATOM   270  C  CB  . GLU A 1 26  ? 2.522   2.974   32.489  1.00 17.04 ? 26  GLU A CB  1 
ATOM   271  C  CG  . GLU A 1 26  ? 3.919   3.141   33.065  1.00 18.23 ? 26  GLU A CG  1 
ATOM   272  C  CD  . GLU A 1 26  ? 4.518   1.837   33.707  1.00 22.38 ? 26  GLU A CD  1 
ATOM   273  O  OE1 . GLU A 1 26  ? 3.878   1.121   34.556  1.00 29.60 ? 26  GLU A OE1 1 
ATOM   274  O  OE2 . GLU A 1 26  ? 5.658   1.524   33.343  1.00 29.47 ? 26  GLU A OE2 1 
ATOM   275  N  N   . ARG A 1 27  ? 0.671   1.930   29.798  1.00 9.12  ? 27  ARG A N   1 
ATOM   276  C  CA  . ARG A 1 27  ? -0.744  1.682   29.436  1.00 8.50  ? 27  ARG A CA  1 
ATOM   277  C  C   . ARG A 1 27  ? -0.842  1.232   27.970  1.00 7.29  ? 27  ARG A C   1 
ATOM   278  O  O   . ARG A 1 27  ? -1.532  1.823   27.158  1.00 7.48  ? 27  ARG A O   1 
ATOM   279  C  CB  . ARG A 1 27  ? -1.670  2.895   29.746  1.00 9.91  ? 27  ARG A CB  1 
ATOM   280  C  CG  . ARG A 1 27  ? -1.234  4.198   29.177  1.00 10.81 ? 27  ARG A CG  1 
ATOM   281  C  CD  . ARG A 1 27  ? -2.231  5.388   29.363  1.00 11.35 ? 27  ARG A CD  1 
ATOM   282  N  NE  . ARG A 1 27  ? -3.349  5.279   28.437  1.00 9.62  ? 27  ARG A NE  1 
ATOM   283  C  CZ  . ARG A 1 27  ? -4.328  6.153   28.424  1.00 8.98  ? 27  ARG A CZ  1 
ATOM   284  N  NH1 . ARG A 1 27  ? -4.330  7.176   29.308  1.00 11.15 ? 27  ARG A NH1 1 
ATOM   285  N  NH2 . ARG A 1 27  ? -5.269  6.061   27.575  1.00 10.14 ? 27  ARG A NH2 1 
ATOM   286  N  N   . GLN A 1 28  ? -0.102  0.172   27.675  1.00 7.53  ? 28  GLN A N   1 
ATOM   287  C  CA  . GLN A 1 28  ? -0.069  -0.379  26.307  1.00 6.93  ? 28  GLN A CA  1 
ATOM   288  C  C   . GLN A 1 28  ? -1.256  -1.333  26.068  1.00 6.98  ? 28  GLN A C   1 
ATOM   289  O  O   . GLN A 1 28  ? -1.725  -2.018  26.965  1.00 7.54  ? 28  GLN A O   1 
ATOM   290  C  CB  . GLN A 1 28  ? 1.273   -1.053  26.072  1.00 8.10  ? 28  GLN A CB  1 
ATOM   291  C  CG  . GLN A 1 28  ? 2.395   0.018   25.930  1.00 8.31  ? 28  GLN A CG  1 
ATOM   292  C  CD  . GLN A 1 28  ? 2.279   0.807   24.696  1.00 7.29  ? 28  GLN A CD  1 
ATOM   293  O  OE1 . GLN A 1 28  ? 2.448   0.255   23.598  1.00 8.07  ? 28  GLN A OE1 1 
ATOM   294  N  NE2 . GLN A 1 28  ? 1.970   2.099   24.812  1.00 7.85  ? 28  GLN A NE2 1 
ATOM   295  N  N   . SER A 1 29  ? -1.599  -1.423  24.780  1.00 6.70  ? 29  SER A N   1 
ATOM   296  C  CA  . SER A 1 29  ? -2.669  -2.293  24.304  1.00 5.95  ? 29  SER A CA  1 
ATOM   297  C  C   . SER A 1 29  ? -2.143  -3.198  23.200  1.00 5.82  ? 29  SER A C   1 
ATOM   298  O  O   . SER A 1 29  ? -1.159  -2.838  22.541  1.00 6.76  ? 29  SER A O   1 
ATOM   299  C  CB  . SER A 1 29  ? -3.796  -1.441  23.738  1.00 5.78  ? 29  SER A CB  1 
ATOM   300  O  OG  . SER A 1 29  ? -4.409  -0.697  24.813  1.00 6.26  ? 29  SER A OG  1 
ATOM   301  N  N   . PRO A 1 30  ? -2.778  -4.315  22.958  1.00 5.78  ? 30  PRO A N   1 
ATOM   302  C  CA  . PRO A 1 30  ? -3.949  -4.847  23.669  1.00 5.56  ? 30  PRO A CA  1 
ATOM   303  C  C   . PRO A 1 30  ? -3.531  -5.503  24.961  1.00 6.23  ? 30  PRO A C   1 
ATOM   304  O  O   . PRO A 1 30  ? -2.358  -5.536  25.333  1.00 7.14  ? 30  PRO A O   1 
ATOM   305  C  CB  . PRO A 1 30  ? -4.482  -5.862  22.638  1.00 6.10  ? 30  PRO A CB  1 
ATOM   306  C  CG  . PRO A 1 30  ? -3.195  -6.452  22.098  1.00 6.49  ? 30  PRO A CG  1 
ATOM   307  C  CD  . PRO A 1 30  ? -2.297  -5.233  21.911  1.00 6.36  ? 30  PRO A CD  1 
ATOM   308  N  N   . VAL A 1 31  ? -4.542  -6.063  25.633  1.00 6.67  ? 31  VAL A N   1 
ATOM   309  C  CA  . VAL A 1 31  ? -4.362  -6.801  26.906  1.00 6.74  ? 31  VAL A CA  1 
ATOM   310  C  C   . VAL A 1 31  ? -5.242  -8.014  26.874  1.00 6.96  ? 31  VAL A C   1 
ATOM   311  O  O   . VAL A 1 31  ? -6.217  -8.078  26.097  1.00 7.11  ? 31  VAL A O   1 
ATOM   312  C  CB  . VAL A 1 31  ? -4.698  -5.944  28.136  1.00 7.13  ? 31  VAL A CB  1 
ATOM   313  C  CG1 . VAL A 1 31  ? -3.779  -4.769  28.235  1.00 8.75  ? 31  VAL A CG1 1 
ATOM   314  C  CG2 . VAL A 1 31  ? -6.154  -5.521  28.169  1.00 8.24  ? 31  VAL A CG2 1 
ATOM   315  N  N   . ASP A 1 32  ? -4.919  -9.000  27.716  1.00 7.08  ? 32  ASP A N   1 
ATOM   316  C  CA  . ASP A 1 32  ? -5.862  -10.072 28.023  1.00 6.96  ? 32  ASP A CA  1 
ATOM   317  C  C   . ASP A 1 32  ? -6.900  -9.523  28.965  1.00 7.67  ? 32  ASP A C   1 
ATOM   318  O  O   . ASP A 1 32  ? -6.591  -8.852  29.959  1.00 8.77  ? 32  ASP A O   1 
ATOM   319  C  CB  . ASP A 1 32  ? -5.128  -11.245 28.651  1.00 8.13  ? 32  ASP A CB  1 
ATOM   320  C  CG  . ASP A 1 32  ? -6.064  -12.410 28.922  1.00 8.76  ? 32  ASP A CG  1 
ATOM   321  O  OD1 . ASP A 1 32  ? -6.746  -12.878 27.981  1.00 8.38  ? 32  ASP A OD1 1 
ATOM   322  O  OD2 . ASP A 1 32  ? -6.116  -12.816 30.138  1.00 10.71 ? 32  ASP A OD2 1 
ATOM   323  N  N   . ILE A 1 33  ? -8.131  -9.879  28.705  1.00 7.74  ? 33  ILE A N   1 
ATOM   324  C  CA  . ILE A 1 33  ? -9.277  -9.517  29.557  1.00 7.80  ? 33  ILE A CA  1 
ATOM   325  C  C   . ILE A 1 33  ? -9.558  -10.751 30.388  1.00 7.78  ? 33  ILE A C   1 
ATOM   326  O  O   . ILE A 1 33  ? -10.113 -11.728 29.897  1.00 8.59  ? 33  ILE A O   1 
ATOM   327  C  CB  . ILE A 1 33  ? -10.473 -9.083  28.707  1.00 7.52  ? 33  ILE A CB  1 
ATOM   328  C  CG1 . ILE A 1 33  ? -10.114 -7.876  27.856  1.00 8.22  ? 33  ILE A CG1 1 
ATOM   329  C  CG2 . ILE A 1 33  ? -11.685 -8.855  29.606  1.00 9.82  ? 33  ILE A CG2 1 
ATOM   330  C  CD1 . ILE A 1 33  ? -11.161 -7.587  26.750  1.00 10.01 ? 33  ILE A CD1 1 
ATOM   331  N  N   A ASP A 1 34  ? -9.323  -10.638 31.693  0.50 8.70  ? 34  ASP A N   1 
ATOM   332  N  N   B ASP A 1 34  ? -9.029  -10.722 31.621  0.50 9.98  ? 34  ASP A N   1 
ATOM   333  C  CA  A ASP A 1 34  ? -9.657  -11.698 32.636  0.50 9.92  ? 34  ASP A CA  1 
ATOM   334  C  CA  B ASP A 1 34  ? -9.278  -11.781 32.579  0.50 10.15 ? 34  ASP A CA  1 
ATOM   335  C  C   A ASP A 1 34  ? -11.116 -11.451 33.095  0.50 9.00  ? 34  ASP A C   1 
ATOM   336  C  C   B ASP A 1 34  ? -10.679 -11.511 33.128  0.50 10.53 ? 34  ASP A C   1 
ATOM   337  O  O   A ASP A 1 34  ? -11.397 -10.546 33.890  0.50 12.12 ? 34  ASP A O   1 
ATOM   338  O  O   B ASP A 1 34  ? -10.892 -10.561 33.911  0.50 11.64 ? 34  ASP A O   1 
ATOM   339  C  CB  A ASP A 1 34  ? -8.614  -11.696 33.744  0.50 10.93 ? 34  ASP A CB  1 
ATOM   340  C  CB  B ASP A 1 34  ? -8.281  -11.766 33.688  0.50 13.28 ? 34  ASP A CB  1 
ATOM   341  C  CG  A ASP A 1 34  ? -8.591  -13.020 34.539  0.50 10.73 ? 34  ASP A CG  1 
ATOM   342  C  CG  B ASP A 1 34  ? -8.742  -12.640 34.889  0.50 13.78 ? 34  ASP A CG  1 
ATOM   343  O  OD1 A ASP A 1 34  ? -9.077  -12.955 35.652  0.50 10.44 ? 34  ASP A OD1 1 
ATOM   344  O  OD1 B ASP A 1 34  ? -9.915  -13.076 35.038  0.50 13.22 ? 34  ASP A OD1 1 
ATOM   345  O  OD2 A ASP A 1 34  ? -8.153  -14.095 34.066  0.50 12.86 ? 34  ASP A OD2 1 
ATOM   346  O  OD2 B ASP A 1 34  ? -7.912  -12.799 35.757  0.50 18.29 ? 34  ASP A OD2 1 
ATOM   347  N  N   A THR A 1 35  ? -12.059 -12.251 32.610  0.50 9.12  ? 35  THR A N   1 
ATOM   348  N  N   B THR A 1 35  ? -11.630 -12.327 32.717  0.50 10.70 ? 35  THR A N   1 
ATOM   349  C  CA  A THR A 1 35  ? -13.488 -11.910 32.802  0.50 13.01 ? 35  THR A CA  1 
ATOM   350  C  CA  B THR A 1 35  ? -13.003 -12.029 33.024  0.50 9.66  ? 35  THR A CA  1 
ATOM   351  C  C   A THR A 1 35  ? -13.917 -12.040 34.223  0.50 11.54 ? 35  THR A C   1 
ATOM   352  C  C   B THR A 1 35  ? -13.288 -12.073 34.525  0.50 11.88 ? 35  THR A C   1 
ATOM   353  O  O   A THR A 1 35  ? -14.889 -11.428 34.610  0.50 13.25 ? 35  THR A O   1 
ATOM   354  O  O   B THR A 1 35  ? -14.197 -11.390 35.000  0.50 13.28 ? 35  THR A O   1 
ATOM   355  C  CB  A THR A 1 35  ? -14.390 -12.881 32.034  0.50 13.28 ? 35  THR A CB  1 
ATOM   356  C  CB  B THR A 1 35  ? -13.942 -12.926 32.196  0.50 10.35 ? 35  THR A CB  1 
ATOM   357  O  OG1 A THR A 1 35  ? -14.223 -14.225 32.529  0.50 12.14 ? 35  THR A OG1 1 
ATOM   358  O  OG1 B THR A 1 35  ? -13.744 -14.310 32.547  0.50 13.45 ? 35  THR A OG1 1 
ATOM   359  C  CG2 A THR A 1 35  ? -14.176 -12.788 30.491  0.50 13.68 ? 35  THR A CG2 1 
ATOM   360  C  CG2 B THR A 1 35  ? -13.650 -12.720 30.665  0.50 13.45 ? 35  THR A CG2 1 
ATOM   361  N  N   A HIS A 1 36  ? -13.291 -12.951 34.955  0.50 12.22 ? 36  HIS A N   1 
ATOM   362  N  N   B HIS A 1 36  ? -12.501 -12.858 35.283  0.50 11.43 ? 36  HIS A N   1 
ATOM   363  C  CA  A HIS A 1 36  ? -13.539 -13.111 36.393  0.50 10.31 ? 36  HIS A CA  1 
ATOM   364  C  CA  B HIS A 1 36  ? -12.632 -13.001 36.751  0.50 10.27 ? 36  HIS A CA  1 
ATOM   365  C  C   A HIS A 1 36  ? -12.956 -11.998 37.261  0.50 11.98 ? 36  HIS A C   1 
ATOM   366  C  C   B HIS A 1 36  ? -11.911 -11.933 37.506  0.50 10.87 ? 36  HIS A C   1 
ATOM   367  O  O   A HIS A 1 36  ? -13.470 -11.729 38.342  0.50 12.39 ? 36  HIS A O   1 
ATOM   368  O  O   B HIS A 1 36  ? -11.903 -11.925 38.746  0.50 13.54 ? 36  HIS A O   1 
ATOM   369  C  CB  A HIS A 1 36  ? -13.089 -14.505 36.836  0.50 11.25 ? 36  HIS A CB  1 
ATOM   370  C  CB  B HIS A 1 36  ? -12.151 -14.351 37.166  0.50 10.29 ? 36  HIS A CB  1 
ATOM   371  C  CG  A HIS A 1 36  ? -14.038 -15.545 36.428  0.50 10.57 ? 36  HIS A CG  1 
ATOM   372  C  CG  B HIS A 1 36  ? -12.930 -15.441 36.502  0.50 11.54 ? 36  HIS A CG  1 
ATOM   373  N  ND1 A HIS A 1 36  ? -13.754 -16.537 35.554  0.50 13.44 ? 36  HIS A ND1 1 
ATOM   374  N  ND1 B HIS A 1 36  ? -14.066 -16.001 37.019  0.50 19.46 ? 36  HIS A ND1 1 
ATOM   375  C  CD2 A HIS A 1 36  ? -15.367 -15.708 36.812  0.50 10.81 ? 36  HIS A CD2 1 
ATOM   376  C  CD2 B HIS A 1 36  ? -12.658 -16.114 35.317  0.50 11.66 ? 36  HIS A CD2 1 
ATOM   377  C  CE1 A HIS A 1 36  ? -14.898 -17.299 35.378  0.50 12.84 ? 36  HIS A CE1 1 
ATOM   378  C  CE1 B HIS A 1 36  ? -14.493 -16.965 36.177  0.50 18.10 ? 36  HIS A CE1 1 
ATOM   379  N  NE2 A HIS A 1 36  ? -15.863 -16.795 36.164  0.50 16.62 ? 36  HIS A NE2 1 
ATOM   380  N  NE2 B HIS A 1 36  ? -13.608 -17.043 35.140  0.50 14.70 ? 36  HIS A NE2 1 
ATOM   381  N  N   A THR A 1 37  ? -11.864 -11.361 36.841  0.50 13.15 ? 37  THR A N   1 
ATOM   382  N  N   B THR A 1 37  ? -11.339 -10.983 36.809  0.50 14.58 ? 37  THR A N   1 
ATOM   383  C  CA  A THR A 1 37  ? -11.295 -10.200 37.548  0.50 13.95 ? 37  THR A CA  1 
ATOM   384  C  CA  B THR A 1 37  ? -10.805 -9.863  37.529  0.50 12.93 ? 37  THR A CA  1 
ATOM   385  C  C   A THR A 1 37  ? -11.888 -8.824  37.231  0.50 13.00 ? 37  THR A C   1 
ATOM   386  C  C   B THR A 1 37  ? -11.413 -8.571  37.072  0.50 13.18 ? 37  THR A C   1 
ATOM   387  O  O   A THR A 1 37  ? -12.000 -7.937  38.056  0.50 12.96 ? 37  THR A O   1 
ATOM   388  O  O   B THR A 1 37  ? -11.239 -7.552  37.767  0.50 14.58 ? 37  THR A O   1 
ATOM   389  C  CB  A THR A 1 37  ? -9.788  -10.103 37.270  0.50 15.36 ? 37  THR A CB  1 
ATOM   390  C  CB  B THR A 1 37  ? -9.279  -9.947  37.511  0.50 19.88 ? 37  THR A CB  1 
ATOM   391  O  OG1 A THR A 1 37  ? -9.195  -11.356 37.571  0.50 20.12 ? 37  THR A OG1 1 
ATOM   392  O  OG1 B THR A 1 37  ? -8.933  -11.107 38.294  0.50 23.44 ? 37  THR A OG1 1 
ATOM   393  C  CG2 A THR A 1 37  ? -9.131  -9.077  38.138  0.50 16.86 ? 37  THR A CG2 1 
ATOM   394  C  CG2 B THR A 1 37  ? -8.563  -8.675  38.056  0.50 19.47 ? 37  THR A CG2 1 
ATOM   395  N  N   . ALA A 1 38  ? -12.225 -8.599  35.987  1.00 13.73 ? 38  ALA A N   1 
ATOM   396  C  CA  . ALA A 1 38  ? -12.882 -7.376  35.544  1.00 13.11 ? 38  ALA A CA  1 
ATOM   397  C  C   . ALA A 1 38  ? -14.020 -7.100  36.456  1.00 16.11 ? 38  ALA A C   1 
ATOM   398  O  O   . ALA A 1 38  ? -14.790 -7.985  36.769  1.00 25.75 ? 38  ALA A O   1 
ATOM   399  C  CB  . ALA A 1 38  ? -13.373 -7.586  34.116  1.00 14.81 ? 38  ALA A CB  1 
ATOM   400  N  N   . LYS A 1 39  ? -14.122 -5.863  36.929  1.00 16.92 ? 39  LYS A N   1 
ATOM   401  C  CA  . LYS A 1 39  ? -15.173 -5.578  37.881  1.00 21.64 ? 39  LYS A CA  1 
ATOM   402  C  C   . LYS A 1 39  ? -16.358 -4.940  37.224  1.00 15.78 ? 39  LYS A C   1 
ATOM   403  O  O   . LYS A 1 39  ? -16.241 -3.940  36.492  1.00 14.30 ? 39  LYS A O   1 
ATOM   404  C  CB  . LYS A 1 39  ? -14.708 -4.800  39.037  1.00 27.64 ? 39  LYS A CB  1 
ATOM   405  C  CG  . LYS A 1 39  ? -15.683 -4.995  40.187  1.00 26.48 ? 39  LYS A CG  1 
ATOM   406  C  CD  . LYS A 1 39  ? -15.147 -4.228  41.356  1.00 27.06 ? 39  LYS A CD  1 
ATOM   407  C  CE  . LYS A 1 39  ? -16.154 -3.364  42.055  1.00 30.07 ? 39  LYS A CE  1 
ATOM   408  N  NZ  . LYS A 1 39  ? -16.662 -4.308  43.022  1.00 29.56 ? 39  LYS A NZ  1 
ATOM   409  N  N   . TYR A 1 40  ? -17.536 -5.444  37.524  1.00 17.59 ? 40  TYR A N   1 
ATOM   410  C  CA  . TYR A 1 40  ? -18.737 -4.785  37.075  1.00 15.77 ? 40  TYR A CA  1 
ATOM   411  C  C   . TYR A 1 40  ? -18.810 -3.413  37.724  1.00 12.84 ? 40  TYR A C   1 
ATOM   412  O  O   . TYR A 1 40  ? -18.736 -3.307  38.955  1.00 16.35 ? 40  TYR A O   1 
ATOM   413  C  CB  . TYR A 1 40  ? -19.953 -5.635  37.489  1.00 20.57 ? 40  TYR A CB  1 
ATOM   414  C  CG  . TYR A 1 40  ? -21.202 -4.893  37.354  1.00 20.23 ? 40  TYR A CG  1 
ATOM   415  C  CD1 . TYR A 1 40  ? -21.604 -4.364  36.118  1.00 20.71 ? 40  TYR A CD1 1 
ATOM   416  C  CD2 . TYR A 1 40  ? -22.037 -4.754  38.436  1.00 24.49 ? 40  TYR A CD2 1 
ATOM   417  C  CE1 . TYR A 1 40  ? -22.793 -3.677  35.971  1.00 21.05 ? 40  TYR A CE1 1 
ATOM   418  C  CE2 . TYR A 1 40  ? -23.230 -4.053  38.295  1.00 24.24 ? 40  TYR A CE2 1 
ATOM   419  C  CZ  . TYR A 1 40  ? -23.620 -3.505  37.078  1.00 23.98 ? 40  TYR A CZ  1 
ATOM   420  O  OH  . TYR A 1 40  ? -24.831 -2.829  36.937  1.00 31.49 ? 40  TYR A OH  1 
ATOM   421  N  N   . ASP A 1 41  ? -19.022 -2.388  36.918  1.00 12.82 ? 41  ASP A N   1 
ATOM   422  C  CA  . ASP A 1 41  ? -19.086 -1.006  37.375  1.00 13.23 ? 41  ASP A CA  1 
ATOM   423  C  C   . ASP A 1 41  ? -20.451 -0.465  37.120  1.00 13.36 ? 41  ASP A C   1 
ATOM   424  O  O   . ASP A 1 41  ? -20.767 -0.134  36.001  1.00 15.21 ? 41  ASP A O   1 
ATOM   425  C  CB  . ASP A 1 41  ? -18.028 -0.152  36.671  1.00 15.74 ? 41  ASP A CB  1 
ATOM   426  C  CG  . ASP A 1 41  ? -17.963 1.224   37.219  1.00 19.07 ? 41  ASP A CG  1 
ATOM   427  O  OD1 . ASP A 1 41  ? -18.867 1.615   38.006  1.00 19.91 ? 41  ASP A OD1 1 
ATOM   428  O  OD2 . ASP A 1 41  ? -17.000 1.927   36.833  1.00 20.87 ? 41  ASP A OD2 1 
ATOM   429  N  N   . PRO A 1 42  ? -21.313 -0.411  38.159  1.00 17.63 ? 42  PRO A N   1 
ATOM   430  C  CA  . PRO A 1 42  ? -22.701 -0.041  37.953  1.00 19.94 ? 42  PRO A CA  1 
ATOM   431  C  C   . PRO A 1 42  ? -22.801 1.411   37.523  1.00 19.14 ? 42  PRO A C   1 
ATOM   432  O  O   . PRO A 1 42  ? -23.887 1.854   37.110  1.00 27.34 ? 42  PRO A O   1 
ATOM   433  C  CB  . PRO A 1 42  ? -23.344 -0.282  39.343  1.00 23.92 ? 42  PRO A CB  1 
ATOM   434  C  CG  . PRO A 1 42  ? -22.226 -0.151  40.322  1.00 23.77 ? 42  PRO A CG  1 
ATOM   435  C  CD  . PRO A 1 42  ? -21.069 -0.788  39.579  1.00 19.51 ? 42  PRO A CD  1 
ATOM   436  N  N   . SER A 1 43  ? -21.741 2.178   37.722  1.00 20.82 ? 43  SER A N   1 
ATOM   437  C  CA  . SER A 1 43  ? -21.725 3.614   37.271  1.00 23.22 ? 43  SER A CA  1 
ATOM   438  C  C   . SER A 1 43  ? -21.431 3.843   35.798  1.00 22.00 ? 43  SER A C   1 
ATOM   439  O  O   . SER A 1 43  ? -21.698 4.922   35.304  1.00 28.03 ? 43  SER A O   1 
ATOM   440  C  CB  . SER A 1 43  ? -20.724 4.410   38.072  1.00 27.16 ? 43  SER A CB  1 
ATOM   441  O  OG  . SER A 1 43  ? -19.373 4.189   37.697  1.00 27.42 ? 43  SER A OG  1 
ATOM   442  N  N   . LEU A 1 44  ? -20.932 2.846   35.090  1.00 20.78 ? 44  LEU A N   1 
ATOM   443  C  CA  . LEU A 1 44  ? -20.766 2.888   33.612  1.00 20.38 ? 44  LEU A CA  1 
ATOM   444  C  C   . LEU A 1 44  ? -22.115 3.010   32.916  1.00 19.70 ? 44  LEU A C   1 
ATOM   445  O  O   . LEU A 1 44  ? -23.130 2.410   33.295  1.00 26.82 ? 44  LEU A O   1 
ATOM   446  C  CB  . LEU A 1 44  ? -20.048 1.645   33.133  1.00 16.98 ? 44  LEU A CB  1 
ATOM   447  C  CG  . LEU A 1 44  ? -18.566 1.626   33.352  1.00 15.37 ? 44  LEU A CG  1 
ATOM   448  C  CD1 . LEU A 1 44  ? -18.117 0.291   32.909  1.00 16.34 ? 44  LEU A CD1 1 
ATOM   449  C  CD2 . LEU A 1 44  ? -17.879 2.692   32.589  1.00 15.62 ? 44  LEU A CD2 1 
ATOM   450  N  N   A LYS A 1 45  ? -22.247 3.996   32.022  0.50 25.72 ? 45  LYS A N   1 
ATOM   451  N  N   B LYS A 1 45  ? -22.075 3.752   31.828  0.50 14.86 ? 45  LYS A N   1 
ATOM   452  C  CA  A LYS A 1 45  ? -23.504 4.222   31.258  0.50 15.50 ? 45  LYS A CA  1 
ATOM   453  C  CA  B LYS A 1 45  ? -23.228 3.961   31.003  0.50 19.77 ? 45  LYS A CA  1 
ATOM   454  C  C   A LYS A 1 45  ? -23.622 3.383   29.973  0.50 16.44 ? 45  LYS A C   1 
ATOM   455  C  C   B LYS A 1 45  ? -23.297 2.937   29.916  0.50 16.45 ? 45  LYS A C   1 
ATOM   456  O  O   A LYS A 1 45  ? -22.609 2.746   29.458  0.50 15.13 ? 45  LYS A O   1 
ATOM   457  O  O   B LYS A 1 45  ? -22.288 2.109   29.719  0.50 19.11 ? 45  LYS A O   1 
ATOM   458  C  CB  A LYS A 1 45  ? -23.708 5.695   30.896  0.50 22.73 ? 45  LYS A CB  1 
ATOM   459  C  CB  B LYS A 1 45  ? -23.344 5.386   30.552  0.50 13.97 ? 45  LYS A CB  1 
ATOM   460  C  CG  A LYS A 1 45  ? -23.983 6.662   32.041  0.50 21.51 ? 45  LYS A CG  1 
ATOM   461  C  CG  B LYS A 1 45  ? -23.301 6.271   31.754  0.50 19.88 ? 45  LYS A CG  1 
ATOM   462  C  CD  A LYS A 1 45  ? -24.046 8.085   31.491  0.50 26.98 ? 45  LYS A CD  1 
ATOM   463  C  CD  B LYS A 1 45  ? -23.007 7.701   31.347  0.50 26.27 ? 45  LYS A CD  1 
ATOM   464  C  CE  A LYS A 1 45  ? -24.861 8.230   30.199  0.50 35.10 ? 45  LYS A CE  1 
ATOM   465  C  CE  B LYS A 1 45  ? -23.538 8.692   32.388  0.50 36.13 ? 45  LYS A CE  1 
ATOM   466  N  NZ  A LYS A 1 45  ? -24.781 9.632   29.655  0.50 40.54 ? 45  LYS A NZ  1 
ATOM   467  N  NZ  B LYS A 1 45  ? -24.480 9.693   31.778  0.50 41.06 ? 45  LYS A NZ  1 
ATOM   468  N  N   A PRO A 1 46  ? -24.890 3.338   29.435  0.50 18.87 ? 46  PRO A N   1 
ATOM   469  N  N   B PRO A 1 46  ? -24.503 2.878   29.282  0.50 14.25 ? 46  PRO A N   1 
ATOM   470  C  CA  A PRO A 1 46  ? -25.012 2.693   28.186  0.50 19.94 ? 46  PRO A CA  1 
ATOM   471  C  CA  B PRO A 1 46  ? -24.688 2.190   28.033  0.50 12.50 ? 46  PRO A CA  1 
ATOM   472  C  C   A PRO A 1 46  ? -24.113 3.523   27.358  0.50 18.84 ? 46  PRO A C   1 
ATOM   473  C  C   B PRO A 1 46  ? -23.917 2.961   26.972  0.50 11.66 ? 46  PRO A C   1 
ATOM   474  O  O   A PRO A 1 46  ? -24.011 4.786   27.496  0.50 16.04 ? 46  PRO A O   1 
ATOM   475  O  O   B PRO A 1 46  ? -23.783 4.153   27.009  0.50 11.15 ? 46  PRO A O   1 
ATOM   476  C  CB  A PRO A 1 46  ? -26.479 2.928   27.769  0.50 20.77 ? 46  PRO A CB  1 
ATOM   477  C  CB  B PRO A 1 46  ? -26.223 2.249   27.818  0.50 13.11 ? 46  PRO A CB  1 
ATOM   478  C  CG  A PRO A 1 46  ? -27.192 2.934   29.034  0.50 21.03 ? 46  PRO A CG  1 
ATOM   479  C  CG  B PRO A 1 46  ? -26.794 2.378   29.189  0.50 15.19 ? 46  PRO A CG  1 
ATOM   480  C  CD  A PRO A 1 46  ? -26.204 3.524   30.037  0.50 18.47 ? 46  PRO A CD  1 
ATOM   481  C  CD  B PRO A 1 46  ? -25.793 3.361   29.787  0.50 16.65 ? 46  PRO A CD  1 
ATOM   482  N  N   A LEU A 1 47  ? -23.432 2.781   26.544  0.50 18.61 ? 47  LEU A N   1 
ATOM   483  N  N   B LEU A 1 47  ? -23.286 2.248   26.046  0.50 11.06 ? 47  LEU A N   1 
ATOM   484  C  CA  A LEU A 1 47  ? -22.783 3.330   25.464  0.50 16.75 ? 47  LEU A CA  1 
ATOM   485  C  CA  B LEU A 1 47  ? -22.566 2.930   25.004  0.50 11.97 ? 47  LEU A CA  1 
ATOM   486  C  C   A LEU A 1 47  ? -23.846 3.905   24.533  0.50 16.86 ? 47  LEU A C   1 
ATOM   487  C  C   B LEU A 1 47  ? -23.584 3.529   24.020  0.50 11.37 ? 47  LEU A C   1 
ATOM   488  O  O   A LEU A 1 47  ? -24.975 3.441   24.522  0.50 17.92 ? 47  LEU A O   1 
ATOM   489  O  O   B LEU A 1 47  ? -24.602 2.847   23.728  0.50 11.38 ? 47  LEU A O   1 
ATOM   490  C  CB  A LEU A 1 47  ? -22.172 2.150   24.766  0.50 20.30 ? 47  LEU A CB  1 
ATOM   491  C  CB  B LEU A 1 47  ? -21.758 1.928   24.245  0.50 13.24 ? 47  LEU A CB  1 
ATOM   492  C  CG  A LEU A 1 47  ? -20.713 1.824   24.830  0.50 23.00 ? 47  LEU A CG  1 
ATOM   493  C  CG  B LEU A 1 47  ? -20.813 2.344   23.205  0.50 13.77 ? 47  LEU A CG  1 
ATOM   494  C  CD1 A LEU A 1 47  ? -20.516 0.816   23.723  0.50 20.73 ? 47  LEU A CD1 1 
ATOM   495  C  CD1 B LEU A 1 47  ? -19.753 3.259   23.843  0.50 14.91 ? 47  LEU A CD1 1 
ATOM   496  C  CD2 A LEU A 1 47  ? -19.766 3.037   24.759  0.50 16.09 ? 47  LEU A CD2 1 
ATOM   497  C  CD2 B LEU A 1 47  ? -20.112 1.110   22.643  0.50 13.90 ? 47  LEU A CD2 1 
ATOM   498  N  N   . SER A 1 48  ? -23.417 4.815   23.676  1.00 14.12 ? 48  SER A N   1 
ATOM   499  C  CA  . SER A 1 48  ? -24.229 5.413   22.627  1.00 13.68 ? 48  SER A CA  1 
ATOM   500  C  C   . SER A 1 48  ? -23.466 5.407   21.302  1.00 12.90 ? 48  SER A C   1 
ATOM   501  O  O   . SER A 1 48  ? -22.455 6.110   21.149  1.00 13.32 ? 48  SER A O   1 
ATOM   502  C  CB  . SER A 1 48  ? -24.609 6.847   23.021  1.00 15.74 ? 48  SER A CB  1 
ATOM   503  O  OG  . SER A 1 48  ? -25.235 7.483   21.941  1.00 19.28 ? 48  SER A OG  1 
ATOM   504  N  N   . VAL A 1 49  ? -23.867 4.542   20.402  1.00 15.40 ? 49  VAL A N   1 
ATOM   505  C  CA  . VAL A 1 49  ? -23.289 4.454   19.076  1.00 17.42 ? 49  VAL A CA  1 
ATOM   506  C  C   . VAL A 1 49  ? -24.263 5.099   18.063  1.00 18.13 ? 49  VAL A C   1 
ATOM   507  O  O   . VAL A 1 49  ? -25.339 4.552   17.890  1.00 23.54 ? 49  VAL A O   1 
ATOM   508  C  CB  . VAL A 1 49  ? -23.072 2.968   18.730  1.00 20.37 ? 49  VAL A CB  1 
ATOM   509  C  CG1 . VAL A 1 49  ? -22.394 2.868   17.385  1.00 23.90 ? 49  VAL A CG1 1 
ATOM   510  C  CG2 . VAL A 1 49  ? -22.277 2.271   19.820  1.00 20.46 ? 49  VAL A CG2 1 
ATOM   511  N  N   . SER A 1 50  ? -24.012 6.287   17.526  1.00 17.34 ? 50  SER A N   1 
ATOM   512  C  CA  . SER A 1 50  ? -24.932 6.994   16.632  1.00 21.04 ? 50  SER A CA  1 
ATOM   513  C  C   . SER A 1 50  ? -24.242 7.029   15.308  1.00 17.96 ? 50  SER A C   1 
ATOM   514  O  O   . SER A 1 50  ? -23.458 7.933   15.034  1.00 18.19 ? 50  SER A O   1 
ATOM   515  C  CB  . SER A 1 50  ? -25.255 8.425   17.151  1.00 25.05 ? 50  SER A CB  1 
ATOM   516  O  OG  . SER A 1 50  ? -25.810 8.339   18.430  1.00 31.37 ? 50  SER A OG  1 
ATOM   517  N  N   . TYR A 1 51  ? -24.531 6.009   14.476  1.00 17.55 ? 51  TYR A N   1 
ATOM   518  C  CA  . TYR A 1 51  ? -23.938 5.878   13.191  1.00 19.08 ? 51  TYR A CA  1 
ATOM   519  C  C   . TYR A 1 51  ? -24.923 6.123   12.048  1.00 19.65 ? 51  TYR A C   1 
ATOM   520  O  O   . TYR A 1 51  ? -24.506 5.964   10.896  1.00 20.38 ? 51  TYR A O   1 
ATOM   521  C  CB  . TYR A 1 51  ? -23.264 4.496   13.021  1.00 17.55 ? 51  TYR A CB  1 
ATOM   522  C  CG  . TYR A 1 51  ? -21.993 4.227   13.819  1.00 14.46 ? 51  TYR A CG  1 
ATOM   523  C  CD1 . TYR A 1 51  ? -21.293 5.215   14.504  1.00 14.37 ? 51  TYR A CD1 1 
ATOM   524  C  CD2 . TYR A 1 51  ? -21.523 2.935   13.879  1.00 13.50 ? 51  TYR A CD2 1 
ATOM   525  C  CE1 . TYR A 1 51  ? -20.107 4.907   15.176  1.00 13.90 ? 51  TYR A CE1 1 
ATOM   526  C  CE2 . TYR A 1 51  ? -20.341 2.602   14.538  1.00 13.72 ? 51  TYR A CE2 1 
ATOM   527  C  CZ  . TYR A 1 51  ? -19.642 3.594   15.208  1.00 13.47 ? 51  TYR A CZ  1 
ATOM   528  O  OH  . TYR A 1 51  ? -18.467 3.230   15.841  1.00 13.30 ? 51  TYR A OH  1 
ATOM   529  N  N   A ASP A 1 52  ? -26.131 6.611   12.407  0.50 22.30 ? 52  ASP A N   1 
ATOM   530  N  N   B ASP A 1 52  ? -26.202 6.454   12.298  0.50 22.65 ? 52  ASP A N   1 
ATOM   531  C  CA  A ASP A 1 52  ? -27.222 6.867   11.462  0.50 21.92 ? 52  ASP A CA  1 
ATOM   532  C  CA  B ASP A 1 52  ? -27.177 6.721   11.211  0.50 26.99 ? 52  ASP A CA  1 
ATOM   533  C  C   A ASP A 1 52  ? -26.888 7.801   10.282  0.50 19.82 ? 52  ASP A C   1 
ATOM   534  C  C   B ASP A 1 52  ? -26.586 7.628   10.089  0.50 26.37 ? 52  ASP A C   1 
ATOM   535  O  O   A ASP A 1 52  ? -27.463 7.605   9.187   0.50 18.35 ? 52  ASP A O   1 
ATOM   536  O  O   B ASP A 1 52  ? -26.701 7.302   8.868   0.50 22.02 ? 52  ASP A O   1 
ATOM   537  C  CB  A ASP A 1 52  ? -28.536 7.276   12.156  0.50 23.03 ? 52  ASP A CB  1 
ATOM   538  C  CB  B ASP A 1 52  ? -28.476 7.315   11.817  0.50 28.30 ? 52  ASP A CB  1 
ATOM   539  C  CG  A ASP A 1 52  ? -28.323 8.287   13.269  0.50 27.56 ? 52  ASP A CG  1 
ATOM   540  C  CG  B ASP A 1 52  ? -29.656 7.381   10.839  0.50 28.32 ? 52  ASP A CG  1 
ATOM   541  O  OD1 A ASP A 1 52  ? -27.677 7.916   14.289  0.50 39.07 ? 52  ASP A OD1 1 
ATOM   542  O  OD1 B ASP A 1 52  ? -30.170 6.313   10.408  0.50 28.83 ? 52  ASP A OD1 1 
ATOM   543  O  OD2 A ASP A 1 52  ? -28.796 9.448   13.117  0.50 35.62 ? 52  ASP A OD2 1 
ATOM   544  O  OD2 B ASP A 1 52  ? -30.126 8.524   10.578  0.50 31.01 ? 52  ASP A OD2 1 
ATOM   545  N  N   . GLN A 1 53  ? -25.939 8.732   10.480  1.00 24.40 ? 53  GLN A N   1 
ATOM   546  C  CA  . GLN A 1 53  ? -25.518 9.692   9.447   1.00 29.21 ? 53  GLN A CA  1 
ATOM   547  C  C   . GLN A 1 53  ? -24.088 9.474   8.902   1.00 20.88 ? 53  GLN A C   1 
ATOM   548  O  O   . GLN A 1 53  ? -23.513 10.363  8.284   1.00 24.22 ? 53  GLN A O   1 
ATOM   549  C  CB  . GLN A 1 53  ? -25.735 11.128  9.973   1.00 38.13 ? 53  GLN A CB  1 
ATOM   550  C  CG  . GLN A 1 53  ? -27.200 11.550  9.921   1.00 37.63 ? 53  GLN A CG  1 
ATOM   551  C  CD  . GLN A 1 53  ? -27.792 11.335  8.540   1.00 47.45 ? 53  GLN A CD  1 
ATOM   552  O  OE1 . GLN A 1 53  ? -27.283 11.872  7.523   1.00 44.17 ? 53  GLN A OE1 1 
ATOM   553  N  NE2 . GLN A 1 53  ? -28.855 10.534  8.470   1.00 48.78 ? 53  GLN A NE2 1 
ATOM   554  N  N   . ALA A 1 54  ? -23.505 8.297   9.137   1.00 19.89 ? 54  ALA A N   1 
ATOM   555  C  CA  . ALA A 1 54  ? -22.124 8.034   8.709   1.00 17.70 ? 54  ALA A CA  1 
ATOM   556  C  C   . ALA A 1 54  ? -21.886 8.164   7.206   1.00 20.27 ? 54  ALA A C   1 
ATOM   557  O  O   . ALA A 1 54  ? -22.743 7.794   6.388   1.00 23.39 ? 54  ALA A O   1 
ATOM   558  C  CB  . ALA A 1 54  ? -21.688 6.652   9.142   1.00 20.43 ? 54  ALA A CB  1 
ATOM   559  N  N   A THR A 1 55  ? -20.895 8.886   6.842   0.50 14.15 ? 55  THR A N   1 
ATOM   560  N  N   B THR A 1 55  ? -20.654 8.646   6.853   0.50 17.05 ? 55  THR A N   1 
ATOM   561  C  CA  A THR A 1 55  ? -20.781 8.973   5.460   0.50 14.12 ? 55  THR A CA  1 
ATOM   562  C  CA  B THR A 1 55  ? -20.069 8.888   5.435   0.50 13.50 ? 55  THR A CA  1 
ATOM   563  C  C   A THR A 1 55  ? -19.521 8.258   5.301   0.50 9.44  ? 55  THR A C   1 
ATOM   564  C  C   B THR A 1 55  ? -18.679 8.256   5.143   0.50 11.00 ? 55  THR A C   1 
ATOM   565  O  O   A THR A 1 55  ? -18.466 8.827   5.585   0.50 13.00 ? 55  THR A O   1 
ATOM   566  O  O   B THR A 1 55  ? -17.603 8.845   5.440   0.50 11.24 ? 55  THR A O   1 
ATOM   567  C  CB  A THR A 1 55  ? -20.636 10.424  4.980   0.50 14.27 ? 55  THR A CB  1 
ATOM   568  C  CB  B THR A 1 55  ? -19.907 10.405  5.028   0.50 14.89 ? 55  THR A CB  1 
ATOM   569  O  OG1 A THR A 1 55  ? -21.878 11.128  5.233   0.50 21.30 ? 55  THR A OG1 1 
ATOM   570  O  OG1 B THR A 1 55  ? -21.150 11.014  5.021   0.50 15.33 ? 55  THR A OG1 1 
ATOM   571  C  CG2 A THR A 1 55  ? -20.269 10.361  3.531   0.50 16.53 ? 55  THR A CG2 1 
ATOM   572  C  CG2 B THR A 1 55  ? -19.390 10.558  3.595   0.50 13.76 ? 55  THR A CG2 1 
ATOM   573  N  N   A SER A 1 56  ? -19.591 6.986   4.885   0.50 8.62  ? 56  SER A N   1 
ATOM   574  N  N   B SER A 1 56  ? -18.664 7.043   4.603   0.50 9.35  ? 56  SER A N   1 
ATOM   575  C  CA  A SER A 1 56  ? -18.354 6.370   4.492   0.50 9.30  ? 56  SER A CA  1 
ATOM   576  C  CA  B SER A 1 56  ? -17.386 6.415   4.211   0.50 9.30  ? 56  SER A CA  1 
ATOM   577  C  C   A SER A 1 56  ? -17.900 7.003   3.184   0.50 10.90 ? 56  SER A C   1 
ATOM   578  C  C   B SER A 1 56  ? -16.812 7.123   2.973   0.50 8.87  ? 56  SER A C   1 
ATOM   579  O  O   A SER A 1 56  ? -18.709 7.476   2.407   0.50 10.79 ? 56  SER A O   1 
ATOM   580  O  O   B SER A 1 56  ? -17.555 7.623   2.122   0.50 10.24 ? 56  SER A O   1 
ATOM   581  C  CB  A SER A 1 56  ? -18.548 4.871   4.382   0.50 9.45  ? 56  SER A CB  1 
ATOM   582  C  CB  B SER A 1 56  ? -17.504 4.881   4.028   0.50 9.02  ? 56  SER A CB  1 
ATOM   583  O  OG  A SER A 1 56  ? -19.339 4.539   3.219   0.50 10.89 ? 56  SER A OG  1 
ATOM   584  O  OG  B SER A 1 56  ? -18.307 4.573   2.880   0.50 9.94  ? 56  SER A OG  1 
ATOM   585  N  N   A LEU A 1 57  ? -16.591 7.022   2.942   0.50 9.50  ? 57  LEU A N   1 
ATOM   586  N  N   B LEU A 1 57  ? -15.497 7.197   2.886   0.50 10.06 ? 57  LEU A N   1 
ATOM   587  C  CA  A LEU A 1 57  ? -16.100 7.719   1.756   0.50 9.95  ? 57  LEU A CA  1 
ATOM   588  C  CA  B LEU A 1 57  ? -14.837 7.832   1.720   0.50 9.10  ? 57  LEU A CA  1 
ATOM   589  C  C   A LEU A 1 57  ? -15.200 6.822   0.921   0.50 9.19  ? 57  LEU A C   1 
ATOM   590  C  C   B LEU A 1 57  ? -14.021 6.879   0.898   0.50 8.93  ? 57  LEU A C   1 
ATOM   591  O  O   A LEU A 1 57  ? -15.267 6.843   -0.301  0.50 8.47  ? 57  LEU A O   1 
ATOM   592  O  O   B LEU A 1 57  ? -14.192 6.792   -0.336  0.50 8.83  ? 57  LEU A O   1 
ATOM   593  C  CB  A LEU A 1 57  ? -15.264 8.891   2.196   0.50 11.68 ? 57  LEU A CB  1 
ATOM   594  C  CB  B LEU A 1 57  ? -13.985 8.986   2.217   0.50 10.59 ? 57  LEU A CB  1 
ATOM   595  C  CG  A LEU A 1 57  ? -16.091 10.021  2.764   0.50 12.01 ? 57  LEU A CG  1 
ATOM   596  C  CG  B LEU A 1 57  ? -14.805 10.131  2.821   0.50 13.99 ? 57  LEU A CG  1 
ATOM   597  C  CD1 A LEU A 1 57  ? -15.195 11.132  3.265   0.50 14.08 ? 57  LEU A CD1 1 
ATOM   598  C  CD1 B LEU A 1 57  ? -13.875 11.147  3.489   0.50 17.10 ? 57  LEU A CD1 1 
ATOM   599  C  CD2 A LEU A 1 57  ? -17.068 10.582  1.727   0.50 13.98 ? 57  LEU A CD2 1 
ATOM   600  C  CD2 B LEU A 1 57  ? -15.567 10.795  1.692   0.50 20.72 ? 57  LEU A CD2 1 
ATOM   601  N  N   A ARG A 1 58  ? -14.310 6.022   1.568   0.50 8.65  ? 58  ARG A N   1 
ATOM   602  N  N   B ARG A 1 58  ? -13.096 6.163   1.519   0.50 9.32  ? 58  ARG A N   1 
ATOM   603  C  CA  A ARG A 1 58  ? -13.228 5.370   0.844   0.50 8.63  ? 58  ARG A CA  1 
ATOM   604  C  CA  B ARG A 1 58  ? -12.112 5.411   0.733   0.50 9.68  ? 58  ARG A CA  1 
ATOM   605  C  C   A ARG A 1 58  ? -12.705 4.176   1.625   0.50 7.11  ? 58  ARG A C   1 
ATOM   606  C  C   B ARG A 1 58  ? -11.622 4.230   1.553   0.50 9.01  ? 58  ARG A C   1 
ATOM   607  O  O   A ARG A 1 58  ? -12.746 4.138   2.827   0.50 8.52  ? 58  ARG A O   1 
ATOM   608  O  O   B ARG A 1 58  ? -11.685 4.253   2.809   0.50 10.34 ? 58  ARG A O   1 
ATOM   609  C  CB  A ARG A 1 58  ? -12.049 6.355   0.651   0.50 9.03  ? 58  ARG A CB  1 
ATOM   610  C  CB  B ARG A 1 58  ? -10.908 6.294   0.433   0.50 11.22 ? 58  ARG A CB  1 
ATOM   611  C  CG  A ARG A 1 58  ? -10.981 5.912   -0.346  0.50 10.55 ? 58  ARG A CG  1 
ATOM   612  C  CG  B ARG A 1 58  ? -11.183 7.522   -0.424  0.50 13.86 ? 58  ARG A CG  1 
ATOM   613  C  CD  A ARG A 1 58  ? -9.910  6.978   -0.552  0.50 11.33 ? 58  ARG A CD  1 
ATOM   614  C  CD  B ARG A 1 58  ? -9.896  8.146   -1.012  0.50 13.53 ? 58  ARG A CD  1 
ATOM   615  N  NE  A ARG A 1 58  ? -9.059  7.053   0.636   0.50 10.85 ? 58  ARG A NE  1 
ATOM   616  N  NE  B ARG A 1 58  ? -9.087  7.223   -1.815  0.50 14.79 ? 58  ARG A NE  1 
ATOM   617  C  CZ  A ARG A 1 58  ? -7.747  7.188   0.658   0.50 13.67 ? 58  ARG A CZ  1 
ATOM   618  C  CZ  B ARG A 1 58  ? -9.301  6.999   -3.107  0.50 14.47 ? 58  ARG A CZ  1 
ATOM   619  N  NH1 A ARG A 1 58  ? -7.086  7.500   -0.441  0.50 11.60 ? 58  ARG A NH1 1 
ATOM   620  N  NH1 B ARG A 1 58  ? -10.290 7.683   -3.677  0.50 17.35 ? 58  ARG A NH1 1 
ATOM   621  N  NH2 A ARG A 1 58  ? -7.108  7.287   1.821   0.50 10.03 ? 58  ARG A NH2 1 
ATOM   622  N  NH2 B ARG A 1 58  ? -8.528  6.180   -3.814  0.50 14.84 ? 58  ARG A NH2 1 
ATOM   623  N  N   A ILE A 1 59  ? -12.206 3.167   0.911   0.50 7.45  ? 59  ILE A N   1 
ATOM   624  N  N   B ILE A 1 59  ? -11.108 3.200   0.870   0.50 8.16  ? 59  ILE A N   1 
ATOM   625  C  CA  A ILE A 1 59  ? -11.524 2.050   1.557   0.50 7.26  ? 59  ILE A CA  1 
ATOM   626  C  CA  B ILE A 1 59  ? -10.489 2.074   1.507   0.50 8.16  ? 59  ILE A CA  1 
ATOM   627  C  C   A ILE A 1 59  ? -10.117 2.046   1.036   0.50 6.48  ? 59  ILE A C   1 
ATOM   628  C  C   B ILE A 1 59  ? -9.075  1.994   0.980   0.50 9.25  ? 59  ILE A C   1 
ATOM   629  O  O   A ILE A 1 59  ? -9.866  2.229   -0.198  0.50 8.29  ? 59  ILE A O   1 
ATOM   630  O  O   B ILE A 1 59  ? -8.794  2.217   -0.219  0.50 8.87  ? 59  ILE A O   1 
ATOM   631  C  CB  A ILE A 1 59  ? -12.279 0.740   1.332   0.50 6.90  ? 59  ILE A CB  1 
ATOM   632  C  CB  B ILE A 1 59  ? -11.275 0.803   1.180   0.50 7.87  ? 59  ILE A CB  1 
ATOM   633  C  CG1 A ILE A 1 59  ? -11.740 -0.413  2.154   0.50 8.14  ? 59  ILE A CG1 1 
ATOM   634  C  CG1 B ILE A 1 59  ? -10.788 -0.438  2.000   0.50 8.46  ? 59  ILE A CG1 1 
ATOM   635  C  CG2 A ILE A 1 59  ? -12.281 0.345   -0.155  0.50 8.38  ? 59  ILE A CG2 1 
ATOM   636  C  CG2 B ILE A 1 59  ? -11.239 0.444   -0.338  0.50 8.63  ? 59  ILE A CG2 1 
ATOM   637  C  CD1 A ILE A 1 59  ? -12.653 -1.641  2.172   0.50 9.44  ? 59  ILE A CD1 1 
ATOM   638  C  CD1 B ILE A 1 59  ? -11.769 -1.589  1.958   0.50 10.34 ? 59  ILE A CD1 1 
ATOM   639  N  N   A LEU A 1 60  ? -9.172  1.783   1.914   0.50 8.06  ? 60  LEU A N   1 
ATOM   640  N  N   B LEU A 1 60  ? -8.149  1.675   1.854   0.50 8.95  ? 60  LEU A N   1 
ATOM   641  C  CA  A LEU A 1 60  ? -7.745  1.893   1.613   0.50 6.45  ? 60  LEU A CA  1 
ATOM   642  C  CA  B LEU A 1 60  ? -6.747  1.682   1.534   0.50 8.54  ? 60  LEU A CA  1 
ATOM   643  C  C   A LEU A 1 60  ? -6.982  0.714   2.174   0.50 7.04  ? 60  LEU A C   1 
ATOM   644  C  C   B LEU A 1 60  ? -6.056  0.463   2.130   0.50 7.69  ? 60  LEU A C   1 
ATOM   645  O  O   A LEU A 1 60  ? -7.143  0.380   3.358   0.50 7.04  ? 60  LEU A O   1 
ATOM   646  O  O   B LEU A 1 60  ? -6.270  0.153   3.286   0.50 8.92  ? 60  LEU A O   1 
ATOM   647  C  CB  A LEU A 1 60  ? -7.128  3.175   2.223   0.50 8.30  ? 60  LEU A CB  1 
ATOM   648  C  CB  B LEU A 1 60  ? -6.095  2.969   2.102   0.50 12.61 ? 60  LEU A CB  1 
ATOM   649  C  CG  A LEU A 1 60  ? -5.607  3.305   2.251   0.50 7.65  ? 60  LEU A CG  1 
ATOM   650  C  CG  B LEU A 1 60  ? -4.573  3.065   2.156   0.50 11.48 ? 60  LEU A CG  1 
ATOM   651  C  CD1 A LEU A 1 60  ? -5.025  3.559   0.847   0.50 9.50  ? 60  LEU A CD1 1 
ATOM   652  C  CD1 B LEU A 1 60  ? -3.932  3.213   0.780   0.50 12.49 ? 60  LEU A CD1 1 
ATOM   653  C  CD2 A LEU A 1 60  ? -5.216  4.454   3.153   0.50 9.82  ? 60  LEU A CD2 1 
ATOM   654  C  CD2 B LEU A 1 60  ? -4.315  4.291   3.015   0.50 13.34 ? 60  LEU A CD2 1 
ATOM   655  N  N   A ASN A 1 61  ? -6.127  0.104   1.344   0.50 6.69  ? 61  ASN A N   1 
ATOM   656  N  N   B ASN A 1 61  ? -5.165  -0.149  1.362   0.50 8.77  ? 61  ASN A N   1 
ATOM   657  C  CA  A ASN A 1 61  ? -5.158  -0.860  1.851   0.50 7.79  ? 61  ASN A CA  1 
ATOM   658  C  CA  B ASN A 1 61  ? -4.240  -1.136  1.887   0.50 7.11  ? 61  ASN A CA  1 
ATOM   659  C  C   A ASN A 1 61  ? -3.953  -0.022  2.263   0.50 7.92  ? 61  ASN A C   1 
ATOM   660  C  C   B ASN A 1 61  ? -2.988  -0.362  2.335   0.50 8.79  ? 61  ASN A C   1 
ATOM   661  O  O   A ASN A 1 61  ? -3.278  0.559   1.413   0.50 7.66  ? 61  ASN A O   1 
ATOM   662  O  O   B ASN A 1 61  ? -2.296  0.200   1.499   0.50 8.20  ? 61  ASN A O   1 
ATOM   663  C  CB  A ASN A 1 61  ? -4.790  -1.868  0.766   0.50 7.95  ? 61  ASN A CB  1 
ATOM   664  C  CB  B ASN A 1 61  ? -3.887  -2.166  0.838   0.50 8.52  ? 61  ASN A CB  1 
ATOM   665  C  CG  A ASN A 1 61  ? -3.684  -2.799  1.190   0.50 7.68  ? 61  ASN A CG  1 
ATOM   666  C  CG  B ASN A 1 61  ? -2.881  -3.208  1.310   0.50 7.32  ? 61  ASN A CG  1 
ATOM   667  O  OD1 A ASN A 1 61  ? -2.840  -2.490  2.060   0.50 8.62  ? 61  ASN A OD1 1 
ATOM   668  O  OD1 B ASN A 1 61  ? -2.075  -2.937  2.236   0.50 8.10  ? 61  ASN A OD1 1 
ATOM   669  N  ND2 A ASN A 1 61  ? -3.716  -3.999  0.602   0.50 9.18  ? 61  ASN A ND2 1 
ATOM   670  N  ND2 B ASN A 1 61  ? -2.927  -4.418  0.736   0.50 7.89  ? 61  ASN A ND2 1 
ATOM   671  N  N   A ASN A 1 62  ? -3.712  0.079   3.576   0.50 6.46  ? 62  ASN A N   1 
ATOM   672  N  N   B ASN A 1 62  ? -2.740  -0.280  3.642   0.50 7.65  ? 62  ASN A N   1 
ATOM   673  C  CA  A ASN A 1 62  ? -2.638  0.874   4.075   0.50 7.07  ? 62  ASN A CA  1 
ATOM   674  C  CA  B ASN A 1 62  ? -1.668  0.558   4.110   0.50 9.27  ? 62  ASN A CA  1 
ATOM   675  C  C   A ASN A 1 62  ? -1.339  0.186   4.271   0.50 7.49  ? 62  ASN A C   1 
ATOM   676  C  C   B ASN A 1 62  ? -0.393  -0.247  4.355   0.50 9.59  ? 62  ASN A C   1 
ATOM   677  O  O   A ASN A 1 62  ? -0.371  0.826   4.802   0.50 11.17 ? 62  ASN A O   1 
ATOM   678  O  O   B ASN A 1 62  ? 0.609   0.268   4.890   0.50 11.53 ? 62  ASN A O   1 
ATOM   679  C  CB  A ASN A 1 62  ? -3.051  1.596   5.364   0.50 9.14  ? 62  ASN A CB  1 
ATOM   680  C  CB  B ASN A 1 62  ? -2.062  1.349   5.385   0.50 12.45 ? 62  ASN A CB  1 
ATOM   681  C  CG  A ASN A 1 62  ? -3.388  0.623   6.472   0.50 9.21  ? 62  ASN A CG  1 
ATOM   682  C  CG  B ASN A 1 62  ? -2.550  0.428   6.501   0.50 12.89 ? 62  ASN A CG  1 
ATOM   683  O  OD1 A ASN A 1 62  ? -2.638  -0.294  6.702   0.50 9.55  ? 62  ASN A OD1 1 
ATOM   684  O  OD1 B ASN A 1 62  ? -1.967  -0.627  6.695   0.50 12.26 ? 62  ASN A OD1 1 
ATOM   685  N  ND2 A ASN A 1 62  ? -4.488  0.833   7.164   0.50 9.89  ? 62  ASN A ND2 1 
ATOM   686  N  ND2 B ASN A 1 62  ? -3.610  0.824   7.234   0.50 13.58 ? 62  ASN A ND2 1 
ATOM   687  N  N   A GLY A 1 63  ? -1.236  -1.075  3.851   0.50 6.90  ? 63  GLY A N   1 
ATOM   688  N  N   B GLY A 1 63  ? -0.429  -1.510  3.978   0.50 9.19  ? 63  GLY A N   1 
ATOM   689  C  CA  A GLY A 1 63  ? -0.023  -1.799  3.937   0.50 7.07  ? 63  GLY A CA  1 
ATOM   690  C  CA  B GLY A 1 63  ? 0.782   -2.309  4.099   0.50 8.79  ? 63  GLY A CA  1 
ATOM   691  C  C   A GLY A 1 63  ? 0.108   -2.602  5.216   0.50 8.60  ? 63  GLY A C   1 
ATOM   692  C  C   B GLY A 1 63  ? 0.828   -3.060  5.434   0.50 9.45  ? 63  GLY A C   1 
ATOM   693  O  O   A GLY A 1 63  ? 1.002   -3.431  5.332   0.50 10.42 ? 63  GLY A O   1 
ATOM   694  O  O   B GLY A 1 63  ? 1.682   -3.946  5.655   0.50 10.21 ? 63  GLY A O   1 
ATOM   695  N  N   A HIS A 1 64  ? -0.786  -2.338  6.173   0.50 8.50  ? 64  HIS A N   1 
ATOM   696  N  N   B HIS A 1 64  ? -0.117  -2.759  6.310   0.50 8.66  ? 64  HIS A N   1 
ATOM   697  C  CA  A HIS A 1 64  ? -0.767  -2.994  7.508   0.50 10.02 ? 64  HIS A CA  1 
ATOM   698  C  CA  B HIS A 1 64  ? -0.259  -3.408  7.631   0.50 10.69 ? 64  HIS A CA  1 
ATOM   699  C  C   A HIS A 1 64  ? -2.081  -3.686  7.756   0.50 9.12  ? 64  HIS A C   1 
ATOM   700  C  C   B HIS A 1 64  ? -1.627  -4.054  7.780   0.50 11.77 ? 64  HIS A C   1 
ATOM   701  O  O   A HIS A 1 64  ? -2.133  -4.881  8.156   0.50 13.13 ? 64  HIS A O   1 
ATOM   702  O  O   B HIS A 1 64  ? -1.714  -5.175  8.318   0.50 14.10 ? 64  HIS A O   1 
ATOM   703  C  CB  A HIS A 1 64  ? -0.542  -1.990  8.642   0.50 9.89  ? 64  HIS A CB  1 
ATOM   704  C  CB  B HIS A 1 64  ? -0.062  -2.396  8.747   0.50 11.22 ? 64  HIS A CB  1 
ATOM   705  C  CG  A HIS A 1 64  ? 0.671   -1.189  8.463   0.50 10.38 ? 64  HIS A CG  1 
ATOM   706  C  CG  B HIS A 1 64  ? 1.195   -1.667  8.619   0.50 9.89  ? 64  HIS A CG  1 
ATOM   707  N  ND1 A HIS A 1 64  ? 1.889   -1.707  8.549   0.50 11.52 ? 64  HIS A ND1 1 
ATOM   708  N  ND1 B HIS A 1 64  ? 2.376   -2.273  8.820   0.50 12.07 ? 64  HIS A ND1 1 
ATOM   709  C  CD2 A HIS A 1 64  ? 0.822   0.140   8.175   0.50 10.84 ? 64  HIS A CD2 1 
ATOM   710  C  CD2 B HIS A 1 64  ? 1.459   -0.359  8.304   0.50 10.97 ? 64  HIS A CD2 1 
ATOM   711  C  CE1 A HIS A 1 64  ? 2.815   -0.757  8.307   0.50 12.95 ? 64  HIS A CE1 1 
ATOM   712  C  CE1 B HIS A 1 64  ? 3.366   -1.364  8.661   0.50 11.88 ? 64  HIS A CE1 1 
ATOM   713  N  NE2 A HIS A 1 64  ? 2.155   0.370   8.028   0.50 14.46 ? 64  HIS A NE2 1 
ATOM   714  N  NE2 B HIS A 1 64  ? 2.804   -0.198  8.343   0.50 12.76 ? 64  HIS A NE2 1 
ATOM   715  N  N   A SER A 1 65  ? -3.133  -2.959  7.491   0.50 9.88  ? 65  SER A N   1 
ATOM   716  N  N   B SER A 1 65  ? -2.681  -3.405  7.223   0.50 11.09 ? 65  SER A N   1 
ATOM   717  C  CA  A SER A 1 65  ? -4.415  -3.506  7.485   0.50 9.21  ? 65  SER A CA  1 
ATOM   718  C  CA  B SER A 1 65  ? -4.109  -3.805  7.230   0.50 12.61 ? 65  SER A CA  1 
ATOM   719  C  C   A SER A 1 65  ? -5.015  -2.888  6.243   0.50 11.55 ? 65  SER A C   1 
ATOM   720  C  C   B SER A 1 65  ? -4.948  -2.986  6.150   0.50 10.12 ? 65  SER A C   1 
ATOM   721  O  O   A SER A 1 65  ? -4.299  -2.333  5.376   0.50 13.80 ? 65  SER A O   1 
ATOM   722  O  O   B SER A 1 65  ? -4.316  -2.291  5.320   0.50 13.16 ? 65  SER A O   1 
ATOM   723  C  CB  A SER A 1 65  ? -5.101  -3.131  8.784   0.50 8.04  ? 65  SER A CB  1 
ATOM   724  C  CB  B SER A 1 65  ? -4.638  -3.612  8.652   0.50 11.45 ? 65  SER A CB  1 
ATOM   725  O  OG  A SER A 1 65  ? -6.354  -3.762  8.810   0.50 9.33  ? 65  SER A OG  1 
ATOM   726  O  OG  B SER A 1 65  ? -4.961  -2.272  8.826   0.50 15.28 ? 65  SER A OG  1 
ATOM   727  N  N   . PHE A 1 66  ? -6.312  -3.036  6.123   1.00 10.94 ? 66  PHE A N   1 
ATOM   728  C  CA  . PHE A 1 66  ? -7.098  -2.122  5.323   1.00 11.93 ? 66  PHE A CA  1 
ATOM   729  C  C   . PHE A 1 66  ? -7.977  -1.290  6.202   1.00 11.18 ? 66  PHE A C   1 
ATOM   730  O  O   . PHE A 1 66  ? -8.399  -1.702  7.301   1.00 11.50 ? 66  PHE A O   1 
ATOM   731  C  CB  . PHE A 1 66  ? -7.913  -2.862  4.234   1.00 11.60 ? 66  PHE A CB  1 
ATOM   732  C  CG  . PHE A 1 66  ? -9.045  -3.697  4.755   1.00 11.52 ? 66  PHE A CG  1 
ATOM   733  C  CD1 . PHE A 1 66  ? -10.303 -3.132  4.933   1.00 12.60 ? 66  PHE A CD1 1 
ATOM   734  C  CD2 . PHE A 1 66  ? -8.869  -5.043  5.099   1.00 11.78 ? 66  PHE A CD2 1 
ATOM   735  C  CE1 . PHE A 1 66  ? -11.325 -3.889  5.426   1.00 13.40 ? 66  PHE A CE1 1 
ATOM   736  C  CE2 . PHE A 1 66  ? -9.910  -5.793  5.578   1.00 12.36 ? 66  PHE A CE2 1 
ATOM   737  C  CZ  . PHE A 1 66  ? -11.164 -5.238  5.728   1.00 11.26 ? 66  PHE A CZ  1 
ATOM   738  N  N   . GLN A 1 67  ? -8.264  -0.091  5.723   1.00 12.62 ? 67  GLN A N   1 
ATOM   739  C  CA  . GLN A 1 67  ? -9.055  0.795   6.521   1.00 12.12 ? 67  GLN A CA  1 
ATOM   740  C  C   . GLN A 1 67  ? -10.203 1.392   5.710   1.00 12.18 ? 67  GLN A C   1 
ATOM   741  O  O   . GLN A 1 67  ? -10.038 1.781   4.512   1.00 15.54 ? 67  GLN A O   1 
ATOM   742  C  CB  . GLN A 1 67  ? -8.230  1.923   7.138   1.00 15.49 ? 67  GLN A CB  1 
ATOM   743  C  CG  . GLN A 1 67  ? -7.574  2.719   6.059   1.00 17.86 ? 67  GLN A CG  1 
ATOM   744  C  CD  . GLN A 1 67  ? -6.657  3.679   6.690   1.00 18.38 ? 67  GLN A CD  1 
ATOM   745  O  OE1 . GLN A 1 67  ? -5.671  3.295   7.315   1.00 17.29 ? 67  GLN A OE1 1 
ATOM   746  N  NE2 . GLN A 1 67  ? -6.945  4.980   6.525   1.00 21.84 ? 67  GLN A NE2 1 
ATOM   747  N  N   A VAL A 1 68  ? -11.462 1.364   6.253   0.50 12.62 ? 68  VAL A N   1 
ATOM   748  N  N   B VAL A 1 68  ? -11.234 1.630   6.342   0.50 12.34 ? 68  VAL A N   1 
ATOM   749  C  CA  A VAL A 1 68  ? -12.750 2.121   5.802   0.50 8.56  ? 68  VAL A CA  1 
ATOM   750  C  CA  B VAL A 1 68  ? -11.997 2.395   5.570   0.50 7.38  ? 68  VAL A CA  1 
ATOM   751  C  C   A VAL A 1 68  ? -12.931 3.518   6.435   0.50 7.52  ? 68  VAL A C   1 
ATOM   752  C  C   B VAL A 1 68  ? -12.054 3.658   6.357   0.50 6.16  ? 68  VAL A C   1 
ATOM   753  O  O   A VAL A 1 68  ? -13.029 3.600   7.653   0.50 7.59  ? 68  VAL A O   1 
ATOM   754  O  O   B VAL A 1 68  ? -12.250 3.628   7.563   0.50 8.48  ? 68  VAL A O   1 
ATOM   755  C  CB  A VAL A 1 68  ? -14.140 1.364   5.914   0.50 7.86  ? 68  VAL A CB  1 
ATOM   756  C  CB  B VAL A 1 68  ? -13.313 1.668   5.573   0.50 8.36  ? 68  VAL A CB  1 
ATOM   757  C  CG1 A VAL A 1 68  ? -15.285 2.279   5.447   0.50 7.68  ? 68  VAL A CG1 1 
ATOM   758  C  CG1 B VAL A 1 68  ? -14.354 2.527   4.982   0.50 10.84 ? 68  VAL A CG1 1 
ATOM   759  C  CG2 A VAL A 1 68  ? -14.124 0.075   5.095   0.50 7.58  ? 68  VAL A CG2 1 
ATOM   760  C  CG2 B VAL A 1 68  ? -13.230 0.305   4.870   0.50 9.38  ? 68  VAL A CG2 1 
ATOM   761  N  N   A GLU A 1 69  ? -12.950 4.574   5.637   0.50 6.45  ? 69  GLU A N   1 
ATOM   762  N  N   B GLU A 1 69  ? -11.883 4.775   5.661   0.50 7.47  ? 69  GLU A N   1 
ATOM   763  C  CA  A GLU A 1 69  ? -12.824 5.950   6.098   0.50 6.88  ? 69  GLU A CA  1 
ATOM   764  C  CA  B GLU A 1 69  ? -11.867 6.058   6.292   0.50 8.45  ? 69  GLU A CA  1 
ATOM   765  C  C   A GLU A 1 69  ? -14.132 6.672   6.050   0.50 6.19  ? 69  GLU A C   1 
ATOM   766  C  C   B GLU A 1 69  ? -13.143 6.784   5.977   0.50 8.06  ? 69  GLU A C   1 
ATOM   767  O  O   A GLU A 1 69  ? -14.910 6.448   5.135   0.50 8.35  ? 69  GLU A O   1 
ATOM   768  O  O   B GLU A 1 69  ? -13.646 6.641   4.861   0.50 11.67 ? 69  GLU A O   1 
ATOM   769  C  CB  A GLU A 1 69  ? -11.828 6.718   5.263   0.50 8.80  ? 69  GLU A CB  1 
ATOM   770  C  CB  B GLU A 1 69  ? -10.684 6.863   5.847   0.50 12.23 ? 69  GLU A CB  1 
ATOM   771  C  CG  A GLU A 1 69  ? -10.450 6.182   5.333   0.50 8.89  ? 69  GLU A CG  1 
ATOM   772  C  CG  B GLU A 1 69  ? -9.490  6.022   5.626   0.50 18.14 ? 69  GLU A CG  1 
ATOM   773  C  CD  A GLU A 1 69  ? -9.562  6.653   4.222   0.50 10.29 ? 69  GLU A CD  1 
ATOM   774  C  CD  B GLU A 1 69  ? -8.638  6.651   4.541   0.50 20.12 ? 69  GLU A CD  1 
ATOM   775  O  OE1 A GLU A 1 69  ? -10.050 7.400   3.293   0.50 11.20 ? 69  GLU A OE1 1 
ATOM   776  O  OE1 B GLU A 1 69  ? -9.204  7.094   3.500   0.50 32.61 ? 69  GLU A OE1 1 
ATOM   777  O  OE2 A GLU A 1 69  ? -8.369  6.262   4.206   0.50 12.75 ? 69  GLU A OE2 1 
ATOM   778  O  OE2 B GLU A 1 69  ? -7.395  6.763   4.739   0.50 22.15 ? 69  GLU A OE2 1 
ATOM   779  N  N   A PHE A 1 70  ? -14.360 7.536   7.028   0.50 8.38  ? 70  PHE A N   1 
ATOM   780  N  N   B PHE A 1 70  ? -13.588 7.585   6.949   0.50 9.37  ? 70  PHE A N   1 
ATOM   781  C  CA  A PHE A 1 70  ? -15.549 8.333   7.166   0.50 10.52 ? 70  PHE A CA  1 
ATOM   782  C  CA  B PHE A 1 70  ? -14.908 8.307   6.915   0.50 10.45 ? 70  PHE A CA  1 
ATOM   783  C  C   A PHE A 1 70  ? -15.154 9.781   7.184   0.50 13.38 ? 70  PHE A C   1 
ATOM   784  C  C   B PHE A 1 70  ? -14.885 9.843   6.901   0.50 14.60 ? 70  PHE A C   1 
ATOM   785  O  O   A PHE A 1 70  ? -14.066 10.181  7.589   0.50 15.39 ? 70  PHE A O   1 
ATOM   786  O  O   B PHE A 1 70  ? -13.840 10.381  7.236   0.50 13.96 ? 70  PHE A O   1 
ATOM   787  C  CB  A PHE A 1 70  ? -16.267 7.979   8.437   0.50 9.52  ? 70  PHE A CB  1 
ATOM   788  C  CB  B PHE A 1 70  ? -15.702 7.957   8.177   0.50 11.59 ? 70  PHE A CB  1 
ATOM   789  C  CG  A PHE A 1 70  ? -16.790 6.571   8.387   0.50 10.52 ? 70  PHE A CG  1 
ATOM   790  C  CG  B PHE A 1 70  ? -16.239 6.551   8.173   0.50 9.74  ? 70  PHE A CG  1 
ATOM   791  C  CD1 A PHE A 1 70  ? -15.929 5.484   8.465   0.50 10.81 ? 70  PHE A CD1 1 
ATOM   792  C  CD1 B PHE A 1 70  ? -17.501 6.309   7.709   0.50 10.75 ? 70  PHE A CD1 1 
ATOM   793  C  CD2 A PHE A 1 70  ? -18.096 6.344   8.134   0.50 9.19  ? 70  PHE A CD2 1 
ATOM   794  C  CD2 B PHE A 1 70  ? -15.476 5.483   8.638   0.50 12.58 ? 70  PHE A CD2 1 
ATOM   795  C  CE1 A PHE A 1 70  ? -16.393 4.168   8.299   0.50 10.73 ? 70  PHE A CE1 1 
ATOM   796  C  CE1 B PHE A 1 70  ? -18.008 5.003   7.691   0.50 10.31 ? 70  PHE A CE1 1 
ATOM   797  C  CE2 A PHE A 1 70  ? -18.615 5.030   8.026   0.50 10.24 ? 70  PHE A CE2 1 
ATOM   798  C  CE2 B PHE A 1 70  ? -15.955 4.175   8.598   0.50 13.09 ? 70  PHE A CE2 1 
ATOM   799  C  CZ  A PHE A 1 70  ? -17.757 3.948   8.095   0.50 11.52 ? 70  PHE A CZ  1 
ATOM   800  C  CZ  B PHE A 1 70  ? -17.223 3.944   8.115   0.50 10.65 ? 70  PHE A CZ  1 
ATOM   801  N  N   . ASP A 1 71  ? -16.016 10.533  6.588   1.00 17.20 ? 71  ASP A N   1 
ATOM   802  C  CA  . ASP A 1 71  ? -16.000 12.015  6.771   1.00 16.20 ? 71  ASP A CA  1 
ATOM   803  C  C   . ASP A 1 71  ? -16.211 12.354  8.257   1.00 15.72 ? 71  ASP A C   1 
ATOM   804  O  O   . ASP A 1 71  ? -17.279 12.157  8.800   1.00 22.34 ? 71  ASP A O   1 
ATOM   805  C  CB  . ASP A 1 71  ? -17.076 12.591  5.896   1.00 21.74 ? 71  ASP A CB  1 
ATOM   806  C  CG  . ASP A 1 71  ? -17.296 14.071  6.122   1.00 20.39 ? 71  ASP A CG  1 
ATOM   807  O  OD1 . ASP A 1 71  ? -16.394 14.692  6.708   1.00 20.58 ? 71  ASP A OD1 1 
ATOM   808  O  OD2 . ASP A 1 71  ? -18.415 14.572  5.812   1.00 23.71 ? 71  ASP A OD2 1 
ATOM   809  N  N   . ASP A 1 72  ? -15.129 12.860  8.866   1.00 16.28 ? 72  ASP A N   1 
ATOM   810  C  CA  . ASP A 1 72  ? -15.166 13.224  10.281  1.00 16.55 ? 72  ASP A CA  1 
ATOM   811  C  C   . ASP A 1 72  ? -15.044 14.763  10.418  1.00 16.90 ? 72  ASP A C   1 
ATOM   812  O  O   . ASP A 1 72  ? -14.493 15.233  11.438  1.00 19.81 ? 72  ASP A O   1 
ATOM   813  C  CB  . ASP A 1 72  ? -14.014 12.606  11.075  1.00 17.17 ? 72  ASP A CB  1 
ATOM   814  C  CG  . ASP A 1 72  ? -12.625 13.010  10.552  1.00 18.06 ? 72  ASP A CG  1 
ATOM   815  O  OD1 . ASP A 1 72  ? -12.475 13.573  9.407   1.00 22.80 ? 72  ASP A OD1 1 
ATOM   816  O  OD2 . ASP A 1 72  ? -11.616 12.786  11.276  1.00 19.68 ? 72  ASP A OD2 1 
ATOM   817  N  N   . SER A 1 73  ? -15.471 15.487  9.405   1.00 18.09 ? 73  SER A N   1 
ATOM   818  C  CA  . SER A 1 73  ? -15.429 16.974  9.394   1.00 20.48 ? 73  SER A CA  1 
ATOM   819  C  C   . SER A 1 73  ? -16.701 17.573  10.065  1.00 22.38 ? 73  SER A C   1 
ATOM   820  O  O   . SER A 1 73  ? -16.829 18.788  10.135  1.00 21.71 ? 73  SER A O   1 
ATOM   821  C  CB  . SER A 1 73  ? -15.260 17.489  7.979   1.00 24.19 ? 73  SER A CB  1 
ATOM   822  O  OG  . SER A 1 73  ? -16.466 17.337  7.229   1.00 20.55 ? 73  SER A OG  1 
ATOM   823  N  N   . GLN A 1 74  ? -17.643 16.732  10.498  1.00 21.56 ? 74  GLN A N   1 
ATOM   824  C  CA  . GLN A 1 74  ? -18.820 17.098  11.363  1.00 21.62 ? 74  GLN A CA  1 
ATOM   825  C  C   . GLN A 1 74  ? -19.235 15.927  12.203  1.00 21.39 ? 74  GLN A C   1 
ATOM   826  O  O   . GLN A 1 74  ? -18.751 14.837  11.956  1.00 19.17 ? 74  GLN A O   1 
ATOM   827  C  CB  . GLN A 1 74  ? -20.047 17.343  10.506  1.00 29.39 ? 74  GLN A CB  1 
ATOM   828  C  CG  . GLN A 1 74  ? -19.907 18.289  9.355   1.00 33.34 ? 74  GLN A CG  1 
ATOM   829  C  CD  . GLN A 1 74  ? -21.276 18.472  8.725   1.00 34.12 ? 74  GLN A CD  1 
ATOM   830  O  OE1 . GLN A 1 74  ? -22.195 18.988  9.389   1.00 41.08 ? 74  GLN A OE1 1 
ATOM   831  N  NE2 . GLN A 1 74  ? -21.432 18.064  7.447   1.00 28.89 ? 74  GLN A NE2 1 
ATOM   832  N  N   . ASP A 1 75  ? -20.187 16.129  13.127  1.00 24.57 ? 75  ASP A N   1 
ATOM   833  C  CA  . ASP A 1 75  ? -20.692 15.093  14.042  1.00 24.50 ? 75  ASP A CA  1 
ATOM   834  C  C   . ASP A 1 75  ? -21.695 14.077  13.450  1.00 21.33 ? 75  ASP A C   1 
ATOM   835  O  O   . ASP A 1 75  ? -22.807 13.842  13.988  1.00 32.09 ? 75  ASP A O   1 
ATOM   836  C  CB  . ASP A 1 75  ? -21.286 15.731  15.295  1.00 23.79 ? 75  ASP A CB  1 
ATOM   837  C  CG  . ASP A 1 75  ? -20.245 16.324  16.255  1.00 23.10 ? 75  ASP A CG  1 
ATOM   838  O  OD1 . ASP A 1 75  ? -19.013 16.367  15.963  1.00 23.38 ? 75  ASP A OD1 1 
ATOM   839  O  OD2 . ASP A 1 75  ? -20.698 16.818  17.305  1.00 30.20 ? 75  ASP A OD2 1 
ATOM   840  N  N   A LYS A 1 76  ? -21.223 13.342  12.443  0.50 16.72 ? 76  LYS A N   1 
ATOM   841  N  N   B LYS A 1 76  ? -21.311 13.458  12.355  0.50 18.16 ? 76  LYS A N   1 
ATOM   842  C  CA  A LYS A 1 76  ? -22.054 12.446  11.623  0.50 18.06 ? 76  LYS A CA  1 
ATOM   843  C  CA  B LYS A 1 76  ? -22.174 12.434  11.815  0.50 18.55 ? 76  LYS A CA  1 
ATOM   844  C  C   A LYS A 1 76  ? -22.100 10.997  12.133  0.50 12.36 ? 76  LYS A C   1 
ATOM   845  C  C   B LYS A 1 76  ? -22.107 11.209  12.758  0.50 20.34 ? 76  LYS A C   1 
ATOM   846  O  O   A LYS A 1 76  ? -23.099 10.250  11.933  0.50 17.73 ? 76  LYS A O   1 
ATOM   847  O  O   B LYS A 1 76  ? -22.784 11.157  13.824  0.50 23.68 ? 76  LYS A O   1 
ATOM   848  C  CB  A LYS A 1 76  ? -21.476 12.430  10.227  0.50 19.54 ? 76  LYS A CB  1 
ATOM   849  C  CB  B LYS A 1 76  ? -21.719 12.093  10.398  0.50 23.69 ? 76  LYS A CB  1 
ATOM   850  C  CG  A LYS A 1 76  ? -21.619 13.744  9.526   0.50 22.34 ? 76  LYS A CG  1 
ATOM   851  C  CG  B LYS A 1 76  ? -21.919 13.223  9.410   0.50 19.75 ? 76  LYS A CG  1 
ATOM   852  C  CD  A LYS A 1 76  ? -20.962 13.676  8.150   0.50 28.72 ? 76  LYS A CD  1 
ATOM   853  C  CD  B LYS A 1 76  ? -21.119 13.016  8.113   0.50 23.92 ? 76  LYS A CD  1 
ATOM   854  C  CE  A LYS A 1 76  ? -21.736 14.521  7.158   0.50 23.92 ? 76  LYS A CE  1 
ATOM   855  C  CE  B LYS A 1 76  ? -21.771 13.819  7.008   0.50 25.97 ? 76  LYS A CE  1 
ATOM   856  N  NZ  A LYS A 1 76  ? -21.667 14.004  5.750   0.50 22.81 ? 76  LYS A NZ  1 
ATOM   857  N  NZ  B LYS A 1 76  ? -20.923 13.816  5.782   0.50 19.24 ? 76  LYS A NZ  1 
ATOM   858  N  N   A ALA A 1 77  ? -21.031 10.613  12.808  0.50 14.05 ? 77  ALA A N   1 
ATOM   859  N  N   B ALA A 1 77  ? -21.322 10.214  12.358  0.50 17.06 ? 77  ALA A N   1 
ATOM   860  C  CA  A ALA A 1 77  ? -20.886 9.236   13.183  0.50 15.04 ? 77  ALA A CA  1 
ATOM   861  C  CA  B ALA A 1 77  ? -21.145 9.048   13.188  0.50 14.72 ? 77  ALA A CA  1 
ATOM   862  C  C   A ALA A 1 77  ? -20.171 9.246   14.516  0.50 13.67 ? 77  ALA A C   1 
ATOM   863  C  C   B ALA A 1 77  ? -20.335 9.422   14.441  0.50 14.35 ? 77  ALA A C   1 
ATOM   864  O  O   A ALA A 1 77  ? -18.928 9.326   14.586  0.50 12.50 ? 77  ALA A O   1 
ATOM   865  O  O   B ALA A 1 77  ? -19.192 9.890   14.375  0.50 15.90 ? 77  ALA A O   1 
ATOM   866  C  CB  A ALA A 1 77  ? -20.074 8.536   12.117  0.50 13.62 ? 77  ALA A CB  1 
ATOM   867  C  CB  B ALA A 1 77  ? -20.474 7.949   12.392  0.50 15.77 ? 77  ALA A CB  1 
ATOM   868  N  N   . VAL A 1 78  ? -20.923 9.227   15.610  1.00 13.26 ? 78  VAL A N   1 
ATOM   869  C  CA  . VAL A 1 78  ? -20.255 9.541   16.905  1.00 15.19 ? 78  VAL A CA  1 
ATOM   870  C  C   . VAL A 1 78  ? -20.518 8.483   17.940  1.00 12.68 ? 78  VAL A C   1 
ATOM   871  O  O   . VAL A 1 78  ? -21.569 7.800   17.932  1.00 15.06 ? 78  VAL A O   1 
ATOM   872  C  CB  . VAL A 1 78  ? -20.583 10.913  17.463  1.00 17.80 ? 78  VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 78  ? -20.198 12.041  16.505  1.00 18.05 ? 78  VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 78  ? -22.032 10.975  17.842  1.00 20.85 ? 78  VAL A CG2 1 
ATOM   875  N  N   . LEU A 1 79  ? -19.547 8.315   18.796  1.00 10.55 ? 79  LEU A N   1 
ATOM   876  C  CA  . LEU A 1 79  ? -19.609 7.497   19.972  1.00 10.97 ? 79  LEU A CA  1 
ATOM   877  C  C   . LEU A 1 79  ? -19.610 8.359   21.229  1.00 11.35 ? 79  LEU A C   1 
ATOM   878  O  O   . LEU A 1 79  ? -18.806 9.299   21.351  1.00 13.36 ? 79  LEU A O   1 
ATOM   879  C  CB  . LEU A 1 79  ? -18.372 6.547   19.939  1.00 13.87 ? 79  LEU A CB  1 
ATOM   880  C  CG  . LEU A 1 79  ? -18.247 5.491   20.980  1.00 12.87 ? 79  LEU A CG  1 
ATOM   881  C  CD1 . LEU A 1 79  ? -19.297 4.402   20.764  1.00 16.87 ? 79  LEU A CD1 1 
ATOM   882  C  CD2 . LEU A 1 79  ? -16.876 4.854   20.887  1.00 12.75 ? 79  LEU A CD2 1 
ATOM   883  N  N   . LYS A 1 80  ? -20.530 8.045   22.132  1.00 13.46 ? 80  LYS A N   1 
ATOM   884  C  CA  . LYS A 1 80  ? -20.640 8.791   23.411  1.00 15.19 ? 80  LYS A CA  1 
ATOM   885  C  C   . LYS A 1 80  ? -21.068 7.840   24.503  1.00 13.47 ? 80  LYS A C   1 
ATOM   886  O  O   . LYS A 1 80  ? -21.311 6.668   24.242  1.00 14.19 ? 80  LYS A O   1 
ATOM   887  C  CB  . LYS A 1 80  ? -21.685 9.955   23.319  1.00 20.55 ? 80  LYS A CB  1 
ATOM   888  C  CG  . LYS A 1 80  ? -21.703 10.986  22.209  1.00 21.87 ? 80  LYS A CG  1 
ATOM   889  C  CD  . LYS A 1 80  ? -23.098 11.585  22.189  1.00 28.98 ? 80  LYS A CD  1 
ATOM   890  C  CE  . LYS A 1 80  ? -23.545 11.682  23.638  1.00 41.52 ? 80  LYS A CE  1 
ATOM   891  N  NZ  . LYS A 1 80  ? -24.998 11.350  23.795  1.00 52.34 ? 80  LYS A NZ  1 
ATOM   892  N  N   . GLY A 1 81  ? -21.128 8.334   25.731  1.00 15.19 ? 81  GLY A N   1 
ATOM   893  C  CA  . GLY A 1 81  ? -21.592 7.551   26.842  1.00 14.71 ? 81  GLY A CA  1 
ATOM   894  C  C   . GLY A 1 81  ? -20.600 6.443   27.163  1.00 13.90 ? 81  GLY A C   1 
ATOM   895  O  O   . GLY A 1 81  ? -19.404 6.599   26.943  1.00 12.91 ? 81  GLY A O   1 
ATOM   896  N  N   . GLY A 1 82  ? -21.100 5.373   27.743  1.00 17.89 ? 82  GLY A N   1 
ATOM   897  C  CA  . GLY A 1 82  ? -20.171 4.376   28.210  1.00 19.68 ? 82  GLY A CA  1 
ATOM   898  C  C   . GLY A 1 82  ? -19.254 5.022   29.238  1.00 17.29 ? 82  GLY A C   1 
ATOM   899  O  O   . GLY A 1 82  ? -19.684 5.799   30.130  1.00 24.65 ? 82  GLY A O   1 
ATOM   900  N  N   . PRO A 1 83  ? -17.950 4.735   29.118  1.00 15.68 ? 83  PRO A N   1 
ATOM   901  C  CA  . PRO A 1 83  ? -17.020 5.340   29.989  1.00 15.77 ? 83  PRO A CA  1 
ATOM   902  C  C   . PRO A 1 83  ? -16.641 6.787   29.575  1.00 14.31 ? 83  PRO A C   1 
ATOM   903  O  O   . PRO A 1 83  ? -15.797 7.396   30.206  1.00 17.37 ? 83  PRO A O   1 
ATOM   904  C  CB  . PRO A 1 83  ? -15.766 4.428   29.822  1.00 13.68 ? 83  PRO A CB  1 
ATOM   905  C  CG  . PRO A 1 83  ? -15.820 4.032   28.379  1.00 12.42 ? 83  PRO A CG  1 
ATOM   906  C  CD  . PRO A 1 83  ? -17.326 3.878   28.107  1.00 13.21 ? 83  PRO A CD  1 
ATOM   907  N  N   . LEU A 1 84  ? -17.126 7.241   28.433  1.00 12.21 ? 84  LEU A N   1 
ATOM   908  C  CA  . LEU A 1 84  ? -16.564 8.460   27.835  1.00 12.37 ? 84  LEU A CA  1 
ATOM   909  C  C   . LEU A 1 84  ? -17.229 9.724   28.367  1.00 12.83 ? 84  LEU A C   1 
ATOM   910  O  O   . LEU A 1 84  ? -18.427 9.706   28.651  1.00 15.27 ? 84  LEU A O   1 
ATOM   911  C  CB  . LEU A 1 84  ? -16.834 8.419   26.348  1.00 12.11 ? 84  LEU A CB  1 
ATOM   912  C  CG  . LEU A 1 84  ? -16.262 7.147   25.654  1.00 10.29 ? 84  LEU A CG  1 
ATOM   913  C  CD1 . LEU A 1 84  ? -16.686 7.107   24.227  1.00 11.79 ? 84  LEU A CD1 1 
ATOM   914  C  CD2 . LEU A 1 84  ? -14.706 7.117   25.725  1.00 10.35 ? 84  LEU A CD2 1 
ATOM   915  N  N   . ASP A 1 85  ? -16.463 10.792  28.340  1.00 15.04 ? 85  ASP A N   1 
ATOM   916  C  CA  . ASP A 1 85  ? -16.969 12.140  28.644  1.00 17.58 ? 85  ASP A CA  1 
ATOM   917  C  C   . ASP A 1 85  ? -16.882 12.802  27.236  1.00 19.29 ? 85  ASP A C   1 
ATOM   918  O  O   . ASP A 1 85  ? -15.864 12.716  26.564  1.00 23.91 ? 85  ASP A O   1 
ATOM   919  C  CB  . ASP A 1 85  ? -16.050 12.771  29.682  1.00 24.31 ? 85  ASP A CB  1 
ATOM   920  C  CG  . ASP A 1 85  ? -16.426 12.361  31.125  1.00 40.50 ? 85  ASP A CG  1 
ATOM   921  O  OD1 . ASP A 1 85  ? -17.593 11.928  31.393  1.00 43.79 ? 85  ASP A OD1 1 
ATOM   922  O  OD2 . ASP A 1 85  ? -15.543 12.486  32.019  1.00 34.65 ? 85  ASP A OD2 1 
ATOM   923  N  N   . GLY A 1 86  ? -17.961 13.455  26.785  1.00 20.18 ? 86  GLY A N   1 
ATOM   924  C  CA  . GLY A 1 86  ? -17.940 14.151  25.513  1.00 20.75 ? 86  GLY A CA  1 
ATOM   925  C  C   . GLY A 1 86  ? -18.166 13.245  24.280  1.00 18.17 ? 86  GLY A C   1 
ATOM   926  O  O   . GLY A 1 86  ? -18.700 12.086  24.369  1.00 20.77 ? 86  GLY A O   1 
ATOM   927  N  N   . THR A 1 87  ? -17.845 13.759  23.102  1.00 13.54 ? 87  THR A N   1 
ATOM   928  C  CA  . THR A 1 87  ? -18.278 13.218  21.853  1.00 14.23 ? 87  THR A CA  1 
ATOM   929  C  C   . THR A 1 87  ? -17.039 12.805  21.057  1.00 11.51 ? 87  THR A C   1 
ATOM   930  O  O   . THR A 1 87  ? -16.103 13.592  20.970  1.00 12.56 ? 87  THR A O   1 
ATOM   931  C  CB  . THR A 1 87  ? -19.023 14.323  21.059  1.00 18.13 ? 87  THR A CB  1 
ATOM   932  O  OG1 . THR A 1 87  ? -20.199 14.679  21.804  1.00 24.05 ? 87  THR A OG1 1 
ATOM   933  C  CG2 . THR A 1 87  ? -19.493 13.785  19.705  1.00 18.67 ? 87  THR A CG2 1 
ATOM   934  N  N   . TYR A 1 88  ? -17.094 11.606  20.481  1.00 10.39 ? 88  TYR A N   1 
ATOM   935  C  CA  . TYR A 1 88  ? -15.980 11.075  19.759  1.00 10.32 ? 88  TYR A CA  1 
ATOM   936  C  C   . TYR A 1 88  ? -16.407 10.779  18.319  1.00 10.29 ? 88  TYR A C   1 
ATOM   937  O  O   . TYR A 1 88  ? -17.361 10.009  18.115  1.00 12.94 ? 88  TYR A O   1 
ATOM   938  C  CB  . TYR A 1 88  ? -15.414 9.806   20.400  1.00 9.82  ? 88  TYR A CB  1 
ATOM   939  C  CG  . TYR A 1 88  ? -14.653 10.055  21.701  1.00 9.54  ? 88  TYR A CG  1 
ATOM   940  C  CD1 . TYR A 1 88  ? -15.295 10.478  22.856  1.00 9.46  ? 88  TYR A CD1 1 
ATOM   941  C  CD2 . TYR A 1 88  ? -13.268 9.807   21.752  1.00 8.90  ? 88  TYR A CD2 1 
ATOM   942  C  CE1 . TYR A 1 88  ? -14.599 10.633  24.017  1.00 9.74  ? 88  TYR A CE1 1 
ATOM   943  C  CE2 . TYR A 1 88  ? -12.583 9.965   22.916  1.00 8.66  ? 88  TYR A CE2 1 
ATOM   944  C  CZ  . TYR A 1 88  ? -13.188 10.342  24.043  1.00 8.71  ? 88  TYR A CZ  1 
ATOM   945  O  OH  . TYR A 1 88  ? -12.541 10.461  25.231  1.00 9.69  ? 88  TYR A OH  1 
ATOM   946  N  N   . ARG A 1 89  ? -15.781 11.349  17.310  1.00 9.83  ? 89  ARG A N   1 
ATOM   947  C  CA  . ARG A 1 89  ? -16.170 11.177  15.945  1.00 10.92 ? 89  ARG A CA  1 
ATOM   948  C  C   . ARG A 1 89  ? -15.470 9.973   15.328  1.00 8.50  ? 89  ARG A C   1 
ATOM   949  O  O   . ARG A 1 89  ? -14.276 9.778   15.483  1.00 8.68  ? 89  ARG A O   1 
ATOM   950  C  CB  . ARG A 1 89  ? -15.710 12.398  15.159  1.00 13.81 ? 89  ARG A CB  1 
ATOM   951  C  CG  . ARG A 1 89  ? -16.529 13.674  15.243  1.00 15.93 ? 89  ARG A CG  1 
ATOM   952  C  CD  . ARG A 1 89  ? -16.204 14.694  14.147  1.00 21.22 ? 89  ARG A CD  1 
ATOM   953  N  NE  . ARG A 1 89  ? -16.754 16.039  14.417  1.00 19.73 ? 89  ARG A NE  1 
ATOM   954  C  CZ  . ARG A 1 89  ? -16.235 17.212  14.039  1.00 20.47 ? 89  ARG A CZ  1 
ATOM   955  N  NH1 . ARG A 1 89  ? -15.212 17.242  13.169  1.00 20.68 ? 89  ARG A NH1 1 
ATOM   956  N  NH2 . ARG A 1 89  ? -16.804 18.354  14.460  1.00 23.11 ? 89  ARG A NH2 1 
ATOM   957  N  N   . LEU A 1 90  ? -16.257 9.208   14.548  1.00 9.74  ? 90  LEU A N   1 
ATOM   958  C  CA  . LEU A 1 90  ? -15.668 8.050   13.838  1.00 9.46  ? 90  LEU A CA  1 
ATOM   959  C  C   . LEU A 1 90  ? -14.760 8.510   12.700  1.00 9.86  ? 90  LEU A C   1 
ATOM   960  O  O   . LEU A 1 90  ? -15.238 9.255   11.797  1.00 12.15 ? 90  LEU A O   1 
ATOM   961  C  CB  . LEU A 1 90  ? -16.802 7.199   13.280  1.00 10.14 ? 90  LEU A CB  1 
ATOM   962  C  CG  . LEU A 1 90  ? -16.386 6.000   12.412  1.00 11.35 ? 90  LEU A CG  1 
ATOM   963  C  CD1 . LEU A 1 90  ? -15.624 4.966   13.260  1.00 11.79 ? 90  LEU A CD1 1 
ATOM   964  C  CD2 . LEU A 1 90  ? -17.619 5.302   11.794  1.00 14.13 ? 90  LEU A CD2 1 
ATOM   965  N  N   . LEU A 1 91  ? -13.533 8.060   12.724  1.00 9.10  ? 91  LEU A N   1 
ATOM   966  C  CA  . LEU A 1 91  ? -12.561 8.328   11.688  1.00 9.38  ? 91  LEU A CA  1 
ATOM   967  C  C   . LEU A 1 91  ? -12.443 7.206   10.695  1.00 8.46  ? 91  LEU A C   1 
ATOM   968  O  O   . LEU A 1 91  ? -12.463 7.431   9.482   1.00 9.33  ? 91  LEU A O   1 
ATOM   969  C  CB  . LEU A 1 91  ? -11.187 8.585   12.350  1.00 10.63 ? 91  LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 91  ? -10.023 8.730   11.392  1.00 11.63 ? 91  LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 91  ? -10.108 9.907   10.450  1.00 17.27 ? 91  LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 91  ? -8.716  8.781   12.195  1.00 17.44 ? 91  LEU A CD2 1 
ATOM   973  N  N   A GLN A 1 92  ? -12.092 5.984   11.162  0.50 8.18  ? 92  GLN A N   1 
ATOM   974  N  N   B GLN A 1 92  ? -12.498 5.964   11.185  0.50 8.09  ? 92  GLN A N   1 
ATOM   975  C  CA  A GLN A 1 92  ? -11.815 4.863   10.255  0.50 7.44  ? 92  GLN A CA  1 
ATOM   976  C  CA  B GLN A 1 92  ? -12.272 4.845   10.299  0.50 7.30  ? 92  GLN A CA  1 
ATOM   977  C  C   A GLN A 1 92  ? -12.069 3.554   10.999  0.50 6.43  ? 92  GLN A C   1 
ATOM   978  C  C   B GLN A 1 92  ? -12.525 3.579   11.099  0.50 6.85  ? 92  GLN A C   1 
ATOM   979  O  O   A GLN A 1 92  ? -12.111 3.532   12.228  0.50 6.94  ? 92  GLN A O   1 
ATOM   980  O  O   B GLN A 1 92  ? -12.581 3.633   12.314  0.50 6.90  ? 92  GLN A O   1 
ATOM   981  C  CB  A GLN A 1 92  ? -10.344 4.858   9.766   0.50 9.53  ? 92  GLN A CB  1 
ATOM   982  C  CB  B GLN A 1 92  ? -10.826 4.839   9.811   0.50 8.89  ? 92  GLN A CB  1 
ATOM   983  C  CG  A GLN A 1 92  ? -9.350  4.767   10.906  0.50 9.87  ? 92  GLN A CG  1 
ATOM   984  C  CG  B GLN A 1 92  ? -9.720  4.858   10.877  0.50 9.39  ? 92  GLN A CG  1 
ATOM   985  C  CD  A GLN A 1 92  ? -8.413  3.699   10.566  0.50 9.88  ? 92  GLN A CD  1 
ATOM   986  C  CD  B GLN A 1 92  ? -8.882  3.585   10.904  0.50 8.78  ? 92  GLN A CD  1 
ATOM   987  O  OE1 A GLN A 1 92  ? -8.650  2.536   10.955  0.50 16.41 ? 92  GLN A OE1 1 
ATOM   988  O  OE1 B GLN A 1 92  ? -9.423  2.553   11.203  0.50 9.09  ? 92  GLN A OE1 1 
ATOM   989  N  NE2 A GLN A 1 92  ? -7.328  4.051   9.944   0.50 10.54 ? 92  GLN A NE2 1 
ATOM   990  N  NE2 B GLN A 1 92  ? -7.569  3.660   10.673  0.50 11.70 ? 92  GLN A NE2 1 
ATOM   991  N  N   A PHE A 1 93  ? -12.211 2.497   10.243  0.50 7.47  ? 93  PHE A N   1 
ATOM   992  N  N   B PHE A 1 93  ? -12.681 2.473   10.404  0.50 7.29  ? 93  PHE A N   1 
ATOM   993  C  CA  A PHE A 1 93  ? -12.118 1.179   10.820  0.50 7.04  ? 93  PHE A CA  1 
ATOM   994  C  CA  B PHE A 1 93  ? -12.512 1.144   11.003  0.50 6.97  ? 93  PHE A CA  1 
ATOM   995  C  C   A PHE A 1 93  ? -11.145 0.376   10.087  0.50 7.65  ? 93  PHE A C   1 
ATOM   996  C  C   B PHE A 1 93  ? -11.491 0.321   10.173  0.50 6.98  ? 93  PHE A C   1 
ATOM   997  O  O   A PHE A 1 93  ? -10.814 0.548   8.912   0.50 8.06  ? 93  PHE A O   1 
ATOM   998  O  O   B PHE A 1 93  ? -11.355 0.573   8.961   0.50 8.04  ? 93  PHE A O   1 
ATOM   999  C  CB  A PHE A 1 93  ? -13.449 0.421   10.986  0.50 6.41  ? 93  PHE A CB  1 
ATOM   1000 C  CB  B PHE A 1 93  ? -13.896 0.503   11.234  0.50 7.35  ? 93  PHE A CB  1 
ATOM   1001 C  CG  A PHE A 1 93  ? -14.109 0.004   9.708   0.50 7.15  ? 93  PHE A CG  1 
ATOM   1002 C  CG  B PHE A 1 93  ? -14.643 0.064   9.992   0.50 7.17  ? 93  PHE A CG  1 
ATOM   1003 C  CD1 A PHE A 1 93  ? -13.709 -1.127  8.991   0.50 7.22  ? 93  PHE A CD1 1 
ATOM   1004 C  CD1 B PHE A 1 93  ? -14.242 -1.070  9.260   0.50 7.28  ? 93  PHE A CD1 1 
ATOM   1005 C  CD2 A PHE A 1 93  ? -15.220 0.701   9.268   0.50 7.26  ? 93  PHE A CD2 1 
ATOM   1006 C  CD2 B PHE A 1 93  ? -15.829 0.738   9.606   0.50 7.61  ? 93  PHE A CD2 1 
ATOM   1007 C  CE1 A PHE A 1 93  ? -14.331 -1.476  7.812   0.50 7.36  ? 93  PHE A CE1 1 
ATOM   1008 C  CE1 B PHE A 1 93  ? -15.006 -1.495  8.172   0.50 7.04  ? 93  PHE A CE1 1 
ATOM   1009 C  CE2 A PHE A 1 93  ? -15.858 0.309   8.118   0.50 6.64  ? 93  PHE A CE2 1 
ATOM   1010 C  CE2 B PHE A 1 93  ? -16.567 0.295   8.500   0.50 7.58  ? 93  PHE A CE2 1 
ATOM   1011 C  CZ  A PHE A 1 93  ? -15.424 -0.774  7.408   0.50 7.52  ? 93  PHE A CZ  1 
ATOM   1012 C  CZ  B PHE A 1 93  ? -16.146 -0.819  7.795   0.50 6.80  ? 93  PHE A CZ  1 
ATOM   1013 N  N   . HIS A 1 94  ? -10.770 -0.636  10.822  1.00 7.58  ? 94  HIS A N   1 
ATOM   1014 C  CA  . HIS A 1 94  ? -9.859  -1.598  10.266  1.00 7.56  ? 94  HIS A CA  1 
ATOM   1015 C  C   . HIS A 1 94  ? -9.972  -2.875  11.050  1.00 6.85  ? 94  HIS A C   1 
ATOM   1016 O  O   . HIS A 1 94  ? -10.666 -2.946  12.047  1.00 7.25  ? 94  HIS A O   1 
ATOM   1017 C  CB  . HIS A 1 94  ? -8.387  -1.080  10.302  1.00 8.39  ? 94  HIS A CB  1 
ATOM   1018 C  CG  . HIS A 1 94  ? -7.955  -0.818  11.713  1.00 7.36  ? 94  HIS A CG  1 
ATOM   1019 N  ND1 . HIS A 1 94  ? -8.152  0.366   12.354  1.00 7.12  ? 94  HIS A ND1 1 
ATOM   1020 C  CD2 . HIS A 1 94  ? -7.334  -1.679  12.615  1.00 7.11  ? 94  HIS A CD2 1 
ATOM   1021 C  CE1 . HIS A 1 94  ? -7.759  0.213   13.622  1.00 6.96  ? 94  HIS A CE1 1 
ATOM   1022 N  NE2 . HIS A 1 94  ? -7.252  -1.036  13.816  1.00 6.39  ? 94  HIS A NE2 1 
ATOM   1023 N  N   . PHE A 1 95  ? -9.235  -3.899  10.604  1.00 7.06  ? 95  PHE A N   1 
ATOM   1024 C  CA  . PHE A 1 95  ? -9.271  -5.204  11.260  1.00 7.22  ? 95  PHE A CA  1 
ATOM   1025 C  C   . PHE A 1 95  ? -7.880  -5.699  11.504  1.00 6.69  ? 95  PHE A C   1 
ATOM   1026 O  O   . PHE A 1 95  ? -6.902  -5.287  10.845  1.00 7.87  ? 95  PHE A O   1 
ATOM   1027 C  CB  . PHE A 1 95  ? -9.990  -6.258  10.360  1.00 8.17  ? 95  PHE A CB  1 
ATOM   1028 C  CG  . PHE A 1 95  ? -11.413 -5.955  10.048  1.00 7.47  ? 95  PHE A CG  1 
ATOM   1029 C  CD1 . PHE A 1 95  ? -11.803 -5.039  9.016   1.00 8.90  ? 95  PHE A CD1 1 
ATOM   1030 C  CD2 . PHE A 1 95  ? -12.468 -6.633  10.716  1.00 8.69  ? 95  PHE A CD2 1 
ATOM   1031 C  CE1 . PHE A 1 95  ? -13.133 -4.834  8.693   1.00 9.81  ? 95  PHE A CE1 1 
ATOM   1032 C  CE2 . PHE A 1 95  ? -13.756 -6.425  10.388  1.00 9.35  ? 95  PHE A CE2 1 
ATOM   1033 C  CZ  . PHE A 1 95  ? -14.120 -5.509  9.368   1.00 9.59  ? 95  PHE A CZ  1 
ATOM   1034 N  N   . HIS A 1 96  ? -7.786  -6.676  12.410  1.00 6.70  ? 96  HIS A N   1 
ATOM   1035 C  CA  . HIS A 1 96  ? -6.621  -7.505  12.607  1.00 6.50  ? 96  HIS A CA  1 
ATOM   1036 C  C   . HIS A 1 96  ? -7.071  -8.932  12.475  1.00 6.56  ? 96  HIS A C   1 
ATOM   1037 O  O   . HIS A 1 96  ? -8.139  -9.275  12.947  1.00 6.68  ? 96  HIS A O   1 
ATOM   1038 C  CB  . HIS A 1 96  ? -6.020  -7.299  14.018  1.00 7.74  ? 96  HIS A CB  1 
ATOM   1039 C  CG  . HIS A 1 96  ? -5.746  -5.829  14.269  1.00 6.48  ? 96  HIS A CG  1 
ATOM   1040 N  ND1 . HIS A 1 96  ? -4.517  -5.256  14.062  1.00 6.89  ? 96  HIS A ND1 1 
ATOM   1041 C  CD2 . HIS A 1 96  ? -6.547  -4.816  14.724  1.00 7.28  ? 96  HIS A CD2 1 
ATOM   1042 C  CE1 . HIS A 1 96  ? -4.552  -3.984  14.368  1.00 6.99  ? 96  HIS A CE1 1 
ATOM   1043 N  NE2 . HIS A 1 96  ? -5.804  -3.669  14.780  1.00 6.83  ? 96  HIS A NE2 1 
ATOM   1044 N  N   . TRP A 1 97  ? -6.289  -9.791  11.824  1.00 6.93  ? 97  TRP A N   1 
ATOM   1045 C  CA  . TRP A 1 97  ? -6.675  -11.169 11.647  1.00 6.99  ? 97  TRP A CA  1 
ATOM   1046 C  C   . TRP A 1 97  ? -5.495  -12.078 11.528  1.00 7.12  ? 97  TRP A C   1 
ATOM   1047 O  O   . TRP A 1 97  ? -4.316  -11.636 11.454  1.00 7.79  ? 97  TRP A O   1 
ATOM   1048 C  CB  . TRP A 1 97  ? -7.588  -11.294 10.422  1.00 7.47  ? 97  TRP A CB  1 
ATOM   1049 C  CG  . TRP A 1 97  ? -6.937  -10.943 9.129   1.00 7.69  ? 97  TRP A CG  1 
ATOM   1050 C  CD1 . TRP A 1 97  ? -6.220  -11.787 8.299   1.00 8.46  ? 97  TRP A CD1 1 
ATOM   1051 C  CD2 . TRP A 1 97  ? -6.867  -9.631  8.511   1.00 7.78  ? 97  TRP A CD2 1 
ATOM   1052 N  NE1 . TRP A 1 97  ? -5.796  -11.085 7.191   1.00 9.45  ? 97  TRP A NE1 1 
ATOM   1053 C  CE2 . TRP A 1 97  ? -6.170  -9.764  7.313   1.00 8.63  ? 97  TRP A CE2 1 
ATOM   1054 C  CE3 . TRP A 1 97  ? -7.363  -8.376  8.855   1.00 7.76  ? 97  TRP A CE3 1 
ATOM   1055 C  CZ2 . TRP A 1 97  ? -5.953  -8.704  6.452   1.00 8.61  ? 97  TRP A CZ2 1 
ATOM   1056 C  CZ3 . TRP A 1 97  ? -7.121  -7.287  8.014   1.00 8.89  ? 97  TRP A CZ3 1 
ATOM   1057 C  CH2 . TRP A 1 97  ? -6.420  -7.470  6.841   1.00 9.27  ? 97  TRP A CH2 1 
ATOM   1058 N  N   . GLY A 1 98  ? -5.786  -13.386 11.546  1.00 7.45  ? 98  GLY A N   1 
ATOM   1059 C  CA  . GLY A 1 98  ? -4.728  -14.393 11.595  1.00 7.75  ? 98  GLY A CA  1 
ATOM   1060 C  C   . GLY A 1 98  ? -4.537  -15.126 10.288  1.00 7.71  ? 98  GLY A C   1 
ATOM   1061 O  O   . GLY A 1 98  ? -5.285  -14.979 9.332   1.00 8.48  ? 98  GLY A O   1 
ATOM   1062 N  N   . SER A 1 99  ? -3.532  -15.994 10.300  1.00 8.87  ? 99  SER A N   1 
ATOM   1063 C  CA  . SER A 1 99  ? -3.305  -16.934 9.224   1.00 9.95  ? 99  SER A CA  1 
ATOM   1064 C  C   . SER A 1 99  ? -4.236  -18.163 9.365   1.00 9.34  ? 99  SER A C   1 
ATOM   1065 O  O   . SER A 1 99  ? -4.442  -18.848 8.369   1.00 11.70 ? 99  SER A O   1 
ATOM   1066 C  CB  . SER A 1 99  ? -1.834  -17.393 9.226   1.00 11.15 ? 99  SER A CB  1 
ATOM   1067 O  OG  . SER A 1 99  ? -1.405  -17.751 10.486  1.00 11.31 ? 99  SER A OG  1 
ATOM   1068 N  N   A LEU A 1 100 ? -4.703  -18.390 10.583  0.50 9.14  ? 100 LEU A N   1 
ATOM   1069 N  N   B LEU A 1 100 ? -4.686  -18.458 10.556  0.50 9.17  ? 100 LEU A N   1 
ATOM   1070 C  CA  A LEU A 1 100 ? -5.475  -19.587 11.040  0.50 9.62  ? 100 LEU A CA  1 
ATOM   1071 C  CA  B LEU A 1 100 ? -5.684  -19.525 10.767  0.50 10.52 ? 100 LEU A CA  1 
ATOM   1072 C  C   A LEU A 1 100 ? -6.596  -19.025 11.885  0.50 9.42  ? 100 LEU A C   1 
ATOM   1073 C  C   B LEU A 1 100 ? -6.635  -19.003 11.793  0.50 9.17  ? 100 LEU A C   1 
ATOM   1074 O  O   A LEU A 1 100 ? -6.444  -17.960 12.507  0.50 9.79  ? 100 LEU A O   1 
ATOM   1075 O  O   B LEU A 1 100 ? -6.391  -17.983 12.469  0.50 10.07 ? 100 LEU A O   1 
ATOM   1076 C  CB  A LEU A 1 100 ? -4.635  -20.545 11.905  0.50 11.26 ? 100 LEU A CB  1 
ATOM   1077 C  CB  B LEU A 1 100 ? -5.083  -20.832 11.257  0.50 8.83  ? 100 LEU A CB  1 
ATOM   1078 C  CG  A LEU A 1 100 ? -3.377  -20.945 11.167  0.50 13.23 ? 100 LEU A CG  1 
ATOM   1079 C  CG  B LEU A 1 100 ? -4.235  -21.540 10.223  0.50 11.79 ? 100 LEU A CG  1 
ATOM   1080 C  CD1 A LEU A 1 100 ? -2.398  -21.626 12.101  0.50 17.73 ? 100 LEU A CD1 1 
ATOM   1081 C  CD1 B LEU A 1 100 ? -3.433  -22.643 10.884  0.50 16.59 ? 100 LEU A CD1 1 
ATOM   1082 C  CD2 A LEU A 1 100 ? -3.806  -21.821 9.996   0.50 16.14 ? 100 LEU A CD2 1 
ATOM   1083 C  CD2 B LEU A 1 100 ? -5.042  -22.086 9.069   0.50 13.16 ? 100 LEU A CD2 1 
ATOM   1084 N  N   . ASP A 1 101 ? -7.726  -19.733 11.985  1.00 9.40  ? 101 ASP A N   1 
ATOM   1085 C  CA  . ASP A 1 101 ? -8.856  -19.204 12.715  1.00 9.72  ? 101 ASP A CA  1 
ATOM   1086 C  C   . ASP A 1 101 ? -8.607  -19.080 14.242  1.00 9.43  ? 101 ASP A C   1 
ATOM   1087 O  O   . ASP A 1 101 ? -9.304  -18.321 14.923  1.00 11.87 ? 101 ASP A O   1 
ATOM   1088 C  CB  . ASP A 1 101 ? -10.104 -20.031 12.540  1.00 11.32 ? 101 ASP A CB  1 
ATOM   1089 C  CG  . ASP A 1 101 ? -10.651 -20.040 11.180  1.00 13.71 ? 101 ASP A CG  1 
ATOM   1090 O  OD1 . ASP A 1 101 ? -10.214 -19.305 10.302  1.00 12.64 ? 101 ASP A OD1 1 
ATOM   1091 O  OD2 . ASP A 1 101 ? -11.586 -20.855 10.970  1.00 18.28 ? 101 ASP A OD2 1 
ATOM   1092 N  N   . GLY A 1 102 ? -7.599  -19.762 14.772  1.00 9.19  ? 102 GLY A N   1 
ATOM   1093 C  CA  . GLY A 1 102 ? -7.250  -19.734 16.171  1.00 10.84 ? 102 GLY A CA  1 
ATOM   1094 C  C   . GLY A 1 102 ? -6.388  -18.578 16.626  1.00 9.59  ? 102 GLY A C   1 
ATOM   1095 O  O   . GLY A 1 102 ? -5.999  -18.568 17.809  1.00 9.95  ? 102 GLY A O   1 
ATOM   1096 N  N   A GLN A 1 103 ? -6.211  -17.598 15.752  0.50 9.01  ? 103 GLN A N   1 
ATOM   1097 N  N   B GLN A 1 103 ? -6.053  -17.628 15.762  0.50 8.47  ? 103 GLN A N   1 
ATOM   1098 C  CA  A GLN A 1 103 ? -5.469  -16.428 16.100  0.50 8.24  ? 103 GLN A CA  1 
ATOM   1099 C  CA  B GLN A 1 103 ? -5.373  -16.428 16.221  0.50 8.47  ? 103 GLN A CA  1 
ATOM   1100 C  C   A GLN A 1 103 ? -5.930  -15.298 15.241  0.50 6.62  ? 103 GLN A C   1 
ATOM   1101 C  C   B GLN A 1 103 ? -5.751  -15.335 15.253  0.50 6.87  ? 103 GLN A C   1 
ATOM   1102 O  O   A GLN A 1 103 ? -6.558  -15.508 14.176  0.50 6.93  ? 103 GLN A O   1 
ATOM   1103 O  O   B GLN A 1 103 ? -6.155  -15.607 14.138  0.50 7.70  ? 103 GLN A O   1 
ATOM   1104 C  CB  A GLN A 1 103 ? -3.972  -16.680 15.946  0.50 9.15  ? 103 GLN A CB  1 
ATOM   1105 C  CB  B GLN A 1 103 ? -3.847  -16.635 16.330  0.50 9.75  ? 103 GLN A CB  1 
ATOM   1106 C  CG  A GLN A 1 103 ? -3.527  -16.957 14.513  0.50 9.89  ? 103 GLN A CG  1 
ATOM   1107 C  CG  B GLN A 1 103 ? -3.157  -16.957 14.984  0.50 8.23  ? 103 GLN A CG  1 
ATOM   1108 C  CD  A GLN A 1 103 ? -2.224  -17.690 14.491  0.50 10.19 ? 103 GLN A CD  1 
ATOM   1109 C  CD  B GLN A 1 103 ? -1.684  -17.264 15.168  0.50 9.39  ? 103 GLN A CD  1 
ATOM   1110 O  OE1 A GLN A 1 103 ? -2.067  -18.740 15.141  0.50 14.36 ? 103 GLN A OE1 1 
ATOM   1111 O  OE1 B GLN A 1 103 ? -1.288  -17.815 16.191  0.50 11.44 ? 103 GLN A OE1 1 
ATOM   1112 N  NE2 A GLN A 1 103 ? -1.262  -17.119 13.833  0.50 13.01 ? 103 GLN A NE2 1 
ATOM   1113 N  NE2 B GLN A 1 103 ? -0.886  -16.936 14.195  0.50 12.99 ? 103 GLN A NE2 1 
ATOM   1114 N  N   . GLY A 1 104 ? -5.561  -14.083 15.671  1.00 6.88  ? 104 GLY A N   1 
ATOM   1115 C  CA  . GLY A 1 104 ? -5.918  -12.914 14.849  1.00 7.14  ? 104 GLY A CA  1 
ATOM   1116 C  C   . GLY A 1 104 ? -6.352  -11.754 15.681  1.00 6.32  ? 104 GLY A C   1 
ATOM   1117 O  O   . GLY A 1 104 ? -6.098  -10.604 15.327  1.00 7.03  ? 104 GLY A O   1 
ATOM   1118 N  N   . SER A 1 105 ? -7.040  -12.002 16.825  1.00 5.91  ? 105 SER A N   1 
ATOM   1119 C  CA  . SER A 1 105 ? -7.440  -10.884 17.635  1.00 5.71  ? 105 SER A CA  1 
ATOM   1120 C  C   . SER A 1 105 ? -6.246  -10.343 18.398  1.00 5.38  ? 105 SER A C   1 
ATOM   1121 O  O   . SER A 1 105 ? -5.216  -11.012 18.621  1.00 6.65  ? 105 SER A O   1 
ATOM   1122 C  CB  . SER A 1 105 ? -8.613  -11.261 18.552  1.00 6.76  ? 105 SER A CB  1 
ATOM   1123 O  OG  . SER A 1 105 ? -8.223  -12.211 19.544  1.00 6.70  ? 105 SER A OG  1 
ATOM   1124 N  N   . GLU A 1 106 ? -6.407  -9.094  18.820  1.00 5.33  ? 106 GLU A N   1 
ATOM   1125 C  CA  . GLU A 1 106 ? -5.415  -8.391  19.641  1.00 6.00  ? 106 GLU A CA  1 
ATOM   1126 C  C   . GLU A 1 106 ? -5.759  -8.544  21.098  1.00 5.62  ? 106 GLU A C   1 
ATOM   1127 O  O   . GLU A 1 106 ? -4.967  -9.109  21.867  1.00 6.40  ? 106 GLU A O   1 
ATOM   1128 C  CB  . GLU A 1 106 ? -5.359  -6.923  19.167  1.00 6.06  ? 106 GLU A CB  1 
ATOM   1129 C  CG  . GLU A 1 106 ? -4.819  -6.833  17.748  1.00 7.56  ? 106 GLU A CG  1 
ATOM   1130 C  CD  . GLU A 1 106 ? -4.202  -5.532  17.445  1.00 6.12  ? 106 GLU A CD  1 
ATOM   1131 O  OE1 . GLU A 1 106 ? -4.813  -4.469  17.716  1.00 6.51  ? 106 GLU A OE1 1 
ATOM   1132 O  OE2 . GLU A 1 106 ? -3.057  -5.550  16.941  1.00 7.40  ? 106 GLU A OE2 1 
ATOM   1133 N  N   . HIS A 1 107 ? -6.963  -8.105  21.495  1.00 5.88  ? 107 HIS A N   1 
ATOM   1134 C  CA  . HIS A 1 107 ? -7.400  -8.477  22.809  1.00 5.33  ? 107 HIS A CA  1 
ATOM   1135 C  C   . HIS A 1 107 ? -7.679  -9.975  22.851  1.00 6.18  ? 107 HIS A C   1 
ATOM   1136 O  O   . HIS A 1 107 ? -8.061  -10.587 21.837  1.00 6.16  ? 107 HIS A O   1 
ATOM   1137 C  CB  . HIS A 1 107 ? -8.679  -7.676  23.172  1.00 6.21  ? 107 HIS A CB  1 
ATOM   1138 C  CG  . HIS A 1 107 ? -8.353  -6.240  23.308  1.00 5.38  ? 107 HIS A CG  1 
ATOM   1139 N  ND1 . HIS A 1 107 ? -8.412  -5.356  22.258  1.00 5.77  ? 107 HIS A ND1 1 
ATOM   1140 C  CD2 . HIS A 1 107 ? -7.869  -5.500  24.363  1.00 5.93  ? 107 HIS A CD2 1 
ATOM   1141 C  CE1 . HIS A 1 107 ? -7.971  -4.154  22.702  1.00 6.08  ? 107 HIS A CE1 1 
ATOM   1142 N  NE2 . HIS A 1 107 ? -7.623  -4.220  23.974  1.00 5.48  ? 107 HIS A NE2 1 
ATOM   1143 N  N   . THR A 1 108 ? -7.576  -10.544 24.043  1.00 6.09  ? 108 THR A N   1 
ATOM   1144 C  CA  . THR A 1 108 ? -7.932  -11.926 24.304  1.00 6.25  ? 108 THR A CA  1 
ATOM   1145 C  C   . THR A 1 108 ? -8.879  -11.927 25.497  1.00 6.42  ? 108 THR A C   1 
ATOM   1146 O  O   . THR A 1 108 ? -8.905  -10.947 26.250  1.00 6.87  ? 108 THR A O   1 
ATOM   1147 C  CB  . THR A 1 108 ? -6.706  -12.826 24.504  1.00 7.45  ? 108 THR A CB  1 
ATOM   1148 O  OG1 . THR A 1 108 ? -5.897  -12.319 25.553  1.00 7.75  ? 108 THR A OG1 1 
ATOM   1149 C  CG2 . THR A 1 108 ? -5.909  -12.857 23.228  1.00 8.96  ? 108 THR A CG2 1 
ATOM   1150 N  N   . VAL A 1 109 ? -9.672  -13.011 25.620  1.00 7.50  ? 109 VAL A N   1 
ATOM   1151 C  CA  . VAL A 1 109 ? -10.634 -13.066 26.705  1.00 8.13  ? 109 VAL A CA  1 
ATOM   1152 C  C   . VAL A 1 109 ? -10.309 -14.354 27.437  1.00 8.08  ? 109 VAL A C   1 
ATOM   1153 O  O   . VAL A 1 109 ? -10.466 -15.485 26.877  1.00 8.55  ? 109 VAL A O   1 
ATOM   1154 C  CB  . VAL A 1 109 ? -12.074 -13.085 26.179  1.00 9.06  ? 109 VAL A CB  1 
ATOM   1155 C  CG1 . VAL A 1 109 ? -13.091 -13.212 27.306  1.00 10.60 ? 109 VAL A CG1 1 
ATOM   1156 C  CG2 . VAL A 1 109 ? -12.392 -11.832 25.361  1.00 8.82  ? 109 VAL A CG2 1 
ATOM   1157 N  N   . ASP A 1 110 ? -9.855  -14.262 28.678  1.00 8.38  ? 110 ASP A N   1 
ATOM   1158 C  CA  . ASP A 1 110 ? -9.367  -15.482 29.363  1.00 9.46  ? 110 ASP A CA  1 
ATOM   1159 C  C   . ASP A 1 110 ? -8.371  -16.269 28.518  1.00 9.41  ? 110 ASP A C   1 
ATOM   1160 O  O   . ASP A 1 110 ? -8.440  -17.511 28.470  1.00 10.17 ? 110 ASP A O   1 
ATOM   1161 C  CB  . ASP A 1 110 ? -10.560 -16.300 29.852  1.00 11.22 ? 110 ASP A CB  1 
ATOM   1162 C  CG  . ASP A 1 110 ? -11.362 -15.556 30.904  1.00 10.50 ? 110 ASP A CG  1 
ATOM   1163 O  OD1 . ASP A 1 110 ? -10.833 -14.655 31.544  1.00 11.89 ? 110 ASP A OD1 1 
ATOM   1164 O  OD2 . ASP A 1 110 ? -12.523 -15.904 31.030  1.00 12.81 ? 110 ASP A OD2 1 
ATOM   1165 N  N   . LYS A 1 111 ? -7.510  -15.532 27.828  1.00 8.57  ? 111 LYS A N   1 
ATOM   1166 C  CA  . LYS A 1 111 ? -6.506  -16.079 26.967  1.00 10.02 ? 111 LYS A CA  1 
ATOM   1167 C  C   . LYS A 1 111 ? -6.994  -16.591 25.659  1.00 9.59  ? 111 LYS A C   1 
ATOM   1168 O  O   . LYS A 1 111 ? -6.181  -16.955 24.791  1.00 10.69 ? 111 LYS A O   1 
ATOM   1169 C  CB  . LYS A 1 111 ? -5.520  -17.081 27.637  1.00 11.28 ? 111 LYS A CB  1 
ATOM   1170 C  CG  . LYS A 1 111 ? -4.800  -16.468 28.896  1.00 14.45 ? 111 LYS A CG  1 
ATOM   1171 C  CD  . LYS A 1 111 ? -3.845  -15.289 28.570  1.00 17.29 ? 111 LYS A CD  1 
ATOM   1172 C  CE  . LYS A 1 111 ? -3.156  -14.618 29.794  1.00 20.95 ? 111 LYS A CE  1 
ATOM   1173 N  NZ  . LYS A 1 111 ? -2.011  -15.415 30.192  1.00 21.71 ? 111 LYS A NZ  1 
ATOM   1174 N  N   . LYS A 1 112 ? -8.315  -16.583 25.417  1.00 8.75  ? 112 LYS A N   1 
ATOM   1175 C  CA  . LYS A 1 112 ? -8.844  -16.993 24.128  1.00 9.24  ? 112 LYS A CA  1 
ATOM   1176 C  C   . LYS A 1 112 ? -8.580  -15.940 23.068  1.00 7.61  ? 112 LYS A C   1 
ATOM   1177 O  O   . LYS A 1 112 ? -8.858  -14.765 23.275  1.00 7.44  ? 112 LYS A O   1 
ATOM   1178 C  CB  . LYS A 1 112 ? -10.394 -17.148 24.241  1.00 10.80 ? 112 LYS A CB  1 
ATOM   1179 C  CG  . LYS A 1 112 ? -11.049 -17.545 22.868  1.00 12.00 ? 112 LYS A CG  1 
ATOM   1180 C  CD  . LYS A 1 112 ? -12.560 -17.528 22.979  1.00 14.72 ? 112 LYS A CD  1 
ATOM   1181 C  CE  . LYS A 1 112 ? -13.168 -17.708 21.595  1.00 14.86 ? 112 LYS A CE  1 
ATOM   1182 N  NZ  . LYS A 1 112 ? -12.984 -19.055 21.095  1.00 16.55 ? 112 LYS A NZ  1 
ATOM   1183 N  N   A LYS A 1 113 ? -8.041  -16.404 21.959  0.50 7.99  ? 113 LYS A N   1 
ATOM   1184 N  N   B LYS A 1 113 ? -8.029  -16.380 21.949  0.50 7.84  ? 113 LYS A N   1 
ATOM   1185 C  CA  A LYS A 1 113 ? -7.887  -15.608 20.765  0.50 8.41  ? 113 LYS A CA  1 
ATOM   1186 C  CA  B LYS A 1 113 ? -7.776  -15.551 20.771  0.50 8.22  ? 113 LYS A CA  1 
ATOM   1187 C  C   A LYS A 1 113 ? -9.078  -15.852 19.870  0.50 7.45  ? 113 LYS A C   1 
ATOM   1188 C  C   B LYS A 1 113 ? -8.880  -15.821 19.773  0.50 7.73  ? 113 LYS A C   1 
ATOM   1189 O  O   A LYS A 1 113 ? -9.570  -16.997 19.720  0.50 8.55  ? 113 LYS A O   1 
ATOM   1190 O  O   B LYS A 1 113 ? -9.104  -16.991 19.434  0.50 8.10  ? 113 LYS A O   1 
ATOM   1191 C  CB  A LYS A 1 113 ? -6.578  -15.967 20.010  0.50 8.59  ? 113 LYS A CB  1 
ATOM   1192 C  CB  B LYS A 1 113 ? -6.426  -15.948 20.105  0.50 8.76  ? 113 LYS A CB  1 
ATOM   1193 C  CG  A LYS A 1 113 ? -5.320  -15.703 20.815  0.50 8.45  ? 113 LYS A CG  1 
ATOM   1194 C  CG  B LYS A 1 113 ? -5.225  -15.492 20.882  0.50 10.06 ? 113 LYS A CG  1 
ATOM   1195 C  CD  A LYS A 1 113 ? -4.103  -16.155 19.984  0.50 9.37  ? 113 LYS A CD  1 
ATOM   1196 C  CD  B LYS A 1 113 ? -3.988  -16.285 20.471  0.50 9.74  ? 113 LYS A CD  1 
ATOM   1197 C  CE  A LYS A 1 113 ? -2.776  -15.714 20.640  0.50 10.43 ? 113 LYS A CE  1 
ATOM   1198 C  CE  B LYS A 1 113 ? -2.877  -15.715 21.304  0.50 12.00 ? 113 LYS A CE  1 
ATOM   1199 N  NZ  A LYS A 1 113 ? -2.410  -16.403 21.898  0.50 10.64 ? 113 LYS A NZ  1 
ATOM   1200 N  NZ  B LYS A 1 113 ? -1.643  -16.374 20.890  0.50 13.46 ? 113 LYS A NZ  1 
ATOM   1201 N  N   . TYR A 1 114 ? -9.532  -14.764 19.258  1.00 7.13  ? 114 TYR A N   1 
ATOM   1202 C  CA  . TYR A 1 114 ? -10.530 -14.846 18.228  1.00 7.46  ? 114 TYR A CA  1 
ATOM   1203 C  C   . TYR A 1 114 ? -9.836  -14.820 16.832  1.00 7.17  ? 114 TYR A C   1 
ATOM   1204 O  O   . TYR A 1 114 ? -8.659  -14.485 16.709  1.00 7.52  ? 114 TYR A O   1 
ATOM   1205 C  CB  . TYR A 1 114 ? -11.580 -13.736 18.327  1.00 7.48  ? 114 TYR A CB  1 
ATOM   1206 C  CG  . TYR A 1 114 ? -12.540 -13.941 19.476  1.00 7.48  ? 114 TYR A CG  1 
ATOM   1207 C  CD1 . TYR A 1 114 ? -12.235 -13.498 20.753  1.00 8.62  ? 114 TYR A CD1 1 
ATOM   1208 C  CD2 . TYR A 1 114 ? -13.750 -14.576 19.266  1.00 8.86  ? 114 TYR A CD2 1 
ATOM   1209 C  CE1 . TYR A 1 114 ? -13.125 -13.669 21.795  1.00 11.05 ? 114 TYR A CE1 1 
ATOM   1210 C  CE2 . TYR A 1 114 ? -14.644 -14.753 20.305  1.00 11.60 ? 114 TYR A CE2 1 
ATOM   1211 C  CZ  . TYR A 1 114 ? -14.320 -14.303 21.569  1.00 12.04 ? 114 TYR A CZ  1 
ATOM   1212 O  OH  . TYR A 1 114 ? -15.181 -14.464 22.638  1.00 17.28 ? 114 TYR A OH  1 
ATOM   1213 N  N   . ALA A 1 115 ? -10.598 -15.164 15.801  1.00 7.24  ? 115 ALA A N   1 
ATOM   1214 C  CA  . ALA A 1 115 ? -10.076 -15.182 14.429  1.00 7.17  ? 115 ALA A CA  1 
ATOM   1215 C  C   . ALA A 1 115 ? -9.709  -13.799 13.958  1.00 6.74  ? 115 ALA A C   1 
ATOM   1216 O  O   . ALA A 1 115 ? -8.837  -13.661 13.086  1.00 7.66  ? 115 ALA A O   1 
ATOM   1217 C  CB  . ALA A 1 115 ? -11.067 -15.825 13.491  1.00 8.66  ? 115 ALA A CB  1 
ATOM   1218 N  N   . ALA A 1 116 ? -10.393 -12.757 14.460  1.00 6.55  ? 116 ALA A N   1 
ATOM   1219 C  CA  . ALA A 1 116 ? -10.081 -11.416 13.995  1.00 6.70  ? 116 ALA A CA  1 
ATOM   1220 C  C   . ALA A 1 116 ? -10.672 -10.445 14.993  1.00 5.85  ? 116 ALA A C   1 
ATOM   1221 O  O   . ALA A 1 116 ? -11.425 -10.843 15.905  1.00 6.56  ? 116 ALA A O   1 
ATOM   1222 C  CB  . ALA A 1 116 ? -10.643 -11.155 12.559  1.00 7.48  ? 116 ALA A CB  1 
ATOM   1223 N  N   . GLU A 1 117 ? -10.339 -9.179  14.806  1.00 6.30  ? 117 GLU A N   1 
ATOM   1224 C  CA  . GLU A 1 117 ? -10.885 -8.127  15.657  1.00 6.30  ? 117 GLU A CA  1 
ATOM   1225 C  C   . GLU A 1 117 ? -11.057 -6.871  14.801  1.00 6.15  ? 117 GLU A C   1 
ATOM   1226 O  O   . GLU A 1 117 ? -10.159 -6.496  14.069  1.00 6.97  ? 117 GLU A O   1 
ATOM   1227 C  CB  . GLU A 1 117 ? -9.920  -7.880  16.861  1.00 5.98  ? 117 GLU A CB  1 
ATOM   1228 C  CG  . GLU A 1 117 ? -10.522 -6.990  17.938  1.00 6.33  ? 117 GLU A CG  1 
ATOM   1229 C  CD  . GLU A 1 117 ? -9.624  -6.905  19.158  1.00 5.89  ? 117 GLU A CD  1 
ATOM   1230 O  OE1 . GLU A 1 117 ? -8.860  -7.880  19.409  1.00 6.58  ? 117 GLU A OE1 1 
ATOM   1231 O  OE2 . GLU A 1 117 ? -9.652  -5.855  19.844  1.00 6.79  ? 117 GLU A OE2 1 
ATOM   1232 N  N   . LEU A 1 118 ? -12.238 -6.303  14.898  1.00 6.21  ? 118 LEU A N   1 
ATOM   1233 C  CA  . LEU A 1 118 ? -12.613 -5.053  14.209  1.00 5.95  ? 118 LEU A CA  1 
ATOM   1234 C  C   . LEU A 1 118 ? -12.419 -3.928  15.186  1.00 5.51  ? 118 LEU A C   1 
ATOM   1235 O  O   . LEU A 1 118 ? -12.861 -3.969  16.335  1.00 6.32  ? 118 LEU A O   1 
ATOM   1236 C  CB  . LEU A 1 118 ? -14.104 -5.189  13.850  1.00 7.25  ? 118 LEU A CB  1 
ATOM   1237 C  CG  . LEU A 1 118 ? -14.873 -3.903  13.502  1.00 8.05  ? 118 LEU A CG  1 
ATOM   1238 C  CD1 . LEU A 1 118 ? -14.262 -3.189  12.247  1.00 8.66  ? 118 LEU A CD1 1 
ATOM   1239 C  CD2 . LEU A 1 118 ? -16.329 -4.230  13.198  1.00 9.35  ? 118 LEU A CD2 1 
ATOM   1240 N  N   . HIS A 1 119 ? -11.805 -2.847  14.722  1.00 5.72  ? 119 HIS A N   1 
ATOM   1241 C  CA  . HIS A 1 119 ? -11.574 -1.628  15.499  1.00 5.52  ? 119 HIS A CA  1 
ATOM   1242 C  C   . HIS A 1 119 ? -12.158 -0.447  14.809  1.00 5.49  ? 119 HIS A C   1 
ATOM   1243 O  O   . HIS A 1 119 ? -11.790 -0.144  13.656  1.00 6.36  ? 119 HIS A O   1 
ATOM   1244 C  CB  . HIS A 1 119 ? -10.080 -1.395  15.670  1.00 6.65  ? 119 HIS A CB  1 
ATOM   1245 C  CG  . HIS A 1 119 ? -9.461  -2.405  16.585  1.00 6.02  ? 119 HIS A CG  1 
ATOM   1246 N  ND1 . HIS A 1 119 ? -8.093  -2.671  16.593  1.00 6.01  ? 119 HIS A ND1 1 
ATOM   1247 C  CD2 . HIS A 1 119 ? -10.038 -3.167  17.574  1.00 6.41  ? 119 HIS A CD2 1 
ATOM   1248 C  CE1 . HIS A 1 119 ? -7.878  -3.601  17.560  1.00 6.17  ? 119 HIS A CE1 1 
ATOM   1249 N  NE2 . HIS A 1 119 ? -9.044  -3.891  18.130  1.00 6.46  ? 119 HIS A NE2 1 
ATOM   1250 N  N   . LEU A 1 120 ? -13.098 0.221   15.477  1.00 5.84  ? 120 LEU A N   1 
ATOM   1251 C  CA  . LEU A 1 120 ? -13.671 1.467   14.973  1.00 6.84  ? 120 LEU A CA  1 
ATOM   1252 C  C   . LEU A 1 120 ? -13.024 2.604   15.796  1.00 6.23  ? 120 LEU A C   1 
ATOM   1253 O  O   . LEU A 1 120 ? -13.158 2.663   17.024  1.00 6.50  ? 120 LEU A O   1 
ATOM   1254 C  CB  . LEU A 1 120 ? -15.181 1.457   15.134  1.00 7.44  ? 120 LEU A CB  1 
ATOM   1255 C  CG  . LEU A 1 120 ? -15.876 0.381   14.286  1.00 8.60  ? 120 LEU A CG  1 
ATOM   1256 C  CD1 . LEU A 1 120 ? -16.621 -0.608  15.181  1.00 11.93 ? 120 LEU A CD1 1 
ATOM   1257 C  CD2 . LEU A 1 120 ? -16.809 1.066   13.307  1.00 11.79 ? 120 LEU A CD2 1 
ATOM   1258 N  N   . VAL A 1 121 ? -12.261 3.439   15.096  1.00 6.60  ? 121 VAL A N   1 
ATOM   1259 C  CA  . VAL A 1 121 ? -11.394 4.434   15.717  1.00 7.41  ? 121 VAL A CA  1 
ATOM   1260 C  C   . VAL A 1 121 ? -12.127 5.777   15.724  1.00 7.39  ? 121 VAL A C   1 
ATOM   1261 O  O   . VAL A 1 121 ? -12.551 6.251   14.667  1.00 8.58  ? 121 VAL A O   1 
ATOM   1262 C  CB  . VAL A 1 121 ? -10.043 4.563   14.945  1.00 7.67  ? 121 VAL A CB  1 
ATOM   1263 C  CG1 . VAL A 1 121 ? -9.180  5.640   15.562  1.00 8.67  ? 121 VAL A CG1 1 
ATOM   1264 C  CG2 . VAL A 1 121 ? -9.311  3.233   14.850  1.00 8.55  ? 121 VAL A CG2 1 
ATOM   1265 N  N   . HIS A 1 122 ? -12.231 6.377   16.884  1.00 6.93  ? 122 HIS A N   1 
ATOM   1266 C  CA  . HIS A 1 122 ? -12.917 7.661   17.040  1.00 7.44  ? 122 HIS A CA  1 
ATOM   1267 C  C   . HIS A 1 122 ? -12.036 8.633   17.810  1.00 7.27  ? 122 HIS A C   1 
ATOM   1268 O  O   . HIS A 1 122 ? -11.238 8.227   18.657  1.00 7.60  ? 122 HIS A O   1 
ATOM   1269 C  CB  . HIS A 1 122 ? -14.166 7.510   17.876  1.00 7.36  ? 122 HIS A CB  1 
ATOM   1270 C  CG  . HIS A 1 122 ? -15.097 6.364   17.507  1.00 7.83  ? 122 HIS A CG  1 
ATOM   1271 N  ND1 . HIS A 1 122 ? -14.802 5.072   17.733  1.00 7.55  ? 122 HIS A ND1 1 
ATOM   1272 C  CD2 . HIS A 1 122 ? -16.348 6.363   16.916  1.00 9.55  ? 122 HIS A CD2 1 
ATOM   1273 C  CE1 . HIS A 1 122 ? -15.830 4.307   17.328  1.00 9.07  ? 122 HIS A CE1 1 
ATOM   1274 N  NE2 . HIS A 1 122 ? -16.782 5.088   16.800  1.00 9.17  ? 122 HIS A NE2 1 
ATOM   1275 N  N   . TRP A 1 123 ? -12.216 9.938   17.560  1.00 7.25  ? 123 TRP A N   1 
ATOM   1276 C  CA  . TRP A 1 123 ? -11.378 10.939  18.285  1.00 7.74  ? 123 TRP A CA  1 
ATOM   1277 C  C   . TRP A 1 123 ? -12.278 11.952  18.965  1.00 7.55  ? 123 TRP A C   1 
ATOM   1278 O  O   . TRP A 1 123 ? -13.375 12.299  18.511  1.00 8.26  ? 123 TRP A O   1 
ATOM   1279 C  CB  . TRP A 1 123 ? -10.360 11.613  17.329  1.00 10.33 ? 123 TRP A CB  1 
ATOM   1280 C  CG  . TRP A 1 123 ? -10.916 12.239  16.140  1.00 11.13 ? 123 TRP A CG  1 
ATOM   1281 C  CD1 . TRP A 1 123 ? -11.135 11.640  14.927  1.00 12.51 ? 123 TRP A CD1 1 
ATOM   1282 C  CD2 . TRP A 1 123 ? -11.313 13.593  15.991  1.00 10.61 ? 123 TRP A CD2 1 
ATOM   1283 N  NE1 . TRP A 1 123 ? -11.657 12.530  14.055  1.00 14.32 ? 123 TRP A NE1 1 
ATOM   1284 C  CE2 . TRP A 1 123 ? -11.778 13.744  14.664  1.00 13.64 ? 123 TRP A CE2 1 
ATOM   1285 C  CE3 . TRP A 1 123 ? -11.294 14.718  16.840  1.00 12.05 ? 123 TRP A CE3 1 
ATOM   1286 C  CZ2 . TRP A 1 123 ? -12.247 14.930  14.192  1.00 13.93 ? 123 TRP A CZ2 1 
ATOM   1287 C  CZ3 . TRP A 1 123 ? -11.815 15.904  16.353  1.00 13.92 ? 123 TRP A CZ3 1 
ATOM   1288 C  CH2 . TRP A 1 123 ? -12.254 16.026  15.029  1.00 15.61 ? 123 TRP A CH2 1 
ATOM   1289 N  N   . ASN A 1 124 ? -11.734 12.442  20.059  1.00 7.60  ? 124 ASN A N   1 
ATOM   1290 C  CA  . ASN A 1 124 ? -12.512 13.360  20.942  1.00 8.63  ? 124 ASN A CA  1 
ATOM   1291 C  C   . ASN A 1 124 ? -12.584 14.740  20.349  1.00 8.76  ? 124 ASN A C   1 
ATOM   1292 O  O   . ASN A 1 124 ? -11.552 15.391  20.141  1.00 8.32  ? 124 ASN A O   1 
ATOM   1293 C  CB  . ASN A 1 124 ? -11.747 13.384  22.260  1.00 9.05  ? 124 ASN A CB  1 
ATOM   1294 C  CG  . ASN A 1 124 ? -12.491 14.000  23.370  1.00 9.65  ? 124 ASN A CG  1 
ATOM   1295 O  OD1 . ASN A 1 124 ? -13.333 14.894  23.132  1.00 10.91 ? 124 ASN A OD1 1 
ATOM   1296 N  ND2 . ASN A 1 124 ? -12.223 13.603  24.615  1.00 10.50 ? 124 ASN A ND2 1 
ATOM   1297 N  N   A THR A 1 125 ? -13.828 15.181  20.215  0.50 9.22  ? 125 THR A N   1 
ATOM   1298 N  N   B THR A 1 125 ? -13.772 15.200  19.955  0.50 9.72  ? 125 THR A N   1 
ATOM   1299 C  CA  A THR A 1 125 ? -14.122 16.450  19.580  0.50 11.52 ? 125 THR A CA  1 
ATOM   1300 C  CA  B THR A 1 125 ? -13.861 16.466  19.178  0.50 10.16 ? 125 THR A CA  1 
ATOM   1301 C  C   A THR A 1 125 ? -13.609 17.599  20.399  0.50 9.29  ? 125 THR A C   1 
ATOM   1302 C  C   B THR A 1 125 ? -13.370 17.680  19.961  0.50 9.46  ? 125 THR A C   1 
ATOM   1303 O  O   A THR A 1 125 ? -13.476 18.667  19.861  0.50 11.81 ? 125 THR A O   1 
ATOM   1304 O  O   B THR A 1 125 ? -13.072 18.737  19.378  0.50 10.81 ? 125 THR A O   1 
ATOM   1305 C  CB  A THR A 1 125 ? -15.618 16.648  19.427  0.50 12.40 ? 125 THR A CB  1 
ATOM   1306 C  CB  B THR A 1 125 ? -15.292 16.733  18.698  0.50 10.42 ? 125 THR A CB  1 
ATOM   1307 O  OG1 A THR A 1 125 ? -16.236 16.672  20.721  0.50 12.04 ? 125 THR A OG1 1 
ATOM   1308 O  OG1 B THR A 1 125 ? -16.217 16.774  19.818  0.50 10.38 ? 125 THR A OG1 1 
ATOM   1309 C  CG2 A THR A 1 125 ? -16.212 15.550  18.601  0.50 15.48 ? 125 THR A CG2 1 
ATOM   1310 C  CG2 B THR A 1 125 ? -15.704 15.675  17.742  0.50 11.61 ? 125 THR A CG2 1 
ATOM   1311 N  N   A LYS A 1 126 ? -13.276 17.384  21.774  0.50 10.17 ? 126 LYS A N   1 
ATOM   1312 N  N   B LYS A 1 126 ? -13.185 17.596  21.311  0.50 10.10 ? 126 LYS A N   1 
ATOM   1313 C  CA  A LYS A 1 126 ? -12.850 18.608  22.427  0.50 13.97 ? 126 LYS A CA  1 
ATOM   1314 C  CA  B LYS A 1 126 ? -12.599 18.656  22.101  0.50 11.53 ? 126 LYS A CA  1 
ATOM   1315 C  C   A LYS A 1 126 ? -11.379 18.941  22.062  0.50 12.02 ? 126 LYS A C   1 
ATOM   1316 C  C   B LYS A 1 126 ? -11.214 19.084  21.555  0.50 11.41 ? 126 LYS A C   1 
ATOM   1317 O  O   A LYS A 1 126 ? -10.832 19.947  22.454  0.50 9.65  ? 126 LYS A O   1 
ATOM   1318 O  O   B LYS A 1 126 ? -10.899 20.279  21.583  0.50 11.02 ? 126 LYS A O   1 
ATOM   1319 C  CB  A LYS A 1 126 ? -13.014 18.461  23.938  0.50 17.19 ? 126 LYS A CB  1 
ATOM   1320 C  CB  B LYS A 1 126 ? -12.618 18.332  23.624  0.50 14.15 ? 126 LYS A CB  1 
ATOM   1321 C  CG  A LYS A 1 126 ? -11.999 17.543  24.536  0.50 12.24 ? 126 LYS A CG  1 
ATOM   1322 C  CG  B LYS A 1 126 ? -11.478 17.579  24.270  0.50 15.00 ? 126 LYS A CG  1 
ATOM   1323 C  CD  A LYS A 1 126 ? -12.392 17.270  25.957  0.50 17.70 ? 126 LYS A CD  1 
ATOM   1324 C  CD  B LYS A 1 126 ? -11.798 17.110  25.699  0.50 21.44 ? 126 LYS A CD  1 
ATOM   1325 C  CE  A LYS A 1 126 ? -11.250 16.698  26.731  0.50 17.00 ? 126 LYS A CE  1 
ATOM   1326 C  CE  B LYS A 1 126 ? -11.271 18.061  26.754  0.50 24.73 ? 126 LYS A CE  1 
ATOM   1327 N  NZ  A LYS A 1 126 ? -11.775 16.002  27.931  0.50 21.55 ? 126 LYS A NZ  1 
ATOM   1328 N  NZ  B LYS A 1 126 ? -10.497 17.407  27.862  0.50 28.73 ? 126 LYS A NZ  1 
ATOM   1329 N  N   A TYR A 1 127 ? -10.767 18.076  21.254  0.50 9.90  ? 127 TYR A N   1 
ATOM   1330 N  N   B TYR A 1 127 ? -10.441 18.128  21.035  0.50 8.86  ? 127 TYR A N   1 
ATOM   1331 C  CA  A TYR A 1 127 ? -9.398  18.340  20.798  0.50 10.04 ? 127 TYR A CA  1 
ATOM   1332 C  CA  B TYR A 1 127 ? -9.100  18.428  20.557  0.50 9.91  ? 127 TYR A CA  1 
ATOM   1333 C  C   A TYR A 1 127 ? -9.244  18.783  19.314  0.50 10.06 ? 127 TYR A C   1 
ATOM   1334 C  C   B TYR A 1 127 ? -9.138  18.807  19.102  0.50 10.38 ? 127 TYR A C   1 
ATOM   1335 O  O   A TYR A 1 127 ? -8.103  19.062  18.880  0.50 9.50  ? 127 TYR A O   1 
ATOM   1336 O  O   B TYR A 1 127 ? -8.073  19.088  18.471  0.50 10.57 ? 127 TYR A O   1 
ATOM   1337 C  CB  A TYR A 1 127 ? -8.455  17.161  21.099  0.50 9.14  ? 127 TYR A CB  1 
ATOM   1338 C  CB  B TYR A 1 127 ? -8.145  17.268  20.789  0.50 9.71  ? 127 TYR A CB  1 
ATOM   1339 C  CG  A TYR A 1 127 ? -8.433  16.794  22.556  0.50 8.57  ? 127 TYR A CG  1 
ATOM   1340 C  CG  B TYR A 1 127 ? -8.123  16.953  22.254  0.50 9.33  ? 127 TYR A CG  1 
ATOM   1341 C  CD1 A TYR A 1 127 ? -8.124  17.741  23.530  0.50 8.76  ? 127 TYR A CD1 1 
ATOM   1342 C  CD1 B TYR A 1 127 ? -7.683  17.900  23.165  0.50 10.44 ? 127 TYR A CD1 1 
ATOM   1343 C  CD2 A TYR A 1 127 ? -8.725  15.493  22.975  0.50 9.54  ? 127 TYR A CD2 1 
ATOM   1344 C  CD2 B TYR A 1 127 ? -8.519  15.700  22.738  0.50 9.84  ? 127 TYR A CD2 1 
ATOM   1345 C  CE1 A TYR A 1 127 ? -8.122  17.411  24.857  0.50 9.50  ? 127 TYR A CE1 1 
ATOM   1346 C  CE1 B TYR A 1 127 ? -7.665  17.614  24.515  0.50 9.11  ? 127 TYR A CE1 1 
ATOM   1347 C  CE2 A TYR A 1 127 ? -8.761  15.150  24.304  0.50 9.67  ? 127 TYR A CE2 1 
ATOM   1348 C  CE2 B TYR A 1 127 ? -8.529  15.423  24.082  0.50 9.68  ? 127 TYR A CE2 1 
ATOM   1349 C  CZ  A TYR A 1 127 ? -8.421  16.100  25.247  0.50 9.65  ? 127 TYR A CZ  1 
ATOM   1350 C  CZ  B TYR A 1 127 ? -8.061  16.386  24.967  0.50 11.28 ? 127 TYR A CZ  1 
ATOM   1351 O  OH  A TYR A 1 127 ? -8.492  15.811  26.579  0.50 11.59 ? 127 TYR A OH  1 
ATOM   1352 O  OH  B TYR A 1 127 ? -8.071  16.167  26.325  0.50 11.62 ? 127 TYR A OH  1 
ATOM   1353 N  N   . GLY A 1 128 ? -10.344 18.846  18.560  1.00 11.03 ? 128 GLY A N   1 
ATOM   1354 C  CA  . GLY A 1 128 ? -10.412 19.484  17.264  1.00 11.10 ? 128 GLY A CA  1 
ATOM   1355 C  C   . GLY A 1 128 ? -9.928  18.698  16.052  1.00 10.83 ? 128 GLY A C   1 
ATOM   1356 O  O   . GLY A 1 128 ? -10.529 18.775  14.974  1.00 11.15 ? 128 GLY A O   1 
ATOM   1357 N  N   . ASP A 1 129 ? -8.829  17.919  16.156  1.00 11.09 ? 129 ASP A N   1 
ATOM   1358 C  CA  . ASP A 1 129 ? -8.403  17.031  15.074  1.00 12.11 ? 129 ASP A CA  1 
ATOM   1359 C  C   . ASP A 1 129 ? -7.703  15.824  15.655  1.00 9.90  ? 129 ASP A C   1 
ATOM   1360 O  O   . ASP A 1 129 ? -7.293  15.840  16.819  1.00 10.39 ? 129 ASP A O   1 
ATOM   1361 C  CB  . ASP A 1 129 ? -7.478  17.769  14.013  1.00 11.39 ? 129 ASP A CB  1 
ATOM   1362 C  CG  . ASP A 1 129 ? -6.131  18.209  14.526  1.00 11.15 ? 129 ASP A CG  1 
ATOM   1363 O  OD1 . ASP A 1 129 ? -5.226  17.360  14.823  1.00 13.85 ? 129 ASP A OD1 1 
ATOM   1364 O  OD2 . ASP A 1 129 ? -5.841  19.363  14.495  1.00 15.05 ? 129 ASP A OD2 1 
ATOM   1365 N  N   . VAL A 1 130 ? -7.547  14.776  14.862  1.00 11.04 ? 130 VAL A N   1 
ATOM   1366 C  CA  . VAL A 1 130 ? -7.018  13.521  15.366  1.00 10.35 ? 130 VAL A CA  1 
ATOM   1367 C  C   . VAL A 1 130 ? -5.575  13.642  15.762  1.00 10.19 ? 130 VAL A C   1 
ATOM   1368 O  O   . VAL A 1 130 ? -5.200  13.030  16.732  1.00 9.69  ? 130 VAL A O   1 
ATOM   1369 C  CB  . VAL A 1 130 ? -7.291  12.365  14.373  1.00 11.99 ? 130 VAL A CB  1 
ATOM   1370 C  CG1 . VAL A 1 130 ? -6.443  12.484  13.146  1.00 15.23 ? 130 VAL A CG1 1 
ATOM   1371 C  CG2 . VAL A 1 130 ? -7.032  10.993  15.036  1.00 13.79 ? 130 VAL A CG2 1 
ATOM   1372 N  N   . GLY A 1 131 ? -4.766  14.467  15.058  1.00 10.46 ? 131 GLY A N   1 
ATOM   1373 C  CA  . GLY A 1 131 ? -3.387  14.551  15.418  1.00 12.06 ? 131 GLY A CA  1 
ATOM   1374 C  C   . GLY A 1 131 ? -3.212  15.174  16.815  1.00 9.76  ? 131 GLY A C   1 
ATOM   1375 O  O   . GLY A 1 131 ? -2.348  14.809  17.565  1.00 11.15 ? 131 GLY A O   1 
ATOM   1376 N  N   . LYS A 1 132 ? -4.044  16.177  17.142  1.00 9.96  ? 132 LYS A N   1 
ATOM   1377 C  CA  . LYS A 1 132 ? -3.990  16.749  18.522  1.00 9.30  ? 132 LYS A CA  1 
ATOM   1378 C  C   . LYS A 1 132 ? -4.514  15.725  19.501  1.00 8.32  ? 132 LYS A C   1 
ATOM   1379 O  O   . LYS A 1 132 ? -4.026  15.613  20.597  1.00 8.85  ? 132 LYS A O   1 
ATOM   1380 C  CB  . LYS A 1 132 ? -4.849  18.037  18.541  1.00 10.33 ? 132 LYS A CB  1 
ATOM   1381 C  CG  . LYS A 1 132 ? -4.140  19.210  17.850  1.00 13.98 ? 132 LYS A CG  1 
ATOM   1382 C  CD  . LYS A 1 132 ? -2.939  19.717  18.675  1.00 16.70 ? 132 LYS A CD  1 
ATOM   1383 C  CE  . LYS A 1 132 ? -2.429  21.033  18.037  1.00 17.71 ? 132 LYS A CE  1 
ATOM   1384 N  NZ  . LYS A 1 132 ? -1.799  20.716  16.719  1.00 23.93 ? 132 LYS A NZ  1 
ATOM   1385 N  N   . ALA A 1 133 ? -5.591  14.999  19.139  1.00 8.64  ? 133 ALA A N   1 
ATOM   1386 C  CA  . ALA A 1 133 ? -6.131  14.003  20.025  1.00 8.43  ? 133 ALA A CA  1 
ATOM   1387 C  C   . ALA A 1 133 ? -5.128  12.919  20.382  1.00 7.76  ? 133 ALA A C   1 
ATOM   1388 O  O   . ALA A 1 133 ? -5.133  12.411  21.511  1.00 8.51  ? 133 ALA A O   1 
ATOM   1389 C  CB  . ALA A 1 133 ? -7.379  13.391  19.395  1.00 8.87  ? 133 ALA A CB  1 
ATOM   1390 N  N   . LEU A 1 134 ? -4.213  12.590  19.441  1.00 8.52  ? 134 LEU A N   1 
ATOM   1391 C  CA  . LEU A 1 134 ? -3.208  11.568  19.700  1.00 9.56  ? 134 LEU A CA  1 
ATOM   1392 C  C   . LEU A 1 134 ? -2.286  11.942  20.852  1.00 8.81  ? 134 LEU A C   1 
ATOM   1393 O  O   . LEU A 1 134 ? -1.592  11.071  21.392  1.00 10.22 ? 134 LEU A O   1 
ATOM   1394 C  CB  . LEU A 1 134 ? -2.356  11.361  18.452  1.00 11.42 ? 134 LEU A CB  1 
ATOM   1395 C  CG  . LEU A 1 134 ? -2.740  10.546  17.317  1.00 18.05 ? 134 LEU A CG  1 
ATOM   1396 C  CD1 . LEU A 1 134 ? -1.553  10.313  16.417  1.00 22.78 ? 134 LEU A CD1 1 
ATOM   1397 C  CD2 . LEU A 1 134 ? -3.399  9.203   17.669  1.00 13.81 ? 134 LEU A CD2 1 
ATOM   1398 N  N   . GLN A 1 135 ? -2.228  13.241  21.192  1.00 9.07  ? 135 GLN A N   1 
ATOM   1399 C  CA  . GLN A 1 135 ? -1.353  13.741  22.219  1.00 9.98  ? 135 GLN A CA  1 
ATOM   1400 C  C   . GLN A 1 135 ? -1.991  13.807  23.581  1.00 9.03  ? 135 GLN A C   1 
ATOM   1401 O  O   . GLN A 1 135 ? -1.394  14.367  24.506  1.00 11.76 ? 135 GLN A O   1 
ATOM   1402 C  CB  . GLN A 1 135 ? -0.809  15.120  21.780  1.00 11.62 ? 135 GLN A CB  1 
ATOM   1403 C  CG  . GLN A 1 135 ? -0.061  15.015  20.461  1.00 13.72 ? 135 GLN A CG  1 
ATOM   1404 C  CD  . GLN A 1 135 ? 0.389   16.358  19.985  1.00 18.42 ? 135 GLN A CD  1 
ATOM   1405 O  OE1 . GLN A 1 135 ? 1.246   16.969  20.572  1.00 26.90 ? 135 GLN A OE1 1 
ATOM   1406 N  NE2 . GLN A 1 135 ? -0.184  16.809  18.886  1.00 23.55 ? 135 GLN A NE2 1 
ATOM   1407 N  N   . GLN A 1 136 ? -3.187  13.268  23.724  1.00 8.74  ? 136 GLN A N   1 
ATOM   1408 C  CA  . GLN A 1 136 ? -3.954  13.407  24.958  1.00 8.43  ? 136 GLN A CA  1 
ATOM   1409 C  C   . GLN A 1 136 ? -4.356  12.062  25.507  1.00 7.72  ? 136 GLN A C   1 
ATOM   1410 O  O   . GLN A 1 136 ? -4.690  11.152  24.736  1.00 8.41  ? 136 GLN A O   1 
ATOM   1411 C  CB  . GLN A 1 136 ? -5.232  14.183  24.694  1.00 9.26  ? 136 GLN A CB  1 
ATOM   1412 C  CG  . GLN A 1 136 ? -4.967  15.547  23.980  1.00 12.03 ? 136 GLN A CG  1 
ATOM   1413 C  CD  . GLN A 1 136 ? -4.159  16.458  24.807  1.00 17.17 ? 136 GLN A CD  1 
ATOM   1414 O  OE1 . GLN A 1 136 ? -4.137  16.346  26.009  1.00 25.25 ? 136 GLN A OE1 1 
ATOM   1415 N  NE2 . GLN A 1 136 ? -3.559  17.416  24.188  1.00 32.22 ? 136 GLN A NE2 1 
ATOM   1416 N  N   A PRO A 1 137 ? -4.415  11.924  26.829  0.50 7.62  ? 137 PRO A N   1 
ATOM   1417 N  N   B PRO A 1 137 ? -4.346  11.910  26.843  0.50 7.92  ? 137 PRO A N   1 
ATOM   1418 C  CA  A PRO A 1 137 ? -4.732  10.609  27.421  0.50 8.21  ? 137 PRO A CA  1 
ATOM   1419 C  CA  B PRO A 1 137 ? -4.692  10.591  27.402  0.50 8.61  ? 137 PRO A CA  1 
ATOM   1420 C  C   A PRO A 1 137 ? -6.126  10.152  27.152  0.50 8.25  ? 137 PRO A C   1 
ATOM   1421 C  C   B PRO A 1 137 ? -6.108  10.152  27.135  0.50 8.37  ? 137 PRO A C   1 
ATOM   1422 O  O   A PRO A 1 137 ? -6.391  8.931   27.198  0.50 11.66 ? 137 PRO A O   1 
ATOM   1423 O  O   B PRO A 1 137 ? -6.367  8.930   27.171  0.50 11.35 ? 137 PRO A O   1 
ATOM   1424 C  CB  A PRO A 1 137 ? -4.480  10.815  28.920  0.50 10.61 ? 137 PRO A CB  1 
ATOM   1425 C  CB  B PRO A 1 137 ? -4.394  10.727  28.911  0.50 11.45 ? 137 PRO A CB  1 
ATOM   1426 C  CG  A PRO A 1 137 ? -4.629  12.273  29.110  0.50 9.89  ? 137 PRO A CG  1 
ATOM   1427 C  CG  B PRO A 1 137 ? -3.529  11.924  29.049  0.50 14.74 ? 137 PRO A CG  1 
ATOM   1428 C  CD  A PRO A 1 137 ? -4.119  12.954  27.847  0.50 9.34  ? 137 PRO A CD  1 
ATOM   1429 C  CD  B PRO A 1 137 ? -3.732  12.832  27.836  0.50 9.32  ? 137 PRO A CD  1 
ATOM   1430 N  N   . ASP A 1 138 ? -7.008  11.079  26.839  1.00 8.69  ? 138 ASP A N   1 
ATOM   1431 C  CA  . ASP A 1 138 ? -8.398  10.783  26.515  1.00 9.33  ? 138 ASP A CA  1 
ATOM   1432 C  C   . ASP A 1 138 ? -8.692  11.238  25.058  1.00 7.65  ? 138 ASP A C   1 
ATOM   1433 O  O   . ASP A 1 138 ? -9.797  11.681  24.768  1.00 9.17  ? 138 ASP A O   1 
ATOM   1434 C  CB  . ASP A 1 138 ? -9.356  11.400  27.532  1.00 11.42 ? 138 ASP A CB  1 
ATOM   1435 C  CG  . ASP A 1 138 ? -9.227  12.896  27.604  1.00 11.83 ? 138 ASP A CG  1 
ATOM   1436 O  OD1 . ASP A 1 138 ? -8.287  13.487  27.015  1.00 12.32 ? 138 ASP A OD1 1 
ATOM   1437 O  OD2 . ASP A 1 138 ? -10.054 13.500  28.286  1.00 15.35 ? 138 ASP A OD2 1 
ATOM   1438 N  N   . GLY A 1 139 ? -7.750  11.144  24.174  1.00 6.90  ? 139 GLY A N   1 
ATOM   1439 C  CA  . GLY A 1 139 ? -7.913  11.651  22.835  1.00 7.31  ? 139 GLY A CA  1 
ATOM   1440 C  C   . GLY A 1 139 ? -8.749  10.766  21.951  1.00 5.94  ? 139 GLY A C   1 
ATOM   1441 O  O   . GLY A 1 139 ? -9.423  11.285  21.044  1.00 7.32  ? 139 GLY A O   1 
ATOM   1442 N  N   . LEU A 1 140 ? -8.609  9.449   22.084  1.00 6.76  ? 140 LEU A N   1 
ATOM   1443 C  CA  . LEU A 1 140 ? -9.248  8.492   21.140  1.00 6.62  ? 140 LEU A CA  1 
ATOM   1444 C  C   . LEU A 1 140 ? -10.098 7.527   21.909  1.00 5.97  ? 140 LEU A C   1 
ATOM   1445 O  O   . LEU A 1 140 ? -9.824  7.252   23.093  1.00 6.37  ? 140 LEU A O   1 
ATOM   1446 C  CB  . LEU A 1 140 ? -8.183  7.703   20.370  1.00 7.45  ? 140 LEU A CB  1 
ATOM   1447 C  CG  . LEU A 1 140 ? -7.604  8.354   19.138  1.00 10.13 ? 140 LEU A CG  1 
ATOM   1448 C  CD1 . LEU A 1 140 ? -6.975  9.712   19.253  1.00 12.36 ? 140 LEU A CD1 1 
ATOM   1449 C  CD2 . LEU A 1 140 ? -6.666  7.368   18.420  1.00 10.94 ? 140 LEU A CD2 1 
ATOM   1450 N  N   . ALA A 1 141 ? -11.085 6.974   21.251  1.00 6.61  ? 141 ALA A N   1 
ATOM   1451 C  CA  . ALA A 1 141 ? -11.865 5.843   21.783  1.00 6.38  ? 141 ALA A CA  1 
ATOM   1452 C  C   . ALA A 1 141 ? -11.938 4.848   20.661  1.00 6.06  ? 141 ALA A C   1 
ATOM   1453 O  O   . ALA A 1 141 ? -12.336 5.193   19.539  1.00 6.94  ? 141 ALA A O   1 
ATOM   1454 C  CB  . ALA A 1 141 ? -13.273 6.283   22.169  1.00 8.25  ? 141 ALA A CB  1 
ATOM   1455 N  N   . VAL A 1 142 ? -11.510 3.629   20.958  1.00 5.54  ? 142 VAL A N   1 
ATOM   1456 C  CA  . VAL A 1 142 ? -11.561 2.544   19.936  1.00 6.23  ? 142 VAL A CA  1 
ATOM   1457 C  C   . VAL A 1 142 ? -12.552 1.531   20.441  1.00 5.67  ? 142 VAL A C   1 
ATOM   1458 O  O   . VAL A 1 142 ? -12.438 1.037   21.568  1.00 6.10  ? 142 VAL A O   1 
ATOM   1459 C  CB  . VAL A 1 142 ? -10.149 1.968   19.591  1.00 6.52  ? 142 VAL A CB  1 
ATOM   1460 C  CG1 . VAL A 1 142 ? -10.326 0.950   18.474  1.00 7.02  ? 142 VAL A CG1 1 
ATOM   1461 C  CG2 . VAL A 1 142 ? -9.218  3.069   19.167  1.00 6.88  ? 142 VAL A CG2 1 
ATOM   1462 N  N   . LEU A 1 143 ? -13.534 1.264   19.584  1.00 6.21  ? 143 LEU A N   1 
ATOM   1463 C  CA  . LEU A 1 143 ? -14.541 0.247   19.826  1.00 5.95  ? 143 LEU A CA  1 
ATOM   1464 C  C   . LEU A 1 143 ? -14.074 -1.013  19.173  1.00 5.63  ? 143 LEU A C   1 
ATOM   1465 O  O   . LEU A 1 143 ? -13.873 -1.054  17.935  1.00 6.61  ? 143 LEU A O   1 
ATOM   1466 C  CB  . LEU A 1 143 ? -15.888 0.748   19.251  1.00 7.35  ? 143 LEU A CB  1 
ATOM   1467 C  CG  . LEU A 1 143 ? -17.080 -0.210  19.404  1.00 8.66  ? 143 LEU A CG  1 
ATOM   1468 C  CD1 . LEU A 1 143 ? -17.358 -0.554  20.856  1.00 10.10 ? 143 LEU A CD1 1 
ATOM   1469 C  CD2 . LEU A 1 143 ? -18.325 0.379   18.732  1.00 10.47 ? 143 LEU A CD2 1 
ATOM   1470 N  N   . GLY A 1 144 ? -13.862 -2.062  19.954  1.00 5.90  ? 144 GLY A N   1 
ATOM   1471 C  CA  . GLY A 1 144 ? -13.343 -3.341  19.479  1.00 5.88  ? 144 GLY A CA  1 
ATOM   1472 C  C   . GLY A 1 144 ? -14.424 -4.408  19.487  1.00 5.72  ? 144 GLY A C   1 
ATOM   1473 O  O   . GLY A 1 144 ? -15.161 -4.512  20.464  1.00 6.74  ? 144 GLY A O   1 
ATOM   1474 N  N   . ILE A 1 145 ? -14.435 -5.182  18.421  1.00 5.69  ? 145 ILE A N   1 
ATOM   1475 C  CA  . ILE A 1 145 ? -15.435 -6.240  18.230  1.00 6.16  ? 145 ILE A CA  1 
ATOM   1476 C  C   . ILE A 1 145 ? -14.691 -7.467  17.757  1.00 5.96  ? 145 ILE A C   1 
ATOM   1477 O  O   . ILE A 1 145 ? -14.001 -7.422  16.758  1.00 6.53  ? 145 ILE A O   1 
ATOM   1478 C  CB  . ILE A 1 145 ? -16.531 -5.769  17.220  1.00 7.53  ? 145 ILE A CB  1 
ATOM   1479 C  CG1 . ILE A 1 145 ? -17.187 -4.497  17.726  1.00 10.18 ? 145 ILE A CG1 1 
ATOM   1480 C  CG2 . ILE A 1 145 ? -17.521 -6.885  16.986  1.00 9.05  ? 145 ILE A CG2 1 
ATOM   1481 C  CD1 . ILE A 1 145 ? -18.146 -3.823  16.796  1.00 11.71 ? 145 ILE A CD1 1 
ATOM   1482 N  N   . PHE A 1 146 ? -14.896 -8.567  18.462  1.00 5.94  ? 146 PHE A N   1 
ATOM   1483 C  CA  . PHE A 1 146 ? -14.293 -9.841  18.070  1.00 6.05  ? 146 PHE A CA  1 
ATOM   1484 C  C   . PHE A 1 146 ? -15.058 -10.481 16.929  1.00 6.22  ? 146 PHE A C   1 
ATOM   1485 O  O   . PHE A 1 146 ? -16.276 -10.349 16.852  1.00 7.31  ? 146 PHE A O   1 
ATOM   1486 C  CB  . PHE A 1 146 ? -14.331 -10.776 19.279  1.00 6.44  ? 146 PHE A CB  1 
ATOM   1487 C  CG  . PHE A 1 146 ? -13.485 -10.312 20.413  1.00 5.91  ? 146 PHE A CG  1 
ATOM   1488 C  CD1 . PHE A 1 146 ? -12.083 -10.141 20.243  1.00 6.95  ? 146 PHE A CD1 1 
ATOM   1489 C  CD2 . PHE A 1 146 ? -14.017 -10.043 21.647  1.00 6.69  ? 146 PHE A CD2 1 
ATOM   1490 C  CE1 . PHE A 1 146 ? -11.309 -9.759  21.302  1.00 6.84  ? 146 PHE A CE1 1 
ATOM   1491 C  CE2 . PHE A 1 146 ? -13.238 -9.659  22.708  1.00 7.67  ? 146 PHE A CE2 1 
ATOM   1492 C  CZ  . PHE A 1 146 ? -11.854 -9.555  22.554  1.00 6.95  ? 146 PHE A CZ  1 
ATOM   1493 N  N   . LEU A 1 147 ? -14.322 -11.188 16.090  1.00 6.31  ? 147 LEU A N   1 
ATOM   1494 C  CA  . LEU A 1 147 ? -14.894 -11.978 15.005  1.00 6.66  ? 147 LEU A CA  1 
ATOM   1495 C  C   . LEU A 1 147 ? -14.587 -13.433 15.248  1.00 6.76  ? 147 LEU A C   1 
ATOM   1496 O  O   . LEU A 1 147 ? -13.412 -13.803 15.464  1.00 7.16  ? 147 LEU A O   1 
ATOM   1497 C  CB  . LEU A 1 147 ? -14.281 -11.586 13.661  1.00 8.04  ? 147 LEU A CB  1 
ATOM   1498 C  CG  . LEU A 1 147 ? -14.886 -10.348 12.942  1.00 8.36  ? 147 LEU A CG  1 
ATOM   1499 C  CD1 . LEU A 1 147 ? -14.713 -9.078  13.822  1.00 9.59  ? 147 LEU A CD1 1 
ATOM   1500 C  CD2 . LEU A 1 147 ? -14.238 -10.096 11.603  1.00 8.77  ? 147 LEU A CD2 1 
ATOM   1501 N  N   . LYS A 1 148 ? -15.601 -14.278 15.189  1.00 7.46  ? 148 LYS A N   1 
ATOM   1502 C  CA  . LYS A 1 148 ? -15.437 -15.724 15.173  1.00 7.87  ? 148 LYS A CA  1 
ATOM   1503 C  C   . LYS A 1 148 ? -15.912 -16.258 13.836  1.00 8.51  ? 148 LYS A C   1 
ATOM   1504 O  O   . LYS A 1 148 ? -16.703 -15.581 13.159  1.00 9.49  ? 148 LYS A O   1 
ATOM   1505 C  CB  . LYS A 1 148 ? -16.157 -16.415 16.309  1.00 8.93  ? 148 LYS A CB  1 
ATOM   1506 C  CG  . LYS A 1 148 ? -17.633 -16.244 16.299  1.00 10.70 ? 148 LYS A CG  1 
ATOM   1507 C  CD  . LYS A 1 148 ? -18.288 -16.879 17.516  1.00 15.09 ? 148 LYS A CD  1 
ATOM   1508 C  CE  . LYS A 1 148 ? -19.772 -16.988 17.379  1.00 25.03 ? 148 LYS A CE  1 
ATOM   1509 N  NZ  . LYS A 1 148 ? -20.256 -17.791 18.580  1.00 37.99 ? 148 LYS A NZ  1 
ATOM   1510 N  N   . VAL A 1 149 ? -15.459 -17.431 13.434  1.00 9.40  ? 149 VAL A N   1 
ATOM   1511 C  CA  . VAL A 1 149 ? -15.814 -17.969 12.145  1.00 9.62  ? 149 VAL A CA  1 
ATOM   1512 C  C   . VAL A 1 149 ? -16.973 -18.922 12.290  1.00 10.82 ? 149 VAL A C   1 
ATOM   1513 O  O   . VAL A 1 149 ? -16.915 -19.889 13.071  1.00 13.36 ? 149 VAL A O   1 
ATOM   1514 C  CB  . VAL A 1 149 ? -14.617 -18.679 11.511  1.00 11.51 ? 149 VAL A CB  1 
ATOM   1515 C  CG1 . VAL A 1 149 ? -14.991 -19.408 10.220  1.00 14.34 ? 149 VAL A CG1 1 
ATOM   1516 C  CG2 . VAL A 1 149 ? -13.457 -17.695 11.281  1.00 13.03 ? 149 VAL A CG2 1 
ATOM   1517 N  N   . GLY A 1 150 ? -18.036 -18.653 11.577  1.00 10.81 ? 150 GLY A N   1 
ATOM   1518 C  CA  . GLY A 1 150 ? -19.211 -19.503 11.571  1.00 13.38 ? 150 GLY A CA  1 
ATOM   1519 C  C   . GLY A 1 150 ? -20.081 -19.025 10.459  1.00 11.82 ? 150 GLY A C   1 
ATOM   1520 O  O   . GLY A 1 150 ? -19.697 -19.124 9.290   1.00 12.10 ? 150 GLY A O   1 
ATOM   1521 N  N   A SER A 1 151 ? -21.286 -18.544 10.783  0.50 13.33 ? 151 SER A N   1 
ATOM   1522 N  N   B SER A 1 151 ? -21.267 -18.533 10.817  0.50 13.46 ? 151 SER A N   1 
ATOM   1523 C  CA  A SER A 1 151 ? -22.180 -17.983 9.750   0.50 15.20 ? 151 SER A CA  1 
ATOM   1524 C  CA  B SER A 1 151 ? -22.141 -17.898 9.834   0.50 12.94 ? 151 SER A CA  1 
ATOM   1525 C  C   A SER A 1 151 ? -21.677 -16.625 9.245   0.50 13.19 ? 151 SER A C   1 
ATOM   1526 C  C   B SER A 1 151 ? -21.490 -16.677 9.184   0.50 10.02 ? 151 SER A C   1 
ATOM   1527 O  O   A SER A 1 151 ? -21.094 -15.836 10.019  0.50 10.00 ? 151 SER A O   1 
ATOM   1528 O  O   B SER A 1 151 ? -20.637 -16.021 9.812   0.50 10.01 ? 151 SER A O   1 
ATOM   1529 C  CB  A SER A 1 151 ? -23.603 -17.856 10.292  0.50 18.70 ? 151 SER A CB  1 
ATOM   1530 C  CB  B SER A 1 151 ? -23.500 -17.586 10.473  0.50 16.53 ? 151 SER A CB  1 
ATOM   1531 O  OG  A SER A 1 151 ? -23.610 -16.983 11.410  0.50 21.17 ? 151 SER A OG  1 
ATOM   1532 O  OG  B SER A 1 151 ? -24.082 -18.751 11.038  0.50 20.14 ? 151 SER A OG  1 
ATOM   1533 N  N   . ALA A 1 152 ? -21.919 -16.309 7.970   1.00 12.00 ? 152 ALA A N   1 
ATOM   1534 C  CA  . ALA A 1 152 ? -21.506 -15.028 7.365   1.00 12.31 ? 152 ALA A CA  1 
ATOM   1535 C  C   . ALA A 1 152 ? -22.148 -13.856 8.077   1.00 11.58 ? 152 ALA A C   1 
ATOM   1536 O  O   . ALA A 1 152 ? -23.314 -13.908 8.492   1.00 13.36 ? 152 ALA A O   1 
ATOM   1537 C  CB  . ALA A 1 152 ? -21.901 -14.995 5.882   1.00 14.94 ? 152 ALA A CB  1 
ATOM   1538 N  N   . LYS A 1 153 ? -21.429 -12.710 8.027   1.00 12.17 ? 153 LYS A N   1 
ATOM   1539 C  CA  . LYS A 1 153 ? -21.983 -11.446 8.488   1.00 12.45 ? 153 LYS A CA  1 
ATOM   1540 C  C   . LYS A 1 153 ? -22.432 -10.680 7.237   1.00 12.32 ? 153 LYS A C   1 
ATOM   1541 O  O   . LYS A 1 153 ? -21.566 -10.231 6.413   1.00 12.23 ? 153 LYS A O   1 
ATOM   1542 C  CB  . LYS A 1 153 ? -20.920 -10.653 9.218   1.00 12.90 ? 153 LYS A CB  1 
ATOM   1543 C  CG  . LYS A 1 153 ? -21.431 -9.401  9.913   1.00 15.19 ? 153 LYS A CG  1 
ATOM   1544 C  CD  . LYS A 1 153 ? -22.362 -9.747  11.040  1.00 16.81 ? 153 LYS A CD  1 
ATOM   1545 C  CE  . LYS A 1 153 ? -22.513 -8.517  11.897  1.00 21.62 ? 153 LYS A CE  1 
ATOM   1546 N  NZ  . LYS A 1 153 ? -23.516 -8.863  12.885  1.00 22.00 ? 153 LYS A NZ  1 
ATOM   1547 N  N   . PRO A 1 154 ? -23.743 -10.549 6.989   1.00 12.92 ? 154 PRO A N   1 
ATOM   1548 C  CA  . PRO A 1 154 ? -24.150 -9.945  5.705   1.00 15.83 ? 154 PRO A CA  1 
ATOM   1549 C  C   . PRO A 1 154 ? -23.625 -8.514  5.499   1.00 13.89 ? 154 PRO A C   1 
ATOM   1550 O  O   . PRO A 1 154 ? -23.209 -8.133  4.439   1.00 17.15 ? 154 PRO A O   1 
ATOM   1551 C  CB  . PRO A 1 154 ? -25.703 -9.987  5.762   1.00 15.43 ? 154 PRO A CB  1 
ATOM   1552 C  CG  . PRO A 1 154 ? -26.044 -11.066 6.782   1.00 19.84 ? 154 PRO A CG  1 
ATOM   1553 C  CD  . PRO A 1 154 ? -24.891 -11.111 7.739   1.00 14.02 ? 154 PRO A CD  1 
ATOM   1554 N  N   . GLY A 1 155 ? -23.494 -7.807  6.630   1.00 14.68 ? 155 GLY A N   1 
ATOM   1555 C  CA  . GLY A 1 155 ? -23.082 -6.393  6.562   1.00 16.50 ? 155 GLY A CA  1 
ATOM   1556 C  C   . GLY A 1 155 ? -21.602 -6.241  6.274   1.00 14.67 ? 155 GLY A C   1 
ATOM   1557 O  O   . GLY A 1 155 ? -21.144 -5.131  6.039   1.00 17.28 ? 155 GLY A O   1 
ATOM   1558 N  N   A LEU A 1 156 ? -20.909 -7.319  6.510   0.50 13.27 ? 156 LEU A N   1 
ATOM   1559 N  N   B LEU A 1 156 ? -20.810 -7.337  6.214   0.50 13.23 ? 156 LEU A N   1 
ATOM   1560 C  CA  A LEU A 1 156 ? -19.565 -7.305  6.199   0.50 11.51 ? 156 LEU A CA  1 
ATOM   1561 C  CA  B LEU A 1 156 ? -19.346 -7.319  5.851   0.50 12.33 ? 156 LEU A CA  1 
ATOM   1562 C  C   A LEU A 1 156 ? -19.412 -7.545  4.711   0.50 10.22 ? 156 LEU A C   1 
ATOM   1563 C  C   B LEU A 1 156 ? -18.979 -7.562  4.362   0.50 11.81 ? 156 LEU A C   1 
ATOM   1564 O  O   A LEU A 1 156 ? -18.359 -7.240  4.160   0.50 10.97 ? 156 LEU A O   1 
ATOM   1565 O  O   B LEU A 1 156 ? -17.832 -7.319  3.900   0.50 11.17 ? 156 LEU A O   1 
ATOM   1566 C  CB  A LEU A 1 156 ? -18.828 -8.346  7.083   0.50 12.45 ? 156 LEU A CB  1 
ATOM   1567 C  CB  B LEU A 1 156 ? -18.539 -8.366  6.687   0.50 10.02 ? 156 LEU A CB  1 
ATOM   1568 C  CG  A LEU A 1 156 ? -17.319 -8.373  6.849   0.50 11.06 ? 156 LEU A CG  1 
ATOM   1569 C  CG  B LEU A 1 156 ? -17.028 -8.551  6.489   0.50 9.28  ? 156 LEU A CG  1 
ATOM   1570 C  CD1 A LEU A 1 156 ? -16.649 -7.019  7.183   0.50 11.33 ? 156 LEU A CD1 1 
ATOM   1571 C  CD1 B LEU A 1 156 ? -16.211 -7.281  6.840   0.50 9.41  ? 156 LEU A CD1 1 
ATOM   1572 C  CD2 A LEU A 1 156 ? -16.719 -9.505  7.678   0.50 10.88 ? 156 LEU A CD2 1 
ATOM   1573 C  CD2 B LEU A 1 156 ? -16.473 -9.724  7.308   0.50 10.65 ? 156 LEU A CD2 1 
ATOM   1574 N  N   A GLN A 1 157 ? -20.442 -8.063  4.020   0.50 10.09 ? 157 GLN A N   1 
ATOM   1575 N  N   B GLN A 1 157 ? -19.913 -8.140  3.613   0.50 9.68  ? 157 GLN A N   1 
ATOM   1576 C  CA  A GLN A 1 157 ? -20.221 -8.552  2.643   0.50 9.65  ? 157 GLN A CA  1 
ATOM   1577 C  CA  B GLN A 1 157 ? -19.535 -8.669  2.314   0.50 9.21  ? 157 GLN A CA  1 
ATOM   1578 C  C   A GLN A 1 157 ? -19.822 -7.439  1.705   0.50 9.03  ? 157 GLN A C   1 
ATOM   1579 C  C   B GLN A 1 157 ? -19.082 -7.525  1.372   0.50 10.04 ? 157 GLN A C   1 
ATOM   1580 O  O   A GLN A 1 157 ? -18.933 -7.638  0.877   0.50 10.12 ? 157 GLN A O   1 
ATOM   1581 O  O   B GLN A 1 157 ? -18.210 -7.728  0.545   0.50 9.39  ? 157 GLN A O   1 
ATOM   1582 C  CB  A GLN A 1 157 ? -21.430 -9.306  2.094   0.50 13.42 ? 157 GLN A CB  1 
ATOM   1583 C  CB  B GLN A 1 157 ? -20.714 -9.436  1.723   0.50 10.39 ? 157 GLN A CB  1 
ATOM   1584 C  CG  A GLN A 1 157 ? -21.215 -10.157 0.865   0.50 13.25 ? 157 GLN A CG  1 
ATOM   1585 C  CG  B GLN A 1 157 ? -20.330 -10.171 0.454   0.50 10.64 ? 157 GLN A CG  1 
ATOM   1586 C  CD  A GLN A 1 157 ? -20.087 -11.137 1.019   0.50 11.61 ? 157 GLN A CD  1 
ATOM   1587 C  CD  B GLN A 1 157 ? -19.234 -11.201 0.635   0.50 10.97 ? 157 GLN A CD  1 
ATOM   1588 O  OE1 A GLN A 1 157 ? -19.838 -11.703 2.111   0.50 12.51 ? 157 GLN A OE1 1 
ATOM   1589 O  OE1 B GLN A 1 157 ? -18.500 -11.480 -0.309  0.50 14.15 ? 157 GLN A OE1 1 
ATOM   1590 N  NE2 A GLN A 1 157 ? -19.394 -11.365 -0.083  0.50 14.82 ? 157 GLN A NE2 1 
ATOM   1591 N  NE2 B GLN A 1 157 ? -19.096 -11.759 1.822   0.50 10.62 ? 157 GLN A NE2 1 
ATOM   1592 N  N   A LYS A 1 158 ? -20.426 -6.249  1.809   0.50 9.80  ? 158 LYS A N   1 
ATOM   1593 N  N   B LYS A 1 158 ? -19.642 -6.327  1.485   0.50 8.49  ? 158 LYS A N   1 
ATOM   1594 C  CA  A LYS A 1 158 ? -19.941 -5.146  0.949   0.50 9.83  ? 158 LYS A CA  1 
ATOM   1595 C  CA  B LYS A 1 158 ? -19.305 -5.225  0.591   0.50 10.86 ? 158 LYS A CA  1 
ATOM   1596 C  C   A LYS A 1 158 ? -18.458 -4.872  1.066   0.50 9.57  ? 158 LYS A C   1 
ATOM   1597 C  C   B LYS A 1 158 ? -17.771 -4.858  0.776   0.50 10.67 ? 158 LYS A C   1 
ATOM   1598 O  O   A LYS A 1 158 ? -17.825 -4.485  0.092   0.50 10.84 ? 158 LYS A O   1 
ATOM   1599 O  O   B LYS A 1 158 ? -17.077 -4.490  -0.170  0.50 9.80  ? 158 LYS A O   1 
ATOM   1600 C  CB  A LYS A 1 158 ? -20.657 -3.821  1.203   0.50 13.31 ? 158 LYS A CB  1 
ATOM   1601 C  CB  B LYS A 1 158 ? -20.306 -4.060  0.741   0.50 10.82 ? 158 LYS A CB  1 
ATOM   1602 C  CG  A LYS A 1 158 ? -20.179 -2.785  0.188   0.50 16.30 ? 158 LYS A CG  1 
ATOM   1603 C  CG  B LYS A 1 158 ? -21.769 -4.287  0.214   0.50 15.68 ? 158 LYS A CG  1 
ATOM   1604 C  CD  A LYS A 1 158 ? -21.054 -1.531  0.338   0.50 16.75 ? 158 LYS A CD  1 
ATOM   1605 C  CD  B LYS A 1 158 ? -22.678 -3.054  0.188   0.50 20.01 ? 158 LYS A CD  1 
ATOM   1606 C  CE  A LYS A 1 158 ? -20.558 -0.243  -0.363  0.50 22.55 ? 158 LYS A CE  1 
ATOM   1607 C  CE  B LYS A 1 158 ? -24.176 -3.326  -0.060  0.50 20.38 ? 158 LYS A CE  1 
ATOM   1608 N  NZ  A LYS A 1 158 ? -21.119 -0.263  -1.731  0.50 21.70 ? 158 LYS A NZ  1 
ATOM   1609 N  NZ  B LYS A 1 158 ? -24.885 -2.016  -0.322  0.50 23.72 ? 158 LYS A NZ  1 
ATOM   1610 N  N   A VAL A 1 159 ? -17.919 -5.004  2.275   0.50 8.36  ? 159 VAL A N   1 
ATOM   1611 N  N   B VAL A 1 159 ? -17.258 -5.000  2.000   0.50 9.91  ? 159 VAL A N   1 
ATOM   1612 C  CA  A VAL A 1 159 ? -16.525 -4.765  2.478   0.50 8.33  ? 159 VAL A CA  1 
ATOM   1613 C  CA  B VAL A 1 159 ? -15.826 -4.815  2.275   0.50 9.17  ? 159 VAL A CA  1 
ATOM   1614 C  C   A VAL A 1 159 ? -15.719 -5.874  1.844   0.50 9.03  ? 159 VAL A C   1 
ATOM   1615 C  C   B VAL A 1 159 ? -14.982 -5.910  1.622   0.50 10.95 ? 159 VAL A C   1 
ATOM   1616 O  O   A VAL A 1 159 ? -14.764 -5.606  1.118   0.50 9.12  ? 159 VAL A O   1 
ATOM   1617 O  O   B VAL A 1 159 ? -14.042 -5.656  0.841   0.50 10.92 ? 159 VAL A O   1 
ATOM   1618 C  CB  A VAL A 1 159 ? -16.191 -4.697  3.969   0.50 9.65  ? 159 VAL A CB  1 
ATOM   1619 C  CB  B VAL A 1 159 ? -15.579 -4.863  3.787   0.50 10.49 ? 159 VAL A CB  1 
ATOM   1620 C  CG1 A VAL A 1 159 ? -14.681 -4.626  4.134   0.50 11.29 ? 159 VAL A CG1 1 
ATOM   1621 C  CG1 B VAL A 1 159 ? -14.085 -4.920  4.064   0.50 12.48 ? 159 VAL A CG1 1 
ATOM   1622 C  CG2 A VAL A 1 159 ? -16.824 -3.472  4.568   0.50 12.74 ? 159 VAL A CG2 1 
ATOM   1623 C  CG2 B VAL A 1 159 ? -16.295 -3.715  4.491   0.50 14.24 ? 159 VAL A CG2 1 
ATOM   1624 N  N   A VAL A 1 160 ? -16.073 -7.131  2.084   0.50 8.69  ? 160 VAL A N   1 
ATOM   1625 N  N   B VAL A 1 160 ? -15.332 -7.162  1.925   0.50 8.43  ? 160 VAL A N   1 
ATOM   1626 C  CA  A VAL A 1 160 ? -15.335 -8.212  1.472   0.50 10.54 ? 160 VAL A CA  1 
ATOM   1627 C  CA  B VAL A 1 160 ? -14.490 -8.228  1.438   0.50 9.69  ? 160 VAL A CA  1 
ATOM   1628 C  C   A VAL A 1 160 ? -15.285 -8.110  -0.054  0.50 10.34 ? 160 VAL A C   1 
ATOM   1629 C  C   B VAL A 1 160 ? -14.481 -8.256  -0.100  0.50 9.62  ? 160 VAL A C   1 
ATOM   1630 O  O   A VAL A 1 160 ? -14.289 -8.453  -0.643  0.50 12.10 ? 160 VAL A O   1 
ATOM   1631 O  O   B VAL A 1 160 ? -13.476 -8.567  -0.750  0.50 11.04 ? 160 VAL A O   1 
ATOM   1632 C  CB  A VAL A 1 160 ? -15.958 -9.587  1.855   0.50 13.34 ? 160 VAL A CB  1 
ATOM   1633 C  CB  B VAL A 1 160 ? -14.898 -9.582  2.084   0.50 11.28 ? 160 VAL A CB  1 
ATOM   1634 C  CG1 A VAL A 1 160 ? -15.466 -10.772 0.999   0.50 15.23 ? 160 VAL A CG1 1 
ATOM   1635 C  CG1 B VAL A 1 160 ? -14.646 -9.465  3.568   0.50 16.25 ? 160 VAL A CG1 1 
ATOM   1636 C  CG2 A VAL A 1 160 ? -15.819 -9.863  3.343   0.50 13.58 ? 160 VAL A CG2 1 
ATOM   1637 C  CG2 B VAL A 1 160 ? -16.367 -9.990  1.861   0.50 14.47 ? 160 VAL A CG2 1 
ATOM   1638 N  N   A ASP A 1 161 ? -16.358 -7.658  -0.686  0.50 11.42 ? 161 ASP A N   1 
ATOM   1639 N  N   B ASP A 1 161 ? -15.601 -7.900  -0.692  0.50 12.05 ? 161 ASP A N   1 
ATOM   1640 C  CA  A ASP A 1 161 ? -16.368 -7.705  -2.153  0.50 13.77 ? 161 ASP A CA  1 
ATOM   1641 C  CA  B ASP A 1 161 ? -15.705 -8.029  -2.130  0.50 14.43 ? 161 ASP A CA  1 
ATOM   1642 C  C   A ASP A 1 161 ? -15.512 -6.662  -2.876  0.50 13.99 ? 161 ASP A C   1 
ATOM   1643 C  C   B ASP A 1 161 ? -14.911 -6.941  -2.800  0.50 14.45 ? 161 ASP A C   1 
ATOM   1644 O  O   A ASP A 1 161 ? -15.448 -6.743  -4.097  0.50 16.64 ? 161 ASP A O   1 
ATOM   1645 O  O   B ASP A 1 161 ? -14.471 -7.140  -3.943  0.50 13.50 ? 161 ASP A O   1 
ATOM   1646 C  CB  A ASP A 1 161 ? -17.801 -7.747  -2.633  0.50 17.44 ? 161 ASP A CB  1 
ATOM   1647 C  CB  B ASP A 1 161 ? -17.128 -7.905  -2.515  0.50 15.48 ? 161 ASP A CB  1 
ATOM   1648 C  CG  A ASP A 1 161 ? -18.335 -9.143  -2.619  0.50 15.16 ? 161 ASP A CG  1 
ATOM   1649 C  CG  B ASP A 1 161 ? -17.883 -9.205  -2.383  0.50 20.38 ? 161 ASP A CG  1 
ATOM   1650 O  OD1 A ASP A 1 161 ? -17.501 -10.087 -2.779  0.50 16.38 ? 161 ASP A OD1 1 
ATOM   1651 O  OD1 B ASP A 1 161 ? -17.293 -10.332 -2.417  0.50 22.49 ? 161 ASP A OD1 1 
ATOM   1652 O  OD2 A ASP A 1 161 ? -19.560 -9.293  -2.449  0.50 20.53 ? 161 ASP A OD2 1 
ATOM   1653 O  OD2 B ASP A 1 161 ? -19.114 -9.107  -2.248  0.50 25.33 ? 161 ASP A OD2 1 
ATOM   1654 N  N   . VAL A 1 162 ? -14.764 -5.782  -2.175  1.00 16.12 ? 162 VAL A N   1 
ATOM   1655 C  CA  . VAL A 1 162 ? -13.848 -4.789  -2.791  1.00 18.47 ? 162 VAL A CA  1 
ATOM   1656 C  C   . VAL A 1 162 ? -12.368 -5.081  -2.547  1.00 16.30 ? 162 VAL A C   1 
ATOM   1657 O  O   . VAL A 1 162 ? -11.550 -4.396  -3.097  1.00 16.75 ? 162 VAL A O   1 
ATOM   1658 C  CB  . VAL A 1 162 ? -14.163 -3.384  -2.386  1.00 23.51 ? 162 VAL A CB  1 
ATOM   1659 C  CG1 . VAL A 1 162 ? -15.539 -3.076  -2.934  1.00 27.86 ? 162 VAL A CG1 1 
ATOM   1660 C  CG2 . VAL A 1 162 ? -13.821 -3.025  -0.939  1.00 19.05 ? 162 VAL A CG2 1 
ATOM   1661 N  N   . LEU A 1 163 ? -12.051 -6.055  -1.694  1.00 14.91 ? 163 LEU A N   1 
ATOM   1662 C  CA  . LEU A 1 163 ? -10.689 -6.245  -1.345  1.00 14.19 ? 163 LEU A CA  1 
ATOM   1663 C  C   . LEU A 1 163 ? -9.794  -6.599  -2.548  1.00 14.19 ? 163 LEU A C   1 
ATOM   1664 O  O   . LEU A 1 163 ? -8.577  -6.316  -2.532  1.00 16.00 ? 163 LEU A O   1 
ATOM   1665 C  CB  . LEU A 1 163 ? -10.541 -7.241  -0.241  1.00 14.56 ? 163 LEU A CB  1 
ATOM   1666 C  CG  . LEU A 1 163 ? -11.178 -6.839  1.102   1.00 13.49 ? 163 LEU A CG  1 
ATOM   1667 C  CD1 . LEU A 1 163 ? -10.951 -7.952  2.153   1.00 14.12 ? 163 LEU A CD1 1 
ATOM   1668 C  CD2 . LEU A 1 163 ? -10.632 -5.497  1.589   1.00 14.47 ? 163 LEU A CD2 1 
ATOM   1669 N  N   . ASP A 1 164 ? -10.340 -7.315  -3.523  1.00 17.08 ? 164 ASP A N   1 
ATOM   1670 C  CA  . ASP A 1 164 ? -9.487  -7.633  -4.670  1.00 17.55 ? 164 ASP A CA  1 
ATOM   1671 C  C   . ASP A 1 164 ? -9.031  -6.396  -5.421  1.00 17.97 ? 164 ASP A C   1 
ATOM   1672 O  O   . ASP A 1 164 ? -8.071  -6.507  -6.186  1.00 21.84 ? 164 ASP A O   1 
ATOM   1673 C  CB  . ASP A 1 164 ? -10.203 -8.531  -5.663  1.00 22.23 ? 164 ASP A CB  1 
ATOM   1674 C  CG  . ASP A 1 164 ? -11.162 -7.754  -6.437  1.00 23.97 ? 164 ASP A CG  1 
ATOM   1675 O  OD1 . ASP A 1 164 ? -12.088 -7.236  -5.797  1.00 32.20 ? 164 ASP A OD1 1 
ATOM   1676 O  OD2 . ASP A 1 164 ? -10.979 -7.594  -7.702  1.00 42.36 ? 164 ASP A OD2 1 
ATOM   1677 N  N   A SER A 1 165 ? -9.934  -5.375  -5.352  0.50 15.87 ? 165 SER A N   1 
ATOM   1678 N  N   B SER A 1 165 ? -9.456  -5.194  -5.128  0.50 15.24 ? 165 SER A N   1 
ATOM   1679 C  CA  A SER A 1 165 ? -9.750  -3.983  -5.899  0.50 13.44 ? 165 SER A CA  1 
ATOM   1680 C  CA  B SER A 1 165 ? -8.854  -4.063  -5.843  0.50 12.34 ? 165 SER A CA  1 
ATOM   1681 C  C   A SER A 1 165 ? -8.752  -3.138  -5.098  0.50 9.95  ? 165 SER A C   1 
ATOM   1682 C  C   B SER A 1 165 ? -7.705  -3.339  -5.114  0.50 10.30 ? 165 SER A C   1 
ATOM   1683 O  O   A SER A 1 165 ? -8.269  -2.150  -5.611  0.50 10.60 ? 165 SER A O   1 
ATOM   1684 O  O   B SER A 1 165 ? -7.169  -2.347  -5.618  0.50 11.01 ? 165 SER A O   1 
ATOM   1685 C  CB  A SER A 1 165 ? -11.071 -3.219  -6.127  0.50 16.00 ? 165 SER A CB  1 
ATOM   1686 C  CB  B SER A 1 165 ? -9.995  -3.138  -6.119  0.50 12.86 ? 165 SER A CB  1 
ATOM   1687 O  OG  A SER A 1 165 ? -11.504 -2.444  -5.011  0.50 13.33 ? 165 SER A OG  1 
ATOM   1688 O  OG  B SER A 1 165 ? -10.439 -2.532  -4.923  0.50 12.70 ? 165 SER A OG  1 
ATOM   1689 N  N   A ILE A 1 166 ? -8.446  -3.518  -3.846  0.50 8.16  ? 166 ILE A N   1 
ATOM   1690 N  N   B ILE A 1 166 ? -7.420  -3.765  -3.883  0.50 8.09  ? 166 ILE A N   1 
ATOM   1691 C  CA  A ILE A 1 166 ? -7.401  -2.879  -3.060  0.50 8.51  ? 166 ILE A CA  1 
ATOM   1692 C  CA  B ILE A 1 166 ? -6.394  -3.180  -3.046  0.50 8.75  ? 166 ILE A CA  1 
ATOM   1693 C  C   A ILE A 1 166 ? -6.406  -3.931  -2.533  0.50 7.18  ? 166 ILE A C   1 
ATOM   1694 C  C   B ILE A 1 166 ? -5.427  -4.233  -2.487  0.50 7.20  ? 166 ILE A C   1 
ATOM   1695 O  O   A ILE A 1 166 ? -6.000  -3.945  -1.392  0.50 7.52  ? 166 ILE A O   1 
ATOM   1696 O  O   B ILE A 1 166 ? -5.060  -4.237  -1.314  0.50 8.22  ? 166 ILE A O   1 
ATOM   1697 C  CB  A ILE A 1 166 ? -8.012  -2.039  -1.912  0.50 8.35  ? 166 ILE A CB  1 
ATOM   1698 C  CB  B ILE A 1 166 ? -7.034  -2.317  -1.918  0.50 7.70  ? 166 ILE A CB  1 
ATOM   1699 C  CG1 A ILE A 1 166 ? -8.907  -2.885  -0.974  0.50 8.11  ? 166 ILE A CG1 1 
ATOM   1700 C  CG1 B ILE A 1 166 ? -7.958  -3.131  -1.019  0.50 9.92  ? 166 ILE A CG1 1 
ATOM   1701 C  CG2 A ILE A 1 166 ? -8.753  -0.858  -2.487  0.50 8.60  ? 166 ILE A CG2 1 
ATOM   1702 C  CG2 B ILE A 1 166 ? -7.712  -1.097  -2.544  0.50 8.97  ? 166 ILE A CG2 1 
ATOM   1703 C  CD1 A ILE A 1 166 ? -8.986  -2.274  0.438   0.50 9.42  ? 166 ILE A CD1 1 
ATOM   1704 C  CD1 B ILE A 1 166 ? -8.110  -2.462  0.348   0.50 9.43  ? 166 ILE A CD1 1 
ATOM   1705 N  N   A LYS A 1 167 ? -5.938  -4.773  -3.450  0.50 9.31  ? 167 LYS A N   1 
ATOM   1706 N  N   B LYS A 1 167 ? -5.035  -5.146  -3.372  0.50 8.33  ? 167 LYS A N   1 
ATOM   1707 C  CA  A LYS A 1 167 ? -5.221  -5.984  -3.018  0.50 8.42  ? 167 LYS A CA  1 
ATOM   1708 C  CA  B LYS A 1 167 ? -4.274  -6.306  -2.971  0.50 8.02  ? 167 LYS A CA  1 
ATOM   1709 C  C   A LYS A 1 167 ? -3.887  -5.594  -2.373  0.50 7.91  ? 167 LYS A C   1 
ATOM   1710 C  C   B LYS A 1 167 ? -2.971  -5.939  -2.237  0.50 7.71  ? 167 LYS A C   1 
ATOM   1711 O  O   A LYS A 1 167 ? -3.483  -6.253  -1.414  0.50 9.65  ? 167 LYS A O   1 
ATOM   1712 O  O   B LYS A 1 167 ? -2.591  -6.589  -1.237  0.50 9.36  ? 167 LYS A O   1 
ATOM   1713 C  CB  A LYS A 1 167 ? -4.939  -6.910  -4.224  0.50 10.91 ? 167 LYS A CB  1 
ATOM   1714 C  CB  B LYS A 1 167 ? -3.955  -7.226  -4.131  0.50 10.71 ? 167 LYS A CB  1 
ATOM   1715 C  CG  A LYS A 1 167 ? -4.116  -8.142  -3.840  0.50 12.62 ? 167 LYS A CG  1 
ATOM   1716 C  CG  B LYS A 1 167 ? -3.286  -8.535  -3.696  0.50 12.01 ? 167 LYS A CG  1 
ATOM   1717 C  CD  A LYS A 1 167 ? -3.947  -9.165  -4.982  0.50 15.97 ? 167 LYS A CD  1 
ATOM   1718 C  CD  B LYS A 1 167 ? -2.979  -9.340  -4.980  0.50 16.22 ? 167 LYS A CD  1 
ATOM   1719 C  CE  A LYS A 1 167 ? -3.080  -10.325 -4.618  0.50 18.66 ? 167 LYS A CE  1 
ATOM   1720 C  CE  B LYS A 1 167 ? -2.295  -10.642 -4.657  0.50 20.14 ? 167 LYS A CE  1 
ATOM   1721 N  NZ  A LYS A 1 167 ? -3.292  -11.269 -5.760  0.50 24.03 ? 167 LYS A NZ  1 
ATOM   1722 N  NZ  B LYS A 1 167 ? -2.251  -11.574 -5.847  0.50 22.29 ? 167 LYS A NZ  1 
ATOM   1723 N  N   A THR A 1 168 ? -3.238  -4.537  -2.884  0.50 7.96  ? 168 THR A N   1 
ATOM   1724 N  N   B THR A 1 168 ? -2.251  -4.933  -2.754  0.50 8.56  ? 168 THR A N   1 
ATOM   1725 C  CA  A THR A 1 168 ? -1.895  -4.164  -2.507  0.50 8.64  ? 168 THR A CA  1 
ATOM   1726 C  CA  B THR A 1 168 ? -0.893  -4.664  -2.298  0.50 8.94  ? 168 THR A CA  1 
ATOM   1727 C  C   A THR A 1 168 ? -1.816  -2.792  -1.805  0.50 8.18  ? 168 THR A C   1 
ATOM   1728 C  C   B THR A 1 168 ? -0.838  -3.269  -1.660  0.50 7.45  ? 168 THR A C   1 
ATOM   1729 O  O   A THR A 1 168 ? -2.707  -1.919  -1.964  0.50 8.59  ? 168 THR A O   1 
ATOM   1730 O  O   B THR A 1 168 ? -1.706  -2.392  -1.852  0.50 8.76  ? 168 THR A O   1 
ATOM   1731 C  CB  A THR A 1 168 ? -0.945  -4.189  -3.730  0.50 9.80  ? 168 THR A CB  1 
ATOM   1732 C  CB  B THR A 1 168 ? 0.043   -4.744  -3.501  0.50 9.22  ? 168 THR A CB  1 
ATOM   1733 O  OG1 A THR A 1 168 ? -1.559  -3.445  -4.800  0.50 9.52  ? 168 THR A OG1 1 
ATOM   1734 O  OG1 B THR A 1 168 ? -0.494  -4.016  -4.596  0.50 9.73  ? 168 THR A OG1 1 
ATOM   1735 C  CG2 A THR A 1 168 ? -0.724  -5.643  -4.183  0.50 11.86 ? 168 THR A CG2 1 
ATOM   1736 C  CG2 B THR A 1 168 ? 0.291   -6.190  -3.927  0.50 11.54 ? 168 THR A CG2 1 
ATOM   1737 N  N   A LYS A 1 169 ? -0.739  -2.636  -1.039  0.50 8.85  ? 169 LYS A N   1 
ATOM   1738 N  N   B LYS A 1 169 ? 0.226   -3.090  -0.900  0.50 8.91  ? 169 LYS A N   1 
ATOM   1739 C  CA  A LYS A 1 169 ? -0.484  -1.428  -0.311  0.50 8.27  ? 169 LYS A CA  1 
ATOM   1740 C  CA  B LYS A 1 169 ? 0.515   -1.860  -0.170  0.50 8.99  ? 169 LYS A CA  1 
ATOM   1741 C  C   A LYS A 1 169 ? -0.611  -0.181  -1.172  0.50 8.34  ? 169 LYS A C   1 
ATOM   1742 C  C   B LYS A 1 169 ? 0.436   -0.625  -1.072  0.50 8.25  ? 169 LYS A C   1 
ATOM   1743 O  O   A LYS A 1 169 ? -0.037  -0.079  -2.203  0.50 9.65  ? 169 LYS A O   1 
ATOM   1744 O  O   B LYS A 1 169 ? 1.030   -0.616  -2.170  0.50 10.41 ? 169 LYS A O   1 
ATOM   1745 C  CB  A LYS A 1 169 ? 0.921   -1.539  0.291   0.50 10.22 ? 169 LYS A CB  1 
ATOM   1746 C  CB  B LYS A 1 169 ? 1.924   -1.914  0.425   0.50 10.71 ? 169 LYS A CB  1 
ATOM   1747 C  CG  A LYS A 1 169 ? 1.364   -0.348  1.136   0.50 11.03 ? 169 LYS A CG  1 
ATOM   1748 C  CG  B LYS A 1 169 ? 2.259   -0.666  1.220   0.50 10.10 ? 169 LYS A CG  1 
ATOM   1749 C  CD  A LYS A 1 169 ? 2.768   -0.519  1.799   0.50 13.52 ? 169 LYS A CD  1 
ATOM   1750 C  CD  B LYS A 1 169 ? 3.652   -0.709  1.872   0.50 13.51 ? 169 LYS A CD  1 
ATOM   1751 C  CE  A LYS A 1 169 ? 3.663   0.741   1.716   0.50 22.53 ? 169 LYS A CE  1 
ATOM   1752 C  CE  B LYS A 1 169 ? 3.813   0.496   2.825   0.50 22.11 ? 169 LYS A CE  1 
ATOM   1753 N  NZ  A LYS A 1 169 ? 5.098   0.590   2.094   0.50 32.96 ? 169 LYS A NZ  1 
ATOM   1754 N  NZ  B LYS A 1 169 ? 4.805   0.303   3.922   0.50 32.45 ? 169 LYS A NZ  1 
ATOM   1755 N  N   A GLY A 1 170 ? -1.389  0.761   -0.660  0.50 8.30  ? 170 GLY A N   1 
ATOM   1756 N  N   B GLY A 1 170 ? -0.356  0.371   -0.648  0.50 9.21  ? 170 GLY A N   1 
ATOM   1757 C  CA  A GLY A 1 170 ? -1.580  2.060   -1.274  0.50 9.31  ? 170 GLY A CA  1 
ATOM   1758 C  CA  B GLY A 1 170 ? -0.379  1.641   -1.361  0.50 11.63 ? 170 GLY A CA  1 
ATOM   1759 C  C   A GLY A 1 170 ? -2.712  2.149   -2.270  0.50 10.05 ? 170 GLY A C   1 
ATOM   1760 C  C   B GLY A 1 170 ? -1.604  1.743   -2.245  0.50 9.03  ? 170 GLY A C   1 
ATOM   1761 O  O   A GLY A 1 170 ? -3.060  3.248   -2.777  0.50 11.90 ? 170 GLY A O   1 
ATOM   1762 O  O   B GLY A 1 170 ? -1.884  2.798   -2.712  0.50 12.71 ? 170 GLY A O   1 
ATOM   1763 N  N   A LYS A 1 171 ? -3.337  1.019   -2.528  0.50 8.82  ? 171 LYS A N   1 
ATOM   1764 N  N   B LYS A 1 171 ? -2.308  0.651   -2.510  0.50 9.48  ? 171 LYS A N   1 
ATOM   1765 C  CA  A LYS A 1 171 ? -4.546  1.006   -3.332  0.50 8.41  ? 171 LYS A CA  1 
ATOM   1766 C  CA  B LYS A 1 171 ? -3.517  0.702   -3.344  0.50 8.21  ? 171 LYS A CA  1 
ATOM   1767 C  C   A LYS A 1 171 ? -5.768  1.428   -2.542  0.50 9.33  ? 171 LYS A C   1 
ATOM   1768 C  C   B LYS A 1 171 ? -4.709  1.142   -2.519  0.50 8.06  ? 171 LYS A C   1 
ATOM   1769 O  O   A LYS A 1 171 ? -5.936  1.044   -1.383  0.50 8.99  ? 171 LYS A O   1 
ATOM   1770 O  O   B LYS A 1 171 ? -4.963  0.660   -1.408  0.50 11.03 ? 171 LYS A O   1 
ATOM   1771 C  CB  A LYS A 1 171 ? -4.824  -0.367  -3.988  0.50 9.93  ? 171 LYS A CB  1 
ATOM   1772 C  CB  B LYS A 1 171 ? -3.834  -0.667  -3.953  0.50 8.99  ? 171 LYS A CB  1 
ATOM   1773 C  CG  A LYS A 1 171 ? -3.731  -0.737  -4.957  0.50 14.03 ? 171 LYS A CG  1 
ATOM   1774 C  CG  B LYS A 1 171 ? -2.813  -1.111  -4.988  0.50 12.37 ? 171 LYS A CG  1 
ATOM   1775 C  CD  A LYS A 1 171 ? -4.136  -1.371  -6.293  0.50 19.67 ? 171 LYS A CD  1 
ATOM   1776 C  CD  B LYS A 1 171 ? -3.407  -2.189  -5.910  0.50 15.85 ? 171 LYS A CD  1 
ATOM   1777 C  CE  A LYS A 1 171 ? -3.082  -0.951  -7.313  0.50 28.02 ? 171 LYS A CE  1 
ATOM   1778 C  CE  B LYS A 1 171 ? -2.665  -2.529  -7.181  0.50 17.88 ? 171 LYS A CE  1 
ATOM   1779 N  NZ  A LYS A 1 171 ? -3.659  -0.601  -8.618  0.50 32.33 ? 171 LYS A NZ  1 
ATOM   1780 N  NZ  B LYS A 1 171 ? -3.568  -3.106  -8.222  0.50 30.81 ? 171 LYS A NZ  1 
ATOM   1781 N  N   A SER A 1 172 ? -6.599  2.250   -3.178  0.50 10.36 ? 172 SER A N   1 
ATOM   1782 N  N   B SER A 1 172 ? -5.471  2.062   -3.090  0.50 8.28  ? 172 SER A N   1 
ATOM   1783 C  CA  A SER A 1 172 ? -7.834  2.672   -2.536  0.50 10.74 ? 172 SER A CA  1 
ATOM   1784 C  CA  B SER A 1 172 ? -6.694  2.541   -2.499  0.50 7.79  ? 172 SER A CA  1 
ATOM   1785 C  C   A SER A 1 172 ? -8.997  2.562   -3.514  0.50 9.37  ? 172 SER A C   1 
ATOM   1786 C  C   B SER A 1 172 ? -7.792  2.623   -3.545  0.50 8.83  ? 172 SER A C   1 
ATOM   1787 O  O   A SER A 1 172 ? -8.811  2.494   -4.769  0.50 10.75 ? 172 SER A O   1 
ATOM   1788 O  O   B SER A 1 172 ? -7.544  2.545   -4.764  0.50 10.82 ? 172 SER A O   1 
ATOM   1789 C  CB  A SER A 1 172 ? -7.740  4.104   -1.977  0.50 10.90 ? 172 SER A CB  1 
ATOM   1790 C  CB  B SER A 1 172 ? -6.487  3.892   -1.819  0.50 9.93  ? 172 SER A CB  1 
ATOM   1791 O  OG  A SER A 1 172 ? -7.545  5.023   -3.064  0.50 13.76 ? 172 SER A OG  1 
ATOM   1792 O  OG  B SER A 1 172 ? -6.191  4.878   -2.778  0.50 10.95 ? 172 SER A OG  1 
ATOM   1793 N  N   A ALA A 1 173 ? -10.213 2.578   -2.961  0.50 9.66  ? 173 ALA A N   1 
ATOM   1794 N  N   B ALA A 1 173 ? -9.018  2.796   -3.057  0.50 10.15 ? 173 ALA A N   1 
ATOM   1795 C  CA  A ALA A 1 173 ? -11.391 2.588   -3.826  0.50 10.16 ? 173 ALA A CA  1 
ATOM   1796 C  CA  B ALA A 1 173 ? -10.180 2.934   -3.942  0.50 10.88 ? 173 ALA A CA  1 
ATOM   1797 C  C   A ALA A 1 173 ? -12.484 3.404   -3.183  0.50 10.24 ? 173 ALA A C   1 
ATOM   1798 C  C   B ALA A 1 173 ? -11.216 3.789   -3.222  0.50 9.39  ? 173 ALA A C   1 
ATOM   1799 O  O   A ALA A 1 173 ? -12.533 3.535   -1.948  0.50 10.18 ? 173 ALA A O   1 
ATOM   1800 O  O   B ALA A 1 173 ? -11.311 3.757   -1.994  0.50 10.79 ? 173 ALA A O   1 
ATOM   1801 C  CB  A ALA A 1 173 ? -11.865 1.177   -4.038  0.50 12.22 ? 173 ALA A CB  1 
ATOM   1802 C  CB  B ALA A 1 173 ? -10.770 1.574   -4.287  0.50 10.76 ? 173 ALA A CB  1 
ATOM   1803 N  N   A ASP A 1 174 ? -13.318 4.015   -3.985  0.50 9.63  ? 174 ASP A N   1 
ATOM   1804 N  N   B ASP A 1 174 ? -11.999 4.530   -3.960  0.50 10.05 ? 174 ASP A N   1 
ATOM   1805 C  CA  A ASP A 1 174 ? -14.422 4.677   -3.352  0.50 11.29 ? 174 ASP A CA  1 
ATOM   1806 C  CA  B ASP A 1 174 ? -13.152 5.123   -3.473  0.50 10.80 ? 174 ASP A CA  1 
ATOM   1807 C  C   A ASP A 1 174 ? -15.300 3.669   -2.601  0.50 12.01 ? 174 ASP A C   1 
ATOM   1808 C  C   B ASP A 1 174 ? -14.018 4.025   -2.814  0.50 13.03 ? 174 ASP A C   1 
ATOM   1809 O  O   A ASP A 1 174 ? -15.451 2.511   -2.979  0.50 15.14 ? 174 ASP A O   1 
ATOM   1810 O  O   B ASP A 1 174 ? -14.152 2.919   -3.334  0.50 13.31 ? 174 ASP A O   1 
ATOM   1811 C  CB  A ASP A 1 174 ? -15.140 5.734   -4.200  0.50 25.29 ? 174 ASP A CB  1 
ATOM   1812 C  CB  B ASP A 1 174 ? -13.962 5.782   -4.627  0.50 16.51 ? 174 ASP A CB  1 
ATOM   1813 C  CG  A ASP A 1 174 ? -15.092 5.429   -5.608  0.50 28.67 ? 174 ASP A CG  1 
ATOM   1814 C  CG  B ASP A 1 174 ? -13.327 7.034   -5.131  0.50 23.89 ? 174 ASP A CG  1 
ATOM   1815 O  OD1 A ASP A 1 174 ? -15.638 4.361   -5.926  0.50 42.17 ? 174 ASP A OD1 1 
ATOM   1816 O  OD1 B ASP A 1 174 ? -13.011 7.895   -4.303  0.50 29.50 ? 174 ASP A OD1 1 
ATOM   1817 O  OD2 A ASP A 1 174 ? -14.556 6.257   -6.394  0.50 32.89 ? 174 ASP A OD2 1 
ATOM   1818 O  OD2 B ASP A 1 174 ? -13.140 7.150   -6.350  0.50 34.16 ? 174 ASP A OD2 1 
ATOM   1819 N  N   A PHE A 1 175 ? -15.850 4.128   -1.493  0.50 11.00 ? 175 PHE A N   1 
ATOM   1820 N  N   B PHE A 1 175 ? -14.620 4.362   -1.676  0.50 10.98 ? 175 PHE A N   1 
ATOM   1821 C  CA  A PHE A 1 175 ? -16.618 3.246   -0.647  0.50 10.65 ? 175 PHE A CA  1 
ATOM   1822 C  CA  B PHE A 1 175 ? -15.463 3.374   -1.000  0.50 10.35 ? 175 PHE A CA  1 
ATOM   1823 C  C   A PHE A 1 175 ? -17.658 4.005   0.142   0.50 10.25 ? 175 PHE A C   1 
ATOM   1824 C  C   B PHE A 1 175 ? -16.603 4.077   -0.269  0.50 11.26 ? 175 PHE A C   1 
ATOM   1825 O  O   A PHE A 1 175 ? -17.676 4.083   1.316   0.50 13.36 ? 175 PHE A O   1 
ATOM   1826 O  O   B PHE A 1 175 ? -16.473 4.415   0.909   0.50 10.76 ? 175 PHE A O   1 
ATOM   1827 C  CB  A PHE A 1 175 ? -15.694 2.437   0.261   0.50 10.56 ? 175 PHE A CB  1 
ATOM   1828 C  CB  B PHE A 1 175 ? -14.624 2.513   -0.060  0.50 10.28 ? 175 PHE A CB  1 
ATOM   1829 C  CG  A PHE A 1 175 ? -16.285 1.152   0.721   0.50 11.81 ? 175 PHE A CG  1 
ATOM   1830 C  CG  B PHE A 1 175 ? -15.353 1.308   0.512   0.50 10.31 ? 175 PHE A CG  1 
ATOM   1831 C  CD1 A PHE A 1 175 ? -16.558 0.116   -0.166  0.50 14.64 ? 175 PHE A CD1 1 
ATOM   1832 C  CD1 B PHE A 1 175 ? -15.671 0.188   -0.242  0.50 13.19 ? 175 PHE A CD1 1 
ATOM   1833 C  CD2 A PHE A 1 175 ? -16.494 0.972   2.071   0.50 12.99 ? 175 PHE A CD2 1 
ATOM   1834 C  CD2 B PHE A 1 175 ? -15.703 1.292   1.845   0.50 13.77 ? 175 PHE A CD2 1 
ATOM   1835 C  CE1 A PHE A 1 175 ? -17.095 -1.074  0.268   0.50 16.91 ? 175 PHE A CE1 1 
ATOM   1836 C  CE1 B PHE A 1 175 ? -16.339 -0.892  0.310   0.50 14.10 ? 175 PHE A CE1 1 
ATOM   1837 C  CE2 A PHE A 1 175 ? -17.009 -0.225  2.534   0.50 15.24 ? 175 PHE A CE2 1 
ATOM   1838 C  CE2 B PHE A 1 175 ? -16.384 0.239   2.406   0.50 15.47 ? 175 PHE A CE2 1 
ATOM   1839 C  CZ  A PHE A 1 175 ? -17.272 -1.246  1.632   0.50 13.61 ? 175 PHE A CZ  1 
ATOM   1840 C  CZ  B PHE A 1 175 ? -16.686 -0.883  1.644   0.50 16.14 ? 175 PHE A CZ  1 
ATOM   1841 N  N   A THR A 1 176 ? -18.576 4.590   -0.603  0.50 11.45 ? 176 THR A N   1 
ATOM   1842 N  N   B THR A 1 176 ? -17.683 4.335   -0.974  0.50 11.88 ? 176 THR A N   1 
ATOM   1843 C  CA  A THR A 1 176 ? -19.639 5.385   -0.051  0.50 10.68 ? 176 THR A CA  1 
ATOM   1844 C  CA  B THR A 1 176 ? -18.766 5.171   -0.481  0.50 11.74 ? 176 THR A CA  1 
ATOM   1845 C  C   A THR A 1 176 ? -20.856 4.526   0.317   0.50 10.52 ? 176 THR A C   1 
ATOM   1846 C  C   B THR A 1 176 ? -19.995 4.416   -0.043  0.50 9.00  ? 176 THR A C   1 
ATOM   1847 O  O   A THR A 1 176 ? -21.079 3.392   -0.162  0.50 11.60 ? 176 THR A O   1 
ATOM   1848 O  O   B THR A 1 176 ? -20.199 3.256   -0.408  0.50 11.46 ? 176 THR A O   1 
ATOM   1849 C  CB  A THR A 1 176 ? -20.065 6.482   -1.093  0.50 10.05 ? 176 THR A CB  1 
ATOM   1850 C  CB  B THR A 1 176 ? -19.097 6.224   -1.589  0.50 11.78 ? 176 THR A CB  1 
ATOM   1851 O  OG1 A THR A 1 176 ? -20.364 5.870   -2.351  0.50 15.52 ? 176 THR A OG1 1 
ATOM   1852 O  OG1 B THR A 1 176 ? -19.513 5.532   -2.796  0.50 13.38 ? 176 THR A OG1 1 
ATOM   1853 C  CG2 A THR A 1 176 ? -18.963 7.507   -1.229  0.50 14.42 ? 176 THR A CG2 1 
ATOM   1854 C  CG2 B THR A 1 176 ? -17.855 7.127   -1.844  0.50 15.21 ? 176 THR A CG2 1 
ATOM   1855 N  N   A ASN A 1 177 ? -21.666 5.073   1.209   0.50 10.67 ? 177 ASN A N   1 
ATOM   1856 N  N   B ASN A 1 177 ? -20.747 5.085   0.783   0.50 10.29 ? 177 ASN A N   1 
ATOM   1857 C  CA  A ASN A 1 177 ? -22.929 4.487   1.566   0.50 10.83 ? 177 ASN A CA  1 
ATOM   1858 C  CA  B ASN A 1 177 ? -22.000 4.584   1.310   0.50 10.90 ? 177 ASN A CA  1 
ATOM   1859 C  C   A ASN A 1 177 ? -22.831 3.193   2.322   0.50 11.35 ? 177 ASN A C   1 
ATOM   1860 C  C   B ASN A 1 177 ? -21.905 3.261   2.067   0.50 11.06 ? 177 ASN A C   1 
ATOM   1861 O  O   A ASN A 1 177 ? -23.756 2.378   2.281   0.50 14.46 ? 177 ASN A O   1 
ATOM   1862 O  O   B ASN A 1 177 ? -22.865 2.491   2.066   0.50 12.89 ? 177 ASN A O   1 
ATOM   1863 C  CB  A ASN A 1 177 ? -23.724 4.352   0.300   0.50 13.06 ? 177 ASN A CB  1 
ATOM   1864 C  CB  B ASN A 1 177 ? -23.052 4.519   0.206   0.50 15.21 ? 177 ASN A CB  1 
ATOM   1865 C  CG  A ASN A 1 177 ? -23.881 5.709   -0.364  0.50 17.36 ? 177 ASN A CG  1 
ATOM   1866 C  CG  B ASN A 1 177 ? -23.462 5.910   -0.265  0.50 18.63 ? 177 ASN A CG  1 
ATOM   1867 O  OD1 A ASN A 1 177 ? -24.667 6.529   0.146   0.50 15.10 ? 177 ASN A OD1 1 
ATOM   1868 O  OD1 B ASN A 1 177 ? -23.928 6.760   0.499   0.50 19.77 ? 177 ASN A OD1 1 
ATOM   1869 N  ND2 A ASN A 1 177 ? -23.018 6.040   -1.418  0.50 14.46 ? 177 ASN A ND2 1 
ATOM   1870 N  ND2 B ASN A 1 177 ? -23.288 6.149   -1.570  0.50 22.00 ? 177 ASN A ND2 1 
ATOM   1871 N  N   A PHE A 1 178 ? -21.724 2.944   3.004   0.50 9.34  ? 178 PHE A N   1 
ATOM   1872 N  N   B PHE A 1 178 ? -20.755 2.972   2.702   0.50 11.15 ? 178 PHE A N   1 
ATOM   1873 C  CA  A PHE A 1 178 ? -21.605 1.762   3.802   0.50 10.13 ? 178 PHE A CA  1 
ATOM   1874 C  CA  B PHE A 1 178 ? -20.684 1.793   3.513   0.50 10.12 ? 178 PHE A CA  1 
ATOM   1875 C  C   A PHE A 1 178 ? -22.055 2.089   5.231   0.50 9.37  ? 178 PHE A C   1 
ATOM   1876 C  C   B PHE A 1 178 ? -21.220 2.109   4.902   0.50 9.87  ? 178 PHE A C   1 
ATOM   1877 O  O   A PHE A 1 178 ? -21.631 3.084   5.820   0.50 9.92  ? 178 PHE A O   1 
ATOM   1878 O  O   B PHE A 1 178 ? -20.756 3.054   5.524   0.50 11.31 ? 178 PHE A O   1 
ATOM   1879 C  CB  A PHE A 1 178 ? -20.179 1.266   3.798   0.50 9.37  ? 178 PHE A CB  1 
ATOM   1880 C  CB  B PHE A 1 178 ? -19.266 1.315   3.646   0.50 10.36 ? 178 PHE A CB  1 
ATOM   1881 C  CG  A PHE A 1 178 ? -20.034 0.060   4.646   0.50 9.51  ? 178 PHE A CG  1 
ATOM   1882 C  CG  B PHE A 1 178 ? -19.171 0.106   4.519   0.50 10.56 ? 178 PHE A CG  1 
ATOM   1883 C  CD1 A PHE A 1 178 ? -20.472 -1.169  4.182   0.50 11.09 ? 178 PHE A CD1 1 
ATOM   1884 C  CD1 B PHE A 1 178 ? -19.562 -1.170  4.053   0.50 9.96  ? 178 PHE A CD1 1 
ATOM   1885 C  CD2 A PHE A 1 178 ? -19.573 0.125   5.967   0.50 10.23 ? 178 PHE A CD2 1 
ATOM   1886 C  CD2 B PHE A 1 178 ? -18.797 0.221   5.862   0.50 9.66  ? 178 PHE A CD2 1 
ATOM   1887 C  CE1 A PHE A 1 178 ? -20.437 -2.302  4.939   0.50 10.64 ? 178 PHE A CE1 1 
ATOM   1888 C  CE1 B PHE A 1 178 ? -19.519 -2.267  4.878   0.50 9.48  ? 178 PHE A CE1 1 
ATOM   1889 C  CE2 A PHE A 1 178 ? -19.501 -1.063  6.725   0.50 8.60  ? 178 PHE A CE2 1 
ATOM   1890 C  CE2 B PHE A 1 178 ? -18.792 -0.913  6.676   0.50 11.49 ? 178 PHE A CE2 1 
ATOM   1891 C  CZ  A PHE A 1 178 ? -19.938 -2.254  6.218   0.50 9.44  ? 178 PHE A CZ  1 
ATOM   1892 C  CZ  B PHE A 1 178 ? -19.159 -2.123  6.193   0.50 10.65 ? 178 PHE A CZ  1 
ATOM   1893 N  N   A ASP A 1 179 ? -22.923 1.244   5.776   0.50 9.47  ? 179 ASP A N   1 
ATOM   1894 N  N   B ASP A 1 179 ? -22.143 1.293   5.405   0.50 9.91  ? 179 ASP A N   1 
ATOM   1895 C  CA  A ASP A 1 179 ? -23.463 1.454   7.108   0.50 10.01 ? 179 ASP A CA  1 
ATOM   1896 C  CA  B ASP A 1 179 ? -22.779 1.545   6.705   0.50 9.71  ? 179 ASP A CA  1 
ATOM   1897 C  C   A ASP A 1 179 ? -22.803 0.539   8.098   0.50 10.23 ? 179 ASP A C   1 
ATOM   1898 C  C   B ASP A 1 179 ? -22.184 0.665   7.804   0.50 10.95 ? 179 ASP A C   1 
ATOM   1899 O  O   A ASP A 1 179 ? -23.077 -0.668  8.143   0.50 10.11 ? 179 ASP A O   1 
ATOM   1900 O  O   B ASP A 1 179 ? -22.384 -0.560  7.832   0.50 8.87  ? 179 ASP A O   1 
ATOM   1901 C  CB  A ASP A 1 179 ? -24.929 1.141   7.040   0.50 11.82 ? 179 ASP A CB  1 
ATOM   1902 C  CB  B ASP A 1 179 ? -24.278 1.241   6.599   0.50 11.94 ? 179 ASP A CB  1 
ATOM   1903 C  CG  A ASP A 1 179 ? -25.691 1.622   8.218   0.50 14.48 ? 179 ASP A CG  1 
ATOM   1904 C  CG  B ASP A 1 179 ? -25.035 1.438   7.895   0.50 13.54 ? 179 ASP A CG  1 
ATOM   1905 O  OD1 A ASP A 1 179 ? -25.121 1.750   9.310   0.50 10.09 ? 179 ASP A OD1 1 
ATOM   1906 O  OD1 B ASP A 1 179 ? -24.432 1.826   8.891   0.50 12.90 ? 179 ASP A OD1 1 
ATOM   1907 O  OD2 A ASP A 1 179 ? -26.922 1.735   8.030   0.50 19.47 ? 179 ASP A OD2 1 
ATOM   1908 O  OD2 B ASP A 1 179 ? -26.278 1.150   7.896   0.50 20.40 ? 179 ASP A OD2 1 
ATOM   1909 N  N   A PRO A 1 180 ? -21.899 1.098   8.911   0.50 10.22 ? 180 PRO A N   1 
ATOM   1910 N  N   B PRO A 1 180 ? -21.518 1.280   8.784   0.50 10.85 ? 180 PRO A N   1 
ATOM   1911 C  CA  A PRO A 1 180 ? -21.060 0.302   9.817   0.50 10.99 ? 180 PRO A CA  1 
ATOM   1912 C  CA  B PRO A 1 180 ? -20.901 0.424   9.818   0.50 12.25 ? 180 PRO A CA  1 
ATOM   1913 C  C   A PRO A 1 180 ? -21.951 -0.308  10.841  0.50 11.31 ? 180 PRO A C   1 
ATOM   1914 C  C   B PRO A 1 180 ? -21.866 -0.166  10.879  0.50 10.79 ? 180 PRO A C   1 
ATOM   1915 O  O   A PRO A 1 180 ? -21.557 -1.249  11.543  0.50 10.90 ? 180 PRO A O   1 
ATOM   1916 O  O   B PRO A 1 180 ? -21.386 -1.005  11.648  0.50 11.20 ? 180 PRO A O   1 
ATOM   1917 C  CB  A PRO A 1 180 ? -20.163 1.358   10.436  0.50 11.77 ? 180 PRO A CB  1 
ATOM   1918 C  CB  B PRO A 1 180 ? -19.794 1.333   10.393  0.50 13.76 ? 180 PRO A CB  1 
ATOM   1919 C  CG  A PRO A 1 180 ? -20.974 2.641   10.395  0.50 9.88  ? 180 PRO A CG  1 
ATOM   1920 C  CG  B PRO A 1 180 ? -20.310 2.738   10.163  0.50 12.08 ? 180 PRO A CG  1 
ATOM   1921 C  CD  A PRO A 1 180 ? -21.669 2.544   9.052   0.50 10.61 ? 180 PRO A CD  1 
ATOM   1922 C  CD  B PRO A 1 180 ? -21.071 2.687   8.862   0.50 10.76 ? 180 PRO A CD  1 
ATOM   1923 N  N   . ARG A 1 181 ? -23.176 0.182   10.910  1.00 12.48 ? 181 ARG A N   1 
ATOM   1924 C  CA  . ARG A 1 181 ? -24.090 -0.459  11.822  1.00 12.69 ? 181 ARG A CA  1 
ATOM   1925 C  C   . ARG A 1 181 ? -24.202 -1.959  11.501  1.00 12.46 ? 181 ARG A C   1 
ATOM   1926 O  O   . ARG A 1 181 ? -24.557 -2.769  12.404  1.00 14.74 ? 181 ARG A O   1 
ATOM   1927 C  CB  . ARG A 1 181 ? -25.432 0.181   11.846  1.00 14.23 ? 181 ARG A CB  1 
ATOM   1928 C  CG  . ARG A 1 181 ? -25.410 1.595   12.437  1.00 16.35 ? 181 ARG A CG  1 
ATOM   1929 C  CD  . ARG A 1 181 ? -26.762 2.307   12.346  1.00 18.95 ? 181 ARG A CD  1 
ATOM   1930 N  NE  . ARG A 1 181 ? -27.130 2.528   10.955  1.00 18.80 ? 181 ARG A NE  1 
ATOM   1931 C  CZ  . ARG A 1 181 ? -28.216 3.244   10.657  1.00 18.55 ? 181 ARG A CZ  1 
ATOM   1932 N  NH1 . ARG A 1 181 ? -28.998 3.692   11.643  1.00 25.11 ? 181 ARG A NH1 1 
ATOM   1933 N  NH2 . ARG A 1 181 ? -28.543 3.467   9.398   1.00 25.10 ? 181 ARG A NH2 1 
ATOM   1934 N  N   . GLY A 1 182 ? -23.951 -2.366  10.261  1.00 13.80 ? 182 GLY A N   1 
ATOM   1935 C  CA  . GLY A 1 182 ? -24.111 -3.774  9.904   1.00 15.59 ? 182 GLY A CA  1 
ATOM   1936 C  C   . GLY A 1 182 ? -23.007 -4.632  10.419  1.00 13.65 ? 182 GLY A C   1 
ATOM   1937 O  O   . GLY A 1 182 ? -23.055 -5.819  10.145  1.00 15.28 ? 182 GLY A O   1 
ATOM   1938 N  N   . LEU A 1 183 ? -22.008 -4.045  11.124  1.00 13.23 ? 183 LEU A N   1 
ATOM   1939 C  CA  . LEU A 1 183 ? -20.871 -4.787  11.640  1.00 12.06 ? 183 LEU A CA  1 
ATOM   1940 C  C   . LEU A 1 183 ? -21.041 -5.073  13.147  1.00 11.84 ? 183 LEU A C   1 
ATOM   1941 O  O   . LEU A 1 183 ? -20.151 -5.711  13.755  1.00 12.26 ? 183 LEU A O   1 
ATOM   1942 C  CB  . LEU A 1 183 ? -19.587 -4.057  11.387  1.00 12.25 ? 183 LEU A CB  1 
ATOM   1943 C  CG  . LEU A 1 183 ? -19.207 -3.926  9.895   1.00 14.47 ? 183 LEU A CG  1 
ATOM   1944 C  CD1 . LEU A 1 183 ? -17.940 -3.138  9.808   1.00 18.14 ? 183 LEU A CD1 1 
ATOM   1945 C  CD2 . LEU A 1 183 ? -19.058 -5.218  9.178   1.00 17.10 ? 183 LEU A CD2 1 
ATOM   1946 N  N   A LEU A 1 184 ? -22.149 -4.611  13.765  0.50 12.27 ? 184 LEU A N   1 
ATOM   1947 N  N   B LEU A 1 184 ? -22.007 -4.460  13.760  0.50 11.40 ? 184 LEU A N   1 
ATOM   1948 C  CA  A LEU A 1 184 ? -22.386 -4.574  15.283  0.50 11.01 ? 184 LEU A CA  1 
ATOM   1949 C  CA  B LEU A 1 184 ? -22.014 -4.608  15.176  0.50 11.23 ? 184 LEU A CA  1 
ATOM   1950 C  C   A LEU A 1 184 ? -23.245 -5.710  15.902  0.50 9.45  ? 184 LEU A C   1 
ATOM   1951 C  C   B LEU A 1 184 ? -22.670 -5.955  15.434  0.50 9.88  ? 184 LEU A C   1 
ATOM   1952 O  O   A LEU A 1 184 ? -24.273 -6.071  15.419  0.50 9.64  ? 184 LEU A O   1 
ATOM   1953 O  O   B LEU A 1 184 ? -23.396 -6.517  14.615  0.50 9.92  ? 184 LEU A O   1 
ATOM   1954 C  CB  A LEU A 1 184 ? -23.116 -3.272  15.670  0.50 10.75 ? 184 LEU A CB  1 
ATOM   1955 C  CB  B LEU A 1 184 ? -22.832 -3.470  15.785  0.50 10.51 ? 184 LEU A CB  1 
ATOM   1956 C  CG  A LEU A 1 184 ? -22.524 -1.925  15.224  0.50 9.64  ? 184 LEU A CG  1 
ATOM   1957 C  CG  B LEU A 1 184 ? -22.181 -2.119  15.405  0.50 10.27 ? 184 LEU A CG  1 
ATOM   1958 C  CD1 A LEU A 1 184 ? -23.355 -0.799  15.825  0.50 11.22 ? 184 LEU A CD1 1 
ATOM   1959 C  CD1 B LEU A 1 184 ? -23.081 -0.955  15.786  0.50 12.81 ? 184 LEU A CD1 1 
ATOM   1960 C  CD2 A LEU A 1 184 ? -21.066 -1.773  15.641  0.50 11.63 ? 184 LEU A CD2 1 
ATOM   1961 C  CD2 B LEU A 1 184 ? -20.819 -1.995  16.067  0.50 11.36 ? 184 LEU A CD2 1 
ATOM   1962 N  N   A PRO A 1 185 ? -22.791 -6.295  17.006  0.50 8.82  ? 185 PRO A N   1 
ATOM   1963 N  N   B PRO A 1 185 ? -22.412 -6.488  16.639  0.50 9.72  ? 185 PRO A N   1 
ATOM   1964 C  CA  A PRO A 1 185 ? -23.511 -7.388  17.659  0.50 8.11  ? 185 PRO A CA  1 
ATOM   1965 C  CA  B PRO A 1 185 ? -23.157 -7.613  17.159  0.50 8.65  ? 185 PRO A CA  1 
ATOM   1966 C  C   A PRO A 1 185 ? -24.800 -6.881  18.344  0.50 8.01  ? 185 PRO A C   1 
ATOM   1967 C  C   B PRO A 1 185 ? -24.464 -7.046  17.692  0.50 8.76  ? 185 PRO A C   1 
ATOM   1968 O  O   A PRO A 1 185 ? -24.977 -5.679  18.514  0.50 7.52  ? 185 PRO A O   1 
ATOM   1969 O  O   B PRO A 1 185 ? -24.694 -5.807  17.615  0.50 8.80  ? 185 PRO A O   1 
ATOM   1970 C  CB  A PRO A 1 185 ? -22.522 -7.940  18.672  0.50 8.97  ? 185 PRO A CB  1 
ATOM   1971 C  CB  B PRO A 1 185 ? -22.272 -8.153  18.298  0.50 9.10  ? 185 PRO A CB  1 
ATOM   1972 C  CG  A PRO A 1 185 ? -21.724 -6.719  19.046  0.50 7.91  ? 185 PRO A CG  1 
ATOM   1973 C  CG  B PRO A 1 185 ? -21.552 -6.920  18.825  0.50 10.12 ? 185 PRO A CG  1 
ATOM   1974 C  CD  A PRO A 1 185 ? -21.597 -5.900  17.752  0.50 8.64  ? 185 PRO A CD  1 
ATOM   1975 C  CD  B PRO A 1 185 ? -21.337 -6.070  17.556  0.50 8.78  ? 185 PRO A CD  1 
ATOM   1976 N  N   A GLU A 1 186 ? -25.661 -7.794  18.783  0.50 9.51  ? 186 GLU A N   1 
ATOM   1977 N  N   B GLU A 1 186 ? -25.297 -7.918  18.243  0.50 10.50 ? 186 GLU A N   1 
ATOM   1978 C  CA  A GLU A 1 186 ? -26.944 -7.344  19.421  0.50 10.51 ? 186 GLU A CA  1 
ATOM   1979 C  CA  B GLU A 1 186 ? -26.500 -7.459  18.930  0.50 11.84 ? 186 GLU A CA  1 
ATOM   1980 C  C   A GLU A 1 186 ? -26.605 -6.563  20.617  0.50 11.54 ? 186 GLU A C   1 
ATOM   1981 C  C   B GLU A 1 186 ? -26.375 -6.622  20.247  0.50 12.67 ? 186 GLU A C   1 
ATOM   1982 O  O   A GLU A 1 186 ? -27.178 -5.506  20.925  0.50 11.63 ? 186 GLU A O   1 
ATOM   1983 O  O   B GLU A 1 186 ? -27.014 -5.536  20.237  0.50 12.54 ? 186 GLU A O   1 
ATOM   1984 C  CB  A GLU A 1 186 ? -27.799 -8.498  19.917  0.50 11.14 ? 186 GLU A CB  1 
ATOM   1985 C  CB  B GLU A 1 186 ? -27.424 -8.648  19.173  0.50 10.69 ? 186 GLU A CB  1 
ATOM   1986 C  CG  A GLU A 1 186 ? -28.478 -9.223  18.842  0.50 11.92 ? 186 GLU A CG  1 
ATOM   1987 C  CG  B GLU A 1 186 ? -28.147 -9.186  17.992  0.50 12.86 ? 186 GLU A CG  1 
ATOM   1988 C  CD  A GLU A 1 186 ? -29.126 -10.496 19.313  0.50 12.43 ? 186 GLU A CD  1 
ATOM   1989 C  CD  B GLU A 1 186 ? -28.961 -10.448 18.332  0.50 16.37 ? 186 GLU A CD  1 
ATOM   1990 O  OE1 A GLU A 1 186 ? -29.638 -11.224 18.463  0.50 13.72 ? 186 GLU A OE1 1 
ATOM   1991 O  OE1 B GLU A 1 186 ? -29.145 -10.848 19.534  0.50 15.73 ? 186 GLU A OE1 1 
ATOM   1992 O  OE2 A GLU A 1 186 ? -29.125 -10.763 20.517  0.50 13.76 ? 186 GLU A OE2 1 
ATOM   1993 O  OE2 B GLU A 1 186 ? -29.427 -11.048 17.351  0.50 21.41 ? 186 GLU A OE2 1 
ATOM   1994 N  N   . SER A 1 187 ? -25.681 -7.128  21.326  1.00 13.58 ? 187 SER A N   1 
ATOM   1995 C  CA  . SER A 1 187 ? -25.444 -6.514  22.582  1.00 12.71 ? 187 SER A CA  1 
ATOM   1996 C  C   . SER A 1 187 ? -24.315 -5.462  22.576  1.00 12.23 ? 187 SER A C   1 
ATOM   1997 O  O   . SER A 1 187 ? -23.311 -5.702  21.911  1.00 13.12 ? 187 SER A O   1 
ATOM   1998 C  CB  . SER A 1 187 ? -25.077 -7.545  23.605  1.00 14.19 ? 187 SER A CB  1 
ATOM   1999 O  OG  . SER A 1 187 ? -24.824 -6.972  24.866  1.00 14.62 ? 187 SER A OG  1 
ATOM   2000 N  N   . LEU A 1 188 ? -24.492 -4.376  23.310  1.00 12.66 ? 188 LEU A N   1 
ATOM   2001 C  CA  . LEU A 1 188 ? -23.410 -3.420  23.547  1.00 12.92 ? 188 LEU A CA  1 
ATOM   2002 C  C   . LEU A 1 188 ? -22.790 -3.576  24.890  1.00 12.16 ? 188 LEU A C   1 
ATOM   2003 O  O   . LEU A 1 188 ? -22.084 -2.659  25.365  1.00 14.03 ? 188 LEU A O   1 
ATOM   2004 C  CB  . LEU A 1 188 ? -23.892 -1.970  23.262  1.00 16.22 ? 188 LEU A CB  1 
ATOM   2005 C  CG  . LEU A 1 188 ? -24.297 -1.555  21.881  1.00 15.91 ? 188 LEU A CG  1 
ATOM   2006 C  CD1 . LEU A 1 188 ? -24.857 -0.139  21.844  1.00 19.81 ? 188 LEU A CD1 1 
ATOM   2007 C  CD2 . LEU A 1 188 ? -23.215 -1.785  20.829  1.00 17.99 ? 188 LEU A CD2 1 
ATOM   2008 N  N   . ASP A 1 189 ? -22.920 -4.747  25.537  1.00 12.49 ? 189 ASP A N   1 
ATOM   2009 C  CA  . ASP A 1 189 ? -22.207 -4.959  26.780  1.00 13.64 ? 189 ASP A CA  1 
ATOM   2010 C  C   . ASP A 1 189 ? -20.679 -4.958  26.449  1.00 9.50  ? 189 ASP A C   1 
ATOM   2011 O  O   . ASP A 1 189 ? -20.242 -5.460  25.429  1.00 9.33  ? 189 ASP A O   1 
ATOM   2012 C  CB  . ASP A 1 189 ? -22.512 -6.281  27.412  1.00 15.48 ? 189 ASP A CB  1 
ATOM   2013 C  CG  . ASP A 1 189 ? -23.943 -6.392  28.000  1.00 20.08 ? 189 ASP A CG  1 
ATOM   2014 O  OD1 . ASP A 1 189 ? -24.586 -5.373  28.136  1.00 25.19 ? 189 ASP A OD1 1 
ATOM   2015 O  OD2 . ASP A 1 189 ? -24.349 -7.535  28.236  1.00 29.58 ? 189 ASP A OD2 1 
ATOM   2016 N  N   . TYR A 1 190 ? -19.907 -4.352  27.340  1.00 9.43  ? 190 TYR A N   1 
ATOM   2017 C  CA  . TYR A 1 190 ? -18.485 -4.122  27.050  1.00 8.41  ? 190 TYR A CA  1 
ATOM   2018 C  C   . TYR A 1 190 ? -17.603 -4.197  28.258  1.00 7.40  ? 190 TYR A C   1 
ATOM   2019 O  O   . TYR A 1 190 ? -18.045 -4.034  29.395  1.00 9.45  ? 190 TYR A O   1 
ATOM   2020 C  CB  . TYR A 1 190 ? -18.329 -2.729  26.336  1.00 8.92  ? 190 TYR A CB  1 
ATOM   2021 C  CG  . TYR A 1 190 ? -18.700 -1.579  27.206  1.00 9.00  ? 190 TYR A CG  1 
ATOM   2022 C  CD1 . TYR A 1 190 ? -17.783 -0.971  28.063  1.00 9.37  ? 190 TYR A CD1 1 
ATOM   2023 C  CD2 . TYR A 1 190 ? -19.984 -1.013  27.150  1.00 10.85 ? 190 TYR A CD2 1 
ATOM   2024 C  CE1 . TYR A 1 190 ? -18.139 0.077   28.916  1.00 10.62 ? 190 TYR A CE1 1 
ATOM   2025 C  CE2 . TYR A 1 190 ? -20.361 0.055   27.966  1.00 11.29 ? 190 TYR A CE2 1 
ATOM   2026 C  CZ  . TYR A 1 190 ? -19.415 0.625   28.824  1.00 10.70 ? 190 TYR A CZ  1 
ATOM   2027 O  OH  . TYR A 1 190 ? -19.770 1.632   29.682  1.00 12.43 ? 190 TYR A OH  1 
ATOM   2028 N  N   . TRP A 1 191 ? -16.308 -4.340  27.962  1.00 7.27  ? 191 TRP A N   1 
ATOM   2029 C  CA  . TRP A 1 191 ? -15.247 -4.069  28.920  1.00 7.54  ? 191 TRP A CA  1 
ATOM   2030 C  C   . TRP A 1 191 ? -14.538 -2.782  28.494  1.00 6.77  ? 191 TRP A C   1 
ATOM   2031 O  O   . TRP A 1 191 ? -14.445 -2.480  27.307  1.00 8.00  ? 191 TRP A O   1 
ATOM   2032 C  CB  . TRP A 1 191 ? -14.208 -5.197  28.920  1.00 8.69  ? 191 TRP A CB  1 
ATOM   2033 C  CG  . TRP A 1 191 ? -14.744 -6.530  29.350  1.00 7.69  ? 191 TRP A CG  1 
ATOM   2034 C  CD1 . TRP A 1 191 ? -14.989 -6.919  30.627  1.00 9.89  ? 191 TRP A CD1 1 
ATOM   2035 C  CD2 . TRP A 1 191 ? -15.028 -7.663  28.512  1.00 8.41  ? 191 TRP A CD2 1 
ATOM   2036 N  NE1 . TRP A 1 191 ? -15.396 -8.263  30.645  1.00 10.82 ? 191 TRP A NE1 1 
ATOM   2037 C  CE2 . TRP A 1 191 ? -15.460 -8.738  29.357  1.00 9.07  ? 191 TRP A CE2 1 
ATOM   2038 C  CE3 . TRP A 1 191 ? -14.955 -7.881  27.103  1.00 8.92  ? 191 TRP A CE3 1 
ATOM   2039 C  CZ2 . TRP A 1 191 ? -15.767 -10.002 28.833  1.00 10.24 ? 191 TRP A CZ2 1 
ATOM   2040 C  CZ3 . TRP A 1 191 ? -15.215 -9.143  26.639  1.00 10.03 ? 191 TRP A CZ3 1 
ATOM   2041 C  CH2 . TRP A 1 191 ? -15.633 -10.149 27.479  1.00 10.59 ? 191 TRP A CH2 1 
ATOM   2042 N  N   . THR A 1 192 ? -13.970 -2.069  29.462  1.00 7.16  ? 192 THR A N   1 
ATOM   2043 C  CA  . THR A 1 192 ? -13.221 -0.862  29.144  1.00 6.97  ? 192 THR A CA  1 
ATOM   2044 C  C   . THR A 1 192 ? -12.010 -0.707  29.992  1.00 7.04  ? 192 THR A C   1 
ATOM   2045 O  O   . THR A 1 192 ? -11.990 -1.089  31.195  1.00 8.00  ? 192 THR A O   1 
ATOM   2046 C  CB  . THR A 1 192 ? -14.172 0.379   29.223  1.00 7.44  ? 192 THR A CB  1 
ATOM   2047 O  OG1 . THR A 1 192 ? -13.449 1.553   28.841  1.00 7.34  ? 192 THR A OG1 1 
ATOM   2048 C  CG2 . THR A 1 192 ? -14.699 0.586   30.630  1.00 8.56  ? 192 THR A CG2 1 
ATOM   2049 N  N   . TYR A 1 193 ? -10.946 -0.109  29.432  1.00 6.72  ? 193 TYR A N   1 
ATOM   2050 C  CA  . TYR A 1 193 ? -9.731  0.150   30.172  1.00 7.28  ? 193 TYR A CA  1 
ATOM   2051 C  C   . TYR A 1 193 ? -8.960  1.234   29.407  1.00 6.97  ? 193 TYR A C   1 
ATOM   2052 O  O   . TYR A 1 193 ? -9.156  1.397   28.194  1.00 6.80  ? 193 TYR A O   1 
ATOM   2053 C  CB  . TYR A 1 193 ? -8.899  -1.122  30.371  1.00 7.17  ? 193 TYR A CB  1 
ATOM   2054 C  CG  . TYR A 1 193 ? -8.228  -1.601  29.099  1.00 6.60  ? 193 TYR A CG  1 
ATOM   2055 C  CD1 . TYR A 1 193 ? -8.890  -2.346  28.133  1.00 7.14  ? 193 TYR A CD1 1 
ATOM   2056 C  CD2 . TYR A 1 193 ? -6.891  -1.262  28.859  1.00 7.06  ? 193 TYR A CD2 1 
ATOM   2057 C  CE1 . TYR A 1 193 ? -8.276  -2.663  26.920  1.00 6.33  ? 193 TYR A CE1 1 
ATOM   2058 C  CE2 . TYR A 1 193 ? -6.240  -1.599  27.677  1.00 7.13  ? 193 TYR A CE2 1 
ATOM   2059 C  CZ  . TYR A 1 193 ? -6.955  -2.298  26.684  1.00 6.05  ? 193 TYR A CZ  1 
ATOM   2060 O  OH  . TYR A 1 193 ? -6.301  -2.594  25.542  1.00 6.08  ? 193 TYR A OH  1 
ATOM   2061 N  N   . PRO A 1 194 ? -8.046  1.927   30.076  1.00 6.81  ? 194 PRO A N   1 
ATOM   2062 C  CA  . PRO A 1 194 ? -7.197  2.944   29.419  1.00 7.05  ? 194 PRO A CA  1 
ATOM   2063 C  C   . PRO A 1 194 ? -5.989  2.276   28.747  1.00 6.03  ? 194 PRO A C   1 
ATOM   2064 O  O   . PRO A 1 194 ? -5.281  1.489   29.397  1.00 7.29  ? 194 PRO A O   1 
ATOM   2065 C  CB  . PRO A 1 194 ? -6.724  3.818   30.573  1.00 8.34  ? 194 PRO A CB  1 
ATOM   2066 C  CG  . PRO A 1 194 ? -6.744  2.919   31.762  1.00 8.99  ? 194 PRO A CG  1 
ATOM   2067 C  CD  . PRO A 1 194 ? -7.937  1.954   31.550  1.00 8.19  ? 194 PRO A CD  1 
ATOM   2068 N  N   . GLY A 1 195 ? -5.759  2.566   27.476  1.00 5.84  ? 195 GLY A N   1 
ATOM   2069 C  CA  . GLY A 1 195 ? -4.638  1.948   26.788  1.00 7.02  ? 195 GLY A CA  1 
ATOM   2070 C  C   . GLY A 1 195 ? -4.073  2.816   25.681  1.00 6.32  ? 195 GLY A C   1 
ATOM   2071 O  O   . GLY A 1 195 ? -3.942  4.049   25.841  1.00 6.61  ? 195 GLY A O   1 
ATOM   2072 N  N   . SER A 1 196 ? -3.700  2.143   24.614  1.00 6.13  ? 196 SER A N   1 
ATOM   2073 C  CA  . SER A 1 196 ? -2.858  2.770   23.598  1.00 6.77  ? 196 SER A CA  1 
ATOM   2074 C  C   . SER A 1 196 ? -3.305  2.349   22.229  1.00 5.90  ? 196 SER A C   1 
ATOM   2075 O  O   . SER A 1 196 ? -4.073  1.398   22.059  1.00 5.97  ? 196 SER A O   1 
ATOM   2076 C  CB  . SER A 1 196 ? -1.364  2.387   23.749  1.00 6.56  ? 196 SER A CB  1 
ATOM   2077 O  OG  . SER A 1 196 ? -1.141  1.051   23.363  1.00 6.36  ? 196 SER A OG  1 
ATOM   2078 N  N   . LEU A 1 197 ? -2.745  2.987   21.178  1.00 5.97  ? 197 LEU A N   1 
ATOM   2079 C  CA  . LEU A 1 197 ? -2.778  2.416   19.850  1.00 6.38  ? 197 LEU A CA  1 
ATOM   2080 C  C   . LEU A 1 197 ? -2.050  1.084   19.899  1.00 5.98  ? 197 LEU A C   1 
ATOM   2081 O  O   . LEU A 1 197 ? -1.046  0.934   20.625  1.00 6.45  ? 197 LEU A O   1 
ATOM   2082 C  CB  . LEU A 1 197 ? -2.092  3.314   18.875  1.00 6.84  ? 197 LEU A CB  1 
ATOM   2083 C  CG  . LEU A 1 197 ? -2.607  4.721   18.709  1.00 7.91  ? 197 LEU A CG  1 
ATOM   2084 C  CD1 . LEU A 1 197 ? -1.707  5.468   17.731  1.00 9.55  ? 197 LEU A CD1 1 
ATOM   2085 C  CD2 . LEU A 1 197 ? -4.066  4.724   18.244  1.00 9.45  ? 197 LEU A CD2 1 
ATOM   2086 N  N   . THR A 1 198 ? -2.458  0.153   19.044  1.00 6.02  ? 198 THR A N   1 
ATOM   2087 C  CA  . THR A 1 198 ? -1.736  -1.135  18.974  1.00 6.66  ? 198 THR A CA  1 
ATOM   2088 C  C   . THR A 1 198 ? -0.763  -1.213  17.837  1.00 6.93  ? 198 THR A C   1 
ATOM   2089 O  O   . THR A 1 198 ? -0.155  -2.266  17.630  1.00 7.54  ? 198 THR A O   1 
ATOM   2090 C  CB  . THR A 1 198 ? -2.718  -2.314  18.913  1.00 6.39  ? 198 THR A CB  1 
ATOM   2091 O  OG1 . THR A 1 198 ? -3.342  -2.279  17.601  1.00 6.26  ? 198 THR A OG1 1 
ATOM   2092 C  CG2 . THR A 1 198 ? -3.716  -2.295  20.061  1.00 7.25  ? 198 THR A CG2 1 
ATOM   2093 N  N   . THR A 1 199 ? -0.618  -0.119  17.082  1.00 7.15  ? 199 THR A N   1 
ATOM   2094 C  CA  . THR A 1 199 ? 0.436   0.024   16.062  1.00 7.86  ? 199 THR A CA  1 
ATOM   2095 C  C   . THR A 1 199 ? 1.202   1.239   16.405  1.00 8.34  ? 199 THR A C   1 
ATOM   2096 O  O   . THR A 1 199 ? 0.718   2.172   17.043  1.00 7.69  ? 199 THR A O   1 
ATOM   2097 C  CB  . THR A 1 199 ? -0.157  0.262   14.664  1.00 9.29  ? 199 THR A CB  1 
ATOM   2098 O  OG1 . THR A 1 199 ? -1.036  1.401   14.641  1.00 10.46 ? 199 THR A OG1 1 
ATOM   2099 C  CG2 . THR A 1 199 ? -0.930  -0.968  14.177  1.00 10.45 ? 199 THR A CG2 1 
ATOM   2100 N  N   . PRO A 1 200 ? 2.478   1.324   15.932  1.00 8.36  ? 200 PRO A N   1 
ATOM   2101 C  CA  . PRO A 1 200 ? 3.224   2.591   15.971  1.00 9.00  ? 200 PRO A CA  1 
ATOM   2102 C  C   . PRO A 1 200 ? 2.280   3.707   15.499  1.00 9.32  ? 200 PRO A C   1 
ATOM   2103 O  O   . PRO A 1 200 ? 1.510   3.553   14.536  1.00 9.81  ? 200 PRO A O   1 
ATOM   2104 C  CB  . PRO A 1 200 ? 4.348   2.283   14.938  1.00 11.32 ? 200 PRO A CB  1 
ATOM   2105 C  CG  . PRO A 1 200 ? 4.641   0.850   15.252  1.00 10.91 ? 200 PRO A CG  1 
ATOM   2106 C  CD  . PRO A 1 200 ? 3.249   0.237   15.324  1.00 10.04 ? 200 PRO A CD  1 
ATOM   2107 N  N   . PRO A 1 201 ? 2.312   4.844   16.184  1.00 9.41  ? 201 PRO A N   1 
ATOM   2108 C  CA  . PRO A 1 201 ? 3.277   5.245   17.235  1.00 8.65  ? 201 PRO A CA  1 
ATOM   2109 C  C   . PRO A 1 201 ? 3.008   4.726   18.640  1.00 8.03  ? 201 PRO A C   1 
ATOM   2110 O  O   . PRO A 1 201 ? 3.672   5.156   19.557  1.00 9.46  ? 201 PRO A O   1 
ATOM   2111 C  CB  . PRO A 1 201 ? 3.250   6.765   17.176  1.00 10.84 ? 201 PRO A CB  1 
ATOM   2112 C  CG  . PRO A 1 201 ? 1.782   7.075   16.781  1.00 11.06 ? 201 PRO A CG  1 
ATOM   2113 C  CD  . PRO A 1 201 ? 1.449   5.988   15.767  1.00 9.55  ? 201 PRO A CD  1 
ATOM   2114 N  N   . LEU A 1 202 ? 1.967   3.897   18.813  1.00 7.63  ? 202 LEU A N   1 
ATOM   2115 C  CA  . LEU A 1 202 ? 1.724   3.263   20.125  1.00 7.45  ? 202 LEU A CA  1 
ATOM   2116 C  C   . LEU A 1 202 ? 1.319   4.293   21.171  1.00 7.61  ? 202 LEU A C   1 
ATOM   2117 O  O   . LEU A 1 202 ? 1.478   4.060   22.385  1.00 7.49  ? 202 LEU A O   1 
ATOM   2118 C  CB  . LEU A 1 202 ? 2.878   2.380   20.591  1.00 7.92  ? 202 LEU A CB  1 
ATOM   2119 C  CG  . LEU A 1 202 ? 3.220   1.253   19.590  1.00 8.44  ? 202 LEU A CG  1 
ATOM   2120 C  CD1 . LEU A 1 202 ? 4.510   0.617   20.037  1.00 10.28 ? 202 LEU A CD1 1 
ATOM   2121 C  CD2 . LEU A 1 202 ? 2.136   0.204   19.482  1.00 8.55  ? 202 LEU A CD2 1 
ATOM   2122 N  N   . ALA A 1 203 ? 0.774   5.423   20.748  1.00 7.32  ? 203 ALA A N   1 
ATOM   2123 C  CA  . ALA A 1 203 ? 0.478   6.542   21.626  1.00 8.01  ? 203 ALA A CA  1 
ATOM   2124 C  C   . ALA A 1 203 ? -0.535  6.078   22.686  1.00 6.95  ? 203 ALA A C   1 
ATOM   2125 O  O   . ALA A 1 203 ? -1.500  5.367   22.390  1.00 7.12  ? 203 ALA A O   1 
ATOM   2126 C  CB  . ALA A 1 203 ? -0.102  7.659   20.803  1.00 8.35  ? 203 ALA A CB  1 
ATOM   2127 N  N   . GLU A 1 204 ? -0.353  6.562   23.896  1.00 7.17  ? 204 GLU A N   1 
ATOM   2128 C  CA  . GLU A 1 204 ? -1.131  6.201   25.053  1.00 7.08  ? 204 GLU A CA  1 
ATOM   2129 C  C   . GLU A 1 204 ? -2.332  7.148   25.227  1.00 7.40  ? 204 GLU A C   1 
ATOM   2130 O  O   . GLU A 1 204 ? -2.448  7.850   26.233  1.00 8.49  ? 204 GLU A O   1 
ATOM   2131 C  CB  . GLU A 1 204 ? -0.249  6.085   26.280  1.00 8.37  ? 204 GLU A CB  1 
ATOM   2132 C  CG  . GLU A 1 204 ? 0.641   4.824   26.144  1.00 9.63  ? 204 GLU A CG  1 
ATOM   2133 C  CD  . GLU A 1 204 ? 1.523   4.528   27.338  1.00 8.85  ? 204 GLU A CD  1 
ATOM   2134 O  OE1 . GLU A 1 204 ? 1.861   5.482   28.085  1.00 11.34 ? 204 GLU A OE1 1 
ATOM   2135 O  OE2 . GLU A 1 204 ? 1.898   3.357   27.497  1.00 9.96  ? 204 GLU A OE2 1 
ATOM   2136 N  N   . CYS A 1 205 ? -3.197  7.095   24.248  1.00 7.04  ? 205 CYS A N   1 
ATOM   2137 C  CA  . CYS A 1 205 ? -4.236  8.068   24.054  1.00 6.75  ? 205 CYS A CA  1 
ATOM   2138 C  C   . CYS A 1 205 ? -5.611  7.467   23.924  1.00 6.11  ? 205 CYS A C   1 
ATOM   2139 O  O   . CYS A 1 205 ? -6.558  8.175   23.567  1.00 7.96  ? 205 CYS A O   1 
ATOM   2140 C  CB  . CYS A 1 205 ? -3.921  8.933   22.846  1.00 7.95  ? 205 CYS A CB  1 
ATOM   2141 S  SG  . CYS A 1 205 ? -3.891  8.016   21.289  1.00 8.49  ? 205 CYS A SG  1 
ATOM   2142 N  N   . VAL A 1 206 ? -5.768  6.151   24.202  1.00 6.14  ? 206 VAL A N   1 
ATOM   2143 C  CA  . VAL A 1 206 ? -6.996  5.460   23.840  1.00 6.05  ? 206 VAL A CA  1 
ATOM   2144 C  C   . VAL A 1 206 ? -7.782  5.010   25.027  1.00 6.33  ? 206 VAL A C   1 
ATOM   2145 O  O   . VAL A 1 206 ? -7.244  4.344   25.919  1.00 7.17  ? 206 VAL A O   1 
ATOM   2146 C  CB  . VAL A 1 206 ? -6.699  4.217   22.956  1.00 6.28  ? 206 VAL A CB  1 
ATOM   2147 C  CG1 . VAL A 1 206 ? -8.013  3.496   22.611  1.00 6.95  ? 206 VAL A CG1 1 
ATOM   2148 C  CG2 . VAL A 1 206 ? -5.942  4.593   21.694  1.00 7.37  ? 206 VAL A CG2 1 
ATOM   2149 N  N   . THR A 1 207 ? -9.077  5.298   25.070  1.00 5.99  ? 207 THR A N   1 
ATOM   2150 C  CA  . THR A 1 207 ? -10.014 4.580   25.918  1.00 6.60  ? 207 THR A CA  1 
ATOM   2151 C  C   . THR A 1 207 ? -10.538 3.398   25.065  1.00 6.02  ? 207 THR A C   1 
ATOM   2152 O  O   . THR A 1 207 ? -11.195 3.606   24.034  1.00 6.42  ? 207 THR A O   1 
ATOM   2153 C  CB  . THR A 1 207 ? -11.206 5.429   26.340  1.00 6.74  ? 207 THR A CB  1 
ATOM   2154 O  OG1 . THR A 1 207 ? -10.700 6.571   27.048  1.00 8.04  ? 207 THR A OG1 1 
ATOM   2155 C  CG2 . THR A 1 207 ? -12.135 4.608   27.243  1.00 8.58  ? 207 THR A CG2 1 
ATOM   2156 N  N   . TRP A 1 208 ? -10.225 2.178   25.505  1.00 5.37  ? 208 TRP A N   1 
ATOM   2157 C  CA  . TRP A 1 208 ? -10.676 0.988   24.823  1.00 5.27  ? 208 TRP A CA  1 
ATOM   2158 C  C   . TRP A 1 208 ? -12.040 0.602   25.321  1.00 5.23  ? 208 TRP A C   1 
ATOM   2159 O  O   . TRP A 1 208 ? -12.282 0.568   26.526  1.00 6.12  ? 208 TRP A O   1 
ATOM   2160 C  CB  . TRP A 1 208 ? -9.668  -0.166  25.039  1.00 6.16  ? 208 TRP A CB  1 
ATOM   2161 C  CG  . TRP A 1 208 ? -8.543  -0.083  24.057  1.00 5.60  ? 208 TRP A CG  1 
ATOM   2162 C  CD1 . TRP A 1 208 ? -7.329  0.517   24.233  1.00 6.20  ? 208 TRP A CD1 1 
ATOM   2163 C  CD2 . TRP A 1 208 ? -8.580  -0.484  22.683  1.00 5.71  ? 208 TRP A CD2 1 
ATOM   2164 N  NE1 . TRP A 1 208 ? -6.612  0.488   23.074  1.00 6.61  ? 208 TRP A NE1 1 
ATOM   2165 C  CE2 . TRP A 1 208 ? -7.349  -0.126  22.106  1.00 6.54  ? 208 TRP A CE2 1 
ATOM   2166 C  CE3 . TRP A 1 208 ? -9.562  -1.134  21.910  1.00 5.84  ? 208 TRP A CE3 1 
ATOM   2167 C  CZ2 . TRP A 1 208 ? -7.067  -0.389  20.762  1.00 7.04  ? 208 TRP A CZ2 1 
ATOM   2168 C  CZ3 . TRP A 1 208 ? -9.275  -1.434  20.591  1.00 6.86  ? 208 TRP A CZ3 1 
ATOM   2169 C  CH2 . TRP A 1 208 ? -8.024  -1.041  20.046  1.00 7.68  ? 208 TRP A CH2 1 
ATOM   2170 N  N   . ILE A 1 209 ? -12.916 0.229   24.381  1.00 5.74  ? 209 ILE A N   1 
ATOM   2171 C  CA  . ILE A 1 209 ? -14.253 -0.263  24.653  1.00 5.66  ? 209 ILE A CA  1 
ATOM   2172 C  C   . ILE A 1 209 ? -14.345 -1.537  23.849  1.00 5.44  ? 209 ILE A C   1 
ATOM   2173 O  O   . ILE A 1 209 ? -14.424 -1.461  22.624  1.00 6.96  ? 209 ILE A O   1 
ATOM   2174 C  CB  . ILE A 1 209 ? -15.333 0.756   24.291  1.00 7.43  ? 209 ILE A CB  1 
ATOM   2175 C  CG1 . ILE A 1 209 ? -15.105 2.054   25.087  1.00 9.06  ? 209 ILE A CG1 1 
ATOM   2176 C  CG2 . ILE A 1 209 ? -16.713 0.129   24.538  1.00 8.33  ? 209 ILE A CG2 1 
ATOM   2177 C  CD1 . ILE A 1 209 ? -15.906 3.221   24.590  1.00 11.75 ? 209 ILE A CD1 1 
ATOM   2178 N  N   . VAL A 1 210 ? -14.316 -2.732  24.498  1.00 5.47  ? 210 VAL A N   1 
ATOM   2179 C  CA  . VAL A 1 210 ? -14.311 -3.994  23.799  1.00 5.40  ? 210 VAL A CA  1 
ATOM   2180 C  C   . VAL A 1 210 ? -15.623 -4.692  24.053  1.00 5.80  ? 210 VAL A C   1 
ATOM   2181 O  O   . VAL A 1 210 ? -15.938 -4.965  25.216  1.00 7.14  ? 210 VAL A O   1 
ATOM   2182 C  CB  . VAL A 1 210 ? -13.095 -4.850  24.258  1.00 6.26  ? 210 VAL A CB  1 
ATOM   2183 C  CG1 . VAL A 1 210 ? -13.120 -6.204  23.592  1.00 7.42  ? 210 VAL A CG1 1 
ATOM   2184 C  CG2 . VAL A 1 210 ? -11.780 -4.123  24.010  1.00 7.44  ? 210 VAL A CG2 1 
ATOM   2185 N  N   . LEU A 1 211 ? -16.362 -4.944  22.995  1.00 6.98  ? 211 LEU A N   1 
ATOM   2186 C  CA  . LEU A 1 211 ? -17.642 -5.579  23.189  1.00 6.89  ? 211 LEU A CA  1 
ATOM   2187 C  C   . LEU A 1 211 ? -17.499 -7.051  23.558  1.00 7.66  ? 211 LEU A C   1 
ATOM   2188 O  O   . LEU A 1 211 ? -16.653 -7.770  23.051  1.00 7.46  ? 211 LEU A O   1 
ATOM   2189 C  CB  . LEU A 1 211 ? -18.493 -5.466  21.915  1.00 8.34  ? 211 LEU A CB  1 
ATOM   2190 C  CG  . LEU A 1 211 ? -18.835 -4.051  21.483  1.00 7.97  ? 211 LEU A CG  1 
ATOM   2191 C  CD1 . LEU A 1 211 ? -19.870 -4.133  20.331  1.00 10.71 ? 211 LEU A CD1 1 
ATOM   2192 C  CD2 . LEU A 1 211 ? -19.373 -3.200  22.632  1.00 9.60  ? 211 LEU A CD2 1 
ATOM   2193 N  N   A LYS A 1 212 ? -18.371 -7.456  24.478  0.50 8.52  ? 212 LYS A N   1 
ATOM   2194 N  N   B LYS A 1 212 ? -18.322 -7.525  24.483  0.50 7.75  ? 212 LYS A N   1 
ATOM   2195 C  CA  A LYS A 1 212 ? -18.450 -8.832  24.968  0.50 9.46  ? 212 LYS A CA  1 
ATOM   2196 C  CA  B LYS A 1 212 ? -18.240 -8.945  24.848  0.50 7.52  ? 212 LYS A CA  1 
ATOM   2197 C  C   A LYS A 1 212 ? -18.873 -9.837  23.891  0.50 8.40  ? 212 LYS A C   1 
ATOM   2198 C  C   B LYS A 1 212 ? -18.754 -9.867  23.736  0.50 8.00  ? 212 LYS A C   1 
ATOM   2199 O  O   A LYS A 1 212 ? -18.377 -10.949 23.878  0.50 8.71  ? 212 LYS A O   1 
ATOM   2200 O  O   B LYS A 1 212 ? -18.188 -10.951 23.542  0.50 10.17 ? 212 LYS A O   1 
ATOM   2201 C  CB  A LYS A 1 212 ? -19.416 -8.909  26.178  0.50 11.64 ? 212 LYS A CB  1 
ATOM   2202 C  CB  B LYS A 1 212 ? -18.958 -9.201  26.152  0.50 7.58  ? 212 LYS A CB  1 
ATOM   2203 C  CG  A LYS A 1 212 ? -19.526 -10.330 26.716  0.50 14.51 ? 212 LYS A CG  1 
ATOM   2204 C  CG  B LYS A 1 212 ? -18.988 -10.647 26.614  0.50 11.78 ? 212 LYS A CG  1 
ATOM   2205 C  CD  A LYS A 1 212 ? -20.558 -10.525 27.802  0.50 17.44 ? 212 LYS A CD  1 
ATOM   2206 C  CD  B LYS A 1 212 ? -19.623 -10.779 27.974  0.50 12.38 ? 212 LYS A CD  1 
ATOM   2207 C  CE  A LYS A 1 212 ? -21.695 -9.625  27.441  0.50 19.06 ? 212 LYS A CE  1 
ATOM   2208 C  CE  B LYS A 1 212 ? -20.058 -12.243 28.211  0.50 18.20 ? 212 LYS A CE  1 
ATOM   2209 N  NZ  A LYS A 1 212 ? -21.353 -8.342  28.051  0.50 25.57 ? 212 LYS A NZ  1 
ATOM   2210 N  NZ  B LYS A 1 212 ? -20.652 -12.601 29.530  0.50 26.46 ? 212 LYS A NZ  1 
ATOM   2211 N  N   . GLU A 1 213 ? -19.818 -9.474  23.059  1.00 7.81  ? 213 GLU A N   1 
ATOM   2212 C  CA  . GLU A 1 213 ? -20.403 -10.364 22.072  1.00 8.57  ? 213 GLU A CA  1 
ATOM   2213 C  C   . GLU A 1 213 ? -19.644 -10.316 20.789  1.00 6.79  ? 213 GLU A C   1 
ATOM   2214 O  O   . GLU A 1 213 ? -19.558 -9.245  20.200  1.00 8.25  ? 213 GLU A O   1 
ATOM   2215 C  CB  . GLU A 1 213 ? -21.871 -9.974  21.844  1.00 10.02 ? 213 GLU A CB  1 
ATOM   2216 C  CG  . GLU A 1 213 ? -22.635 -10.940 20.933  1.00 12.23 ? 213 GLU A CG  1 
ATOM   2217 C  CD  . GLU A 1 213 ? -24.048 -10.423 20.660  1.00 14.93 ? 213 GLU A CD  1 
ATOM   2218 O  OE1 . GLU A 1 213 ? -24.653 -9.827  21.581  1.00 15.52 ? 213 GLU A OE1 1 
ATOM   2219 O  OE2 . GLU A 1 213 ? -24.564 -10.593 19.531  1.00 20.46 ? 213 GLU A OE2 1 
ATOM   2220 N  N   A PRO A 1 214 ? -19.136 -11.457 20.302  0.50 8.04  ? 214 PRO A N   1 
ATOM   2221 N  N   B PRO A 1 214 ? -19.029 -11.428 20.363  0.50 7.95  ? 214 PRO A N   1 
ATOM   2222 C  CA  A PRO A 1 214 ? -18.512 -11.384 19.007  0.50 8.38  ? 214 PRO A CA  1 
ATOM   2223 C  CA  B PRO A 1 214 ? -18.384 -11.433 19.049  0.50 8.35  ? 214 PRO A CA  1 
ATOM   2224 C  C   A PRO A 1 214 ? -19.525 -11.296 17.904  0.50 7.78  ? 214 PRO A C   1 
ATOM   2225 C  C   B PRO A 1 214 ? -19.402 -11.454 17.898  0.50 8.24  ? 214 PRO A C   1 
ATOM   2226 O  O   A PRO A 1 214 ? -20.714 -11.579 18.117  0.50 8.55  ? 214 PRO A O   1 
ATOM   2227 O  O   B PRO A 1 214 ? -20.504 -11.960 18.079  0.50 9.42  ? 214 PRO A O   1 
ATOM   2228 C  CB  A PRO A 1 214 ? -17.799 -12.753 18.858  0.50 7.81  ? 214 PRO A CB  1 
ATOM   2229 C  CB  B PRO A 1 214 ? -17.572 -12.776 19.049  0.50 8.58  ? 214 PRO A CB  1 
ATOM   2230 C  CG  A PRO A 1 214 ? -18.547 -13.676 19.771  0.50 8.71  ? 214 PRO A CG  1 
ATOM   2231 C  CG  B PRO A 1 214 ? -17.486 -13.162 20.497  0.50 11.28 ? 214 PRO A CG  1 
ATOM   2232 C  CD  A PRO A 1 214 ? -19.157 -12.825 20.872  0.50 8.39  ? 214 PRO A CD  1 
ATOM   2233 C  CD  B PRO A 1 214 ? -18.758 -12.658 21.148  0.50 9.36  ? 214 PRO A CD  1 
ATOM   2234 N  N   . ILE A 1 215 ? -19.042 -10.954 16.713  1.00 8.01  ? 215 ILE A N   1 
ATOM   2235 C  CA  . ILE A 1 215 ? -19.818 -11.227 15.508  1.00 8.63  ? 215 ILE A CA  1 
ATOM   2236 C  C   . ILE A 1 215 ? -19.300 -12.483 14.843  1.00 8.64  ? 215 ILE A C   1 
ATOM   2237 O  O   . ILE A 1 215 ? -18.128 -12.846 15.021  1.00 9.04  ? 215 ILE A O   1 
ATOM   2238 C  CB  . ILE A 1 215 ? -19.824 -10.038 14.514  1.00 9.29  ? 215 ILE A CB  1 
ATOM   2239 C  CG1 . ILE A 1 215 ? -18.420 -9.684  14.052  1.00 9.61  ? 215 ILE A CG1 1 
ATOM   2240 C  CG2 . ILE A 1 215 ? -20.487 -8.799  15.168  1.00 10.69 ? 215 ILE A CG2 1 
ATOM   2241 C  CD1 . ILE A 1 215 ? -18.445 -8.716  12.844  1.00 12.27 ? 215 ILE A CD1 1 
ATOM   2242 N  N   A SER A 1 216 ? -20.181 -13.162 14.094  0.50 9.36  ? 216 SER A N   1 
ATOM   2243 N  N   B SER A 1 216 ? -20.206 -13.172 14.134  0.50 9.20  ? 216 SER A N   1 
ATOM   2244 C  CA  A SER A 1 216 ? -19.723 -14.262 13.272  0.50 9.49  ? 216 SER A CA  1 
ATOM   2245 C  CA  B SER A 1 216 ? -19.858 -14.317 13.319  0.50 9.72  ? 216 SER A CA  1 
ATOM   2246 C  C   A SER A 1 216 ? -19.530 -13.792 11.875  0.50 8.16  ? 216 SER A C   1 
ATOM   2247 C  C   B SER A 1 216 ? -19.602 -13.895 11.878  0.50 8.83  ? 216 SER A C   1 
ATOM   2248 O  O   A SER A 1 216 ? -20.315 -13.010 11.340  0.50 9.49  ? 216 SER A O   1 
ATOM   2249 O  O   B SER A 1 216 ? -20.438 -13.189 11.323  0.50 10.28 ? 216 SER A O   1 
ATOM   2250 C  CB  A SER A 1 216 ? -20.721 -15.418 13.245  0.50 8.87  ? 216 SER A CB  1 
ATOM   2251 C  CB  B SER A 1 216 ? -21.028 -15.296 13.322  0.50 12.83 ? 216 SER A CB  1 
ATOM   2252 O  OG  A SER A 1 216 ? -20.907 -15.967 14.517  0.50 11.03 ? 216 SER A OG  1 
ATOM   2253 O  OG  B SER A 1 216 ? -20.609 -16.434 12.634  0.50 14.82 ? 216 SER A OG  1 
ATOM   2254 N  N   . VAL A 1 217 ? -18.454 -14.288 11.284  1.00 8.92  ? 217 VAL A N   1 
ATOM   2255 C  CA  . VAL A 1 217 ? -18.183 -14.109 9.868   1.00 8.90  ? 217 VAL A CA  1 
ATOM   2256 C  C   . VAL A 1 217 ? -17.943 -15.476 9.287   1.00 9.31  ? 217 VAL A C   1 
ATOM   2257 O  O   . VAL A 1 217 ? -17.572 -16.455 9.986   1.00 9.49  ? 217 VAL A O   1 
ATOM   2258 C  CB  . VAL A 1 217 ? -16.964 -13.181 9.664   1.00 9.65  ? 217 VAL A CB  1 
ATOM   2259 C  CG1 . VAL A 1 217 ? -17.236 -11.830 10.321  1.00 10.13 ? 217 VAL A CG1 1 
ATOM   2260 C  CG2 . VAL A 1 217 ? -15.694 -13.776 10.204  1.00 11.58 ? 217 VAL A CG2 1 
ATOM   2261 N  N   . SER A 1 218 ? -18.080 -15.621 7.975   1.00 9.29  ? 218 SER A N   1 
ATOM   2262 C  CA  . SER A 1 218 ? -17.908 -16.952 7.404   1.00 10.67 ? 218 SER A CA  1 
ATOM   2263 C  C   . SER A 1 218 ? -16.446 -17.191 7.088   1.00 9.57  ? 218 SER A C   1 
ATOM   2264 O  O   . SER A 1 218 ? -15.623 -16.280 6.924   1.00 9.53  ? 218 SER A O   1 
ATOM   2265 C  CB  . SER A 1 218 ? -18.728 -17.113 6.150   1.00 11.06 ? 218 SER A CB  1 
ATOM   2266 O  OG  . SER A 1 218 ? -18.296 -16.228 5.166   1.00 11.39 ? 218 SER A OG  1 
ATOM   2267 N  N   A SER A 1 219 ? -16.127 -18.462 6.931   0.50 10.17 ? 219 SER A N   1 
ATOM   2268 N  N   B SER A 1 219 ? -16.086 -18.455 6.915   0.50 10.23 ? 219 SER A N   1 
ATOM   2269 C  CA  A SER A 1 219 ? -14.806 -18.836 6.458   0.50 10.90 ? 219 SER A CA  1 
ATOM   2270 C  CA  B SER A 1 219 ? -14.735 -18.790 6.432   0.50 11.21 ? 219 SER A CA  1 
ATOM   2271 C  C   A SER A 1 219 ? -14.464 -18.159 5.122   0.50 11.56 ? 219 SER A C   1 
ATOM   2272 C  C   B SER A 1 219 ? -14.431 -18.141 5.086   0.50 11.44 ? 219 SER A C   1 
ATOM   2273 O  O   A SER A 1 219 ? -13.367 -17.670 4.944   0.50 12.74 ? 219 SER A O   1 
ATOM   2274 O  O   B SER A 1 219 ? -13.322 -17.694 4.848   0.50 12.77 ? 219 SER A O   1 
ATOM   2275 C  CB  A SER A 1 219 ? -14.663 -20.359 6.440   0.50 12.05 ? 219 SER A CB  1 
ATOM   2276 C  CB  B SER A 1 219 ? -14.547 -20.304 6.372   0.50 14.67 ? 219 SER A CB  1 
ATOM   2277 O  OG  A SER A 1 219 ? -15.560 -20.931 5.481   0.50 10.80 ? 219 SER A OG  1 
ATOM   2278 O  OG  B SER A 1 219 ? -13.193 -20.704 6.322   0.50 19.34 ? 219 SER A OG  1 
ATOM   2279 N  N   . GLU A 1 220 ? -15.411 -18.053 4.198   1.00 11.56 ? 220 GLU A N   1 
ATOM   2280 C  CA  . GLU A 1 220 ? -15.165 -17.382 2.923   1.00 13.30 ? 220 GLU A CA  1 
ATOM   2281 C  C   . GLU A 1 220 ? -14.863 -15.920 3.105   1.00 11.74 ? 220 GLU A C   1 
ATOM   2282 O  O   . GLU A 1 220 ? -14.035 -15.354 2.369   1.00 13.67 ? 220 GLU A O   1 
ATOM   2283 C  CB  . GLU A 1 220 ? -16.331 -17.496 1.965   1.00 16.40 ? 220 GLU A CB  1 
ATOM   2284 C  CG  . GLU A 1 220 ? -16.587 -18.971 1.508   1.00 18.46 ? 220 GLU A CG  1 
ATOM   2285 C  CD  . GLU A 1 220 ? -17.507 -19.731 2.438   1.00 17.88 ? 220 GLU A CD  1 
ATOM   2286 O  OE1 . GLU A 1 220 ? -17.970 -19.229 3.484   1.00 17.14 ? 220 GLU A OE1 1 
ATOM   2287 O  OE2 . GLU A 1 220 ? -17.879 -20.872 2.053   1.00 28.80 ? 220 GLU A OE2 1 
ATOM   2288 N  N   . GLN A 1 221 ? -15.501 -15.257 4.071   1.00 10.49 ? 221 GLN A N   1 
ATOM   2289 C  CA  . GLN A 1 221 ? -15.208 -13.861 4.311   1.00 10.10 ? 221 GLN A CA  1 
ATOM   2290 C  C   . GLN A 1 221 ? -13.775 -13.660 4.824   1.00 10.68 ? 221 GLN A C   1 
ATOM   2291 O  O   . GLN A 1 221 ? -12.995 -12.796 4.329   1.00 11.19 ? 221 GLN A O   1 
ATOM   2292 C  CB  . GLN A 1 221 ? -16.221 -13.269 5.242   1.00 10.64 ? 221 GLN A CB  1 
ATOM   2293 C  CG  . GLN A 1 221 ? -17.607 -13.125 4.613   1.00 10.84 ? 221 GLN A CG  1 
ATOM   2294 C  CD  . GLN A 1 221 ? -18.709 -12.603 5.475   1.00 11.48 ? 221 GLN A CD  1 
ATOM   2295 O  OE1 . GLN A 1 221 ? -18.818 -12.955 6.662   1.00 10.54 ? 221 GLN A OE1 1 
ATOM   2296 N  NE2 . GLN A 1 221 ? -19.533 -11.729 4.916   1.00 12.79 ? 221 GLN A NE2 1 
ATOM   2297 N  N   A VAL A 1 222 ? -13.399 -14.442 5.840   0.50 10.43 ? 222 VAL A N   1 
ATOM   2298 N  N   B VAL A 1 222 ? -13.392 -14.451 5.830   0.50 10.64 ? 222 VAL A N   1 
ATOM   2299 C  CA  A VAL A 1 222 ? -12.074 -14.264 6.396   0.50 11.50 ? 222 VAL A CA  1 
ATOM   2300 C  CA  B VAL A 1 222 ? -12.036 -14.368 6.356   0.50 11.73 ? 222 VAL A CA  1 
ATOM   2301 C  C   A VAL A 1 222 ? -10.967 -14.751 5.411   0.50 12.08 ? 222 VAL A C   1 
ATOM   2302 C  C   B VAL A 1 222 ? -10.979 -14.707 5.329   0.50 11.96 ? 222 VAL A C   1 
ATOM   2303 O  O   A VAL A 1 222 ? -9.861  -14.196 5.397   0.50 12.61 ? 222 VAL A O   1 
ATOM   2304 O  O   B VAL A 1 222 ? -9.915  -14.079 5.250   0.50 11.31 ? 222 VAL A O   1 
ATOM   2305 C  CB  A VAL A 1 222 ? -11.985 -14.797 7.837   0.50 10.95 ? 222 VAL A CB  1 
ATOM   2306 C  CB  B VAL A 1 222 ? -11.872 -15.316 7.509   0.50 13.50 ? 222 VAL A CB  1 
ATOM   2307 C  CG1 A VAL A 1 222 ? -11.972 -16.328 7.806   0.50 12.58 ? 222 VAL A CG1 1 
ATOM   2308 C  CG1 B VAL A 1 222 ? -10.413 -15.401 7.900   0.50 16.13 ? 222 VAL A CG1 1 
ATOM   2309 C  CG2 A VAL A 1 222 ? -10.757 -14.246 8.503   0.50 10.35 ? 222 VAL A CG2 1 
ATOM   2310 C  CG2 B VAL A 1 222 ? -12.708 -14.759 8.630   0.50 14.63 ? 222 VAL A CG2 1 
ATOM   2311 N  N   . LEU A 1 223 ? -11.301 -15.686 4.512   1.00 12.29 ? 223 LEU A N   1 
ATOM   2312 C  CA  . LEU A 1 223 ? -10.377 -16.057 3.475   1.00 15.13 ? 223 LEU A CA  1 
ATOM   2313 C  C   . LEU A 1 223 ? -10.073 -14.880 2.556   1.00 13.32 ? 223 LEU A C   1 
ATOM   2314 O  O   . LEU A 1 223 ? -8.932  -14.758 2.077   1.00 14.58 ? 223 LEU A O   1 
ATOM   2315 C  CB  . LEU A 1 223 ? -10.856 -17.297 2.718   1.00 20.32 ? 223 LEU A CB  1 
ATOM   2316 C  CG  . LEU A 1 223 ? -10.574 -18.607 3.484   1.00 27.84 ? 223 LEU A CG  1 
ATOM   2317 C  CD1 . LEU A 1 223 ? -11.293 -19.783 2.865   1.00 37.04 ? 223 LEU A CD1 1 
ATOM   2318 C  CD2 . LEU A 1 223 ? -9.086  -18.907 3.604   1.00 34.99 ? 223 LEU A CD2 1 
ATOM   2319 N  N   . LYS A 1 224 ? -11.038 -14.014 2.316   1.00 12.73 ? 224 LYS A N   1 
ATOM   2320 C  CA  . LYS A 1 224 ? -10.780 -12.854 1.468   1.00 13.72 ? 224 LYS A CA  1 
ATOM   2321 C  C   . LYS A 1 224 ? -9.816  -11.872 2.181   1.00 11.12 ? 224 LYS A C   1 
ATOM   2322 O  O   . LYS A 1 224 ? -8.979  -11.265 1.529   1.00 13.11 ? 224 LYS A O   1 
ATOM   2323 C  CB  . LYS A 1 224 ? -12.087 -12.251 1.065   1.00 18.44 ? 224 LYS A CB  1 
ATOM   2324 C  CG  . LYS A 1 224 ? -12.704 -13.167 0.006   1.00 23.21 ? 224 LYS A CG  1 
ATOM   2325 C  CD  . LYS A 1 224 ? -14.149 -12.915 -0.367  1.00 30.97 ? 224 LYS A CD  1 
ATOM   2326 C  CE  . LYS A 1 224 ? -14.312 -12.110 -1.641  1.00 36.51 ? 224 LYS A CE  1 
ATOM   2327 N  NZ  . LYS A 1 224 ? -13.531 -12.734 -2.741  1.00 40.49 ? 224 LYS A NZ  1 
ATOM   2328 N  N   . PHE A 1 225 ? -9.918  -11.740 3.500   1.00 10.87 ? 225 PHE A N   1 
ATOM   2329 C  CA  . PHE A 1 225 ? -9.009  -10.868 4.195   1.00 9.82  ? 225 PHE A CA  1 
ATOM   2330 C  C   . PHE A 1 225 ? -7.579  -11.431 3.963   1.00 10.06 ? 225 PHE A C   1 
ATOM   2331 O  O   . PHE A 1 225 ? -6.638  -10.668 3.750   1.00 10.77 ? 225 PHE A O   1 
ATOM   2332 C  CB  . PHE A 1 225 ? -9.208  -10.942 5.717   1.00 10.70 ? 225 PHE A CB  1 
ATOM   2333 C  CG  . PHE A 1 225 ? -10.372 -10.169 6.278   1.00 11.45 ? 225 PHE A CG  1 
ATOM   2334 C  CD1 . PHE A 1 225 ? -11.332 -9.570  5.484   1.00 14.87 ? 225 PHE A CD1 1 
ATOM   2335 C  CD2 . PHE A 1 225 ? -10.493 -10.070 7.658   1.00 12.93 ? 225 PHE A CD2 1 
ATOM   2336 C  CE1 . PHE A 1 225 ? -12.385 -8.877  6.066   1.00 15.48 ? 225 PHE A CE1 1 
ATOM   2337 C  CE2 . PHE A 1 225 ? -11.536 -9.384  8.241   1.00 15.01 ? 225 PHE A CE2 1 
ATOM   2338 C  CZ  . PHE A 1 225 ? -12.486 -8.785  7.444   1.00 13.73 ? 225 PHE A CZ  1 
ATOM   2339 N  N   . ARG A 1 226 ? -7.441  -12.786 4.022   1.00 10.04 ? 226 ARG A N   1 
ATOM   2340 C  CA  . ARG A 1 226 ? -6.134  -13.394 3.977   1.00 10.33 ? 226 ARG A CA  1 
ATOM   2341 C  C   . ARG A 1 226 ? -5.520  -13.424 2.560   1.00 11.31 ? 226 ARG A C   1 
ATOM   2342 O  O   . ARG A 1 226 ? -4.381  -13.812 2.436   1.00 12.27 ? 226 ARG A O   1 
ATOM   2343 C  CB  . ARG A 1 226 ? -6.199  -14.837 4.472   1.00 10.56 ? 226 ARG A CB  1 
ATOM   2344 C  CG  . ARG A 1 226 ? -6.629  -14.957 5.952   1.00 10.47 ? 226 ARG A CG  1 
ATOM   2345 C  CD  . ARG A 1 226 ? -6.653  -16.401 6.394   1.00 12.55 ? 226 ARG A CD  1 
ATOM   2346 N  NE  . ARG A 1 226 ? -7.089  -16.513 7.745   1.00 10.84 ? 226 ARG A NE  1 
ATOM   2347 C  CZ  . ARG A 1 226 ? -7.897  -17.450 8.230   1.00 11.67 ? 226 ARG A CZ  1 
ATOM   2348 N  NH1 . ARG A 1 226 ? -8.328  -18.445 7.432   1.00 15.40 ? 226 ARG A NH1 1 
ATOM   2349 N  NH2 . ARG A 1 226 ? -8.297  -17.413 9.458   1.00 12.88 ? 226 ARG A NH2 1 
ATOM   2350 N  N   . LYS A 1 227 ? -6.241  -12.939 1.563   1.00 10.46 ? 227 LYS A N   1 
ATOM   2351 C  CA  . LYS A 1 227 ? -5.652  -12.830 0.241   1.00 11.88 ? 227 LYS A CA  1 
ATOM   2352 C  C   . LYS A 1 227 ? -5.089  -11.448 -0.028  1.00 12.13 ? 227 LYS A C   1 
ATOM   2353 O  O   . LYS A 1 227 ? -4.431  -11.236 -1.055  1.00 14.39 ? 227 LYS A O   1 
ATOM   2354 C  CB  . LYS A 1 227 ? -6.772  -13.025 -0.807  1.00 14.75 ? 227 LYS A CB  1 
ATOM   2355 C  CG  . LYS A 1 227 ? -7.300  -14.427 -0.896  1.00 19.59 ? 227 LYS A CG  1 
ATOM   2356 C  CD  . LYS A 1 227 ? -8.366  -14.577 -2.022  1.00 25.27 ? 227 LYS A CD  1 
ATOM   2357 C  CE  . LYS A 1 227 ? -7.786  -14.816 -3.417  1.00 34.12 ? 227 LYS A CE  1 
ATOM   2358 N  NZ  . LYS A 1 227 ? -8.805  -14.826 -4.554  1.00 59.71 ? 227 LYS A NZ  1 
ATOM   2359 N  N   . LEU A 1 228 ? -5.275  -10.498 0.873   1.00 11.39 ? 228 LEU A N   1 
ATOM   2360 C  CA  . LEU A 1 228 ? -4.599  -9.248  0.821   1.00 12.69 ? 228 LEU A CA  1 
ATOM   2361 C  C   . LEU A 1 228 ? -3.118  -9.433  0.931   1.00 13.41 ? 228 LEU A C   1 
ATOM   2362 O  O   . LEU A 1 228 ? -2.610  -10.489 1.343   1.00 14.03 ? 228 LEU A O   1 
ATOM   2363 C  CB  . LEU A 1 228 ? -5.131  -8.272  1.905   1.00 12.88 ? 228 LEU A CB  1 
ATOM   2364 C  CG  . LEU A 1 228 ? -6.518  -7.758  1.634   1.00 13.23 ? 228 LEU A CG  1 
ATOM   2365 C  CD1 . LEU A 1 228 ? -7.050  -7.134  2.957   1.00 13.06 ? 228 LEU A CD1 1 
ATOM   2366 C  CD2 . LEU A 1 228 ? -6.610  -6.735  0.499   1.00 16.58 ? 228 LEU A CD2 1 
ATOM   2367 N  N   . ASN A 1 229 ? -2.385  -8.389  0.508   1.00 14.51 ? 229 ASN A N   1 
ATOM   2368 C  CA  . ASN A 1 229 ? -0.907  -8.416  0.563   1.00 14.41 ? 229 ASN A CA  1 
ATOM   2369 C  C   . ASN A 1 229 ? -0.330  -7.277  1.397   1.00 14.96 ? 229 ASN A C   1 
ATOM   2370 O  O   . ASN A 1 229 ? -0.849  -6.121  1.309   1.00 16.23 ? 229 ASN A O   1 
ATOM   2371 C  CB  . ASN A 1 229 ? -0.235  -8.241  -0.836  1.00 16.07 ? 229 ASN A CB  1 
ATOM   2372 C  CG  . ASN A 1 229 ? -0.317  -9.430  -1.783  1.00 18.11 ? 229 ASN A CG  1 
ATOM   2373 O  OD1 . ASN A 1 229 ? 0.195   -9.290  -2.884  1.00 21.91 ? 229 ASN A OD1 1 
ATOM   2374 N  ND2 . ASN A 1 229 ? -0.990  -10.535 -1.415  1.00 15.94 ? 229 ASN A ND2 1 
ATOM   2375 N  N   A PHE A 1 230 ? 0.696   -7.460  2.168   0.50 16.90 ? 230 PHE A N   1 
ATOM   2376 N  N   B PHE A 1 230 ? 0.769   -7.673  2.163   0.50 15.05 ? 230 PHE A N   1 
ATOM   2377 C  CA  A PHE A 1 230 ? 1.188   -6.278  2.777   0.50 10.89 ? 230 PHE A CA  1 
ATOM   2378 C  CA  B PHE A 1 230 ? 1.801   -6.830  2.953   0.50 9.05  ? 230 PHE A CA  1 
ATOM   2379 C  C   A PHE A 1 230 ? 1.951   -5.472  1.735   0.50 10.51 ? 230 PHE A C   1 
ATOM   2380 C  C   B PHE A 1 230 ? 2.695   -5.998  2.020   0.50 10.84 ? 230 PHE A C   1 
ATOM   2381 O  O   A PHE A 1 230 ? 2.199   -4.293  1.943   0.50 10.46 ? 230 PHE A O   1 
ATOM   2382 O  O   B PHE A 1 230 ? 2.937   -4.819  2.231   0.50 9.97  ? 230 PHE A O   1 
ATOM   2383 C  CB  A PHE A 1 230 ? 2.153   -6.773  3.804   0.50 10.69 ? 230 PHE A CB  1 
ATOM   2384 C  CB  B PHE A 1 230 ? 2.792   -7.549  3.938   0.50 9.69  ? 230 PHE A CB  1 
ATOM   2385 C  CG  A PHE A 1 230 ? 1.535   -7.408  5.013   0.50 9.11  ? 230 PHE A CG  1 
ATOM   2386 C  CG  B PHE A 1 230 ? 2.203   -8.056  5.241   0.50 10.30 ? 230 PHE A CG  1 
ATOM   2387 C  CD1 A PHE A 1 230 ? 0.792   -6.649  5.874   0.50 8.86  ? 230 PHE A CD1 1 
ATOM   2388 C  CD1 B PHE A 1 230 ? 1.546   -7.195  6.123   0.50 10.43 ? 230 PHE A CD1 1 
ATOM   2389 C  CD2 A PHE A 1 230 ? 1.942   -8.636  5.426   0.50 9.55  ? 230 PHE A CD2 1 
ATOM   2390 C  CD2 B PHE A 1 230 ? 2.474   -9.359  5.631   0.50 12.24 ? 230 PHE A CD2 1 
ATOM   2391 C  CE1 A PHE A 1 230 ? 0.361   -7.142  7.078   0.50 9.34  ? 230 PHE A CE1 1 
ATOM   2392 C  CE1 B PHE A 1 230 ? 1.105   -7.669  7.357   0.50 9.07  ? 230 PHE A CE1 1 
ATOM   2393 C  CE2 A PHE A 1 230 ? 1.481   -9.192  6.618   0.50 10.69 ? 230 PHE A CE2 1 
ATOM   2394 C  CE2 B PHE A 1 230 ? 2.020   -9.832  6.842   0.50 11.68 ? 230 PHE A CE2 1 
ATOM   2395 C  CZ  A PHE A 1 230 ? 0.673   -8.438  7.429   0.50 8.51  ? 230 PHE A CZ  1 
ATOM   2396 C  CZ  B PHE A 1 230 ? 1.316   -9.006  7.694   0.50 10.76 ? 230 PHE A CZ  1 
ATOM   2397 N  N   A ASN A 1 231 ? 2.419   -6.106  0.656   0.50 9.57  ? 231 ASN A N   1 
ATOM   2398 N  N   B ASN A 1 231 ? 3.268   -6.652  1.055   0.50 8.95  ? 231 ASN A N   1 
ATOM   2399 C  CA  A ASN A 1 231 ? 3.340   -5.477  -0.273  0.50 10.90 ? 231 ASN A CA  1 
ATOM   2400 C  CA  B ASN A 1 231 ? 4.214   -6.074  0.101   0.50 9.01  ? 231 ASN A CA  1 
ATOM   2401 C  C   A ASN A 1 231 ? 2.572   -4.565  -1.175  0.50 10.39 ? 231 ASN A C   1 
ATOM   2402 C  C   B ASN A 1 231 ? 3.532   -5.124  -0.874  0.50 9.30  ? 231 ASN A C   1 
ATOM   2403 O  O   A ASN A 1 231 ? 1.377   -4.703  -1.375  0.50 9.87  ? 231 ASN A O   1 
ATOM   2404 O  O   B ASN A 1 231 ? 2.305   -5.187  -1.096  0.50 9.96  ? 231 ASN A O   1 
ATOM   2405 C  CB  A ASN A 1 231 ? 3.983   -6.545  -1.172  0.50 12.19 ? 231 ASN A CB  1 
ATOM   2406 C  CB  B ASN A 1 231 ? 4.895   -7.155  -0.689  0.50 9.33  ? 231 ASN A CB  1 
ATOM   2407 C  CG  A ASN A 1 231 ? 2.956   -7.487  -1.737  0.50 11.34 ? 231 ASN A CG  1 
ATOM   2408 C  CG  B ASN A 1 231 ? 3.928   -8.052  -1.406  0.50 8.69  ? 231 ASN A CG  1 
ATOM   2409 O  OD1 A ASN A 1 231 ? 2.460   -8.371  -1.002  0.50 13.62 ? 231 ASN A OD1 1 
ATOM   2410 O  OD1 B ASN A 1 231 ? 3.635   -7.910  -2.655  0.50 11.11 ? 231 ASN A OD1 1 
ATOM   2411 N  ND2 A ASN A 1 231 ? 2.662   -7.371  -3.041  0.50 14.78 ? 231 ASN A ND2 1 
ATOM   2412 N  ND2 B ASN A 1 231 ? 3.360   -8.941  -0.632  0.50 8.52  ? 231 ASN A ND2 1 
ATOM   2413 N  N   A GLY A 1 232 ? 3.305   -3.680  -1.803  0.50 11.88 ? 232 GLY A N   1 
ATOM   2414 N  N   B GLY A 1 232 ? 4.324   -4.210  -1.449  0.50 9.21  ? 232 GLY A N   1 
ATOM   2415 C  CA  A GLY A 1 232 ? 2.773   -2.944  -2.922  0.50 12.64 ? 232 GLY A CA  1 
ATOM   2416 C  CA  B GLY A 1 232 ? 3.852   -3.498  -2.618  0.50 10.12 ? 232 GLY A CA  1 
ATOM   2417 C  C   A GLY A 1 232 ? 2.862   -3.748  -4.171  0.50 12.04 ? 232 GLY A C   1 
ATOM   2418 C  C   B GLY A 1 232 ? 3.989   -4.312  -3.877  0.50 10.74 ? 232 GLY A C   1 
ATOM   2419 O  O   A GLY A 1 232 ? 3.505   -4.806  -4.237  0.50 16.86 ? 232 GLY A O   1 
ATOM   2420 O  O   B GLY A 1 232 ? 4.630   -5.340  -3.890  0.50 10.30 ? 232 GLY A O   1 
ATOM   2421 N  N   A GLU A 1 233 ? 2.175   -3.329  -5.181  0.50 12.88 ? 233 GLU A N   1 
ATOM   2422 N  N   B GLU A 1 233 ? 3.260   -3.931  -4.902  0.50 11.30 ? 233 GLU A N   1 
ATOM   2423 C  CA  A GLU A 1 233 ? 2.402   -4.218  -6.284  0.50 15.91 ? 233 GLU A CA  1 
ATOM   2424 C  CA  B GLU A 1 233 ? 3.395   -4.600  -6.180  0.50 12.07 ? 233 GLU A CA  1 
ATOM   2425 C  C   A GLU A 1 233 ? 3.773   -4.149  -6.899  0.50 19.75 ? 233 GLU A C   1 
ATOM   2426 C  C   B GLU A 1 233 ? 4.804   -4.518  -6.678  0.50 12.85 ? 233 GLU A C   1 
ATOM   2427 O  O   A GLU A 1 233 ? 4.161   -3.062  -7.087  0.50 20.54 ? 233 GLU A O   1 
ATOM   2428 O  O   B GLU A 1 233 ? 5.392   -3.533  -6.498  0.50 13.49 ? 233 GLU A O   1 
ATOM   2429 C  CB  A GLU A 1 233 ? 1.495   -3.920  -7.355  0.50 20.34 ? 233 GLU A CB  1 
ATOM   2430 C  CB  B GLU A 1 233 ? 2.523   -3.859  -7.154  0.50 16.81 ? 233 GLU A CB  1 
ATOM   2431 C  CG  A GLU A 1 233 ? 1.034   -2.556  -7.427  0.50 15.17 ? 233 GLU A CG  1 
ATOM   2432 C  CG  B GLU A 1 233 ? 2.255   -4.628  -8.444  0.50 16.17 ? 233 GLU A CG  1 
ATOM   2433 C  CD  A GLU A 1 233 ? 0.301   -2.473  -8.723  0.50 21.85 ? 233 GLU A CD  1 
ATOM   2434 C  CD  B GLU A 1 233 ? 1.068   -4.058  -9.212  0.50 18.88 ? 233 GLU A CD  1 
ATOM   2435 O  OE1 A GLU A 1 233 ? 0.192   -3.635  -9.180  0.50 20.00 ? 233 GLU A OE1 1 
ATOM   2436 O  OE1 B GLU A 1 233 ? 0.719   -4.641  -10.273 0.50 22.04 ? 233 GLU A OE1 1 
ATOM   2437 O  OE2 A GLU A 1 233 ? -0.119  -1.385  -9.247  0.50 22.99 ? 233 GLU A OE2 1 
ATOM   2438 O  OE2 B GLU A 1 233 ? 0.512   -3.017  -8.815  0.50 24.28 ? 233 GLU A OE2 1 
ATOM   2439 N  N   A GLY A 1 234 ? 4.425   -5.299  -7.255  0.50 24.05 ? 234 GLY A N   1 
ATOM   2440 N  N   B GLY A 1 234 ? 5.319   -5.591  -7.302  0.50 18.72 ? 234 GLY A N   1 
ATOM   2441 C  CA  A GLY A 1 234 ? 5.827   -5.425  -7.814  0.50 21.47 ? 234 GLY A CA  1 
ATOM   2442 C  CA  B GLY A 1 234 ? 6.733   -5.580  -7.900  0.50 12.64 ? 234 GLY A CA  1 
ATOM   2443 C  C   A GLY A 1 234 ? 6.914   -6.080  -6.942  0.50 17.75 ? 234 GLY A C   1 
ATOM   2444 C  C   B GLY A 1 234 ? 7.731   -6.064  -6.835  0.50 19.58 ? 234 GLY A C   1 
ATOM   2445 O  O   A GLY A 1 234 ? 8.050   -6.375  -7.375  0.50 27.20 ? 234 GLY A O   1 
ATOM   2446 O  O   B GLY A 1 234 ? 8.926   -6.232  -7.174  0.50 24.74 ? 234 GLY A O   1 
ATOM   2447 N  N   A GLU A 1 235 ? 6.487   -6.324  -5.711  0.50 12.88 ? 235 GLU A N   1 
ATOM   2448 N  N   B GLU A 1 235 ? 7.258   -6.332  -5.607  0.50 18.19 ? 235 GLU A N   1 
ATOM   2449 C  CA  A GLU A 1 235 ? 7.332   -6.669  -4.692  0.50 20.20 ? 235 GLU A CA  1 
ATOM   2450 C  CA  B GLU A 1 235 ? 8.090   -6.955  -4.571  0.50 14.71 ? 235 GLU A CA  1 
ATOM   2451 C  C   A GLU A 1 235 ? 6.807   -8.051  -4.510  0.50 17.61 ? 235 GLU A C   1 
ATOM   2452 C  C   B GLU A 1 235 ? 7.622   -8.392  -4.325  0.50 14.07 ? 235 GLU A C   1 
ATOM   2453 O  O   A GLU A 1 235 ? 5.609   -8.342  -4.858  0.50 22.68 ? 235 GLU A O   1 
ATOM   2454 O  O   B GLU A 1 235 ? 6.551   -8.777  -4.752  0.50 15.16 ? 235 GLU A O   1 
ATOM   2455 C  CB  A GLU A 1 235 ? 6.987   -5.742  -3.538  0.50 23.22 ? 235 GLU A CB  1 
ATOM   2456 C  CB  B GLU A 1 235 ? 7.978   -6.205  -3.227  0.50 15.97 ? 235 GLU A CB  1 
ATOM   2457 C  CG  A GLU A 1 235 ? 7.155   -4.292  -3.961  0.50 19.18 ? 235 GLU A CG  1 
ATOM   2458 C  CG  B GLU A 1 235 ? 8.323   -4.728  -3.264  0.50 20.73 ? 235 GLU A CG  1 
ATOM   2459 C  CD  A GLU A 1 235 ? 6.893   -3.354  -2.821  0.50 21.36 ? 235 GLU A CD  1 
ATOM   2460 C  CD  B GLU A 1 235 ? 7.981   -3.978  -1.979  0.50 23.91 ? 235 GLU A CD  1 
ATOM   2461 O  OE1 A GLU A 1 235 ? 6.229   -3.799  -1.869  0.50 24.50 ? 235 GLU A OE1 1 
ATOM   2462 O  OE1 B GLU A 1 235 ? 7.255   -4.494  -1.071  0.50 22.41 ? 235 GLU A OE1 1 
ATOM   2463 O  OE2 A GLU A 1 235 ? 7.362   -2.201  -2.896  0.50 26.91 ? 235 GLU A OE2 1 
ATOM   2464 O  OE2 B GLU A 1 235 ? 8.475   -2.818  -1.897  0.50 29.08 ? 235 GLU A OE2 1 
ATOM   2465 N  N   A PRO A 1 236 ? 7.629   -8.921  -3.945  0.50 20.81 ? 236 PRO A N   1 
ATOM   2466 N  N   B PRO A 1 236 ? 8.433   -9.257  -3.698  0.50 12.56 ? 236 PRO A N   1 
ATOM   2467 C  CA  A PRO A 1 236 ? 7.066   -10.224 -3.829  0.50 24.08 ? 236 PRO A CA  1 
ATOM   2468 C  CA  B PRO A 1 236 ? 7.982   -10.611 -3.470  0.50 12.91 ? 236 PRO A CA  1 
ATOM   2469 C  C   A PRO A 1 236 ? 5.761   -10.125 -3.035  0.50 16.93 ? 236 PRO A C   1 
ATOM   2470 C  C   B PRO A 1 236 ? 6.662   -10.661 -2.611  0.50 10.42 ? 236 PRO A C   1 
ATOM   2471 O  O   A PRO A 1 236 ? 5.599   -9.195  -2.192  0.50 17.99 ? 236 PRO A O   1 
ATOM   2472 O  O   B PRO A 1 236 ? 6.432   -9.894  -1.663  0.50 11.33 ? 236 PRO A O   1 
ATOM   2473 C  CB  A PRO A 1 236 ? 8.168   -10.999 -3.081  0.50 32.06 ? 236 PRO A CB  1 
ATOM   2474 C  CB  B PRO A 1 236 ? 9.120   -11.243 -2.649  0.50 13.02 ? 236 PRO A CB  1 
ATOM   2475 C  CG  A PRO A 1 236 ? 8.849   -9.913  -2.316  0.50 29.34 ? 236 PRO A CG  1 
ATOM   2476 C  CG  B PRO A 1 236 ? 9.844   -10.037 -2.045  0.50 21.03 ? 236 PRO A CG  1 
ATOM   2477 C  CD  A PRO A 1 236 ? 8.983   -8.867  -3.380  0.50 30.47 ? 236 PRO A CD  1 
ATOM   2478 C  CD  B PRO A 1 236 ? 9.757   -9.004  -3.167  0.50 14.87 ? 236 PRO A CD  1 
ATOM   2479 N  N   A GLU A 1 237 ? 4.889   -11.066 -3.364  0.50 18.43 ? 237 GLU A N   1 
ATOM   2480 N  N   B GLU A 1 237 ? 5.766   -11.571 -2.947  0.50 10.16 ? 237 GLU A N   1 
ATOM   2481 C  CA  A GLU A 1 237 ? 3.640   -11.216 -2.605  0.50 14.42 ? 237 GLU A CA  1 
ATOM   2482 C  CA  B GLU A 1 237 ? 4.471   -11.697 -2.291  0.50 10.90 ? 237 GLU A CA  1 
ATOM   2483 C  C   A GLU A 1 237 ? 3.891   -11.686 -1.201  0.50 11.18 ? 237 GLU A C   1 
ATOM   2484 C  C   B GLU A 1 237 ? 4.581   -12.307 -0.903  0.50 9.57  ? 237 GLU A C   1 
ATOM   2485 O  O   A GLU A 1 237 ? 4.436   -12.749 -0.997  0.50 12.07 ? 237 GLU A O   1 
ATOM   2486 O  O   B GLU A 1 237 ? 5.033   -13.443 -0.733  0.50 11.56 ? 237 GLU A O   1 
ATOM   2487 C  CB  A GLU A 1 237 ? 2.641   -12.175 -3.310  0.50 18.22 ? 237 GLU A CB  1 
ATOM   2488 C  CB  B GLU A 1 237 ? 3.509   -12.540 -3.134  0.50 10.86 ? 237 GLU A CB  1 
ATOM   2489 C  CG  A GLU A 1 237 ? 1.225   -12.176 -2.697  0.50 17.94 ? 237 GLU A CG  1 
ATOM   2490 C  CG  B GLU A 1 237 ? 2.150   -12.639 -2.485  0.50 12.97 ? 237 GLU A CG  1 
ATOM   2491 C  CD  A GLU A 1 237 ? 0.116   -12.681 -3.661  0.50 17.46 ? 237 GLU A CD  1 
ATOM   2492 C  CD  B GLU A 1 237 ? 1.091   -13.286 -3.352  0.50 14.45 ? 237 GLU A CD  1 
ATOM   2493 O  OE1 A GLU A 1 237 ? 0.446   -13.171 -4.785  0.50 30.79 ? 237 GLU A OE1 1 
ATOM   2494 O  OE1 B GLU A 1 237 ? 1.430   -13.975 -4.313  0.50 19.94 ? 237 GLU A OE1 1 
ATOM   2495 O  OE2 A GLU A 1 237 ? -1.106  -12.598 -3.333  0.50 15.05 ? 237 GLU A OE2 1 
ATOM   2496 O  OE2 B GLU A 1 237 ? -0.103  -13.077 -3.059  0.50 14.07 ? 237 GLU A OE2 1 
ATOM   2497 N  N   A GLU A 1 238 ? 3.397   -10.912 -0.241  0.50 11.01 ? 238 GLU A N   1 
ATOM   2498 N  N   B GLU A 1 238 ? 4.087   -11.561 0.082   0.50 9.86  ? 238 GLU A N   1 
ATOM   2499 C  CA  A GLU A 1 238 ? 3.417   -11.222 1.198   0.50 13.13 ? 238 GLU A CA  1 
ATOM   2500 C  CA  B GLU A 1 238 ? 3.943   -12.069 1.444   0.50 10.56 ? 238 GLU A CA  1 
ATOM   2501 C  C   A GLU A 1 238 ? 1.959   -11.120 1.668   0.50 12.59 ? 238 GLU A C   1 
ATOM   2502 C  C   B GLU A 1 238 ? 2.513   -11.744 1.841   0.50 11.65 ? 238 GLU A C   1 
ATOM   2503 O  O   A GLU A 1 238 ? 1.374   -10.048 1.688   0.50 12.14 ? 238 GLU A O   1 
ATOM   2504 O  O   B GLU A 1 238 ? 2.089   -10.578 1.821   0.50 11.23 ? 238 GLU A O   1 
ATOM   2505 C  CB  A GLU A 1 238 ? 4.483   -10.384 2.025   0.50 16.31 ? 238 GLU A CB  1 
ATOM   2506 C  CB  B GLU A 1 238 ? 4.931   -11.318 2.326   0.50 10.46 ? 238 GLU A CB  1 
ATOM   2507 C  CG  A GLU A 1 238 ? 5.970   -10.992 1.953   0.50 21.12 ? 238 GLU A CG  1 
ATOM   2508 C  CG  B GLU A 1 238 ? 6.407   -11.701 2.070   0.50 16.30 ? 238 GLU A CG  1 
ATOM   2509 C  CD  A GLU A 1 238 ? 7.131   -10.652 2.986   0.50 14.98 ? 238 GLU A CD  1 
ATOM   2510 C  CD  B GLU A 1 238 ? 7.375   -10.626 2.432   0.50 27.82 ? 238 GLU A CD  1 
ATOM   2511 O  OE1 A GLU A 1 238 ? 7.144   -11.020 4.210   0.50 18.92 ? 238 GLU A OE1 1 
ATOM   2512 O  OE1 B GLU A 1 238 ? 6.898   -9.444  2.708   0.50 48.10 ? 238 GLU A OE1 1 
ATOM   2513 O  OE2 A GLU A 1 238 ? 8.136   -9.981  2.565   0.50 14.29 ? 238 GLU A OE2 1 
ATOM   2514 O  OE2 B GLU A 1 238 ? 8.596   -10.994 2.425   0.50 34.16 ? 238 GLU A OE2 1 
ATOM   2515 N  N   A LEU A 1 239 ? 1.382   -12.290 1.978   0.50 11.86 ? 239 LEU A N   1 
ATOM   2516 N  N   B LEU A 1 239 ? 1.668   -12.724 2.127   0.50 13.05 ? 239 LEU A N   1 
ATOM   2517 C  CA  A LEU A 1 239 ? -0.014  -12.379 2.394   0.50 12.10 ? 239 LEU A CA  1 
ATOM   2518 C  CA  B LEU A 1 239 ? 0.232   -12.413 2.347   0.50 13.65 ? 239 LEU A CA  1 
ATOM   2519 C  C   A LEU A 1 239 ? -0.141  -11.601 3.677   0.50 11.70 ? 239 LEU A C   1 
ATOM   2520 C  C   B LEU A 1 239 ? -0.013  -11.511 3.605   0.50 12.27 ? 239 LEU A C   1 
ATOM   2521 O  O   A LEU A 1 239 ? 0.585   -11.823 4.669   0.50 12.30 ? 239 LEU A O   1 
ATOM   2522 O  O   B LEU A 1 239 ? 0.773   -11.609 4.560   0.50 13.98 ? 239 LEU A O   1 
ATOM   2523 C  CB  A LEU A 1 239 ? -0.454  -13.827 2.622   0.50 11.88 ? 239 LEU A CB  1 
ATOM   2524 C  CB  B LEU A 1 239 ? -0.546  -13.724 2.477   0.50 12.92 ? 239 LEU A CB  1 
ATOM   2525 C  CG  A LEU A 1 239 ? -0.713  -14.684 1.372   0.50 11.20 ? 239 LEU A CG  1 
ATOM   2526 C  CG  B LEU A 1 239 ? -0.442  -14.582 1.201   0.50 12.60 ? 239 LEU A CG  1 
ATOM   2527 C  CD1 A LEU A 1 239 ? -1.416  -15.889 1.970   0.50 13.02 ? 239 LEU A CD1 1 
ATOM   2528 C  CD1 B LEU A 1 239 ? -0.846  -15.973 1.566   0.50 14.10 ? 239 LEU A CD1 1 
ATOM   2529 C  CD2 A LEU A 1 239 ? -1.555  -13.902 0.367   0.50 10.52 ? 239 LEU A CD2 1 
ATOM   2530 C  CD2 B LEU A 1 239 ? -1.286  -13.995 0.072   0.50 15.21 ? 239 LEU A CD2 1 
ATOM   2531 N  N   . MET A 1 240 ? -1.116  -10.729 3.666   1.00 13.52 ? 240 MET A N   1 
ATOM   2532 C  CA  . MET A 1 240 ? -1.445  -9.906  4.853   1.00 12.20 ? 240 MET A CA  1 
ATOM   2533 C  C   . MET A 1 240 ? -2.241  -10.833 5.768   1.00 9.51  ? 240 MET A C   1 
ATOM   2534 O  O   . MET A 1 240 ? -3.468  -10.961 5.647   1.00 10.50 ? 240 MET A O   1 
ATOM   2535 C  CB  . MET A 1 240 ? -2.249  -8.718  4.380   1.00 13.78 ? 240 MET A CB  1 
ATOM   2536 C  CG  . MET A 1 240 ? -2.596  -7.757  5.537   1.00 12.74 ? 240 MET A CG  1 
ATOM   2537 S  SD  . MET A 1 240 ? -3.588  -6.343  5.036   1.00 13.72 ? 240 MET A SD  1 
ATOM   2538 C  CE  . MET A 1 240 ? -2.252  -5.301  4.357   1.00 14.31 ? 240 MET A CE  1 
ATOM   2539 N  N   . VAL A 1 241 ? -1.477  -11.408 6.707   1.00 10.15 ? 241 VAL A N   1 
ATOM   2540 C  CA  . VAL A 1 241 ? -2.038  -12.269 7.759   1.00 9.66  ? 241 VAL A CA  1 
ATOM   2541 C  C   . VAL A 1 241 ? -1.239  -12.057 9.013   1.00 8.48  ? 241 VAL A C   1 
ATOM   2542 O  O   . VAL A 1 241 ? -0.063  -11.645 8.968   1.00 10.57 ? 241 VAL A O   1 
ATOM   2543 C  CB  . VAL A 1 241 ? -1.994  -13.783 7.390   1.00 9.66  ? 241 VAL A CB  1 
ATOM   2544 C  CG1 . VAL A 1 241 ? -2.898  -14.102 6.207   1.00 11.52 ? 241 VAL A CG1 1 
ATOM   2545 C  CG2 . VAL A 1 241 ? -0.548  -14.262 7.160   1.00 12.52 ? 241 VAL A CG2 1 
ATOM   2546 N  N   . ASP A 1 242 ? -1.832  -12.326 10.201  1.00 8.30  ? 242 ASP A N   1 
ATOM   2547 C  CA  . ASP A 1 242 ? -1.131  -12.167 11.450  1.00 8.77  ? 242 ASP A CA  1 
ATOM   2548 C  C   . ASP A 1 242 ? -0.661  -10.752 11.684  1.00 8.39  ? 242 ASP A C   1 
ATOM   2549 O  O   . ASP A 1 242 ? 0.452   -10.513 12.159  1.00 10.21 ? 242 ASP A O   1 
ATOM   2550 C  CB  . ASP A 1 242 ? -0.053  -13.260 11.636  1.00 9.26  ? 242 ASP A CB  1 
ATOM   2551 C  CG  . ASP A 1 242 ? -0.629  -14.585 11.725  1.00 9.31  ? 242 ASP A CG  1 
ATOM   2552 O  OD1 . ASP A 1 242 ? -1.704  -14.792 12.426  1.00 8.65  ? 242 ASP A OD1 1 
ATOM   2553 O  OD2 . ASP A 1 242 ? -0.068  -15.544 11.149  1.00 10.87 ? 242 ASP A OD2 1 
ATOM   2554 N  N   . ASN A 1 243 ? -1.553  -9.808  11.380  1.00 7.90  ? 243 ASN A N   1 
ATOM   2555 C  CA  . ASN A 1 243 ? -1.297  -8.401  11.593  1.00 7.62  ? 243 ASN A CA  1 
ATOM   2556 C  C   . ASN A 1 243 ? -1.880  -7.916  12.939  1.00 7.67  ? 243 ASN A C   1 
ATOM   2557 O  O   . ASN A 1 243 ? -2.561  -6.912  13.024  1.00 8.41  ? 243 ASN A O   1 
ATOM   2558 C  CB  . ASN A 1 243 ? -1.837  -7.560  10.403  1.00 8.77  ? 243 ASN A CB  1 
ATOM   2559 C  CG  . ASN A 1 243 ? -3.301  -7.742  10.175  1.00 8.46  ? 243 ASN A CG  1 
ATOM   2560 O  OD1 . ASN A 1 243 ? -3.933  -8.599  10.784  1.00 9.18  ? 243 ASN A OD1 1 
ATOM   2561 N  ND2 . ASN A 1 243 ? -3.875  -6.998  9.239   1.00 10.89 ? 243 ASN A ND2 1 
ATOM   2562 N  N   . TRP A 1 244 ? -1.531  -8.640  13.989  1.00 7.46  ? 244 TRP A N   1 
ATOM   2563 C  CA  . TRP A 1 244 ? -1.992  -8.387  15.364  1.00 7.23  ? 244 TRP A CA  1 
ATOM   2564 C  C   . TRP A 1 244 ? -0.796  -8.269  16.265  1.00 7.25  ? 244 TRP A C   1 
ATOM   2565 O  O   . TRP A 1 244 ? 0.174   -8.988  16.179  1.00 8.55  ? 244 TRP A O   1 
ATOM   2566 C  CB  . TRP A 1 244 ? -2.957  -9.487  15.852  1.00 6.85  ? 244 TRP A CB  1 
ATOM   2567 C  CG  . TRP A 1 244 ? -2.484  -10.864 15.718  1.00 6.76  ? 244 TRP A CG  1 
ATOM   2568 C  CD1 . TRP A 1 244 ? -2.556  -11.647 14.578  1.00 7.57  ? 244 TRP A CD1 1 
ATOM   2569 C  CD2 . TRP A 1 244 ? -1.862  -11.709 16.722  1.00 7.17  ? 244 TRP A CD2 1 
ATOM   2570 N  NE1 . TRP A 1 244 ? -2.034  -12.885 14.801  1.00 7.74  ? 244 TRP A NE1 1 
ATOM   2571 C  CE2 . TRP A 1 244 ? -1.611  -12.969 16.094  1.00 7.92  ? 244 TRP A CE2 1 
ATOM   2572 C  CE3 . TRP A 1 244 ? -1.588  -11.541 18.076  1.00 7.70  ? 244 TRP A CE3 1 
ATOM   2573 C  CZ2 . TRP A 1 244 ? -1.012  -14.024 16.758  1.00 8.97  ? 244 TRP A CZ2 1 
ATOM   2574 C  CZ3 . TRP A 1 244 ? -1.015  -12.608 18.756  1.00 9.05  ? 244 TRP A CZ3 1 
ATOM   2575 C  CH2 . TRP A 1 244 ? -0.800  -13.836 18.114  1.00 9.54  ? 244 TRP A CH2 1 
ATOM   2576 N  N   . ARG A 1 245 ? -0.945  -7.340  17.221  1.00 7.25  ? 245 ARG A N   1 
ATOM   2577 C  CA  . ARG A 1 245 ? -0.008  -7.226  18.350  1.00 7.35  ? 245 ARG A CA  1 
ATOM   2578 C  C   . ARG A 1 245 ? -0.475  -8.119  19.476  1.00 6.60  ? 245 ARG A C   1 
ATOM   2579 O  O   . ARG A 1 245 ? -1.642  -8.114  19.800  1.00 7.72  ? 245 ARG A O   1 
ATOM   2580 C  CB  . ARG A 1 245 ? 0.064   -5.764  18.816  1.00 7.17  ? 245 ARG A CB  1 
ATOM   2581 C  CG  . ARG A 1 245 ? 1.186   -5.494  19.835  1.00 7.27  ? 245 ARG A CG  1 
ATOM   2582 C  CD  . ARG A 1 245 ? 1.092   -4.137  20.434  1.00 7.11  ? 245 ARG A CD  1 
ATOM   2583 N  NE  . ARG A 1 245 ? 2.340   -3.843  21.144  1.00 7.90  ? 245 ARG A NE  1 
ATOM   2584 C  CZ  . ARG A 1 245 ? 2.521   -2.818  21.974  1.00 8.12  ? 245 ARG A CZ  1 
ATOM   2585 N  NH1 . ARG A 1 245 ? 1.520   -2.038  22.322  1.00 8.46  ? 245 ARG A NH1 1 
ATOM   2586 N  NH2 . ARG A 1 245 ? 3.758   -2.526  22.385  1.00 9.55  ? 245 ARG A NH2 1 
ATOM   2587 N  N   A PRO A 1 246 ? 0.420   -8.908  20.064  0.50 7.19  ? 246 PRO A N   1 
ATOM   2588 N  N   B PRO A 1 246 ? 0.449   -8.875  20.104  0.50 7.35  ? 246 PRO A N   1 
ATOM   2589 C  CA  A PRO A 1 246 ? -0.041  -9.714  21.200  0.50 7.57  ? 246 PRO A CA  1 
ATOM   2590 C  CA  B PRO A 1 246 ? 0.027   -9.727  21.227  0.50 7.95  ? 246 PRO A CA  1 
ATOM   2591 C  C   A PRO A 1 246 ? -0.388  -8.859  22.453  0.50 7.25  ? 246 PRO A C   1 
ATOM   2592 C  C   B PRO A 1 246 ? -0.288  -8.890  22.486  0.50 7.21  ? 246 PRO A C   1 
ATOM   2593 O  O   A PRO A 1 246 ? -0.095  -7.663  22.561  0.50 7.09  ? 246 PRO A O   1 
ATOM   2594 O  O   B PRO A 1 246 ? 0.090   -7.728  22.609  0.50 7.65  ? 246 PRO A O   1 
ATOM   2595 C  CB  A PRO A 1 246 ? 1.163   -10.603 21.493  0.50 9.09  ? 246 PRO A CB  1 
ATOM   2596 C  CB  B PRO A 1 246 ? 1.259   -10.591 21.492  0.50 10.51 ? 246 PRO A CB  1 
ATOM   2597 C  CG  A PRO A 1 246 ? 1.985   -10.600 20.220  0.50 9.30  ? 246 PRO A CG  1 
ATOM   2598 C  CG  B PRO A 1 246 ? 2.390   -9.732  21.102  0.50 12.61 ? 246 PRO A CG  1 
ATOM   2599 C  CD  A PRO A 1 246 ? 1.815   -9.212  19.670  0.50 8.03  ? 246 PRO A CD  1 
ATOM   2600 C  CD  B PRO A 1 246 ? 1.920   -8.923  19.900  0.50 9.57  ? 246 PRO A CD  1 
ATOM   2601 N  N   . ALA A 1 247 ? -0.970  -9.534  23.416  1.00 8.09  ? 247 ALA A N   1 
ATOM   2602 C  CA  . ALA A 1 247 ? -1.318  -8.900  24.672  1.00 8.45  ? 247 ALA A CA  1 
ATOM   2603 C  C   . ALA A 1 247 ? -0.088  -8.398  25.407  1.00 7.77  ? 247 ALA A C   1 
ATOM   2604 O  O   . ALA A 1 247 ? 0.960   -9.040  25.446  1.00 9.37  ? 247 ALA A O   1 
ATOM   2605 C  CB  . ALA A 1 247 ? -2.083  -9.894  25.557  1.00 10.26 ? 247 ALA A CB  1 
ATOM   2606 N  N   . GLN A 1 248 ? -0.248  -7.202  25.975  1.00 7.64  ? 248 GLN A N   1 
ATOM   2607 C  CA  . GLN A 1 248 ? 0.787   -6.471  26.713  1.00 7.91  ? 248 GLN A CA  1 
ATOM   2608 C  C   . GLN A 1 248 ? 0.518   -6.493  28.205  1.00 9.07  ? 248 GLN A C   1 
ATOM   2609 O  O   . GLN A 1 248 ? -0.612  -6.713  28.616  1.00 9.43  ? 248 GLN A O   1 
ATOM   2610 C  CB  . GLN A 1 248 ? 0.835   -5.051  26.173  1.00 8.73  ? 248 GLN A CB  1 
ATOM   2611 C  CG  . GLN A 1 248 ? 1.158   -4.995  24.671  1.00 8.76  ? 248 GLN A CG  1 
ATOM   2612 C  CD  . GLN A 1 248 ? 2.485   -5.640  24.351  1.00 9.94  ? 248 GLN A CD  1 
ATOM   2613 O  OE1 . GLN A 1 248 ? 3.512   -5.287  24.907  1.00 12.14 ? 248 GLN A OE1 1 
ATOM   2614 N  NE2 . GLN A 1 248 ? 2.451   -6.574  23.405  1.00 10.81 ? 248 GLN A NE2 1 
ATOM   2615 N  N   . PRO A 1 249 ? 1.525   -6.180  29.037  1.00 9.98  ? 249 PRO A N   1 
ATOM   2616 C  CA  . PRO A 1 249 ? 1.311   -6.197  30.452  1.00 10.92 ? 249 PRO A CA  1 
ATOM   2617 C  C   . PRO A 1 249 ? 0.205   -5.257  30.896  1.00 9.70  ? 249 PRO A C   1 
ATOM   2618 O  O   . PRO A 1 249 ? 0.249   -4.059  30.571  1.00 9.67  ? 249 PRO A O   1 
ATOM   2619 C  CB  . PRO A 1 249 ? 2.672   -5.779  31.014  1.00 14.76 ? 249 PRO A CB  1 
ATOM   2620 C  CG  . PRO A 1 249 ? 3.636   -6.207  29.955  1.00 15.41 ? 249 PRO A CG  1 
ATOM   2621 C  CD  . PRO A 1 249 ? 2.909   -5.877  28.675  1.00 12.28 ? 249 PRO A CD  1 
ATOM   2622 N  N   . LEU A 1 250 ? -0.659  -5.724  31.809  1.00 10.35 ? 250 LEU A N   1 
ATOM   2623 C  CA  . LEU A 1 250 ? -1.735  -4.877  32.320  1.00 9.88  ? 250 LEU A CA  1 
ATOM   2624 C  C   . LEU A 1 250 ? -1.223  -3.775  33.219  1.00 9.95  ? 250 LEU A C   1 
ATOM   2625 O  O   . LEU A 1 250 ? -1.788  -2.692  33.283  1.00 10.66 ? 250 LEU A O   1 
ATOM   2626 C  CB  . LEU A 1 250 ? -2.758  -5.757  33.032  1.00 12.18 ? 250 LEU A CB  1 
ATOM   2627 C  CG  . LEU A 1 250 ? -4.098  -5.049  33.427  1.00 12.40 ? 250 LEU A CG  1 
ATOM   2628 C  CD1 . LEU A 1 250 ? -4.834  -4.436  32.250  1.00 13.03 ? 250 LEU A CD1 1 
ATOM   2629 C  CD2 . LEU A 1 250 ? -4.970  -6.023  34.208  1.00 18.70 ? 250 LEU A CD2 1 
ATOM   2630 N  N   . LYS A 1 251 ? -0.163  -4.064  33.944  1.00 11.64 ? 251 LYS A N   1 
ATOM   2631 C  CA  . LYS A 1 251 ? 0.409   -3.051  34.836  1.00 13.27 ? 251 LYS A CA  1 
ATOM   2632 C  C   . LYS A 1 251 ? -0.610  -2.515  35.830  1.00 14.21 ? 251 LYS A C   1 
ATOM   2633 O  O   . LYS A 1 251 ? -1.426  -3.318  36.304  1.00 16.32 ? 251 LYS A O   1 
ATOM   2634 C  CB  . LYS A 1 251 ? 1.202   -1.987  34.082  1.00 14.71 ? 251 LYS A CB  1 
ATOM   2635 C  CG  . LYS A 1 251 ? 2.411   -2.655  33.426  1.00 19.99 ? 251 LYS A CG  1 
ATOM   2636 C  CD  . LYS A 1 251 ? 3.267   -1.757  32.644  1.00 18.26 ? 251 LYS A CD  1 
ATOM   2637 C  CE  . LYS A 1 251 ? 4.518   -2.443  32.200  1.00 22.75 ? 251 LYS A CE  1 
ATOM   2638 N  NZ  . LYS A 1 251 ? 5.371   -1.532  31.388  1.00 28.32 ? 251 LYS A NZ  1 
ATOM   2639 N  N   . ASN A 1 252 ? -0.626  -1.228  36.064  1.00 13.29 ? 252 ASN A N   1 
ATOM   2640 C  CA  . ASN A 1 252 ? -1.450  -0.737  37.110  1.00 19.22 ? 252 ASN A CA  1 
ATOM   2641 C  C   . ASN A 1 252 ? -2.759  -0.275  36.490  1.00 18.24 ? 252 ASN A C   1 
ATOM   2642 O  O   . ASN A 1 252 ? -2.962  1.031   36.444  1.00 19.04 ? 252 ASN A O   1 
ATOM   2643 C  CB  . ASN A 1 252 ? -0.771  0.442   37.808  1.00 25.92 ? 252 ASN A CB  1 
ATOM   2644 C  CG  . ASN A 1 252 ? -1.552  0.929   39.042  1.00 22.91 ? 252 ASN A CG  1 
ATOM   2645 O  OD1 . ASN A 1 252 ? -2.146  0.135   39.791  1.00 35.48 ? 252 ASN A OD1 1 
ATOM   2646 N  ND2 . ASN A 1 252 ? -1.622  2.262   39.229  1.00 29.13 ? 252 ASN A ND2 1 
ATOM   2647 N  N   . ARG A 1 253 ? -3.546  -1.281  35.890  1.00 13.70 ? 253 ARG A N   1 
ATOM   2648 C  CA  . ARG A 1 253 ? -4.815  -0.957  35.309  1.00 10.74 ? 253 ARG A CA  1 
ATOM   2649 C  C   . ARG A 1 253 ? -5.951  -1.853  35.725  1.00 10.61 ? 253 ARG A C   1 
ATOM   2650 O  O   . ARG A 1 253 ? -5.713  -3.022  36.044  1.00 17.13 ? 253 ARG A O   1 
ATOM   2651 C  CB  . ARG A 1 253 ? -4.745  -0.933  33.801  1.00 10.23 ? 253 ARG A CB  1 
ATOM   2652 C  CG  . ARG A 1 253 ? -3.798  0.202   33.307  1.00 9.99  ? 253 ARG A CG  1 
ATOM   2653 C  CD  . ARG A 1 253 ? -3.727  0.189   31.828  1.00 9.31  ? 253 ARG A CD  1 
ATOM   2654 N  NE  . ARG A 1 253 ? -2.879  -0.965  31.388  1.00 8.37  ? 253 ARG A NE  1 
ATOM   2655 C  CZ  . ARG A 1 253 ? -2.633  -1.220  30.098  1.00 8.03  ? 253 ARG A CZ  1 
ATOM   2656 N  NH1 . ARG A 1 253 ? -3.239  -0.545  29.128  1.00 7.65  ? 253 ARG A NH1 1 
ATOM   2657 N  NH2 . ARG A 1 253 ? -1.800  -2.225  29.764  1.00 7.60  ? 253 ARG A NH2 1 
ATOM   2658 N  N   A GLN A 1 254 ? -7.186  -1.349  35.814  0.50 11.30 ? 254 GLN A N   1 
ATOM   2659 N  N   B GLN A 1 254 ? -7.141  -1.267  35.656  0.50 11.84 ? 254 GLN A N   1 
ATOM   2660 C  CA  A GLN A 1 254 ? -8.353  -2.217  36.048  0.50 12.36 ? 254 GLN A CA  1 
ATOM   2661 C  CA  B GLN A 1 254 ? -8.383  -1.900  35.976  0.50 12.68 ? 254 GLN A CA  1 
ATOM   2662 C  C   A GLN A 1 254 ? -9.269  -2.137  34.845  0.50 10.80 ? 254 GLN A C   1 
ATOM   2663 C  C   B GLN A 1 254 ? -9.115  -2.098  34.655  0.50 10.69 ? 254 GLN A C   1 
ATOM   2664 O  O   A GLN A 1 254 ? -9.615  -1.083  34.294  0.50 10.74 ? 254 GLN A O   1 
ATOM   2665 O  O   B GLN A 1 254 ? -9.172  -1.158  33.838  0.50 13.41 ? 254 GLN A O   1 
ATOM   2666 C  CB  A GLN A 1 254 ? -9.190  -1.876  37.298  0.50 13.62 ? 254 GLN A CB  1 
ATOM   2667 C  CB  B GLN A 1 254 ? -9.237  -0.997  36.894  0.50 11.06 ? 254 GLN A CB  1 
ATOM   2668 C  CG  A GLN A 1 254 ? -9.773  -3.072  38.148  0.50 22.17 ? 254 GLN A CG  1 
ATOM   2669 C  CG  B GLN A 1 254 ? -10.074 -1.816  37.874  0.50 17.88 ? 254 GLN A CG  1 
ATOM   2670 C  CD  A GLN A 1 254 ? -11.328 -3.261  38.206  0.50 34.11 ? 254 GLN A CD  1 
ATOM   2671 C  CD  B GLN A 1 254 ? -9.140  -2.129  39.060  0.50 27.82 ? 254 GLN A CD  1 
ATOM   2672 O  OE1 A GLN A 1 254 ? -11.895 -4.173  37.545  0.50 27.13 ? 254 GLN A OE1 1 
ATOM   2673 O  OE1 B GLN A 1 254 ? -9.547  -2.454  40.174  0.50 35.59 ? 254 GLN A OE1 1 
ATOM   2674 N  NE2 A GLN A 1 254 ? -12.004 -2.484  39.099  0.50 38.45 ? 254 GLN A NE2 1 
ATOM   2675 N  NE2 B GLN A 1 254 ? -7.862  -1.953  38.805  0.50 24.04 ? 254 GLN A NE2 1 
ATOM   2676 N  N   . ILE A 1 255 ? -9.631  -3.310  34.424  1.00 9.67  ? 255 ILE A N   1 
ATOM   2677 C  CA  . ILE A 1 255 ? -10.615 -3.493  33.359  1.00 9.47  ? 255 ILE A CA  1 
ATOM   2678 C  C   . ILE A 1 255 ? -12.026 -3.511  33.971  1.00 9.45  ? 255 ILE A C   1 
ATOM   2679 O  O   . ILE A 1 255 ? -12.205 -4.244  34.975  1.00 11.43 ? 255 ILE A O   1 
ATOM   2680 C  CB  . ILE A 1 255 ? -10.365 -4.735  32.566  1.00 9.66  ? 255 ILE A CB  1 
ATOM   2681 C  CG1 . ILE A 1 255 ? -8.885  -4.750  31.987  1.00 10.42 ? 255 ILE A CG1 1 
ATOM   2682 C  CG2 . ILE A 1 255 ? -11.379 -4.882  31.443  1.00 10.98 ? 255 ILE A CG2 1 
ATOM   2683 C  CD1 . ILE A 1 255 ? -8.522  -6.018  31.243  1.00 11.66 ? 255 ILE A CD1 1 
ATOM   2684 N  N   . LYS A 1 256 ? -12.894 -2.648  33.540  1.00 9.44  ? 256 LYS A N   1 
ATOM   2685 C  CA  . LYS A 1 256 ? -14.244 -2.589  34.074  1.00 9.65  ? 256 LYS A CA  1 
ATOM   2686 C  C   . LYS A 1 256 ? -15.242 -3.194  33.107  1.00 10.01 ? 256 LYS A C   1 
ATOM   2687 O  O   . LYS A 1 256 ? -15.081 -3.037  31.904  1.00 11.97 ? 256 LYS A O   1 
ATOM   2688 C  CB  . LYS A 1 256 ? -14.588 -1.109  34.316  1.00 11.52 ? 256 LYS A CB  1 
ATOM   2689 C  CG  . LYS A 1 256 ? -13.622 -0.541  35.334  1.00 14.69 ? 256 LYS A CG  1 
ATOM   2690 C  CD  . LYS A 1 256 ? -13.881 0.880   35.588  1.00 22.01 ? 256 LYS A CD  1 
ATOM   2691 C  CE  . LYS A 1 256 ? -12.771 1.437   36.485  1.00 29.13 ? 256 LYS A CE  1 
ATOM   2692 N  NZ  . LYS A 1 256 ? -12.891 2.901   36.509  1.00 37.35 ? 256 LYS A NZ  1 
ATOM   2693 N  N   . ALA A 1 257 ? -16.258 -3.855  33.631  1.00 11.03 ? 257 ALA A N   1 
ATOM   2694 C  CA  . ALA A 1 257 ? -17.350 -4.412  32.857  1.00 11.10 ? 257 ALA A CA  1 
ATOM   2695 C  C   . ALA A 1 257 ? -18.567 -3.568  33.003  1.00 9.90  ? 257 ALA A C   1 
ATOM   2696 O  O   . ALA A 1 257 ? -18.944 -3.145  34.094  1.00 12.34 ? 257 ALA A O   1 
ATOM   2697 C  CB  . ALA A 1 257 ? -17.616 -5.854  33.251  1.00 12.63 ? 257 ALA A CB  1 
ATOM   2698 N  N   . SER A 1 258 ? -19.299 -3.398  31.905  1.00 9.91  ? 258 SER A N   1 
ATOM   2699 C  CA  . SER A 1 258 ? -20.568 -2.688  31.901  1.00 10.96 ? 258 SER A CA  1 
ATOM   2700 C  C   . SER A 1 258 ? -21.742 -3.551  32.314  1.00 12.43 ? 258 SER A C   1 
ATOM   2701 O  O   . SER A 1 258 ? -22.835 -3.006  32.392  1.00 16.82 ? 258 SER A O   1 
ATOM   2702 C  CB  . SER A 1 258 ? -20.873 -2.145  30.518  1.00 11.43 ? 258 SER A CB  1 
ATOM   2703 O  OG  . SER A 1 258 ? -21.264 -3.158  29.643  1.00 11.65 ? 258 SER A OG  1 
ATOM   2704 N  N   . PHE A 1 259 ? -21.467 -4.821  32.587  1.00 12.47 ? 259 PHE A N   1 
ATOM   2705 C  CA  . PHE A 1 259 ? -22.556 -5.840  32.674  1.00 15.34 ? 259 PHE A CA  1 
ATOM   2706 C  C   . PHE A 1 259 ? -22.176 -6.746  33.843  1.00 18.93 ? 259 PHE A C   1 
ATOM   2707 O  O   . PHE A 1 259 ? -20.957 -6.978  34.198  1.00 19.17 ? 259 PHE A O   1 
ATOM   2708 C  CB  . PHE A 1 259 ? -22.678 -6.641  31.396  1.00 14.16 ? 259 PHE A CB  1 
ATOM   2709 C  CG  . PHE A 1 259 ? -21.409 -7.325  31.054  1.00 13.47 ? 259 PHE A CG  1 
ATOM   2710 C  CD1 . PHE A 1 259 ? -20.422 -6.661  30.336  1.00 12.48 ? 259 PHE A CD1 1 
ATOM   2711 C  CD2 . PHE A 1 259 ? -21.234 -8.666  31.434  1.00 18.42 ? 259 PHE A CD2 1 
ATOM   2712 C  CE1 . PHE A 1 259 ? -19.200 -7.288  30.047  1.00 15.47 ? 259 PHE A CE1 1 
ATOM   2713 C  CE2 . PHE A 1 259 ? -20.044 -9.302  31.173  1.00 19.75 ? 259 PHE A CE2 1 
ATOM   2714 C  CZ  . PHE A 1 259 ? -19.010 -8.603  30.472  1.00 19.61 ? 259 PHE A CZ  1 
ATOM   2715 N  N   . LYS A 1 260 ? -23.247 -7.280  34.409  1.00 26.41 ? 260 LYS A N   1 
ATOM   2716 C  CA  . LYS A 1 260 ? -23.166 -8.210  35.550  1.00 32.38 ? 260 LYS A CA  1 
ATOM   2717 C  C   . LYS A 1 260 ? -22.885 -9.611  35.063  1.00 43.54 ? 260 LYS A C   1 
ATOM   2718 O  O   . LYS A 1 260 ? -23.452 -10.069 34.060  1.00 48.57 ? 260 LYS A O   1 
ATOM   2719 C  CB  . LYS A 1 260 ? -24.390 -8.183  36.509  1.00 38.78 ? 260 LYS A CB  1 
ATOM   2720 C  CG  . LYS A 1 260 ? -24.400 -7.068  37.519  1.00 40.10 ? 260 LYS A CG  1 
ATOM   2721 C  CD  . LYS A 1 260 ? -25.774 -6.923  38.204  1.00 55.24 ? 260 LYS A CD  1 
ATOM   2722 C  CE  . LYS A 1 260 ? -25.644 -6.647  39.715  1.00 71.03 ? 260 LYS A CE  1 
ATOM   2723 N  NZ  . LYS A 1 260 ? -26.753 -5.812  40.303  1.00 73.25 ? 260 LYS A NZ  1 
ATOM   2724 O  OXT . LYS A 1 260 ? -22.061 -10.296 35.672  1.00 56.90 ? 260 LYS A OXT 1 
HETATM 2725 ZN ZN  . ZN  B 2 .   ? -6.583  -1.941  15.474  1.00 6.23  ? 301 ZN  A ZN  1 
HETATM 2726 S  S   . DMS C 3 .   ? 1.478   -11.719 15.080  1.00 18.25 ? 302 DMS A S   1 
HETATM 2727 O  O   . DMS C 3 .   ? 2.009   -13.069 14.573  1.00 26.14 ? 302 DMS A O   1 
HETATM 2728 C  C1  . DMS C 3 .   ? 1.869   -11.514 16.701  1.00 16.38 ? 302 DMS A C1  1 
HETATM 2729 C  C2  . DMS C 3 .   ? 2.614   -10.533 14.605  1.00 20.77 ? 302 DMS A C2  1 
HETATM 2730 F  F20 A V14 D 4 .   ? -5.773  3.340   15.486  0.50 10.90 ? 303 V14 A F20 1 
HETATM 2731 F  F20 B V14 D 4 .   ? -5.774  3.350   15.483  0.50 9.49  ? 303 V14 A F20 1 
HETATM 2732 C  C5  A V14 D 4 .   ? -5.185  2.458   14.607  0.50 11.98 ? 303 V14 A C5  1 
HETATM 2733 C  C5  B V14 D 4 .   ? -5.168  2.491   14.612  0.50 8.54  ? 303 V14 A C5  1 
HETATM 2734 C  C4  A V14 D 4 .   ? -4.984  1.166   15.079  0.50 10.93 ? 303 V14 A C4  1 
HETATM 2735 C  C4  B V14 D 4 .   ? -4.959  1.195   15.089  0.50 7.61  ? 303 V14 A C4  1 
HETATM 2736 S  S7  A V14 D 4 .   ? -5.640  0.690   16.689  0.50 7.39  ? 303 V14 A S7  1 
HETATM 2737 S  S7  B V14 D 4 .   ? -5.642  0.691   16.689  0.50 7.10  ? 303 V14 A S7  1 
HETATM 2738 O  O9  A V14 D 4 .   ? -7.035  1.106   16.654  0.50 7.89  ? 303 V14 A O9  1 
HETATM 2739 O  O9  B V14 D 4 .   ? -7.033  1.105   16.653  0.50 8.07  ? 303 V14 A O9  1 
HETATM 2740 N  N10 A V14 D 4 .   ? -5.567  -0.859  16.704  0.50 7.59  ? 303 V14 A N10 1 
HETATM 2741 N  N10 B V14 D 4 .   ? -5.567  -0.857  16.704  0.50 7.41  ? 303 V14 A N10 1 
HETATM 2742 O  O8  A V14 D 4 .   ? -4.772  1.266   17.723  0.50 8.59  ? 303 V14 A O8  1 
HETATM 2743 O  O8  B V14 D 4 .   ? -4.778  1.265   17.723  0.50 8.44  ? 303 V14 A O8  1 
HETATM 2744 C  C3  A V14 D 4 .   ? -4.419  0.303   14.152  0.50 10.30 ? 303 V14 A C3  1 
HETATM 2745 C  C3  B V14 D 4 .   ? -4.382  0.316   14.157  0.50 7.93  ? 303 V14 A C3  1 
HETATM 2746 F  F12 A V14 D 4 .   ? -4.122  -0.992  14.490  0.50 11.37 ? 303 V14 A F12 1 
HETATM 2747 F  F12 B V14 D 4 .   ? -4.097  -0.987  14.500  0.50 9.22  ? 303 V14 A F12 1 
HETATM 2748 C  C2  A V14 D 4 .   ? -4.201  0.632   12.861  0.50 10.78 ? 303 V14 A C2  1 
HETATM 2749 C  C2  B V14 D 4 .   ? -4.166  0.636   12.873  0.50 11.39 ? 303 V14 A C2  1 
HETATM 2750 F  F13 A V14 D 4 .   ? -3.748  -0.318  12.026  0.50 11.00 ? 303 V14 A F13 1 
HETATM 2751 F  F13 B V14 D 4 .   ? -3.700  -0.302  12.034  0.50 16.49 ? 303 V14 A F13 1 
HETATM 2752 C  C6  A V14 D 4 .   ? -4.938  2.882   13.298  0.50 11.95 ? 303 V14 A C6  1 
HETATM 2753 C  C6  B V14 D 4 .   ? -4.898  2.905   13.306  0.50 9.70  ? 303 V14 A C6  1 
HETATM 2754 C  C1  A V14 D 4 .   ? -4.441  1.936   12.380  0.50 11.21 ? 303 V14 A C1  1 
HETATM 2755 C  C1  B V14 D 4 .   ? -4.397  1.943   12.409  0.50 13.93 ? 303 V14 A C1  1 
HETATM 2756 S  S11 A V14 D 4 .   ? -4.203  2.175   10.660  0.50 11.06 ? 303 V14 A S11 1 
HETATM 2757 S  S11 B V14 D 4 .   ? -4.065  2.163   10.705  0.50 23.62 ? 303 V14 A S11 1 
HETATM 2758 O  O16 A V14 D 4 .   ? -4.451  3.624   10.375  0.50 14.61 ? 303 V14 A O16 1 
HETATM 2759 O  O16 B V14 D 4 .   ? -4.386  3.608   10.403  0.50 21.73 ? 303 V14 A O16 1 
HETATM 2760 O  O17 A V14 D 4 .   ? -5.146  1.239   9.965   0.50 14.86 ? 303 V14 A O17 1 
HETATM 2761 O  O17 B V14 D 4 .   ? -5.105  1.278   10.009  0.50 22.09 ? 303 V14 A O17 1 
HETATM 2762 C  C15 A V14 D 4 .   ? -2.594  1.793   10.212  0.50 13.16 ? 303 V14 A C15 1 
HETATM 2763 C  C15 B V14 D 4 .   ? -2.430  1.640   10.341  0.50 21.14 ? 303 V14 A C15 1 
HETATM 2764 C  C18 A V14 D 4 .   ? -1.720  2.587   11.145  0.50 13.48 ? 303 V14 A C18 1 
HETATM 2765 C  C18 B V14 D 4 .   ? -1.557  2.406   11.312  0.50 17.95 ? 303 V14 A C18 1 
HETATM 2766 O  O21 A V14 D 4 .   ? -0.423  2.414   10.717  0.50 19.67 ? 303 V14 A O21 1 
HETATM 2767 O  O21 B V14 D 4 .   ? -1.373  3.710   10.847  0.50 19.20 ? 303 V14 A O21 1 
HETATM 2768 N  N19 A V14 D 4 .   ? -5.242  4.200   12.950  0.50 15.71 ? 303 V14 A N19 1 
HETATM 2769 N  N19 B V14 D 4 .   ? -5.189  4.208   12.934  0.50 11.92 ? 303 V14 A N19 1 
HETATM 2770 C  C14 A V14 D 4 .   ? -5.020  5.388   13.752  0.50 14.71 ? 303 V14 A C14 1 
HETATM 2771 C  C14 B V14 D 4 .   ? -5.030  5.423   13.750  0.50 13.98 ? 303 V14 A C14 1 
HETATM 2772 C  C28 A V14 D 4 .   ? -3.651  5.361   14.462  0.50 14.26 ? 303 V14 A C28 1 
HETATM 2773 C  C28 B V14 D 4 .   ? -3.658  5.421   14.466  0.50 14.94 ? 303 V14 A C28 1 
HETATM 2774 C  C27 A V14 D 4 .   ? -2.448  5.692   13.600  0.50 18.12 ? 303 V14 A C27 1 
HETATM 2775 C  C27 B V14 D 4 .   ? -2.456  5.694   13.579  0.50 15.14 ? 303 V14 A C27 1 
HETATM 2776 C  C26 A V14 D 4 .   ? -1.970  7.110   13.853  0.50 22.94 ? 303 V14 A C26 1 
HETATM 2777 C  C26 B V14 D 4 .   ? -1.933  7.088   13.804  0.50 13.74 ? 303 V14 A C26 1 
HETATM 2778 C  C25 A V14 D 4 .   ? -2.772  8.181   13.118  0.50 18.48 ? 303 V14 A C25 1 
HETATM 2779 C  C25 B V14 D 4 .   ? -2.756  8.179   13.126  0.50 16.66 ? 303 V14 A C25 1 
HETATM 2780 C  C24 A V14 D 4 .   ? -3.972  8.601   13.907  0.50 19.33 ? 303 V14 A C24 1 
HETATM 2781 C  C24 B V14 D 4 .   ? -3.951  8.518   13.955  0.50 15.44 ? 303 V14 A C24 1 
HETATM 2782 C  C23 A V14 D 4 .   ? -5.263  7.967   13.405  0.50 15.30 ? 303 V14 A C23 1 
HETATM 2783 C  C23 B V14 D 4 .   ? -5.260  8.015   13.373  0.50 17.16 ? 303 V14 A C23 1 
HETATM 2784 C  C22 A V14 D 4 .   ? -5.251  6.554   12.815  0.50 15.46 ? 303 V14 A C22 1 
HETATM 2785 C  C22 B V14 D 4 .   ? -5.346  6.587   12.838  0.50 18.42 ? 303 V14 A C22 1 
HETATM 2786 N  N1  . BCN E 5 .   ? -20.130 -14.264 23.265  1.00 32.08 ? 304 BCN A N1  1 
HETATM 2787 C  C1  . BCN E 5 .   ? -19.796 -15.658 22.766  1.00 21.70 ? 304 BCN A C1  1 
HETATM 2788 C  C2  . BCN E 5 .   ? -18.719 -16.298 21.871  1.00 32.70 ? 304 BCN A C2  1 
HETATM 2789 O  O21 . BCN E 5 .   ? -17.360 -16.296 22.028  1.00 22.15 ? 304 BCN A O21 1 
HETATM 2790 O  O22 . BCN E 5 .   ? -19.356 -16.836 20.898  1.00 49.05 ? 304 BCN A O22 1 
HETATM 2791 C  C3  . BCN E 5 .   ? -21.575 -13.912 23.212  1.00 22.94 ? 304 BCN A C3  1 
HETATM 2792 C  C4  . BCN E 5 .   ? -22.053 -12.564 23.762  1.00 33.63 ? 304 BCN A C4  1 
HETATM 2793 O  O4  . BCN E 5 .   ? -22.338 -12.441 25.160  1.00 33.26 ? 304 BCN A O4  1 
HETATM 2794 C  C5  . BCN E 5 .   ? -19.619 -13.924 24.616  1.00 28.55 ? 304 BCN A C5  1 
HETATM 2795 C  C6  . BCN E 5 .   ? -19.966 -15.080 25.565  1.00 33.00 ? 304 BCN A C6  1 
HETATM 2796 O  O6  . BCN E 5 .   ? -19.116 -14.971 26.675  1.00 38.50 ? 304 BCN A O6  1 
HETATM 2797 O  O   . HOH F 6 .   ? -16.921 -8.430  20.410  1.00 7.86  ? 401 HOH A O   1 
HETATM 2798 O  O   . HOH F 6 .   ? -4.357  -13.546 18.177  1.00 7.82  ? 402 HOH A O   1 
HETATM 2799 O  O   . HOH F 6 .   ? 3.743   5.016   29.940  1.00 16.67 ? 403 HOH A O   1 
HETATM 2800 O  O   . HOH F 6 .   ? -3.266  -13.230 25.286  1.00 9.93  ? 404 HOH A O   1 
HETATM 2801 O  O   . HOH F 6 .   ? -3.685  -15.885 24.534  1.00 11.99 ? 405 HOH A O   1 
HETATM 2802 O  O   . HOH F 6 .   ? -1.963  -12.320 22.966  1.00 9.01  ? 406 HOH A O   1 
HETATM 2803 O  O   . HOH F 6 .   ? -2.394  -8.702  29.163  1.00 10.31 ? 407 HOH A O   1 
HETATM 2804 O  O   . HOH F 6 .   ? -1.125  -4.096  15.728  1.00 8.82  ? 408 HOH A O   1 
HETATM 2805 O  O   . HOH F 6 .   ? -7.766  -15.635 11.585  1.00 9.29  ? 409 HOH A O   1 
HETATM 2806 O  O   . HOH F 6 .   ? -3.382  -11.175 21.007  1.00 8.87  ? 410 HOH A O   1 
HETATM 2807 O  O   . HOH F 6 .   ? -1.760  -17.393 25.761  1.00 22.85 ? 411 HOH A O   1 
HETATM 2808 O  O   . HOH F 6 .   ? -21.468 -7.081  23.537  1.00 12.17 ? 412 HOH A O   1 
HETATM 2809 O  O   . HOH F 6 .   ? -14.262 -16.653 29.055  1.00 17.14 ? 413 HOH A O   1 
HETATM 2810 O  O   . HOH F 6 .   ? -10.426 8.659   25.442  1.00 9.31  ? 414 HOH A O   1 
HETATM 2811 O  O   . HOH F 6 .   ? 0.654   -1.674  -4.566  1.00 22.87 ? 415 HOH A O   1 
HETATM 2812 O  O   . HOH F 6 .   ? -21.639 5.681   4.740   1.00 20.34 ? 416 HOH A O   1 
HETATM 2813 O  O   . HOH F 6 .   ? -17.538 10.386  11.168  1.00 17.91 ? 417 HOH A O   1 
HETATM 2814 O  O   . HOH F 6 .   ? 5.017   -4.841  21.053  1.00 12.57 ? 418 HOH A O   1 
HETATM 2815 O  O   . HOH F 6 .   ? -0.939  9.168   28.056  1.00 14.42 ? 419 HOH A O   1 
HETATM 2816 O  O   . HOH F 6 .   ? 7.613   6.196   21.782  1.00 16.21 ? 420 HOH A O   1 
HETATM 2817 O  O   . HOH F 6 .   ? 8.700   -3.763  21.089  1.00 13.90 ? 421 HOH A O   1 
HETATM 2818 O  O   . HOH F 6 .   ? 1.342   -1.587  29.441  1.00 12.48 ? 422 HOH A O   1 
HETATM 2819 O  O   . HOH F 6 .   ? -23.593 -0.843  3.894   1.00 23.40 ? 423 HOH A O   1 
HETATM 2820 O  O   . HOH F 6 .   ? -12.927 -16.880 26.714  1.00 12.91 ? 424 HOH A O   1 
HETATM 2821 O  O   . HOH F 6 .   ? -19.049 9.976   8.838   1.00 17.01 ? 425 HOH A O   1 
HETATM 2822 O  O   . HOH F 6 .   ? 13.460  0.399   24.471  1.00 19.00 ? 426 HOH A O   1 
HETATM 2823 O  O   . HOH F 6 .   ? -25.897 2.754   20.808  1.00 23.41 ? 427 HOH A O   1 
HETATM 2824 O  O   . HOH F 6 .   ? -10.274 -18.336 17.405  1.00 11.96 ? 428 HOH A O   1 
HETATM 2825 O  O   . HOH F 6 .   ? -13.601 10.375  27.775  1.00 14.80 ? 429 HOH A O   1 
HETATM 2826 O  O   . HOH F 6 .   ? -20.845 7.681   1.806   1.00 21.63 ? 430 HOH A O   1 
HETATM 2827 O  O   . HOH F 6 .   ? -8.054  -19.392 21.813  1.00 13.45 ? 431 HOH A O   1 
HETATM 2828 O  O   . HOH F 6 .   ? -4.937  15.800  12.390  1.00 26.09 ? 432 HOH A O   1 
HETATM 2829 O  O   . HOH F 6 .   ? -15.960 -12.303 24.486  1.00 13.07 ? 433 HOH A O   1 
HETATM 2830 O  O   . HOH F 6 .   ? 4.369   -3.368  26.532  1.00 17.13 ? 434 HOH A O   1 
HETATM 2831 O  O   . HOH F 6 .   ? -4.681  -11.954 32.210  1.00 18.37 ? 435 HOH A O   1 
HETATM 2832 O  O   . HOH F 6 .   ? 2.022   -15.830 9.399   1.00 18.70 ? 436 HOH A O   1 
HETATM 2833 O  O   . HOH F 6 .   ? -9.033  5.867   28.971  1.00 14.53 ? 437 HOH A O   1 
HETATM 2834 O  O   . HOH F 6 .   ? -11.910 2.688   30.987  1.00 14.23 ? 438 HOH A O   1 
HETATM 2835 O  O   . HOH F 6 .   ? -17.682 -20.643 8.111   1.00 14.68 ? 439 HOH A O   1 
HETATM 2836 O  O   . HOH F 6 .   ? -9.533  -7.961  34.130  1.00 19.29 ? 440 HOH A O   1 
HETATM 2837 O  O   . HOH F 6 .   ? 1.559   8.705   24.086  1.00 12.17 ? 441 HOH A O   1 
HETATM 2838 O  O   . HOH F 6 .   ? -0.155  -14.339 22.330  1.00 17.17 ? 442 HOH A O   1 
HETATM 2839 O  O   . HOH F 6 .   ? -6.470  20.980  19.773  1.00 11.05 ? 443 HOH A O   1 
HETATM 2840 O  O   . HOH F 6 .   ? -22.778 -11.660 14.041  1.00 19.17 ? 444 HOH A O   1 
HETATM 2841 O  O   . HOH F 6 .   ? 2.067   -14.081 20.814  1.00 25.96 ? 445 HOH A O   1 
HETATM 2842 O  O   . HOH F 6 .   ? -12.769 -17.272 16.996  1.00 12.03 ? 446 HOH A O   1 
HETATM 2843 O  O   . HOH F 6 .   ? -13.139 19.931  15.053  1.00 19.09 ? 447 HOH A O   1 
HETATM 2844 O  O   . HOH F 6 .   ? -22.988 -3.074  6.823   1.00 22.27 ? 448 HOH A O   1 
HETATM 2845 O  O   . HOH F 6 .   ? -6.939  -14.838 31.673  1.00 17.64 ? 449 HOH A O   1 
HETATM 2846 O  O   . HOH F 6 .   ? -8.880  15.167  12.242  1.00 19.83 ? 450 HOH A O   1 
HETATM 2847 O  O   . HOH F 6 .   ? -0.388  10.647  23.828  1.00 16.48 ? 451 HOH A O   1 
HETATM 2848 O  O   . HOH F 6 .   ? -8.985  -5.721  35.990  1.00 18.02 ? 452 HOH A O   1 
HETATM 2849 O  O   . HOH F 6 .   ? -2.051  -11.751 31.707  1.00 28.72 ? 453 HOH A O   1 
HETATM 2850 O  O   . HOH F 6 .   ? -1.127  -11.080 29.122  1.00 15.28 ? 454 HOH A O   1 
HETATM 2851 O  O   . HOH F 6 .   ? -8.150  -22.219 10.657  1.00 18.19 ? 455 HOH A O   1 
HETATM 2852 O  O   . HOH F 6 .   ? 5.219   7.162   20.496  1.00 16.82 ? 456 HOH A O   1 
HETATM 2853 O  O   . HOH F 6 .   ? -7.314  -8.667  32.656  1.00 15.03 ? 457 HOH A O   1 
HETATM 2854 O  O   . HOH F 6 .   ? 1.065   11.254  20.446  1.00 24.87 ? 458 HOH A O   1 
HETATM 2855 O  O   . HOH F 6 .   ? -14.512 20.160  17.584  1.00 17.26 ? 459 HOH A O   1 
HETATM 2856 O  O   . HOH F 6 .   ? -1.293  -13.009 27.138  1.00 21.62 ? 460 HOH A O   1 
HETATM 2857 O  O   . HOH F 6 .   ? -25.419 9.665   13.268  1.00 33.76 ? 461 HOH A O   1 
HETATM 2858 O  O   . HOH F 6 .   ? 11.312  1.425   25.948  1.00 24.02 ? 462 HOH A O   1 
HETATM 2859 O  O   . HOH F 6 .   ? -5.887  -4.909  -6.365  1.00 24.15 ? 463 HOH A O   1 
HETATM 2860 O  O   . HOH F 6 .   ? 1.264   -11.795 25.192  1.00 19.15 ? 464 HOH A O   1 
HETATM 2861 O  O   . HOH F 6 .   ? -1.512  -5.230  -6.964  1.00 29.45 ? 465 HOH A O   1 
HETATM 2862 O  O   . HOH F 6 .   ? -17.432 19.913  17.505  1.00 24.14 ? 466 HOH A O   1 
HETATM 2863 O  O   . HOH F 6 .   ? -31.480 -10.807 16.273  1.00 19.82 ? 467 HOH A O   1 
HETATM 2864 O  O   . HOH F 6 .   ? -13.760 -8.971  -5.181  1.00 26.14 ? 468 HOH A O   1 
HETATM 2865 O  O   . HOH F 6 .   ? -5.179  2.214   37.493  1.00 19.38 ? 469 HOH A O   1 
HETATM 2866 O  O   . HOH F 6 .   ? 4.477   -2.508  28.995  1.00 22.77 ? 470 HOH A O   1 
HETATM 2867 O  O   . HOH F 6 .   ? 5.167   -7.355  22.350  1.00 24.29 ? 471 HOH A O   1 
HETATM 2868 O  O   . HOH F 6 .   ? -23.241 -11.131 17.232  1.00 20.94 ? 472 HOH A O   1 
HETATM 2869 O  O   . HOH F 6 .   ? -8.733  -15.407 36.832  1.00 16.84 ? 473 HOH A O   1 
HETATM 2870 O  O   . HOH F 6 .   ? -1.205  11.443  26.309  1.00 19.25 ? 474 HOH A O   1 
HETATM 2871 O  O   . HOH F 6 .   ? -11.089 11.829  7.184   1.00 24.43 ? 475 HOH A O   1 
HETATM 2872 O  O   . HOH F 6 .   ? -3.706  -13.127 -2.823  1.00 24.96 ? 476 HOH A O   1 
HETATM 2873 O  O   . HOH F 6 .   ? -11.072 -19.702 7.777   1.00 31.53 ? 477 HOH A O   1 
HETATM 2874 O  O   . HOH F 6 .   ? -12.714 13.134  31.944  1.00 23.37 ? 478 HOH A O   1 
HETATM 2875 O  O   . HOH F 6 .   ? -8.959  -10.255 -1.142  1.00 22.37 ? 479 HOH A O   1 
HETATM 2876 O  O   . HOH F 6 .   ? -4.132  -8.455  31.205  1.00 16.30 ? 480 HOH A O   1 
HETATM 2877 O  O   . HOH F 6 .   ? -12.803 -19.566 26.236  1.00 20.43 ? 481 HOH A O   1 
HETATM 2878 O  O   . HOH F 6 .   ? -15.842 15.944  23.493  1.00 18.16 ? 482 HOH A O   1 
HETATM 2879 O  O   . HOH F 6 .   ? -10.525 4.968   30.960  1.00 16.12 ? 483 HOH A O   1 
HETATM 2880 O  O   . HOH F 6 .   ? -20.002 10.859  26.480  1.00 18.08 ? 484 HOH A O   1 
HETATM 2881 O  O   . HOH F 6 .   ? -14.466 -18.610 18.805  1.00 14.54 ? 485 HOH A O   1 
HETATM 2882 O  O   . HOH F 6 .   ? -9.863  15.649  29.790  1.00 30.83 ? 486 HOH A O   1 
HETATM 2883 O  O   . HOH F 6 .   ? 2.587   -13.488 5.215   1.00 18.75 ? 487 HOH A O   1 
HETATM 2884 O  O   . HOH F 6 .   ? -23.786 8.701   20.063  1.00 22.56 ? 488 HOH A O   1 
HETATM 2885 O  O   . HOH F 6 .   ? 4.367   -6.855  7.944   1.00 24.63 ? 489 HOH A O   1 
HETATM 2886 O  O   . HOH F 6 .   ? -21.927 -18.471 13.613  1.00 22.34 ? 490 HOH A O   1 
HETATM 2887 O  O   . HOH F 6 .   ? 0.035   13.993  16.643  1.00 26.00 ? 491 HOH A O   1 
HETATM 2888 O  O   . HOH F 6 .   ? -11.039 1.226   33.447  1.00 15.72 ? 492 HOH A O   1 
HETATM 2889 O  O   . HOH F 6 .   ? -19.962 -16.712 3.158   1.00 20.48 ? 493 HOH A O   1 
HETATM 2890 O  O   . HOH F 6 .   ? -0.593  -8.556  32.613  1.00 21.28 ? 494 HOH A O   1 
HETATM 2891 O  O   . HOH F 6 .   ? -12.673 7.896   28.607  1.00 22.17 ? 495 HOH A O   1 
HETATM 2892 O  O   . HOH F 6 .   ? -16.785 -14.038 26.373  1.00 19.83 ? 496 HOH A O   1 
HETATM 2893 O  O   . HOH F 6 .   ? -6.920  1.576   35.289  1.00 16.55 ? 497 HOH A O   1 
HETATM 2894 O  O   . HOH F 6 .   ? -16.262 -9.934  32.927  1.00 17.42 ? 498 HOH A O   1 
HETATM 2895 O  O   . HOH F 6 .   ? -19.807 -4.168  41.229  1.00 32.22 ? 499 HOH A O   1 
HETATM 2896 O  O   . HOH F 6 .   ? 0.075   1.117   34.575  1.00 22.74 ? 500 HOH A O   1 
HETATM 2897 O  O   . HOH F 6 .   ? -8.121  -19.120 30.739  1.00 25.48 ? 501 HOH A O   1 
HETATM 2898 O  O   . HOH F 6 .   ? -22.721 -6.059  2.806   1.00 23.23 ? 502 HOH A O   1 
HETATM 2899 O  O   . HOH F 6 .   ? 2.853   -4.583  7.816   1.00 21.05 ? 503 HOH A O   1 
HETATM 2900 O  O   . HOH F 6 .   ? -2.631  -17.979 31.322  1.00 21.85 ? 504 HOH A O   1 
HETATM 2901 O  O   . HOH F 6 .   ? 1.615   -6.269  34.486  1.00 19.74 ? 505 HOH A O   1 
HETATM 2902 O  O   . HOH F 6 .   ? -26.530 -3.750  25.211  1.00 20.23 ? 506 HOH A O   1 
HETATM 2903 O  O   . HOH F 6 .   ? 2.642   0.895   -2.198  1.00 30.60 ? 507 HOH A O   1 
HETATM 2904 O  O   . HOH F 6 .   ? -23.220 -13.327 11.368  1.00 18.06 ? 508 HOH A O   1 
HETATM 2905 O  O   . HOH F 6 .   ? -18.003 -20.874 -1.256  1.00 34.08 ? 509 HOH A O   1 
HETATM 2906 O  O   . HOH F 6 .   ? -16.386 -15.370 33.018  1.00 30.94 ? 510 HOH A O   1 
HETATM 2907 O  O   . HOH F 6 .   ? -17.600 19.018  6.076   1.00 14.78 ? 511 HOH A O   1 
HETATM 2908 O  O   . HOH F 6 .   ? 13.189  -5.750  24.592  1.00 26.07 ? 512 HOH A O   1 
HETATM 2909 O  O   . HOH F 6 .   ? -15.412 8.844   -2.078  1.00 27.18 ? 513 HOH A O   1 
HETATM 2910 O  O   . HOH F 6 .   ? -11.112 -11.532 -2.822  1.00 29.19 ? 514 HOH A O   1 
HETATM 2911 O  O   . HOH F 6 .   ? 3.616   8.777   22.112  1.00 22.02 ? 515 HOH A O   1 
HETATM 2912 O  O   . HOH F 6 .   ? -21.092 -19.694 6.679   1.00 24.12 ? 516 HOH A O   1 
HETATM 2913 O  O   . HOH F 6 .   ? -10.403 17.458  12.211  1.00 19.94 ? 517 HOH A O   1 
HETATM 2914 O  O   . HOH F 6 .   ? -3.835  -15.752 -2.153  1.00 29.64 ? 518 HOH A O   1 
HETATM 2915 O  O   . HOH F 6 .   ? -20.077 13.944  28.521  1.00 34.54 ? 519 HOH A O   1 
HETATM 2916 O  O   . HOH F 6 .   ? -8.767  -21.620 8.371   1.00 24.66 ? 520 HOH A O   1 
HETATM 2917 O  O   . HOH F 6 .   ? -17.462 4.747   -3.879  1.00 33.03 ? 521 HOH A O   1 
HETATM 2918 O  O   . HOH F 6 .   ? -4.727  20.481  21.855  1.00 17.29 ? 522 HOH A O   1 
HETATM 2919 O  O   . HOH F 6 .   ? -10.360 21.727  19.935  1.00 18.52 ? 523 HOH A O   1 
HETATM 2920 O  O   . HOH F 6 .   ? -15.732 -12.218 39.101  1.00 20.92 ? 524 HOH A O   1 
HETATM 2921 O  O   . HOH F 6 .   ? 1.798   -17.684 14.070  1.00 32.79 ? 525 HOH A O   1 
HETATM 2922 O  O   . HOH F 6 .   ? -4.976  3.158   -5.730  1.00 26.08 ? 526 HOH A O   1 
HETATM 2923 O  O   . HOH F 6 .   ? -25.794 -6.279  33.489  1.00 35.18 ? 527 HOH A O   1 
HETATM 2924 O  O   . HOH F 6 .   ? 5.183   -10.842 18.858  1.00 39.27 ? 528 HOH A O   1 
HETATM 2925 O  O   . HOH F 6 .   ? 1.630   8.098   28.417  1.00 19.03 ? 529 HOH A O   1 
HETATM 2926 O  O   . HOH F 6 .   ? 4.875   -3.722  3.004   1.00 27.80 ? 530 HOH A O   1 
HETATM 2927 O  O   . HOH F 6 .   ? -13.291 -18.586 14.788  1.00 17.25 ? 531 HOH A O   1 
HETATM 2928 O  O   . HOH F 6 .   ? 8.591   -4.581  23.696  1.00 22.66 ? 532 HOH A O   1 
HETATM 2929 O  O   . HOH F 6 .   ? 8.144   -9.332  16.628  1.00 20.14 ? 533 HOH A O   1 
HETATM 2930 O  O   . HOH F 6 .   ? -10.948 -15.097 34.182  1.00 19.65 ? 534 HOH A O   1 
HETATM 2931 O  O   . HOH F 6 .   ? 2.646   -11.474 9.600   1.00 21.15 ? 535 HOH A O   1 
HETATM 2932 O  O   . HOH F 6 .   ? -20.836 -7.176  -1.866  1.00 30.18 ? 536 HOH A O   1 
HETATM 2933 O  O   . HOH F 6 .   ? -12.639 -9.121  -3.138  1.00 23.68 ? 537 HOH A O   1 
HETATM 2934 O  O   . HOH F 6 .   ? -21.791 -14.144 18.866  1.00 27.17 ? 538 HOH A O   1 
HETATM 2935 O  O   A HOH F 6 .   ? 10.300  -9.105  8.314   0.50 20.87 ? 539 HOH A O   1 
HETATM 2936 O  O   B HOH F 6 .   ? 10.811  -9.252  9.415   0.50 19.89 ? 539 HOH A O   1 
HETATM 2937 O  O   . HOH F 6 .   ? -7.142  -16.893 1.430   1.00 19.78 ? 540 HOH A O   1 
HETATM 2938 O  O   . HOH F 6 .   ? -6.731  -8.868  -6.939  1.00 27.73 ? 541 HOH A O   1 
HETATM 2939 O  O   . HOH F 6 .   ? 11.730  -7.156  22.422  1.00 28.35 ? 542 HOH A O   1 
HETATM 2940 O  O   . HOH F 6 .   ? -18.693 2.196   40.696  1.00 37.34 ? 543 HOH A O   1 
HETATM 2941 O  O   . HOH F 6 .   ? 2.630   9.619   26.386  1.00 24.90 ? 544 HOH A O   1 
HETATM 2942 O  O   . HOH F 6 .   ? -3.053  4.538   7.648   1.00 25.12 ? 545 HOH A O   1 
HETATM 2943 O  O   . HOH F 6 .   ? -25.964 3.104   15.582  1.00 35.67 ? 546 HOH A O   1 
HETATM 2944 O  O   . HOH F 6 .   ? -4.444  -8.363  -8.395  1.00 35.15 ? 547 HOH A O   1 
HETATM 2945 O  O   . HOH F 6 .   ? -4.878  -9.640  33.567  1.00 24.33 ? 548 HOH A O   1 
HETATM 2946 O  O   . HOH F 6 .   ? -6.144  -2.579  -8.194  1.00 30.93 ? 549 HOH A O   1 
HETATM 2947 O  O   . HOH F 6 .   ? 9.323   7.622   18.721  1.00 35.29 ? 550 HOH A O   1 
HETATM 2948 O  O   . HOH F 6 .   ? -17.809 -12.026 31.548  1.00 28.19 ? 551 HOH A O   1 
HETATM 2949 O  O   . HOH F 6 .   ? -3.115  -18.023 0.137   1.00 25.08 ? 552 HOH A O   1 
HETATM 2950 O  O   . HOH F 6 .   ? -25.305 -8.783  11.274  1.00 25.70 ? 553 HOH A O   1 
HETATM 2951 O  O   . HOH F 6 .   ? -24.444 -20.685 8.765   1.00 40.33 ? 554 HOH A O   1 
HETATM 2952 O  O   . HOH F 6 .   ? -3.129  -19.813 6.338   1.00 23.67 ? 555 HOH A O   1 
HETATM 2953 O  O   . HOH F 6 .   ? -25.717 6.401   26.907  1.00 21.60 ? 556 HOH A O   1 
HETATM 2954 O  O   . HOH F 6 .   ? -19.189 -20.930 5.219   1.00 21.33 ? 557 HOH A O   1 
HETATM 2955 O  O   . HOH F 6 .   ? -23.065 -0.262  34.391  1.00 29.28 ? 558 HOH A O   1 
HETATM 2956 O  O   . HOH F 6 .   ? -7.306  -17.334 32.361  1.00 25.03 ? 559 HOH A O   1 
HETATM 2957 O  O   . HOH F 6 .   ? -23.784 -0.546  26.454  1.00 18.40 ? 560 HOH A O   1 
HETATM 2958 O  O   . HOH F 6 .   ? -8.092  0.373   -6.471  1.00 27.46 ? 561 HOH A O   1 
HETATM 2959 O  O   . HOH F 6 .   ? -13.706 3.725   33.145  1.00 21.26 ? 562 HOH A O   1 
HETATM 2960 O  O   . HOH F 6 .   ? -0.279  12.075  13.824  1.00 38.02 ? 563 HOH A O   1 
HETATM 2961 O  O   . HOH F 6 .   ? 3.515   -14.051 -5.929  1.00 29.38 ? 564 HOH A O   1 
HETATM 2962 O  O   . HOH F 6 .   ? 11.909  0.622   28.619  1.00 34.71 ? 565 HOH A O   1 
HETATM 2963 O  O   . HOH F 6 .   ? 15.347  -2.415  14.508  1.00 19.29 ? 566 HOH A O   1 
HETATM 2964 O  O   . HOH F 6 .   ? -18.382 -4.004  -2.563  1.00 24.57 ? 567 HOH A O   1 
HETATM 2965 O  O   . HOH F 6 .   ? -2.512  17.691  14.366  1.00 21.37 ? 568 HOH A O   1 
HETATM 2966 O  O   . HOH F 6 .   ? -0.851  18.668  23.196  1.00 36.29 ? 569 HOH A O   1 
HETATM 2967 O  O   . HOH F 6 .   ? -7.173  -9.060  -2.324  1.00 27.38 ? 570 HOH A O   1 
HETATM 2968 O  O   . HOH F 6 .   ? -23.576 -7.637  0.036   1.00 33.29 ? 571 HOH A O   1 
HETATM 2969 O  O   . HOH F 6 .   ? 2.989   -13.663 8.152   1.00 23.17 ? 572 HOH A O   1 
HETATM 2970 O  O   . HOH F 6 .   ? -4.677  -16.094 0.751   1.00 27.75 ? 573 HOH A O   1 
HETATM 2971 O  O   . HOH F 6 .   ? 1.500   -16.164 -4.742  1.00 38.44 ? 574 HOH A O   1 
HETATM 2972 O  O   . HOH F 6 .   ? -25.889 -6.435  13.078  1.00 20.81 ? 575 HOH A O   1 
HETATM 2973 O  O   . HOH F 6 .   ? -3.279  18.071  21.941  1.00 16.72 ? 576 HOH A O   1 
HETATM 2974 O  O   . HOH F 6 .   ? -6.716  -5.311  37.454  1.00 18.29 ? 577 HOH A O   1 
HETATM 2975 O  O   . HOH F 6 .   ? 6.985   -3.572  30.167  1.00 27.38 ? 578 HOH A O   1 
HETATM 2976 O  O   . HOH F 6 .   ? -23.451 -18.117 6.369   1.00 27.21 ? 579 HOH A O   1 
HETATM 2977 O  O   . HOH F 6 .   ? -15.006 -16.042 25.281  1.00 32.51 ? 580 HOH A O   1 
HETATM 2978 O  O   . HOH F 6 .   ? -9.075  13.262  10.229  1.00 26.11 ? 581 HOH A O   1 
HETATM 2979 O  O   . HOH F 6 .   ? -26.510 -1.051  25.984  1.00 22.38 ? 582 HOH A O   1 
HETATM 2980 O  O   . HOH F 6 .   ? -11.983 9.264   3.176   1.00 21.16 ? 583 HOH A O   1 
HETATM 2981 O  O   . HOH F 6 .   ? -19.298 17.223  5.990   1.00 24.37 ? 584 HOH A O   1 
HETATM 2982 O  O   . HOH F 6 .   ? 8.697   -10.410 -6.868  1.00 36.25 ? 585 HOH A O   1 
HETATM 2983 O  O   . HOH F 6 .   ? 3.453   4.191   10.640  1.00 28.63 ? 586 HOH A O   1 
HETATM 2984 O  O   . HOH F 6 .   ? -6.062  -19.855 24.158  1.00 21.26 ? 587 HOH A O   1 
HETATM 2985 O  O   . HOH F 6 .   ? -14.014 -21.058 3.174   1.00 29.28 ? 588 HOH A O   1 
HETATM 2986 O  O   . HOH F 6 .   ? -12.317 12.490  29.102  1.00 27.56 ? 589 HOH A O   1 
HETATM 2987 O  O   . HOH F 6 .   ? -16.588 -18.249 20.386  1.00 25.35 ? 590 HOH A O   1 
HETATM 2988 O  O   . HOH F 6 .   ? -2.786  6.183   9.775   1.00 26.67 ? 591 HOH A O   1 
HETATM 2989 O  O   . HOH F 6 .   ? 4.715   -1.124  -5.260  1.00 22.41 ? 592 HOH A O   1 
HETATM 2990 O  O   . HOH F 6 .   ? 10.315  -2.550  13.664  1.00 29.25 ? 593 HOH A O   1 
HETATM 2991 O  O   . HOH F 6 .   ? 8.197   -8.751  0.022   1.00 25.28 ? 594 HOH A O   1 
HETATM 2992 O  O   . HOH F 6 .   ? -7.446  8.037   29.709  1.00 23.65 ? 595 HOH A O   1 
HETATM 2993 O  O   . HOH F 6 .   ? -12.863 3.520   -6.835  1.00 29.40 ? 596 HOH A O   1 
HETATM 2994 O  O   . HOH F 6 .   ? -2.360  22.014  21.773  1.00 20.73 ? 597 HOH A O   1 
HETATM 2995 O  O   . HOH F 6 .   ? -22.751 -14.867 16.181  1.00 27.95 ? 598 HOH A O   1 
HETATM 2996 O  O   . HOH F 6 .   ? 13.044  -3.704  13.480  1.00 26.14 ? 599 HOH A O   1 
HETATM 2997 O  O   . HOH F 6 .   ? -25.118 11.172  19.622  1.00 30.57 ? 600 HOH A O   1 
HETATM 2998 O  O   . HOH F 6 .   ? 1.078   4.526   12.090  1.00 21.77 ? 601 HOH A O   1 
HETATM 2999 O  O   . HOH F 6 .   ? 14.193  2.448   23.163  1.00 32.87 ? 602 HOH A O   1 
HETATM 3000 O  O   . HOH F 6 .   ? 7.971   -12.552 -6.929  1.00 28.43 ? 603 HOH A O   1 
HETATM 3001 O  O   . HOH F 6 .   ? -16.523 -14.992 28.779  1.00 26.50 ? 604 HOH A O   1 
HETATM 3002 O  O   . HOH F 6 .   ? -25.474 -15.203 7.873   1.00 32.54 ? 605 HOH A O   1 
HETATM 3003 O  O   . HOH F 6 .   ? -26.968 -10.387 14.696  1.00 28.57 ? 606 HOH A O   1 
HETATM 3004 O  O   . HOH F 6 .   ? -24.556 -9.737  1.967   1.00 25.09 ? 607 HOH A O   1 
HETATM 3005 O  O   . HOH F 6 .   ? -0.797  -17.403 18.442  1.00 26.75 ? 608 HOH A O   1 
HETATM 3006 O  O   . HOH F 6 .   ? -18.355 -20.041 19.845  1.00 44.53 ? 609 HOH A O   1 
HETATM 3007 O  O   . HOH F 6 .   ? -18.876 -12.430 -3.417  1.00 27.87 ? 610 HOH A O   1 
HETATM 3008 O  O   . HOH F 6 .   ? -9.230  3.046   34.796  1.00 16.00 ? 611 HOH A O   1 
HETATM 3009 O  O   . HOH F 6 .   ? -15.163 20.890  22.817  1.00 28.36 ? 612 HOH A O   1 
HETATM 3010 O  O   . HOH F 6 .   ? -13.691 14.331  27.151  1.00 26.74 ? 613 HOH A O   1 
HETATM 3011 O  O   . HOH F 6 .   ? -16.162 -12.658 -6.316  1.00 32.68 ? 614 HOH A O   1 
HETATM 3012 O  O   . HOH F 6 .   ? 12.221  4.366   27.529  1.00 31.77 ? 615 HOH A O   1 
HETATM 3013 O  O   . HOH F 6 .   ? 6.909   -4.120  -10.720 1.00 20.08 ? 616 HOH A O   1 
HETATM 3014 O  O   . HOH F 6 .   ? -24.751 -7.793  9.139   1.00 16.67 ? 617 HOH A O   1 
HETATM 3015 O  O   . HOH F 6 .   ? -12.444 6.944   31.119  1.00 22.82 ? 618 HOH A O   1 
HETATM 3016 O  O   . HOH F 6 .   ? -18.441 12.137  12.932  1.00 20.56 ? 619 HOH A O   1 
HETATM 3017 O  O   . HOH F 6 .   ? 0.019   -14.296 31.367  1.00 31.12 ? 620 HOH A O   1 
HETATM 3018 O  O   . HOH F 6 .   ? -18.555 17.660  18.864  1.00 23.06 ? 621 HOH A O   1 
HETATM 3019 O  O   . HOH F 6 .   ? -26.349 -6.451  5.137   1.00 27.65 ? 622 HOH A O   1 
HETATM 3020 O  O   . HOH F 6 .   ? -12.653 -22.276 8.896   1.00 29.94 ? 623 HOH A O   1 
HETATM 3021 O  O   . HOH F 6 .   ? -31.507 5.385   12.927  1.00 34.50 ? 624 HOH A O   1 
HETATM 3022 O  O   . HOH F 6 .   ? 14.711  -7.013  7.942   1.00 28.28 ? 625 HOH A O   1 
HETATM 3023 O  O   . HOH F 6 .   ? -5.171  -17.156 -3.920  1.00 37.27 ? 626 HOH A O   1 
HETATM 3024 O  O   . HOH F 6 .   ? -13.694 -16.237 -0.302  1.00 33.06 ? 627 HOH A O   1 
HETATM 3025 O  O   . HOH F 6 .   ? -27.799 -1.321  28.481  1.00 32.23 ? 628 HOH A O   1 
HETATM 3026 O  O   . HOH F 6 .   ? 6.256   -10.981 15.582  1.00 30.94 ? 629 HOH A O   1 
HETATM 3027 O  O   . HOH F 6 .   ? -20.287 8.477   29.877  1.00 25.16 ? 630 HOH A O   1 
HETATM 3028 O  O   . HOH F 6 .   ? -14.866 6.234   32.595  1.00 27.67 ? 631 HOH A O   1 
HETATM 3029 O  O   . HOH F 6 .   ? -20.519 18.892  13.655  1.00 26.16 ? 632 HOH A O   1 
HETATM 3030 O  O   . HOH F 6 .   ? 6.519   5.246   29.275  1.00 39.15 ? 633 HOH A O   1 
HETATM 3031 O  O   . HOH F 6 .   ? -24.600 4.634   8.447   1.00 36.43 ? 634 HOH A O   1 
HETATM 3032 O  O   . HOH F 6 .   ? -26.134 -7.561  30.300  1.00 31.50 ? 635 HOH A O   1 
HETATM 3033 O  O   . HOH F 6 .   ? -0.505  6.704   32.176  1.00 23.80 ? 636 HOH A O   1 
HETATM 3034 O  O   . HOH F 6 .   ? -13.179 -1.024  -5.817  1.00 30.54 ? 637 HOH A O   1 
HETATM 3035 O  O   . HOH F 6 .   ? -0.242  3.244   8.039   1.00 34.20 ? 638 HOH A O   1 
HETATM 3036 O  O   . HOH F 6 .   ? -24.846 8.954   25.902  1.00 32.77 ? 639 HOH A O   1 
HETATM 3037 O  O   . HOH F 6 .   ? -5.916  -11.591 36.612  1.00 34.41 ? 640 HOH A O   1 
HETATM 3038 O  O   . HOH F 6 .   ? -7.268  -10.305 -4.309  1.00 31.10 ? 641 HOH A O   1 
HETATM 3039 O  O   . HOH F 6 .   ? -16.653 14.412  33.377  1.00 30.56 ? 642 HOH A O   1 
HETATM 3040 O  O   . HOH F 6 .   ? 8.337   3.138   27.670  1.00 31.24 ? 643 HOH A O   1 
HETATM 3041 O  O   . HOH F 6 .   ? 6.769   -8.864  -9.629  1.00 31.93 ? 644 HOH A O   1 
HETATM 3042 O  O   . HOH F 6 .   ? 1.614   12.358  18.003  1.00 35.52 ? 645 HOH A O   1 
HETATM 3043 O  O   . HOH F 6 .   ? 9.546   1.973   12.311  1.00 33.89 ? 646 HOH A O   1 
HETATM 3044 O  O   . HOH F 6 .   ? -8.511  -19.918 26.909  1.00 23.87 ? 647 HOH A O   1 
HETATM 3045 O  O   . HOH F 6 .   ? -1.798  4.379   -4.984  1.00 29.81 ? 648 HOH A O   1 
HETATM 3046 O  O   . HOH F 6 .   ? -27.159 -7.494  26.138  1.00 30.14 ? 649 HOH A O   1 
HETATM 3047 O  O   . HOH F 6 .   ? -15.910 17.299  25.979  1.00 33.03 ? 650 HOH A O   1 
HETATM 3048 O  O   . HOH F 6 .   ? -24.705 -9.978  15.067  1.00 34.45 ? 651 HOH A O   1 
HETATM 3049 O  O   . HOH F 6 .   ? -2.863  -14.835 33.060  1.00 29.34 ? 652 HOH A O   1 
HETATM 3050 O  O   . HOH F 6 .   ? 0.983   -9.868  -5.366  1.00 33.67 ? 653 HOH A O   1 
HETATM 3051 O  O   . HOH F 6 .   ? -25.203 4.072   4.035   1.00 35.38 ? 654 HOH A O   1 
HETATM 3052 O  O   . HOH F 6 .   ? 2.736   6.462   32.189  1.00 32.10 ? 655 HOH A O   1 
HETATM 3053 O  O   . HOH F 6 .   ? -27.088 -10.654 22.634  1.00 30.19 ? 656 HOH A O   1 
HETATM 3054 O  O   . HOH F 6 .   ? -12.664 10.487  -5.347  1.00 37.10 ? 657 HOH A O   1 
HETATM 3055 O  O   . HOH F 6 .   ? 6.647   8.596   18.483  1.00 33.15 ? 658 HOH A O   1 
HETATM 3056 O  O   . HOH F 6 .   ? -2.465  -3.705  11.416  1.00 27.69 ? 659 HOH A O   1 
HETATM 3057 O  O   . HOH F 6 .   ? 9.501   -7.124  23.706  1.00 31.16 ? 660 HOH A O   1 
HETATM 3058 O  O   . HOH F 6 .   ? 14.539  0.117   15.135  1.00 27.18 ? 661 HOH A O   1 
HETATM 3059 O  O   . HOH F 6 .   ? -14.961 -10.307 37.497  1.00 26.94 ? 662 HOH A O   1 
HETATM 3060 O  O   . HOH F 6 .   ? -15.672 3.750   35.290  1.00 29.75 ? 663 HOH A O   1 
HETATM 3061 O  O   . HOH F 6 .   ? -23.883 -2.955  29.212  1.00 31.91 ? 664 HOH A O   1 
HETATM 3062 O  O   . HOH F 6 .   ? -16.901 18.230  4.063   1.00 35.76 ? 665 HOH A O   1 
HETATM 3063 O  O   . HOH F 6 .   ? -18.653 20.724  15.198  1.00 33.25 ? 666 HOH A O   1 
HETATM 3064 O  O   . HOH F 6 .   ? 0.123   -20.713 15.063  1.00 39.32 ? 667 HOH A O   1 
HETATM 3065 O  O   . HOH F 6 .   ? -3.560  20.725  14.833  1.00 28.31 ? 668 HOH A O   1 
HETATM 3066 O  O   . HOH F 6 .   ? -0.990  17.813  16.421  1.00 35.04 ? 669 HOH A O   1 
HETATM 3067 O  O   . HOH F 6 .   ? 1.555   13.756  24.583  1.00 35.76 ? 670 HOH A O   1 
HETATM 3068 O  O   . HOH F 6 .   ? 5.691   -3.186  6.707   1.00 31.10 ? 671 HOH A O   1 
HETATM 3069 O  O   . HOH F 6 .   ? -13.834 -5.414  -6.479  1.00 32.13 ? 672 HOH A O   1 
HETATM 3070 O  O   . HOH F 6 .   ? 6.424   -6.112  6.615   1.00 34.19 ? 673 HOH A O   1 
HETATM 3071 O  O   . HOH F 6 .   ? 2.893   -14.717 1.330   1.00 25.39 ? 674 HOH A O   1 
HETATM 3072 O  O   . HOH F 6 .   ? -5.927  17.329  27.828  1.00 35.73 ? 675 HOH A O   1 
HETATM 3073 O  O   . HOH F 6 .   ? -23.307 -0.131  32.017  1.00 30.71 ? 676 HOH A O   1 
HETATM 3074 O  O   . HOH F 6 .   ? -25.532 -1.033  34.995  1.00 32.66 ? 677 HOH A O   1 
HETATM 3075 O  O   . HOH F 6 .   ? -10.478 20.790  25.135  1.00 23.51 ? 678 HOH A O   1 
HETATM 3076 O  O   . HOH F 6 .   ? -17.519 -6.961  42.133  1.00 33.63 ? 679 HOH A O   1 
HETATM 3077 O  O   . HOH F 6 .   ? -15.426 -10.677 -4.521  1.00 32.89 ? 680 HOH A O   1 
HETATM 3078 O  O   . HOH F 6 .   ? 2.370   12.797  22.367  1.00 31.80 ? 681 HOH A O   1 
HETATM 3079 O  O   . HOH F 6 .   ? 2.387   12.072  26.589  1.00 31.95 ? 682 HOH A O   1 
HETATM 3080 O  O   . HOH F 6 .   ? -18.603 -9.045  34.453  1.00 35.91 ? 683 HOH A O   1 
HETATM 3081 O  O   . HOH F 6 .   ? 5.072   -12.074 -6.846  1.00 35.88 ? 684 HOH A O   1 
HETATM 3082 O  O   . HOH F 6 .   ? -1.706  -17.621 5.126   1.00 32.54 ? 685 HOH A O   1 
HETATM 3083 O  O   . HOH F 6 .   ? -2.951  12.044  12.674  1.00 33.60 ? 686 HOH A O   1 
HETATM 3084 O  O   . HOH F 6 .   ? -22.523 -9.546  25.318  1.00 24.61 ? 687 HOH A O   1 
HETATM 3085 O  O   . HOH F 6 .   ? -11.030 -19.133 5.629   1.00 26.07 ? 688 HOH A O   1 
HETATM 3086 O  O   . HOH F 6 .   ? 14.124  5.713   19.258  1.00 30.92 ? 689 HOH A O   1 
HETATM 3087 O  O   . HOH F 6 .   ? 3.501   2.669   8.155   1.00 37.96 ? 690 HOH A O   1 
HETATM 3088 O  O   . HOH F 6 .   ? 3.677   -13.656 12.516  1.00 36.46 ? 691 HOH A O   1 
HETATM 3089 O  O   . HOH F 6 .   ? -6.380  5.165   -6.167  1.00 33.59 ? 692 HOH A O   1 
HETATM 3090 O  O   . HOH F 6 .   ? -10.592 8.422   7.726   1.00 26.36 ? 693 HOH A O   1 
HETATM 3091 O  O   . HOH F 6 .   ? 1.429   2.996   1.896   1.00 31.18 ? 694 HOH A O   1 
HETATM 3092 O  O   . HOH F 6 .   ? 6.088   0.858   8.428   1.00 30.69 ? 695 HOH A O   1 
HETATM 3093 O  O   . HOH F 6 .   ? 5.765   -9.048  7.325   1.00 33.71 ? 696 HOH A O   1 
HETATM 3094 O  O   . HOH F 6 .   ? -10.866 -5.587  38.726  1.00 32.55 ? 697 HOH A O   1 
HETATM 3095 O  O   . HOH F 6 .   ? -27.847 5.300   25.454  1.00 31.57 ? 698 HOH A O   1 
HETATM 3096 O  O   . HOH F 6 .   ? -6.478  6.398   9.639   1.00 31.92 ? 699 HOH A O   1 
HETATM 3097 O  O   . HOH F 6 .   ? -5.995  -20.844 26.527  1.00 30.89 ? 700 HOH A O   1 
HETATM 3098 O  O   . HOH F 6 .   ? -2.868  14.402  11.591  1.00 27.77 ? 701 HOH A O   1 
HETATM 3099 O  O   . HOH F 6 .   ? 2.509   9.720   19.202  1.00 32.17 ? 702 HOH A O   1 
HETATM 3100 O  O   . HOH F 6 .   ? 1.781   -9.752  31.642  1.00 34.42 ? 703 HOH A O   1 
HETATM 3101 O  O   . HOH F 6 .   ? 1.515   -10.031 29.414  1.00 35.70 ? 704 HOH A O   1 
HETATM 3102 O  O   . HOH F 6 .   ? -5.931  0.449   39.277  1.00 35.60 ? 705 HOH A O   1 
HETATM 3103 O  O   . HOH F 6 .   ? -22.440 -12.161 32.408  1.00 36.05 ? 706 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   ? 0.3587 0.3713 0.3810 0.0436  0.1907  0.1307  4   HIS A N   
2    N  N   B HIS A 4   ? 0.1286 0.3433 0.4399 0.1137  0.1932  0.1128  4   HIS A N   
3    C  CA  A HIS A 4   ? 0.3461 0.3598 0.3865 -0.0639 0.2038  0.0340  4   HIS A CA  
4    C  CA  B HIS A 4   ? 0.3059 0.2684 0.4597 -0.1004 0.2275  0.0063  4   HIS A CA  
5    C  C   A HIS A 4   ? 0.2696 0.3215 0.3691 0.0329  0.1616  0.0706  4   HIS A C   
6    C  C   B HIS A 4   ? 0.3222 0.3404 0.3546 0.0200  0.1598  0.0593  4   HIS A C   
7    O  O   A HIS A 4   ? 0.2903 0.3138 0.2770 -0.0233 0.1712  0.0342  4   HIS A O   
8    O  O   B HIS A 4   ? 0.2991 0.3531 0.3424 -0.0141 0.1352  -0.0283 4   HIS A O   
9    C  CB  A HIS A 4   ? 0.2989 0.5388 0.4727 -0.0205 0.1666  0.0626  4   HIS A CB  
10   C  CB  B HIS A 4   ? 0.3330 0.5831 0.4607 -0.0243 0.1489  0.0366  4   HIS A CB  
11   C  CG  A HIS A 4   ? 0.6182 0.2298 0.4399 -0.1422 -0.0427 0.0626  4   HIS A CG  
12   C  CG  B HIS A 4   ? 0.5522 0.4828 0.5065 -0.2090 -0.0108 0.0943  4   HIS A CG  
13   N  ND1 A HIS A 4   ? 0.6065 0.3971 0.1597 -0.1631 -0.1018 -0.0154 4   HIS A ND1 
14   N  ND1 B HIS A 4   ? 0.4354 0.6638 0.5370 -0.1230 -0.1938 -0.0812 4   HIS A ND1 
15   C  CD2 A HIS A 4   ? 0.4011 0.6736 0.5345 -0.0131 -0.3264 0.0020  4   HIS A CD2 
16   C  CD2 B HIS A 4   ? 0.3932 0.3172 0.4781 -0.1879 -0.1975 0.1520  4   HIS A CD2 
17   C  CE1 A HIS A 4   ? 0.6190 0.5752 0.3341 -0.1027 0.0768  -0.1395 4   HIS A CE1 
18   C  CE1 B HIS A 4   ? 0.4530 0.7361 0.5220 -0.1225 -0.1274 -0.0671 4   HIS A CE1 
19   N  NE2 A HIS A 4   ? 0.8032 0.4573 0.3921 -0.0588 -0.1189 -0.0023 4   HIS A NE2 
20   N  NE2 B HIS A 4   ? 0.6261 0.8001 0.2958 0.1544  -0.2105 0.0417  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1881 0.2527 0.3167 -0.0388 0.1167  0.0377  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1488 0.1867 0.2432 -0.0344 0.0724  0.0124  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1535 0.1796 0.2305 -0.0068 0.0991  -0.0226 5   TRP A C   
24   O  O   . TRP A 5   ? 0.1890 0.2064 0.2316 -0.0115 0.0790  0.0098  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1527 0.1939 0.2457 -0.0346 0.0693  0.0030  5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1553 0.1747 0.1895 -0.0416 0.0579  -0.0104 5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.1710 0.1996 0.2885 -0.0386 0.0678  0.0249  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1532 0.1659 0.1576 0.0040  0.0472  -0.0285 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.2009 0.1854 0.2179 0.0243  0.0671  0.0167  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.2008 0.1939 0.1526 0.0239  0.0412  -0.0037 5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1385 0.1743 0.1394 -0.0230 0.0348  -0.0482 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1905 0.2578 0.1206 0.0024  0.0294  -0.0217 5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1565 0.2048 0.1193 -0.0043 0.0326  -0.0507 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1518 0.2554 0.1378 0.0177  0.0436  -0.0533 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1633 0.1441 0.2459 -0.0040 0.0935  -0.0302 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.2097 0.1653 0.2271 -0.0377 0.0723  -0.0326 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1660 0.1465 0.2053 -0.0152 0.1062  -0.0302 6   GLY A C   
38   O  O   . GLY A 6   ? 0.1307 0.1858 0.2179 0.0120  0.0957  -0.0273 6   GLY A O   
39   N  N   A TYR A 7   ? 0.1353 0.1455 0.2849 -0.0077 0.0988  -0.0386 7   TYR A N   
40   N  N   B TYR A 7   ? 0.1097 0.1509 0.3129 -0.0048 0.1360  -0.0715 7   TYR A N   
41   C  CA  A TYR A 7   ? 0.1001 0.1544 0.2669 0.0038  0.0842  -0.0227 7   TYR A CA  
42   C  CA  B TYR A 7   ? 0.1265 0.1249 0.2278 -0.0204 0.0366  -0.0755 7   TYR A CA  
43   C  C   A TYR A 7   ? 0.1251 0.1356 0.2989 0.0342  0.0463  0.0244  7   TYR A C   
44   C  C   B TYR A 7   ? 0.0807 0.1960 0.2597 -0.0054 0.0007  -0.0381 7   TYR A C   
45   O  O   A TYR A 7   ? 0.1611 0.1312 0.4957 0.0333  0.0441  0.0549  7   TYR A O   
46   O  O   B TYR A 7   ? 0.0820 0.1849 0.2714 0.0082  -0.0070 -0.0329 7   TYR A O   
47   C  CB  A TYR A 7   ? 0.0992 0.1477 0.2238 0.0119  0.0724  -0.0359 7   TYR A CB  
48   C  CB  B TYR A 7   ? 0.1351 0.1814 0.2290 -0.0077 0.0115  -0.1159 7   TYR A CB  
49   C  CG  A TYR A 7   ? 0.0812 0.1319 0.1861 -0.0093 0.0619  -0.0456 7   TYR A CG  
50   C  CG  B TYR A 7   ? 0.0886 0.1606 0.1957 -0.0516 0.0675  -0.1027 7   TYR A CG  
51   C  CD1 A TYR A 7   ? 0.1124 0.1527 0.1926 -0.0285 0.0763  -0.0467 7   TYR A CD1 
52   C  CD1 B TYR A 7   ? 0.0872 0.1347 0.1817 -0.0432 0.0430  -0.0794 7   TYR A CD1 
53   C  CD2 A TYR A 7   ? 0.0949 0.1237 0.2066 -0.0054 0.0714  -0.0478 7   TYR A CD2 
54   C  CD2 B TYR A 7   ? 0.1400 0.1347 0.2727 -0.0320 0.0767  -0.0456 7   TYR A CD2 
55   C  CE1 A TYR A 7   ? 0.0930 0.1242 0.1532 -0.0507 0.0494  -0.0397 7   TYR A CE1 
56   C  CE1 B TYR A 7   ? 0.1383 0.1344 0.1249 -0.0167 0.0564  -0.0406 7   TYR A CE1 
57   C  CE2 A TYR A 7   ? 0.0953 0.1633 0.1283 0.0027  0.0644  -0.0675 7   TYR A CE2 
58   C  CE2 B TYR A 7   ? 0.1270 0.1360 0.1504 -0.0480 0.0886  -0.0299 7   TYR A CE2 
59   C  CZ  A TYR A 7   ? 0.1093 0.1362 0.1332 -0.0192 0.0584  -0.0511 7   TYR A CZ  
60   C  CZ  B TYR A 7   ? 0.1299 0.1142 0.1477 -0.0337 0.0649  -0.0225 7   TYR A CZ  
61   O  OH  A TYR A 7   ? 0.1393 0.1114 0.1621 0.0046  0.0423  -0.0292 7   TYR A OH  
62   O  OH  B TYR A 7   ? 0.1507 0.1365 0.1021 -0.0141 0.0798  -0.0088 7   TYR A OH  
63   N  N   A GLY A 8   ? 0.1420 0.0908 0.3792 0.0283  0.0974  -0.0340 8   GLY A N   
64   N  N   B GLY A 8   ? 0.1362 0.2142 0.1998 0.0728  0.0220  -0.0211 8   GLY A N   
65   C  CA  A GLY A 8   ? 0.1579 0.1516 0.4734 0.0776  0.0851  -0.0080 8   GLY A CA  
66   C  CA  B GLY A 8   ? 0.0992 0.1633 0.2624 0.0307  0.0161  -0.0109 8   GLY A CA  
67   C  C   A GLY A 8   ? 0.1242 0.1793 0.3555 0.0728  0.1228  -0.0331 8   GLY A C   
68   C  C   B GLY A 8   ? 0.1409 0.1097 0.3095 0.0230  -0.0131 -0.0269 8   GLY A C   
69   O  O   A GLY A 8   ? 0.1471 0.1802 0.4077 0.0043  0.1014  -0.0529 8   GLY A O   
70   O  O   B GLY A 8   ? 0.1450 0.1716 0.2897 0.0187  0.0995  -0.0815 8   GLY A O   
71   N  N   A LYS A 9   ? 0.1376 0.1667 0.4778 0.0715  0.0895  -0.0206 9   LYS A N   
72   N  N   B LYS A 9   ? 0.1357 0.1660 0.2335 0.0445  -0.0292 -0.0617 9   LYS A N   
73   C  CA  A LYS A 9   ? 0.1520 0.1818 0.3506 0.0012  0.1061  -0.0375 9   LYS A CA  
74   C  CA  B LYS A 9   ? 0.1294 0.1738 0.3492 0.0186  -0.0630 0.0092  9   LYS A CA  
75   C  C   A LYS A 9   ? 0.0797 0.2041 0.2865 0.0198  0.0680  -0.0340 9   LYS A C   
76   C  C   B LYS A 9   ? 0.1603 0.1928 0.2172 0.0074  -0.0208 -0.0174 9   LYS A C   
77   O  O   A LYS A 9   ? 0.1710 0.1802 0.2484 0.0197  0.0665  0.0006  9   LYS A O   
78   O  O   B LYS A 9   ? 0.1337 0.1915 0.2069 -0.0076 0.0142  0.0384  9   LYS A O   
79   C  CB  A LYS A 9   ? 0.2964 0.0978 0.4411 0.0104  0.0270  0.0502  9   LYS A CB  
80   C  CB  B LYS A 9   ? 0.1628 0.2569 0.3106 -0.0309 0.0469  -0.0509 9   LYS A CB  
81   C  CG  A LYS A 9   ? 0.1809 0.1872 0.4838 0.0037  0.0511  0.0006  9   LYS A CG  
82   C  CG  B LYS A 9   ? 0.1558 0.2693 0.4616 -0.0450 0.0035  -0.0452 9   LYS A CG  
83   C  CD  A LYS A 9   ? 0.2958 0.1491 0.6524 -0.0137 0.0816  -0.0326 9   LYS A CD  
84   C  CD  B LYS A 9   ? 0.2942 0.4049 0.5946 0.1010  0.0361  -0.0491 9   LYS A CD  
85   C  CE  A LYS A 9   ? 0.3077 0.2061 0.8277 0.0296  -0.0165 0.0359  9   LYS A CE  
86   C  CE  B LYS A 9   ? 0.4052 0.2883 0.5960 0.2060  0.0410  -0.0522 9   LYS A CE  
87   N  NZ  A LYS A 9   ? 0.3819 0.2651 0.9764 0.0115  -0.1342 -0.2639 9   LYS A NZ  
88   N  NZ  B LYS A 9   ? 0.2919 0.4138 0.8999 0.1888  0.1261  -0.0649 9   LYS A NZ  
89   N  N   A HIS A 10  ? 0.0973 0.1965 0.3055 0.0344  0.0970  -0.0227 10  HIS A N   
90   N  N   B HIS A 10  ? 0.0982 0.1730 0.1861 0.0076  0.0205  -0.0500 10  HIS A N   
91   C  CA  A HIS A 10  ? 0.0949 0.2500 0.1985 0.0285  0.0904  -0.0159 10  HIS A CA  
92   C  CA  B HIS A 10  ? 0.0965 0.1344 0.1901 0.0120  0.0366  -0.0225 10  HIS A CA  
93   C  C   A HIS A 10  ? 0.0534 0.2454 0.2002 0.0012  0.0671  -0.0414 10  HIS A C   
94   C  C   B HIS A 10  ? 0.1102 0.1319 0.2158 0.0137  -0.0136 -0.0197 10  HIS A C   
95   O  O   A HIS A 10  ? 0.0797 0.2630 0.3616 0.0043  0.0711  -0.1424 10  HIS A O   
96   O  O   B HIS A 10  ? 0.1360 0.1396 0.2251 0.0006  -0.0148 -0.0379 10  HIS A O   
97   C  CB  A HIS A 10  ? 0.1416 0.2161 0.1605 0.0274  0.0715  -0.0307 10  HIS A CB  
98   C  CB  B HIS A 10  ? 0.0956 0.1725 0.1955 0.0491  0.0295  -0.0295 10  HIS A CB  
99   C  CG  A HIS A 10  ? 0.1277 0.2002 0.1633 -0.0024 0.0054  -0.0452 10  HIS A CG  
100  C  CG  B HIS A 10  ? 0.1225 0.1508 0.1831 0.0320  -0.0136 -0.0474 10  HIS A CG  
101  N  ND1 A HIS A 10  ? 0.1428 0.1827 0.2348 0.0183  -0.0063 -0.0384 10  HIS A ND1 
102  N  ND1 B HIS A 10  ? 0.0900 0.1762 0.2002 0.0136  -0.0093 -0.0516 10  HIS A ND1 
103  C  CD2 A HIS A 10  ? 0.1472 0.2386 0.1703 0.0271  -0.0164 -0.0710 10  HIS A CD2 
104  C  CD2 B HIS A 10  ? 0.1360 0.1639 0.1221 0.0307  0.0359  -0.0522 10  HIS A CD2 
105  C  CE1 A HIS A 10  ? 0.1581 0.2179 0.2980 0.0265  0.0148  -0.0997 10  HIS A CE1 
106  C  CE1 B HIS A 10  ? 0.1136 0.1545 0.1599 0.0195  0.0049  -0.0065 10  HIS A CE1 
107  N  NE2 A HIS A 10  ? 0.1253 0.2350 0.3427 0.0031  -0.0049 -0.0636 10  HIS A NE2 
108  N  NE2 B HIS A 10  ? 0.0750 0.2098 0.2027 0.0208  0.0132  -0.0232 10  HIS A NE2 
109  N  N   A ASN A 11  ? 0.0754 0.1912 0.1832 0.0386  0.0452  -0.0109 11  ASN A N   
110  N  N   B ASN A 11  ? 0.1215 0.1586 0.1948 0.0476  -0.0007 0.0142  11  ASN A N   
111  C  CA  A ASN A 11  ? 0.0951 0.2161 0.2328 0.0178  0.0983  -0.0384 11  ASN A CA  
112  C  CA  B ASN A 11  ? 0.1386 0.1613 0.2377 0.0137  0.0903  -0.0288 11  ASN A CA  
113  C  C   A ASN A 11  ? 0.1714 0.1660 0.2371 0.0362  0.1430  -0.0073 11  ASN A C   
114  C  C   B ASN A 11  ? 0.1499 0.1581 0.3005 -0.0038 0.1181  -0.0054 11  ASN A C   
115  O  O   A ASN A 11  ? 0.1635 0.1820 0.2903 0.0456  0.1221  -0.0057 11  ASN A O   
116  O  O   B ASN A 11  ? 0.1193 0.1687 0.2937 -0.0151 0.1106  -0.0175 11  ASN A O   
117  C  CB  A ASN A 11  ? 0.0573 0.2254 0.2132 -0.0060 0.0763  -0.0476 11  ASN A CB  
118  C  CB  B ASN A 11  ? 0.0957 0.1664 0.2357 -0.0405 0.0929  -0.0285 11  ASN A CB  
119  C  CG  A ASN A 11  ? 0.1773 0.1490 0.2263 -0.0189 0.0465  -0.0625 11  ASN A CG  
120  C  CG  B ASN A 11  ? 0.1498 0.2265 0.1888 -0.0164 0.0983  -0.0732 11  ASN A CG  
121  O  OD1 A ASN A 11  ? 0.1021 0.2293 0.3601 -0.0262 0.0276  0.0282  11  ASN A OD1 
122  O  OD1 B ASN A 11  ? 0.0982 0.2152 0.3648 -0.0154 0.0526  -0.0606 11  ASN A OD1 
123  N  ND2 A ASN A 11  ? 0.2053 0.2097 0.1962 -0.0399 0.1120  -0.0666 11  ASN A ND2 
124  N  ND2 B ASN A 11  ? 0.2542 0.3531 0.1748 -0.0010 0.1289  -0.0434 11  ASN A ND2 
125  N  N   . GLY A 12  ? 0.1242 0.1771 0.2759 0.0148  0.1120  -0.0073 12  GLY A N   
126  C  CA  . GLY A 12  ? 0.1294 0.1518 0.2443 0.0093  0.1054  -0.0474 12  GLY A CA  
127  C  C   . GLY A 12  ? 0.1247 0.1075 0.2239 0.0248  0.0785  -0.0054 12  GLY A C   
128  O  O   . GLY A 12  ? 0.1066 0.1405 0.2763 -0.0006 0.0520  -0.0015 12  GLY A O   
129  N  N   . PRO A 13  ? 0.1030 0.1387 0.1935 -0.0019 0.0599  -0.0206 13  PRO A N   
130  C  CA  . PRO A 13  ? 0.1003 0.1281 0.2086 0.0006  0.0693  -0.0135 13  PRO A CA  
131  C  C   . PRO A 13  ? 0.1221 0.1133 0.2117 0.0085  0.0671  -0.0037 13  PRO A C   
132  O  O   . PRO A 13  ? 0.0924 0.1391 0.2617 0.0114  0.0439  -0.0304 13  PRO A O   
133  C  CB  . PRO A 13  ? 0.1181 0.1333 0.2043 -0.0185 0.0573  -0.0175 13  PRO A CB  
134  C  CG  . PRO A 13  ? 0.1026 0.1416 0.2080 -0.0140 0.0649  -0.0351 13  PRO A CG  
135  C  CD  . PRO A 13  ? 0.1124 0.1782 0.2069 -0.0026 0.0658  -0.0401 13  PRO A CD  
136  N  N   . GLU A 14  ? 0.1085 0.1197 0.2791 0.0096  0.0463  -0.0163 14  GLU A N   
137  C  CA  . GLU A 14  ? 0.1249 0.1093 0.3289 0.0119  0.0082  -0.0027 14  GLU A CA  
138  C  C   . GLU A 14  ? 0.1249 0.1262 0.2754 0.0395  0.0277  -0.0091 14  GLU A C   
139  O  O   . GLU A 14  ? 0.1281 0.1578 0.3379 0.0368  0.0233  0.0192  14  GLU A O   
140  C  CB  . GLU A 14  ? 0.2583 0.1314 0.2827 0.0350  0.0274  0.0423  14  GLU A CB  
141  C  CG  . GLU A 14  ? 0.2623 0.1820 0.5115 -0.0425 0.0077  -0.0324 14  GLU A CG  
142  C  CD  . GLU A 14  ? 0.4971 0.3420 0.4013 -0.0838 -0.0035 0.0236  14  GLU A CD  
143  O  OE1 . GLU A 14  ? 0.5554 0.3452 0.4063 0.0777  0.1233  -0.0631 14  GLU A OE1 
144  O  OE2 . GLU A 14  ? 0.5651 0.4873 0.3012 -0.0975 0.0052  0.0313  14  GLU A OE2 
145  N  N   . HIS A 15  ? 0.0741 0.1141 0.2752 0.0283  0.0286  -0.0077 15  HIS A N   
146  C  CA  . HIS A 15  ? 0.0956 0.1242 0.2921 0.0109  0.0623  0.0110  15  HIS A CA  
147  C  C   . HIS A 15  ? 0.0818 0.1412 0.2948 0.0186  0.0231  -0.0194 15  HIS A C   
148  O  O   . HIS A 15  ? 0.0723 0.1398 0.3201 0.0148  0.0288  -0.0005 15  HIS A O   
149  C  CB  . HIS A 15  ? 0.1154 0.1333 0.3014 0.0140  0.0586  -0.0085 15  HIS A CB  
150  C  CG  . HIS A 15  ? 0.1091 0.1509 0.3578 0.0296  0.0538  -0.0076 15  HIS A CG  
151  N  ND1 . HIS A 15  ? 0.1172 0.1984 0.3808 0.0392  0.0527  -0.0281 15  HIS A ND1 
152  C  CD2 . HIS A 15  ? 0.1962 0.1696 0.3289 0.0755  0.0886  -0.0362 15  HIS A CD2 
153  C  CE1 . HIS A 15  ? 0.2219 0.1967 0.3454 0.0623  0.0342  -0.0348 15  HIS A CE1 
154  N  NE2 . HIS A 15  ? 0.1835 0.1802 0.3124 0.0733  0.0793  -0.0263 15  HIS A NE2 
155  N  N   . TRP A 16  ? 0.0737 0.1274 0.2368 0.0244  0.0375  0.0038  16  TRP A N   
156  C  CA  . TRP A 16  ? 0.0658 0.1030 0.2445 -0.0035 0.0326  -0.0142 16  TRP A CA  
157  C  C   . TRP A 16  ? 0.0564 0.1141 0.2260 0.0063  0.0186  -0.0048 16  TRP A C   
158  O  O   . TRP A 16  ? 0.0732 0.1030 0.2572 -0.0003 0.0031  -0.0076 16  TRP A O   
159  C  CB  . TRP A 16  ? 0.0661 0.1277 0.2237 -0.0065 0.0178  -0.0188 16  TRP A CB  
160  C  CG  . TRP A 16  ? 0.0524 0.1188 0.1798 0.0174  0.0085  -0.0019 16  TRP A CG  
161  C  CD1 . TRP A 16  ? 0.0820 0.1206 0.1935 -0.0137 0.0410  -0.0200 16  TRP A CD1 
162  C  CD2 . TRP A 16  ? 0.0627 0.1070 0.1859 0.0046  0.0326  -0.0098 16  TRP A CD2 
163  N  NE1 . TRP A 16  ? 0.0809 0.1313 0.2037 0.0023  0.0562  -0.0329 16  TRP A NE1 
164  C  CE2 . TRP A 16  ? 0.0885 0.1075 0.1729 0.0063  0.0412  -0.0082 16  TRP A CE2 
165  C  CE3 . TRP A 16  ? 0.0582 0.1005 0.2005 0.0054  0.0270  -0.0136 16  TRP A CE3 
166  C  CZ2 . TRP A 16  ? 0.0974 0.1064 0.1727 0.0019  0.0482  -0.0216 16  TRP A CZ2 
167  C  CZ3 . TRP A 16  ? 0.0847 0.0940 0.1576 -0.0060 0.0313  -0.0181 16  TRP A CZ3 
168  C  CH2 . TRP A 16  ? 0.0969 0.1066 0.1499 0.0023  0.0364  -0.0155 16  TRP A CH2 
169  N  N   . HIS A 17  ? 0.0701 0.1215 0.2299 0.0082  0.0091  0.0074  17  HIS A N   
170  C  CA  . HIS A 17  ? 0.0750 0.1387 0.2687 -0.0108 -0.0006 -0.0054 17  HIS A CA  
171  C  C   . HIS A 17  ? 0.0856 0.1366 0.2949 -0.0041 0.0115  0.0109  17  HIS A C   
172  O  O   . HIS A 17  ? 0.0741 0.1639 0.3070 0.0005  -0.0120 -0.0097 17  HIS A O   
173  C  CB  . HIS A 17  ? 0.0696 0.1838 0.3045 0.0037  0.0428  0.0232  17  HIS A CB  
174  C  CG  . HIS A 17  ? 0.0767 0.1788 0.3169 0.0027  0.0098  0.0248  17  HIS A CG  
175  N  ND1 . HIS A 17  ? 0.0930 0.2010 0.3070 0.0175  -0.0057 0.0307  17  HIS A ND1 
176  C  CD2 . HIS A 17  ? 0.0953 0.1908 0.2782 0.0559  0.0120  0.0288  17  HIS A CD2 
177  C  CE1 . HIS A 17  ? 0.1271 0.1971 0.3242 0.0361  0.0074  0.0625  17  HIS A CE1 
178  N  NE2 . HIS A 17  ? 0.0942 0.2183 0.2899 0.0364  0.0035  0.0516  17  HIS A NE2 
179  N  N   . LYS A 18  ? 0.0407 0.1732 0.3048 0.0034  0.0166  0.0119  18  LYS A N   
180  C  CA  . LYS A 18  ? 0.0675 0.1800 0.3472 -0.0098 0.0126  0.0469  18  LYS A CA  
181  C  C   . LYS A 18  ? 0.1041 0.1642 0.3138 -0.0342 -0.0013 0.0482  18  LYS A C   
182  O  O   . LYS A 18  ? 0.1150 0.1795 0.4941 -0.0469 -0.0753 0.0680  18  LYS A O   
183  C  CB  . LYS A 18  ? 0.0370 0.2070 0.2955 0.0038  -0.0153 0.0524  18  LYS A CB  
184  C  CG  . LYS A 18  ? 0.0965 0.1938 0.3648 0.0507  0.0706  0.0939  18  LYS A CG  
185  C  CD  . LYS A 18  ? 0.0718 0.1832 0.3300 0.0262  0.0351  0.0458  18  LYS A CD  
186  C  CE  . LYS A 18  ? 0.0929 0.1807 0.3045 0.0425  0.0175  0.0417  18  LYS A CE  
187  N  NZ  . LYS A 18  ? 0.0811 0.2122 0.3176 0.0524  0.0577  0.0719  18  LYS A NZ  
188  N  N   . ASP A 19  ? 0.0741 0.1844 0.3136 0.0171  0.0043  0.0377  19  ASP A N   
189  C  CA  . ASP A 19  ? 0.0976 0.1462 0.3657 0.0015  0.0297  0.0043  19  ASP A CA  
190  C  C   . ASP A 19  ? 0.1073 0.1435 0.3366 -0.0206 0.0203  0.0019  19  ASP A C   
191  O  O   . ASP A 19  ? 0.1258 0.1545 0.3251 -0.0228 0.0231  0.0186  19  ASP A O   
192  C  CB  . ASP A 19  ? 0.1260 0.3161 0.3142 -0.0060 0.0405  0.0181  19  ASP A CB  
193  C  CG  . ASP A 19  ? 0.1371 0.3427 0.4065 0.0215  0.0599  -0.1040 19  ASP A CG  
194  O  OD1 . ASP A 19  ? 0.1459 0.4210 0.3925 0.0076  0.0533  0.0214  19  ASP A OD1 
195  O  OD2 . ASP A 19  ? 0.3882 0.5824 0.4325 0.0035  0.1030  -0.2347 19  ASP A OD2 
196  N  N   A PHE A 20  ? 0.0476 0.1461 0.2842 -0.0131 0.0017  0.0063  20  PHE A N   
197  N  N   B PHE A 20  ? 0.0491 0.1405 0.2915 -0.0076 -0.0086 0.0115  20  PHE A N   
198  C  CA  A PHE A 20  ? 0.0657 0.0772 0.2630 -0.0131 0.0023  0.0098  20  PHE A CA  
199  C  CA  B PHE A 20  ? 0.0614 0.2050 0.2768 -0.0015 -0.0104 -0.0063 20  PHE A CA  
200  C  C   A PHE A 20  ? 0.0684 0.1145 0.2445 -0.0024 0.0060  -0.0164 20  PHE A C   
201  C  C   B PHE A 20  ? 0.1356 0.1102 0.2662 -0.0480 -0.0148 -0.0296 20  PHE A C   
202  O  O   A PHE A 20  ? 0.0807 0.1071 0.2763 -0.0076 0.0121  -0.0159 20  PHE A O   
203  O  O   B PHE A 20  ? 0.0579 0.1221 0.2915 -0.0184 -0.0103 -0.0074 20  PHE A O   
204  C  CB  A PHE A 20  ? 0.0798 0.1091 0.2154 -0.0452 0.0214  -0.0076 20  PHE A CB  
205  C  CB  B PHE A 20  ? 0.0599 0.1490 0.2585 0.0121  -0.0156 0.0154  20  PHE A CB  
206  C  CG  A PHE A 20  ? 0.1001 0.1190 0.2109 -0.0533 0.0274  -0.0173 20  PHE A CG  
207  C  CG  B PHE A 20  ? 0.0402 0.1987 0.2217 -0.0362 -0.0027 0.0119  20  PHE A CG  
208  C  CD1 A PHE A 20  ? 0.1376 0.1195 0.1863 -0.0636 -0.0010 -0.0141 20  PHE A CD1 
209  C  CD1 B PHE A 20  ? 0.0702 0.2187 0.2156 0.0017  0.0154  0.0399  20  PHE A CD1 
210  C  CD2 A PHE A 20  ? 0.0755 0.1371 0.2476 -0.0258 0.0318  -0.0248 20  PHE A CD2 
211  C  CD2 B PHE A 20  ? 0.1064 0.2312 0.2224 -0.0537 0.0041  0.0013  20  PHE A CD2 
212  C  CE1 A PHE A 20  ? 0.0967 0.2199 0.1845 -0.0516 0.0000  -0.0035 20  PHE A CE1 
213  C  CE1 B PHE A 20  ? 0.0915 0.2572 0.2324 -0.0342 0.0653  0.0575  20  PHE A CE1 
214  C  CE2 A PHE A 20  ? 0.1102 0.1651 0.2405 -0.0046 0.0710  -0.0549 20  PHE A CE2 
215  C  CE2 B PHE A 20  ? 0.1562 0.2075 0.2712 -0.0768 0.0467  0.0524  20  PHE A CE2 
216  C  CZ  A PHE A 20  ? 0.0960 0.2114 0.1531 -0.0292 0.0357  0.0258  20  PHE A CZ  
217  C  CZ  B PHE A 20  ? 0.1739 0.2494 0.2159 -0.0043 0.0379  0.0759  20  PHE A CZ  
218  N  N   A PRO A 21  ? 0.0930 0.1190 0.2926 -0.0230 -0.0140 -0.0048 21  PRO A N   
219  N  N   B PRO A 21  ? 0.0820 0.1486 0.3125 -0.0333 -0.0175 -0.0305 21  PRO A N   
220  C  CA  A PRO A 21  ? 0.0342 0.1983 0.2919 -0.0209 -0.0401 -0.0068 21  PRO A CA  
221  C  CA  B PRO A 21  ? 0.0836 0.1674 0.2976 -0.0219 -0.0153 -0.0251 21  PRO A CA  
222  C  C   A PRO A 21  ? 0.0877 0.1498 0.2824 -0.0118 -0.0304 -0.0215 21  PRO A C   
223  C  C   B PRO A 21  ? 0.0987 0.1492 0.2727 0.0142  -0.0174 -0.0034 21  PRO A C   
224  O  O   A PRO A 21  ? 0.0600 0.1578 0.2933 -0.0006 -0.0450 -0.0136 21  PRO A O   
225  O  O   B PRO A 21  ? 0.0926 0.1725 0.2495 -0.0096 -0.0516 -0.0020 21  PRO A O   
226  C  CB  A PRO A 21  ? 0.0872 0.2845 0.2917 -0.0820 -0.0535 -0.0026 21  PRO A CB  
227  C  CB  B PRO A 21  ? 0.0692 0.1894 0.3986 -0.0538 -0.0204 -0.0137 21  PRO A CB  
228  C  CG  A PRO A 21  ? 0.1504 0.2275 0.3388 -0.0802 -0.0208 0.0276  21  PRO A CG  
229  C  CG  B PRO A 21  ? 0.1676 0.1659 0.3183 -0.0882 -0.0137 -0.0649 21  PRO A CG  
230  C  CD  A PRO A 21  ? 0.0829 0.1902 0.3334 -0.0604 0.0054  -0.0232 21  PRO A CD  
231  C  CD  B PRO A 21  ? 0.1499 0.1152 0.2820 -0.0361 -0.0456 -0.0170 21  PRO A CD  
232  N  N   A ILE A 22  ? 0.0608 0.1384 0.2059 -0.0242 -0.0281 -0.0313 22  ILE A N   
233  N  N   B ILE A 22  ? 0.0948 0.1297 0.2143 0.0175  -0.0277 -0.0465 22  ILE A N   
234  C  CA  A ILE A 22  ? 0.0776 0.1109 0.2231 -0.0439 -0.0296 0.0197  22  ILE A CA  
235  C  CA  B ILE A 22  ? 0.1305 0.1315 0.1436 0.0020  -0.0283 -0.0318 22  ILE A CA  
236  C  C   A ILE A 22  ? 0.0666 0.1116 0.2217 -0.0170 -0.0304 -0.0520 22  ILE A C   
237  C  C   B ILE A 22  ? 0.0821 0.1328 0.1549 0.0057  -0.0035 -0.0170 22  ILE A C   
238  O  O   A ILE A 22  ? 0.0781 0.0854 0.1905 0.0284  -0.0381 -0.0108 22  ILE A O   
239  O  O   B ILE A 22  ? 0.0852 0.1477 0.1274 0.0187  0.0005  -0.0132 22  ILE A O   
240  C  CB  A ILE A 22  ? 0.0852 0.1154 0.1515 -0.0108 0.0119  -0.0271 22  ILE A CB  
241  C  CB  B ILE A 22  ? 0.1199 0.1271 0.1106 -0.0082 -0.0219 -0.0020 22  ILE A CB  
242  C  CG1 A ILE A 22  ? 0.1409 0.1118 0.2188 0.0131  0.0684  -0.0283 22  ILE A CG1 
243  C  CG1 B ILE A 22  ? 0.1220 0.0908 0.0961 -0.0263 -0.0248 -0.0292 22  ILE A CG1 
244  C  CG2 A ILE A 22  ? 0.0710 0.1529 0.1623 0.0120  -0.0082 -0.0031 22  ILE A CG2 
245  C  CG2 B ILE A 22  ? 0.1225 0.1673 0.1392 -0.0476 -0.0362 -0.0296 22  ILE A CG2 
246  C  CD1 A ILE A 22  ? 0.2197 0.1684 0.2585 -0.0434 -0.0216 0.0031  22  ILE A CD1 
247  C  CD1 B ILE A 22  ? 0.0869 0.1211 0.2296 -0.0142 -0.0175 -0.0120 22  ILE A CD1 
248  N  N   . ALA A 23  ? 0.0924 0.1048 0.2001 -0.0031 -0.0218 -0.0375 23  ALA A N   
249  C  CA  . ALA A 23  ? 0.0802 0.1190 0.1841 0.0000  -0.0048 -0.0199 23  ALA A CA  
250  C  C   . ALA A 23  ? 0.0767 0.1292 0.1894 -0.0065 0.0000  -0.0285 23  ALA A C   
251  O  O   . ALA A 23  ? 0.1009 0.1269 0.1978 -0.0024 -0.0060 -0.0333 23  ALA A O   
252  C  CB  . ALA A 23  ? 0.0645 0.1444 0.1913 -0.0027 -0.0040 -0.0239 23  ALA A CB  
253  N  N   . LYS A 24  ? 0.1012 0.1412 0.1756 0.0057  -0.0252 -0.0119 24  LYS A N   
254  C  CA  . LYS A 24  ? 0.0802 0.1805 0.1917 0.0049  -0.0244 -0.0306 24  LYS A CA  
255  C  C   . LYS A 24  ? 0.0909 0.1693 0.1892 -0.0098 -0.0230 -0.0375 24  LYS A C   
256  O  O   . LYS A 24  ? 0.1398 0.2251 0.2236 -0.0098 -0.0595 -0.0142 24  LYS A O   
257  C  CB  . LYS A 24  ? 0.0952 0.2163 0.2565 0.0186  -0.0395 -0.0377 24  LYS A CB  
258  C  CG  . LYS A 24  ? 0.1393 0.2125 0.2592 0.0425  -0.0043 -0.0225 24  LYS A CG  
259  C  CD  . LYS A 24  ? 0.1632 0.2574 0.3754 0.0979  -0.0108 0.0264  24  LYS A CD  
260  C  CE  . LYS A 24  ? 0.1721 0.3084 0.4336 0.0913  -0.0060 0.0507  24  LYS A CE  
261  N  NZ  . LYS A 24  ? 0.2357 0.2694 0.4948 0.0397  0.0803  -0.0331 24  LYS A NZ  
262  N  N   . GLY A 25  ? 0.0908 0.1651 0.1972 0.0200  -0.0244 -0.0357 25  GLY A N   
263  C  CA  . GLY A 25  ? 0.1093 0.1870 0.1991 -0.0065 -0.0137 -0.0568 25  GLY A CA  
264  C  C   . GLY A 25  ? 0.0996 0.1698 0.1827 -0.0035 -0.0460 -0.0491 25  GLY A C   
265  O  O   . GLY A 25  ? 0.1206 0.1743 0.1737 0.0146  -0.0307 -0.0307 25  GLY A O   
266  N  N   . GLU A 26  ? 0.1075 0.2117 0.1531 -0.0023 -0.0417 -0.0463 26  GLU A N   
267  C  CA  . GLU A 26  ? 0.1574 0.2192 0.1292 0.0007  -0.0458 -0.0465 26  GLU A CA  
268  C  C   . GLU A 26  ? 0.1342 0.1571 0.1163 0.0131  -0.0229 -0.0364 26  GLU A C   
269  O  O   . GLU A 26  ? 0.1682 0.1879 0.0960 -0.0035 -0.0362 -0.0164 26  GLU A O   
270  C  CB  . GLU A 26  ? 0.2248 0.2608 0.1617 -0.0015 -0.0771 -0.1010 26  GLU A CB  
271  C  CG  . GLU A 26  ? 0.2095 0.2808 0.2023 -0.0153 -0.0474 -0.0231 26  GLU A CG  
272  C  CD  . GLU A 26  ? 0.2170 0.3713 0.2621 -0.0276 -0.1365 -0.0059 26  GLU A CD  
273  O  OE1 . GLU A 26  ? 0.4041 0.3598 0.3607 -0.0746 -0.1905 0.0474  26  GLU A OE1 
274  O  OE2 . GLU A 26  ? 0.2883 0.4406 0.3907 0.0855  -0.0649 0.0286  26  GLU A OE2 
275  N  N   . ARG A 27  ? 0.1137 0.1206 0.1120 0.0024  -0.0377 -0.0329 27  ARG A N   
276  C  CA  . ARG A 27  ? 0.1084 0.1125 0.1019 0.0093  -0.0261 -0.0124 27  ARG A CA  
277  C  C   . ARG A 27  ? 0.0842 0.1075 0.0850 0.0000  -0.0102 -0.0162 27  ARG A C   
278  O  O   . ARG A 27  ? 0.0929 0.0982 0.0931 0.0024  -0.0102 -0.0125 27  ARG A O   
279  C  CB  . ARG A 27  ? 0.1516 0.1150 0.1098 0.0225  -0.0189 -0.0188 27  ARG A CB  
280  C  CG  . ARG A 27  ? 0.1518 0.1233 0.1358 0.0010  -0.0096 -0.0143 27  ARG A CG  
281  C  CD  . ARG A 27  ? 0.1714 0.1308 0.1292 0.0115  -0.0288 -0.0315 27  ARG A CD  
282  N  NE  . ARG A 27  ? 0.1486 0.1176 0.0994 -0.0031 0.0113  -0.0275 27  ARG A NE  
283  C  CZ  . ARG A 27  ? 0.1398 0.1319 0.0696 0.0076  0.0154  0.0048  27  ARG A CZ  
284  N  NH1 . ARG A 27  ? 0.1685 0.1389 0.1161 0.0160  0.0193  -0.0381 27  ARG A NH1 
285  N  NH2 . ARG A 27  ? 0.1234 0.1403 0.1213 -0.0023 0.0131  -0.0071 27  ARG A NH2 
286  N  N   . GLN A 28  ? 0.0772 0.1111 0.0978 0.0087  -0.0109 -0.0156 28  GLN A N   
287  C  CA  . GLN A 28  ? 0.0750 0.1000 0.0881 -0.0030 0.0030  -0.0175 28  GLN A CA  
288  C  C   . GLN A 28  ? 0.0728 0.1084 0.0838 0.0104  -0.0041 -0.0040 28  GLN A C   
289  O  O   . GLN A 28  ? 0.0942 0.1134 0.0790 0.0000  -0.0043 -0.0076 28  GLN A O   
290  C  CB  . GLN A 28  ? 0.0579 0.1146 0.1353 -0.0043 -0.0097 -0.0198 28  GLN A CB  
291  C  CG  . GLN A 28  ? 0.0894 0.1224 0.1039 -0.0019 -0.0126 -0.0293 28  GLN A CG  
292  C  CD  . GLN A 28  ? 0.0559 0.1067 0.1143 -0.0027 -0.0310 -0.0244 28  GLN A CD  
293  O  OE1 . GLN A 28  ? 0.0771 0.1093 0.1203 -0.0115 -0.0027 -0.0183 28  GLN A OE1 
294  N  NE2 . GLN A 28  ? 0.0666 0.0952 0.1364 -0.0062 -0.0120 -0.0193 28  GLN A NE2 
295  N  N   . SER A 29  ? 0.0710 0.0944 0.0890 0.0091  -0.0048 -0.0181 29  SER A N   
296  C  CA  . SER A 29  ? 0.0535 0.0809 0.0917 0.0085  -0.0020 -0.0195 29  SER A CA  
297  C  C   . SER A 29  ? 0.0719 0.0807 0.0687 0.0010  0.0017  -0.0043 29  SER A C   
298  O  O   . SER A 29  ? 0.0604 0.0873 0.1089 -0.0019 0.0043  -0.0093 29  SER A O   
299  C  CB  . SER A 29  ? 0.0750 0.0785 0.0661 0.0104  0.0023  -0.0110 29  SER A CB  
300  O  OG  . SER A 29  ? 0.0772 0.0750 0.0856 0.0115  -0.0027 -0.0173 29  SER A OG  
301  N  N   . PRO A 30  ? 0.0627 0.0777 0.0790 0.0041  0.0052  -0.0132 30  PRO A N   
302  C  CA  . PRO A 30  ? 0.0606 0.0820 0.0688 0.0038  0.0046  -0.0087 30  PRO A CA  
303  C  C   . PRO A 30  ? 0.0811 0.0820 0.0736 0.0159  0.0142  -0.0129 30  PRO A C   
304  O  O   . PRO A 30  ? 0.0864 0.0917 0.0929 0.0140  -0.0035 -0.0077 30  PRO A O   
305  C  CB  . PRO A 30  ? 0.0793 0.0845 0.0680 0.0098  0.0074  -0.0174 30  PRO A CB  
306  C  CG  . PRO A 30  ? 0.0759 0.0854 0.0852 0.0068  0.0071  -0.0156 30  PRO A CG  
307  C  CD  . PRO A 30  ? 0.0820 0.0715 0.0879 0.0003  -0.0013 -0.0326 30  PRO A CD  
308  N  N   . VAL A 31  ? 0.0854 0.0917 0.0763 0.0209  0.0109  -0.0060 31  VAL A N   
309  C  CA  . VAL A 31  ? 0.1021 0.0838 0.0702 -0.0007 -0.0060 -0.0054 31  VAL A CA  
310  C  C   . VAL A 31  ? 0.0988 0.0957 0.0697 0.0160  0.0077  -0.0007 31  VAL A C   
311  O  O   . VAL A 31  ? 0.0996 0.0906 0.0798 0.0054  0.0054  0.0052  31  VAL A O   
312  C  CB  . VAL A 31  ? 0.0938 0.1046 0.0724 0.0038  -0.0057 -0.0126 31  VAL A CB  
313  C  CG1 . VAL A 31  ? 0.1290 0.1066 0.0967 -0.0080 0.0054  -0.0210 31  VAL A CG1 
314  C  CG2 . VAL A 31  ? 0.1017 0.1064 0.1049 0.0093  0.0031  -0.0104 31  VAL A CG2 
315  N  N   . ASP A 32  ? 0.1091 0.0917 0.0683 0.0194  0.0027  0.0096  32  ASP A N   
316  C  CA  . ASP A 32  ? 0.1158 0.0809 0.0678 0.0171  0.0141  0.0099  32  ASP A CA  
317  C  C   . ASP A 32  ? 0.1290 0.0961 0.0662 0.0222  0.0097  0.0030  32  ASP A C   
318  O  O   . ASP A 32  ? 0.1145 0.1317 0.0870 0.0104  0.0000  -0.0142 32  ASP A O   
319  C  CB  . ASP A 32  ? 0.1259 0.0852 0.0978 0.0153  -0.0040 0.0054  32  ASP A CB  
320  C  CG  . ASP A 32  ? 0.1380 0.0942 0.1008 0.0263  0.0131  0.0054  32  ASP A CG  
321  O  OD1 . ASP A 32  ? 0.1298 0.0870 0.1017 0.0110  -0.0046 0.0124  32  ASP A OD1 
322  O  OD2 . ASP A 32  ? 0.1887 0.1233 0.0948 0.0049  0.0034  0.0175  32  ASP A OD2 
323  N  N   . ILE A 33  ? 0.1211 0.0926 0.0803 0.0181  0.0194  0.0151  33  ILE A N   
324  C  CA  . ILE A 33  ? 0.1274 0.0951 0.0737 0.0177  0.0146  0.0193  33  ILE A CA  
325  C  C   . ILE A 33  ? 0.1125 0.1037 0.0794 0.0120  0.0196  0.0182  33  ILE A C   
326  O  O   . ILE A 33  ? 0.1306 0.1116 0.0842 0.0052  0.0220  0.0199  33  ILE A O   
327  C  CB  . ILE A 33  ? 0.1141 0.0929 0.0785 0.0296  0.0237  0.0153  33  ILE A CB  
328  C  CG1 . ILE A 33  ? 0.1246 0.0900 0.0978 0.0062  0.0003  0.0186  33  ILE A CG1 
329  C  CG2 . ILE A 33  ? 0.1283 0.1346 0.1102 0.0445  0.0340  0.0031  33  ILE A CG2 
330  C  CD1 . ILE A 33  ? 0.1222 0.1260 0.1323 0.0274  -0.0017 0.0326  33  ILE A CD1 
331  N  N   A ASP A 34  ? 0.1827 0.0924 0.0555 0.0549  0.0419  0.0331  34  ASP A N   
332  N  N   B ASP A 34  ? 0.1565 0.1477 0.0750 0.0295  0.0074  0.0421  34  ASP A N   
333  C  CA  A ASP A 34  ? 0.1805 0.1249 0.0715 0.0361  0.0351  0.0498  34  ASP A CA  
334  C  CA  B ASP A 34  ? 0.1630 0.1410 0.0815 0.0265  0.0141  0.0326  34  ASP A CA  
335  C  C   A ASP A 34  ? 0.1605 0.1262 0.0552 0.0303  0.0326  0.0366  34  ASP A C   
336  C  C   B ASP A 34  ? 0.1719 0.1444 0.0838 0.0364  0.0288  0.0258  34  ASP A C   
337  O  O   A ASP A 34  ? 0.2098 0.1673 0.0834 0.0617  0.0395  0.0104  34  ASP A O   
338  O  O   B ASP A 34  ? 0.1984 0.1568 0.0872 0.0372  0.0441  0.0226  34  ASP A O   
339  C  CB  A ASP A 34  ? 0.2166 0.1477 0.0511 0.0419  0.0307  0.0286  34  ASP A CB  
340  C  CB  B ASP A 34  ? 0.2122 0.1513 0.1411 0.0261  -0.0333 0.0588  34  ASP A CB  
341  C  CG  A ASP A 34  ? 0.1967 0.1154 0.0956 0.0494  0.0082  0.0172  34  ASP A CG  
342  C  CG  B ASP A 34  ? 0.2102 0.1809 0.1324 -0.0249 -0.0164 0.0373  34  ASP A CG  
343  O  OD1 A ASP A 34  ? 0.1745 0.1258 0.0961 0.0164  -0.0003 0.0362  34  ASP A OD1 
344  O  OD1 B ASP A 34  ? 0.1784 0.1910 0.1330 0.0370  -0.0296 0.0487  34  ASP A OD1 
345  O  OD2 A ASP A 34  ? 0.2687 0.1296 0.0903 0.0601  0.0408  0.0275  34  ASP A OD2 
346  O  OD2 B ASP A 34  ? 0.2642 0.2592 0.1714 -0.0208 -0.0443 0.1181  34  ASP A OD2 
347  N  N   A THR A 35  ? 0.1307 0.1486 0.0674 0.0372  0.0544  0.0471  35  THR A N   
348  N  N   B THR A 35  ? 0.1410 0.1493 0.1163 0.0450  0.0241  0.0531  35  THR A N   
349  C  CA  A THR A 35  ? 0.1571 0.2493 0.0878 0.0834  0.0666  0.0346  35  THR A CA  
350  C  CA  B THR A 35  ? 0.1366 0.1089 0.1215 0.0500  0.0057  0.0683  35  THR A CA  
351  C  C   A THR A 35  ? 0.1360 0.2215 0.0809 0.0662  0.0414  0.0733  35  THR A C   
352  C  C   B THR A 35  ? 0.1872 0.1366 0.1277 0.0869  0.0432  0.0441  35  THR A C   
353  O  O   A THR A 35  ? 0.1802 0.2186 0.1048 0.1001  0.0615  0.0854  35  THR A O   
354  O  O   B THR A 35  ? 0.1912 0.1791 0.1344 0.0957  0.0298  0.0063  35  THR A O   
355  C  CB  A THR A 35  ? 0.1556 0.2044 0.1445 0.0746  0.0296  0.0666  35  THR A CB  
356  C  CB  B THR A 35  ? 0.0979 0.1398 0.1556 0.0324  0.0017  0.0513  35  THR A CB  
357  O  OG1 A THR A 35  ? 0.1773 0.1676 0.1163 0.0535  0.0784  0.0153  35  THR A OG1 
358  O  OG1 B THR A 35  ? 0.1793 0.1448 0.1869 0.0207  0.0511  0.0701  35  THR A OG1 
359  C  CG2 A THR A 35  ? 0.1206 0.2563 0.1428 0.0590  0.0507  0.0679  35  THR A CG2 
360  C  CG2 B THR A 35  ? 0.1799 0.1969 0.1342 0.0153  -0.0296 0.0392  35  THR A CG2 
361  N  N   A HIS A 36  ? 0.1660 0.2019 0.0965 0.0759  0.0522  0.0693  36  HIS A N   
362  N  N   B HIS A 36  ? 0.2089 0.1418 0.0836 0.0819  0.0643  0.0645  36  HIS A N   
363  C  CA  A HIS A 36  ? 0.1527 0.1592 0.0798 0.0474  0.0071  0.0599  36  HIS A CA  
364  C  CA  B HIS A 36  ? 0.2190 0.0982 0.0732 0.0048  0.0621  0.0249  36  HIS A CA  
365  C  C   A HIS A 36  ? 0.1739 0.1919 0.0891 0.0469  0.0344  0.0283  36  HIS A C   
366  C  C   B HIS A 36  ? 0.1825 0.1256 0.1048 0.0164  0.0674  0.0027  36  HIS A C   
367  O  O   A HIS A 36  ? 0.1978 0.1809 0.0922 0.0577  0.0339  0.0280  36  HIS A O   
368  O  O   B HIS A 36  ? 0.2549 0.1552 0.1044 0.0697  0.0621  0.0449  36  HIS A O   
369  C  CB  A HIS A 36  ? 0.2181 0.1362 0.0732 0.0215  -0.0104 0.0392  36  HIS A CB  
370  C  CB  B HIS A 36  ? 0.2213 0.1215 0.0480 0.0140  -0.0059 0.0263  36  HIS A CB  
371  C  CG  A HIS A 36  ? 0.1798 0.1188 0.1032 0.0308  -0.0012 0.0658  36  HIS A CG  
372  C  CG  B HIS A 36  ? 0.1865 0.1080 0.1441 0.0344  -0.0252 0.0348  36  HIS A CG  
373  N  ND1 A HIS A 36  ? 0.2278 0.1513 0.1316 0.0187  0.0264  0.0344  36  HIS A ND1 
374  N  ND1 B HIS A 36  ? 0.2870 0.2610 0.1915 -0.0564 0.0434  -0.0175 36  HIS A ND1 
375  C  CD2 A HIS A 36  ? 0.1795 0.1136 0.1173 0.0381  0.0273  0.0436  36  HIS A CD2 
376  C  CD2 B HIS A 36  ? 0.1868 0.1506 0.1057 0.0068  0.0119  0.0614  36  HIS A CD2 
377  C  CE1 A HIS A 36  ? 0.2030 0.1558 0.1290 0.0384  -0.0588 0.0274  36  HIS A CE1 
378  C  CE1 B HIS A 36  ? 0.2028 0.2289 0.2560 -0.0548 0.0250  0.0038  36  HIS A CE1 
379  N  NE2 A HIS A 36  ? 0.3154 0.1091 0.2071 0.0097  0.0010  0.0307  36  HIS A NE2 
380  N  NE2 B HIS A 36  ? 0.1978 0.1838 0.1768 -0.0057 -0.0237 0.0538  36  HIS A NE2 
381  N  N   A THR A 37  ? 0.2630 0.1054 0.1312 0.0013  0.0812  0.0302  37  THR A N   
382  N  N   B THR A 37  ? 0.2888 0.1071 0.1579 0.0452  0.0427  0.0715  37  THR A N   
383  C  CA  A THR A 37  ? 0.2206 0.1508 0.1588 0.0012  0.0197  0.0297  37  THR A CA  
384  C  CA  B THR A 37  ? 0.2316 0.1448 0.1150 0.0436  0.0922  0.0731  37  THR A CA  
385  C  C   A THR A 37  ? 0.2240 0.1761 0.0938 0.0241  0.0383  0.0326  37  THR A C   
386  C  C   B THR A 37  ? 0.2064 0.1438 0.1506 0.0348  0.0148  0.0383  37  THR A C   
387  O  O   A THR A 37  ? 0.2353 0.1712 0.0859 0.0264  0.0489  0.0308  37  THR A O   
388  O  O   B THR A 37  ? 0.2364 0.1649 0.1525 -0.0219 0.0604  0.0255  37  THR A O   
389  C  CB  A THR A 37  ? 0.1714 0.1981 0.2142 0.0430  -0.1163 0.0148  37  THR A CB  
390  C  CB  B THR A 37  ? 0.2319 0.1901 0.3334 0.1281  -0.0710 -0.0705 37  THR A CB  
391  O  OG1 A THR A 37  ? 0.4160 0.2127 0.1359 0.1164  -0.0447 0.0348  37  THR A OG1 
392  O  OG1 B THR A 37  ? 0.3680 0.2793 0.2434 0.0961  -0.0255 -0.0221 37  THR A OG1 
393  C  CG2 A THR A 37  ? 0.2795 0.1738 0.1874 0.0491  -0.1071 0.0086  37  THR A CG2 
394  C  CG2 B THR A 37  ? 0.3415 0.2511 0.1472 0.0054  0.0303  -0.0469 37  THR A CG2 
395  N  N   . ALA A 38  ? 0.2433 0.1771 0.1012 0.0625  0.0233  0.0296  38  ALA A N   
396  C  CA  . ALA A 38  ? 0.2476 0.1290 0.1215 0.0639  0.0308  0.0310  38  ALA A CA  
397  C  C   . ALA A 38  ? 0.2563 0.1746 0.1811 0.0684  0.0599  0.0480  38  ALA A C   
398  O  O   . ALA A 38  ? 0.3810 0.2254 0.3718 0.0753  0.2026  0.0719  38  ALA A O   
399  C  CB  . ALA A 38  ? 0.2350 0.2060 0.1215 0.0627  0.0185  0.0489  38  ALA A CB  
400  N  N   . LYS A 39  ? 0.2784 0.2354 0.1292 0.0931  0.0118  -0.0187 39  LYS A N   
401  C  CA  . LYS A 39  ? 0.3251 0.3361 0.1610 0.1885  0.0397  -0.0335 39  LYS A CA  
402  C  C   . LYS A 39  ? 0.2160 0.2415 0.1421 0.0441  -0.0031 0.0048  39  LYS A C   
403  O  O   . LYS A 39  ? 0.1766 0.2411 0.1256 0.0447  0.0222  -0.0071 39  LYS A O   
404  C  CB  . LYS A 39  ? 0.3406 0.4954 0.2143 0.2585  -0.0384 -0.1044 39  LYS A CB  
405  C  CG  . LYS A 39  ? 0.3370 0.2885 0.3806 0.1106  -0.0441 0.0597  39  LYS A CG  
406  C  CD  . LYS A 39  ? 0.4422 0.3420 0.2439 0.1331  0.0071  -0.0063 39  LYS A CD  
407  C  CE  . LYS A 39  ? 0.3986 0.4444 0.2996 0.1296  0.0966  0.0966  39  LYS A CE  
408  N  NZ  . LYS A 39  ? 0.3736 0.3628 0.3867 0.1303  0.0198  0.1476  39  LYS A NZ  
409  N  N   . TYR A 40  ? 0.2684 0.2605 0.1396 0.0421  0.0375  0.0377  40  TYR A N   
410  C  CA  . TYR A 40  ? 0.2276 0.2048 0.1666 -0.0189 0.0634  -0.0060 40  TYR A CA  
411  C  C   . TYR A 40  ? 0.1622 0.2120 0.1136 0.0208  0.0280  -0.0027 40  TYR A C   
412  O  O   . TYR A 40  ? 0.2236 0.2896 0.1082 0.0436  0.0456  -0.0003 40  TYR A O   
413  C  CB  . TYR A 40  ? 0.2673 0.3242 0.1899 -0.0626 0.0715  0.0671  40  TYR A CB  
414  C  CG  . TYR A 40  ? 0.2806 0.3156 0.1726 -0.0709 0.0812  0.0113  40  TYR A CG  
415  C  CD1 . TYR A 40  ? 0.2484 0.3158 0.2226 -0.0753 0.0388  0.0309  40  TYR A CD1 
416  C  CD2 . TYR A 40  ? 0.2849 0.4061 0.2396 -0.0471 0.1318  0.0208  40  TYR A CD2 
417  C  CE1 . TYR A 40  ? 0.2684 0.3731 0.1583 -0.0842 0.0465  -0.0241 40  TYR A CE1 
418  C  CE2 . TYR A 40  ? 0.3395 0.4207 0.1608 0.0197  0.0908  0.0091  40  TYR A CE2 
419  C  CZ  . TYR A 40  ? 0.2039 0.5016 0.2057 -0.0120 0.0724  0.0520  40  TYR A CZ  
420  O  OH  . TYR A 40  ? 0.2102 0.6750 0.3113 0.0046  0.0482  -0.0961 40  TYR A OH  
421  N  N   . ASP A 41  ? 0.1635 0.1775 0.1461 0.0054  0.0498  -0.0143 41  ASP A N   
422  C  CA  . ASP A 41  ? 0.1366 0.2102 0.1560 -0.0126 0.0109  -0.0026 41  ASP A CA  
423  C  C   . ASP A 41  ? 0.1639 0.2032 0.1407 0.0197  0.0346  -0.0259 41  ASP A C   
424  O  O   . ASP A 41  ? 0.1605 0.2603 0.1572 0.0271  0.0057  -0.0249 41  ASP A O   
425  C  CB  . ASP A 41  ? 0.2036 0.1877 0.2069 -0.0230 -0.0043 -0.0170 41  ASP A CB  
426  C  CG  . ASP A 41  ? 0.2377 0.2063 0.2806 0.0065  -0.0148 -0.0452 41  ASP A CG  
427  O  OD1 . ASP A 41  ? 0.3310 0.2206 0.2048 0.0331  -0.0304 -0.0359 41  ASP A OD1 
428  O  OD2 . ASP A 41  ? 0.3000 0.2721 0.2208 -0.0417 -0.0406 -0.0324 41  ASP A OD2 
429  N  N   . PRO A 42  ? 0.1860 0.3231 0.1606 0.0335  0.0546  -0.0167 42  PRO A N   
430  C  CA  . PRO A 42  ? 0.1942 0.3206 0.2429 0.0719  0.0912  0.0205  42  PRO A CA  
431  C  C   . PRO A 42  ? 0.2055 0.2935 0.2283 0.0869  0.0876  0.0086  42  PRO A C   
432  O  O   . PRO A 42  ? 0.2617 0.4399 0.3370 0.1544  0.0154  -0.0283 42  PRO A O   
433  C  CB  . PRO A 42  ? 0.2136 0.4514 0.2436 0.0286  0.1098  -0.0461 42  PRO A CB  
434  C  CG  . PRO A 42  ? 0.2357 0.4526 0.2150 0.1351  0.0759  0.0098  42  PRO A CG  
435  C  CD  . PRO A 42  ? 0.2382 0.3447 0.1585 0.0304  0.0882  -0.0114 42  PRO A CD  
436  N  N   . SER A 43  ? 0.2752 0.2944 0.2213 0.0586  0.0527  -0.0593 43  SER A N   
437  C  CA  . SER A 43  ? 0.4146 0.2307 0.2368 0.0882  -0.0120 -0.0895 43  SER A CA  
438  C  C   . SER A 43  ? 0.2734 0.2702 0.2924 0.0644  0.0436  -0.0308 43  SER A C   
439  O  O   . SER A 43  ? 0.4627 0.2601 0.3424 0.1045  0.0511  -0.0082 43  SER A O   
440  C  CB  . SER A 43  ? 0.3939 0.2980 0.3402 0.0900  -0.0214 -0.1474 43  SER A CB  
441  O  OG  . SER A 43  ? 0.4232 0.2969 0.3217 0.0373  -0.0277 -0.1507 43  SER A OG  
442  N  N   . LEU A 44  ? 0.2980 0.2861 0.2055 0.0926  0.0331  -0.0104 44  LEU A N   
443  C  CA  . LEU A 44  ? 0.2257 0.3574 0.1912 0.0855  -0.0386 0.0000  44  LEU A CA  
444  C  C   . LEU A 44  ? 0.1845 0.3319 0.2321 0.0366  -0.0013 0.0384  44  LEU A C   
445  O  O   . LEU A 44  ? 0.2236 0.4769 0.3185 -0.0441 0.0065  0.0843  44  LEU A O   
446  C  CB  . LEU A 44  ? 0.1570 0.2960 0.1921 -0.0251 0.0205  -0.0063 44  LEU A CB  
447  C  CG  . LEU A 44  ? 0.1473 0.2678 0.1687 -0.0430 0.0057  -0.0031 44  LEU A CG  
448  C  CD1 . LEU A 44  ? 0.2138 0.2727 0.1342 -0.0513 0.0568  -0.0175 44  LEU A CD1 
449  C  CD2 . LEU A 44  ? 0.2272 0.1972 0.1691 -0.0219 -0.0291 0.0126  44  LEU A CD2 
450  N  N   A LYS A 45  ? 0.2325 0.4099 0.3350 0.0505  -0.0346 0.1133  45  LYS A N   
451  N  N   B LYS A 45  ? 0.1568 0.1711 0.2366 0.0263  0.0579  -0.0401 45  LYS A N   
452  C  CA  A LYS A 45  ? 0.1262 0.2585 0.2041 0.0377  0.0635  -0.0340 45  LYS A CA  
453  C  CA  B LYS A 45  ? 0.2470 0.1359 0.3684 0.0166  -0.0784 -0.0689 45  LYS A CA  
454  C  C   A LYS A 45  ? 0.1744 0.2712 0.1791 0.1080  -0.0017 -0.0307 45  LYS A C   
455  C  C   B LYS A 45  ? 0.1289 0.2912 0.2048 0.0549  0.0417  -0.0307 45  LYS A C   
456  O  O   A LYS A 45  ? 0.1797 0.1120 0.2833 0.0310  0.0608  0.0272  45  LYS A O   
457  O  O   B LYS A 45  ? 0.0960 0.3488 0.2813 0.0328  0.0538  -0.1626 45  LYS A O   
458  C  CB  A LYS A 45  ? 0.2653 0.2779 0.3203 0.1261  0.1507  -0.0054 45  LYS A CB  
459  C  CB  B LYS A 45  ? 0.1529 0.1734 0.2044 0.0732  0.0304  -0.0590 45  LYS A CB  
460  C  CG  A LYS A 45  ? 0.1933 0.2407 0.3831 0.1115  0.0057  -0.0597 45  LYS A CG  
461  C  CG  B LYS A 45  ? 0.2043 0.3176 0.2336 0.0529  0.0395  -0.1216 45  LYS A CG  
462  C  CD  A LYS A 45  ? 0.2660 0.2635 0.4957 0.0671  0.0456  -0.0265 45  LYS A CD  
463  C  CD  B LYS A 45  ? 0.2612 0.3174 0.4194 0.0344  0.0644  -0.0608 45  LYS A CD  
464  C  CE  A LYS A 45  ? 0.5490 0.3361 0.4483 0.0216  0.0293  0.0000  45  LYS A CE  
465  C  CE  B LYS A 45  ? 0.4119 0.3752 0.5856 0.0917  0.1124  -0.1499 45  LYS A CE  
466  N  NZ  A LYS A 45  ? 0.8269 0.2350 0.4783 0.0841  -0.1893 -0.1080 45  LYS A NZ  
467  N  NZ  B LYS A 45  ? 0.3061 0.5616 0.6923 0.1508  0.2317  -0.0732 45  LYS A NZ  
468  N  N   A PRO A 46  ? 0.0832 0.3258 0.3079 -0.0794 0.0644  -0.0549 46  PRO A N   
469  N  N   B PRO A 46  ? 0.1389 0.2158 0.1869 0.0653  0.0315  -0.0148 46  PRO A N   
470  C  CA  A PRO A 46  ? 0.1908 0.2861 0.2809 -0.0509 0.0035  0.0118  46  PRO A CA  
471  C  CA  B PRO A 46  ? 0.0958 0.1905 0.1888 0.0252  0.0208  0.0043  46  PRO A CA  
472  C  C   A PRO A 46  ? 0.1378 0.3176 0.2603 -0.0259 0.0518  -0.0035 46  PRO A C   
473  C  C   B PRO A 46  ? 0.1114 0.1509 0.1806 0.0328  0.0639  -0.0203 46  PRO A C   
474  O  O   A PRO A 46  ? 0.0974 0.3395 0.1726 0.0232  0.0364  0.0489  46  PRO A O   
475  O  O   B PRO A 46  ? 0.0788 0.1610 0.1840 0.0118  0.0274  -0.0253 46  PRO A O   
476  C  CB  A PRO A 46  ? 0.1700 0.2906 0.3285 -0.0461 0.0291  0.0283  46  PRO A CB  
477  C  CB  B PRO A 46  ? 0.0979 0.1932 0.2068 0.0247  0.0206  -0.0306 46  PRO A CB  
478  C  CG  A PRO A 46  ? 0.1251 0.3643 0.3097 0.0745  -0.0062 -0.1106 46  PRO A CG  
479  C  CG  B PRO A 46  ? 0.0657 0.2829 0.2285 0.0571  0.0337  -0.0326 46  PRO A CG  
480  C  CD  A PRO A 46  ? 0.1238 0.2485 0.3294 0.0204  0.0603  -0.1409 46  PRO A CD  
481  C  CD  B PRO A 46  ? 0.1039 0.2874 0.2412 0.0355  0.0483  -0.0346 46  PRO A CD  
482  N  N   A LEU A 47  ? 0.1368 0.2808 0.2894 -0.0359 0.0408  -0.0063 47  LEU A N   
483  N  N   B LEU A 47  ? 0.1332 0.1380 0.1491 0.0377  0.0087  -0.0476 47  LEU A N   
484  C  CA  A LEU A 47  ? 0.1886 0.2091 0.2389 -0.0474 -0.0043 0.0562  47  LEU A CA  
485  C  CA  B LEU A 47  ? 0.1109 0.1653 0.1787 0.0318  0.0344  -0.0535 47  LEU A CA  
486  C  C   A LEU A 47  ? 0.1500 0.1956 0.2951 -0.0322 0.0285  0.0693  47  LEU A C   
487  C  C   B LEU A 47  ? 0.0406 0.1773 0.2141 -0.0153 0.0306  -0.0087 47  LEU A C   
488  O  O   A LEU A 47  ? 0.1486 0.2741 0.2583 -0.0346 0.0091  0.0412  47  LEU A O   
489  O  O   B LEU A 47  ? 0.0861 0.1574 0.1890 -0.0187 -0.0010 -0.0013 47  LEU A O   
490  C  CB  A LEU A 47  ? 0.1407 0.1917 0.4388 -0.0983 -0.0114 -0.0027 47  LEU A CB  
491  C  CB  B LEU A 47  ? 0.1283 0.2236 0.1513 0.1022  0.0331  -0.0151 47  LEU A CB  
492  C  CG  A LEU A 47  ? 0.1488 0.3357 0.3894 -0.0974 0.0120  0.0108  47  LEU A CG  
493  C  CG  B LEU A 47  ? 0.1283 0.2014 0.1935 -0.0284 0.0211  -0.0597 47  LEU A CG  
494  C  CD1 A LEU A 47  ? 0.1870 0.2928 0.3077 -0.1569 -0.0951 0.0263  47  LEU A CD1 
495  C  CD1 B LEU A 47  ? 0.1093 0.2791 0.1780 -0.0527 -0.0164 -0.0109 47  LEU A CD1 
496  C  CD2 A LEU A 47  ? 0.1084 0.2858 0.2170 -0.0732 -0.0745 -0.0370 47  LEU A CD2 
497  C  CD2 B LEU A 47  ? 0.0992 0.2497 0.1791 0.0527  0.0597  -0.0026 47  LEU A CD2 
498  N  N   . SER A 48  ? 0.1228 0.1924 0.2213 -0.0291 0.0174  0.0377  48  SER A N   
499  C  CA  . SER A 48  ? 0.1106 0.1835 0.2256 -0.0196 0.0200  0.0303  48  SER A CA  
500  C  C   . SER A 48  ? 0.0895 0.1978 0.2028 -0.0207 -0.0153 0.0104  48  SER A C   
501  O  O   . SER A 48  ? 0.1100 0.1859 0.2102 -0.0386 -0.0099 -0.0088 48  SER A O   
502  C  CB  . SER A 48  ? 0.1362 0.2314 0.2303 -0.0073 -0.0141 0.0051  48  SER A CB  
503  O  OG  . SER A 48  ? 0.1565 0.2809 0.2951 0.0286  -0.0031 0.0370  48  SER A OG  
504  N  N   . VAL A 49  ? 0.1281 0.1999 0.2569 -0.0754 -0.0115 -0.0068 49  VAL A N   
505  C  CA  . VAL A 49  ? 0.1708 0.2303 0.2606 -0.0520 0.0081  -0.0216 49  VAL A CA  
506  C  C   . VAL A 49  ? 0.1867 0.2518 0.2502 -0.0904 -0.0120 -0.0082 49  VAL A C   
507  O  O   . VAL A 49  ? 0.2466 0.3826 0.2651 -0.1809 -0.0500 -0.0006 49  VAL A O   
508  C  CB  . VAL A 49  ? 0.1908 0.2694 0.3136 -0.0898 0.0406  -0.0662 49  VAL A CB  
509  C  CG1 . VAL A 49  ? 0.3136 0.2655 0.3289 -0.1168 0.1079  -0.0619 49  VAL A CG1 
510  C  CG2 . VAL A 49  ? 0.2080 0.2314 0.3379 -0.0381 0.0586  -0.0491 49  VAL A CG2 
511  N  N   . SER A 50  ? 0.1682 0.2481 0.2424 -0.0750 -0.0186 -0.0189 50  SER A N   
512  C  CA  . SER A 50  ? 0.1965 0.2906 0.3122 -0.0472 -0.0421 -0.0317 50  SER A CA  
513  C  C   . SER A 50  ? 0.1269 0.2687 0.2869 -0.0203 -0.0772 -0.0218 50  SER A C   
514  O  O   . SER A 50  ? 0.1527 0.2483 0.2903 -0.0260 -0.0693 0.0059  50  SER A O   
515  C  CB  . SER A 50  ? 0.3030 0.2957 0.3528 -0.0617 0.0281  -0.0361 50  SER A CB  
516  O  OG  . SER A 50  ? 0.3501 0.4104 0.4314 0.0153  -0.0167 -0.0768 50  SER A OG  
517  N  N   . TYR A 51  ? 0.1396 0.2413 0.2861 -0.0386 -0.0697 -0.0143 51  TYR A N   
518  C  CA  . TYR A 51  ? 0.2082 0.2520 0.2648 -0.0082 -0.0762 0.0209  51  TYR A CA  
519  C  C   . TYR A 51  ? 0.2224 0.2228 0.3014 -0.0147 -0.0754 0.0518  51  TYR A C   
520  O  O   . TYR A 51  ? 0.2560 0.2526 0.2657 -0.0221 -0.1254 0.0151  51  TYR A O   
521  C  CB  . TYR A 51  ? 0.1629 0.2675 0.2364 -0.0161 -0.0674 0.0057  51  TYR A CB  
522  C  CG  . TYR A 51  ? 0.1606 0.2161 0.1727 -0.0496 -0.0461 0.0164  51  TYR A CG  
523  C  CD1 . TYR A 51  ? 0.1459 0.1543 0.2459 -0.0121 -0.0399 0.0068  51  TYR A CD1 
524  C  CD2 . TYR A 51  ? 0.1540 0.1849 0.1741 -0.0439 -0.0284 -0.0074 51  TYR A CD2 
525  C  CE1 . TYR A 51  ? 0.1474 0.1905 0.1903 -0.0315 -0.0505 -0.0017 51  TYR A CE1 
526  C  CE2 . TYR A 51  ? 0.1562 0.1904 0.1746 -0.0531 -0.0315 -0.0040 51  TYR A CE2 
527  C  CZ  . TYR A 51  ? 0.1220 0.1678 0.2221 -0.0619 -0.0276 0.0031  51  TYR A CZ  
528  O  OH  . TYR A 51  ? 0.1247 0.1551 0.2254 -0.0379 -0.0306 -0.0239 51  TYR A OH  
529  N  N   A ASP A 52  ? 0.2039 0.2597 0.3837 -0.0421 -0.0785 0.0019  52  ASP A N   
530  N  N   B ASP A 52  ? 0.2066 0.3454 0.3086 -0.0285 -0.0922 0.0878  52  ASP A N   
531  C  CA  A ASP A 52  ? 0.2169 0.2788 0.3373 0.0700  -0.0243 0.0494  52  ASP A CA  
532  C  CA  B ASP A 52  ? 0.3088 0.4336 0.2829 0.0469  -0.1032 0.1155  52  ASP A CA  
533  C  C   A ASP A 52  ? 0.1712 0.2757 0.3061 0.0153  -0.0273 0.0146  52  ASP A C   
534  C  C   B ASP A 52  ? 0.3461 0.3300 0.3257 -0.0526 -0.1624 0.0772  52  ASP A C   
535  O  O   A ASP A 52  ? 0.1603 0.2181 0.3188 0.0608  -0.0458 -0.0071 52  ASP A O   
536  O  O   B ASP A 52  ? 0.1809 0.3472 0.3086 0.1180  0.0307  0.1010  52  ASP A O   
537  C  CB  A ASP A 52  ? 0.0976 0.3397 0.4377 0.0370  -0.0829 0.0421  52  ASP A CB  
538  C  CB  B ASP A 52  ? 0.3152 0.3337 0.4264 0.0258  -0.0662 0.0476  52  ASP A CB  
539  C  CG  A ASP A 52  ? 0.1323 0.4336 0.4813 0.0137  -0.0199 -0.0178 52  ASP A CG  
540  C  CG  B ASP A 52  ? 0.2441 0.3018 0.5303 0.0335  -0.0313 0.0754  52  ASP A CG  
541  O  OD1 A ASP A 52  ? 0.2572 0.6593 0.5680 -0.0231 -0.1085 0.0197  52  ASP A OD1 
542  O  OD1 B ASP A 52  ? 0.2372 0.3716 0.4867 0.0966  -0.1342 0.0741  52  ASP A OD1 
543  O  OD2 A ASP A 52  ? 0.4174 0.4406 0.4954 0.0142  -0.0293 0.0439  52  ASP A OD2 
544  O  OD2 B ASP A 52  ? 0.4088 0.4095 0.3601 0.1247  0.0375  0.1686  52  ASP A OD2 
545  N  N   . GLN A 53  ? 0.2021 0.3037 0.4212 0.0052  -0.0802 0.0430  53  GLN A N   
546  C  CA  . GLN A 53  ? 0.3041 0.3246 0.4810 -0.0582 -0.0231 0.0533  53  GLN A CA  
547  C  C   . GLN A 53  ? 0.3095 0.2469 0.2370 0.0342  -0.0789 0.0337  53  GLN A C   
548  O  O   . GLN A 53  ? 0.3555 0.2648 0.3000 0.0331  -0.0913 0.0467  53  GLN A O   
549  C  CB  . GLN A 53  ? 0.4541 0.4146 0.5799 0.0373  -0.2057 -0.0631 53  GLN A CB  
550  C  CG  . GLN A 53  ? 0.4433 0.5098 0.4765 -0.0051 -0.1775 0.1243  53  GLN A CG  
551  C  CD  . GLN A 53  ? 0.5399 0.7774 0.4857 -0.1250 -0.1837 0.1676  53  GLN A CD  
552  O  OE1 . GLN A 53  ? 0.3533 0.6686 0.6560 0.0359  -0.1133 0.2788  53  GLN A OE1 
553  N  NE2 . GLN A 53  ? 0.3734 0.5691 0.9110 0.0617  -0.0170 0.3140  53  GLN A NE2 
554  N  N   . ALA A 54  ? 0.3102 0.1703 0.2754 -0.0474 -0.0746 0.0353  54  ALA A N   
555  C  CA  . ALA A 54  ? 0.2718 0.1744 0.2263 -0.0154 -0.1062 -0.0093 54  ALA A CA  
556  C  C   . ALA A 54  ? 0.3106 0.2678 0.1917 -0.0292 -0.1076 -0.0071 54  ALA A C   
557  O  O   . ALA A 54  ? 0.3560 0.3037 0.2290 -0.0763 -0.1318 -0.0183 54  ALA A O   
558  C  CB  . ALA A 54  ? 0.3021 0.1802 0.2939 -0.0010 -0.0489 0.0114  54  ALA A CB  
559  N  N   A THR A 55  ? 0.2380 0.1190 0.1808 0.0432  -0.0785 0.0063  55  THR A N   
560  N  N   B THR A 55  ? 0.3079 0.1714 0.1687 0.0357  -0.0820 0.0489  55  THR A N   
561  C  CA  A THR A 55  ? 0.1820 0.1938 0.1606 0.0793  -0.0794 0.0348  55  THR A CA  
562  C  CA  B THR A 55  ? 0.1656 0.1553 0.1920 0.0408  -0.0702 0.0507  55  THR A CA  
563  C  C   A THR A 55  ? 0.1579 0.1256 0.0750 0.0340  -0.0006 0.0218  55  THR A C   
564  C  C   B THR A 55  ? 0.1472 0.1170 0.1538 0.0000  -0.0491 0.0856  55  THR A C   
565  O  O   A THR A 55  ? 0.2071 0.0992 0.1875 0.0183  -0.0564 0.0441  55  THR A O   
566  O  O   B THR A 55  ? 0.1646 0.1296 0.1330 -0.0070 -0.0392 0.0441  55  THR A O   
567  C  CB  A THR A 55  ? 0.2011 0.1827 0.1585 0.0777  -0.0860 0.0287  55  THR A CB  
568  C  CB  B THR A 55  ? 0.1926 0.1638 0.2093 0.0309  -0.0474 0.0634  55  THR A CB  
569  O  OG1 A THR A 55  ? 0.2490 0.2168 0.3434 0.0913  -0.0635 0.0375  55  THR A OG1 
570  O  OG1 B THR A 55  ? 0.2309 0.1238 0.2276 0.0538  -0.0304 -0.0099 55  THR A OG1 
571  C  CG2 A THR A 55  ? 0.1982 0.2583 0.1717 0.1375  -0.0559 0.0472  55  THR A CG2 
572  C  CG2 B THR A 55  ? 0.2222 0.1055 0.1953 0.0239  -0.0935 0.0520  55  THR A CG2 
573  N  N   A SER A 56  ? 0.1097 0.1181 0.0996 0.0208  -0.0153 0.0344  56  SER A N   
574  N  N   B SER A 56  ? 0.0829 0.1568 0.1155 -0.0333 -0.0063 0.0434  56  SER A N   
575  C  CA  A SER A 56  ? 0.1168 0.1312 0.1054 0.0060  0.0007  0.0153  56  SER A CA  
576  C  CA  B SER A 56  ? 0.1177 0.1389 0.0967 -0.0087 -0.0166 0.0390  56  SER A CA  
577  C  C   A SER A 56  ? 0.1322 0.1699 0.1120 0.0120  -0.0148 0.0359  56  SER A C   
578  C  C   B SER A 56  ? 0.1349 0.1080 0.0942 0.0046  -0.0203 0.0476  56  SER A C   
579  O  O   A SER A 56  ? 0.1181 0.1601 0.1317 0.0119  -0.0143 0.0439  56  SER A O   
580  O  O   B SER A 56  ? 0.1228 0.1428 0.1233 -0.0104 -0.0401 0.0688  56  SER A O   
581  C  CB  A SER A 56  ? 0.1315 0.1249 0.1026 -0.0137 -0.0183 0.0154  56  SER A CB  
582  C  CB  B SER A 56  ? 0.1231 0.1378 0.0818 -0.0088 -0.0182 0.0092  56  SER A CB  
583  O  OG  A SER A 56  ? 0.1143 0.1553 0.1441 -0.0281 -0.0524 0.0436  56  SER A OG  
584  O  OG  B SER A 56  ? 0.1134 0.1409 0.1233 -0.0186 -0.0423 0.0131  56  SER A OG  
585  N  N   A LEU A 57  ? 0.1206 0.1276 0.1128 0.0081  -0.0041 0.0274  57  LEU A N   
586  N  N   B LEU A 57  ? 0.1484 0.1172 0.1168 0.0041  0.0109  0.0129  57  LEU A N   
587  C  CA  A LEU A 57  ? 0.1105 0.1373 0.1301 0.0043  -0.0107 0.0436  57  LEU A CA  
588  C  CA  B LEU A 57  ? 0.1396 0.1256 0.0807 0.0088  -0.0216 0.0208  57  LEU A CA  
589  C  C   A LEU A 57  ? 0.1247 0.1276 0.0967 0.0038  -0.0199 0.0340  57  LEU A C   
590  C  C   B LEU A 57  ? 0.1497 0.0679 0.1217 -0.0125 0.0082  0.0397  57  LEU A C   
591  O  O   A LEU A 57  ? 0.0957 0.1362 0.0899 0.0333  -0.0027 0.0294  57  LEU A O   
592  O  O   B LEU A 57  ? 0.1116 0.1120 0.1118 0.0153  0.0020  0.0335  57  LEU A O   
593  C  CB  A LEU A 57  ? 0.1592 0.1371 0.1474 0.0003  -0.0013 0.0298  57  LEU A CB  
594  C  CB  B LEU A 57  ? 0.1495 0.1003 0.1524 0.0248  0.0155  0.0040  57  LEU A CB  
595  C  CG  A LEU A 57  ? 0.1434 0.1125 0.2005 0.0175  -0.0430 0.0148  57  LEU A CG  
596  C  CG  B LEU A 57  ? 0.1721 0.0816 0.2777 0.0471  0.0030  -0.0107 57  LEU A CG  
597  C  CD1 A LEU A 57  ? 0.1754 0.1213 0.2382 -0.0419 -0.0023 0.0264  57  LEU A CD1 
598  C  CD1 B LEU A 57  ? 0.2035 0.0891 0.3571 -0.0065 0.0697  -0.0432 57  LEU A CD1 
599  C  CD2 A LEU A 57  ? 0.2301 0.1389 0.1623 0.0153  -0.0427 0.0593  57  LEU A CD2 
600  C  CD2 B LEU A 57  ? 0.2942 0.1326 0.3603 0.0948  -0.0383 0.0329  57  LEU A CD2 
601  N  N   A ARG A 58  ? 0.0900 0.1023 0.1362 -0.0063 -0.0076 0.0412  58  ARG A N   
602  N  N   B ARG A 58  ? 0.1288 0.1088 0.1164 -0.0006 0.0166  0.0401  58  ARG A N   
603  C  CA  A ARG A 58  ? 0.1125 0.1048 0.1106 0.0000  -0.0065 0.0381  58  ARG A CA  
604  C  CA  B ARG A 58  ? 0.1290 0.1172 0.1216 0.0000  0.0120  0.0249  58  ARG A CA  
605  C  C   A ARG A 58  ? 0.0895 0.1027 0.0781 -0.0120 0.0104  0.0288  58  ARG A C   
606  C  C   B ARG A 58  ? 0.1303 0.1274 0.0847 0.0104  0.0322  0.0165  58  ARG A C   
607  O  O   A ARG A 58  ? 0.1179 0.1276 0.0781 -0.0126 -0.0046 0.0109  58  ARG A O   
608  O  O   B ARG A 58  ? 0.1811 0.1301 0.0818 0.0261  0.0124  0.0218  58  ARG A O   
609  C  CB  A ARG A 58  ? 0.0985 0.1271 0.1173 0.0070  -0.0073 0.0348  58  ARG A CB  
610  C  CB  B ARG A 58  ? 0.1224 0.1075 0.1965 0.0091  0.0463  -0.0006 58  ARG A CB  
611  C  CG  A ARG A 58  ? 0.1513 0.1310 0.1185 -0.0183 0.0285  0.0362  58  ARG A CG  
612  C  CG  B ARG A 58  ? 0.1867 0.0969 0.2430 0.0043  0.0727  0.0041  58  ARG A CG  
613  C  CD  A ARG A 58  ? 0.1973 0.1197 0.1134 -0.0414 0.0096  0.0416  58  ARG A CD  
614  C  CD  B ARG A 58  ? 0.1637 0.1340 0.2163 -0.0263 0.0471  -0.0063 58  ARG A CD  
615  N  NE  A ARG A 58  ? 0.0942 0.1509 0.1673 0.0074  -0.0003 0.0379  58  ARG A NE  
616  N  NE  B ARG A 58  ? 0.1639 0.1660 0.2321 0.0059  0.0175  -0.0076 58  ARG A NE  
617  C  CZ  A ARG A 58  ? 0.1111 0.2951 0.1133 -0.0829 -0.0135 0.1063  58  ARG A CZ  
618  C  CZ  B ARG A 58  ? 0.1824 0.1500 0.2174 -0.0082 0.0351  0.0445  58  ARG A CZ  
619  N  NH1 A ARG A 58  ? 0.1964 0.1127 0.1315 -0.0269 0.0688  0.0228  58  ARG A NH1 
620  N  NH1 B ARG A 58  ? 0.1976 0.1534 0.3082 0.0114  0.0068  0.0434  58  ARG A NH1 
621  N  NH2 A ARG A 58  ? 0.1278 0.1414 0.1120 -0.0364 -0.0093 0.0476  58  ARG A NH2 
622  N  NH2 B ARG A 58  ? 0.1967 0.1746 0.1926 0.0003  0.0584  0.0447  58  ARG A NH2 
623  N  N   A ILE A 59  ? 0.0921 0.0949 0.0960 -0.0010 -0.0027 0.0186  59  ILE A N   
624  N  N   B ILE A 59  ? 0.1559 0.0944 0.0595 0.0115  0.0156  0.0265  59  ILE A N   
625  C  CA  A ILE A 59  ? 0.0653 0.1032 0.1071 0.0000  0.0034  0.0221  59  ILE A CA  
626  C  CA  B ILE A 59  ? 0.1310 0.1116 0.0674 0.0052  -0.0126 0.0281  59  ILE A CA  
627  C  C   A ILE A 59  ? 0.0790 0.0861 0.0811 -0.0026 0.0176  0.0043  59  ILE A C   
628  C  C   B ILE A 59  ? 0.1491 0.1154 0.0870 -0.0020 0.0015  0.0091  59  ILE A C   
629  O  O   A ILE A 59  ? 0.0649 0.1723 0.0775 0.0068  0.0031  0.0241  59  ILE A O   
630  O  O   B ILE A 59  ? 0.1313 0.1335 0.0722 0.0000  -0.0099 0.0115  59  ILE A O   
631  C  CB  A ILE A 59  ? 0.0648 0.1158 0.0815 -0.0178 -0.0043 0.0196  59  ILE A CB  
632  C  CB  B ILE A 59  ? 0.1373 0.1111 0.0504 -0.0031 -0.0063 0.0322  59  ILE A CB  
633  C  CG1 A ILE A 59  ? 0.1190 0.0882 0.1018 -0.0141 0.0088  0.0175  59  ILE A CG1 
634  C  CG1 B ILE A 59  ? 0.1405 0.0996 0.0815 -0.0034 -0.0264 0.0199  59  ILE A CG1 
635  C  CG2 A ILE A 59  ? 0.1297 0.1036 0.0852 -0.0207 -0.0285 0.0322  59  ILE A CG2 
636  C  CG2 B ILE A 59  ? 0.1179 0.1475 0.0626 -0.0110 -0.0043 0.0230  59  ILE A CG2 
637  C  CD1 A ILE A 59  ? 0.1124 0.1317 0.1145 -0.0485 -0.0057 -0.0087 59  ILE A CD1 
638  C  CD1 B ILE A 59  ? 0.1870 0.1003 0.1055 -0.0142 -0.0573 0.0170  59  ILE A CD1 
639  N  N   A LEU A 60  ? 0.0705 0.1281 0.1075 -0.0118 0.0038  -0.0059 60  LEU A N   
640  N  N   B LEU A 60  ? 0.1565 0.1263 0.0573 0.0026  0.0077  0.0104  60  LEU A N   
641  C  CA  A LEU A 60  ? 0.0724 0.1179 0.0546 0.0143  0.0231  0.0163  60  LEU A CA  
642  C  CA  B LEU A 60  ? 0.1601 0.1046 0.0597 -0.0173 0.0124  0.0219  60  LEU A CA  
643  C  C   A LEU A 60  ? 0.0956 0.0845 0.0872 -0.0052 0.0417  0.0296  60  LEU A C   
644  C  C   B LEU A 60  ? 0.1447 0.0861 0.0612 -0.0173 0.0130  -0.0020 60  LEU A C   
645  O  O   A LEU A 60  ? 0.0790 0.1202 0.0683 -0.0152 0.0110  0.0236  60  LEU A O   
646  O  O   B LEU A 60  ? 0.1380 0.1414 0.0596 -0.0125 0.0068  0.0186  60  LEU A O   
647  C  CB  A LEU A 60  ? 0.0820 0.1518 0.0815 0.0074  0.0087  -0.0074 60  LEU A CB  
648  C  CB  B LEU A 60  ? 0.2039 0.1378 0.1373 -0.0509 0.0000  -0.0057 60  LEU A CB  
649  C  CG  A LEU A 60  ? 0.0754 0.0992 0.1161 0.0076  0.0142  -0.0031 60  LEU A CG  
650  C  CG  B LEU A 60  ? 0.2258 0.1039 0.1064 -0.0339 -0.0057 0.0041  60  LEU A CG  
651  C  CD1 A LEU A 60  ? 0.0811 0.1583 0.1215 0.0260  0.0261  0.0131  60  LEU A CD1 
652  C  CD1 B LEU A 60  ? 0.2366 0.1045 0.1335 -0.0432 0.0285  0.0250  60  LEU A CD1 
653  C  CD2 A LEU A 60  ? 0.0636 0.1268 0.1827 -0.0171 -0.0003 -0.0263 60  LEU A CD2 
654  C  CD2 B LEU A 60  ? 0.2644 0.0872 0.1553 -0.0333 0.0097  -0.0093 60  LEU A CD2 
655  N  N   A ASN A 61  ? 0.0702 0.0935 0.0906 -0.0063 0.0226  0.0159  61  ASN A N   
656  N  N   B ASN A 61  ? 0.1554 0.1170 0.0609 -0.0035 0.0077  -0.0296 61  ASN A N   
657  C  CA  A ASN A 61  ? 0.0784 0.1136 0.1040 0.0148  0.0171  -0.0043 61  ASN A CA  
658  C  CA  B ASN A 61  ? 0.1394 0.0851 0.0456 -0.0346 0.0217  0.0076  61  ASN A CA  
659  C  C   A ASN A 61  ? 0.0929 0.1242 0.0838 -0.0031 0.0355  -0.0104 61  ASN A C   
660  C  C   B ASN A 61  ? 0.1558 0.0894 0.0888 -0.0436 0.0099  0.0175  61  ASN A C   
661  O  O   A ASN A 61  ? 0.0790 0.0931 0.1190 -0.0076 0.0146  0.0137  61  ASN A O   
662  O  O   B ASN A 61  ? 0.1386 0.0820 0.0908 -0.0292 0.0178  0.0131  61  ASN A O   
663  C  CB  A ASN A 61  ? 0.1044 0.1242 0.0732 0.0315  0.0104  0.0109  61  ASN A CB  
664  C  CB  B ASN A 61  ? 0.1412 0.1115 0.0710 0.0015  0.0165  -0.0110 61  ASN A CB  
665  C  CG  A ASN A 61  ? 0.1163 0.1057 0.0697 0.0247  0.0074  0.0024  61  ASN A CG  
666  C  CG  B ASN A 61  ? 0.1592 0.0606 0.0582 -0.0118 0.0177  0.0043  61  ASN A CG  
667  O  OD1 A ASN A 61  ? 0.1362 0.1041 0.0872 0.0329  -0.0031 0.0126  61  ASN A OD1 
668  O  OD1 B ASN A 61  ? 0.1523 0.0781 0.0772 -0.0040 0.0096  0.0082  61  ASN A OD1 
669  N  ND2 A ASN A 61  ? 0.1418 0.0838 0.1230 -0.0097 0.0288  0.0057  61  ASN A ND2 
670  N  ND2 B ASN A 61  ? 0.1626 0.0671 0.0701 -0.0307 0.0175  -0.0051 61  ASN A ND2 
671  N  N   A ASN A 62  ? 0.0697 0.0882 0.0872 -0.0038 0.0182  0.0020  62  ASN A N   
672  N  N   B ASN A 62  ? 0.1145 0.0926 0.0836 -0.0386 0.0035  -0.0098 62  ASN A N   
673  C  CA  A ASN A 62  ? 0.0755 0.1115 0.0815 -0.0155 0.0012  0.0274  62  ASN A CA  
674  C  CA  B ASN A 62  ? 0.1453 0.1009 0.1062 -0.0491 -0.0175 -0.0183 62  ASN A CA  
675  C  C   A ASN A 62  ? 0.0838 0.1088 0.0920 0.0062  0.0452  0.0167  62  ASN A C   
676  C  C   B ASN A 62  ? 0.1549 0.1123 0.0969 -0.0458 0.0262  -0.0003 62  ASN A C   
677  O  O   A ASN A 62  ? 0.1376 0.1626 0.1242 -0.0052 0.0076  0.0210  62  ASN A O   
678  O  O   B ASN A 62  ? 0.1969 0.1173 0.1237 -0.0581 -0.0010 -0.0015 62  ASN A O   
679  C  CB  A ASN A 62  ? 0.1023 0.1048 0.1400 -0.0142 0.0283  0.0000  62  ASN A CB  
680  C  CB  B ASN A 62  ? 0.1877 0.1238 0.1615 -0.0555 0.0041  -0.0496 62  ASN A CB  
681  C  CG  A ASN A 62  ? 0.1238 0.1048 0.1213 -0.0318 -0.0006 -0.0020 62  ASN A CG  
682  C  CG  B ASN A 62  ? 0.2246 0.1802 0.0851 -0.0192 -0.0370 -0.0357 62  ASN A CG  
683  O  OD1 A ASN A 62  ? 0.1330 0.0997 0.1299 -0.0152 0.0275  -0.0063 62  ASN A OD1 
684  O  OD1 B ASN A 62  ? 0.1957 0.1475 0.1224 -0.0447 0.0377  -0.0130 62  ASN A OD1 
685  N  ND2 A ASN A 62  ? 0.1272 0.1814 0.0671 -0.0250 -0.0262 -0.0035 62  ASN A ND2 
686  N  ND2 B ASN A 62  ? 0.1694 0.2068 0.1396 -0.0335 -0.0410 -0.0282 62  ASN A ND2 
687  N  N   A GLY A 63  ? 0.0653 0.1181 0.0785 0.0303  0.0249  0.0261  63  GLY A N   
688  N  N   B GLY A 63  ? 0.1603 0.1152 0.0737 -0.0034 0.0219  0.0043  63  GLY A N   
689  C  CA  A GLY A 63  ? 0.0315 0.1109 0.1261 -0.0031 0.0176  0.0285  63  GLY A CA  
690  C  CA  B GLY A 63  ? 0.1213 0.1071 0.1055 -0.0359 0.0219  0.0060  63  GLY A CA  
691  C  C   A GLY A 63  ? 0.1091 0.0961 0.1215 0.0183  0.0309  0.0171  63  GLY A C   
692  C  C   B GLY A 63  ? 0.1649 0.1079 0.0861 -0.0217 0.0041  -0.0196 63  GLY A C   
693  O  O   A GLY A 63  ? 0.1036 0.1571 0.1353 0.0384  0.0118  0.0368  63  GLY A O   
694  O  O   B GLY A 63  ? 0.1365 0.1459 0.1055 -0.0324 -0.0046 0.0065  63  GLY A O   
695  N  N   A HIS A 64  ? 0.0732 0.1526 0.0969 -0.0082 0.0087  0.0012  64  HIS A N   
696  N  N   B HIS A 64  ? 0.1373 0.1053 0.0864 -0.0630 0.0207  0.0085  64  HIS A N   
697  C  CA  A HIS A 64  ? 0.1231 0.1448 0.1127 -0.0428 0.0206  0.0113  64  HIS A CA  
698  C  CA  B HIS A 64  ? 0.1710 0.1477 0.0873 -0.0644 0.0344  0.0140  64  HIS A CA  
699  C  C   A HIS A 64  ? 0.1129 0.1243 0.1091 -0.0233 0.0221  0.0006  64  HIS A C   
700  C  C   B HIS A 64  ? 0.1958 0.1536 0.0978 -0.0841 0.0259  0.0296  64  HIS A C   
701  O  O   A HIS A 64  ? 0.1746 0.1468 0.1773 0.0087  0.0115  0.0493  64  HIS A O   
702  O  O   B HIS A 64  ? 0.1450 0.1983 0.1923 -0.0667 0.0076  0.1027  64  HIS A O   
703  C  CB  A HIS A 64  ? 0.1335 0.1498 0.0926 -0.0065 0.0006  0.0153  64  HIS A CB  
704  C  CB  B HIS A 64  ? 0.1508 0.1655 0.1100 -0.0498 0.0152  -0.0017 64  HIS A CB  
705  C  CG  A HIS A 64  ? 0.1367 0.1640 0.0935 0.0020  0.0264  0.0135  64  HIS A CG  
706  C  CG  B HIS A 64  ? 0.1032 0.1773 0.0951 -0.0114 -0.0043 0.0006  64  HIS A CG  
707  N  ND1 A HIS A 64  ? 0.1398 0.1766 0.1213 -0.0012 0.0293  -0.0208 64  HIS A ND1 
708  N  ND1 B HIS A 64  ? 0.1339 0.1933 0.1313 0.0200  -0.0183 -0.0529 64  HIS A ND1 
709  C  CD2 A HIS A 64  ? 0.1353 0.1739 0.1027 -0.0353 0.0216  0.0230  64  HIS A CD2 
710  C  CD2 B HIS A 64  ? 0.1378 0.1626 0.1163 -0.0046 0.0146  -0.0265 64  HIS A CD2 
711  C  CE1 A HIS A 64  ? 0.1319 0.1747 0.1856 -0.0046 0.0344  -0.0120 64  HIS A CE1 
712  C  CE1 B HIS A 64  ? 0.1443 0.1768 0.1301 0.0020  0.0390  -0.0428 64  HIS A CE1 
713  N  NE2 A HIS A 64  ? 0.1304 0.1653 0.2538 -0.0197 0.0250  -0.0087 64  HIS A NE2 
714  N  NE2 B HIS A 64  ? 0.1391 0.1571 0.1887 -0.0137 0.0115  -0.0458 64  HIS A NE2 
715  N  N   A SER A 65  ? 0.1190 0.1425 0.1137 -0.0172 0.0151  -0.0015 65  SER A N   
716  N  N   B SER A 65  ? 0.1762 0.1213 0.1240 -0.0533 0.0081  -0.0017 65  SER A N   
717  C  CA  A SER A 65  ? 0.1678 0.0935 0.0888 -0.0612 0.0250  0.0216  65  SER A CA  
718  C  CA  B SER A 65  ? 0.1657 0.1985 0.1150 -0.0285 0.0054  0.0063  65  SER A CA  
719  C  C   A SER A 65  ? 0.2213 0.1280 0.0895 -0.0370 0.0048  0.0186  65  SER A C   
720  C  C   B SER A 65  ? 0.2335 0.0863 0.0649 -0.0516 0.0136  -0.0087 65  SER A C   
721  O  O   A SER A 65  ? 0.2770 0.1506 0.0967 -0.0754 0.0211  0.0140  65  SER A O   
722  O  O   B SER A 65  ? 0.2748 0.1267 0.0987 -0.0834 0.0258  0.0098  65  SER A O   
723  C  CB  A SER A 65  ? 0.1410 0.0701 0.0944 -0.0207 0.0113  0.0082  65  SER A CB  
724  C  CB  B SER A 65  ? 0.2099 0.1328 0.0922 -0.0595 0.0043  0.0621  65  SER A CB  
725  O  OG  A SER A 65  ? 0.1633 0.1120 0.0790 -0.0626 -0.0147 0.0505  65  SER A OG  
726  O  OG  B SER A 65  ? 0.2795 0.1676 0.1335 -0.0785 -0.0208 0.0187  65  SER A OG  
727  N  N   . PHE A 66  ? 0.2131 0.1185 0.0838 -0.0478 -0.0006 0.0166  66  PHE A N   
728  C  CA  . PHE A 66  ? 0.2592 0.1085 0.0856 -0.0163 -0.0087 -0.0020 66  PHE A CA  
729  C  C   . PHE A 66  ? 0.2601 0.1023 0.0623 -0.0288 -0.0140 -0.0181 66  PHE A C   
730  O  O   . PHE A 66  ? 0.2375 0.1331 0.0662 -0.0306 -0.0110 -0.0038 66  PHE A O   
731  C  CB  . PHE A 66  ? 0.2337 0.1364 0.0705 -0.0214 -0.0161 -0.0035 66  PHE A CB  
732  C  CG  . PHE A 66  ? 0.2578 0.1199 0.0600 -0.0652 -0.0181 0.0000  66  PHE A CG  
733  C  CD1 . PHE A 66  ? 0.2578 0.1265 0.0944 -0.0383 -0.0326 0.0082  66  PHE A CD1 
734  C  CD2 . PHE A 66  ? 0.2145 0.1292 0.1039 -0.0137 -0.0148 -0.0313 66  PHE A CD2 
735  C  CE1 . PHE A 66  ? 0.2619 0.1163 0.1308 -0.0227 -0.0386 0.0020  66  PHE A CE1 
736  C  CE2 . PHE A 66  ? 0.2418 0.1240 0.1037 -0.0436 -0.0221 -0.0074 66  PHE A CE2 
737  C  CZ  . PHE A 66  ? 0.2178 0.1097 0.1003 -0.0164 -0.0193 -0.0093 66  PHE A CZ  
738  N  N   . GLN A 67  ? 0.2958 0.1134 0.0702 -0.0205 0.0043  0.0043  67  GLN A N   
739  C  CA  . GLN A 67  ? 0.2400 0.1297 0.0908 -0.0205 -0.0260 -0.0209 67  GLN A CA  
740  C  C   . GLN A 67  ? 0.2653 0.1181 0.0793 -0.0366 -0.0526 0.0181  67  GLN A C   
741  O  O   . GLN A 67  ? 0.3341 0.1905 0.0658 -0.0329 0.0013  0.0131  67  GLN A O   
742  C  CB  . GLN A 67  ? 0.2998 0.2005 0.0881 -0.0606 -0.0211 0.0140  67  GLN A CB  
743  C  CG  . GLN A 67  ? 0.3061 0.1669 0.2057 -0.0930 -0.0040 0.0103  67  GLN A CG  
744  C  CD  . GLN A 67  ? 0.2536 0.1899 0.2547 -0.0886 -0.0164 0.0397  67  GLN A CD  
745  O  OE1 . GLN A 67  ? 0.2678 0.1980 0.1912 -0.0410 -0.0286 -0.0631 67  GLN A OE1 
746  N  NE2 . GLN A 67  ? 0.2842 0.2020 0.3434 -0.0131 0.0046  -0.0806 67  GLN A NE2 
747  N  N   A VAL A 68  ? 0.2849 0.0996 0.0949 0.0247  -0.0353 -0.0142 68  VAL A N   
748  N  N   B VAL A 68  ? 0.2892 0.0349 0.1448 0.0142  -0.0430 0.0121  68  VAL A N   
749  C  CA  A VAL A 68  ? 0.1613 0.1261 0.0377 -0.0193 0.0227  0.0026  68  VAL A CA  
750  C  CA  B VAL A 68  ? 0.0768 0.0865 0.1168 0.0178  0.0015  -0.0098 68  VAL A CA  
751  C  C   A VAL A 68  ? 0.1109 0.0872 0.0878 -0.0230 0.0292  0.0313  68  VAL A C   
752  C  C   B VAL A 68  ? 0.0940 0.0772 0.0627 -0.0209 -0.0087 0.0178  68  VAL A C   
753  O  O   A VAL A 68  ? 0.1280 0.0768 0.0836 0.0005  -0.0049 0.0172  68  VAL A O   
754  O  O   B VAL A 68  ? 0.1705 0.0969 0.0546 0.0000  -0.0281 0.0124  68  VAL A O   
755  C  CB  A VAL A 68  ? 0.1499 0.0653 0.0834 -0.0126 -0.0104 0.0335  68  VAL A CB  
756  C  CB  B VAL A 68  ? 0.1263 0.1298 0.0614 -0.0260 -0.0195 0.0097  68  VAL A CB  
757  C  CG1 A VAL A 68  ? 0.1199 0.0992 0.0728 0.0013  0.0023  0.0197  68  VAL A CG1 
758  C  CG1 B VAL A 68  ? 0.0335 0.1845 0.1935 -0.0114 -0.0331 -0.0237 68  VAL A CG1 
759  C  CG2 A VAL A 68  ? 0.1190 0.0876 0.0815 -0.0504 -0.0203 0.0204  68  VAL A CG2 
760  C  CG2 B VAL A 68  ? 0.1732 0.1046 0.0785 -0.0577 -0.0386 0.0124  68  VAL A CG2 
761  N  N   A GLU A 69  ? 0.0667 0.0878 0.0904 0.0104  0.0076  0.0252  69  GLU A N   
762  N  N   B GLU A 69  ? 0.1154 0.0885 0.0797 -0.0035 -0.0076 0.0333  69  GLU A N   
763  C  CA  A GLU A 69  ? 0.0985 0.0854 0.0776 0.0141  -0.0082 0.0241  69  GLU A CA  
764  C  CA  B GLU A 69  ? 0.1041 0.0688 0.1479 -0.0146 -0.0125 0.0186  69  GLU A CA  
765  C  C   A GLU A 69  ? 0.0869 0.0559 0.0924 0.0020  0.0003  0.0275  69  GLU A C   
766  C  C   B GLU A 69  ? 0.1066 0.0833 0.1163 -0.0220 -0.0200 0.0447  69  GLU A C   
767  O  O   A GLU A 69  ? 0.1231 0.1107 0.0833 0.0000  -0.0020 0.0098  69  GLU A O   
768  O  O   B GLU A 69  ? 0.2129 0.1222 0.1082 0.0315  -0.0383 0.0284  69  GLU A O   
769  C  CB  A GLU A 69  ? 0.0511 0.1395 0.1437 -0.0198 -0.0153 0.0329  69  GLU A CB  
770  C  CB  B GLU A 69  ? 0.1642 0.1392 0.1611 -0.0461 0.0531  0.0109  69  GLU A CB  
771  C  CG  A GLU A 69  ? 0.0546 0.1585 0.1247 -0.0057 0.0129  0.0076  69  GLU A CG  
772  C  CG  B GLU A 69  ? 0.1536 0.1518 0.3840 -0.0579 0.0599  0.0307  69  GLU A CG  
773  C  CD  A GLU A 69  ? 0.1012 0.1457 0.1439 -0.0242 0.0125  0.0476  69  GLU A CD  
774  C  CD  B GLU A 69  ? 0.2996 0.1543 0.3106 -0.0395 0.0120  0.1263  69  GLU A CD  
775  O  OE1 A GLU A 69  ? 0.1332 0.1554 0.1371 -0.0026 0.0198  0.0505  69  GLU A OE1 
776  O  OE1 B GLU A 69  ? 0.4684 0.2849 0.4856 0.0790  -0.1438 0.0829  69  GLU A OE1 
777  O  OE2 A GLU A 69  ? 0.1337 0.1601 0.1905 0.0020  0.0030  -0.0092 69  GLU A OE2 
778  O  OE2 B GLU A 69  ? 0.2863 0.2610 0.2944 -0.0399 -0.0811 0.0527  69  GLU A OE2 
779  N  N   A PHE A 70  ? 0.1290 0.1111 0.0784 0.0054  0.0251  0.0215  70  PHE A N   
780  N  N   B PHE A 70  ? 0.1549 0.0722 0.1290 -0.0015 -0.0152 0.0210  70  PHE A N   
781  C  CA  A PHE A 70  ? 0.1923 0.0687 0.1387 0.0434  0.0178  0.0348  70  PHE A CA  
782  C  CA  B PHE A 70  ? 0.1958 0.0924 0.1089 0.0364  -0.0231 0.0017  70  PHE A CA  
783  C  C   A PHE A 70  ? 0.2795 0.0754 0.1533 0.0260  0.0019  0.0142  70  PHE A C   
784  C  C   B PHE A 70  ? 0.3174 0.0985 0.1389 -0.0104 -0.0392 0.0553  70  PHE A C   
785  O  O   A PHE A 70  ? 0.3030 0.0922 0.1897 -0.0151 -0.0137 0.0706  70  PHE A O   
786  O  O   B PHE A 70  ? 0.3296 0.0749 0.1261 -0.0249 -0.0187 0.0571  70  PHE A O   
787  C  CB  A PHE A 70  ? 0.1845 0.0780 0.0992 0.0401  0.0020  0.0120  70  PHE A CB  
788  C  CB  B PHE A 70  ? 0.2113 0.1163 0.1125 -0.0226 -0.0353 0.0364  70  PHE A CB  
789  C  CG  A PHE A 70  ? 0.1615 0.0933 0.1448 0.0146  0.0019  0.0441  70  PHE A CG  
790  C  CG  B PHE A 70  ? 0.1935 0.0920 0.0847 0.0152  -0.0496 0.0220  70  PHE A CG  
791  C  CD1 A PHE A 70  ? 0.2152 0.0895 0.1062 0.0262  -0.0777 0.0193  70  PHE A CD1 
792  C  CD1 B PHE A 70  ? 0.1518 0.0985 0.1581 -0.0027 -0.0163 0.0076  70  PHE A CD1 
793  C  CD2 A PHE A 70  ? 0.1635 0.0917 0.0939 0.0104  -0.0031 0.0447  70  PHE A CD2 
794  C  CD2 B PHE A 70  ? 0.2334 0.0978 0.1466 0.0091  -0.1150 0.0329  70  PHE A CD2 
795  C  CE1 A PHE A 70  ? 0.2002 0.0951 0.1123 0.0160  -0.0610 0.0509  70  PHE A CE1 
796  C  CE1 B PHE A 70  ? 0.2129 0.0965 0.0825 0.0086  0.0000  0.0231  70  PHE A CE1 
797  C  CE2 A PHE A 70  ? 0.1831 0.0912 0.1149 0.0236  -0.0048 0.0143  70  PHE A CE2 
798  C  CE2 B PHE A 70  ? 0.1981 0.1341 0.1651 -0.0109 -0.0794 0.0124  70  PHE A CE2 
799  C  CZ  A PHE A 70  ? 0.1885 0.1308 0.1184 0.0414  -0.0318 0.0193  70  PHE A CZ  
800  C  CZ  B PHE A 70  ? 0.1717 0.0951 0.1380 -0.0173 -0.0304 0.0230  70  PHE A CZ  
801  N  N   . ASP A 71  ? 0.3720 0.0836 0.1981 0.0373  -0.0544 0.0496  71  ASP A N   
802  C  CA  . ASP A 71  ? 0.3224 0.0816 0.2114 0.0087  -0.0333 0.0511  71  ASP A CA  
803  C  C   . ASP A 71  ? 0.2930 0.0724 0.2319 0.0306  -0.0403 0.0119  71  ASP A C   
804  O  O   . ASP A 71  ? 0.3736 0.1826 0.2928 -0.0379 -0.0274 0.0048  71  ASP A O   
805  C  CB  . ASP A 71  ? 0.4203 0.1062 0.2996 0.0406  -0.0750 0.0859  71  ASP A CB  
806  C  CG  . ASP A 71  ? 0.3355 0.1536 0.2856 0.0610  -0.1622 0.0024  71  ASP A CG  
807  O  OD1 . ASP A 71  ? 0.3689 0.1163 0.2967 0.0107  -0.0812 0.0604  71  ASP A OD1 
808  O  OD2 . ASP A 71  ? 0.3659 0.1732 0.3616 0.0496  -0.1347 0.0172  71  ASP A OD2 
809  N  N   . ASP A 72  ? 0.2991 0.0781 0.2415 0.0216  -0.0406 0.0480  72  ASP A N   
810  C  CA  . ASP A 72  ? 0.2967 0.1018 0.2305 0.0152  0.0161  0.0335  72  ASP A CA  
811  C  C   . ASP A 72  ? 0.2770 0.1082 0.2569 0.0109  -0.0252 0.0262  72  ASP A C   
812  O  O   . ASP A 72  ? 0.3524 0.1097 0.2906 0.0092  -0.0456 0.0136  72  ASP A O   
813  C  CB  . ASP A 72  ? 0.3055 0.0974 0.2493 0.0362  0.0026  0.0238  72  ASP A CB  
814  C  CG  . ASP A 72  ? 0.3088 0.1547 0.2226 0.0373  -0.0295 0.0575  72  ASP A CG  
815  O  OD1 . ASP A 72  ? 0.4036 0.2646 0.1981 0.0284  -0.0156 0.0873  72  ASP A OD1 
816  O  OD2 . ASP A 72  ? 0.2770 0.2486 0.2221 0.0370  -0.0097 0.0643  72  ASP A OD2 
817  N  N   . SER A 73  ? 0.2721 0.1123 0.3030 0.0293  -0.0434 0.0348  73  SER A N   
818  C  CA  . SER A 73  ? 0.3034 0.1208 0.3540 -0.0324 -0.0135 0.0728  73  SER A CA  
819  C  C   . SER A 73  ? 0.3738 0.1272 0.3495 0.0087  -0.0080 0.0082  73  SER A C   
820  O  O   . SER A 73  ? 0.4029 0.1186 0.3032 0.0205  -0.1008 0.0010  73  SER A O   
821  C  CB  . SER A 73  ? 0.3849 0.1621 0.3720 -0.0091 -0.0537 0.0820  73  SER A CB  
822  O  OG  . SER A 73  ? 0.3398 0.1306 0.3104 0.0054  -0.0093 0.0505  73  SER A OG  
823  N  N   . GLN A 74  ? 0.3151 0.1856 0.3183 0.0220  0.0093  0.0093  74  GLN A N   
824  C  CA  . GLN A 74  ? 0.3662 0.2244 0.2310 0.0878  -0.0531 0.0197  74  GLN A CA  
825  C  C   . GLN A 74  ? 0.2718 0.1518 0.3892 0.0297  -0.1272 0.0297  74  GLN A C   
826  O  O   . GLN A 74  ? 0.2407 0.1315 0.3562 -0.0194 -0.0487 -0.0410 74  GLN A O   
827  C  CB  . GLN A 74  ? 0.4083 0.3145 0.3939 0.1250  -0.1084 0.0361  74  GLN A CB  
828  C  CG  . GLN A 74  ? 0.4708 0.1975 0.5982 -0.0220 -0.1295 0.1049  74  GLN A CG  
829  C  CD  . GLN A 74  ? 0.4690 0.4480 0.3795 0.1307  -0.0895 0.1842  74  GLN A CD  
830  O  OE1 . GLN A 74  ? 0.4250 0.4618 0.6739 0.0098  0.0568  0.0979  74  GLN A OE1 
831  N  NE2 . GLN A 74  ? 0.3790 0.3458 0.3727 -0.0048 -0.0219 0.0834  74  GLN A NE2 
832  N  N   . ASP A 75  ? 0.3810 0.2515 0.3009 0.0542  -0.1124 0.0019  75  ASP A N   
833  C  CA  . ASP A 75  ? 0.3526 0.2951 0.2833 -0.0273 -0.0772 -0.0553 75  ASP A CA  
834  C  C   . ASP A 75  ? 0.2248 0.2773 0.3082 0.0683  -0.0876 -0.0430 75  ASP A C   
835  O  O   . ASP A 75  ? 0.3061 0.4683 0.4449 0.0529  -0.0296 -0.0322 75  ASP A O   
836  C  CB  . ASP A 75  ? 0.3379 0.1905 0.3756 0.0260  -0.0970 -0.0833 75  ASP A CB  
837  C  CG  . ASP A 75  ? 0.3183 0.2849 0.2745 -0.0147 -0.0175 -0.1124 75  ASP A CG  
838  O  OD1 . ASP A 75  ? 0.3091 0.2536 0.3258 0.0401  -0.0229 0.0015  75  ASP A OD1 
839  O  OD2 . ASP A 75  ? 0.4329 0.3134 0.4013 0.0136  0.1074  -0.0979 75  ASP A OD2 
840  N  N   A LYS A 76  ? 0.2346 0.1358 0.2648 -0.0065 -0.0447 0.0282  76  LYS A N   
841  N  N   B LYS A 76  ? 0.1869 0.2554 0.2477 0.0070  -0.0649 0.0259  76  LYS A N   
842  C  CA  A LYS A 76  ? 0.3084 0.1335 0.2443 -0.0141 -0.0917 0.0474  76  LYS A CA  
843  C  CA  B LYS A 76  ? 0.2784 0.1926 0.2337 -0.0230 -0.0496 0.0560  76  LYS A CA  
844  C  C   A LYS A 76  ? 0.1605 0.1278 0.1814 0.0043  -0.0205 0.0255  76  LYS A C   
845  C  C   B LYS A 76  ? 0.3219 0.2127 0.2384 0.0535  -0.0617 0.0671  76  LYS A C   
846  O  O   A LYS A 76  ? 0.2621 0.1527 0.2590 -0.0275 -0.1102 0.0007  76  LYS A O   
847  O  O   B LYS A 76  ? 0.3813 0.2423 0.2763 0.0299  -0.0551 0.0297  76  LYS A O   
848  C  CB  A LYS A 76  ? 0.3725 0.0996 0.2702 -0.0891 -0.0370 0.0593  76  LYS A CB  
849  C  CB  B LYS A 76  ? 0.3993 0.2989 0.2021 -0.0054 0.0113  0.1067  76  LYS A CB  
850  C  CG  A LYS A 76  ? 0.4462 0.1262 0.2763 -0.0864 -0.0970 0.0731  76  LYS A CG  
851  C  CG  B LYS A 76  ? 0.3222 0.0996 0.3285 -0.0581 0.0120  0.0568  76  LYS A CG  
852  C  CD  A LYS A 76  ? 0.4241 0.3319 0.3352 -0.0126 -0.0164 0.1871  76  LYS A CD  
853  C  CD  B LYS A 76  ? 0.4422 0.1861 0.2806 -0.1350 0.0126  0.0895  76  LYS A CD  
854  C  CE  A LYS A 76  ? 0.3319 0.3079 0.2691 0.0147  -0.1054 0.0172  76  LYS A CE  
855  C  CE  B LYS A 76  ? 0.3912 0.3447 0.2509 -0.0357 0.0252  0.0693  76  LYS A CE  
856  N  NZ  A LYS A 76  ? 0.2002 0.3551 0.3115 0.1562  -0.0081 -0.0155 76  LYS A NZ  
857  N  NZ  B LYS A 76  ? 0.2804 0.2585 0.1923 0.0513  -0.0540 0.0461  76  LYS A NZ  
858  N  N   A ALA A 77  ? 0.1960 0.1615 0.1763 -0.0010 -0.0785 -0.0126 77  ALA A N   
859  N  N   B ALA A 77  ? 0.2583 0.1398 0.2500 0.0170  -0.1049 0.0551  77  ALA A N   
860  C  CA  A ALA A 77  ? 0.1867 0.1668 0.2181 -0.0260 -0.0719 0.0137  77  ALA A CA  
861  C  CA  B ALA A 77  ? 0.2037 0.1565 0.1991 0.0184  -0.0785 0.0461  77  ALA A CA  
862  C  C   A ALA A 77  ? 0.1563 0.1465 0.2166 0.0024  -0.0634 -0.0096 77  ALA A C   
863  C  C   B ALA A 77  ? 0.2009 0.1360 0.2084 -0.0120 -0.0736 0.0406  77  ALA A C   
864  O  O   A ALA A 77  ? 0.1411 0.1450 0.1887 0.0275  -0.0266 -0.0178 77  ALA A O   
865  O  O   B ALA A 77  ? 0.1689 0.1865 0.2488 0.0104  -0.0737 0.0964  77  ALA A O   
866  C  CB  A ALA A 77  ? 0.1800 0.1773 0.1601 -0.0472 -0.0697 0.0414  77  ALA A CB  
867  C  CB  B ALA A 77  ? 0.2395 0.1622 0.1976 0.0031  -0.0777 0.0247  77  ALA A CB  
868  N  N   . VAL A 78  ? 0.1520 0.1444 0.2073 0.0153  -0.0494 0.0104  78  VAL A N   
869  C  CA  . VAL A 78  ? 0.2255 0.1475 0.2041 -0.0071 -0.0643 0.0370  78  VAL A CA  
870  C  C   . VAL A 78  ? 0.1466 0.1386 0.1964 -0.0147 -0.0493 0.0086  78  VAL A C   
871  O  O   . VAL A 78  ? 0.1491 0.1577 0.2653 -0.0259 -0.0593 0.0231  78  VAL A O   
872  C  CB  . VAL A 78  ? 0.2077 0.2172 0.2513 -0.0035 -0.0568 0.0205  78  VAL A CB  
873  C  CG1 . VAL A 78  ? 0.2718 0.1669 0.2472 0.0478  -0.0397 0.0285  78  VAL A CG1 
874  C  CG2 . VAL A 78  ? 0.2107 0.2809 0.3005 -0.0013 -0.0054 -0.0419 78  VAL A CG2 
875  N  N   . LEU A 79  ? 0.1333 0.1107 0.1568 -0.0017 -0.0348 -0.0012 79  LEU A N   
876  C  CA  . LEU A 79  ? 0.1111 0.1206 0.1852 -0.0017 -0.0175 -0.0054 79  LEU A CA  
877  C  C   . LEU A 79  ? 0.1471 0.1197 0.1644 -0.0041 -0.0110 -0.0137 79  LEU A C   
878  O  O   . LEU A 79  ? 0.1736 0.1272 0.2070 -0.0241 0.0113  -0.0230 79  LEU A O   
879  C  CB  . LEU A 79  ? 0.0983 0.1735 0.2551 -0.0043 -0.0353 0.0555  79  LEU A CB  
880  C  CG  . LEU A 79  ? 0.1225 0.1628 0.2036 -0.0020 -0.0137 0.0166  79  LEU A CG  
881  C  CD1 . LEU A 79  ? 0.1396 0.1888 0.3127 -0.0048 0.0276  0.0640  79  LEU A CD1 
882  C  CD2 . LEU A 79  ? 0.1375 0.1671 0.1799 0.0281  0.0088  0.0087  79  LEU A CD2 
883  N  N   . LYS A 80  ? 0.1335 0.1978 0.1800 -0.0243 0.0013  -0.0051 80  LYS A N   
884  C  CA  . LYS A 80  ? 0.1844 0.1905 0.2021 -0.0291 -0.0051 0.0019  80  LYS A CA  
885  C  C   . LYS A 80  ? 0.1425 0.1448 0.2246 0.0087  0.0254  -0.0065 80  LYS A C   
886  O  O   . LYS A 80  ? 0.1308 0.1673 0.2412 -0.0141 0.0274  0.0003  80  LYS A O   
887  C  CB  . LYS A 80  ? 0.4124 0.1581 0.2104 0.0423  0.0829  -0.0140 80  LYS A CB  
888  C  CG  . LYS A 80  ? 0.2208 0.2583 0.3519 0.0054  0.0732  0.0454  80  LYS A CG  
889  C  CD  . LYS A 80  ? 0.2273 0.4873 0.3865 0.0834  -0.0051 0.0456  80  LYS A CD  
890  C  CE  . LYS A 80  ? 0.4140 0.7148 0.4487 0.0000  0.1098  -0.0304 80  LYS A CE  
891  N  NZ  . LYS A 80  ? 0.3695 1.0097 0.6093 0.1120  -0.0115 0.3384  80  LYS A NZ  
892  N  N   . GLY A 81  ? 0.1708 0.1788 0.2274 0.0034  0.0728  -0.0119 81  GLY A N   
893  C  CA  . GLY A 81  ? 0.1136 0.2011 0.2442 0.0232  0.0478  0.0178  81  GLY A CA  
894  C  C   . GLY A 81  ? 0.1170 0.1595 0.2515 0.0177  0.0544  0.0107  81  GLY A C   
895  O  O   . GLY A 81  ? 0.1217 0.1836 0.1851 -0.0189 0.0397  -0.0214 81  GLY A O   
896  N  N   . GLY A 82  ? 0.1355 0.2269 0.3172 0.0030  0.0617  0.0715  82  GLY A N   
897  C  CA  . GLY A 82  ? 0.1120 0.2339 0.4018 0.0182  0.0741  0.0593  82  GLY A CA  
898  C  C   . GLY A 82  ? 0.1556 0.1980 0.3034 0.0434  0.0674  0.0549  82  GLY A C   
899  O  O   . GLY A 82  ? 0.2467 0.4059 0.2838 0.1703  0.1480  0.0798  82  GLY A O   
900  N  N   . PRO A 83  ? 0.1500 0.1951 0.2506 0.0329  0.0693  0.0188  83  PRO A N   
901  C  CA  . PRO A 83  ? 0.2150 0.1648 0.2193 0.0469  0.0562  -0.0126 83  PRO A CA  
902  C  C   . PRO A 83  ? 0.1572 0.1886 0.1981 0.0386  0.0456  -0.0326 83  PRO A C   
903  O  O   . PRO A 83  ? 0.2100 0.2458 0.2041 0.0342  -0.0086 -0.0375 83  PRO A O   
904  C  CB  . PRO A 83  ? 0.1829 0.1561 0.1806 0.0274  0.0219  0.0065  83  PRO A CB  
905  C  CG  . PRO A 83  ? 0.1254 0.1558 0.1906 0.0219  0.0207  -0.0185 83  PRO A CG  
906  C  CD  . PRO A 83  ? 0.1080 0.1404 0.2535 0.0049  0.0313  -0.0249 83  PRO A CD  
907  N  N   . LEU A 84  ? 0.1538 0.1552 0.1550 0.0286  0.0286  -0.0131 84  LEU A N   
908  C  CA  . LEU A 84  ? 0.1414 0.1420 0.1867 0.0364  0.0392  -0.0432 84  LEU A CA  
909  C  C   . LEU A 84  ? 0.1552 0.1480 0.1841 0.0275  0.0156  -0.0579 84  LEU A C   
910  O  O   . LEU A 84  ? 0.1545 0.1738 0.2520 0.0386  0.0535  -0.0658 84  LEU A O   
911  C  CB  . LEU A 84  ? 0.1799 0.1249 0.1554 0.0275  0.0436  -0.0296 84  LEU A CB  
912  C  CG  . LEU A 84  ? 0.1251 0.1152 0.1506 0.0364  0.0159  -0.0164 84  LEU A CG  
913  C  CD1 . LEU A 84  ? 0.1263 0.1574 0.1642 0.0318  0.0063  -0.0410 84  LEU A CD1 
914  C  CD2 . LEU A 84  ? 0.1168 0.1142 0.1623 0.0193  0.0271  -0.0302 84  LEU A CD2 
915  N  N   . ASP A 85  ? 0.1883 0.1595 0.2237 0.0077  0.0326  -0.0864 85  ASP A N   
916  C  CA  . ASP A 85  ? 0.2896 0.1249 0.2533 0.0093  -0.0098 -0.0772 85  ASP A CA  
917  C  C   . ASP A 85  ? 0.2312 0.1224 0.3792 0.0381  0.0746  -0.0263 85  ASP A C   
918  O  O   . ASP A 85  ? 0.2978 0.2527 0.3580 0.0364  0.1014  -0.0551 85  ASP A O   
919  C  CB  . ASP A 85  ? 0.3813 0.1847 0.3578 0.0489  -0.0443 -0.1456 85  ASP A CB  
920  C  CG  . ASP A 85  ? 0.3822 0.6553 0.5012 0.0074  0.0172  -0.0670 85  ASP A CG  
921  O  OD1 . ASP A 85  ? 0.4541 0.7289 0.4808 -0.0921 0.0156  -0.1459 85  ASP A OD1 
922  O  OD2 . ASP A 85  ? 0.3190 0.4521 0.5454 0.0746  0.0366  0.0329  85  ASP A OD2 
923  N  N   . GLY A 86  ? 0.2460 0.2443 0.2763 -0.0065 -0.0046 -0.0520 86  GLY A N   
924  C  CA  . GLY A 86  ? 0.2896 0.2075 0.2912 -0.0071 -0.0308 -0.0540 86  GLY A CA  
925  C  C   . GLY A 86  ? 0.2619 0.1953 0.2332 -0.0395 -0.0120 -0.0359 86  GLY A C   
926  O  O   . GLY A 86  ? 0.3147 0.2188 0.2556 -0.0957 -0.0230 -0.0156 86  GLY A O   
927  N  N   . THR A 87  ? 0.1492 0.1558 0.2093 0.0253  0.0200  -0.0403 87  THR A N   
928  C  CA  . THR A 87  ? 0.1523 0.1779 0.2105 0.0361  0.0098  -0.0559 87  THR A CA  
929  C  C   . THR A 87  ? 0.1277 0.1040 0.2057 0.0164  -0.0076 -0.0401 87  THR A C   
930  O  O   . THR A 87  ? 0.1520 0.0942 0.2310 -0.0049 -0.0081 -0.0331 87  THR A O   
931  C  CB  . THR A 87  ? 0.1709 0.2939 0.2242 0.1290  -0.0294 -0.0667 87  THR A CB  
932  O  OG1 . THR A 87  ? 0.1933 0.3050 0.4156 0.1036  0.0167  -0.0746 87  THR A OG1 
933  C  CG2 . THR A 87  ? 0.2220 0.2494 0.2380 0.0854  -0.0088 -0.0450 87  THR A CG2 
934  N  N   . TYR A 88  ? 0.0935 0.1096 0.1917 0.0216  -0.0063 -0.0295 88  TYR A N   
935  C  CA  . TYR A 88  ? 0.1030 0.1181 0.1709 0.0196  -0.0015 -0.0120 88  TYR A CA  
936  C  C   . TYR A 88  ? 0.1179 0.0958 0.1771 0.0027  -0.0285 -0.0225 88  TYR A C   
937  O  O   . TYR A 88  ? 0.1403 0.1472 0.2041 -0.0219 -0.0480 0.0142  88  TYR A O   
938  C  CB  . TYR A 88  ? 0.1102 0.1058 0.1570 0.0243  -0.0137 -0.0200 88  TYR A CB  
939  C  CG  . TYR A 88  ? 0.1057 0.0895 0.1673 0.0155  -0.0125 -0.0252 88  TYR A CG  
940  C  CD1 . TYR A 88  ? 0.0876 0.1023 0.1694 0.0012  -0.0082 -0.0263 88  TYR A CD1 
941  C  CD2 . TYR A 88  ? 0.1040 0.0759 0.1581 0.0129  -0.0020 0.0013  88  TYR A CD2 
942  C  CE1 . TYR A 88  ? 0.1084 0.1116 0.1499 0.0054  0.0041  -0.0205 88  TYR A CE1 
943  C  CE2 . TYR A 88  ? 0.1141 0.0852 0.1299 0.0071  0.0060  -0.0137 88  TYR A CE2 
944  C  CZ  . TYR A 88  ? 0.1161 0.0759 0.1387 -0.0031 -0.0040 -0.0251 88  TYR A CZ  
945  O  OH  . TYR A 88  ? 0.1091 0.1222 0.1367 0.0037  0.0120  -0.0307 88  TYR A OH  
946  N  N   . ARG A 89  ? 0.1145 0.1057 0.1532 0.0230  -0.0146 -0.0340 89  ARG A N   
947  C  CA  . ARG A 89  ? 0.1651 0.0781 0.1717 0.0194  -0.0540 -0.0054 89  ARG A CA  
948  C  C   . ARG A 89  ? 0.1304 0.0780 0.1145 0.0027  -0.0395 0.0186  89  ARG A C   
949  O  O   . ARG A 89  ? 0.1225 0.0799 0.1271 -0.0035 -0.0373 0.0065  89  ARG A O   
950  C  CB  . ARG A 89  ? 0.2208 0.0671 0.2368 0.0104  -0.0644 0.0217  89  ARG A CB  
951  C  CG  . ARG A 89  ? 0.2309 0.1409 0.2333 0.0346  -0.0339 -0.0152 89  ARG A CG  
952  C  CD  . ARG A 89  ? 0.3853 0.1170 0.3039 0.0263  -0.0863 0.0610  89  ARG A CD  
953  N  NE  . ARG A 89  ? 0.2838 0.2036 0.2624 0.0351  -0.0926 -0.0065 89  ARG A NE  
954  C  CZ  . ARG A 89  ? 0.3546 0.1360 0.2870 0.0458  -0.0489 0.0054  89  ARG A CZ  
955  N  NH1 . ARG A 89  ? 0.3810 0.1727 0.2319 0.0375  -0.0452 -0.0230 89  ARG A NH1 
956  N  NH2 . ARG A 89  ? 0.3718 0.1651 0.3411 0.0649  0.0280  0.0043  89  ARG A NH2 
957  N  N   . LEU A 90  ? 0.1384 0.0847 0.1468 0.0005  -0.0408 0.0048  90  LEU A N   
958  C  CA  . LEU A 90  ? 0.1516 0.0740 0.1339 -0.0096 -0.0274 -0.0041 90  LEU A CA  
959  C  C   . LEU A 90  ? 0.1662 0.0921 0.1163 0.0006  -0.0421 0.0063  90  LEU A C   
960  O  O   . LEU A 90  ? 0.2220 0.1048 0.1349 0.0115  -0.0469 0.0307  90  LEU A O   
961  C  CB  . LEU A 90  ? 0.1685 0.0788 0.1380 -0.0010 -0.0419 0.0175  90  LEU A CB  
962  C  CG  . LEU A 90  ? 0.2026 0.0926 0.1359 -0.0280 -0.0287 -0.0097 90  LEU A CG  
963  C  CD1 . LEU A 90  ? 0.2082 0.0827 0.1569 -0.0086 -0.0242 0.0230  90  LEU A CD1 
964  C  CD2 . LEU A 90  ? 0.1966 0.1432 0.1971 -0.0355 -0.0397 -0.0142 90  LEU A CD2 
965  N  N   . LEU A 91  ? 0.1671 0.0643 0.1145 0.0185  -0.0254 0.0000  91  LEU A N   
966  C  CA  . LEU A 91  ? 0.1730 0.0754 0.1079 0.0051  -0.0178 0.0020  91  LEU A CA  
967  C  C   . LEU A 91  ? 0.1659 0.0671 0.0882 -0.0177 -0.0131 0.0136  91  LEU A C   
968  O  O   . LEU A 91  ? 0.1806 0.0820 0.0920 -0.0277 -0.0247 0.0120  91  LEU A O   
969  C  CB  . LEU A 91  ? 0.1877 0.1005 0.1154 0.0166  -0.0379 -0.0087 91  LEU A CB  
970  C  CG  . LEU A 91  ? 0.1969 0.0876 0.1572 -0.0171 -0.0205 -0.0043 91  LEU A CG  
971  C  CD1 . LEU A 91  ? 0.2531 0.1322 0.2707 -0.0542 -0.0798 0.0662  91  LEU A CD1 
972  C  CD2 . LEU A 91  ? 0.1845 0.2389 0.2393 -0.0153 -0.0480 -0.0401 91  LEU A CD2 
973  N  N   A GLN A 92  ? 0.1559 0.0631 0.0917 -0.0120 0.0010  0.0131  92  GLN A N   
974  N  N   B GLN A 92  ? 0.1517 0.0471 0.1084 0.0068  -0.0208 0.0060  92  GLN A N   
975  C  CA  A GLN A 92  ? 0.1405 0.0544 0.0876 -0.0096 -0.0120 0.0163  92  GLN A CA  
976  C  CA  B GLN A 92  ? 0.1353 0.0606 0.0816 -0.0068 0.0181  0.0119  92  GLN A CA  
977  C  C   A GLN A 92  ? 0.1176 0.0666 0.0600 -0.0308 0.0177  -0.0019 92  GLN A C   
978  C  C   B GLN A 92  ? 0.1143 0.0678 0.0781 0.0108  0.0165  0.0163  92  GLN A C   
979  O  O   A GLN A 92  ? 0.1216 0.0841 0.0577 -0.0161 -0.0020 0.0162  92  GLN A O   
980  O  O   B GLN A 92  ? 0.1337 0.0552 0.0731 0.0046  0.0104  -0.0017 92  GLN A O   
981  C  CB  A GLN A 92  ? 0.1515 0.1199 0.0908 -0.0164 -0.0043 0.0230  92  GLN A CB  
982  C  CB  B GLN A 92  ? 0.1513 0.0613 0.1252 -0.0052 0.0103  -0.0035 92  GLN A CB  
983  C  CG  A GLN A 92  ? 0.1506 0.1387 0.0856 -0.0107 0.0010  -0.0010 92  GLN A CG  
984  C  CG  B GLN A 92  ? 0.1777 0.0763 0.1027 -0.0186 0.0140  0.0087  92  GLN A CG  
985  C  CD  A GLN A 92  ? 0.1727 0.1075 0.0951 -0.0137 -0.0060 0.0071  92  GLN A CD  
986  C  CD  B GLN A 92  ? 0.1221 0.0908 0.1206 -0.0192 0.0353  0.0273  92  GLN A CD  
987  O  OE1 A GLN A 92  ? 0.1847 0.3792 0.0597 0.0020  0.0007  -0.0159 92  GLN A OE1 
988  O  OE1 B GLN A 92  ? 0.1653 0.0538 0.1263 0.0019  0.0238  0.0175  92  GLN A OE1 
989  N  NE2 A GLN A 92  ? 0.1933 0.0881 0.1190 0.0024  -0.0285 0.0063  92  GLN A NE2 
990  N  NE2 B GLN A 92  ? 0.1450 0.1998 0.0997 0.0049  0.0414  0.0142  92  GLN A NE2 
991  N  N   A PHE A 93  ? 0.1571 0.0498 0.0768 -0.0074 0.0017  -0.0017 93  PHE A N   
992  N  N   B PHE A 93  ? 0.1437 0.0688 0.0644 0.0013  0.0054  0.0219  93  PHE A N   
993  C  CA  A PHE A 93  ? 0.1396 0.0542 0.0737 -0.0274 -0.0241 -0.0027 93  PHE A CA  
994  C  CA  B PHE A 93  ? 0.1492 0.0741 0.0414 -0.0174 0.0122  0.0243  93  PHE A CA  
995  C  C   A PHE A 93  ? 0.1838 0.0318 0.0750 -0.0195 0.0006  0.0063  93  PHE A C   
996  C  C   B PHE A 93  ? 0.1362 0.0693 0.0597 -0.0199 -0.0013 0.0164  93  PHE A C   
997  O  O   A PHE A 93  ? 0.1817 0.0657 0.0590 0.0065  -0.0087 0.0082  93  PHE A O   
998  O  O   B PHE A 93  ? 0.1586 0.0966 0.0502 -0.0107 0.0076  0.0097  93  PHE A O   
999  C  CB  A PHE A 93  ? 0.1154 0.0719 0.0561 0.0038  -0.0076 -0.0135 93  PHE A CB  
1000 C  CB  B PHE A 93  ? 0.1353 0.0865 0.0573 -0.0165 -0.0026 0.0436  93  PHE A CB  
1001 C  CG  A PHE A 93  ? 0.1301 0.0732 0.0680 -0.0120 -0.0253 0.0115  93  PHE A CG  
1002 C  CG  B PHE A 93  ? 0.1286 0.0719 0.0718 0.0024  -0.0015 0.0208  93  PHE A CG  
1003 C  CD1 A PHE A 93  ? 0.1238 0.0732 0.0772 -0.0286 -0.0220 0.0000  93  PHE A CD1 
1004 C  CD1 B PHE A 93  ? 0.1084 0.0935 0.0746 0.0161  0.0027  0.0172  93  PHE A CD1 
1005 C  CD2 A PHE A 93  ? 0.1057 0.0772 0.0931 -0.0189 -0.0215 -0.0043 93  PHE A CD2 
1006 C  CD2 B PHE A 93  ? 0.1432 0.0811 0.0649 0.0156  -0.0065 0.0320  93  PHE A CD2 
1007 C  CE1 A PHE A 93  ? 0.1242 0.0915 0.0639 -0.0068 -0.0259 0.0175  93  PHE A CE1 
1008 C  CE1 B PHE A 93  ? 0.0912 0.0802 0.0960 0.0038  0.0015  0.0070  93  PHE A CE1 
1009 C  CE2 A PHE A 93  ? 0.1048 0.0820 0.0652 -0.0230 -0.0172 0.0263  93  PHE A CE2 
1010 C  CE2 B PHE A 93  ? 0.1041 0.0917 0.0922 0.0131  0.0153  0.0000  93  PHE A CE2 
1011 C  CZ  A PHE A 93  ? 0.1190 0.0956 0.0710 -0.0030 -0.0182 0.0152  93  PHE A CZ  
1012 C  CZ  B PHE A 93  ? 0.1036 0.0615 0.0931 -0.0005 -0.0065 0.0104  93  PHE A CZ  
1013 N  N   . HIS A 94  ? 0.1529 0.0590 0.0762 -0.0184 -0.0282 0.0081  94  HIS A N   
1014 C  CA  . HIS A 94  ? 0.1626 0.0640 0.0606 -0.0143 -0.0030 0.0120  94  HIS A CA  
1015 C  C   . HIS A 94  ? 0.1215 0.0724 0.0661 -0.0187 -0.0060 0.0137  94  HIS A C   
1016 O  O   . HIS A 94  ? 0.1441 0.0617 0.0697 -0.0118 0.0137  0.0093  94  HIS A O   
1017 C  CB  . HIS A 94  ? 0.1766 0.0894 0.0529 -0.0291 0.0086  0.0142  94  HIS A CB  
1018 C  CG  . HIS A 94  ? 0.1270 0.0746 0.0780 -0.0306 0.0152  0.0006  94  HIS A CG  
1019 N  ND1 . HIS A 94  ? 0.1242 0.0732 0.0728 -0.0253 0.0041  -0.0024 94  HIS A ND1 
1020 C  CD2 . HIS A 94  ? 0.1307 0.0958 0.0436 -0.0175 0.0155  -0.0024 94  HIS A CD2 
1021 C  CE1 . HIS A 94  ? 0.1179 0.0701 0.0763 -0.0216 -0.0054 0.0098  94  HIS A CE1 
1022 N  NE2 . HIS A 94  ? 0.1075 0.0781 0.0571 -0.0200 0.0026  0.0024  94  HIS A NE2 
1023 N  N   . PHE A 95  ? 0.1386 0.0568 0.0727 -0.0177 0.0043  0.0054  95  PHE A N   
1024 C  CA  . PHE A 95  ? 0.1367 0.0662 0.0715 -0.0143 -0.0148 0.0148  95  PHE A CA  
1025 C  C   . PHE A 95  ? 0.1265 0.0746 0.0529 -0.0119 0.0135  -0.0030 95  PHE A C   
1026 O  O   . PHE A 95  ? 0.1292 0.0926 0.0772 -0.0137 0.0175  0.0081  95  PHE A O   
1027 C  CB  . PHE A 95  ? 0.1395 0.0881 0.0827 -0.0195 0.0010  -0.0091 95  PHE A CB  
1028 C  CG  . PHE A 95  ? 0.1391 0.0710 0.0737 -0.0252 -0.0088 -0.0092 95  PHE A CG  
1029 C  CD1 . PHE A 95  ? 0.1696 0.0890 0.0794 -0.0060 -0.0173 -0.0006 95  PHE A CD1 
1030 C  CD2 . PHE A 95  ? 0.1254 0.1143 0.0904 -0.0188 -0.0038 -0.0192 95  PHE A CD2 
1031 C  CE1 . PHE A 95  ? 0.1626 0.1176 0.0924 0.0054  -0.0340 -0.0115 95  PHE A CE1 
1032 C  CE2 . PHE A 95  ? 0.1274 0.1134 0.1143 -0.0080 -0.0088 -0.0265 95  PHE A CE2 
1033 C  CZ  . PHE A 95  ? 0.1457 0.1061 0.1127 0.0109  -0.0229 -0.0326 95  PHE A CZ  
1034 N  N   . HIS A 96  ? 0.1290 0.0706 0.0551 -0.0159 0.0107  0.0020  96  HIS A N   
1035 C  CA  . HIS A 96  ? 0.1118 0.0675 0.0675 -0.0135 0.0115  -0.0010 96  HIS A CA  
1036 C  C   . HIS A 96  ? 0.1030 0.0688 0.0776 -0.0103 0.0006  -0.0010 96  HIS A C   
1037 O  O   . HIS A 96  ? 0.1030 0.0696 0.0812 -0.0178 0.0148  -0.0026 96  HIS A O   
1038 C  CB  . HIS A 96  ? 0.1398 0.0865 0.0675 -0.0236 0.0020  -0.0154 96  HIS A CB  
1039 C  CG  . HIS A 96  ? 0.1204 0.0775 0.0485 -0.0024 0.0186  -0.0035 96  HIS A CG  
1040 N  ND1 . HIS A 96  ? 0.1037 0.0728 0.0854 0.0000  0.0065  -0.0076 96  HIS A ND1 
1041 C  CD2 . HIS A 96  ? 0.1547 0.0421 0.0798 -0.0038 -0.0010 -0.0236 96  HIS A CD2 
1042 C  CE1 . HIS A 96  ? 0.1061 0.0706 0.0886 0.0073  0.0178  -0.0063 96  HIS A CE1 
1043 N  NE2 . HIS A 96  ? 0.1331 0.0671 0.0590 -0.0093 0.0024  -0.0093 96  HIS A NE2 
1044 N  N   . TRP A 97  ? 0.1299 0.0627 0.0706 -0.0170 0.0131  -0.0087 97  TRP A N   
1045 C  CA  . TRP A 97  ? 0.1158 0.0684 0.0811 -0.0228 0.0166  -0.0151 97  TRP A CA  
1046 C  C   . TRP A 97  ? 0.1274 0.0794 0.0636 -0.0137 0.0261  -0.0147 97  TRP A C   
1047 O  O   . TRP A 97  ? 0.1274 0.0820 0.0864 -0.0074 0.0248  -0.0159 97  TRP A O   
1048 C  CB  . TRP A 97  ? 0.1481 0.0785 0.0570 -0.0230 0.0153  -0.0121 97  TRP A CB  
1049 C  CG  . TRP A 97  ? 0.1387 0.0807 0.0727 -0.0175 0.0093  -0.0068 97  TRP A CG  
1050 C  CD1 . TRP A 97  ? 0.1491 0.1048 0.0674 -0.0141 0.0207  -0.0151 97  TRP A CD1 
1051 C  CD2 . TRP A 97  ? 0.1430 0.0843 0.0684 -0.0342 0.0153  -0.0098 97  TRP A CD2 
1052 N  NE1 . TRP A 97  ? 0.1852 0.0872 0.0865 -0.0264 0.0226  -0.0087 97  TRP A NE1 
1053 C  CE2 . TRP A 97  ? 0.1606 0.0938 0.0736 -0.0443 0.0307  -0.0114 97  TRP A CE2 
1054 C  CE3 . TRP A 97  ? 0.1483 0.0836 0.0631 -0.0205 0.0060  -0.0073 97  TRP A CE3 
1055 C  CZ2 . TRP A 97  ? 0.1708 0.0917 0.0645 -0.0263 0.0131  -0.0132 97  TRP A CZ2 
1056 C  CZ3 . TRP A 97  ? 0.1675 0.1032 0.0670 -0.0335 0.0035  0.0027  97  TRP A CZ3 
1057 C  CH2 . TRP A 97  ? 0.1930 0.0838 0.0754 -0.0333 0.0131  -0.0038 97  TRP A CH2 
1058 N  N   . GLY A 98  ? 0.1383 0.0662 0.0785 -0.0074 0.0266  -0.0125 98  GLY A N   
1059 C  CA  . GLY A 98  ? 0.1508 0.0653 0.0784 -0.0026 0.0244  -0.0046 98  GLY A CA  
1060 C  C   . GLY A 98  ? 0.1208 0.0753 0.0967 -0.0192 0.0077  -0.0142 98  GLY A C   
1061 O  O   . GLY A 98  ? 0.1389 0.0908 0.0926 -0.0088 0.0121  -0.0197 98  GLY A O   
1062 N  N   . SER A 99  ? 0.1465 0.0860 0.1044 -0.0023 0.0326  -0.0315 99  SER A N   
1063 C  CA  . SER A 99  ? 0.1714 0.0956 0.1111 -0.0148 0.0240  -0.0505 99  SER A CA  
1064 C  C   . SER A 99  ? 0.1712 0.0812 0.1023 -0.0020 0.0230  -0.0359 99  SER A C   
1065 O  O   . SER A 99  ? 0.1878 0.1262 0.1304 -0.0238 0.0328  -0.0623 99  SER A O   
1066 C  CB  . SER A 99  ? 0.1592 0.1251 0.1392 -0.0163 0.0524  -0.0702 99  SER A CB  
1067 O  OG  . SER A 99  ? 0.1507 0.1089 0.1702 -0.0065 0.0348  -0.0386 99  SER A OG  
1068 N  N   A LEU A 100 ? 0.1522 0.0750 0.1199 -0.0215 0.0275  -0.0222 100 LEU A N   
1069 N  N   B LEU A 100 ? 0.1429 0.0869 0.1188 -0.0087 0.0296  -0.0243 100 LEU A N   
1070 C  CA  A LEU A 100 ? 0.1711 0.0507 0.1439 -0.0026 0.0206  -0.0337 100 LEU A CA  
1071 C  CA  B LEU A 100 ? 0.1461 0.0879 0.1657 0.0063  0.0344  -0.0226 100 LEU A CA  
1072 C  C   A LEU A 100 ? 0.1387 0.0754 0.1437 -0.0110 0.0125  -0.0162 100 LEU A C   
1073 C  C   B LEU A 100 ? 0.1472 0.0785 0.1225 -0.0131 0.0276  -0.0102 100 LEU A C   
1074 O  O   A LEU A 100 ? 0.1590 0.0854 0.1274 -0.0063 0.0353  -0.0313 100 LEU A O   
1075 O  O   B LEU A 100 ? 0.1617 0.0843 0.1368 -0.0086 0.0298  -0.0280 100 LEU A O   
1076 C  CB  A LEU A 100 ? 0.1324 0.1437 0.1518 0.0309  0.0124  -0.0249 100 LEU A CB  
1077 C  CB  B LEU A 100 ? 0.1423 0.1008 0.0924 -0.0076 0.0015  -0.0164 100 LEU A CB  
1078 C  CG  A LEU A 100 ? 0.1716 0.1272 0.2039 0.0469  0.0535  0.0023  100 LEU A CG  
1079 C  CG  B LEU A 100 ? 0.1795 0.1256 0.1428 0.0115  0.0434  -0.0104 100 LEU A CG  
1080 C  CD1 A LEU A 100 ? 0.2185 0.1777 0.2775 0.0702  0.0043  0.0003  100 LEU A CD1 
1081 C  CD1 B LEU A 100 ? 0.2721 0.1401 0.2181 0.1019  0.0439  -0.0469 100 LEU A CD1 
1082 C  CD2 A LEU A 100 ? 0.1978 0.1680 0.2475 0.0922  0.0610  -0.0649 100 LEU A CD2 
1083 C  CD2 B LEU A 100 ? 0.2170 0.1041 0.1787 0.0296  0.0097  -0.0445 100 LEU A CD2 
1084 N  N   . ASP A 101 ? 0.1249 0.0755 0.1565 0.0013  0.0051  -0.0147 101 ASP A N   
1085 C  CA  . ASP A 101 ? 0.1387 0.0809 0.1498 0.0124  0.0141  0.0162  101 ASP A CA  
1086 C  C   . ASP A 101 ? 0.1251 0.0834 0.1499 0.0015  0.0155  0.0137  101 ASP A C   
1087 O  O   . ASP A 101 ? 0.1874 0.1023 0.1613 0.0270  0.0297  0.0215  101 ASP A O   
1088 C  CB  . ASP A 101 ? 0.1700 0.0799 0.1802 -0.0302 -0.0012 0.0329  101 ASP A CB  
1089 C  CG  . ASP A 101 ? 0.1721 0.1351 0.2136 -0.0263 -0.0182 0.0494  101 ASP A CG  
1090 O  OD1 . ASP A 101 ? 0.1993 0.1185 0.1624 -0.0255 -0.0153 0.0318  101 ASP A OD1 
1091 O  OD2 . ASP A 101 ? 0.2165 0.2003 0.2777 -0.0715 -0.0648 0.0728  101 ASP A OD2 
1092 N  N   . GLY A 102 ? 0.1253 0.0879 0.1359 -0.0038 -0.0040 0.0062  102 GLY A N   
1093 C  CA  . GLY A 102 ? 0.1702 0.0903 0.1515 -0.0186 0.0024  0.0076  102 GLY A CA  
1094 C  C   . GLY A 102 ? 0.1599 0.0790 0.1254 -0.0057 0.0188  0.0068  102 GLY A C   
1095 O  O   . GLY A 102 ? 0.1773 0.0807 0.1199 -0.0070 0.0109  0.0108  102 GLY A O   
1096 N  N   A GLN A 103 ? 0.1362 0.0845 0.1215 -0.0005 0.0200  0.0109  103 GLN A N   
1097 N  N   B GLN A 103 ? 0.1346 0.0697 0.1177 0.0043  0.0315  0.0000  103 GLN A N   
1098 C  CA  A GLN A 103 ? 0.1377 0.0802 0.0951 0.0000  0.0313  0.0057  103 GLN A CA  
1099 C  CA  B GLN A 103 ? 0.1228 0.0577 0.1412 0.0120  0.0160  0.0065  103 GLN A CA  
1100 C  C   A GLN A 103 ? 0.0864 0.0781 0.0870 -0.0076 0.0364  0.0010  103 GLN A C   
1101 C  C   B GLN A 103 ? 0.1019 0.0818 0.0772 -0.0065 0.0076  -0.0038 103 GLN A C   
1102 O  O   A GLN A 103 ? 0.0908 0.0811 0.0913 0.0120  0.0520  -0.0148 103 GLN A O   
1103 O  O   B GLN A 103 ? 0.1305 0.0656 0.0966 -0.0087 -0.0096 -0.0035 103 GLN A O   
1104 C  CB  A GLN A 103 ? 0.1447 0.0714 0.1314 0.0170  0.0303  0.0175  103 GLN A CB  
1105 C  CB  B GLN A 103 ? 0.1170 0.1513 0.1023 0.0087  0.0132  0.0017  103 GLN A CB  
1106 C  CG  A GLN A 103 ? 0.0924 0.1529 0.1305 0.0527  0.0281  0.0027  103 GLN A CG  
1107 C  CG  B GLN A 103 ? 0.0967 0.0940 0.1220 0.0030  0.0335  0.0208  103 GLN A CG  
1108 C  CD  A GLN A 103 ? 0.0872 0.1014 0.1984 0.0280  0.0304  0.0035  103 GLN A CD  
1109 C  CD  B GLN A 103 ? 0.1070 0.1100 0.1396 0.0046  0.0043  -0.0294 103 GLN A CD  
1110 O  OE1 A GLN A 103 ? 0.1580 0.1481 0.2395 0.0710  0.0680  0.0242  103 GLN A OE1 
1111 O  OE1 B GLN A 103 ? 0.1533 0.1127 0.1685 0.0068  0.0000  -0.0120 103 GLN A OE1 
1112 N  NE2 A GLN A 103 ? 0.1096 0.1859 0.1987 0.0263  0.0850  -0.0082 103 GLN A NE2 
1113 N  NE2 B GLN A 103 ? 0.1637 0.1561 0.1737 0.0414  0.0531  0.0315  103 GLN A NE2 
1114 N  N   . GLY A 104 ? 0.0966 0.0700 0.0949 0.0132  0.0270  0.0019  104 GLY A N   
1115 C  CA  . GLY A 104 ? 0.1221 0.0763 0.0728 0.0024  0.0136  -0.0096 104 GLY A CA  
1116 C  C   . GLY A 104 ? 0.0942 0.0706 0.0750 -0.0024 0.0076  -0.0082 104 GLY A C   
1117 O  O   . GLY A 104 ? 0.1071 0.0856 0.0744 -0.0131 0.0126  -0.0040 104 GLY A O   
1118 N  N   . SER A 105 ? 0.0829 0.0737 0.0678 0.0052  0.0054  -0.0040 105 SER A N   
1119 C  CA  . SER A 105 ? 0.0781 0.0802 0.0587 0.0063  0.0071  -0.0142 105 SER A CA  
1120 C  C   . SER A 105 ? 0.0667 0.0705 0.0671 0.0007  0.0210  0.0006  105 SER A C   
1121 O  O   . SER A 105 ? 0.0815 0.0811 0.0900 0.0087  -0.0073 -0.0114 105 SER A O   
1122 C  CB  . SER A 105 ? 0.1003 0.0706 0.0856 -0.0012 0.0147  0.0088  105 SER A CB  
1123 O  OG  . SER A 105 ? 0.1012 0.0666 0.0868 0.0035  0.0187  0.0070  105 SER A OG  
1124 N  N   . GLU A 106 ? 0.0888 0.0622 0.0516 -0.0070 0.0142  -0.0077 106 GLU A N   
1125 C  CA  . GLU A 106 ? 0.0985 0.0652 0.0643 -0.0012 -0.0023 -0.0135 106 GLU A CA  
1126 C  C   . GLU A 106 ? 0.0864 0.0546 0.0724 -0.0031 -0.0035 -0.0087 106 GLU A C   
1127 O  O   . GLU A 106 ? 0.0869 0.0715 0.0847 0.0027  0.0024  0.0000  106 GLU A O   
1128 C  CB  . GLU A 106 ? 0.0988 0.0665 0.0649 -0.0052 0.0068  -0.0074 106 GLU A CB  
1129 C  CG  . GLU A 106 ? 0.1272 0.0890 0.0710 -0.0189 0.0275  -0.0092 106 GLU A CG  
1130 C  CD  . GLU A 106 ? 0.0888 0.0807 0.0631 0.0076  0.0136  -0.0098 106 GLU A CD  
1131 O  OE1 . GLU A 106 ? 0.0811 0.0736 0.0926 -0.0068 0.0142  -0.0076 106 GLU A OE1 
1132 O  OE2 . GLU A 106 ? 0.0909 0.0890 0.1012 -0.0013 0.0167  -0.0093 106 GLU A OE2 
1133 N  N   . HIS A 107 ? 0.0882 0.0706 0.0644 0.0038  0.0151  -0.0005 107 HIS A N   
1134 C  CA  . HIS A 107 ? 0.0781 0.0662 0.0582 0.0000  0.0153  -0.0068 107 HIS A CA  
1135 C  C   . HIS A 107 ? 0.0746 0.0869 0.0731 0.0092  -0.0003 -0.0076 107 HIS A C   
1136 O  O   . HIS A 107 ? 0.1021 0.0693 0.0627 0.0013  0.0093  0.0057  107 HIS A O   
1137 C  CB  . HIS A 107 ? 0.0865 0.0689 0.0802 0.0071  0.0222  -0.0041 107 HIS A CB  
1138 C  CG  . HIS A 107 ? 0.0636 0.0737 0.0671 0.0140  0.0119  -0.0024 107 HIS A CG  
1139 N  ND1 . HIS A 107 ? 0.0886 0.0608 0.0697 0.0082  0.0175  0.0082  107 HIS A ND1 
1140 C  CD2 . HIS A 107 ? 0.0687 0.0755 0.0811 0.0265  0.0023  -0.0068 107 HIS A CD2 
1141 C  CE1 . HIS A 107 ? 0.0847 0.0737 0.0727 0.0099  0.0062  -0.0135 107 HIS A CE1 
1142 N  NE2 . HIS A 107 ? 0.0635 0.0693 0.0754 0.0126  -0.0038 -0.0167 107 HIS A NE2 
1143 N  N   . THR A 108 ? 0.0920 0.0697 0.0696 0.0120  0.0024  0.0043  108 THR A N   
1144 C  CA  . THR A 108 ? 0.1003 0.0615 0.0758 0.0098  0.0126  0.0030  108 THR A CA  
1145 C  C   . THR A 108 ? 0.1061 0.0749 0.0627 0.0026  -0.0027 0.0007  108 THR A C   
1146 O  O   . THR A 108 ? 0.1136 0.0785 0.0687 0.0082  0.0052  0.0020  108 THR A O   
1147 C  CB  . THR A 108 ? 0.1066 0.0825 0.0940 0.0120  -0.0013 -0.0153 108 THR A CB  
1148 O  OG1 . THR A 108 ? 0.1159 0.0798 0.0987 0.0181  -0.0027 0.0027  108 THR A OG1 
1149 C  CG2 . THR A 108 ? 0.1176 0.1111 0.1118 0.0296  0.0177  0.0000  108 THR A CG2 
1150 N  N   . VAL A 109 ? 0.1254 0.0780 0.0815 0.0019  0.0274  0.0199  109 VAL A N   
1151 C  CA  . VAL A 109 ? 0.1105 0.1001 0.0982 -0.0006 0.0318  0.0375  109 VAL A CA  
1152 C  C   . VAL A 109 ? 0.1367 0.0899 0.0803 0.0098  0.0377  0.0114  109 VAL A C   
1153 O  O   . VAL A 109 ? 0.1295 0.0922 0.1032 0.0054  0.0162  0.0129  109 VAL A O   
1154 C  CB  . VAL A 109 ? 0.1436 0.1030 0.0978 -0.0003 0.0192  0.0209  109 VAL A CB  
1155 C  CG1 . VAL A 109 ? 0.1296 0.1380 0.1353 0.0035  0.0262  0.0447  109 VAL A CG1 
1156 C  CG2 . VAL A 109 ? 0.1355 0.1010 0.0985 0.0102  0.0132  0.0197  109 VAL A CG2 
1157 N  N   . ASP A 110 ? 0.1474 0.0930 0.0781 0.0219  0.0248  0.0307  110 ASP A N   
1158 C  CA  . ASP A 110 ? 0.1775 0.0913 0.0906 0.0204  0.0214  0.0384  110 ASP A CA  
1159 C  C   . ASP A 110 ? 0.1674 0.0897 0.1005 0.0230  0.0211  0.0164  110 ASP A C   
1160 O  O   . ASP A 110 ? 0.1966 0.0926 0.0974 0.0228  0.0221  0.0262  110 ASP A O   
1161 C  CB  . ASP A 110 ? 0.1911 0.1088 0.1263 0.0292  0.0452  0.0452  110 ASP A CB  
1162 C  CG  . ASP A 110 ? 0.1657 0.1274 0.1057 -0.0074 0.0313  0.0445  110 ASP A CG  
1163 O  OD1 . ASP A 110 ? 0.2100 0.1177 0.1240 0.0054  0.0306  0.0326  110 ASP A OD1 
1164 O  OD2 . ASP A 110 ? 0.1757 0.1716 0.1393 0.0013  0.0408  0.0199  110 ASP A OD2 
1165 N  N   . LYS A 111 ? 0.1339 0.0992 0.0924 0.0204  0.0046  0.0237  111 LYS A N   
1166 C  CA  . LYS A 111 ? 0.1340 0.1238 0.1229 0.0315  0.0000  0.0027  111 LYS A CA  
1167 C  C   . LYS A 111 ? 0.1659 0.1014 0.0969 0.0269  0.0135  0.0027  111 LYS A C   
1168 O  O   . LYS A 111 ? 0.1511 0.1254 0.1297 0.0381  0.0043  -0.0054 111 LYS A O   
1169 C  CB  . LYS A 111 ? 0.1917 0.1129 0.1238 0.0644  0.0068  0.0175  111 LYS A CB  
1170 C  CG  . LYS A 111 ? 0.2163 0.2046 0.1283 0.0948  -0.0211 0.0147  111 LYS A CG  
1171 C  CD  . LYS A 111 ? 0.2725 0.1732 0.2111 0.0732  -0.0220 -0.0130 111 LYS A CD  
1172 C  CE  . LYS A 111 ? 0.2429 0.3127 0.2405 0.0476  -0.0706 0.0068  111 LYS A CE  
1173 N  NZ  . LYS A 111 ? 0.2100 0.2614 0.3533 0.0293  -0.0230 0.0636  111 LYS A NZ  
1174 N  N   . LYS A 112 ? 0.1595 0.0811 0.0917 0.0175  0.0063  0.0148  112 LYS A N   
1175 C  CA  . LYS A 112 ? 0.1492 0.1163 0.0854 -0.0027 0.0052  0.0076  112 LYS A CA  
1176 C  C   . LYS A 112 ? 0.1186 0.0818 0.0886 0.0148  -0.0098 0.0054  112 LYS A C   
1177 O  O   . LYS A 112 ? 0.1075 0.0807 0.0944 0.0121  0.0057  -0.0013 112 LYS A O   
1178 C  CB  . LYS A 112 ? 0.1635 0.1324 0.1145 -0.0253 0.0175  -0.0085 112 LYS A CB  
1179 C  CG  . LYS A 112 ? 0.1561 0.1614 0.1385 -0.0280 0.0167  -0.0414 112 LYS A CG  
1180 C  CD  . LYS A 112 ? 0.1766 0.2023 0.1804 -0.0071 -0.0219 -0.0131 112 LYS A CD  
1181 C  CE  . LYS A 112 ? 0.1782 0.2050 0.1815 0.0195  -0.0054 -0.0107 112 LYS A CE  
1182 N  NZ  . LYS A 112 ? 0.2384 0.1762 0.2141 0.0142  -0.0649 0.0141  112 LYS A NZ  
1183 N  N   A LYS A 113 ? 0.1132 0.0960 0.0944 0.0264  -0.0010 0.0071  113 LYS A N   
1184 N  N   B LYS A 113 ? 0.1145 0.0915 0.0920 0.0296  0.0005  0.0124  113 LYS A N   
1185 C  CA  A LYS A 113 ? 0.1252 0.0790 0.1152 0.0000  0.0031  0.0130  113 LYS A CA  
1186 C  CA  B LYS A 113 ? 0.1097 0.1057 0.0969 0.0140  0.0102  0.0167  113 LYS A CA  
1187 C  C   A LYS A 113 ? 0.1150 0.0674 0.1005 0.0068  0.0251  0.0063  113 LYS A C   
1188 C  C   B LYS A 113 ? 0.1199 0.0829 0.0908 0.0254  0.0186  -0.0020 113 LYS A C   
1189 O  O   A LYS A 113 ? 0.1208 0.0630 0.1411 0.0020  0.0005  0.0126  113 LYS A O   
1190 O  O   B LYS A 113 ? 0.1477 0.0827 0.0772 0.0115  0.0231  -0.0114 113 LYS A O   
1191 C  CB  A LYS A 113 ? 0.1215 0.1014 0.1032 0.0103  0.0030  -0.0013 113 LYS A CB  
1192 C  CB  B LYS A 113 ? 0.1177 0.1341 0.0809 0.0281  0.0195  -0.0184 113 LYS A CB  
1193 C  CG  A LYS A 113 ? 0.1017 0.0829 0.1364 0.0027  0.0087  -0.0136 113 LYS A CG  
1194 C  CG  B LYS A 113 ? 0.1208 0.1571 0.1044 0.0328  0.0003  -0.0098 113 LYS A CG  
1195 C  CD  A LYS A 113 ? 0.1256 0.1064 0.1242 0.0254  0.0230  -0.0146 113 LYS A CD  
1196 C  CD  B LYS A 113 ? 0.0684 0.1917 0.1098 0.0104  0.0043  0.0381  113 LYS A CD  
1197 C  CE  A LYS A 113 ? 0.1299 0.1835 0.0829 0.0120  0.0260  -0.0178 113 LYS A CE  
1198 C  CE  B LYS A 113 ? 0.0921 0.2020 0.1620 0.0175  -0.0359 0.0164  113 LYS A CE  
1199 N  NZ  A LYS A 113 ? 0.1341 0.0974 0.1727 0.0226  -0.0298 0.0126  113 LYS A NZ  
1200 N  NZ  B LYS A 113 ? 0.1256 0.1407 0.2452 -0.0023 0.0082  -0.0320 113 LYS A NZ  
1201 N  N   . TYR A 114 ? 0.1012 0.0776 0.0922 0.0035  0.0093  0.0085  114 TYR A N   
1202 C  CA  . TYR A 114 ? 0.1032 0.0754 0.1048 -0.0003 0.0006  0.0071  114 TYR A CA  
1203 C  C   . TYR A 114 ? 0.1137 0.0511 0.1076 -0.0137 0.0063  -0.0048 114 TYR A C   
1204 O  O   . TYR A 114 ? 0.1136 0.0697 0.1023 -0.0073 0.0255  0.0060  114 TYR A O   
1205 C  CB  . TYR A 114 ? 0.1045 0.0711 0.1084 0.0063  0.0120  0.0171  114 TYR A CB  
1206 C  CG  . TYR A 114 ? 0.1150 0.0684 0.1005 -0.0023 -0.0027 0.0015  114 TYR A CG  
1207 C  CD1 . TYR A 114 ? 0.1507 0.0772 0.0996 0.0233  0.0048  0.0097  114 TYR A CD1 
1208 C  CD2 . TYR A 114 ? 0.1252 0.0658 0.1455 -0.0043 0.0295  0.0115  114 TYR A CD2 
1209 C  CE1 . TYR A 114 ? 0.1942 0.1371 0.0886 0.0427  0.0193  0.0052  114 TYR A CE1 
1210 C  CE2 . TYR A 114 ? 0.1463 0.1161 0.1782 0.0010  0.0597  0.0175  114 TYR A CE2 
1211 C  CZ  . TYR A 114 ? 0.1726 0.1461 0.1386 0.0175  0.0465  0.0306  114 TYR A CZ  
1212 O  OH  . TYR A 114 ? 0.2669 0.2132 0.1764 0.0417  0.1093  0.0456  114 TYR A OH  
1213 N  N   . ALA A 115 ? 0.1136 0.0590 0.1026 -0.0115 -0.0003 -0.0017 115 ALA A N   
1214 C  CA  . ALA A 115 ? 0.1044 0.0588 0.1091 -0.0077 0.0051  -0.0120 115 ALA A CA  
1215 C  C   . ALA A 115 ? 0.1044 0.0653 0.0863 0.0026  0.0071  0.0020  115 ALA A C   
1216 O  O   . ALA A 115 ? 0.1154 0.0741 0.1014 -0.0068 0.0104  -0.0020 115 ALA A O   
1217 C  CB  . ALA A 115 ? 0.1518 0.0697 0.1076 -0.0153 -0.0120 -0.0104 115 ALA A CB  
1218 N  N   . ALA A 116 ? 0.1127 0.0597 0.0762 -0.0017 0.0046  -0.0005 116 ALA A N   
1219 C  CA  . ALA A 116 ? 0.1173 0.0592 0.0777 -0.0038 0.0000  0.0005  116 ALA A CA  
1220 C  C   . ALA A 116 ? 0.0807 0.0630 0.0785 -0.0006 -0.0040 0.0012  116 ALA A C   
1221 O  O   . ALA A 116 ? 0.0983 0.0702 0.0809 -0.0107 0.0020  0.0054  116 ALA A O   
1222 C  CB  . ALA A 116 ? 0.1161 0.0856 0.0825 -0.0065 -0.0035 -0.0037 116 ALA A CB  
1223 N  N   . GLU A 117 ? 0.1021 0.0573 0.0798 -0.0015 0.0114  0.0000  117 GLU A N   
1224 C  CA  . GLU A 117 ? 0.1249 0.0581 0.0562 -0.0104 0.0043  -0.0054 117 GLU A CA  
1225 C  C   . GLU A 117 ? 0.1057 0.0667 0.0613 -0.0120 0.0082  -0.0020 117 GLU A C   
1226 O  O   . GLU A 117 ? 0.1010 0.0740 0.0897 -0.0048 0.0172  0.0164  117 GLU A O   
1227 C  CB  . GLU A 117 ? 0.0904 0.0785 0.0582 0.0007  0.0065  -0.0010 117 GLU A CB  
1228 C  CG  . GLU A 117 ? 0.0933 0.0899 0.0573 0.0131  0.0031  0.0017  117 GLU A CG  
1229 C  CD  . GLU A 117 ? 0.0908 0.0697 0.0634 0.0052  0.0098  0.0054  117 GLU A CD  
1230 O  OE1 . GLU A 117 ? 0.0872 0.0886 0.0741 0.0041  -0.0035 0.0013  117 GLU A OE1 
1231 O  OE2 . GLU A 117 ? 0.1146 0.0793 0.0640 0.0000  -0.0110 0.0003  117 GLU A OE2 
1232 N  N   . LEU A 118 ? 0.1026 0.0535 0.0798 0.0012  -0.0038 -0.0010 118 LEU A N   
1233 C  CA  . LEU A 118 ? 0.1023 0.0553 0.0684 -0.0068 -0.0013 0.0071  118 LEU A CA  
1234 C  C   . LEU A 118 ? 0.1021 0.0529 0.0542 -0.0003 -0.0051 0.0063  118 LEU A C   
1235 O  O   . LEU A 118 ? 0.1149 0.0671 0.0579 -0.0137 -0.0034 0.0027  118 LEU A O   
1236 C  CB  . LEU A 118 ? 0.1208 0.0718 0.0827 -0.0137 -0.0170 0.0200  118 LEU A CB  
1237 C  CG  . LEU A 118 ? 0.1383 0.0794 0.0881 -0.0026 -0.0165 0.0093  118 LEU A CG  
1238 C  CD1 . LEU A 118 ? 0.1545 0.0759 0.0987 -0.0006 -0.0305 0.0326  118 LEU A CD1 
1239 C  CD2 . LEU A 118 ? 0.1298 0.1206 0.1048 -0.0130 -0.0447 0.0120  118 LEU A CD2 
1240 N  N   . HIS A 119 ? 0.1124 0.0441 0.0608 -0.0092 -0.0052 -0.0019 119 HIS A N   
1241 C  CA  . HIS A 119 ? 0.1037 0.0456 0.0606 -0.0088 -0.0015 0.0041  119 HIS A CA  
1242 C  C   . HIS A 119 ? 0.0926 0.0555 0.0604 -0.0115 -0.0119 0.0026  119 HIS A C   
1243 O  O   . HIS A 119 ? 0.1173 0.0639 0.0604 -0.0109 -0.0026 0.0034  119 HIS A O   
1244 C  CB  . HIS A 119 ? 0.0992 0.0768 0.0767 0.0006  0.0115  0.0108  119 HIS A CB  
1245 C  CG  . HIS A 119 ? 0.1009 0.0662 0.0615 -0.0063 0.0046  -0.0131 119 HIS A CG  
1246 N  ND1 . HIS A 119 ? 0.0888 0.0737 0.0658 -0.0175 0.0135  -0.0043 119 HIS A ND1 
1247 C  CD2 . HIS A 119 ? 0.1167 0.0627 0.0640 0.0099  0.0043  -0.0087 119 HIS A CD2 
1248 C  CE1 . HIS A 119 ? 0.0983 0.0838 0.0524 -0.0031 -0.0071 -0.0096 119 HIS A CE1 
1249 N  NE2 . HIS A 119 ? 0.0960 0.0718 0.0776 0.0143  0.0114  -0.0065 119 HIS A NE2 
1250 N  N   . LEU A 120 ? 0.0900 0.0562 0.0755 0.0013  -0.0110 0.0000  120 LEU A N   
1251 C  CA  . LEU A 120 ? 0.1181 0.0570 0.0847 0.0065  -0.0086 -0.0012 120 LEU A CA  
1252 C  C   . LEU A 120 ? 0.1100 0.0500 0.0768 0.0131  -0.0048 0.0065  120 LEU A C   
1253 O  O   . LEU A 120 ? 0.1109 0.0662 0.0697 -0.0030 -0.0109 0.0027  120 LEU A O   
1254 C  CB  . LEU A 120 ? 0.1150 0.0807 0.0870 -0.0096 -0.0291 0.0052  120 LEU A CB  
1255 C  CG  . LEU A 120 ? 0.1265 0.0881 0.1120 -0.0177 -0.0406 0.0093  120 LEU A CG  
1256 C  CD1 . LEU A 120 ? 0.1971 0.1215 0.1347 -0.0842 -0.0124 -0.0031 120 LEU A CD1 
1257 C  CD2 . LEU A 120 ? 0.1856 0.1231 0.1394 -0.0024 -0.0788 0.0020  120 LEU A CD2 
1258 N  N   . VAL A 121 ? 0.1082 0.0625 0.0802 -0.0043 0.0000  0.0093  121 VAL A N   
1259 C  CA  . VAL A 121 ? 0.1243 0.0605 0.0965 -0.0104 -0.0031 0.0087  121 VAL A CA  
1260 C  C   . VAL A 121 ? 0.1048 0.0745 0.1014 -0.0164 -0.0110 0.0000  121 VAL A C   
1261 O  O   . VAL A 121 ? 0.1691 0.0665 0.0903 -0.0015 -0.0130 0.0038  121 VAL A O   
1262 C  CB  . VAL A 121 ? 0.1326 0.0626 0.0961 0.0024  -0.0020 0.0063  121 VAL A CB  
1263 C  CG1 . VAL A 121 ? 0.1371 0.0856 0.1066 -0.0097 0.0048  -0.0063 121 VAL A CG1 
1264 C  CG2 . VAL A 121 ? 0.1359 0.0881 0.1009 0.0162  0.0005  0.0076  121 VAL A CG2 
1265 N  N   . HIS A 122 ? 0.1057 0.0671 0.0904 -0.0093 -0.0104 0.0071  122 HIS A N   
1266 C  CA  . HIS A 122 ? 0.1285 0.0588 0.0953 -0.0020 -0.0126 -0.0046 122 HIS A CA  
1267 C  C   . HIS A 122 ? 0.0983 0.0719 0.1062 0.0020  -0.0160 0.0000  122 HIS A C   
1268 O  O   . HIS A 122 ? 0.1124 0.0710 0.1053 -0.0120 -0.0172 0.0024  122 HIS A O   
1269 C  CB  . HIS A 122 ? 0.1001 0.0520 0.1276 0.0109  -0.0211 0.0073  122 HIS A CB  
1270 C  CG  . HIS A 122 ? 0.1128 0.0670 0.1177 0.0065  -0.0153 -0.0102 122 HIS A CG  
1271 N  ND1 . HIS A 122 ? 0.0978 0.0648 0.1240 -0.0015 0.0071  0.0006  122 HIS A ND1 
1272 C  CD2 . HIS A 122 ? 0.1134 0.1066 0.1427 -0.0076 -0.0252 0.0063  122 HIS A CD2 
1273 C  CE1 . HIS A 122 ? 0.0935 0.1120 0.1389 -0.0080 -0.0017 0.0030  122 HIS A CE1 
1274 N  NE2 . HIS A 122 ? 0.1019 0.1096 0.1369 -0.0225 -0.0299 0.0037  122 HIS A NE2 
1275 N  N   . TRP A 123 ? 0.1055 0.0627 0.1073 0.0030  -0.0164 -0.0020 123 TRP A N   
1276 C  CA  . TRP A 123 ? 0.1075 0.0648 0.1217 -0.0142 0.0041  -0.0108 123 TRP A CA  
1277 C  C   . TRP A 123 ? 0.1048 0.0648 0.1173 0.0082  -0.0238 -0.0006 123 TRP A C   
1278 O  O   . TRP A 123 ? 0.0967 0.0745 0.1428 0.0010  -0.0200 -0.0074 123 TRP A O   
1279 C  CB  . TRP A 123 ? 0.1297 0.1326 0.1301 -0.0187 0.0186  -0.0015 123 TRP A CB  
1280 C  CG  . TRP A 123 ? 0.1845 0.0847 0.1536 -0.0375 0.0057  -0.0017 123 TRP A CG  
1281 C  CD1 . TRP A 123 ? 0.2360 0.1252 0.1143 -0.0639 0.0131  0.0175  123 TRP A CD1 
1282 C  CD2 . TRP A 123 ? 0.1844 0.0843 0.1346 -0.0309 0.0104  0.0199  123 TRP A CD2 
1283 N  NE1 . TRP A 123 ? 0.3023 0.0877 0.1540 -0.0631 -0.0135 0.0043  123 TRP A NE1 
1284 C  CE2 . TRP A 123 ? 0.2809 0.0715 0.1658 -0.0693 -0.0192 0.0273  123 TRP A CE2 
1285 C  CE3 . TRP A 123 ? 0.1744 0.0715 0.2118 -0.0381 -0.0137 0.0015  123 TRP A CE3 
1286 C  CZ2 . TRP A 123 ? 0.2327 0.0864 0.2102 -0.0612 -0.0353 0.0243  123 TRP A CZ2 
1287 C  CZ3 . TRP A 123 ? 0.2445 0.0746 0.2096 -0.0340 -0.0200 -0.0186 123 TRP A CZ3 
1288 C  CH2 . TRP A 123 ? 0.2964 0.0877 0.2090 -0.0623 -0.0460 0.0074  123 TRP A CH2 
1289 N  N   . ASN A 124 ? 0.1115 0.0727 0.1046 0.0020  0.0003  -0.0178 124 ASN A N   
1290 C  CA  . ASN A 124 ? 0.1170 0.0776 0.1332 0.0019  0.0059  -0.0276 124 ASN A CA  
1291 C  C   . ASN A 124 ? 0.1039 0.0746 0.1544 0.0017  -0.0041 -0.0340 124 ASN A C   
1292 O  O   . ASN A 124 ? 0.1071 0.0702 0.1389 0.0074  -0.0031 -0.0197 124 ASN A O   
1293 C  CB  . ASN A 124 ? 0.1331 0.0906 0.1202 -0.0109 0.0211  -0.0337 124 ASN A CB  
1294 C  CG  . ASN A 124 ? 0.1319 0.0940 0.1407 -0.0114 0.0115  -0.0244 124 ASN A CG  
1295 O  OD1 . ASN A 124 ? 0.1412 0.1010 0.1723 0.0136  0.0183  -0.0340 124 ASN A OD1 
1296 N  ND2 . ASN A 124 ? 0.1515 0.1080 0.1396 0.0034  0.0164  -0.0438 124 ASN A ND2 
1297 N  N   A THR A 125 ? 0.1299 0.0500 0.1703 0.0253  0.0126  -0.0115 125 THR A N   
1298 N  N   B THR A 125 ? 0.1111 0.0833 0.1750 0.0092  -0.0041 -0.0329 125 THR A N   
1299 C  CA  A THR A 125 ? 0.1554 0.0573 0.2251 -0.0005 0.0130  0.0161  125 THR A CA  
1300 C  CA  B THR A 125 ? 0.1177 0.0781 0.1903 0.0085  0.0052  -0.0263 125 THR A CA  
1301 C  C   A THR A 125 ? 0.1080 0.0807 0.1644 0.0097  0.0186  0.0274  125 THR A C   
1302 C  C   B THR A 125 ? 0.1098 0.0771 0.1725 0.0185  0.0087  -0.0205 125 THR A C   
1303 O  O   A THR A 125 ? 0.1588 0.0931 0.1969 0.0419  0.0524  0.0522  125 THR A O   
1304 O  O   B THR A 125 ? 0.1184 0.0938 0.1985 0.0264  0.0102  -0.0082 125 THR A O   
1305 C  CB  A THR A 125 ? 0.1438 0.1495 0.1777 -0.0303 0.0291  0.0428  125 THR A CB  
1306 C  CB  B THR A 125 ? 0.1204 0.1188 0.1568 -0.0197 -0.0051 -0.0088 125 THR A CB  
1307 O  OG1 A THR A 125 ? 0.1283 0.1344 0.1949 0.0065  0.0355  -0.0017 125 THR A OG1 
1308 O  OG1 B THR A 125 ? 0.1462 0.1091 0.1391 0.0392  -0.0006 0.0007  125 THR A OG1 
1309 C  CG2 A THR A 125 ? 0.1820 0.1594 0.2469 0.0160  -0.0790 0.0373  125 THR A CG2 
1310 C  CG2 B THR A 125 ? 0.1524 0.1172 0.1714 -0.0147 -0.0649 0.0013  125 THR A CG2 
1311 N  N   A LYS A 126 ? 0.1206 0.1005 0.1653 0.0159  0.0476  -0.0173 126 LYS A N   
1312 N  N   B LYS A 126 ? 0.1412 0.0697 0.1728 -0.0155 0.0023  -0.0368 126 LYS A N   
1313 C  CA  A LYS A 126 ? 0.1727 0.1335 0.2247 -0.0357 0.0458  -0.0324 126 LYS A CA  
1314 C  CA  B LYS A 126 ? 0.1687 0.0573 0.2122 -0.0186 0.0403  -0.0635 126 LYS A CA  
1315 C  C   A LYS A 126 ? 0.1766 0.0815 0.1985 -0.0432 0.0364  -0.0230 126 LYS A C   
1316 C  C   B LYS A 126 ? 0.1526 0.0606 0.2204 -0.0046 0.0274  -0.0529 126 LYS A C   
1317 O  O   A LYS A 126 ? 0.2226 0.0597 0.0845 -0.0241 0.0366  -0.0049 126 LYS A O   
1318 O  O   B LYS A 126 ? 0.1624 0.0706 0.1856 -0.0160 0.0071  -0.0215 126 LYS A O   
1319 C  CB  A LYS A 126 ? 0.2442 0.1820 0.2269 0.0412  0.0146  -0.0093 126 LYS A CB  
1320 C  CB  B LYS A 126 ? 0.2036 0.1326 0.2016 -0.0326 -0.0381 -0.1052 126 LYS A CB  
1321 C  CG  A LYS A 126 ? 0.1176 0.1574 0.1899 -0.0270 0.0342  -0.0120 126 LYS A CG  
1322 C  CG  B LYS A 126 ? 0.2115 0.1606 0.1978 0.0232  0.0571  -0.0794 126 LYS A CG  
1323 C  CD  A LYS A 126 ? 0.2005 0.2833 0.1888 -0.0185 0.0531  -0.0434 126 LYS A CD  
1324 C  CD  B LYS A 126 ? 0.3481 0.3152 0.1513 0.0087  0.0951  -0.1247 126 LYS A CD  
1325 C  CE  A LYS A 126 ? 0.2384 0.1644 0.2432 0.0152  0.0294  -0.0788 126 LYS A CE  
1326 C  CE  B LYS A 126 ? 0.5156 0.2127 0.2113 -0.0847 0.0693  -0.0593 126 LYS A CE  
1327 N  NZ  A LYS A 126 ? 0.2662 0.2797 0.2730 0.0258  0.0428  -0.0160 126 LYS A NZ  
1328 N  NZ  B LYS A 126 ? 0.3691 0.4099 0.3125 0.0070  0.1297  -0.0447 126 LYS A NZ  
1329 N  N   A TYR A 127 ? 0.1314 0.0811 0.1635 -0.0104 0.0040  -0.0020 127 TYR A N   
1330 N  N   B TYR A 127 ? 0.1243 0.0543 0.1581 -0.0027 0.0034  -0.0386 127 TYR A N   
1331 C  CA  A TYR A 127 ? 0.1271 0.0719 0.1823 -0.0208 0.0104  -0.0183 127 TYR A CA  
1332 C  CA  B TYR A 127 ? 0.0958 0.0885 0.1923 0.0035  -0.0292 -0.0109 127 TYR A CA  
1333 C  C   A TYR A 127 ? 0.1398 0.0776 0.1646 -0.0024 0.0184  -0.0445 127 TYR A C   
1334 C  C   B TYR A 127 ? 0.1499 0.0684 0.1759 0.0082  0.0063  -0.0410 127 TYR A C   
1335 O  O   A TYR A 127 ? 0.1473 0.1037 0.1098 -0.0185 -0.0035 0.0040  127 TYR A O   
1336 O  O   B TYR A 127 ? 0.1488 0.0608 0.1921 -0.0051 0.0057  -0.0520 127 TYR A O   
1337 C  CB  A TYR A 127 ? 0.0897 0.1023 0.1554 -0.0091 0.0471  -0.0017 127 TYR A CB  
1338 C  CB  B TYR A 127 ? 0.1536 0.0503 0.1651 0.0142  0.0006  -0.0273 127 TYR A CB  
1339 C  CG  A TYR A 127 ? 0.1093 0.0644 0.1518 0.0034  0.0164  0.0043  127 TYR A CG  
1340 C  CG  B TYR A 127 ? 0.1009 0.0983 0.1554 -0.0199 0.0186  -0.0253 127 TYR A CG  
1341 C  CD1 A TYR A 127 ? 0.1193 0.0582 0.1553 0.0019  0.0164  -0.0031 127 TYR A CD1 
1342 C  CD1 B TYR A 127 ? 0.1308 0.1057 0.1601 -0.0337 -0.0219 -0.0163 127 TYR A CD1 
1343 C  CD2 A TYR A 127 ? 0.1435 0.0732 0.1459 -0.0076 0.0340  0.0155  127 TYR A CD2 
1344 C  CD2 B TYR A 127 ? 0.1118 0.0863 0.1759 -0.0088 0.0096  -0.0186 127 TYR A CD2 
1345 C  CE1 A TYR A 127 ? 0.1242 0.0957 0.1411 0.0048  0.0412  -0.0209 127 TYR A CE1 
1346 C  CE1 B TYR A 127 ? 0.0803 0.1114 0.1545 -0.0255 -0.0109 -0.0041 127 TYR A CE1 
1347 C  CE2 A TYR A 127 ? 0.1269 0.1234 0.1172 -0.0043 0.0353  -0.0183 127 TYR A CE2 
1348 C  CE2 B TYR A 127 ? 0.1508 0.0437 0.1732 -0.0161 -0.0006 -0.0013 127 TYR A CE2 
1349 C  CZ  A TYR A 127 ? 0.1366 0.1181 0.1118 -0.0043 0.0170  0.0027  127 TYR A CZ  
1350 C  CZ  B TYR A 127 ? 0.1766 0.0868 0.1653 -0.0068 0.0076  -0.0231 127 TYR A CZ  
1351 O  OH  A TYR A 127 ? 0.2041 0.1395 0.0969 0.0130  0.0271  0.0000  127 TYR A OH  
1352 O  OH  B TYR A 127 ? 0.1996 0.0706 0.1714 -0.0124 -0.0035 -0.0175 127 TYR A OH  
1353 N  N   . GLY A 128 ? 0.1718 0.0798 0.1674 0.0007  -0.0131 -0.0086 128 GLY A N   
1354 C  CA  . GLY A 128 ? 0.1484 0.1036 0.1698 -0.0155 -0.0167 -0.0104 128 GLY A CA  
1355 C  C   . GLY A 128 ? 0.1811 0.0949 0.1356 -0.0187 -0.0233 0.0154  128 GLY A C   
1356 O  O   . GLY A 128 ? 0.1851 0.0886 0.1500 -0.0174 -0.0232 0.0222  128 GLY A O   
1357 N  N   . ASP A 129 ? 0.1728 0.0856 0.1629 0.0046  -0.0109 -0.0082 129 ASP A N   
1358 C  CA  . ASP A 129 ? 0.2197 0.0970 0.1432 0.0114  0.0031  0.0024  129 ASP A CA  
1359 C  C   . ASP A 129 ? 0.1615 0.0834 0.1314 -0.0076 -0.0185 -0.0118 129 ASP A C   
1360 O  O   . ASP A 129 ? 0.1836 0.0879 0.1233 0.0051  -0.0239 -0.0170 129 ASP A O   
1361 C  CB  . ASP A 129 ? 0.1802 0.1145 0.1378 -0.0010 -0.0177 0.0070  129 ASP A CB  
1362 C  CG  . ASP A 129 ? 0.1770 0.0974 0.1491 0.0102  -0.0024 -0.0098 129 ASP A CG  
1363 O  OD1 . ASP A 129 ? 0.1980 0.1418 0.1865 0.0121  0.0160  0.0227  129 ASP A OD1 
1364 O  OD2 . ASP A 129 ? 0.1594 0.1332 0.2791 0.0109  -0.0153 0.0346  129 ASP A OD2 
1365 N  N   . VAL A 130 ? 0.1881 0.0852 0.1462 -0.0043 -0.0148 -0.0281 130 VAL A N   
1366 C  CA  . VAL A 130 ? 0.1894 0.0861 0.1176 0.0027  0.0015  -0.0163 130 VAL A CA  
1367 C  C   . VAL A 130 ? 0.1973 0.0886 0.1012 -0.0035 0.0035  -0.0262 130 VAL A C   
1368 O  O   . VAL A 130 ? 0.1612 0.1172 0.0897 -0.0115 0.0020  -0.0070 130 VAL A O   
1369 C  CB  . VAL A 130 ? 0.2052 0.0978 0.1525 0.0165  -0.0187 -0.0544 130 VAL A CB  
1370 C  CG1 . VAL A 130 ? 0.2858 0.1492 0.1438 -0.0617 -0.0030 -0.0164 130 VAL A CG1 
1371 C  CG2 . VAL A 130 ? 0.2481 0.0881 0.1879 -0.0057 -0.0239 -0.0427 130 VAL A CG2 
1372 N  N   . GLY A 131 ? 0.1699 0.1075 0.1199 -0.0034 0.0000  -0.0076 131 GLY A N   
1373 C  CA  . GLY A 131 ? 0.1748 0.1490 0.1344 -0.0136 0.0093  0.0035  131 GLY A CA  
1374 C  C   . GLY A 131 ? 0.1204 0.1136 0.1368 -0.0091 0.0063  0.0082  131 GLY A C   
1375 O  O   . GLY A 131 ? 0.1411 0.1272 0.1554 0.0031  0.0031  -0.0057 131 GLY A O   
1376 N  N   . LYS A 132 ? 0.1511 0.1012 0.1262 -0.0175 0.0000  0.0109  132 LYS A N   
1377 C  CA  . LYS A 132 ? 0.1398 0.0882 0.1253 -0.0210 -0.0140 0.0109  132 LYS A CA  
1378 C  C   . LYS A 132 ? 0.1286 0.0863 0.1014 -0.0164 -0.0074 -0.0043 132 LYS A C   
1379 O  O   . LYS A 132 ? 0.1360 0.0885 0.1118 -0.0237 -0.0065 -0.0015 132 LYS A O   
1380 C  CB  . LYS A 132 ? 0.1743 0.0807 0.1375 -0.0073 -0.0126 -0.0102 132 LYS A CB  
1381 C  CG  . LYS A 132 ? 0.2120 0.1026 0.2167 -0.0483 -0.0423 0.0156  132 LYS A CG  
1382 C  CD  . LYS A 132 ? 0.1826 0.1328 0.3190 -0.0513 -0.0359 0.0236  132 LYS A CD  
1383 C  CE  . LYS A 132 ? 0.2509 0.1919 0.2301 -0.0882 -0.0082 0.0265  132 LYS A CE  
1384 N  NZ  . LYS A 132 ? 0.3628 0.2386 0.3079 -0.0759 0.0280  0.0187  132 LYS A NZ  
1385 N  N   . ALA A 133 ? 0.1398 0.0715 0.1170 -0.0178 0.0000  -0.0006 133 ALA A N   
1386 C  CA  . ALA A 133 ? 0.1268 0.0818 0.1118 -0.0176 -0.0027 0.0020  133 ALA A CA  
1387 C  C   . ALA A 133 ? 0.1019 0.0818 0.1111 -0.0196 0.0000  -0.0063 133 ALA A C   
1388 O  O   . ALA A 133 ? 0.1154 0.1098 0.0983 -0.0170 -0.0060 -0.0137 133 ALA A O   
1389 C  CB  . ALA A 133 ? 0.1170 0.1127 0.1075 -0.0143 0.0000  0.0000  133 ALA A CB  
1390 N  N   . LEU A 134 ? 0.1465 0.0688 0.1082 -0.0074 0.0194  -0.0035 134 LEU A N   
1391 C  CA  . LEU A 134 ? 0.1480 0.1048 0.1102 0.0040  0.0071  -0.0142 134 LEU A CA  
1392 C  C   . LEU A 134 ? 0.1052 0.1088 0.1208 -0.0006 0.0109  -0.0030 134 LEU A C   
1393 O  O   . LEU A 134 ? 0.1436 0.1062 0.1387 0.0135  0.0030  -0.0051 134 LEU A O   
1394 C  CB  . LEU A 134 ? 0.1875 0.0921 0.1544 0.0024  0.0355  -0.0151 134 LEU A CB  
1395 C  CG  . LEU A 134 ? 0.2350 0.2231 0.2278 -0.0693 0.0768  -0.0772 134 LEU A CG  
1396 C  CD1 . LEU A 134 ? 0.3154 0.3194 0.2308 -0.0802 0.1343  -0.1590 134 LEU A CD1 
1397 C  CD2 . LEU A 134 ? 0.1820 0.1793 0.1633 -0.0485 0.0207  -0.0575 134 LEU A CD2 
1398 N  N   . GLN A 135 ? 0.1141 0.0917 0.1386 -0.0154 0.0177  -0.0091 135 GLN A N   
1399 C  CA  . GLN A 135 ? 0.1234 0.1105 0.1452 -0.0285 -0.0023 -0.0057 135 GLN A CA  
1400 C  C   . GLN A 135 ? 0.1215 0.0985 0.1231 -0.0252 -0.0087 -0.0038 135 GLN A C   
1401 O  O   . GLN A 135 ? 0.1371 0.1572 0.1527 -0.0478 0.0054  -0.0432 135 GLN A O   
1402 C  CB  . GLN A 135 ? 0.1471 0.1371 0.1574 -0.0582 0.0159  0.0013  135 GLN A CB  
1403 C  CG  . GLN A 135 ? 0.1570 0.2097 0.1545 -0.0557 0.0208  0.0286  135 GLN A CG  
1404 C  CD  . GLN A 135 ? 0.2064 0.2354 0.2578 -0.0797 0.0120  0.0377  135 GLN A CD  
1405 O  OE1 . GLN A 135 ? 0.3291 0.2847 0.4083 -0.1553 -0.0308 0.0515  135 GLN A OE1 
1406 N  NE2 . GLN A 135 ? 0.2964 0.2709 0.3276 -0.0436 0.0631  0.1119  135 GLN A NE2 
1407 N  N   . GLN A 136 ? 0.1237 0.0967 0.1116 -0.0052 0.0052  -0.0104 136 GLN A N   
1408 C  CA  . GLN A 136 ? 0.1373 0.0873 0.0956 -0.0115 -0.0104 -0.0183 136 GLN A CA  
1409 C  C   . GLN A 136 ? 0.1089 0.0861 0.0983 -0.0035 0.0092  -0.0140 136 GLN A C   
1410 O  O   . GLN A 136 ? 0.1301 0.0811 0.1082 0.0010  0.0073  -0.0218 136 GLN A O   
1411 C  CB  . GLN A 136 ? 0.1531 0.0881 0.1106 -0.0043 -0.0091 -0.0060 136 GLN A CB  
1412 C  CG  . GLN A 136 ? 0.2206 0.1111 0.1251 0.0065  -0.0043 0.0115  136 GLN A CG  
1413 C  CD  . GLN A 136 ? 0.1635 0.1170 0.3720 -0.0129 -0.0203 0.0434  136 GLN A CD  
1414 O  OE1 . GLN A 136 ? 0.4271 0.1558 0.3765 0.0390  -0.1296 -0.1298 136 GLN A OE1 
1415 N  NE2 . GLN A 136 ? 0.3237 0.2375 0.6632 -0.0834 -0.0710 0.1835  136 GLN A NE2 
1416 N  N   A PRO A 137 ? 0.0991 0.1019 0.0886 -0.0062 0.0006  -0.0164 137 PRO A N   
1417 N  N   B PRO A 137 ? 0.1017 0.1105 0.0888 -0.0205 0.0097  -0.0208 137 PRO A N   
1418 C  CA  A PRO A 137 ? 0.1120 0.1053 0.0944 0.0087  0.0024  0.0031  137 PRO A CA  
1419 C  CA  B PRO A 137 ? 0.1279 0.1089 0.0904 0.0006  -0.0043 0.0035  137 PRO A CA  
1420 C  C   A PRO A 137 ? 0.1154 0.1023 0.0957 -0.0024 0.0051  -0.0097 137 PRO A C   
1421 C  C   B PRO A 137 ? 0.1220 0.1023 0.0935 -0.0012 0.0040  -0.0057 137 PRO A C   
1422 O  O   A PRO A 137 ? 0.1429 0.1040 0.1962 -0.0065 -0.0041 0.0141  137 PRO A O   
1423 O  O   B PRO A 137 ? 0.1314 0.1064 0.1935 -0.0071 -0.0013 0.0153  137 PRO A O   
1424 C  CB  A PRO A 137 ? 0.1723 0.1295 0.1014 0.0076  0.0103  -0.0108 137 PRO A CB  
1425 C  CB  B PRO A 137 ? 0.2149 0.1272 0.0929 -0.0099 0.0119  -0.0207 137 PRO A CB  
1426 C  CG  A PRO A 137 ? 0.1569 0.1362 0.0825 0.0329  -0.0120 -0.0322 137 PRO A CG  
1427 C  CG  B PRO A 137 ? 0.2411 0.2143 0.1045 -0.0749 -0.0152 0.0071  137 PRO A CG  
1428 C  CD  A PRO A 137 ? 0.1055 0.1588 0.0904 -0.0051 0.0038  -0.0452 137 PRO A CD  
1429 C  CD  B PRO A 137 ? 0.1179 0.1154 0.1208 -0.0366 0.0006  -0.0251 137 PRO A CD  
1430 N  N   . ASP A 138 ? 0.1161 0.1179 0.0960 0.0057  0.0155  -0.0049 138 ASP A N   
1431 C  CA  . ASP A 138 ? 0.1237 0.1263 0.1044 -0.0254 0.0185  0.0010  138 ASP A CA  
1432 C  C   . ASP A 138 ? 0.0852 0.0877 0.1177 -0.0087 0.0125  -0.0054 138 ASP A C   
1433 O  O   . ASP A 138 ? 0.1000 0.1188 0.1298 0.0043  0.0103  -0.0206 138 ASP A O   
1434 C  CB  . ASP A 138 ? 0.1638 0.1705 0.0996 -0.0013 0.0328  -0.0205 138 ASP A CB  
1435 C  CG  . ASP A 138 ? 0.1145 0.1726 0.1624 0.0219  0.0166  -0.0342 138 ASP A CG  
1436 O  OD1 . ASP A 138 ? 0.1910 0.1216 0.1553 0.0195  0.0165  -0.0269 138 ASP A OD1 
1437 O  OD2 . ASP A 138 ? 0.1705 0.2081 0.2046 0.0337  0.0313  -0.0692 138 ASP A OD2 
1438 N  N   . GLY A 139 ? 0.0944 0.0816 0.0861 -0.0073 0.0035  -0.0214 139 GLY A N   
1439 C  CA  . GLY A 139 ? 0.0996 0.0856 0.0924 -0.0197 -0.0126 -0.0071 139 GLY A CA  
1440 C  C   . GLY A 139 ? 0.0662 0.0667 0.0926 -0.0046 0.0093  -0.0007 139 GLY A C   
1441 O  O   . GLY A 139 ? 0.0969 0.0710 0.1102 0.0115  -0.0098 -0.0046 139 GLY A O   
1442 N  N   . LEU A 140 ? 0.0854 0.0649 0.1066 0.0015  0.0031  -0.0162 140 LEU A N   
1443 C  CA  . LEU A 140 ? 0.0908 0.0719 0.0890 -0.0120 0.0126  -0.0126 140 LEU A CA  
1444 C  C   . LEU A 140 ? 0.0794 0.0538 0.0935 -0.0031 0.0003  -0.0163 140 LEU A C   
1445 O  O   . LEU A 140 ? 0.0802 0.0719 0.0900 -0.0093 -0.0023 -0.0060 140 LEU A O   
1446 C  CB  . LEU A 140 ? 0.0985 0.0785 0.1061 0.0109  0.0229  -0.0073 140 LEU A CB  
1447 C  CG  . LEU A 140 ? 0.1439 0.1044 0.1365 0.0199  0.0450  -0.0086 140 LEU A CG  
1448 C  CD1 . LEU A 140 ? 0.1611 0.1314 0.1773 0.0043  0.0518  -0.0076 140 LEU A CD1 
1449 C  CD2 . LEU A 140 ? 0.1553 0.1240 0.1362 0.0054  0.0610  -0.0153 140 LEU A CD2 
1450 N  N   . ALA A 141 ? 0.0809 0.0622 0.1082 -0.0141 -0.0041 -0.0152 141 ALA A N   
1451 C  CA  . ALA A 141 ? 0.0838 0.0614 0.0973 -0.0108 0.0000  -0.0063 141 ALA A CA  
1452 C  C   . ALA A 141 ? 0.0824 0.0702 0.0776 -0.0092 -0.0015 0.0027  141 ALA A C   
1453 O  O   . ALA A 141 ? 0.1097 0.0666 0.0872 0.0027  -0.0092 0.0027  141 ALA A O   
1454 C  CB  . ALA A 141 ? 0.1036 0.0790 0.1308 -0.0131 0.0104  -0.0141 141 ALA A CB  
1455 N  N   . VAL A 142 ? 0.0724 0.0588 0.0790 -0.0065 -0.0046 0.0010  142 VAL A N   
1456 C  CA  . VAL A 142 ? 0.0771 0.0741 0.0856 -0.0102 0.0043  -0.0130 142 VAL A CA  
1457 C  C   . VAL A 142 ? 0.0869 0.0529 0.0754 -0.0013 0.0027  -0.0027 142 VAL A C   
1458 O  O   . VAL A 142 ? 0.0812 0.0732 0.0772 -0.0012 0.0030  0.0082  142 VAL A O   
1459 C  CB  . VAL A 142 ? 0.0847 0.0776 0.0854 -0.0012 0.0000  -0.0129 142 VAL A CB  
1460 C  CG1 . VAL A 142 ? 0.0988 0.0931 0.0746 0.0000  -0.0043 -0.0208 142 VAL A CG1 
1461 C  CG2 . VAL A 142 ? 0.0861 0.0931 0.0821 -0.0109 0.0098  0.0087  142 VAL A CG2 
1462 N  N   . LEU A 143 ? 0.0854 0.0571 0.0935 -0.0131 -0.0030 -0.0129 143 LEU A N   
1463 C  CA  . LEU A 143 ? 0.0680 0.0561 0.1019 0.0000  -0.0041 -0.0043 143 LEU A CA  
1464 C  C   . LEU A 143 ? 0.0799 0.0608 0.0731 -0.0065 -0.0026 -0.0019 143 LEU A C   
1465 O  O   . LEU A 143 ? 0.1085 0.0697 0.0728 -0.0131 0.0027  0.0031  143 LEU A O   
1466 C  CB  . LEU A 143 ? 0.0777 0.0802 0.1212 0.0034  -0.0204 0.0130  143 LEU A CB  
1467 C  CG  . LEU A 143 ? 0.0938 0.1001 0.1353 -0.0051 -0.0142 0.0107  143 LEU A CG  
1468 C  CD1 . LEU A 143 ? 0.0929 0.1462 0.1448 -0.0038 0.0098  0.0399  143 LEU A CD1 
1469 C  CD2 . LEU A 143 ? 0.0960 0.1484 0.1533 0.0188  -0.0230 0.0077  143 LEU A CD2 
1470 N  N   . GLY A 144 ? 0.0780 0.0615 0.0847 -0.0003 -0.0030 -0.0040 144 GLY A N   
1471 C  CA  . GLY A 144 ? 0.1045 0.0535 0.0653 -0.0027 0.0013  0.0057  144 GLY A CA  
1472 C  C   . GLY A 144 ? 0.0895 0.0640 0.0639 -0.0052 -0.0019 0.0017  144 GLY A C   
1473 O  O   . GLY A 144 ? 0.1096 0.0732 0.0732 -0.0099 0.0219  -0.0020 144 GLY A O   
1474 N  N   . ILE A 145 ? 0.0904 0.0600 0.0657 0.0000  0.0003  -0.0019 145 ILE A N   
1475 C  CA  . ILE A 145 ? 0.0906 0.0627 0.0806 0.0010  -0.0098 0.0081  145 ILE A CA  
1476 C  C   . ILE A 145 ? 0.0931 0.0662 0.0670 0.0048  -0.0071 0.0096  145 ILE A C   
1477 O  O   . ILE A 145 ? 0.0996 0.0640 0.0843 -0.0038 0.0074  0.0031  145 ILE A O   
1478 C  CB  . ILE A 145 ? 0.1073 0.0750 0.1039 0.0126  -0.0225 -0.0019 145 ILE A CB  
1479 C  CG1 . ILE A 145 ? 0.1621 0.0976 0.1272 0.0524  -0.0226 -0.0007 145 ILE A CG1 
1480 C  CG2 . ILE A 145 ? 0.0992 0.1023 0.1423 0.0026  -0.0204 0.0093  145 ILE A CG2 
1481 C  CD1 . ILE A 145 ? 0.1700 0.1159 0.1592 0.0216  -0.0496 0.0284  145 ILE A CD1 
1482 N  N   . PHE A 146 ? 0.0944 0.0662 0.0649 0.0017  -0.0135 0.0113  146 PHE A N   
1483 C  CA  . PHE A 146 ? 0.0940 0.0597 0.0763 0.0073  -0.0076 0.0081  146 PHE A CA  
1484 C  C   . PHE A 146 ? 0.0877 0.0763 0.0722 0.0024  -0.0005 0.0057  146 PHE A C   
1485 O  O   . PHE A 146 ? 0.0869 0.0935 0.0974 0.0000  -0.0027 0.0027  146 PHE A O   
1486 C  CB  . PHE A 146 ? 0.0978 0.0719 0.0750 -0.0085 -0.0054 0.0115  146 PHE A CB  
1487 C  CG  . PHE A 146 ? 0.0967 0.0630 0.0649 0.0062  -0.0024 0.0126  146 PHE A CG  
1488 C  CD1 . PHE A 146 ? 0.1005 0.0763 0.0870 0.0071  -0.0006 0.0065  146 PHE A CD1 
1489 C  CD2 . PHE A 146 ? 0.1115 0.0631 0.0794 0.0041  0.0000  0.0162  146 PHE A CD2 
1490 C  CE1 . PHE A 146 ? 0.1129 0.0588 0.0881 -0.0052 0.0000  0.0065  146 PHE A CE1 
1491 C  CE2 . PHE A 146 ? 0.1179 0.0882 0.0854 0.0076  0.0015  0.0088  146 PHE A CE2 
1492 C  CZ  . PHE A 146 ? 0.1085 0.0771 0.0784 -0.0006 -0.0017 0.0219  146 PHE A CZ  
1493 N  N   . LEU A 147 ? 0.0978 0.0692 0.0728 -0.0040 0.0020  0.0015  147 LEU A N   
1494 C  CA  . LEU A 147 ? 0.1141 0.0586 0.0802 -0.0082 -0.0164 -0.0043 147 LEU A CA  
1495 C  C   . LEU A 147 ? 0.1085 0.0680 0.0802 -0.0059 -0.0110 -0.0031 147 LEU A C   
1496 O  O   . LEU A 147 ? 0.1062 0.0706 0.0952 -0.0035 0.0000  0.0046  147 LEU A O   
1497 C  CB  . LEU A 147 ? 0.1495 0.0724 0.0836 -0.0051 0.0020  -0.0043 147 LEU A CB  
1498 C  CG  . LEU A 147 ? 0.1617 0.0627 0.0933 -0.0241 -0.0182 0.0024  147 LEU A CG  
1499 C  CD1 . LEU A 147 ? 0.1973 0.0727 0.0944 -0.0131 -0.0370 0.0026  147 LEU A CD1 
1500 C  CD2 . LEU A 147 ? 0.1420 0.1005 0.0906 -0.0219 -0.0087 0.0173  147 LEU A CD2 
1501 N  N   . LYS A 148 ? 0.1159 0.0625 0.1048 -0.0184 0.0015  -0.0049 148 LYS A N   
1502 C  CA  . LYS A 148 ? 0.1317 0.0689 0.0982 -0.0023 0.0043  0.0035  148 LYS A CA  
1503 C  C   . LYS A 148 ? 0.1272 0.0790 0.1172 -0.0065 -0.0015 -0.0043 148 LYS A C   
1504 O  O   . LYS A 148 ? 0.1396 0.1027 0.1181 0.0129  -0.0259 -0.0147 148 LYS A O   
1505 C  CB  . LYS A 148 ? 0.1203 0.0926 0.1263 -0.0170 0.0120  -0.0024 148 LYS A CB  
1506 C  CG  . LYS A 148 ? 0.1371 0.1308 0.1387 -0.0219 0.0120  0.0244  148 LYS A CG  
1507 C  CD  . LYS A 148 ? 0.2012 0.1726 0.1994 -0.0601 0.0478  0.0315  148 LYS A CD  
1508 C  CE  . LYS A 148 ? 0.2592 0.4426 0.2493 -0.1111 0.0670  0.0881  148 LYS A CE  
1509 N  NZ  . LYS A 148 ? 0.4476 0.5899 0.4059 -0.1599 0.1455  0.1913  148 LYS A NZ  
1510 N  N   . VAL A 149 ? 0.1596 0.0776 0.1199 0.0155  -0.0208 -0.0076 149 VAL A N   
1511 C  CA  . VAL A 149 ? 0.1414 0.1118 0.1123 0.0000  -0.0170 -0.0283 149 VAL A CA  
1512 C  C   . VAL A 149 ? 0.1608 0.0992 0.1513 -0.0098 -0.0114 -0.0052 149 VAL A C   
1513 O  O   . VAL A 149 ? 0.2226 0.1067 0.1784 -0.0317 -0.0208 0.0071  149 VAL A O   
1514 C  CB  . VAL A 149 ? 0.1744 0.1242 0.1387 0.0200  -0.0263 -0.0241 149 VAL A CB  
1515 C  CG1 . VAL A 149 ? 0.2382 0.1877 0.1190 -0.0038 -0.0326 -0.0271 149 VAL A CG1 
1516 C  CG2 . VAL A 149 ? 0.1560 0.1684 0.1705 -0.0102 0.0026  -0.0269 149 VAL A CG2 
1517 N  N   . GLY A 150 ? 0.1398 0.1154 0.1556 -0.0204 -0.0243 -0.0085 150 GLY A N   
1518 C  CA  . GLY A 150 ? 0.1858 0.1732 0.1495 -0.0601 -0.0188 0.0303  150 GLY A CA  
1519 C  C   . GLY A 150 ? 0.1651 0.1312 0.1527 -0.0630 -0.0209 0.0104  150 GLY A C   
1520 O  O   . GLY A 150 ? 0.1581 0.1403 0.1615 -0.0423 -0.0120 -0.0131 150 GLY A O   
1521 N  N   A SER A 151 ? 0.1820 0.1648 0.1596 -0.0697 -0.0299 -0.0098 151 SER A N   
1522 N  N   B SER A 151 ? 0.1847 0.1493 0.1773 -0.0767 -0.0210 -0.0167 151 SER A N   
1523 C  CA  A SER A 151 ? 0.2069 0.1942 0.1764 -0.0351 -0.0255 0.0068  151 SER A CA  
1524 C  CA  B SER A 151 ? 0.1805 0.1222 0.1890 -0.0895 -0.0344 -0.0379 151 SER A CA  
1525 C  C   A SER A 151 ? 0.2118 0.1393 0.1502 -0.0198 -0.0355 -0.0485 151 SER A C   
1526 C  C   B SER A 151 ? 0.1337 0.1215 0.1256 -0.0421 -0.0043 -0.0483 151 SER A C   
1527 O  O   A SER A 151 ? 0.1091 0.1319 0.1389 -0.0110 -0.0074 -0.0333 151 SER A O   
1528 O  O   B SER A 151 ? 0.1562 0.1124 0.1116 -0.0377 -0.0211 -0.0277 151 SER A O   
1529 C  CB  A SER A 151 ? 0.2163 0.2237 0.2707 -0.0504 -0.0037 0.0099  151 SER A CB  
1530 C  CB  B SER A 151 ? 0.2190 0.1132 0.2958 -0.0719 -0.0060 -0.0621 151 SER A CB  
1531 O  OG  A SER A 151 ? 0.2364 0.3508 0.2172 -0.0806 -0.0386 -0.0071 151 SER A OG  
1532 O  OG  B SER A 151 ? 0.1951 0.2314 0.3388 -0.0731 0.0093  0.0653  151 SER A OG  
1533 N  N   . ALA A 152 ? 0.1669 0.1324 0.1567 -0.0241 -0.0401 -0.0219 152 ALA A N   
1534 C  CA  . ALA A 152 ? 0.1987 0.1179 0.1511 -0.0077 -0.0384 -0.0285 152 ALA A CA  
1535 C  C   . ALA A 152 ? 0.1762 0.1454 0.1184 0.0041  -0.0509 -0.0351 152 ALA A C   
1536 O  O   . ALA A 152 ? 0.1824 0.1457 0.1796 0.0000  -0.0381 -0.0337 152 ALA A O   
1537 C  CB  . ALA A 152 ? 0.2483 0.1705 0.1489 -0.0253 -0.0423 -0.0584 152 ALA A CB  
1538 N  N   . LYS A 153 ? 0.2100 0.1001 0.1522 0.0065  -0.0772 -0.0195 153 LYS A N   
1539 C  CA  . LYS A 153 ? 0.2098 0.1066 0.1565 0.0091  -0.0728 -0.0280 153 LYS A CA  
1540 C  C   . LYS A 153 ? 0.1890 0.1387 0.1405 0.0163  -0.0483 -0.0181 153 LYS A C   
1541 O  O   . LYS A 153 ? 0.1845 0.1479 0.1321 0.0043  -0.0533 -0.0183 153 LYS A O   
1542 C  CB  . LYS A 153 ? 0.1926 0.1263 0.1711 0.0013  -0.0772 -0.0207 153 LYS A CB  
1543 C  CG  . LYS A 153 ? 0.2921 0.1054 0.1798 0.0194  -0.0939 -0.0197 153 LYS A CG  
1544 C  CD  . LYS A 153 ? 0.3323 0.1142 0.1923 0.0408  -0.0920 -0.0131 153 LYS A CD  
1545 C  CE  . LYS A 153 ? 0.4701 0.1394 0.2118 0.0115  -0.0156 -0.0263 153 LYS A CE  
1546 N  NZ  . LYS A 153 ? 0.4921 0.1717 0.1720 0.0241  0.0065  -0.0270 153 LYS A NZ  
1547 N  N   . PRO A 154 ? 0.1978 0.1438 0.1493 -0.0109 -0.0566 0.0006  154 PRO A N   
1548 C  CA  . PRO A 154 ? 0.1981 0.2178 0.1854 -0.0178 -0.0688 0.0416  154 PRO A CA  
1549 C  C   . PRO A 154 ? 0.1877 0.1892 0.1509 0.0274  -0.0847 0.0355  154 PRO A C   
1550 O  O   . PRO A 154 ? 0.2574 0.2269 0.1673 -0.0322 -0.0983 0.0675  154 PRO A O   
1551 C  CB  . PRO A 154 ? 0.1692 0.2120 0.2050 -0.0024 -0.0516 -0.0031 154 PRO A CB  
1552 C  CG  . PRO A 154 ? 0.2036 0.2994 0.2508 0.0052  -0.0621 0.0706  154 PRO A CG  
1553 C  CD  . PRO A 154 ? 0.2008 0.1741 0.1578 0.0074  -0.0277 -0.0081 154 PRO A CD  
1554 N  N   . GLY A 155 ? 0.1984 0.1416 0.2179 0.0240  -0.0706 0.0113  155 GLY A N   
1555 C  CA  . GLY A 155 ? 0.2196 0.1551 0.2522 0.0274  -0.0759 0.0298  155 GLY A CA  
1556 C  C   . GLY A 155 ? 0.2560 0.1473 0.1542 0.0233  -0.0601 0.0193  155 GLY A C   
1557 O  O   . GLY A 155 ? 0.2477 0.1342 0.2748 0.0182  -0.0485 0.0373  155 GLY A O   
1558 N  N   A LEU A 156 ? 0.1822 0.1443 0.1777 0.0110  -0.0696 0.0054  156 LEU A N   
1559 N  N   B LEU A 156 ? 0.2587 0.1181 0.1259 0.0003  -0.0794 -0.0013 156 LEU A N   
1560 C  CA  A LEU A 156 ? 0.1725 0.1263 0.1386 0.0148  -0.0445 0.0048  156 LEU A CA  
1561 C  CA  B LEU A 156 ? 0.2470 0.1482 0.0731 0.0019  -0.0546 0.0049  156 LEU A CA  
1562 C  C   A LEU A 156 ? 0.1529 0.1085 0.1267 0.0115  -0.0361 0.0395  156 LEU A C   
1563 C  C   B LEU A 156 ? 0.2055 0.1349 0.1084 -0.0057 -0.0434 -0.0403 156 LEU A C   
1564 O  O   A LEU A 156 ? 0.1518 0.1377 0.1274 0.0142  -0.0197 0.0012  156 LEU A O   
1565 O  O   B LEU A 156 ? 0.2025 0.1158 0.1062 -0.0076 -0.0614 -0.0303 156 LEU A O   
1566 C  CB  A LEU A 156 ? 0.1757 0.1253 0.1719 -0.0104 -0.0412 0.0384  156 LEU A CB  
1567 C  CB  B LEU A 156 ? 0.1811 0.1048 0.0947 -0.0164 -0.0494 -0.0295 156 LEU A CB  
1568 C  CG  A LEU A 156 ? 0.1730 0.1444 0.1028 -0.0162 -0.0086 -0.0030 156 LEU A CG  
1569 C  CG  B LEU A 156 ? 0.1629 0.0920 0.0976 -0.0076 -0.0557 -0.0109 156 LEU A CG  
1570 C  CD1 A LEU A 156 ? 0.1595 0.1380 0.1331 -0.0243 -0.0098 0.0175  156 LEU A CD1 
1571 C  CD1 B LEU A 156 ? 0.1626 0.1118 0.0832 -0.0206 -0.0236 -0.0219 156 LEU A CD1 
1572 C  CD2 A LEU A 156 ? 0.1443 0.1371 0.1319 0.0017  0.0193  -0.0115 156 LEU A CD2 
1573 C  CD2 B LEU A 156 ? 0.2251 0.0974 0.0820 0.0071  -0.0390 -0.0153 156 LEU A CD2 
1574 N  N   A GLN A 157 ? 0.1387 0.1254 0.1194 0.0173  -0.0109 0.0057  157 GLN A N   
1575 N  N   B GLN A 157 ? 0.1930 0.1208 0.0538 -0.0115 -0.0243 -0.0071 157 GLN A N   
1576 C  CA  A GLN A 157 ? 0.0807 0.1596 0.1262 0.0232  -0.0037 -0.0038 157 GLN A CA  
1577 C  CA  B GLN A 157 ? 0.1741 0.1123 0.0636 -0.0219 -0.0210 -0.0174 157 GLN A CA  
1578 C  C   A GLN A 157 ? 0.1109 0.1141 0.1181 0.0093  -0.0082 -0.0337 157 GLN A C   
1579 C  C   B GLN A 157 ? 0.1373 0.1349 0.1093 0.0020  0.0073  0.0178  157 GLN A C   
1580 O  O   A GLN A 157 ? 0.1140 0.1608 0.1098 0.0164  -0.0020 -0.0113 157 GLN A O   
1581 O  O   B GLN A 157 ? 0.1425 0.1500 0.0640 -0.0041 -0.0125 -0.0198 157 GLN A O   
1582 C  CB  A GLN A 157 ? 0.1116 0.2540 0.1444 -0.0143 -0.0129 -0.0447 157 GLN A CB  
1583 C  CB  B GLN A 157 ? 0.1957 0.1380 0.0608 -0.0353 -0.0264 -0.0155 157 GLN A CB  
1584 C  CG  A GLN A 157 ? 0.1953 0.1707 0.1374 0.0052  0.0159  0.0000  157 GLN A CG  
1585 C  CG  B GLN A 157 ? 0.1838 0.1398 0.0806 -0.0474 -0.0109 -0.0306 157 GLN A CG  
1586 C  CD  A GLN A 157 ? 0.1560 0.1303 0.1547 -0.0375 0.0063  0.0057  157 GLN A CD  
1587 C  CD  B GLN A 157 ? 0.1468 0.1481 0.1220 -0.0588 -0.0017 0.0098  157 GLN A CD  
1588 O  OE1 A GLN A 157 ? 0.2240 0.1188 0.1326 -0.0285 0.0076  -0.0074 157 GLN A OE1 
1589 O  OE1 B GLN A 157 ? 0.1923 0.2014 0.1438 -0.0485 -0.0086 -0.0575 157 GLN A OE1 
1590 N  NE2 A GLN A 157 ? 0.2055 0.1522 0.2054 0.0148  0.0562  0.0062  157 GLN A NE2 
1591 N  NE2 B GLN A 157 ? 0.1962 0.1199 0.0872 -0.0233 -0.0264 -0.0193 157 GLN A NE2 
1592 N  N   A LYS A 158 ? 0.0958 0.1515 0.1251 0.0285  -0.0068 0.0252  158 LYS A N   
1593 N  N   B LYS A 158 ? 0.1229 0.1224 0.0772 -0.0197 -0.0162 -0.0102 158 LYS A N   
1594 C  CA  A LYS A 158 ? 0.1184 0.1484 0.1067 0.0041  -0.0140 -0.0020 158 LYS A CA  
1595 C  CA  B LYS A 158 ? 0.1711 0.1448 0.0969 0.0162  -0.0186 0.0318  158 LYS A CA  
1596 C  C   A LYS A 158 ? 0.1168 0.1446 0.1023 0.0208  -0.0098 -0.0070 158 LYS A C   
1597 C  C   B LYS A 158 ? 0.1718 0.1344 0.0992 -0.0131 -0.0103 0.0292  158 LYS A C   
1598 O  O   A LYS A 158 ? 0.1233 0.1669 0.1216 -0.0197 -0.0035 -0.0027 158 LYS A O   
1599 O  O   B LYS A 158 ? 0.1254 0.1341 0.1129 -0.0159 -0.0252 0.0368  158 LYS A O   
1600 C  CB  A LYS A 158 ? 0.1750 0.1687 0.1621 0.0414  -0.0240 0.0198  158 LYS A CB  
1601 C  CB  B LYS A 158 ? 0.2064 0.1482 0.0564 0.0152  -0.0194 0.0198  158 LYS A CB  
1602 C  CG  A LYS A 158 ? 0.2317 0.1919 0.1956 0.0274  -0.0737 0.0533  158 LYS A CG  
1603 C  CG  B LYS A 158 ? 0.2549 0.1577 0.1832 -0.0121 -0.0824 0.0184  158 LYS A CG  
1604 C  CD  A LYS A 158 ? 0.2278 0.2127 0.1958 0.0159  -0.1171 0.0007  158 LYS A CD  
1605 C  CD  B LYS A 158 ? 0.2865 0.1947 0.2791 -0.0017 -0.0511 -0.0441 158 LYS A CD  
1606 C  CE  A LYS A 158 ? 0.3501 0.2011 0.3055 0.0696  -0.0957 0.0511  158 LYS A CE  
1607 C  CE  B LYS A 158 ? 0.2829 0.2615 0.2301 -0.0318 -0.0571 -0.0017 158 LYS A CE  
1608 N  NZ  A LYS A 158 ? 0.3786 0.2538 0.1922 0.0974  0.0142  0.0912  158 LYS A NZ  
1609 N  NZ  B LYS A 158 ? 0.2721 0.3846 0.2447 -0.0395 -0.0491 0.1683  158 LYS A NZ  
1610 N  N   A VAL A 159 ? 0.1115 0.0974 0.1089 0.0193  -0.0240 -0.0216 159 VAL A N   
1611 N  N   B VAL A 159 ? 0.1513 0.1288 0.0966 -0.0125 -0.0196 -0.0097 159 VAL A N   
1612 C  CA  A VAL A 159 ? 0.1283 0.1005 0.0877 0.0065  -0.0271 -0.0171 159 VAL A CA  
1613 C  CA  B VAL A 159 ? 0.1443 0.1082 0.0960 -0.0146 -0.0037 0.0035  159 VAL A CA  
1614 C  C   A VAL A 159 ? 0.1543 0.1001 0.0886 0.0038  -0.0167 -0.0294 159 VAL A C   
1615 C  C   B VAL A 159 ? 0.1558 0.0996 0.1606 0.0070  0.0107  0.0285  159 VAL A C   
1616 O  O   A VAL A 159 ? 0.1529 0.0755 0.1179 0.0006  -0.0140 -0.0161 159 VAL A O   
1617 O  O   B VAL A 159 ? 0.1693 0.1407 0.1049 -0.0068 -0.0017 0.0052  159 VAL A O   
1618 C  CB  A VAL A 159 ? 0.1630 0.0992 0.1045 0.0375  -0.0630 -0.0538 159 VAL A CB  
1619 C  CB  B VAL A 159 ? 0.1330 0.1541 0.1116 0.0118  -0.0264 -0.0299 159 VAL A CB  
1620 C  CG1 A VAL A 159 ? 0.1887 0.1435 0.0967 -0.0082 -0.0987 -0.0319 159 VAL A CG1 
1621 C  CG1 B VAL A 159 ? 0.1365 0.1741 0.1635 -0.0010 -0.0640 0.0304  159 VAL A CG1 
1622 C  CG2 A VAL A 159 ? 0.2080 0.1443 0.1317 0.0781  -0.0916 -0.0856 159 VAL A CG2 
1623 C  CG2 B VAL A 159 ? 0.2070 0.1594 0.1745 0.0996  -0.0509 -0.0181 159 VAL A CG2 
1624 N  N   A VAL A 160 ? 0.1107 0.0908 0.1286 0.0003  -0.0377 -0.0370 160 VAL A N   
1625 N  N   B VAL A 160 ? 0.1395 0.0953 0.0854 -0.0007 0.0049  0.0115  160 VAL A N   
1626 C  CA  A VAL A 160 ? 0.1678 0.1125 0.1199 0.0115  -0.0164 -0.0243 160 VAL A CA  
1627 C  CA  B VAL A 160 ? 0.1567 0.0888 0.1228 0.0166  0.0035  0.0114  160 VAL A CA  
1628 C  C   A VAL A 160 ? 0.1362 0.1378 0.1190 0.0031  -0.0248 -0.0408 160 VAL A C   
1629 C  C   B VAL A 160 ? 0.1569 0.0789 0.1299 0.0251  -0.0098 0.0076  160 VAL A C   
1630 O  O   A VAL A 160 ? 0.1782 0.1500 0.1316 -0.0063 0.0351  -0.0177 160 VAL A O   
1631 O  O   B VAL A 160 ? 0.1951 0.0969 0.1274 0.0120  0.0126  -0.0187 160 VAL A O   
1632 C  CB  A VAL A 160 ? 0.2465 0.1322 0.1283 -0.0307 -0.0282 -0.0392 160 VAL A CB  
1633 C  CB  B VAL A 160 ? 0.2134 0.0951 0.1202 0.0147  -0.0237 0.0294  160 VAL A CB  
1634 C  CG1 A VAL A 160 ? 0.2639 0.1288 0.1861 -0.0296 0.0082  -0.0299 160 VAL A CG1 
1635 C  CG1 B VAL A 160 ? 0.3095 0.1933 0.1145 -0.0240 -0.0197 0.0683  160 VAL A CG1 
1636 C  CG2 A VAL A 160 ? 0.2808 0.1032 0.1319 0.0131  -0.0208 -0.0087 160 VAL A CG2 
1637 C  CG2 B VAL A 160 ? 0.2299 0.1380 0.1818 -0.0037 -0.0241 -0.0173 160 VAL A CG2 
1638 N  N   A ASP A 161 ? 0.1856 0.1395 0.1089 -0.0006 -0.0617 -0.0210 161 ASP A N   
1639 N  N   B ASP A 161 ? 0.1985 0.1204 0.1389 0.0214  -0.0644 -0.0377 161 ASP A N   
1640 C  CA  A ASP A 161 ? 0.2468 0.1699 0.1064 -0.0474 -0.0482 -0.0260 161 ASP A CA  
1641 C  CA  B ASP A 161 ? 0.2511 0.1630 0.1342 0.0093  -0.0304 -0.0035 161 ASP A CA  
1642 C  C   A ASP A 161 ? 0.2253 0.1877 0.1185 -0.0377 -0.0575 0.0000  161 ASP A C   
1643 C  C   B ASP A 161 ? 0.2840 0.1324 0.1328 0.0366  -0.0205 -0.0320 161 ASP A C   
1644 O  O   A ASP A 161 ? 0.2346 0.2845 0.1133 -0.0065 -0.0869 -0.0485 161 ASP A O   
1645 O  O   B ASP A 161 ? 0.2061 0.1838 0.1231 0.0082  -0.0318 -0.0135 161 ASP A O   
1646 C  CB  A ASP A 161 ? 0.3210 0.2269 0.1149 -0.0296 -0.1115 -0.0342 161 ASP A CB  
1647 C  CB  B ASP A 161 ? 0.2856 0.2030 0.0996 0.0031  -0.0820 0.0019  161 ASP A CB  
1648 C  CG  A ASP A 161 ? 0.3093 0.1700 0.0969 0.0152  -0.1137 -0.0671 161 ASP A CG  
1649 C  CG  B ASP A 161 ? 0.4422 0.1719 0.1601 -0.0093 -0.0275 0.0461  161 ASP A CG  
1650 O  OD1 A ASP A 161 ? 0.2824 0.2104 0.1294 -0.0013 -0.0487 -0.0351 161 ASP A OD1 
1651 O  OD1 B ASP A 161 ? 0.5052 0.1323 0.2170 -0.0449 -0.1339 0.0671  161 ASP A OD1 
1652 O  OD2 A ASP A 161 ? 0.3287 0.2759 0.1756 -0.0383 -0.1429 -0.0214 161 ASP A OD2 
1653 O  OD2 B ASP A 161 ? 0.4142 0.2242 0.3239 -0.0080 -0.1247 -0.0370 161 ASP A OD2 
1654 N  N   . VAL A 162 ? 0.3564 0.1391 0.1170 -0.0410 -0.0710 0.0041  162 VAL A N   
1655 C  CA  . VAL A 162 ? 0.4241 0.1615 0.1161 -0.0337 -0.1096 0.0236  162 VAL A CA  
1656 C  C   . VAL A 162 ? 0.3628 0.1308 0.1258 -0.0768 -0.0582 0.0261  162 VAL A C   
1657 O  O   . VAL A 162 ? 0.3910 0.1396 0.1058 -0.0772 -0.0275 0.0006  162 VAL A O   
1658 C  CB  . VAL A 162 ? 0.4844 0.1256 0.2833 -0.0197 -0.1780 0.0601  162 VAL A CB  
1659 C  CG1 . VAL A 162 ? 0.4762 0.2348 0.3474 0.0412  -0.1137 0.0073  162 VAL A CG1 
1660 C  CG2 . VAL A 162 ? 0.3776 0.0996 0.2465 -0.0125 -0.1167 0.0232  162 VAL A CG2 
1661 N  N   . LEU A 163 ? 0.3386 0.1303 0.0976 -0.0562 -0.0137 0.0153  163 LEU A N   
1662 C  CA  . LEU A 163 ? 0.3154 0.1294 0.0944 -0.0564 -0.0148 0.0120  163 LEU A CA  
1663 C  C   . LEU A 163 ? 0.2930 0.1490 0.0969 -0.0126 -0.0249 -0.0093 163 LEU A C   
1664 O  O   . LEU A 163 ? 0.3463 0.1698 0.0917 -0.0546 -0.0024 0.0175  163 LEU A O   
1665 C  CB  . LEU A 163 ? 0.3472 0.1172 0.0886 -0.0538 -0.0119 0.0060  163 LEU A CB  
1666 C  CG  . LEU A 163 ? 0.3115 0.1213 0.0798 -0.0244 -0.0203 0.0243  163 LEU A CG  
1667 C  CD1 . LEU A 163 ? 0.3054 0.0983 0.1328 -0.0355 -0.0298 0.0309  163 LEU A CD1 
1668 C  CD2 . LEU A 163 ? 0.3226 0.1356 0.0917 -0.0410 -0.0196 -0.0027 163 LEU A CD2 
1669 N  N   . ASP A 164 ? 0.4293 0.1454 0.0741 -0.0472 -0.0074 -0.0017 164 ASP A N   
1670 C  CA  . ASP A 164 ? 0.3747 0.1692 0.1230 -0.0662 -0.0017 -0.0113 164 ASP A CA  
1671 C  C   . ASP A 164 ? 0.3880 0.1996 0.0951 -0.0458 0.0005  -0.0136 164 ASP A C   
1672 O  O   . ASP A 164 ? 0.4365 0.2492 0.1441 -0.0333 0.0469  0.0046  164 ASP A O   
1673 C  CB  . ASP A 164 ? 0.4322 0.2091 0.2032 -0.0627 -0.0359 -0.0511 164 ASP A CB  
1674 C  CG  . ASP A 164 ? 0.4541 0.2752 0.1813 -0.1023 -0.0608 -0.0603 164 ASP A CG  
1675 O  OD1 . ASP A 164 ? 0.4832 0.5325 0.2079 -0.1283 -0.0386 -0.0798 164 ASP A OD1 
1676 O  OD2 . ASP A 164 ? 0.6441 0.7681 0.1973 -0.1782 0.0820  -0.1632 164 ASP A OD2 
1677 N  N   A SER A 165 ? 0.3077 0.2364 0.0590 -0.0705 -0.0339 0.0052  165 SER A N   
1678 N  N   B SER A 165 ? 0.3768 0.1204 0.0818 -0.0843 -0.0706 -0.0046 165 SER A N   
1679 C  CA  A SER A 165 ? 0.2362 0.1955 0.0788 -0.0296 -0.0175 -0.0054 165 SER A CA  
1680 C  CA  B SER A 165 ? 0.2152 0.1461 0.1076 -0.0359 -0.0335 0.0252  165 SER A CA  
1681 C  C   A SER A 165 ? 0.1127 0.1922 0.0732 -0.0178 0.0119  0.0181  165 SER A C   
1682 C  C   B SER A 165 ? 0.1646 0.1208 0.1057 -0.0115 -0.0125 0.0401  165 SER A C   
1683 O  O   A SER A 165 ? 0.1221 0.1762 0.1044 -0.0285 -0.0099 0.0196  165 SER A O   
1684 O  O   B SER A 165 ? 0.1714 0.1386 0.1084 -0.0258 0.0068  0.0401  165 SER A O   
1685 C  CB  A SER A 165 ? 0.2727 0.2021 0.1332 -0.0326 -0.0271 0.0049  165 SER A CB  
1686 C  CB  B SER A 165 ? 0.1702 0.1687 0.1499 -0.0176 0.0041  0.0126  165 SER A CB  
1687 O  OG  A SER A 165 ? 0.2179 0.1441 0.1444 0.0023  -0.0515 0.0285  165 SER A OG  
1688 O  OG  B SER A 165 ? 0.1926 0.1437 0.1463 -0.0060 -0.0357 0.0296  165 SER A OG  
1689 N  N   A ILE A 166 ? 0.0798 0.1536 0.0766 -0.0017 -0.0060 0.0081  166 ILE A N   
1690 N  N   B ILE A 166 ? 0.1269 0.0956 0.0847 -0.0184 0.0063  0.0250  166 ILE A N   
1691 C  CA  A ILE A 166 ? 0.1143 0.1285 0.0807 -0.0020 -0.0177 0.0000  166 ILE A CA  
1692 C  CA  B ILE A 166 ? 0.1465 0.0870 0.0987 -0.0046 0.0031  -0.0065 166 ILE A CA  
1693 C  C   A ILE A 166 ? 0.1125 0.0948 0.0656 -0.0098 0.0077  0.0054  166 ILE A C   
1694 C  C   B ILE A 166 ? 0.0872 0.0845 0.1019 -0.0080 0.0065  -0.0211 166 ILE A C   
1695 O  O   A ILE A 166 ? 0.1124 0.1177 0.0556 0.0081  0.0205  0.0000  166 ILE A O   
1696 O  O   B ILE A 166 ? 0.1120 0.1055 0.0948 -0.0030 0.0082  -0.0107 166 ILE A O   
1697 C  CB  A ILE A 166 ? 0.1163 0.0987 0.1023 0.0049  0.0141  0.0176  166 ILE A CB  
1698 C  CB  B ILE A 166 ? 0.0872 0.1052 0.1003 -0.0037 -0.0146 -0.0093 166 ILE A CB  
1699 C  CG1 A ILE A 166 ? 0.1259 0.1071 0.0753 -0.0109 0.0126  -0.0013 166 ILE A CG1 
1700 C  CG1 B ILE A 166 ? 0.1366 0.1646 0.0759 0.0057  0.0228  -0.0104 166 ILE A CG1 
1701 C  CG2 A ILE A 166 ? 0.1188 0.1193 0.0885 -0.0015 0.0098  0.0397  166 ILE A CG2 
1702 C  CG2 B ILE A 166 ? 0.1140 0.0829 0.1439 0.0054  0.0060  -0.0131 166 ILE A CG2 
1703 C  CD1 A ILE A 166 ? 0.1046 0.1511 0.1021 0.0121  0.0125  -0.0494 166 ILE A CD1 
1704 C  CD1 B ILE A 166 ? 0.1265 0.1269 0.1048 -0.0171 0.0432  -0.0280 166 ILE A CD1 
1705 N  N   A LYS A 167 ? 0.1278 0.1362 0.0899 0.0098  0.0320  -0.0098 167 LYS A N   
1706 N  N   B LYS A 167 ? 0.1375 0.0944 0.0845 -0.0024 0.0097  -0.0197 167 LYS A N   
1707 C  CA  A LYS A 167 ? 0.1145 0.1093 0.0960 -0.0137 0.0062  -0.0140 167 LYS A CA  
1708 C  CA  B LYS A 167 ? 0.0859 0.1237 0.0951 0.0102  0.0189  -0.0104 167 LYS A CA  
1709 C  C   A LYS A 167 ? 0.1071 0.1301 0.0635 -0.0177 0.0249  -0.0137 167 LYS A C   
1710 C  C   B LYS A 167 ? 0.1128 0.0754 0.1046 -0.0006 0.0040  -0.0136 167 LYS A C   
1711 O  O   A LYS A 167 ? 0.1405 0.1490 0.0772 -0.0430 -0.0284 -0.0131 167 LYS A O   
1712 O  O   B LYS A 167 ? 0.1197 0.1446 0.0913 -0.0485 -0.0005 0.0097  167 LYS A O   
1713 C  CB  A LYS A 167 ? 0.1798 0.1709 0.0636 0.0124  -0.0040 -0.0186 167 LYS A CB  
1714 C  CB  B LYS A 167 ? 0.1563 0.1347 0.1161 0.0077  0.0195  -0.0335 167 LYS A CB  
1715 C  CG  A LYS A 167 ? 0.1752 0.1667 0.1375 0.0113  0.0019  -0.0445 167 LYS A CG  
1716 C  CG  B LYS A 167 ? 0.1588 0.1518 0.1457 0.0237  -0.0109 -0.0219 167 LYS A CG  
1717 C  CD  A LYS A 167 ? 0.2350 0.2281 0.1435 0.0351  -0.0065 -0.0601 167 LYS A CD  
1718 C  CD  B LYS A 167 ? 0.2373 0.1753 0.2036 0.0207  -0.0305 -0.0872 167 LYS A CD  
1719 C  CE  A LYS A 167 ? 0.2181 0.2381 0.2529 0.0513  -0.0228 -0.0938 167 LYS A CE  
1720 C  CE  B LYS A 167 ? 0.1665 0.2565 0.3424 0.0493  -0.0377 -0.0873 167 LYS A CE  
1721 N  NZ  A LYS A 167 ? 0.3801 0.1978 0.3352 -0.0432 -0.0533 -0.1067 167 LYS A NZ  
1722 N  NZ  B LYS A 167 ? 0.1944 0.3075 0.3452 0.0878  -0.0337 -0.1088 167 LYS A NZ  
1723 N  N   A THR A 168 ? 0.1137 0.1231 0.0656 -0.0007 0.0161  0.0054  168 THR A N   
1724 N  N   B THR A 168 ? 0.1023 0.1296 0.0931 -0.0124 0.0198  0.0015  168 THR A N   
1725 C  CA  A THR A 168 ? 0.1079 0.1395 0.0809 0.0015  0.0271  0.0108  168 THR A CA  
1726 C  CA  B THR A 168 ? 0.1136 0.1203 0.1057 -0.0137 0.0182  -0.0085 168 THR A CA  
1727 C  C   A THR A 168 ? 0.1265 0.1199 0.0643 0.0088  0.0421  0.0318  168 THR A C   
1728 C  C   B THR A 168 ? 0.0820 0.1084 0.0924 0.0041  0.0353  0.0142  168 THR A C   
1729 O  O   A THR A 168 ? 0.1274 0.1093 0.0895 0.0113  0.0181  0.0208  168 THR A O   
1730 O  O   B THR A 168 ? 0.1276 0.0715 0.1337 0.0077  0.0339  0.0010  168 THR A O   
1731 C  CB  A THR A 168 ? 0.1347 0.1492 0.0885 0.0024  0.0423  0.0233  168 THR A CB  
1732 C  CB  B THR A 168 ? 0.1315 0.1387 0.0802 0.0113  -0.0013 -0.0027 168 THR A CB  
1733 O  OG1 A THR A 168 ? 0.1656 0.1333 0.0627 -0.0003 0.0406  0.0041  168 THR A OG1 
1734 O  OG1 B THR A 168 ? 0.1594 0.1267 0.0836 0.0087  0.0283  0.0220  168 THR A OG1 
1735 C  CG2 A THR A 168 ? 0.2034 0.1694 0.0777 0.0315  0.0913  0.0241  168 THR A CG2 
1736 C  CG2 B THR A 168 ? 0.2256 0.1064 0.1064 -0.0003 -0.0125 0.0209  168 THR A CG2 
1737 N  N   A LYS A 169 ? 0.0960 0.1254 0.1150 -0.0005 0.0425  0.0151  169 LYS A N   
1738 N  N   B LYS A 169 ? 0.1172 0.0949 0.1262 -0.0052 0.0068  0.0085  169 LYS A N   
1739 C  CA  A LYS A 169 ? 0.1073 0.1242 0.0829 -0.0271 0.0222  0.0303  169 LYS A CA  
1740 C  CA  B LYS A 169 ? 0.1070 0.1052 0.1292 -0.0046 0.0153  0.0017  169 LYS A CA  
1741 C  C   A LYS A 169 ? 0.0897 0.1208 0.1062 -0.0104 0.0544  0.0447  169 LYS A C   
1742 C  C   B LYS A 169 ? 0.1010 0.1100 0.1023 -0.0237 0.0020  -0.0086 169 LYS A C   
1743 O  O   A LYS A 169 ? 0.1109 0.1619 0.0939 -0.0285 0.0500  0.0283  169 LYS A O   
1744 O  O   B LYS A 169 ? 0.1328 0.1511 0.1116 -0.0049 0.0131  0.0031  169 LYS A O   
1745 C  CB  A LYS A 169 ? 0.1252 0.1718 0.0913 -0.0296 0.0148  0.0109  169 LYS A CB  
1746 C  CB  B LYS A 169 ? 0.1339 0.1249 0.1480 -0.0091 -0.0135 0.0093  169 LYS A CB  
1747 C  CG  A LYS A 169 ? 0.1328 0.1617 0.1247 -0.0511 0.0240  0.0137  169 LYS A CG  
1748 C  CG  B LYS A 169 ? 0.1054 0.1188 0.1597 -0.0024 0.0430  -0.0013 169 LYS A CG  
1749 C  CD  A LYS A 169 ? 0.1328 0.2513 0.1295 -0.0318 0.0441  0.0899  169 LYS A CD  
1750 C  CD  B LYS A 169 ? 0.1261 0.1658 0.2213 0.0220  0.0017  0.0441  169 LYS A CD  
1751 C  CE  A LYS A 169 ? 0.3021 0.3091 0.2450 -0.1067 0.1290  0.0087  169 LYS A CE  
1752 C  CE  B LYS A 169 ? 0.3488 0.2095 0.2818 -0.1254 -0.0776 0.0476  169 LYS A CE  
1753 N  NZ  A LYS A 169 ? 0.3560 0.4684 0.4280 0.0136  0.0419  0.0463  169 LYS A NZ  
1754 N  NZ  B LYS A 169 ? 0.3679 0.3282 0.5370 0.0684  -0.2222 -0.0776 169 LYS A NZ  
1755 N  N   A GLY A 170 ? 0.0988 0.1048 0.1118 -0.0141 0.0280  -0.0027 170 GLY A N   
1756 N  N   B GLY A 170 ? 0.1203 0.0710 0.1588 -0.0252 0.0000  0.0063  170 GLY A N   
1757 C  CA  A GLY A 170 ? 0.1170 0.1301 0.1066 -0.0099 0.0160  0.0206  170 GLY A CA  
1758 C  CA  B GLY A 170 ? 0.1443 0.0842 0.2134 -0.0509 0.0017  0.0291  170 GLY A CA  
1759 C  C   A GLY A 170 ? 0.1328 0.1333 0.1158 -0.0210 0.0120  0.0480  170 GLY A C   
1760 C  C   B GLY A 170 ? 0.1430 0.0949 0.1052 -0.0208 0.0250  0.0249  170 GLY A C   
1761 O  O   A GLY A 170 ? 0.1835 0.1127 0.1558 -0.0353 -0.0262 0.0449  170 GLY A O   
1762 O  O   B GLY A 170 ? 0.1931 0.0992 0.1908 -0.0381 -0.0359 0.0535  170 GLY A O   
1763 N  N   A LYS A 171 ? 0.1018 0.1597 0.0736 -0.0392 0.0176  0.0324  171 LYS A N   
1764 N  N   B LYS A 171 ? 0.1137 0.1261 0.1204 -0.0351 0.0209  0.0218  171 LYS A N   
1765 C  CA  A LYS A 171 ? 0.1001 0.1412 0.0781 -0.0142 0.0359  0.0412  171 LYS A CA  
1766 C  CA  B LYS A 171 ? 0.0956 0.0997 0.1164 -0.0124 0.0260  0.0230  171 LYS A CA  
1767 C  C   A LYS A 171 ? 0.1299 0.1279 0.0966 0.0186  0.0487  0.0377  171 LYS A C   
1768 C  C   B LYS A 171 ? 0.1558 0.0706 0.0798 0.0006  0.0283  0.0052  171 LYS A C   
1769 O  O   A LYS A 171 ? 0.1430 0.1149 0.0836 0.0262  0.0326  0.0214  171 LYS A O   
1770 O  O   B LYS A 171 ? 0.2000 0.1230 0.0960 0.0417  0.0511  0.0331  171 LYS A O   
1771 C  CB  A LYS A 171 ? 0.1240 0.1484 0.1048 -0.0082 0.0240  0.0344  171 LYS A CB  
1772 C  CB  B LYS A 171 ? 0.1190 0.1229 0.0994 -0.0154 0.0063  0.0070  171 LYS A CB  
1773 C  CG  A LYS A 171 ? 0.1559 0.2044 0.1726 -0.0165 0.0665  -0.0051 171 LYS A CG  
1774 C  CG  B LYS A 171 ? 0.1380 0.1579 0.1741 -0.0193 0.0427  -0.0307 171 LYS A CG  
1775 C  CD  A LYS A 171 ? 0.1222 0.3763 0.2488 0.0974  -0.0293 -0.0109 171 LYS A CD  
1776 C  CD  B LYS A 171 ? 0.2987 0.1764 0.1271 -0.0375 -0.0034 -0.0082 171 LYS A CD  
1777 C  CE  A LYS A 171 ? 0.2301 0.4810 0.3537 0.0509  0.0230  0.0842  171 LYS A CE  
1778 C  CE  B LYS A 171 ? 0.3713 0.1798 0.1281 -0.0500 0.0043  -0.0031 171 LYS A CE  
1779 N  NZ  A LYS A 171 ? 0.3375 0.6007 0.2901 0.1418  -0.0277 -0.1096 171 LYS A NZ  
1780 N  NZ  B LYS A 171 ? 0.4801 0.3143 0.3763 -0.1324 -0.2072 0.0865  171 LYS A NZ  
1781 N  N   A SER A 172 ? 0.1154 0.1623 0.1158 0.0052  0.0154  0.0265  172 SER A N   
1782 N  N   B SER A 172 ? 0.1134 0.1152 0.0860 -0.0174 0.0035  0.0073  172 SER A N   
1783 C  CA  A SER A 172 ? 0.1049 0.1852 0.1179 -0.0125 0.0017  0.0065  172 SER A CA  
1784 C  CA  B SER A 172 ? 0.1163 0.0890 0.0908 -0.0082 0.0162  0.0285  172 SER A CA  
1785 C  C   A SER A 172 ? 0.1328 0.1504 0.0727 -0.0273 0.0093  0.0197  172 SER A C   
1786 C  C   B SER A 172 ? 0.1154 0.1330 0.0870 -0.0103 0.0115  0.0259  172 SER A C   
1787 O  O   A SER A 172 ? 0.1606 0.1784 0.0693 -0.0070 0.0155  0.0163  172 SER A O   
1788 O  O   B SER A 172 ? 0.1626 0.1711 0.0772 -0.0114 0.0132  0.0458  172 SER A O   
1789 C  CB  A SER A 172 ? 0.1254 0.1989 0.0899 -0.0472 0.0026  -0.0027 172 SER A CB  
1790 C  CB  B SER A 172 ? 0.1450 0.0917 0.1404 -0.0208 0.0258  0.0175  172 SER A CB  
1791 O  OG  A SER A 172 ? 0.2201 0.1693 0.1335 0.0060  -0.0153 0.0184  172 SER A OG  
1792 O  OG  B SER A 172 ? 0.1423 0.1342 0.1396 0.0086  0.0483  0.0241  172 SER A OG  
1793 N  N   A ALA A 173 ? 0.1154 0.1488 0.1030 0.0041  0.0020  0.0463  173 ALA A N   
1794 N  N   B ALA A 173 ? 0.1280 0.1726 0.0852 -0.0172 0.0199  0.0041  173 ALA A N   
1795 C  CA  A ALA A 173 ? 0.1407 0.1669 0.0785 -0.0046 -0.0108 0.0392  173 ALA A CA  
1796 C  CA  B ALA A 173 ? 0.0992 0.1411 0.1732 -0.0141 0.0017  0.0203  173 ALA A CA  
1797 C  C   A ALA A 173 ? 0.1234 0.1861 0.0794 -0.0124 -0.0182 0.0500  173 ALA A C   
1798 C  C   B ALA A 173 ? 0.1254 0.1384 0.0929 0.0082  -0.0034 0.0476  173 ALA A C   
1799 O  O   A ALA A 173 ? 0.1432 0.1673 0.0763 0.0452  -0.0182 0.0329  173 ALA A O   
1800 O  O   B ALA A 173 ? 0.1619 0.1725 0.0755 0.0610  0.0131  0.0353  173 ALA A O   
1801 C  CB  A ALA A 173 ? 0.1726 0.1782 0.1136 -0.0109 -0.0010 -0.0132 173 ALA A CB  
1802 C  CB  B ALA A 173 ? 0.1304 0.1583 0.1202 0.0038  0.0000  -0.0210 173 ALA A CB  
1803 N  N   A ASP A 174 ? 0.1552 0.1622 0.0485 -0.0184 -0.0131 0.0513  174 ASP A N   
1804 N  N   B ASP A 174 ? 0.1185 0.1750 0.0885 0.0296  0.0148  0.0566  174 ASP A N   
1805 C  CA  A ASP A 174 ? 0.1524 0.2116 0.0649 -0.0129 -0.0077 0.0054  174 ASP A CA  
1806 C  CA  B ASP A 174 ? 0.0872 0.1721 0.1508 0.0255  0.0161  0.0627  174 ASP A CA  
1807 C  C   A ASP A 174 ? 0.1814 0.1527 0.1222 0.0098  -0.0175 0.0274  174 ASP A C   
1808 C  C   B ASP A 174 ? 0.1969 0.1666 0.1317 -0.0315 -0.0038 0.0511  174 ASP A C   
1809 O  O   A ASP A 174 ? 0.1279 0.1955 0.2517 0.0043  -0.0285 -0.0577 174 ASP A O   
1810 O  O   B ASP A 174 ? 0.1495 0.2231 0.1330 0.0313  -0.0579 0.0010  174 ASP A O   
1811 C  CB  A ASP A 174 ? 0.2894 0.3790 0.2926 0.1023  -0.0239 0.1115  174 ASP A CB  
1812 C  CB  B ASP A 174 ? 0.1360 0.2443 0.2469 0.0872  -0.0164 0.0922  174 ASP A CB  
1813 C  CG  A ASP A 174 ? 0.3777 0.3777 0.3341 0.0520  -0.0894 0.0798  174 ASP A CG  
1814 C  CG  B ASP A 174 ? 0.3935 0.2741 0.2400 0.0012  -0.0891 0.1333  174 ASP A CG  
1815 O  OD1 A ASP A 174 ? 0.5023 0.4555 0.6445 -0.1273 -0.0148 0.2319  174 ASP A OD1 
1816 O  OD1 B ASP A 174 ? 0.4027 0.4370 0.2813 -0.0768 -0.0303 0.1164  174 ASP A OD1 
1817 O  OD2 A ASP A 174 ? 0.1723 0.4595 0.6176 -0.1503 -0.0493 0.0421  174 ASP A OD2 
1818 O  OD2 B ASP A 174 ? 0.6294 0.4043 0.2644 -0.0432 0.0000  0.0679  174 ASP A OD2 
1819 N  N   A PHE A 175 ? 0.1502 0.1824 0.0852 0.0082  -0.0355 0.0262  175 PHE A N   
1820 N  N   B PHE A 175 ? 0.1423 0.1526 0.1221 -0.0088 -0.0273 0.0227  175 PHE A N   
1821 C  CA  A PHE A 175 ? 0.1375 0.1353 0.1319 0.0104  -0.0251 0.0183  175 PHE A CA  
1822 C  CA  B PHE A 175 ? 0.1622 0.1089 0.1222 0.0137  -0.0141 0.0381  175 PHE A CA  
1823 C  C   A PHE A 175 ? 0.1107 0.1418 0.1368 0.0132  -0.0340 0.0233  175 PHE A C   
1824 C  C   B PHE A 175 ? 0.1055 0.2075 0.1149 -0.0054 -0.0230 0.0197  175 PHE A C   
1825 O  O   A PHE A 175 ? 0.1714 0.1911 0.1450 0.0439  -0.0581 -0.0126 175 PHE A O   
1826 O  O   B PHE A 175 ? 0.1711 0.1179 0.1199 -0.0038 -0.0507 0.0186  175 PHE A O   
1827 C  CB  A PHE A 175 ? 0.0987 0.1488 0.1536 -0.0057 -0.0093 0.0386  175 PHE A CB  
1828 C  CB  B PHE A 175 ? 0.1168 0.1452 0.1287 -0.0020 -0.0296 0.0317  175 PHE A CB  
1829 C  CG  A PHE A 175 ? 0.1375 0.1351 0.1762 -0.0381 -0.0766 0.0154  175 PHE A CG  
1830 C  CG  B PHE A 175 ? 0.1635 0.1111 0.1172 0.0131  -0.0237 0.0219  175 PHE A CG  
1831 C  CD1 A PHE A 175 ? 0.2373 0.1064 0.2125 0.0353  -0.0816 -0.0093 175 PHE A CD1 
1832 C  CD1 B PHE A 175 ? 0.1779 0.1177 0.2055 0.0104  -0.0978 0.0142  175 PHE A CD1 
1833 C  CD2 A PHE A 175 ? 0.2567 0.0715 0.1653 -0.0239 -0.1180 0.0132  175 PHE A CD2 
1834 C  CD2 B PHE A 175 ? 0.2666 0.1170 0.1396 0.0355  0.0226  0.0666  175 PHE A CD2 
1835 C  CE1 A PHE A 175 ? 0.3431 0.1324 0.1671 0.0141  -0.0454 -0.0337 175 PHE A CE1 
1836 C  CE1 B PHE A 175 ? 0.2091 0.1127 0.2140 0.0087  -0.0865 -0.0136 175 PHE A CE1 
1837 C  CE2 A PHE A 175 ? 0.3300 0.0683 0.1806 -0.0375 -0.1679 0.0244  175 PHE A CE2 
1838 C  CE2 B PHE A 175 ? 0.2827 0.1172 0.1878 -0.0441 -0.0293 0.0093  175 PHE A CE2 
1839 C  CZ  A PHE A 175 ? 0.2662 0.0755 0.1753 0.0115  -0.0983 -0.0126 175 PHE A CZ  
1840 C  CZ  B PHE A 175 ? 0.2779 0.1371 0.1981 0.0428  -0.0873 -0.0318 175 PHE A CZ  
1841 N  N   A THR A 176 ? 0.1933 0.1552 0.0863 0.0577  -0.0197 0.0513  176 THR A N   
1842 N  N   B THR A 176 ? 0.1305 0.1735 0.1475 0.0307  -0.0318 0.0142  176 THR A N   
1843 C  CA  A THR A 176 ? 0.1568 0.1364 0.1125 0.0252  -0.0185 0.0595  176 THR A CA  
1844 C  CA  B THR A 176 ? 0.0881 0.1951 0.1629 0.0230  0.0057  0.0656  176 THR A CA  
1845 C  C   A THR A 176 ? 0.1648 0.1091 0.1259 0.0189  0.0000  0.0307  176 THR A C   
1846 C  C   B THR A 176 ? 0.1170 0.1640 0.0609 -0.0013 -0.0208 0.0579  176 THR A C   
1847 O  O   A THR A 176 ? 0.1947 0.1326 0.1136 0.0027  -0.0617 0.0310  176 THR A O   
1848 O  O   B THR A 176 ? 0.1391 0.1358 0.1604 0.0185  -0.0222 0.0825  176 THR A O   
1849 C  CB  A THR A 176 ? 0.1757 0.1190 0.0872 0.0283  0.0081  0.0472  176 THR A CB  
1850 C  CB  B THR A 176 ? 0.1614 0.1506 0.1355 -0.0071 -0.0074 0.0304  176 THR A CB  
1851 O  OG1 A THR A 176 ? 0.2919 0.2125 0.0854 0.1084  -0.0041 0.0439  176 THR A OG1 
1852 O  OG1 B THR A 176 ? 0.2039 0.1872 0.1173 0.0228  -0.0244 0.0456  176 THR A OG1 
1853 C  CG2 A THR A 176 ? 0.1755 0.1958 0.1766 0.0222  0.0196  0.1076  176 THR A CG2 
1854 C  CG2 B THR A 176 ? 0.1554 0.2070 0.2154 -0.0054 0.0197  0.0551  176 THR A CG2 
1855 N  N   A ASN A 177 ? 0.1629 0.1554 0.0872 0.0015  -0.0052 0.0566  177 ASN A N   
1856 N  N   B ASN A 177 ? 0.1475 0.1787 0.0648 0.0000  0.0000  0.0706  177 ASN A N   
1857 C  CA  A ASN A 177 ? 0.1398 0.1632 0.1084 -0.0130 -0.0656 0.0500  177 ASN A CA  
1858 C  CA  B ASN A 177 ? 0.1362 0.1886 0.0891 -0.0225 -0.0006 0.0324  177 ASN A CA  
1859 C  C   A ASN A 177 ? 0.1376 0.1447 0.1491 -0.0313 -0.0548 0.0467  177 ASN A C   
1860 C  C   B ASN A 177 ? 0.0888 0.1685 0.1628 -0.0189 -0.0320 0.0395  177 ASN A C   
1861 O  O   A ASN A 177 ? 0.1254 0.1793 0.2449 -0.0432 -0.1026 0.0843  177 ASN A O   
1862 O  O   B ASN A 177 ? 0.0913 0.2107 0.1879 -0.0313 -0.0227 0.0974  177 ASN A O   
1863 C  CB  A ASN A 177 ? 0.2298 0.1190 0.1473 -0.0153 -0.1198 0.0264  177 ASN A CB  
1864 C  CB  B ASN A 177 ? 0.1996 0.2159 0.1624 -0.0474 -0.0706 0.0834  177 ASN A CB  
1865 C  CG  A ASN A 177 ? 0.3298 0.0845 0.2454 0.0038  -0.0595 0.0152  177 ASN A CG  
1866 C  CG  B ASN A 177 ? 0.3046 0.2475 0.1556 0.0035  -0.1534 0.0485  177 ASN A CG  
1867 O  OD1 A ASN A 177 ? 0.2980 0.1567 0.1190 0.0153  -0.0948 0.0364  177 ASN A OD1 
1868 O  OD1 B ASN A 177 ? 0.3294 0.2125 0.2091 0.0209  -0.1203 0.0577  177 ASN A OD1 
1869 N  ND2 A ASN A 177 ? 0.2991 0.1133 0.1369 0.0625  -0.0948 0.0364  177 ASN A ND2 
1870 N  ND2 B ASN A 177 ? 0.4887 0.2131 0.1341 -0.0137 -0.1862 0.0700  177 ASN A ND2 
1871 N  N   A PHE A 178 ? 0.1538 0.1129 0.0879 -0.0041 -0.0423 0.0220  178 PHE A N   
1872 N  N   B PHE A 178 ? 0.1225 0.1869 0.1142 -0.0030 -0.0395 0.0693  178 PHE A N   
1873 C  CA  A PHE A 178 ? 0.1326 0.1509 0.1014 0.0173  -0.0346 0.0529  178 PHE A CA  
1874 C  CA  B PHE A 178 ? 0.1116 0.1707 0.1023 0.0080  -0.0020 0.0540  178 PHE A CA  
1875 C  C   A PHE A 178 ? 0.1299 0.1272 0.0988 -0.0177 -0.0232 0.0405  178 PHE A C   
1876 C  C   B PHE A 178 ? 0.1057 0.1456 0.1237 -0.0132 -0.0108 0.0197  178 PHE A C   
1877 O  O   A PHE A 178 ? 0.1382 0.1402 0.0985 -0.0194 -0.0240 0.0377  178 PHE A O   
1878 O  O   B PHE A 178 ? 0.1879 0.1423 0.0996 -0.0209 -0.0218 0.0137  178 PHE A O   
1879 C  CB  A PHE A 178 ? 0.1439 0.1281 0.0841 0.0041  -0.0140 0.0251  178 PHE A CB  
1880 C  CB  B PHE A 178 ? 0.1061 0.1885 0.0988 -0.0040 -0.0295 0.0762  178 PHE A CB  
1881 C  CG  A PHE A 178 ? 0.1355 0.1230 0.1027 -0.0231 -0.0305 0.0252  178 PHE A CG  
1882 C  CG  B PHE A 178 ? 0.1500 0.1421 0.1091 -0.0351 -0.0553 0.0483  178 PHE A CG  
1883 C  CD1 A PHE A 178 ? 0.1412 0.1513 0.1290 -0.0399 -0.0573 0.0209  178 PHE A CD1 
1884 C  CD1 B PHE A 178 ? 0.1369 0.1692 0.0722 -0.0408 -0.0463 0.0372  178 PHE A CD1 
1885 C  CD2 A PHE A 178 ? 0.1522 0.1418 0.0947 -0.0595 -0.0242 0.0340  178 PHE A CD2 
1886 C  CD2 B PHE A 178 ? 0.1283 0.1507 0.0879 -0.0186 -0.0339 0.0439  178 PHE A CD2 
1887 C  CE1 A PHE A 178 ? 0.1647 0.1134 0.1263 -0.0043 -0.0436 -0.0026 178 PHE A CE1 
1888 C  CE1 B PHE A 178 ? 0.1036 0.1385 0.1181 -0.0244 -0.0114 0.0395  178 PHE A CE1 
1889 C  CE2 A PHE A 178 ? 0.1102 0.1254 0.0913 0.0065  -0.0177 0.0136  178 PHE A CE2 
1890 C  CE2 B PHE A 178 ? 0.1281 0.1109 0.1974 -0.0071 -0.0829 0.0527  178 PHE A CE2 
1891 C  CZ  A PHE A 178 ? 0.1066 0.1495 0.1023 -0.0154 -0.0065 0.0170  178 PHE A CZ  
1892 C  CZ  B PHE A 178 ? 0.1635 0.1229 0.1181 -0.0331 -0.0439 0.0667  178 PHE A CZ  
1893 N  N   A ASP A 179 ? 0.1127 0.1301 0.1172 -0.0161 -0.0294 0.0379  179 ASP A N   
1894 N  N   B ASP A 179 ? 0.1036 0.1807 0.0924 0.0000  -0.0137 0.0548  179 ASP A N   
1895 C  CA  A ASP A 179 ? 0.0994 0.1569 0.1242 0.0006  -0.0247 0.0109  179 ASP A CA  
1896 C  CA  B ASP A 179 ? 0.0956 0.1561 0.1172 0.0080  -0.0054 0.0377  179 ASP A CA  
1897 C  C   A ASP A 179 ? 0.1513 0.1215 0.1159 -0.0141 -0.0368 0.0000  179 ASP A C   
1898 C  C   B ASP A 179 ? 0.1611 0.1109 0.1441 -0.0054 -0.0584 0.0195  179 ASP A C   
1899 O  O   A ASP A 179 ? 0.1500 0.1102 0.1238 0.0027  -0.0160 -0.0043 179 ASP A O   
1900 O  O   B ASP A 179 ? 0.1299 0.1170 0.0900 -0.0110 -0.0172 0.0109  179 ASP A O   
1901 C  CB  A ASP A 179 ? 0.0951 0.2287 0.1253 -0.0091 -0.0348 0.0397  179 ASP A CB  
1902 C  CB  B ASP A 179 ? 0.1158 0.1669 0.1710 -0.0333 0.0220  0.0423  179 ASP A CB  
1903 C  CG  A ASP A 179 ? 0.1653 0.2030 0.1818 0.0604  -0.0469 -0.0186 179 ASP A CG  
1904 C  CG  B ASP A 179 ? 0.0966 0.2266 0.1912 0.0394  0.0204  -0.0065 179 ASP A CG  
1905 O  OD1 A ASP A 179 ? 0.1098 0.1446 0.1289 0.0292  -0.0006 0.0445  179 ASP A OD1 
1906 O  OD1 B ASP A 179 ? 0.1502 0.1976 0.1423 0.0098  0.0121  0.0403  179 ASP A OD1 
1907 O  OD2 A ASP A 179 ? 0.1793 0.3161 0.2445 0.1080  -0.0931 -0.0617 179 ASP A OD2 
1908 O  OD2 B ASP A 179 ? 0.1163 0.3323 0.3264 0.0164  0.0230  -0.0617 179 ASP A OD2 
1909 N  N   A PRO A 180 ? 0.1739 0.1231 0.0913 0.0013  -0.0623 0.0037  180 PRO A N   
1910 N  N   B PRO A 180 ? 0.1737 0.1204 0.1181 -0.0318 -0.0579 0.0362  180 PRO A N   
1911 C  CA  A PRO A 180 ? 0.2003 0.1071 0.1102 0.0121  -0.0535 0.0173  180 PRO A CA  
1912 C  CA  B PRO A 180 ? 0.1965 0.1268 0.1421 -0.0062 -0.0666 0.0331  180 PRO A CA  
1913 C  C   A PRO A 180 ? 0.1696 0.1362 0.1240 0.0104  -0.0581 0.0081  180 PRO A C   
1914 C  C   B PRO A 180 ? 0.1671 0.1137 0.1290 0.0073  -0.0763 0.0092  180 PRO A C   
1915 O  O   A PRO A 180 ? 0.1736 0.1455 0.0951 0.0030  -0.0417 0.0054  180 PRO A O   
1916 O  O   B PRO A 180 ? 0.1910 0.0850 0.1497 0.0031  -0.0653 0.0104  180 PRO A O   
1917 C  CB  A PRO A 180 ? 0.2127 0.1511 0.0833 0.0199  -0.0746 -0.0131 180 PRO A CB  
1918 C  CB  B PRO A 180 ? 0.1723 0.1599 0.1906 0.0030  -0.0974 0.0230  180 PRO A CB  
1919 C  CG  A PRO A 180 ? 0.1610 0.1067 0.1075 -0.0285 -0.0342 0.0017  180 PRO A CG  
1920 C  CG  B PRO A 180 ? 0.1492 0.1430 0.1667 -0.0261 -0.0606 0.0285  180 PRO A CG  
1921 C  CD  A PRO A 180 ? 0.1347 0.1395 0.1290 -0.0151 -0.0636 0.0065  180 PRO A CD  
1922 C  CD  B PRO A 180 ? 0.1565 0.1220 0.1303 -0.0206 -0.0364 0.0291  180 PRO A CD  
1923 N  N   . ARG A 181 ? 0.1747 0.1371 0.1624 0.0152  -0.0649 0.0195  181 ARG A N   
1924 C  CA  . ARG A 181 ? 0.1596 0.1392 0.1832 0.0166  -0.0772 0.0060  181 ARG A CA  
1925 C  C   . ARG A 181 ? 0.1612 0.1383 0.1739 0.0172  -0.0900 0.0093  181 ARG A C   
1926 O  O   . ARG A 181 ? 0.2070 0.1502 0.2030 0.0104  -0.0784 0.0296  181 ARG A O   
1927 C  CB  . ARG A 181 ? 0.1454 0.1486 0.2467 0.0027  -0.0586 0.0088  181 ARG A CB  
1928 C  CG  . ARG A 181 ? 0.1841 0.1459 0.2912 0.0173  -0.0115 -0.0074 181 ARG A CG  
1929 C  CD  . ARG A 181 ? 0.1797 0.1895 0.3508 0.0255  0.0260  0.0148  181 ARG A CD  
1930 N  NE  . ARG A 181 ? 0.1644 0.2113 0.3386 0.0397  -0.0162 0.0636  181 ARG A NE  
1931 C  CZ  . ARG A 181 ? 0.1468 0.2228 0.3352 0.0147  0.0196  0.0643  181 ARG A CZ  
1932 N  NH1 . ARG A 181 ? 0.1601 0.4068 0.3871 0.0441  0.0597  0.0711  181 ARG A NH1 
1933 N  NH2 . ARG A 181 ? 0.2987 0.2687 0.3862 0.0346  -0.0153 0.1424  181 ARG A NH2 
1934 N  N   . GLY A 182 ? 0.2053 0.1430 0.1761 0.0281  -0.1106 -0.0013 182 GLY A N   
1935 C  CA  . GLY A 182 ? 0.2784 0.1197 0.1944 0.0351  -0.0982 0.0049  182 GLY A CA  
1936 C  C   . GLY A 182 ? 0.2230 0.1208 0.1747 0.0196  -0.0890 -0.0005 182 GLY A C   
1937 O  O   . GLY A 182 ? 0.2818 0.1365 0.1623 0.0030  -0.0882 0.0024  182 GLY A O   
1938 N  N   . LEU A 183 ? 0.2208 0.1348 0.1470 0.0265  -0.0873 -0.0041 183 LEU A N   
1939 C  CA  . LEU A 183 ? 0.1910 0.1347 0.1324 0.0368  -0.0710 -0.0080 183 LEU A CA  
1940 C  C   . LEU A 183 ? 0.1908 0.1009 0.1581 0.0024  -0.0661 0.0015  183 LEU A C   
1941 O  O   . LEU A 183 ? 0.1800 0.1240 0.1620 0.0193  -0.0540 0.0221  183 LEU A O   
1942 C  CB  . LEU A 183 ? 0.1747 0.1590 0.1319 0.0432  -0.0640 0.0073  183 LEU A CB  
1943 C  CG  . LEU A 183 ? 0.2818 0.1653 0.1026 0.0649  -0.0929 0.0068  183 LEU A CG  
1944 C  CD1 . LEU A 183 ? 0.3046 0.2481 0.1364 0.0265  -0.0601 0.0252  183 LEU A CD1 
1945 C  CD2 . LEU A 183 ? 0.2982 0.1983 0.1532 0.0975  -0.0456 -0.0251 183 LEU A CD2 
1946 N  N   A LEU A 184 ? 0.1784 0.1333 0.1545 0.0187  -0.0653 0.0178  184 LEU A N   
1947 N  N   B LEU A 184 ? 0.1867 0.0992 0.1474 0.0031  -0.0505 -0.0026 184 LEU A N   
1948 C  CA  A LEU A 184 ? 0.1416 0.1172 0.1596 -0.0162 -0.0737 0.0175  184 LEU A CA  
1949 C  CA  B LEU A 184 ? 0.1651 0.1127 0.1488 -0.0148 -0.0454 -0.0037 184 LEU A CA  
1950 C  C   A LEU A 184 ? 0.1046 0.1053 0.1493 0.0206  -0.0351 0.0153  184 LEU A C   
1951 C  C   B LEU A 184 ? 0.1167 0.1155 0.1430 -0.0071 -0.0494 -0.0104 184 LEU A C   
1952 O  O   A LEU A 184 ? 0.0992 0.1301 0.1369 -0.0085 -0.0043 0.0060  184 LEU A O   
1953 O  O   B LEU A 184 ? 0.1254 0.1259 0.1256 -0.0092 -0.0386 -0.0137 184 LEU A O   
1954 C  CB  A LEU A 184 ? 0.1495 0.1145 0.1445 -0.0015 -0.0586 0.0331  184 LEU A CB  
1955 C  CB  B LEU A 184 ? 0.0899 0.1376 0.1718 -0.0317 -0.0522 -0.0065 184 LEU A CB  
1956 C  CG  A LEU A 184 ? 0.0772 0.1150 0.1739 0.0086  -0.0292 0.0326  184 LEU A CG  
1957 C  CG  B LEU A 184 ? 0.1208 0.1331 0.1364 -0.0207 0.0017  0.0071  184 LEU A CG  
1958 C  CD1 A LEU A 184 ? 0.1010 0.1277 0.1975 0.0038  0.0126  0.0263  184 LEU A CD1 
1959 C  CD1 B LEU A 184 ? 0.1389 0.1861 0.1619 -0.0006 0.0401  -0.0020 184 LEU A CD1 
1960 C  CD2 A LEU A 184 ? 0.0852 0.1387 0.2181 0.0074  -0.0500 0.0381  184 LEU A CD2 
1961 C  CD2 B LEU A 184 ? 0.1018 0.1290 0.2007 -0.0247 -0.0059 0.0220  184 LEU A CD2 
1962 N  N   A PRO A 185 ? 0.0931 0.1111 0.1308 0.0068  -0.0109 0.0207  185 PRO A N   
1963 N  N   B PRO A 185 ? 0.1398 0.1049 0.1247 -0.0219 -0.0287 -0.0121 185 PRO A N   
1964 C  CA  A PRO A 185 ? 0.0640 0.1035 0.1405 0.0200  0.0120  0.0137  185 PRO A CA  
1965 C  CA  B PRO A 185 ? 0.1091 0.1057 0.1137 0.0136  -0.0068 0.0120  185 PRO A CA  
1966 C  C   A PRO A 185 ? 0.0631 0.1084 0.1328 0.0085  0.0152  0.0000  185 PRO A C   
1967 C  C   B PRO A 185 ? 0.0737 0.1287 0.1304 -0.0120 -0.0205 0.0206  185 PRO A C   
1968 O  O   A PRO A 185 ? 0.0636 0.0940 0.1280 0.0071  0.0231  0.0097  185 PRO A O   
1969 O  O   B PRO A 185 ? 0.0612 0.1333 0.1398 0.0098  0.0065  0.0189  185 PRO A O   
1970 C  CB  A PRO A 185 ? 0.0648 0.1199 0.1562 0.0480  0.0110  -0.0104 185 PRO A CB  
1971 C  CB  B PRO A 185 ? 0.1292 0.1152 0.1014 -0.0156 -0.0175 0.0178  185 PRO A CB  
1972 C  CG  A PRO A 185 ? 0.0719 0.1215 0.1071 0.0395  -0.0024 0.0131  185 PRO A CG  
1973 C  CG  B PRO A 185 ? 0.1355 0.1298 0.1190 -0.0153 0.0096  -0.0148 185 PRO A CG  
1974 C  CD  A PRO A 185 ? 0.0758 0.1534 0.0992 0.0183  0.0068  0.0156  185 PRO A CD  
1975 C  CD  B PRO A 185 ? 0.1301 0.0886 0.1149 -0.0193 -0.0080 -0.0276 185 PRO A CD  
1976 N  N   A GLU A 186 ? 0.0617 0.1107 0.1887 0.0024  0.0331  -0.0049 186 GLU A N   
1977 N  N   B GLU A 186 ? 0.0640 0.1194 0.2154 -0.0274 -0.0035 -0.0037 186 GLU A N   
1978 C  CA  A GLU A 186 ? 0.0776 0.1265 0.1951 0.0228  0.0337  -0.0054 186 GLU A CA  
1979 C  CA  B GLU A 186 ? 0.0715 0.1499 0.2282 -0.0406 -0.0019 -0.0230 186 GLU A CA  
1980 C  C   A GLU A 186 ? 0.0432 0.1459 0.2495 -0.0020 0.0052  -0.0115 186 GLU A C   
1981 C  C   B GLU A 186 ? 0.1170 0.1344 0.2299 -0.0174 -0.0023 -0.0010 186 GLU A C   
1982 O  O   A GLU A 186 ? 0.0771 0.1684 0.1965 0.0238  0.0247  0.0051  186 GLU A O   
1983 O  O   B GLU A 186 ? 0.0737 0.1892 0.2134 0.0214  -0.0048 0.0284  186 GLU A O   
1984 C  CB  A GLU A 186 ? 0.1233 0.1308 0.1689 -0.0086 0.0299  -0.0228 186 GLU A CB  
1985 C  CB  B GLU A 186 ? 0.1193 0.1511 0.1359 -0.0504 0.0162  -0.0046 186 GLU A CB  
1986 C  CG  A GLU A 186 ? 0.1908 0.1380 0.1240 -0.0394 0.0416  -0.0137 186 GLU A CG  
1987 C  CG  B GLU A 186 ? 0.1084 0.1337 0.2463 -0.0097 -0.0225 -0.0615 186 GLU A CG  
1988 C  CD  A GLU A 186 ? 0.1357 0.1720 0.1647 -0.0518 0.0357  0.0046  186 GLU A CD  
1989 C  CD  B GLU A 186 ? 0.2120 0.1755 0.2346 -0.0386 -0.0087 0.0027  186 GLU A CD  
1990 O  OE1 A GLU A 186 ? 0.1772 0.1462 0.1978 -0.0368 -0.0252 0.0184  186 GLU A OE1 
1991 O  OE1 B GLU A 186 ? 0.1728 0.2213 0.2035 -0.0160 -0.0293 -0.0062 186 GLU A OE1 
1992 O  OE2 A GLU A 186 ? 0.1420 0.2229 0.1578 -0.0904 0.0010  0.0054  186 GLU A OE2 
1993 O  OE2 B GLU A 186 ? 0.3143 0.2703 0.2289 -0.0537 -0.0656 0.0167  186 GLU A OE2 
1994 N  N   . SER A 187 ? 0.0824 0.1556 0.2779 -0.0129 -0.0254 0.0038  187 SER A N   
1995 C  CA  . SER A 187 ? 0.0679 0.1640 0.2511 -0.0034 -0.0010 0.0077  187 SER A CA  
1996 C  C   . SER A 187 ? 0.0662 0.1720 0.2265 -0.0063 0.0162  0.0024  187 SER A C   
1997 O  O   . SER A 187 ? 0.0827 0.1844 0.2314 -0.0065 0.0156  -0.0208 187 SER A O   
1998 C  CB  . SER A 187 ? 0.1272 0.1756 0.2364 0.0024  0.0125  0.0065  187 SER A CB  
1999 O  OG  . SER A 187 ? 0.1111 0.2093 0.2350 -0.0205 0.0186  0.0162  187 SER A OG  
2000 N  N   . LEU A 188 ? 0.0838 0.1565 0.2406 0.0048  0.0006  -0.0104 188 LEU A N   
2001 C  CA  . LEU A 188 ? 0.1206 0.1385 0.2319 -0.0153 0.0031  -0.0109 188 LEU A CA  
2002 C  C   . LEU A 188 ? 0.0827 0.1538 0.2255 0.0048  0.0263  -0.0474 188 LEU A C   
2003 O  O   . LEU A 188 ? 0.1285 0.2034 0.2010 -0.0194 0.0041  -0.0520 188 LEU A O   
2004 C  CB  . LEU A 188 ? 0.1181 0.1775 0.3206 -0.0269 -0.0054 0.0174  188 LEU A CB  
2005 C  CG  . LEU A 188 ? 0.0929 0.1559 0.3558 -0.0003 -0.0031 0.0038  188 LEU A CG  
2006 C  CD1 . LEU A 188 ? 0.1486 0.1474 0.4566 -0.0142 -0.0640 0.0102  188 LEU A CD1 
2007 C  CD2 . LEU A 188 ? 0.1058 0.2187 0.3591 -0.0060 0.0131  0.0540  188 LEU A CD2 
2008 N  N   . ASP A 189 ? 0.0838 0.2084 0.1825 -0.0003 0.0294  -0.0219 189 ASP A N   
2009 C  CA  . ASP A 189 ? 0.0794 0.2466 0.1922 -0.0500 0.0379  -0.0209 189 ASP A CA  
2010 C  C   . ASP A 189 ? 0.0667 0.1446 0.1495 -0.0068 0.0230  -0.0129 189 ASP A C   
2011 O  O   . ASP A 189 ? 0.0827 0.1384 0.1335 -0.0148 0.0218  -0.0054 189 ASP A O   
2012 C  CB  . ASP A 189 ? 0.1472 0.2682 0.1728 -0.1096 0.0564  0.0010  189 ASP A CB  
2013 C  CG  . ASP A 189 ? 0.1411 0.3689 0.2531 -0.1014 0.0271  -0.0277 189 ASP A CG  
2014 O  OD1 . ASP A 189 ? 0.1290 0.5199 0.3082 -0.0841 0.1272  -0.1106 189 ASP A OD1 
2015 O  OD2 . ASP A 189 ? 0.2274 0.6183 0.2782 -0.1914 0.0000  0.1164  189 ASP A OD2 
2016 N  N   . TYR A 190 ? 0.0794 0.1635 0.1152 -0.0164 0.0297  -0.0017 190 TYR A N   
2017 C  CA  . TYR A 190 ? 0.0706 0.1378 0.1111 -0.0130 0.0175  -0.0020 190 TYR A CA  
2018 C  C   . TYR A 190 ? 0.0868 0.1199 0.0745 -0.0114 0.0178  -0.0048 190 TYR A C   
2019 O  O   . TYR A 190 ? 0.1085 0.1541 0.0961 -0.0020 0.0474  -0.0010 190 TYR A O   
2020 C  CB  . TYR A 190 ? 0.0967 0.1384 0.1037 0.0043  0.0357  -0.0057 190 TYR A CB  
2021 C  CG  . TYR A 190 ? 0.1003 0.1412 0.1003 -0.0115 0.0062  0.0109  190 TYR A CG  
2022 C  CD1 . TYR A 190 ? 0.0917 0.1660 0.0983 -0.0192 0.0263  0.0006  190 TYR A CD1 
2023 C  CD2 . TYR A 190 ? 0.1093 0.1576 0.1455 -0.0038 0.0251  0.0010  190 TYR A CD2 
2024 C  CE1 . TYR A 190 ? 0.1106 0.1581 0.1348 -0.0211 0.0373  -0.0068 190 TYR A CE1 
2025 C  CE2 . TYR A 190 ? 0.1401 0.1500 0.1387 -0.0062 0.0146  -0.0019 190 TYR A CE2 
2026 C  CZ  . TYR A 190 ? 0.1271 0.1571 0.1224 -0.0194 0.0315  -0.0143 190 TYR A CZ  
2027 O  OH  . TYR A 190 ? 0.1427 0.1716 0.1579 0.0081  0.0183  -0.0331 190 TYR A OH  
2028 N  N   . TRP A 191 ? 0.0798 0.1061 0.0900 -0.0104 0.0219  0.0081  191 TRP A N   
2029 C  CA  . TRP A 191 ? 0.0944 0.1003 0.0917 0.0003  0.0177  0.0034  191 TRP A CA  
2030 C  C   . TRP A 191 ? 0.0753 0.1143 0.0675 -0.0059 0.0175  0.0043  191 TRP A C   
2031 O  O   . TRP A 191 ? 0.1185 0.1125 0.0728 -0.0247 0.0175  -0.0019 191 TRP A O   
2032 C  CB  . TRP A 191 ? 0.1159 0.1040 0.1102 0.0057  0.0155  -0.0006 191 TRP A CB  
2033 C  CG  . TRP A 191 ? 0.0951 0.1001 0.0969 0.0146  0.0219  0.0000  191 TRP A CG  
2034 C  CD1 . TRP A 191 ? 0.1493 0.1154 0.1111 0.0052  0.0296  0.0159  191 TRP A CD1 
2035 C  CD2 . TRP A 191 ? 0.0920 0.1161 0.1116 0.0170  0.0160  0.0065  191 TRP A CD2 
2036 N  NE1 . TRP A 191 ? 0.1571 0.1369 0.1170 0.0020  0.0208  0.0200  191 TRP A NE1 
2037 C  CE2 . TRP A 191 ? 0.1076 0.1136 0.1233 -0.0026 0.0136  0.0126  191 TRP A CE2 
2038 C  CE3 . TRP A 191 ? 0.1005 0.1129 0.1254 0.0109  0.0108  -0.0065 191 TRP A CE3 
2039 C  CZ2 . TRP A 191 ? 0.1231 0.1125 0.1536 0.0167  -0.0063 0.0082  191 TRP A CZ2 
2040 C  CZ3 . TRP A 191 ? 0.0861 0.1335 0.1614 -0.0046 0.0164  -0.0074 191 TRP A CZ3 
2041 C  CH2 . TRP A 191 ? 0.1145 0.1186 0.1692 0.0093  -0.0003 -0.0148 191 TRP A CH2 
2042 N  N   . THR A 192 ? 0.0900 0.1014 0.0803 -0.0126 0.0120  0.0030  192 THR A N   
2043 C  CA  . THR A 192 ? 0.0872 0.0944 0.0833 -0.0023 0.0046  0.0020  192 THR A CA  
2044 C  C   . THR A 192 ? 0.0895 0.1057 0.0722 0.0088  0.0054  -0.0109 192 THR A C   
2045 O  O   . THR A 192 ? 0.1088 0.1315 0.0636 0.0068  0.0126  -0.0087 192 THR A O   
2046 C  CB  . THR A 192 ? 0.0970 0.1066 0.0790 0.0080  0.0252  0.0003  192 THR A CB  
2047 O  OG1 . THR A 192 ? 0.0917 0.0872 0.1000 0.0060  0.0119  -0.0065 192 THR A OG1 
2048 C  CG2 . THR A 192 ? 0.1206 0.1228 0.0818 0.0146  0.0350  -0.0076 192 THR A CG2 
2049 N  N   . TYR A 193 ? 0.0829 0.0922 0.0803 0.0024  0.0129  -0.0131 193 TYR A N   
2050 C  CA  . TYR A 193 ? 0.0970 0.1037 0.0759 0.0006  0.0031  -0.0110 193 TYR A CA  
2051 C  C   . TYR A 193 ? 0.0872 0.1100 0.0675 0.0119  0.0000  -0.0147 193 TYR A C   
2052 O  O   . TYR A 193 ? 0.0885 0.0988 0.0709 0.0027  0.0126  -0.0109 193 TYR A O   
2053 C  CB  . TYR A 193 ? 0.1084 0.1054 0.0586 0.0163  0.0048  -0.0054 193 TYR A CB  
2054 C  CG  . TYR A 193 ? 0.0997 0.0863 0.0644 0.0194  -0.0051 0.0038  193 TYR A CG  
2055 C  CD1 . TYR A 193 ? 0.1143 0.0935 0.0636 0.0185  0.0065  0.0000  193 TYR A CD1 
2056 C  CD2 . TYR A 193 ? 0.1001 0.0953 0.0728 0.0154  -0.0077 -0.0052 193 TYR A CD2 
2057 C  CE1 . TYR A 193 ? 0.0864 0.0785 0.0755 0.0155  0.0104  0.0040  193 TYR A CE1 
2058 C  CE2 . TYR A 193 ? 0.1084 0.0917 0.0706 0.0142  0.0017  -0.0206 193 TYR A CE2 
2059 C  CZ  . TYR A 193 ? 0.0833 0.0753 0.0710 0.0175  0.0082  -0.0104 193 TYR A CZ  
2060 O  OH  . TYR A 193 ? 0.0834 0.0789 0.0688 0.0060  0.0140  -0.0059 193 TYR A OH  
2061 N  N   . PRO A 194 ? 0.0933 0.1005 0.0649 0.0006  0.0035  -0.0170 194 PRO A N   
2062 C  CA  . PRO A 194 ? 0.0807 0.0935 0.0938 -0.0010 0.0068  -0.0262 194 PRO A CA  
2063 C  C   . PRO A 194 ? 0.0728 0.0878 0.0684 0.0010  -0.0129 -0.0182 194 PRO A C   
2064 O  O   . PRO A 194 ? 0.1019 0.1109 0.0643 0.0219  -0.0098 -0.0140 194 PRO A O   
2065 C  CB  . PRO A 194 ? 0.1168 0.1123 0.0876 0.0065  -0.0013 -0.0326 194 PRO A CB  
2066 C  CG  . PRO A 194 ? 0.1238 0.1305 0.0872 -0.0086 -0.0006 -0.0297 194 PRO A CG  
2067 C  CD  . PRO A 194 ? 0.1073 0.1443 0.0597 -0.0129 0.0031  -0.0328 194 PRO A CD  
2068 N  N   . GLY A 195 ? 0.0802 0.0746 0.0671 0.0065  0.0006  -0.0131 195 GLY A N   
2069 C  CA  . GLY A 195 ? 0.0854 0.0987 0.0827 0.0041  0.0197  -0.0153 195 GLY A CA  
2070 C  C   . GLY A 195 ? 0.0863 0.0705 0.0832 0.0010  0.0065  -0.0147 195 GLY A C   
2071 O  O   . GLY A 195 ? 0.0856 0.0820 0.0834 -0.0020 0.0063  -0.0148 195 GLY A O   
2072 N  N   . SER A 196 ? 0.0671 0.0926 0.0732 -0.0060 -0.0013 -0.0093 196 SER A N   
2073 C  CA  . SER A 196 ? 0.0732 0.0965 0.0876 -0.0059 0.0081  -0.0147 196 SER A CA  
2074 C  C   . SER A 196 ? 0.0790 0.0652 0.0798 0.0087  0.0027  -0.0062 196 SER A C   
2075 O  O   . SER A 196 ? 0.0702 0.0834 0.0731 0.0015  0.0099  -0.0185 196 SER A O   
2076 C  CB  . SER A 196 ? 0.0715 0.0688 0.1089 -0.0019 0.0006  -0.0294 196 SER A CB  
2077 O  OG  . SER A 196 ? 0.0578 0.0806 0.1032 0.0013  -0.0062 -0.0219 196 SER A OG  
2078 N  N   . LEU A 197 ? 0.0732 0.0785 0.0750 0.0031  0.0038  -0.0143 197 LEU A N   
2079 C  CA  . LEU A 197 ? 0.0847 0.0856 0.0723 0.0003  0.0104  -0.0230 197 LEU A CA  
2080 C  C   . LEU A 197 ? 0.0688 0.0865 0.0718 -0.0130 0.0140  -0.0153 197 LEU A C   
2081 O  O   . LEU A 197 ? 0.0737 0.0885 0.0829 -0.0003 0.0054  -0.0270 197 LEU A O   
2082 C  CB  . LEU A 197 ? 0.0785 0.0915 0.0899 0.0037  0.0141  -0.0096 197 LEU A CB  
2083 C  CG  . LEU A 197 ? 0.1073 0.0942 0.0992 -0.0010 0.0164  -0.0003 197 LEU A CG  
2084 C  CD1 . LEU A 197 ? 0.1136 0.1159 0.1333 -0.0113 0.0187  0.0082  197 LEU A CD1 
2085 C  CD2 . LEU A 197 ? 0.1044 0.1234 0.1310 0.0326  0.0241  0.0211  197 LEU A CD2 
2086 N  N   . THR A 198 ? 0.0755 0.0754 0.0776 -0.0063 0.0054  -0.0217 198 THR A N   
2087 C  CA  . THR A 198 ? 0.0741 0.0768 0.1019 -0.0020 0.0182  -0.0184 198 THR A CA  
2088 C  C   . THR A 198 ? 0.0705 0.0912 0.1017 -0.0013 0.0147  -0.0251 198 THR A C   
2089 O  O   . THR A 198 ? 0.0781 0.0841 0.1242 -0.0040 0.0165  -0.0271 198 THR A O   
2090 C  CB  . THR A 198 ? 0.0715 0.0876 0.0838 -0.0074 0.0026  -0.0186 198 THR A CB  
2091 O  OG1 . THR A 198 ? 0.0825 0.0798 0.0754 -0.0060 0.0054  -0.0043 198 THR A OG1 
2092 C  CG2 . THR A 198 ? 0.1008 0.0829 0.0915 -0.0013 0.0193  -0.0006 198 THR A CG2 
2093 N  N   . THR A 199 ? 0.0702 0.0960 0.1053 -0.0104 0.0195  -0.0109 199 THR A N   
2094 C  CA  . THR A 199 ? 0.0864 0.1064 0.1058 -0.0087 0.0175  -0.0265 199 THR A CA  
2095 C  C   . THR A 199 ? 0.1037 0.1014 0.1118 -0.0040 0.0351  -0.0187 199 THR A C   
2096 O  O   . THR A 199 ? 0.0781 0.1000 0.1141 -0.0115 0.0208  -0.0206 199 THR A O   
2097 C  CB  . THR A 199 ? 0.1231 0.1172 0.1127 -0.0153 0.0104  -0.0156 199 THR A CB  
2098 O  OG1 . THR A 199 ? 0.1344 0.1287 0.1342 -0.0006 -0.0222 -0.0197 199 THR A OG1 
2099 C  CG2 . THR A 199 ? 0.1324 0.1441 0.1204 -0.0439 0.0249  -0.0399 199 THR A CG2 
2100 N  N   . PRO A 200 ? 0.0969 0.1032 0.1177 -0.0118 0.0262  -0.0269 200 PRO A N   
2101 C  CA  . PRO A 200 ? 0.0915 0.1149 0.1357 -0.0199 0.0307  -0.0188 200 PRO A CA  
2102 C  C   . PRO A 200 ? 0.1145 0.1213 0.1181 -0.0288 0.0172  -0.0175 200 PRO A C   
2103 O  O   . PRO A 200 ? 0.1164 0.1359 0.1203 -0.0060 0.0275  -0.0035 200 PRO A O   
2104 C  CB  . PRO A 200 ? 0.0988 0.1484 0.1827 -0.0093 0.0621  -0.0162 200 PRO A CB  
2105 C  CG  . PRO A 200 ? 0.0965 0.1470 0.1712 -0.0214 0.0397  -0.0295 200 PRO A CG  
2106 C  CD  . PRO A 200 ? 0.0873 0.1425 0.1516 -0.0131 0.0359  -0.0566 200 PRO A CD  
2107 N  N   . PRO A 201 ? 0.1039 0.1134 0.1404 -0.0247 0.0220  -0.0165 201 PRO A N   
2108 C  CA  . PRO A 201 ? 0.1048 0.0988 0.1251 -0.0295 0.0210  -0.0043 201 PRO A CA  
2109 C  C   . PRO A 201 ? 0.0807 0.0979 0.1263 -0.0063 0.0294  -0.0192 201 PRO A C   
2110 O  O   . PRO A 201 ? 0.0942 0.1259 0.1394 -0.0331 0.0114  -0.0263 201 PRO A O   
2111 C  CB  . PRO A 201 ? 0.1384 0.1114 0.1619 -0.0465 0.0237  0.0010  201 PRO A CB  
2112 C  CG  . PRO A 201 ? 0.1321 0.1225 0.1657 -0.0281 0.0366  -0.0218 201 PRO A CG  
2113 C  CD  . PRO A 201 ? 0.1213 0.1199 0.1216 -0.0186 0.0199  -0.0104 201 PRO A CD  
2114 N  N   . LEU A 202 ? 0.0724 0.0913 0.1263 -0.0146 0.0178  -0.0140 202 LEU A N   
2115 C  CA  . LEU A 202 ? 0.0759 0.0961 0.1107 -0.0077 0.0115  -0.0241 202 LEU A CA  
2116 C  C   . LEU A 202 ? 0.0693 0.0885 0.1314 -0.0017 0.0046  -0.0282 202 LEU A C   
2117 O  O   . LEU A 202 ? 0.0662 0.1014 0.1168 -0.0071 -0.0031 -0.0274 202 LEU A O   
2118 C  CB  . LEU A 202 ? 0.0652 0.0908 0.1448 -0.0030 -0.0088 -0.0438 202 LEU A CB  
2119 C  CG  . LEU A 202 ? 0.0606 0.1052 0.1550 0.0057  -0.0020 -0.0386 202 LEU A CG  
2120 C  CD1 . LEU A 202 ? 0.0687 0.1233 0.1985 0.0041  -0.0031 -0.0441 202 LEU A CD1 
2121 C  CD2 . LEU A 202 ? 0.0750 0.1096 0.1402 0.0076  -0.0020 -0.0274 202 LEU A CD2 
2122 N  N   . ALA A 203 ? 0.0850 0.0736 0.1197 -0.0031 0.0147  -0.0274 203 ALA A N   
2123 C  CA  . ALA A 203 ? 0.1058 0.0845 0.1141 0.0015  0.0147  -0.0225 203 ALA A CA  
2124 C  C   . ALA A 203 ? 0.0820 0.0755 0.1064 -0.0096 0.0065  -0.0318 203 ALA A C   
2125 O  O   . ALA A 203 ? 0.0881 0.0794 0.1030 -0.0038 -0.0019 -0.0185 203 ALA A O   
2126 C  CB  . ALA A 203 ? 0.1055 0.0772 0.1346 0.0046  0.0135  -0.0115 203 ALA A CB  
2127 N  N   . GLU A 204 ? 0.0776 0.0942 0.1005 0.0041  0.0026  -0.0263 204 GLU A N   
2128 C  CA  . GLU A 204 ? 0.0861 0.0974 0.0856 0.0052  0.0030  -0.0206 204 GLU A CA  
2129 C  C   . GLU A 204 ? 0.1111 0.0794 0.0908 0.0048  -0.0156 -0.0215 204 GLU A C   
2130 O  O   . GLU A 204 ? 0.1109 0.1073 0.1044 0.0153  -0.0143 -0.0348 204 GLU A O   
2131 C  CB  . GLU A 204 ? 0.1179 0.1010 0.0992 0.0165  -0.0131 -0.0065 204 GLU A CB  
2132 C  CG  . GLU A 204 ? 0.1088 0.1203 0.1367 0.0195  -0.0262 -0.0208 204 GLU A CG  
2133 C  CD  . GLU A 204 ? 0.1084 0.1061 0.1217 -0.0082 -0.0131 -0.0247 204 GLU A CD  
2134 O  OE1 . GLU A 204 ? 0.1522 0.1272 0.1513 0.0015  -0.0416 -0.0421 204 GLU A OE1 
2135 O  OE2 . GLU A 204 ? 0.1170 0.1267 0.1346 -0.0023 -0.0208 -0.0176 204 GLU A OE2 
2136 N  N   . CYS A 205 ? 0.0816 0.0820 0.1037 0.0038  -0.0013 -0.0187 205 CYS A N   
2137 C  CA  . CYS A 205 ? 0.0674 0.0816 0.1075 -0.0023 -0.0043 -0.0098 205 CYS A CA  
2138 C  C   . CYS A 205 ? 0.0622 0.0759 0.0939 0.0049  -0.0120 -0.0236 205 CYS A C   
2139 O  O   . CYS A 205 ? 0.0859 0.0811 0.1356 0.0051  -0.0255 -0.0086 205 CYS A O   
2140 C  CB  . CYS A 205 ? 0.1037 0.0982 0.1003 0.0000  -0.0052 0.0006  205 CYS A CB  
2141 S  SG  . CYS A 205 ? 0.1247 0.0939 0.1039 0.0000  0.0087  -0.0109 205 CYS A SG  
2142 N  N   . VAL A 206 ? 0.0715 0.0728 0.0890 -0.0048 0.0031  -0.0170 206 VAL A N   
2143 C  CA  . VAL A 206 ? 0.0622 0.0693 0.0983 0.0000  0.0126  -0.0054 206 VAL A CA  
2144 C  C   . VAL A 206 ? 0.0825 0.0733 0.0845 0.0085  0.0023  -0.0115 206 VAL A C   
2145 O  O   . VAL A 206 ? 0.0926 0.0912 0.0888 0.0054  0.0006  0.0035  206 VAL A O   
2146 C  CB  . VAL A 206 ? 0.0666 0.0741 0.0978 0.0048  -0.0006 -0.0167 206 VAL A CB  
2147 C  CG1 . VAL A 206 ? 0.0741 0.0870 0.1027 0.0003  -0.0091 -0.0048 206 VAL A CG1 
2148 C  CG2 . VAL A 206 ? 0.1067 0.0780 0.0952 0.0099  0.0197  -0.0126 206 VAL A CG2 
2149 N  N   . THR A 207 ? 0.0693 0.0608 0.0974 -0.0070 0.0088  -0.0207 207 THR A N   
2150 C  CA  . THR A 207 ? 0.0763 0.0802 0.0942 -0.0010 0.0153  -0.0126 207 THR A CA  
2151 C  C   . THR A 207 ? 0.0845 0.0718 0.0724 0.0019  0.0093  -0.0107 207 THR A C   
2152 O  O   . THR A 207 ? 0.0827 0.0825 0.0789 0.0048  0.0000  -0.0086 207 THR A O   
2153 C  CB  . THR A 207 ? 0.0825 0.0785 0.0951 0.0131  0.0137  -0.0125 207 THR A CB  
2154 O  OG1 . THR A 207 ? 0.1064 0.0845 0.1145 0.0010  0.0167  -0.0225 207 THR A OG1 
2155 C  CG2 . THR A 207 ? 0.0860 0.1102 0.1297 0.0068  0.0320  -0.0035 207 THR A CG2 
2156 N  N   . TRP A 208 ? 0.0662 0.0657 0.0723 0.0073  0.0146  -0.0142 208 TRP A N   
2157 C  CA  . TRP A 208 ? 0.0688 0.0614 0.0700 -0.0023 0.0027  -0.0015 208 TRP A CA  
2158 C  C   . TRP A 208 ? 0.0656 0.0736 0.0596 0.0065  0.0110  -0.0071 208 TRP A C   
2159 O  O   . TRP A 208 ? 0.0776 0.0951 0.0599 0.0086  0.0098  -0.0082 208 TRP A O   
2160 C  CB  . TRP A 208 ? 0.0697 0.0917 0.0727 0.0109  -0.0027 0.0024  208 TRP A CB  
2161 C  CG  . TRP A 208 ? 0.0777 0.0689 0.0658 0.0074  0.0003  -0.0023 208 TRP A CG  
2162 C  CD1 . TRP A 208 ? 0.0732 0.0746 0.0877 0.0059  0.0124  -0.0049 208 TRP A CD1 
2163 C  CD2 . TRP A 208 ? 0.0872 0.0588 0.0710 0.0131  0.0046  -0.0124 208 TRP A CD2 
2164 N  NE1 . TRP A 208 ? 0.0940 0.0755 0.0816 0.0012  0.0151  -0.0071 208 TRP A NE1 
2165 C  CE2 . TRP A 208 ? 0.0890 0.0706 0.0888 0.0125  0.0120  0.0041  208 TRP A CE2 
2166 C  CE3 . TRP A 208 ? 0.0860 0.0636 0.0724 0.0108  -0.0081 -0.0027 208 TRP A CE3 
2167 C  CZ2 . TRP A 208 ? 0.0890 0.0915 0.0870 0.0357  0.0126  0.0000  208 TRP A CZ2 
2168 C  CZ3 . TRP A 208 ? 0.1040 0.0863 0.0702 0.0081  -0.0049 -0.0108 208 TRP A CZ3 
2169 C  CH2 . TRP A 208 ? 0.1208 0.0841 0.0869 0.0242  0.0054  -0.0081 208 TRP A CH2 
2170 N  N   . ILE A 209 ? 0.0671 0.0785 0.0724 0.0000  0.0065  -0.0093 209 ILE A N   
2171 C  CA  . ILE A 209 ? 0.0588 0.0798 0.0763 -0.0077 0.0046  -0.0074 209 ILE A CA  
2172 C  C   . ILE A 209 ? 0.0546 0.0820 0.0700 0.0019  0.0065  -0.0099 209 ILE A C   
2173 O  O   . ILE A 209 ? 0.1089 0.0886 0.0670 0.0052  -0.0046 -0.0060 209 ILE A O   
2174 C  CB  . ILE A 209 ? 0.0666 0.0897 0.1261 0.0005  0.0192  -0.0043 209 ILE A CB  
2175 C  CG1 . ILE A 209 ? 0.0926 0.0891 0.1623 0.0251  0.0013  -0.0266 209 ILE A CG1 
2176 C  CG2 . ILE A 209 ? 0.0579 0.1387 0.1199 0.0040  -0.0013 0.0010  209 ILE A CG2 
2177 C  CD1 . ILE A 209 ? 0.1380 0.0881 0.2205 0.0252  -0.0037 0.0017  209 ILE A CD1 
2178 N  N   . VAL A 210 ? 0.0546 0.0777 0.0753 0.0096  0.0057  -0.0035 210 VAL A N   
2179 C  CA  . VAL A 210 ? 0.0670 0.0666 0.0715 -0.0030 0.0026  -0.0015 210 VAL A CA  
2180 C  C   . VAL A 210 ? 0.0776 0.0658 0.0767 0.0035  0.0281  0.0000  210 VAL A C   
2181 O  O   . VAL A 210 ? 0.0890 0.1045 0.0776 -0.0068 0.0304  -0.0024 210 VAL A O   
2182 C  CB  . VAL A 210 ? 0.0753 0.0736 0.0888 0.0076  0.0076  0.0015  210 VAL A CB  
2183 C  CG1 . VAL A 210 ? 0.0894 0.0872 0.1053 0.0015  0.0080  -0.0010 210 VAL A CG1 
2184 C  CG2 . VAL A 210 ? 0.0944 0.0931 0.0951 -0.0017 0.0020  0.0113  210 VAL A CG2 
2185 N  N   . LEU A 211 ? 0.0759 0.0888 0.1005 -0.0210 0.0068  -0.0059 211 LEU A N   
2186 C  CA  . LEU A 211 ? 0.0710 0.0964 0.0944 -0.0087 0.0046  0.0031  211 LEU A CA  
2187 C  C   . LEU A 211 ? 0.0710 0.1177 0.1021 -0.0159 0.0140  0.0071  211 LEU A C   
2188 O  O   . LEU A 211 ? 0.0912 0.1096 0.0827 -0.0054 0.0143  0.0063  211 LEU A O   
2189 C  CB  . LEU A 211 ? 0.0951 0.1152 0.1066 0.0026  0.0038  0.0054  211 LEU A CB  
2190 C  CG  . LEU A 211 ? 0.0737 0.1206 0.1085 -0.0027 0.0007  0.0174  211 LEU A CG  
2191 C  CD1 . LEU A 211 ? 0.1017 0.1497 0.1556 -0.0115 -0.0425 0.0041  211 LEU A CD1 
2192 C  CD2 . LEU A 211 ? 0.0929 0.1350 0.1368 0.0159  0.0194  0.0088  211 LEU A CD2 
2193 N  N   A LYS A 212 ? 0.0888 0.1208 0.1143 -0.0351 0.0186  0.0087  212 LYS A N   
2194 N  N   B LYS A 212 ? 0.0806 0.1035 0.1102 -0.0178 0.0206  0.0057  212 LYS A N   
2195 C  CA  A LYS A 212 ? 0.1259 0.1261 0.1075 -0.0162 0.0131  0.0048  212 LYS A CA  
2196 C  CA  B LYS A 212 ? 0.0715 0.1140 0.1001 -0.0038 0.0273  0.0177  212 LYS A CA  
2197 C  C   A LYS A 212 ? 0.1019 0.0973 0.1199 -0.0182 0.0080  0.0216  212 LYS A C   
2198 C  C   B LYS A 212 ? 0.0833 0.1120 0.1084 -0.0115 0.0219  0.0230  212 LYS A C   
2199 O  O   A LYS A 212 ? 0.1073 0.1073 0.1164 -0.0068 0.0082  0.0439  212 LYS A O   
2200 O  O   B LYS A 212 ? 0.1386 0.1143 0.1335 -0.0091 -0.0024 0.0148  212 LYS A O   
2201 C  CB  A LYS A 212 ? 0.1683 0.1703 0.1037 -0.0518 0.0137  0.0102  212 LYS A CB  
2202 C  CB  B LYS A 212 ? 0.0482 0.1263 0.1134 0.0166  0.0308  0.0263  212 LYS A CB  
2203 C  CG  A LYS A 212 ? 0.2023 0.2026 0.1464 -0.0648 0.0034  0.0353  212 LYS A CG  
2204 C  CG  B LYS A 212 ? 0.1554 0.1455 0.1468 0.0160  0.0469  0.0461  212 LYS A CG  
2205 C  CD  A LYS A 212 ? 0.1764 0.2890 0.1972 -0.0824 0.0081  -0.0023 212 LYS A CD  
2206 C  CD  B LYS A 212 ? 0.1161 0.2003 0.1541 0.0131  0.0441  0.0579  212 LYS A CD  
2207 C  CE  A LYS A 212 ? 0.3346 0.2788 0.1107 0.0054  0.0878  0.0750  212 LYS A CE  
2208 C  CE  B LYS A 212 ? 0.2578 0.2247 0.2090 -0.0304 0.0344  0.1137  212 LYS A CE  
2209 N  NZ  A LYS A 212 ? 0.3546 0.3932 0.2235 -0.0252 -0.0456 0.0115  212 LYS A NZ  
2210 N  NZ  B LYS A 212 ? 0.2752 0.4928 0.2373 -0.0302 0.0619  0.1527  212 LYS A NZ  
2211 N  N   . GLU A 213 ? 0.0790 0.1089 0.1089 -0.0073 0.0104  0.0126  213 GLU A N   
2212 C  CA  . GLU A 213 ? 0.1030 0.1064 0.1163 -0.0170 -0.0006 0.0060  213 GLU A CA  
2213 C  C   . GLU A 213 ? 0.0675 0.0948 0.0956 -0.0131 -0.0118 0.0162  213 GLU A C   
2214 O  O   . GLU A 213 ? 0.0933 0.1014 0.1186 0.0006  0.0054  0.0153  213 GLU A O   
2215 C  CB  . GLU A 213 ? 0.0985 0.1477 0.1347 -0.0207 -0.0114 0.0115  213 GLU A CB  
2216 C  CG  . GLU A 213 ? 0.1179 0.1718 0.1748 -0.0305 0.0020  -0.0076 213 GLU A CG  
2217 C  CD  . GLU A 213 ? 0.1268 0.2343 0.2063 -0.0772 -0.0115 -0.0164 213 GLU A CD  
2218 O  OE1 . GLU A 213 ? 0.1190 0.1844 0.2863 -0.0170 -0.0131 0.0000  213 GLU A OE1 
2219 O  OE2 . GLU A 213 ? 0.1894 0.3050 0.2831 -0.0120 -0.0719 0.0034  213 GLU A OE2 
2220 N  N   A PRO A 214 ? 0.0906 0.1100 0.1048 -0.0130 -0.0031 -0.0040 214 PRO A N   
2221 N  N   B PRO A 214 ? 0.0982 0.0890 0.1149 -0.0162 0.0017  0.0151  214 PRO A N   
2222 C  CA  A PRO A 214 ? 0.1208 0.0935 0.1040 -0.0098 -0.0003 0.0027  214 PRO A CA  
2223 C  CA  B PRO A 214 ? 0.1075 0.0960 0.1136 0.0103  0.0006  0.0062  214 PRO A CA  
2224 C  C   A PRO A 214 ? 0.0931 0.0785 0.1240 0.0109  0.0026  -0.0081 214 PRO A C   
2225 C  C   B PRO A 214 ? 0.1120 0.0741 0.1269 0.0034  -0.0074 0.0049  214 PRO A C   
2226 O  O   A PRO A 214 ? 0.0926 0.1213 0.1109 0.0037  -0.0020 -0.0098 214 PRO A O   
2227 O  O   B PRO A 214 ? 0.1301 0.0969 0.1310 -0.0216 -0.0126 0.0206  214 PRO A O   
2228 C  CB  A PRO A 214 ? 0.1185 0.0920 0.0863 -0.0124 -0.0153 0.0148  214 PRO A CB  
2229 C  CB  B PRO A 214 ? 0.0744 0.0908 0.1608 0.0065  0.0015  -0.0019 214 PRO A CB  
2230 C  CG  A PRO A 214 ? 0.1317 0.0983 0.1010 0.0046  0.0199  0.0059  214 PRO A CG  
2231 C  CG  B PRO A 214 ? 0.1179 0.1461 0.1644 -0.0098 0.0153  0.0065  214 PRO A CG  
2232 C  CD  A PRO A 214 ? 0.1014 0.0847 0.1324 0.0143  -0.0087 -0.0184 214 PRO A CD  
2233 C  CD  B PRO A 214 ? 0.1231 0.0982 0.1342 -0.0076 0.0109  0.0366  214 PRO A CD  
2234 N  N   . ILE A 215 ? 0.1158 0.0881 0.1005 0.0038  -0.0137 -0.0065 215 ILE A N   
2235 C  CA  . ILE A 215 ? 0.1242 0.1010 0.1027 0.0006  -0.0137 -0.0192 215 ILE A CA  
2236 C  C   . ILE A 215 ? 0.1170 0.0949 0.1163 0.0048  -0.0262 -0.0049 215 ILE A C   
2237 O  O   . ILE A 215 ? 0.1001 0.0917 0.1515 0.0019  -0.0135 -0.0131 215 ILE A O   
2238 C  CB  . ILE A 215 ? 0.1283 0.1028 0.1220 0.0218  -0.0250 -0.0060 215 ILE A CB  
2239 C  CG1 . ILE A 215 ? 0.1495 0.1046 0.1111 0.0071  -0.0197 0.0024  215 ILE A CG1 
2240 C  CG2 . ILE A 215 ? 0.1626 0.1005 0.1432 0.0244  -0.0340 -0.0219 215 ILE A CG2 
2241 C  CD1 . ILE A 215 ? 0.2138 0.1301 0.1224 -0.0057 -0.0240 0.0142  215 ILE A CD1 
2242 N  N   A SER A 216 ? 0.1170 0.1107 0.1281 0.0054  -0.0221 -0.0331 216 SER A N   
2243 N  N   B SER A 216 ? 0.1164 0.1109 0.1220 -0.0048 -0.0175 -0.0193 216 SER A N   
2244 C  CA  A SER A 216 ? 0.1393 0.0935 0.1276 -0.0153 -0.0034 -0.0285 216 SER A CA  
2245 C  CA  B SER A 216 ? 0.1319 0.1134 0.1240 0.0052  -0.0230 -0.0186 216 SER A CA  
2246 C  C   A SER A 216 ? 0.1159 0.0856 0.1085 -0.0115 -0.0344 -0.0348 216 SER A C   
2247 C  C   B SER A 216 ? 0.1240 0.0948 0.1167 0.0113  -0.0303 -0.0120 216 SER A C   
2248 O  O   A SER A 216 ? 0.1374 0.0908 0.1323 -0.0183 -0.0377 -0.0010 216 SER A O   
2249 O  O   B SER A 216 ? 0.1321 0.1202 0.1383 0.0060  -0.0452 0.0037  216 SER A O   
2250 C  CB  A SER A 216 ? 0.1310 0.0719 0.1340 0.0013  -0.0093 -0.0173 216 SER A CB  
2251 C  CB  B SER A 216 ? 0.2336 0.1026 0.1513 -0.0546 0.0120  -0.0051 216 SER A CB  
2252 O  OG  A SER A 216 ? 0.1615 0.1238 0.1339 -0.0469 -0.0189 -0.0049 216 SER A OG  
2253 O  OG  B SER A 216 ? 0.2026 0.1811 0.1793 -0.0186 -0.0108 -0.0370 216 SER A OG  
2254 N  N   . VAL A 217 ? 0.1240 0.0956 0.1193 -0.0135 -0.0096 -0.0197 217 VAL A N   
2255 C  CA  . VAL A 217 ? 0.1347 0.0856 0.1177 -0.0003 -0.0199 -0.0182 217 VAL A CA  
2256 C  C   . VAL A 217 ? 0.1398 0.0915 0.1224 -0.0408 -0.0285 -0.0161 217 VAL A C   
2257 O  O   . VAL A 217 ? 0.1533 0.0878 0.1195 -0.0148 -0.0163 -0.0093 217 VAL A O   
2258 C  CB  . VAL A 217 ? 0.1455 0.0879 0.1333 -0.0211 -0.0274 -0.0148 217 VAL A CB  
2259 C  CG1 . VAL A 217 ? 0.1635 0.0842 0.1371 -0.0027 -0.0241 -0.0087 217 VAL A CG1 
2260 C  CG2 . VAL A 217 ? 0.1385 0.1055 0.1958 -0.0093 -0.0272 -0.0221 217 VAL A CG2 
2261 N  N   . SER A 218 ? 0.1439 0.0904 0.1188 -0.0185 -0.0241 -0.0203 218 SER A N   
2262 C  CA  . SER A 218 ? 0.1680 0.0877 0.1499 -0.0115 -0.0384 -0.0337 218 SER A CA  
2263 C  C   . SER A 218 ? 0.1789 0.0671 0.1173 -0.0295 -0.0272 -0.0140 218 SER A C   
2264 O  O   . SER A 218 ? 0.1599 0.0740 0.1283 -0.0087 -0.0237 -0.0148 218 SER A O   
2265 C  CB  . SER A 218 ? 0.1860 0.0996 0.1344 -0.0249 -0.0248 -0.0207 218 SER A CB  
2266 O  OG  . SER A 218 ? 0.1852 0.1222 0.1252 -0.0197 -0.0291 -0.0092 218 SER A OG  
2267 N  N   A SER A 219 ? 0.1799 0.0724 0.1342 -0.0137 -0.0104 -0.0156 219 SER A N   
2268 N  N   B SER A 219 ? 0.1820 0.0631 0.1437 -0.0277 -0.0102 -0.0080 219 SER A N   
2269 C  CA  A SER A 219 ? 0.1754 0.0908 0.1481 -0.0141 -0.0187 -0.0253 219 SER A CA  
2270 C  CA  B SER A 219 ? 0.1849 0.0780 0.1631 -0.0221 -0.0060 0.0006  219 SER A CA  
2271 C  C   A SER A 219 ? 0.2027 0.0754 0.1612 -0.0153 -0.0183 -0.0208 219 SER A C   
2272 C  C   B SER A 219 ? 0.2084 0.0670 0.1594 -0.0119 -0.0165 -0.0041 219 SER A C   
2273 O  O   A SER A 219 ? 0.1881 0.1048 0.1912 -0.0126 -0.0110 0.0154  219 SER A O   
2274 O  O   B SER A 219 ? 0.2100 0.1091 0.1662 -0.0262 -0.0020 -0.0142 219 SER A O   
2275 C  CB  A SER A 219 ? 0.1585 0.1125 0.1869 0.0281  -0.0274 -0.0520 219 SER A CB  
2276 C  CB  B SER A 219 ? 0.2416 0.0750 0.2409 -0.0577 0.0143  0.0428  219 SER A CB  
2277 O  OG  A SER A 219 ? 0.1908 0.0812 0.1384 0.0015  -0.0353 -0.0146 219 SER A OG  
2278 O  OG  B SER A 219 ? 0.2651 0.2188 0.2509 -0.0136 -0.0469 0.0013  219 SER A OG  
2279 N  N   . GLU A 220 ? 0.1951 0.0987 0.1453 -0.0231 -0.0141 -0.0362 220 GLU A N   
2280 C  CA  . GLU A 220 ? 0.2352 0.1010 0.1692 -0.0167 -0.0121 -0.0124 220 GLU A CA  
2281 C  C   . GLU A 220 ? 0.2059 0.1234 0.1164 -0.0115 -0.0242 -0.0220 220 GLU A C   
2282 O  O   . GLU A 220 ? 0.2346 0.1492 0.1356 -0.0160 0.0274  -0.0263 220 GLU A O   
2283 C  CB  . GLU A 220 ? 0.3267 0.1536 0.1428 -0.0381 -0.0623 -0.0615 220 GLU A CB  
2284 C  CG  . GLU A 220 ? 0.2919 0.1777 0.2318 -0.0511 -0.0266 -0.0494 220 GLU A CG  
2285 C  CD  . GLU A 220 ? 0.3079 0.1454 0.2260 -0.0504 -0.0375 -0.0478 220 GLU A CD  
2286 O  OE1 . GLU A 220 ? 0.2876 0.1490 0.2147 -0.0472 -0.0447 -0.0443 220 GLU A OE1 
2287 O  OE2 . GLU A 220 ? 0.4857 0.2264 0.3822 -0.1380 0.0434  -0.1577 220 GLU A OE2 
2288 N  N   . GLN A 221 ? 0.1892 0.1048 0.1046 -0.0136 -0.0255 -0.0046 221 GLN A N   
2289 C  CA  . GLN A 221 ? 0.1723 0.0920 0.1195 -0.0293 -0.0156 0.0006  221 GLN A CA  
2290 C  C   . GLN A 221 ? 0.1888 0.0899 0.1271 -0.0054 -0.0076 -0.0081 221 GLN A C   
2291 O  O   . GLN A 221 ? 0.1881 0.1167 0.1203 -0.0183 -0.0041 0.0097  221 GLN A O   
2292 C  CB  . GLN A 221 ? 0.1757 0.1177 0.1109 -0.0219 -0.0373 0.0031  221 GLN A CB  
2293 C  CG  . GLN A 221 ? 0.1879 0.0996 0.1242 -0.0197 -0.0397 -0.0076 221 GLN A CG  
2294 C  CD  . GLN A 221 ? 0.2057 0.0951 0.1353 -0.0125 -0.0395 -0.0253 221 GLN A CD  
2295 O  OE1 . GLN A 221 ? 0.1699 0.1186 0.1120 -0.0057 -0.0307 -0.0104 221 GLN A OE1 
2296 N  NE2 . GLN A 221 ? 0.2079 0.1287 0.1495 -0.0060 -0.0474 0.0118  221 GLN A NE2 
2297 N  N   A VAL A 222 ? 0.1784 0.1091 0.1089 -0.0153 -0.0140 0.0013  222 VAL A N   
2298 N  N   B VAL A 222 ? 0.1814 0.1114 0.1116 -0.0120 -0.0099 0.0054  222 VAL A N   
2299 C  CA  A VAL A 222 ? 0.1676 0.1252 0.1441 -0.0046 -0.0091 0.0164  222 VAL A CA  
2300 C  CA  B VAL A 222 ? 0.1736 0.1252 0.1470 -0.0093 -0.0020 0.0208  222 VAL A CA  
2301 C  C   A VAL A 222 ? 0.2046 0.0767 0.1775 -0.0070 0.0098  0.0057  222 VAL A C   
2302 C  C   B VAL A 222 ? 0.2019 0.0785 0.1741 -0.0264 0.0222  0.0126  222 VAL A C   
2303 O  O   A VAL A 222 ? 0.2021 0.1195 0.1574 -0.0161 -0.0063 0.0228  222 VAL A O   
2304 O  O   B VAL A 222 ? 0.1901 0.1204 0.1194 -0.0364 0.0071  0.0252  222 VAL A O   
2305 C  CB  A VAL A 222 ? 0.2062 0.0933 0.1163 -0.0200 0.0048  -0.0252 222 VAL A CB  
2306 C  CB  B VAL A 222 ? 0.1646 0.1931 0.1553 0.0254  0.0423  0.0559  222 VAL A CB  
2307 C  CG1 A VAL A 222 ? 0.2012 0.0917 0.1849 -0.0113 0.0209  0.0597  222 VAL A CG1 
2308 C  CG1 B VAL A 222 ? 0.1953 0.2339 0.1835 0.0264  -0.0152 0.0597  222 VAL A CG1 
2309 C  CG2 A VAL A 222 ? 0.1606 0.0881 0.1447 -0.0076 0.0057  0.0012  222 VAL A CG2 
2310 C  CG2 B VAL A 222 ? 0.1404 0.2605 0.1550 0.0353  0.0051  0.0126  222 VAL A CG2 
2311 N  N   . LEU A 223 ? 0.2154 0.1019 0.1497 -0.0230 0.0152  0.0073  223 LEU A N   
2312 C  CA  . LEU A 223 ? 0.2434 0.1274 0.2041 -0.0107 0.0241  -0.0173 223 LEU A CA  
2313 C  C   . LEU A 223 ? 0.1942 0.1615 0.1504 -0.0193 0.0241  -0.0210 223 LEU A C   
2314 O  O   . LEU A 223 ? 0.1899 0.1772 0.1868 -0.0174 0.0162  -0.0483 223 LEU A O   
2315 C  CB  . LEU A 223 ? 0.3474 0.1105 0.3140 -0.0807 0.0917  -0.0722 223 LEU A CB  
2316 C  CG  . LEU A 223 ? 0.3977 0.2156 0.4444 -0.0904 0.0219  -0.0540 223 LEU A CG  
2317 C  CD1 . LEU A 223 ? 0.5457 0.1565 0.7052 -0.0377 -0.1500 -0.0788 223 LEU A CD1 
2318 C  CD2 . LEU A 223 ? 0.5149 0.4115 0.4029 -0.0104 -0.2090 -0.1659 223 LEU A CD2 
2319 N  N   . LYS A 224 ? 0.2318 0.1256 0.1261 -0.0282 -0.0006 -0.0197 224 LYS A N   
2320 C  CA  . LYS A 224 ? 0.2217 0.1678 0.1319 -0.0377 0.0237  -0.0172 224 LYS A CA  
2321 C  C   . LYS A 224 ? 0.1976 0.1290 0.0958 -0.0120 -0.0052 0.0049  224 LYS A C   
2322 O  O   . LYS A 224 ? 0.2587 0.1475 0.0917 -0.0285 0.0093  0.0103  224 LYS A O   
2323 C  CB  . LYS A 224 ? 0.3142 0.2222 0.1641 0.0065  -0.0610 0.0410  224 LYS A CB  
2324 C  CG  . LYS A 224 ? 0.3183 0.3761 0.1875 -0.0816 -0.1115 0.0368  224 LYS A CG  
2325 C  CD  . LYS A 224 ? 0.3935 0.5271 0.2563 -0.0494 -0.1444 0.0305  224 LYS A CD  
2326 C  CE  . LYS A 224 ? 0.5230 0.4537 0.4106 0.1404  -0.0373 0.1316  224 LYS A CE  
2327 N  NZ  . LYS A 224 ? 0.7279 0.4765 0.3341 -0.2134 0.0575  -0.0119 224 LYS A NZ  
2328 N  N   . PHE A 225 ? 0.2134 0.1145 0.0852 -0.0109 -0.0093 -0.0054 225 PHE A N   
2329 C  CA  . PHE A 225 ? 0.1838 0.1106 0.0788 -0.0225 0.0109  0.0115  225 PHE A CA  
2330 C  C   . PHE A 225 ? 0.2044 0.1089 0.0688 -0.0511 0.0087  0.0065  225 PHE A C   
2331 O  O   . PHE A 225 ? 0.2030 0.1167 0.0895 -0.0392 0.0286  -0.0137 225 PHE A O   
2332 C  CB  . PHE A 225 ? 0.1836 0.1242 0.0987 -0.0187 0.0318  0.0034  225 PHE A CB  
2333 C  CG  . PHE A 225 ? 0.1951 0.1145 0.1254 -0.0335 0.0293  -0.0230 225 PHE A CG  
2334 C  CD1 . PHE A 225 ? 0.2449 0.1702 0.1498 0.0195  0.0333  0.0038  225 PHE A CD1 
2335 C  CD2 . PHE A 225 ? 0.1736 0.1892 0.1286 -0.0258 0.0126  -0.0461 225 PHE A CD2 
2336 C  CE1 . PHE A 225 ? 0.2739 0.1421 0.1723 -0.0049 0.0340  -0.0003 225 PHE A CE1 
2337 C  CE2 . PHE A 225 ? 0.1933 0.2177 0.1595 0.0000  0.0136  -0.0507 225 PHE A CE2 
2338 C  CZ  . PHE A 225 ? 0.2030 0.1448 0.1739 -0.0333 0.0292  -0.0546 225 PHE A CZ  
2339 N  N   . ARG A 226 ? 0.1849 0.1107 0.0859 -0.0203 0.0038  0.0068  226 ARG A N   
2340 C  CA  . ARG A 226 ? 0.1673 0.1419 0.0833 -0.0357 -0.0024 0.0226  226 ARG A CA  
2341 C  C   . ARG A 226 ? 0.1928 0.1195 0.1173 -0.0460 0.0108  -0.0120 226 ARG A C   
2342 O  O   . ARG A 226 ? 0.2125 0.1518 0.1019 -0.0355 0.0283  -0.0037 226 ARG A O   
2343 C  CB  . ARG A 226 ? 0.1935 0.1259 0.0820 -0.0322 0.0164  -0.0013 226 ARG A CB  
2344 C  CG  . ARG A 226 ? 0.1890 0.1190 0.0899 -0.0228 0.0118  0.0000  226 ARG A CG  
2345 C  CD  . ARG A 226 ? 0.2494 0.1194 0.1082 -0.0109 0.0194  0.0051  226 ARG A CD  
2346 N  NE  . ARG A 226 ? 0.1885 0.1247 0.0987 -0.0436 0.0093  -0.0074 226 ARG A NE  
2347 C  CZ  . ARG A 226 ? 0.2245 0.1269 0.0920 -0.0621 0.0046  -0.0137 226 ARG A CZ  
2348 N  NH1 . ARG A 226 ? 0.2700 0.1709 0.1444 -0.1032 0.0003  -0.0370 226 ARG A NH1 
2349 N  NH2 . ARG A 226 ? 0.2529 0.1252 0.1114 -0.0604 0.0368  -0.0088 226 ARG A NH2 
2350 N  N   . LYS A 227 ? 0.1888 0.1208 0.0879 -0.0421 0.0184  -0.0237 227 LYS A N   
2351 C  CA  . LYS A 227 ? 0.2195 0.1434 0.0882 -0.0680 0.0351  -0.0359 227 LYS A CA  
2352 C  C   . LYS A 227 ? 0.2479 0.1520 0.0608 -0.0649 0.0285  -0.0296 227 LYS A C   
2353 O  O   . LYS A 227 ? 0.2917 0.1676 0.0876 -0.0750 0.0597  -0.0230 227 LYS A O   
2354 C  CB  . LYS A 227 ? 0.2680 0.1718 0.1208 -0.0768 0.0460  -0.0496 227 LYS A CB  
2355 C  CG  . LYS A 227 ? 0.2976 0.2075 0.2391 -0.1142 0.0208  -0.0939 227 LYS A CG  
2356 C  CD  . LYS A 227 ? 0.3874 0.3759 0.1969 -0.0741 0.0035  -0.1084 227 LYS A CD  
2357 C  CE  . LYS A 227 ? 0.4584 0.5759 0.2621 -0.1190 0.0851  -0.0886 227 LYS A CE  
2358 N  NZ  . LYS A 227 ? 0.6948 1.1095 0.4641 -0.2222 -0.1391 -0.2078 227 LYS A NZ  
2359 N  N   . LEU A 228 ? 0.2290 0.1177 0.0859 -0.0573 0.0417  -0.0207 228 LEU A N   
2360 C  CA  . LEU A 228 ? 0.2669 0.1414 0.0737 -0.0688 0.0284  -0.0109 228 LEU A CA  
2361 C  C   . LEU A 228 ? 0.2689 0.1468 0.0939 -0.0864 0.0851  -0.0496 228 LEU A C   
2362 O  O   . LEU A 228 ? 0.2572 0.1562 0.1197 -0.0820 0.0570  -0.0399 228 LEU A O   
2363 C  CB  . LEU A 228 ? 0.2720 0.1378 0.0794 -0.0679 0.0288  -0.0113 228 LEU A CB  
2364 C  CG  . LEU A 228 ? 0.2775 0.1371 0.0879 -0.0684 0.0337  -0.0012 228 LEU A CG  
2365 C  CD1 . LEU A 228 ? 0.2752 0.1283 0.0926 -0.0487 0.0265  -0.0071 228 LEU A CD1 
2366 C  CD2 . LEU A 228 ? 0.3260 0.1813 0.1228 -0.0745 0.0148  0.0441  228 LEU A CD2 
2367 N  N   . ASN A 229 ? 0.2799 0.1725 0.0991 -0.1146 0.0436  -0.0262 229 ASN A N   
2368 C  CA  . ASN A 229 ? 0.2978 0.1675 0.0820 -0.0992 0.0610  -0.0328 229 ASN A CA  
2369 C  C   . ASN A 229 ? 0.2806 0.1949 0.0931 -0.1120 0.0917  -0.0377 229 ASN A C   
2370 O  O   . ASN A 229 ? 0.3185 0.1804 0.1177 -0.1177 0.0640  -0.0304 229 ASN A O   
2371 C  CB  . ASN A 229 ? 0.2838 0.2129 0.1140 -0.1177 0.0934  -0.0450 229 ASN A CB  
2372 C  CG  . ASN A 229 ? 0.3609 0.2275 0.0996 -0.1062 0.0582  -0.0390 229 ASN A CG  
2373 O  OD1 . ASN A 229 ? 0.4474 0.2782 0.1066 -0.1039 0.0974  -0.0693 229 ASN A OD1 
2374 N  ND2 . ASN A 229 ? 0.2597 0.1942 0.1516 -0.0806 0.0461  -0.0456 229 ASN A ND2 
2375 N  N   A PHE A 230 ? 0.2998 0.2343 0.1082 -0.1506 0.0526  -0.0458 230 PHE A N   
2376 N  N   B PHE A 230 ? 0.2734 0.1879 0.1107 -0.1190 0.0697  -0.0410 230 PHE A N   
2377 C  CA  A PHE A 230 ? 0.1515 0.1229 0.1392 -0.0399 0.0368  -0.0109 230 PHE A CA  
2378 C  CA  B PHE A 230 ? 0.0900 0.1518 0.1019 -0.0098 0.0491  -0.0046 230 PHE A CA  
2379 C  C   A PHE A 230 ? 0.1332 0.1414 0.1247 -0.0537 -0.0023 0.0065  230 PHE A C   
2380 C  C   B PHE A 230 ? 0.1599 0.1307 0.1212 -0.0243 0.0593  0.0000  230 PHE A C   
2381 O  O   A PHE A 230 ? 0.1568 0.1492 0.0915 -0.0579 0.0109  0.0148  230 PHE A O   
2382 O  O   B PHE A 230 ? 0.1328 0.1190 0.1271 -0.0074 0.0184  0.0092  230 PHE A O   
2383 C  CB  A PHE A 230 ? 0.1647 0.0829 0.1585 -0.0187 0.0261  0.0082  230 PHE A CB  
2384 C  CB  B PHE A 230 ? 0.1646 0.1102 0.0933 -0.0043 0.0243  0.0040  230 PHE A CB  
2385 C  CG  A PHE A 230 ? 0.1416 0.0671 0.1374 -0.0115 0.0241  -0.0238 230 PHE A CG  
2386 C  CG  B PHE A 230 ? 0.1553 0.1217 0.1141 -0.0010 0.0516  0.0093  230 PHE A CG  
2387 C  CD1 A PHE A 230 ? 0.1242 0.1045 0.1080 0.0005  0.0048  -0.0302 230 PHE A CD1 
2388 C  CD1 B PHE A 230 ? 0.1712 0.1109 0.1141 0.0007  0.0355  0.0115  230 PHE A CD1 
2389 C  CD2 A PHE A 230 ? 0.1737 0.0852 0.1040 0.0174  0.0445  -0.0188 230 PHE A CD2 
2390 C  CD2 B PHE A 230 ? 0.2461 0.0688 0.1500 -0.0675 0.0754  -0.0337 230 PHE A CD2 
2391 C  CE1 A PHE A 230 ? 0.0859 0.1357 0.1333 -0.0242 0.0049  0.0057  230 PHE A CE1 
2392 C  CE1 B PHE A 230 ? 0.1039 0.1439 0.0967 -0.0450 0.0120  -0.0110 230 PHE A CE1 
2393 C  CE2 A PHE A 230 ? 0.2120 0.0961 0.0978 -0.0163 0.0401  -0.0274 230 PHE A CE2 
2394 C  CE2 B PHE A 230 ? 0.2007 0.1231 0.1199 -0.0527 0.0573  -0.0154 230 PHE A CE2 
2395 C  CZ  A PHE A 230 ? 0.0958 0.1283 0.0992 -0.0379 0.0329  -0.0049 230 PHE A CZ  
2396 C  CZ  B PHE A 230 ? 0.1692 0.1046 0.1351 -0.0520 0.0120  -0.0427 230 PHE A CZ  
2397 N  N   A ASN A 231 ? 0.1023 0.1592 0.1021 -0.0186 0.0186  0.0432  231 ASN A N   
2398 N  N   B ASN A 231 ? 0.1152 0.1292 0.0957 0.0015  0.0198  0.0000  231 ASN A N   
2399 C  CA  A ASN A 231 ? 0.1001 0.1615 0.1527 -0.0307 0.0421  0.0299  231 ASN A CA  
2400 C  CA  B ASN A 231 ? 0.0758 0.1247 0.1418 -0.0098 0.0104  0.0049  231 ASN A CA  
2401 C  C   A ASN A 231 ? 0.1048 0.1843 0.1057 -0.0093 0.0577  -0.0026 231 ASN A C   
2402 C  C   B ASN A 231 ? 0.0917 0.1109 0.1507 0.0162  0.0304  -0.0027 231 ASN A C   
2403 O  O   A ASN A 231 ? 0.1070 0.1640 0.1039 -0.0187 0.0425  -0.0220 231 ASN A O   
2404 O  O   B ASN A 231 ? 0.1028 0.1213 0.1545 0.0172  0.0035  0.0006  231 ASN A O   
2405 C  CB  A ASN A 231 ? 0.1152 0.1852 0.1628 0.0162  0.0478  0.0395  231 ASN A CB  
2406 C  CB  B ASN A 231 ? 0.1279 0.1123 0.1142 -0.0070 -0.0126 0.0000  231 ASN A CB  
2407 C  CG  A ASN A 231 ? 0.0888 0.1818 0.1604 0.0333  0.0586  -0.0208 231 ASN A CG  
2408 C  CG  B ASN A 231 ? 0.0974 0.1134 0.1195 0.0288  -0.0342 0.0054  231 ASN A CG  
2409 O  OD1 A ASN A 231 ? 0.1396 0.1820 0.1960 -0.0208 0.0784  -0.0368 231 ASN A OD1 
2410 O  OD1 B ASN A 231 ? 0.1405 0.1613 0.1202 0.0364  -0.0392 -0.0131 231 ASN A OD1 
2411 N  ND2 A ASN A 231 ? 0.1581 0.2382 0.1653 0.0313  0.0480  -0.0076 231 ASN A ND2 
2412 N  ND2 B ASN A 231 ? 0.1032 0.1170 0.1037 0.0240  0.0125  -0.0176 231 ASN A ND2 
2413 N  N   A GLY A 232 ? 0.1321 0.1358 0.1834 0.0093  0.0724  0.0126  232 GLY A N   
2414 N  N   B GLY A 232 ? 0.1216 0.1079 0.1202 0.0154  0.0193  0.0041  232 GLY A N   
2415 C  CA  A GLY A 232 ? 0.1498 0.2007 0.1299 -0.0153 0.0702  -0.0027 232 GLY A CA  
2416 C  CA  B GLY A 232 ? 0.1098 0.1289 0.1459 0.0449  -0.0110 0.0013  232 GLY A CA  
2417 C  C   A GLY A 232 ? 0.1439 0.1960 0.1173 -0.0102 0.0825  0.0082  232 GLY A C   
2418 C  C   B GLY A 232 ? 0.1323 0.1030 0.1727 0.0383  0.0005  -0.0192 232 GLY A C   
2419 O  O   A GLY A 232 ? 0.2201 0.2309 0.1897 0.0428  0.1440  -0.0051 232 GLY A O   
2420 O  O   B GLY A 232 ? 0.1071 0.1398 0.1444 0.0562  0.0193  0.0206  232 GLY A O   
2421 N  N   A GLU A 233 ? 0.1861 0.2020 0.1012 -0.0930 0.0675  -0.0216 233 GLU A N   
2422 N  N   B GLU A 233 ? 0.0728 0.2023 0.1540 0.0251  0.0054  -0.0193 233 GLU A N   
2423 C  CA  A GLU A 233 ? 0.2147 0.2657 0.1240 -0.1256 0.0487  -0.0714 233 GLU A CA  
2424 C  CA  B GLU A 233 ? 0.1578 0.1712 0.1297 0.0007  0.0043  0.0205  233 GLU A CA  
2425 C  C   A GLU A 233 ? 0.2355 0.3445 0.1703 -0.0388 0.1058  -0.0394 233 GLU A C   
2426 C  C   B GLU A 233 ? 0.1583 0.1736 0.1562 0.0379  0.0281  -0.0229 233 GLU A C   
2427 O  O   A GLU A 233 ? 0.3472 0.2991 0.1342 0.0342  0.1049  0.0428  233 GLU A O   
2428 O  O   B GLU A 233 ? 0.1495 0.1766 0.1863 0.0395  0.0230  0.0395  233 GLU A O   
2429 C  CB  A GLU A 233 ? 0.1612 0.2709 0.3407 -0.0140 -0.0059 0.0259  233 GLU A CB  
2430 C  CB  B GLU A 233 ? 0.3865 0.1610 0.0913 -0.0441 -0.0881 0.0582  233 GLU A CB  
2431 C  CG  A GLU A 233 ? 0.1669 0.2655 0.1439 0.0328  0.0322  0.0516  233 GLU A CG  
2432 C  CG  B GLU A 233 ? 0.3517 0.1757 0.0868 -0.0710 0.0320  0.0164  233 GLU A CG  
2433 C  CD  A GLU A 233 ? 0.2953 0.3291 0.2057 0.0074  -0.0368 0.0196  233 GLU A CD  
2434 C  CD  B GLU A 233 ? 0.2870 0.2494 0.1809 -0.0447 0.0172  -0.0465 233 GLU A CD  
2435 O  OE1 A GLU A 233 ? 0.2946 0.3454 0.1199 -0.0241 0.0745  -0.0188 233 GLU A OE1 
2436 O  OE1 B GLU A 233 ? 0.3264 0.3458 0.1651 -0.1500 0.0148  -0.0120 233 GLU A OE1 
2437 O  OE2 A GLU A 233 ? 0.2788 0.3582 0.2366 -0.0531 0.0674  0.1438  233 GLU A OE2 
2438 O  OE2 B GLU A 233 ? 0.3476 0.2815 0.2935 -0.0709 0.0671  -0.1110 233 GLU A OE2 
2439 N  N   A GLY A 234 ? 0.3589 0.3248 0.2301 -0.1146 0.2141  -0.0913 234 GLY A N   
2440 N  N   B GLY A 234 ? 0.1770 0.2098 0.3244 0.0929  0.0723  -0.0575 234 GLY A N   
2441 C  CA  A GLY A 234 ? 0.2265 0.3801 0.2090 0.0357  -0.0043 0.0193  234 GLY A CA  
2442 C  CA  B GLY A 234 ? 0.2037 0.1224 0.1540 0.0885  0.0384  0.0441  234 GLY A CA  
2443 C  C   A GLY A 234 ? 0.2021 0.2703 0.2019 0.0110  0.0759  0.0943  234 GLY A C   
2444 C  C   B GLY A 234 ? 0.2264 0.3226 0.1949 0.1146  0.0275  0.0891  234 GLY A C   
2445 O  O   A GLY A 234 ? 0.2687 0.5181 0.2465 -0.0038 0.1331  -0.0131 234 GLY A O   
2446 O  O   B GLY A 234 ? 0.2341 0.3698 0.3361 0.2003  0.0135  -0.0485 234 GLY A O   
2447 N  N   A GLU A 235 ? 0.1892 0.1375 0.1626 -0.0146 0.0348  0.0114  235 GLU A N   
2448 N  N   B GLU A 235 ? 0.2623 0.2574 0.1714 0.0491  -0.0399 0.0986  235 GLU A N   
2449 C  CA  A GLU A 235 ? 0.3578 0.2933 0.1163 -0.0430 -0.0209 -0.0027 235 GLU A CA  
2450 C  CA  B GLU A 235 ? 0.1838 0.2071 0.1680 0.0406  -0.0302 0.0381  235 GLU A CA  
2451 C  C   A GLU A 235 ? 0.2149 0.2648 0.1895 -0.0252 0.1699  -0.0582 235 GLU A C   
2452 C  C   B GLU A 235 ? 0.2357 0.1604 0.1386 0.0724  0.0057  0.0428  235 GLU A C   
2453 O  O   A GLU A 235 ? 0.2815 0.2554 0.3246 -0.0296 0.1749  -0.0868 235 GLU A O   
2454 O  O   B GLU A 235 ? 0.2174 0.1626 0.1960 0.0606  -0.0427 0.0575  235 GLU A O   
2455 C  CB  A GLU A 235 ? 0.3533 0.2560 0.2730 -0.1074 0.1826  -0.0242 235 GLU A CB  
2456 C  CB  B GLU A 235 ? 0.1784 0.2278 0.2005 0.0273  -0.0102 0.0107  235 GLU A CB  
2457 C  CG  A GLU A 235 ? 0.2421 0.2433 0.2432 -0.0916 0.1262  -0.0007 235 GLU A CG  
2458 C  CG  B GLU A 235 ? 0.3612 0.2445 0.1820 -0.0230 0.0230  0.1300  235 GLU A CG  
2459 C  CD  A GLU A 235 ? 0.2185 0.2337 0.3592 -0.0241 0.1336  -0.0186 235 GLU A CD  
2460 C  CD  B GLU A 235 ? 0.2027 0.4178 0.2881 -0.1234 0.0322  0.0165  235 GLU A CD  
2461 O  OE1 A GLU A 235 ? 0.1933 0.2942 0.4435 -0.0502 0.1729  0.0071  235 GLU A OE1 
2462 O  OE1 B GLU A 235 ? 0.1860 0.3916 0.2736 -0.0939 -0.0147 0.0697  235 GLU A OE1 
2463 O  OE2 A GLU A 235 ? 0.3449 0.3158 0.3616 -0.1133 0.1669  0.0617  235 GLU A OE2 
2464 O  OE2 B GLU A 235 ? 0.2784 0.4165 0.4099 -0.0926 -0.0041 0.0718  235 GLU A OE2 
2465 N  N   A PRO A 236 ? 0.1752 0.4110 0.2046 -0.0406 0.0812  -0.0195 236 PRO A N   
2466 N  N   B PRO A 236 ? 0.1486 0.1920 0.1368 0.0353  -0.0326 0.0076  236 PRO A N   
2467 C  CA  A PRO A 236 ? 0.1904 0.4101 0.3143 -0.0293 0.1142  0.0322  236 PRO A CA  
2468 C  CA  B PRO A 236 ? 0.1662 0.1868 0.1374 0.0737  0.0441  0.0781  236 PRO A CA  
2469 C  C   A PRO A 236 ? 0.1527 0.2860 0.2045 0.0348  0.0662  0.0428  236 PRO A C   
2470 C  C   B PRO A 236 ? 0.1328 0.1368 0.1262 0.0489  -0.0099 0.0217  236 PRO A C   
2471 O  O   A PRO A 236 ? 0.1693 0.2256 0.2887 0.0104  0.0715  0.0471  236 PRO A O   
2472 O  O   B PRO A 236 ? 0.1333 0.1718 0.1254 0.0566  -0.0137 -0.0080 236 PRO A O   
2473 C  CB  A PRO A 236 ? 0.2506 0.4996 0.4681 -0.0272 0.0229  0.0496  236 PRO A CB  
2474 C  CB  B PRO A 236 ? 0.1263 0.1655 0.2030 0.0392  0.0326  0.0746  236 PRO A CB  
2475 C  CG  A PRO A 236 ? 0.1658 0.4433 0.5058 0.0092  0.0247  0.0392  236 PRO A CG  
2476 C  CG  B PRO A 236 ? 0.2628 0.2804 0.2560 0.0592  -0.0450 0.0329  236 PRO A CG  
2477 C  CD  A PRO A 236 ? 0.3269 0.5271 0.3037 -0.0597 -0.1184 0.0137  236 PRO A CD  
2478 C  CD  B PRO A 236 ? 0.1159 0.2102 0.2389 0.0684  -0.0386 0.0187  236 PRO A CD  
2479 N  N   A GLU A 237 ? 0.1808 0.2502 0.2691 0.0776  0.0895  -0.0175 237 GLU A N   
2480 N  N   B GLU A 237 ? 0.1507 0.1351 0.1001 0.0386  0.0000  -0.0043 237 GLU A N   
2481 C  CA  A GLU A 237 ? 0.1747 0.2518 0.1215 0.0766  0.0474  -0.0340 237 GLU A CA  
2482 C  CA  B GLU A 237 ? 0.1386 0.1630 0.1125 0.0236  -0.0211 0.0129  237 GLU A CA  
2483 C  C   A GLU A 237 ? 0.0933 0.1660 0.1655 0.0219  0.0469  0.0088  237 GLU A C   
2484 C  C   B GLU A 237 ? 0.1405 0.0903 0.1328 0.0062  -0.0160 0.0196  237 GLU A C   
2485 O  O   A GLU A 237 ? 0.1085 0.1699 0.1800 0.0472  0.0324  -0.0309 237 GLU A O   
2486 O  O   B GLU A 237 ? 0.1924 0.1281 0.1186 0.0570  -0.0054 -0.0019 237 GLU A O   
2487 C  CB  A GLU A 237 ? 0.2454 0.2500 0.1969 0.0644  0.0434  -0.0674 237 GLU A CB  
2488 C  CB  B GLU A 237 ? 0.1463 0.1330 0.1332 0.0230  -0.0244 0.0288  237 GLU A CB  
2489 C  CG  A GLU A 237 ? 0.2393 0.2942 0.1480 0.0313  0.0184  -0.0019 237 GLU A CG  
2490 C  CG  B GLU A 237 ? 0.1233 0.1604 0.2091 -0.0209 -0.0487 0.0082  237 GLU A CG  
2491 C  CD  A GLU A 237 ? 0.2364 0.2032 0.2238 -0.0046 0.0333  -0.0678 237 GLU A CD  
2492 C  CD  B GLU A 237 ? 0.1826 0.2109 0.1554 0.0264  -0.0873 -0.0384 237 GLU A CD  
2493 O  OE1 A GLU A 237 ? 0.4871 0.4957 0.1870 0.0900  -0.0615 -0.1360 237 GLU A OE1 
2494 O  OE1 B GLU A 237 ? 0.2504 0.2186 0.2885 0.0355  -0.0992 -0.1402 237 GLU A OE1 
2495 O  OE2 A GLU A 237 ? 0.2158 0.2014 0.1545 -0.0109 -0.0031 -0.0749 237 GLU A OE2 
2496 O  OE2 B GLU A 237 ? 0.1885 0.1958 0.1502 -0.0487 0.0077  0.0006  237 GLU A OE2 
2497 N  N   A GLU A 238 ? 0.1186 0.1601 0.1396 -0.0076 0.0566  -0.0097 238 GLU A N   
2498 N  N   B GLU A 238 ? 0.1098 0.1222 0.1425 0.0115  0.0027  0.0270  238 GLU A N   
2499 C  CA  A GLU A 238 ? 0.1590 0.1994 0.1405 -0.0120 0.0593  -0.0296 238 GLU A CA  
2500 C  CA  B GLU A 238 ? 0.1163 0.1547 0.1303 -0.0104 0.0284  0.0113  238 GLU A CA  
2501 C  C   A GLU A 238 ? 0.1617 0.1568 0.1597 -0.0148 0.0821  -0.0203 238 GLU A C   
2502 C  C   B GLU A 238 ? 0.1383 0.1635 0.1407 0.0068  0.0339  -0.0164 238 GLU A C   
2503 O  O   A GLU A 238 ? 0.1448 0.1658 0.1508 -0.0085 0.1085  -0.0010 238 GLU A O   
2504 O  O   B GLU A 238 ? 0.0842 0.1680 0.1744 0.0152  0.0282  0.0065  238 GLU A O   
2505 C  CB  A GLU A 238 ? 0.1849 0.2091 0.2258 -0.0593 0.0483  -0.0206 238 GLU A CB  
2506 C  CB  B GLU A 238 ? 0.1163 0.1308 0.1504 0.0048  -0.0035 0.0439  238 GLU A CB  
2507 C  CG  A GLU A 238 ? 0.1886 0.3201 0.2939 -0.0670 -0.0161 -0.0658 238 GLU A CG  
2508 C  CG  B GLU A 238 ? 0.0908 0.3140 0.2145 0.0086  -0.0353 0.0287  238 GLU A CG  
2509 C  CD  A GLU A 238 ? 0.1172 0.2655 0.1865 0.0231  0.0456  -0.0838 238 GLU A CD  
2510 C  CD  B GLU A 238 ? 0.3030 0.3113 0.4426 -0.0060 -0.0049 -0.1498 238 GLU A CD  
2511 O  OE1 A GLU A 238 ? 0.2406 0.3068 0.1716 -0.0750 -0.0377 -0.0062 238 GLU A OE1 
2512 O  OE1 B GLU A 238 ? 0.6014 0.4147 0.8115 0.2495  -0.0335 -0.1430 238 GLU A OE1 
2513 O  OE2 A GLU A 238 ? 0.1725 0.1685 0.2019 -0.0137 0.0249  -0.0537 238 GLU A OE2 
2514 O  OE2 B GLU A 238 ? 0.4521 0.5005 0.3452 0.2513  -0.1861 -0.0834 238 GLU A OE2 
2515 N  N   A LEU A 239 ? 0.1536 0.1666 0.1304 -0.0397 0.0750  -0.0295 239 LEU A N   
2516 N  N   B LEU A 239 ? 0.2010 0.1847 0.1100 -0.0513 0.0113  -0.0170 239 LEU A N   
2517 C  CA  A LEU A 239 ? 0.1583 0.1626 0.1389 -0.0678 0.0869  -0.0427 239 LEU A CA  
2518 C  CA  B LEU A 239 ? 0.2093 0.2276 0.0818 -0.0700 0.0370  -0.0489 239 LEU A CA  
2519 C  C   A LEU A 239 ? 0.1872 0.1543 0.1030 -0.0807 0.0428  -0.0209 239 LEU A C   
2520 C  C   B LEU A 239 ? 0.2208 0.1779 0.0675 -0.0741 0.0671  -0.0137 239 LEU A C   
2521 O  O   A LEU A 239 ? 0.2081 0.1606 0.0987 -0.1031 0.0408  0.0120  239 LEU A O   
2522 O  O   B LEU A 239 ? 0.1845 0.2336 0.1132 -0.0562 0.0715  -0.0768 239 LEU A O   
2523 C  CB  A LEU A 239 ? 0.1468 0.1474 0.1572 -0.0364 0.0500  -0.0242 239 LEU A CB  
2524 C  CB  B LEU A 239 ? 0.1911 0.1872 0.1125 -0.0285 0.0151  -0.0231 239 LEU A CB  
2525 C  CG  A LEU A 239 ? 0.0900 0.1750 0.1603 -0.0175 0.0348  -0.0295 239 LEU A CG  
2526 C  CG  B LEU A 239 ? 0.1553 0.1419 0.1815 -0.0248 0.0379  -0.0518 239 LEU A CG  
2527 C  CD1 A LEU A 239 ? 0.1163 0.1638 0.2147 0.0076  0.0794  -0.0417 239 LEU A CD1 
2528 C  CD1 B LEU A 239 ? 0.1172 0.1297 0.2888 -0.0164 0.0315  -0.0397 239 LEU A CD1 
2529 C  CD2 A LEU A 239 ? 0.1716 0.1486 0.0794 0.0109  0.0381  -0.0657 239 LEU A CD2 
2530 C  CD2 B LEU A 239 ? 0.1753 0.2108 0.1920 0.0689  0.0436  -0.0509 239 LEU A CD2 
2531 N  N   . MET A 240 ? 0.2344 0.1601 0.1190 -0.0502 0.0689  -0.0115 240 MET A N   
2532 C  CA  . MET A 240 ? 0.2124 0.1665 0.0847 -0.0522 0.0675  -0.0104 240 MET A CA  
2533 C  C   . MET A 240 ? 0.1500 0.1353 0.0759 -0.0388 0.0390  -0.0315 240 MET A C   
2534 O  O   . MET A 240 ? 0.1664 0.1523 0.0802 -0.0441 0.0299  -0.0160 240 MET A O   
2535 C  CB  . MET A 240 ? 0.2587 0.1635 0.1014 -0.0601 0.0697  -0.0020 240 MET A CB  
2536 C  CG  . MET A 240 ? 0.2397 0.1439 0.1003 -0.0723 0.0644  -0.0195 240 MET A CG  
2537 S  SD  . MET A 240 ? 0.2578 0.1376 0.1260 -0.0763 0.0476  -0.0060 240 MET A SD  
2538 C  CE  . MET A 240 ? 0.2653 0.1606 0.1179 -0.0935 0.0518  -0.0041 240 MET A CE  
2539 N  N   . VAL A 241 ? 0.1750 0.1140 0.0965 -0.0491 0.0439  -0.0350 241 VAL A N   
2540 C  CA  . VAL A 241 ? 0.1814 0.0951 0.0906 -0.0414 0.0269  -0.0247 241 VAL A CA  
2541 C  C   . VAL A 241 ? 0.1371 0.0873 0.0976 -0.0175 0.0287  -0.0241 241 VAL A C   
2542 O  O   . VAL A 241 ? 0.1567 0.1310 0.1137 -0.0421 0.0588  -0.0498 241 VAL A O   
2543 C  CB  . VAL A 241 ? 0.1479 0.1005 0.1186 -0.0231 0.0337  -0.0414 241 VAL A CB  
2544 C  CG1 . VAL A 241 ? 0.2041 0.1328 0.1008 -0.0320 0.0119  -0.0383 241 VAL A CG1 
2545 C  CG2 . VAL A 241 ? 0.1899 0.1272 0.1586 -0.0313 0.0544  -0.0709 241 VAL A CG2 
2546 N  N   . ASP A 242 ? 0.1430 0.0897 0.0827 -0.0137 0.0416  -0.0280 242 ASP A N   
2547 C  CA  . ASP A 242 ? 0.1479 0.0992 0.0863 0.0000  0.0342  -0.0322 242 ASP A CA  
2548 C  C   . ASP A 242 ? 0.1364 0.1009 0.0815 -0.0131 0.0335  -0.0295 242 ASP A C   
2549 O  O   . ASP A 242 ? 0.1321 0.1212 0.1346 -0.0153 0.0161  -0.0401 242 ASP A O   
2550 C  CB  . ASP A 242 ? 0.1500 0.0994 0.1023 -0.0135 0.0386  -0.0337 242 ASP A CB  
2551 C  CG  . ASP A 242 ? 0.1506 0.0904 0.1127 0.0003  0.0399  -0.0331 242 ASP A CG  
2552 O  OD1 . ASP A 242 ? 0.1420 0.0807 0.1058 -0.0027 0.0307  -0.0219 242 ASP A OD1 
2553 O  OD2 . ASP A 242 ? 0.1565 0.1127 0.1438 0.0005  0.0441  -0.0463 242 ASP A OD2 
2554 N  N   . ASN A 243 ? 0.1179 0.0879 0.0944 -0.0282 0.0452  -0.0258 243 ASN A N   
2555 C  CA  . ASN A 243 ? 0.1204 0.0821 0.0869 -0.0232 0.0395  -0.0233 243 ASN A CA  
2556 C  C   . ASN A 243 ? 0.1111 0.0966 0.0838 -0.0170 0.0303  -0.0143 243 ASN A C   
2557 O  O   . ASN A 243 ? 0.1398 0.1023 0.0772 -0.0005 0.0386  -0.0136 243 ASN A O   
2558 C  CB  . ASN A 243 ? 0.1459 0.1097 0.0776 -0.0306 0.0156  -0.0035 243 ASN A CB  
2559 C  CG  . ASN A 243 ? 0.1441 0.1120 0.0652 -0.0452 0.0230  -0.0162 243 ASN A CG  
2560 O  OD1 . ASN A 243 ? 0.1369 0.0974 0.1145 -0.0175 0.0342  0.0131  243 ASN A OD1 
2561 N  ND2 . ASN A 243 ? 0.1594 0.1608 0.0935 -0.0575 0.0087  0.0082  243 ASN A ND2 
2562 N  N   . TRP A 244 ? 0.1071 0.0876 0.0886 -0.0176 0.0211  -0.0200 244 TRP A N   
2563 C  CA  . TRP A 244 ? 0.0978 0.0953 0.0812 -0.0148 0.0204  -0.0186 244 TRP A CA  
2564 C  C   . TRP A 244 ? 0.1030 0.0746 0.0978 -0.0027 0.0258  -0.0148 244 TRP A C   
2565 O  O   . TRP A 244 ? 0.0891 0.1111 0.1246 0.0068  0.0148  -0.0397 244 TRP A O   
2566 C  CB  . TRP A 244 ? 0.1066 0.0710 0.0827 -0.0035 0.0275  -0.0143 244 TRP A CB  
2567 C  CG  . TRP A 244 ? 0.0818 0.0799 0.0951 -0.0082 0.0351  -0.0049 244 TRP A CG  
2568 C  CD1 . TRP A 244 ? 0.1163 0.0821 0.0890 -0.0043 0.0458  -0.0104 244 TRP A CD1 
2569 C  CD2 . TRP A 244 ? 0.0895 0.0881 0.0948 -0.0026 0.0320  -0.0093 244 TRP A CD2 
2570 N  NE1 . TRP A 244 ? 0.1080 0.0834 0.1028 -0.0065 0.0313  -0.0126 244 TRP A NE1 
2571 C  CE2 . TRP A 244 ? 0.0894 0.0895 0.1222 0.0030  0.0241  -0.0103 244 TRP A CE2 
2572 C  CE3 . TRP A 244 ? 0.0974 0.1044 0.0906 0.0074  0.0230  -0.0085 244 TRP A CE3 
2573 C  CZ2 . TRP A 244 ? 0.1041 0.1102 0.1265 0.0147  0.0085  -0.0156 244 TRP A CZ2 
2574 C  CZ3 . TRP A 244 ? 0.1080 0.1027 0.1332 0.0076  0.0172  -0.0071 244 TRP A CZ3 
2575 C  CH2 . TRP A 244 ? 0.1249 0.1052 0.1324 0.0216  -0.0006 -0.0031 244 TRP A CH2 
2576 N  N   . ARG A 245 ? 0.0924 0.0881 0.0947 0.0007  0.0197  -0.0200 245 ARG A N   
2577 C  CA  . ARG A 245 ? 0.0944 0.0940 0.0906 -0.0010 0.0198  -0.0205 245 ARG A CA  
2578 C  C   . ARG A 245 ? 0.0802 0.0781 0.0926 0.0080  0.0015  -0.0230 245 ARG A C   
2579 O  O   . ARG A 245 ? 0.0842 0.1019 0.1071 0.0049  0.0125  -0.0153 245 ARG A O   
2580 C  CB  . ARG A 245 ? 0.0865 0.0931 0.0926 0.0019  0.0132  -0.0221 245 ARG A CB  
2581 C  CG  . ARG A 245 ? 0.0750 0.0879 0.1132 -0.0006 0.0013  -0.0262 245 ARG A CG  
2582 C  CD  . ARG A 245 ? 0.0608 0.0909 0.1181 0.0068  0.0241  -0.0204 245 ARG A CD  
2583 N  NE  . ARG A 245 ? 0.0740 0.0996 0.1263 -0.0148 0.0043  -0.0197 245 ARG A NE  
2584 C  CZ  . ARG A 245 ? 0.0767 0.1071 0.1249 -0.0054 0.0065  -0.0296 245 ARG A CZ  
2585 N  NH1 . ARG A 245 ? 0.0917 0.1127 0.1172 -0.0031 0.0228  -0.0200 245 ARG A NH1 
2586 N  NH2 . ARG A 245 ? 0.0744 0.1261 0.1624 -0.0211 0.0054  -0.0275 245 ARG A NH2 
2587 N  N   A PRO A 246 ? 0.0781 0.0872 0.1080 0.0125  0.0147  -0.0131 246 PRO A N   
2588 N  N   B PRO A 246 ? 0.0897 0.0811 0.1084 0.0087  0.0023  -0.0219 246 PRO A N   
2589 C  CA  A PRO A 246 ? 0.0974 0.0894 0.1009 0.0229  0.0080  -0.0093 246 PRO A CA  
2590 C  CA  B PRO A 246 ? 0.1045 0.0891 0.1082 0.0137  -0.0038 -0.0131 246 PRO A CA  
2591 C  C   A PRO A 246 ? 0.0789 0.0926 0.1039 0.0266  0.0000  -0.0024 246 PRO A C   
2592 C  C   B PRO A 246 ? 0.0688 0.0958 0.1093 -0.0040 -0.0153 -0.0109 246 PRO A C   
2593 O  O   A PRO A 246 ? 0.0623 0.1062 0.1010 0.0068  0.0013  -0.0196 246 PRO A O   
2594 O  O   B PRO A 246 ? 0.0956 0.0798 0.1154 0.0137  -0.0076 -0.0142 246 PRO A O   
2595 C  CB  A PRO A 246 ? 0.1058 0.1228 0.1164 0.0401  0.0184  -0.0107 246 PRO A CB  
2596 C  CB  B PRO A 246 ? 0.1240 0.1271 0.1483 0.0335  -0.0148 -0.0187 246 PRO A CB  
2597 C  CG  A PRO A 246 ? 0.1317 0.1032 0.1186 0.0388  0.0320  0.0113  246 PRO A CG  
2598 C  CG  B PRO A 246 ? 0.1254 0.1682 0.1854 0.0498  0.0439  0.0177  246 PRO A CG  
2599 C  CD  A PRO A 246 ? 0.0785 0.0824 0.1441 0.0231  0.0164  -0.0071 246 PRO A CD  
2600 C  CD  B PRO A 246 ? 0.0921 0.1322 0.1393 0.0296  0.0142  -0.0309 246 PRO A CD  
2601 N  N   . ALA A 247 ? 0.1075 0.0969 0.1030 0.0093  0.0175  -0.0137 247 ALA A N   
2602 C  CA  . ALA A 247 ? 0.1124 0.1091 0.0996 0.0048  -0.0031 -0.0080 247 ALA A CA  
2603 C  C   . ALA A 247 ? 0.0967 0.1044 0.0940 0.0198  0.0109  -0.0088 247 ALA A C   
2604 O  O   . ALA A 247 ? 0.1240 0.1071 0.1249 0.0386  -0.0120 -0.0172 247 ALA A O   
2605 C  CB  . ALA A 247 ? 0.1332 0.1346 0.1220 -0.0054 0.0182  -0.0103 247 ALA A CB  
2606 N  N   . GLN A 248 ? 0.0890 0.0878 0.1134 0.0031  -0.0035 -0.0063 248 GLN A N   
2607 C  CA  . GLN A 248 ? 0.0881 0.0970 0.1154 0.0187  -0.0108 -0.0140 248 GLN A CA  
2608 C  C   . GLN A 248 ? 0.1129 0.1118 0.1199 0.0239  -0.0070 -0.0120 248 GLN A C   
2609 O  O   . GLN A 248 ? 0.1213 0.1298 0.1071 0.0142  -0.0065 -0.0065 248 GLN A O   
2610 C  CB  . GLN A 248 ? 0.1134 0.0997 0.1184 0.0054  -0.0199 -0.0099 248 GLN A CB  
2611 C  CG  . GLN A 248 ? 0.1075 0.1039 0.1215 0.0049  -0.0166 -0.0175 248 GLN A CG  
2612 C  CD  . GLN A 248 ? 0.0973 0.1316 0.1486 -0.0074 -0.0027 -0.0023 248 GLN A CD  
2613 O  OE1 . GLN A 248 ? 0.1082 0.1974 0.1556 -0.0126 -0.0076 -0.0390 248 GLN A OE1 
2614 N  NE2 . GLN A 248 ? 0.1283 0.1405 0.1418 0.0130  -0.0087 -0.0232 248 GLN A NE2 
2615 N  N   . PRO A 249 ? 0.1233 0.1479 0.1080 0.0199  -0.0208 -0.0081 249 PRO A N   
2616 C  CA  . PRO A 249 ? 0.1547 0.1562 0.1039 0.0355  -0.0170 0.0000  249 PRO A CA  
2617 C  C   . PRO A 249 ? 0.1393 0.1290 0.1003 0.0236  -0.0447 0.0013  249 PRO A C   
2618 O  O   . PRO A 249 ? 0.1215 0.1290 0.1168 0.0326  -0.0197 0.0034  249 PRO A O   
2619 C  CB  . PRO A 249 ? 0.1563 0.2184 0.1860 0.0494  -0.0373 -0.0399 249 PRO A CB  
2620 C  CG  . PRO A 249 ? 0.1723 0.2560 0.1572 0.0333  -0.0272 -0.0156 249 PRO A CG  
2621 C  CD  . PRO A 249 ? 0.1149 0.1904 0.1613 0.0131  -0.0544 -0.0087 249 PRO A CD  
2622 N  N   . LEU A 250 ? 0.1682 0.1204 0.1046 0.0491  -0.0252 0.0013  250 LEU A N   
2623 C  CA  . LEU A 250 ? 0.1640 0.1163 0.0949 0.0232  -0.0074 0.0005  250 LEU A CA  
2624 C  C   . LEU A 250 ? 0.1506 0.1215 0.1058 0.0384  -0.0186 0.0000  250 LEU A C   
2625 O  O   . LEU A 250 ? 0.1526 0.1281 0.1242 0.0368  -0.0421 -0.0017 250 LEU A O   
2626 C  CB  . LEU A 250 ? 0.1705 0.1414 0.1508 0.0051  -0.0077 0.0155  250 LEU A CB  
2627 C  CG  . LEU A 250 ? 0.1513 0.1551 0.1648 -0.0126 0.0110  -0.0251 250 LEU A CG  
2628 C  CD1 . LEU A 250 ? 0.1497 0.1808 0.1644 0.0218  -0.0272 -0.0564 250 LEU A CD1 
2629 C  CD2 . LEU A 250 ? 0.2632 0.1739 0.2736 -0.0428 0.0891  -0.0115 250 LEU A CD2 
2630 N  N   . LYS A 251 ? 0.1721 0.1560 0.1141 0.0666  -0.0377 -0.0137 251 LYS A N   
2631 C  CA  . LYS A 251 ? 0.2197 0.1581 0.1263 0.0476  -0.0216 -0.0305 251 LYS A CA  
2632 C  C   . LYS A 251 ? 0.1747 0.2000 0.1651 0.0166  -0.0606 -0.0317 251 LYS A C   
2633 O  O   . LYS A 251 ? 0.2138 0.2359 0.1702 -0.0085 -0.0098 -0.0119 251 LYS A O   
2634 C  CB  . LYS A 251 ? 0.2093 0.1601 0.1896 0.0068  -0.0688 -0.0262 251 LYS A CB  
2635 C  CG  . LYS A 251 ? 0.2567 0.2366 0.2664 -0.0450 0.0859  -0.0727 251 LYS A CG  
2636 C  CD  . LYS A 251 ? 0.2662 0.2310 0.1965 0.0052  -0.0282 -0.0340 251 LYS A CD  
2637 C  CE  . LYS A 251 ? 0.1768 0.3100 0.3777 0.0124  0.0317  0.0082  251 LYS A CE  
2638 N  NZ  . LYS A 251 ? 0.2228 0.3377 0.5156 0.0403  0.0970  0.0452  251 LYS A NZ  
2639 N  N   . ASN A 252 ? 0.2034 0.1958 0.1058 0.0329  -0.0452 -0.0474 252 ASN A N   
2640 C  CA  . ASN A 252 ? 0.2335 0.3558 0.1409 0.0487  -0.0193 -0.0847 252 ASN A CA  
2641 C  C   . ASN A 252 ? 0.2415 0.2427 0.2090 0.0372  -0.0217 -0.0163 252 ASN A C   
2642 O  O   . ASN A 252 ? 0.2727 0.2266 0.2242 0.0210  0.0030  -0.0383 252 ASN A O   
2643 C  CB  . ASN A 252 ? 0.4302 0.3833 0.1712 0.0114  -0.0262 -0.1441 252 ASN A CB  
2644 C  CG  . ASN A 252 ? 0.3122 0.3328 0.2255 -0.0208 -0.0177 -0.0952 252 ASN A CG  
2645 O  OD1 . ASN A 252 ? 0.6150 0.4666 0.2666 -0.0741 0.1489  -0.0081 252 ASN A OD1 
2646 N  ND2 . ASN A 252 ? 0.3630 0.3474 0.3964 -0.0182 -0.0313 -0.1763 252 ASN A ND2 
2647 N  N   . ARG A 253 ? 0.1703 0.2533 0.0969 0.0489  -0.0148 -0.0140 253 ARG A N   
2648 C  CA  . ARG A 253 ? 0.1430 0.1772 0.0878 0.0186  0.0043  -0.0241 253 ARG A CA  
2649 C  C   . ARG A 253 ? 0.1626 0.1401 0.1005 0.0125  0.0003  -0.0228 253 ARG A C   
2650 O  O   . ARG A 253 ? 0.2384 0.1809 0.2317 0.0665  0.0798  0.0335  253 ARG A O   
2651 C  CB  . ARG A 253 ? 0.1574 0.1538 0.0776 0.0166  -0.0080 -0.0276 253 ARG A CB  
2652 C  CG  . ARG A 253 ? 0.1477 0.1483 0.0836 0.0049  -0.0027 -0.0231 253 ARG A CG  
2653 C  CD  . ARG A 253 ? 0.1696 0.1067 0.0772 0.0263  0.0038  -0.0261 253 ARG A CD  
2654 N  NE  . ARG A 253 ? 0.1283 0.1075 0.0820 0.0204  -0.0131 0.0000  253 ARG A NE  
2655 C  CZ  . ARG A 253 ? 0.1238 0.0924 0.0890 0.0219  -0.0065 0.0012  253 ARG A CZ  
2656 N  NH1 . ARG A 253 ? 0.0924 0.0996 0.0987 -0.0027 -0.0197 0.0013  253 ARG A NH1 
2657 N  NH2 . ARG A 253 ? 0.0900 0.1023 0.0961 0.0177  -0.0208 -0.0102 253 ARG A NH2 
2658 N  N   A GLN A 254 ? 0.1592 0.1836 0.0863 0.0137  0.0043  -0.0209 254 GLN A N   
2659 N  N   B GLN A 254 ? 0.1533 0.2152 0.0811 0.0229  -0.0003 -0.0606 254 GLN A N   
2660 C  CA  A GLN A 254 ? 0.1890 0.2136 0.0671 -0.0020 0.0076  -0.0230 254 GLN A CA  
2661 C  CA  B GLN A 254 ? 0.1703 0.1902 0.1212 0.0205  0.0131  -0.0204 254 GLN A CA  
2662 C  C   A GLN A 254 ? 0.1782 0.1360 0.0960 -0.0049 -0.0131 0.0059  254 GLN A C   
2663 C  C   B GLN A 254 ? 0.1723 0.1389 0.0948 0.0120  0.0243  -0.0102 254 GLN A C   
2664 O  O   A GLN A 254 ? 0.1483 0.1080 0.1517 0.0041  -0.0109 -0.0315 254 GLN A O   
2665 O  O   B GLN A 254 ? 0.2123 0.1815 0.1159 0.0023  0.0640  0.0170  254 GLN A O   
2666 C  CB  A GLN A 254 ? 0.2779 0.1739 0.0657 0.0019  0.0251  -0.0324 254 GLN A CB  
2667 C  CB  B GLN A 254 ? 0.1274 0.2125 0.0802 0.0211  0.0038  -0.0031 254 GLN A CB  
2668 C  CG  A GLN A 254 ? 0.3962 0.1430 0.3030 -0.1312 0.0040  -0.0259 254 GLN A CG  
2669 C  CG  B GLN A 254 ? 0.1876 0.2646 0.2272 0.0142  0.1146  -0.0148 254 GLN A CG  
2670 C  CD  A GLN A 254 ? 0.4241 0.3975 0.4745 -0.0294 -0.0606 -0.1447 254 GLN A CD  
2671 C  CD  B GLN A 254 ? 0.3014 0.3903 0.3652 0.0922  -0.0395 0.0017  254 GLN A CD  
2672 O  OE1 A GLN A 254 ? 0.5773 0.3373 0.1163 -0.0986 -0.0262 0.0377  254 GLN A OE1 
2673 O  OE1 B GLN A 254 ? 0.2964 0.6456 0.4104 -0.0052 0.1624  -0.2104 254 GLN A OE1 
2674 N  NE2 A GLN A 254 ? 0.7088 0.5855 0.1666 -0.0825 0.0584  -0.1481 254 GLN A NE2 
2675 N  NE2 B GLN A 254 ? 0.3952 0.4016 0.1167 0.0619  0.0706  -0.0027 254 GLN A NE2 
2676 N  N   . ILE A 255 ? 0.1464 0.1312 0.0899 0.0146  0.0076  -0.0015 255 ILE A N   
2677 C  CA  . ILE A 255 ? 0.1484 0.1233 0.0882 0.0146  0.0186  0.0087  255 ILE A CA  
2678 C  C   . ILE A 255 ? 0.1533 0.1335 0.0724 0.0103  0.0154  0.0000  255 ILE A C   
2679 O  O   . ILE A 255 ? 0.1499 0.1725 0.1120 0.0164  0.0436  0.0425  255 ILE A O   
2680 C  CB  . ILE A 255 ? 0.1536 0.1274 0.0860 0.0197  0.0156  -0.0023 255 ILE A CB  
2681 C  CG1 . ILE A 255 ? 0.1423 0.1367 0.1170 0.0247  0.0017  -0.0199 255 ILE A CG1 
2682 C  CG2 . ILE A 255 ? 0.1319 0.1712 0.1142 0.0119  0.0013  -0.0068 255 ILE A CG2 
2683 C  CD1 . ILE A 255 ? 0.1779 0.1394 0.1258 -0.0142 0.0120  -0.0410 255 ILE A CD1 
2684 N  N   . LYS A 256 ? 0.1222 0.1509 0.0856 0.0048  0.0226  0.0052  256 LYS A N   
2685 C  CA  . LYS A 256 ? 0.1247 0.1414 0.1005 0.0120  0.0271  -0.0041 256 LYS A CA  
2686 C  C   . LYS A 256 ? 0.1378 0.1597 0.0827 -0.0098 0.0187  0.0015  256 LYS A C   
2687 O  O   . LYS A 256 ? 0.1620 0.2176 0.0750 -0.0377 0.0237  -0.0037 256 LYS A O   
2688 C  CB  . LYS A 256 ? 0.1647 0.1613 0.1118 0.0141  0.0148  -0.0074 256 LYS A CB  
2689 C  CG  . LYS A 256 ? 0.2053 0.1861 0.1668 -0.0331 0.0172  -0.0416 256 LYS A CG  
2690 C  CD  . LYS A 256 ? 0.2709 0.2267 0.3388 -0.0483 0.1127  -0.0753 256 LYS A CD  
2691 C  CE  . LYS A 256 ? 0.3145 0.3355 0.4569 -0.1324 0.1349  -0.1652 256 LYS A CE  
2692 N  NZ  . LYS A 256 ? 0.3100 0.2820 0.8270 -0.1225 0.2134  -0.0775 256 LYS A NZ  
2693 N  N   . ALA A 257 ? 0.1346 0.1888 0.0956 -0.0159 0.0335  -0.0003 257 ALA A N   
2694 C  CA  . ALA A 257 ? 0.1186 0.1596 0.1434 -0.0054 0.0384  0.0000  257 ALA A CA  
2695 C  C   . ALA A 257 ? 0.1096 0.1635 0.1032 0.0003  0.0438  -0.0137 257 ALA A C   
2696 O  O   . ALA A 257 ? 0.1577 0.2118 0.0992 -0.0087 0.0615  -0.0219 257 ALA A O   
2697 C  CB  . ALA A 257 ? 0.1780 0.1649 0.1368 -0.0292 0.0320  -0.0148 257 ALA A CB  
2698 N  N   . SER A 258 ? 0.1055 0.1611 0.1098 -0.0132 0.0271  -0.0115 258 SER A N   
2699 C  CA  . SER A 258 ? 0.1091 0.1678 0.1395 0.0049  0.0368  -0.0041 258 SER A CA  
2700 C  C   . SER A 258 ? 0.1256 0.1949 0.1518 -0.0104 0.0683  -0.0065 258 SER A C   
2701 O  O   . SER A 258 ? 0.1067 0.3420 0.1903 0.0137  0.0610  0.0000  258 SER A O   
2702 C  CB  . SER A 258 ? 0.0994 0.1987 0.1362 0.0031  0.0096  0.0120  258 SER A CB  
2703 O  OG  . SER A 258 ? 0.1085 0.2050 0.1289 -0.0148 0.0368  -0.0068 258 SER A OG  
2704 N  N   . PHE A 259 ? 0.1398 0.1982 0.1357 -0.0313 0.0520  -0.0041 259 PHE A N   
2705 C  CA  . PHE A 259 ? 0.2023 0.2152 0.1653 -0.0675 0.0449  -0.0020 259 PHE A CA  
2706 C  C   . PHE A 259 ? 0.2195 0.2930 0.2066 -0.0671 0.0640  0.0522  259 PHE A C   
2707 O  O   . PHE A 259 ? 0.3125 0.2400 0.1757 -0.0615 0.0285  0.0333  259 PHE A O   
2708 C  CB  . PHE A 259 ? 0.1414 0.2267 0.1698 -0.0460 0.0057  0.0043  259 PHE A CB  
2709 C  CG  . PHE A 259 ? 0.1362 0.1817 0.1938 -0.0436 -0.0087 0.0131  259 PHE A CG  
2710 C  CD1 . PHE A 259 ? 0.1337 0.1929 0.1477 -0.0370 0.0003  -0.0070 259 PHE A CD1 
2711 C  CD2 . PHE A 259 ? 0.2269 0.2063 0.2666 -0.0324 0.0472  0.0318  259 PHE A CD2 
2712 C  CE1 . PHE A 259 ? 0.1787 0.2147 0.1944 -0.0034 0.0318  -0.0159 259 PHE A CE1 
2713 C  CE2 . PHE A 259 ? 0.1637 0.2463 0.3404 0.0012  -0.0447 0.0421  259 PHE A CE2 
2714 C  CZ  . PHE A 259 ? 0.2197 0.1836 0.3418 -0.0197 0.0287  -0.0266 259 PHE A CZ  
2715 N  N   . LYS A 260 ? 0.3373 0.3856 0.2804 -0.1523 0.1247  0.0807  260 LYS A N   
2716 C  CA  . LYS A 260 ? 0.4835 0.4867 0.2601 -0.1102 0.1098  0.1474  260 LYS A CA  
2717 C  C   . LYS A 260 ? 0.5616 0.5824 0.5105 0.0207  0.1538  0.1202  260 LYS A C   
2718 O  O   . LYS A 260 ? 0.5799 0.5766 0.6891 -0.2284 -0.0480 0.2935  260 LYS A O   
2719 C  CB  . LYS A 260 ? 0.6172 0.6043 0.2517 -0.1351 0.1509  0.0489  260 LYS A CB  
2720 C  CG  . LYS A 260 ? 0.4672 0.5608 0.4956 0.0259  0.2266  -0.0425 260 LYS A CG  
2721 C  CD  . LYS A 260 ? 0.5001 0.9695 0.6291 -0.1154 0.2906  -0.0515 260 LYS A CD  
2722 C  CE  . LYS A 260 ? 0.8212 1.1763 0.7013 0.0408  0.1720  -0.0370 260 LYS A CE  
2723 N  NZ  . LYS A 260 ? 0.8353 1.0916 0.8561 0.0597  0.2743  0.0230  260 LYS A NZ  
2724 O  OXT . LYS A 260 ? 0.6790 0.7436 0.7393 -0.0460 0.0285  0.3476  260 LYS A OXT 
2725 ZN ZN  . ZN  B .   ? 0.0957 0.0732 0.0678 -0.0092 0.0048  -0.0082 301 ZN  A ZN  
2726 S  S   . DMS C .   ? 0.2143 0.2278 0.2515 -0.0026 0.0441  -0.0362 302 DMS A S   
2727 O  O   . DMS C .   ? 0.3804 0.3368 0.2761 0.0908  0.0461  -0.1298 302 DMS A O   
2728 C  C1  . DMS C .   ? 0.2208 0.2154 0.1860 0.0315  0.0595  -0.0794 302 DMS A C1  
2729 C  C2  . DMS C .   ? 0.2393 0.2048 0.3449 -0.0458 0.0298  -0.0728 302 DMS A C2  
2730 F  F20 A V14 D .   ? 0.1711 0.0988 0.1443 0.0074  0.0076  -0.0037 303 V14 A F20 
2731 F  F20 B V14 D .   ? 0.1457 0.1039 0.1107 0.0000  -0.0060 -0.0065 303 V14 A F20 
2732 C  C5  A V14 D .   ? 0.2120 0.1251 0.1179 -0.0006 0.0271  0.0000  303 V14 A C5  
2733 C  C5  B V14 D .   ? 0.1412 0.0897 0.0935 -0.0397 0.0091  -0.0048 303 V14 A C5  
2734 C  C4  A V14 D .   ? 0.1542 0.1423 0.1188 0.0243  0.0071  -0.0082 303 V14 A C4  
2735 C  C4  B V14 D .   ? 0.0938 0.0958 0.0996 -0.0137 -0.0217 -0.0208 303 V14 A C4  
2736 S  S7  A V14 D .   ? 0.1197 0.0715 0.0895 -0.0041 -0.0135 -0.0073 303 V14 A S7  
2737 S  S7  B V14 D .   ? 0.1136 0.0693 0.0865 -0.0126 -0.0132 -0.0076 303 V14 A S7  
2738 O  O9  A V14 D .   ? 0.1136 0.0997 0.0861 0.0160  -0.0054 -0.0063 303 V14 A O9  
2739 O  O9  B V14 D .   ? 0.1142 0.1026 0.0899 0.0183  -0.0054 -0.0071 303 V14 A O9  
2740 N  N10 A V14 D .   ? 0.1145 0.0784 0.0952 -0.0076 -0.0030 -0.0263 303 V14 A N10 
2741 N  N10 B V14 D .   ? 0.1093 0.0768 0.0956 -0.0096 -0.0119 -0.0254 303 V14 A N10 
2742 O  O8  A V14 D .   ? 0.1335 0.0785 0.1143 0.0037  -0.0292 -0.0181 303 V14 A O8  
2743 O  O8  B V14 D .   ? 0.1339 0.0718 0.1150 0.0115  -0.0406 -0.0195 303 V14 A O8  
2744 C  C3  A V14 D .   ? 0.1601 0.1256 0.1057 0.0091  0.0010  -0.0073 303 V14 A C3  
2745 C  C3  B V14 D .   ? 0.0737 0.1118 0.1155 -0.0162 0.0266  -0.0038 303 V14 A C3  
2746 F  F12 A V14 D .   ? 0.1750 0.1305 0.1265 0.0286  0.0351  -0.0073 303 V14 A F12 
2747 F  F12 B V14 D .   ? 0.0931 0.1089 0.1483 -0.0126 0.0253  0.0006  303 V14 A F12 
2748 C  C2  A V14 D .   ? 0.1881 0.1082 0.1134 -0.0087 0.0406  -0.0231 303 V14 A C2  
2749 C  C2  B V14 D .   ? 0.1617 0.1590 0.1120 0.0082  0.0104  0.0109  303 V14 A C2  
2750 F  F13 A V14 D .   ? 0.1581 0.1299 0.1299 -0.0088 0.0421  -0.0337 303 V14 A F13 
2751 F  F13 B V14 D .   ? 0.2500 0.2217 0.1549 0.0237  0.0485  -0.0181 303 V14 A F13 
2752 C  C6  A V14 D .   ? 0.2133 0.1145 0.1262 0.0120  0.0208  -0.0082 303 V14 A C6  
2753 C  C6  B V14 D .   ? 0.1509 0.0861 0.1315 -0.0181 0.0003  0.0355  303 V14 A C6  
2754 C  C1  A V14 D .   ? 0.1797 0.1294 0.1168 0.0063  0.0200  -0.0113 303 V14 A C1  
2755 C  C1  B V14 D .   ? 0.1973 0.1421 0.1897 0.0030  0.0247  0.0104  303 V14 A C1  
2756 S  S11 A V14 D .   ? 0.1437 0.1836 0.0931 -0.0027 0.0153  -0.0186 303 V14 A S11 
2757 S  S11 B V14 D .   ? 0.3634 0.3194 0.2145 0.0142  0.0263  0.0979  303 V14 A S11 
2758 O  O16 A V14 D .   ? 0.1962 0.2099 0.1490 0.0461  0.0241  0.0361  303 V14 A O16 
2759 O  O16 B V14 D .   ? 0.2953 0.2711 0.2594 0.0438  0.0619  0.0948  303 V14 A O16 
2760 O  O17 A V14 D .   ? 0.2104 0.2266 0.1276 -0.0546 -0.0006 -0.0120 303 V14 A O17 
2761 O  O17 B V14 D .   ? 0.2910 0.3456 0.2028 -0.0295 0.0549  0.0299  303 V14 A O17 
2762 C  C15 A V14 D .   ? 0.1924 0.1899 0.1179 0.0099  0.0419  -0.0617 303 V14 A C15 
2763 C  C15 B V14 D .   ? 0.2777 0.3280 0.1974 -0.1489 -0.0015 0.1005  303 V14 A C15 
2764 C  C18 A V14 D .   ? 0.2375 0.1547 0.1199 -0.0465 0.0208  0.0031  303 V14 A C18 
2765 C  C18 B V14 D .   ? 0.1612 0.2669 0.2538 -0.0706 0.0296  0.0458  303 V14 A C18 
2766 O  O21 A V14 D .   ? 0.2342 0.2842 0.2291 -0.0240 0.0000  -0.0274 303 V14 A O21 
2767 O  O21 B V14 D .   ? 0.2402 0.2257 0.2637 -0.0635 0.0351  0.0211  303 V14 A O21 
2768 N  N19 A V14 D .   ? 0.2343 0.1256 0.2370 0.0003  -0.0023 0.0198  303 V14 A N19 
2769 N  N19 B V14 D .   ? 0.1852 0.1057 0.1619 0.0366  0.0303  0.0373  303 V14 A N19 
2770 C  C14 A V14 D .   ? 0.1685 0.1924 0.1981 0.0225  0.0285  -0.0410 303 V14 A C14 
2771 C  C14 B V14 D .   ? 0.2109 0.0847 0.2355 0.0110  0.0131  0.0294  303 V14 A C14 
2772 C  C28 A V14 D .   ? 0.1656 0.1568 0.2195 -0.0197 0.0219  -0.0515 303 V14 A C28 
2773 C  C28 B V14 D .   ? 0.1777 0.1315 0.2583 -0.0436 0.0500  0.0203  303 V14 A C28 
2774 C  C27 A V14 D .   ? 0.2055 0.2258 0.2572 -0.0196 0.0353  0.0153  303 V14 A C27 
2775 C  C27 B V14 D .   ? 0.2141 0.1723 0.1887 -0.0644 0.0282  0.0590  303 V14 A C27 
2776 C  C26 A V14 D .   ? 0.3449 0.1809 0.3458 0.0219  -0.0203 0.0076  303 V14 A C26 
2777 C  C26 B V14 D .   ? 0.1738 0.1572 0.1911 -0.0211 0.0109  0.0065  303 V14 A C26 
2778 C  C25 A V14 D .   ? 0.2224 0.1579 0.3217 -0.0164 0.0383  0.0195  303 V14 A C25 
2779 C  C25 B V14 D .   ? 0.1953 0.1353 0.3023 -0.0147 0.0130  0.0266  303 V14 A C25 
2780 C  C24 A V14 D .   ? 0.2099 0.2590 0.2657 -0.0031 0.0175  -0.0344 303 V14 A C24 
2781 C  C24 B V14 D .   ? 0.1854 0.1666 0.2346 0.0272  -0.0258 -0.0340 303 V14 A C24 
2782 C  C23 A V14 D .   ? 0.2152 0.1847 0.1815 0.0452  -0.0252 -0.0164 303 V14 A C23 
2783 C  C23 B V14 D .   ? 0.2003 0.2170 0.2348 -0.0154 -0.0082 -0.0309 303 V14 A C23 
2784 C  C22 A V14 D .   ? 0.1432 0.1800 0.2642 -0.0027 0.0080  -0.0359 303 V14 A C22 
2785 C  C22 B V14 D .   ? 0.3165 0.1524 0.2310 0.0130  -0.0623 0.0513  303 V14 A C22 
2786 N  N1  . BCN E .   ? 0.3713 0.4354 0.4122 0.0819  -0.0131 -0.0912 304 BCN A N1  
2787 C  C1  . BCN E .   ? 0.2350 0.2201 0.3693 -0.0789 0.0339  0.0160  304 BCN A C1  
2788 C  C2  . BCN E .   ? 0.2930 0.3810 0.5684 -0.0399 0.0767  -0.0252 304 BCN A C2  
2789 O  O21 . BCN E .   ? 0.2687 0.2217 0.3512 -0.0248 0.0925  0.0860  304 BCN A O21 
2790 O  O22 . BCN E .   ? 0.7929 0.3695 0.7013 -0.3688 -0.0184 -0.0252 304 BCN A O22 
2791 C  C3  . BCN E .   ? 0.2829 0.2892 0.2994 -0.0120 0.0494  0.1172  304 BCN A C3  
2792 C  C4  . BCN E .   ? 0.4601 0.4370 0.3808 0.0291  -0.0364 -0.0419 304 BCN A C4  
2793 O  O4  . BCN E .   ? 0.5001 0.3648 0.3986 -0.1080 0.1140  0.0104  304 BCN A O4  
2794 C  C5  . BCN E .   ? 0.3032 0.5091 0.2725 -0.1164 0.0049  0.0577  304 BCN A C5  
2795 C  C6  . BCN E .   ? 0.4128 0.5892 0.2520 0.0916  0.0837  0.1334  304 BCN A C6  
2796 O  O6  . BCN E .   ? 0.5213 0.4957 0.4458 -0.1360 -0.0038 0.1817  304 BCN A O6  
2797 O  O   . HOH F .   ? 0.0924 0.1073 0.0991 0.0000  0.0175  0.0015  401 HOH A O   
2798 O  O   . HOH F .   ? 0.1080 0.0899 0.0991 0.0065  0.0074  -0.0207 402 HOH A O   
2799 O  O   . HOH F .   ? 0.2140 0.1757 0.2436 0.0322  -0.1076 -0.0657 403 HOH A O   
2800 O  O   . HOH F .   ? 0.1170 0.1242 0.1359 0.0251  -0.0074 0.0198  404 HOH A O   
2801 O  O   . HOH F .   ? 0.1632 0.1384 0.1541 0.0425  0.0142  0.0080  405 HOH A O   
2802 O  O   . HOH F .   ? 0.1145 0.0930 0.1347 0.0219  -0.0006 -0.0102 406 HOH A O   
2803 O  O   . HOH F .   ? 0.1332 0.1330 0.1256 0.0215  -0.0170 0.0141  407 HOH A O   
2804 O  O   . HOH F .   ? 0.1111 0.1046 0.1194 -0.0114 0.0370  -0.0214 408 HOH A O   
2805 O  O   . HOH F .   ? 0.1364 0.1023 0.1141 -0.0093 0.0155  -0.0076 409 HOH A O   
2806 O  O   . HOH F .   ? 0.1224 0.1100 0.1046 0.0296  0.0092  -0.0082 410 HOH A O   
2807 O  O   . HOH F .   ? 0.2912 0.2572 0.3197 0.1159  -0.0535 -0.0059 411 HOH A O   
2808 O  O   . HOH F .   ? 0.0827 0.1684 0.2114 -0.0049 0.0071  -0.0487 412 HOH A O   
2809 O  O   . HOH F .   ? 0.2352 0.2355 0.1804 -0.0595 0.0564  0.0093  413 HOH A O   
2810 O  O   . HOH F .   ? 0.1285 0.1040 0.1212 -0.0086 0.0131  -0.0104 414 HOH A O   
2811 O  O   . HOH F .   ? 0.4648 0.2576 0.1464 -0.1800 0.0377  0.0182  415 HOH A O   
2812 O  O   . HOH F .   ? 0.3973 0.1606 0.2151 0.0141  -0.1437 0.0355  416 HOH A O   
2813 O  O   . HOH F .   ? 0.2260 0.2508 0.2036 0.0776  -0.0520 0.0070  417 HOH A O   
2814 O  O   . HOH F .   ? 0.0785 0.1838 0.2152 0.0280  0.0115  -0.0340 418 HOH A O   
2815 O  O   . HOH F .   ? 0.1861 0.1851 0.1766 -0.0142 -0.0126 -0.0615 419 HOH A O   
2816 O  O   . HOH F .   ? 0.1540 0.1696 0.2921 -0.0065 -0.0092 -0.0205 420 HOH A O   
2817 O  O   . HOH F .   ? 0.1170 0.1356 0.2754 -0.0120 0.0163  0.0077  421 HOH A O   
2818 O  O   . HOH F .   ? 0.1360 0.1867 0.1513 -0.0006 -0.0494 0.0340  422 HOH A O   
2819 O  O   . HOH F .   ? 0.4598 0.2202 0.2090 -0.0270 -0.1342 -0.0280 423 HOH A O   
2820 O  O   . HOH F .   ? 0.1723 0.1310 0.1874 -0.0121 0.0355  -0.0152 424 HOH A O   
2821 O  O   . HOH F .   ? 0.3129 0.1531 0.1804 -0.0131 -0.0754 0.0197  425 HOH A O   
2822 O  O   . HOH F .   ? 0.1262 0.2712 0.3246 -0.0097 -0.0487 0.0151  426 HOH A O   
2823 O  O   . HOH F .   ? 0.1592 0.2477 0.4824 -0.0348 -0.0603 0.0653  427 HOH A O   
2824 O  O   . HOH F .   ? 0.1956 0.1023 0.1567 -0.0035 0.0093  0.0200  428 HOH A O   
2825 O  O   . HOH F .   ? 0.1790 0.2104 0.1729 0.0214  0.0478  -0.0533 429 HOH A O   
2826 O  O   . HOH F .   ? 0.5041 0.1375 0.1802 0.0211  -0.1578 0.0372  430 HOH A O   
2827 O  O   . HOH F .   ? 0.2111 0.1127 0.1872 0.0269  0.0209  -0.0167 431 HOH A O   
2828 O  O   . HOH F .   ? 0.4022 0.3517 0.2373 0.0166  0.0498  0.0982  432 HOH A O   
2829 O  O   . HOH F .   ? 0.1471 0.1685 0.1809 0.0156  0.0126  0.0065  433 HOH A O   
2830 O  O   . HOH F .   ? 0.2702 0.1750 0.2057 -0.0700 -0.0260 -0.0186 434 HOH A O   
2831 O  O   . HOH F .   ? 0.3160 0.2352 0.1468 -0.0328 -0.0131 0.0059  435 HOH A O   
2832 O  O   . HOH F .   ? 0.2407 0.2698 0.2002 0.0366  0.0838  -0.0174 436 HOH A O   
2833 O  O   . HOH F .   ? 0.1779 0.1825 0.1917 0.0219  -0.0082 -0.0215 437 HOH A O   
2834 O  O   . HOH F .   ? 0.2032 0.1509 0.1867 0.0109  -0.0324 -0.0644 438 HOH A O   
2835 O  O   . HOH F .   ? 0.2342 0.1247 0.1987 -0.0331 0.0000  -0.0027 439 HOH A O   
2836 O  O   . HOH F .   ? 0.2912 0.1958 0.2458 0.0653  0.0326  0.0163  440 HOH A O   
2837 O  O   . HOH F .   ? 0.1350 0.1337 0.1937 -0.0498 -0.0219 -0.0340 441 HOH A O   
2838 O  O   . HOH F .   ? 0.1854 0.2073 0.2597 0.0724  -0.0199 -0.0264 442 HOH A O   
2839 O  O   . HOH F .   ? 0.1533 0.1152 0.1513 -0.0092 0.0073  -0.0080 443 HOH A O   
2840 O  O   . HOH F .   ? 0.1874 0.2696 0.2714 0.0584  -0.0230 -0.0065 444 HOH A O   
2841 O  O   . HOH F .   ? 0.2567 0.2944 0.4352 0.0832  0.0428  0.0397  445 HOH A O   
2842 O  O   . HOH F .   ? 0.1594 0.1140 0.1835 -0.0121 -0.0087 0.0071  446 HOH A O   
2843 O  O   . HOH F .   ? 0.2903 0.1066 0.3285 0.0043  -0.0731 0.0126  447 HOH A O   
2844 O  O   . HOH F .   ? 0.3115 0.1847 0.3499 -0.0423 -0.0502 -0.0291 448 HOH A O   
2845 O  O   . HOH F .   ? 0.3359 0.1811 0.1534 -0.0320 0.0208  0.0227  449 HOH A O   
2846 O  O   . HOH F .   ? 0.4074 0.1962 0.1498 0.0019  -0.0794 -0.0193 450 HOH A O   
2847 O  O   . HOH F .   ? 0.2280 0.2100 0.1881 0.0522  -0.0059 -0.0043 451 HOH A O   
2848 O  O   . HOH F .   ? 0.3027 0.1678 0.2140 0.0631  -0.0217 0.0318  452 HOH A O   
2849 O  O   . HOH F .   ? 0.3555 0.5503 0.1854 0.0575  0.0026  0.0207  453 HOH A O   
2850 O  O   . HOH F .   ? 0.2034 0.1805 0.1965 0.0361  -0.0329 0.0148  454 HOH A O   
2851 O  O   . HOH F .   ? 0.3551 0.1154 0.2208 0.0031  -0.0952 -0.0430 455 HOH A O   
2852 O  O   . HOH F .   ? 0.1730 0.1702 0.2960 -0.0601 -0.0531 0.0027  456 HOH A O   
2853 O  O   . HOH F .   ? 0.2484 0.1966 0.1260 0.0020  0.0118  -0.0148 457 HOH A O   
2854 O  O   . HOH F .   ? 0.2458 0.3287 0.3704 -0.0109 0.0666  -0.0035 458 HOH A O   
2855 O  O   . HOH F .   ? 0.2596 0.2267 0.1696 -0.0595 -0.0060 -0.0131 459 HOH A O   
2856 O  O   . HOH F .   ? 0.3064 0.2134 0.3016 0.0931  -0.1517 -0.0494 460 HOH A O   
2857 O  O   . HOH F .   ? 0.2906 0.4620 0.5299 -0.0564 -0.1317 -0.0346 461 HOH A O   
2858 O  O   . HOH F .   ? 0.1221 0.3610 0.4296 0.0438  -0.0317 0.0573  462 HOH A O   
2859 O  O   . HOH F .   ? 0.5562 0.2768 0.0847 -0.0666 0.0163  0.0052  463 HOH A O   
2860 O  O   . HOH F .   ? 0.2903 0.1739 0.2633 0.0741  -0.0296 -0.0098 464 HOH A O   
2861 O  O   . HOH F .   ? 0.5285 0.3749 0.2157 -0.1999 0.1018  -0.0566 465 HOH A O   
2862 O  O   . HOH F .   ? 0.3016 0.2935 0.3222 -0.0080 -0.0322 0.1202  466 HOH A O   
2863 O  O   . HOH F .   ? 0.1874 0.1570 0.4088 0.0153  0.0302  -0.0373 467 HOH A O   
2864 O  O   . HOH F .   ? 0.5719 0.2698 0.1515 -0.0705 0.0074  -0.0456 468 HOH A O   
2865 O  O   . HOH F .   ? 0.3012 0.1746 0.2605 -0.0043 0.0339  -0.0653 469 HOH A O   
2866 O  O   . HOH F .   ? 0.3106 0.2481 0.3064 -0.0825 0.0766  -0.1128 470 HOH A O   
2867 O  O   . HOH F .   ? 0.2887 0.2623 0.3720 0.0803  0.0728  0.0170  471 HOH A O   
2868 O  O   . HOH F .   ? 0.2003 0.3504 0.2451 -0.0200 -0.0615 0.0286  472 HOH A O   
2869 O  O   . HOH F .   ? 0.2502 0.1881 0.2014 0.0043  -0.0217 0.0658  473 HOH A O   
2870 O  O   . HOH F .   ? 0.2014 0.2863 0.2438 0.0562  0.0031  0.0313  474 HOH A O   
2871 O  O   . HOH F .   ? 0.2897 0.2856 0.3528 -0.0575 0.0027  0.0074  475 HOH A O   
2872 O  O   . HOH F .   ? 0.4555 0.2917 0.2011 -0.0626 0.1067  -0.1159 476 HOH A O   
2873 O  O   . HOH F .   ? 0.4997 0.3691 0.3291 -0.2000 -0.2362 0.0697  477 HOH A O   
2874 O  O   . HOH F .   ? 0.2994 0.3005 0.2881 -0.0710 0.0987  -0.0947 478 HOH A O   
2875 O  O   . HOH F .   ? 0.4092 0.2337 0.2071 -0.0010 -0.0285 0.0182  479 HOH A O   
2876 O  O   . HOH F .   ? 0.1978 0.2610 0.1606 0.0214  -0.0381 -0.0450 480 HOH A O   
2877 O  O   . HOH F .   ? 0.2870 0.1307 0.3587 -0.0023 0.0930  -0.0087 481 HOH A O   
2878 O  O   . HOH F .   ? 0.1875 0.1780 0.3246 0.0060  0.0454  -0.0608 482 HOH A O   
2879 O  O   . HOH F .   ? 0.1973 0.2093 0.2057 -0.0414 -0.0348 -0.0302 483 HOH A O   
2880 O  O   . HOH F .   ? 0.1933 0.1908 0.3027 -0.0124 0.0362  -0.0384 484 HOH A O   
2881 O  O   . HOH F .   ? 0.2122 0.1644 0.1759 -0.0006 -0.0076 0.0214  485 HOH A O   
2882 O  O   . HOH F .   ? 0.4885 0.3578 0.3251 -0.1464 0.1599  -0.1631 486 HOH A O   
2883 O  O   . HOH F .   ? 0.2788 0.2682 0.1653 -0.0478 0.0170  0.0076  487 HOH A O   
2884 O  O   . HOH F .   ? 0.2612 0.2082 0.3878 0.0529  -0.0579 -0.0063 488 HOH A O   
2885 O  O   . HOH F .   ? 0.3244 0.3161 0.2953 -0.0211 0.1062  -0.1268 489 HOH A O   
2886 O  O   . HOH F .   ? 0.3923 0.2127 0.2438 -0.0388 0.0091  0.0107  490 HOH A O   
2887 O  O   . HOH F .   ? 0.2230 0.4239 0.3409 0.0390  0.1172  0.0258  491 HOH A O   
2888 O  O   . HOH F .   ? 0.2124 0.1852 0.1996 -0.0121 0.0445  -0.0247 492 HOH A O   
2889 O  O   . HOH F .   ? 0.2786 0.3578 0.1419 -0.0873 -0.1098 0.0193  493 HOH A O   
2890 O  O   . HOH F .   ? 0.3910 0.1647 0.2529 0.0573  0.0626  0.0537  494 HOH A O   
2891 O  O   . HOH F .   ? 0.3027 0.3170 0.2224 0.1031  0.0843  -0.0135 495 HOH A O   
2892 O  O   . HOH F .   ? 0.2176 0.2840 0.2517 0.0137  0.0197  0.1171  496 HOH A O   
2893 O  O   . HOH F .   ? 0.2054 0.1755 0.2481 0.0295  0.0220  0.0041  497 HOH A O   
2894 O  O   . HOH F .   ? 0.2495 0.2043 0.2080 0.0417  0.0562  0.1071  498 HOH A O   
2895 O  O   . HOH F .   ? 0.4478 0.6251 0.1513 -0.0542 0.0846  0.0803  499 HOH A O   
2896 O  O   . HOH F .   ? 0.4895 0.2457 0.1288 0.0494  -0.0098 -0.0088 500 HOH A O   
2897 O  O   . HOH F .   ? 0.4906 0.2382 0.2395 0.0816  0.0472  0.0604  501 HOH A O   
2898 O  O   . HOH F .   ? 0.3289 0.2829 0.2709 0.0159  -0.0283 0.1119  502 HOH A O   
2899 O  O   . HOH F .   ? 0.2820 0.2483 0.2696 -0.0842 0.0549  -0.0575 503 HOH A O   
2900 O  O   . HOH F .   ? 0.2551 0.2998 0.2754 0.0208  0.0026  0.0388  504 HOH A O   
2901 O  O   . HOH F .   ? 0.3055 0.2630 0.1817 0.1333  -0.0562 0.0046  505 HOH A O   
2902 O  O   . HOH F .   ? 0.1633 0.2757 0.3296 0.0687  0.0627  0.0197  506 HOH A O   
2903 O  O   . HOH F .   ? 0.3519 0.4341 0.3768 -0.0381 0.1017  0.0394  507 HOH A O   
2904 O  O   . HOH F .   ? 0.1872 0.2766 0.2224 0.0082  -0.0068 -0.0040 508 HOH A O   
2905 O  O   . HOH F .   ? 0.5374 0.2711 0.4863 0.0476  -0.1194 -0.1151 509 HOH A O   
2906 O  O   . HOH F .   ? 0.2809 0.5048 0.3898 -0.0496 0.0417  0.2205  510 HOH A O   
2907 O  O   . HOH F .   ? 0.2554 0.1145 0.1917 -0.0359 -0.0171 -0.0031 511 HOH A O   
2908 O  O   . HOH F .   ? 0.2247 0.2689 0.4971 0.0193  0.1272  0.0956  512 HOH A O   
2909 O  O   . HOH F .   ? 0.5156 0.2344 0.2827 -0.0182 -0.0601 0.1852  513 HOH A O   
2910 O  O   . HOH F .   ? 0.5174 0.2888 0.3027 -0.0288 -0.0326 0.0806  514 HOH A O   
2911 O  O   . HOH F .   ? 0.3210 0.2257 0.2901 -0.0745 0.1272  -0.0494 515 HOH A O   
2912 O  O   . HOH F .   ? 0.3750 0.2272 0.3142 0.0242  -0.0452 -0.0082 516 HOH A O   
2913 O  O   . HOH F .   ? 0.3206 0.1238 0.3131 -0.0271 -0.0966 0.0538  517 HOH A O   
2914 O  O   . HOH F .   ? 0.4401 0.3587 0.3273 -0.1599 0.0692  -0.0763 518 HOH A O   
2915 O  O   . HOH F .   ? 0.3296 0.5001 0.4826 0.0995  0.1643  -0.0215 519 HOH A O   
2916 O  O   . HOH F .   ? 0.3425 0.2617 0.3327 -0.0825 0.0797  0.0216  520 HOH A O   
2917 O  O   . HOH F .   ? 0.3282 0.5713 0.3553 0.0076  -0.1612 0.1518  521 HOH A O   
2918 O  O   . HOH F .   ? 0.2285 0.1906 0.2378 0.0046  -0.0724 -0.0034 522 HOH A O   
2919 O  O   . HOH F .   ? 0.3032 0.1574 0.2430 0.0013  -0.0204 -0.0043 523 HOH A O   
2920 O  O   . HOH F .   ? 0.2574 0.2612 0.2763 -0.0214 -0.0031 0.0838  524 HOH A O   
2921 O  O   . HOH F .   ? 0.2845 0.3882 0.5733 0.0489  -0.0227 0.0359  525 HOH A O   
2922 O  O   . HOH F .   ? 0.5317 0.3027 0.1565 -0.0916 0.0124  0.1375  526 HOH A O   
2923 O  O   . HOH F .   ? 0.1904 0.6452 0.5011 -0.1137 0.0454  0.0847  527 HOH A O   
2924 O  O   . HOH F .   ? 0.3513 0.4185 0.7221 -0.0767 0.3088  -0.2398 528 HOH A O   
2925 O  O   . HOH F .   ? 0.2583 0.1949 0.2698 -0.0049 -0.0395 -0.0732 529 HOH A O   
2926 O  O   . HOH F .   ? 0.3533 0.3456 0.3574 -0.1062 -0.0489 -0.0395 530 HOH A O   
2927 O  O   . HOH F .   ? 0.2714 0.1849 0.1993 0.0715  -0.0178 -0.0093 531 HOH A O   
2928 O  O   . HOH F .   ? 0.2418 0.3115 0.3077 -0.0024 -0.0362 -0.0197 532 HOH A O   
2929 O  O   . HOH F .   ? 0.2048 0.2156 0.3447 0.0772  -0.0390 -0.1004 533 HOH A O   
2930 O  O   . HOH F .   ? 0.3707 0.2037 0.1723 0.0469  0.0063  0.0303  534 HOH A O   
2931 O  O   . HOH F .   ? 0.2276 0.2551 0.3208 -0.0023 0.0868  -0.0329 535 HOH A O   
2932 O  O   . HOH F .   ? 0.4185 0.3278 0.4004 -0.0232 -0.1993 -0.1368 536 HOH A O   
2933 O  O   . HOH F .   ? 0.4638 0.2529 0.1832 -0.0961 0.0187  -0.0767 537 HOH A O   
2934 O  O   . HOH F .   ? 0.3594 0.2282 0.4449 -0.1576 0.0159  0.0627  538 HOH A O   
2935 O  O   A HOH F .   ? 0.1569 0.4532 0.1827 0.0037  -0.0344 -0.0942 539 HOH A O   
2936 O  O   B HOH F .   ? 0.1605 0.4352 0.1601 -0.0228 -0.0776 0.0115  539 HOH A O   
2937 O  O   . HOH F .   ? 0.2205 0.2278 0.3034 -0.0221 -0.0137 -0.0593 540 HOH A O   
2938 O  O   . HOH F .   ? 0.4657 0.3373 0.2508 -0.1146 0.0121  -0.0214 541 HOH A O   
2939 O  O   . HOH F .   ? 0.3249 0.3059 0.4465 0.1110  0.0322  0.0515  542 HOH A O   
2940 O  O   . HOH F .   ? 0.6014 0.5661 0.2511 0.0948  -0.0410 -0.1658 543 HOH A O   
2941 O  O   . HOH F .   ? 0.3783 0.2549 0.3127 -0.0007 -0.1298 -0.1274 544 HOH A O   
2942 O  O   . HOH F .   ? 0.4257 0.2863 0.2425 -0.1484 -0.0031 0.0197  545 HOH A O   
2943 O  O   . HOH F .   ? 0.1542 0.7397 0.4614 0.0192  -0.0093 -0.2637 546 HOH A O   
2944 O  O   . HOH F .   ? 0.5137 0.4415 0.3804 -0.0803 0.0447  -0.1333 547 HOH A O   
2945 O  O   . HOH F .   ? 0.3740 0.2639 0.2865 0.0156  0.0125  -0.0348 548 HOH A O   
2946 O  O   . HOH F .   ? 0.6395 0.3136 0.2220 -0.0333 0.1120  -0.0003 549 HOH A O   
2947 O  O   . HOH F .   ? 0.3323 0.2433 0.7651 -0.0339 -0.0507 0.0048  550 HOH A O   
2948 O  O   . HOH F .   ? 0.3190 0.3328 0.4192 0.0054  -0.0329 0.0754  551 HOH A O   
2949 O  O   . HOH F .   ? 0.3325 0.3138 0.3066 -0.0035 0.0434  -0.0474 552 HOH A O   
2950 O  O   . HOH F .   ? 0.3095 0.3558 0.3111 0.0776  -0.0535 0.0205  553 HOH A O   
2951 O  O   . HOH F .   ? 0.5949 0.2962 0.6413 -0.1246 -0.1826 -0.0082 554 HOH A O   
2952 O  O   . HOH F .   ? 0.3535 0.3616 0.1843 0.0060  0.0886  -0.0766 555 HOH A O   
2953 O  O   . HOH F .   ? 0.1768 0.2808 0.3632 0.0333  -0.0231 -0.0175 556 HOH A O   
2954 O  O   . HOH F .   ? 0.3222 0.1883 0.3000 -0.0377 -0.0172 -0.0318 557 HOH A O   
2955 O  O   . HOH F .   ? 0.2883 0.5665 0.2576 -0.0974 -0.0164 0.0749  558 HOH A O   
2956 O  O   . HOH F .   ? 0.4609 0.2402 0.2500 0.0562  0.0054  0.0252  559 HOH A O   
2957 O  O   . HOH F .   ? 0.1532 0.3021 0.2438 0.0065  0.0302  -0.0320 560 HOH A O   
2958 O  O   . HOH F .   ? 0.6370 0.2262 0.1800 -0.0054 0.0269  0.0230  561 HOH A O   
2959 O  O   . HOH F .   ? 0.3339 0.2666 0.2073 -0.0043 0.0674  -0.0513 562 HOH A O   
2960 O  O   . HOH F .   ? 0.3583 0.6323 0.4539 0.0917  0.0471  0.1546  563 HOH A O   
2961 O  O   . HOH F .   ? 0.5019 0.2782 0.3361 0.1342  -0.0719 -0.0908 564 HOH A O   
2962 O  O   . HOH F .   ? 0.2520 0.4993 0.5673 -0.0372 -0.0456 -0.1482 565 HOH A O   
2963 O  O   . HOH F .   ? 0.1761 0.2675 0.2894 0.0137  0.0034  0.0666  566 HOH A O   
2964 O  O   . HOH F .   ? 0.3039 0.4029 0.2269 -0.0221 -0.0825 0.1092  567 HOH A O   
2965 O  O   . HOH F .   ? 0.2285 0.2452 0.3384 0.0219  0.0815  0.0447  568 HOH A O   
2966 O  O   . HOH F .   ? 0.3510 0.3935 0.6345 -0.1717 -0.1615 0.0841  569 HOH A O   
2967 O  O   . HOH F .   ? 0.4341 0.4158 0.1903 -0.0280 -0.0074 0.0189  570 HOH A O   
2968 O  O   . HOH F .   ? 0.4277 0.3361 0.5008 -0.0625 -0.2079 0.1755  571 HOH A O   
2969 O  O   . HOH F .   ? 0.2748 0.3409 0.2648 -0.0645 -0.0031 0.0120  572 HOH A O   
2970 O  O   . HOH F .   ? 0.2373 0.2653 0.5515 -0.0469 0.0272  -0.1366 573 HOH A O   
2971 O  O   . HOH F .   ? 0.6437 0.2824 0.5343 0.1202  0.0798  -0.0908 574 HOH A O   
2972 O  O   . HOH F .   ? 0.2319 0.2797 0.2791 0.0087  -0.0318 -0.0441 575 HOH A O   
2973 O  O   . HOH F .   ? 0.2345 0.1477 0.2531 0.0035  -0.0335 -0.0012 576 HOH A O   
2974 O  O   . HOH F .   ? 0.2404 0.2397 0.2147 0.0439  -0.0177 0.0209  577 HOH A O   
2975 O  O   . HOH F .   ? 0.2791 0.3373 0.4239 0.1181  -0.0759 -0.0680 578 HOH A O   
2976 O  O   . HOH F .   ? 0.4284 0.2603 0.3452 -0.0988 -0.1976 -0.0439 579 HOH A O   
2977 O  O   . HOH F .   ? 0.3122 0.3892 0.5339 0.1203  -0.1022 -0.0688 580 HOH A O   
2978 O  O   . HOH F .   ? 0.4873 0.2104 0.2942 -0.1379 -0.1323 0.0063  581 HOH A O   
2979 O  O   . HOH F .   ? 0.1768 0.2511 0.4223 0.0006  0.0432  -0.0102 582 HOH A O   
2980 O  O   . HOH F .   ? 0.2836 0.2258 0.2944 -0.0261 -0.0196 0.0649  583 HOH A O   
2981 O  O   . HOH F .   ? 0.3201 0.2432 0.3625 -0.0399 -0.0073 0.0777  584 HOH A O   
2982 O  O   . HOH F .   ? 0.3804 0.7376 0.2592 -0.1658 0.0851  -0.1333 585 HOH A O   
2983 O  O   . HOH F .   ? 0.4393 0.2511 0.3975 0.0175  0.1347  -0.0088 586 HOH A O   
2984 O  O   . HOH F .   ? 0.3892 0.1640 0.2547 0.0392  0.0020  -0.0320 587 HOH A O   
2985 O  O   . HOH F .   ? 0.3474 0.4447 0.3203 0.0516  0.0046  -0.0496 588 HOH A O   
2986 O  O   . HOH F .   ? 0.2890 0.4472 0.3111 -0.1014 0.1105  -0.1849 589 HOH A O   
2987 O  O   . HOH F .   ? 0.2860 0.3503 0.3269 -0.0441 0.0414  -0.0381 590 HOH A O   
2988 O  O   . HOH F .   ? 0.4404 0.2745 0.2984 -0.1076 0.0368  -0.0007 591 HOH A O   
2989 O  O   . HOH F .   ? 0.3041 0.3161 0.2312 -0.0417 0.0705  0.0562  592 HOH A O   
2990 O  O   . HOH F .   ? 0.3235 0.2084 0.5795 -0.0172 -0.0538 -0.0015 593 HOH A O   
2991 O  O   . HOH F .   ? 0.2996 0.4180 0.2430 -0.1657 0.0052  0.0197  594 HOH A O   
2992 O  O   . HOH F .   ? 0.3847 0.2127 0.3012 -0.0749 0.0414  -0.0500 595 HOH A O   
2993 O  O   . HOH F .   ? 0.4683 0.4747 0.1741 0.0790  -0.0086 0.0126  596 HOH A O   
2994 O  O   . HOH F .   ? 0.2238 0.1739 0.3901 0.0151  -0.0428 -0.0182 597 HOH A O   
2995 O  O   . HOH F .   ? 0.3007 0.3765 0.3847 -0.0891 0.0926  -0.0476 598 HOH A O   
2996 O  O   . HOH F .   ? 0.1746 0.4499 0.3688 -0.0557 -0.0520 0.0027  599 HOH A O   
2997 O  O   . HOH F .   ? 0.4397 0.3102 0.4115 0.0904  -0.0142 0.0237  600 HOH A O   
2998 O  O   . HOH F .   ? 0.3215 0.3043 0.2014 -0.0292 0.0020  0.0537  601 HOH A O   
2999 O  O   . HOH F .   ? 0.3014 0.3880 0.5597 0.1976  0.1888  0.2108  602 HOH A O   
3000 O  O   . HOH F .   ? 0.2666 0.3564 0.4573 0.0250  -0.0230 -0.0877 603 HOH A O   
3001 O  O   . HOH F .   ? 0.3282 0.4435 0.2351 -0.0164 0.0573  0.1048  604 HOH A O   
3002 O  O   . HOH F .   ? 0.2229 0.3950 0.6183 -0.1403 -0.1057 -0.0085 605 HOH A O   
3003 O  O   . HOH F .   ? 0.3801 0.2272 0.4781 0.0869  -0.0361 -0.0855 606 HOH A O   
3004 O  O   . HOH F .   ? 0.3989 0.3501 0.2044 0.0248  -0.0812 -0.0297 607 HOH A O   
3005 O  O   . HOH F .   ? 0.4332 0.2309 0.3524 0.0942  0.0511  0.0264  608 HOH A O   
3006 O  O   . HOH F .   ? 0.4571 0.3964 0.8385 -0.0793 0.0939  0.1827  609 HOH A O   
3007 O  O   . HOH F .   ? 0.5554 0.2326 0.2709 -0.0789 -0.1923 -0.0197 610 HOH A O   
3008 O  O   . HOH F .   ? 0.2416 0.2167 0.1497 0.0263  0.0081  -0.0397 611 HOH A O   
3009 O  O   . HOH F .   ? 0.3871 0.2027 0.4877 0.0974  0.1362  0.0597  612 HOH A O   
3010 O  O   . HOH F .   ? 0.4444 0.3314 0.2402 -0.1142 0.1141  -0.1260 613 HOH A O   
3011 O  O   . HOH F .   ? 0.5339 0.3267 0.3810 0.0068  -0.1912 -0.0851 614 HOH A O   
3012 O  O   . HOH F .   ? 0.2664 0.4347 0.5059 -0.0516 -0.0109 -0.0412 615 HOH A O   
3013 O  O   . HOH F .   ? 0.4011 0.2089 0.1529 -0.0922 0.0500  0.0020  616 HOH A O   
3014 O  O   . HOH F .   ? 0.2513 0.1775 0.2046 0.0342  -0.0737 -0.0148 617 HOH A O   
3015 O  O   . HOH F .   ? 0.2933 0.3258 0.2481 0.0590  0.0439  0.0137  618 HOH A O   
3016 O  O   . HOH F .   ? 0.2581 0.1861 0.3370 -0.0006 -0.0755 -0.0049 619 HOH A O   
3017 O  O   . HOH F .   ? 0.4514 0.2754 0.4554 -0.0155 -0.1580 0.1018  620 HOH A O   
3018 O  O   . HOH F .   ? 0.2018 0.2736 0.4007 0.0043  -0.0115 -0.0219 621 HOH A O   
3019 O  O   . HOH F .   ? 0.3222 0.3495 0.3788 0.0806  -0.0293 0.0656  622 HOH A O   
3020 O  O   . HOH F .   ? 0.4982 0.3000 0.3393 0.0203  -0.0706 0.0254  623 HOH A O   
3021 O  O   . HOH F .   ? 0.3828 0.4749 0.4530 -0.0118 0.0249  0.1272  624 HOH A O   
3022 O  O   . HOH F .   ? 0.2086 0.4656 0.4004 0.0833  -0.0304 0.0375  625 HOH A O   
3023 O  O   . HOH F .   ? 0.6431 0.2687 0.5044 -0.0522 -0.1704 -0.0675 626 HOH A O   
3024 O  O   . HOH F .   ? 0.4659 0.5593 0.2310 -0.1307 0.1377  -0.2001 627 HOH A O   
3025 O  O   . HOH F .   ? 0.2312 0.5335 0.4598 0.0015  0.0015  -0.0372 628 HOH A O   
3026 O  O   . HOH F .   ? 0.2942 0.3088 0.5723 -0.0474 -0.1234 -0.0155 629 HOH A O   
3027 O  O   . HOH F .   ? 0.2513 0.4194 0.2854 0.0368  0.0781  -0.0992 630 HOH A O   
3028 O  O   . HOH F .   ? 0.4250 0.2842 0.3418 0.0728  -0.0087 -0.0412 631 HOH A O   
3029 O  O   . HOH F .   ? 0.3537 0.2026 0.4377 0.0542  -0.0057 -0.0370 632 HOH A O   
3030 O  O   . HOH F .   ? 0.3258 0.4201 0.7415 -0.1256 -0.2327 0.0126  633 HOH A O   
3031 O  O   . HOH F .   ? 0.6190 0.2183 0.5468 -0.0626 -0.1334 -0.0564 634 HOH A O   
3032 O  O   . HOH F .   ? 0.2612 0.5539 0.3819 -0.0612 0.1739  0.0882  635 HOH A O   
3033 O  O   . HOH F .   ? 0.3689 0.3483 0.1872 -0.0626 -0.0046 -0.0286 636 HOH A O   
3034 O  O   . HOH F .   ? 0.5817 0.1972 0.3815 0.0480  0.0584  -0.0104 637 HOH A O   
3035 O  O   . HOH F .   ? 0.6754 0.3652 0.2590 -0.0640 0.1735  0.0120  638 HOH A O   
3036 O  O   . HOH F .   ? 0.3041 0.4864 0.4546 0.0970  -0.0346 -0.0299 639 HOH A O   
3037 O  O   . HOH F .   ? 0.5550 0.3555 0.3968 -0.0878 -0.0697 0.0564  640 HOH A O   
3038 O  O   . HOH F .   ? 0.3689 0.3564 0.4562 -0.0192 -0.0719 -0.0584 641 HOH A O   
3039 O  O   . HOH F .   ? 0.4607 0.3461 0.3542 -0.0197 0.0137  -0.1789 642 HOH A O   
3040 O  O   . HOH F .   ? 0.2910 0.4990 0.3971 -0.0996 -0.0259 -0.0115 643 HOH A O   
3041 O  O   . HOH F .   ? 0.3673 0.3679 0.4780 -0.0120 0.0974  -0.1018 644 HOH A O   
3042 O  O   . HOH F .   ? 0.2597 0.5676 0.5224 0.0535  0.1272  0.0904  645 HOH A O   
3043 O  O   . HOH F .   ? 0.2434 0.5001 0.5440 0.0189  0.1206  0.0684  646 HOH A O   
3044 O  O   . HOH F .   ? 0.4054 0.1639 0.3375 -0.0073 -0.0275 -0.0177 647 HOH A O   
3045 O  O   . HOH F .   ? 0.6413 0.2479 0.2436 -0.1508 0.0571  0.0408  648 HOH A O   
3046 O  O   . HOH F .   ? 0.1867 0.4601 0.4982 -0.0595 0.0922  0.0619  649 HOH A O   
3047 O  O   . HOH F .   ? 0.3623 0.5281 0.3643 0.0337  0.0483  -0.2549 650 HOH A O   
3048 O  O   . HOH F .   ? 0.5899 0.4893 0.2296 -0.3878 0.1545  -0.0878 651 HOH A O   
3049 O  O   . HOH F .   ? 0.3865 0.3680 0.3603 -0.0093 0.0684  0.0216  652 HOH A O   
3050 O  O   . HOH F .   ? 0.6129 0.4501 0.2161 0.1484  0.0688  -0.0041 653 HOH A O   
3051 O  O   . HOH F .   ? 0.4250 0.5001 0.4189 -0.0170 -0.0843 0.1825  654 HOH A O   
3052 O  O   . HOH F .   ? 0.6118 0.3470 0.2608 0.0807  -0.0197 -0.1835 655 HOH A O   
3053 O  O   . HOH F .   ? 0.3237 0.3375 0.4857 -0.0829 0.0020  0.1052  656 HOH A O   
3054 O  O   . HOH F .   ? 0.2955 0.6506 0.4634 -0.1014 -0.1243 0.2838  657 HOH A O   
3055 O  O   . HOH F .   ? 0.3677 0.3558 0.5360 -0.1594 0.0295  0.1846  658 HOH A O   
3056 O  O   . HOH F .   ? 0.3165 0.5195 0.2161 -0.0098 0.0261  -0.1195 659 HOH A O   
3057 O  O   . HOH F .   ? 0.3036 0.3912 0.4893 0.0693  0.0520  0.0238  660 HOH A O   
3058 O  O   . HOH F .   ? 0.3991 0.2469 0.3869 0.0518  0.0577  0.0397  661 HOH A O   
3059 O  O   . HOH F .   ? 0.4875 0.2545 0.2815 -0.0298 0.1111  0.0318  662 HOH A O   
3060 O  O   . HOH F .   ? 0.4650 0.3609 0.3045 -0.0590 -0.0631 -0.0193 663 HOH A O   
3061 O  O   . HOH F .   ? 0.1759 0.6351 0.4013 0.0724  -0.0129 -0.2689 664 HOH A O   
3062 O  O   . HOH F .   ? 0.6139 0.3479 0.3971 -0.1756 0.0566  -0.0152 665 HOH A O   
3063 O  O   . HOH F .   ? 0.5245 0.4755 0.2635 0.1066  0.0452  0.2152  666 HOH A O   
3064 O  O   . HOH F .   ? 0.4244 0.3675 0.7020 0.1765  0.0020  0.0218  667 HOH A O   
3065 O  O   . HOH F .   ? 0.2748 0.3808 0.4199 -0.1273 -0.0627 -0.0401 668 HOH A O   
3066 O  O   . HOH F .   ? 0.4541 0.3386 0.5385 -0.1123 0.1634  0.0093  669 HOH A O   
3067 O  O   . HOH F .   ? 0.2745 0.7088 0.3754 -0.1603 -0.0461 0.0829  670 HOH A O   
3068 O  O   . HOH F .   ? 0.4589 0.3592 0.3634 -0.0441 0.1076  0.0406  671 HOH A O   
3069 O  O   . HOH F .   ? 0.3844 0.4345 0.4018 -0.0428 -0.1314 0.1010  672 HOH A O   
3070 O  O   . HOH F .   ? 0.5113 0.4390 0.3488 0.0671  0.1556  0.0254  673 HOH A O   
3071 O  O   . HOH F .   ? 0.2781 0.2120 0.4745 -0.0295 0.0557  -0.1230 674 HOH A O   
3072 O  O   . HOH F .   ? 0.3262 0.7027 0.3285 -0.1181 0.0017  -0.0463 675 HOH A O   
3073 O  O   . HOH F .   ? 0.3668 0.3564 0.4435 -0.0230 0.2204  -0.0088 676 HOH A O   
3074 O  O   . HOH F .   ? 0.2134 0.6010 0.4266 -0.0346 0.0063  0.0239  677 HOH A O   
3075 O  O   . HOH F .   ? 0.3544 0.2145 0.3242 0.0436  -0.0110 -0.0135 678 HOH A O   
3076 O  O   . HOH F .   ? 0.4900 0.4916 0.2962 0.1439  0.0137  0.0942  679 HOH A O   
3077 O  O   . HOH F .   ? 0.5712 0.3041 0.3743 -0.0662 -0.0252 -0.1430 680 HOH A O   
3078 O  O   . HOH F .   ? 0.4626 0.4411 0.3046 -0.0390 -0.0621 -0.0619 681 HOH A O   
3079 O  O   . HOH F .   ? 0.5709 0.2869 0.3560 -0.0922 0.0082  -0.0208 682 HOH A O   
3080 O  O   . HOH F .   ? 0.6373 0.3052 0.4217 0.0148  0.2696  0.0702  683 HOH A O   
3081 O  O   . HOH F .   ? 0.3925 0.6636 0.3070 0.1967  0.0013  -0.1225 684 HOH A O   
3082 O  O   . HOH F .   ? 0.6197 0.2684 0.3483 -0.0035 -0.0507 -0.0671 685 HOH A O   
3083 O  O   . HOH F .   ? 0.5156 0.3009 0.4602 0.0326  0.0825  0.0377  686 HOH A O   
3084 O  O   . HOH F .   ? 0.1964 0.3488 0.3898 -0.0052 -0.0306 -0.0038 687 HOH A O   
3085 O  O   . HOH F .   ? 0.3319 0.3192 0.3393 0.1009  0.0265  0.0254  688 HOH A O   
3086 O  O   . HOH F .   ? 0.2321 0.3064 0.6363 -0.0361 0.0249  -0.0163 689 HOH A O   
3087 O  O   . HOH F .   ? 0.5781 0.4002 0.4640 -0.2840 0.1111  0.0185  690 HOH A O   
3088 O  O   . HOH F .   ? 0.2727 0.6614 0.4510 0.1162  -0.0115 -0.1140 691 HOH A O   
3089 O  O   . HOH F .   ? 0.4410 0.4873 0.3479 -0.0068 0.0595  0.0113  692 HOH A O   
3090 O  O   . HOH F .   ? 0.2536 0.3172 0.4309 -0.1123 0.0031  0.0324  693 HOH A O   
3091 O  O   . HOH F .   ? 0.3878 0.4946 0.3023 0.0597  0.0988  0.0166  694 HOH A O   
3092 O  O   . HOH F .   ? 0.3474 0.4090 0.4095 -0.0247 0.0287  0.0337  695 HOH A O   
3093 O  O   . HOH F .   ? 0.4681 0.4221 0.3905 0.0148  -0.0242 -0.0766 696 HOH A O   
3094 O  O   . HOH F .   ? 0.4519 0.3688 0.4160 -0.0200 0.0119  0.0082  697 HOH A O   
3095 O  O   . HOH F .   ? 0.2766 0.4352 0.4878 -0.1430 -0.1133 0.0737  698 HOH A O   
3096 O  O   . HOH F .   ? 0.4805 0.3815 0.3510 -0.1938 0.0951  0.0296  699 HOH A O   
3097 O  O   . HOH F .   ? 0.4727 0.3052 0.3959 0.0049  -0.0218 -0.0324 700 HOH A O   
3098 O  O   . HOH F .   ? 0.3578 0.3713 0.3258 -0.0015 0.0135  0.0899  701 HOH A O   
3099 O  O   . HOH F .   ? 0.3411 0.4438 0.4374 -0.0283 0.0579  -0.0724 702 HOH A O   
3100 O  O   . HOH F .   ? 0.4424 0.3804 0.4851 0.0445  0.0080  0.0109  703 HOH A O   
3101 O  O   . HOH F .   ? 0.4535 0.4246 0.4785 0.0907  0.0013  -0.0586 704 HOH A O   
3102 O  O   . HOH F .   ? 0.5557 0.3434 0.4535 -0.0544 0.0983  -0.0640 705 HOH A O   
3103 O  O   . HOH F .   ? 0.4480 0.5033 0.4185 -0.0546 -0.0082 0.0555  706 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  GLN 67  67  67  GLN GLN 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  LEU 91  91  91  LEU LEU 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 VAL 130 130 130 VAL VAL 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 LEU 134 134 134 LEU LEU 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 ALA 203 203 203 ALA ALA 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 V14 1   303 1   V14 V14 A . 
E 5 BCN 1   304 1   BCN BCN A . 
F 6 HOH 1   401 1   HOH HOH A . 
F 6 HOH 2   402 2   HOH HOH A . 
F 6 HOH 3   403 3   HOH HOH A . 
F 6 HOH 4   404 4   HOH HOH A . 
F 6 HOH 5   405 5   HOH HOH A . 
F 6 HOH 6   406 6   HOH HOH A . 
F 6 HOH 7   407 7   HOH HOH A . 
F 6 HOH 8   408 8   HOH HOH A . 
F 6 HOH 9   409 9   HOH HOH A . 
F 6 HOH 10  410 10  HOH HOH A . 
F 6 HOH 11  411 11  HOH HOH A . 
F 6 HOH 12  412 12  HOH HOH A . 
F 6 HOH 13  413 13  HOH HOH A . 
F 6 HOH 14  414 14  HOH HOH A . 
F 6 HOH 15  415 15  HOH HOH A . 
F 6 HOH 16  416 16  HOH HOH A . 
F 6 HOH 17  417 17  HOH HOH A . 
F 6 HOH 18  418 18  HOH HOH A . 
F 6 HOH 19  419 19  HOH HOH A . 
F 6 HOH 20  420 20  HOH HOH A . 
F 6 HOH 21  421 21  HOH HOH A . 
F 6 HOH 22  422 22  HOH HOH A . 
F 6 HOH 23  423 23  HOH HOH A . 
F 6 HOH 24  424 24  HOH HOH A . 
F 6 HOH 25  425 25  HOH HOH A . 
F 6 HOH 26  426 26  HOH HOH A . 
F 6 HOH 27  427 27  HOH HOH A . 
F 6 HOH 28  428 28  HOH HOH A . 
F 6 HOH 29  429 29  HOH HOH A . 
F 6 HOH 30  430 30  HOH HOH A . 
F 6 HOH 31  431 31  HOH HOH A . 
F 6 HOH 32  432 32  HOH HOH A . 
F 6 HOH 33  433 33  HOH HOH A . 
F 6 HOH 34  434 34  HOH HOH A . 
F 6 HOH 35  435 35  HOH HOH A . 
F 6 HOH 36  436 36  HOH HOH A . 
F 6 HOH 37  437 37  HOH HOH A . 
F 6 HOH 38  438 38  HOH HOH A . 
F 6 HOH 39  439 39  HOH HOH A . 
F 6 HOH 40  440 40  HOH HOH A . 
F 6 HOH 41  441 41  HOH HOH A . 
F 6 HOH 42  442 42  HOH HOH A . 
F 6 HOH 43  443 43  HOH HOH A . 
F 6 HOH 44  444 44  HOH HOH A . 
F 6 HOH 45  445 45  HOH HOH A . 
F 6 HOH 46  446 46  HOH HOH A . 
F 6 HOH 47  447 47  HOH HOH A . 
F 6 HOH 48  448 48  HOH HOH A . 
F 6 HOH 49  449 49  HOH HOH A . 
F 6 HOH 50  450 50  HOH HOH A . 
F 6 HOH 51  451 51  HOH HOH A . 
F 6 HOH 52  452 52  HOH HOH A . 
F 6 HOH 53  453 53  HOH HOH A . 
F 6 HOH 54  454 54  HOH HOH A . 
F 6 HOH 55  455 55  HOH HOH A . 
F 6 HOH 56  456 56  HOH HOH A . 
F 6 HOH 57  457 57  HOH HOH A . 
F 6 HOH 58  458 58  HOH HOH A . 
F 6 HOH 59  459 59  HOH HOH A . 
F 6 HOH 60  460 60  HOH HOH A . 
F 6 HOH 61  461 61  HOH HOH A . 
F 6 HOH 62  462 62  HOH HOH A . 
F 6 HOH 63  463 63  HOH HOH A . 
F 6 HOH 64  464 64  HOH HOH A . 
F 6 HOH 65  465 65  HOH HOH A . 
F 6 HOH 66  466 66  HOH HOH A . 
F 6 HOH 67  467 67  HOH HOH A . 
F 6 HOH 68  468 68  HOH HOH A . 
F 6 HOH 69  469 69  HOH HOH A . 
F 6 HOH 70  470 70  HOH HOH A . 
F 6 HOH 71  471 71  HOH HOH A . 
F 6 HOH 72  472 72  HOH HOH A . 
F 6 HOH 73  473 73  HOH HOH A . 
F 6 HOH 74  474 74  HOH HOH A . 
F 6 HOH 75  475 75  HOH HOH A . 
F 6 HOH 76  476 76  HOH HOH A . 
F 6 HOH 77  477 77  HOH HOH A . 
F 6 HOH 78  478 78  HOH HOH A . 
F 6 HOH 79  479 79  HOH HOH A . 
F 6 HOH 80  480 80  HOH HOH A . 
F 6 HOH 81  481 81  HOH HOH A . 
F 6 HOH 82  482 82  HOH HOH A . 
F 6 HOH 83  483 83  HOH HOH A . 
F 6 HOH 84  484 84  HOH HOH A . 
F 6 HOH 85  485 85  HOH HOH A . 
F 6 HOH 86  486 86  HOH HOH A . 
F 6 HOH 87  487 87  HOH HOH A . 
F 6 HOH 88  488 88  HOH HOH A . 
F 6 HOH 89  489 89  HOH HOH A . 
F 6 HOH 90  490 90  HOH HOH A . 
F 6 HOH 91  491 91  HOH HOH A . 
F 6 HOH 92  492 92  HOH HOH A . 
F 6 HOH 93  493 93  HOH HOH A . 
F 6 HOH 94  494 94  HOH HOH A . 
F 6 HOH 95  495 95  HOH HOH A . 
F 6 HOH 96  496 96  HOH HOH A . 
F 6 HOH 97  497 97  HOH HOH A . 
F 6 HOH 98  498 98  HOH HOH A . 
F 6 HOH 99  499 99  HOH HOH A . 
F 6 HOH 100 500 100 HOH HOH A . 
F 6 HOH 101 501 101 HOH HOH A . 
F 6 HOH 102 502 102 HOH HOH A . 
F 6 HOH 103 503 103 HOH HOH A . 
F 6 HOH 104 504 104 HOH HOH A . 
F 6 HOH 105 505 105 HOH HOH A . 
F 6 HOH 106 506 106 HOH HOH A . 
F 6 HOH 107 507 107 HOH HOH A . 
F 6 HOH 108 508 108 HOH HOH A . 
F 6 HOH 109 509 109 HOH HOH A . 
F 6 HOH 110 510 110 HOH HOH A . 
F 6 HOH 111 511 111 HOH HOH A . 
F 6 HOH 112 512 112 HOH HOH A . 
F 6 HOH 113 513 113 HOH HOH A . 
F 6 HOH 114 514 114 HOH HOH A . 
F 6 HOH 115 515 115 HOH HOH A . 
F 6 HOH 116 516 116 HOH HOH A . 
F 6 HOH 117 517 117 HOH HOH A . 
F 6 HOH 118 518 118 HOH HOH A . 
F 6 HOH 119 519 119 HOH HOH A . 
F 6 HOH 120 520 120 HOH HOH A . 
F 6 HOH 121 521 121 HOH HOH A . 
F 6 HOH 122 522 122 HOH HOH A . 
F 6 HOH 123 523 123 HOH HOH A . 
F 6 HOH 124 524 124 HOH HOH A . 
F 6 HOH 125 525 125 HOH HOH A . 
F 6 HOH 126 526 126 HOH HOH A . 
F 6 HOH 127 527 127 HOH HOH A . 
F 6 HOH 128 528 128 HOH HOH A . 
F 6 HOH 129 529 129 HOH HOH A . 
F 6 HOH 130 530 130 HOH HOH A . 
F 6 HOH 131 531 131 HOH HOH A . 
F 6 HOH 132 532 132 HOH HOH A . 
F 6 HOH 133 533 133 HOH HOH A . 
F 6 HOH 134 534 134 HOH HOH A . 
F 6 HOH 135 535 135 HOH HOH A . 
F 6 HOH 136 536 136 HOH HOH A . 
F 6 HOH 137 537 137 HOH HOH A . 
F 6 HOH 138 538 138 HOH HOH A . 
F 6 HOH 139 539 139 HOH HOH A . 
F 6 HOH 140 540 140 HOH HOH A . 
F 6 HOH 141 541 141 HOH HOH A . 
F 6 HOH 142 542 142 HOH HOH A . 
F 6 HOH 143 543 143 HOH HOH A . 
F 6 HOH 144 544 144 HOH HOH A . 
F 6 HOH 145 545 145 HOH HOH A . 
F 6 HOH 146 546 146 HOH HOH A . 
F 6 HOH 147 547 147 HOH HOH A . 
F 6 HOH 148 548 148 HOH HOH A . 
F 6 HOH 149 549 149 HOH HOH A . 
F 6 HOH 150 550 150 HOH HOH A . 
F 6 HOH 151 551 151 HOH HOH A . 
F 6 HOH 152 552 152 HOH HOH A . 
F 6 HOH 153 553 153 HOH HOH A . 
F 6 HOH 154 554 154 HOH HOH A . 
F 6 HOH 155 555 155 HOH HOH A . 
F 6 HOH 156 556 156 HOH HOH A . 
F 6 HOH 157 557 157 HOH HOH A . 
F 6 HOH 158 558 158 HOH HOH A . 
F 6 HOH 159 559 159 HOH HOH A . 
F 6 HOH 160 560 160 HOH HOH A . 
F 6 HOH 161 561 161 HOH HOH A . 
F 6 HOH 162 562 162 HOH HOH A . 
F 6 HOH 163 563 163 HOH HOH A . 
F 6 HOH 164 564 164 HOH HOH A . 
F 6 HOH 165 565 165 HOH HOH A . 
F 6 HOH 166 566 166 HOH HOH A . 
F 6 HOH 167 567 167 HOH HOH A . 
F 6 HOH 168 568 168 HOH HOH A . 
F 6 HOH 169 569 169 HOH HOH A . 
F 6 HOH 170 570 170 HOH HOH A . 
F 6 HOH 171 571 171 HOH HOH A . 
F 6 HOH 172 572 172 HOH HOH A . 
F 6 HOH 173 573 173 HOH HOH A . 
F 6 HOH 174 574 174 HOH HOH A . 
F 6 HOH 175 575 175 HOH HOH A . 
F 6 HOH 176 576 176 HOH HOH A . 
F 6 HOH 177 577 177 HOH HOH A . 
F 6 HOH 178 578 178 HOH HOH A . 
F 6 HOH 179 579 179 HOH HOH A . 
F 6 HOH 180 580 180 HOH HOH A . 
F 6 HOH 181 581 181 HOH HOH A . 
F 6 HOH 182 582 182 HOH HOH A . 
F 6 HOH 183 583 183 HOH HOH A . 
F 6 HOH 184 584 184 HOH HOH A . 
F 6 HOH 185 585 185 HOH HOH A . 
F 6 HOH 186 586 186 HOH HOH A . 
F 6 HOH 187 587 187 HOH HOH A . 
F 6 HOH 188 588 188 HOH HOH A . 
F 6 HOH 189 589 189 HOH HOH A . 
F 6 HOH 190 590 190 HOH HOH A . 
F 6 HOH 191 591 191 HOH HOH A . 
F 6 HOH 192 592 192 HOH HOH A . 
F 6 HOH 193 593 193 HOH HOH A . 
F 6 HOH 194 594 194 HOH HOH A . 
F 6 HOH 195 595 195 HOH HOH A . 
F 6 HOH 196 596 196 HOH HOH A . 
F 6 HOH 197 597 197 HOH HOH A . 
F 6 HOH 198 598 198 HOH HOH A . 
F 6 HOH 199 599 199 HOH HOH A . 
F 6 HOH 200 600 200 HOH HOH A . 
F 6 HOH 201 601 201 HOH HOH A . 
F 6 HOH 202 602 202 HOH HOH A . 
F 6 HOH 203 603 203 HOH HOH A . 
F 6 HOH 204 604 204 HOH HOH A . 
F 6 HOH 205 605 205 HOH HOH A . 
F 6 HOH 206 606 206 HOH HOH A . 
F 6 HOH 207 607 207 HOH HOH A . 
F 6 HOH 208 608 208 HOH HOH A . 
F 6 HOH 209 609 209 HOH HOH A . 
F 6 HOH 210 610 210 HOH HOH A . 
F 6 HOH 211 611 211 HOH HOH A . 
F 6 HOH 212 612 212 HOH HOH A . 
F 6 HOH 213 613 213 HOH HOH A . 
F 6 HOH 214 614 214 HOH HOH A . 
F 6 HOH 215 615 215 HOH HOH A . 
F 6 HOH 216 616 216 HOH HOH A . 
F 6 HOH 217 617 217 HOH HOH A . 
F 6 HOH 218 618 218 HOH HOH A . 
F 6 HOH 219 619 219 HOH HOH A . 
F 6 HOH 220 620 220 HOH HOH A . 
F 6 HOH 221 621 221 HOH HOH A . 
F 6 HOH 222 622 222 HOH HOH A . 
F 6 HOH 223 623 223 HOH HOH A . 
F 6 HOH 224 624 224 HOH HOH A . 
F 6 HOH 225 625 225 HOH HOH A . 
F 6 HOH 226 626 226 HOH HOH A . 
F 6 HOH 227 627 227 HOH HOH A . 
F 6 HOH 228 628 228 HOH HOH A . 
F 6 HOH 229 629 229 HOH HOH A . 
F 6 HOH 230 630 230 HOH HOH A . 
F 6 HOH 231 631 231 HOH HOH A . 
F 6 HOH 232 632 232 HOH HOH A . 
F 6 HOH 233 633 233 HOH HOH A . 
F 6 HOH 234 634 234 HOH HOH A . 
F 6 HOH 235 635 235 HOH HOH A . 
F 6 HOH 236 636 236 HOH HOH A . 
F 6 HOH 237 637 237 HOH HOH A . 
F 6 HOH 238 638 238 HOH HOH A . 
F 6 HOH 239 639 239 HOH HOH A . 
F 6 HOH 240 640 240 HOH HOH A . 
F 6 HOH 241 641 241 HOH HOH A . 
F 6 HOH 242 642 242 HOH HOH A . 
F 6 HOH 243 643 243 HOH HOH A . 
F 6 HOH 244 644 244 HOH HOH A . 
F 6 HOH 245 645 245 HOH HOH A . 
F 6 HOH 246 646 246 HOH HOH A . 
F 6 HOH 247 647 247 HOH HOH A . 
F 6 HOH 248 648 248 HOH HOH A . 
F 6 HOH 249 649 249 HOH HOH A . 
F 6 HOH 250 650 250 HOH HOH A . 
F 6 HOH 251 651 251 HOH HOH A . 
F 6 HOH 252 652 252 HOH HOH A . 
F 6 HOH 253 653 253 HOH HOH A . 
F 6 HOH 254 654 254 HOH HOH A . 
F 6 HOH 255 655 255 HOH HOH A . 
F 6 HOH 256 656 256 HOH HOH A . 
F 6 HOH 257 657 257 HOH HOH A . 
F 6 HOH 258 658 258 HOH HOH A . 
F 6 HOH 259 659 259 HOH HOH A . 
F 6 HOH 260 660 260 HOH HOH A . 
F 6 HOH 261 661 261 HOH HOH A . 
F 6 HOH 262 662 262 HOH HOH A . 
F 6 HOH 263 663 263 HOH HOH A . 
F 6 HOH 264 664 264 HOH HOH A . 
F 6 HOH 265 665 265 HOH HOH A . 
F 6 HOH 266 666 266 HOH HOH A . 
F 6 HOH 267 667 267 HOH HOH A . 
F 6 HOH 268 668 268 HOH HOH A . 
F 6 HOH 269 669 269 HOH HOH A . 
F 6 HOH 270 670 270 HOH HOH A . 
F 6 HOH 271 671 271 HOH HOH A . 
F 6 HOH 272 672 272 HOH HOH A . 
F 6 HOH 273 673 273 HOH HOH A . 
F 6 HOH 274 674 274 HOH HOH A . 
F 6 HOH 275 675 275 HOH HOH A . 
F 6 HOH 276 676 276 HOH HOH A . 
F 6 HOH 277 677 277 HOH HOH A . 
F 6 HOH 278 678 278 HOH HOH A . 
F 6 HOH 279 679 279 HOH HOH A . 
F 6 HOH 280 680 280 HOH HOH A . 
F 6 HOH 281 681 281 HOH HOH A . 
F 6 HOH 282 682 282 HOH HOH A . 
F 6 HOH 283 683 283 HOH HOH A . 
F 6 HOH 284 684 284 HOH HOH A . 
F 6 HOH 285 685 285 HOH HOH A . 
F 6 HOH 286 686 286 HOH HOH A . 
F 6 HOH 287 687 287 HOH HOH A . 
F 6 HOH 288 688 288 HOH HOH A . 
F 6 HOH 289 689 289 HOH HOH A . 
F 6 HOH 290 690 290 HOH HOH A . 
F 6 HOH 291 691 291 HOH HOH A . 
F 6 HOH 292 692 292 HOH HOH A . 
F 6 HOH 293 693 293 HOH HOH A . 
F 6 HOH 294 694 294 HOH HOH A . 
F 6 HOH 295 695 295 HOH HOH A . 
F 6 HOH 296 696 296 HOH HOH A . 
F 6 HOH 297 697 297 HOH HOH A . 
F 6 HOH 298 698 298 HOH HOH A . 
F 6 HOH 299 699 299 HOH HOH A . 
F 6 HOH 300 700 300 HOH HOH A . 
F 6 HOH 301 701 301 HOH HOH A . 
F 6 HOH 302 702 302 HOH HOH A . 
F 6 HOH 303 703 303 HOH HOH A . 
F 6 HOH 304 704 304 HOH HOH A . 
F 6 HOH 305 705 305 HOH HOH A . 
F 6 HOH 306 706 306 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.4 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.9 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.8  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A D V14 .   ? A V14 303 ? 1_555 116.8 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A D V14 .   ? A V14 303 ? 1_555 119.8 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A D V14 .   ? A V14 303 ? 1_555 104.1 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B D V14 .   ? A V14 303 ? 1_555 116.7 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B D V14 .   ? A V14 303 ? 1_555 119.8 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B D V14 .   ? A V14 303 ? 1_555 104.1 ? 
10 N10 A D V14 .   ? A V14 303 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B D V14 .   ? A V14 303 ? 1_555 0.0   ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLN 
_pdbx_validate_close_contact.auth_seq_id_1    254 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    697 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 N A HIS 4  ? B CA A HIS 4  ? B 1.580 1.459 0.121  0.020 N 
2 1 N A VAL 68 ? B CA A VAL 68 ? B 1.328 1.459 -0.131 0.020 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 34 ? B CG A ASP 34 ? B OD1 A ASP 34 ? B 124.17 118.30 5.87  0.90 N 
2 1 NE A ARG 58 ? B CZ A ARG 58 ? B NH1 A ARG 58 ? B 116.72 120.30 -3.58 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -143.56 55.44   
2 1 SER A 65  ? B -164.82 -169.59 
3 1 LYS A 76  ? B -71.46  -100.54 
4 1 LYS A 111 ? ? 75.65   -4.05   
5 1 PHE A 175 ? A -152.98 63.41   
6 1 ASN A 243 ? ? -95.78  51.68   
7 1 LYS A 251 ? ? 56.24   -137.85 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MET N    N  N N 264 
MET CA   C  N S 265 
MET C    C  N N 266 
MET O    O  N N 267 
MET CB   C  N N 268 
MET CG   C  N N 269 
MET SD   S  N N 270 
MET CE   C  N N 271 
MET OXT  O  N N 272 
MET H    H  N N 273 
MET H2   H  N N 274 
MET HA   H  N N 275 
MET HB2  H  N N 276 
MET HB3  H  N N 277 
MET HG2  H  N N 278 
MET HG3  H  N N 279 
MET HE1  H  N N 280 
MET HE2  H  N N 281 
MET HE3  H  N N 282 
MET HXT  H  N N 283 
PHE N    N  N N 284 
PHE CA   C  N S 285 
PHE C    C  N N 286 
PHE O    O  N N 287 
PHE CB   C  N N 288 
PHE CG   C  Y N 289 
PHE CD1  C  Y N 290 
PHE CD2  C  Y N 291 
PHE CE1  C  Y N 292 
PHE CE2  C  Y N 293 
PHE CZ   C  Y N 294 
PHE OXT  O  N N 295 
PHE H    H  N N 296 
PHE H2   H  N N 297 
PHE HA   H  N N 298 
PHE HB2  H  N N 299 
PHE HB3  H  N N 300 
PHE HD1  H  N N 301 
PHE HD2  H  N N 302 
PHE HE1  H  N N 303 
PHE HE2  H  N N 304 
PHE HZ   H  N N 305 
PHE HXT  H  N N 306 
PRO N    N  N N 307 
PRO CA   C  N S 308 
PRO C    C  N N 309 
PRO O    O  N N 310 
PRO CB   C  N N 311 
PRO CG   C  N N 312 
PRO CD   C  N N 313 
PRO OXT  O  N N 314 
PRO H    H  N N 315 
PRO HA   H  N N 316 
PRO HB2  H  N N 317 
PRO HB3  H  N N 318 
PRO HG2  H  N N 319 
PRO HG3  H  N N 320 
PRO HD2  H  N N 321 
PRO HD3  H  N N 322 
PRO HXT  H  N N 323 
SER N    N  N N 324 
SER CA   C  N S 325 
SER C    C  N N 326 
SER O    O  N N 327 
SER CB   C  N N 328 
SER OG   O  N N 329 
SER OXT  O  N N 330 
SER H    H  N N 331 
SER H2   H  N N 332 
SER HA   H  N N 333 
SER HB2  H  N N 334 
SER HB3  H  N N 335 
SER HG   H  N N 336 
SER HXT  H  N N 337 
THR N    N  N N 338 
THR CA   C  N S 339 
THR C    C  N N 340 
THR O    O  N N 341 
THR CB   C  N R 342 
THR OG1  O  N N 343 
THR CG2  C  N N 344 
THR OXT  O  N N 345 
THR H    H  N N 346 
THR H2   H  N N 347 
THR HA   H  N N 348 
THR HB   H  N N 349 
THR HG1  H  N N 350 
THR HG21 H  N N 351 
THR HG22 H  N N 352 
THR HG23 H  N N 353 
THR HXT  H  N N 354 
TRP N    N  N N 355 
TRP CA   C  N S 356 
TRP C    C  N N 357 
TRP O    O  N N 358 
TRP CB   C  N N 359 
TRP CG   C  Y N 360 
TRP CD1  C  Y N 361 
TRP CD2  C  Y N 362 
TRP NE1  N  Y N 363 
TRP CE2  C  Y N 364 
TRP CE3  C  Y N 365 
TRP CZ2  C  Y N 366 
TRP CZ3  C  Y N 367 
TRP CH2  C  Y N 368 
TRP OXT  O  N N 369 
TRP H    H  N N 370 
TRP H2   H  N N 371 
TRP HA   H  N N 372 
TRP HB2  H  N N 373 
TRP HB3  H  N N 374 
TRP HD1  H  N N 375 
TRP HE1  H  N N 376 
TRP HE3  H  N N 377 
TRP HZ2  H  N N 378 
TRP HZ3  H  N N 379 
TRP HH2  H  N N 380 
TRP HXT  H  N N 381 
TYR N    N  N N 382 
TYR CA   C  N S 383 
TYR C    C  N N 384 
TYR O    O  N N 385 
TYR CB   C  N N 386 
TYR CG   C  Y N 387 
TYR CD1  C  Y N 388 
TYR CD2  C  Y N 389 
TYR CE1  C  Y N 390 
TYR CE2  C  Y N 391 
TYR CZ   C  Y N 392 
TYR OH   O  N N 393 
TYR OXT  O  N N 394 
TYR H    H  N N 395 
TYR H2   H  N N 396 
TYR HA   H  N N 397 
TYR HB2  H  N N 398 
TYR HB3  H  N N 399 
TYR HD1  H  N N 400 
TYR HD2  H  N N 401 
TYR HE1  H  N N 402 
TYR HE2  H  N N 403 
TYR HH   H  N N 404 
TYR HXT  H  N N 405 
V14 F20  F  N N 406 
V14 C5   C  Y N 407 
V14 C4   C  Y N 408 
V14 S7   S  N N 409 
V14 O9   O  N N 410 
V14 N10  N  N N 411 
V14 O8   O  N N 412 
V14 C3   C  Y N 413 
V14 F12  F  N N 414 
V14 C2   C  Y N 415 
V14 F13  F  N N 416 
V14 C6   C  Y N 417 
V14 C1   C  Y N 418 
V14 S11  S  N N 419 
V14 O16  O  N N 420 
V14 O17  O  N N 421 
V14 C15  C  N N 422 
V14 C18  C  N N 423 
V14 O21  O  N N 424 
V14 N19  N  N N 425 
V14 C14  C  N N 426 
V14 C28  C  N N 427 
V14 C27  C  N N 428 
V14 C26  C  N N 429 
V14 C25  C  N N 430 
V14 C24  C  N N 431 
V14 C23  C  N N 432 
V14 C22  C  N N 433 
V14 H1   H  N N 434 
V14 H2   H  N N 435 
V14 H3   H  N N 436 
V14 H4   H  N N 437 
V14 H5   H  N N 438 
V14 H6   H  N N 439 
V14 H7   H  N N 440 
V14 H8   H  N N 441 
V14 H9   H  N N 442 
V14 H10  H  N N 443 
V14 H11  H  N N 444 
V14 H12  H  N N 445 
V14 H13  H  N N 446 
V14 H14  H  N N 447 
V14 H15  H  N N 448 
V14 H16  H  N N 449 
V14 H17  H  N N 450 
V14 H18  H  N N 451 
V14 H19  H  N N 452 
V14 H20  H  N N 453 
V14 H21  H  N N 454 
V14 H22  H  N N 455 
V14 H23  H  N N 456 
VAL N    N  N N 457 
VAL CA   C  N S 458 
VAL C    C  N N 459 
VAL O    O  N N 460 
VAL CB   C  N N 461 
VAL CG1  C  N N 462 
VAL CG2  C  N N 463 
VAL OXT  O  N N 464 
VAL H    H  N N 465 
VAL H2   H  N N 466 
VAL HA   H  N N 467 
VAL HB   H  N N 468 
VAL HG11 H  N N 469 
VAL HG12 H  N N 470 
VAL HG13 H  N N 471 
VAL HG21 H  N N 472 
VAL HG22 H  N N 473 
VAL HG23 H  N N 474 
VAL HXT  H  N N 475 
ZN  ZN   ZN N N 476 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MET N   CA   sing N N 250 
MET N   H    sing N N 251 
MET N   H2   sing N N 252 
MET CA  C    sing N N 253 
MET CA  CB   sing N N 254 
MET CA  HA   sing N N 255 
MET C   O    doub N N 256 
MET C   OXT  sing N N 257 
MET CB  CG   sing N N 258 
MET CB  HB2  sing N N 259 
MET CB  HB3  sing N N 260 
MET CG  SD   sing N N 261 
MET CG  HG2  sing N N 262 
MET CG  HG3  sing N N 263 
MET SD  CE   sing N N 264 
MET CE  HE1  sing N N 265 
MET CE  HE2  sing N N 266 
MET CE  HE3  sing N N 267 
MET OXT HXT  sing N N 268 
PHE N   CA   sing N N 269 
PHE N   H    sing N N 270 
PHE N   H2   sing N N 271 
PHE CA  C    sing N N 272 
PHE CA  CB   sing N N 273 
PHE CA  HA   sing N N 274 
PHE C   O    doub N N 275 
PHE C   OXT  sing N N 276 
PHE CB  CG   sing N N 277 
PHE CB  HB2  sing N N 278 
PHE CB  HB3  sing N N 279 
PHE CG  CD1  doub Y N 280 
PHE CG  CD2  sing Y N 281 
PHE CD1 CE1  sing Y N 282 
PHE CD1 HD1  sing N N 283 
PHE CD2 CE2  doub Y N 284 
PHE CD2 HD2  sing N N 285 
PHE CE1 CZ   doub Y N 286 
PHE CE1 HE1  sing N N 287 
PHE CE2 CZ   sing Y N 288 
PHE CE2 HE2  sing N N 289 
PHE CZ  HZ   sing N N 290 
PHE OXT HXT  sing N N 291 
PRO N   CA   sing N N 292 
PRO N   CD   sing N N 293 
PRO N   H    sing N N 294 
PRO CA  C    sing N N 295 
PRO CA  CB   sing N N 296 
PRO CA  HA   sing N N 297 
PRO C   O    doub N N 298 
PRO C   OXT  sing N N 299 
PRO CB  CG   sing N N 300 
PRO CB  HB2  sing N N 301 
PRO CB  HB3  sing N N 302 
PRO CG  CD   sing N N 303 
PRO CG  HG2  sing N N 304 
PRO CG  HG3  sing N N 305 
PRO CD  HD2  sing N N 306 
PRO CD  HD3  sing N N 307 
PRO OXT HXT  sing N N 308 
SER N   CA   sing N N 309 
SER N   H    sing N N 310 
SER N   H2   sing N N 311 
SER CA  C    sing N N 312 
SER CA  CB   sing N N 313 
SER CA  HA   sing N N 314 
SER C   O    doub N N 315 
SER C   OXT  sing N N 316 
SER CB  OG   sing N N 317 
SER CB  HB2  sing N N 318 
SER CB  HB3  sing N N 319 
SER OG  HG   sing N N 320 
SER OXT HXT  sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
V14 C18 O21  sing N N 390 
V14 C18 C15  sing N N 391 
V14 C15 S11  sing N N 392 
V14 O17 S11  doub N N 393 
V14 C22 C23  sing N N 394 
V14 C22 C14  sing N N 395 
V14 C23 C24  sing N N 396 
V14 N19 C14  sing N N 397 
V14 N19 C6   sing N N 398 
V14 C24 C25  sing N N 399 
V14 S11 C1   sing N N 400 
V14 S11 O16  doub N N 401 
V14 C14 C28  sing N N 402 
V14 C6  C1   doub Y N 403 
V14 C6  C5   sing Y N 404 
V14 C1  C2   sing Y N 405 
V14 F20 C5   sing N N 406 
V14 C25 C26  sing N N 407 
V14 C5  C4   doub Y N 408 
V14 C26 C27  sing N N 409 
V14 C28 C27  sing N N 410 
V14 C2  F13  sing N N 411 
V14 C2  C3   doub Y N 412 
V14 C4  C3   sing Y N 413 
V14 C4  S7   sing N N 414 
V14 C3  F12  sing N N 415 
V14 N10 S7   sing N N 416 
V14 S7  O9   doub N N 417 
V14 S7  O8   doub N N 418 
V14 N10 H1   sing N N 419 
V14 N10 H2   sing N N 420 
V14 C15 H3   sing N N 421 
V14 C15 H4   sing N N 422 
V14 C18 H5   sing N N 423 
V14 C18 H6   sing N N 424 
V14 O21 H7   sing N N 425 
V14 N19 H8   sing N N 426 
V14 C14 H9   sing N N 427 
V14 C28 H10  sing N N 428 
V14 C28 H11  sing N N 429 
V14 C27 H12  sing N N 430 
V14 C27 H13  sing N N 431 
V14 C26 H14  sing N N 432 
V14 C26 H15  sing N N 433 
V14 C25 H16  sing N N 434 
V14 C25 H17  sing N N 435 
V14 C24 H18  sing N N 436 
V14 C24 H19  sing N N 437 
V14 C23 H20  sing N N 438 
V14 C23 H21  sing N N 439 
V14 C22 H22  sing N N 440 
V14 C22 H23  sing N N 441 
VAL N   CA   sing N N 442 
VAL N   H    sing N N 443 
VAL N   H2   sing N N 444 
VAL CA  C    sing N N 445 
VAL CA  CB   sing N N 446 
VAL CA  HA   sing N N 447 
VAL C   O    doub N N 448 
VAL C   OXT  sing N N 449 
VAL CB  CG1  sing N N 450 
VAL CB  CG2  sing N N 451 
VAL CB  HB   sing N N 452 
VAL CG1 HG11 sing N N 453 
VAL CG1 HG12 sing N N 454 
VAL CG1 HG13 sing N N 455 
VAL CG2 HG21 sing N N 456 
VAL CG2 HG22 sing N N 457 
VAL CG2 HG23 sing N N 458 
VAL OXT HXT  sing N N 459 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                           ZN  
3 'DIMETHYL SULFOXIDE'                                                                 DMS 
4 '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V14 
5 BICINE                                                                               BCN 
6 water                                                                                HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          'PDB ENTRY 3HLJ' 
# 
